data_8PWG
# 
_entry.id   8PWG 
# 
_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   8PWG         pdb_00008pwg 10.2210/pdb8pwg/pdb 
WWPDB D_1292131773 ?            ?                   
# 
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                        8PWG 
_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 . 8PWI 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 
'Ortolani, G.' 1 0000-0001-6373-9919 
'Bosman, R.'   2 0000-0002-9939-602X 
'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    23 ? ? ? ? 
# 
_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  33  GLU GLU 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 2   HOH HOH A . 
D 4 HOH 2  402 17  HOH HOH A . 
D 4 HOH 3  403 3   HOH HOH A . 
D 4 HOH 4  404 5   HOH HOH A . 
D 4 HOH 5  405 7   HOH HOH A . 
D 4 HOH 6  406 32  HOH HOH A . 
D 4 HOH 7  407 19  HOH HOH A . 
D 4 HOH 8  408 1   HOH HOH A . 
D 4 HOH 9  409 4   HOH HOH A . 
D 4 HOH 10 410 6   HOH HOH A . 
D 4 HOH 11 411 34  HOH HOH A . 
D 4 HOH 12 412 8   HOH HOH A . 
D 4 HOH 13 413 10  HOH HOH A . 
D 4 HOH 14 414 25  HOH HOH A . 
D 4 HOH 15 415 29  HOH HOH A . 
D 4 HOH 16 416 9   HOH HOH A . 
D 4 HOH 17 417 43  HOH HOH A . 
D 4 HOH 18 418 35  HOH HOH A . 
D 4 HOH 19 419 26  HOH HOH A . 
D 4 HOH 20 420 44  HOH HOH A . 
D 4 HOH 21 421 12  HOH HOH A . 
D 4 HOH 22 422 49  HOH HOH A . 
D 4 HOH 23 423 42  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 33 ? CG  ? A GLU 33 CG  
2 1 Y 1 A GLU 33 ? CD  ? A GLU 33 CD  
3 1 Y 1 A GLU 33 ? OE1 ? A GLU 33 OE1 
4 1 Y 1 A GLU 33 ? OE2 ? A GLU 33 OE2 
5 1 Y 1 A GLU 97 ? CG  ? A GLU 97 CG  
6 1 Y 1 A GLU 97 ? CD  ? A GLU 97 CD  
7 1 Y 1 A GLU 97 ? OE1 ? A GLU 97 OE1 
8 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                     8PWG 
_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                         8PWG 
_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                   8PWG 
_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             2.80 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.05 
_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 150 mM, 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                          28.5 
_reflns.entry_id                                       8PWG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.94 
_reflns.d_resolution_low                               44.8 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                76.20 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.07 
_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                                   0.9814 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.94 
_reflns_shell.d_res_low                                     44.8 
_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                             4429 
_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                                  0.9814 
_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                               45.80 
_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                                 8PWG 
_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                            1.94 
_refine.ls_d_res_low                             44.8 
_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                  703 
_refine.ls_number_reflns_R_work                  12900 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    59.26 
_refine.ls_percent_reflns_R_free                 5.17 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2534 
_refine.ls_R_factor_R_free                       0.2863 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2516 
_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                 38.1441 
_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                            0.3695 
_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                       1.94 
_refine_hist.d_res_low                        44.8 
_refine_hist.number_atoms_solvent             23 
_refine_hist.number_atoms_total               1624 
_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        1580 
_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' ? 0.0124  ? 3282 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4928  ? 4496 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0696  ? 544  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0097  ? 536  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.6809 ? 1088 ? 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' 1.94 2.09 . . 1   6    0.16  . . . . 0.6667 . . . . . . . . . . . 0.0229 
'X-RAY DIFFRACTION' 2.10 2.30 . . 26  477  12.38 . . . . 0.4581 . . . . . . . . . . . 0.5059 
'X-RAY DIFFRACTION' 2.30 2.63 . . 219 3528 82.39 . . . . 0.3433 . . . . . . . . . . . 0.3958 
'X-RAY DIFFRACTION' 2.63 3.31 . . 221 4359 99.87 . . . . 0.2565 . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 3.31 44.8 . . 236 4530 99.94 . . . . 0.2165 . . . . . . . . . . . 0.2436 
# 
_struct.entry_id                     8PWG 
_struct.title                        
'Light structure of sensory rhodopsin-II solved by serial millisecond crystallography 90-120 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        8PWG 
_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              8PWG 
_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 8PWG GLU A 240 ? UNP P42196 ? ? 'expression tag' 240 1  
1 8PWG ASN A 241 ? UNP P42196 ? ? 'expression tag' 241 2  
1 8PWG SER A 242 ? UNP P42196 ? ? 'expression tag' 242 3  
1 8PWG HIS A 243 ? UNP P42196 ? ? 'expression tag' 243 4  
1 8PWG HIS A 244 ? UNP P42196 ? ? 'expression tag' 244 5  
1 8PWG HIS A 245 ? UNP P42196 ? ? 'expression tag' 245 6  
1 8PWG HIS A 246 ? UNP P42196 ? ? 'expression tag' 246 7  
1 8PWG HIS A 247 ? UNP P42196 ? ? 'expression tag' 247 8  
1 8PWG HIS A 248 ? UNP P42196 ? ? 'expression tag' 248 9  
1 8PWG 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)'  9540 ? 
# 
_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 34  ? LEU A 56  ? ARG A 34  LEU A 56  1 ? 23 
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 ? ? ? ? ? ? ? 1.269 ? ? 
# 
_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                   8PWG 
_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_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 16  ? B CB A LEU 16  ? B CG A LEU 16  ? B 96.97  115.30 -18.33 2.30 N 
2 1 CA A LEU 56  ? B CB A LEU 56  ? B CG A LEU 56  ? B 99.56  115.30 -15.74 2.30 N 
3 1 CA A MET 129 ? B CB A MET 129 ? B CG A MET 129 ? B 101.50 113.30 -11.80 1.70 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 ALA A 25  ? B -48.61  -17.10  
2  1 ALA A 64  ? A 55.36   -106.96 
3  1 ALA A 64  ? B 61.18   -111.63 
4  1 ASP A 75  ? B -15.72  -73.53  
5  1 VAL A 142 ? B -51.39  -71.45  
6  1 PRO A 144 ? B -29.86  -61.37  
7  1 SER A 150 ? B -47.18  -0.66   
8  1 ALA A 186 ? B 55.46   13.62   
9  1 LEU A 187 ? B -53.74  -90.73  
10 1 LEU A 188 ? B -31.45  130.10  
11 1 LYS A 205 ? B -102.98 -60.41  
12 1 ALA A 215 ? B -62.44  -71.17  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     421 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      A 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       423 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   8.64 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 ALA 217 ? A ALA 217 
9  1 Y 1 A THR 218 ? A THR 218 
10 1 Y 1 A LEU 219 ? A LEU 219 
11 1 Y 1 A ARG 220 ? A ARG 220 
12 1 Y 1 A ALA 221 ? A ALA 221 
13 1 Y 1 A GLU 222 ? A GLU 222 
14 1 Y 1 A HIS 223 ? A HIS 223 
15 1 Y 1 A GLY 224 ? A GLY 224 
16 1 Y 1 A GLU 225 ? A GLU 225 
17 1 Y 1 A SER 226 ? A SER 226 
18 1 Y 1 A LEU 227 ? A LEU 227 
19 1 Y 1 A ALA 228 ? A ALA 228 
20 1 Y 1 A GLY 229 ? A GLY 229 
21 1 Y 1 A VAL 230 ? A VAL 230 
22 1 Y 1 A ASP 231 ? A ASP 231 
23 1 Y 1 A THR 232 ? A THR 232 
24 1 Y 1 A ASP 233 ? A ASP 233 
25 1 Y 1 A ALA 234 ? A ALA 234 
26 1 Y 1 A PRO 235 ? A PRO 235 
27 1 Y 1 A ALA 236 ? A ALA 236 
28 1 Y 1 A VAL 237 ? A VAL 237 
29 1 Y 1 A ALA 238 ? A ALA 238 
30 1 Y 1 A ASP 239 ? A ASP 239 
31 1 Y 1 A GLU 240 ? A GLU 240 
32 1 Y 1 A ASN 241 ? A ASN 241 
33 1 Y 1 A SER 242 ? A SER 242 
34 1 Y 1 A HIS 243 ? A HIS 243 
35 1 Y 1 A HIS 244 ? A HIS 244 
36 1 Y 1 A HIS 245 ? A HIS 245 
37 1 Y 1 A HIS 246 ? A HIS 246 
38 1 Y 1 A HIS 247 ? A HIS 247 
39 1 Y 1 A HIS 248 ? A HIS 248 
40 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                    8PWG 
_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 0.790 106.66000 ?  2   VAL A N   1 
ATOM   2    N  N   B VAL A 1 2   ? 36.59500 18.51900 -14.04900 0.210 106.66000 ?  2   VAL A N   1 
ATOM   3    C  CA  A VAL A 1 2   ? 36.86200 19.80200 -13.23400 0.790 94.33000  ?  2   VAL A CA  1 
ATOM   4    C  CA  B VAL A 1 2   ? 36.80100 19.55500 -13.04800 0.210 94.58000  ?  2   VAL A CA  1 
ATOM   5    C  C   A VAL A 1 2   ? 36.65600 19.32200 -11.80300 0.790 84.84000  ?  2   VAL A C   1 
ATOM   6    C  C   B VAL A 1 2   ? 36.45200 18.99200 -11.65700 0.210 85.50000  ?  2   VAL A C   1 
ATOM   7    O  O   A VAL A 1 2   ? 35.53000 19.00100 -11.40300 0.790 85.84000  ?  2   VAL A O   1 
ATOM   8    O  O   B VAL A 1 2   ? 35.37100 18.43900 -11.45200 0.210 86.54000  ?  2   VAL A O   1 
ATOM   9    C  CB  A VAL A 1 2   ? 35.91100 20.96000 -13.57800 0.790 96.89000  ?  2   VAL A CB  1 
ATOM   10   C  CB  B VAL A 1 2   ? 35.98600 20.84700 -13.40300 0.210 96.60000  ?  2   VAL A CB  1 
ATOM   11   C  CG1 A VAL A 1 2   ? 34.45400 20.56800 -13.35600 0.790 96.41000  ?  2   VAL A CG1 1 
ATOM   12   C  CG1 B VAL A 1 2   ? 34.48300 20.58900 -13.43900 0.210 96.40000  ?  2   VAL A CG1 1 
ATOM   13   C  CG2 A VAL A 1 2   ? 36.26600 22.20300 -12.76800 0.790 88.53000  ?  2   VAL A CG2 1 
ATOM   14   C  CG2 B VAL A 1 2   ? 36.33800 22.01200 -12.49300 0.210 88.53000  ?  2   VAL A CG2 1 
ATOM   15   N  N   A GLY A 1 3   ? 37.74400 19.26100 -11.03500 0.790 83.81000  ?  3   GLY A N   1 
ATOM   16   N  N   B GLY A 1 3   ? 37.42000 19.06400 -10.73400 0.210 78.40000  ?  3   GLY A N   1 
ATOM   17   C  CA  A GLY A 1 3   ? 37.69300 18.80200 -9.66700  0.790 55.68000  ?  3   GLY A CA  1 
ATOM   18   C  CA  B GLY A 1 3   ? 37.24500 18.67600 -9.35300  0.210 56.95000  ?  3   GLY A CA  1 
ATOM   19   C  C   A GLY A 1 3   ? 37.58900 19.94900 -8.67400  0.790 55.22000  ?  3   GLY A C   1 
ATOM   20   C  C   B GLY A 1 3   ? 37.55000 19.85400 -8.43000  0.210 54.46000  ?  3   GLY A C   1 
ATOM   21   O  O   A GLY A 1 3   ? 37.79600 21.11500 -8.99900  0.790 50.18000  ?  3   GLY A O   1 
ATOM   22   O  O   B GLY A 1 3   ? 38.03200 20.90500 -8.85700  0.210 51.31000  ?  3   GLY A O   1 
ATOM   23   N  N   A LEU A 1 4   ? 37.25400 19.58400 -7.43400  0.790 48.96000  ?  4   LEU A N   1 
ATOM   24   N  N   B LEU A 1 4   ? 37.28000 19.64700 -7.13500  0.210 48.36000  ?  4   LEU A N   1 
ATOM   25   C  CA  A LEU A 1 4   ? 37.14800 20.58400 -6.37800  0.790 41.93000  ?  4   LEU A CA  1 
ATOM   26   C  CA  B LEU A 1 4   ? 37.20600 20.76600 -6.19100  0.210 42.20000  ?  4   LEU A CA  1 
ATOM   27   C  C   A LEU A 1 4   ? 38.43900 21.38000 -6.24400  0.790 34.50000  ?  4   LEU A C   1 
ATOM   28   C  C   B LEU A 1 4   ? 38.47600 21.60200 -6.18300  0.210 36.92000  ?  4   LEU A C   1 
ATOM   29   O  O   A LEU A 1 4   ? 38.41100 22.60800 -6.09900  0.790 45.77000  ?  4   LEU A O   1 
ATOM   30   O  O   B LEU A 1 4   ? 38.42000 22.82300 -6.03000  0.210 44.87000  ?  4   LEU A O   1 
ATOM   31   C  CB  A LEU A 1 4   ? 36.81100 19.91300 -5.04900  0.790 47.55000  ?  4   LEU A CB  1 
ATOM   32   C  CB  B LEU A 1 4   ? 36.92300 20.24200 -4.78000  0.210 43.77000  ?  4   LEU A CB  1 
ATOM   33   C  CG  A LEU A 1 4   ? 35.45600 19.22400 -4.92000  0.790 39.86000  ?  4   LEU A CG  1 
ATOM   34   C  CG  B LEU A 1 4   ? 35.56500 19.62200 -4.43600  0.210 39.37000  ?  4   LEU A CG  1 
ATOM   35   C  CD1 A LEU A 1 4   ? 35.32700 18.59800 -3.53700  0.790 42.53000  ?  4   LEU A CD1 1 
ATOM   36   C  CD1 B LEU A 1 4   ? 35.65400 18.90900 -3.17100  0.210 44.67000  ?  4   LEU A CD1 1 
ATOM   37   C  CD2 A LEU A 1 4   ? 34.32700 20.20100 -5.17600  0.790 52.76000  ?  4   LEU A CD2 1 
ATOM   38   C  CD2 B LEU A 1 4   ? 34.59800 20.67400 -4.23700  0.210 38.66000  ?  4   LEU A CD2 1 
ATOM   39   N  N   A THR A 1 5   ? 39.58500 20.69600 -6.28200  0.790 41.54000  ?  5   THR A N   1 
ATOM   40   N  N   B THR A 1 5   ? 39.62800 20.97400 -6.31700  0.210 42.26000  ?  5   THR A N   1 
ATOM   41   C  CA  A THR A 1 5   ? 40.85600 21.39100 -6.10900  0.790 41.04000  ?  5   THR A CA  1 
ATOM   42   C  CA  B THR A 1 5   ? 40.88200 21.67000 -6.03900  0.210 41.33000  ?  5   THR A CA  1 
ATOM   43   C  C   A THR A 1 5   ? 41.07400 22.41800 -7.21300  0.790 45.18000  ?  5   THR A C   1 
ATOM   44   C  C   B THR A 1 5   ? 41.34900 22.56100 -7.17000  0.210 43.23000  ?  5   THR A C   1 
ATOM   45   O  O   A THR A 1 5   ? 41.55100 23.52900 -6.95200  0.790 46.28000  ?  5   THR A O   1 
ATOM   46   O  O   B THR A 1 5   ? 42.05400 23.53900 -6.89100  0.210 41.84000  ?  5   THR A O   1 
ATOM   47   C  CB  A THR A 1 5   ? 42.01200 20.38900 -6.07300  0.790 44.68000  ?  5   THR A CB  1 
ATOM   48   C  CB  B THR A 1 5   ? 41.96200 20.66100 -5.66500  0.210 43.40000  ?  5   THR A CB  1 
ATOM   49   O  OG1 A THR A 1 5   ? 41.77500 19.33200 -7.01100  0.790 49.44000  ?  5   THR A OG1 1 
ATOM   50   O  OG1 B THR A 1 5   ? 41.58700 19.38100 -6.19100  0.210 45.23000  ?  5   THR A OG1 1 
ATOM   51   C  CG2 A THR A 1 5   ? 42.16200 19.79700 -4.67500  0.790 41.82000  ?  5   THR A CG2 1 
ATOM   52   C  CG2 B THR A 1 5   ? 42.10700 20.57900 -4.16800  0.210 40.55000  ?  5   THR A CG2 1 
ATOM   53   N  N   A THR A 1 6   ? 40.72100 22.07100 -8.45400  0.790 31.68000  ?  6   THR A N   1 
ATOM   54   N  N   B THR A 1 6   ? 40.96500 22.27300 -8.41800  0.210 35.75000  ?  6   THR A N   1 
ATOM   55   C  CA  A THR A 1 6   ? 40.86300 23.02900 -9.54700  0.790 32.73000  ?  6   THR A CA  1 
ATOM   56   C  CA  B THR A 1 6   ? 41.11000 23.29000 -9.45000  0.210 33.76000  ?  6   THR A CA  1 
ATOM   57   C  C   A THR A 1 6   ? 40.05300 24.29100 -9.27400  0.790 33.23000  ?  6   THR A C   1 
ATOM   58   C  C   B THR A 1 6   ? 40.37500 24.53200 -9.01300  0.210 34.79000  ?  6   THR A C   1 
ATOM   59   O  O   A THR A 1 6   ? 40.52200 25.40700 -9.52600  0.790 39.65000  ?  6   THR A O   1 
ATOM   60   O  O   B THR A 1 6   ? 40.96800 25.59400 -8.80000  0.210 33.89000  ?  6   THR A O   1 
ATOM   61   C  CB  A THR A 1 6   ? 40.42300 22.40200 -10.87100 0.790 48.86000  ?  6   THR A CB  1 
ATOM   62   C  CB  B THR A 1 6   ? 40.54500 22.82200 -10.81000 0.210 46.85000  ?  6   THR A CB  1 
ATOM   63   O  OG1 A THR A 1 6   ? 41.09700 21.15500 -11.07100 0.790 44.47000  ?  6   THR A OG1 1 
ATOM   64   O  OG1 B THR A 1 6   ? 41.06500 21.53600 -11.16900 0.210 44.78000  ?  6   THR A OG1 1 
ATOM   65   C  CG2 A THR A 1 6   ? 40.74400 23.34200 -12.03100 0.790 30.13000  ?  6   THR A CG2 1 
ATOM   66   C  CG2 B THR A 1 6   ? 40.83200 23.81900 -11.90000 0.210 34.72000  ?  6   THR A CG2 1 
ATOM   67   N  N   A LEU A 1 7   ? 38.83000 24.13100 -8.76400  0.790 40.23000  ?  7   LEU A N   1 
ATOM   68   N  N   B LEU A 1 7   ? 39.07000 24.38100 -8.82100  0.210 38.56000  ?  7   LEU A N   1 
ATOM   69   C  CA  A LEU A 1 7   ? 37.99400 25.28900 -8.47100  0.790 35.45000  ?  7   LEU A CA  1 
ATOM   70   C  CA  B LEU A 1 7   ? 38.22800 25.48900 -8.40000  0.210 36.64000  ?  7   LEU A CA  1 
ATOM   71   C  C   A LEU A 1 7   ? 38.59100 26.12600 -7.34800  0.790 36.19000  ?  7   LEU A C   1 
ATOM   72   C  C   B LEU A 1 7   ? 38.82700 26.22900 -7.20400  0.210 35.57000  ?  7   LEU A C   1 
ATOM   73   O  O   A LEU A 1 7   ? 38.56100 27.36100 -7.40300  0.790 36.49000  ?  7   LEU A O   1 
ATOM   74   O  O   B LEU A 1 7   ? 38.94400 27.45900 -7.21000  0.210 33.21000  ?  7   LEU A O   1 
ATOM   75   C  CB  A LEU A 1 7   ? 36.58100 24.82900 -8.11300  0.790 31.45000  ?  7   LEU A CB  1 
ATOM   76   C  CB  B LEU A 1 7   ? 36.84700 24.96300 -8.08000  0.210 31.64000  ?  7   LEU A CB  1 
ATOM   77   C  CG  A LEU A 1 7   ? 35.81200 24.19300 -9.27100  0.790 37.70000  ?  7   LEU A CG  1 
ATOM   78   C  CG  B LEU A 1 7   ? 36.29600 24.24000 -9.31600  0.210 37.68000  ?  7   LEU A CG  1 
ATOM   79   C  CD1 A LEU A 1 7   ? 34.49900 23.59500 -8.81400  0.790 28.74000  ?  7   LEU A CD1 1 
ATOM   80   C  CD1 B LEU A 1 7   ? 34.92800 23.66000 -8.98300  0.210 32.96000  ?  7   LEU A CD1 1 
ATOM   81   C  CD2 A LEU A 1 7   ? 35.58100 25.23200 -10.36600 0.790 30.48000  ?  7   LEU A CD2 1 
ATOM   82   C  CD2 B LEU A 1 7   ? 36.29500 25.08900 -10.62000 0.210 30.78000  ?  7   LEU A CD2 1 
ATOM   83   N  N   A PHE A 1 8   ? 39.14100 25.47200 -6.32200  0.790 29.68000  ?  8   PHE A N   1 
ATOM   84   N  N   B PHE A 1 8   ? 39.23300 25.51800 -6.17200  0.210 30.58000  ?  8   PHE A N   1 
ATOM   85   C  CA  A PHE A 1 8   ? 39.78400 26.21100 -5.24200  0.790 38.96000  ?  8   PHE A CA  1 
ATOM   86   C  CA  B PHE A 1 8   ? 39.78800 26.31400 -5.08300  0.210 38.60000  ?  8   PHE A CA  1 
ATOM   87   C  C   A PHE A 1 8   ? 40.99300 26.98900 -5.75600  0.790 37.85000  ?  8   PHE A C   1 
ATOM   88   C  C   B PHE A 1 8   ? 41.01300 27.10800 -5.54300  0.210 37.37000  ?  8   PHE A C   1 
ATOM   89   O  O   A PHE A 1 8   ? 41.18100 28.15900 -5.40200  0.790 37.99000  ?  8   PHE A O   1 
ATOM   90   O  O   B PHE A 1 8   ? 41.18700 28.27900 -5.15400  0.210 35.89000  ?  8   PHE A O   1 
ATOM   91   C  CB  A PHE A 1 8   ? 40.17800 25.25300 -4.11500  0.790 36.46000  ?  8   PHE A CB  1 
ATOM   92   C  CB  B PHE A 1 8   ? 40.07300 25.40400 -3.91300  0.210 36.60000  ?  8   PHE A CB  1 
ATOM   93   C  CG  A PHE A 1 8   ? 39.00100 24.72000 -3.32800  0.790 41.71000  ?  8   PHE A CG  1 
ATOM   94   C  CG  B PHE A 1 8   ? 38.84300 24.79400 -3.35200  0.210 41.26000  ?  8   PHE A CG  1 
ATOM   95   C  CD1 A PHE A 1 8   ? 37.92600 25.53900 -3.01300  0.790 38.90000  ?  8   PHE A CD1 1 
ATOM   96   C  CD1 B PHE A 1 8   ? 37.72500 25.57800 -3.14600  0.210 38.82000  ?  8   PHE A CD1 1 
ATOM   97   C  CD2 A PHE A 1 8   ? 38.97200 23.39900 -2.90500  0.790 43.99000  ?  8   PHE A CD2 1 
ATOM   98   C  CD2 B PHE A 1 8   ? 38.78600 23.46100 -3.03600  0.210 43.09000  ?  8   PHE A CD2 1 
ATOM   99   C  CE1 A PHE A 1 8   ? 36.84600 25.05400 -2.29600  0.790 29.13000  ?  8   PHE A CE1 1 
ATOM   100  C  CE1 B PHE A 1 8   ? 36.59100 25.06100 -2.61600  0.210 33.65000  ?  8   PHE A CE1 1 
ATOM   101  C  CE2 A PHE A 1 8   ? 37.89300 22.90900 -2.18500  0.790 33.88000  ?  8   PHE A CE2 1 
ATOM   102  C  CE2 B PHE A 1 8   ? 37.62600 22.92700 -2.50300  0.210 37.08000  ?  8   PHE A CE2 1 
ATOM   103  C  CZ  A PHE A 1 8   ? 36.82900 23.74000 -1.88100  0.790 33.20000  ?  8   PHE A CZ  1 
ATOM   104  C  CZ  B PHE A 1 8   ? 36.52700 23.73400 -2.31600  0.210 35.02000  ?  8   PHE A CZ  1 
ATOM   105  N  N   A TRP A 1 9   ? 41.81400 26.36900 -6.61000  0.790 38.66000  ?  9   TRP A N   1 
ATOM   106  N  N   B TRP A 1 9   ? 41.79000 26.53500 -6.46200  0.210 37.68000  ?  9   TRP A N   1 
ATOM   107  C  CA  A TRP A 1 9   ? 42.96100 27.08700 -7.15900  0.790 33.21000  ?  9   TRP A CA  1 
ATOM   108  C  CA  B TRP A 1 9   ? 42.95800 27.22100 -6.98000  0.210 34.26000  ?  9   TRP A CA  1 
ATOM   109  C  C   A TRP A 1 9   ? 42.51000 28.30600 -7.95500  0.790 31.43000  ?  9   TRP A C   1 
ATOM   110  C  C   B TRP A 1 9   ? 42.59200 28.43600 -7.82000  0.210 31.90000  ?  9   TRP A C   1 
ATOM   111  O  O   A TRP A 1 9   ? 43.13600 29.37000 -7.88200  0.790 29.03000  ?  9   TRP A O   1 
ATOM   112  O  O   B TRP A 1 9   ? 43.21700 29.51200 -7.70200  0.210 28.12000  ?  9   TRP A O   1 
ATOM   113  C  CB  A TRP A 1 9   ? 43.80800 26.15400 -8.02700  0.790 36.28000  ?  9   TRP A CB  1 
ATOM   114  C  CB  B TRP A 1 9   ? 43.77000 26.26800 -7.81800  0.210 36.21000  ?  9   TRP A CB  1 
ATOM   115  C  CG  A TRP A 1 9   ? 44.73200 25.28100 -7.22600  0.790 41.53000  ?  9   TRP A CG  1 
ATOM   116  C  CG  B TRP A 1 9   ? 44.71200 25.51700 -7.04900  0.210 40.17000  ?  9   TRP A CG  1 
ATOM   117  C  CD1 A TRP A 1 9   ? 44.70800 23.91800 -7.14700  0.790 41.04000  ?  9   TRP A CD1 1 
ATOM   118  C  CD1 B TRP A 1 9   ? 44.83800 24.16700 -7.04200  0.210 40.60000  ?  9   TRP A CD1 1 
ATOM   119  C  CD2 A TRP A 1 9   ? 45.81500 25.71100 -6.38500  0.790 34.96000  ?  9   TRP A CD2 1 
ATOM   120  C  CD2 B TRP A 1 9   ? 45.68000 26.02000 -6.14600  0.210 37.55000  ?  9   TRP A CD2 1 
ATOM   121  N  NE1 A TRP A 1 9   ? 45.70600 23.47300 -6.31200  0.790 44.75000  ?  9   TRP A NE1 1 
ATOM   122  N  NE1 B TRP A 1 9   ? 45.82500 23.79000 -6.19400  0.210 42.50000  ?  9   TRP A NE1 1 
ATOM   123  C  CE2 A TRP A 1 9   ? 46.40000 24.55300 -5.83300  0.790 35.76000  ?  9   TRP A CE2 1 
ATOM   124  C  CE2 B TRP A 1 9   ? 46.36300 24.90800 -5.62000  0.210 35.76000  ?  9   TRP A CE2 1 
ATOM   125  C  CE3 A TRP A 1 9   ? 46.34500 26.96100 -6.04600  0.790 41.52000  ?  9   TRP A CE3 1 
ATOM   126  C  CE3 B TRP A 1 9   ? 46.04500 27.29500 -5.73100  0.210 40.18000  ?  9   TRP A CE3 1 
ATOM   127  C  CZ2 A TRP A 1 9   ? 47.48500 24.60700 -4.96000  0.790 39.57000  ?  9   TRP A CZ2 1 
ATOM   128  C  CZ2 B TRP A 1 9   ? 47.39800 25.02300 -4.70900  0.210 43.23000  ?  9   TRP A CZ2 1 
ATOM   129  C  CZ3 A TRP A 1 9   ? 47.42400 27.01200 -5.18000  0.790 48.64000  ?  9   TRP A CZ3 1 
ATOM   130  C  CZ3 B TRP A 1 9   ? 47.06900 27.41700 -4.80500  0.210 46.62000  ?  9   TRP A CZ3 1 
ATOM   131  C  CH2 A TRP A 1 9   ? 47.98200 25.84300 -4.64700  0.790 46.92000  ?  9   TRP A CH2 1 
ATOM   132  C  CH2 B TRP A 1 9   ? 47.73600 26.28100 -4.30100  0.210 46.90000  ?  9   TRP A CH2 1 
ATOM   133  N  N   A LEU A 1 10  ? 41.41800 28.17500 -8.71200  0.790 33.28000  ?  10  LEU A N   1 
ATOM   134  N  N   B LEU A 1 10  ? 41.65700 28.25400 -8.75000  0.210 33.24000  ?  10  LEU A N   1 
ATOM   135  C  CA  A LEU A 1 10  ? 40.90800 29.30700 -9.48100  0.790 28.53000  ?  10  LEU A CA  1 
ATOM   136  C  CA  B LEU A 1 10  ? 41.15900 29.42400 -9.45200  0.210 29.58000  ?  10  LEU A CA  1 
ATOM   137  C  C   A LEU A 1 10  ? 40.53300 30.46300 -8.56500  0.790 31.36000  ?  10  LEU A C   1 
ATOM   138  C  C   B LEU A 1 10  ? 40.84700 30.47600 -8.43400  0.210 32.05000  ?  10  LEU A C   1 
ATOM   139  O  O   A LEU A 1 10  ? 40.84000 31.62700 -8.85000  0.790 27.78000  ?  10  LEU A O   1 
ATOM   140  O  O   B LEU A 1 10  ? 41.37800 31.59800 -8.49300  0.210 31.45000  ?  10  LEU A O   1 
ATOM   141  C  CB  A LEU A 1 10  ? 39.69600 28.87900 -10.30600 0.790 29.03000  ?  10  LEU A CB  1 
ATOM   142  C  CB  B LEU A 1 10  ? 39.91200 29.10600 -10.27900 0.210 31.04000  ?  10  LEU A CB  1 
ATOM   143  C  CG  A LEU A 1 10  ? 39.96600 27.93000 -11.46900 0.790 48.99000  ?  10  LEU A CG  1 
ATOM   144  C  CG  B LEU A 1 10  ? 40.15700 28.38100 -11.58300 0.210 45.76000  ?  10  LEU A CG  1 
ATOM   145  C  CD1 A LEU A 1 10  ? 38.67100 27.44600 -12.09100 0.790 49.03000  ?  10  LEU A CD1 1 
ATOM   146  C  CD1 B LEU A 1 10  ? 38.84000 27.94900 -12.13900 0.210 45.87000  ?  10  LEU A CD1 1 
ATOM   147  C  CD2 A LEU A 1 10  ? 40.84500 28.62000 -12.50400 0.790 42.62000  ?  10  LEU A CD2 1 
ATOM   148  C  CD2 B LEU A 1 10  ? 40.89700 29.26300 -12.61600 0.210 39.59000  ?  10  LEU A CD2 1 
ATOM   149  N  N   A GLY A 1 11  ? 39.84100 30.16100 -7.46600  0.790 33.95000  ?  11  GLY A N   1 
ATOM   150  N  N   B GLY A 1 11  ? 40.03400 30.07400 -7.44300  0.210 33.60000  ?  11  GLY A N   1 
ATOM   151  C  CA  A GLY A 1 11  ? 39.52000 31.20200 -6.50700  0.790 32.20000  ?  11  GLY A CA  1 
ATOM   152  C  CA  B GLY A 1 11  ? 39.73300 30.80600 -6.23300  0.210 31.59000  ?  11  GLY A CA  1 
ATOM   153  C  C   A GLY A 1 11  ? 40.76300 31.81400 -5.89600  0.790 30.29000  ?  11  GLY A C   1 
ATOM   154  C  C   B GLY A 1 11  ? 40.94700 31.58000 -5.82300  0.210 29.54000  ?  11  GLY A C   1 
ATOM   155  O  O   A GLY A 1 11  ? 40.84700 33.03200 -5.72400  0.790 32.54000  ?  11  GLY A O   1 
ATOM   156  O  O   B GLY A 1 11  ? 40.93400 32.83400 -5.87000  0.210 32.80000  ?  11  GLY A O   1 
ATOM   157  N  N   A ALA A 1 12  ? 41.75400 30.97800 -5.57800  0.790 27.36000  ?  12  ALA A N   1 
ATOM   158  N  N   B ALA A 1 12  ? 42.02700 30.83000 -5.53700  0.210 26.47000  ?  12  ALA A N   1 
ATOM   159  C  CA  A ALA A 1 12  ? 43.01500 31.48500 -5.05000  0.790 35.30000  ?  12  ALA A CA  1 
ATOM   160  C  CA  B ALA A 1 12  ? 43.25000 31.45700 -5.03200  0.210 34.39000  ?  12  ALA A CA  1 
ATOM   161  C  C   A ALA A 1 12  ? 43.65400 32.47300 -6.01700  0.790 34.47000  ?  12  ALA A C   1 
ATOM   162  C  C   B ALA A 1 12  ? 43.70800 32.55000 -5.97300  0.210 34.14000  ?  12  ALA A C   1 
ATOM   163  O  O   A ALA A 1 12  ? 44.07200 33.56700 -5.61900  0.790 34.94000  ?  12  ALA A O   1 
ATOM   164  O  O   B ALA A 1 12  ? 43.93300 33.69300 -5.54100  0.210 33.81000  ?  12  ALA A O   1 
ATOM   165  C  CB  A ALA A 1 12  ? 43.96300 30.32000 -4.76800  0.790 38.53000  ?  12  ALA A CB  1 
ATOM   166  C  CB  B ALA A 1 12  ? 44.33900 30.39500 -4.82700  0.210 36.36000  ?  12  ALA A CB  1 
ATOM   167  N  N   A ILE A 1 13  ? 43.73400 32.10500 -7.29800  0.790 34.41000  ?  13  ILE A N   1 
ATOM   168  N  N   B ILE A 1 13  ? 43.75000 32.22700 -7.28200  0.210 34.26000  ?  13  ILE A N   1 
ATOM   169  C  CA  A ILE A 1 13  ? 44.37300 32.97700 -8.28200  0.790 39.06000  ?  13  ILE A CA  1 
ATOM   170  C  CA  B ILE A 1 13  ? 44.28600 33.12900 -8.30200  0.210 35.84000  ?  13  ILE A CA  1 
ATOM   171  C  C   A ILE A 1 13  ? 43.60500 34.28400 -8.40300  0.790 30.90000  ?  13  ILE A C   1 
ATOM   172  C  C   B ILE A 1 13  ? 43.55800 34.44600 -8.28500  0.210 30.50000  ?  13  ILE A C   1 
ATOM   173  O  O   A ILE A 1 13  ? 44.19100 35.37200 -8.45700  0.790 34.51000  ?  13  ILE A O   1 
ATOM   174  O  O   B ILE A 1 13  ? 44.18000 35.51400 -8.19700  0.210 34.22000  ?  13  ILE A O   1 
ATOM   175  C  CB  A ILE A 1 13  ? 44.47400 32.27300 -9.64600  0.790 26.77000  ?  13  ILE A CB  1 
ATOM   176  C  CB  B ILE A 1 13  ? 44.18900 32.51600 -9.71100  0.210 28.20000  ?  13  ILE A CB  1 
ATOM   177  C  CG1 A ILE A 1 13  ? 45.46900 31.11600 -9.59400  0.790 30.48000  ?  13  ILE A CG1 1 
ATOM   178  C  CG1 B ILE A 1 13  ? 45.09600 31.33000 -9.82400  0.210 30.48000  ?  13  ILE A CG1 1 
ATOM   179  C  CG2 A ILE A 1 13  ? 44.88200 33.27700 -10.72100 0.790 28.61000  ?  13  ILE A CG2 1 
ATOM   180  C  CG2 B ILE A 1 13  ? 44.56400 33.54200 -10.68300 0.210 28.61000  ?  13  ILE A CG2 1 
ATOM   181  C  CD1 A ILE A 1 13  ? 45.26300 30.10300 -10.69500 0.790 42.04000  ?  13  ILE A CD1 1 
ATOM   182  C  CD1 B ILE A 1 13  ? 44.70700 30.44500 -10.93400 0.210 40.15000  ?  13  ILE A CD1 1 
ATOM   183  N  N   A GLY A 1 14  ? 42.27700 34.19200 -8.47400  0.790 27.09000  ?  14  GLY A N   1 
ATOM   184  N  N   B GLY A 1 14  ? 42.23200 34.38700 -8.44000  0.210 26.58000  ?  14  GLY A N   1 
ATOM   185  C  CA  A GLY A 1 14  ? 41.47000 35.39200 -8.57200  0.790 16.78000  ?  14  GLY A CA  1 
ATOM   186  C  CA  B GLY A 1 14  ? 41.43600 35.59800 -8.52700  0.210 16.78000  ?  14  GLY A CA  1 
ATOM   187  C  C   A GLY A 1 14  ? 41.64800 36.31200 -7.38300  0.790 30.13000  ?  14  GLY A C   1 
ATOM   188  C  C   B GLY A 1 14  ? 41.49100 36.41300 -7.25700  0.210 30.50000  ?  14  GLY A C   1 
ATOM   189  O  O   A GLY A 1 14  ? 41.73700 37.53100 -7.53900  0.790 29.86000  ?  14  GLY A O   1 
ATOM   190  O  O   B GLY A 1 14  ? 41.37600 37.63900 -7.29600  0.210 29.50000  ?  14  GLY A O   1 
ATOM   191  N  N   A MET A 1 15  ? 41.69000 35.74800 -6.17500  0.790 29.26000  ?  15  MET A N   1 
ATOM   192  N  N   B MET A 1 15  ? 41.66100 35.75100 -6.10600  0.210 28.23000  ?  15  MET A N   1 
ATOM   193  C  CA  A MET A 1 15  ? 41.88600 36.59000 -5.00200  0.790 37.09000  ?  15  MET A CA  1 
ATOM   194  C  CA  B MET A 1 15  ? 41.84300 36.52900 -4.89100  0.210 36.85000  ?  15  MET A CA  1 
ATOM   195  C  C   A MET A 1 15  ? 43.28000 37.20500 -5.00200  0.790 40.87000  ?  15  MET A C   1 
ATOM   196  C  C   B MET A 1 15  ? 43.25300 37.15000 -4.86600  0.210 40.31000  ?  15  MET A C   1 
ATOM   197  O  O   A MET A 1 15  ? 43.44700 38.37500 -4.64000  0.790 36.16000  ?  15  MET A O   1 
ATOM   198  O  O   B MET A 1 15  ? 43.45000 38.27300 -4.37600  0.210 37.23000  ?  15  MET A O   1 
ATOM   199  C  CB  A MET A 1 15  ? 41.63500 35.77900 -3.73300  0.790 29.29000  ?  15  MET A CB  1 
ATOM   200  C  CB  B MET A 1 15  ? 41.52900 35.63300 -3.68400  0.210 29.50000  ?  15  MET A CB  1 
ATOM   201  C  CG  A MET A 1 15  ? 40.19000 35.27700 -3.61300  0.790 32.95000  ?  15  MET A CG  1 
ATOM   202  C  CG  B MET A 1 15  ? 40.09200 34.94500 -3.64000  0.210 30.60000  ?  15  MET A CG  1 
ATOM   203  S  SD  A MET A 1 15  ? 38.98900 36.62000 -3.46600  0.790 33.15000  ?  15  MET A SD  1 
ATOM   204  S  SD  B MET A 1 15  ? 38.70400 36.08600 -3.61700  0.210 34.50000  ?  15  MET A SD  1 
ATOM   205  C  CE  A MET A 1 15  ? 37.44100 35.72900 -3.50800  0.790 40.08000  ?  15  MET A CE  1 
ATOM   206  C  CE  B MET A 1 15  ? 37.33000 34.96700 -3.49200  0.210 40.79000  ?  15  MET A CE  1 
ATOM   207  N  N   A LEU A 1 16  ? 44.28800 36.44700 -5.44000  0.790 38.33000  ?  16  LEU A N   1 
ATOM   208  N  N   B LEU A 1 16  ? 44.23900 36.44500 -5.42500  0.210 38.39000  ?  16  LEU A N   1 
ATOM   209  C  CA  A LEU A 1 16  ? 45.65200 36.96700 -5.46300  0.790 38.83000  ?  16  LEU A CA  1 
ATOM   210  C  CA  B LEU A 1 16  ? 45.56200 37.03500 -5.57500  0.210 38.71000  ?  16  LEU A CA  1 
ATOM   211  C  C   A LEU A 1 16  ? 45.77300 38.15600 -6.41000  0.790 39.96000  ?  16  LEU A C   1 
ATOM   212  C  C   B LEU A 1 16  ? 45.49700 38.27700 -6.42900  0.210 39.76000  ?  16  LEU A C   1 
ATOM   213  O  O   A LEU A 1 16  ? 46.37500 39.18000 -6.06800  0.790 38.86000  ?  16  LEU A O   1 
ATOM   214  O  O   B LEU A 1 16  ? 45.73500 39.39000 -5.95000  0.210 38.59000  ?  16  LEU A O   1 
ATOM   215  C  CB  A LEU A 1 16  ? 46.62500 35.85900 -5.86900  0.790 35.95000  ?  16  LEU A CB  1 
ATOM   216  C  CB  B LEU A 1 16  ? 46.51600 36.04900 -6.20600  0.210 35.95000  ?  16  LEU A CB  1 
ATOM   217  C  CG  A LEU A 1 16  ? 46.98700 34.86100 -4.76800  0.790 60.61000  ?  16  LEU A CG  1 
ATOM   218  C  CG  B LEU A 1 16  ? 46.94100 35.37100 -4.93900  0.210 53.85000  ?  16  LEU A CG  1 
ATOM   219  C  CD1 A LEU A 1 16  ? 47.11100 33.44600 -5.31200  0.790 63.89000  ?  16  LEU A CD1 1 
ATOM   220  C  CD1 B LEU A 1 16  ? 47.43500 33.91100 -5.12800  0.210 59.10000  ?  16  LEU A CD1 1 
ATOM   221  C  CD2 A LEU A 1 16  ? 48.27300 35.28000 -4.06400  0.790 76.38000  ?  16  LEU A CD2 1 
ATOM   222  C  CD2 B LEU A 1 16  ? 47.91600 36.29100 -4.16400  0.210 58.30000  ?  16  LEU A CD2 1 
ATOM   223  N  N   A VAL A 1 17  ? 45.20800 38.03500 -7.61300  0.790 35.06000  ?  17  VAL A N   1 
ATOM   224  N  N   B VAL A 1 17  ? 45.15300 38.09600 -7.71000  0.210 36.33000  ?  17  VAL A N   1 
ATOM   225  C  CA  A VAL A 1 17  ? 45.26400 39.13300 -8.57500  0.790 36.95000  ?  17  VAL A CA  1 
ATOM   226  C  CA  B VAL A 1 17  ? 45.12000 39.23800 -8.61300  0.210 36.89000  ?  17  VAL A CA  1 
ATOM   227  C  C   A VAL A 1 17  ? 44.59000 40.37000 -7.99700  0.790 36.66000  ?  17  VAL A C   1 
ATOM   228  C  C   B VAL A 1 17  ? 44.36400 40.37500 -7.96300  0.210 36.75000  ?  17  VAL A C   1 
ATOM   229  O  O   A VAL A 1 17  ? 45.11000 41.48900 -8.09700  0.790 34.97000  ?  17  VAL A O   1 
ATOM   230  O  O   B VAL A 1 17  ? 44.86000 41.51400 -7.89400  0.210 34.76000  ?  17  VAL A O   1 
ATOM   231  C  CB  A VAL A 1 17  ? 44.61500 38.71300 -9.90600  0.790 44.86000  ?  17  VAL A CB  1 
ATOM   232  C  CB  B VAL A 1 17  ? 44.50400 38.84700 -9.96700  0.210 43.74000  ?  17  VAL A CB  1 
ATOM   233  C  CG1 A VAL A 1 17  ? 44.42900 39.92900 -10.80800 0.790 41.82000  ?  17  VAL A CG1 1 
ATOM   234  C  CG1 B VAL A 1 17  ? 44.06500 40.07500 -10.70600 0.210 40.84000  ?  17  VAL A CG1 1 
ATOM   235  C  CG2 A VAL A 1 17  ? 45.44900 37.65200 -10.60100 0.790 28.44000  ?  17  VAL A CG2 1 
ATOM   236  C  CG2 B VAL A 1 17  ? 45.51300 38.07800 -10.81800 0.210 28.90000  ?  17  VAL A CG2 1 
ATOM   237  N  N   A GLY A 1 18  ? 43.41700 40.18900 -7.38900  0.790 35.49000  ?  18  GLY A N   1 
ATOM   238  N  N   B GLY A 1 18  ? 43.17800 40.05900 -7.40500  0.210 34.35000  ?  18  GLY A N   1 
ATOM   239  C  CA  A GLY A 1 18  ? 42.77000 41.30600 -6.72400  0.790 35.25000  ?  18  GLY A CA  1 
ATOM   240  C  CA  B GLY A 1 18  ? 42.49400 41.02400 -6.57700  0.210 35.72000  ?  18  GLY A CA  1 
ATOM   241  C  C   A GLY A 1 18  ? 43.65300 41.91500 -5.65400  0.790 40.08000  ?  18  GLY A C   1 
ATOM   242  C  C   B GLY A 1 18  ? 43.43500 41.79100 -5.66400  0.210 39.58000  ?  18  GLY A C   1 
ATOM   243  O  O   A GLY A 1 18  ? 43.79900 43.13600 -5.57000  0.790 37.54000  ?  18  GLY A O   1 
ATOM   244  O  O   B GLY A 1 18  ? 43.56900 43.00400 -5.81000  0.210 36.42000  ?  18  GLY A O   1 
ATOM   245  N  N   A THR A 1 19  ? 44.27400 41.06300 -4.83700  0.790 32.97000  ?  19  THR A N   1 
ATOM   246  N  N   B THR A 1 19  ? 44.18400 41.06700 -4.82300  0.210 32.81000  ?  19  THR A N   1 
ATOM   247  C  CA  A THR A 1 19  ? 45.10100 41.54500 -3.73600  0.790 40.21000  ?  19  THR A CA  1 
ATOM   248  C  CA  B THR A 1 19  ? 44.93000 41.67000 -3.71600  0.210 40.49000  ?  19  THR A CA  1 
ATOM   249  C  C   A THR A 1 19  ? 46.23800 42.42600 -4.24200  0.790 44.51000  ?  19  THR A C   1 
ATOM   250  C  C   B THR A 1 19  ? 46.03400 42.61500 -4.19000  0.210 44.45000  ?  19  THR A C   1 
ATOM   251  O  O   A THR A 1 19  ? 46.47100 43.52200 -3.71800  0.790 52.33000  ?  19  THR A O   1 
ATOM   252  O  O   B THR A 1 19  ? 46.04800 43.80500 -3.86300  0.210 48.85000  ?  19  THR A O   1 
ATOM   253  C  CB  A THR A 1 19  ? 45.66100 40.35900 -2.94900  0.790 39.05000  ?  19  THR A CB  1 
ATOM   254  C  CB  B THR A 1 19  ? 45.54700 40.57300 -2.86100  0.210 39.79000  ?  19  THR A CB  1 
ATOM   255  O  OG1 A THR A 1 19  ? 44.59000 39.61300 -2.35700  0.790 44.74000  ?  19  THR A OG1 1 
ATOM   256  O  OG1 B THR A 1 19  ? 44.58400 39.52500 -2.62100  0.210 41.03000  ?  19  THR A OG1 1 
ATOM   257  C  CG2 A THR A 1 19  ? 46.60900 40.84300 -1.86000  0.790 51.40000  ?  19  THR A CG2 1 
ATOM   258  C  CG2 B THR A 1 19  ? 45.94600 41.18500 -1.60300  0.210 46.85000  ?  19  THR A CG2 1 
ATOM   259  N  N   A LEU A 1 20  ? 46.96900 41.95500 -5.25500  0.790 44.25000  ?  20  LEU A N   1 
ATOM   260  N  N   B LEU A 1 20  ? 47.02500 42.07100 -4.87900  0.210 42.95000  ?  20  LEU A N   1 
ATOM   261  C  CA  A LEU A 1 20  ? 48.08500 42.73500 -5.78000  0.790 51.39000  ?  20  LEU A CA  1 
ATOM   262  C  CA  B LEU A 1 20  ? 47.94300 42.88800 -5.66500  0.210 50.64000  ?  20  LEU A CA  1 
ATOM   263  C  C   A LEU A 1 20  ? 47.59800 44.02700 -6.42100  0.790 56.99000  ?  20  LEU A C   1 
ATOM   264  C  C   B LEU A 1 20  ? 47.25800 44.09600 -6.32300  0.210 54.25000  ?  20  LEU A C   1 
ATOM   265  O  O   A LEU A 1 20  ? 48.24500 45.07400 -6.29700  0.790 54.96000  ?  20  LEU A O   1 
ATOM   266  O  O   B LEU A 1 20  ? 47.58500 45.23800 -6.00000  0.210 55.57000  ?  20  LEU A O   1 
ATOM   267  C  CB  A LEU A 1 20  ? 48.87200 41.90400 -6.79000  0.790 49.36000  ?  20  LEU A CB  1 
ATOM   268  C  CB  B LEU A 1 20  ? 48.63000 42.03000 -6.73600  0.210 49.35000  ?  20  LEU A CB  1 
ATOM   269  C  CG  A LEU A 1 20  ? 49.45800 40.59500 -6.26300  0.790 45.04000  ?  20  LEU A CG  1 
ATOM   270  C  CG  B LEU A 1 20  ? 49.50400 40.90200 -6.18500  0.210 47.01000  ?  20  LEU A CG  1 
ATOM   271  C  CD1 A LEU A 1 20  ? 50.16200 39.83700 -7.38000  0.790 51.65000  ?  20  LEU A CD1 1 
ATOM   272  C  CD1 B LEU A 1 20  ? 50.33400 40.22300 -7.28300  0.210 51.47000  ?  20  LEU A CD1 1 
ATOM   273  C  CD2 A LEU A 1 20  ? 50.41000 40.86100 -5.10900  0.790 60.26000  ?  20  LEU A CD2 1 
ATOM   274  C  CD2 B LEU A 1 20  ? 50.35800 41.44500 -5.06500  0.210 58.27000  ?  20  LEU A CD2 1 
ATOM   275  N  N   A ALA A 1 21  ? 46.46100 43.97200 -7.11700  0.790 51.87000  ?  21  ALA A N   1 
ATOM   276  N  N   B ALA A 1 21  ? 46.34800 43.87400 -7.29100  0.210 50.08000  ?  21  ALA A N   1 
ATOM   277  C  CA  A ALA A 1 21  ? 45.91400 45.17700 -7.73200  0.790 40.87000  ?  21  ALA A CA  1 
ATOM   278  C  CA  B ALA A 1 21  ? 45.76800 45.01600 -8.01600  0.210 41.90000  ?  21  ALA A CA  1 
ATOM   279  C  C   A ALA A 1 21  ? 45.58600 46.22500 -6.67600  0.790 46.92000  ?  21  ALA A C   1 
ATOM   280  C  C   B ALA A 1 21  ? 45.29200 46.11300 -7.06600  0.210 46.34000  ?  21  ALA A C   1 
ATOM   281  O  O   A ALA A 1 21  ? 45.93000 47.40300 -6.82500  0.790 43.66000  ?  21  ALA A O   1 
ATOM   282  O  O   B ALA A 1 21  ? 45.58600 47.29800 -7.26000  0.210 46.65000  ?  21  ALA A O   1 
ATOM   283  C  CB  A ALA A 1 21  ? 44.67100 44.83100 -8.55200  0.790 31.18000  ?  21  ALA A CB  1 
ATOM   284  C  CB  B ALA A 1 21  ? 44.61100 44.57800 -8.91400  0.210 35.06000  ?  21  ALA A CB  1 
ATOM   285  N  N   A PHE A 1 22  ? 44.91500 45.81400 -5.59500  0.790 47.72000  ?  22  PHE A N   1 
ATOM   286  N  N   B PHE A 1 22  ? 44.57100 45.74400 -6.01500  0.210 48.04000  ?  22  PHE A N   1 
ATOM   287  C  CA  A PHE A 1 22  ? 44.55000 46.77200 -4.55600  0.790 49.09000  ?  22  PHE A CA  1 
ATOM   288  C  CA  B PHE A 1 22  ? 44.23700 46.75400 -5.02500  0.210 48.06000  ?  22  PHE A CA  1 
ATOM   289  C  C   A PHE A 1 22  ? 45.79000 47.31900 -3.85400  0.790 52.79000  ?  22  PHE A C   1 
ATOM   290  C  C   B PHE A 1 22  ? 45.49300 47.26300 -4.34700  0.210 50.89000  ?  22  PHE A C   1 
ATOM   291  O  O   A PHE A 1 22  ? 45.87300 48.52300 -3.58500  0.790 49.64000  ?  22  PHE A O   1 
ATOM   292  O  O   B PHE A 1 22  ? 45.62400 48.47300 -4.12300  0.210 51.03000  ?  22  PHE A O   1 
ATOM   293  C  CB  A PHE A 1 22  ? 43.59500 46.13100 -3.54400  0.790 50.77000  ?  22  PHE A CB  1 
ATOM   294  C  CB  B PHE A 1 22  ? 43.23300 46.18800 -4.02700  0.210 50.10000  ?  22  PHE A CB  1 
ATOM   295  C  CG  A PHE A 1 22  ? 42.37300 45.50700 -4.16900  0.790 47.99000  ?  22  PHE A CG  1 
ATOM   296  C  CG  B PHE A 1 22  ? 41.99900 45.68100 -4.68400  0.210 44.17000  ?  22  PHE A CG  1 
ATOM   297  C  CD1 A PHE A 1 22  ? 41.72300 46.12400 -5.22900  0.790 41.47000  ?  22  PHE A CD1 1 
ATOM   298  C  CD1 B PHE A 1 22  ? 41.34400 46.46100 -5.61700  0.210 44.72000  ?  22  PHE A CD1 1 
ATOM   299  C  CD2 A PHE A 1 22  ? 41.87800 44.29900 -3.70100  0.790 41.52000  ?  22  PHE A CD2 1 
ATOM   300  C  CD2 B PHE A 1 22  ? 41.52600 44.40200 -4.41700  0.210 42.70000  ?  22  PHE A CD2 1 
ATOM   301  C  CE1 A PHE A 1 22  ? 40.60500 45.54900 -5.80700  0.790 45.86000  ?  22  PHE A CE1 1 
ATOM   302  C  CE1 B PHE A 1 22  ? 40.20300 45.99800 -6.25600  0.210 43.51000  ?  22  PHE A CE1 1 
ATOM   303  C  CE2 A PHE A 1 22  ? 40.76100 43.72000 -4.27600  0.790 40.04000  ?  22  PHE A CE2 1 
ATOM   304  C  CE2 B PHE A 1 22  ? 40.41200 43.91100 -5.05600  0.210 38.32000  ?  22  PHE A CE2 1 
ATOM   305  C  CZ  A PHE A 1 22  ? 40.12600 44.34500 -5.33100  0.790 41.08000  ?  22  PHE A CZ  1 
ATOM   306  C  CZ  B PHE A 1 22  ? 39.73800 44.71600 -5.97900  0.210 44.12000  ?  22  PHE A CZ  1 
ATOM   307  N  N   A ALA A 1 23  ? 46.76600 46.45700 -3.55600  0.790 51.95000  ?  23  ALA A N   1 
ATOM   308  N  N   B ALA A 1 23  ? 46.45400 46.36600 -4.07400  0.210 49.68000  ?  23  ALA A N   1 
ATOM   309  C  CA  A ALA A 1 23  ? 47.97800 46.92500 -2.88800  0.790 58.27000  ?  23  ALA A CA  1 
ATOM   310  C  CA  B ALA A 1 23  ? 47.67500 46.81800 -3.42000  0.210 54.46000  ?  23  ALA A CA  1 
ATOM   311  C  C   A ALA A 1 23  ? 48.69900 47.96000 -3.73900  0.790 66.04000  ?  23  ALA A C   1 
ATOM   312  C  C   B ALA A 1 23  ? 48.37900 47.88200 -4.25900  0.210 60.92000  ?  23  ALA A C   1 
ATOM   313  O  O   A ALA A 1 23  ? 49.19000 48.97500 -3.22400  0.790 69.71000  ?  23  ALA A O   1 
ATOM   314  O  O   B ALA A 1 23  ? 48.84000 48.90100 -3.72000  0.210 66.02000  ?  23  ALA A O   1 
ATOM   315  C  CB  A ALA A 1 23  ? 48.89900 45.74300 -2.58400  0.790 49.39000  ?  23  ALA A CB  1 
ATOM   316  C  CB  B ALA A 1 23  ? 48.59300 45.63500 -3.12100  0.210 52.71000  ?  23  ALA A CB  1 
ATOM   317  N  N   A TRP A 1 24  ? 48.76400 47.72200 -5.04900  0.790 54.10000  ?  24  TRP A N   1 
ATOM   318  N  N   B TRP A 1 24  ? 48.40000 47.71700 -5.58900  0.210 56.02000  ?  24  TRP A N   1 
ATOM   319  C  CA  A TRP A 1 24  ? 49.41500 48.66800 -5.94700  0.790 67.11000  ?  24  TRP A CA  1 
ATOM   320  C  CA  B TRP A 1 24  ? 49.10700 48.69900 -6.40600  0.210 64.85000  ?  24  TRP A CA  1 
ATOM   321  C  C   A TRP A 1 24  ? 48.71200 50.02000 -5.93600  0.790 65.88000  ?  24  TRP A C   1 
ATOM   322  C  C   B TRP A 1 24  ? 48.40200 50.04100 -6.39300  0.210 65.48000  ?  24  TRP A C   1 
ATOM   323  O  O   A TRP A 1 24  ? 49.34600 51.06500 -5.78100  0.790 75.72000  ?  24  TRP A O   1 
ATOM   324  O  O   B TRP A 1 24  ? 49.01300 51.07300 -6.10100  0.210 73.64000  ?  24  TRP A O   1 
ATOM   325  C  CB  A TRP A 1 24  ? 49.41600 48.12500 -7.36700  0.790 65.92000  ?  24  TRP A CB  1 
ATOM   326  C  CB  B TRP A 1 24  ? 49.28400 48.24900 -7.85500  0.210 66.06000  ?  24  TRP A CB  1 
ATOM   327  C  CG  A TRP A 1 24  ? 50.41600 48.79300 -8.22600  0.790 80.96000  ?  24  TRP A CG  1 
ATOM   328  C  CG  B TRP A 1 24  ? 50.35200 49.14800 -8.48500  0.210 80.73000  ?  24  TRP A CG  1 
ATOM   329  C  CD1 A TRP A 1 24  ? 50.19000 49.48300 -9.37600  0.790 84.83000  ?  24  TRP A CD1 1 
ATOM   330  C  CD1 B TRP A 1 24  ? 50.18900 50.11800 -9.46200  0.210 80.70000  ?  24  TRP A CD1 1 
ATOM   331  C  CD2 A TRP A 1 24  ? 51.82100 48.85500 -7.98800  0.790 95.85000  ?  24  TRP A CD2 1 
