data_9H1X
# 
_entry.id   9H1X 
# 
_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   9H1X         pdb_00009h1x 10.2210/pdb9h1x/pdb 
WWPDB D_1292142184 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2025-04-30 
_pdbx_database_PDB_obs_spr.pdb_id           9H1X 
_pdbx_database_PDB_obs_spr.replace_pdb_id   8QQO 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H1X 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-10 
_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 . 8PWP unspecified 
PDB . 8PWJ unspecified 
PDB . 8PWI unspecified 
PDB . 8PWG unspecified 
PDB . 8PWQ unspecified 
PDB . 9H1W 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 syn 'CHLORIDE ION'        35.453    1  ? ? ? ? 
4 water       nat water                 18.015    21 ? ? ? ? 
# 
_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   1   MET MET 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  ?   ?   ?   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 217 217 217 ALA ALA A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ARG 220 220 ?   ?   ?   A . n 
A 1 221 ALA 221 221 ?   ?   ?   A . n 
A 1 222 GLU 222 222 ?   ?   ?   A . n 
A 1 223 HIS 223 223 ?   ?   ?   A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
A 1 225 GLU 225 225 ?   ?   ?   A . n 
A 1 226 SER 226 226 ?   ?   ?   A . n 
A 1 227 LEU 227 227 ?   ?   ?   A . n 
A 1 228 ALA 228 228 ?   ?   ?   A . n 
A 1 229 GLY 229 229 ?   ?   ?   A . n 
A 1 230 VAL 230 230 ?   ?   ?   A . n 
A 1 231 ASP 231 231 ?   ?   ?   A . n 
A 1 232 THR 232 232 ?   ?   ?   A . n 
A 1 233 ASP 233 233 ?   ?   ?   A . n 
A 1 234 ALA 234 234 ?   ?   ?   A . n 
A 1 235 PRO 235 235 ?   ?   ?   A . n 
A 1 236 ALA 236 236 ?   ?   ?   A . n 
A 1 237 VAL 237 237 ?   ?   ?   A . n 
A 1 238 ALA 238 238 ?   ?   ?   A . n 
A 1 239 ASP 239 239 ?   ?   ?   A . n 
A 1 240 GLU 240 240 ?   ?   ?   A . n 
A 1 241 ASN 241 241 ?   ?   ?   A . n 
A 1 242 SER 242 242 ?   ?   ?   A . n 
A 1 243 HIS 243 243 ?   ?   ?   A . n 
A 1 244 HIS 244 244 ?   ?   ?   A . n 
A 1 245 HIS 245 245 ?   ?   ?   A . n 
A 1 246 HIS 246 246 ?   ?   ?   A . n 
A 1 247 HIS 247 247 ?   ?   ?   A . n 
A 1 248 HIS 248 248 ?   ?   ?   A . n 
A 1 249 HIS 249 249 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 RET ? ? RET ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 RET 1  301 300 RET RET A . 
C 3 CL  1  302 1   CL  CL  A . 
D 4 HOH 1  401 17  HOH HOH A . 
D 4 HOH 2  402 3   HOH HOH A . 
D 4 HOH 3  403 5   HOH HOH A . 
D 4 HOH 4  404 2   HOH HOH A . 
D 4 HOH 5  405 7   HOH HOH A . 
D 4 HOH 6  406 36  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 8   HOH HOH A . 
D 4 HOH 11 411 10  HOH HOH A . 
D 4 HOH 12 412 25  HOH HOH A . 
D 4 HOH 13 413 29  HOH HOH A . 
D 4 HOH 14 414 26  HOH HOH A . 
D 4 HOH 15 415 43  HOH HOH A . 
D 4 HOH 16 416 33  HOH HOH A . 
D 4 HOH 17 417 38  HOH HOH A . 
D 4 HOH 18 418 44  HOH HOH A . 
D 4 HOH 19 419 37  HOH HOH A . 
D 4 HOH 20 420 12  HOH HOH A . 
D 4 HOH 21 421 49  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLU 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                     9H1X 
_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                         9H1X 
_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                   9H1X 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'CaCl2 150mM, Glycine 100mM, 38%(v/v) PEG 400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     296 
_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                          29.11 
_reflns.entry_id                                       9H1X 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_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                                     17156 
_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                                246.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.3 
_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                                   0.994 
_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                                    1.85 
_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                             17156 
_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                                  0.994 
_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                               60.96 
_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                                 9H1X 
_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                            1.85 
_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                     17156 
_refine.ls_number_reflns_R_free                  827 
_refine.ls_number_reflns_R_work                  16329 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    64.98 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2590 
_refine.ls_R_factor_R_free                       0.2763 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2581 
_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                 39.3259 
_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                            0.2990 
_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                       1.85 
_refine_hist.d_res_low                        44.8 
_refine_hist.number_atoms_solvent             21 
_refine_hist.number_atoms_total               1639 
_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        1597 
_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' ? 0.0310  ? 3315 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4781  ? 4541 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0575  ? 554  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0146  ? 539  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.2919 ? 1095 ? 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' 1.85 1.95 . . 0   10   0.26  . . . . 0.4818 . . . . . . . . . . . .      
'X-RAY DIFFRACTION' 1.96 2.11 . . 21  361  8.85  . . . . 0.5027 . . . . . . . . . . . 0.4622 
'X-RAY DIFFRACTION' 2.11 2.33 . . 164 3237 78.13 . . . . 0.4265 . . . . . . . . . . . 0.4195 
'X-RAY DIFFRACTION' 2.33 2.66 . . 192 4186 99.86 . . . . 0.3191 . . . . . . . . . . . 0.3666 
'X-RAY DIFFRACTION' 2.66 3.35 . . 213 4187 99.89 . . . . 0.2470 . . . . . . . . . . . 0.2921 
'X-RAY DIFFRACTION' 3.36 44.8 . . 237 4348 99.91 . . . . 0.2065 . . . . . . . . . . . 0.2233 
# 
_struct.entry_id                     9H1X 
_struct.title                        
'Continuously illuminated structure of Sensory Rhodopsin II solved by serial millisecond crystallography' 
_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        9H1X 
_struct_keywords.text            
'SRII, serial millisecond crystallography, sensory rhodopsin, sensory rhodopsin II, SMX, SSX, 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              9H1X 
_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 9H1X GLU A 240 ? UNP P42196 ? ? 'expression tag' 240 1  
1 9H1X ASN A 241 ? UNP P42196 ? ? 'expression tag' 241 2  
1 9H1X SER A 242 ? UNP P42196 ? ? 'expression tag' 242 3  
1 9H1X HIS A 243 ? UNP P42196 ? ? 'expression tag' 243 4  
1 9H1X HIS A 244 ? UNP P42196 ? ? 'expression tag' 244 5  
1 9H1X HIS A 245 ? UNP P42196 ? ? 'expression tag' 245 6  
1 9H1X HIS A 246 ? UNP P42196 ? ? 'expression tag' 246 7  
1 9H1X HIS A 247 ? UNP P42196 ? ? 'expression tag' 247 8  
1 9H1X HIS A 248 ? UNP P42196 ? ? 'expression tag' 248 9  
1 9H1X 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)'  9870 ? 