ATOM   332  C  CD2 B TRP A 1 24  ? 51.74100 49.20100 -8.10500  0.210 91.08000  ?  24  TRP A CD2 1 
ATOM   333  N  NE1 A TRP A 1 24  ? 51.37700 49.94700 -9.89000  0.790 85.94000  ?  24  TRP A NE1 1 
ATOM   334  N  NE1 B TRP A 1 24  ? 51.39900 50.73900 -9.72300  0.210 77.81000  ?  24  TRP A NE1 1 
ATOM   335  C  CE2 A TRP A 1 24  ? 52.39300 49.58500 -9.04500  0.790 92.50000  ?  24  TRP A CE2 1 
ATOM   336  C  CE2 B TRP A 1 24  ? 52.36500 50.19500 -8.90800  0.210 88.83000  ?  24  TRP A CE2 1 
ATOM   337  C  CE3 A TRP A 1 24  ? 52.65200 48.36300 -6.97900  0.790 100.90000 ?  24  TRP A CE3 1 
ATOM   338  C  CE3 B TRP A 1 24  ? 52.52300 48.49100 -7.16800  0.210 97.73000  ?  24  TRP A CE3 1 
ATOM   339  C  CZ2 A TRP A 1 24  ? 53.76000 49.83200 -9.12400  0.790 92.77000  ?  24  TRP A CZ2 1 
ATOM   340  C  CZ2 B TRP A 1 24  ? 53.74000 50.49300 -8.80000  0.210 91.12000  ?  24  TRP A CZ2 1 
ATOM   341  C  CZ3 A TRP A 1 24  ? 54.00700 48.60900 -7.05800  0.790 106.48000 ?  24  TRP A CZ3 1 
ATOM   342  C  CZ3 B TRP A 1 24  ? 53.89100 48.79100 -7.05900  0.210 103.90000 ?  24  TRP A CZ3 1 
ATOM   343  C  CH2 A TRP A 1 24  ? 54.54900 49.33600 -8.12300  0.790 104.84000 ?  24  TRP A CH2 1 
ATOM   344  C  CH2 B TRP A 1 24  ? 54.48200 49.78600 -7.87300  0.210 99.97000  ?  24  TRP A CH2 1 
ATOM   345  N  N   A ALA A 1 25  ? 47.39200 50.01700 -6.10900  0.790 58.70000  ?  25  ALA A N   1 
ATOM   346  N  N   B ALA A 1 25  ? 47.11700 50.04800 -6.71100  0.210 60.45000  ?  25  ALA A N   1 
ATOM   347  C  CA  A ALA A 1 25  ? 46.63900 51.26400 -6.13400  0.790 59.46000  ?  25  ALA A CA  1 
ATOM   348  C  CA  B ALA A 1 25  ? 46.40000 51.30300 -6.80300  0.210 60.37000  ?  25  ALA A CA  1 
ATOM   349  C  C   A ALA A 1 25  ? 46.74100 52.01200 -4.81700  0.790 66.47000  ?  25  ALA A C   1 
ATOM   350  C  C   B ALA A 1 25  ? 46.63700 52.19400 -5.59400  0.210 69.15000  ?  25  ALA A C   1 
ATOM   351  O  O   A ALA A 1 25  ? 46.56500 53.23300 -4.79400  0.790 82.77000  ?  25  ALA A O   1 
ATOM   352  O  O   B ALA A 1 25  ? 46.41100 53.40400 -5.67700  0.210 78.46000  ?  25  ALA A O   1 
ATOM   353  C  CB  A ALA A 1 25  ? 45.17300 50.97100 -6.46100  0.790 50.15000  ?  25  ALA A CB  1 
ATOM   354  C  CB  B ALA A 1 25  ? 44.92100 51.00900 -6.98600  0.210 50.19000  ?  25  ALA A CB  1 
ATOM   355  N  N   A GLY A 1 26  ? 47.01500 51.30900 -3.72200  0.790 67.30000  ?  26  GLY A N   1 
ATOM   356  N  N   B GLY A 1 26  ? 47.13600 51.63300 -4.49600  0.210 68.53000  ?  26  GLY A N   1 
ATOM   357  C  CA  A GLY A 1 26  ? 47.15100 51.95500 -2.43100  0.790 90.26000  ?  26  GLY A CA  1 
ATOM   358  C  CA  B GLY A 1 26  ? 47.19300 52.33600 -3.23300  0.210 85.32000  ?  26  GLY A CA  1 
ATOM   359  C  C   A GLY A 1 26  ? 48.48700 52.60700 -2.16400  0.790 109.01000 ?  26  GLY A C   1 
ATOM   360  C  C   B GLY A 1 26  ? 48.57900 52.63700 -2.70600  0.210 108.07000 ?  26  GLY A C   1 
ATOM   361  O  O   A GLY A 1 26  ? 48.60400 53.36200 -1.19400  0.790 119.61000 ?  26  GLY A O   1 
ATOM   362  O  O   B GLY A 1 26  ? 48.82300 52.62400 -1.48700  0.210 111.30000 ?  26  GLY A O   1 
ATOM   363  N  N   A GLU A 1 33  ? 43.14800 58.19900 2.79100   0.790 97.25000  ?  33  GLU A N   1 
ATOM   364  N  N   B GLU A 1 33  ? 43.44600 58.89800 2.38700   0.210 93.72000  ?  33  GLU A N   1 
ATOM   365  C  CA  A GLU A 1 33  ? 42.47600 57.18500 1.99000   0.790 76.38000  ?  33  GLU A CA  1 
ATOM   366  C  CA  B GLU A 1 33  ? 42.60300 57.97000 1.64000   0.210 78.66000  ?  33  GLU A CA  1 
ATOM   367  C  C   A GLU A 1 33  ? 43.17300 55.83200 2.06200   0.790 80.49000  ?  33  GLU A C   1 
ATOM   368  C  C   B GLU A 1 33  ? 43.09900 56.53100 1.73000   0.210 80.86000  ?  33  GLU A C   1 
ATOM   369  O  O   A GLU A 1 33  ? 42.64600 54.85200 1.52500   0.790 73.90000  ?  33  GLU A O   1 
ATOM   370  O  O   B GLU A 1 33  ? 42.49200 55.64900 1.11600   0.210 79.07000  ?  33  GLU A O   1 
ATOM   371  C  CB  A GLU A 1 33  ? 42.38400 57.64200 0.53200   0.790 67.65000  ?  33  GLU A CB  1 
ATOM   372  C  CB  B GLU A 1 33  ? 42.51800 58.40000 0.17800   0.210 70.70000  ?  33  GLU A CB  1 
ATOM   373  N  N   A ARG A 1 34  ? 44.34400 55.76300 2.70100   0.790 89.79000  ?  34  ARG A N   1 
ATOM   374  N  N   B ARG A 1 34  ? 44.18000 56.28200 2.48000   0.210 87.71000  ?  34  ARG A N   1 
ATOM   375  C  CA  A ARG A 1 34  ? 45.02700 54.48700 2.88300   0.790 90.05000  ?  34  ARG A CA  1 
ATOM   376  C  CA  B ARG A 1 34  ? 44.82500 54.97000 2.52600   0.210 87.42000  ?  34  ARG A CA  1 
ATOM   377  C  C   A ARG A 1 34  ? 44.11200 53.44500 3.51100   0.790 75.26000  ?  34  ARG A C   1 
ATOM   378  C  C   B ARG A 1 34  ? 43.88700 53.88800 3.09100   0.210 77.33000  ?  34  ARG A C   1 
ATOM   379  O  O   A ARG A 1 34  ? 44.22600 52.25200 3.20600   0.790 63.15000  ?  34  ARG A O   1 
ATOM   380  O  O   B ARG A 1 34  ? 44.07500 52.69500 2.81800   0.210 68.42000  ?  34  ARG A O   1 
ATOM   381  C  CB  A ARG A 1 34  ? 46.26900 54.69000 3.75600   0.790 96.30000  ?  34  ARG A CB  1 
ATOM   382  C  CB  B ARG A 1 34  ? 46.13100 55.10700 3.36400   0.210 97.20000  ?  34  ARG A CB  1 
ATOM   383  C  CG  A ARG A 1 34  ? 47.52100 53.97400 3.27700   0.790 107.89000 ?  34  ARG A CG  1 
ATOM   384  C  CG  B ARG A 1 34  ? 47.51300 54.70600 2.71200   0.210 105.02000 ?  34  ARG A CG  1 
ATOM   385  C  CD  A ARG A 1 34  ? 48.51800 53.77600 4.42000   0.790 114.36000 ?  34  ARG A CD  1 
ATOM   386  C  CD  B ARG A 1 34  ? 48.63400 54.55200 3.79000   0.210 114.23000 ?  34  ARG A CD  1 
ATOM   387  N  NE  A ARG A 1 34  ? 48.83600 55.02700 5.10800   0.790 125.22000 ?  34  ARG A NE  1 
ATOM   388  N  NE  B ARG A 1 34  ? 48.89300 55.77600 4.55800   0.210 122.52000 ?  34  ARG A NE  1 
ATOM   389  C  CZ  A ARG A 1 34  ? 49.69500 55.13100 6.11900   0.790 124.75000 ?  34  ARG A CZ  1 
ATOM   390  C  CZ  B ARG A 1 34  ? 49.68100 55.86000 5.63000   0.210 124.18000 ?  34  ARG A CZ  1 
ATOM   391  N  NH1 A ARG A 1 34  ? 50.32900 54.05700 6.57000   0.790 128.67000 ?  34  ARG A NH1 1 
ATOM   392  N  NH1 B ARG A 1 34  ? 50.26600 54.79100 6.15200   0.210 125.96000 ?  34  ARG A NH1 1 
ATOM   393  N  NH2 A ARG A 1 34  ? 49.92000 56.31100 6.68100   0.790 117.58000 ?  34  ARG A NH2 1 
ATOM   394  N  NH2 B ARG A 1 34  ? 49.87400 57.04500 6.20700   0.210 119.91000 ?  34  ARG A NH2 1 
ATOM   395  N  N   A ARG A 1 35  ? 43.19400 53.87700 4.38000   0.790 75.40000  ?  35  ARG A N   1 
ATOM   396  N  N   B ARG A 1 35  ? 42.86000 54.27800 3.86300   0.210 76.04000  ?  35  ARG A N   1 
ATOM   397  C  CA  A ARG A 1 35  ? 42.33400 52.93500 5.09100   0.790 73.62000  ?  35  ARG A CA  1 
ATOM   398  C  CA  B ARG A 1 35  ? 42.07100 53.28300 4.59300   0.210 70.61000  ?  35  ARG A CA  1 
ATOM   399  C  C   A ARG A 1 35  ? 41.56700 52.04500 4.12100   0.790 62.34000  ?  35  ARG A C   1 
ATOM   400  C  C   B ARG A 1 35  ? 41.32600 52.34900 3.66700   0.210 62.83000  ?  35  ARG A C   1 
ATOM   401  O  O   A ARG A 1 35  ? 41.52100 50.82000 4.28600   0.790 53.62000  ?  35  ARG A O   1 
ATOM   402  O  O   B ARG A 1 35  ? 41.16600 51.15700 3.96200   0.210 59.65000  ?  35  ARG A O   1 
ATOM   403  C  CB  A ARG A 1 35  ? 41.35900 53.69400 5.99000   0.790 74.29000  ?  35  ARG A CB  1 
ATOM   404  C  CB  B ARG A 1 35  ? 41.06400 53.94100 5.52700   0.210 74.73000  ?  35  ARG A CB  1 
ATOM   405  C  CG  A ARG A 1 35  ? 41.81700 53.86500 7.42500   0.790 77.73000  ?  35  ARG A CG  1 
ATOM   406  C  CG  B ARG A 1 35  ? 41.29400 53.68900 7.01800   0.210 76.83000  ?  35  ARG A CG  1 
ATOM   407  C  CD  A ARG A 1 35  ? 40.88600 54.80200 8.18900   0.790 88.96000  ?  35  ARG A CD  1 
ATOM   408  C  CD  B ARG A 1 35  ? 40.36500 54.59000 7.80300   0.210 86.39000  ?  35  ARG A CD  1 
ATOM   409  N  NE  A ARG A 1 35  ? 40.48600 55.95800 7.38700   0.790 104.80000 ?  35  ARG A NE  1 
ATOM   410  N  NE  B ARG A 1 35  ? 40.18800 55.78800 6.98800   0.210 98.29000  ?  35  ARG A NE  1 
ATOM   411  C  CZ  A ARG A 1 35  ? 39.52600 56.81300 7.72300   0.790 99.30000  ?  35  ARG A CZ  1 
ATOM   412  C  CZ  B ARG A 1 35  ? 39.44200 56.83900 7.29200   0.210 98.31000  ?  35  ARG A CZ  1 
ATOM   413  N  NH1 A ARG A 1 35  ? 38.85600 56.65100 8.85500   0.790 107.35000 ?  35  ARG A NH1 1 
ATOM   414  N  NH1 B ARG A 1 35  ? 38.82600 56.93600 8.45900   0.210 105.24000 ?  35  ARG A NH1 1 
ATOM   415  N  NH2 A ARG A 1 35  ? 39.23700 57.83100 6.92400   0.790 93.86000  ?  35  ARG A NH2 1 
ATOM   416  N  NH2 B ARG A 1 35  ? 39.34400 57.83600 6.41600   0.210 94.97000  ?  35  ARG A NH2 1 
ATOM   417  N  N   A TYR A 1 36  ? 40.94000 52.65000 3.11100   0.790 60.14000  ?  36  TYR A N   1 
ATOM   418  N  N   B TYR A 1 36  ? 40.81800 52.88100 2.56700   0.210 63.15000  ?  36  TYR A N   1 
ATOM   419  C  CA  A TYR A 1 36  ? 40.12900 51.88000 2.17500   0.790 62.82000  ?  36  TYR A CA  1 
ATOM   420  C  CA  B TYR A 1 36  ? 39.99700 52.07000 1.68200   0.210 61.97000  ?  36  TYR A CA  1 
ATOM   421  C  C   A TYR A 1 36  ? 40.97400 50.84000 1.45000   0.790 53.06000  ?  36  TYR A C   1 
ATOM   422  C  C   B TYR A 1 36  ? 40.82100 50.96400 1.05100   0.210 54.82000  ?  36  TYR A C   1 
ATOM   423  O  O   A TYR A 1 36  ? 40.60200 49.66300 1.37200   0.790 56.07000  ?  36  TYR A O   1 
ATOM   424  O  O   B TYR A 1 36  ? 40.48300 49.77700 1.15800   0.210 56.60000  ?  36  TYR A O   1 
ATOM   425  C  CB  A TYR A 1 36  ? 39.45700 52.81800 1.17200   0.790 67.03000  ?  36  TYR A CB  1 
ATOM   426  C  CB  B TYR A 1 36  ? 39.35700 52.94200 0.60100   0.210 64.28000  ?  36  TYR A CB  1 
ATOM   427  C  CG  A TYR A 1 36  ? 38.56800 53.86300 1.80400   0.790 58.37000  ?  36  TYR A CG  1 
ATOM   428  C  CG  B TYR A 1 36  ? 38.40900 54.03500 1.09500   0.210 62.28000  ?  36  TYR A CG  1 
ATOM   429  C  CD1 A TYR A 1 36  ? 37.22700 53.60500 2.05000   0.790 57.68000  ?  36  TYR A CD1 1 
ATOM   430  C  CD1 B TYR A 1 36  ? 38.89300 55.19000 1.71300   0.210 65.43000  ?  36  TYR A CD1 1 
ATOM   431  C  CD2 A TYR A 1 36  ? 39.07000 55.11000 2.15400   0.790 62.44000  ?  36  TYR A CD2 1 
ATOM   432  C  CD2 B TYR A 1 36  ? 37.02600 53.92300 0.91300   0.210 62.00000  ?  36  TYR A CD2 1 
ATOM   433  C  CE1 A TYR A 1 36  ? 36.41000 54.55600 2.62800   0.790 72.21000  ?  36  TYR A CE1 1 
ATOM   434  C  CE1 B TYR A 1 36  ? 38.01300 56.20400 2.13700   0.210 70.22000  ?  36  TYR A CE1 1 
ATOM   435  C  CE2 A TYR A 1 36  ? 38.26000 56.06900 2.73300   0.790 68.84000  ?  36  TYR A CE2 1 
ATOM   436  C  CE2 B TYR A 1 36  ? 36.13800 54.93800 1.33800   0.210 61.89000  ?  36  TYR A CE2 1 
ATOM   437  C  CZ  A TYR A 1 36  ? 36.93100 55.78600 2.96700   0.790 71.15000  ?  36  TYR A CZ  1 
ATOM   438  C  CZ  B TYR A 1 36  ? 36.64600 56.07600 1.94400   0.210 61.95000  ?  36  TYR A CZ  1 
ATOM   439  O  OH  A TYR A 1 36  ? 36.11500 56.73200 3.54200   0.790 73.91000  ?  36  TYR A OH  1 
ATOM   440  O  OH  B TYR A 1 36  ? 35.78400 57.06400 2.37200   0.210 66.68000  ?  36  TYR A OH  1 
ATOM   441  N  N   A TYR A 1 37  ? 42.12100 51.25800 0.91100   0.790 61.78000  ?  37  TYR A N   1 
ATOM   442  N  N   B TYR A 1 37  ? 41.92800 51.33800 0.41200   0.210 61.95000  ?  37  TYR A N   1 
ATOM   443  C  CA  A TYR A 1 37  ? 42.95500 50.33300 0.15300   0.790 58.09000  ?  37  TYR A CA  1 
ATOM   444  C  CA  B TYR A 1 37  ? 42.67800 50.39700 -0.42100  0.210 55.19000  ?  37  TYR A CA  1 
ATOM   445  C  C   A TYR A 1 37  ? 43.48500 49.21200 1.03900   0.790 59.16000  ?  37  TYR A C   1 
ATOM   446  C  C   B TYR A 1 37  ? 43.29800 49.27900 0.41500   0.210 56.65000  ?  37  TYR A C   1 
ATOM   447  O  O   A TYR A 1 37  ? 43.57600 48.05800 0.60400   0.790 51.71000  ?  37  TYR A O   1 
ATOM   448  O  O   B TYR A 1 37  ? 43.60000 48.19000 -0.10700  0.210 53.19000  ?  37  TYR A O   1 
ATOM   449  C  CB  A TYR A 1 37  ? 44.10600 51.09200 -0.50600  0.790 62.28000  ?  37  TYR A CB  1 
ATOM   450  C  CB  B TYR A 1 37  ? 43.78600 51.13200 -1.18100  0.210 60.93000  ?  37  TYR A CB  1 
ATOM   451  C  CG  A TYR A 1 37  ? 43.67500 52.01300 -1.62600  0.790 69.02000  ?  37  TYR A CG  1 
ATOM   452  C  CG  B TYR A 1 37  ? 43.40600 52.21000 -2.22000  0.210 66.48000  ?  37  TYR A CG  1 
ATOM   453  C  CD1 A TYR A 1 37  ? 43.49100 51.53000 -2.91500  0.790 59.72000  ?  37  TYR A CD1 1 
ATOM   454  C  CD1 B TYR A 1 37  ? 43.13400 51.88700 -3.53800  0.210 60.58000  ?  37  TYR A CD1 1 
ATOM   455  C  CD2 A TYR A 1 37  ? 43.45300 53.36300 -1.39500  0.790 72.93000  ?  37  TYR A CD2 1 
ATOM   456  C  CD2 B TYR A 1 37  ? 43.41200 53.56400 -1.88500  0.210 69.05000  ?  37  TYR A CD2 1 
ATOM   457  C  CE1 A TYR A 1 37  ? 43.09900 52.36700 -3.94200  0.790 60.85000  ?  37  TYR A CE1 1 
ATOM   458  C  CE1 B TYR A 1 37  ? 42.83400 52.87100 -4.47000  0.210 62.58000  ?  37  TYR A CE1 1 
ATOM   459  C  CE2 A TYR A 1 37  ? 43.06100 54.20900 -2.41500  0.790 64.66000  ?  37  TYR A CE2 1 
ATOM   460  C  CE2 B TYR A 1 37  ? 43.11300 54.54100 -2.81900  0.210 65.73000  ?  37  TYR A CE2 1 
ATOM   461  C  CZ  A TYR A 1 37  ? 42.88600 53.70500 -3.68700  0.790 58.15000  ?  37  TYR A CZ  1 
ATOM   462  C  CZ  B TYR A 1 37  ? 42.83900 54.19100 -4.10200  0.210 64.16000  ?  37  TYR A CZ  1 
ATOM   463  O  OH  A TYR A 1 37  ? 42.49400 54.54200 -4.70700  0.790 73.64000  ?  37  TYR A OH  1 
ATOM   464  O  OH  B TYR A 1 37  ? 42.54100 55.17200 -5.02000  0.210 75.39000  ?  37  TYR A OH  1 
ATOM   465  N  N   A VAL A 1 38  ? 43.83700 49.52700 2.28600   0.790 51.43000  ?  38  VAL A N   1 
ATOM   466  N  N   B VAL A 1 38  ? 43.54300 49.54300 1.70500   0.210 55.33000  ?  38  VAL A N   1 
ATOM   467  C  CA  A VAL A 1 38  ? 44.33500 48.49300 3.18800   0.790 46.58000  ?  38  VAL A CA  1 
ATOM   468  C  CA  B VAL A 1 38  ? 44.00300 48.47400 2.58300   0.210 49.26000  ?  38  VAL A CA  1 
ATOM   469  C  C   A VAL A 1 38  ? 43.23000 47.49700 3.51700   0.790 47.00000  ?  38  VAL A C   1 
ATOM   470  C  C   B VAL A 1 38  ? 42.85700 47.49800 2.89300   0.210 46.23000  ?  38  VAL A C   1 
ATOM   471  O  O   A VAL A 1 38  ? 43.48200 46.29600 3.66700   0.790 39.57000  ?  38  VAL A O   1 
ATOM   472  O  O   B VAL A 1 38  ? 43.06800 46.27800 2.94100   0.210 42.23000  ?  38  VAL A O   1 
ATOM   473  C  CB  A VAL A 1 38  ? 44.92400 49.13000 4.46000   0.790 62.40000  ?  38  VAL A CB  1 
ATOM   474  C  CB  B VAL A 1 38  ? 44.61600 49.10700 3.84200   0.210 54.11000  ?  38  VAL A CB  1 
ATOM   475  C  CG1 A VAL A 1 38  ? 45.22100 48.06300 5.50300   0.790 45.10000  ?  38  VAL A CG1 1 
ATOM   476  C  CG1 B VAL A 1 38  ? 44.99900 48.02900 4.88700   0.210 54.70000  ?  38  VAL A CG1 1 
ATOM   477  C  CG2 A VAL A 1 38  ? 46.17700 49.92500 4.11700   0.790 55.10000  ?  38  VAL A CG2 1 
ATOM   478  C  CG2 B VAL A 1 38  ? 45.80300 49.97400 3.46600   0.210 52.93000  ?  38  VAL A CG2 1 
ATOM   479  N  N   A THR A 1 39  ? 41.98900 47.97700 3.63800   0.790 46.71000  ?  39  THR A N   1 
ATOM   480  N  N   B THR A 1 39  ? 41.62600 48.01100 3.05400   0.210 47.01000  ?  39  THR A N   1 
ATOM   481  C  CA  A THR A 1 39  ? 40.87700 47.07300 3.91300   0.790 49.35000  ?  39  THR A CA  1 
ATOM   482  C  CA  B THR A 1 39  ? 40.46100 47.15900 3.29100   0.210 45.71000  ?  39  THR A CA  1 
ATOM   483  C  C   A THR A 1 39  ? 40.64800 46.12000 2.74700   0.790 45.54000  ?  39  THR A C   1 
ATOM   484  C  C   B THR A 1 39  ? 40.29700 46.14600 2.17900   0.210 43.24000  ?  39  THR A C   1 
ATOM   485  O  O   A THR A 1 39  ? 40.44200 44.91900 2.95000   0.790 51.71000  ?  39  THR A O   1 
ATOM   486  O  O   B THR A 1 39  ? 40.12900 44.93800 2.41100   0.210 42.71000  ?  39  THR A O   1 
ATOM   487  C  CB  A THR A 1 39  ? 39.60800 47.87500 4.20700   0.790 45.50000  ?  39  THR A CB  1 
ATOM   488  C  CB  B THR A 1 39  ? 39.18800 47.99600 3.37900   0.210 45.95000  ?  39  THR A CB  1 
ATOM   489  O  OG1 A THR A 1 39  ? 39.87300 48.82200 5.25000   0.790 41.76000  ?  39  THR A OG1 1 
ATOM   490  O  OG1 B THR A 1 39  ? 39.47600 49.23300 4.02900   0.210 48.64000  ?  39  THR A OG1 1 
ATOM   491  C  CG2 A THR A 1 39  ? 38.47000 46.95600 4.63600   0.790 43.67000  ?  39  THR A CG2 1 
ATOM   492  C  CG2 B THR A 1 39  ? 38.12200 47.26500 4.19400   0.210 42.54000  ?  39  THR A CG2 1 
ATOM   493  N  N   A LEU A 1 40  ? 40.69700 46.63200 1.51800   0.790 44.67000  ?  40  LEU A N   1 
ATOM   494  N  N   B LEU A 1 40  ? 40.30300 46.63300 0.95100   0.210 44.85000  ?  40  LEU A N   1 
ATOM   495  C  CA  A LEU A 1 40  ? 40.48200 45.77000 0.36100   0.790 42.16000  ?  40  LEU A CA  1 
ATOM   496  C  CA  B LEU A 1 40  ? 40.22900 45.71900 -0.16700  0.210 42.16000  ?  40  LEU A CA  1 
ATOM   497  C  C   A LEU A 1 40  ? 41.58100 44.72000 0.24900   0.790 40.14000  ?  40  LEU A C   1 
ATOM   498  C  C   B LEU A 1 40  ? 41.32800 44.66900 -0.10200  0.210 40.58000  ?  40  LEU A C   1 
ATOM   499  O  O   A LEU A 1 40  ? 41.32000 43.57600 -0.14600  0.790 43.13000  ?  40  LEU A O   1 
ATOM   500  O  O   B LEU A 1 40  ? 41.04600 43.46200 -0.14900  0.210 42.60000  ?  40  LEU A O   1 
ATOM   501  C  CB  A LEU A 1 40  ? 40.39200 46.62000 -0.90500  0.790 42.69000  ?  40  LEU A CB  1 
ATOM   502  C  CB  B LEU A 1 40  ? 40.28800 46.52500 -1.44500  0.210 44.10000  ?  40  LEU A CB  1 
ATOM   503  C  CG  A LEU A 1 40  ? 39.10200 47.44700 -0.94200  0.790 43.25000  ?  40  LEU A CG  1 
ATOM   504  C  CG  B LEU A 1 40  ? 38.98100 47.32000 -1.39100  0.210 41.85000  ?  40  LEU A CG  1 
ATOM   505  C  CD1 A LEU A 1 40  ? 39.22500 48.54900 -1.97600  0.790 46.24000  ?  40  LEU A CD1 1 
ATOM   506  C  CD1 B LEU A 1 40  ? 39.01200 48.45000 -2.37100  0.210 42.96000  ?  40  LEU A CD1 1 
ATOM   507  C  CD2 A LEU A 1 40  ? 37.89800 46.55900 -1.21400  0.790 42.73000  ?  40  LEU A CD2 1 
ATOM   508  C  CD2 B LEU A 1 40  ? 37.75200 46.46500 -1.62500  0.210 40.13000  ?  40  LEU A CD2 1 
ATOM   509  N  N   A VAL A 1 41  ? 42.81900 45.08200 0.58900   0.790 44.44000  ?  41  VAL A N   1 
ATOM   510  N  N   B VAL A 1 41  ? 42.57800 45.09800 0.08700   0.210 41.07000  ?  41  VAL A N   1 
ATOM   511  C  CA  A VAL A 1 41  ? 43.88300 44.08100 0.59500   0.790 32.13000  ?  41  VAL A CA  1 
ATOM   512  C  CA  B VAL A 1 41  ? 43.69500 44.15800 0.02300   0.210 37.41000  ?  41  VAL A CA  1 
ATOM   513  C  C   A VAL A 1 41  ? 43.56000 42.97900 1.59800   0.790 40.46000  ?  41  VAL A C   1 
ATOM   514  C  C   B VAL A 1 41  ? 43.55200 43.02100 1.02500   0.210 39.19000  ?  41  VAL A C   1 
ATOM   515  O  O   A VAL A 1 41  ? 43.76400 41.78900 1.32700   0.790 44.07000  ?  41  VAL A O   1 
ATOM   516  O  O   B VAL A 1 41  ? 44.02800 41.90400 0.76600   0.210 38.19000  ?  41  VAL A O   1 
ATOM   517  C  CB  A VAL A 1 41  ? 45.24900 44.73000 0.88900   0.790 35.53000  ?  41  VAL A CB  1 
ATOM   518  C  CB  B VAL A 1 41  ? 45.02500 44.91500 0.19000   0.210 40.57000  ?  41  VAL A CB  1 
ATOM   519  C  CG1 A VAL A 1 41  ? 46.30800 43.65500 1.13200   0.790 42.40000  ?  41  VAL A CG1 1 
ATOM   520  C  CG1 B VAL A 1 41  ? 46.13000 43.94700 0.33200   0.210 41.65000  ?  41  VAL A CG1 1 
ATOM   521  C  CG2 A VAL A 1 41  ? 45.66100 45.63500 -0.26000  0.790 37.87000  ?  41  VAL A CG2 1 
ATOM   522  C  CG2 B VAL A 1 41  ? 45.30300 45.80300 -1.01300  0.210 35.96000  ?  41  VAL A CG2 1 
ATOM   523  N  N   A GLY A 1 42  ? 43.04400 43.35600 2.76900   0.790 33.58000  ?  42  GLY A N   1 
ATOM   524  N  N   B GLY A 1 42  ? 42.87800 43.26600 2.15300   0.210 36.61000  ?  42  GLY A N   1 
ATOM   525  C  CA  A GLY A 1 42  ? 42.67900 42.35600 3.75800   0.790 28.57000  ?  42  GLY A CA  1 
ATOM   526  C  CA  B GLY A 1 42  ? 42.68700 42.22800 3.15000   0.210 34.27000  ?  42  GLY A CA  1 
ATOM   527  C  C   A GLY A 1 42  ? 41.53700 41.47100 3.29800   0.790 36.86000  ?  42  GLY A C   1 
ATOM   528  C  C   B GLY A 1 42  ? 41.46700 41.38500 2.85100   0.210 35.23000  ?  42  GLY A C   1 
ATOM   529  O  O   A GLY A 1 42  ? 41.55500 40.25500 3.51300   0.790 32.82000  ?  42  GLY A O   1 
ATOM   530  O  O   B GLY A 1 42  ? 41.46800 40.15000 3.01500   0.210 32.52000  ?  42  GLY A O   1 
ATOM   531  N  N   A ILE A 1 43  ? 40.53900 42.06600 2.64000   0.790 31.97000  ?  43  ILE A N   1 
ATOM   532  N  N   B ILE A 1 43  ? 40.40000 42.08400 2.45700   0.210 32.00000  ?  43  ILE A N   1 
ATOM   533  C  CA  A ILE A 1 43  ? 39.37700 41.30400 2.19000   0.790 38.51000  ?  43  ILE A CA  1 
ATOM   534  C  CA  B ILE A 1 43  ? 39.21700 41.39500 1.97000   0.210 38.21000  ?  43  ILE A CA  1 
ATOM   535  C  C   A ILE A 1 43  ? 39.79800 40.20100 1.22800   0.790 32.57000  ?  43  ILE A C   1 
ATOM   536  C  C   B ILE A 1 43  ? 39.62000 40.25400 1.05200   0.210 32.24000  ?  43  ILE A C   1 
ATOM   537  O  O   A ILE A 1 43  ? 39.42700 39.03500 1.39300   0.790 38.85000  ?  43  ILE A O   1 
ATOM   538  O  O   B ILE A 1 43  ? 39.20100 39.11600 1.22600   0.210 40.01000  ?  43  ILE A O   1 
ATOM   539  C  CB  A ILE A 1 43  ? 38.33900 42.24000 1.54500   0.790 38.89000  ?  43  ILE A CB  1 
ATOM   540  C  CB  B ILE A 1 43  ? 38.27900 42.37500 1.25200   0.210 38.97000  ?  43  ILE A CB  1 
ATOM   541  C  CG1 A ILE A 1 43  ? 37.66500 43.10100 2.61100   0.790 30.35000  ?  43  ILE A CG1 1 
ATOM   542  C  CG1 B ILE A 1 43  ? 37.50000 43.21200 2.28000   0.210 32.54000  ?  43  ILE A CG1 1 
ATOM   543  C  CG2 A ILE A 1 43  ? 37.31600 41.44000 0.75800   0.790 28.45000  ?  43  ILE A CG2 1 
ATOM   544  C  CG2 B ILE A 1 43  ? 37.46500 41.57500 0.26300   0.210 27.79000  ?  43  ILE A CG2 1 
ATOM   545  C  CD1 A ILE A 1 43  ? 37.05800 44.37300 2.07100   0.790 27.99000  ?  43  ILE A CD1 1 
ATOM   546  C  CD1 B ILE A 1 43  ? 36.99100 44.54600 1.81800   0.210 30.02000  ?  43  ILE A CD1 1 
ATOM   547  N  N   A SER A 1 44  ? 40.54500 40.55200 0.18600   0.790 38.46000  ?  44  SER A N   1 
ATOM   548  N  N   B SER A 1 44  ? 40.46900 40.52500 0.07900   0.210 37.13000  ?  44  SER A N   1 
ATOM   549  C  CA  A SER A 1 44  ? 40.93600 39.54700 -0.79500  0.790 41.26000  ?  44  SER A CA  1 
ATOM   550  C  CA  B SER A 1 44  ? 40.78600 39.45000 -0.85500  0.210 41.19000  ?  44  SER A CA  1 
ATOM   551  C  C   A SER A 1 44  ? 42.17700 38.77300 -0.37800  0.790 43.31000  ?  44  SER A C   1 
ATOM   552  C  C   B SER A 1 44  ? 42.01200 38.69700 -0.42100  0.210 40.17000  ?  44  SER A C   1 
ATOM   553  O  O   A SER A 1 44  ? 42.32100 37.60100 -0.74800  0.790 35.99000  ?  44  SER A O   1 
ATOM   554  O  O   B SER A 1 44  ? 42.09700 37.47700 -0.65500  0.210 33.77000  ?  44  SER A O   1 
ATOM   555  C  CB  A SER A 1 44  ? 41.16800 40.19500 -2.16200  0.790 40.87000  ?  44  SER A CB  1 
ATOM   556  C  CB  B SER A 1 44  ? 41.00700 40.01800 -2.24700  0.210 39.24000  ?  44  SER A CB  1 
ATOM   557  O  OG  A SER A 1 44  ? 42.02900 41.31200 -2.06600  0.790 48.63000  ?  44  SER A OG  1 
ATOM   558  O  OG  B SER A 1 44  ? 41.99200 41.02200 -2.18000  0.210 46.57000  ?  44  SER A OG  1 
ATOM   559  N  N   A GLY A 1 45  ? 43.05900 39.39100 0.40900   0.790 32.00000  ?  45  GLY A N   1 
ATOM   560  N  N   B GLY A 1 45  ? 42.95200 39.42200 0.19300   0.210 31.82000  ?  45  GLY A N   1 
ATOM   561  C  CA  A GLY A 1 45  ? 44.24200 38.68600 0.86800   0.790 32.93000  ?  45  GLY A CA  1 
ATOM   562  C  CA  B GLY A 1 45  ? 44.12300 38.77100 0.73700   0.210 33.07000  ?  45  GLY A CA  1 
ATOM   563  C  C   A GLY A 1 45  ? 43.91300 37.52600 1.78500   0.790 33.51000  ?  45  GLY A C   1 
ATOM   564  C  C   B GLY A 1 45  ? 43.72300 37.64800 1.66800   0.210 33.01000  ?  45  GLY A C   1 
ATOM   565  O  O   A GLY A 1 45  ? 44.49900 36.44800 1.67000   0.790 34.16000  ?  45  GLY A O   1 
ATOM   566  O  O   B GLY A 1 45  ? 44.18500 36.50500 1.53800   0.210 34.34000  ?  45  GLY A O   1 
ATOM   567  N  N   A ILE A 1 46  ? 42.97700 37.73100 2.71400   0.790 27.81000  ?  46  ILE A N   1 
ATOM   568  N  N   B ILE A 1 46  ? 42.79400 37.92600 2.57300   0.210 28.04000  ?  46  ILE A N   1 
ATOM   569  C  CA  A ILE A 1 46  ? 42.57400 36.64400 3.59700   0.790 34.12000  ?  46  ILE A CA  1 
ATOM   570  C  CA  B ILE A 1 46  ? 42.38300 36.84300 3.44100   0.210 34.19000  ?  46  ILE A CA  1 
ATOM   571  C  C   A ILE A 1 46  ? 41.90200 35.53600 2.79600   0.790 32.29000  ?  46  ILE A C   1 
ATOM   572  C  C   B ILE A 1 46  ? 41.67800 35.79900 2.61800   0.210 32.26000  ?  46  ILE A C   1 
ATOM   573  O  O   A ILE A 1 46  ? 42.18500 34.34900 2.99500   0.790 40.21000  ?  46  ILE A O   1 
ATOM   574  O  O   B ILE A 1 46  ? 41.86200 34.59400 2.81900   0.210 38.65000  ?  46  ILE A O   1 
ATOM   575  C  CB  A ILE A 1 46  ? 41.65600 37.17700 4.71200   0.790 30.74000  ?  46  ILE A CB  1 
ATOM   576  C  CB  B ILE A 1 46  ? 41.51300 37.37700 4.58000   0.210 30.16000  ?  46  ILE A CB  1 
ATOM   577  C  CG1 A ILE A 1 46  ? 42.45700 38.03800 5.69300   0.790 35.95000  ?  46  ILE A CG1 1 
ATOM   578  C  CG1 B ILE A 1 46  ? 42.33100 38.40000 5.35300   0.210 35.77000  ?  46  ILE A CG1 1 
ATOM   579  C  CG2 A ILE A 1 46  ? 40.98600 36.02400 5.44700   0.790 27.09000  ?  46  ILE A CG2 1 
ATOM   580  C  CG2 B ILE A 1 46  ? 41.23700 36.26800 5.51700   0.210 27.78000  ?  46  ILE A CG2 1 
ATOM   581  C  CD1 A ILE A 1 46  ? 41.61500 38.95800 6.55400   0.790 31.90000  ?  46  ILE A CD1 1 
ATOM   582  C  CD1 B ILE A 1 46  ? 41.50000 39.36500 6.13100   0.210 36.16000  ?  46  ILE A CD1 1 
ATOM   583  N  N   A ALA A 1 47  ? 41.01400 35.90400 1.86900   0.790 30.21000  ?  47  ALA A N   1 
ATOM   584  N  N   B ALA A 1 47  ? 40.90800 36.25300 1.63500   0.210 29.68000  ?  47  ALA A N   1 
ATOM   585  C  CA  A ALA A 1 47  ? 40.34600 34.89600 1.05200   0.790 24.02000  ?  47  ALA A CA  1 
ATOM   586  C  CA  B ALA A 1 47  ? 40.25600 35.32300 0.73000   0.210 28.25000  ?  47  ALA A CA  1 
ATOM   587  C  C   A ALA A 1 47  ? 41.35100 34.11700 0.21100   0.790 31.84000  ?  47  ALA A C   1 
ATOM   588  C  C   B ALA A 1 47  ? 41.25800 34.56600 -0.13200  0.210 30.92000  ?  47  ALA A C   1 
ATOM   589  O  O   A ALA A 1 47  ? 41.22100 32.89800 0.05200   0.790 31.26000  ?  47  ALA A O   1 
ATOM   590  O  O   B ALA A 1 47  ? 41.05700 33.39200 -0.41400  0.210 30.90000  ?  47  ALA A O   1 
ATOM   591  C  CB  A ALA A 1 47  ? 39.28900 35.55700 0.16700   0.790 26.08000  ?  47  ALA A CB  1 
ATOM   592  C  CB  B ALA A 1 47  ? 39.25600 36.04400 -0.15700  0.210 29.63000  ?  47  ALA A CB  1 
ATOM   593  N  N   A ALA A 1 48  ? 42.36400 34.79800 -0.33100  0.790 29.26000  ?  48  ALA A N   1 
ATOM   594  N  N   B ALA A 1 48  ? 42.35200 35.17300 -0.55300  0.210 29.04000  ?  48  ALA A N   1 
ATOM   595  C  CA  A ALA A 1 48  ? 43.40900 34.09000 -1.06400  0.790 33.45000  ?  48  ALA A CA  1 
ATOM   596  C  CA  B ALA A 1 48  ? 43.28200 34.33100 -1.31700  0.210 34.16000  ?  48  ALA A CA  1 
ATOM   597  C  C   A ALA A 1 48  ? 43.96600 32.94200 -0.22900  0.790 39.92000  ?  48  ALA A C   1 
ATOM   598  C  C   B ALA A 1 48  ? 43.83700 33.22300 -0.43300  0.210 38.06000  ?  48  ALA A C   1 
ATOM   599  O  O   A ALA A 1 48  ? 44.02600 31.79400 -0.68400  0.790 34.48000  ?  48  ALA A O   1 
ATOM   600  O  O   B ALA A 1 48  ? 43.83500 32.04200 -0.81100  0.210 34.45000  ?  48  ALA A O   1 
ATOM   601  C  CB  A ALA A 1 48  ? 44.52800 35.05500 -1.45900  0.790 35.30000  ?  48  ALA A CB  1 
ATOM   602  C  CB  B ALA A 1 48  ? 44.40100 35.16100 -1.94100  0.210 34.24000  ?  48  ALA A CB  1 
ATOM   603  N  N   A VAL A 1 49  ? 44.35900 33.23400 1.01200   0.790 40.76000  ?  49  VAL A N   1 
ATOM   604  N  N   B VAL A 1 49  ? 44.23000 33.58600 0.80000   0.210 40.69000  ?  49  VAL A N   1 
ATOM   605  C  CA  A VAL A 1 49  ? 44.95600 32.21000 1.86500   0.790 29.09000  ?  49  VAL A CA  1 
ATOM   606  C  CA  B VAL A 1 49  ? 44.82900 32.62200 1.72100   0.210 34.06000  ?  49  VAL A CA  1 
ATOM   607  C  C   A VAL A 1 49  ? 43.97500 31.06500 2.09400   0.790 42.97000  ?  49  VAL A C   1 
ATOM   608  C  C   B VAL A 1 49  ? 43.87900 31.46500 1.99900   0.210 39.01000  ?  49  VAL A C   1 
ATOM   609  O  O   A VAL A 1 49  ? 44.33500 29.88700 1.99300   0.790 43.33000  ?  49  VAL A O   1 
ATOM   610  O  O   B VAL A 1 49  ? 44.23700 30.29300 1.79300   0.210 42.43000  ?  49  VAL A O   1 
ATOM   611  C  CB  A VAL A 1 49  ? 45.42500 32.82800 3.19600   0.790 41.97000  ?  49  VAL A CB  1 
ATOM   612  C  CB  B VAL A 1 49  ? 45.25500 33.32000 3.01100   0.210 42.82000  ?  49  VAL A CB  1 
ATOM   613  C  CG1 A VAL A 1 49  ? 45.82000 31.73600 4.18300   0.790 35.62000  ?  49  VAL A CG1 1 
ATOM   614  C  CG1 B VAL A 1 49  ? 45.67300 32.29300 4.03600   0.210 38.50000  ?  49  VAL A CG1 1 
ATOM   615  C  CG2 A VAL A 1 49  ? 46.58300 33.78700 2.95300   0.790 43.59000  ?  49  VAL A CG2 1 
ATOM   616  C  CG2 B VAL A 1 49  ? 46.37300 34.28800 2.69100   0.210 42.05000  ?  49  VAL A CG2 1 
ATOM   617  N  N   A ALA A 1 50  ? 42.72000 31.39200 2.41000   0.790 32.77000  ?  50  ALA A N   1 
ATOM   618  N  N   B ALA A 1 50  ? 42.66100 31.76400 2.47600   0.210 31.54000  ?  50  ALA A N   1 
ATOM   619  C  CA  A ALA A 1 50  ? 41.73900 30.33900 2.66000   0.790 27.30000  ?  50  ALA A CA  1 
ATOM   620  C  CA  B ALA A 1 50  ? 41.63900 30.71700 2.55500   0.210 31.37000  ?  50  ALA A CA  1 
ATOM   621  C  C   A ALA A 1 50  ? 41.60500 29.41600 1.45600   0.790 36.63000  ?  50  ALA A C   1 
ATOM   622  C  C   B ALA A 1 50  ? 41.62000 29.83200 1.30400   0.210 36.00000  ?  50  ALA A C   1 
ATOM   623  O  O   A ALA A 1 50  ? 41.52800 28.19200 1.60500   0.790 38.74000  ?  50  ALA A O   1 
ATOM   624  O  O   B ALA A 1 50  ? 41.64800 28.59200 1.39600   0.210 40.03000  ?  50  ALA A O   1 
ATOM   625  C  CB  A ALA A 1 50  ? 40.38600 30.95200 3.02000   0.790 38.95000  ?  50  ALA A CB  1 
ATOM   626  C  CB  B ALA A 1 50  ? 40.26100 31.35800 2.81400   0.210 36.22000  ?  50  ALA A CB  1 
ATOM   627  N  N   A TYR A 1 51  ? 41.59300 29.98000 0.24900   0.790 35.30000  ?  51  TYR A N   1 
ATOM   628  N  N   B TYR A 1 51  ? 41.70300 30.46200 0.12300   0.210 33.44000  ?  51  TYR A N   1 
ATOM   629  C  CA  A TYR A 1 51  ? 41.41100 29.15100 -0.93800  0.790 36.47000  ?  51  TYR A CA  1 
ATOM   630  C  CA  B TYR A 1 51  ? 41.53700 29.70500 -1.11100  0.210 35.66000  ?  51  TYR A CA  1 
ATOM   631  C  C   A TYR A 1 51  ? 42.63500 28.28500 -1.21500  0.790 37.72000  ?  51  TYR A C   1 
ATOM   632  C  C   B TYR A 1 51  ? 42.69600 28.75600 -1.34500  0.210 37.90000  ?  51  TYR A C   1 
ATOM   633  O  O   A TYR A 1 51  ? 42.49700 27.12500 -1.62100  0.790 34.71000  ?  51  TYR A O   1 
ATOM   634  O  O   B TYR A 1 51  ? 42.49500 27.57800 -1.68700  0.210 35.47000  ?  51  TYR A O   1 
ATOM   635  C  CB  A TYR A 1 51  ? 41.07200 30.03600 -2.13300  0.790 31.18000  ?  51  TYR A CB  1 
ATOM   636  C  CB  B TYR A 1 51  ? 41.31600 30.64900 -2.28800  0.210 30.59000  ?  51  TYR A CB  1 
ATOM   637  C  CG  A TYR A 1 51  ? 39.58200 30.22800 -2.28600  0.790 36.01000  ?  51  TYR A CG  1 
ATOM   638  C  CG  B TYR A 1 51  ? 39.83000 30.77500 -2.35300  0.210 34.81000  ?  51  TYR A CG  1 
ATOM   639  C  CD1 A TYR A 1 51  ? 38.78400 29.20800 -2.78500  0.790 27.77000  ?  51  TYR A CD1 1 
ATOM   640  C  CD1 B TYR A 1 51  ? 39.11600 29.70500 -2.82400  0.210 30.23000  ?  51  TYR A CD1 1 
ATOM   641  C  CD2 A TYR A 1 51  ? 38.96800 31.41500 -1.91000  0.790 30.82000  ?  51  TYR A CD2 1 
ATOM   642  C  CD2 B TYR A 1 51  ? 39.12400 31.88400 -1.82000  0.210 29.45000  ?  51  TYR A CD2 1 
ATOM   643  C  CE1 A TYR A 1 51  ? 37.42300 29.36800 -2.91600  0.790 31.86000  ?  51  TYR A CE1 1 
ATOM   644  C  CE1 B TYR A 1 51  ? 37.81700 29.70300 -2.83400  0.210 29.68000  ?  51  TYR A CE1 1 
ATOM   645  C  CE2 A TYR A 1 51  ? 37.60200 31.58400 -2.04200  0.790 33.50000  ?  51  TYR A CE2 1 
ATOM   646  C  CE2 B TYR A 1 51  ? 37.75500 31.90800 -1.86300  0.210 32.25000  ?  51  TYR A CE2 1 
ATOM   647  C  CZ  A TYR A 1 51  ? 36.83600 30.55500 -2.54400  0.790 27.05000  ?  51  TYR A CZ  1 
ATOM   648  C  CZ  B TYR A 1 51  ? 37.11900 30.77300 -2.39000  0.210 30.91000  ?  51  TYR A CZ  1 
ATOM   649  O  OH  A TYR A 1 51  ? 35.47600 30.70700 -2.68200  0.790 39.80000  ?  51  TYR A OH  1 
ATOM   650  O  OH  B TYR A 1 51  ? 35.78100 30.57600 -2.48300  0.210 36.29000  ?  51  TYR A OH  1 
ATOM   651  N  N   A VAL A 1 52  ? 43.83900 28.81200 -0.98700  0.790 37.25000  ?  52  VAL A N   1 
ATOM   652  N  N   B VAL A 1 52  ? 43.91800 29.24100 -1.12900  0.210 31.93000  ?  52  VAL A N   1 
ATOM   653  C  CA  A VAL A 1 52  ? 45.03700 27.99100 -1.15800  0.790 40.20000  ?  52  VAL A CA  1 
ATOM   654  C  CA  B VAL A 1 52  ? 45.09000 28.35900 -1.21800  0.210 39.06000  ?  52  VAL A CA  1 
ATOM   655  C  C   A VAL A 1 52  ? 45.00000 26.80600 -0.20000  0.790 42.34000  ?  52  VAL A C   1 
ATOM   656  C  C   B VAL A 1 52  ? 44.98700 27.21400 -0.21100  0.210 40.03000  ?  52  VAL A C   1 
ATOM   657  O  O   A VAL A 1 52  ? 45.21900 25.65500 -0.59700  0.790 41.69000  ?  52  VAL A O   1 
ATOM   658  O  O   B VAL A 1 52  ? 45.22500 26.04200 -0.55300  0.210 41.88000  ?  52  VAL A O   1 
ATOM   659  C  CB  A VAL A 1 52  ? 46.30800 28.83500 -0.95500  0.790 34.97000  ?  52  VAL A CB  1 
ATOM   660  C  CB  B VAL A 1 52  ? 46.38900 29.14100 -0.98200  0.210 34.63000  ?  52  VAL A CB  1 
ATOM   661  C  CG1 A VAL A 1 52  ? 47.53300 27.92600 -0.90800  0.790 25.75000  ?  52  VAL A CG1 1 
ATOM   662  C  CG1 B VAL A 1 52  ? 47.53400 28.16100 -0.85400  0.210 27.02000  ?  52  VAL A CG1 1 
ATOM   663  C  CG2 A VAL A 1 52  ? 46.45200 29.87100 -2.05400  0.790 28.52000  ?  52  VAL A CG2 1 
ATOM   664  C  CG2 B VAL A 1 52  ? 46.57700 30.17000 -2.04700  0.210 28.84000  ?  52  VAL A CG2 1 
ATOM   665  N  N   A VAL A 1 53  ? 44.71800 27.07200 1.07700   0.790 37.97000  ?  53  VAL A N   1 
ATOM   666  N  N   B VAL A 1 53  ? 44.65400 27.54200 1.05800   0.210 36.37000  ?  53  VAL A N   1 
ATOM   667  C  CA  A VAL A 1 53  ? 44.63900 26.00100 2.06900   0.790 30.98000  ?  53  VAL A CA  1 
ATOM   668  C  CA  B VAL A 1 53  ? 44.45400 26.53900 2.10000   0.210 35.70000  ?  53  VAL A CA  1 
ATOM   669  C  C   A VAL A 1 53  ? 43.66400 24.92900 1.60300   0.790 31.45000  ?  53  VAL A C   1 
ATOM   670  C  C   B VAL A 1 53  ? 43.53700 25.43700 1.63400   0.210 35.12000  ?  53  VAL A C   1 
ATOM   671  O  O   A VAL A 1 53  ? 43.94800 23.72700 1.66700   0.790 44.89000  ?  53  VAL A O   1 
ATOM   672  O  O   B VAL A 1 53  ? 43.94500 24.28500 1.56200   0.210 37.95000  ?  53  VAL A O   1 
ATOM   673  C  CB  A VAL A 1 53  ? 44.23300 26.57400 3.43900   0.790 41.29000  ?  53  VAL A CB  1 
ATOM   674  C  CB  B VAL A 1 53  ? 43.90200 27.16500 3.38000   0.210 45.52000  ?  53  VAL A CB  1 
ATOM   675  C  CG1 A VAL A 1 53  ? 43.90400 25.45900 4.41700   0.790 45.62000  ?  53  VAL A CG1 1 
ATOM   676  C  CG1 B VAL A 1 53  ? 43.05400 26.17600 4.14500   0.210 38.91000  ?  53  VAL A CG1 1 
ATOM   677  C  CG2 A VAL A 1 53  ? 45.33900 27.45900 3.98700   0.790 41.03000  ?  53  VAL A CG2 1 
ATOM   678  C  CG2 B VAL A 1 53  ? 45.04900 27.57600 4.23200   0.210 43.91000  ?  53  VAL A CG2 1 
ATOM   679  N  N   A MET A 1 54  ? 42.49100 25.35500 1.13400   0.790 31.88000  ?  54  MET A N   1 
ATOM   680  N  N   B MET A 1 54  ? 42.30900 25.79000 1.27900   0.210 34.21000  ?  54  MET A N   1 
ATOM   681  C  CA  A MET A 1 54  ? 41.50400 24.40000 0.64700   0.790 38.94000  ?  54  MET A CA  1 
ATOM   682  C  CA  B MET A 1 54  ? 41.37000 24.77600 0.84300   0.210 38.79000  ?  54  MET A CA  1 
ATOM   683  C  C   A MET A 1 54  ? 41.99800 23.70100 -0.61400  0.790 46.88000  ?  54  MET A C   1 
ATOM   684  C  C   B MET A 1 54  ? 41.91600 24.01600 -0.34200  0.210 43.78000  ?  54  MET A C   1 
ATOM   685  O  O   A MET A 1 54  ? 41.81700 22.48700 -0.76500  0.790 39.66000  ?  54  MET A O   1 
ATOM   686  O  O   B MET A 1 54  ? 41.79800 22.78400 -0.41700  0.210 41.41000  ?  54  MET A O   1 
ATOM   687  C  CB  A MET A 1 54  ? 40.17400 25.11300 0.40200   0.790 35.75000  ?  54  MET A CB  1 
ATOM   688  C  CB  B MET A 1 54  ? 40.05900 25.41200 0.43000   0.210 36.85000  ?  54  MET A CB  1 
ATOM   689  C  CG  A MET A 1 54  ? 39.44100 25.45000 1.68700   0.790 42.97000  ?  54  MET A CG  1 
ATOM   690  C  CG  B MET A 1 54  ? 39.15500 25.83400 1.54500   0.210 39.79000  ?  54  MET A CG  1 
ATOM   691  S  SD  A MET A 1 54  ? 37.71600 25.91700 1.45500   0.790 44.54000  ?  54  MET A SD  1 
ATOM   692  S  SD  B MET A 1 54  ? 37.54400 26.23300 0.78300   0.210 31.45000  ?  54  MET A SD  1 
ATOM   693  C  CE  A MET A 1 54  ? 37.88500 27.65600 1.00900   0.790 40.28000  ?  54  MET A CE  1 
ATOM   694  C  CE  B MET A 1 54  ? 37.96100 27.77600 -0.05100  0.210 34.42000  ?  54  MET A CE  1 
ATOM   695  N  N   A ALA A 1 55  ? 42.63900 24.44300 -1.52000  0.790 36.75000  ?  55  ALA A N   1 
ATOM   696  N  N   B ALA A 1 55  ? 42.48100 24.76300 -1.29900  0.210 37.74000  ?  55  ALA A N   1 
ATOM   697  C  CA  A ALA A 1 55  ? 43.18200 23.82400 -2.72500  0.790 36.67000  ?  55  ALA A CA  1 
ATOM   698  C  CA  B ALA A 1 55  ? 42.98000 24.19000 -2.53000  0.210 36.37000  ?  55  ALA A CA  1 
ATOM   699  C  C   A ALA A 1 55  ? 44.16800 22.71800 -2.37600  0.790 43.87000  ?  55  ALA A C   1 
ATOM   700  C  C   B ALA A 1 55  ? 44.05700 23.17400 -2.24200  0.210 42.97000  ?  55  ALA A C   1 
ATOM   701  O  O   A ALA A 1 55  ? 44.23200 21.69100 -3.06200  0.790 43.05000  ?  55  ALA A O   1 
ATOM   702  O  O   B ALA A 1 55  ? 44.24900 22.23700 -3.02200  0.210 42.25000  ?  55  ALA A O   1 
ATOM   703  C  CB  A ALA A 1 55  ? 43.85600 24.88000 -3.60100  0.790 40.90000  ?  55  ALA A CB  1 
ATOM   704  C  CB  B ALA A 1 55  ? 43.54200 25.28300 -3.43800  0.210 40.91000  ?  55  ALA A CB  1 
ATOM   705  N  N   A LEU A 1 56  ? 44.94300 22.90500 -1.31100  0.790 40.19000  ?  56  LEU A N   1 
ATOM   706  N  N   B LEU A 1 56  ? 44.76300 23.33600 -1.12900  0.210 40.46000  ?  56  LEU A N   1 
ATOM   707  C  CA  A LEU A 1 56  ? 45.90000 21.89700 -0.87800  0.790 47.85000  ?  56  LEU A CA  1 
ATOM   708  C  CA  B LEU A 1 56  ? 45.70700 22.32800 -0.68900  0.210 46.96000  ?  56  LEU A CA  1 
ATOM   709  C  C   A LEU A 1 56  ? 45.24600 20.73700 -0.13900  0.790 45.73000  ?  56  LEU A C   1 
ATOM   710  C  C   B LEU A 1 56  ? 45.07500 21.24400 0.16600   0.210 44.69000  ?  56  LEU A C   1 
ATOM   711  O  O   A LEU A 1 56  ? 45.95600 19.82400 0.29500   0.790 48.68000  ?  56  LEU A O   1 
ATOM   712  O  O   B LEU A 1 56  ? 45.79800 20.36700 0.63100   0.210 47.64000  ?  56  LEU A O   1 
ATOM   713  C  CB  A LEU A 1 56  ? 46.96600 22.53800 0.01400   0.790 41.19000  ?  56  LEU A CB  1 
ATOM   714  C  CB  B LEU A 1 56  ? 46.87400 22.98500 0.04400   0.210 41.82000  ?  56  LEU A CB  1 
ATOM   715  C  CG  A LEU A 1 56  ? 47.90400 23.51500 -0.69600  0.790 41.32000  ?  56  LEU A CG  1 
ATOM   716  C  CG  B LEU A 1 56  ? 47.60000 23.58600 -1.13000  0.210 40.97000  ?  56  LEU A CG  1 
ATOM   717  C  CD1 A LEU A 1 56  ? 48.75800 24.28500 0.29800   0.790 46.68000  ?  56  LEU A CD1 1 
ATOM   718  C  CD1 B LEU A 1 56  ? 48.68700 24.53000 -0.69300  0.210 42.14000  ?  56  LEU A CD1 1 
ATOM   719  C  CD2 A LEU A 1 56  ? 48.78300 22.77400 -1.70000  0.790 48.04000  ?  56  LEU A CD2 1 
ATOM   720  C  CD2 B LEU A 1 56  ? 48.14600 22.39200 -1.86400  0.210 41.64000  ?  56  LEU A CD2 1 
ATOM   721  N  N   A GLY A 1 57  ? 43.92500 20.74400 0.01500   0.790 44.47000  ?  57  GLY A N   1 
ATOM   722  N  N   B GLY A 1 57  ? 43.75700 21.23700 0.33300   0.210 43.32000  ?  57  GLY A N   1 
ATOM   723  C  CA  A GLY A 1 57  ? 43.24200 19.67500 0.70900   0.790 45.21000  ?  57  GLY A CA  1 
ATOM   724  C  CA  B GLY A 1 57  ? 43.12100 20.11900 0.98300   0.210 49.26000  ?  57  GLY A CA  1 
ATOM   725  C  C   A GLY A 1 57  ? 43.20600 19.80700 2.21100   0.790 57.36000  ?  57  GLY A C   1 
ATOM   726  C  C   B GLY A 1 57  ? 43.11400 20.18900 2.49600   0.210 52.43000  ?  57  GLY A C   1 
ATOM   727  O  O   A GLY A 1 57  ? 42.89900 18.82400 2.89600   0.790 59.81000  ?  57  GLY A O   1 
ATOM   728  O  O   B GLY A 1 57  ? 42.42700 19.39500 3.16000   0.210 51.24000  ?  57  GLY A O   1 
ATOM   729  N  N   A VAL A 1 58  ? 43.50100 20.97300 2.74500   0.790 47.04000  ?  58  VAL A N   1 
ATOM   730  N  N   B VAL A 1 58  ? 43.87500 21.09900 3.06900   0.210 48.77000  ?  58  VAL A N   1 
ATOM   731  C  CA  A VAL A 1 58  ? 43.53100 21.18000 4.18600   0.790 55.43000  ?  58  VAL A CA  1 
ATOM   732  C  CA  B VAL A 1 58  ? 43.74600 21.35700 4.48800   0.210 54.17000  ?  58  VAL A CA  1 
ATOM   733  C  C   A VAL A 1 58  ? 42.18600 21.73200 4.63400   0.790 55.87000  ?  58  VAL A C   1 
ATOM   734  C  C   B VAL A 1 58  ? 42.35600 21.91900 4.77400   0.210 54.61000  ?  58  VAL A C   1 
ATOM   735  O  O   A VAL A 1 58  ? 41.59600 22.59400 3.97200   0.790 45.02000  ?  58  VAL A O   1 
ATOM   736  O  O   B VAL A 1 58  ? 41.88600 22.85300 4.10200   0.210 44.44000  ?  58  VAL A O   1 
ATOM   737  C  CB  A VAL A 1 58  ? 44.68400 22.12200 4.57900   0.790 46.58000  ?  58  VAL A CB  1 
ATOM   738  C  CB  B VAL A 1 58  ? 44.85000 22.32100 4.92500   0.210 48.48000  ?  58  VAL A CB  1 
ATOM   739  C  CG1 A VAL A 1 58  ? 44.53400 22.55700 6.02800   0.790 53.88000  ?  58  VAL A CG1 1 
ATOM   740  C  CG1 B VAL A 1 58  ? 44.58300 22.80400 6.31700   0.210 54.92000  ?  58  VAL A CG1 1 
ATOM   741  C  CG2 A VAL A 1 58  ? 46.02600 21.43700 4.35100   0.790 47.37000  ?  58  VAL A CG2 1 
ATOM   742  C  CG2 B VAL A 1 58  ? 46.21400 21.64500 4.80900   0.210 49.18000  ?  58  VAL A CG2 1 
ATOM   743  N  N   A GLY A 1 59  ? 41.69300 21.22000 5.75700   0.790 54.13000  ?  59  GLY A N   1 
ATOM   744  N  N   B GLY A 1 59  ? 41.67400 21.33600 5.75300   0.210 53.73000  ?  59  GLY A N   1 
ATOM   745  C  CA  A GLY A 1 59  ? 40.46900 21.73200 6.33600   0.790 45.33000  ?  59  GLY A CA  1 
ATOM   746  C  CA  B GLY A 1 59  ? 40.45100 21.92500 6.26300   0.210 45.48000  ?  59  GLY A CA  1 
ATOM   747  C  C   A GLY A 1 59  ? 39.19300 21.15700 5.77300   0.790 47.26000  ?  59  GLY A C   1 