# 
_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 TYR A 36  ? LEU A 56  ? TYR A 36  LEU A 56  1 ? 21 
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 ? LEU A 219 ? THR A 189 LEU A 219 1 ? 31 
# 
_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 ? ? ? ? ? ? ? 1.438 ? ? 
# 
_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                   9H1X 
_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_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 64  ? A 55.36  -106.96 
2 1 ALA A 64  ? B 65.08  -118.03 
3 1 ILE A 100 ? B -50.52 -78.06  
4 1 VAL A 185 ? B -66.75 8.30    
5 1 ALA A 186 ? B 47.31  23.05   
6 1 LEU A 187 ? B -65.35 -82.81  
7 1 LEU A 188 ? B -37.77 141.85  
8 1 PHE A 208 ? B -21.05 -61.02  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     72 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    A 
_pdbx_validate_planes.rmsd            0.082 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_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     420 
_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 
# 
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 ARG 27  ? A ARG 27  
2  1 Y 1 A ASP 28  ? A ASP 28  
3  1 Y 1 A ALA 29  ? A ALA 29  
4  1 Y 1 A GLY 30  ? A GLY 30  
5  1 Y 1 A SER 31  ? A SER 31  
6  1 Y 1 A GLY 32  ? A GLY 32  
7  1 Y 1 A ARG 34  ? A ARG 34  
8  1 Y 1 A ARG 220 ? A ARG 220 
9  1 Y 1 A ALA 221 ? A ALA 221 
10 1 Y 1 A GLU 222 ? A GLU 222 
11 1 Y 1 A HIS 223 ? A HIS 223 
12 1 Y 1 A GLY 224 ? A GLY 224 
13 1 Y 1 A GLU 225 ? A GLU 225 
14 1 Y 1 A SER 226 ? A SER 226 
15 1 Y 1 A LEU 227 ? A LEU 227 
16 1 Y 1 A ALA 228 ? A ALA 228 
17 1 Y 1 A GLY 229 ? A GLY 229 
18 1 Y 1 A VAL 230 ? A VAL 230 
19 1 Y 1 A ASP 231 ? A ASP 231 
20 1 Y 1 A THR 232 ? A THR 232 
21 1 Y 1 A ASP 233 ? A ASP 233 
22 1 Y 1 A ALA 234 ? A ALA 234 
23 1 Y 1 A PRO 235 ? A PRO 235 
24 1 Y 1 A ALA 236 ? A ALA 236 
25 1 Y 1 A VAL 237 ? A VAL 237 
26 1 Y 1 A ALA 238 ? A ALA 238 
27 1 Y 1 A ASP 239 ? A ASP 239 
28 1 Y 1 A GLU 240 ? A GLU 240 
29 1 Y 1 A ASN 241 ? A ASN 241 
30 1 Y 1 A SER 242 ? A SER 242 
31 1 Y 1 A HIS 243 ? A HIS 243 
32 1 Y 1 A HIS 244 ? A HIS 244 
33 1 Y 1 A HIS 245 ? A HIS 245 
34 1 Y 1 A HIS 246 ? A HIS 246 
35 1 Y 1 A HIS 247 ? A HIS 247 
36 1 Y 1 A HIS 248 ? A HIS 248 
37 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                    9H1X 
_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  ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
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 MET A 1 1   ? 36.42700 16.10400 -15.10900 0.560 152.21000 ?  1   MET A N   1 
ATOM   2    N  N   B MET A 1 1   ? 36.30800 16.19900 -15.31300 0.440 152.57000 ?  1   MET A N   1 
ATOM   3    C  CA  A MET A 1 1   ? 37.13000 17.12600 -15.93700 0.560 153.06000 ?  1   MET A CA  1 
ATOM   4    C  CA  B MET A 1 1   ? 37.18900 17.17600 -15.96100 0.440 153.03000 ?  1   MET A CA  1 
ATOM   5    C  C   A MET A 1 1   ? 37.51000 18.33700 -15.09300 0.560 142.73000 ?  1   MET A C   1 
ATOM   6    C  C   B MET A 1 1   ? 37.52100 18.30200 -14.95300 0.440 142.43000 ?  1   MET A C   1 
ATOM   7    O  O   A MET A 1 1   ? 38.54500 18.96400 -15.31900 0.560 142.21000 ?  1   MET A O   1 
ATOM   8    O  O   B MET A 1 1   ? 38.61700 18.87500 -15.00600 0.440 142.17000 ?  1   MET A O   1 
ATOM   9    C  CB  A MET A 1 1   ? 36.25200 17.56700 -17.10800 0.560 160.34000 ?  1   MET A CB  1 
ATOM   10   C  CB  B MET A 1 1   ? 36.54100 17.73000 -17.27200 0.440 160.44000 ?  1   MET A CB  1 
ATOM   11   C  CG  A MET A 1 1   ? 36.92000 18.56000 -18.04900 0.560 165.83000 ?  1   MET A CG  1 
ATOM   12   C  CG  B MET A 1 1   ? 37.40300 18.71800 -18.17000 0.440 166.15000 ?  1   MET A CG  1 
ATOM   13   S  SD  A MET A 1 1   ? 36.37700 18.37400 -19.75900 0.560 167.65000 ?  1   MET A SD  1 
ATOM   14   S  SD  B MET A 1 1   ? 37.07800 18.80200 -19.98500 0.440 163.05000 ?  1   MET A SD  1 