ATOM   748  C  C   B GLY A 1 59  ? 39.15000 21.32300 5.78100   0.210 47.09000  ?  59  GLY A C   1 
ATOM   749  O  O   A GLY A 1 59  ? 38.13100 21.76500 5.93700   0.790 44.51000  ?  59  GLY A O   1 
ATOM   750  O  O   B GLY A 1 59  ? 38.08200 21.84700 6.12500   0.210 44.13000  ?  59  GLY A O   1 
ATOM   751  N  N   A TRP A 1 60  ? 39.25800 20.00700 5.11100   0.790 42.59000  ?  60  TRP A N   1 
ATOM   752  N  N   B TRP A 1 60  ? 39.18700 20.26400 4.99600   0.210 43.66000  ?  60  TRP A N   1 
ATOM   753  C  CA  A TRP A 1 60  ? 38.06200 19.33400 4.61000   0.790 45.88000  ?  60  TRP A CA  1 
ATOM   754  C  CA  B TRP A 1 60  ? 37.94300 19.65800 4.55200   0.210 45.19000  ?  60  TRP A CA  1 
ATOM   755  C  C   A TRP A 1 60  ? 37.57000 18.42800 5.73200   0.790 59.16000  ?  60  TRP A C   1 
ATOM   756  C  C   B TRP A 1 60  ? 37.46500 18.74900 5.69100   0.210 57.54000  ?  60  TRP A C   1 
ATOM   757  O  O   A TRP A 1 60  ? 38.13100 17.35700 5.96100   0.790 64.96000  ?  60  TRP A O   1 
ATOM   758  O  O   B TRP A 1 60  ? 38.25900 17.94400 6.21300   0.210 59.56000  ?  60  TRP A O   1 
ATOM   759  C  CB  A TRP A 1 60  ? 38.36500 18.52700 3.35500   0.790 44.48000  ?  60  TRP A CB  1 
ATOM   760  C  CB  B TRP A 1 60  ? 38.14200 18.88400 3.24000   0.210 44.96000  ?  60  TRP A CB  1 
ATOM   761  C  CG  A TRP A 1 60  ? 38.89200 19.30600 2.18700   0.790 44.82000  ?  60  TRP A CG  1 
ATOM   762  C  CG  B TRP A 1 60  ? 38.87900 19.64100 2.09100   0.210 45.46000  ?  60  TRP A CG  1 
ATOM   763  C  CD1 A TRP A 1 60  ? 39.54100 20.50600 2.21400   0.790 48.36000  ?  60  TRP A CD1 1 
ATOM   764  C  CD1 B TRP A 1 60  ? 39.74600 20.72600 2.21400   0.210 47.32000  ?  60  TRP A CD1 1 
ATOM   765  C  CD2 A TRP A 1 60  ? 38.81700 18.92200 0.80900   0.790 35.78000  ?  60  TRP A CD2 1 
ATOM   766  C  CD2 B TRP A 1 60  ? 38.89900 19.28600 0.70000   0.210 41.53000  ?  60  TRP A CD2 1 
ATOM   767  N  NE1 A TRP A 1 60  ? 39.87500 20.89300 0.93800   0.790 54.58000  ?  60  TRP A NE1 1 
ATOM   768  N  NE1 B TRP A 1 60  ? 40.23700 21.09300 0.97700   0.210 49.00000  ?  60  TRP A NE1 1 
ATOM   769  C  CE2 A TRP A 1 60  ? 39.44100 19.93700 0.05700   0.790 46.35000  ?  60  TRP A CE2 1 
ATOM   770  C  CE2 B TRP A 1 60  ? 39.76300 20.21400 0.03500   0.210 45.32000  ?  60  TRP A CE2 1 
ATOM   771  C  CE3 A TRP A 1 60  ? 38.28200 17.81800 0.13900   0.790 34.77000  ?  60  TRP A CE3 1 
ATOM   772  C  CE3 B TRP A 1 60  ? 38.27900 18.28700 -0.04900  0.210 38.88000  ?  60  TRP A CE3 1 
ATOM   773  C  CZ2 A TRP A 1 60  ? 39.54400 19.88100 -1.33100  0.790 48.33000  ?  60  TRP A CZ2 1 
ATOM   774  C  CZ2 B TRP A 1 60  ? 39.99500 20.17800 -1.34400  0.210 45.27000  ?  60  TRP A CZ2 1 
ATOM   775  C  CZ3 A TRP A 1 60  ? 38.38300 17.76300 -1.23700  0.790 48.17000  ?  60  TRP A CZ3 1 
ATOM   776  C  CZ3 B TRP A 1 60  ? 38.50900 18.25400 -1.44200  0.210 49.14000  ?  60  TRP A CZ3 1 
ATOM   777  C  CH2 A TRP A 1 60  ? 39.01000 18.78800 -1.95900  0.790 51.15000  ?  60  TRP A CH2 1 
ATOM   778  C  CH2 B TRP A 1 60  ? 39.35800 19.20000 -2.07100  0.210 49.32000  ?  60  TRP A CH2 1 
ATOM   779  N  N   A VAL A 1 61  ? 36.53200 18.84600 6.45000   0.790 59.49000  ?  61  VAL A N   1 
ATOM   780  N  N   B VAL A 1 61  ? 36.22100 18.91200 6.10400   0.210 57.07000  ?  61  VAL A N   1 
ATOM   781  C  CA  A VAL A 1 61  ? 36.08300 18.15200 7.65500   0.790 54.67000  ?  61  VAL A CA  1 
ATOM   782  C  CA  B VAL A 1 61  ? 35.64000 18.24800 7.29500   0.210 51.62000  ?  61  VAL A CA  1 
ATOM   783  C  C   A VAL A 1 61  ? 34.86300 17.29400 7.31000   0.790 48.59000  ?  61  VAL A C   1 
ATOM   784  C  C   B VAL A 1 61  ? 34.54000 17.34100 6.86500   0.210 51.42000  ?  61  VAL A C   1 
ATOM   785  O  O   A VAL A 1 61  ? 33.83700 17.84700 6.89300   0.790 48.45000  ?  61  VAL A O   1 
ATOM   786  O  O   B VAL A 1 61  ? 33.60400 17.77000 6.16800   0.210 48.73000  ?  61  VAL A O   1 
ATOM   787  C  CB  A VAL A 1 61  ? 35.76000 19.12200 8.80300   0.790 50.02000  ?  61  VAL A CB  1 
ATOM   788  C  CB  B VAL A 1 61  ? 35.10200 19.28100 8.31500   0.210 51.31000  ?  61  VAL A CB  1 
ATOM   789  C  CG1 A VAL A 1 61  ? 35.42700 18.30300 10.05200  0.790 66.84000  ?  61  VAL A CG1 1 
ATOM   790  C  CG1 B VAL A 1 61  ? 34.36000 18.56600 9.47400   0.210 55.49000  ?  61  VAL A CG1 1 
ATOM   791  C  CG2 A VAL A 1 61  ? 36.92700 20.04400 9.05000   0.790 45.19000  ?  61  VAL A CG2 1 
ATOM   792  C  CG2 B VAL A 1 61  ? 36.19500 20.14300 8.83500   0.210 45.98000  ?  61  VAL A CG2 1 
ATOM   793  N  N   A PRO A 1 62  ? 34.92500 15.97700 7.46700   0.790 65.22000  ?  62  PRO A N   1 
ATOM   794  N  N   B PRO A 1 62  ? 34.50300 16.07600 7.28300   0.210 61.03000  ?  62  PRO A N   1 
ATOM   795  C  CA  A PRO A 1 62  ? 33.73200 15.14800 7.25400   0.790 57.85000  ?  62  PRO A CA  1 
ATOM   796  C  CA  B PRO A 1 62  ? 33.27200 15.32200 7.13900   0.210 56.61000  ?  62  PRO A CA  1 
ATOM   797  C  C   A PRO A 1 62  ? 32.75800 15.30200 8.41100   0.790 52.53000  ?  62  PRO A C   1 
ATOM   798  C  C   B PRO A 1 62  ? 32.40200 15.65200 8.33000   0.210 54.16000  ?  62  PRO A C   1 
ATOM   799  O  O   A PRO A 1 62  ? 33.14700 15.30500 9.58200   0.790 55.72000  ?  62  PRO A O   1 
ATOM   800  O  O   B PRO A 1 62  ? 32.87500 15.82400 9.46400   0.210 53.36000  ?  62  PRO A O   1 
ATOM   801  C  CB  A PRO A 1 62  ? 34.30400 13.72900 7.18900   0.790 48.73000  ?  62  PRO A CB  1 
ATOM   802  C  CB  B PRO A 1 62  ? 33.73700 13.86300 7.08700   0.210 52.72000  ?  62  PRO A CB  1 
ATOM   803  C  CG  A PRO A 1 62  ? 35.48700 13.78700 8.12800   0.790 57.38000  ?  62  PRO A CG  1 
ATOM   804  C  CG  B PRO A 1 62  ? 34.93000 13.86600 7.91000   0.210 55.70000  ?  62  PRO A CG  1 
ATOM   805  C  CD  A PRO A 1 62  ? 36.03800 15.20200 8.03900   0.790 56.98000  ?  62  PRO A CD  1 
ATOM   806  C  CD  B PRO A 1 62  ? 35.56600 15.24100 7.88500   0.210 57.77000  ?  62  PRO A CD  1 
ATOM   807  N  N   A VAL A 1 63  ? 31.48100 15.44000 8.07000   0.790 55.46000  ?  63  VAL A N   1 
ATOM   808  N  N   B VAL A 1 63  ? 31.12800 15.82600 8.02300   0.210 56.93000  ?  63  VAL A N   1 
ATOM   809  C  CA  A VAL A 1 63  ? 30.42500 15.63300 9.05500   0.790 55.45000  ?  63  VAL A CA  1 
ATOM   810  C  CA  B VAL A 1 63  ? 30.08800 16.18200 8.96700   0.210 57.06000  ?  63  VAL A CA  1 
ATOM   811  C  C   A VAL A 1 63  ? 29.23000 14.80100 8.60900   0.790 55.85000  ?  63  VAL A C   1 
ATOM   812  C  C   B VAL A 1 63  ? 28.92000 15.31100 8.54400   0.210 58.93000  ?  63  VAL A C   1 
ATOM   813  O  O   A VAL A 1 63  ? 28.60200 15.11200 7.58900   0.790 54.92000  ?  63  VAL A O   1 
ATOM   814  O  O   B VAL A 1 63  ? 28.21600 15.62500 7.58000   0.210 58.68000  ?  63  VAL A O   1 
ATOM   815  C  CB  A VAL A 1 63  ? 30.03500 17.10900 9.21000   0.790 47.93000  ?  63  VAL A CB  1 
ATOM   816  C  CB  B VAL A 1 63  ? 29.72900 17.67300 8.93200   0.210 48.28000  ?  63  VAL A CB  1 
ATOM   817  C  CG1 A VAL A 1 63  ? 28.88200 17.25000 10.18600  0.790 62.67000  ?  63  VAL A CG1 1 
ATOM   818  C  CG1 B VAL A 1 63  ? 28.35600 17.90000 9.50100   0.210 57.58000  ?  63  VAL A CG1 1 
ATOM   819  C  CG2 A VAL A 1 63  ? 31.23700 17.92700 9.67000   0.790 50.94000  ?  63  VAL A CG2 1 
ATOM   820  C  CG2 B VAL A 1 63  ? 30.70900 18.46300 9.74100   0.210 49.88000  ?  63  VAL A CG2 1 
ATOM   821  N  N   A ALA A 1 64  ? 28.91300 13.75000 9.37200   0.790 81.14000  ?  64  ALA A N   1 
ATOM   822  N  N   B ALA A 1 64  ? 28.72600 14.20600 9.24500   0.210 73.19000  ?  64  ALA A N   1 
ATOM   823  C  CA  A ALA A 1 64  ? 27.87000 12.80600 8.99000   0.790 72.36000  ?  64  ALA A CA  1 
ATOM   824  C  CA  B ALA A 1 64  ? 27.79800 13.18600 8.79600   0.210 70.44000  ?  64  ALA A CA  1 
ATOM   825  C  C   A ALA A 1 64  ? 28.18200 12.25500 7.60400   0.790 73.75000  ?  64  ALA A C   1 
ATOM   826  C  C   B ALA A 1 64  ? 28.27200 12.67000 7.46100   0.210 73.14000  ?  64  ALA A C   1 
ATOM   827  O  O   A ALA A 1 64  ? 29.10700 11.45100 7.44700   0.790 88.65000  ?  64  ALA A O   1 
ATOM   828  O  O   B ALA A 1 64  ? 29.33800 12.05600 7.34600   0.210 79.50000  ?  64  ALA A O   1 
ATOM   829  C  CB  A ALA A 1 64  ? 26.49800 13.47500 9.03200   0.790 68.42000  ?  64  ALA A CB  1 
ATOM   830  C  CB  B ALA A 1 64  ? 26.38500 13.74200 8.65900   0.210 67.74000  ?  64  ALA A CB  1 
ATOM   831  N  N   A GLU A 1 65  ? 27.42800 12.68500 6.59000   0.790 75.64000  ?  65  GLU A N   1 
ATOM   832  N  N   B GLU A 1 65  ? 27.49400 12.98400 6.44200   0.210 75.01000  ?  65  GLU A N   1 
ATOM   833  C  CA  A GLU A 1 65  ? 27.61500 12.19600 5.22800   0.790 77.55000  ?  65  GLU A CA  1 
ATOM   834  C  CA  B GLU A 1 65  ? 27.68000 12.42800 5.12200   0.210 77.84000  ?  65  GLU A CA  1 
ATOM   835  C  C   A GLU A 1 65  ? 28.06000 13.29100 4.26300   0.790 77.72000  ?  65  GLU A C   1 
ATOM   836  C  C   B GLU A 1 65  ? 28.21400 13.44700 4.12200   0.210 77.00000  ?  65  GLU A C   1 
ATOM   837  O  O   A GLU A 1 65  ? 28.14600 13.04200 3.05300   0.790 81.87000  ?  65  GLU A O   1 
ATOM   838  O  O   B GLU A 1 65  ? 28.39400 13.10800 2.95100   0.210 81.21000  ?  65  GLU A O   1 
ATOM   839  C  CB  A GLU A 1 65  ? 26.32300 11.55300 4.71600   0.790 88.70000  ?  65  GLU A CB  1 
ATOM   840  C  CB  B GLU A 1 65  ? 26.35100 11.83800 4.63600   0.210 87.73000  ?  65  GLU A CB  1 
ATOM   841  C  CG  A GLU A 1 65  ? 26.03500 10.18500 5.29600   0.790 101.88000 ?  65  GLU A CG  1 
ATOM   842  C  CG  B GLU A 1 65  ? 25.94400 10.60300 5.44700   0.210 98.13000  ?  65  GLU A CG  1 
ATOM   843  C  CD  A GLU A 1 65  ? 26.59600 9.05900  4.44200   0.790 120.80000 ?  65  GLU A CD  1 
ATOM   844  C  CD  B GLU A 1 65  ? 26.56800 9.31300  4.91600   0.210 113.83000 ?  65  GLU A CD  1 
ATOM   845  O  OE1 A GLU A 1 65  ? 27.34500 9.34200  3.48300   0.790 130.19000 ?  65  GLU A OE1 1 
ATOM   846  O  OE1 B GLU A 1 65  ? 27.43000 9.40000  4.01000   0.210 122.03000 ?  65  GLU A OE1 1 
ATOM   847  O  OE2 A GLU A 1 65  ? 26.28500 7.88400  4.73200   0.790 123.39000 -1 65  GLU A OE2 1 
ATOM   848  O  OE2 B GLU A 1 65  ? 26.23200 8.21800  5.42200   0.210 118.05000 -1 65  GLU A OE2 1 
ATOM   849  N  N   A ARG A 1 66  ? 28.35300 14.48500 4.76200   0.790 72.58000  ?  66  ARG A N   1 
ATOM   850  N  N   B ARG A 1 66  ? 28.49700 14.66900 4.55100   0.210 70.33000  ?  66  ARG A N   1 
ATOM   851  C  CA  A ARG A 1 66  ? 28.75700 15.61600 3.94100   0.790 55.53000  ?  66  ARG A CA  1 
ATOM   852  C  CA  B ARG A 1 66  ? 28.94400 15.73600 3.67900   0.210 56.75000  ?  66  ARG A CA  1 
ATOM   853  C  C   A ARG A 1 66  ? 30.21800 15.95500 4.20600   0.790 60.04000  ?  66  ARG A C   1 
ATOM   854  C  C   B ARG A 1 66  ? 30.37700 16.10400 4.00600   0.210 60.03000  ?  66  ARG A C   1 
ATOM   855  O  O   A ARG A 1 66  ? 30.83500 15.47300 5.15800   0.790 56.99000  ?  66  ARG A O   1 
ATOM   856  O  O   B ARG A 1 66  ? 31.01000 15.55300 4.91100   0.210 56.82000  ?  66  ARG A O   1 
ATOM   857  C  CB  A ARG A 1 66  ? 27.87200 16.83600 4.22800   0.790 57.43000  ?  66  ARG A CB  1 
ATOM   858  C  CB  B ARG A 1 66  ? 28.10400 16.98800 3.85200   0.210 58.24000  ?  66  ARG A CB  1 
ATOM   859  C  CG  A ARG A 1 66  ? 26.38800 16.59700 4.05100   0.790 76.89000  ?  66  ARG A CG  1 
ATOM   860  C  CG  B ARG A 1 66  ? 26.64800 16.77900 3.82000   0.210 72.83000  ?  66  ARG A CG  1 
ATOM   861  C  CD  A ARG A 1 66  ? 25.61000 16.80000 5.34900   0.790 80.80000  ?  66  ARG A CD  1 
ATOM   862  C  CD  B ARG A 1 66  ? 26.02400 17.25000 5.14200   0.210 71.69000  ?  66  ARG A CD  1 
ATOM   863  N  NE  A ARG A 1 66  ? 26.06300 17.95900 6.11500   0.790 58.74000  ?  66  ARG A NE  1 
ATOM   864  N  NE  B ARG A 1 66  ? 26.71200 18.39900 5.72000   0.210 58.62000  ?  66  ARG A NE  1 
ATOM   865  C  CZ  A ARG A 1 66  ? 25.70200 18.22000 7.36700   0.790 76.47000  ?  66  ARG A CZ  1 
ATOM   866  C  CZ  B ARG A 1 66  ? 26.33900 18.99800 6.84500   0.210 63.86000  ?  66  ARG A CZ  1 
ATOM   867  N  NH1 A ARG A 1 66  ? 24.86900 17.40800 8.00100   0.790 69.71000  ?  66  ARG A NH1 1 
ATOM   868  N  NH1 B ARG A 1 66  ? 25.22000 18.65600 7.47300   0.210 72.28000  ?  66  ARG A NH1 1 
ATOM   869  N  NH2 A ARG A 1 66  ? 26.16900 19.29600 7.98500   0.790 65.07000  ?  66  ARG A NH2 1 
ATOM   870  N  NH2 B ARG A 1 66  ? 27.07500 19.99700 7.32700   0.210 61.07000  ?  66  ARG A NH2 1 
ATOM   871  N  N   A THR A 1 67  ? 30.77200 16.79800 3.34200   0.790 50.62000  ?  67  THR A N   1 
ATOM   872  N  N   B THR A 1 67  ? 30.86600 17.08700 3.26300   0.210 49.82000  ?  67  THR A N   1 
ATOM   873  C  CA  A THR A 1 67  ? 32.09800 17.36700 3.54100   0.790 51.38000  ?  67  THR A CA  1 
ATOM   874  C  CA  B THR A 1 67  ? 32.07500 17.81900 3.58200   0.210 50.75000  ?  67  THR A CA  1 
ATOM   875  C  C   A THR A 1 67  ? 31.95000 18.86800 3.74700   0.790 43.76000  ?  67  THR A C   1 
ATOM   876  C  C   B THR A 1 67  ? 31.66800 19.25800 3.90900   0.210 43.01000  ?  67  THR A C   1 
ATOM   877  O  O   A THR A 1 67  ? 31.31300 19.54800 2.93700   0.790 44.50000  ?  67  THR A O   1 
ATOM   878  O  O   B THR A 1 67  ? 30.58500 19.70900 3.54600   0.210 43.20000  ?  67  THR A O   1 
ATOM   879  C  CB  A THR A 1 67  ? 33.02000 17.07800 2.35700   0.790 47.05000  ?  67  THR A CB  1 
ATOM   880  C  CB  B THR A 1 67  ? 33.10700 17.67100 2.42500   0.210 46.30000  ?  67  THR A CB  1 
ATOM   881  O  OG1 A THR A 1 67  ? 33.08500 15.66400 2.14000   0.790 53.18000  ?  67  THR A OG1 1 
ATOM   882  O  OG1 B THR A 1 67  ? 33.35700 16.27800 2.20300   0.210 50.25000  ?  67  THR A OG1 1 
ATOM   883  C  CG2 A THR A 1 67  ? 34.42000 17.60700 2.64000   0.790 42.39000  ?  67  THR A CG2 1 
ATOM   884  C  CG2 B THR A 1 67  ? 34.43500 18.35900 2.68900   0.210 43.09000  ?  67  THR A CG2 1 
ATOM   885  N  N   A VAL A 1 68  ? 32.52700 19.37500 4.83300   0.790 42.00000  ?  68  VAL A N   1 
ATOM   886  N  N   B VAL A 1 68  ? 32.48300 19.92800 4.71100   0.210 43.89000  ?  68  VAL A N   1 
ATOM   887  C  CA  A VAL A 1 68  ? 32.45000 20.78700 5.19600   0.790 45.14000  ?  68  VAL A CA  1 
ATOM   888  C  CA  B VAL A 1 68  ? 32.27600 21.32000 5.11300   0.210 43.60000  ?  68  VAL A CA  1 
ATOM   889  C  C   A VAL A 1 68  ? 33.83800 21.40200 5.06000   0.790 42.56000  ?  68  VAL A C   1 
ATOM   890  C  C   B VAL A 1 68  ? 33.61900 22.00600 5.01900   0.210 40.90000  ?  68  VAL A C   1 
ATOM   891  O  O   A VAL A 1 68  ? 34.83700 20.80600 5.47500   0.790 48.60000  ?  68  VAL A O   1 
ATOM   892  O  O   B VAL A 1 68  ? 34.59100 21.54700 5.62000   0.210 44.89000  ?  68  VAL A O   1 
ATOM   893  C  CB  A VAL A 1 68  ? 31.90900 20.98500 6.62500   0.790 43.84000  ?  68  VAL A CB  1 
ATOM   894  C  CB  B VAL A 1 68  ? 31.73300 21.47000 6.54500   0.210 45.62000  ?  68  VAL A CB  1 
ATOM   895  C  CG1 A VAL A 1 68  ? 32.42200 22.29900 7.20300   0.790 43.86000  ?  68  VAL A CG1 1 
ATOM   896  C  CG1 B VAL A 1 68  ? 32.09500 22.84900 7.09000   0.210 43.86000  ?  68  VAL A CG1 1 
ATOM   897  C  CG2 A VAL A 1 68  ? 30.39200 20.95800 6.61600   0.790 60.08000  ?  68  VAL A CG2 1 
ATOM   898  C  CG2 B VAL A 1 68  ? 30.22000 21.25500 6.57000   0.210 57.94000  ?  68  VAL A CG2 1 
ATOM   899  N  N   A PHE A 1 69  ? 33.89400 22.60000 4.48600   0.790 38.87000  ?  69  PHE A N   1 
ATOM   900  N  N   B PHE A 1 69  ? 33.69300 23.09100 4.27900   0.210 41.34000  ?  69  PHE A N   1 
ATOM   901  C  CA  A PHE A 1 69  ? 35.14800 23.29300 4.19100   0.790 41.09000  ?  69  PHE A CA  1 
ATOM   902  C  CA  B PHE A 1 69  ? 34.99800 23.71800 4.11700   0.210 41.00000  ?  69  PHE A CA  1 
ATOM   903  C  C   A PHE A 1 69  ? 35.34800 24.37500 5.24300   0.790 40.37000  ?  69  PHE A C   1 
ATOM   904  C  C   B PHE A 1 69  ? 35.08800 24.79600 5.17500   0.210 41.68000  ?  69  PHE A C   1 
ATOM   905  O  O   A PHE A 1 69  ? 34.79500 25.47300 5.14000   0.790 45.80000  ?  69  PHE A O   1 
ATOM   906  O  O   B PHE A 1 69  ? 34.60000 25.92900 4.99900   0.210 40.41000  ?  69  PHE A O   1 
ATOM   907  C  CB  A PHE A 1 69  ? 35.10100 23.86200 2.78000   0.790 33.86000  ?  69  PHE A CB  1 
ATOM   908  C  CB  B PHE A 1 69  ? 35.19900 24.22300 2.69600   0.210 33.57000  ?  69  PHE A CB  1 
ATOM   909  C  CG  A PHE A 1 69  ? 34.87600 22.81700 1.72800   0.790 36.09000  ?  69  PHE A CG  1 
ATOM   910  C  CG  B PHE A 1 69  ? 35.02200 23.13300 1.68800   0.210 36.07000  ?  69  PHE A CG  1 
ATOM   911  C  CD1 A PHE A 1 69  ? 35.90300 21.96900 1.35500   0.790 32.84000  ?  69  PHE A CD1 1 
ATOM   912  C  CD1 B PHE A 1 69  ? 36.07100 22.29300 1.36600   0.210 33.48000  ?  69  PHE A CD1 1 
ATOM   913  C  CD2 A PHE A 1 69  ? 33.63900 22.67100 1.12500   0.790 27.05000  ?  69  PHE A CD2 1 
ATOM   914  C  CD2 B PHE A 1 69  ? 33.77700 22.87800 1.16800   0.210 28.76000  ?  69  PHE A CD2 1 
ATOM   915  C  CE1 A PHE A 1 69  ? 35.70300 20.99700 0.39200   0.790 34.50000  ?  69  PHE A CE1 1 
ATOM   916  C  CE1 B PHE A 1 69  ? 35.88200 21.26600 0.52200   0.210 34.59000  ?  69  PHE A CE1 1 
ATOM   917  C  CE2 A PHE A 1 69  ? 33.43200 21.70400 0.16300   0.790 37.20000  ?  69  PHE A CE2 1 
ATOM   918  C  CE2 B PHE A 1 69  ? 33.59700 21.86500 0.32200   0.210 35.82000  ?  69  PHE A CE2 1 
ATOM   919  C  CZ  A PHE A 1 69  ? 34.46600 20.86400 -0.20400  0.790 25.51000  ?  69  PHE A CZ  1 
ATOM   920  C  CZ  B PHE A 1 69  ? 34.64300 21.03700 -0.00500  0.210 27.35000  ?  69  PHE A CZ  1 
ATOM   921  N  N   A ALA A 1 70  ? 36.15100 24.05900 6.25100   0.790 36.60000  ?  70  ALA A N   1 
ATOM   922  N  N   B ALA A 1 70  ? 35.70500 24.42500 6.29100   0.210 39.07000  ?  70  ALA A N   1 
ATOM   923  C  CA  A ALA A 1 70  ? 36.29500 24.92500 7.40900   0.790 37.79000  ?  70  ALA A CA  1 
ATOM   924  C  CA  B ALA A 1 70  ? 36.02600 25.41100 7.31200   0.210 36.77000  ?  70  ALA A CA  1 
ATOM   925  C  C   A ALA A 1 70  ? 36.98400 26.23800 7.06100   0.790 38.61000  ?  70  ALA A C   1 
ATOM   926  C  C   B ALA A 1 70  ? 36.58600 26.67700 6.70200   0.210 36.44000  ?  70  ALA A C   1 
ATOM   927  O  O   A ALA A 1 70  ? 36.59600 27.28500 7.59300   0.790 37.81000  ?  70  ALA A O   1 
ATOM   928  O  O   B ALA A 1 70  ? 36.14200 27.76300 7.09700   0.210 35.98000  ?  70  ALA A O   1 
ATOM   929  C  CB  A ALA A 1 70  ? 37.06800 24.20400 8.51400   0.790 38.62000  ?  70  ALA A CB  1 
ATOM   930  C  CB  B ALA A 1 70  ? 37.00200 24.82800 8.34600   0.210 36.86000  ?  70  ALA A CB  1 
ATOM   931  N  N   A PRO A 1 71  ? 38.00700 26.24300 6.20100   0.790 35.19000  ?  71  PRO A N   1 
ATOM   932  N  N   B PRO A 1 71  ? 37.51200 26.62000 5.73600   0.210 35.01000  ?  71  PRO A N   1 
ATOM   933  C  CA  A PRO A 1 71  ? 38.64900 27.52900 5.87300   0.790 42.43000  ?  71  PRO A CA  1 
ATOM   934  C  CA  B PRO A 1 71  ? 38.17300 27.89000 5.32000   0.210 39.81000  ?  71  PRO A CA  1 
ATOM   935  C  C   A PRO A 1 71  ? 37.68300 28.54100 5.28200   0.790 37.24000  ?  71  PRO A C   1 
ATOM   936  C  C   B PRO A 1 71  ? 37.26400 28.83100 4.55100   0.210 31.74000  ?  71  PRO A C   1 
ATOM   937  O  O   A PRO A 1 71  ? 37.85100 29.74900 5.49800   0.790 28.18000  ?  71  PRO A O   1 
ATOM   938  O  O   B PRO A 1 71  ? 37.46400 30.05000 4.57200   0.210 26.20000  ?  71  PRO A O   1 
ATOM   939  C  CB  A PRO A 1 71  ? 39.74900 27.13200 4.87800   0.790 39.16000  ?  71  PRO A CB  1 
ATOM   940  C  CB  B PRO A 1 71  ? 39.36100 27.41300 4.48000   0.210 39.45000  ?  71  PRO A CB  1 
ATOM   941  C  CG  A PRO A 1 71  ? 40.07500 25.71100 5.24300   0.790 43.30000  ?  71  PRO A CG  1 
ATOM   942  C  CG  B PRO A 1 71  ? 39.59500 25.98400 4.94000   0.210 41.24000  ?  71  PRO A CG  1 
ATOM   943  C  CD  A PRO A 1 71  ? 38.74200 25.09900 5.62400   0.790 32.96000  ?  71  PRO A CD  1 
ATOM   944  C  CD  B PRO A 1 71  ? 38.24900 25.42600 5.27200   0.210 34.34000  ?  71  PRO A CD  1 
ATOM   945  N  N   A ARG A 1 72  ? 36.66300 28.07900 4.55600   0.790 32.40000  ?  72  ARG A N   1 
ATOM   946  N  N   B ARG A 1 72  ? 36.23600 28.27800 3.91800   0.210 36.29000  ?  72  ARG A N   1 
ATOM   947  C  CA  A ARG A 1 72  ? 35.67900 28.99800 3.99600   0.790 34.63000  ?  72  ARG A CA  1 
ATOM   948  C  CA  B ARG A 1 72  ? 35.11200 29.06200 3.42500   0.210 36.11000  ?  72  ARG A CA  1 
ATOM   949  C  C   A ARG A 1 72  ? 35.02800 29.84300 5.08400   0.790 28.97000  ?  72  ARG A C   1 
ATOM   950  C  C   B ARG A 1 72  ? 34.45000 29.89100 4.53200   0.210 31.08000  ?  72  ARG A C   1 
ATOM   951  O  O   A ARG A 1 72  ? 34.82100 31.04800 4.90200   0.790 33.06000  ?  72  ARG A O   1 
ATOM   952  O  O   B ARG A 1 72  ? 34.19100 31.07800 4.34200   0.210 37.26000  ?  72  ARG A O   1 
ATOM   953  C  CB  A ARG A 1 72  ? 34.62300 28.21300 3.21500   0.790 35.07000  ?  72  ARG A CB  1 
ATOM   954  C  CB  B ARG A 1 72  ? 34.10200 28.13400 2.76300   0.210 32.62000  ?  72  ARG A CB  1 
ATOM   955  C  CG  A ARG A 1 72  ? 33.29000 28.91800 3.06800   0.790 31.64000  ?  72  ARG A CG  1 
ATOM   956  C  CG  B ARG A 1 72  ? 32.72100 28.48900 3.08400   0.210 34.60000  ?  72  ARG A CG  1 
ATOM   957  C  CD  A ARG A 1 72  ? 32.22300 27.96400 2.53700   0.790 29.71000  ?  72  ARG A CD  1 
ATOM   958  C  CD  B ARG A 1 72  ? 31.85300 27.38000 2.67300   0.210 29.18000  ?  72  ARG A CD  1 
ATOM   959  N  NE  A ARG A 1 72  ? 32.43400 27.64800 1.12300   0.790 35.57000  ?  72  ARG A NE  1 
ATOM   960  N  NE  B ARG A 1 72  ? 31.87300 27.32800 1.21400   0.210 35.92000  ?  72  ARG A NE  1 
ATOM   961  C  CZ  A ARG A 1 72  ? 31.81300 26.67200 0.46700   0.790 36.70000  ?  72  ARG A CZ  1 
ATOM   962  C  CZ  B ARG A 1 72  ? 31.41400 26.32100 0.48000   0.210 35.39000  ?  72  ARG A CZ  1 
ATOM   963  N  NH1 A ARG A 1 72  ? 30.93500 25.90300 1.09300   0.790 41.71000  ?  72  ARG A NH1 1 
ATOM   964  N  NH1 B ARG A 1 72  ? 30.82300 25.27600 1.01500   0.210 41.24000  ?  72  ARG A NH1 1 
ATOM   965  N  NH2 A ARG A 1 72  ? 32.07500 26.46600 -0.81500  0.790 39.92000  ?  72  ARG A NH2 1 
ATOM   966  N  NH2 B ARG A 1 72  ? 31.52800 26.36700 -0.83100  0.210 36.16000  ?  72  ARG A NH2 1 
ATOM   967  N  N   A TYR A 1 73  ? 34.66900 29.22900 6.21200   0.790 42.06000  ?  73  TYR A N   1 
ATOM   968  N  N   B TYR A 1 73  ? 34.13100 29.30000 5.68600   0.210 34.14000  ?  73  TYR A N   1 
ATOM   969  C  CA  A TYR A 1 73  ? 33.93600 29.97100 7.23200   0.790 26.32000  ?  73  TYR A CA  1 
ATOM   970  C  CA  B TYR A 1 73  ? 33.39800 30.10100 6.67900   0.210 30.01000  ?  73  TYR A CA  1 
ATOM   971  C  C   A TYR A 1 73  ? 34.85100 30.87900 8.04300   0.790 27.72000  ?  73  TYR A C   1 
ATOM   972  C  C   B TYR A 1 73  ? 34.33700 31.06900 7.41600   0.210 27.02000  ?  73  TYR A C   1 
ATOM   973  O  O   A TYR A 1 73  ? 34.44200 31.98000 8.42500   0.790 32.00000  ?  73  TYR A O   1 
ATOM   974  O  O   B TYR A 1 73  ? 33.97700 32.21400 7.65600   0.210 25.13000  ?  73  TYR A O   1 
ATOM   975  C  CB  A TYR A 1 73  ? 33.18000 29.00100 8.13500   0.790 32.20000  ?  73  TYR A CB  1 
ATOM   976  C  CB  B TYR A 1 73  ? 32.60200 29.20000 7.64300   0.210 32.40000  ?  73  TYR A CB  1 
ATOM   977  C  CG  A TYR A 1 73  ? 32.10800 28.25500 7.38000   0.790 31.13000  ?  73  TYR A CG  1 
ATOM   978  C  CG  B TYR A 1 73  ? 31.56900 28.27000 6.95100   0.210 31.19000  ?  73  TYR A CG  1 
ATOM   979  C  CD1 A TYR A 1 73  ? 30.86800 28.83100 7.13900   0.790 33.14000  ?  73  TYR A CD1 1 
ATOM   980  C  CD1 B TYR A 1 73  ? 30.27500 28.69000 6.58800   0.210 32.02000  ?  73  TYR A CD1 1 
ATOM   981  C  CD2 A TYR A 1 73  ? 32.34500 26.98400 6.88100   0.790 28.99000  ?  73  TYR A CD2 1 
ATOM   982  C  CD2 B TYR A 1 73  ? 31.93300 26.98900 6.61800   0.210 29.22000  ?  73  TYR A CD2 1 
ATOM   983  C  CE1 A TYR A 1 73  ? 29.89100 28.15400 6.43700   0.790 25.87000  ?  73  TYR A CE1 1 
ATOM   984  C  CE1 B TYR A 1 73  ? 29.34900 27.82500 5.94000   0.210 23.13000  ?  73  TYR A CE1 1 
ATOM   985  C  CE2 A TYR A 1 73  ? 31.37500 26.30000 6.17700   0.790 28.51000  ?  73  TYR A CE2 1 
ATOM   986  C  CE2 B TYR A 1 73  ? 31.07100 26.14700 5.95700   0.210 32.09000  ?  73  TYR A CE2 1 
ATOM   987  C  CZ  A TYR A 1 73  ? 30.15100 26.89000 5.95900   0.790 32.75000  ?  73  TYR A CZ  1 
ATOM   988  C  CZ  B TYR A 1 73  ? 29.80500 26.54900 5.61000   0.210 34.25000  ?  73  TYR A CZ  1 
ATOM   989  O  OH  A TYR A 1 73  ? 29.18300 26.20900 5.25700   0.790 40.71000  ?  73  TYR A OH  1 
ATOM   990  O  OH  B TYR A 1 73  ? 29.06400 25.59700 4.96500   0.210 43.40000  ?  73  TYR A OH  1 
ATOM   991  N  N   A ILE A 1 74  ? 36.09100 30.46000 8.30100   0.790 28.67000  ?  74  ILE A N   1 
ATOM   992  N  N   B ILE A 1 74  ? 35.56600 30.66900 7.72800   0.210 28.83000  ?  74  ILE A N   1 
ATOM   993  C  CA  A ILE A 1 74  ? 37.04400 31.37400 8.92600   0.790 32.24000  ?  74  ILE A CA  1 
ATOM   994  C  CA  B ILE A 1 74  ? 36.45100 31.60100 8.43400   0.210 30.44000  ?  74  ILE A CA  1 
ATOM   995  C  C   A ILE A 1 74  ? 37.24000 32.60000 8.04000   0.790 30.27000  ?  74  ILE A C   1 
ATOM   996  C  C   B ILE A 1 74  ? 36.50600 32.90800 7.66900   0.210 27.69000  ?  74  ILE A C   1 
ATOM   997  O  O   A ILE A 1 74  ? 37.22300 33.74200 8.51200   0.790 37.31000  ?  74  ILE A O   1 
ATOM   998  O  O   B ILE A 1 74  ? 36.17300 33.97800 8.17600   0.210 27.20000  ?  74  ILE A O   1 
ATOM   999  C  CB  A ILE A 1 74  ? 38.37700 30.66000 9.20500   0.790 39.16000  ?  74  ILE A CB  1 
ATOM   1000 C  CB  B ILE A 1 74  ? 37.87000 31.02300 8.63400   0.210 35.33000  ?  74  ILE A CB  1 
ATOM   1001 C  CG1 A ILE A 1 74  ? 38.22500 29.67300 10.36500  0.790 35.82000  ?  74  ILE A CG1 1 
ATOM   1002 C  CG1 B ILE A 1 74  ? 37.89800 29.91800 9.68900   0.210 39.72000  ?  74  ILE A CG1 1 
ATOM   1003 C  CG2 A ILE A 1 74  ? 39.45800 31.67200 9.55200   0.790 29.88000  ?  74  ILE A CG2 1 
ATOM   1004 C  CG2 B ILE A 1 74  ? 38.80500 32.06800 9.27300   0.210 35.84000  ?  74  ILE A CG2 1 
ATOM   1005 C  CD1 A ILE A 1 74  ? 37.63700 28.34600 9.97000   0.790 51.97000  ?  74  ILE A CD1 1 
ATOM   1006 C  CD1 B ILE A 1 74  ? 37.56600 28.64000 9.23400   0.210 43.19000  ?  74  ILE A CD1 1 
ATOM   1007 N  N   A ASP A 1 75  ? 37.43000 32.37200 6.73800   0.790 32.90000  ?  75  ASP A N   1 
ATOM   1008 N  N   B ASP A 1 75  ? 36.97700 32.82300 6.44000   0.210 30.46000  ?  75  ASP A N   1 
ATOM   1009 C  CA  A ASP A 1 75  ? 37.48100 33.45200 5.75600   0.790 25.43000  ?  75  ASP A CA  1 
ATOM   1010 C  CA  B ASP A 1 75  ? 36.89100 33.80900 5.38400   0.210 28.11000  ?  75  ASP A CA  1 
ATOM   1011 C  C   A ASP A 1 75  ? 36.29000 34.38800 5.91100   0.790 27.88000  ?  75  ASP A C   1 
ATOM   1012 C  C   B ASP A 1 75  ? 35.84000 34.86200 5.71500   0.210 27.47000  ?  75  ASP A C   1 
ATOM   1013 O  O   A ASP A 1 75  ? 36.45400 35.59400 6.12600   0.790 28.57000  ?  75  ASP A O   1 
ATOM   1014 O  O   B ASP A 1 75  ? 36.13800 36.00900 6.10900   0.210 25.01000  ?  75  ASP A O   1 
ATOM   1015 C  CB  A ASP A 1 75  ? 37.54300 32.82400 4.35500   0.790 31.70000  ?  75  ASP A CB  1 
ATOM   1016 C  CB  B ASP A 1 75  ? 36.59100 33.02500 4.08200   0.210 28.83000  ?  75  ASP A CB  1 
ATOM   1017 C  CG  A ASP A 1 75  ? 37.21300 33.79700 3.22100   0.790 30.25000  ?  75  ASP A CG  1 
ATOM   1018 C  CG  B ASP A 1 75  ? 36.63800 33.89600 2.81400   0.210 33.97000  ?  75  ASP A CG  1 
ATOM   1019 O  OD1 A ASP A 1 75  ? 36.92900 34.98800 3.46200   0.790 30.50000  ?  75  ASP A OD1 1 
ATOM   1020 O  OD1 B ASP A 1 75  ? 37.14500 35.02500 2.94000   0.210 30.18000  ?  75  ASP A OD1 1 
ATOM   1021 O  OD2 A ASP A 1 75  ? 37.24200 33.34600 2.05200   0.790 32.13000  -1 75  ASP A OD2 1 
ATOM   1022 O  OD2 B ASP A 1 75  ? 36.19600 33.42800 1.70300   0.210 32.51000  -1 75  ASP A OD2 1 
ATOM   1023 N  N   A TRP A 1 76  ? 35.07600 33.84300 5.81400   0.790 24.77000  ?  76  TRP A N   1 
ATOM   1024 N  N   B TRP A 1 76  ? 34.61300 34.39200 5.58300   0.210 23.18000  ?  76  TRP A N   1 
ATOM   1025 C  CA  A TRP A 1 76  ? 33.88800 34.68900 5.84900   0.790 19.84000  ?  76  TRP A CA  1 
ATOM   1026 C  CA  B TRP A 1 76  ? 33.41300 35.17500 5.75800   0.210 19.89000  ?  76  TRP A CA  1 
ATOM   1027 C  C   A TRP A 1 76  ? 33.81800 35.49200 7.14400   0.790 27.36000  ?  76  TRP A C   1 
ATOM   1028 C  C   B TRP A 1 76  ? 33.30900 35.75900 7.14800   0.210 26.55000  ?  76  TRP A C   1 
ATOM   1029 O  O   A TRP A 1 76  ? 33.44500 36.67000 7.13100   0.790 29.14000  ?  76  TRP A O   1 
ATOM   1030 O  O   B TRP A 1 76  ? 32.67500 36.81200 7.31600   0.210 25.47000  ?  76  TRP A O   1 
ATOM   1031 C  CB  A TRP A 1 76  ? 32.63400 33.83000 5.67500   0.790 21.99000  ?  76  TRP A CB  1 
ATOM   1032 C  CB  B TRP A 1 76  ? 32.19800 34.28000 5.53500   0.210 22.46000  ?  76  TRP A CB  1 
ATOM   1033 C  CG  A TRP A 1 76  ? 32.44500 33.27600 4.28100   0.790 30.23000  ?  76  TRP A CG  1 
ATOM   1034 C  CG  B TRP A 1 76  ? 32.02400 33.67900 4.13800   0.210 29.36000  ?  76  TRP A CG  1 
ATOM   1035 C  CD1 A TRP A 1 76  ? 33.23900 33.49400 3.19500   0.790 28.57000  ?  76  TRP A CD1 1 
ATOM   1036 C  CD1 B TRP A 1 76  ? 32.72900 33.97100 2.99300   0.210 28.30000  ?  76  TRP A CD1 1 
ATOM   1037 C  CD2 A TRP A 1 76  ? 31.39100 32.41200 3.83900   0.790 27.75000  ?  76  TRP A CD2 1 
ATOM   1038 C  CD2 B TRP A 1 76  ? 31.09800 32.66600 3.78300   0.210 28.85000  ?  76  TRP A CD2 1 
ATOM   1039 N  NE1 A TRP A 1 76  ? 32.74300 32.82600 2.10200   0.790 32.91000  ?  76  TRP A NE1 1 
ATOM   1040 N  NE1 B TRP A 1 76  ? 32.26900 33.21400 1.93900   0.210 32.27000  ?  76  TRP A NE1 1 
ATOM   1041 C  CE2 A TRP A 1 76  ? 31.61000 32.14900 2.47200   0.790 32.27000  ?  76  TRP A CE2 1 
ATOM   1042 C  CE2 B TRP A 1 76  ? 31.26200 32.40200 2.40200   0.210 31.42000  ?  76  TRP A CE2 1 
ATOM   1043 C  CE3 A TRP A 1 76  ? 30.28300 31.83300 4.46700   0.790 30.27000  ?  76  TRP A CE3 1 
ATOM   1044 C  CE3 B TRP A 1 76  ? 30.11800 31.95500 4.50600   0.210 30.53000  ?  76  TRP A CE3 1 
ATOM   1045 C  CZ2 A TRP A 1 76  ? 30.76100 31.33400 1.72200   0.790 25.99000  ?  76  TRP A CZ2 1 
ATOM   1046 C  CZ2 B TRP A 1 76  ? 30.46000 31.48200 1.71900   0.210 27.02000  ?  76  TRP A CZ2 1 
ATOM   1047 C  CZ3 A TRP A 1 76  ? 29.44200 31.02300 3.72000   0.790 38.64000  ?  76  TRP A CZ3 1 
ATOM   1048 C  CZ3 B TRP A 1 76  ? 29.35400 31.02600 3.85200   0.210 37.35000  ?  76  TRP A CZ3 1 
ATOM   1049 C  CH2 A TRP A 1 76  ? 29.68600 30.78200 2.36400   0.790 35.23000  ?  76  TRP A CH2 1 
ATOM   1050 C  CH2 B TRP A 1 76  ? 29.50600 30.82300 2.44400   0.210 34.45000  ?  76  TRP A CH2 1 
ATOM   1051 N  N   A ILE A 1 77  ? 34.17600 34.87300 8.27200   0.790 27.85000  ?  77  ILE A N   1 
ATOM   1052 N  N   B ILE A 1 77  ? 33.78400 35.02700 8.18000   0.210 28.87000  ?  77  ILE A N   1 
ATOM   1053 C  CA  A ILE A 1 77  ? 34.04600 35.54200 9.56500   0.790 24.06000  ?  77  ILE A CA  1 
ATOM   1054 C  CA  B ILE A 1 77  ? 33.77800 35.61000 9.50800   0.210 24.86000  ?  77  ILE A CA  1 
ATOM   1055 C  C   A ILE A 1 77  ? 34.96800 36.74900 9.65500   0.790 26.93000  ?  77  ILE A C   1 
ATOM   1056 C  C   B ILE A 1 77  ? 34.57400 36.86600 9.47900   0.210 24.78000  ?  77  ILE A C   1 
ATOM   1057 O  O   A ILE A 1 77  ? 34.66900 37.71900 10.36500  0.790 26.75000  ?  77  ILE A O   1 
ATOM   1058 O  O   B ILE A 1 77  ? 34.13700 37.90700 9.97400   0.210 21.00000  ?  77  ILE A O   1 
ATOM   1059 C  CB  A ILE A 1 77  ? 34.34100 34.55300 10.71200  0.790 28.48000  ?  77  ILE A CB  1 
ATOM   1060 C  CB  B ILE A 1 77  ? 34.35200 34.64200 10.54900  0.210 28.64000  ?  77  ILE A CB  1 
ATOM   1061 C  CG1 A ILE A 1 77  ? 33.25200 33.48500 10.82700  0.790 30.40000  ?  77  ILE A CG1 1 
ATOM   1062 C  CG1 B ILE A 1 77  ? 33.47500 33.40300 10.59100  0.210 29.71000  ?  77  ILE A CG1 1 
ATOM   1063 C  CG2 A ILE A 1 77  ? 34.48500 35.30100 12.04300  0.790 27.66000  ?  77  ILE A CG2 1 
ATOM   1064 C  CG2 B ILE A 1 77  ? 34.44100 35.40700 11.87700  0.210 26.95000  ?  77  ILE A CG2 1 
ATOM   1065 C  CD1 A ILE A 1 77  ? 33.66200 32.27300 11.66000  0.790 34.71000  ?  77  ILE A CD1 1 
ATOM   1066 C  CD1 B ILE A 1 77  ? 34.06200 32.28400 11.25200  0.210 34.77000  ?  77  ILE A CD1 1 
ATOM   1067 N  N   A LEU A 1 78  ? 36.10700 36.70600 8.96700   0.790 27.70000  ?  78  LEU A N   1 
ATOM   1068 N  N   B LEU A 1 78  ? 35.76600 36.77000 8.88800   0.210 27.83000  ?  78  LEU A N   1 
ATOM   1069 C  CA  A LEU A 1 78  ? 37.06000 37.80400 9.03000   0.790 28.25000  ?  78  LEU A CA  1 
ATOM   1070 C  CA  B LEU A 1 78  ? 36.72100 37.86300 8.81900   0.210 28.18000  ?  78  LEU A CA  1 
ATOM   1071 C  C   A LEU A 1 78  ? 36.87200 38.81000 7.91000   0.790 35.06000  ?  78  LEU A C   1 
ATOM   1072 C  C   B LEU A 1 78  ? 36.42400 38.82800 7.68400   0.210 33.18000  ?  78  LEU A C   1 
ATOM   1073 O  O   A LEU A 1 78  ? 37.12500 40.00400 8.11300   0.790 38.49000  ?  78  LEU A O   1 
ATOM   1074 O  O   B LEU A 1 78  ? 36.59000 40.03900 7.84800   0.210 36.33000  ?  78  LEU A O   1 
ATOM   1075 C  CB  A LEU A 1 78  ? 38.49000 37.26600 8.97400   0.790 33.25000  ?  78  LEU A CB  1 
ATOM   1076 C  CB  B LEU A 1 78  ? 38.15000 37.31800 8.65500   0.210 30.08000  ?  78  LEU A CB  1 
ATOM   1077 C  CG  A LEU A 1 78  ? 38.90800 36.33500 10.11100  0.790 36.40000  ?  78  LEU A CG  1 
ATOM   1078 C  CG  B LEU A 1 78  ? 39.07500 36.92300 9.81300   0.210 37.12000  ?  78  LEU A CG  1 
ATOM   1079 C  CD1 A LEU A 1 78  ? 40.23100 35.67100 9.76900   0.790 35.69000  ?  78  LEU A CD1 1 
ATOM   1080 C  CD1 B LEU A 1 78  ? 40.32200 36.22900 9.32100   0.210 30.62000  ?  78  LEU A CD1 1 
ATOM   1081 C  CD2 A LEU A 1 78  ? 38.98800 37.10000 11.41200  0.790 36.18000  ?  78  LEU A CD2 1 
ATOM   1082 C  CD2 B LEU A 1 78  ? 39.46200 38.21700 10.62300  0.210 32.80000  ?  78  LEU A CD2 1 
ATOM   1083 N  N   A THR A 1 79  ? 36.44300 38.35900 6.73200   0.790 33.99000  ?  79  THR A N   1 
ATOM   1084 N  N   B THR A 1 79  ? 36.12800 38.32900 6.48100   0.210 31.00000  ?  79  THR A N   1 
ATOM   1085 C  CA  A THR A 1 79  ? 36.37400 39.24600 5.57900   0.790 27.44000  ?  79  THR A CA  1 
ATOM   1086 C  CA  B THR A 1 79  ? 36.24800 39.27000 5.37000   0.210 28.20000  ?  79  THR A CA  1 
ATOM   1087 C  C   A THR A 1 79  ? 35.04700 39.99000 5.48900   0.790 32.22000  ?  79  THR A C   1 
ATOM   1088 C  C   B THR A 1 79  ? 35.05600 40.19700 5.35500   0.210 31.67000  ?  79  THR A C   1 
ATOM   1089 O  O   A THR A 1 79  ? 35.02800 41.16300 5.09800   0.790 32.53000  ?  79  THR A O   1 
ATOM   1090 O  O   B THR A 1 79  ? 35.20600 41.38000 5.06900   0.210 31.05000  ?  79  THR A O   1 
ATOM   1091 C  CB  A THR A 1 79  ? 36.61300 38.46800 4.27700   0.790 29.85000  ?  79  THR A CB  1 
ATOM   1092 C  CB  B THR A 1 79  ? 36.43200 38.58800 3.98300   0.210 27.73000  ?  79  THR A CB  1 
ATOM   1093 O  OG1 A THR A 1 79  ? 35.61000 37.46200 4.10700   0.790 32.17000  ?  79  THR A OG1 1 
ATOM   1094 O  OG1 B THR A 1 79  ? 35.36500 37.67400 3.69200   0.210 27.41000  ?  79  THR A OG1 1 
ATOM   1095 C  CG2 A THR A 1 79  ? 37.98900 37.81800 4.28400   0.790 33.06000  ?  79  THR A CG2 1 
ATOM   1096 C  CG2 B THR A 1 79  ? 37.81700 37.95800 3.75600   0.210 28.80000  ?  79  THR A CG2 1 
ATOM   1097 N  N   A THR A 1 80  ? 33.93100 39.35000 5.84400   0.790 28.80000  ?  80  THR A N   1 
ATOM   1098 N  N   B THR A 1 80  ? 33.89600 39.69800 5.71900   0.210 29.51000  ?  80  THR A N   1 
ATOM   1099 C  CA  A THR A 1 80  ? 32.65200 40.04700 5.73700   0.790 32.12000  ?  80  THR A CA  1 
ATOM   1100 C  CA  B THR A 1 80  ? 32.67600 40.49200 5.61500   0.210 32.23000  ?  80  THR A CA  1 
ATOM   1101 C  C   A THR A 1 80  ? 32.55800 41.25500 6.66400   0.790 32.35000  ?  80  THR A C   1 
ATOM   1102 C  C   B THR A 1 80  ? 32.53700 41.65100 6.61700   0.210 33.98000  ?  80  THR A C   1 
ATOM   1103 O  O   A THR A 1 80  ? 31.98900 42.27500 6.23600   0.790 36.20000  ?  80  THR A O   1 
ATOM   1104 O  O   B THR A 1 80  ? 31.85700 42.63400 6.29100   0.210 35.50000  ?  80  THR A O   1 
ATOM   1105 C  CB  A THR A 1 80  ? 31.47500 39.08800 5.98000   0.790 25.69000  ?  80  THR A CB  1 
ATOM   1106 C  CB  B THR A 1 80  ? 31.44600 39.55400 5.66100   0.210 28.73000  ?  80  THR A CB  1 
ATOM   1107 O  OG1 A THR A 1 80  ? 31.57900 38.47200 7.27100   0.790 31.54000  ?  80  THR A OG1 1 
ATOM   1108 O  OG1 B THR A 1 80  ? 31.09100 39.22600 6.99500   0.210 25.61000  ?  80  THR A OG1 1 
ATOM   1109 C  CG2 A THR A 1 80  ? 31.42100 38.02100 4.89000   0.790 27.91000  ?  80  THR A CG2 1 
ATOM   1110 C  CG2 B THR A 1 80  ? 31.77000 38.25500 4.88100   0.210 27.32000  ?  80  THR A CG2 1 
ATOM   1111 N  N   A PRO A 1 81  ? 33.06400 41.23400 7.90700   0.790 37.09000  ?  81  PRO A N   1 
ATOM   1112 N  N   B PRO A 1 81  ? 33.14100 41.62800 7.80500   0.210 37.46000  ?  81  PRO A N   1 
ATOM   1113 C  CA  A PRO A 1 81  ? 33.03500 42.47900 8.69800   0.790 32.80000  ?  81  PRO A CA  1 
ATOM   1114 C  CA  B PRO A 1 81  ? 33.12900 42.86700 8.58400   0.210 33.60000  ?  81  PRO A CA  1 
ATOM   1115 C  C   A PRO A 1 81  ? 33.88400 43.57800 8.08400   0.790 36.21000  ?  81  PRO A C   1 
ATOM   1116 C  C   B PRO A 1 81  ? 33.93000 43.92900 7.88800   0.210 34.88000  ?  81  PRO A C   1 
ATOM   1117 O  O   A PRO A 1 81  ? 33.57700 44.76200 8.26700   0.790 33.45000  ?  81  PRO A O   1 
ATOM   1118 O  O   B PRO A 1 81  ? 33.53600 45.10000 7.89900   0.210 31.40000  ?  81  PRO A O   1 
ATOM   1119 C  CB  A PRO A 1 81  ? 33.55900 42.05200 10.07800  0.790 35.37000  ?  81  PRO A CB  1 
ATOM   1120 C  CB  B PRO A 1 81  ? 33.76200 42.46800 9.90800   0.210 34.57000  ?  81  PRO A CB  1 
ATOM   1121 C  CG  A PRO A 1 81  ? 34.34100 40.80500 9.82500   0.790 41.95000  ?  81  PRO A CG  1 
ATOM   1122 C  CG  B PRO A 1 81  ? 34.58000 41.28500 9.57600   0.210 34.36000  ?  81  PRO A CG  1 
ATOM   1123 C  CD  A PRO A 1 81  ? 33.66900 40.11500 8.65700   0.790 32.08000  ?  81  PRO A CD  1 
ATOM   1124 C  CD  B PRO A 1 81  ? 33.75600 40.53800 8.56600   0.210 32.46000  ?  81  PRO A CD  1 
ATOM   1125 N  N   A LEU A 1 82  ? 34.93700 43.21600 7.34800   0.790 31.92000  ?  82  LEU A N   1 
ATOM   1126 N  N   B LEU A 1 82  ? 35.06600 43.54000 7.30700   0.210 31.15000  ?  82  LEU A N   1 
ATOM   1127 C  CA  A LEU A 1 82  ? 35.74900 44.21600 6.66600   0.790 31.77000  ?  82  LEU A CA  1 
ATOM   1128 C  CA  B LEU A 1 82  ? 35.82800 44.38700 6.40100   0.210 32.50000  ?  82  LEU A CA  1 
ATOM   1129 C  C   A LEU A 1 82  ? 34.98200 44.85200 5.51400   0.790 36.88000  ?  82  LEU A C   1 
ATOM   1130 C  C   B LEU A 1 82  ? 34.95200 44.97300 5.29900   0.210 37.08000  ?  82  LEU A C   1 
ATOM   1131 O  O   A LEU A 1 82  ? 35.15500 46.04300 5.22800   0.790 40.23000  ?  82  LEU A O   1 
ATOM   1132 O  O   B LEU A 1 82  ? 34.95500 46.18700 5.03300   0.210 39.96000  ?  82  LEU A O   1 
ATOM   1133 C  CB  A LEU A 1 82  ? 37.03800 43.57300 6.16100   0.790 30.96000  ?  82  LEU A CB  1 
ATOM   1134 C  CB  B LEU A 1 82  ? 36.96300 43.55100 5.79200   0.210 31.10000  ?  82  LEU A CB  1 
ATOM   1135 C  CG  A LEU A 1 82  ? 38.07600 43.18700 7.21900   0.790 26.22000  ?  82  LEU A CG  1 
ATOM   1136 C  CG  B LEU A 1 82  ? 38.04700 43.02000 6.71500   0.210 29.25000  ?  82  LEU A CG  1 
ATOM   1137 C  CD1 A LEU A 1 82  ? 39.19300 42.38500 6.57000   0.790 38.07000  ?  82  LEU A CD1 1 
ATOM   1138 C  CD1 B LEU A 1 82  ? 38.92000 42.00800 6.00800   0.210 36.13000  ?  82  LEU A CD1 1 
ATOM   1139 C  CD2 A LEU A 1 82  ? 38.61100 44.42300 7.91000   0.790 29.79000  ?  82  LEU A CD2 1 
ATOM   1140 C  CD2 B LEU A 1 82  ? 38.84500 44.24300 6.98700   0.210 27.55000  ?  82  LEU A CD2 1 
ATOM   1141 N  N   A ILE A 1 83  ? 34.13800 44.07400 4.83700   0.790 37.11000  ?  83  ILE A N   1 
ATOM   1142 N  N   B ILE A 1 83  ? 34.22100 44.09900 4.61100   0.210 36.81000  ?  83  ILE A N   1 
ATOM   1143 C  CA  A ILE A 1 83  ? 33.28700 44.63900 3.79700   0.790 40.05000  ?  83  ILE A CA  1 
ATOM   1144 C  CA  B ILE A 1 83  ? 33.33000 44.57200 3.55000   0.210 40.28000  ?  83  ILE A CA  1 
ATOM   1145 C  C   A ILE A 1 83  ? 32.27200 45.59500 4.41000   0.790 38.76000  ?  83  ILE A C   1 
ATOM   1146 C  C   B ILE A 1 83  ? 32.29800 45.52200 4.13200   0.210 39.53000  ?  83  ILE A C   1 
ATOM   1147 O  O   A ILE A 1 83  ? 32.01700 46.68100 3.87500   0.790 37.03000  ?  83  ILE A O   1 
ATOM   1148 O  O   B ILE A 1 83  ? 32.08000 46.62300 3.62000   0.210 36.77000  ?  83  ILE A O   1 
ATOM   1149 C  CB  A ILE A 1 83  ? 32.59100 43.51600 3.00800   0.790 38.07000  ?  83  ILE A CB  1 
ATOM   1150 C  CB  B ILE A 1 83  ? 32.65900 43.38700 2.82700   0.210 38.39000  ?  83  ILE A CB  1 
ATOM   1151 C  CG1 A ILE A 1 83  ? 33.61300 42.68600 2.23200   0.790 34.90000  ?  83  ILE A CG1 1 
ATOM   1152 C  CG1 B ILE A 1 83  ? 33.68000 42.45100 2.22300   0.210 34.88000  ?  83  ILE A CG1 1 
ATOM   1153 C  CG2 A ILE A 1 83  ? 31.55600 44.10400 2.06200   0.790 24.29000  ?  83  ILE A CG2 1 
ATOM   1154 C  CG2 B ILE A 1 83  ? 31.72100 43.86900 1.81100   0.210 25.50000  ?  83  ILE A CG2 1 
ATOM   1155 C  CD1 A ILE A 1 83  ? 33.03300 41.43900 1.58600   0.790 28.26000  ?  83  ILE A CD1 1 
ATOM   1156 C  CD1 B ILE A 1 83  ? 33.06600 41.12100 1.81400   0.210 29.86000  ?  83  ILE A CD1 1 
ATOM   1157 N  N   A VAL A 1 84  ? 31.66900 45.20200 5.53500   0.790 34.26000  ?  84  VAL A N   1 
ATOM   1158 N  N   B VAL A 1 84  ? 31.64300 45.10300 5.22000   0.210 35.42000  ?  84  VAL A N   1 
ATOM   1159 C  CA  A VAL A 1 84  ? 30.72500 46.07900 6.22100   0.790 40.62000  ?  84  VAL A CA  1 
ATOM   1160 C  CA  B VAL A 1 84  ? 30.75300 46.02100 5.94600   0.210 39.59000  ?  84  VAL A CA  1 
ATOM   1161 C  C   A VAL A 1 84  ? 31.44100 47.31400 6.74900   0.790 38.27000  ?  84  VAL A C   1 
ATOM   1162 C  C   B VAL A 1 84  ? 31.49900 47.29700 6.36400   0.210 37.96000  ?  84  VAL A C   1 
ATOM   1163 O  O   A VAL A 1 84  ? 30.89700 48.42500 6.72300   0.790 36.57000  ?  84  VAL A O   1 
ATOM   1164 O  O   B VAL A 1 84  ? 31.01500 48.41800 6.18400   0.210 35.61000  ?  84  VAL A O   1 
ATOM   1165 C  CB  A VAL A 1 84  ? 30.01000 45.30700 7.34600   0.790 40.16000  ?  84  VAL A CB  1 
ATOM   1166 C  CB  B VAL A 1 84  ? 30.13000 45.32600 7.18200   0.210 39.96000  ?  84  VAL A CB  1 
ATOM   1167 C  CG1 A VAL A 1 84  ? 29.25100 46.25400 8.25600   0.790 38.02000  ?  84  VAL A CG1 1 
ATOM   1168 C  CG1 B VAL A 1 84  ? 29.55300 46.38000 8.14500   0.210 37.18000  ?  84  VAL A CG1 1 
ATOM   1169 C  CG2 A VAL A 1 84  ? 29.08200 44.25300 6.75100   0.790 26.73000  ?  84  VAL A CG2 1 
ATOM   1170 C  CG2 B VAL A 1 84  ? 29.08100 44.31600 6.80100   0.210 31.98000  ?  84  VAL A CG2 1 
ATOM   1171 N  N   A TYR A 1 85  ? 32.67400 47.14600 7.22500   0.790 37.59000  ?  85  TYR A N   1 
ATOM   1172 N  N   B TYR A 1 85  ? 32.65300 47.14500 6.99300   0.210 37.54000  ?  85  TYR A N   1 
ATOM   1173 C  CA  A TYR A 1 85  ? 33.46200 48.29500 7.65800   0.790 44.80000  ?  85  TYR A CA  1 
ATOM   1174 C  CA  B TYR A 1 85  ? 33.40600 48.33200 7.37800   0.210 43.87000  ?  85  TYR A CA  1 
ATOM   1175 C  C   A TYR A 1 85  ? 33.69000 49.26400 6.50400   0.790 38.96000  ?  85  TYR A C   1 
ATOM   1176 C  C   B TYR A 1 85  ? 33.46200 49.33500 6.22800   0.210 40.36000  ?  85  TYR A C   1 
ATOM   1177 O  O   A TYR A 1 85  ? 33.49100 50.47600 6.64600   0.790 36.97000  ?  85  TYR A O   1 
ATOM   1178 O  O   B TYR A 1 85  ? 32.97500 50.46900 6.32200   0.210 37.97000  ?  85  TYR A O   1 
ATOM   1179 C  CB  A TYR A 1 85  ? 34.79100 47.81400 8.24000   0.790 35.86000  ?  85  TYR A CB  1 
ATOM   1180 C  CB  B TYR A 1 85  ? 34.80900 47.90200 7.83900   0.210 38.53000  ?  85  TYR A CB  1 
ATOM   1181 C  CG  A TYR A 1 85  ? 35.72500 48.92400 8.64700   0.790 49.40000  ?  85  TYR A CG  1 
ATOM   1182 C  CG  B TYR A 1 85  ? 35.76100 49.01700 8.09600   0.210 47.84000  ?  85  TYR A CG  1 
ATOM   1183 C  CD1 A TYR A 1 85  ? 35.36500 49.83700 9.62700   0.790 58.36000  ?  85  TYR A CD1 1 
ATOM   1184 C  CD1 B TYR A 1 85  ? 35.40500 50.11000 8.89600   0.210 53.44000  ?  85  TYR A CD1 1 
ATOM   1185 C  CD2 A TYR A 1 85  ? 36.97100 49.05800 8.05000   0.790 52.90000  ?  85  TYR A CD2 1 
ATOM   1186 C  CD2 B TYR A 1 85  ? 37.03500 48.98100 7.57100   0.210 50.04000  ?  85  TYR A CD2 1 
ATOM   1187 C  CE1 A TYR A 1 85  ? 36.22000 50.85400 10.00100  0.790 49.51000  ?  85  TYR A CE1 1 
ATOM   1188 C  CE1 B TYR A 1 85  ? 36.29600 51.16800 9.15200   0.210 44.21000  ?  85  TYR A CE1 1 
ATOM   1189 C  CE2 A TYR A 1 85  ? 37.83000 50.06800 8.41500   0.790 68.63000  ?  85  TYR A CE2 1 
ATOM   1190 C  CE2 B TYR A 1 85  ? 37.93900 50.02500 7.82400   0.210 60.50000  ?  85  TYR A CE2 1 
ATOM   1191 C  CZ  A TYR A 1 85  ? 37.45300 50.96500 9.39100   0.790 48.52000  ?  85  TYR A CZ  1 
ATOM   1192 C  CZ  B TYR A 1 85  ? 37.56100 51.12100 8.62800   0.210 55.13000  ?  85  TYR A CZ  1 
ATOM   1193 O  OH  A TYR A 1 85  ? 38.31300 51.97600 9.75700   0.790 59.53000  ?  85  TYR A OH  1 
ATOM   1194 O  OH  B TYR A 1 85  ? 38.47500 52.14000 8.84900   0.210 54.56000  ?  85  TYR A OH  1 
ATOM   1195 N  N   A PHE A 1 86  ? 34.09900 48.74500 5.34400   0.790 42.41000  ?  86  PHE A N   1 
ATOM   1196 N  N   B PHE A 1 86  ? 33.96500 48.86800 5.09600   0.210 41.48000  ?  86  PHE A N   1 
ATOM   1197 C  CA  A PHE A 1 86  ? 34.29000 49.59200 4.17000   0.790 43.49000  ?  86  PHE A CA  1 
ATOM   1198 C  CA  B PHE A 1 86  ? 34.02000 49.66200 3.88000   0.210 43.21000  ?  86  PHE A CA  1 
ATOM   1199 C  C   A PHE A 1 86  ? 33.02800 50.38900 3.86200   0.790 46.47000  ?  86  PHE A C   1 
ATOM   1200 C  C   B PHE A 1 86  ? 32.72700 50.43100 3.61200   0.210 44.10000  ?  86  PHE A C   1 
ATOM   1201 O  O   A PHE A 1 86  ? 33.07900 51.60700 3.65500   0.790 45.00000  ?  86  PHE A O   1 
ATOM   1202 O  O   B PHE A 1 86  ? 32.75800 51.61700 3.30300   0.210 44.09000  ?  86  PHE A O   1 
ATOM   1203 C  CB  A PHE A 1 86  ? 34.69700 48.72200 2.97600   0.790 45.07000  ?  86  PHE A CB  1 
ATOM   1204 C  CB  B PHE A 1 86  ? 34.33300 48.71500 2.73600   0.210 43.03000  ?  86  PHE A CB  1 
ATOM   1205 C  CG  A PHE A 1 86  ? 35.12400 49.50100 1.76300   0.790 37.14000  ?  86  PHE A CG  1 
ATOM   1206 C  CG  B PHE A 1 86  ? 34.78000 49.38500 1.51800   0.210 38.50000  ?  86  PHE A CG  1 
ATOM   1207 C  CD1 A PHE A 1 86  ? 34.18600 50.12800 0.96100   0.790 38.99000  ?  86  PHE A CD1 1 
ATOM   1208 C  CD1 B PHE A 1 86  ? 33.88700 49.93500 0.61600   0.210 38.37000  ?  86  PHE A CD1 1 
ATOM   1209 C  CD2 A PHE A 1 86  ? 36.46300 49.58800 1.41200   0.790 44.33000  ?  86  PHE A CD2 1 
ATOM   1210 C  CD2 B PHE A 1 86  ? 36.14400 49.54100 1.31600   0.210 43.63000  ?  86  PHE A CD2 1 
ATOM   1211 C  CE1 A PHE A 1 86  ? 34.57400 50.84000 -0.15600  0.790 47.11000  ?  86  PHE A CE1 1 
ATOM   1212 C  CE1 B PHE A 1 86  ? 34.37200 50.56800 -0.52600  0.210 47.04000  ?  86  PHE A CE1 1 
ATOM   1213 C  CE2 A PHE A 1 86  ? 36.85400 50.29600 0.29500   0.790 45.63000  ?  86  PHE A CE2 1 
ATOM   1214 C  CE2 B PHE A 1 86  ? 36.63400 50.15700 0.18700   0.210 47.16000  ?  86  PHE A CE2 1 
ATOM   1215 C  CZ  A PHE A 1 86  ? 35.90900 50.92100 -0.49000  0.790 43.85000  ?  86  PHE A CZ  1 
ATOM   1216 C  CZ  B PHE A 1 86  ? 35.74700 50.68100 -0.73900  0.210 43.53000  ?  86  PHE A CZ  1 
ATOM   1217 N  N   A LEU A 1 87  ? 31.87700 49.71100 3.83500   0.790 39.74000  ?  87  LEU A N   1 
ATOM   1218 N  N   B LEU A 1 87  ? 31.57700 49.77700 3.70700   0.210 38.82000  ?  87  LEU A N   1 
ATOM   1219 C  CA  A LEU A 1 87  ? 30.62100 50.40700 3.58100   0.790 38.97000  ?  87  LEU A CA  1 
ATOM   1220 C  CA  B LEU A 1 87  ? 30.33700 50.51900 3.49200   0.210 39.93000  ?  87  LEU A CA  1 
ATOM   1221 C  C   A LEU A 1 87  ? 30.31400 51.42700 4.66900   0.790 44.44000  ?  87  LEU A C   1 
ATOM   1222 C  C   B LEU A 1 87  ? 30.07600 51.52800 4.58900   0.210 44.80000  ?  87  LEU A C   1 
ATOM   1223 O  O   A LEU A 1 87  ? 29.75100 52.49000 4.38500   0.790 45.92000  ?  87  LEU A O   1 
ATOM   1224 O  O   B LEU A 1 87  ? 29.58200 52.62400 4.31500   0.210 45.84000  ?  87  LEU A O   1 
ATOM   1225 C  CB  A LEU A 1 87  ? 29.47500 49.40300 3.48100   0.790 39.33000  ?  87  LEU A CB  1 
ATOM   1226 C  CB  B LEU A 1 87  ? 29.12300 49.59700 3.38900   0.210 37.93000  ?  87  LEU A CB  1 
ATOM   1227 C  CG  A LEU A 1 87  ? 29.61000 48.33300 2.40200   0.790 48.39000  ?  87  LEU A CG  1 
ATOM   1228 C  CG  B LEU A 1 87  ? 29.09400 48.52500 2.28700   0.210 45.37000  ?  87  LEU A CG  1 
ATOM   1229 C  CD1 A LEU A 1 87  ? 28.65400 47.18200 2.66200   0.790 47.35000  ?  87  LEU A CD1 1 
ATOM   1230 C  CD1 B LEU A 1 87  ? 27.75900 47.69600 2.28500   0.210 28.89000  ?  87  LEU A CD1 1 
ATOM   1231 C  CD2 A LEU A 1 87  ? 29.35100 48.94600 1.03300   0.790 36.32000  ?  87  LEU A CD2 1 
ATOM   1232 C  CD2 B LEU A 1 87  ? 29.43900 49.16000 0.93600   0.210 36.88000  ?  87  LEU A CD2 1 
ATOM   1233 N  N   A GLY A 1 88  ? 30.65900 51.11800 5.91900   0.790 48.91000  ?  88  GLY A N   1 
ATOM   1234 N  N   B GLY A 1 88  ? 30.30800 51.15100 5.84700   0.210 49.08000  ?  88  GLY A N   1 
ATOM   1235 C  CA  A GLY A 1 88  ? 30.39000 52.04300 7.00300   0.790 52.14000  ?  88  GLY A CA  1 
ATOM   1236 C  CA  B GLY A 1 88  ? 30.09300 52.11300 6.91800   0.210 51.51000  ?  88  GLY A CA  1 
ATOM   1237 C  C   A GLY A 1 88  ? 31.21800 53.30400 6.93000   0.790 50.48000  ?  88  GLY A C   1 
ATOM   1238 C  C   B GLY A 1 88  ? 30.87200 53.39400 6.68500   0.210 50.93000  ?  88  GLY A C   1 
ATOM   1239 O  O   A GLY A 1 88  ? 30.74800 54.37700 7.31900   0.790 52.99000  ?  88  GLY A O   1 
ATOM   1240 O  O   B GLY A 1 88  ? 30.32300 54.48900 6.80800   0.210 53.30000  ?  88  GLY A O   1 
ATOM   1241 N  N   A LEU A 1 89  ? 32.45300 53.19900 6.43900   0.790 42.36000  ?  89  LEU A N   1 
ATOM   1242 N  N   B LEU A 1 89  ? 32.16200 53.26400 6.31600   0.210 46.35000  ?  89  LEU A N   1 
ATOM   1243 C  CA  A LEU A 1 89  ? 33.26100 54.39200 6.22700   0.790 48.37000  ?  89  LEU A CA  1 
ATOM   1244 C  CA  B LEU A 1 89  ? 33.02800 54.38500 5.95900   0.210 49.41000  ?  89  LEU A CA  1 
ATOM   1245 C  C   A LEU A 1 89  ? 32.64300 55.27900 5.15400   0.790 57.22000  ?  89  LEU A C   1 
ATOM   1246 C  C   B LEU A 1 89  ? 32.57500 55.12500 4.71600   0.210 57.12000  ?  89  LEU A C   1 
ATOM   1247 O  O   A LEU A 1 89  ? 32.54300 56.49900 5.32400   0.790 64.87000  ?  89  LEU A O   1 
ATOM   1248 O  O   B LEU A 1 89  ? 33.06900 56.23000 4.46700   0.210 64.25000  ?  89  LEU A O   1 
ATOM   1249 C  CB  A LEU A 1 89  ? 34.68500 53.99900 5.84000   0.790 47.37000  ?  89  LEU A CB  1 
ATOM   1250 C  CB  B LEU A 1 89  ? 34.44000 53.90600 5.69300   0.210 47.94000  ?  89  LEU A CB  1 
ATOM   1251 C  CG  A LEU A 1 89  ? 35.56200 53.36000 6.91700   0.790 53.64000  ?  89  LEU A CG  1 
ATOM   1252 C  CG  B LEU A 1 89  ? 35.39500 53.38200 6.75700   0.210 53.04000  ?  89  LEU A CG  1 
ATOM   1253 C  CD1 A LEU A 1 89  ? 36.88100 52.90100 6.29400   0.790 52.63000  ?  89  LEU A CD1 1 
ATOM   1254 C  CD1 B LEU A 1 89  ? 36.63000 52.75700 6.05400   0.210 53.74000  ?  89  LEU A CD1 1 
ATOM   1255 C  CD2 A LEU A 1 89  ? 35.81200 54.31400 8.06600   0.790 55.03000  ?  89  LEU A CD2 1 
ATOM   1256 C  CD2 B LEU A 1 89  ? 35.83500 54.49300 7.65900   0.210 54.46000  ?  89  LEU A CD2 1 
ATOM   1257 N  N   A LEU A 1 90  ? 32.23200 54.68000 4.03300   0.790 54.89000  ?  90  LEU A N   1 
ATOM   1258 N  N   B LEU A 1 90  ? 31.70300 54.53900 3.89800   0.210 52.08000  ?  90  LEU A N   1 
ATOM   1259 C  CA  A LEU A 1 90  ? 31.59300 55.45500 2.97600   0.790 56.35000  ?  90  LEU A CA  1 
ATOM   1260 C  CA  B LEU A 1 90  ? 31.12200 55.32800 2.81900   0.210 55.67000  ?  90  LEU A CA  1 
ATOM   1261 C  C   A LEU A 1 90  ? 30.37600 56.20000 3.50500   0.790 55.50000  ?  90  LEU A C   1 
ATOM   1262 C  C   B LEU A 1 90  ? 29.78800 55.93000 3.21100   0.210 56.02000  ?  90  LEU A C   1 
ATOM   1263 O  O   A LEU A 1 90  ? 30.16800 57.37600 3.18400   0.790 68.54000  ?  90  LEU A O   1 
ATOM   1264 O  O   B LEU A 1 90  ? 29.38100 56.95200 2.64200   0.210 59.04000  ?  90  LEU A O   1 
ATOM   1265 C  CB  A LEU A 1 90  ? 31.18100 54.54000 1.82700   0.790 53.90000  ?  90  LEU A CB  1 
ATOM   1266 C  CB  B LEU A 1 90  ? 30.91800 54.49300 1.55700   0.210 53.15000  ?  90  LEU A CB  1 
ATOM   1267 C  CG  A LEU A 1 90  ? 32.19100 54.20100 0.73300   0.790 55.45000  ?  90  LEU A CG  1 
ATOM   1268 C  CG  B LEU A 1 90  ? 32.04200 54.32200 0.52700   0.210 55.46000  ?  90  LEU A CG  1 
ATOM   1269 C  CD1 A LEU A 1 90  ? 31.49800 53.32300 -0.31300  0.790 49.99000  ?  90  LEU A CD1 1 
ATOM   1270 C  CD1 B LEU A 1 90  ? 31.44400 53.55300 -0.61600  0.210 49.88000  ?  90  LEU A CD1 1 
ATOM   1271 C  CD2 A LEU A 1 90  ? 32.77400 55.43600 0.09800   0.790 59.59000  ?  90  LEU A CD2 1 
ATOM   1272 C  CD2 B LEU A 1 90  ? 32.63900 55.62000 0.05000   0.210 59.94000  ?  90  LEU A CD2 1 
ATOM   1273 N  N   A ALA A 1 91  ? 29.55400 55.52800 4.31000   0.790 50.30000  ?  91  ALA A N   1 
ATOM   1274 N  N   B ALA A 1 91  ? 29.09000 55.31800 4.15000   0.210 51.65000  ?  91  ALA A N   1 
ATOM   1275 C  CA  A ALA A 1 91  ? 28.33500 56.12700 4.83200   0.790 53.67000  ?  91  ALA A CA  1 
ATOM   1276 C  CA  B ALA A 1 91  ? 27.89200 55.97300 4.63000   0.210 51.96000  ?  91  ALA A CA  1 
ATOM   1277 C  C   A ALA A 1 91  ? 28.59100 57.09000 5.98200   0.790 53.97000  ?  91  ALA A C   1 
ATOM   1278 C  C   B ALA A 1 91  ? 28.24300 57.00700 5.68800   0.210 55.34000  ?  91  ALA A C   1 
ATOM   1279 O  O   A ALA A 1 91  ? 27.69100 57.86200 6.33100   0.790 53.25000  ?  91  ALA A O   1 
ATOM   1280 O  O   B ALA A 1 91  ? 27.80600 58.15400 5.60200   0.210 54.28000  ?  91  ALA A O   1 
ATOM   1281 C  CB  A ALA A 1 91  ? 27.37200 55.02800 5.28900   0.790 51.67000  ?  91  ALA A CB  1 
ATOM   1282 C  CB  B ALA A 1 91  ? 26.90800 54.94200 5.17900   0.210 51.85000  ?  91  ALA A CB  1 
ATOM   1283 N  N   A GLY A 1 92  ? 29.78200 57.06600 6.57400   0.790 56.06000  ?  92  GLY A N   1 
ATOM   1284 N  N   B GLY A 1 92  ? 29.07100 56.63200 6.65800   0.210 55.05000  ?  92  GLY A N   1 
ATOM   1285 C  CA  A GLY A 1 92  ? 30.10000 57.96300 7.66600   0.790 63.30000  ?  92  GLY A CA  1 
ATOM   1286 C  CA  B GLY A 1 92  ? 29.46900 57.54800 7.70400   0.210 60.14000  ?  92  GLY A CA  1 
ATOM   1287 C  C   A GLY A 1 92  ? 29.41300 57.60300 8.96500   0.790 66.42000  ?  92  GLY A C   1 
ATOM   1288 C  C   B GLY A 1 92  ? 28.75300 57.26400 9.00300   0.210 65.48000  ?  92  GLY A C   1 
ATOM   1289 O  O   A GLY A 1 92  ? 28.80900 58.46200 9.61600   0.790 66.96000  ?  92  GLY A O   1 
ATOM   1290 O  O   B GLY A 1 92  ? 28.18800 58.16700 9.63000   0.210 66.37000  ?  92  GLY A O   1 
ATOM   1291 N  N   A LEU A 1 93  ? 29.50100 56.33800 9.36000   0.790 60.29000  ?  93  LEU A N   1 
ATOM   1292 N  N   B LEU A 1 93  ? 28.75400 56.00400 9.41400   0.210 60.58000  ?  93  LEU A N   1 
ATOM   1293 C  CA  A LEU A 1 93  ? 28.88000 55.89300 10.59700  0.790 65.02000  ?  93  LEU A CA  1 
ATOM   1294 C  CA  B LEU A 1 93  ? 28.15800 55.64400 10.68500  0.210 65.19000  ?  93  LEU A CA  1 
ATOM   1295 C  C   A LEU A 1 93  ? 29.70400 56.32600 11.80200  0.790 69.75000  ?  93  LEU A C   1 
ATOM   1296 C  C   B LEU A 1 93  ? 29.07200 56.09600 11.81000  0.210 68.52000  ?  93  LEU A C   1 
ATOM   1297 O  O   A LEU A 1 93  ? 30.93800 56.33900 11.75900  0.790 68.41000  ?  93  LEU A O   1 
ATOM   1298 O  O   B LEU A 1 93  ? 30.29800 56.03400 11.68800  0.210 69.63000  ?  93  LEU A O   1 
ATOM   1299 C  CB  A LEU A 1 93  ? 28.73600 54.37400 10.60400  0.790 64.21000  ?  93  LEU A CB  1 
ATOM   1300 C  CB  B LEU A 1 93  ? 27.93600 54.13600 10.75100  0.210 62.85000  ?  93  LEU A CB  1 
ATOM   1301 C  CG  A LEU A 1 93  ? 27.61900 53.76200 9.76300   0.790 58.21000  ?  93  LEU A CG  1 
ATOM   1302 C  CG  B LEU A 1 93  ? 26.77500 53.63300 9.89200   0.210 56.82000  ?  93  LEU A CG  1 
ATOM   1303 C  CD1 A LEU A 1 93  ? 27.63300 52.24800 9.94800   0.790 49.18000  ?  93  LEU A CD1 1 
ATOM   1304 C  CD1 B LEU A 1 93  ? 26.67300 52.14300 10.08300  0.210 54.68000  ?  93  LEU A CD1 1 
ATOM   1305 C  CD2 A LEU A 1 93  ? 26.27200 54.34400 10.12900  0.790 54.56000  ?  93  LEU A CD2 1 
ATOM   1306 C  CD2 B LEU A 1 93  ? 25.46000 54.31400 10.24200  0.210 54.63000  ?  93  LEU A CD2 1 
ATOM   1307 N  N   A ASP A 1 94  ? 29.01400 56.67900 12.88200  0.790 75.64000  ?  94  ASP A N   1 
ATOM   1308 N  N   B ASP A 1 94  ? 28.46900 56.61800 12.87500  0.210 70.92000  ?  94  ASP A N   1 
ATOM   1309 C  CA  A ASP A 1 94  ? 29.68600 56.87000 14.15600  0.790 80.83000  ?  94  ASP A CA  1 
ATOM   1310 C  CA  B ASP A 1 94  ? 29.13600 56.75400 14.17300  0.210 79.53000  ?  94  ASP A CA  1 
ATOM   1311 C  C   A ASP A 1 94  ? 30.08900 55.51400 14.73100  0.790 71.03000  ?  94  ASP A C   1 
ATOM   1312 C  C   B ASP A 1 94  ? 29.85500 55.47300 14.52900  0.210 72.11000  ?  94  ASP A C   1 
ATOM   1313 O  O   A ASP A 1 94  ? 29.50500 54.47200 14.41100  0.790 73.14000  ?  94  ASP A O   1 
ATOM   1314 O  O   B ASP A 1 94  ? 29.39600 54.39100 14.17900  0.210 72.34000  ?  94  ASP A O   1 
ATOM   1315 C  CB  A ASP A 1 94  ? 28.78600 57.62500 15.13300  0.790 74.12000  ?  94  ASP A CB  1 
ATOM   1316 C  CB  B ASP A 1 94  ? 28.06200 57.02600 15.19400  0.210 82.16000  ?  94  ASP A CB  1 
ATOM   1317 C  CG  A ASP A 1 94  ? 27.55500 56.83800 15.51900  0.790 86.15000  ?  94  ASP A CG  1 
ATOM   1318 C  CG  B ASP A 1 94  ? 26.88600 56.11900 14.94600  0.210 87.49000  ?  94  ASP A CG  1 
ATOM   1319 O  OD1 A ASP A 1 94  ? 26.80700 56.41200 14.61500  0.790 94.67000  ?  94  ASP A OD1 1 
ATOM   1320 O  OD1 B ASP A 1 94  ? 26.48300 56.09100 13.74500  0.210 79.36000  ?  94  ASP A OD1 1 
ATOM   1321 O  OD2 A ASP A 1 94  ? 27.33600 56.64700 16.73200  0.790 100.14000 -1 94  ASP A OD2 1 
ATOM   1322 O  OD2 B ASP A 1 94  ? 26.40800 55.44100 15.86800  0.210 83.33000  -1 94  ASP A OD2 1 
ATOM   1323 N  N   A SER A 1 95  ? 31.10500 55.53800 15.59700  0.790 82.77000  ?  95  SER A N   1 
ATOM   1324 N  N   B SER A 1 95  ? 30.95500 55.56800 15.28100  0.210 81.21000  ?  95  SER A N   1 
ATOM   1325 C  CA  A SER A 1 95  ? 31.67300 54.30100 16.12200  0.790 74.77000  ?  95  SER A CA  1 
ATOM   1326 C  CA  B SER A 1 95  ? 31.57000 54.29900 15.65600  0.210 77.03000  ?  95  SER A CA  1 
ATOM   1327 C  C   A SER A 1 95  ? 30.64000 53.40700 16.79500  0.790 68.51000  ?  95  SER A C   1 
ATOM   1328 C  C   B SER A 1 95  ? 30.63400 53.46600 16.51200  0.210 69.65000  ?  95  SER A C   1 
ATOM   1329 O  O   A SER A 1 95  ? 30.90700 52.21800 17.00100  0.790 69.31000  ?  95  SER A O   1 
ATOM   1330 O  O   B SER A 1 95  ? 30.93700 52.29500 16.76700  0.210 69.31000  ?  95  SER A O   1 
ATOM   1331 C  CB  A SER A 1 95  ? 32.77800 54.62100 17.12800  0.790 82.99000  ?  95  SER A CB  1 
ATOM   1332 C  CB  B SER A 1 95  ? 32.90400 54.46600 16.37900  0.210 81.61000  ?  95  SER A CB  1 
ATOM   1333 O  OG  A SER A 1 95  ? 32.29100 54.54100 18.46100  0.790 104.87000 ?  95  SER A OG  1 
ATOM   1334 O  OG  B SER A 1 95  ? 32.80300 54.12900 17.74800  0.210 89.49000  ?  95  SER A OG  1 
ATOM   1335 N  N   A ARG A 1 96  ? 29.46400 53.93800 17.12700  0.790 71.31000  ?  96  ARG A N   1 
ATOM   1336 N  N   B ARG A 1 96  ? 29.47300 54.01400 16.88900  0.210 71.89000  ?  96  ARG A N   1 
ATOM   1337 C  CA  A ARG A 1 96  ? 28.44300 53.13400 17.78900  0.790 77.27000  ?  96  ARG A CA  1 
ATOM   1338 C  CA  B ARG A 1 96  ? 28.45200 53.21900 17.56900  0.210 76.88000  ?  96  ARG A CA  1 
ATOM   1339 C  C   A ARG A 1 96  ? 27.61400 52.35200 16.77900  0.790 67.23000  ?  96  ARG A C   1 
ATOM   1340 C  C   B ARG A 1 96  ? 27.57300 52.43000 16.61800  0.210 67.52000  ?  96  ARG A C   1 
ATOM   1341 O  O   A ARG A 1 96  ? 27.29500 51.18000 17.00600  0.790 51.05000  ?  96  ARG A O   1 
ATOM   1342 O  O   B ARG A 1 96  ? 27.40200 51.21700 16.79500  0.210 53.25000  ?  96  ARG A O   1 
ATOM   1343 C  CB  A ARG A 1 96  ? 27.54800 54.03700 18.63700  0.790 88.82000  ?  96  ARG A CB  1 
ATOM   1344 C  CB  B ARG A 1 96  ? 27.55900 54.10400 18.41100  0.210 88.11000  ?  96  ARG A CB  1 
ATOM   1345 C  CG  A ARG A 1 96  ? 26.32900 53.35400 19.23100  0.790 86.99000  ?  96  ARG A CG  1 
ATOM   1346 C  CG  B ARG A 1 96  ? 26.30800 53.39400 18.94000  0.210 87.71000  ?  96  ARG A CG  1 
ATOM   1347 C  CD  A ARG A 1 96  ? 25.40300 54.38400 19.88100  0.790 110.01000 ?  96  ARG A CD  1 
ATOM   1348 C  CD  B ARG A 1 96  ? 25.45400 54.37700 19.73600  0.210 109.75000 ?  96  ARG A CD  1 
ATOM   1349 N  NE  A ARG A 1 96  ? 26.13200 55.33800 20.71700  0.790 121.29000 ?  96  ARG A NE  1 
ATOM   1350 N  NE  B ARG A 1 96  ? 26.24700 55.17800 20.67500  0.210 120.31000 ?  96  ARG A NE  1 
ATOM   1351 C  CZ  A ARG A 1 96  ? 26.49300 56.55900 20.33100  0.790 125.65000 ?  96  ARG A CZ  1 
ATOM   1352 C  CZ  B ARG A 1 96  ? 26.58800 56.45400 20.50600  0.210 125.21000 ?  96  ARG A CZ  1 
ATOM   1353 N  NH1 A ARG A 1 96  ? 26.19700 56.99700 19.11400  0.790 124.54000 ?  96  ARG A NH1 1 
ATOM   1354 N  NH1 B ARG A 1 96  ? 26.23300 57.13600 19.42300  0.210 125.02000 ?  96  ARG A NH1 1 
ATOM   1355 N  NH2 A ARG A 1 96  ? 27.15300 57.34700 21.16800  0.790 129.00000 ?  96  ARG A NH2 1 
ATOM   1356 N  NH2 B ARG A 1 96  ? 27.30400 57.06400 21.45000  0.210 128.92000 ?  96  ARG A NH2 1 
ATOM   1357 N  N   A GLU A 1 97  ? 27.24600 52.98900 15.66500  0.790 77.37000  ?  97  GLU A N   1 
ATOM   1358 N  N   B GLU A 1 97  ? 26.95800 53.12200 15.63700  0.210 75.44000  ?  97  GLU A N   1 
ATOM   1359 C  CA  A GLU A 1 97  ? 26.50900 52.28300 14.62200  0.790 69.78000  ?  97  GLU A CA  1 
ATOM   1360 C  CA  B GLU A 1 97  ? 26.06600 52.45100 14.68800  0.210 66.96000  ?  97  GLU A CA  1 
ATOM   1361 C  C   A GLU A 1 97  ? 27.33800 51.14300 14.04400  0.790 56.74000  ?  97  GLU A C   1 
ATOM   1362 C  C   B GLU A 1 97  ? 26.79800 51.33700 13.95600  0.210 56.80000  ?  97  GLU A C   1 
ATOM   1363 O  O   A GLU A 1 97  ? 26.80000 50.07900 13.71000  0.790 46.08000  ?  97  GLU A O   1 
ATOM   1364 O  O   B GLU A 1 97  ? 26.19800 50.32100 13.59300  0.210 49.18000  ?  97  GLU A O   1 
ATOM   1365 C  CB  A GLU A 1 97  ? 26.10100 53.25800 13.51800  0.790 56.30000  ?  97  GLU A CB  1 
ATOM   1366 C  CB  B GLU A 1 97  ? 25.47300 53.43700 13.69000  0.210 60.50000  ?  97  GLU A CB  1 
ATOM   1367 N  N   A PHE A 1 98  ? 28.65200 51.34800 13.91900  0.790 50.86000  ?  98  PHE A N   1 
ATOM   1368 N  N   B PHE A 1 98  ? 28.11400 51.49900 13.78600  0.210 54.58000  ?  98  PHE A N   1 
ATOM   1369 C  CA  A PHE A 1 98  ? 29.54300 50.27100 13.50100  0.790 44.69000  ?  98  PHE A CA  1 
ATOM   1370 C  CA  B PHE A 1 98  ? 28.98100 50.43100 13.30100  0.210 49.84000  ?  98  PHE A CA  1 
ATOM   1371 C  C   A PHE A 1 98  ? 29.32500 49.02600 14.35600  0.790 53.19000  ?  98  PHE A C   1 
ATOM   1372 C  C   B PHE A 1 98  ? 28.78400 49.13500 14.05500  0.210 48.68000  ?  98  PHE A C   1 
ATOM   1373 O  O   A PHE A 1 98  ? 29.25400 47.90300 13.84500  0.790 49.12000  ?  98  PHE A O   1 
ATOM   1374 O  O   B PHE A 1 98  ? 28.71700 48.06200 13.44400  0.210 42.31000  ?  98  PHE A O   1 
ATOM   1375 C  CB  A PHE A 1 98  ? 31.00000 50.73100 13.60800  0.790 58.47000  ?  98  PHE A CB  1 
ATOM   1376 C  CB  B PHE A 1 98  ? 30.42500 50.86400 13.41000  0.210 55.28000  ?  98  PHE A CB  1 
ATOM   1377 C  CG  A PHE A 1 98  ? 31.52200 51.42200 12.37900  0.790 66.20000  ?  98  PHE A CG  1 
ATOM   1378 C  CG  B PHE A 1 98  ? 30.90600 51.53800 12.20500  0.210 62.28000  ?  98  PHE A CG  1 
ATOM   1379 C  CD1 A PHE A 1 98  ? 31.68100 50.73200 11.19000  0.790 61.06000  ?  98  PHE A CD1 1 
ATOM   1380 C  CD1 B PHE A 1 98  ? 31.08600 50.81500 11.04600  0.210 56.57000  ?  98  PHE A CD1 1 
ATOM   1381 C  CD2 A PHE A 1 98  ? 31.86800 52.76300 12.42100  0.790 70.39000  ?  98  PHE A CD2 1 
ATOM   1382 C  CD2 B PHE A 1 98  ? 31.18700 52.89400 12.21300  0.210 67.66000  ?  98  PHE A CD2 1 
ATOM   1383 C  CE1 A PHE A 1 98  ? 32.16600 51.36900 10.06300  0.790 60.39000  ?  98  PHE A CE1 1 
ATOM   1384 C  CE1 B PHE A 1 98  ? 31.53600 51.41800 9.91300   0.210 59.77000  ?  98  PHE A CE1 1 
ATOM   1385 C  CE2 A PHE A 1 98  ? 32.35200 53.40600 11.30000  0.790 70.46000  ?  98  PHE A CE2 1 
ATOM   1386 C  CE2 B PHE A 1 98  ? 31.63400 53.51200 11.07800  0.210 64.95000  ?  98  PHE A CE2 1 
ATOM   1387 C  CZ  A PHE A 1 98  ? 32.50100 52.70700 10.11700  0.790 60.69000  ?  98  PHE A CZ  1 
ATOM   1388 C  CZ  B PHE A 1 98  ? 31.81400 52.77300 9.92500   0.210 60.99000  ?  98  PHE A CZ  1 
ATOM   1389 N  N   A GLY A 1 99  ? 29.22100 49.21300 15.67200  0.790 62.08000  ?  99  GLY A N   1 
ATOM   1390 N  N   B GLY A 1 99  ? 28.70900 49.21500 15.39400  0.210 59.68000  ?  99  GLY A N   1 
ATOM   1391 C  CA  A GLY A 1 99  ? 29.11000 48.06900 16.56400  0.790 41.68000  ?  99  GLY A CA  1 
ATOM   1392 C  CA  B GLY A 1 99  ? 28.85200 48.01900 16.22000  0.210 44.90000  ?  99  GLY A CA  1 
ATOM   1393 C  C   A GLY A 1 99  ? 27.88900 47.21700 16.28100  0.790 39.99000  ?  99  GLY A C   1 
ATOM   1394 C  C   B GLY A 1 99  ? 27.57100 47.20900 16.28700  0.210 41.71000  ?  99  GLY A C   1 
ATOM   1395 O  O   A GLY A 1 99  ? 27.96100 45.98500 16.29600  0.790 36.49000  ?  99  GLY A O   1 
ATOM   1396 O  O   B GLY A 1 99  ? 27.59100 45.99600 16.47500  0.210 40.76000  ?  99  GLY A O   1 
ATOM   1397 N  N   A ILE A 1 100 ? 26.75300 47.86100 16.01600  0.790 38.52000  ?  100 ILE A N   1 
ATOM   1398 N  N   B ILE A 1 100 ? 26.44300 47.87500 16.18900  0.210 41.32000  ?  100 ILE A N   1 
ATOM   1399 C  CA  A ILE A 1 100 ? 25.52600 47.11900 15.74900  0.790 42.01000  ?  100 ILE A CA  1 
ATOM   1400 C  CA  B ILE A 1 100 ? 25.24200 47.18100 15.76500  0.210 44.98000  ?  100 ILE A CA  1 
ATOM   1401 C  C   A ILE A 1 100 ? 25.68900 46.25100 14.50700  0.790 53.93000  ?  100 ILE A C   1 
ATOM   1402 C  C   B ILE A 1 100 ? 25.59200 46.32500 14.53300  0.210 53.00000  ?  100 ILE A C   1 
ATOM   1403 O  O   A ILE A 1 100 ? 25.45900 45.03700 14.54400  0.790 52.17000  ?  100 ILE A O   1 
ATOM   1404 O  O   B ILE A 1 100 ? 25.65600 45.08200 14.63600  0.210 49.65000  ?  100 ILE A O   1 
ATOM   1405 C  CB  A ILE A 1 100 ? 24.33400 48.08300 15.60700  0.790 56.85000  ?  100 ILE A CB  1 
ATOM   1406 C  CB  B ILE A 1 100 ? 24.12500 48.21400 15.50900  0.210 57.11000  ?  100 ILE A CB  1 
ATOM   1407 C  CG1 A ILE A 1 100 ? 24.03600 48.77100 16.94100  0.790 69.34000  ?  100 ILE A CG1 1 
ATOM   1408 C  CG1 B ILE A 1 100 ? 23.99900 49.08600 16.77500  0.210 67.67000  ?  100 ILE A CG1 1 
ATOM   1409 C  CG2 A ILE A 1 100 ? 23.10800 47.33500 15.10100  0.790 54.88000  ?  100 ILE A CG2 1 
ATOM   1410 C  CG2 B ILE A 1 100 ? 22.80600 47.55600 15.15200  0.210 54.92000  ?  100 ILE A CG2 1 
ATOM   1411 C  CD1 A ILE A 1 100 ? 23.79700 50.26600 16.82300  0.790 69.86000  ?  100 ILE A CD1 1 
ATOM   1412 C  CD1 B ILE A 1 100 ? 24.01500 50.60700 16.57000  0.210 65.38000  ?  100 ILE A CD1 1 
ATOM   1413 N  N   A VAL A 1 101 ? 26.08700 46.85600 13.38500  0.790 41.17000  ?  101 VAL A N   1 
ATOM   1414 N  N   B VAL A 1 101 ? 25.92000 46.96200 13.38500  0.210 41.98000  ?  101 VAL A N   1 
ATOM   1415 C  CA  A VAL A 1 101 ? 26.09800 46.10900 12.12900  0.790 39.84000  ?  101 VAL A CA  1 
ATOM   1416 C  CA  B VAL A 1 101 ? 25.91700 46.17100 12.14800  0.210 40.37000  ?  101 VAL A CA  1 
ATOM   1417 C  C   A VAL A 1 101 ? 27.17000 45.02700 12.15600  0.790 32.93000  ?  101 VAL A C   1 
ATOM   1418 C  C   B VAL A 1 101 ? 27.10500 45.21700 12.04600  0.210 33.61000  ?  101 VAL A C   1 
ATOM   1419 O  O   A VAL A 1 101 ? 26.95700 43.91500 11.65900  0.790 32.47000  ?  101 VAL A O   1 
ATOM   1420 O  O   B VAL A 1 101 ? 26.96400 44.16700 11.40400  0.210 33.34000  ?  101 VAL A O   1 
ATOM   1421 C  CB  A VAL A 1 101 ? 26.27700 47.05500 10.92500  0.790 43.80000  ?  101 VAL A CB  1 
ATOM   1422 C  CB  B VAL A 1 101 ? 25.80600 47.02700 10.86900  0.210 41.76000  ?  101 VAL A CB  1 
ATOM   1423 C  CG1 A VAL A 1 101 ? 25.12100 48.04700 10.86000  0.790 42.71000  ?  101 VAL A CG1 1 
ATOM   1424 C  CG1 B VAL A 1 101 ? 24.60500 47.96500 10.98800  0.210 42.54000  ?  101 VAL A CG1 1 
ATOM   1425 C  CG2 A VAL A 1 101 ? 27.61500 47.77100 10.96900  0.790 44.88000  ?  101 VAL A CG2 1 
ATOM   1426 C  CG2 B VAL A 1 101 ? 27.09200 47.80300 10.58800  0.210 39.44000  ?  101 VAL A CG2 1 
ATOM   1427 N  N   A ILE A 1 102 ? 28.33500 45.32300 12.73800  0.790 30.74000  ?  102 ILE A N   1 
ATOM   1428 N  N   B ILE A 1 102 ? 28.23900 45.45100 12.71600  0.210 30.48000  ?  102 ILE A N   1 
ATOM   1429 C  CA  A ILE A 1 102 ? 29.37700 44.30500 12.81000  0.790 35.85000  ?  102 ILE A CA  1 
ATOM   1430 C  CA  B ILE A 1 102 ? 29.22400 44.34900 12.62600  0.210 37.33000  ?  102 ILE A CA  1 
ATOM   1431 C  C   A ILE A 1 102 ? 28.95900 43.18400 13.75400  0.790 43.04000  ?  102 ILE A C   1 
ATOM   1432 C  C   B ILE A 1 102 ? 28.89300 43.13900 13.50300  0.210 41.65000  ?  102 ILE A C   1 
ATOM   1433 O  O   A ILE A 1 102 ? 29.30200 42.01700 13.52900  0.790 43.98000  ?  102 ILE A O   1 
ATOM   1434 O  O   B ILE A 1 102 ? 29.25600 42.00600 13.14700  0.210 41.19000  ?  102 ILE A O   1 
ATOM   1435 C  CB  A ILE A 1 102 ? 30.71900 44.94100 13.22000  0.790 40.95000  ?  102 ILE A CB  1 
ATOM   1436 C  CB  B ILE A 1 102 ? 30.65600 44.84000 12.84800  0.210 41.87000  ?  102 ILE A CB  1 
ATOM   1437 C  CG1 A ILE A 1 102 ? 31.36000 45.62900 12.01000  0.790 49.31000  ?  102 ILE A CG1 1 
ATOM   1438 C  CG1 B ILE A 1 102 ? 31.22800 45.18400 11.45300  0.210 37.75000  ?  102 ILE A CG1 1 
ATOM   1439 C  CG2 A ILE A 1 102 ? 31.66400 43.89300 13.78400  0.790 39.20000  ?  102 ILE A CG2 1 
ATOM   1440 C  CG2 B ILE A 1 102 ? 31.50200 43.78900 13.58600  0.210 39.51000  ?  102 ILE A CG2 1 
ATOM   1441 C  CD1 A ILE A 1 102 ? 32.12300 46.89000 12.32800  0.790 59.04000  ?  102 ILE A CD1 1 
ATOM   1442 C  CD1 B ILE A 1 102 ? 32.03700 46.46400 11.37500  0.210 40.79000  ?  102 ILE A CD1 1 
ATOM   1443 N  N   A THR A 1 103 ? 28.20500 43.50100 14.81100  0.790 40.97000  ?  103 THR A N   1 
ATOM   1444 N  N   B THR A 1 103 ? 28.11600 43.31700 14.57700  0.210 41.25000  ?  103 THR A N   1 
ATOM   1445 C  CA  A THR A 1 103 ? 27.68500 42.44800 15.67900  0.790 38.56000  ?  103 THR A CA  1 
ATOM   1446 C  CA  B THR A 1 103 ? 27.72600 42.18400 15.42500  0.210 36.54000  ?  103 THR A CA  1 
ATOM   1447 C  C   A THR A 1 103 ? 26.68300 41.57700 14.93000  0.790 38.52000  ?  103 THR A C   1 
ATOM   1448 C  C   B THR A 1 103 ? 26.67200 41.30100 14.74800  0.210 37.66000  ?  103 THR A C   1 
ATOM   1449 O  O   A THR A 1 103 ? 26.77000 40.34300 14.96100  0.790 33.64000  ?  103 THR A O   1 
ATOM   1450 O  O   B THR A 1 103 ? 26.79900 40.07400 14.75300  0.210 33.38000  ?  103 THR A O   1 
ATOM   1451 C  CB  A THR A 1 103 ? 27.03900 43.05600 16.92600  0.790 41.48000  ?  103 THR A CB  1 
ATOM   1452 C  CB  B THR A 1 103 ? 27.20200 42.70500 16.78400  0.210 42.13000  ?  103 THR A CB  1 
ATOM   1453 O  OG1 A THR A 1 103 ? 28.04400 43.66900 17.74300  0.790 31.60000  ?  103 THR A OG1 1 
ATOM   1454 O  OG1 B THR A 1 103 ? 28.22200 43.48800 17.44400  0.210 35.04000  ?  103 THR A OG1 1 
ATOM   1455 C  CG2 A THR A 1 103 ? 26.31800 41.98100 17.73600  0.790 35.76000  ?  103 THR A CG2 1 
ATOM   1456 C  CG2 B THR A 1 103 ? 26.72000 41.51100 17.69500  0.210 36.85000  ?  103 THR A CG2 1 
ATOM   1457 N  N   A LEU A 1 104 ? 25.72500 42.20600 14.24000  0.790 36.60000  ?  104 LEU A N   1 
ATOM   1458 N  N   B LEU A 1 104 ? 25.59600 41.91500 14.21000  0.210 35.64000  ?  104 LEU A N   1 
ATOM   1459 C  CA  A LEU A 1 104 ? 24.76400 41.45000 13.44000  0.790 28.86000  ?  104 LEU A CA  1 
ATOM   1460 C  CA  B LEU A 1 104 ? 24.66900 41.24600 13.28200  0.210 30.73000  ?  104 LEU A CA  1 
ATOM   1461 C  C   A LEU A 1 104 ? 25.46700 40.58400 12.40200  0.790 34.46000  ?  104 LEU A C   1 
ATOM   1462 C  C   B LEU A 1 104 ? 25.37200 40.46000 12.15800  0.210 33.32000  ?  104 LEU A C   1 
ATOM   1463 O  O   A LEU A 1 104 ? 25.09500 39.42300 12.19400  0.790 30.34000  ?  104 LEU A O   1 
ATOM   1464 O  O   B LEU A 1 104 ? 25.02800 39.29100 11.90400  0.210 30.55000  ?  104 LEU A O   1 
ATOM   1465 C  CB  A LEU A 1 104 ? 23.78900 42.40200 12.74500  0.790 32.11000  ?  104 LEU A CB  1 
ATOM   1466 C  CB  B LEU A 1 104 ? 23.69600 42.26900 12.65700  0.210 32.35000  ?  104 LEU A CB  1 
ATOM   1467 C  CG  A LEU A 1 104 ? 22.61900 42.97900 13.53800  0.790 31.14000  ?  104 LEU A CG  1 
ATOM   1468 C  CG  B LEU A 1 104 ? 22.40200 42.43100 13.42900  0.210 33.69000  ?  104 LEU A CG  1 
ATOM   1469 C  CD1 A LEU A 1 104 ? 21.79200 43.92400 12.66200  0.790 37.98000  ?  104 LEU A CD1 1 
ATOM   1470 C  CD1 B LEU A 1 104 ? 21.28500 43.11100 12.65100  0.210 28.71000  ?  104 LEU A CD1 1 
ATOM   1471 C  CD2 A LEU A 1 104 ? 21.73700 41.87700 14.09200  0.790 43.20000  ?  104 LEU A CD2 1 
ATOM   1472 C  CD2 B LEU A 1 104 ? 22.01800 41.01400 13.94200  0.210 33.85000  ?  104 LEU A CD2 1 
ATOM   1473 N  N   A ASN A 1 105 ? 26.48200 41.13300 11.73200  0.790 28.66000  ?  105 ASN A N   1 
ATOM   1474 N  N   B ASN A 1 105 ? 26.32100 41.09800 11.44300  0.210 31.16000  ?  105 ASN A N   1 
ATOM   1475 C  CA  A ASN A 1 105 ? 27.20800 40.35400 10.73500  0.790 34.38000  ?  105 ASN A CA  1 
ATOM   1476 C  CA  B ASN A 1 105 ? 27.14500 40.37100 10.46600  0.210 34.15000  ?  105 ASN A CA  1 
ATOM   1477 C  C   A ASN A 1 105 ? 27.84100 39.11700 11.36100  0.790 34.74000  ?  105 ASN A C   1 
ATOM   1478 C  C   B ASN A 1 105 ? 27.65600 39.08200 11.09600  0.210 34.39000  ?  105 ASN A C   1 
ATOM   1479 O  O   A ASN A 1 105 ? 27.75300 38.01300 10.81000  0.790 36.44000  ?  105 ASN A O   1 
ATOM   1480 O  O   B ASN A 1 105 ? 27.27200 37.97900 10.69500  0.210 33.10000  ?  105 ASN A O   1 
ATOM   1481 C  CB  A ASN A 1 105 ? 28.27700 41.21900 10.06500  0.790 38.89000  ?  105 ASN A CB  1 
ATOM   1482 C  CB  B ASN A 1 105 ? 28.34200 41.23100 10.01300  0.210 38.36000  ?  105 ASN A CB  1 
ATOM   1483 C  CG  A ASN A 1 105 ? 28.93000 40.52500 8.88900   0.790 40.63000  ?  105 ASN A CG  1 
ATOM   1484 C  CG  B ASN A 1 105 ? 29.35000 40.48200 9.03400   0.210 39.07000  ?  105 ASN A CG  1 
ATOM   1485 O  OD1 A ASN A 1 105 ? 28.44000 40.59800 7.76200   0.790 31.42000  ?  105 ASN A OD1 1 
ATOM   1486 O  OD1 B ASN A 1 105 ? 29.29100 40.62400 7.81700   0.210 32.11000  ?  105 ASN A OD1 1 
ATOM   1487 N  ND2 A ASN A 1 105 ? 30.04000 39.84000 9.14600   0.790 38.26000  ?  105 ASN A ND2 1 
ATOM   1488 N  ND2 B ASN A 1 105 ? 30.29800 39.75100 9.60400   0.210 39.56000  ?  105 ASN A ND2 1 
ATOM   1489 N  N   A THR A 1 106 ? 28.47700 39.27800 12.52400  0.790 33.87000  ?  106 THR A N   1 
ATOM   1490 N  N   B THR A 1 106 ? 28.44500 39.22800 12.17300  0.210 34.07000  ?  106 THR A N   1 
ATOM   1491 C  CA  A THR A 1 106 ? 29.16800 38.14900 13.14200  0.790 35.53000  ?  106 THR A CA  1 
ATOM   1492 C  CA  B THR A 1 106 ? 29.09700 38.09700 12.84500  0.210 36.03000  ?  106 THR A CA  1 
ATOM   1493 C  C   A THR A 1 106 ? 28.18800 37.04500 13.52700  0.790 35.01000  ?  106 THR A C   1 
ATOM   1494 C  C   B THR A 1 106 ? 28.08500 37.08000 13.37400  0.210 34.40000  ?  106 THR A C   1 
ATOM   1495 O  O   A THR A 1 106 ? 28.51800 35.85400 13.45700  0.790 35.74000  ?  106 THR A O   1 
ATOM   1496 O  O   B THR A 1 106 ? 28.34300 35.87600 13.32500  0.210 34.34000  ?  106 THR A O   1 
ATOM   1497 C  CB  A THR A 1 106 ? 29.95900 38.61700 14.36400  0.790 36.83000  ?  106 THR A CB  1 
ATOM   1498 C  CB  B THR A 1 106 ? 29.97000 38.62900 13.98100  0.210 37.34000  ?  106 THR A CB  1 
ATOM   1499 O  OG1 A THR A 1 106 ? 30.91900 39.60300 13.96400  0.790 35.96000  ?  106 THR A OG1 1 
ATOM   1500 O  OG1 B THR A 1 106 ? 30.46700 39.93400 13.60200  0.210 31.07000  ?  106 THR A OG1 1 
ATOM   1501 C  CG2 A THR A 1 106 ? 30.67800 37.44200 15.01700  0.790 38.94000  ?  106 THR A CG2 1 
ATOM   1502 C  CG2 B THR A 1 106 ? 31.16300 37.70200 14.18900  0.210 40.59000  ?  106 THR A CG2 1 
ATOM   1503 N  N   A VAL A 1 107 ? 26.97200 37.41800 13.93200  0.790 33.77000  ?  107 VAL A N   1 
ATOM   1504 N  N   B VAL A 1 107 ? 26.91600 37.52600 13.86600  0.210 32.97000  ?  107 VAL A N   1 
ATOM   1505 C  CA  A VAL A 1 107 ? 25.97300 36.40900 14.27500  0.790 29.31000  ?  107 VAL A CA  1 
ATOM   1506 C  CA  B VAL A 1 107 ? 25.86900 36.55600 14.18500  0.210 30.43000  ?  107 VAL A CA  1 
ATOM   1507 C  C   A VAL A 1 107 ? 25.63200 35.56700 13.05300  0.790 34.47000  ?  107 VAL A C   1 
ATOM   1508 C  C   B VAL A 1 107 ? 25.61700 35.59600 13.02700  0.210 34.69000  ?  107 VAL A C   1 
ATOM   1509 O  O   A VAL A 1 107 ? 25.48600 34.34200 13.14400  0.790 40.38000  ?  107 VAL A O   1 
ATOM   1510 O  O   B VAL A 1 107 ? 25.91200 34.40400 13.15900  0.210 35.28000  ?  107 VAL A O   1 
ATOM   1511 C  CB  A VAL A 1 107 ? 24.71400 37.07300 14.86800  0.790 28.66000  ?  107 VAL A CB  1 
ATOM   1512 C  CB  B VAL A 1 107 ? 24.53900 37.21400 14.57500  0.210 28.75000  ?  107 VAL A CB  1 
ATOM   1513 C  CG1 A VAL A 1 107 ? 23.63200 36.02700 15.11300  0.790 30.06000  ?  107 VAL A CG1 1 
ATOM   1514 C  CG1 B VAL A 1 107 ? 23.49500 36.08600 14.89800  0.210 30.68000  ?  107 VAL A CG1 1 
ATOM   1515 C  CG2 A VAL A 1 107 ? 25.04900 37.82000 16.14000  0.790 34.17000  ?  107 VAL A CG2 1 
ATOM   1516 C  CG2 B VAL A 1 107 ? 24.71500 38.16600 15.70000  0.210 35.59000  ?  107 VAL A CG2 1 
ATOM   1517 N  N   A VAL A 1 108 ? 25.48700 36.21100 11.89300  0.790 37.18000  ?  108 VAL A N   1 
ATOM   1518 N  N   B VAL A 1 108 ? 25.06000 36.11900 11.90600  0.210 34.34000  ?  108 VAL A N   1 
ATOM   1519 C  CA  A VAL A 1 108 ? 25.21100 35.47600 10.66100  0.790 26.54000  ?  108 VAL A CA  1 
ATOM   1520 C  CA  B VAL A 1 108 ? 24.74800 35.31200 10.70800  0.210 25.81000  ?  108 VAL A CA  1 
ATOM   1521 C  C   A VAL A 1 108 ? 26.32100 34.47300 10.39200  0.790 30.47000  ?  108 VAL A C   1 
ATOM   1522 C  C   B VAL A 1 108 ? 25.91600 34.39100 10.34800  0.210 29.98000  ?  108 VAL A C   1 
ATOM   1523 O  O   A VAL A 1 108 ? 26.07500 33.28000 10.16300  0.790 26.40000  ?  108 VAL A O   1 
ATOM   1524 O  O   B VAL A 1 108 ? 25.72200 33.21100 10.01900  0.210 26.46000  ?  108 VAL A O   1 
ATOM   1525 C  CB  A VAL A 1 108 ? 25.05800 36.45300 9.48100   0.790 20.93000  ?  108 VAL A CB  1 
ATOM   1526 C  CB  B VAL A 1 108 ? 24.38300 36.18300 9.48000   0.210 24.37000  ?  108 VAL A CB  1 
ATOM   1527 C  CG1 A VAL A 1 108 ? 24.88000 35.68200 8.18200   0.790 24.15000  ?  108 VAL A CG1 1 
ATOM   1528 C  CG1 B VAL A 1 108 ? 23.82900 35.28600 8.34600   0.210 24.97000  ?  108 VAL A CG1 1 
ATOM   1529 C  CG2 A VAL A 1 108 ? 23.90900 37.41600 9.71600   0.790 25.92000  ?  108 VAL A CG2 1 
ATOM   1530 C  CG2 B VAL A 1 108 ? 23.41500 37.31200 9.77900   0.210 26.70000  ?  108 VAL A CG2 1 
ATOM   1531 N  N   A MET A 1 109 ? 27.56600 34.95100 10.41800  0.790 22.00000  ?  109 MET A N   1 
ATOM   1532 N  N   B MET A 1 109 ? 27.14700 34.92400 10.36300  0.210 25.54000  ?  109 MET A N   1 
ATOM   1533 C  CA  A MET A 1 109 ? 28.71100 34.12200 10.06300  0.790 25.82000  ?  109 MET A CA  1 
ATOM   1534 C  CA  B MET A 1 109 ? 28.26000 34.13400 9.84600   0.210 28.06000  ?  109 MET A CA  1 
ATOM   1535 C  C   A MET A 1 109 ? 28.90900 32.97700 11.05000  0.790 32.64000  ?  109 MET A C   1 
ATOM   1536 C  C   B MET A 1 109 ? 28.57200 32.95300 10.74200  0.210 32.14000  ?  109 MET A C   1 
ATOM   1537 O  O   A MET A 1 109 ? 29.12500 31.83300 10.64500  0.790 42.78000  ?  109 MET A O   1 
ATOM   1538 O  O   B MET A 1 109 ? 28.72800 31.82800 10.25000  0.210 35.15000  ?  109 MET A O   1 
ATOM   1539 C  CB  A MET A 1 109 ? 29.96200 34.99200 10.02200  0.790 26.61000  ?  109 MET A CB  1 
ATOM   1540 C  CB  B MET A 1 109 ? 29.45600 35.04000 9.61600   0.210 27.18000  ?  109 MET A CB  1 
ATOM   1541 C  CG  A MET A 1 109 ? 29.95100 36.01300 8.90500   0.790 35.39000  ?  109 MET A CG  1 
ATOM   1542 C  CG  B MET A 1 109 ? 29.09500 36.09000 8.54800   0.210 31.33000  ?  109 MET A CG  1 
ATOM   1543 S  SD  A MET A 1 109 ? 29.72500 35.17500 7.32300   0.790 44.77000  ?  109 MET A SD  1 
ATOM   1544 S  SD  B MET A 1 109 ? 28.50600 35.30100 7.07400   0.210 28.02000  ?  109 MET A SD  1 
ATOM   1545 C  CE  A MET A 1 109 ? 28.38000 36.06300 6.56500   0.790 16.66000  ?  109 MET A CE  1 
ATOM   1546 C  CE  B MET A 1 109 ? 26.88500 35.93400 7.06800   0.210 29.09000  ?  109 MET A CE  1 
ATOM   1547 N  N   A LEU A 1 110 ? 28.81900 33.25700 12.34900  0.790 30.28000  ?  110 LEU A N   1 
ATOM   1548 N  N   B LEU A 1 110 ? 28.58600 33.17800 12.06900  0.210 31.62000  ?  110 LEU A N   1 
ATOM   1549 C  CA  A LEU A 1 110 ? 28.99800 32.20600 13.34400  0.790 30.72000  ?  110 LEU A CA  1 
ATOM   1550 C  CA  B LEU A 1 110 ? 28.74400 32.11000 13.06900  0.210 33.07000  ?  110 LEU A CA  1 
ATOM   1551 C  C   A LEU A 1 110 ? 27.89400 31.16200 13.24700  0.790 40.61000  ?  110 LEU A C   1 
ATOM   1552 C  C   B LEU A 1 110 ? 27.57800 31.13900 13.05100  0.210 37.24000  ?  110 LEU A C   1 
ATOM   1553 O  O   A LEU A 1 110 ? 28.16200 29.95900 13.32900  0.790 33.94000  ?  110 LEU A O   1 
ATOM   1554 O  O   B LEU A 1 110 ? 27.76200 29.91800 13.23700  0.210 34.20000  ?  110 LEU A O   1 
ATOM   1555 C  CB  A LEU A 1 110 ? 29.03500 32.83000 14.73700  0.790 31.05000  ?  110 LEU A CB  1 
ATOM   1556 C  CB  B LEU A 1 110 ? 28.83800 32.75100 14.41700  0.210 29.31000  ?  110 LEU A CB  1 
ATOM   1557 C  CG  A LEU A 1 110 ? 30.29500 33.64000 15.05000  0.790 34.72000  ?  110 LEU A CG  1 
ATOM   1558 C  CG  B LEU A 1 110 ? 29.94300 33.79900 14.30300  0.210 33.46000  ?  110 LEU A CG  1 
ATOM   1559 C  CD1 A LEU A 1 110 ? 30.26100 34.13300 16.48900  0.790 41.20000  ?  110 LEU A CD1 1 
ATOM   1560 C  CD1 B LEU A 1 110 ? 30.07200 34.60400 15.56800  0.210 33.10000  ?  110 LEU A CD1 1 
ATOM   1561 C  CD2 A LEU A 1 110 ? 31.55900 32.83600 14.79200  0.790 30.95000  ?  110 LEU A CD2 1 
ATOM   1562 C  CD2 B LEU A 1 110 ? 31.26800 33.18000 13.84900  0.210 33.20000  ?  110 LEU A CD2 1 
ATOM   1563 N  N   A ALA A 1 111 ? 26.64500 31.60200 13.06700  0.790 30.86000  ?  111 ALA A N   1 
ATOM   1564 N  N   B ALA A 1 111 ? 26.37800 31.67700 12.83100  0.210 30.90000  ?  111 ALA A N   1 
ATOM   1565 C  CA  A ALA A 1 111 ? 25.54500 30.65000 12.95300  0.790 30.12000  ?  111 ALA A CA  1 
ATOM   1566 C  CA  B ALA A 1 111 ? 25.19400 30.84700 12.74300  0.210 30.92000  ?  111 ALA A CA  1 
ATOM   1567 C  C   A ALA A 1 111 ? 25.74000 29.72700 11.75800  0.790 35.84000  ?  111 ALA A C   1 
ATOM   1568 C  C   B ALA A 1 111 ? 25.22300 29.88900 11.56500  0.210 34.28000  ?  111 ALA A C   1 
ATOM   1569 O  O   A ALA A 1 111 ? 25.49200 28.51900 11.85300  0.790 47.73000  ?  111 ALA A O   1 
ATOM   1570 O  O   B ALA A 1 111 ? 24.56900 28.84000 11.62800  0.210 36.41000  ?  111 ALA A O   1 
ATOM   1571 C  CB  A ALA A 1 111 ? 24.21200 31.38800 12.84200  0.790 22.05000  ?  111 ALA A CB  1 
ATOM   1572 C  CB  B ALA A 1 111 ? 23.94300 31.73900 12.72300  0.210 22.05000  ?  111 ALA A CB  1 
ATOM   1573 N  N   A GLY A 1 112 ? 26.17000 30.27400 10.62200  0.790 33.54000  ?  112 GLY A N   1 
ATOM   1574 N  N   B GLY A 1 112 ? 25.96500 30.21100 10.51300  0.210 33.44000  ?  112 GLY A N   1 
ATOM   1575 C  CA  A GLY A 1 112 ? 26.43200 29.42800 9.47000   0.790 28.29000  ?  112 GLY A CA  1 
ATOM   1576 C  CA  B GLY A 1 112 ? 25.96500 29.36600 9.35200   0.210 30.10000  ?  112 GLY A CA  1 
ATOM   1577 C  C   A GLY A 1 112 ? 27.54500 28.43400 9.73200   0.790 28.15000  ?  112 GLY A C   1 
ATOM   1578 C  C   B GLY A 1 112 ? 27.06800 28.36200 9.51900   0.210 30.90000  ?  112 GLY A C   1 
ATOM   1579 O  O   A GLY A 1 112 ? 27.43200 27.25300 9.39300   0.790 28.85000  ?  112 GLY A O   1 