ATOM   15   C  CE  A MET A 1 1   ? 37.70900 19.19000 -20.63700 0.560 163.86000 ?  1   MET A CE  1 
ATOM   16   C  CE  B MET A 1 1   ? 38.48200 19.72700 -20.61500 0.440 164.65000 ?  1   MET A CE  1 
ATOM   17   N  N   A VAL A 1 2   ? 36.66800 18.65400 -14.11200 0.560 130.53000 ?  2   VAL A N   1 
ATOM   18   N  N   B VAL A 1 2   ? 36.60400 18.58700 -14.01600 0.440 130.32000 ?  2   VAL A N   1 
ATOM   19   C  CA  A VAL A 1 2   ? 36.86200 19.80200 -13.23400 0.560 114.78000 ?  2   VAL A CA  1 
ATOM   20   C  CA  B VAL A 1 2   ? 36.78900 19.65700 -13.02600 0.440 113.98000 ?  2   VAL A CA  1 
ATOM   21   C  C   A VAL A 1 2   ? 36.65600 19.32200 -11.80300 0.560 100.49000 ?  2   VAL A C   1 
ATOM   22   C  C   B VAL A 1 2   ? 36.55500 19.10300 -11.61500 0.440 99.99000  ?  2   VAL A C   1 
ATOM   23   O  O   A VAL A 1 2   ? 35.53000 19.00100 -11.40300 0.560 96.14000  ?  2   VAL A O   1 
ATOM   24   O  O   B VAL A 1 2   ? 35.43700 18.69700 -11.27300 0.440 96.51000  ?  2   VAL A O   1 
ATOM   25   C  CB  A VAL A 1 2   ? 35.91100 20.96000 -13.57800 0.560 109.43000 ?  2   VAL A CB  1 
ATOM   26   C  CB  B VAL A 1 2   ? 35.89900 20.88500 -13.31400 0.440 108.65000 ?  2   VAL A CB  1 
ATOM   27   C  CG1 A VAL A 1 2   ? 34.45400 20.56800 -13.35600 0.560 107.97000 ?  2   VAL A CG1 1 
ATOM   28   C  CG1 B VAL A 1 2   ? 34.42200 20.52800 -13.37100 0.440 108.07000 ?  2   VAL A CG1 1 
ATOM   29   C  CG2 A VAL A 1 2   ? 36.26600 22.20300 -12.76800 0.560 95.26000  ?  2   VAL A CG2 1 
ATOM   30   C  CG2 B VAL A 1 2   ? 36.16300 21.99500 -12.30500 0.440 94.61000  ?  2   VAL A CG2 1 
ATOM   31   N  N   A GLY A 1 3   ? 37.74400 19.26100 -11.03500 0.560 93.65000  ?  3   GLY A N   1 
ATOM   32   N  N   B GLY A 1 3   ? 37.62700 19.05400 -10.81200 0.440 92.70000  ?  3   GLY A N   1 
ATOM   33   C  CA  A GLY A 1 3   ? 37.69300 18.80200 -9.66700  0.560 74.50000  ?  3   GLY A CA  1 
ATOM   34   C  CA  B GLY A 1 3   ? 37.61900 18.66100 -9.41400  0.440 72.78000  ?  3   GLY A CA  1 
ATOM   35   C  C   A GLY A 1 3   ? 37.58900 19.94900 -8.67400  0.560 66.56000  ?  3   GLY A C   1 
ATOM   36   C  C   B GLY A 1 3   ? 37.84300 19.83800 -8.48000  0.440 66.45000  ?  3   GLY A C   1 
ATOM   37   O  O   A GLY A 1 3   ? 37.79600 21.11500 -8.99900  0.560 58.37000  ?  3   GLY A O   1 
ATOM   38   O  O   B GLY A 1 3   ? 38.63100 20.74800 -8.78100  0.440 61.40000  ?  3   GLY A O   1 
ATOM   39   N  N   A LEU A 1 4   ? 37.25400 19.58400 -7.43400  0.560 63.52000  ?  4   LEU A N   1 
ATOM   40   N  N   B LEU A 1 4   ? 37.17000 19.79800 -7.31900  0.440 62.79000  ?  4   LEU A N   1 
ATOM   41   C  CA  A LEU A 1 4   ? 37.14800 20.58400 -6.37800  0.560 51.43000  ?  4   LEU A CA  1 
ATOM   42   C  CA  B LEU A 1 4   ? 37.11100 20.93200 -6.38700  0.440 52.16000  ?  4   LEU A CA  1 
ATOM   43   C  C   A LEU A 1 4   ? 38.43900 21.38000 -6.24400  0.560 54.25000  ?  4   LEU A C   1 
ATOM   44   C  C   B LEU A 1 4   ? 38.43800 21.66100 -6.27000  0.440 54.50000  ?  4   LEU A C   1 
ATOM   45   O  O   A LEU A 1 4   ? 38.41100 22.60800 -6.09900  0.560 55.28000  ?  4   LEU A O   1 
ATOM   46   O  O   B LEU A 1 4   ? 38.47300 22.89600 -6.24400  0.440 55.46000  ?  4   LEU A O   1 
ATOM   47   C  CB  A LEU A 1 4   ? 36.81100 19.91300 -5.04900  0.560 53.06000  ?  4   LEU A CB  1 
ATOM   48   C  CB  B LEU A 1 4   ? 36.69500 20.47400 -4.98500  0.440 50.97000  ?  4   LEU A CB  1 
ATOM   49   C  CG  A LEU A 1 4   ? 35.45600 19.22400 -4.92000  0.560 45.84000  ?  4   LEU A CG  1 
ATOM   50   C  CG  B LEU A 1 4   ? 35.37700 19.77400 -4.65700  0.440 45.16000  ?  4   LEU A CG  1 
ATOM   51   C  CD1 A LEU A 1 4   ? 35.32700 18.59800 -3.53700  0.560 57.52000  ?  4   LEU A CD1 1 
ATOM   52   C  CD1 B LEU A 1 4   ? 35.42700 19.59400 -3.21600  0.440 53.16000  ?  4   LEU A CD1 1 
ATOM   53   C  CD2 A LEU A 1 4   ? 34.32700 20.20100 -5.17600  0.560 54.69000  ?  4   LEU A CD2 1 
ATOM   54   C  CD2 B LEU A 1 4   ? 34.15900 20.55200 -5.03600  0.440 54.11000  ?  4   LEU A CD2 1 