ATOM   1580 O  O   B GLY A 1 112 ? 26.95100 27.19700 9.15400   0.210 33.16000  ?  112 GLY A O   1 
ATOM   1581 N  N   A PHE A 1 113 ? 28.63200 28.89900 10.34900  0.790 28.35000  ?  113 PHE A N   1 
ATOM   1582 N  N   B PHE A 1 113 ? 28.17100 28.80800 10.08300  0.210 29.31000  ?  113 PHE A N   1 
ATOM   1583 C  CA  A PHE A 1 113 ? 29.75000 28.02000 10.66800  0.790 38.24000  ?  113 PHE A CA  1 
ATOM   1584 C  CA  B PHE A 1 113 ? 29.21900 27.83900 10.35900  0.210 37.92000  ?  113 PHE A CA  1 
ATOM   1585 C  C   A PHE A 1 113 ? 29.32100 26.90200 11.60400  0.790 36.29000  ?  113 PHE A C   1 
ATOM   1586 C  C   B PHE A 1 113 ? 28.67500 26.69300 11.22200  0.210 41.78000  ?  113 PHE A C   1 
ATOM   1587 O  O   A PHE A 1 113 ? 29.70000 25.74200 11.41000  0.790 40.42000  ?  113 PHE A O   1 
ATOM   1588 O  O   B PHE A 1 113 ? 28.67600 25.52300 10.80300  0.210 38.36000  ?  113 PHE A O   1 
ATOM   1589 C  CB  A PHE A 1 113 ? 30.87600 28.84400 11.29000  0.790 35.64000  ?  113 PHE A CB  1 
ATOM   1590 C  CB  B PHE A 1 113 ? 30.40600 28.55900 10.99300  0.210 38.37000  ?  113 PHE A CB  1 
ATOM   1591 C  CG  A PHE A 1 113 ? 32.18000 28.10900 11.42700  0.790 50.75000  ?  113 PHE A CG  1 
ATOM   1592 C  CG  B PHE A 1 113 ? 31.62400 27.74500 11.05800  0.210 43.99000  ?  113 PHE A CG  1 
ATOM   1593 C  CD1 A PHE A 1 113 ? 32.41900 26.93700 10.73000  0.790 42.53000  ?  113 PHE A CD1 1 
ATOM   1594 C  CD1 B PHE A 1 113 ? 31.78800 26.65100 10.22300  0.210 40.89000  ?  113 PHE A CD1 1 
ATOM   1595 C  CD2 A PHE A 1 113 ? 33.17600 28.60400 12.25400  0.790 50.16000  ?  113 PHE A CD2 1 
ATOM   1596 C  CD2 B PHE A 1 113 ? 32.63700 28.08800 11.93400  0.210 51.51000  ?  113 PHE A CD2 1 
ATOM   1597 C  CE1 A PHE A 1 113 ? 33.62400 26.27000 10.85900  0.790 47.42000  ?  113 PHE A CE1 1 
ATOM   1598 C  CE1 B PHE A 1 113 ? 32.90000 25.86400 10.30000  0.210 42.41000  ?  113 PHE A CE1 1 
ATOM   1599 C  CE2 A PHE A 1 113 ? 34.37900 27.94400 12.38600  0.790 53.44000  ?  113 PHE A CE2 1 
ATOM   1600 C  CE2 B PHE A 1 113 ? 33.77200 27.33000 12.00600  0.210 52.72000  ?  113 PHE A CE2 1 
ATOM   1601 C  CZ  A PHE A 1 113 ? 34.60400 26.77500 11.68900  0.790 58.49000  ?  113 PHE A CZ  1 
ATOM   1602 C  CZ  B PHE A 1 113 ? 33.90800 26.21600 11.16800  0.210 49.52000  ?  113 PHE A CZ  1 
ATOM   1603 N  N   A ALA A 1 114 ? 28.52300 27.23000 12.62300  0.790 35.22000  ?  114 ALA A N   1 
ATOM   1604 N  N   B ALA A 1 114 ? 28.06400 27.02400 12.35700  0.210 36.26000  ?  114 ALA A N   1 
ATOM   1605 C  CA  A ALA A 1 114 ? 28.08800 26.21600 13.57600  0.790 33.02000  ?  114 ALA A CA  1 
ATOM   1606 C  CA  B ALA A 1 114 ? 27.62000 25.94800 13.23800  0.210 30.77000  ?  114 ALA A CA  1 
ATOM   1607 C  C   A ALA A 1 114 ? 27.10800 25.24300 12.93600  0.790 25.87000  ?  114 ALA A C   1 
ATOM   1608 C  C   B ALA A 1 114 ? 26.41300 25.21700 12.67700  0.210 34.17000  ?  114 ALA A C   1 
ATOM   1609 O  O   A ALA A 1 114 ? 27.20400 24.02800 13.14800  0.790 32.48000  ?  114 ALA A O   1 
ATOM   1610 O  O   B ALA A 1 114 ? 26.22000 24.03900 12.97000  0.210 33.03000  ?  114 ALA A O   1 
ATOM   1611 C  CB  A ALA A 1 114 ? 27.46100 26.88500 14.79700  0.790 28.91000  ?  114 ALA A CB  1 
ATOM   1612 C  CB  B ALA A 1 114 ? 27.37600 26.51200 14.63300  0.210 32.81000  ?  114 ALA A CB  1 
ATOM   1613 N  N   A GLY A 1 115 ? 26.16400 25.75600 12.14300  0.790 32.59000  ?  115 GLY A N   1 
ATOM   1614 N  N   B GLY A 1 115 ? 25.61600 25.84200 11.82000  0.210 33.34000  ?  115 GLY A N   1 
ATOM   1615 C  CA  A GLY A 1 115 ? 25.21300 24.87900 11.48200  0.790 31.06000  ?  115 GLY A CA  1 
ATOM   1616 C  CA  B GLY A 1 115 ? 24.63800 25.04800 11.10600  0.210 36.15000  ?  115 GLY A CA  1 
ATOM   1617 C  C   A GLY A 1 115 ? 25.88500 23.90800 10.53300  0.790 48.06000  ?  115 GLY A C   1 
ATOM   1618 C  C   B GLY A 1 115 ? 25.30500 23.94400 10.30400  0.210 45.05000  ?  115 GLY A C   1 
ATOM   1619 O  O   A GLY A 1 115 ? 25.50800 22.73700 10.45600  0.790 45.14000  ?  115 GLY A O   1 
ATOM   1620 O  O   B GLY A 1 115 ? 24.89600 22.78400 10.35400  0.210 43.77000  ?  115 GLY A O   1 
ATOM   1621 N  N   A ALA A 1 116 ? 26.88800 24.38100 9.79400   0.790 37.56000  ?  116 ALA A N   1 
ATOM   1622 N  N   B ALA A 1 116 ? 26.39700 24.28800 9.61300   0.210 40.35000  ?  116 ALA A N   1 
ATOM   1623 C  CA  A ALA A 1 116 ? 27.61700 23.49200 8.89900   0.790 47.46000  ?  116 ALA A CA  1 
ATOM   1624 C  CA  B ALA A 1 116 ? 27.09000 23.33000 8.76600   0.210 43.95000  ?  116 ALA A CA  1 
ATOM   1625 C  C   A ALA A 1 116 ? 28.31200 22.37200 9.66300   0.790 48.79000  ?  116 ALA A C   1 
ATOM   1626 C  C   B ALA A 1 116 ? 27.72900 22.20300 9.58700   0.210 46.74000  ?  116 ALA A C   1 
ATOM   1627 O  O   A ALA A 1 116 ? 28.43600 21.25500 9.14900   0.790 39.22000  ?  116 ALA A O   1 
ATOM   1628 O  O   B ALA A 1 116 ? 27.61800 21.03100 9.22000   0.210 46.51000  ?  116 ALA A O   1 
ATOM   1629 C  CB  A ALA A 1 116 ? 28.64100 24.28800 8.08800   0.790 46.87000  ?  116 ALA A CB  1 
ATOM   1630 C  CB  B ALA A 1 116 ? 28.12300 24.07300 7.90100   0.210 46.87000  ?  116 ALA A CB  1 
ATOM   1631 N  N   A MET A 1 117 ? 28.76200 22.64200 10.88800  0.790 42.33000  ?  117 MET A N   1 
ATOM   1632 N  N   B MET A 1 117 ? 28.37700 22.52100 10.71900  0.210 43.49000  ?  117 MET A N   1 
ATOM   1633 C  CA  A MET A 1 117 ? 29.54600 21.68000 11.65200  0.790 39.99000  ?  117 MET A CA  1 
ATOM   1634 C  CA  B MET A 1 117 ? 29.04400 21.47000 11.49400  0.210 45.78000  ?  117 MET A CA  1 
ATOM   1635 C  C   A MET A 1 117 ? 28.69700 20.75400 12.51600  0.790 55.66000  ?  117 MET A C   1 
ATOM   1636 C  C   B MET A 1 117 ? 28.02500 20.59200 12.23500  0.210 50.58000  ?  117 MET A C   1 
ATOM   1637 O  O   A MET A 1 117 ? 29.25600 19.88800 13.19700  0.790 53.94000  ?  117 MET A O   1 
ATOM   1638 O  O   B MET A 1 117 ? 28.34900 19.47900 12.62300  0.210 47.99000  ?  117 MET A O   1 
ATOM   1639 C  CB  A MET A 1 117 ? 30.55300 22.41500 12.54600  0.790 41.98000  ?  117 MET A CB  1 
ATOM   1640 C  CB  B MET A 1 117 ? 30.03500 22.06400 12.50400  0.210 42.34000  ?  117 MET A CB  1 
ATOM   1641 C  CG  A MET A 1 117 ? 31.67800 23.10700 11.79600  0.790 46.92000  ?  117 MET A CG  1 
ATOM   1642 C  CG  B MET A 1 117 ? 31.10100 22.87500 11.83000  0.210 46.48000  ?  117 MET A CG  1 
ATOM   1643 S  SD  A MET A 1 117 ? 32.83500 21.94400 11.05100  0.790 60.24000  ?  117 MET A SD  1 
ATOM   1644 S  SD  B MET A 1 117 ? 32.38400 22.00200 10.93000  0.210 54.91000  ?  117 MET A SD  1 
ATOM   1645 C  CE  A MET A 1 117 ? 33.63400 21.27000 12.51100  0.790 68.39000  ?  117 MET A CE  1 
ATOM   1646 C  CE  B MET A 1 117 ? 33.45400 21.63500 12.33500  0.210 64.31000  ?  117 MET A CE  1 
ATOM   1647 N  N   A VAL A 1 118 ? 27.38100 20.90700 12.50700  0.790 45.18000  ?  118 VAL A N   1 
ATOM   1648 N  N   B VAL A 1 118 ? 26.80900 21.09100 12.35200  0.210 47.69000  ?  118 VAL A N   1 
ATOM   1649 C  CA  A VAL A 1 118 ? 26.47900 20.10400 13.33200  0.790 46.48000  ?  118 VAL A CA  1 
ATOM   1650 C  CA  B VAL A 1 118 ? 25.75100 20.38500 13.15100  0.210 52.70000  ?  118 VAL A CA  1 
ATOM   1651 C  C   A VAL A 1 118 ? 25.81700 19.06200 12.44400  0.790 50.53000  ?  118 VAL A C   1 
ATOM   1652 C  C   B VAL A 1 118 ? 25.12900 19.33900 12.19700  0.210 52.72000  ?  118 VAL A C   1 
ATOM   1653 O  O   A VAL A 1 118 ? 25.21000 19.42800 11.42600  0.790 49.47000  ?  118 VAL A O   1 
ATOM   1654 O  O   B VAL A 1 118 ? 24.34000 19.71300 11.33800  0.210 45.92000  ?  118 VAL A O   1 
ATOM   1655 C  CB  A VAL A 1 118 ? 25.41800 20.98200 14.02300  0.790 51.87000  ?  118 VAL A CB  1 
ATOM   1656 C  CB  B VAL A 1 118 ? 24.70500 21.38500 13.66700  0.210 44.28000  ?  118 VAL A CB  1 
ATOM   1657 C  CG1 A VAL A 1 118 ? 24.24900 20.13100 14.49200  0.790 45.11000  ?  118 VAL A CG1 1 
ATOM   1658 C  CG1 B VAL A 1 118 ? 23.46600 20.66600 14.06000  0.210 46.47000  ?  118 VAL A CG1 1 
ATOM   1659 C  CG2 A VAL A 1 118 ? 26.03700 21.75100 15.18200  0.790 43.11000  ?  118 VAL A CG2 1 
ATOM   1660 C  CG2 B VAL A 1 118 ? 25.23200 22.13400 14.82100  0.210 41.03000  ?  118 VAL A CG2 1 
ATOM   1661 N  N   A PRO A 1 119 ? 25.87800 17.76800 12.79300  0.790 61.12000  ?  119 PRO A N   1 
ATOM   1662 N  N   B PRO A 1 119 ? 25.46000 18.05800 12.38600  0.210 57.13000  ?  119 PRO A N   1 
ATOM   1663 C  CA  A PRO A 1 119 ? 25.33800 16.74200 11.88800  0.790 49.96000  ?  119 PRO A CA  1 
ATOM   1664 C  CA  B PRO A 1 119 ? 24.93100 17.05400 11.42600  0.210 50.30000  ?  119 PRO A CA  1 
ATOM   1665 C  C   A PRO A 1 119 ? 23.81800 16.65600 11.88400  0.790 52.58000  ?  119 PRO A C   1 
ATOM   1666 C  C   B PRO A 1 119 ? 23.43400 17.07100 11.35300  0.210 56.80000  ?  119 PRO A C   1 
ATOM   1667 O  O   A PRO A 1 119 ? 23.21700 16.35600 10.84800  0.790 53.48000  ?  119 PRO A O   1 
ATOM   1668 O  O   B PRO A 1 119 ? 22.86300 17.15400 10.25400  0.210 49.22000  ?  119 PRO A O   1 
ATOM   1669 C  CB  A PRO A 1 119 ? 25.96100 15.43400 12.40300  0.790 50.59000  ?  119 PRO A CB  1 
ATOM   1670 C  CB  B PRO A 1 119 ? 25.43900 15.70800 11.98400  0.210 50.64000  ?  119 PRO A CB  1 
ATOM   1671 C  CG  A PRO A 1 119 ? 26.64800 15.75800 13.70300  0.790 58.12000  ?  119 PRO A CG  1 
ATOM   1672 C  CG  B PRO A 1 119 ? 26.18900 16.00100 13.21000  0.210 57.10000  ?  119 PRO A CG  1 
ATOM   1673 C  CD  A PRO A 1 119 ? 26.41900 17.20000 14.04200  0.790 58.53000  ?  119 PRO A CD  1 
ATOM   1674 C  CD  B PRO A 1 119 ? 26.09100 17.44900 13.56100  0.210 58.35000  ?  119 PRO A CD  1 
ATOM   1675 N  N   A GLY A 1 120 ? 23.18500 16.90700 13.02900  0.790 57.12000  ?  120 GLY A N   1 
ATOM   1676 N  N   B GLY A 1 120 ? 22.78100 17.07200 12.51600  0.210 64.21000  ?  120 GLY A N   1 
ATOM   1677 C  CA  A GLY A 1 120 ? 21.75200 16.74600 13.15500  0.790 68.69000  ?  120 GLY A CA  1 
ATOM   1678 C  CA  B GLY A 1 120 ? 21.35400 16.86500 12.57400  0.210 69.97000  ?  120 GLY A CA  1 
ATOM   1679 C  C   A GLY A 1 120 ? 20.96100 17.91500 12.60200  0.790 65.46000  ?  120 GLY A C   1 
ATOM   1680 C  C   B GLY A 1 120 ? 20.53200 17.98900 11.98100  0.210 65.44000  ?  120 GLY A C   1 
ATOM   1681 O  O   A GLY A 1 120 ? 21.50000 18.91300 12.12300  0.790 66.66000  ?  120 GLY A O   1 
ATOM   1682 O  O   B GLY A 1 120 ? 21.02700 18.98300 11.45500  0.210 63.74000  ?  120 GLY A O   1 
ATOM   1683 N  N   A ILE A 1 121 ? 19.63400 17.78300 12.70000  0.790 72.20000  ?  121 ILE A N   1 
ATOM   1684 N  N   B ILE A 1 121 ? 19.21800 17.81400 12.08700  0.210 70.39000  ?  121 ILE A N   1 
ATOM   1685 C  CA  A ILE A 1 121 ? 18.73100 18.82400 12.22700  0.790 70.69000  ?  121 ILE A CA  1 
ATOM   1686 C  CA  B ILE A 1 121 ? 18.29300 18.79300 11.55000  0.210 67.16000  ?  121 ILE A CA  1 
ATOM   1687 C  C   A ILE A 1 121 ? 18.82600 20.09900 13.04100  0.790 64.25000  ?  121 ILE A C   1 
ATOM   1688 C  C   B ILE A 1 121 ? 18.31000 20.11100 12.32500  0.210 61.70000  ?  121 ILE A C   1 
ATOM   1689 O  O   A ILE A 1 121 ? 18.32000 21.14100 12.60500  0.790 55.52000  ?  121 ILE A O   1 
ATOM   1690 O  O   B ILE A 1 121 ? 17.95900 21.15900 11.76900  0.210 61.72000  ?  121 ILE A O   1 
ATOM   1691 C  CB  A ILE A 1 121 ? 17.27800 18.33300 12.25900  0.790 77.88000  ?  121 ILE A CB  1 
ATOM   1692 C  CB  B ILE A 1 121 ? 16.89900 18.17600 11.54900  0.210 74.85000  ?  121 ILE A CB  1 
ATOM   1693 C  CG1 A ILE A 1 121 ? 16.35700 19.25200 11.47300  0.790 80.12000  ?  121 ILE A CG1 1 
ATOM   1694 C  CG1 B ILE A 1 121 ? 16.04400 18.88100 10.51800  0.210 76.86000  ?  121 ILE A CG1 1 
ATOM   1695 C  CG2 A ILE A 1 121 ? 16.76400 18.34900 13.69700  0.790 69.48000  ?  121 ILE A CG2 1 
ATOM   1696 C  CG2 B ILE A 1 121 ? 16.28500 18.34000 12.93400  0.210 76.16000  ?  121 ILE A CG2 1 
ATOM   1697 C  CD1 A ILE A 1 121 ? 15.32800 18.51600 10.64500  0.790 80.84000  ?  121 ILE A CD1 1 
ATOM   1698 C  CD1 B ILE A 1 121 ? 15.17900 17.95800 9.72600   0.210 79.68000  ?  121 ILE A CD1 1 
ATOM   1699 N  N   A GLU A 1 122 ? 19.41800 20.05000 14.24000  0.790 65.74000  ?  122 GLU A N   1 
ATOM   1700 N  N   B GLU A 1 122 ? 18.71500 20.09800 13.59700  0.210 64.06000  ?  122 GLU A N   1 
ATOM   1701 C  CA  A GLU A 1 122 ? 19.62400 21.30300 14.95800  0.790 68.11000  ?  122 GLU A CA  1 
ATOM   1702 C  CA  B GLU A 1 122 ? 18.92500 21.35700 14.30300  0.210 61.97000  ?  122 GLU A CA  1 
ATOM   1703 C  C   A GLU A 1 122 ? 20.32600 22.32200 14.06600  0.790 54.08000  ?  122 GLU A C   1 
ATOM   1704 C  C   B GLU A 1 122 ? 19.77600 22.32100 13.50300  0.210 51.53000  ?  122 GLU A C   1 
ATOM   1705 O  O   A GLU A 1 122 ? 20.24700 23.53000 14.31900  0.790 53.52000  ?  122 GLU A O   1 
ATOM   1706 O  O   B GLU A 1 122 ? 19.80600 23.51800 13.79800  0.210 50.85000  ?  122 GLU A O   1 
ATOM   1707 C  CB  A GLU A 1 122 ? 20.46500 21.13400 16.23000  0.790 56.84000  ?  122 GLU A CB  1 
ATOM   1708 C  CB  B GLU A 1 122 ? 19.60800 21.12200 15.63800  0.210 64.57000  ?  122 GLU A CB  1 
ATOM   1709 C  CG  A GLU A 1 122 ? 20.20400 19.89900 17.03600  0.790 61.27000  ?  122 GLU A CG  1 
ATOM   1710 C  CG  B GLU A 1 122 ? 19.29800 19.79600 16.27700  0.210 61.22000  ?  122 GLU A CG  1 
ATOM   1711 C  CD  A GLU A 1 122 ? 21.21100 18.81500 16.72000  0.790 69.75000  ?  122 GLU A CD  1 
ATOM   1712 C  CD  B GLU A 1 122 ? 20.43500 18.80600 16.18600  0.210 68.23000  ?  122 GLU A CD  1 
ATOM   1713 O  OE1 A GLU A 1 122 ? 22.42300 19.12800 16.60500  0.790 63.04000  ?  122 GLU A OE1 1 
ATOM   1714 O  OE1 B GLU A 1 122 ? 21.61400 19.20400 16.40400  0.210 66.69000  ?  122 GLU A OE1 1 
ATOM   1715 O  OE2 A GLU A 1 122 ? 20.78700 17.64700 16.59100  0.790 64.66000  -1 122 GLU A OE2 1 
ATOM   1716 O  OE2 B GLU A 1 122 ? 20.15000 17.63300 15.90200  0.210 67.05000  -1 122 GLU A OE2 1 
ATOM   1717 N  N   A ARG A 1 123 ? 21.04500 21.85100 13.04000  0.790 55.25000  ?  123 ARG A N   1 
ATOM   1718 N  N   B ARG A 1 123 ? 20.55300 21.81200 12.54900  0.210 53.44000  ?  123 ARG A N   1 
ATOM   1719 C  CA  A ARG A 1 123 ? 21.76700 22.75700 12.15500  0.790 52.16000  ?  123 ARG A CA  1 
ATOM   1720 C  CA  B ARG A 1 123 ? 21.36700 22.71300 11.75100  0.210 50.24000  ?  123 ARG A CA  1 
ATOM   1721 C  C   A ARG A 1 123 ? 20.82000 23.67600 11.39700  0.790 43.45000  ?  123 ARG A C   1 
ATOM   1722 C  C   B ARG A 1 123 ? 20.49400 23.75300 11.08900  0.210 41.15000  ?  123 ARG A C   1 
ATOM   1723 O  O   A ARG A 1 123 ? 21.20700 24.78800 11.02400  0.790 35.58000  ?  123 ARG A O   1 
ATOM   1724 O  O   B ARG A 1 123 ? 20.87200 24.91900 10.99700  0.210 35.91000  ?  123 ARG A O   1 
ATOM   1725 C  CB  A ARG A 1 123 ? 22.63000 21.95800 11.17700  0.790 46.13000  ?  123 ARG A CB  1 
ATOM   1726 C  CB  B ARG A 1 123 ? 22.18300 21.93600 10.72200  0.210 46.42000  ?  123 ARG A CB  1 
ATOM   1727 C  CG  A ARG A 1 123 ? 21.86200 21.28700 10.04100  0.790 46.57000  ?  123 ARG A CG  1 
ATOM   1728 C  CG  B ARG A 1 123 ? 21.45500 21.46000 9.50700   0.210 49.35000  ?  123 ARG A CG  1 
ATOM   1729 C  CD  A ARG A 1 123 ? 22.76500 20.31500 9.28700   0.790 53.96000  ?  123 ARG A CD  1 
ATOM   1730 C  CD  B ARG A 1 123 ? 22.36000 20.56300 8.67100   0.210 53.15000  ?  123 ARG A CD  1 
ATOM   1731 N  NE  A ARG A 1 123 ? 22.18100 19.83800 8.03600   0.790 51.46000  ?  123 ARG A NE  1 
ATOM   1732 N  NE  B ARG A 1 123 ? 21.70300 20.28200 7.40500   0.210 55.93000  ?  123 ARG A NE  1 
ATOM   1733 C  CZ  A ARG A 1 123 ? 21.27900 18.86600 7.95100   0.790 63.36000  ?  123 ARG A CZ  1 
ATOM   1734 C  CZ  B ARG A 1 123 ? 20.70400 19.42000 7.25900   0.210 58.19000  ?  123 ARG A CZ  1 
ATOM   1735 N  NH1 A ARG A 1 123 ? 20.84400 18.26300 9.04800   0.790 70.09000  ?  123 ARG A NH1 1 
ATOM   1736 N  NH1 B ARG A 1 123 ? 20.31600 18.63000 8.25200   0.210 67.29000  ?  123 ARG A NH1 1 
ATOM   1737 N  NH2 A ARG A 1 123 ? 20.80900 18.49800 6.76700   0.790 50.85000  ?  123 ARG A NH2 1 
ATOM   1738 N  NH2 B ARG A 1 123 ? 20.06800 19.35400 6.09200   0.210 49.41000  ?  123 ARG A NH2 1 
ATOM   1739 N  N   A TYR A 1 124 ? 19.58300 23.24000 11.15400  0.790 34.90000  ?  124 TYR A N   1 
ATOM   1740 N  N   B TYR A 1 124 ? 19.29200 23.36800 10.69900  0.210 36.77000  ?  124 TYR A N   1 
ATOM   1741 C  CA  A TYR A 1 124 ? 18.62300 24.13900 10.52300  0.790 36.22000  ?  124 TYR A CA  1 
ATOM   1742 C  CA  B TYR A 1 124 ? 18.36700 24.35900 10.18100  0.210 36.43000  ?  124 TYR A CA  1 
ATOM   1743 C  C   A TYR A 1 124 ? 18.16400 25.21400 11.49900  0.790 39.99000  ?  124 TYR A C   1 
ATOM   1744 C  C   B TYR A 1 124 ? 17.97100 25.37000 11.27100  0.210 38.13000  ?  124 TYR A C   1 
ATOM   1745 O  O   A TYR A 1 124 ? 17.84500 26.33400 11.08300  0.790 35.02000  ?  124 TYR A O   1 
ATOM   1746 O  O   B TYR A 1 124 ? 17.80000 26.55400 10.99800  0.210 34.21000  ?  124 TYR A O   1 
ATOM   1747 C  CB  A TYR A 1 124 ? 17.43400 23.34900 9.98300   0.790 27.43000  ?  124 TYR A CB  1 
ATOM   1748 C  CB  B TYR A 1 124 ? 17.14400 23.65600 9.62500   0.210 30.95000  ?  124 TYR A CB  1 
ATOM   1749 C  CG  A TYR A 1 124 ? 17.75400 22.53900 8.74100   0.790 43.91000  ?  124 TYR A CG  1 
ATOM   1750 C  CG  B TYR A 1 124 ? 17.36100 22.90400 8.36000   0.210 44.68000  ?  124 TYR A CG  1 
ATOM   1751 C  CD1 A TYR A 1 124 ? 18.05900 23.16100 7.53400   0.790 48.35000  ?  124 TYR A CD1 1 
ATOM   1752 C  CD1 B TYR A 1 124 ? 17.32000 23.54100 7.12100   0.210 43.91000  ?  124 TYR A CD1 1 
ATOM   1753 C  CD2 A TYR A 1 124 ? 17.74900 21.15200 8.77700   0.790 53.21000  ?  124 TYR A CD2 1 
ATOM   1754 C  CD2 B TYR A 1 124 ? 17.58200 21.53300 8.38800   0.210 53.03000  ?  124 TYR A CD2 1 
ATOM   1755 C  CE1 A TYR A 1 124 ? 18.35100 22.41800 6.39900   0.790 50.38000  ?  124 TYR A CE1 1 
ATOM   1756 C  CE1 B TYR A 1 124 ? 17.46400 22.83200 5.95600   0.210 47.16000  ?  124 TYR A CE1 1 
ATOM   1757 C  CE2 A TYR A 1 124 ? 18.03800 20.40500 7.65100   0.790 53.10000  ?  124 TYR A CE2 1 
ATOM   1758 C  CE2 B TYR A 1 124 ? 17.72800 20.82000 7.22700   0.210 55.23000  ?  124 TYR A CE2 1 
ATOM   1759 C  CZ  A TYR A 1 124 ? 18.33800 21.04100 6.46700   0.790 61.28000  ?  124 TYR A CZ  1 
ATOM   1760 C  CZ  B TYR A 1 124 ? 17.68200 21.48100 6.01100   0.210 52.24000  ?  124 TYR A CZ  1 
ATOM   1761 O  OH  A TYR A 1 124 ? 18.62400 20.28900 5.35100   0.790 52.06000  ?  124 TYR A OH  1 
ATOM   1762 O  OH  B TYR A 1 124 ? 17.84900 20.76000 4.86200   0.210 53.62000  ?  124 TYR A OH  1 
ATOM   1763 N  N   A ALA A 1 125 ? 18.13700 24.89900 12.79600  0.790 36.49000  ?  125 ALA A N   1 
ATOM   1764 N  N   B ALA A 1 125 ? 17.80300 24.92600 12.51800  0.210 36.80000  ?  125 ALA A N   1 
ATOM   1765 C  CA  A ALA A 1 125 ? 17.84200 25.91800 13.79800  0.790 33.21000  ?  125 ALA A CA  1 
ATOM   1766 C  CA  B ALA A 1 125 ? 17.61200 25.88200 13.59600  0.210 32.30000  ?  125 ALA A CA  1 
ATOM   1767 C  C   A ALA A 1 125 ? 18.92200 26.99300 13.81500  0.790 36.95000  ?  125 ALA A C   1 
ATOM   1768 C  C   B ALA A 1 125 ? 18.74500 26.89500 13.61400  0.210 35.16000  ?  125 ALA A C   1 
ATOM   1769 O  O   A ALA A 1 125 ? 18.62500 28.18400 13.96600  0.790 32.19000  ?  125 ALA A O   1 
ATOM   1770 O  O   B ALA A 1 125 ? 18.50000 28.11200 13.57700  0.210 33.39000  ?  125 ALA A O   1 
ATOM   1771 C  CB  A ALA A 1 125 ? 17.70700 25.27200 15.17600  0.790 37.01000  ?  125 ALA A CB  1 
ATOM   1772 C  CB  B ALA A 1 125 ? 17.49700 25.15300 14.94800  0.210 38.39000  ?  125 ALA A CB  1 
ATOM   1773 N  N   A LEU A 1 126 ? 20.18700 26.59200 13.67500  0.790 29.81000  ?  126 LEU A N   1 
ATOM   1774 N  N   B LEU A 1 126 ? 19.99600 26.41900 13.66200  0.210 29.79000  ?  126 LEU A N   1 
ATOM   1775 C  CA  A LEU A 1 126 ? 21.26200 27.57600 13.59500  0.790 28.00000  ?  126 LEU A CA  1 
ATOM   1776 C  CA  B LEU A 1 126 ? 21.10600 27.36700 13.54100  0.210 29.42000  ?  126 LEU A CA  1 
ATOM   1777 C  C   A LEU A 1 126 ? 21.16700 28.38400 12.30500  0.790 35.64000  ?  126 LEU A C   1 
ATOM   1778 C  C   B LEU A 1 126 ? 21.06500 28.11200 12.22700  0.210 35.04000  ?  126 LEU A C   1 
ATOM   1779 O  O   A LEU A 1 126 ? 21.35200 29.60700 12.31500  0.790 34.05000  ?  126 LEU A O   1 
ATOM   1780 O  O   B LEU A 1 126 ? 21.32000 29.32100 12.17400  0.210 34.26000  ?  126 LEU A O   1 
ATOM   1781 C  CB  A LEU A 1 126 ? 22.61800 26.87700 13.70100  0.790 34.48000  ?  126 LEU A CB  1 
ATOM   1782 C  CB  B LEU A 1 126 ? 22.45200 26.69000 13.68500  0.210 35.25000  ?  126 LEU A CB  1 
ATOM   1783 C  CG  A LEU A 1 126 ? 22.87500 26.20500 15.05100  0.790 37.85000  ?  126 LEU A CG  1 
ATOM   1784 C  CG  B LEU A 1 126 ? 22.92100 26.37900 15.11100  0.210 38.32000  ?  126 LEU A CG  1 
ATOM   1785 C  CD1 A LEU A 1 126 ? 23.98500 25.17100 14.99200  0.790 43.40000  ?  126 LEU A CD1 1 
ATOM   1786 C  CD1 B LEU A 1 126 ? 24.03800 25.37900 15.03900  0.210 42.50000  ?  126 LEU A CD1 1 
ATOM   1787 C  CD2 A LEU A 1 126 ? 23.18500 27.26700 16.11500  0.790 40.52000  ?  126 LEU A CD2 1 
ATOM   1788 C  CD2 B LEU A 1 126 ? 23.46100 27.65600 15.77300  0.210 36.24000  ?  126 LEU A CD2 1 
ATOM   1789 N  N   A PHE A 1 127 ? 20.85500 27.72100 11.18900  0.790 35.10000  ?  127 PHE A N   1 
ATOM   1790 N  N   B PHE A 1 127 ? 20.76800 27.40900 11.14100  0.210 35.00000  ?  127 PHE A N   1 
ATOM   1791 C  CA  A PHE A 1 127 ? 20.69500 28.43900 9.93000   0.790 37.97000  ?  127 PHE A CA  1 
ATOM   1792 C  CA  B PHE A 1 127 ? 20.53800 28.15000 9.92700   0.210 36.57000  ?  127 PHE A CA  1 
ATOM   1793 C  C   A PHE A 1 127 ? 19.59300 29.48800 10.02900  0.790 31.38000  ?  127 PHE A C   1 
ATOM   1794 C  C   B PHE A 1 127 ? 19.45100 29.17900 10.15300  0.210 30.22000  ?  127 PHE A C   1 
ATOM   1795 O  O   A PHE A 1 127 ? 19.75100 30.61500 9.54500   0.790 31.85000  ?  127 PHE A O   1 
ATOM   1796 O  O   B PHE A 1 127 ? 19.62900 30.37000 9.86800   0.210 29.85000  ?  127 PHE A O   1 
ATOM   1797 C  CB  A PHE A 1 127 ? 20.39400 27.45800 8.79900   0.790 34.70000  ?  127 PHE A CB  1 
ATOM   1798 C  CB  B PHE A 1 127 ? 20.12900 27.24700 8.78200   0.210 34.97000  ?  127 PHE A CB  1 
ATOM   1799 C  CG  A PHE A 1 127 ? 19.94500 28.12300 7.53400   0.790 32.74000  ?  127 PHE A CG  1 
ATOM   1800 C  CG  B PHE A 1 127 ? 19.56500 28.00400 7.64500   0.210 33.58000  ?  127 PHE A CG  1 
ATOM   1801 C  CD1 A PHE A 1 127 ? 20.87200 28.62200 6.63200   0.790 33.39000  ?  127 PHE A CD1 1 
ATOM   1802 C  CD1 B PHE A 1 127 ? 20.40400 28.66600 6.78300   0.210 34.69000  ?  127 PHE A CD1 1 
ATOM   1803 C  CD2 A PHE A 1 127 ? 18.59800 28.25800 7.24600   0.790 37.55000  ?  127 PHE A CD2 1 
ATOM   1804 C  CD2 B PHE A 1 127 ? 18.18700 28.10700 7.47600   0.210 36.26000  ?  127 PHE A CD2 1 
ATOM   1805 C  CE1 A PHE A 1 127 ? 20.46400 29.24000 5.46900   0.790 37.22000  ?  127 PHE A CE1 1 
ATOM   1806 C  CE1 B PHE A 1 127 ? 19.90300 29.38600 5.71600   0.210 39.14000  ?  127 PHE A CE1 1 
ATOM   1807 C  CE2 A PHE A 1 127 ? 18.18400 28.87700 6.07800   0.790 42.16000  ?  127 PHE A CE2 1 
ATOM   1808 C  CE2 B PHE A 1 127 ? 17.64800 28.81900 6.41400   0.210 34.06000  ?  127 PHE A CE2 1 
ATOM   1809 C  CZ  A PHE A 1 127 ? 19.11700 29.36600 5.19300   0.790 47.79000  ?  127 PHE A CZ  1 
ATOM   1810 C  CZ  B PHE A 1 127 ? 18.51600 29.48200 5.53100   0.210 46.96000  ?  127 PHE A CZ  1 
ATOM   1811 N  N   A GLY A 1 128 ? 18.47100 29.13500 10.65800  0.790 29.43000  ?  128 GLY A N   1 
ATOM   1812 N  N   B GLY A 1 128 ? 18.31600 28.72400 10.67900  0.210 29.91000  ?  128 GLY A N   1 
ATOM   1813 C  CA  A GLY A 1 128 ? 17.38700 30.09100 10.81100  0.790 24.01000  ?  128 GLY A CA  1 
ATOM   1814 C  CA  B GLY A 1 128 ? 17.18000 29.61000 10.81200  0.210 25.53000  ?  128 GLY A CA  1 
ATOM   1815 C  C   A GLY A 1 128 ? 17.79200 31.31600 11.60300  0.790 30.38000  ?  128 GLY A C   1 
ATOM   1816 C  C   B GLY A 1 128 ? 17.52800 30.79500 11.68400  0.210 26.89000  ?  128 GLY A C   1 
ATOM   1817 O  O   A GLY A 1 128 ? 17.36900 32.43400 11.29500  0.790 27.05000  ?  128 GLY A O   1 
ATOM   1818 O  O   B GLY A 1 128 ? 17.11400 31.92500 11.42000  0.210 29.97000  ?  128 GLY A O   1 
ATOM   1819 N  N   A MET A 1 129 ? 18.61300 31.12900 12.63800  0.790 23.53000  ?  129 MET A N   1 
ATOM   1820 N  N   B MET A 1 129 ? 18.34600 30.58300 12.69900  0.210 24.01000  ?  129 MET A N   1 
ATOM   1821 C  CA  A MET A 1 129 ? 19.03400 32.27700 13.43200  0.790 22.51000  ?  129 MET A CA  1 
ATOM   1822 C  CA  B MET A 1 129 ? 18.74300 31.78800 13.42400  0.210 26.51000  ?  129 MET A CA  1 
ATOM   1823 C  C   A MET A 1 129 ? 19.90000 33.22600 12.61700  0.790 25.32000  ?  129 MET A C   1 
ATOM   1824 C  C   B MET A 1 129 ? 19.41400 32.79900 12.51300  0.210 25.00000  ?  129 MET A C   1 
ATOM   1825 O  O   A MET A 1 129 ? 19.76500 34.45000 12.72600  0.790 30.56000  ?  129 MET A O   1 
ATOM   1826 O  O   B MET A 1 129 ? 18.88000 33.89000 12.30700  0.210 20.38000  ?  129 MET A O   1 
ATOM   1827 C  CB  A MET A 1 129 ? 19.79800 31.82700 14.67000  0.790 29.38000  ?  129 MET A CB  1 
ATOM   1828 C  CB  B MET A 1 129 ? 19.65000 31.50400 14.60100  0.210 27.99000  ?  129 MET A CB  1 
ATOM   1829 C  CG  A MET A 1 129 ? 19.46700 32.67900 15.86300  0.790 50.06000  ?  129 MET A CG  1 
ATOM   1830 C  CG  B MET A 1 129 ? 19.55200 32.78300 15.36800  0.210 44.43000  ?  129 MET A CG  1 
ATOM   1831 S  SD  A MET A 1 129 ? 20.42500 32.32800 17.35100  0.790 56.52000  ?  129 MET A SD  1 
ATOM   1832 S  SD  B MET A 1 129 ? 20.43900 33.06100 16.84400  0.210 42.28000  ?  129 MET A SD  1 
ATOM   1833 C  CE  A MET A 1 129 ? 22.04800 32.94500 16.86700  0.790 58.02000  ?  129 MET A CE  1 
ATOM   1834 C  CE  B MET A 1 129 ? 22.03100 32.69300 16.13100  0.210 45.64000  ?  129 MET A CE  1 
ATOM   1835 N  N   A GLY A 1 130 ? 20.80900 32.68000 11.81100  0.790 27.03000  ?  130 GLY A N   1 
ATOM   1836 N  N   B GLY A 1 130 ? 20.59400 32.44800 12.00400  0.210 27.44000  ?  130 GLY A N   1 
ATOM   1837 C  CA  A GLY A 1 130 ? 21.58200 33.52300 10.91700  0.790 30.97000  ?  130 GLY A CA  1 
ATOM   1838 C  CA  B GLY A 1 130 ? 21.06500 32.95700 10.72000  0.210 29.36000  ?  130 GLY A CA  1 
ATOM   1839 C  C   A GLY A 1 130 ? 20.70500 34.25200 9.92000   0.790 33.45000  ?  130 GLY A C   1 
ATOM   1840 C  C   B GLY A 1 130 ? 20.17100 33.92800 9.94400   0.210 29.74000  ?  130 GLY A C   1 
ATOM   1841 O  O   A GLY A 1 130 ? 20.96000 35.41200 9.58700   0.790 32.45000  ?  130 GLY A O   1 
ATOM   1842 O  O   B GLY A 1 130 ? 20.39400 35.15400 10.06100  0.210 30.68000  ?  130 GLY A O   1 
ATOM   1843 N  N   A ALA A 1 131 ? 19.65700 33.58500 9.43100   0.790 24.40000  ?  131 ALA A N   1 
ATOM   1844 N  N   B ALA A 1 131 ? 19.15300 33.43400 9.21300   0.210 21.98000  ?  131 ALA A N   1 
ATOM   1845 C  CA  A ALA A 1 131 ? 18.74100 34.24300 8.50600   0.790 16.18000  ?  131 ALA A CA  1 
ATOM   1846 C  CA  B ALA A 1 131 ? 18.40600 34.32400 8.32200   0.210 18.87000  ?  131 ALA A CA  1 
ATOM   1847 C  C   A ALA A 1 131 ? 18.06700 35.43900 9.16300   0.790 26.50000  ?  131 ALA A C   1 
ATOM   1848 C  C   B ALA A 1 131 ? 17.89400 35.57000 9.04300   0.210 27.99000  ?  131 ALA A C   1 
ATOM   1849 O  O   A ALA A 1 131 ? 17.94200 36.50600 8.55200   0.790 34.88000  ?  131 ALA A O   1 
ATOM   1850 O  O   B ALA A 1 131 ? 17.97800 36.70200 8.53800   0.210 33.78000  ?  131 ALA A O   1 
ATOM   1851 C  CB  A ALA A 1 131 ? 17.69000 33.25400 8.00700   0.790 24.27000  ?  131 ALA A CB  1 
ATOM   1852 C  CB  B ALA A 1 131 ? 17.23500 33.58100 7.70700   0.210 20.90000  ?  131 ALA A CB  1 
ATOM   1853 N  N   A VAL A 1 132 ? 17.62200 35.28000 10.41000  0.790 27.58000  ?  132 VAL A N   1 
ATOM   1854 N  N   B VAL A 1 132 ? 17.30700 35.36900 10.20800  0.210 27.26000  ?  132 VAL A N   1 
ATOM   1855 C  CA  A VAL A 1 132 ? 16.95800 36.38200 11.09900  0.790 28.59000  ?  132 VAL A CA  1 
ATOM   1856 C  CA  B VAL A 1 132 ? 16.82000 36.45300 11.05300  0.210 28.16000  ?  132 VAL A CA  1 
ATOM   1857 C  C   A VAL A 1 132 ? 17.91600 37.55700 11.25900  0.790 23.98000  ?  132 VAL A C   1 
ATOM   1858 C  C   B VAL A 1 132 ? 17.78300 37.61600 11.19100  0.210 24.39000  ?  132 VAL A C   1 
ATOM   1859 O  O   A VAL A 1 132 ? 17.56600 38.71100 10.98400  0.790 31.88000  ?  132 VAL A O   1 
ATOM   1860 O  O   B VAL A 1 132 ? 17.47000 38.75900 10.85300  0.210 31.09000  ?  132 VAL A O   1 
ATOM   1861 C  CB  A VAL A 1 132 ? 16.40600 35.91400 12.45700  0.790 38.34000  ?  132 VAL A CB  1 
ATOM   1862 C  CB  B VAL A 1 132 ? 16.51200 35.86500 12.42200  0.210 35.20000  ?  132 VAL A CB  1 
ATOM   1863 C  CG1 A VAL A 1 132 ? 15.95100 37.11100 13.27500  0.790 32.80000  ?  132 VAL A CG1 1 
ATOM   1864 C  CG1 B VAL A 1 132 ? 16.38800 36.96900 13.42900  0.210 31.29000  ?  132 VAL A CG1 1 
ATOM   1865 C  CG2 A VAL A 1 132 ? 15.26400 34.93300 12.25500  0.790 25.92000  ?  132 VAL A CG2 1 
ATOM   1866 C  CG2 B VAL A 1 132 ? 15.26400 34.99200 12.25600  0.210 25.59000  ?  132 VAL A CG2 1 
ATOM   1867 N  N   A ALA A 1 133 ? 19.14500 37.27600 11.70000  0.790 25.93000  ?  133 ALA A N   1 
ATOM   1868 N  N   B ALA A 1 133 ? 18.97400 37.33500 11.68700  0.210 25.94000  ?  133 ALA A N   1 
ATOM   1869 C  CA  A ALA A 1 133 ? 20.12800 38.33900 11.87800  0.790 29.22000  ?  133 ALA A CA  1 
ATOM   1870 C  CA  B ALA A 1 133 ? 20.00200 38.36500 11.76500  0.210 28.96000  ?  133 ALA A CA  1 
ATOM   1871 C  C   A ALA A 1 133 ? 20.50700 38.98000 10.55100  0.790 32.86000  ?  133 ALA A C   1 
ATOM   1872 C  C   B ALA A 1 133 ? 20.34400 38.92700 10.38000  0.210 32.53000  ?  133 ALA A C   1 
ATOM   1873 O  O   A ALA A 1 133 ? 20.81000 40.17700 10.50800  0.790 32.59000  ?  133 ALA A O   1 
ATOM   1874 O  O   B ALA A 1 133 ? 20.71700 40.10000 10.24500  0.210 31.06000  ?  133 ALA A O   1 
ATOM   1875 C  CB  A ALA A 1 133 ? 21.37500 37.79300 12.57400  0.790 29.25000  ?  133 ALA A CB  1 
ATOM   1876 C  CB  B ALA A 1 133 ? 21.24300 37.76700 12.44200  0.210 28.96000  ?  133 ALA A CB  1 
ATOM   1877 N  N   A PHE A 1 134 ? 20.50200 38.20300 9.46700   0.790 35.91000  ?  134 PHE A N   1 
ATOM   1878 N  N   B PHE A 1 134 ? 20.20400 38.10300 9.32700   0.210 34.51000  ?  134 PHE A N   1 
ATOM   1879 C  CA  A PHE A 1 134 ? 20.79900 38.76300 8.15500   0.790 35.07000  ?  134 PHE A CA  1 
ATOM   1880 C  CA  B PHE A 1 134 ? 20.48600 38.58700 7.97200   0.210 34.79000  ?  134 PHE A CA  1 
ATOM   1881 C  C   A PHE A 1 134 ? 19.75000 39.79100 7.75100   0.790 31.35000  ?  134 PHE A C   1 
ATOM   1882 C  C   B PHE A 1 134 ? 19.50600 39.63900 7.53400   0.210 31.25000  ?  134 PHE A C   1 
ATOM   1883 O  O   A PHE A 1 134 ? 20.08500 40.84500 7.19600   0.790 31.39000  ?  134 PHE A O   1 
ATOM   1884 O  O   B PHE A 1 134 ? 19.90800 40.65200 6.95100   0.210 29.66000  ?  134 PHE A O   1 
ATOM   1885 C  CB  A PHE A 1 134 ? 20.88500 37.63800 7.12400   0.790 27.92000  ?  134 PHE A CB  1 
ATOM   1886 C  CB  B PHE A 1 134 ? 20.47300 37.48500 6.91800   0.210 26.46000  ?  134 PHE A CB  1 
ATOM   1887 C  CG  A PHE A 1 134 ? 21.23500 38.10600 5.74600   0.790 26.91000  ?  134 PHE A CG  1 
ATOM   1888 C  CG  B PHE A 1 134 ? 20.88000 38.00800 5.60300   0.210 27.63000  ?  134 PHE A CG  1 
ATOM   1889 C  CD1 A PHE A 1 134 ? 22.49400 38.60900 5.47100   0.790 26.63000  ?  134 PHE A CD1 1 
ATOM   1890 C  CD1 B PHE A 1 134 ? 22.05300 38.72900 5.52200   0.210 29.94000  ?  134 PHE A CD1 1 
ATOM   1891 C  CD2 A PHE A 1 134 ? 20.30100 38.04900 4.72400   0.790 35.80000  ?  134 PHE A CD2 1 
ATOM   1892 C  CD2 B PHE A 1 134 ? 20.16500 37.78900 4.44900   0.210 36.48000  ?  134 PHE A CD2 1 
ATOM   1893 C  CE1 A PHE A 1 134 ? 22.81600 39.04300 4.19500   0.790 37.92000  ?  134 PHE A CE1 1 
ATOM   1894 C  CE1 B PHE A 1 134 ? 22.48900 39.28400 4.34900   0.210 35.51000  ?  134 PHE A CE1 1 
ATOM   1895 C  CE2 A PHE A 1 134 ? 20.61900 38.48100 3.45300   0.790 40.81000  ?  134 PHE A CE2 1 
ATOM   1896 C  CE2 B PHE A 1 134 ? 20.61100 38.32700 3.20100   0.210 39.77000  ?  134 PHE A CE2 1 
ATOM   1897 C  CZ  A PHE A 1 134 ? 21.87800 38.97800 3.19100   0.790 34.32000  ?  134 PHE A CZ  1 
ATOM   1898 C  CZ  B PHE A 1 134 ? 21.77300 39.07700 3.15400   0.210 34.10000  ?  134 PHE A CZ  1 
ATOM   1899 N  N   A LEU A 1 135 ? 18.47400 39.51000 8.02400   0.790 32.23000  ?  135 LEU A N   1 
ATOM   1900 N  N   B LEU A 1 135 ? 18.21700 39.39700 7.77700   0.210 33.00000  ?  135 LEU A N   1 
ATOM   1901 C  CA  A LEU A 1 135 ? 17.43400 40.48100 7.70300   0.790 34.31000  ?  135 LEU A CA  1 
ATOM   1902 C  CA  B LEU A 1 135 ? 17.23200 40.44400 7.56300   0.210 34.03000  ?  135 LEU A CA  1 
ATOM   1903 C  C   A LEU A 1 135 ? 17.66300 41.78900 8.45000   0.790 36.17000  ?  135 LEU A C   1 
ATOM   1904 C  C   B LEU A 1 135 ? 17.58700 41.69100 8.34100   0.210 35.52000  ?  135 LEU A C   1 
ATOM   1905 O  O   A LEU A 1 135 ? 17.44800 42.87400 7.89800   0.790 39.18000  ?  135 LEU A O   1 
ATOM   1906 O  O   B LEU A 1 135 ? 17.49900 42.81700 7.83700   0.210 38.28000  ?  135 LEU A O   1 
ATOM   1907 C  CB  A LEU A 1 135 ? 16.05700 39.90700 8.02700   0.790 29.19000  ?  135 LEU A CB  1 
ATOM   1908 C  CB  B LEU A 1 135 ? 15.86600 39.97200 7.99700   0.210 29.16000  ?  135 LEU A CB  1 
ATOM   1909 C  CG  A LEU A 1 135 ? 15.62300 38.76600 7.10700   0.790 31.95000  ?  135 LEU A CG  1 
ATOM   1910 C  CG  B LEU A 1 135 ? 15.19000 38.89900 7.13100   0.210 31.82000  ?  135 LEU A CG  1 
ATOM   1911 C  CD1 A LEU A 1 135 ? 14.36800 38.09500 7.63500   0.790 31.46000  ?  135 LEU A CD1 1 
ATOM   1912 C  CD1 B LEU A 1 135 ? 13.86300 38.72700 7.77200   0.210 31.46000  ?  135 LEU A CD1 1 
ATOM   1913 C  CD2 A LEU A 1 135 ? 15.40800 39.26500 5.68300   0.790 34.17000  ?  135 LEU A CD2 1 
ATOM   1914 C  CD2 B LEU A 1 135 ? 15.09500 39.38000 5.66800   0.210 33.89000  ?  135 LEU A CD2 1 
ATOM   1915 N  N   A GLY A 1 136 ? 18.10200 41.70700 9.70700   0.790 36.41000  ?  136 GLY A N   1 
ATOM   1916 N  N   B GLY A 1 136 ? 17.95800 41.50600 9.58700   0.210 36.51000  ?  136 GLY A N   1 
ATOM   1917 C  CA  A GLY A 1 136 ? 18.43000 42.91900 10.44000  0.790 33.16000  ?  136 GLY A CA  1 
ATOM   1918 C  CA  B GLY A 1 136 ? 18.28100 42.64300 10.38300  0.210 33.12000  ?  136 GLY A CA  1 
ATOM   1919 C  C   A GLY A 1 136 ? 19.60500 43.65800 9.83100   0.790 31.99000  ?  136 GLY A C   1 
ATOM   1920 C  C   B GLY A 1 136 ? 19.35900 43.43900 9.69500   0.210 31.53000  ?  136 GLY A C   1 
ATOM   1921 O  O   A GLY A 1 136 ? 19.62300 44.89100 9.79200   0.790 27.97000  ?  136 GLY A O   1 
ATOM   1922 O  O   B GLY A 1 136 ? 19.17700 44.62600 9.39200   0.210 30.37000  ?  136 GLY A O   1 
ATOM   1923 N  N   A LEU A 1 137 ? 20.60200 42.91600 9.34700   0.790 30.38000  ?  137 LEU A N   1 
ATOM   1924 N  N   B LEU A 1 137 ? 20.51200 42.79700 9.50400   0.210 30.79000  ?  137 LEU A N   1 
ATOM   1925 C  CA  A LEU A 1 137 ? 21.73600 43.54700 8.68200   0.790 29.01000  ?  137 LEU A CA  1 
ATOM   1926 C  CA  B LEU A 1 137 ? 21.58800 43.40600 8.73200   0.210 29.91000  ?  137 LEU A CA  1 
ATOM   1927 C  C   A LEU A 1 137 ? 21.29700 44.26300 7.41300   0.790 39.94000  ?  137 LEU A C   1 
ATOM   1928 C  C   B LEU A 1 137 ? 21.06300 44.04700 7.43900   0.210 38.30000  ?  137 LEU A C   1 
ATOM   1929 O  O   A LEU A 1 137 ? 21.74000 45.38500 7.13900   0.790 36.63000  ?  137 LEU A O   1 
ATOM   1930 O  O   B LEU A 1 137 ? 21.43400 45.17600 7.09900   0.210 34.95000  ?  137 LEU A O   1 
ATOM   1931 C  CB  A LEU A 1 137 ? 22.79800 42.49800 8.36500   0.790 33.83000  ?  137 LEU A CB  1 
ATOM   1932 C  CB  B LEU A 1 137 ? 22.63000 42.35800 8.42100   0.210 33.84000  ?  137 LEU A CB  1 
ATOM   1933 C  CG  A LEU A 1 137 ? 24.06100 42.99000 7.66300   0.790 42.72000  ?  137 LEU A CG  1 
ATOM   1934 C  CG  B LEU A 1 137 ? 23.70200 42.84200 7.47600   0.210 39.55000  ?  137 LEU A CG  1 
ATOM   1935 C  CD1 A LEU A 1 137 ? 24.82700 43.94500 8.56200   0.790 40.70000  ?  137 LEU A CD1 1 
ATOM   1936 C  CD1 B LEU A 1 137 ? 24.44800 43.94600 8.20700   0.210 40.42000  ?  137 LEU A CD1 1 
ATOM   1937 C  CD2 A LEU A 1 137 ? 24.93700 41.81800 7.25700   0.790 35.57000  ?  137 LEU A CD2 1 
ATOM   1938 C  CD2 B LEU A 1 137 ? 24.57500 41.63500 7.20100   0.210 34.00000  ?  137 LEU A CD2 1 
ATOM   1939 N  N   A VAL A 1 138 ? 20.42800 43.62800 6.62300   0.790 36.09000  ?  138 VAL A N   1 
ATOM   1940 N  N   B VAL A 1 138 ? 20.19300 43.33800 6.70500   0.210 34.57000  ?  138 VAL A N   1 
ATOM   1941 C  CA  A VAL A 1 138 ? 19.94100 44.25700 5.39800   0.790 34.23000  ?  138 VAL A CA  1 
ATOM   1942 C  CA  B VAL A 1 138 ? 19.57000 43.88500 5.49800   0.210 35.16000  ?  138 VAL A CA  1 
ATOM   1943 C  C   A VAL A 1 138 ? 19.19500 45.54000 5.72500   0.790 36.20000  ?  138 VAL A C   1 
ATOM   1944 C  C   B VAL A 1 138 ? 18.95200 45.23500 5.81300   0.210 35.81000  ?  138 VAL A C   1 
ATOM   1945 O  O   A VAL A 1 138 ? 19.30900 46.54400 5.00900   0.790 40.40000  ?  138 VAL A O   1 
ATOM   1946 O  O   B VAL A 1 138 ? 19.34200 46.24800 5.22200   0.210 38.97000  ?  138 VAL A O   1 
ATOM   1947 C  CB  A VAL A 1 138 ? 19.05200 43.27700 4.60800   0.790 32.34000  ?  138 VAL A CB  1 
ATOM   1948 C  CB  B VAL A 1 138 ? 18.52400 42.91800 4.92100   0.210 35.44000  ?  138 VAL A CB  1 
ATOM   1949 C  CG1 A VAL A 1 138 ? 18.30600 44.00400 3.49500   0.790 38.08000  ?  138 VAL A CG1 1 
ATOM   1950 C  CG1 B VAL A 1 138 ? 17.57300 43.64400 4.05300   0.210 33.79000  ?  138 VAL A CG1 1 
ATOM   1951 C  CG2 A VAL A 1 138 ? 19.88900 42.14000 4.05000   0.790 25.80000  ?  138 VAL A CG2 1 
ATOM   1952 C  CG2 B VAL A 1 138 ? 19.17800 41.82600 4.13800   0.210 30.95000  ?  138 VAL A CG2 1 
ATOM   1953 N  N   A TYR A 1 139 ? 18.40800 45.52900 6.80300   0.790 39.12000  ?  139 TYR A N   1 
ATOM   1954 N  N   B TYR A 1 139 ? 18.05200 45.27200 6.80100   0.210 36.20000  ?  139 TYR A N   1 
ATOM   1955 C  CA  A TYR A 1 139 ? 17.69300 46.73900 7.18700   0.790 43.00000  ?  139 TYR A CA  1 
ATOM   1956 C  CA  B TYR A 1 139 ? 17.45000 46.54500 7.21700   0.210 42.64000  ?  139 TYR A CA  1 
ATOM   1957 C  C   A TYR A 1 139 ? 18.66200 47.88500 7.44600   0.790 44.44000  ?  139 TYR A C   1 
ATOM   1958 C  C   B TYR A 1 139 ? 18.46600 47.64700 7.54400   0.210 43.79000  ?  139 TYR A C   1 
ATOM   1959 O  O   A TYR A 1 139 ? 18.41400 49.02300 7.03600   0.790 50.36000  ?  139 TYR A O   1 
ATOM   1960 O  O   B TYR A 1 139 ? 18.29000 48.81200 7.14800   0.210 49.28000  ?  139 TYR A O   1 
ATOM   1961 C  CB  A TYR A 1 139 ? 16.83200 46.49800 8.42700   0.790 46.31000  ?  139 TYR A CB  1 
ATOM   1962 C  CB  B TYR A 1 139 ? 16.56600 46.35400 8.43400   0.210 47.07000  ?  139 TYR A CB  1 
ATOM   1963 C  CG  A TYR A 1 139 ? 16.31500 47.79100 9.02900   0.790 56.72000  ?  139 TYR A CG  1 
ATOM   1964 C  CG  B TYR A 1 139 ? 16.21900 47.70300 9.00100   0.210 56.27000  ?  139 TYR A CG  1 
ATOM   1965 C  CD1 A TYR A 1 139 ? 15.16600 48.39700 8.53800   0.790 56.93000  ?  139 TYR A CD1 1 
ATOM   1966 C  CD1 B TYR A 1 139 ? 15.28900 48.50600 8.34700   0.210 56.75000  ?  139 TYR A CD1 1 
ATOM   1967 C  CD2 A TYR A 1 139 ? 16.98900 48.41700 10.07200  0.790 60.71000  ?  139 TYR A CD2 1 
ATOM   1968 C  CD2 B TYR A 1 139 ? 16.84100 48.20800 10.15000  0.210 60.23000  ?  139 TYR A CD2 1 
ATOM   1969 C  CE1 A TYR A 1 139 ? 14.69400 49.58400 9.07600   0.790 60.75000  ?  139 TYR A CE1 1 
ATOM   1970 C  CE1 B TYR A 1 139 ? 14.96300 49.75900 8.80700   0.210 59.77000  ?  139 TYR A CE1 1 
ATOM   1971 C  CE2 A TYR A 1 139 ? 16.52500 49.60600 10.61400  0.790 57.57000  ?  139 TYR A CE2 1 
ATOM   1972 C  CE2 B TYR A 1 139 ? 16.51400 49.48100 10.63000  0.210 57.40000  ?  139 TYR A CE2 1 
ATOM   1973 C  CZ  A TYR A 1 139 ? 15.37700 50.18300 10.11300  0.790 72.25000  ?  139 TYR A CZ  1 
ATOM   1974 C  CZ  B TYR A 1 139 ? 15.57100 50.24700 9.94800   0.210 70.10000  ?  139 TYR A CZ  1 
ATOM   1975 O  OH  A TYR A 1 139 ? 14.91000 51.36300 10.64800  0.790 84.50000  ?  139 TYR A OH  1 
ATOM   1976 O  OH  B TYR A 1 139 ? 15.20900 51.51100 10.37800  0.210 79.83000  ?  139 TYR A OH  1 
ATOM   1977 N  N   A TYR A 1 140 ? 19.77200 47.60900 8.13400   0.790 37.94000  ?  140 TYR A N   1 
ATOM   1978 N  N   B TYR A 1 140 ? 19.50000 47.33000 8.32100   0.210 38.97000  ?  140 TYR A N   1 
ATOM   1979 C  CA  A TYR A 1 140 ? 20.70600 48.68200 8.45800   0.790 33.39000  ?  140 TYR A CA  1 
ATOM   1980 C  CA  B TYR A 1 140 ? 20.48500 48.36700 8.55200   0.210 37.69000  ?  140 TYR A CA  1 
ATOM   1981 C  C   A TYR A 1 140 ? 21.41100 49.19200 7.20900   0.790 44.62000  ?  140 TYR A C   1 
ATOM   1982 C  C   B TYR A 1 140 ? 21.11400 48.85000 7.26300   0.210 43.40000  ?  140 TYR A C   1 
ATOM   1983 O  O   A TYR A 1 140 ? 21.65600 50.39600 7.07800   0.790 47.22000  ?  140 TYR A O   1 
ATOM   1984 O  O   B TYR A 1 140 ? 21.49000 50.01700 7.16300   0.210 46.41000  ?  140 TYR A O   1 
ATOM   1985 C  CB  A TYR A 1 140 ? 21.70600 48.20400 9.50900   0.790 40.31000  ?  140 TYR A CB  1 
ATOM   1986 C  CB  B TYR A 1 140 ? 21.53300 47.88700 9.52500   0.210 40.47000  ?  140 TYR A CB  1 
ATOM   1987 C  CG  A TYR A 1 140 ? 21.18300 48.41400 10.91300  0.790 54.22000  ?  140 TYR A CG  1 
ATOM   1988 C  CG  B TYR A 1 140 ? 21.09400 48.29300 10.91400  0.210 53.63000  ?  140 TYR A CG  1 
ATOM   1989 C  CD1 A TYR A 1 140 ? 20.41800 47.44100 11.54100  0.790 63.00000  ?  140 TYR A CD1 1 
ATOM   1990 C  CD1 B TYR A 1 140 ? 20.17500 47.51900 11.60500  0.210 60.29000  ?  140 TYR A CD1 1 
ATOM   1991 C  CD2 A TYR A 1 140 ? 21.42400 49.60000 11.59500  0.790 49.72000  ?  140 TYR A CD2 1 
ATOM   1992 C  CD2 B TYR A 1 140 ? 21.52200 49.49000 11.50400  0.210 49.81000  ?  140 TYR A CD2 1 
ATOM   1993 C  CE1 A TYR A 1 140 ? 19.92400 47.63400 12.81800  0.790 67.20000  ?  140 TYR A CE1 1 
ATOM   1994 C  CE1 B TYR A 1 140 ? 19.71500 47.88100 12.86500  0.210 64.96000  ?  140 TYR A CE1 1 
ATOM   1995 C  CE2 A TYR A 1 140 ? 20.93400 49.80200 12.87300  0.790 61.10000  ?  140 TYR A CE2 1 