ATOM   55   N  N   A THR A 1 5   ? 39.58500 20.69600 -6.28200  0.560 50.71000  ?  5   THR A N   1 
ATOM   56   N  N   B THR A 1 5   ? 39.54700 20.91800 -6.18900  0.440 51.14000  ?  5   THR A N   1 
ATOM   57   C  CA  A THR A 1 5   ? 40.85600 21.39100 -6.10900  0.560 54.82000  ?  5   THR A CA  1 
ATOM   58   C  CA  B THR A 1 5   ? 40.82900 21.57700 -5.98100  0.440 54.71000  ?  5   THR A CA  1 
ATOM   59   C  C   A THR A 1 5   ? 41.07400 22.41800 -7.21300  0.560 57.45000  ?  5   THR A C   1 
ATOM   60   C  C   B THR A 1 5   ? 41.20600 22.48400 -7.15600  0.440 57.46000  ?  5   THR A C   1 
ATOM   61   O  O   A THR A 1 5   ? 41.55100 23.52900 -6.95200  0.560 58.41000  ?  5   THR A O   1 
ATOM   62   O  O   B THR A 1 5   ? 41.89000 23.49200 -6.94000  0.440 57.27000  ?  5   THR A O   1 
ATOM   63   C  CB  A THR A 1 5   ? 42.01200 20.38900 -6.07300  0.560 58.92000  ?  5   THR A CB  1 
ATOM   64   C  CB  B THR A 1 5   ? 41.93300 20.53600 -5.68700  0.440 57.69000  ?  5   THR A CB  1 
ATOM   65   O  OG1 A THR A 1 5   ? 41.77500 19.33200 -7.01100  0.560 67.85000  ?  5   THR A OG1 1 
ATOM   66   O  OG1 B THR A 1 5   ? 41.68300 19.33100 -6.41600  0.440 64.35000  ?  5   THR A OG1 1 
ATOM   67   C  CG2 A THR A 1 5   ? 42.16200 19.79700 -4.67500  0.560 53.41000  ?  5   THR A CG2 1 
ATOM   68   C  CG2 B THR A 1 5   ? 41.95500 20.16500 -4.21200  0.440 52.00000  ?  5   THR A CG2 1 
ATOM   69   N  N   A THR A 1 6   ? 40.72100 22.07100 -8.45400  0.560 58.11000  ?  6   THR A N   1 
ATOM   70   N  N   B THR A 1 6   ? 40.75300 22.20300 -8.38800  0.440 57.94000  ?  6   THR A N   1 
ATOM   71   C  CA  A THR A 1 6   ? 40.86300 23.02900 -9.54700  0.560 48.66000  ?  6   THR A CA  1 
ATOM   72   C  CA  B THR A 1 6   ? 41.08800 23.16700 -9.43700  0.440 49.02000  ?  6   THR A CA  1 
ATOM   73   C  C   A THR A 1 6   ? 40.05300 24.29100 -9.27400  0.560 46.58000  ?  6   THR A C   1 
ATOM   74   C  C   B THR A 1 6   ? 40.21400 24.39700 -9.29600  0.440 46.62000  ?  6   THR A C   1 
ATOM   75   O  O   A THR A 1 6   ? 40.52200 25.40700 -9.52600  0.560 53.60000  ?  6   THR A O   1 
ATOM   76   O  O   B THR A 1 6   ? 40.67100 25.52100 -9.51100  0.440 54.31000  ?  6   THR A O   1 
ATOM   77   C  CB  A THR A 1 6   ? 40.42300 22.40200 -10.87100 0.560 56.59000  ?  6   THR A CB  1 
ATOM   78   C  CB  B THR A 1 6   ? 40.94800 22.55200 -10.84700 0.440 57.07000  ?  6   THR A CB  1 
ATOM   79   O  OG1 A THR A 1 6   ? 41.09700 21.15500 -11.07100 0.560 59.50000  ?  6   THR A OG1 1 
ATOM   80   O  OG1 B THR A 1 6   ? 41.75200 21.36900 -10.94300 0.440 58.73000  ?  6   THR A OG1 1 
ATOM   81   C  CG2 A THR A 1 6   ? 40.74400 23.34200 -12.03100 0.560 45.57000  ?  6   THR A CG2 1 
ATOM   82   C  CG2 B THR A 1 6   ? 41.44400 23.55300 -11.93800 0.440 46.76000  ?  6   THR A CG2 1 
ATOM   83   N  N   A LEU A 1 7   ? 38.83000 24.13100 -8.76400  0.560 47.28000  ?  7   LEU A N   1 
ATOM   84   N  N   B LEU A 1 7   ? 38.96800 24.19800 -8.89800  0.440 47.01000  ?  7   LEU A N   1 
ATOM   85   C  CA  A LEU A 1 7   ? 37.99400 25.28900 -8.47100  0.560 47.72000  ?  7   LEU A CA  1 
ATOM   86   C  CA  B LEU A 1 7   ? 38.11200 25.29700 -8.49800  0.440 47.78000  ?  7   LEU A CA  1 
ATOM   87   C  C   A LEU A 1 7   ? 38.59100 26.12600 -7.34800  0.560 48.90000  ?  7   LEU A C   1 
ATOM   88   C  C   B LEU A 1 7   ? 38.72500 26.11300 -7.36300  0.440 49.09000  ?  7   LEU A C   1 
ATOM   89   O  O   A LEU A 1 7   ? 38.56100 27.36100 -7.40300  0.560 48.88000  ?  7   LEU A O   1 
ATOM   90   O  O   B LEU A 1 7   ? 38.84000 27.34200 -7.44600  0.440 48.83000  ?  7   LEU A O   1 
ATOM   91   C  CB  A LEU A 1 7   ? 36.58100 24.82900 -8.11300  0.560 49.37000  ?  7   LEU A CB  1 
ATOM   92   C  CB  B LEU A 1 7   ? 36.76500 24.72700 -8.09200  0.440 49.21000  ?  7   LEU A CB  1 
ATOM   93   C  CG  A LEU A 1 7   ? 35.81200 24.19300 -9.27100  0.560 51.55000  ?  7   LEU A CG  1 
ATOM   94   C  CG  B LEU A 1 7   ? 36.03200 24.25400 -9.33300  0.440 51.53000  ?  7   LEU A CG  1 
ATOM   95   C  CD1 A LEU A 1 7   ? 34.49900 23.59500 -8.81400  0.560 51.79000  ?  7   LEU A CD1 1 
ATOM   96   C  CD1 B LEU A 1 7   ? 34.76700 23.50600 -8.95100  0.440 51.55000  ?  7   LEU A CD1 1 
ATOM   97   C  CD2 A LEU A 1 7   ? 35.58100 25.23200 -10.36600 0.560 49.40000  ?  7   LEU A CD2 1 
ATOM   98   C  CD2 B LEU A 1 7   ? 35.71600 25.48300 -10.13700 0.440 51.37000  ?  7   LEU A CD2 1 
ATOM   99   N  N   A PHE A 1 8   ? 39.14100 25.47200 -6.32200  0.560 48.15000  ?  8   PHE A N   1 
ATOM   100  N  N   B PHE A 1 8   ? 39.12900 25.45900 -6.28900  0.440 48.13000  ?  8   PHE A N   1 
ATOM   101  C  CA  A PHE A 1 8   ? 39.78400 26.21100 -5.24200  0.560 50.16000  ?  8   PHE A CA  1 
ATOM   102  C  CA  B PHE A 1 8   ? 39.72300 26.24100 -5.21600  0.440 50.22000  ?  8   PHE A CA  1 
ATOM   103  C  C   A PHE A 1 8   ? 40.99300 26.98900 -5.75600  0.560 50.97000  ?  8   PHE A C   1 
ATOM   104  C  C   B PHE A 1 8   ? 40.94100 27.01100 -5.70300  0.440 50.87000  ?  8   PHE A C   1 
ATOM   105  O  O   A PHE A 1 8   ? 41.18100 28.15900 -5.40200  0.560 52.47000  ?  8   PHE A O   1 
ATOM   106  O  O   B PHE A 1 8   ? 41.12700 28.17700 -5.32500  0.440 52.03000  ?  8   PHE A O   1 
ATOM   107  C  CB  A PHE A 1 8   ? 40.17800 25.25300 -4.11500  0.560 53.60000  ?  8   PHE A CB  1 
ATOM   108  C  CB  B PHE A 1 8   ? 40.07100 25.32600 -4.04700  0.440 53.50000  ?  8   PHE A CB  1 
ATOM   109  C  CG  A PHE A 1 8   ? 39.00100 24.72000 -3.32800  0.560 49.62000  ?  8   PHE A CG  1 
ATOM   110  C  CG  B PHE A 1 8   ? 38.86500 24.79900 -3.34100  0.440 49.13000  ?  8   PHE A CG  1 
ATOM   111  C  CD1 A PHE A 1 8   ? 37.92600 25.53900 -3.01300  0.560 47.08000  ?  8   PHE A CD1 1 
ATOM   112  C  CD1 B PHE A 1 8   ? 37.81900 25.63800 -3.04800  0.440 47.73000  ?  8   PHE A CD1 1 
ATOM   113  C  CD2 A PHE A 1 8   ? 38.97200 23.39900 -2.90500  0.560 54.03000  ?  8   PHE A CD2 1 
ATOM   114  C  CD2 B PHE A 1 8   ? 38.75100 23.46800 -3.00900  0.440 53.95000  ?  8   PHE A CD2 1 
ATOM   115  C  CE1 A PHE A 1 8   ? 36.84600 25.05400 -2.29600  0.560 49.31000  ?  8   PHE A CE1 1 
ATOM   116  C  CE1 B PHE A 1 8   ? 36.68900 25.18600 -2.40200  0.440 49.57000  ?  8   PHE A CE1 1 
ATOM   117  C  CE2 A PHE A 1 8   ? 37.89300 22.90900 -2.18500  0.560 47.06000  ?  8   PHE A CE2 1 
ATOM   118  C  CE2 B PHE A 1 8   ? 37.60600 22.99800 -2.35200  0.440 47.07000  ?  8   PHE A CE2 1 
ATOM   119  C  CZ  A PHE A 1 8   ? 36.82900 23.74000 -1.88100  0.560 45.43000  ?  8   PHE A CZ  1 
ATOM   120  C  CZ  B PHE A 1 8   ? 36.59100 23.85900 -2.05700  0.440 46.71000  ?  8   PHE A CZ  1 
ATOM   121  N  N   A TRP A 1 9   ? 41.81400 26.36900 -6.61000  0.560 50.31000  ?  9   TRP A N   1 
ATOM   122  N  N   B TRP A 1 9   ? 41.75600 26.40400 -6.57500  0.440 50.33000  ?  9   TRP A N   1 
ATOM   123  C  CA  A TRP A 1 9   ? 42.96100 27.08700 -7.15900  0.560 45.83000  ?  9   TRP A CA  1 
ATOM   124  C  CA  B TRP A 1 9   ? 42.92800 27.11500 -7.06100  0.440 46.05000  ?  9   TRP A CA  1 
ATOM   125  C  C   A TRP A 1 9   ? 42.51000 28.30600 -7.95500  0.560 46.36000  ?  9   TRP A C   1 
ATOM   126  C  C   B TRP A 1 9   ? 42.54300 28.32100 -7.90600  0.440 45.98000  ?  9   TRP A C   1 
ATOM   127  O  O   A TRP A 1 9   ? 43.13600 29.37000 -7.88200  0.560 47.68000  ?  9   TRP A O   1 
ATOM   128  O  O   B TRP A 1 9   ? 43.16400 29.39200 -7.78900  0.440 46.93000  ?  9   TRP A O   1 
ATOM   129  C  CB  A TRP A 1 9   ? 43.80800 26.15400 -8.02700  0.560 51.66000  ?  9   TRP A CB  1 
ATOM   130  C  CB  B TRP A 1 9   ? 43.81800 26.20000 -7.86800  0.440 51.24000  ?  9   TRP A CB  1 
ATOM   131  C  CG  A TRP A 1 9   ? 44.73200 25.28100 -7.22600  0.560 54.76000  ?  9   TRP A CG  1 
ATOM   132  C  CG  B TRP A 1 9   ? 44.73600 25.48100 -7.04600  0.440 54.53000  ?  9   TRP A CG  1 
ATOM   133  C  CD1 A TRP A 1 9   ? 44.70800 23.91800 -7.14700  0.560 59.06000  ?  9   TRP A CD1 1 