ATOM   1996 C  CE2 B TYR A 1 140 ? 21.05100 49.87200 12.77300  0.210 60.99000  ?  140 TYR A CE2 1 
ATOM   1997 C  CZ  A TYR A 1 140 ? 20.18400 48.81600 13.48000  0.790 60.59000  ?  140 TYR A CZ  1 
ATOM   1998 C  CZ  B TYR A 1 140 ? 20.14100 49.04600 13.45400  0.210 59.91000  ?  140 TYR A CZ  1 
ATOM   1999 O  OH  A TYR A 1 140 ? 19.69100 49.01000 14.75200  0.790 68.90000  ?  140 TYR A OH  1 
ATOM   2000 O  OH  B TYR A 1 140 ? 19.63600 49.37600 14.70500  0.210 67.55000  ?  140 TYR A OH  1 
ATOM   2001 N  N   A LEU A 1 141 ? 21.72100 48.30100 6.26800   0.790 43.82000  ?  141 LEU A N   1 
ATOM   2002 N  N   B LEU A 1 141 ? 21.20900 47.98100 6.26000   0.210 43.17000  ?  141 LEU A N   1 
ATOM   2003 C  CA  A LEU A 1 141 ? 22.34900 48.73700 5.02600   0.790 47.32000  ?  141 LEU A CA  1 
ATOM   2004 C  CA  B LEU A 1 141 ? 21.80900 48.36500 4.99200   0.210 46.00000  ?  141 LEU A CA  1 
ATOM   2005 C  C   A LEU A 1 141 ? 21.40700 49.61500 4.21400   0.790 47.61000  ?  141 LEU A C   1 
ATOM   2006 C  C   B LEU A 1 141 ? 20.86300 49.25300 4.19200   0.210 43.26000  ?  141 LEU A C   1 
ATOM   2007 O  O   A LEU A 1 141 ? 21.80100 50.67500 3.71300   0.790 44.46000  ?  141 LEU A O   1 
ATOM   2008 O  O   B LEU A 1 141 ? 21.25400 50.31200 3.68200   0.210 46.77000  ?  141 LEU A O   1 
ATOM   2009 C  CB  A LEU A 1 141 ? 22.77800 47.52100 4.20900   0.790 43.49000  ?  141 LEU A CB  1 
ATOM   2010 C  CB  B LEU A 1 141 ? 22.17900 47.11300 4.19900   0.210 40.22000  ?  141 LEU A CB  1 
ATOM   2011 C  CG  A LEU A 1 141 ? 24.00500 46.76700 4.71800   0.790 39.92000  ?  141 LEU A CG  1 
ATOM   2012 C  CG  B LEU A 1 141 ? 23.59300 46.62500 4.38200   0.210 39.10000  ?  141 LEU A CG  1 
ATOM   2013 C  CD1 A LEU A 1 141 ? 24.03600 45.37900 4.10500   0.790 34.92000  ?  141 LEU A CD1 1 
ATOM   2014 C  CD1 B LEU A 1 141 ? 23.67700 45.24400 3.83200   0.210 35.58000  ?  141 LEU A CD1 1 
ATOM   2015 C  CD2 A LEU A 1 141 ? 25.26200 47.54900 4.40400   0.790 53.59000  ?  141 LEU A CD2 1 
ATOM   2016 C  CD2 B LEU A 1 141 ? 24.50600 47.52800 3.62800   0.210 44.46000  ?  141 LEU A CD2 1 
ATOM   2017 N  N   A VAL A 1 142 ? 20.15200 49.18800 4.07400   0.790 38.51000  ?  142 VAL A N   1 
ATOM   2018 N  N   B VAL A 1 142 ? 19.61700 48.81500 4.05100   0.210 44.03000  ?  142 VAL A N   1 
ATOM   2019 C  CA  A VAL A 1 142 ? 19.20400 49.90100 3.22800   0.790 42.61000  ?  142 VAL A CA  1 
ATOM   2020 C  CA  B VAL A 1 142 ? 18.54800 49.67100 3.52300   0.210 44.72000  ?  142 VAL A CA  1 
ATOM   2021 C  C   A VAL A 1 142 ? 18.62000 51.12700 3.90900   0.790 51.40000  ?  142 VAL A C   1 
ATOM   2022 C  C   B VAL A 1 142 ? 18.48200 51.00600 4.26500   0.210 51.80000  ?  142 VAL A C   1 
ATOM   2023 O  O   A VAL A 1 142 ? 18.18500 52.05500 3.21600   0.790 52.61000  ?  142 VAL A O   1 
ATOM   2024 O  O   B VAL A 1 142 ? 18.84900 52.05800 3.72800   0.210 45.76000  ?  142 VAL A O   1 
ATOM   2025 C  CB  A VAL A 1 142 ? 18.08600 48.93600 2.79900   0.790 37.97000  ?  142 VAL A CB  1 
ATOM   2026 C  CB  B VAL A 1 142 ? 17.20300 48.93900 3.60400   0.210 31.39000  ?  142 VAL A CB  1 
ATOM   2027 C  CG1 A VAL A 1 142 ? 16.89500 49.68700 2.24500   0.790 50.41000  ?  142 VAL A CG1 1 
ATOM   2028 C  CG1 B VAL A 1 142 ? 16.06500 49.87300 3.54900   0.210 38.96000  ?  142 VAL A CG1 1 
ATOM   2029 C  CG2 A VAL A 1 142 ? 18.62300 47.93800 1.77700   0.790 37.18000  ?  142 VAL A CG2 1 
ATOM   2030 C  CG2 B VAL A 1 142 ? 17.12700 47.98800 2.47300   0.210 44.11000  ?  142 VAL A CG2 1 
ATOM   2031 N  N   A GLY A 1 143 ? 18.61500 51.16900 5.23800   0.790 50.96000  ?  143 GLY A N   1 
ATOM   2032 N  N   B GLY A 1 143 ? 18.02100 50.98500 5.52200   0.210 50.29000  ?  143 GLY A N   1 
ATOM   2033 C  CA  A GLY A 1 143 ? 17.99600 52.25300 5.95900   0.790 51.04000  ?  143 GLY A CA  1 
ATOM   2034 C  CA  B GLY A 1 143 ? 17.49100 52.19300 6.11400   0.210 48.12000  ?  143 GLY A CA  1 
ATOM   2035 C  C   A GLY A 1 143 ? 18.99200 53.17800 6.62400   0.790 55.13000  ?  143 GLY A C   1 
ATOM   2036 C  C   B GLY A 1 143 ? 18.57300 53.10300 6.64900   0.210 53.03000  ?  143 GLY A C   1 
ATOM   2037 O  O   A GLY A 1 143 ? 19.54400 54.09000 5.99900   0.790 48.61000  ?  143 GLY A O   1 
ATOM   2038 O  O   B GLY A 1 143 ? 19.17100 53.92800 5.94300   0.210 50.52000  ?  143 GLY A O   1 
ATOM   2039 N  N   A PRO A 1 144 ? 19.23100 52.96100 7.92200   0.790 42.88000  ?  144 PRO A N   1 
ATOM   2040 N  N   B PRO A 1 144 ? 18.84500 52.91800 7.92300   0.210 45.48000  ?  144 PRO A N   1 
ATOM   2041 C  CA  A PRO A 1 144 ? 20.10700 53.88500 8.66600   0.790 42.18000  ?  144 PRO A CA  1 
ATOM   2042 C  CA  B PRO A 1 144 ? 19.88900 53.65600 8.64100   0.210 43.63000  ?  144 PRO A CA  1 
ATOM   2043 C  C   A PRO A 1 144 ? 21.41200 54.22200 7.96000   0.790 47.71000  ?  144 PRO A C   1 
ATOM   2044 C  C   B PRO A 1 144 ? 21.09000 54.12000 7.84900   0.210 46.87000  ?  144 PRO A C   1 
ATOM   2045 O  O   A PRO A 1 144 ? 21.80500 55.39500 7.93500   0.790 54.23000  ?  144 PRO A O   1 
ATOM   2046 O  O   B PRO A 1 144 ? 21.34900 55.32200 7.79000   0.210 51.19000  ?  144 PRO A O   1 
ATOM   2047 C  CB  A PRO A 1 144 ? 20.35200 53.13900 9.98500   0.790 39.22000  ?  144 PRO A CB  1 
ATOM   2048 C  CB  B PRO A 1 144 ? 20.31000 52.64700 9.70000   0.210 41.24000  ?  144 PRO A CB  1 
ATOM   2049 C  CG  A PRO A 1 144 ? 19.11600 52.31200 10.18200  0.790 50.64000  ?  144 PRO A CG  1 
ATOM   2050 C  CG  B PRO A 1 144 ? 19.02700 51.96900 10.02700  0.210 52.35000  ?  144 PRO A CG  1 
ATOM   2051 C  CD  A PRO A 1 144 ? 18.61400 51.94500 8.80300   0.790 45.51000  ?  144 PRO A CD  1 
ATOM   2052 C  CD  B PRO A 1 144 ? 18.13600 51.97800 8.78700   0.210 43.87000  ?  144 PRO A CD  1 
ATOM   2053 N  N   A MET A 1 145 ? 22.10400 53.23300 7.39200   0.790 54.85000  ?  145 MET A N   1 
ATOM   2054 N  N   B MET A 1 145 ? 21.84700 53.19100 7.26900   0.210 53.25000  ?  145 MET A N   1 
ATOM   2055 C  CA  A MET A 1 145 ? 23.36700 53.52600 6.72300   0.790 50.89000  ?  145 MET A CA  1 
ATOM   2056 C  CA  B MET A 1 145 ? 23.07500 53.57300 6.58800   0.210 50.78000  ?  145 MET A CA  1 
ATOM   2057 C  C   A MET A 1 145 ? 23.15000 54.35400 5.46500   0.790 52.41000  ?  145 MET A C   1 
ATOM   2058 C  C   B MET A 1 145 ? 22.80400 54.33100 5.30000   0.210 51.59000  ?  145 MET A C   1 
ATOM   2059 O  O   A MET A 1 145 ? 24.00200 55.17800 5.11300   0.790 57.73000  ?  145 MET A O   1 
ATOM   2060 O  O   B MET A 1 145 ? 23.66000 55.11600 4.87600   0.210 54.72000  ?  145 MET A O   1 
ATOM   2061 C  CB  A MET A 1 145 ? 24.09800 52.22200 6.40500   0.790 41.05000  ?  145 MET A CB  1 
ATOM   2062 C  CB  B MET A 1 145 ? 23.92400 52.33500 6.31200   0.210 40.99000  ?  145 MET A CB  1 
ATOM   2063 C  CG  A MET A 1 145 ? 24.49200 51.45400 7.66000   0.790 48.08000  ?  145 MET A CG  1 
ATOM   2064 C  CG  B MET A 1 145 ? 24.06000 51.43100 7.43900   0.210 46.06000  ?  145 MET A CG  1 
ATOM   2065 S  SD  A MET A 1 145 ? 25.43000 49.94200 7.37200   0.790 50.70000  ?  145 MET A SD  1 
ATOM   2066 S  SD  B MET A 1 145 ? 25.07200 50.13300 6.81700   0.210 47.01000  ?  145 MET A SD  1 
ATOM   2067 C  CE  A MET A 1 145 ? 26.77800 50.56000 6.37300   0.790 35.59000  ?  145 MET A CE  1 
ATOM   2068 C  CE  B MET A 1 145 ? 26.54500 51.03500 6.35600   0.210 38.91000  ?  145 MET A CE  1 
ATOM   2069 N  N   A THR A 1 146 ? 22.01700 54.16700 4.78400   0.790 36.92000  ?  146 THR A N   1 
ATOM   2070 N  N   B THR A 1 146 ? 21.64800 54.11800 4.67000   0.210 41.17000  ?  146 THR A N   1 
ATOM   2071 C  CA  A THR A 1 146 ? 21.73500 54.97700 3.60400   0.790 49.59000  ?  146 THR A CA  1 
ATOM   2072 C  CA  B THR A 1 146 ? 21.32500 54.94200 3.51600   0.210 51.57000  ?  146 THR A CA  1 
ATOM   2073 C  C   A THR A 1 146 ? 21.37000 56.40500 3.99400   0.790 58.92000  ?  146 THR A C   1 
ATOM   2074 C  C   B THR A 1 146 ? 21.14800 56.37800 3.95800   0.210 58.93000  ?  146 THR A C   1 
ATOM   2075 O  O   A THR A 1 146 ? 21.80400 57.36200 3.34300   0.790 63.12000  ?  146 THR A O   1 
ATOM   2076 O  O   B THR A 1 146 ? 21.92300 57.26900 3.57600   0.210 62.33000  ?  146 THR A O   1 
ATOM   2077 C  CB  A THR A 1 146 ? 20.62000 54.33800 2.77800   0.790 54.40000  ?  146 THR A CB  1 
ATOM   2078 C  CB  B THR A 1 146 ? 20.03800 54.47900 2.85700   0.210 51.93000  ?  146 THR A CB  1 
ATOM   2079 O  OG1 A THR A 1 146 ? 21.03700 53.03300 2.35700   0.790 36.87000  ?  146 THR A OG1 1 
ATOM   2080 O  OG1 B THR A 1 146 ? 20.13200 53.08100 2.56000   0.210 46.74000  ?  146 THR A OG1 1 
ATOM   2081 C  CG2 A THR A 1 146 ? 20.30300 55.19200 1.55600   0.790 44.55000  ?  146 THR A CG2 1 
ATOM   2082 C  CG2 B THR A 1 146 ? 19.80700 55.24700 1.54100   0.210 44.94000  ?  146 THR A CG2 1 
ATOM   2083 N  N   A GLU A 1 147 ? 20.57500 56.57300 5.05500   0.790 49.92000  ?  147 GLU A N   1 
ATOM   2084 N  N   B GLU A 1 147 ? 20.07600 56.61600 4.72400   0.210 52.27000  ?  147 GLU A N   1 
ATOM   2085 C  CA  A GLU A 1 147 ? 20.33500 57.91300 5.58100   0.790 60.12000  ?  147 GLU A CA  1 
ATOM   2086 C  CA  B GLU A 1 147 ? 19.90500 57.84000 5.49900   0.210 60.16000  ?  147 GLU A CA  1 
ATOM   2087 C  C   A GLU A 1 147 ? 21.65800 58.60600 5.87700   0.790 50.57000  ?  147 GLU A C   1 
ATOM   2088 C  C   B GLU A 1 147 ? 21.27700 58.34400 5.92100   0.210 53.07000  ?  147 GLU A C   1 
ATOM   2089 O  O   A GLU A 1 147 ? 21.86500 59.77100 5.51200   0.790 48.84000  ?  147 GLU A O   1 
ATOM   2090 O  O   B GLU A 1 147 ? 21.71000 59.44400 5.55500   0.210 52.31000  ?  147 GLU A O   1 
ATOM   2091 C  CB  A GLU A 1 147 ? 19.45800 57.84800 6.83900   0.790 59.61000  ?  147 GLU A CB  1 
ATOM   2092 C  CB  B GLU A 1 147 ? 19.01100 57.54100 6.72000   0.210 61.95000  ?  147 GLU A CB  1 
ATOM   2093 C  CG  A GLU A 1 147 ? 18.07900 57.22000 6.63600   0.790 73.86000  ?  147 GLU A CG  1 
ATOM   2094 C  CG  B GLU A 1 147 ? 17.69100 56.76600 6.38000   0.210 71.40000  ?  147 GLU A CG  1 
ATOM   2095 C  CD  A GLU A 1 147 ? 16.99900 57.87700 7.48400   0.790 95.47000  ?  147 GLU A CD  1 
ATOM   2096 C  CD  B GLU A 1 147 ? 16.55500 56.88600 7.44000   0.210 86.38000  ?  147 GLU A CD  1 
ATOM   2097 O  OE1 A GLU A 1 147 ? 16.49500 58.94500 7.08000   0.790 101.47000 ?  147 GLU A OE1 1 
ATOM   2098 O  OE1 B GLU A 1 147 ? 15.81600 57.89800 7.45400   0.210 92.91000  ?  147 GLU A OE1 1 
ATOM   2099 O  OE2 A GLU A 1 147 ? 16.65500 57.32900 8.55300   0.790 91.90000  -1 147 GLU A OE2 1 
ATOM   2100 O  OE2 B GLU A 1 147 ? 16.39300 55.93200 8.24600   0.210 77.71000  -1 147 GLU A OE2 1 
ATOM   2101 N  N   A SER A 1 148 ? 22.57200 57.89400 6.54400   0.790 45.29000  ?  148 SER A N   1 
ATOM   2102 N  N   B SER A 1 148 ? 22.01200 57.47900 6.60700   0.210 51.66000  ?  148 SER A N   1 
ATOM   2103 C  CA  A SER A 1 148 ? 23.84000 58.49700 6.94200   0.790 45.52000  ?  148 SER A CA  1 
ATOM   2104 C  CA  B SER A 1 148 ? 23.29700 57.89300 7.10800   0.210 45.32000  ?  148 SER A CA  1 
ATOM   2105 C  C   A SER A 1 148 ? 24.68400 58.86200 5.72300   0.790 57.13000  ?  148 SER A C   1 
ATOM   2106 C  C   B SER A 1 148 ? 24.19200 58.34000 5.96400   0.210 55.28000  ?  148 SER A C   1 
ATOM   2107 O  O   A SER A 1 148 ? 25.23700 59.96600 5.64500   0.790 60.90000  ?  148 SER A O   1 
ATOM   2108 O  O   B SER A 1 148 ? 25.08500 59.16000 6.18600   0.210 57.09000  ?  148 SER A O   1 
ATOM   2109 C  CB  A SER A 1 148 ? 24.59800 57.54600 7.87100   0.790 48.35000  ?  148 SER A CB  1 
ATOM   2110 C  CB  B SER A 1 148 ? 23.88400 56.75700 7.93900   0.210 46.80000  ?  148 SER A CB  1 
ATOM   2111 O  OG  A SER A 1 148 ? 25.98200 57.84700 7.90800   0.790 63.67000  ?  148 SER A OG  1 
ATOM   2112 O  OG  B SER A 1 148 ? 25.20700 56.99500 8.34800   0.210 57.11000  ?  148 SER A OG  1 
ATOM   2113 N  N   A ALA A 1 149 ? 24.79400 57.94700 4.75700   0.790 58.20000  ?  149 ALA A N   1 
ATOM   2114 N  N   B ALA A 1 149 ? 23.90100 57.90600 4.72900   0.210 55.88000  ?  149 ALA A N   1 
ATOM   2115 C  CA  A ALA A 1 149 ? 25.55800 58.23700 3.54800   0.790 58.86000  ?  149 ALA A CA  1 
ATOM   2116 C  CA  B ALA A 1 149 ? 24.74200 58.19700 3.57200   0.210 57.79000  ?  149 ALA A CA  1 
ATOM   2117 C  C   A ALA A 1 149 ? 25.01600 59.44800 2.80100   0.790 63.72000  ?  149 ALA A C   1 
ATOM   2118 C  C   B ALA A 1 149 ? 24.16900 59.24900 2.63400   0.210 62.64000  ?  149 ALA A C   1 
ATOM   2119 O  O   A ALA A 1 149 ? 25.74400 60.05000 2.00300   0.790 60.19000  ?  149 ALA A O   1 
ATOM   2120 O  O   B ALA A 1 149 ? 24.94300 59.97800 2.00300   0.210 63.19000  ?  149 ALA A O   1 
ATOM   2121 C  CB  A ALA A 1 149 ? 25.55800 57.02300 2.61600   0.790 55.27000  ?  149 ALA A CB  1 
ATOM   2122 C  CB  B ALA A 1 149 ? 25.00300 56.93500 2.75500   0.210 54.59000  ?  149 ALA A CB  1 
ATOM   2123 N  N   A SER A 1 150 ? 23.75600 59.81600 3.03700   0.790 63.16000  ?  150 SER A N   1 
ATOM   2124 N  N   B SER A 1 150 ? 22.84700 59.36500 2.52200   0.210 60.17000  ?  150 SER A N   1 
ATOM   2125 C  CA  A SER A 1 150 ? 23.17200 60.94300 2.32100   0.790 60.17000  ?  150 SER A CA  1 
ATOM   2126 C  CA  B SER A 1 150 ? 22.25300 60.54900 1.91700   0.210 62.03000  ?  150 SER A CA  1 
ATOM   2127 C  C   A SER A 1 150 ? 23.86100 62.25400 2.67200   0.790 67.52000  ?  150 SER A C   1 
ATOM   2128 C  C   B SER A 1 150 ? 22.85800 61.84900 2.46700   0.210 64.16000  ?  150 SER A C   1 
ATOM   2129 O  O   A SER A 1 150 ? 23.88000 63.18000 1.85200   0.790 84.69000  ?  150 SER A O   1 
ATOM   2130 O  O   B SER A 1 150 ? 22.48500 62.93600 2.02000   0.210 71.25000  ?  150 SER A O   1 
ATOM   2131 C  CB  A SER A 1 150 ? 21.67700 61.03600 2.62600   0.790 62.74000  ?  150 SER A CB  1 
ATOM   2132 C  CB  B SER A 1 150 ? 20.73900 60.51200 2.12500   0.210 64.63000  ?  150 SER A CB  1 
ATOM   2133 O  OG  A SER A 1 150 ? 21.43800 61.91600 3.71100   0.790 59.15000  ?  150 SER A OG  1 
ATOM   2134 O  OG  B SER A 1 150 ? 20.37900 60.96500 3.42400   0.210 58.97000  ?  150 SER A OG  1 
ATOM   2135 N  N   A GLN A 1 151 ? 24.43200 62.35500 3.87300   0.790 69.66000  ?  151 GLN A N   1 
ATOM   2136 N  N   B GLN A 1 151 ? 23.81400 61.74900 3.41200   0.210 68.21000  ?  151 GLN A N   1 
ATOM   2137 C  CA  A GLN A 1 151 ? 25.08000 63.59000 4.29700   0.790 73.30000  ?  151 GLN A CA  1 
ATOM   2138 C  CA  B GLN A 1 151 ? 24.55000 62.89500 3.95700   0.210 69.30000  ?  151 GLN A CA  1 
ATOM   2139 C  C   A GLN A 1 151 ? 26.40200 63.84600 3.58200   0.790 64.88000  ?  151 GLN A C   1 
ATOM   2140 C  C   B GLN A 1 151 ? 25.77500 63.30300 3.13700   0.210 63.43000  ?  151 GLN A C   1 
ATOM   2141 O  O   A GLN A 1 151 ? 27.01200 64.89600 3.80200   0.790 68.86000  ?  151 GLN A O   1 
ATOM   2142 O  O   B GLN A 1 151 ? 26.08500 64.49100 3.08300   0.210 68.72000  ?  151 GLN A O   1 
ATOM   2143 C  CB  A GLN A 1 151 ? 25.32100 63.56700 5.80900   0.790 74.88000  ?  151 GLN A CB  1 
ATOM   2144 C  CB  B GLN A 1 151 ? 25.06500 62.61000 5.38700   0.210 75.41000  ?  151 GLN A CB  1 
ATOM   2145 C  CG  A GLN A 1 151 ? 24.12000 63.13900 6.64200   0.790 72.18000  ?  151 GLN A CG  1 
ATOM   2146 C  CG  B GLN A 1 151 ? 24.10800 62.06700 6.45400   0.210 73.99000  ?  151 GLN A CG  1 
ATOM   2147 C  CD  A GLN A 1 151 ? 22.90300 64.01100 6.40700   0.790 86.23000  ?  151 GLN A CD  1 
ATOM   2148 C  CD  B GLN A 1 151 ? 23.03800 63.02900 6.85800   0.210 80.30000  ?  151 GLN A CD  1 
ATOM   2149 O  OE1 A GLN A 1 151 ? 22.36500 64.05800 5.30100   0.790 84.12000  ?  151 GLN A OE1 1 
ATOM   2150 O  OE1 B GLN A 1 151 ? 22.20500 63.41600 6.04600   0.210 82.77000  ?  151 GLN A OE1 1 
ATOM   2151 N  NE2 A GLN A 1 151 ? 22.45800 64.70400 7.45000   0.790 100.29000 ?  151 GLN A NE2 1 
ATOM   2152 N  NE2 B GLN A 1 151 ? 23.02600 63.39800 8.14300   0.210 87.71000  ?  151 GLN A NE2 1 
ATOM   2153 N  N   A ARG A 1 152 ? 26.86600 62.93400 2.74100   0.790 57.98000  ?  152 ARG A N   1 
ATOM   2154 N  N   B ARG A 1 152 ? 26.53600 62.36600 2.57900   0.210 64.15000  ?  152 ARG A N   1 
ATOM   2155 C  CA  A ARG A 1 152 ? 28.15700 63.07500 2.08800   0.790 68.76000  ?  152 ARG A CA  1 
ATOM   2156 C  CA  B ARG A 1 152 ? 27.83900 62.73100 2.03100   0.210 69.11000  ?  152 ARG A CA  1 
ATOM   2157 C  C   A ARG A 1 152 ? 27.98000 63.64000 0.68200   0.790 71.76000  ?  152 ARG A C   1 
ATOM   2158 C  C   B ARG A 1 152 ? 27.67900 63.49800 0.69700   0.210 70.18000  ?  152 ARG A C   1 
ATOM   2159 O  O   A ARG A 1 152 ? 26.86500 63.82300 0.18900   0.790 60.07000  ?  152 ARG A O   1 
ATOM   2160 O  O   B ARG A 1 152 ? 26.58000 63.88900 0.28000   0.210 60.34000  ?  152 ARG A O   1 
ATOM   2161 C  CB  A ARG A 1 152 ? 28.88400 61.72600 2.04600   0.790 63.25000  ?  152 ARG A CB  1 
ATOM   2162 C  CB  B ARG A 1 152 ? 28.72000 61.48100 1.86500   0.210 64.38000  ?  152 ARG A CB  1 
ATOM   2163 C  CG  A ARG A 1 152 ? 28.89900 60.99300 3.38300   0.790 58.62000  ?  152 ARG A CG  1 
ATOM   2164 C  CG  B ARG A 1 152 ? 28.86600 60.56000 3.07400   0.210 60.29000  ?  152 ARG A CG  1 
ATOM   2165 C  CD  A ARG A 1 152 ? 30.18000 61.26600 4.16700   0.790 71.52000  ?  152 ARG A CD  1 
ATOM   2166 C  CD  B ARG A 1 152 ? 30.18200 60.71800 3.82700   0.210 68.40000  ?  152 ARG A CD  1 
ATOM   2167 N  NE  A ARG A 1 152 ? 31.22200 60.28700 3.86500   0.790 70.44000  ?  152 ARG A NE  1 
ATOM   2168 N  NE  B ARG A 1 152 ? 31.17100 59.70900 3.44800   0.210 73.28000  ?  152 ARG A NE  1 
ATOM   2169 C  CZ  A ARG A 1 152 ? 32.47900 60.37100 4.28700   0.790 86.70000  ?  152 ARG A CZ  1 
ATOM   2170 C  CZ  B ARG A 1 152 ? 32.43400 59.66900 3.87400   0.210 78.94000  ?  152 ARG A CZ  1 
ATOM   2171 N  NH1 A ARG A 1 152 ? 32.86500 61.39200 5.03900   0.790 102.59000 ?  152 ARG A NH1 1 
ATOM   2172 N  NH1 B ARG A 1 152 ? 32.90300 60.54900 4.74400   0.210 91.31000  ?  152 ARG A NH1 1 
ATOM   2173 N  NH2 A ARG A 1 152 ? 33.35300 59.43100 3.95500   0.790 80.94000  ?  152 ARG A NH2 1 
ATOM   2174 N  NH2 B ARG A 1 152 ? 33.25000 58.71900 3.41900   0.210 77.30000  ?  152 ARG A NH2 1 
ATOM   2175 N  N   A SER A 1 153 ? 29.11200 63.93100 0.04100   0.790 62.76000  ?  153 SER A N   1 
ATOM   2176 N  N   B SER A 1 153 ? 28.79900 63.73200 0.00900   0.210 65.36000  ?  153 SER A N   1 
ATOM   2177 C  CA  A SER A 1 153 ? 29.10800 64.46600 -1.31500  0.790 66.35000  ?  153 SER A CA  1 
ATOM   2178 C  CA  B SER A 1 153 ? 28.73200 64.25500 -1.35200  0.210 66.88000  ?  153 SER A CA  1 
ATOM   2179 C  C   A SER A 1 153 ? 28.27400 63.57200 -2.22300  0.790 66.08000  ?  153 SER A C   1 
ATOM   2180 C  C   B SER A 1 153 ? 27.83900 63.35800 -2.20400  0.210 68.73000  ?  153 SER A C   1 
ATOM   2181 O  O   A SER A 1 153 ? 28.02400 62.41000 -1.89700  0.790 75.18000  ?  153 SER A O   1 
ATOM   2182 O  O   B SER A 1 153 ? 27.56900 62.20700 -1.85200  0.210 72.03000  ?  153 SER A O   1 
ATOM   2183 C  CB  A SER A 1 153 ? 30.53300 64.58300 -1.85100  0.790 79.03000  ?  153 SER A CB  1 
ATOM   2184 C  CB  B SER A 1 153 ? 30.14500 64.40300 -1.94600  0.210 74.87000  ?  153 SER A CB  1 
ATOM   2185 O  OG  A SER A 1 153 ? 31.02300 63.31700 -2.25600  0.790 74.57000  ?  153 SER A OG  1 
ATOM   2186 O  OG  B SER A 1 153 ? 30.71300 63.16900 -2.33600  0.210 72.66000  ?  153 SER A OG  1 
ATOM   2187 N  N   A SER A 1 154 ? 27.83600 64.09700 -3.36600  0.790 70.27000  ?  154 SER A N   1 
ATOM   2188 N  N   B SER A 1 154 ? 27.30900 63.86900 -3.29900  0.210 69.93000  ?  154 SER A N   1 
ATOM   2189 C  CA  A SER A 1 154 ? 26.99000 63.30400 -4.24900  0.790 75.87000  ?  154 SER A CA  1 
ATOM   2190 C  CA  B SER A 1 154 ? 26.48600 62.98300 -4.11200  0.210 72.18000  ?  154 SER A CA  1 
ATOM   2191 C  C   A SER A 1 154 ? 27.75800 62.13000 -4.83900  0.790 72.61000  ?  154 SER A C   1 
ATOM   2192 C  C   B SER A 1 154 ? 27.33000 61.94100 -4.83700  0.210 69.92000  ?  154 SER A C   1 
ATOM   2193 O  O   A SER A 1 154 ? 27.15900 61.08300 -5.12600  0.790 62.91000  ?  154 SER A O   1 
ATOM   2194 O  O   B SER A 1 154 ? 26.81700 60.88200 -5.22200  0.210 62.49000  ?  154 SER A O   1 
ATOM   2195 C  CB  A SER A 1 154 ? 26.39900 64.19700 -5.34300  0.790 67.53000  ?  154 SER A CB  1 
ATOM   2196 C  CB  B SER A 1 154 ? 25.66500 63.77100 -5.11200  0.210 72.25000  ?  154 SER A CB  1 
ATOM   2197 O  OG  A SER A 1 154 ? 25.17900 63.65100 -5.82300  0.790 81.68000  ?  154 SER A OG  1 
ATOM   2198 O  OG  B SER A 1 154 ? 24.50100 63.02600 -5.38300  0.210 83.58000  ?  154 SER A OG  1 
ATOM   2199 N  N   A GLY A 1 155 ? 29.07100 62.27900 -5.03400  0.790 66.81000  ?  155 GLY A N   1 
ATOM   2200 N  N   B GLY A 1 155 ? 28.61600 62.22000 -5.04200  0.210 69.19000  ?  155 GLY A N   1 
ATOM   2201 C  CA  A GLY A 1 155 ? 29.84400 61.18100 -5.59100  0.790 62.87000  ?  155 GLY A CA  1 
ATOM   2202 C  CA  B GLY A 1 155 ? 29.48700 61.21900 -5.61100  0.210 64.82000  ?  155 GLY A CA  1 
ATOM   2203 C  C   A GLY A 1 155 ? 30.07000 60.05300 -4.59600  0.790 72.94000  ?  155 GLY A C   1 
ATOM   2204 C  C   B GLY A 1 155 ? 29.52000 60.04500 -4.66700  0.210 69.20000  ?  155 GLY A C   1 
ATOM   2205 O  O   A GLY A 1 155 ? 30.03200 58.87400 -4.95800  0.790 71.35000  ?  155 GLY A O   1 
ATOM   2206 O  O   B GLY A 1 155 ? 29.06400 58.93700 -5.00000  0.210 62.76000  ?  155 GLY A O   1 
ATOM   2207 N  N   A ILE A 1 156 ? 30.32400 60.39700 -3.33200  0.790 71.00000  ?  156 ILE A N   1 
ATOM   2208 N  N   B ILE A 1 156 ? 30.04900 60.32500 -3.46800  0.210 70.18000  ?  156 ILE A N   1 
ATOM   2209 C  CA  A ILE A 1 156 ? 30.46500 59.37500 -2.29700  0.790 63.42000  ?  156 ILE A CA  1 
ATOM   2210 C  CA  B ILE A 1 156 ? 30.13800 59.34200 -2.39300  0.210 64.43000  ?  156 ILE A CA  1 
ATOM   2211 C  C   A ILE A 1 156 ? 29.14500 58.64000 -2.09900  0.790 64.44000  ?  156 ILE A C   1 
ATOM   2212 C  C   B ILE A 1 156 ? 28.76700 58.77400 -2.03600  0.210 61.21000  ?  156 ILE A C   1 
ATOM   2213 O  O   A ILE A 1 156 ? 29.10600 57.40700 -2.02100  0.790 59.25000  ?  156 ILE A O   1 
ATOM   2214 O  O   B ILE A 1 156 ? 28.65500 57.60300 -1.65300  0.210 57.86000  ?  156 ILE A O   1 
ATOM   2215 C  CB  A ILE A 1 156 ? 30.95800 60.00900 -0.98400  0.790 61.32000  ?  156 ILE A CB  1 
ATOM   2216 C  CB  B ILE A 1 156 ? 30.84500 59.97800 -1.17700  0.210 61.87000  ?  156 ILE A CB  1 
ATOM   2217 C  CG1 A ILE A 1 156 ? 32.39200 60.52200 -1.14600  0.790 66.85000  ?  156 ILE A CG1 1 
ATOM   2218 C  CG1 B ILE A 1 156 ? 32.34300 60.20200 -1.48700  0.210 64.87000  ?  156 ILE A CG1 1 
ATOM   2219 C  CG2 A ILE A 1 156 ? 30.86100 59.01000 0.16300   0.790 54.73000  ?  156 ILE A CG2 1 
ATOM   2220 C  CG2 B ILE A 1 156 ? 30.66300 59.15300 0.09500   0.210 56.61000  ?  156 ILE A CG2 1 
ATOM   2221 C  CD1 A ILE A 1 156 ? 33.45900 59.50500 -0.79400  0.790 65.68000  ?  156 ILE A CD1 1 
ATOM   2222 C  CD1 B ILE A 1 156 ? 33.28700 59.07000 -1.04900  0.210 64.28000  ?  156 ILE A CD1 1 
ATOM   2223 N  N   A LYS A 1 157 ? 28.04400 59.38900 -2.01200  0.790 52.17000  ?  157 LYS A N   1 
ATOM   2224 N  N   B LYS A 1 157 ? 27.70500 59.55500 -2.16600  0.210 53.42000  ?  157 LYS A N   1 
ATOM   2225 C  CA  A LYS A 1 157 ? 26.73500 58.76100 -1.87400  0.790 52.91000  ?  157 LYS A CA  1 
ATOM   2226 C  CA  B LYS A 1 157 ? 26.43200 58.94900 -1.82000  0.210 55.63000  ?  157 LYS A CA  1 
ATOM   2227 C  C   A LYS A 1 157 ? 26.46800 57.80400 -3.02700  0.790 61.17000  ?  157 LYS A C   1 
ATOM   2228 C  C   B LYS A 1 157 ? 25.91700 58.05100 -2.93700  0.210 62.56000  ?  157 LYS A C   1 
ATOM   2229 O  O   A LYS A 1 157 ? 25.94500 56.70300 -2.82200  0.790 54.69000  ?  157 LYS A O   1 
ATOM   2230 O  O   B LYS A 1 157 ? 25.13700 57.12000 -2.67300  0.210 57.53000  ?  157 LYS A O   1 
ATOM   2231 C  CB  A LYS A 1 157 ? 25.65300 59.83700 -1.79700  0.790 49.78000  ?  157 LYS A CB  1 
ATOM   2232 C  CB  B LYS A 1 157 ? 25.39500 60.00600 -1.48700  0.210 55.11000  ?  157 LYS A CB  1 
ATOM   2233 C  CG  A LYS A 1 157 ? 24.23400 59.30200 -1.73800  0.790 56.87000  ?  157 LYS A CG  1 
ATOM   2234 C  CG  B LYS A 1 157 ? 24.15600 59.37500 -0.93600  0.210 62.65000  ?  157 LYS A CG  1 
ATOM   2235 C  CD  A LYS A 1 157 ? 23.30200 60.11600 -2.63200  0.790 73.07000  ?  157 LYS A CD  1 
ATOM   2236 C  CD  B LYS A 1 157 ? 22.98700 59.78100 -1.73800  0.210 70.15000  ?  157 LYS A CD  1 
ATOM   2237 C  CE  A LYS A 1 157 ? 23.07600 61.51800 -2.08200  0.790 86.00000  ?  157 LYS A CE  1 
ATOM   2238 C  CE  B LYS A 1 157 ? 22.90300 61.29200 -1.68800  0.210 82.89000  ?  157 LYS A CE  1 
ATOM   2239 N  NZ  A LYS A 1 157 ? 21.70800 62.02300 -2.39000  0.790 101.51000 ?  157 LYS A NZ  1 
ATOM   2240 N  NZ  B LYS A 1 157 ? 21.48100 61.70800 -1.78700  0.210 92.52000  ?  157 LYS A NZ  1 
ATOM   2241 N  N   A SER A 1 158 ? 26.83000 58.20400 -4.24900  0.790 68.27000  ?  158 SER A N   1 
ATOM   2242 N  N   B SER A 1 158 ? 26.33600 58.30900 -4.18400  0.210 66.06000  ?  158 SER A N   1 
ATOM   2243 C  CA  A SER A 1 158 ? 26.60100 57.35000 -5.41000  0.790 53.57000  ?  158 SER A CA  1 
ATOM   2244 C  CA  B SER A 1 158 ? 25.91000 57.46200 -5.28900  0.210 53.65000  ?  158 SER A CA  1 
ATOM   2245 C  C   A SER A 1 158 ? 27.42000 56.06800 -5.32200  0.790 54.15000  ?  158 SER A C   1 
ATOM   2246 C  C   B SER A 1 158 ? 26.67500 56.15200 -5.28200  0.210 53.94000  ?  158 SER A C   1 
ATOM   2247 O  O   A SER A 1 158 ? 26.92000 54.97800 -5.62500  0.790 43.71000  ?  158 SER A O   1 
ATOM   2248 O  O   B SER A 1 158 ? 26.06900 55.08300 -5.43500  0.210 44.93000  ?  158 SER A O   1 
ATOM   2249 C  CB  A SER A 1 158 ? 26.93900 58.11900 -6.68800  0.790 57.38000  ?  158 SER A CB  1 
ATOM   2250 C  CB  B SER A 1 158 ? 26.09400 58.17500 -6.62900  0.210 60.89000  ?  158 SER A CB  1 
ATOM   2251 O  OG  A SER A 1 158 ? 26.76800 57.31300 -7.84100  0.790 60.98000  ?  158 SER A OG  1 
ATOM   2252 O  OG  B SER A 1 158 ? 25.63000 57.33300 -7.68400  0.210 66.32000  ?  158 SER A OG  1 
ATOM   2253 N  N   A LEU A 1 159 ? 28.68500 56.17900 -4.91100  0.790 45.81000  ?  159 LEU A N   1 
ATOM   2254 N  N   B LEU A 1 159 ? 28.01400 56.22600 -5.13000  0.210 51.27000  ?  159 LEU A N   1 
ATOM   2255 C  CA  A LEU A 1 159 ? 29.51400 54.99200 -4.73900  0.790 43.98000  ?  159 LEU A CA  1 
ATOM   2256 C  CA  B LEU A 1 159 ? 28.79900 55.02800 -4.84900  0.210 49.48000  ?  159 LEU A CA  1 
ATOM   2257 C  C   A LEU A 1 159 ? 28.93900 54.07200 -3.67200  0.790 55.64000  ?  159 LEU A C   1 
ATOM   2258 C  C   B LEU A 1 159 ? 28.07800 54.18200 -3.77600  0.210 55.46000  ?  159 LEU A C   1 
ATOM   2259 O  O   A LEU A 1 159 ? 28.90400 52.84900 -3.85200  0.790 55.36000  ?  159 LEU A O   1 
ATOM   2260 O  O   B LEU A 1 159 ? 27.78400 53.00500 -4.01400  0.210 49.80000  ?  159 LEU A O   1 
ATOM   2261 C  CB  A LEU A 1 159 ? 30.94100 55.40200 -4.38000  0.790 50.21000  ?  159 LEU A CB  1 
ATOM   2262 C  CB  B LEU A 1 159 ? 30.25600 55.40300 -4.45000  0.210 49.22000  ?  159 LEU A CB  1 
ATOM   2263 C  CG  A LEU A 1 159 ? 31.96400 54.28300 -4.19400  0.790 56.80000  ?  159 LEU A CG  1 
ATOM   2264 C  CG  B LEU A 1 159 ? 31.49700 54.42800 -4.28800  0.210 56.10000  ?  159 LEU A CG  1 
ATOM   2265 C  CD1 A LEU A 1 159 ? 31.97600 53.37300 -5.41400  0.790 59.44000  ?  159 LEU A CD1 1 
ATOM   2266 C  CD1 B LEU A 1 159 ? 31.96000 53.69300 -5.58200  0.210 58.13000  ?  159 LEU A CD1 1 
ATOM   2267 C  CD2 A LEU A 1 159 ? 33.34700 54.86200 -3.93600  0.790 43.37000  ?  159 LEU A CD2 1 
ATOM   2268 C  CD2 B LEU A 1 159 ? 32.79600 54.95800 -3.51500  0.210 46.49000  ?  159 LEU A CD2 1 
ATOM   2269 N  N   A TYR A 1 160 ? 28.47900 54.63800 -2.55400  0.790 45.26000  ?  160 TYR A N   1 
ATOM   2270 N  N   B TYR A 1 160 ? 27.63500 54.80800 -2.65900  0.210 46.11000  ?  160 TYR A N   1 
ATOM   2271 C  CA  A TYR A 1 160 ? 27.90700 53.80400 -1.50300  0.790 51.00000  ?  160 TYR A CA  1 
ATOM   2272 C  CA  B TYR A 1 160 ? 27.04000 54.02400 -1.56600  0.210 52.42000  ?  160 TYR A CA  1 
ATOM   2273 C  C   A TYR A 1 160 ? 26.70400 53.02300 -2.02100  0.790 52.07000  ?  160 TYR A C   1 
ATOM   2274 C  C   B TYR A 1 160 ? 25.77100 53.29500 -1.99700  0.210 48.63000  ?  160 TYR A C   1 
ATOM   2275 O  O   A TYR A 1 160 ? 26.58100 51.81500 -1.78400  0.790 50.09000  ?  160 TYR A O   1 
ATOM   2276 O  O   B TYR A 1 160 ? 25.54400 52.15700 -1.58000  0.210 41.32000  ?  160 TYR A O   1 
ATOM   2277 C  CB  A TYR A 1 160 ? 27.49500 54.64900 -0.29800  0.790 42.52000  ?  160 TYR A CB  1 
ATOM   2278 C  CB  B TYR A 1 160 ? 26.70000 54.83900 -0.28700  0.210 45.52000  ?  160 TYR A CB  1 
ATOM   2279 C  CG  A TYR A 1 160 ? 26.69000 53.82800 0.68500   0.790 51.10000  ?  160 TYR A CG  1 
ATOM   2280 C  CG  B TYR A 1 160 ? 25.94600 53.90700 0.73300   0.210 47.58000  ?  160 TYR A CG  1 
ATOM   2281 C  CD1 A TYR A 1 160 ? 27.32300 52.97600 1.57800   0.790 39.92000  ?  160 TYR A CD1 1 
ATOM   2282 C  CD1 B TYR A 1 160 ? 26.65200 52.95200 1.47600   0.210 41.11000  ?  160 TYR A CD1 1 
ATOM   2283 C  CD2 A TYR A 1 160 ? 25.29900 53.86500 0.68900   0.790 44.84000  ?  160 TYR A CD2 1 
ATOM   2284 C  CD2 B TYR A 1 160 ? 24.53700 53.91500 0.88900   0.210 42.47000  ?  160 TYR A CD2 1 
ATOM   2285 C  CE1 A TYR A 1 160 ? 26.60500 52.20400 2.46200   0.790 42.78000  ?  160 TYR A CE1 1 
ATOM   2286 C  CE1 B TYR A 1 160 ? 26.01300 52.04900 2.33700   0.210 39.90000  ?  160 TYR A CE1 1 
ATOM   2287 C  CE2 A TYR A 1 160 ? 24.56800 53.08900 1.57600   0.790 42.29000  ?  160 TYR A CE2 1 
ATOM   2288 C  CE2 B TYR A 1 160 ? 23.88500 52.99500 1.79500   0.210 43.45000  ?  160 TYR A CE2 1 
ATOM   2289 C  CZ  A TYR A 1 160 ? 25.23200 52.26000 2.45900   0.790 41.00000  ?  160 TYR A CZ  1 
ATOM   2290 C  CZ  B TYR A 1 160 ? 24.66700 52.06900 2.51100   0.210 43.92000  ?  160 TYR A CZ  1 
ATOM   2291 O  OH  A TYR A 1 160 ? 24.53900 51.47900 3.35300   0.790 44.71000  ?  160 TYR A OH  1 
ATOM   2292 O  OH  B TYR A 1 160 ? 24.13700 51.15900 3.41800   0.210 44.29000  ?  160 TYR A OH  1 
ATOM   2293 N  N   A VAL A 1 161 ? 25.79800 53.70400 -2.72700  0.790 46.25000  ?  161 VAL A N   1 
ATOM   2294 N  N   B VAL A 1 161 ? 24.88300 53.93800 -2.74300  0.210 47.95000  ?  161 VAL A N   1 
ATOM   2295 C  CA  A VAL A 1 161 ? 24.58000 53.05200 -3.19900  0.790 56.84000  ?  161 VAL A CA  1 
ATOM   2296 C  CA  B VAL A 1 161 ? 23.77100 53.11900 -3.21400  0.210 55.43000  ?  161 VAL A CA  1 
ATOM   2297 C  C   A VAL A 1 161 ? 24.91800 51.90600 -4.14200  0.790 54.23000  ?  161 VAL A C   1 
ATOM   2298 C  C   B VAL A 1 161 ? 24.19700 52.18700 -4.36400  0.210 53.14000  ?  161 VAL A C   1 
ATOM   2299 O  O   A VAL A 1 161 ? 24.26500 50.85600 -4.12500  0.790 47.91000  ?  161 VAL A O   1 
ATOM   2300 O  O   B VAL A 1 161 ? 23.64100 51.08600 -4.48900  0.210 52.75000  ?  161 VAL A O   1 
ATOM   2301 C  CB  A VAL A 1 161 ? 23.65200 54.08300 -3.87000  0.790 58.61000  ?  161 VAL A CB  1 
ATOM   2302 C  CB  B VAL A 1 161 ? 22.53700 53.99400 -3.50800  0.210 51.53000  ?  161 VAL A CB  1 
ATOM   2303 C  CG1 A VAL A 1 161 ? 22.58900 53.38600 -4.70900  0.790 42.29000  ?  161 VAL A CG1 1 
ATOM   2304 C  CG1 B VAL A 1 161 ? 21.62100 53.34400 -4.54600  0.210 47.20000  ?  161 VAL A CG1 1 
ATOM   2305 C  CG2 A VAL A 1 161 ? 23.01100 54.98300 -2.82100  0.790 52.46000  ?  161 VAL A CG2 1 
ATOM   2306 C  CG2 B VAL A 1 161 ? 21.75200 54.20200 -2.20900  0.210 39.29000  ?  161 VAL A CG2 1 
ATOM   2307 N  N   A ARG A 1 162 ? 25.93600 52.08300 -4.98300  0.790 52.01000  ?  162 ARG A N   1 
ATOM   2308 N  N   B ARG A 1 162 ? 25.24000 52.51200 -5.13500  0.210 54.43000  ?  162 ARG A N   1 
ATOM   2309 C  CA  A ARG A 1 162 ? 26.26800 51.03300 -5.94000  0.790 55.98000  ?  162 ARG A CA  1 
ATOM   2310 C  CA  B ARG A 1 162 ? 25.74300 51.50000 -6.06400  0.210 56.63000  ?  162 ARG A CA  1 
ATOM   2311 C  C   A ARG A 1 162 ? 26.91700 49.83900 -5.24400  0.790 46.60000  ?  162 ARG A C   1 
ATOM   2312 C  C   B ARG A 1 162 ? 26.17100 50.24700 -5.29700  0.210 48.12000  ?  162 ARG A C   1 
ATOM   2313 O  O   A ARG A 1 162 ? 26.57800 48.68700 -5.53700  0.790 44.63000  ?  162 ARG A O   1 
ATOM   2314 O  O   B ARG A 1 162 ? 25.53600 49.19400 -5.40800  0.210 42.90000  ?  162 ARG A O   1 
ATOM   2315 C  CB  A ARG A 1 162 ? 27.15100 51.60900 -7.04800  0.790 66.50000  ?  162 ARG A CB  1 
ATOM   2316 C  CB  B ARG A 1 162 ? 26.87900 52.06600 -6.94500  0.210 66.36000  ?  162 ARG A CB  1 
ATOM   2317 C  CG  A ARG A 1 162 ? 26.37300 52.51800 -7.99900  0.790 68.79000  ?  162 ARG A CG  1 
ATOM   2318 C  CG  B ARG A 1 162 ? 26.42900 53.15100 -7.95700  0.210 69.37000  ?  162 ARG A CG  1 
ATOM   2319 C  CD  A ARG A 1 162 ? 26.81200 52.35500 -9.46200  0.790 95.17000  ?  162 ARG A CD  1 
ATOM   2320 C  CD  B ARG A 1 162 ? 26.79400 52.82700 -9.40500  0.210 91.72000  ?  162 ARG A CD  1 
ATOM   2321 N  NE  A ARG A 1 162 ? 26.31100 51.10900 -10.02300 0.790 103.10000 ?  162 ARG A NE  1 
ATOM   2322 N  NE  B ARG A 1 162 ? 26.00000 51.69500 -9.88700  0.210 99.01000  ?  162 ARG A NE  1 
ATOM   2323 C  CZ  A ARG A 1 162 ? 27.08200 50.17400 -10.56600 0.790 103.63000 ?  162 ARG A CZ  1 
ATOM   2324 C  CZ  B ARG A 1 162 ? 26.49200 50.60800 -10.47000 0.210 100.39000 ?  162 ARG A CZ  1 
ATOM   2325 N  NH1 A ARG A 1 162 ? 28.39100 50.34400 -10.64800 0.790 108.90000 ?  162 ARG A NH1 1 
ATOM   2326 N  NH1 B ARG A 1 162 ? 27.75100 50.54200 -10.84100 0.210 105.29000 ?  162 ARG A NH1 1 
ATOM   2327 N  NH2 A ARG A 1 162 ? 26.54500 49.06600 -11.03700 0.790 100.00000 ?  162 ARG A NH2 1 
ATOM   2328 N  NH2 B ARG A 1 162 ? 25.69500 49.56400 -10.69400 0.210 100.00000 ?  162 ARG A NH2 1 
ATOM   2329 N  N   A LEU A 1 163 ? 27.81200 50.08400 -4.28500  0.790 50.59000  ?  163 LEU A N   1 
ATOM   2330 N  N   B LEU A 1 163 ? 27.18600 50.37800 -4.43400  0.210 52.13000  ?  163 LEU A N   1 
ATOM   2331 C  CA  A LEU A 1 163 ? 28.38800 48.96800 -3.53800  0.790 46.09000  ?  163 LEU A CA  1 
ATOM   2332 C  CA  B LEU A 1 163 ? 27.69500 49.25100 -3.65500  0.210 46.70000  ?  163 LEU A CA  1 
ATOM   2333 C  C   A LEU A 1 163 ? 27.34600 48.31700 -2.63500  0.790 43.47000  ?  163 LEU A C   1 
ATOM   2334 C  C   B LEU A 1 163 ? 26.60900 48.56300 -2.80700  0.210 41.15000  ?  163 LEU A C   1 
ATOM   2335 O  O   A LEU A 1 163 ? 27.32400 47.08900 -2.48200  0.790 40.43000  ?  163 LEU A O   1 
ATOM   2336 O  O   B LEU A 1 163 ? 26.64800 47.34700 -2.60500  0.210 35.91000  ?  163 LEU A O   1 
ATOM   2337 C  CB  A LEU A 1 163 ? 29.58600 49.44600 -2.72300  0.790 44.11000  ?  163 LEU A CB  1 
ATOM   2338 C  CB  B LEU A 1 163 ? 28.86600 49.73400 -2.80200  0.210 39.21000  ?  163 LEU A CB  1 
ATOM   2339 C  CG  A LEU A 1 163 ? 30.81900 49.82400 -3.54500  0.790 37.37000  ?  163 LEU A CG  1 
ATOM   2340 C  CG  B LEU A 1 163 ? 30.15000 50.07200 -3.58600  0.210 39.39000  ?  163 LEU A CG  1 
ATOM   2341 C  CD1 A LEU A 1 163 ? 31.90000 50.42800 -2.66300  0.790 44.81000  ?  163 LEU A CD1 1 
ATOM   2342 C  CD1 B LEU A 1 163 ? 31.31000 50.42200 -2.64500  0.210 44.41000  ?  163 LEU A CD1 1 
ATOM   2343 C  CD2 A LEU A 1 163 ? 31.36000 48.62100 -4.30800  0.790 33.13000  ?  163 LEU A CD2 1 
ATOM   2344 C  CD2 B LEU A 1 163 ? 30.56000 48.93600 -4.48200  0.210 36.34000  ?  163 LEU A CD2 1 
ATOM   2345 N  N   A ARG A 1 164 ? 26.46800 49.12400 -2.03600  0.790 41.93000  ?  164 ARG A N   1 
ATOM   2346 N  N   B ARG A 1 164 ? 25.60600 49.30000 -2.36200  0.210 44.90000  ?  164 ARG A N   1 
ATOM   2347 C  CA  A ARG A 1 164 ? 25.41400 48.57500 -1.19100  0.790 38.91000  ?  164 ARG A CA  1 
ATOM   2348 C  CA  B ARG A 1 164 ? 24.58300 48.74800 -1.47500  0.210 41.91000  ?  164 ARG A CA  1 
ATOM   2349 C  C   A ARG A 1 164 ? 24.52200 47.61400 -1.97100  0.790 36.25000  ?  164 ARG A C   1 
ATOM   2350 C  C   B ARG A 1 164 ? 23.58600 47.86100 -2.23800  0.210 39.28000  ?  164 ARG A C   1 
ATOM   2351 O  O   A ARG A 1 164 ? 24.20900 46.52200 -1.49500  0.790 33.29000  ?  164 ARG A O   1 
ATOM   2352 O  O   B ARG A 1 164 ? 23.14600 46.81300 -1.72900  0.210 29.54000  ?  164 ARG A O   1 
ATOM   2353 C  CB  A ARG A 1 164 ? 24.58500 49.70900 -0.58700  0.790 29.78000  ?  164 ARG A CB  1 
ATOM   2354 C  CB  B ARG A 1 164 ? 23.89600 49.92400 -0.73700  0.210 39.79000  ?  164 ARG A CB  1 
ATOM   2355 C  CG  A ARG A 1 164 ? 23.36700 49.26000 0.21000   0.790 41.73000  ?  164 ARG A CG  1 
ATOM   2356 C  CG  B ARG A 1 164 ? 22.91300 49.56400 0.35900   0.210 41.03000  ?  164 ARG A CG  1 
ATOM   2357 C  CD  A ARG A 1 164 ? 22.30200 50.35500 0.21400   0.790 35.75000  ?  164 ARG A CD  1 
ATOM   2358 C  CD  B ARG A 1 164 ? 21.76100 50.53700 0.53100   0.210 41.47000  ?  164 ARG A CD  1 
ATOM   2359 N  NE  A ARG A 1 164 ? 21.58700 50.41500 -1.05800  0.790 63.16000  ?  164 ARG A NE  1 
ATOM   2360 N  NE  B ARG A 1 164 ? 20.97300 50.55200 -0.70100  0.210 60.61000  ?  164 ARG A NE  1 
ATOM   2361 C  CZ  A ARG A 1 164 ? 20.59000 51.25300 -1.32100  0.790 69.82000  ?  164 ARG A CZ  1 
ATOM   2362 C  CZ  B ARG A 1 164 ? 19.76400 51.09400 -0.88000  0.210 60.04000  ?  164 ARG A CZ  1 
ATOM   2363 N  NH1 A ARG A 1 164 ? 20.18000 52.11200 -0.39800  0.790 58.28000  ?  164 ARG A NH1 1 
ATOM   2364 N  NH1 B ARG A 1 164 ? 19.06700 51.60900 0.12200   0.210 46.56000  ?  164 ARG A NH1 1 
ATOM   2365 N  NH2 A ARG A 1 164 ? 20.00000 51.23100 -2.50800  0.790 62.77000  ?  164 ARG A NH2 1 
ATOM   2366 N  NH2 B ARG A 1 164 ? 19.21900 51.08000 -2.10000  0.210 61.96000  ?  164 ARG A NH2 1 
ATOM   2367 N  N   A ASN A 1 165 ? 24.08500 48.00500 -3.16500  0.790 41.91000  ?  165 ASN A N   1 
ATOM   2368 N  N   B ASN A 1 165 ? 23.23400 48.23400 -3.46800  0.210 48.11000  ?  165 ASN A N   1 
ATOM   2369 C  CA  A ASN A 1 165 ? 23.17900 47.12800 -3.89800  0.790 42.82000  ?  165 ASN A CA  1 
ATOM   2370 C  CA  B ASN A 1 165 ? 22.37800 47.35500 -4.26000  0.210 46.97000  ?  165 ASN A CA  1 
ATOM   2371 C  C   A ASN A 1 165 ? 23.90600 45.88700 -4.38000  0.790 38.55000  ?  165 ASN A C   1 
ATOM   2372 C  C   B ASN A 1 165 ? 23.07600 46.04600 -4.55900  0.210 36.08000  ?  165 ASN A C   1 
ATOM   2373 O  O   A ASN A 1 165 ? 23.34000 44.78200 -4.31200  0.790 31.59000  ?  165 ASN A O   1 
ATOM   2374 O  O   B ASN A 1 165 ? 22.55900 44.97200 -4.24900  0.210 32.91000  ?  165 ASN A O   1 
ATOM   2375 C  CB  A ASN A 1 165 ? 22.47900 47.91400 -5.01000  0.790 53.27000  ?  165 ASN A CB  1 
ATOM   2376 C  CB  B ASN A 1 165 ? 21.96000 48.05500 -5.55400  0.210 52.15000  ?  165 ASN A CB  1 
ATOM   2377 C  CG  A ASN A 1 165 ? 21.53100 48.97900 -4.43500  0.790 54.74000  ?  165 ASN A CG  1 
ATOM   2378 C  CG  B ASN A 1 165 ? 20.69700 48.87900 -5.40300  0.210 55.09000  ?  165 ASN A CG  1 
ATOM   2379 O  OD1 A ASN A 1 165 ? 20.98000 48.83800 -3.33500  0.790 62.48000  ?  165 ASN A OD1 1 
ATOM   2380 O  OD1 B ASN A 1 165 ? 19.70600 48.43200 -4.79900  0.210 50.42000  ?  165 ASN A OD1 1 
ATOM   2381 N  ND2 A ASN A 1 165 ? 21.36600 50.05600 -5.17300  0.790 54.82000  ?  165 ASN A ND2 1 
ATOM   2382 N  ND2 B ASN A 1 165 ? 20.71100 50.07600 -5.97300  0.210 58.27000  ?  165 ASN A ND2 1 
ATOM   2383 N  N   A LEU A 1 166 ? 25.14300 46.03700 -4.87500  0.790 36.08000  ?  166 LEU A N   1 
ATOM   2384 N  N   B LEU A 1 166 ? 24.27900 46.12700 -5.12000  0.210 34.34000  ?  166 LEU A N   1 
ATOM   2385 C  CA  A LEU A 1 166 ? 25.93100 44.84700 -5.17000  0.790 41.15000  ?  166 LEU A CA  1 
ATOM   2386 C  CA  B LEU A 1 166 ? 25.06000 44.92100 -5.38300  0.210 38.36000  ?  166 LEU A CA  1 
ATOM   2387 C  C   A LEU A 1 166 ? 25.95400 43.91200 -3.95900  0.790 41.18000  ?  166 LEU A C   1 
ATOM   2388 C  C   B LEU A 1 166 ? 25.10800 43.99700 -4.14400  0.210 37.54000  ?  166 LEU A C   1 
ATOM   2389 O  O   A LEU A 1 166 ? 25.75200 42.69700 -4.08100  0.790 32.78000  ?  166 LEU A O   1 
ATOM   2390 O  O   B LEU A 1 166 ? 24.57500 42.86500 -4.15900  0.210 32.79000  ?  166 LEU A O   1 
ATOM   2391 C  CB  A LEU A 1 166 ? 27.35700 45.21500 -5.57800  0.790 43.02000  ?  166 LEU A CB  1 
ATOM   2392 C  CB  B LEU A 1 166 ? 26.45600 45.34100 -5.87300  0.210 37.53000  ?  166 LEU A CB  1 
ATOM   2393 C  CG  A LEU A 1 166 ? 28.28000 44.04200 -5.93000  0.790 46.91000  ?  166 LEU A CG  1 
ATOM   2394 C  CG  B LEU A 1 166 ? 27.60600 44.39000 -6.11300  0.210 41.31000  ?  166 LEU A CG  1 
ATOM   2395 C  CD1 A LEU A 1 166 ? 27.99000 43.56200 -7.34700  0.790 39.10000  ?  166 LEU A CD1 1 
ATOM   2396 C  CD1 B LEU A 1 166 ? 27.57700 43.83000 -7.48500  0.210 40.67000  ?  166 LEU A CD1 1 
ATOM   2397 C  CD2 A LEU A 1 166 ? 29.74400 44.42500 -5.78700  0.790 47.03000  ?  166 LEU A CD2 1 
ATOM   2398 C  CD2 B LEU A 1 166 ? 28.96800 45.04900 -5.81600  0.210 37.68000  ?  166 LEU A CD2 1 
ATOM   2399 N  N   A THR A 1 167 ? 26.19100 44.47400 -2.77300  0.790 29.27000  ?  167 THR A N   1 
ATOM   2400 N  N   B THR A 1 167 ? 25.68900 44.50800 -3.03800  0.210 30.42000  ?  167 THR A N   1 
ATOM   2401 C  CA  A THR A 1 167 ? 26.33900 43.65700 -1.57200  0.790 30.25000  ?  167 THR A CA  1 
ATOM   2402 C  CA  B THR A 1 167 ? 25.89500 43.78800 -1.77500  0.210 31.98000  ?  167 THR A CA  1 
ATOM   2403 C  C   A THR A 1 167 ? 25.02500 42.98100 -1.19400  0.790 31.05000  ?  167 THR A C   1 
ATOM   2404 C  C   B THR A 1 167 ? 24.69100 42.95300 -1.39200  0.210 32.21000  ?  167 THR A C   1 
ATOM   2405 O  O   A THR A 1 167 ? 24.98100 41.76600 -0.96500  0.790 29.82000  ?  167 THR A O   1 
ATOM   2406 O  O   B THR A 1 167 ? 24.80300 41.73200 -1.25800  0.210 29.96000  ?  167 THR A O   1 
ATOM   2407 C  CB  A THR A 1 167 ? 26.85600 44.52600 -0.42200  0.790 31.07000  ?  167 THR A CB  1 
ATOM   2408 C  CB  B THR A 1 167 ? 26.25800 44.75200 -0.61600  0.210 29.95000  ?  167 THR A CB  1 
ATOM   2409 O  OG1 A THR A 1 167 ? 28.23000 44.86600 -0.65700  0.790 36.29000  ?  167 THR A OG1 1 
ATOM   2410 O  OG1 B THR A 1 167 ? 27.54300 45.35400 -0.86500  0.210 25.25000  ?  167 THR A OG1 1 
ATOM   2411 C  CG2 A THR A 1 167 ? 26.73400 43.79600 0.90600   0.790 31.47000  ?  167 THR A CG2 1 
ATOM   2412 C  CG2 B THR A 1 167 ? 26.26500 43.99000 0.67600   0.210 31.29000  ?  167 THR A CG2 1 
ATOM   2413 N  N   A VAL A 1 168 ? 23.93900 43.75500 -1.13000  0.790 31.23000  ?  168 VAL A N   1 
ATOM   2414 N  N   B VAL A 1 168 ? 23.53400 43.60500 -1.33200  0.210 31.17000  ?  168 VAL A N   1 
ATOM   2415 C  CA  A VAL A 1 168 ? 22.66700 43.21500 -0.65700  0.790 26.43000  ?  168 VAL A CA  1 
ATOM   2416 C  CA  B VAL A 1 168 ? 22.30100 42.98500 -0.87600  0.210 30.68000  ?  168 VAL A CA  1 
ATOM   2417 C  C   A VAL A 1 168 ? 22.16300 42.12200 -1.59000  0.790 34.79000  ?  168 VAL A C   1 
ATOM   2418 C  C   B VAL A 1 168 ? 21.75000 41.97800 -1.89000  0.210 34.83000  ?  168 VAL A C   1 
ATOM   2419 O  O   A VAL A 1 168 ? 21.71100 41.06300 -1.14000  0.790 36.99000  ?  168 VAL A O   1 
ATOM   2420 O  O   B VAL A 1 168 ? 21.12400 40.95300 -1.52900  0.210 30.72000  ?  168 VAL A O   1 
ATOM   2421 C  CB  A VAL A 1 168 ? 21.63400 44.34800 -0.50700  0.790 39.41000  ?  168 VAL A CB  1 
ATOM   2422 C  CB  B VAL A 1 168 ? 21.31900 44.15000 -0.60900  0.210 39.06000  ?  168 VAL A CB  1 
ATOM   2423 C  CG1 A VAL A 1 168 ? 20.22500 43.77700 -0.38800  0.790 29.50000  ?  168 VAL A CG1 1 
ATOM   2424 C  CG1 B VAL A 1 168 ? 19.89000 43.66800 -0.20000  0.210 29.50000  ?  168 VAL A CG1 1 
ATOM   2425 C  CG2 A VAL A 1 168 ? 21.96700 45.22800 0.69000   0.790 29.20000  ?  168 VAL A CG2 1 
ATOM   2426 C  CG2 B VAL A 1 168 ? 21.95800 45.14600 0.38900   0.210 31.53000  ?  168 VAL A CG2 1 
ATOM   2427 N  N   A ILE A 1 169 ? 22.23300 42.35500 -2.90100  0.790 33.01000  ?  169 ILE A N   1 
ATOM   2428 N  N   B ILE A 1 169 ? 21.92200 42.28300 -3.17500  0.210 34.35000  ?  169 ILE A N   1 
ATOM   2429 C  CA  A ILE A 1 169 ? 21.66600 41.40100 -3.84800  0.790 30.05000  ?  169 ILE A CA  1 
ATOM   2430 C  CA  B ILE A 1 169 ? 21.59700 41.32700 -4.21900  0.210 29.57000  ?  169 ILE A CA  1 
ATOM   2431 C  C   A ILE A 1 169 ? 22.45300 40.09600 -3.82500  0.790 32.33000  ?  169 ILE A C   1 
ATOM   2432 C  C   B ILE A 1 169 ? 22.39000 40.05000 -3.99900  0.210 31.23000  ?  169 ILE A C   1 
ATOM   2433 O  O   A ILE A 1 169 ? 21.87300 39.00600 -3.75500  0.790 32.57000  ?  169 ILE A O   1 
ATOM   2434 O  O   B ILE A 1 169 ? 21.82700 38.95400 -3.86100  0.210 31.91000  ?  169 ILE A O   1 
ATOM   2435 C  CB  A ILE A 1 169 ? 21.61200 42.01400 -5.25900  0.790 43.98000  ?  169 ILE A CB  1 
ATOM   2436 C  CB  B ILE A 1 169 ? 21.92800 41.95300 -5.57700  0.210 40.07000  ?  169 ILE A CB  1 
ATOM   2437 C  CG1 A ILE A 1 169 ? 20.54600 43.11300 -5.30200  0.790 38.11000  ?  169 ILE A CG1 1 
ATOM   2438 C  CG1 B ILE A 1 169 ? 20.96100 43.08300 -5.86200  0.210 41.76000  ?  169 ILE A CG1 1 
ATOM   2439 C  CG2 A ILE A 1 169 ? 21.32600 40.94700 -6.29500  0.790 35.06000  ?  169 ILE A CG2 1 
ATOM   2440 C  CG2 B ILE A 1 169 ? 21.92100 40.88700 -6.61500  0.210 35.59000  ?  169 ILE A CG2 1 
ATOM   2441 C  CD1 A ILE A 1 169 ? 20.67600 44.05600 -6.46700  0.790 55.33000  ?  169 ILE A CD1 1 
ATOM   2442 C  CD1 B ILE A 1 169 ? 21.51500 44.09000 -6.84000  0.210 49.97000  ?  169 ILE A CD1 1 
ATOM   2443 N  N   A LEU A 1 170 ? 23.78600 40.18600 -3.85300  0.790 29.17000  ?  170 LEU A N   1 
ATOM   2444 N  N   B LEU A 1 170 ? 23.71600 40.19900 -3.87900  0.210 27.17000  ?  170 LEU A N   1 
ATOM   2445 C  CA  A LEU A 1 170 ? 24.59400 38.97300 -3.92600  0.790 23.50000  ?  170 LEU A CA  1 
ATOM   2446 C  CA  B LEU A 1 170 ? 24.64400 39.06900 -3.77000  0.210 24.05000  ?  170 LEU A CA  1 
ATOM   2447 C  C   A LEU A 1 170 ? 24.65000 38.25300 -2.58300  0.790 29.38000  ?  170 LEU A C   1 
ATOM   2448 C  C   B LEU A 1 170 ? 24.54200 38.37100 -2.42600  0.210 29.22000  ?  170 LEU A C   1 
ATOM   2449 O  O   A LEU A 1 170 ? 24.59200 37.02000 -2.53800  0.790 32.73000  ?  170 LEU A O   1 
ATOM   2450 O  O   B LEU A 1 170 ? 24.32700 37.15100 -2.36700  0.210 31.45000  ?  170 LEU A O   1 
ATOM   2451 C  CB  A LEU A 1 170 ? 26.00300 39.30400 -4.41600  0.790 27.73000  ?  170 LEU A CB  1 
ATOM   2452 C  CB  B LEU A 1 170 ? 26.06400 39.58400 -4.00400  0.210 27.78000  ?  170 LEU A CB  1 
ATOM   2453 C  CG  A LEU A 1 170 ? 26.05300 39.83600 -5.84500  0.790 34.86000  ?  170 LEU A CG  1 
ATOM   2454 C  CG  B LEU A 1 170 ? 26.34900 39.83900 -5.48000  0.210 33.55000  ?  170 LEU A CG  1 
ATOM   2455 C  CD1 A LEU A 1 170 ? 27.48300 40.01200 -6.31800  0.790 27.98000  ?  170 LEU A CD1 1 
ATOM   2456 C  CD1 B LEU A 1 170 ? 27.67200 40.50500 -5.63100  0.210 37.66000  ?  170 LEU A CD1 1 
ATOM   2457 C  CD2 A LEU A 1 170 ? 25.29900 38.90800 -6.79300  0.790 28.10000  ?  170 LEU A CD2 1 
ATOM   2458 C  CD2 B LEU A 1 170 ? 26.38400 38.51800 -6.29500  0.210 27.63000  ?  170 LEU A CD2 1 
ATOM   2459 N  N   A TRP A 1 171 ? 24.78100 38.99100 -1.47800  0.790 31.07000  ?  171 TRP A N   1 
ATOM   2460 N  N   B TRP A 1 171 ? 24.65900 39.14200 -1.33300  0.210 29.81000  ?  171 TRP A N   1 
ATOM   2461 C  CA  A TRP A 1 171 ? 24.82300 38.32200 -0.18000  0.790 25.06000  ?  171 TRP A CA  1 
ATOM   2462 C  CA  B TRP A 1 171 ? 24.64800 38.57000 0.01300   0.210 28.22000  ?  171 TRP A CA  1 
ATOM   2463 C  C   A TRP A 1 171 ? 23.54600 37.52700 0.06700   0.790 27.28000  ?  171 TRP A C   1 
ATOM   2464 C  C   B TRP A 1 171 ? 23.47600 37.67400 0.17800   0.210 27.22000  ?  171 TRP A C   1 
ATOM   2465 O  O   A TRP A 1 171 ? 23.58400 36.47000 0.70900   0.790 27.58000  ?  171 TRP A O   1 
ATOM   2466 O  O   B TRP A 1 171 ? 23.58100 36.64500 0.84100   0.210 26.94000  ?  171 TRP A O   1 
ATOM   2467 C  CB  A TRP A 1 171 ? 25.03900 39.33600 0.94500   0.790 27.52000  ?  171 TRP A CB  1 
ATOM   2468 C  CB  B TRP A 1 171 ? 24.61900 39.66700 1.09500   0.210 24.68000  ?  171 TRP A CB  1 
ATOM   2469 C  CG  A TRP A 1 171 ? 26.44100 39.86000 1.04400   0.790 24.66000  ?  171 TRP A CG  1 
ATOM   2470 C  CG  B TRP A 1 171 ? 25.98500 40.22900 1.20700   0.210 26.36000  ?  171 TRP A CG  1 
ATOM   2471 C  CD1 A TRP A 1 171 ? 27.30800 40.08300 0.01300   0.790 22.70000  ?  171 TRP A CD1 1 
ATOM   2472 C  CD1 B TRP A 1 171 ? 26.84100 40.46600 0.19700   0.210 27.21000  ?  171 TRP A CD1 1 
ATOM   2473 C  CD2 A TRP A 1 171 ? 27.13700 40.23700 2.24000   0.790 39.45000  ?  171 TRP A CD2 1 
ATOM   2474 C  CD2 B TRP A 1 171 ? 26.70600 40.49900 2.39400   0.210 34.34000  ?  171 TRP A CD2 1 
ATOM   2475 N  NE1 A TRP A 1 171 ? 28.49700 40.57400 0.49100   0.790 25.59000  ?  171 TRP A NE1 1 
ATOM   2476 N  NE1 B TRP A 1 171 ? 28.03200 40.90300 0.66100   0.210 31.44000  ?  171 TRP A NE1 1 
ATOM   2477 C  CE2 A TRP A 1 171 ? 28.41900 40.67800 1.85400   0.790 31.45000  ?  171 TRP A CE2 1 
ATOM   2478 C  CE2 B TRP A 1 171 ? 27.97600 40.95600 2.01200   0.210 31.94000  ?  171 TRP A CE2 1 
ATOM   2479 C  CE3 A TRP A 1 171 ? 26.80300 40.24200 3.60000   0.790 28.35000  ?  171 TRP A CE3 1 
ATOM   2480 C  CE3 B TRP A 1 171 ? 26.41000 40.38400 3.74800   0.210 28.52000  ?  171 TRP A CE3 1 
ATOM   2481 C  CZ2 A TRP A 1 171 ? 29.36600 41.12100 2.77800   0.790 38.72000  ?  171 TRP A CZ2 1 
ATOM   2482 C  CZ2 B TRP A 1 171 ? 28.93700 41.32100 2.91100   0.210 36.20000  ?  171 TRP A CZ2 1 
ATOM   2483 C  CZ3 A TRP A 1 171 ? 27.74500 40.68200 4.51400   0.790 27.70000  ?  171 TRP A CZ3 1 
ATOM   2484 C  CZ3 B TRP A 1 171 ? 27.36200 40.72100 4.64000   0.210 27.67000  ?  171 TRP A CZ3 1 
ATOM   2485 C  CH2 A TRP A 1 171 ? 29.01000 41.11400 4.10000   0.790 40.27000  ?  171 TRP A CH2 1 
ATOM   2486 C  CH2 B TRP A 1 171 ? 28.61400 41.21000 4.22000   0.210 38.05000  ?  171 TRP A CH2 1 
ATOM   2487 N  N   A ALA A 1 172 ? 22.41100 38.01000 -0.44700  0.790 28.68000  ?  172 ALA A N   1 
ATOM   2488 N  N   B ALA A 1 172 ? 22.35000 38.04500 -0.44200  0.210 28.69000  ?  172 ALA A N   1 
ATOM   2489 C  CA  A ALA A 1 172 ? 21.13700 37.32700 -0.25400  0.790 25.13000  ?  172 ALA A CA  1 
ATOM   2490 C  CA  B ALA A 1 172 ? 21.09300 37.31300 -0.32700  0.210 24.90000  ?  172 ALA A CA  1 
ATOM   2491 C  C   A ALA A 1 172 ? 21.08200 35.98800 -0.97200  0.790 32.32000  ?  172 ALA A C   1 
ATOM   2492 C  C   B ALA A 1 172 ? 21.13900 35.98700 -1.03800  0.210 32.20000  ?  172 ALA A C   1 
ATOM   2493 O  O   A ALA A 1 172 ? 20.21100 35.16900 -0.66100  0.790 35.45000  ?  172 ALA A O   1 
ATOM   2494 O  O   B ALA A 1 172 ? 20.32000 35.11400 -0.71600  0.210 35.40000  ?  172 ALA A O   1 
ATOM   2495 C  CB  A ALA A 1 172 ? 19.98900 38.21600 -0.73600  0.790 30.60000  ?  172 ALA A CB  1 
ATOM   2496 C  CB  B ALA A 1 172 ? 19.93400 38.12600 -0.92100  0.210 30.09000  ?  172 ALA A CB  1 
ATOM   2497 N  N   A ILE A 1 173 ? 21.99000 35.74800 -1.91600  0.790 26.90000  ?  173 ILE A N   1 
ATOM   2498 N  N   B ILE A 1 173 ? 22.07400 35.82400 -1.99000  0.210 27.04000  ?  173 ILE A N   1 
ATOM   2499 C  CA  A ILE A 1 173 ? 21.99800 34.48700 -2.64500  0.790 26.99000  ?  173 ILE A CA  1 
ATOM   2500 C  CA  B ILE A 1 173 ? 22.14200 34.58700 -2.75000  0.210 27.54000  ?  173 ILE A CA  1 
ATOM   2501 C  C   A ILE A 1 173 ? 22.70500 33.39800 -1.85100  0.790 28.65000  ?  173 ILE A C   1 
ATOM   2502 C  C   B ILE A 1 173 ? 22.80200 33.48000 -1.94300  0.210 28.28000  ?  173 ILE A C   1 
ATOM   2503 O  O   A ILE A 1 173 ? 22.33900 32.22000 -1.94800  0.790 32.62000  ?  173 ILE A O   1 
ATOM   2504 O  O   B ILE A 1 173 ? 22.33700 32.33500 -1.94900  0.210 32.12000  ?  173 ILE A O   1 
ATOM   2505 C  CB  A ILE A 1 173 ? 22.65700 34.69000 -4.02000  0.790 33.48000  ?  173 ILE A CB  1 
ATOM   2506 C  CB  B ILE A 1 173 ? 22.83500 34.88800 -4.09100  0.210 32.77000  ?  173 ILE A CB  1 
ATOM   2507 C  CG1 A ILE A 1 173 ? 21.79900 35.61000 -4.89400  0.790 30.74000  ?  173 ILE A CG1 1 
ATOM   2508 C  CG1 B ILE A 1 173 ? 21.76400 35.42500 -5.03000  0.210 30.05000  ?  173 ILE A CG1 1 
ATOM   2509 C  CG2 A ILE A 1 173 ? 22.89000 33.35100 -4.70800  0.790 21.94000  ?  173 ILE A CG2 1 
ATOM   2510 C  CG2 B ILE A 1 173 ? 23.61900 33.73500 -4.63400  0.210 17.43000  ?  173 ILE A CG2 1 
ATOM   2511 C  CD1 A ILE A 1 173 ? 22.54600 36.22500 -6.05500  0.790 28.88000  ?  173 ILE A CD1 1 
ATOM   2512 C  CD1 B ILE A 1 173 ? 22.34300 36.24700 -6.05700  0.210 28.74000  ?  173 ILE A CD1 1 
ATOM   2513 N  N   A TYR A 1 174 ? 23.70800 33.76000 -1.05500  0.790 25.88000  ?  174 TYR A N   1 
ATOM   2514 N  N   B TYR A 1 174 ? 23.86100 33.79100 -1.23300  0.210 24.75000  ?  174 TYR A N   1 
ATOM   2515 C  CA  A TYR A 1 174 ? 24.47000 32.75600 -0.31500  0.790 28.46000  ?  174 TYR A CA  1 
ATOM   2516 C  CA  B TYR A 1 174 ? 24.46100 32.74600 -0.40300  0.210 30.28000  ?  174 TYR A CA  1 
ATOM   2517 C  C   A TYR A 1 174 ? 23.60000 31.82600 0.52000   0.790 26.59000  ?  174 TYR A C   1 
ATOM   2518 C  C   B TYR A 1 174 ? 23.45300 31.87500 0.35700   0.210 26.29000  ?  174 TYR A C   1 
ATOM   2519 O  O   A TYR A 1 174 ? 23.81700 30.60400 0.46400   0.790 38.28000  ?  174 TYR A O   1 
ATOM   2520 O  O   B TYR A 1 174 ? 23.46300 30.66700 0.12800   0.210 33.87000  ?  174 TYR A O   1 
ATOM   2521 C  CB  A TYR A 1 174 ? 25.48600 33.43700 0.61100   0.790 22.81000  ?  174 TYR A CB  1 
ATOM   2522 C  CB  B TYR A 1 174 ? 25.43800 33.36800 0.57600   0.210 23.13000  ?  174 TYR A CB  1 
ATOM   2523 C  CG  A TYR A 1 174 ? 26.76800 33.90500 -0.03400  0.790 27.78000  ?  174 TYR A CG  1 
ATOM   2524 C  CG  B TYR A 1 174 ? 26.70800 33.85900 -0.03300  0.210 28.24000  ?  174 TYR A CG  1 
ATOM   2525 C  CD1 A TYR A 1 174 ? 26.82700 35.12600 -0.68800  0.790 30.28000  ?  174 TYR A CD1 1 
ATOM   2526 C  CD1 B TYR A 1 174 ? 26.77600 35.07500 -0.71100  0.210 27.97000  ?  174 TYR A CD1 1 
ATOM   2527 C  CD2 A TYR A 1 174 ? 27.93000 33.14700 0.04800   0.790 26.06000  ?  174 TYR A CD2 1 
ATOM   2528 C  CD2 B TYR A 1 174 ? 27.85600 33.15200 0.12800   0.210 28.74000  ?  174 TYR A CD2 1 
ATOM   2529 C  CE1 A TYR A 1 174 ? 27.99700 35.57200 -1.26500  0.790 22.01000  ?  174 TYR A CE1 1 
ATOM   2530 C  CE1 B TYR A 1 174 ? 27.95700 35.51400 -1.23700  0.210 24.63000  ?  174 TYR A CE1 1 
ATOM   2531 C  CE2 A TYR A 1 174 ? 29.10900 33.58400 -0.52400  0.790 24.91000  ?  174 TYR A CE2 1 
ATOM   2532 C  CE2 B TYR A 1 174 ? 29.01800 33.59800 -0.34500  0.210 25.47000  ?  174 TYR A CE2 1 
ATOM   2533 C  CZ  A TYR A 1 174 ? 29.13500 34.80000 -1.17900  0.790 24.17000  ?  174 TYR A CZ  1 
ATOM   2534 C  CZ  B TYR A 1 174 ? 29.07200 34.79600 -1.05600  0.210 24.10000  ?  174 TYR A CZ  1 
ATOM   2535 O  OH  A TYR A 1 174 ? 30.29800 35.25500 -1.75700  0.790 24.72000  ?  174 TYR A OH  1 
ATOM   2536 O  OH  B TYR A 1 174 ? 30.29800 35.19000 -1.54600  0.210 23.80000  ?  174 TYR A OH  1 
ATOM   2537 N  N   A PRO A 1 175 ? 22.65700 32.31000 1.33800   0.790 29.36000  ?  175 PRO A N   1 
ATOM   2538 N  N   B PRO A 1 175 ? 22.57700 32.41700 1.30500   0.210 31.30000  ?  175 PRO A N   1 
ATOM   2539 C  CA  A PRO A 1 175 ? 21.86900 31.36000 2.14400   0.790 25.58000  ?  175 PRO A CA  1 
ATOM   2540 C  CA  B PRO A 1 175 ? 21.63500 31.53800 2.02900   0.210 29.28000  ?  175 PRO A CA  1 
ATOM   2541 C  C   A PRO A 1 175 ? 21.11800 30.35200 1.29500   0.790 32.69000  ?  175 PRO A C   1 
ATOM   2542 C  C   B PRO A 1 175 ? 21.01000 30.48900 1.13400   0.210 32.53000  ?  175 PRO A C   1 
ATOM   2543 O  O   A PRO A 1 175 ? 20.90700 29.21500 1.73400   0.790 29.55000  ?  175 PRO A O   1 
ATOM   2544 O  O   B PRO A 1 175 ? 20.96300 29.29800 1.47700   0.210 27.26000  ?  175 PRO A O   1 
ATOM   2545 C  CB  A PRO A 1 175 ? 20.91500 32.26000 2.94700   0.790 31.96000  ?  175 PRO A CB  1 
ATOM   2546 C  CB  B PRO A 1 175 ? 20.55900 32.51000 2.55000   0.210 31.06000  ?  175 PRO A CB  1 
ATOM   2547 C  CG  A PRO A 1 175 ? 20.96600 33.60300 2.29900   0.790 28.29000  ?  175 PRO A CG  1 
ATOM   2548 C  CG  B PRO A 1 175 ? 20.89400 33.85000 1.95200   0.210 27.38000  ?  175 PRO A CG  1 
ATOM   2549 C  CD  A PRO A 1 175 ? 22.30000 33.71600 1.61800   0.790 27.62000  ?  175 PRO A CD  1 
ATOM   2550 C  CD  B PRO A 1 175 ? 22.35000 33.82300 1.69100   0.210 27.60000  ?  175 PRO A CD  1 
ATOM   2551 N  N   A PHE A 1 176 ? 20.72600 30.72400 0.07700   0.790 34.77000  ?  176 PHE A N   1 
ATOM   2552 N  N   B PHE A 1 176 ? 20.61200 30.93200 -0.06600  0.210 34.44000  ?  176 PHE A N   1 
ATOM   2553 C  CA  A PHE A 1 176 ? 20.05800 29.76700 -0.79600  0.790 37.61000  ?  176 PHE A CA  1 
ATOM   2554 C  CA  B PHE A 1 176 ? 20.06400 30.01000 -1.04700  0.210 35.59000  ?  176 PHE A CA  1 
ATOM   2555 C  C   A PHE A 1 176 ? 21.03300 28.71800 -1.31500  0.790 40.34000  ?  176 PHE A C   1 
ATOM   2556 C  C   B PHE A 1 176 ? 21.05500 28.98100 -1.52300  0.210 38.45000  ?  176 PHE A C   1 
ATOM   2557 O  O   A PHE A 1 176 ? 20.70000 27.52800 -1.36200  0.790 37.88000  ?  176 PHE A O   1 
ATOM   2558 O  O   B PHE A 1 176 ? 20.71400 27.80100 -1.62400  0.210 36.25000  ?  176 PHE A O   1 
ATOM   2559 C  CB  A PHE A 1 176 ? 19.37700 30.50600 -1.94400  0.790 36.98000  ?  176 PHE A CB  1 
ATOM   2560 C  CB  B PHE A 1 176 ? 19.49600 30.76300 -2.20100  0.210 36.91000  ?  176 PHE A CB  1 
ATOM   2561 C  CG  A PHE A 1 176 ? 18.28300 31.42500 -1.49200  0.790 35.63000  ?  176 PHE A CG  1 
ATOM   2562 C  CG  B PHE A 1 176 ? 18.36900 31.56500 -1.79400  0.210 35.84000  ?  176 PHE A CG  1 
ATOM   2563 C  CD1 A PHE A 1 176 ? 17.00300 30.94400 -1.26900  0.790 43.11000  ?  176 PHE A CD1 1 
ATOM   2564 C  CD1 B PHE A 1 176 ? 17.32900 30.93500 -1.16100  0.210 41.05000  ?  176 PHE A CD1 1 
ATOM   2565 C  CD2 A PHE A 1 176 ? 18.53900 32.76500 -1.26600  0.790 38.85000  ?  176 PHE A CD2 1 
ATOM   2566 C  CD2 B PHE A 1 176 ? 18.29800 32.89700 -2.06700  0.210 43.57000  ?  176 PHE A CD2 1 
ATOM   2567 C  CE1 A PHE A 1 176 ? 15.99800 31.78700 -0.84300  0.790 40.40000  ?  176 PHE A CE1 1 
ATOM   2568 C  CE1 B PHE A 1 176 ? 16.22300 31.64400 -0.77300  0.210 41.53000  ?  176 PHE A CE1 1 
ATOM   2569 C  CE2 A PHE A 1 176 ? 17.53400 33.61300 -0.83700  0.790 40.84000  ?  176 PHE A CE2 1 
ATOM   2570 C  CE2 B PHE A 1 176 ? 17.19100 33.61600 -1.70400  0.210 35.75000  ?  176 PHE A CE2 1 
ATOM   2571 C  CZ  A PHE A 1 176 ? 16.26500 33.12400 -0.62600  0.790 40.05000  ?  176 PHE A CZ  1 
ATOM   2572 C  CZ  B PHE A 1 176 ? 16.15700 32.98800 -1.04400  0.210 40.65000  ?  176 PHE A CZ  1 
ATOM   2573 N  N   A ILE A 1 177 ? 22.24600 29.12900 -1.69500  0.790 30.57000  ?  177 ILE A N   1 
ATOM   2574 N  N   B ILE A 1 177 ? 22.29500 29.37400 -1.78200  0.210 29.24000  ?  177 ILE A N   1 
ATOM   2575 C  CA  A ILE A 1 177 ? 23.23600 28.15700 -2.15200  0.790 30.26000  ?  177 ILE A CA  1 
ATOM   2576 C  CA  B ILE A 1 177 ? 23.18600 28.31100 -2.19200  0.210 30.76000  ?  177 ILE A CA  1 
ATOM   2577 C  C   A ILE A 1 177 ? 23.59900 27.20000 -1.02100  0.790 39.39000  ?  177 ILE A C   1 
ATOM   2578 C  C   B ILE A 1 177 ? 23.61400 27.45100 -0.99600  0.210 38.13000  ?  177 ILE A C   1 
ATOM   2579 O  O   A ILE A 1 177 ? 23.74900 25.98900 -1.22900  0.790 40.38000  ?  177 ILE A O   1 
ATOM   2580 O  O   B ILE A 1 177 ? 24.07400 26.32900 -1.22200  0.210 39.93000  ?  177 ILE A O   1 
ATOM   2581 C  CB  A ILE A 1 177 ? 24.48800 28.87000 -2.69400  0.790 33.49000  ?  177 ILE A CB  1 
ATOM   2582 C  CB  B ILE A 1 177 ? 24.40300 28.81800 -2.98100  0.210 33.93000  ?  177 ILE A CB  1 
ATOM   2583 C  CG1 A ILE A 1 177 ? 24.12700 29.88400 -3.78000  0.790 33.02000  ?  177 ILE A CG1 1 
ATOM   2584 C  CG1 B ILE A 1 177 ? 24.04000 29.92200 -4.03500  0.210 33.12000  ?  177 ILE A CG1 1 
ATOM   2585 C  CG2 A ILE A 1 177 ? 25.48200 27.83800 -3.22700  0.790 36.51000  ?  177 ILE A CG2 1 
ATOM   2586 C  CG2 B ILE A 1 177 ? 24.93400 27.71200 -3.77800  0.210 36.66000  ?  177 ILE A CG2 1 
ATOM   2587 C  CD1 A ILE A 1 177 ? 23.09000 29.40700 -4.76600  0.790 25.95000  ?  177 ILE A CD1 1 
ATOM   2588 C  CD1 B ILE A 1 177 ? 22.83400 29.69300 -4.83500  0.210 25.95000  ?  177 ILE A CD1 1 
ATOM   2589 N  N   A TRP A 1 178 ? 23.78900 27.73800 0.18600   0.790 38.88000  ?  178 TRP A N   1 
ATOM   2590 N  N   B TRP A 1 178 ? 23.45000 27.90600 0.27500   0.210 35.33000  ?  178 TRP A N   1 
ATOM   2591 C  CA  A TRP A 1 178 ? 24.08400 26.91100 1.35400   0.790 33.99000  ?  178 TRP A CA  1 
ATOM   2592 C  CA  B TRP A 1 178 ? 23.67700 27.00900 1.44300   0.210 36.84000  ?  178 TRP A CA  1 
ATOM   2593 C  C   A TRP A 1 178 ? 22.98400 25.88300 1.57900   0.790 33.27000  ?  178 TRP A C   1 
ATOM   2594 C  C   B TRP A 1 178 ? 22.53000 26.05600 1.57200   0.210 36.61000  ?  178 TRP A C   1 
ATOM   2595 O  O   A TRP A 1 178 ? 23.25300 24.68400 1.71900   0.790 53.70000  ?  178 TRP A O   1 
ATOM   2596 O  O   B TRP A 1 178 ? 22.69400 24.84900 1.72400   0.210 42.61000  ?  178 TRP A O   1 
ATOM   2597 C  CB  A TRP A 1 178 ? 24.25000 27.82700 2.57200   0.790 44.20000  ?  178 TRP A CB  1 
ATOM   2598 C  CB  B TRP A 1 178 ? 23.75700 27.79400 2.77500   0.210 41.03000  ?  178 TRP A CB  1 
ATOM   2599 C  CG  A TRP A 1 178 ? 24.74800 27.21300 3.85400   0.790 32.21000  ?  178 TRP A CG  1 
ATOM   2600 C  CG  B TRP A 1 178 ? 24.24600 27.09500 4.13200   0.210 36.98000  ?  178 TRP A CG  1 
ATOM   2601 C  CD1 A TRP A 1 178 ? 26.02500 27.24900 4.34000   0.790 32.12000  ?  178 TRP A CD1 1 
ATOM   2602 C  CD1 B TRP A 1 178 ? 25.49900 27.21100 4.65600   0.210 36.11000  ?  178 TRP A CD1 1 
ATOM   2603 C  CD2 A TRP A 1 178 ? 23.96600 26.52600 4.83800   0.790 32.66000  ?  178 TRP A CD2 1 
ATOM   2604 C  CD2 B TRP A 1 178 ? 23.47700 26.33000 5.14400   0.210 34.54000  ?  178 TRP A CD2 1 
ATOM   2605 N  NE1 A TRP A 1 178 ? 26.08900 26.61200 5.55500   0.790 38.75000  ?  178 TRP A NE1 1 
ATOM   2606 N  NE1 B TRP A 1 178 ? 25.58200 26.55500 5.86600   0.210 40.15000  ?  178 TRP A NE1 1 
ATOM   2607 C  CE2 A TRP A 1 178 ? 24.83800 26.15900 5.88400   0.790 35.10000  ?  178 TRP A CE2 1 
ATOM   2608 C  CE2 B TRP A 1 178 ? 24.36100 26.01400 6.18400   0.210 34.77000  ?  178 TRP A CE2 1 
ATOM   2609 C  CE3 A TRP A 1 178 ? 22.61500 26.18200 4.93400   0.790 43.38000  ?  178 TRP A CE3 1 
ATOM   2610 C  CE3 B TRP A 1 178 ? 22.15200 25.86200 5.23700   0.210 44.61000  ?  178 TRP A CE3 1 
ATOM   2611 C  CZ2 A TRP A 1 178 ? 24.40200 25.45900 7.00800   0.790 47.82000  ?  178 TRP A CZ2 1 
ATOM   2612 C  CZ2 B TRP A 1 178 ? 23.97700 25.23500 7.31600   0.210 48.06000  ?  178 TRP A CZ2 1 
ATOM   2613 C  CZ3 A TRP A 1 178 ? 22.18700 25.48400 6.04800   0.790 47.47000  ?  178 TRP A CZ3 1 
ATOM   2614 C  CZ3 B TRP A 1 178 ? 21.75100 25.08100 6.39900   0.210 44.50000  ?  178 TRP A CZ3 1 
ATOM   2615 C  CH2 A TRP A 1 178 ? 23.07700 25.13200 7.07100   0.790 47.60000  ?  178 TRP A CH2 1 
ATOM   2616 C  CH2 B TRP A 1 178 ? 22.66700 24.78300 7.40800   0.210 42.02000  ?  178 TRP A CH2 1 
ATOM   2617 N  N   A LEU A 1 179 ? 21.73000 26.33400 1.57200   0.790 41.60000  ?  179 LEU A N   1 
ATOM   2618 N  N   B LEU A 1 179 ? 21.34800 26.61400 1.51900   0.210 40.66000  ?  179 LEU A N   1 
ATOM   2619 C  CA  A LEU A 1 179 ? 20.61700 25.44600 1.88900   0.790 30.48000  ?  179 LEU A CA  1 
ATOM   2620 C  CA  B LEU A 1 179 ? 20.14000 25.87900 1.71600   0.210 35.26000  ?  179 LEU A CA  1 
ATOM   2621 C  C   A LEU A 1 179 ? 20.41700 24.38900 0.81200   0.790 46.69000  ?  179 LEU A C   1 
ATOM   2622 C  C   B LEU A 1 179 ? 19.88400 24.84700 0.61500   0.210 43.69000  ?  179 LEU A C   1 
ATOM   2623 O  O   A LEU A 1 179 ? 20.05700 23.24800 1.12000   0.790 46.80000  ?  179 LEU A O   1 
ATOM   2624 O  O   B LEU A 1 179 ? 19.08800 23.92400 0.83700   0.210 40.06000  ?  179 LEU A O   1 
ATOM   2625 C  CB  A LEU A 1 179 ? 19.34700 26.26900 2.07400   0.790 35.51000  ?  179 LEU A CB  1 
ATOM   2626 C  CB  B LEU A 1 179 ? 19.06400 26.92500 1.83800   0.210 34.64000  ?  179 LEU A CB  1 
ATOM   2627 C  CG  A LEU A 1 179 ? 18.25900 25.69900 2.97900   0.790 43.59000  ?  179 LEU A CG  1 
ATOM   2628 C  CG  B LEU A 1 179 ? 17.93100 26.47600 2.71500   0.210 40.39000  ?  179 LEU A CG  1 
ATOM   2629 C  CD1 A LEU A 1 179 ? 18.77900 25.45300 4.37600   0.790 49.22000  ?  179 LEU A CD1 1 
ATOM   2630 C  CD1 B LEU A 1 179 ? 18.55900 25.94300 3.95800   0.210 43.87000  ?  179 LEU A CD1 1 
ATOM   2631 C  CD2 A LEU A 1 179 ? 17.07400 26.65700 2.99000   0.790 39.61000  ?  179 LEU A CD2 1 
ATOM   2632 C  CD2 B LEU A 1 179 ? 17.12400 27.68100 2.97000   0.210 39.61000  ?  179 LEU A CD2 1 
ATOM   2633 N  N   A LEU A 1 180 ? 20.63200 24.74300 -0.45400  0.790 41.89000  ?  180 LEU A N   1 
ATOM   2634 N  N   B LEU A 1 180 ? 20.53500 24.96900 -0.56400  0.210 41.28000  ?  180 LEU A N   1 
ATOM   2635 C  CA  A LEU A 1 180 ? 20.45800 23.77800 -1.53200  0.790 40.27000  ?  180 LEU A CA  1 
ATOM   2636 C  CA  B LEU A 1 180 ? 20.36000 24.00300 -1.65800  0.210 42.06000  ?  180 LEU A CA  1 
ATOM   2637 C  C   A LEU A 1 180 ? 21.66300 22.86400 -1.70400  0.790 45.06000  ?  180 LEU A C   1 
ATOM   2638 C  C   B LEU A 1 180 ? 21.50200 23.02000 -1.79700  0.210 44.70000  ?  180 LEU A C   1 
ATOM   2639 O  O   A LEU A 1 180 ? 21.56100 21.85800 -2.41500  0.790 51.88000  ?  180 LEU A O   1 
ATOM   2640 O  O   B LEU A 1 180 ? 21.27000 21.90000 -2.22100  0.210 52.14000  ?  180 LEU A O   1 
ATOM   2641 C  CB  A LEU A 1 180 ? 20.18100 24.50200 -2.84900  0.790 39.00000  ?  180 LEU A CB  1 
ATOM   2642 C  CB  B LEU A 1 180 ? 20.19000 24.69400 -3.02800  0.210 38.86000  ?  180 LEU A CB  1 
ATOM   2643 C  CG  A LEU A 1 180 ? 18.79600 25.13600 -2.98800  0.790 37.28000  ?  180 LEU A CG  1 
ATOM   2644 C  CG  B LEU A 1 180 ? 18.84900 25.26600 -3.47200  0.210 37.36000  ?  180 LEU A CG  1 
ATOM   2645 C  CD1 A LEU A 1 180 ? 18.73700 26.06700 -4.18900  0.790 33.04000  ?  180 LEU A CD1 1 
ATOM   2646 C  CD1 B LEU A 1 180 ? 19.07400 26.27900 -4.54800  0.210 33.04000  ?  180 LEU A CD1 1 
ATOM   2647 C  CD2 A LEU A 1 180 ? 17.72300 24.06100 -3.10000  0.790 37.75000  ?  180 LEU A CD2 1 
ATOM   2648 C  CD2 B LEU A 1 180 ? 17.95700 24.18100 -3.96100  0.210 36.53000  ?  180 LEU A CD2 1 
ATOM   2649 N  N   A GLY A 1 181 ? 22.78400 23.18100 -1.06500  0.790 47.60000  ?  181 GLY A N   1 
ATOM   2650 N  N   B GLY A 1 181 ? 22.72600 23.39500 -1.48500  0.210 45.71000  ?  181 GLY A N   1 
ATOM   2651 C  CA  A GLY A 1 181 ? 23.99400 22.41400 -1.21400  0.790 42.59000  ?  181 GLY A CA  1 
ATOM   2652 C  CA  B GLY A 1 181 ? 23.81600 22.47500 -1.63300  0.210 43.64000  ?  181 GLY A CA  1 
ATOM   2653 C  C   A GLY A 1 181 ? 24.15500 21.36300 -0.13800  0.790 45.21000  ?  181 GLY A C   1 
ATOM   2654 C  C   B GLY A 1 181 ? 23.83700 21.49000 -0.49800  0.210 45.60000  ?  181 GLY A C   1 
ATOM   2655 O  O   A GLY A 1 181 ? 23.21500 21.02800 0.58900   0.790 43.32000  ?  181 GLY A O   1 
ATOM   2656 O  O   B GLY A 1 181 ? 22.83600 21.24700 0.18000   0.210 43.87000  ?  181 GLY A O   1 
ATOM   2657 N  N   A PRO A 1 182 ? 25.36600 20.82400 -0.01900  0.790 56.84000  ?  182 PRO A N   1 
ATOM   2658 N  N   B PRO A 1 182 ? 25.01400 20.91500 -0.28100  0.210 53.90000  ?  182 PRO A N   1 
ATOM   2659 C  CA  A PRO A 1 182 ? 25.61700 19.74300 0.94800   0.790 57.33000  ?  182 PRO A CA  1 
ATOM   2660 C  CA  B PRO A 1 182 ? 25.23900 19.98500 0.83700   0.210 55.83000  ?  182 PRO A CA  1 
ATOM   2661 C  C   A PRO A 1 182 ? 25.25100 20.13300 2.36900   0.790 51.61000  ?  182 PRO A C   1 
ATOM   2662 C  C   B PRO A 1 182 ? 24.55300 20.40300 2.12900   0.210 52.42000  ?  182 PRO A C   1 
ATOM   2663 O  O   A PRO A 1 182 ? 24.70500 19.30400 3.11500   0.790 51.62000  ?  182 PRO A O   1 
ATOM   2664 O  O   B PRO A 1 182 ? 23.64200 19.68200 2.56300   0.210 48.32000  ?  182 PRO A O   1 
ATOM   2665 C  CB  A PRO A 1 182 ? 27.12700 19.49000 0.80900   0.790 56.15000  ?  182 PRO A CB  1 
ATOM   2666 C  CB  B PRO A 1 182 ? 26.77400 19.97800 0.96300   0.210 56.29000  ?  182 PRO A CB  1 
ATOM   2667 C  CG  A PRO A 1 182 ? 27.43400 19.88100 -0.60900  0.790 46.71000  ?  182 PRO A CG  1 
ATOM   2668 C  CG  B PRO A 1 182 ? 27.22900 20.10400 -0.52700  0.210 48.31000  ?  182 PRO A CG  1 
ATOM   2669 C  CD  A PRO A 1 182 ? 26.51400 21.04300 -0.92200  0.790 52.94000  ?  182 PRO A CD  1 
ATOM   2670 C  CD  B PRO A 1 182 ? 26.17100 20.96900 -1.20000  0.210 52.58000  ?  182 PRO A CD  1 
ATOM   2671 N  N   A PRO A 1 183 ? 25.54700 21.36500 2.80400   0.790 47.20000  ?  183 PRO A N   1 
ATOM   2672 N  N   B PRO A 1 183 ? 24.90800 21.54500 2.76400   0.210 48.38000  ?  183 PRO A N   1 
ATOM   2673 C  CA  A PRO A 1 183 ? 25.22400 21.71600 4.20100   0.790 51.40000  ?  183 PRO A CA  1 
ATOM   2674 C  CA  B PRO A 1 183 ? 24.56200 21.69300 4.19900   0.210 49.91000  ?  183 PRO A CA  1 
ATOM   2675 C  C   A PRO A 1 183 ? 23.74900 21.57400 4.53000   0.790 47.00000  ?  183 PRO A C   1 
ATOM   2676 C  C   B PRO A 1 183 ? 23.07300 21.66100 4.43400   0.210 47.16000  ?  183 PRO A C   1 
ATOM   2677 O  O   A PRO A 1 183 ? 23.40200 21.28800 5.68300   0.790 51.50000  ?  183 PRO A O   1 
ATOM   2678 O  O   B PRO A 1 183 ? 22.63100 21.42900 5.56900   0.210 52.99000  ?  183 PRO A O   1 
ATOM   2679 C  CB  A PRO A 1 183 ? 25.68500 23.17600 4.32400   0.790 51.79000  ?  183 PRO A CB  1 
ATOM   2680 C  CB  B PRO A 1 183 ? 25.16600 23.05700 4.59300   0.210 49.31000  ?  183 PRO A CB  1 
ATOM   2681 C  CG  A PRO A 1 183 ? 26.67300 23.37000 3.22100   0.790 43.63000  ?  183 PRO A CG  1 
ATOM   2682 C  CG  B PRO A 1 183 ? 26.08200 23.47200 3.45400   0.210 46.96000  ?  183 PRO A CG  1 
ATOM   2683 C  CD  A PRO A 1 183 ? 26.21900 22.47400 2.09900   0.790 54.34000  ?  183 PRO A CD  1 
ATOM   2684 C  CD  B PRO A 1 183 ? 25.40100 22.82400 2.23100   0.210 48.38000  ?  183 PRO A CD  1 
ATOM   2685 N  N   A GLY A 1 184 ? 22.87100 21.77400 3.55000   0.790 36.73000  ?  184 GLY A N   1 
ATOM   2686 N  N   B GLY A 1 184 ? 22.29900 21.89100 3.38300   0.210 43.12000  ?  184 GLY A N   1 
ATOM   2687 C  CA  A GLY A 1 184 ? 21.44100 21.71300 3.77500   0.790 42.80000  ?  184 GLY A CA  1 
ATOM   2688 C  CA  B GLY A 1 184 ? 20.86200 21.94900 3.42800   0.210 47.76000  ?  184 GLY A CA  1 
ATOM   2689 C  C   A GLY A 1 184 ? 20.81400 20.45700 3.21300   0.790 53.91000  ?  184 GLY A C   1 
ATOM   2690 C  C   B GLY A 1 184 ? 20.17600 20.80000 2.70400   0.210 50.51000  ?  184 GLY A C   1 
ATOM   2691 O  O   A GLY A 1 184 ? 21.18000 19.34800 3.60900   0.790 59.39000  ?  184 GLY A O   1 
ATOM   2692 O  O   B GLY A 1 184 ? 20.39000 19.62500 3.03900   0.210 53.26000  ?  184 GLY A O   1 
ATOM   2693 N  N   A VAL A 1 185 ? 19.89400 20.60500 2.26300   0.790 44.35000  ?  185 VAL A N   1 
ATOM   2694 N  N   B VAL A 1 185 ? 19.35000 21.11800 1.70200   0.210 48.65000  ?  185 VAL A N   1 
ATOM   2695 C  CA  A VAL A 1 185 ? 19.16600 19.45100 1.74200   0.790 58.73000  ?  185 VAL A CA  1 
ATOM   2696 C  CA  B VAL A 1 185 ? 18.54300 20.08900 1.06000   0.210 53.08000  ?  185 VAL A CA  1 
ATOM   2697 C  C   A VAL A 1 185 ? 20.06800 18.58100 0.87000   0.790 70.57000  ?  185 VAL A C   1 
ATOM   2698 C  C   B VAL A 1 185 ? 19.34200 19.35000 0.00100   0.210 53.75000  ?  185 VAL A C   1 
ATOM   2699 O  O   A VAL A 1 185 ? 19.64100 17.53500 0.36600   0.790 68.28000  ?  185 VAL A O   1 
ATOM   2700 O  O   B VAL A 1 185 ? 18.77200 18.56500 -0.75600  0.210 57.69000  ?  185 VAL A O   1 
ATOM   2701 C  CB  A VAL A 1 185 ? 17.91700 19.87800 0.94600   0.790 50.88000  ?  185 VAL A CB  1 
ATOM   2702 C  CB  B VAL A 1 185 ? 17.25100 20.65300 0.46000   0.210 48.06000  ?  185 VAL A CB  1 
ATOM   2703 C  CG1 A VAL A 1 185 ? 16.88600 20.51700 1.85200   0.790 69.36000  ?  185 VAL A CG1 1 
ATOM   2704 C  CG1 B VAL A 1 185 ? 16.54700 21.48600 1.49300   0.210 57.73000  ?  185 VAL A CG1 1 
ATOM   2705 C  CG2 A VAL A 1 185 ? 18.30600 20.82300 -0.19200  0.790 48.55000  ?  185 VAL A CG2 1 
ATOM   2706 C  CG2 B VAL A 1 185 ? 17.48600 21.43000 -0.79500  0.210 53.74000  ?  185 VAL A CG2 1 
ATOM   2707 N  N   A ALA A 1 186 ? 21.31400 19.00500 0.66700   0.790 69.42000  ?  186 ALA A N   1 
ATOM   2708 N  N   B ALA A 1 186 ? 20.66200 19.60000 -0.05200  0.210 56.52000  ?  186 ALA A N   1 
ATOM   2709 C  CA  A ALA A 1 186 ? 22.28600 18.21200 -0.09400  0.790 60.65000  ?  186 ALA A CA  1 
ATOM   2710 C  CA  B ALA A 1 186 ? 21.69000 18.68600 -0.56400  0.210 53.57000  ?  186 ALA A CA  1 
ATOM   2711 C  C   A ALA A 1 186 ? 21.77400 17.90200 -1.50100  0.790 52.70000  ?  186 ALA A C   1 
ATOM   2712 C  C   B ALA A 1 186 ? 21.41300 18.23600 -1.97200  0.210 58.98000  ?  186 ALA A C   1 
ATOM   2713 O  O   A ALA A 1 186 ? 22.02100 16.82600 -2.05400  0.790 62.82000  ?  186 ALA A O   1 
ATOM   2714 O  O   B ALA A 1 186 ? 21.98600 17.24600 -2.44300  0.210 63.49000  ?  186 ALA A O   1 
ATOM   2715 C  CB  A ALA A 1 186 ? 22.63600 16.91700 0.64400   0.790 67.72000  ?  186 ALA A CB  1 
ATOM   2716 C  CB  B ALA A 1 186 ? 21.86900 17.47400 0.34900   0.210 62.75000  ?  186 ALA A CB  1 
ATOM   2717 N  N   A LEU A 1 187 ? 21.04100 18.85100 -2.08000  0.790 60.61000  ?  187 LEU A N   1 
ATOM   2718 N  N   B LEU A 1 187 ? 20.48200 18.92800 -2.61400  0.210 56.80000  ?  187 LEU A N   1 
ATOM   2719 C  CA  A LEU A 1 187 ? 20.52600 18.69000 -3.43900  0.790 49.49000  ?  187 LEU A CA  1 
ATOM   2720 C  CA  B LEU A 1 187 ? 20.20000 18.80300 -4.02100  0.210 53.16000  ?  187 LEU A CA  1 
ATOM   2721 C  C   A LEU A 1 187 ? 21.63800 18.94100 -4.45300  0.790 65.23000  ?  187 LEU A C   1 
ATOM   2722 C  C   B LEU A 1 187 ? 21.54400 19.01700 -4.71500  0.210 64.70000  ?  187 LEU A C   1 
ATOM   2723 O  O   A LEU A 1 187 ? 22.10400 18.01600 -5.12400  0.790 71.82000  ?  187 LEU A O   1 
ATOM   2724 O  O   B LEU A 1 187 ? 22.31000 18.04900 -4.87700  0.210 67.31000  ?  187 LEU A O   1 
ATOM   2725 C  CB  A LEU A 1 187 ? 19.34500 19.64100 -3.65200  0.790 48.39000  ?  187 LEU A CB  1 
ATOM   2726 C  CB  B LEU A 1 187 ? 19.12100 19.82800 -4.39000  0.210 49.81000  ?  187 LEU A CB  1 
ATOM   2727 C  CG  A LEU A 1 187 ? 18.35900 19.38700 -4.79000  0.790 49.78000  ?  187 LEU A CG  1 
ATOM   2728 C  CG  B LEU A 1 187 ? 18.18700 19.76800 -5.58600  0.210 50.49000  ?  187 LEU A CG  1 
ATOM   2729 C  CD1 A LEU A 1 187 ? 17.92600 17.94500 -4.89000  0.790 57.64000  ?  187 LEU A CD1 1 
ATOM   2730 C  CD1 B LEU A 1 187 ? 17.78800 18.36400 -5.85100  0.210 45.97000  ?  187 LEU A CD1 1 
ATOM   2731 C  CD2 A LEU A 1 187 ? 17.13500 20.30000 -4.60600  0.790 41.65000  ?  187 LEU A CD2 1 
ATOM   2732 C  CD2 B LEU A 1 187 ? 16.96100 20.53000 -5.20200  0.210 45.55000  ?  187 LEU A CD2 1 
ATOM   2733 N  N   A LEU A 1 188 ? 22.08200 20.19200 -4.56500  0.790 56.22000  ?  188 LEU A N   1 
ATOM   2734 N  N   B LEU A 1 188 ? 21.85500 20.28200 -5.06700  0.210 57.63000  ?  188 LEU A N   1 
ATOM   2735 C  CA  A LEU A 1 188 ? 23.22000 20.50300 -5.41700  0.790 51.99000  ?  188 LEU A CA  1 
ATOM   2736 C  CA  B LEU A 1 188 ? 23.12800 20.68900 -5.65600  0.210 52.65000  ?  188 LEU A CA  1 
ATOM   2737 C  C   A LEU A 1 188 ? 24.43300 19.68400 -4.99500  0.790 54.46000  ?  188 LEU A C   1 
ATOM   2738 C  C   B LEU A 1 188 ? 24.30200 19.85800 -5.19400  0.210 54.02000  ?  188 LEU A C   1 
ATOM   2739 O  O   A LEU A 1 188 ? 24.66100 19.44700 -3.80500  0.790 58.07000  ?  188 LEU A O   1 
ATOM   2740 O  O   B LEU A 1 188 ? 24.51000 19.70800 -3.98700  0.210 54.69000  ?  188 LEU A O   1 
ATOM   2741 C  CB  A LEU A 1 188 ? 23.55100 21.99100 -5.33900  0.790 43.82000  ?  188 LEU A CB  1 
ATOM   2742 C  CB  B LEU A 1 188 ? 23.46400 22.11200 -5.28700  0.210 44.31000  ?  188 LEU A CB  1 
ATOM   2743 C  CG  A LEU A 1 188 ? 22.54500 22.95800 -5.95300  0.790 46.55000  ?  188 LEU A CG  1 
ATOM   2744 C  CG  B LEU A 1 188 ? 22.43800 23.07400 -5.76500  0.210 47.40000  ?  188 LEU A CG  1 
ATOM   2745 C  CD1 A LEU A 1 188 ? 22.91000 24.38600 -5.58400  0.790 42.54000  ?  188 LEU A CD1 1 
ATOM   2746 C  CD1 B LEU A 1 188 ? 23.05200 24.42200 -5.48900  0.210 42.67000  ?  188 LEU A CD1 1 
ATOM   2747 C  CD2 A LEU A 1 188 ? 22.50100 22.79200 -7.46000  0.790 59.93000  ?  188 LEU A CD2 1 
ATOM   2748 C  CD2 B LEU A 1 188 ? 22.17600 22.79000 -7.22900  0.210 56.45000  ?  188 LEU A CD2 1 
ATOM   2749 N  N   A THR A 1 189 ? 25.21900 19.25600 -5.97700  0.790 43.80000  ?  189 THR A N   1 
ATOM   2750 N  N   B THR A 1 189 ? 25.08600 19.38000 -6.14800  0.210 44.57000  ?  189 THR A N   1 
ATOM   2751 C  CA  A THR A 1 189 ? 26.41200 18.47400 -5.70000  0.790 41.79000  ?  189 THR A CA  1 
ATOM   2752 C  CA  B THR A 1 189 ? 26.27600 18.62400 -5.85800  0.210 43.72000  ?  189 THR A CA  1 
ATOM   2753 C  C   A THR A 1 189 ? 27.53200 19.37400 -5.19300  0.790 39.11000  ?  189 THR A C   1 
ATOM   2754 C  C   B THR A 1 189 ? 27.40600 19.52700 -5.36400  0.210 40.58000  ?  189 THR A C   1 
ATOM   2755 O  O   A THR A 1 189 ? 27.52300 20.58600 -5.42400  0.790 42.15000  ?  189 THR A O   1 
ATOM   2756 O  O   B THR A 1 189 ? 27.44900 20.72300 -5.66400  0.210 42.81000  ?  189 THR A O   1 
ATOM   2757 C  CB  A THR A 1 189 ? 26.86500 17.74000 -6.95700  0.790 54.53000  ?  189 THR A CB  1 
ATOM   2758 C  CB  B THR A 1 189 ? 26.72600 17.93800 -7.12600  0.210 53.63000  ?  189 THR A CB  1 
ATOM   2759 O  OG1 A THR A 1 189 ? 27.19300 18.69400 -7.97500  0.790 47.58000  ?  189 THR A OG1 1 
ATOM   2760 O  OG1 B THR A 1 189 ? 27.16800 18.94000 -8.04800  0.210 44.82000  ?  189 THR A OG1 1 
ATOM   2761 C  CG2 A THR A 1 189 ? 25.76600 16.81600 -7.46100  0.790 67.36000  ?  189 THR A CG2 1 
ATOM   2762 C  CG2 B THR A 1 189 ? 25.52200 17.25200 -7.79400  0.210 60.98000  ?  189 THR A CG2 1 
ATOM   2763 N  N   A PRO A 1 190 ? 28.51800 18.80200 -4.49600  0.790 42.63000  ?  190 PRO A N   1 
ATOM   2764 N  N   B PRO A 1 190 ? 28.34700 18.97200 -4.62100  0.210 41.57000  ?  190 PRO A N   1 
ATOM   2765 C  CA  A PRO A 1 190 ? 29.61400 19.64500 -3.98300  0.790 35.50000  ?  190 PRO A CA  1 
ATOM   2766 C  CA  B PRO A 1 190 ? 29.48600 19.77800 -4.13800  0.210 37.46000  ?  190 PRO A CA  1 
ATOM   2767 C  C   A PRO A 1 190 ? 30.30700 20.44400 -5.07300  0.790 37.98000  ?  190 PRO A C   1 
ATOM   2768 C  C   B PRO A 1 190 ? 30.25500 20.54400 -5.20600  0.210 37.85000  ?  190 PRO A C   1 
ATOM   2769 O  O   A PRO A 1 190 ? 30.63500 21.61900 -4.86600  0.790 41.59000  ?  190 PRO A O   1 
ATOM   2770 O  O   B PRO A 1 190 ? 30.78500 21.62200 -4.90300  0.210 40.10000  ?  190 PRO A O   1 
ATOM   2771 C  CB  A PRO A 1 190 ? 30.56100 18.63000 -3.32200  0.790 37.68000  ?  190 PRO A CB  1 
ATOM   2772 C  CB  B PRO A 1 190 ? 30.36800 18.73200 -3.45800  0.210 38.48000  ?  190 PRO A CB  1 
ATOM   2773 C  CG  A PRO A 1 190 ? 29.70200 17.42700 -3.03000  0.790 38.86000  ?  190 PRO A CG  1 
ATOM   2774 C  CG  B PRO A 1 190 ? 29.39600 17.72000 -2.95400  0.210 42.34000  ?  190 PRO A CG  1 
ATOM   2775 C  CD  A PRO A 1 190 ? 28.68500 17.38000 -4.14100  0.790 44.07000  ?  190 PRO A CD  1 
ATOM   2776 C  CD  B PRO A 1 190 ? 28.24300 17.67200 -3.94000  0.210 42.99000  ?  190 PRO A CD  1 
ATOM   2777 N  N   A THR A 1 191 ? 30.52800 19.84200 -6.24200  0.790 40.45000  ?  191 THR A N   1 
ATOM   2778 N  N   B THR A 1 191 ? 30.34700 20.03400 -6.43400  0.210 38.88000  ?  191 THR A N   1 
ATOM   2779 C  CA  A THR A 1 191 ? 31.27000 20.52900 -7.29400  0.790 38.93000  ?  191 THR A CA  1 
ATOM   2780 C  CA  B THR A 1 191 ? 31.10000 20.73800 -7.46400  0.210 38.94000  ?  191 THR A CA  1 
ATOM   2781 C  C   A THR A 1 191 ? 30.51100 21.75200 -7.79400  0.790 35.80000  ?  191 THR A C   1 
ATOM   2782 C  C   B THR A 1 191 ? 30.35700 22.00900 -7.85000  0.210 34.05000  ?  191 THR A C   1 
ATOM   2783 O  O   A THR A 1 191 ? 31.08600 22.83800 -7.93400  0.790 31.66000  ?  191 THR A O   1 
ATOM   2784 O  O   B THR A 1 191 ? 30.88400 23.13800 -7.78300  0.210 28.44000  ?  191 THR A O   1 
ATOM   2785 C  CB  A THR A 1 191 ? 31.55800 19.57000 -8.44900  0.790 44.30000  ?  191 THR A CB  1 
ATOM   2786 C  CB  B THR A 1 191 ? 31.27800 19.82600 -8.68900  0.210 43.53000  ?  191 THR A CB  1 
ATOM   2787 O  OG1 A THR A 1 191 ? 32.44200 18.53500 -8.00100  0.790 51.19000  ?  191 THR A OG1 1 
ATOM   2788 O  OG1 B THR A 1 191 ? 31.91800 18.61000 -8.30000  0.210 41.38000  ?  191 THR A OG1 1 
ATOM   2789 C  CG2 A THR A 1 191 ? 32.19300 20.31800 -9.60900  0.790 33.45000  ?  191 THR A CG2 1 
ATOM   2790 C  CG2 B THR A 1 191 ? 32.12400 20.51500 -9.73800  0.210 32.77000  ?  191 THR A CG2 1 
ATOM   2791 N  N   A VAL A 1 192 ? 29.22000 21.59100 -8.08500  0.790 30.07000  ?  192 VAL A N   1 
ATOM   2792 N  N   B VAL A 1 192 ? 29.11200 21.80500 -8.26700  0.210 32.07000  ?  192 VAL A N   1 
ATOM   2793 C  CA  A VAL A 1 192 ? 28.42400 22.72800 -8.53100  0.790 30.08000  ?  192 VAL A CA  1 
ATOM   2794 C  CA  B VAL A 1 192 ? 28.14000 22.87200 -8.46400  0.210 30.58000  ?  192 VAL A CA  1 
ATOM   2795 C  C   A VAL A 1 192 ? 28.30000 23.75700 -7.41600  0.790 33.87000  ?  192 VAL A C   1 
ATOM   2796 C  C   B VAL A 1 192 ? 28.12600 23.76400 -7.25000  0.210 33.22000  ?  192 VAL A C   1 
ATOM   2797 O  O   A VAL A 1 192 ? 28.43200 24.96500 -7.64800  0.790 34.00000  ?  192 VAL A O   1 
ATOM   2798 O  O   B VAL A 1 192 ? 28.22600 24.99200 -7.34200  0.210 31.81000  ?  192 VAL A O   1 
ATOM   2799 C  CB  A VAL A 1 192 ? 27.04300 22.25300 -9.02200  0.790 35.05000  ?  192 VAL A CB  1 
ATOM   2800 C  CB  B VAL A 1 192 ? 26.75100 22.26800 -8.71400  0.210 35.28000  ?  192 VAL A CB  1 
ATOM   2801 C  CG1 A VAL A 1 192 ? 26.18400 23.44100 -9.42700  0.790 32.36000  ?  192 VAL A CG1 1 
ATOM   2802 C  CG1 B VAL A 1 192 ? 25.69300 23.35400 -8.76500  0.210 39.91000  ?  192 VAL A CG1 1 
ATOM   2803 C  CG2 A VAL A 1 192 ? 27.20200 21.27300 -10.17400 0.790 34.97000  ?  192 VAL A CG2 1 
ATOM   2804 C  CG2 B VAL A 1 192 ? 26.77600 21.39600 -9.97800  0.210 38.61000  ?  192 VAL A CG2 1 
ATOM   2805 N  N   A ASP A 1 193 ? 28.05100 23.29900 -6.18700  0.790 37.61000  ?  193 ASP A N   1 
ATOM   2806 N  N   B ASP A 1 193 ? 28.07200 23.13700 -6.07800  0.210 37.17000  ?  193 ASP A N   1 
ATOM   2807 C  CA  A ASP A 1 193 ? 27.89200 24.23100 -5.07600  0.790 26.74000  ?  193 ASP A CA  1 
ATOM   2808 C  CA  B ASP A 1 193 ? 28.09200 23.89900 -4.86100  0.210 29.80000  ?  193 ASP A CA  1 
ATOM   2809 C  C   A ASP A 1 193 ? 29.15500 25.05500 -4.86300  0.790 35.08000  ?  193 ASP A C   1 
ATOM   2810 C  C   B ASP A 1 193 ? 29.31300 24.79100 -4.78200  0.210 34.01000  ?  193 ASP A C   1 
ATOM   2811 O  O   A ASP A 1 193 ? 29.08600 26.27100 -4.64600  0.790 38.77000  ?  193 ASP A O   1 
ATOM   2812 O  O   B ASP A 1 193 ? 29.20400 25.99300 -4.53100  0.210 37.44000  ?  193 ASP A O   1 
ATOM   2813 C  CB  A ASP A 1 193 ? 27.53400 23.47000 -3.80400  0.790 34.32000  ?  193 ASP A CB  1 
ATOM   2814 C  CB  B ASP A 1 193 ? 28.04100 22.97200 -3.67200  0.210 32.34000  ?  193 ASP A CB  1 
ATOM   2815 C  CG  A ASP A 1 193 ? 26.88200 24.35400 -2.77200  0.790 49.03000  ?  193 ASP A CG  1 
ATOM   2816 C  CG  B ASP A 1 193 ? 27.92600 23.73300 -2.43500  0.210 34.22000  ?  193 ASP A CG  1 
ATOM   2817 O  OD1 A ASP A 1 193 ? 25.71000 24.73100 -2.97700  0.790 39.44000  ?  193 ASP A OD1 1 
ATOM   2818 O  OD1 B ASP A 1 193 ? 26.81800 24.24100 -2.17600  0.210 45.44000  ?  193 ASP A OD1 1 
ATOM   2819 O  OD2 A ASP A 1 193 ? 27.54100 24.68000 -1.76500  0.790 35.51000  -1 193 ASP A OD2 1 
ATOM   2820 O  OD2 B ASP A 1 193 ? 28.96700 23.91200 -1.77800  0.210 35.22000  -1 193 ASP A OD2 1 
ATOM   2821 N  N   A VAL A 1 194 ? 30.31800 24.40600 -4.92500  0.790 32.98000  ?  194 VAL A N   1 
ATOM   2822 N  N   B VAL A 1 194 ? 30.49000 24.21700 -4.97400  0.210 31.98000  ?  194 VAL A N   1 
ATOM   2823 C  CA  A VAL A 1 194 ? 31.58400 25.11500 -4.77200  0.790 31.14000  ?  194 VAL A CA  1 
ATOM   2824 C  CA  B VAL A 1 194 ? 31.72300 24.97400 -4.77500  0.210 32.27000  ?  194 VAL A CA  1 
ATOM   2825 C  C   A VAL A 1 194 ? 31.78100 26.09800 -5.91800  0.790 31.59000  ?  194 VAL A C   1 
ATOM   2826 C  C   B VAL A 1 194 ? 31.88300 26.06000 -5.84300  0.210 31.57000  ?  194 VAL A C   1 
ATOM   2827 O  O   A VAL A 1 194 ? 32.17500 27.25100 -5.70800  0.790 31.92000  ?  194 VAL A O   1 
ATOM   2828 O  O   B VAL A 1 194 ? 32.29200 27.19900 -5.53300  0.210 30.95000  ?  194 VAL A O   1 