ATOM   134  C  CD1 B TRP A 1 9   ? 44.84400 24.15000 -6.96200  0.440 58.54000  ?  9   TRP A CD1 1 
ATOM   135  C  CD2 A TRP A 1 9   ? 45.81500 25.71100 -6.38500  0.560 53.35000  ?  9   TRP A CD2 1 
ATOM   136  C  CD2 B TRP A 1 9   ? 45.69500 26.03100 -6.13900  0.440 55.28000  ?  9   TRP A CD2 1 
ATOM   137  N  NE1 A TRP A 1 9   ? 45.70600 23.47300 -6.31200  0.560 63.46000  ?  9   TRP A NE1 1 
ATOM   138  N  NE1 B TRP A 1 9   ? 45.80900 23.80900 -6.06000  0.440 62.50000  ?  9   TRP A NE1 1 
ATOM   139  C  CE2 A TRP A 1 9   ? 46.40000 24.55300 -5.83300  0.560 60.33000  ?  9   TRP A CE2 1 
ATOM   140  C  CE2 B TRP A 1 9   ? 46.35200 24.95200 -5.53700  0.440 58.18000  ?  9   TRP A CE2 1 
ATOM   141  C  CE3 A TRP A 1 9   ? 46.34500 26.96100 -6.04600  0.560 55.18000  ?  9   TRP A CE3 1 
ATOM   142  C  CE3 B TRP A 1 9   ? 46.06000 27.33400 -5.77900  0.440 56.28000  ?  9   TRP A CE3 1 
ATOM   143  C  CZ2 A TRP A 1 9   ? 47.48500 24.60700 -4.96000  0.560 65.13000  ?  9   TRP A CZ2 1 
ATOM   144  C  CZ2 B TRP A 1 9   ? 47.36900 25.12000 -4.60400  0.440 63.58000  ?  9   TRP A CZ2 1 
ATOM   145  C  CZ3 A TRP A 1 9   ? 47.42400 27.01200 -5.18000  0.560 68.78000  ?  9   TRP A CZ3 1 
ATOM   146  C  CZ3 B TRP A 1 9   ? 47.06400 27.50600 -4.85000  0.440 66.36000  ?  9   TRP A CZ3 1 
ATOM   147  C  CH2 A TRP A 1 9   ? 47.98200 25.84300 -4.64700  0.560 63.73000  ?  9   TRP A CH2 1 
ATOM   148  C  CH2 B TRP A 1 9   ? 47.71700 26.39800 -4.27200  0.440 67.13000  ?  9   TRP A CH2 1 
ATOM   149  N  N   A LEU A 1 10  ? 41.41800 28.17500 -8.71200  0.560 43.56000  ?  10  LEU A N   1 
ATOM   150  N  N   B LEU A 1 10  ? 41.55300 28.18500 -8.78800  0.440 44.00000  ?  10  LEU A N   1 
ATOM   151  C  CA  A LEU A 1 10  ? 40.90800 29.30700 -9.48100  0.560 47.65000  ?  10  LEU A CA  1 
ATOM   152  C  CA  B LEU A 1 10  ? 41.15300 29.37700 -9.52400  0.440 48.17000  ?  10  LEU A CA  1 
ATOM   153  C  C   A LEU A 1 10  ? 40.53300 30.46300 -8.56500  0.560 49.01000  ?  10  LEU A C   1 
ATOM   154  C  C   B LEU A 1 10  ? 40.84400 30.49500 -8.55200  0.440 49.04000  ?  10  LEU A C   1 
ATOM   155  O  O   A LEU A 1 10  ? 40.84000 31.62700 -8.85000  0.560 42.77000  ?  10  LEU A O   1 
ATOM   156  O  O   B LEU A 1 10  ? 41.37100 31.61100 -8.68200  0.440 45.37000  ?  10  LEU A O   1 
ATOM   157  C  CB  A LEU A 1 10  ? 39.69600 28.87900 -10.30600 0.560 44.53000  ?  10  LEU A CB  1 
ATOM   158  C  CB  B LEU A 1 10  ? 39.94400 29.11300 -10.40500 0.440 45.56000  ?  10  LEU A CB  1 
ATOM   159  C  CG  A LEU A 1 10  ? 39.96600 27.93000 -11.46900 0.560 60.47000  ?  10  LEU A CG  1 
ATOM   160  C  CG  B LEU A 1 10  ? 40.06100 28.07600 -11.50100 0.440 59.49000  ?  10  LEU A CG  1 
ATOM   161  C  CD1 A LEU A 1 10  ? 38.67100 27.44600 -12.09100 0.560 60.42000  ?  10  LEU A CD1 1 
ATOM   162  C  CD1 B LEU A 1 10  ? 38.66700 27.97000 -12.08200 0.440 59.44000  ?  10  LEU A CD1 1 
ATOM   163  C  CD2 A LEU A 1 10  ? 40.84500 28.62000 -12.50400 0.560 54.81000  ?  10  LEU A CD2 1 
ATOM   164  C  CD2 B LEU A 1 10  ? 41.12600 28.39100 -12.58600 0.440 54.63000  ?  10  LEU A CD2 1 
ATOM   165  N  N   A GLY A 1 11  ? 39.84100 30.16100 -7.46600  0.560 52.56000  ?  11  GLY A N   1 
ATOM   166  N  N   B GLY A 1 11  ? 40.04800 30.16300 -7.51700  0.440 52.14000  ?  11  GLY A N   1 
ATOM   167  C  CA  A GLY A 1 11  ? 39.52000 31.20200 -6.50700  0.560 43.83000  ?  11  GLY A CA  1 
ATOM   168  C  CA  B GLY A 1 11  ? 39.68200 30.98700 -6.38000  0.440 43.29000  ?  11  GLY A CA  1 
ATOM   169  C  C   A GLY A 1 11  ? 40.76300 31.81400 -5.89600  0.560 43.46000  ?  11  GLY A C   1 
ATOM   170  C  C   B GLY A 1 11  ? 40.89300 31.76200 -5.96400  0.440 43.61000  ?  11  GLY A C   1 
ATOM   171  O  O   A GLY A 1 11  ? 40.84700 33.03200 -5.72400  0.560 46.83000  ?  11  GLY A O   1 
ATOM   172  O  O   B GLY A 1 11  ? 40.90200 33.00500 -5.98900  0.440 45.92000  ?  11  GLY A O   1 
ATOM   173  N  N   A ALA A 1 12  ? 41.75400 30.97800 -5.57800  0.560 44.42000  ?  12  ALA A N   1 
ATOM   174  N  N   B ALA A 1 12  ? 41.96400 31.03500 -5.65300  0.440 44.12000  ?  12  ALA A N   1 
ATOM   175  C  CA  A ALA A 1 12  ? 43.01500 31.48500 -5.05000  0.560 48.92000  ?  12  ALA A CA  1 
ATOM   176  C  CA  B ALA A 1 12  ? 43.12000 31.72400 -5.09400  0.440 49.06000  ?  12  ALA A CA  1 
ATOM   177  C  C   A ALA A 1 12  ? 43.65400 32.47300 -6.01700  0.560 51.98000  ?  12  ALA A C   1 
ATOM   178  C  C   B ALA A 1 12  ? 43.68000 32.71200 -6.10500  0.440 51.57000  ?  12  ALA A C   1 
ATOM   179  O  O   A ALA A 1 12  ? 44.07200 33.56700 -5.61900  0.560 51.89000  ?  12  ALA A O   1 
ATOM   180  O  O   B ALA A 1 12  ? 44.08000 33.82600 -5.74000  0.440 51.38000  ?  12  ALA A O   1 
ATOM   181  C  CB  A ALA A 1 12  ? 43.96300 30.32000 -4.76800  0.560 47.66000  ?  12  ALA A CB  1 
ATOM   182  C  CB  B ALA A 1 12  ? 44.17200 30.70400 -4.66600  0.440 47.89000  ?  12  ALA A CB  1 
ATOM   183  N  N   A ILE A 1 13  ? 43.73400 32.10500 -7.29800  0.560 52.50000  ?  13  ILE A N   1 
ATOM   184  N  N   B ILE A 1 13  ? 43.65000 32.33200 -7.38300  0.440 51.87000  ?  13  ILE A N   1 
ATOM   185  C  CA  A ILE A 1 13  ? 44.37300 32.97700 -8.28200  0.560 51.07000  ?  13  ILE A CA  1 
ATOM   186  C  CA  B ILE A 1 13  ? 44.16600 33.18200 -8.44700  0.440 49.77000  ?  13  ILE A CA  1 
ATOM   187  C  C   A ILE A 1 13  ? 43.60500 34.28400 -8.40300  0.560 45.58000  ?  13  ILE A C   1 
ATOM   188  C  C   B ILE A 1 13  ? 43.36600 34.46400 -8.53200  0.440 44.85000  ?  13  ILE A C   1 
ATOM   189  O  O   A ILE A 1 13  ? 44.19100 35.37200 -8.45700  0.560 47.77000  ?  13  ILE A O   1 
ATOM   190  O  O   B ILE A 1 13  ? 43.92600 35.56100 -8.47900  0.440 47.58000  ?  13  ILE A O   1 
ATOM   191  C  CB  A ILE A 1 13  ? 44.47400 32.27300 -9.64600  0.560 48.25000  ?  13  ILE A CB  1 
ATOM   192  C  CB  B ILE A 1 13  ? 44.14900 32.44000 -9.78600  0.440 47.78000  ?  13  ILE A CB  1 
ATOM   193  C  CG1 A ILE A 1 13  ? 45.46900 31.11600 -9.59400  0.560 46.14000  ?  13  ILE A CG1 1 
ATOM   194  C  CG1 B ILE A 1 13  ? 45.03000 31.20600 -9.70500  0.440 47.84000  ?  13  ILE A CG1 1 
ATOM   195  C  CG2 A ILE A 1 13  ? 44.88200 33.27700 -10.72100 0.560 44.09000  ?  13  ILE A CG2 1 
ATOM   196  C  CG2 B ILE A 1 13  ? 44.64800 33.37500 -10.84500 0.440 44.54000  ?  13  ILE A CG2 1 
ATOM   197  C  CD1 A ILE A 1 13  ? 45.26300 30.10300 -10.69500 0.560 55.11000  ?  13  ILE A CD1 1 
ATOM   198  C  CD1 B ILE A 1 13  ? 44.67000 30.21900 -10.75000 0.440 56.48000  ?  13  ILE A CD1 1 
ATOM   199  N  N   A GLY A 1 14  ? 42.27700 34.19200 -8.47400  0.560 40.71000  ?  14  GLY A N   1 
ATOM   200  N  N   B GLY A 1 14  ? 42.04300 34.34800 -8.64200  0.440 39.62000  ?  14  GLY A N   1 
ATOM   201  C  CA  A GLY A 1 14  ? 41.47000 35.39200 -8.57200  0.560 37.79000  ?  14  GLY A CA  1 
ATOM   202  C  CA  B GLY A 1 14  ? 41.22100 35.54400 -8.60000  0.440 39.02000  ?  14  GLY A CA  1 
ATOM   203  C  C   A GLY A 1 14  ? 41.64800 36.31200 -7.38300  0.560 49.46000  ?  14  GLY A C   1 
ATOM   204  C  C   B GLY A 1 14  ? 41.54300 36.39900 -7.38800  0.440 49.24000  ?  14  GLY A C   1 
ATOM   205  O  O   A GLY A 1 14  ? 41.73700 37.53100 -7.53900  0.560 44.14000  ?  14  GLY A O   1 
ATOM   206  O  O   B GLY A 1 14  ? 41.94500 37.57000 -7.51400  0.440 44.80000  ?  14  GLY A O   1 
ATOM   207  N  N   A MET A 1 15  ? 41.69000 35.74800 -6.17500  0.560 42.90000  ?  15  MET A N   1 
ATOM   208  N  N   B MET A 1 15  ? 41.46200 35.80000 -6.19500  0.440 43.76000  ?  15  MET A N   1 
ATOM   209  C  CA  A MET A 1 15  ? 41.88600 36.59000 -5.00200  0.560 47.56000  ?  15  MET A CA  1 
ATOM   210  C  CA  B MET A 1 15  ? 41.67700 36.59500 -4.99100  0.440 47.30000  ?  15  MET A CA  1 
ATOM   211  C  C   A MET A 1 15  ? 43.28000 37.20500 -5.00200  0.560 48.55000  ?  15  MET A C   1 
ATOM   212  C  C   B MET A 1 15  ? 43.06100 37.26400 -5.02400  0.440 48.58000  ?  15  MET A C   1 
ATOM   213  O  O   A MET A 1 15  ? 43.44700 38.37500 -4.64000  0.560 46.77000  ?  15  MET A O   1 