ATOM   2829 C  CB  A VAL A 1 194 ? 32.74400 24.10800 -4.67900  0.790 34.51000  ?  194 VAL A CB  1 
ATOM   2830 C  CB  B VAL A 1 194 ? 32.92100 23.99700 -4.74100  0.210 33.69000  ?  194 VAL A CB  1 
ATOM   2831 C  CG1 A VAL A 1 194 ? 34.06700 24.77000 -4.99400  0.790 35.38000  ?  194 VAL A CG1 1 
ATOM   2832 C  CG1 B VAL A 1 194 ? 34.22700 24.70000 -4.97200  0.210 35.25000  ?  194 VAL A CG1 1 
ATOM   2833 C  CG2 A VAL A 1 194 ? 32.77100 23.46000 -3.29600  0.790 29.23000  ?  194 VAL A CG2 1 
ATOM   2834 C  CG2 B VAL A 1 194 ? 32.93500 23.29700 -3.42800  0.210 28.58000  ?  194 VAL A CG2 1 
ATOM   2835 N  N   A ALA A 1 195 ? 31.50600 25.65800 -7.14900  0.790 34.30000  ?  195 ALA A N   1 
ATOM   2836 N  N   B ALA A 1 195 ? 31.55600 25.74600 -7.11800  0.210 33.72000  ?  195 ALA A N   1 
ATOM   2837 C  CA  A ALA A 1 195 ? 31.66500 26.54500 -8.29800  0.790 31.63000  ?  195 ALA A CA  1 
ATOM   2838 C  CA  B ALA A 1 195 ? 31.81500 26.71400 -8.20700  0.210 31.84000  ?  195 ALA A CA  1 
ATOM   2839 C  C   A ALA A 1 195 ? 30.84200 27.81400 -8.13000  0.790 28.34000  ?  195 ALA A C   1 
ATOM   2840 C  C   B ALA A 1 195 ? 30.93500 27.94600 -8.06200  0.210 28.11000  ?  195 ALA A C   1 
ATOM   2841 O  O   A ALA A 1 195 ? 31.32100 28.91800 -8.41500  0.790 30.41000  ?  195 ALA A O   1 
ATOM   2842 O  O   B ALA A 1 195 ? 31.41900 29.09300 -8.09600  0.210 28.06000  ?  195 ALA A O   1 
ATOM   2843 C  CB  A ALA A 1 195 ? 31.26800 25.81800 -9.58300  0.790 26.11000  ?  195 ALA A CB  1 
ATOM   2844 C  CB  B ALA A 1 195 ? 31.59100 26.07800 -9.58200  0.210 27.33000  ?  195 ALA A CB  1 
ATOM   2845 N  N   A LEU A 1 196 ? 29.60000 27.68100 -7.66200  0.790 28.01000  ?  196 LEU A N   1 
ATOM   2846 N  N   B LEU A 1 196 ? 29.63900 27.69800 -7.84000  0.210 28.15000  ?  196 LEU A N   1 
ATOM   2847 C  CA  A LEU A 1 196 ? 28.76200 28.85900 -7.47500  0.790 24.60000  ?  196 LEU A CA  1 
ATOM   2848 C  CA  B LEU A 1 196 ? 28.66600 28.71600 -7.47700  0.210 24.91000  ?  196 LEU A CA  1 
ATOM   2849 C  C   A LEU A 1 196 ? 29.32600 29.77300 -6.39100  0.790 27.88000  ?  196 LEU A C   1 
ATOM   2850 C  C   B LEU A 1 196 ? 29.04400 29.53900 -6.25800  0.210 27.64000  ?  196 LEU A C   1 
ATOM   2851 O  O   A LEU A 1 196 ? 29.28400 31.00000 -6.52700  0.790 29.00000  ?  196 LEU A O   1 
ATOM   2852 O  O   B LEU A 1 196 ? 28.55500 30.65900 -6.12400  0.210 29.94000  ?  196 LEU A O   1 
ATOM   2853 C  CB  A LEU A 1 196 ? 27.33100 28.43400 -7.14600  0.790 27.01000  ?  196 LEU A CB  1 
ATOM   2854 C  CB  B LEU A 1 196 ? 27.32700 28.07200 -7.19000  0.210 26.82000  ?  196 LEU A CB  1 
ATOM   2855 C  CG  A LEU A 1 196 ? 26.56900 27.79000 -8.30800  0.790 35.60000  ?  196 LEU A CG  1 
ATOM   2856 C  CG  B LEU A 1 196 ? 26.63100 27.56300 -8.41500  0.210 33.84000  ?  196 LEU A CG  1 
ATOM   2857 C  CD1 A LEU A 1 196 ? 25.26800 27.16800 -7.82900  0.790 26.84000  ?  196 LEU A CD1 1 
ATOM   2858 C  CD1 B LEU A 1 196 ? 25.36300 26.88800 -8.02900  0.210 26.51000  ?  196 LEU A CD1 1 
ATOM   2859 C  CD2 A LEU A 1 196 ? 26.30300 28.81300 -9.40600  0.790 35.29000  ?  196 LEU A CD2 1 
ATOM   2860 C  CD2 B LEU A 1 196 ? 26.37700 28.75400 -9.34000  0.210 35.24000  ?  196 LEU A CD2 1 
ATOM   2861 N  N   A ILE A 1 197 ? 29.88000 29.20400 -5.31900  0.790 21.07000  ?  197 ILE A N   1 
ATOM   2862 N  N   B ILE A 1 197 ? 29.82200 29.00000 -5.31200  0.210 21.29000  ?  197 ILE A N   1 
ATOM   2863 C  CA  A ILE A 1 197 ? 30.37700 30.04800 -4.23600  0.790 23.59000  ?  197 ILE A CA  1 
ATOM   2864 C  CA  B ILE A 1 197 ? 30.26000 29.85200 -4.19800  0.210 25.03000  ?  197 ILE A CA  1 
ATOM   2865 C  C   A ILE A 1 197 ? 31.70500 30.69700 -4.61700  0.790 30.26000  ?  197 ILE A C   1 
ATOM   2866 C  C   B ILE A 1 197 ? 31.55100 30.60800 -4.52700  0.210 29.15000  ?  197 ILE A C   1 
ATOM   2867 O  O   A ILE A 1 197 ? 31.97600 31.84100 -4.23400  0.790 30.51000  ?  197 ILE A O   1 
ATOM   2868 O  O   B ILE A 1 197 ? 31.66400 31.78400 -4.17500  0.210 28.00000  ?  197 ILE A O   1 
ATOM   2869 C  CB  A ILE A 1 197 ? 30.48600 29.24300 -2.92800  0.790 27.38000  ?  197 ILE A CB  1 
ATOM   2870 C  CB  B ILE A 1 197 ? 30.31300 29.03500 -2.87900  0.210 27.84000  ?  197 ILE A CB  1 
ATOM   2871 C  CG1 A ILE A 1 197 ? 29.08900 29.01700 -2.34500  0.790 34.64000  ?  197 ILE A CG1 1 
ATOM   2872 C  CG1 B ILE A 1 197 ? 28.84500 28.99600 -2.40900  0.210 33.37000  ?  197 ILE A CG1 1 
ATOM   2873 C  CG2 A ILE A 1 197 ? 31.35600 29.98300 -1.91500  0.790 20.05000  ?  197 ILE A CG2 1 
ATOM   2874 C  CG2 B ILE A 1 197 ? 31.26000 29.64500 -1.89600  0.210 21.11000  ?  197 ILE A CG2 1 
ATOM   2875 C  CD1 A ILE A 1 197 ? 28.93500 27.72300 -1.58600  0.790 49.85000  ?  197 ILE A CD1 1 
ATOM   2876 C  CD1 B ILE A 1 197 ? 28.29500 27.67800 -2.04700  0.210 41.25000  ?  197 ILE A CD1 1 
ATOM   2877 N  N   A VAL A 1 198 ? 32.55900 29.99500 -5.36600  0.790 28.75000  ?  198 VAL A N   1 
ATOM   2878 N  N   B VAL A 1 198 ? 32.48500 29.96200 -5.26400  0.210 28.77000  ?  198 VAL A N   1 
ATOM   2879 C  CA  A VAL A 1 198 ? 33.77900 30.64500 -5.84100  0.790 27.73000  ?  198 VAL A CA  1 
ATOM   2880 C  CA  B VAL A 1 198 ? 33.71500 30.60100 -5.75400  0.210 27.83000  ?  198 VAL A CA  1 
ATOM   2881 C  C   A VAL A 1 198 ? 33.42200 31.87200 -6.67000  0.790 24.25000  ?  198 VAL A C   1 
ATOM   2882 C  C   B VAL A 1 198 ? 33.41300 31.85500 -6.54700  0.210 24.42000  ?  198 VAL A C   1 
ATOM   2883 O  O   A VAL A 1 198 ? 34.05800 32.92800 -6.55500  0.790 31.18000  ?  198 VAL A O   1 
ATOM   2884 O  O   B VAL A 1 198 ? 34.04100 32.90600 -6.36200  0.210 30.70000  ?  198 VAL A O   1 
ATOM   2885 C  CB  A VAL A 1 198 ? 34.66100 29.67000 -6.64400  0.790 35.04000  ?  198 VAL A CB  1 
ATOM   2886 C  CB  B VAL A 1 198 ? 34.53100 29.62400 -6.62600  0.210 34.22000  ?  198 VAL A CB  1 
ATOM   2887 C  CG1 A VAL A 1 198 ? 35.76000 30.44600 -7.36900  0.790 30.67000  ?  198 VAL A CG1 1 
ATOM   2888 C  CG1 B VAL A 1 198 ? 35.61000 30.38100 -7.34100  0.210 30.24000  ?  198 VAL A CG1 1 
ATOM   2889 C  CG2 A VAL A 1 198 ? 35.25800 28.61500 -5.73900  0.790 41.30000  ?  198 VAL A CG2 1 
ATOM   2890 C  CG2 B VAL A 1 198 ? 35.12400 28.50100 -5.80200  0.210 42.77000  ?  198 VAL A CG2 1 
ATOM   2891 N  N   A TYR A 1 199 ? 32.40200 31.75300 -7.52300  0.790 25.85000  ?  199 TYR A N   1 
ATOM   2892 N  N   B TYR A 1 199 ? 32.48000 31.75800 -7.47500  0.210 26.30000  ?  199 TYR A N   1 
ATOM   2893 C  CA  A TYR A 1 199 ? 31.98300 32.89700 -8.32300  0.790 23.39000  ?  199 TYR A CA  1 
ATOM   2894 C  CA  B TYR A 1 199 ? 32.08000 32.94500 -8.22100  0.210 23.14000  ?  199 TYR A CA  1 
ATOM   2895 C  C   A TYR A 1 199 ? 31.51800 34.04200 -7.43300  0.790 25.90000  ?  199 TYR A C   1 
ATOM   2896 C  C   B TYR A 1 199 ? 31.55100 34.04100 -7.29100  0.210 25.67000  ?  199 TYR A C   1 
ATOM   2897 O  O   A TYR A 1 199 ? 31.89400 35.20100 -7.64000  0.790 28.96000  ?  199 TYR A O   1 
ATOM   2898 O  O   B TYR A 1 199 ? 32.07400 35.17400 -7.34100  0.210 31.17000  ?  199 TYR A O   1 
ATOM   2899 C  CB  A TYR A 1 199 ? 30.86600 32.50200 -9.28600  0.790 24.79000  ?  199 TYR A CB  1 
ATOM   2900 C  CB  B TYR A 1 199 ? 31.07500 32.54400 -9.31400  0.210 24.06000  ?  199 TYR A CB  1 
ATOM   2901 C  CG  A TYR A 1 199 ? 30.30500 33.70200 -10.02200 0.790 25.51000  ?  199 TYR A CG  1 
ATOM   2902 C  CG  B TYR A 1 199 ? 30.39700 33.65500 -10.02300 0.210 25.86000  ?  199 TYR A CG  1 
ATOM   2903 C  CD1 A TYR A 1 199 ? 30.95400 34.21600 -11.13700 0.790 25.02000  ?  199 TYR A CD1 1 
ATOM   2904 C  CD1 B TYR A 1 199 ? 29.19900 34.18100 -9.52400  0.210 28.03000  ?  199 TYR A CD1 1 
ATOM   2905 C  CD2 A TYR A 1 199 ? 29.14600 34.33700 -9.58700  0.790 29.01000  ?  199 TYR A CD2 1 
ATOM   2906 C  CD2 B TYR A 1 199 ? 30.90700 34.17900 -11.18500 0.210 22.56000  ?  199 TYR A CD2 1 
ATOM   2907 C  CE1 A TYR A 1 199 ? 30.46400 35.31300 -11.80800 0.790 26.01000  ?  199 TYR A CE1 1 
ATOM   2908 C  CE1 B TYR A 1 199 ? 28.56700 35.22800 -10.15500 0.210 26.58000  ?  199 TYR A CE1 1 
ATOM   2909 C  CE2 A TYR A 1 199 ? 28.64500 35.44200 -10.25300 0.790 25.97000  ?  199 TYR A CE2 1 
ATOM   2910 C  CE2 B TYR A 1 199 ? 30.24200 35.20600 -11.86800 0.210 25.93000  ?  199 TYR A CE2 1 
ATOM   2911 C  CZ  A TYR A 1 199 ? 29.30900 35.92500 -11.36700 0.790 28.13000  ?  199 TYR A CZ  1 
ATOM   2912 C  CZ  B TYR A 1 199 ? 29.07900 35.71400 -11.36500 0.210 28.00000  ?  199 TYR A CZ  1 
ATOM   2913 O  OH  A TYR A 1 199 ? 28.83200 37.02500 -12.04800 0.790 35.20000  ?  199 TYR A OH  1 
ATOM   2914 O  OH  B TYR A 1 199 ? 28.38700 36.74200 -11.99700 0.210 28.76000  ?  199 TYR A OH  1 
ATOM   2915 N  N   A LEU A 1 200 ? 30.69500 33.73200 -6.42700  0.790 24.97000  ?  200 LEU A N   1 
ATOM   2916 N  N   B LEU A 1 200 ? 30.53900 33.71100 -6.42000  0.210 24.20000  ?  200 LEU A N   1 
ATOM   2917 C  CA  A LEU A 1 200 ? 30.15300 34.78000 -5.56400  0.790 18.78000  ?  200 LEU A CA  1 
ATOM   2918 C  CA  B LEU A 1 200 ? 29.99100 34.66900 -5.45100  0.210 18.69000  ?  200 LEU A CA  1 
ATOM   2919 C  C   A LEU A 1 200 ? 31.25400 35.43200 -4.73200  0.790 24.77000  ?  200 LEU A C   1 
ATOM   2920 C  C   B LEU A 1 200 ? 31.10100 35.37300 -4.70600  0.210 23.58000  ?  200 LEU A C   1 
ATOM   2921 O  O   A LEU A 1 200 ? 31.30300 36.66200 -4.60200  0.790 23.97000  ?  200 LEU A O   1 
ATOM   2922 O  O   B LEU A 1 200 ? 31.00500 36.58000 -4.43500  0.210 23.69000  ?  200 LEU A O   1 
ATOM   2923 C  CB  A LEU A 1 200 ? 29.06200 34.20600 -4.65600  0.790 24.52000  ?  200 LEU A CB  1 
ATOM   2924 C  CB  B LEU A 1 200 ? 29.07300 34.00800 -4.41900  0.210 24.90000  ?  200 LEU A CB  1 
ATOM   2925 C  CG  A LEU A 1 200 ? 27.73800 33.83500 -5.32300  0.790 39.65000  ?  200 LEU A CG  1 
ATOM   2926 C  CG  B LEU A 1 200 ? 27.58900 33.55600 -4.64000  0.210 35.76000  ?  200 LEU A CG  1 
ATOM   2927 C  CD1 A LEU A 1 200 ? 26.87000 33.00800 -4.36900  0.790 23.16000  ?  200 LEU A CD1 1 
ATOM   2928 C  CD1 B LEU A 1 200 ? 26.92800 32.91100 -3.41100  0.210 23.16000  ?  200 LEU A CD1 1 
ATOM   2929 C  CD2 A LEU A 1 200 ? 26.97400 35.05900 -5.79400  0.790 28.77000  ?  200 LEU A CD2 1 
ATOM   2930 C  CD2 B LEU A 1 200 ? 26.73900 34.66700 -5.15100  0.210 29.89000  ?  200 LEU A CD2 1 
ATOM   2931 N  N   A ASP A 1 201 ? 32.14400 34.62200 -4.15200  0.790 23.68000  ?  201 ASP A N   1 
ATOM   2932 N  N   B ASP A 1 201 ? 32.19600 34.65700 -4.43400  0.210 22.21000  ?  201 ASP A N   1 
ATOM   2933 C  CA  A ASP A 1 201 ? 33.26200 35.17900 -3.39300  0.790 30.92000  ?  201 ASP A CA  1 
ATOM   2934 C  CA  B ASP A 1 201 ? 33.25900 35.23500 -3.61800  0.210 30.79000  ?  201 ASP A CA  1 
ATOM   2935 C  C   A ASP A 1 201 ? 34.05700 36.16100 -4.24300  0.790 29.38000  ?  201 ASP A C   1 
ATOM   2936 C  C   B ASP A 1 201 ? 34.14800 36.16900 -4.43400  0.210 29.14000  ?  201 ASP A C   1 
ATOM   2937 O  O   A ASP A 1 201 ? 34.37500 37.27100 -3.80300  0.790 30.12000  ?  201 ASP A O   1 
ATOM   2938 O  O   B ASP A 1 201 ? 34.39100 37.32000 -4.02900  0.210 29.03000  ?  201 ASP A O   1 
ATOM   2939 C  CB  A ASP A 1 201 ? 34.17700 34.06100 -2.88800  0.790 28.88000  ?  201 ASP A CB  1 
ATOM   2940 C  CB  B ASP A 1 201 ? 34.02100 34.08300 -2.92500  0.210 28.55000  ?  201 ASP A CB  1 
ATOM   2941 C  CG  A ASP A 1 201 ? 33.61300 33.33700 -1.67700  0.790 28.42000  ?  201 ASP A CG  1 
ATOM   2942 C  CG  B ASP A 1 201 ? 33.12100 33.34000 -1.90600  0.210 28.32000  ?  201 ASP A CG  1 
ATOM   2943 O  OD1 A ASP A 1 201 ? 32.54200 33.74200 -1.17700  0.790 33.97000  ?  201 ASP A OD1 1 
ATOM   2944 O  OD1 B ASP A 1 201 ? 32.02800 33.89400 -1.57000  0.210 27.92000  ?  201 ASP A OD1 1 
ATOM   2945 O  OD2 A ASP A 1 201 ? 34.24900 32.36000 -1.22700  0.790 35.01000  -1 201 ASP A OD2 1 
ATOM   2946 O  OD2 B ASP A 1 201 ? 33.45900 32.22200 -1.50500  0.210 28.90000  -1 201 ASP A OD2 1 
ATOM   2947 N  N   A LEU A 1 202 ? 34.39300 35.76200 -5.47100  0.790 25.96000  ?  202 LEU A N   1 
ATOM   2948 N  N   B LEU A 1 202 ? 34.55600 35.72800 -5.62700  0.210 26.45000  ?  202 LEU A N   1 
ATOM   2949 C  CA  A LEU A 1 202 ? 35.18200 36.63200 -6.33600  0.790 27.86000  ?  202 LEU A CA  1 
ATOM   2950 C  CA  B LEU A 1 202 ? 35.22300 36.62800 -6.56300  0.210 27.56000  ?  202 LEU A CA  1 
ATOM   2951 C  C   A LEU A 1 202 ? 34.45500 37.94200 -6.61800  0.790 27.65000  ?  202 LEU A C   1 
ATOM   2952 C  C   B LEU A 1 202 ? 34.36600 37.85100 -6.81500  0.210 26.20000  ?  202 LEU A C   1 
ATOM   2953 O  O   A LEU A 1 202 ? 35.07400 39.01200 -6.61800  0.790 28.98000  ?  202 LEU A O   1 
ATOM   2954 O  O   B LEU A 1 202 ? 34.82800 38.99100 -6.68200  0.210 26.71000  ?  202 LEU A O   1 
ATOM   2955 C  CB  A LEU A 1 202 ? 35.51700 35.90700 -7.63800  0.790 26.78000  ?  202 LEU A CB  1 
ATOM   2956 C  CB  B LEU A 1 202 ? 35.50900 35.89500 -7.87100  0.210 26.62000  ?  202 LEU A CB  1 
ATOM   2957 C  CG  A LEU A 1 202 ? 36.60500 34.83600 -7.54200  0.790 31.29000  ?  202 LEU A CG  1 
ATOM   2958 C  CG  B LEU A 1 202 ? 36.35600 34.62800 -7.66600  0.210 28.96000  ?  202 LEU A CG  1 
ATOM   2959 C  CD1 A LEU A 1 202 ? 36.70700 34.03400 -8.83300  0.790 32.20000  ?  202 LEU A CD1 1 
ATOM   2960 C  CD1 B LEU A 1 202 ? 36.40100 33.66100 -8.86700  0.210 32.91000  ?  202 LEU A CD1 1 
ATOM   2961 C  CD2 A LEU A 1 202 ? 37.95800 35.44900 -7.18700  0.790 30.49000  ?  202 LEU A CD2 1 
ATOM   2962 C  CD2 B LEU A 1 202 ? 37.83300 34.96900 -7.14900  0.210 31.94000  ?  202 LEU A CD2 1 
ATOM   2963 N  N   A VAL A 1 203 ? 33.14100 37.89000 -6.84700  0.790 28.09000  ?  203 VAL A N   1 
ATOM   2964 N  N   B VAL A 1 203 ? 33.07100 37.62300 -7.06200  0.210 26.91000  ?  203 VAL A N   1 
ATOM   2965 C  CA  A VAL A 1 203 ? 32.42800 39.11500 -7.20300  0.790 30.14000  ?  203 VAL A CA  1 
ATOM   2966 C  CA  B VAL A 1 203 ? 32.13600 38.74000 -7.21300  0.210 29.11000  ?  203 VAL A CA  1 
ATOM   2967 C  C   A VAL A 1 203 ? 32.22500 40.00000 -5.97500  0.790 27.49000  ?  203 VAL A C   1 
ATOM   2968 C  C   B VAL A 1 203 ? 32.06400 39.58100 -5.94000  0.210 27.09000  ?  203 VAL A C   1 
ATOM   2969 O  O   A VAL A 1 203 ? 32.38500 41.22500 -6.04600  0.790 32.26000  ?  203 VAL A O   1 
ATOM   2970 O  O   B VAL A 1 203 ? 32.20700 40.80600 -6.00700  0.210 30.65000  ?  203 VAL A O   1 
ATOM   2971 C  CB  A VAL A 1 203 ? 31.09000 38.79200 -7.89300  0.790 28.34000  ?  203 VAL A CB  1 
ATOM   2972 C  CB  B VAL A 1 203 ? 30.73400 38.26300 -7.63200  0.210 24.57000  ?  203 VAL A CB  1 
ATOM   2973 C  CG1 A VAL A 1 203 ? 30.29200 40.07400 -8.11700  0.790 26.41000  ?  203 VAL A CG1 1 
ATOM   2974 C  CG1 B VAL A 1 203 ? 29.93100 39.42700 -7.78700  0.210 23.29000  ?  203 VAL A CG1 1 
ATOM   2975 C  CG2 A VAL A 1 203 ? 31.32100 38.07800 -9.21700  0.790 23.52000  ?  203 VAL A CG2 1 
ATOM   2976 C  CG2 B VAL A 1 203 ? 30.75900 37.63000 -9.01100  0.210 26.34000  ?  203 VAL A CG2 1 
ATOM   2977 N  N   A THR A 1 204 ? 31.86800 39.40600 -4.83200  0.790 25.39000  ?  204 THR A N   1 
ATOM   2978 N  N   B THR A 1 204 ? 31.80500 38.95300 -4.75700  0.210 23.28000  ?  204 THR A N   1 
ATOM   2979 C  CA  A THR A 1 204 ? 31.61600 40.21700 -3.64400  0.790 25.99000  ?  204 THR A CA  1 
ATOM   2980 C  CA  B THR A 1 204 ? 31.55500 39.80200 -3.58100  0.210 26.08000  ?  204 THR A CA  1 
ATOM   2981 C  C   A THR A 1 204 ? 32.89200 40.77100 -3.02200  0.790 25.36000  ?  204 THR A C   1 
ATOM   2982 C  C   B THR A 1 204 ? 32.81900 40.47900 -3.09200  0.210 25.80000  ?  204 THR A C   1 
ATOM   2983 O  O   A THR A 1 204 ? 32.80400 41.64300 -2.15000  0.790 33.51000  ?  204 THR A O   1 
ATOM   2984 O  O   B THR A 1 204 ? 32.71500 41.59900 -2.58900  0.210 28.27000  ?  204 THR A O   1 
ATOM   2985 C  CB  A THR A 1 204 ? 30.86000 39.42100 -2.57300  0.790 26.49000  ?  204 THR A CB  1 
ATOM   2986 C  CB  B THR A 1 204 ? 30.95200 39.07500 -2.40000  0.210 27.41000  ?  204 THR A CB  1 
ATOM   2987 O  OG1 A THR A 1 204 ? 31.65700 38.30900 -2.14900  0.790 30.44000  ?  204 THR A OG1 1 
ATOM   2988 O  OG1 B THR A 1 204 ? 31.85300 38.08300 -1.90600  0.210 27.09000  ?  204 THR A OG1 1 
ATOM   2989 C  CG2 A THR A 1 204 ? 29.52800 38.92900 -3.10600  0.790 25.19000  ?  204 THR A CG2 1 
ATOM   2990 C  CG2 B THR A 1 204 ? 29.61200 38.44300 -2.75900  0.210 25.38000  ?  204 THR A CG2 1 
ATOM   2991 N  N   A LYS A 1 205 ? 34.06200 40.27900 -3.42400  0.790 29.82000  ?  205 LYS A N   1 
ATOM   2992 N  N   B LYS A 1 205 ? 33.99800 39.91700 -3.35700  0.210 28.11000  ?  205 LYS A N   1 
ATOM   2993 C  CA  A LYS A 1 205 ? 35.33400 40.77600 -2.91600  0.790 26.39000  ?  205 LYS A CA  1 
ATOM   2994 C  CA  B LYS A 1 205 ? 35.24500 40.50800 -2.80000  0.210 27.83000  ?  205 LYS A CA  1 
ATOM   2995 C  C   A LYS A 1 205 ? 36.13000 41.49900 -3.99500  0.790 31.95000  ?  205 LYS A C   1 
ATOM   2996 C  C   B LYS A 1 205 ? 36.01700 41.30400 -3.87000  0.210 31.71000  ?  205 LYS A C   1 
ATOM   2997 O  O   A LYS A 1 205 ? 36.37500 42.70200 -3.87900  0.790 35.85000  ?  205 LYS A O   1 
ATOM   2998 O  O   B LYS A 1 205 ? 36.21100 42.52100 -3.66700  0.210 32.46000  ?  205 LYS A O   1 
ATOM   2999 C  CB  A LYS A 1 205 ? 36.15400 39.61900 -2.32700  0.790 28.26000  ?  205 LYS A CB  1 
ATOM   3000 C  CB  B LYS A 1 205 ? 36.10300 39.39600 -2.18700  0.210 28.82000  ?  205 LYS A CB  1 
ATOM   3001 C  CG  A LYS A 1 205 ? 35.55600 39.01100 -1.06400  0.790 26.71000  ?  205 LYS A CG  1 
ATOM   3002 C  CG  B LYS A 1 205 ? 35.46600 38.67400 -1.00400  0.210 26.08000  ?  205 LYS A CG  1 
ATOM   3003 C  CD  A LYS A 1 205 ? 36.43200 37.89500 -0.51000  0.790 33.10000  ?  205 LYS A CD  1 
ATOM   3004 C  CD  B LYS A 1 205 ? 35.93700 37.23300 -0.85700  0.210 30.67000  ?  205 LYS A CD  1 
ATOM   3005 C  CE  A LYS A 1 205 ? 36.01400 37.51400 0.90200   0.790 23.31000  ?  205 LYS A CE  1 
ATOM   3006 C  CE  B LYS A 1 205 ? 35.47500 36.55300 0.39500   0.210 23.28000  ?  205 LYS A CE  1 
ATOM   3007 N  NZ  A LYS A 1 205 ? 34.86100 36.56600 0.89700   0.790 23.57000  ?  205 LYS A NZ  1 
ATOM   3008 N  NZ  B LYS A 1 205 ? 34.20000 35.85400 0.18100   0.210 21.44000  ?  205 LYS A NZ  1 
ATOM   3009 N  N   A VAL A 1 206 ? 36.54300 40.79600 -5.05200  0.790 34.51000  ?  206 VAL A N   1 
ATOM   3010 N  N   B VAL A 1 206 ? 36.44100 40.65700 -4.95800  0.210 33.30000  ?  206 VAL A N   1 
ATOM   3011 C  CA  A VAL A 1 206 ? 37.37000 41.42300 -6.07900  0.790 29.70000  ?  206 VAL A CA  1 
ATOM   3012 C  CA  B VAL A 1 206 ? 37.28800 41.33900 -5.98600  0.210 30.81000  ?  206 VAL A CA  1 
ATOM   3013 C  C   A VAL A 1 206 ? 36.54200 42.35500 -6.95200  0.790 31.85000  ?  206 VAL A C   1 
ATOM   3014 C  C   B VAL A 1 206 ? 36.45500 42.34100 -6.80500  0.210 32.42000  ?  206 VAL A C   1 
ATOM   3015 O  O   A VAL A 1 206 ? 36.97800 43.46400 -7.27300  0.790 32.14000  ?  206 VAL A O   1 
ATOM   3016 O  O   B VAL A 1 206 ? 36.87700 43.51000 -6.91100  0.210 27.51000  ?  206 VAL A O   1 
ATOM   3017 C  CB  A VAL A 1 206 ? 38.08300 40.34600 -6.91700  0.790 42.55000  ?  206 VAL A CB  1 
ATOM   3018 C  CB  B VAL A 1 206 ? 37.96300 40.28900 -6.88800  0.210 41.81000  ?  206 VAL A CB  1 
ATOM   3019 C  CG1 A VAL A 1 206 ? 38.93500 40.98300 -8.00500  0.790 39.26000  ?  206 VAL A CG1 1 
ATOM   3020 C  CG1 B VAL A 1 206 ? 39.01300 40.90900 -7.79700  0.210 39.35000  ?  206 VAL A CG1 1 
ATOM   3021 C  CG2 A VAL A 1 206 ? 38.92400 39.44800 -6.01300  0.790 28.76000  ?  206 VAL A CG2 1 
ATOM   3022 C  CG2 B VAL A 1 206 ? 38.56600 39.15400 -6.06900  0.210 28.48000  ?  206 VAL A CG2 1 
ATOM   3023 N  N   A GLY A 1 207 ? 35.34600 41.92900 -7.35800  0.790 31.79000  ?  207 GLY A N   1 
ATOM   3024 N  N   B GLY A 1 207 ? 35.33100 41.89900 -7.37100  0.210 31.40000  ?  207 GLY A N   1 
ATOM   3025 C  CA  A GLY A 1 207 ? 34.48300 42.82500 -8.11200  0.790 29.98000  ?  207 GLY A CA  1 
ATOM   3026 C  CA  B GLY A 1 207 ? 34.46700 42.80400 -8.15400  0.210 30.73000  ?  207 GLY A CA  1 
ATOM   3027 C  C   A GLY A 1 207 ? 34.13700 44.07100 -7.32300  0.790 40.67000  ?  207 GLY A C   1 
ATOM   3028 C  C   B GLY A 1 207 ? 34.16600 44.06900 -7.37700  0.210 36.71000  ?  207 GLY A C   1 
ATOM   3029 O  O   A GLY A 1 207 ? 34.28600 45.19400 -7.80900  0.790 42.35000  ?  207 GLY A O   1 
ATOM   3030 O  O   B GLY A 1 207 ? 34.40500 45.16600 -7.92100  0.210 42.02000  ?  207 GLY A O   1 
ATOM   3031 N  N   A PHE A 1 208 ? 33.65400 43.88200 -6.09400  0.790 37.78000  ?  208 PHE A N   1 
ATOM   3032 N  N   B PHE A 1 208 ? 33.66100 43.92700 -6.15100  0.210 31.63000  ?  208 PHE A N   1 
ATOM   3033 C  CA  A PHE A 1 208 ? 33.49600 44.96500 -5.12900  0.790 30.98000  ?  208 PHE A CA  1 
ATOM   3034 C  CA  B PHE A 1 208 ? 33.36400 45.09300 -5.27900  0.210 38.09000  ?  208 PHE A CA  1 
ATOM   3035 C  C   A PHE A 1 208 ? 34.68300 45.91600 -5.16100  0.790 39.89000  ?  208 PHE A C   1 
ATOM   3036 C  C   B PHE A 1 208 ? 34.52000 46.08100 -5.31400  0.210 42.28000  ?  208 PHE A C   1 
ATOM   3037 O  O   A PHE A 1 208 ? 34.52200 47.12600 -5.35500  0.790 31.85000  ?  208 PHE A O   1 
ATOM   3038 O  O   B PHE A 1 208 ? 34.30400 47.28000 -5.58700  0.210 48.95000  ?  208 PHE A O   1 
ATOM   3039 C  CB  A PHE A 1 208 ? 33.31700 44.32400 -3.74500  0.790 31.32000  ?  208 PHE A CB  1 
ATOM   3040 C  CB  B PHE A 1 208 ? 33.16500 44.47600 -3.89500  0.210 34.38000  ?  208 PHE A CB  1 
ATOM   3041 C  CG  A PHE A 1 208 ? 32.99000 45.28000 -2.63600  0.790 35.09000  ?  208 PHE A CG  1 
ATOM   3042 C  CG  B PHE A 1 208 ? 32.85600 45.42000 -2.74200  0.210 34.76000  ?  208 PHE A CG  1 
ATOM   3043 C  CD1 A PHE A 1 208 ? 33.99800 45.91700 -1.93200  0.790 33.67000  ?  208 PHE A CD1 1 
ATOM   3044 C  CD1 B PHE A 1 208 ? 31.54800 45.79100 -2.45800  0.210 35.61000  ?  208 PHE A CD1 1 
ATOM   3045 C  CD2 A PHE A 1 208 ? 31.67600 45.49000 -2.25300  0.790 36.62000  ?  208 PHE A CD2 1 
ATOM   3046 C  CD2 B PHE A 1 208 ? 33.87100 45.90300 -1.92400  0.210 33.29000  ?  208 PHE A CD2 1 
ATOM   3047 C  CE1 A PHE A 1 208 ? 33.70000 46.77700 -0.89300  0.790 34.91000  ?  208 PHE A CE1 1 
ATOM   3048 C  CE1 B PHE A 1 208 ? 31.26700 46.63800 -1.39900  0.210 34.59000  ?  208 PHE A CE1 1 
ATOM   3049 C  CE2 A PHE A 1 208 ? 31.37100 46.34900 -1.21400  0.790 35.43000  ?  208 PHE A CE2 1 
ATOM   3050 C  CE2 B PHE A 1 208 ? 33.58400 46.74900 -0.86700  0.210 32.93000  ?  208 PHE A CE2 1 
ATOM   3051 C  CZ  A PHE A 1 208 ? 32.38500 46.99300 -0.53200  0.790 35.59000  ?  208 PHE A CZ  1 
ATOM   3052 C  CZ  B PHE A 1 208 ? 32.28400 47.11400 -0.60700  0.210 36.48000  ?  208 PHE A CZ  1 
ATOM   3053 N  N   A GLY A 1 209 ? 35.88800 45.37500 -4.99500  0.790 43.97000  ?  209 GLY A N   1 
ATOM   3054 N  N   B GLY A 1 209 ? 35.72800 45.59500 -5.03100  0.210 39.96000  ?  209 GLY A N   1 
ATOM   3055 C  CA  A GLY A 1 209 ? 37.06300 46.22400 -4.93400  0.790 30.37000  ?  209 GLY A CA  1 
ATOM   3056 C  CA  B GLY A 1 209 ? 36.90200 46.48300 -4.97600  0.210 35.30000  ?  209 GLY A CA  1 
ATOM   3057 C  C   A GLY A 1 209 ? 37.27200 47.03700 -6.19600  0.790 45.21000  ?  209 GLY A C   1 
ATOM   3058 C  C   B GLY A 1 209 ? 37.13200 47.21400 -6.28100  0.210 44.86000  ?  209 GLY A C   1 
ATOM   3059 O  O   A GLY A 1 209 ? 37.56800 48.23300 -6.13200  0.790 46.36000  ?  209 GLY A O   1 
ATOM   3060 O  O   B GLY A 1 209 ? 37.43900 48.41600 -6.23300  0.210 45.03000  ?  209 GLY A O   1 
ATOM   3061 N  N   A PHE A 1 210 ? 37.11800 46.40600 -7.36100  0.790 44.99000  ?  210 PHE A N   1 
ATOM   3062 N  N   B PHE A 1 210 ? 37.02100 46.51400 -7.40800  0.210 47.25000  ?  210 PHE A N   1 
ATOM   3063 C  CA  A PHE A 1 210 ? 37.39500 47.11600 -8.60300  0.790 43.06000  ?  210 PHE A CA  1 
ATOM   3064 C  CA  B PHE A 1 210 ? 37.31200 47.15200 -8.71900  0.210 44.36000  ?  210 PHE A CA  1 
ATOM   3065 C  C   A PHE A 1 210 ? 36.36600 48.20600 -8.86900  0.790 40.05000  ?  210 PHE A C   1 
ATOM   3066 C  C   B PHE A 1 210 ? 36.31300 48.28500 -8.94900  0.210 44.76000  ?  210 PHE A C   1 
ATOM   3067 O  O   A PHE A 1 210 ? 36.70500 49.24000 -9.45500  0.790 49.46000  ?  210 PHE A O   1 
ATOM   3068 O  O   B PHE A 1 210 ? 36.71500 49.33900 -9.47600  0.210 49.62000  ?  210 PHE A O   1 
ATOM   3069 C  CB  A PHE A 1 210 ? 37.46400 46.12800 -9.76500  0.790 38.11000  ?  210 PHE A CB  1 
ATOM   3070 C  CB  B PHE A 1 210 ? 37.33500 46.06000 -9.79100  0.210 36.21000  ?  210 PHE A CB  1 
ATOM   3071 C  CG  A PHE A 1 210 ? 38.81200 45.48200 -9.91900  0.790 37.60000  ?  210 PHE A CG  1 
ATOM   3072 C  CG  B PHE A 1 210 ? 38.68700 45.36500 -9.85400  0.210 40.18000  ?  210 PHE A CG  1 
ATOM   3073 C  CD1 A PHE A 1 210 ? 39.94500 46.25100 -10.14300 0.790 54.93000  ?  210 PHE A CD1 1 
ATOM   3074 C  CD1 B PHE A 1 210 ? 39.86200 46.10100 -9.77200  0.210 50.49000  ?  210 PHE A CD1 1 
ATOM   3075 C  CD2 A PHE A 1 210 ? 38.95100 44.11000 -9.82600  0.790 51.59000  ?  210 PHE A CD2 1 
ATOM   3076 C  CD2 B PHE A 1 210 ? 38.78100 43.98500 -9.97300  0.210 49.04000  ?  210 PHE A CD2 1 
ATOM   3077 C  CE1 A PHE A 1 210 ? 41.18400 45.66200 -10.28000 0.790 58.78000  ?  210 PHE A CE1 1 
ATOM   3078 C  CE1 B PHE A 1 210 ? 41.09600 45.47300 -9.82000  0.210 56.33000  ?  210 PHE A CE1 1 
ATOM   3079 C  CE2 A PHE A 1 210 ? 40.19100 43.51400 -9.96200  0.790 54.71000  ?  210 PHE A CE2 1 
ATOM   3080 C  CE2 B PHE A 1 210 ? 40.01800 43.36400 -10.02400 0.210 54.13000  ?  210 PHE A CE2 1 
ATOM   3081 C  CZ  A PHE A 1 210 ? 41.30900 44.29200 -10.18900 0.790 44.96000  ?  210 PHE A CZ  1 
ATOM   3082 C  CZ  B PHE A 1 210 ? 41.17100 44.10700 -9.94500  0.210 45.81000  ?  210 PHE A CZ  1 
ATOM   3083 N  N   A ILE A 1 211 ? 35.11600 48.01000 -8.44400  0.790 51.23000  ?  211 ILE A N   1 
ATOM   3084 N  N   B ILE A 1 211 ? 35.05400 48.08700 -8.55200  0.210 47.87000  ?  211 ILE A N   1 
ATOM   3085 C  CA  A ILE A 1 211 ? 34.14100 49.09000 -8.56000  0.790 46.06000  ?  211 ILE A CA  1 
ATOM   3086 C  CA  B ILE A 1 211 ? 34.04600 49.18300 -8.66300  0.210 43.67000  ?  211 ILE A CA  1 
ATOM   3087 C  C   A ILE A 1 211 ? 34.57000 50.28100 -7.71500  0.790 56.45000  ?  211 ILE A C   1 
ATOM   3088 C  C   B ILE A 1 211 ? 34.54600 50.37800 -7.83500  0.210 51.18000  ?  211 ILE A C   1 
ATOM   3089 O  O   A ILE A 1 211 ? 34.33600 51.43500 -8.09100  0.790 52.78000  ?  211 ILE A O   1 
ATOM   3090 O  O   B ILE A 1 211 ? 34.57200 51.50900 -8.36800  0.210 59.02000  ?  211 ILE A O   1 
ATOM   3091 C  CB  A ILE A 1 211 ? 32.73600 48.60000 -8.16400  0.790 44.30000  ?  211 ILE A CB  1 
ATOM   3092 C  CB  B ILE A 1 211 ? 32.66200 48.70100 -8.19500  0.210 48.58000  ?  211 ILE A CB  1 
ATOM   3093 C  CG1 A ILE A 1 211 ? 32.18400 47.64300 -9.22000  0.790 42.19000  ?  211 ILE A CG1 1 
ATOM   3094 C  CG1 B ILE A 1 211 ? 32.14100 47.56900 -9.07500  0.210 39.50000  ?  211 ILE A CG1 1 
ATOM   3095 C  CG2 A ILE A 1 211 ? 31.79900 49.78600 -7.97800  0.790 41.46000  ?  211 ILE A CG2 1 
ATOM   3096 C  CG2 B ILE A 1 211 ? 31.67000 49.86200 -8.12000  0.210 44.18000  ?  211 ILE A CG2 1 
ATOM   3097 C  CD1 A ILE A 1 211 ? 31.10600 46.71800 -8.69400  0.790 47.93000  ?  211 ILE A CD1 1 
ATOM   3098 C  CD1 B ILE A 1 211 ? 31.18600 46.62700 -8.36700  0.210 46.96000  ?  211 ILE A CD1 1 
ATOM   3099 N  N   A ALA A 1 212 ? 35.20300 50.02800 -6.56600  0.790 65.54000  ?  212 ALA A N   1 
ATOM   3100 N  N   B ALA A 1 212 ? 34.94200 50.13000 -6.58600  0.210 51.92000  ?  212 ALA A N   1 
ATOM   3101 C  CA  A ALA A 1 212 ? 35.68800 51.12400 -5.73600  0.790 63.91000  ?  212 ALA A CA  1 
ATOM   3102 C  CA  B ALA A 1 212 ? 35.49100 51.21600 -5.74000  0.210 62.48000  ?  212 ALA A CA  1 
ATOM   3103 C  C   A ALA A 1 212 ? 36.86400 51.82900 -6.40000  0.790 56.59000  ?  212 ALA A C   1 
ATOM   3104 C  C   B ALA A 1 212 ? 36.65200 51.88900 -6.47300  0.210 56.37000  ?  212 ALA A C   1 
ATOM   3105 O  O   A ALA A 1 212 ? 36.91000 53.06300 -6.45600  0.790 66.66000  ?  212 ALA A O   1 
ATOM   3106 O  O   B ALA A 1 212 ? 36.63900 53.12800 -6.62000  0.210 62.47000  ?  212 ALA A O   1 
ATOM   3107 C  CB  A ALA A 1 212 ? 36.07800 50.60100 -4.35300  0.790 40.89000  ?  212 ALA A CB  1 
ATOM   3108 C  CB  B ALA A 1 212 ? 35.92400 50.65800 -4.40400  0.210 47.10000  ?  212 ALA A CB  1 
ATOM   3109 N  N   A LEU A 1 213 ? 37.82200 51.05800 -6.92200  0.790 52.50000  ?  213 LEU A N   1 
ATOM   3110 N  N   B LEU A 1 213 ? 37.62200 51.09300 -6.93000  0.210 56.17000  ?  213 LEU A N   1 
ATOM   3111 C  CA  A LEU A 1 213 ? 38.95200 51.66100 -7.62200  0.790 53.57000  ?  213 LEU A CA  1 
ATOM   3112 C  CA  B LEU A 1 213 ? 38.80100 51.65000 -7.64100  0.210 54.75000  ?  213 LEU A CA  1 
ATOM   3113 C  C   A LEU A 1 213 ? 38.47200 52.54500 -8.76700  0.790 68.66000  ?  213 LEU A C   1 
ATOM   3114 C  C   B LEU A 1 213 ? 38.31400 52.52700 -8.79900  0.210 64.03000  ?  213 LEU A C   1 
ATOM   3115 O  O   A LEU A 1 213 ? 38.95300 53.67100 -8.94500  0.790 73.00000  ?  213 LEU A O   1 
ATOM   3116 O  O   B LEU A 1 213 ? 38.83800 53.65000 -8.95600  0.210 68.31000  ?  213 LEU A O   1 
ATOM   3117 C  CB  A LEU A 1 213 ? 39.88400 50.57600 -8.15700  0.790 52.86000  ?  213 LEU A CB  1 
ATOM   3118 C  CB  B LEU A 1 213 ? 39.67400 50.51500 -8.17100  0.210 52.96000  ?  213 LEU A CB  1 
ATOM   3119 C  CG  A LEU A 1 213 ? 40.71700 49.75700 -7.17500  0.790 71.18000  ?  213 LEU A CG  1 
ATOM   3120 C  CG  B LEU A 1 213 ? 40.41900 49.66500 -7.13800  0.210 66.37000  ?  213 LEU A CG  1 
ATOM   3121 C  CD1 A LEU A 1 213 ? 41.74000 48.92500 -7.96300  0.790 60.62000  ?  213 LEU A CD1 1 
ATOM   3122 C  CD1 B LEU A 1 213 ? 41.73800 49.20200 -7.72900  0.210 60.83000  ?  213 LEU A CD1 1 
ATOM   3123 C  CD2 A LEU A 1 213 ? 41.41100 50.62200 -6.15400  0.790 58.38000  ?  213 LEU A CD2 1 
ATOM   3124 C  CD2 B LEU A 1 213 ? 40.64600 50.39400 -5.82800  0.210 57.81000  ?  213 LEU A CD2 1 
ATOM   3125 N  N   A ASP A 1 214 ? 37.52600 52.04000 -9.56300  0.790 63.14000  ?  214 ASP A N   1 
ATOM   3126 N  N   B ASP A 1 214 ? 37.34100 52.03700 -9.56800  0.210 63.61000  ?  214 ASP A N   1 
ATOM   3127 C  CA  A ASP A 1 214 ? 37.03500 52.80000 -10.70700 0.790 67.37000  ?  214 ASP A CA  1 
ATOM   3128 C  CA  B ASP A 1 214 ? 36.86700 52.77200 -10.77400 0.210 67.60000  ?  214 ASP A CA  1 
ATOM   3129 C  C   A ASP A 1 214 ? 36.52600 54.17000 -10.28200 0.790 73.46000  ?  214 ASP A C   1 
ATOM   3130 C  C   B ASP A 1 214 ? 36.50300 54.21800 -10.40900 0.210 75.57000  ?  214 ASP A C   1 
ATOM   3131 O  O   A ASP A 1 214 ? 36.76800 55.17200 -10.96600 0.790 91.63000  ?  214 ASP A O   1 
ATOM   3132 O  O   B ASP A 1 214 ? 36.82100 55.11800 -11.21400 0.210 86.09000  ?  214 ASP A O   1 
ATOM   3133 C  CB  A ASP A 1 214 ? 35.93000 52.01600 -11.41500 0.790 64.71000  ?  214 ASP A CB  1 
ATOM   3134 C  CB  B ASP A 1 214 ? 35.77900 51.97300 -11.47900 0.210 65.67000  ?  214 ASP A CB  1 
ATOM   3135 C  CG  A ASP A 1 214 ? 35.55600 52.61800 -12.75200 0.790 76.19000  ?  214 ASP A CG  1 
ATOM   3136 C  CG  B ASP A 1 214 ? 34.49200 52.71700 -11.79400 0.210 77.58000  ?  214 ASP A CG  1 
ATOM   3137 O  OD1 A ASP A 1 214 ? 36.46600 52.86300 -13.56900 0.790 80.41000  ?  214 ASP A OD1 1 
ATOM   3138 O  OD1 B ASP A 1 214 ? 33.61100 52.76500 -10.91100 0.210 83.40000  ?  214 ASP A OD1 1 
ATOM   3139 O  OD2 A ASP A 1 214 ? 34.35000 52.84900 -12.98400 0.790 80.40000  -1 214 ASP A OD2 1 
ATOM   3140 O  OD2 B ASP A 1 214 ? 34.38500 53.24700 -12.91800 0.210 77.00000  -1 214 ASP A OD2 1 
ATOM   3141 N  N   A ALA A 1 215 ? 35.81800 54.23600 -9.15300  0.790 74.65000  ?  215 ALA A N   1 
ATOM   3142 N  N   B ALA A 1 215 ? 35.86200 54.43600 -9.25800  0.210 74.09000  ?  215 ALA A N   1 
ATOM   3143 C  CA  A ALA A 1 215 ? 35.27600 55.51000 -8.69900  0.790 72.25000  ?  215 ALA A CA  1 
ATOM   3144 C  CA  B ALA A 1 215 ? 35.45000 55.80400 -8.85700  0.210 71.75000  ?  215 ALA A CA  1 
ATOM   3145 C  C   A ALA A 1 215 ? 36.36200 56.41100 -8.12500  0.790 77.84000  ?  215 ALA A C   1 
ATOM   3146 C  C   B ALA A 1 215 ? 36.68800 56.68500 -8.68800  0.210 77.82000  ?  215 ALA A C   1 
ATOM   3147 O  O   A ALA A 1 215 ? 36.25600 57.64000 -8.21400  0.790 79.69000  ?  215 ALA A O   1 
ATOM   3148 O  O   B ALA A 1 215 ? 36.90100 57.58800 -9.52600  0.210 80.89000  ?  215 ALA A O   1 
ATOM   3149 C  CB  A ALA A 1 215 ? 34.17700 55.27200 -7.66300  0.790 61.53000  ?  215 ALA A CB  1 
ATOM   3150 C  CB  B ALA A 1 215 ? 34.63700 55.73900 -7.58600  0.210 67.46000  ?  215 ALA A CB  1 
ATOM   3151 N  N   A ALA A 1 216 ? 37.41100 55.82700 -7.54200  0.790 72.23000  ?  216 ALA A N   1 
ATOM   3152 N  N   B ALA A 1 216 ? 37.47100 56.44600 -7.63700  0.210 74.52000  ?  216 ALA A N   1 
ATOM   3153 C  CA  A ALA A 1 216 ? 38.47900 56.63000 -6.95800  0.790 79.46000  ?  216 ALA A CA  1 
ATOM   3154 C  CA  B ALA A 1 216 ? 38.70900 57.18600 -7.37000  0.210 78.59000  ?  216 ALA A CA  1 
ATOM   3155 C  C   A ALA A 1 216 ? 39.26400 57.40400 -8.01000  0.790 81.63000  ?  216 ALA A C   1 
ATOM   3156 C  C   B ALA A 1 216 ? 39.41600 57.64800 -8.64300  0.210 82.74000  ?  216 ALA A C   1 
ATOM   3157 O  O   A ALA A 1 216 ? 39.90500 58.40600 -7.67300  0.790 91.61000  ?  216 ALA A O   1 
ATOM   3158 O  O   B ALA A 1 216 ? 40.53700 58.15700 -8.59000  0.210 85.93000  ?  216 ALA A O   1 
ATOM   3159 C  CB  A ALA A 1 216 ? 39.43100 55.74100 -6.15500  0.790 71.55000  ?  216 ALA A CB  1 
ATOM   3160 C  CB  B ALA A 1 216 ? 39.65800 56.33000 -6.52200  0.210 74.39000  ?  216 ALA A CB  1 
HETATM 3161 C  C1  A RET B 2 .   ? 25.06100 31.73800 5.61700   0.820 41.83000  ?  301 RET A C1  1 
HETATM 3162 C  C1  B RET B 2 .   ? 24.77700 31.82500 5.35200   0.180 35.24000  ?  301 RET A C1  1 
HETATM 3163 C  C2  A RET B 2 .   ? 24.20700 30.70600 6.36900   0.820 25.06000  ?  301 RET A C2  1 
HETATM 3164 C  C2  B RET B 2 .   ? 23.68400 30.86400 5.83600   0.180 29.70000  ?  301 RET A C2  1 
HETATM 3165 C  C3  A RET B 2 .   ? 23.32200 31.28700 7.45900   0.820 28.43000  ?  301 RET A C3  1 
HETATM 3166 C  C3  B RET B 2 .   ? 22.73700 31.45400 6.86300   0.180 29.59000  ?  301 RET A C3  1 
HETATM 3167 C  C4  A RET B 2 .   ? 22.41300 32.36800 6.91000   0.820 29.36000  ?  301 RET A C4  1 
HETATM 3168 C  C4  B RET B 2 .   ? 22.08000 32.73200 6.36900   0.180 29.64000  ?  301 RET A C4  1 
HETATM 3169 C  C5  A RET B 2 .   ? 23.06800 33.26700 5.89500   0.820 30.43000  ?  301 RET A C5  1 
HETATM 3170 C  C5  B RET B 2 .   ? 22.94200 33.55400 5.44700   0.180 29.54000  ?  301 RET A C5  1 
HETATM 3171 C  C6  A RET B 2 .   ? 24.32800 33.07800 5.46400   0.820 34.44000  ?  301 RET A C6  1 
HETATM 3172 C  C6  B RET B 2 .   ? 24.22700 33.25700 5.18600   0.180 31.30000  ?  301 RET A C6  1 
HETATM 3173 C  C7  A RET B 2 .   ? 25.02200 34.13200 4.73900   0.820 22.89000  ?  301 RET A C7  1 
HETATM 3174 C  C7  B RET B 2 .   ? 25.04300 34.22100 4.45800   0.180 24.02000  ?  301 RET A C7  1 
HETATM 3175 C  C8  A RET B 2 .   ? 26.22600 34.09700 4.11300   0.820 29.68000  ?  301 RET A C8  1 
HETATM 3176 C  C8  B RET B 2 .   ? 26.37100 34.34400 4.07900   0.180 29.68000  ?  301 RET A C8  1 
HETATM 3177 C  C9  A RET B 2 .   ? 26.86500 35.20400 3.41500   0.820 30.98000  ?  301 RET A C9  1 
HETATM 3178 C  C9  B RET B 2 .   ? 26.96700 35.46200 3.31400   0.180 28.51000  ?  301 RET A C9  1 
HETATM 3179 C  C10 A RET B 2 .   ? 28.14100 35.05500 2.98000   0.820 23.21000  ?  301 RET A C10 1 
HETATM 3180 C  C10 B RET B 2 .   ? 28.32300 35.53600 3.15700   0.180 25.03000  ?  301 RET A C10 1 
HETATM 3181 C  C11 A RET B 2 .   ? 28.96200 36.03200 2.32100   0.820 21.84000  ?  301 RET A C11 1 
HETATM 3182 C  C11 B RET B 2 .   ? 29.08000 36.55000 2.47000   0.180 25.06000  ?  301 RET A C11 1 
HETATM 3183 C  C12 A RET B 2 .   ? 30.25100 35.80400 2.02800   0.820 27.20000  ?  301 RET A C12 1 
HETATM 3184 C  C12 B RET B 2 .   ? 30.36200 36.40300 1.97800   0.180 26.84000  ?  301 RET A C12 1 
HETATM 3185 C  C13 A RET B 2 .   ? 31.18500 36.73800 1.42300   0.820 28.44000  ?  301 RET A C13 1 
HETATM 3186 C  C13 B RET B 2 .   ? 31.14800 37.43700 1.30200   0.180 27.16000  ?  301 RET A C13 1 
HETATM 3187 C  C14 A RET B 2 .   ? 32.49100 36.39000 1.32400   0.820 26.64000  ?  301 RET A C14 1 
HETATM 3188 C  C14 B RET B 2 .   ? 32.44300 37.22600 0.91300   0.180 25.20000  ?  301 RET A C14 1 
HETATM 3189 C  C15 A RET B 2 .   ? 33.57000 37.18400 0.79500   0.820 19.67000  ?  301 RET A C15 1 
HETATM 3190 C  C15 B RET B 2 .   ? 33.25200 36.04000 1.00400   0.180 25.34000  ?  301 RET A C15 1 
HETATM 3191 C  C16 A RET B 2 .   ? 26.36500 31.92600 6.40300   0.820 21.93000  ?  301 RET A C16 1 
HETATM 3192 C  C16 B RET B 2 .   ? 25.91500 31.79100 6.38500   0.180 27.80000  ?  301 RET A C16 1 
HETATM 3193 C  C17 A RET B 2 .   ? 25.39300 31.14200 4.24200   0.820 31.60000  ?  301 RET A C17 1 
HETATM 3194 C  C17 B RET B 2 .   ? 25.29400 31.27700 4.01500   0.180 31.42000  ?  301 RET A C17 1 
HETATM 3195 C  C18 A RET B 2 .   ? 22.29300 34.53900 5.68700   0.820 29.06000  ?  301 RET A C18 1 
HETATM 3196 C  C18 B RET B 2 .   ? 22.31500 34.88600 5.12500   0.180 30.41000  ?  301 RET A C18 1 
HETATM 3197 C  C19 A RET B 2 .   ? 26.07100 36.46500 3.20800   0.820 27.34000  ?  301 RET A C19 1 
HETATM 3198 C  C19 B RET B 2 .   ? 26.02800 36.48700 2.74400   0.180 26.41000  ?  301 RET A C19 1 
HETATM 3199 C  C20 A RET B 2 .   ? 30.66200 38.08100 0.99400   0.820 30.14000  ?  301 RET A C20 1 
HETATM 3200 C  C20 B RET B 2 .   ? 30.48500 38.76700 1.09300   0.180 29.33000  ?  301 RET A C20 1 
HETATM 3201 CL CL  A CL  C 3 .   ? 30.44400 24.21900 3.41200   0.790 30.00000  ?  302 CL  A CL  1 
HETATM 3202 O  O   A HOH D 4 .   ? 34.94000 33.42100 -0.63700  0.790 42.49000  ?  401 HOH A O   1 
HETATM 3203 O  O   A HOH D 4 .   ? 24.66300 55.77400 13.47900  0.790 53.89000  ?  402 HOH A O   1 
HETATM 3204 O  O   B HOH D 4 .   ? 23.90000 55.71500 12.56300  0.210 53.89000  ?  402 HOH A O   1 
HETATM 3205 O  O   A HOH D 4 .   ? 29.95900 24.55900 -1.06700  0.790 37.01000  ?  403 HOH A O   1 
HETATM 3206 O  O   B HOH D 4 .   ? 31.32200 24.22700 -0.59700  0.210 37.10000  ?  403 HOH A O   1 
HETATM 3207 O  O   A HOH D 4 .   ? 36.99200 31.01200 1.13000   0.790 34.77000  ?  404 HOH A O   1 
HETATM 3208 O  O   A HOH D 4 .   ? 41.41300 17.93700 5.00500   0.790 48.62000  ?  405 HOH A O   1 
HETATM 3209 O  O   B HOH D 4 .   ? 41.06900 19.02500 5.24400   0.210 47.43000  ?  405 HOH A O   1 
HETATM 3210 O  O   A HOH D 4 .   ? 33.51400 54.97100 -11.46200 0.790 169.55000 ?  406 HOH A O   1 
HETATM 3211 O  O   B HOH D 4 .   ? 33.61600 55.47600 -11.40400 0.210 169.55000 ?  406 HOH A O   1 
HETATM 3212 O  O   A HOH D 4 .   ? 34.53000 30.05600 0.39700   0.790 40.36000  ?  407 HOH A O   1 
HETATM 3213 O  O   A HOH D 4 .   ? 30.22200 42.51800 -1.17800  0.790 29.72000  ?  408 HOH A O   1 
HETATM 3214 O  O   B HOH D 4 .   ? 30.72100 42.54400 -1.13900  0.210 26.97000  ?  408 HOH A O   1 
HETATM 3215 O  O   A HOH D 4 .   ? 31.97500 38.23800 11.34100  0.790 39.82000  ?  409 HOH A O   1 
HETATM 3216 O  O   B HOH D 4 .   ? 32.15300 38.60700 11.33000  0.210 36.86000  ?  409 HOH A O   1 
HETATM 3217 O  O   A HOH D 4 .   ? 29.69000 16.91600 0.61900   0.790 61.62000  ?  410 HOH A O   1 
HETATM 3218 O  O   B HOH D 4 .   ? 29.41300 17.77700 0.57600   0.210 55.20000  ?  410 HOH A O   1 
HETATM 3219 O  O   A HOH D 4 .   ? 29.12100 21.11500 4.10700   0.790 53.84000  ?  411 HOH A O   1 
HETATM 3220 O  O   B HOH D 4 .   ? 29.23000 22.56500 2.90700   0.210 52.07000  ?  411 HOH A O   1 
HETATM 3221 O  O   A HOH D 4 .   ? 30.34800 16.61500 -7.05300  0.790 41.85000  ?  412 HOH A O   1 
HETATM 3222 O  O   B HOH D 4 .   ? 30.96000 16.94400 -6.59800  0.210 39.96000  ?  412 HOH A O   1 
HETATM 3223 O  O   A HOH D 4 .   ? 39.65100 17.24900 -6.53800  0.790 56.79000  ?  413 HOH A O   1 
HETATM 3224 O  O   B HOH D 4 .   ? 40.02200 17.48700 -5.83500  0.210 49.03000  ?  413 HOH A O   1 
HETATM 3225 O  O   A HOH D 4 .   ? 34.00600 27.96400 -2.63400  0.790 48.77000  ?  414 HOH A O   1 
HETATM 3226 O  O   B HOH D 4 .   ? 33.77000 27.73800 -3.13200  0.210 40.68000  ?  414 HOH A O   1 
HETATM 3227 O  O   A HOH D 4 .   ? 18.49000 51.82700 14.79800  0.790 112.60000 ?  415 HOH A O   1 
HETATM 3228 O  O   B HOH D 4 .   ? 19.36000 52.48400 14.81200  0.210 112.60000 ?  415 HOH A O   1 
HETATM 3229 O  O   A HOH D 4 .   ? 30.12800 22.12000 1.41500   0.790 50.36000  ?  416 HOH A O   1 
HETATM 3230 O  O   B HOH D 4 .   ? 29.10900 22.41300 0.26200   0.210 45.16000  ?  416 HOH A O   1 
HETATM 3231 O  O   A HOH D 4 .   ? 48.19900 17.96600 -1.24900  0.790 70.10000  ?  417 HOH A O   1 
HETATM 3232 O  O   B HOH D 4 .   ? 48.59500 18.36600 -0.63200  0.210 72.71000  ?  417 HOH A O   1 
HETATM 3233 O  O   A HOH D 4 .   ? 34.71000 15.57400 -1.01200  0.790 54.63000  ?  418 HOH A O   1 
HETATM 3234 O  O   B HOH D 4 .   ? 34.16600 15.75000 -1.05100  0.210 55.29000  ?  418 HOH A O   1 
HETATM 3235 O  O   A HOH D 4 .   ? 22.01200 14.41100 -5.08800  0.790 71.03000  ?  419 HOH A O   1 
HETATM 3236 O  O   B HOH D 4 .   ? 22.39200 14.55600 -5.40300  0.210 71.65000  ?  419 HOH A O   1 
HETATM 3237 O  O   A HOH D 4 .   ? 49.02400 34.31600 -0.12400  0.790 61.69000  ?  420 HOH A O   1 
HETATM 3238 O  O   B HOH D 4 .   ? 48.62700 35.63400 -0.77600  0.210 67.84000  ?  420 HOH A O   1 
HETATM 3239 O  O   A HOH D 4 .   ? 44.87500 26.01700 -12.75000 0.790 73.91000  ?  421 HOH A O   1 
HETATM 3240 O  O   B HOH D 4 .   ? 44.87500 26.54800 -12.75000 0.210 70.30000  ?  421 HOH A O   1 
HETATM 3241 O  O   A HOH D 4 .   ? 35.33100 32.33700 -12.23600 0.790 73.04000  ?  422 HOH A O   1 
HETATM 3242 O  O   B HOH D 4 .   ? 34.32400 30.40900 -11.78300 0.210 62.86000  ?  422 HOH A O   1 
HETATM 3243 O  O   A HOH D 4 .   ? 53.89600 16.50100 -0.42100  0.790 91.61000  ?  423 HOH A O   1 
HETATM 3244 O  O   B HOH D 4 .   ? 54.41100 15.99600 -0.73400  0.210 94.52000  ?  423 HOH A O   1 
# 