ATOM   214  O  O   B MET A 1 15  ? 43.21700 38.46100 -4.70500  0.440 47.16000  ?  15  MET A O   1 
ATOM   215  C  CB  A MET A 1 15  ? 41.63500 35.77900 -3.73300  0.560 45.84000  ?  15  MET A CB  1 
ATOM   216  C  CB  B MET A 1 15  ? 41.48600 35.70900 -3.73500  0.440 45.46000  ?  15  MET A CB  1 
ATOM   217  C  CG  A MET A 1 15  ? 40.19000 35.27700 -3.61300  0.560 33.75000  ?  15  MET A CG  1 
ATOM   218  C  CG  B MET A 1 15  ? 40.13800 34.93000 -3.58100  0.440 33.51000  ?  15  MET A CG  1 
ATOM   219  S  SD  A MET A 1 15  ? 38.98900 36.62000 -3.46600  0.560 42.12000  ?  15  MET A SD  1 
ATOM   220  S  SD  B MET A 1 15  ? 38.86600 36.14500 -3.80700  0.440 40.33000  ?  15  MET A SD  1 
ATOM   221  C  CE  A MET A 1 15  ? 37.44100 35.72900 -3.50800  0.560 37.87000  ?  15  MET A CE  1 
ATOM   222  C  CE  B MET A 1 15  ? 37.35200 35.15000 -3.71600  0.440 37.58000  ?  15  MET A CE  1 
ATOM   223  N  N   A LEU A 1 16  ? 44.28800 36.44700 -5.44000  0.560 44.42000  ?  16  LEU A N   1 
ATOM   224  N  N   B LEU A 1 16  ? 44.07700 36.50200 -5.42100  0.440 44.28000  ?  16  LEU A N   1 
ATOM   225  C  CA  A LEU A 1 16  ? 45.65200 36.96700 -5.46300  0.560 51.35000  ?  16  LEU A CA  1 
ATOM   226  C  CA  B LEU A 1 16  ? 45.40300 37.08900 -5.52100  0.440 51.65000  ?  16  LEU A CA  1 
ATOM   227  C  C   A LEU A 1 16  ? 45.77300 38.15600 -6.41000  0.560 53.76000  ?  16  LEU A C   1 
ATOM   228  C  C   B LEU A 1 16  ? 45.40600 38.29400 -6.42900  0.440 54.31000  ?  16  LEU A C   1 
ATOM   229  O  O   A LEU A 1 16  ? 46.37500 39.18000 -6.06800  0.560 56.91000  ?  16  LEU A O   1 
ATOM   230  O  O   B LEU A 1 16  ? 45.92800 39.35100 -6.06700  0.440 56.57000  ?  16  LEU A O   1 
ATOM   231  C  CB  A LEU A 1 16  ? 46.62500 35.85900 -5.86900  0.560 53.77000  ?  16  LEU A CB  1 
ATOM   232  C  CB  B LEU A 1 16  ? 46.39300 36.09000 -6.05900  0.440 52.90000  ?  16  LEU A CB  1 
ATOM   233  C  CG  A LEU A 1 16  ? 46.98700 34.86100 -4.76800  0.560 69.53000  ?  16  LEU A CG  1 
ATOM   234  C  CG  B LEU A 1 16  ? 46.99800 35.40600 -4.87300  0.440 66.61000  ?  16  LEU A CG  1 
ATOM   235  C  CD1 A LEU A 1 16  ? 47.11100 33.44600 -5.31200  0.560 73.47000  ?  16  LEU A CD1 1 
ATOM   236  C  CD1 B LEU A 1 16  ? 47.40400 33.97200 -5.21500  0.440 70.73000  ?  16  LEU A CD1 1 
ATOM   237  C  CD2 A LEU A 1 16  ? 48.27300 35.28000 -4.06400  0.560 86.60000  ?  16  LEU A CD2 1 
ATOM   238  C  CD2 B LEU A 1 16  ? 48.18400 36.25400 -4.43900  0.440 77.72000  ?  16  LEU A CD2 1 
ATOM   239  N  N   A VAL A 1 17  ? 45.20800 38.03500 -7.61300  0.560 51.14000  ?  17  VAL A N   1 
ATOM   240  N  N   B VAL A 1 17  ? 44.84800 38.14800 -7.62900  0.440 50.57000  ?  17  VAL A N   1 
ATOM   241  C  CA  A VAL A 1 17  ? 45.26400 39.13300 -8.57500  0.560 54.55000  ?  17  VAL A CA  1 
ATOM   242  C  CA  B VAL A 1 17  ? 44.98300 39.22500 -8.59600  0.440 54.45000  ?  17  VAL A CA  1 
ATOM   243  C  C   A VAL A 1 17  ? 44.59000 40.37000 -7.99700  0.560 55.12000  ?  17  VAL A C   1 
ATOM   244  C  C   B VAL A 1 17  ? 44.35000 40.48200 -8.01700  0.440 54.76000  ?  17  VAL A C   1 
ATOM   245  O  O   A VAL A 1 17  ? 45.11000 41.48900 -8.09700  0.560 53.73000  ?  17  VAL A O   1 
ATOM   246  O  O   B VAL A 1 17  ? 44.99000 41.54600 -7.94800  0.440 53.90000  ?  17  VAL A O   1 
ATOM   247  C  CB  A VAL A 1 17  ? 44.61500 38.71300 -9.90600  0.560 52.65000  ?  17  VAL A CB  1 
ATOM   248  C  CB  B VAL A 1 17  ? 44.37800 38.82400 -9.95900  0.440 52.26000  ?  17  VAL A CB  1 
ATOM   249  C  CG1 A VAL A 1 17  ? 44.42900 39.92900 -10.80800 0.560 55.74000  ?  17  VAL A CG1 1 
ATOM   250  C  CG1 B VAL A 1 17  ? 44.62400 39.91000 -10.98600 0.440 55.51000  ?  17  VAL A CG1 1 
ATOM   251  C  CG2 A VAL A 1 17  ? 45.44900 37.65200 -10.60100 0.560 48.88000  ?  17  VAL A CG2 1 
ATOM   252  C  CG2 B VAL A 1 17  ? 44.90500 37.45800 -10.47100 0.440 45.27000  ?  17  VAL A CG2 1 
ATOM   253  N  N   A GLY A 1 18  ? 43.41700 40.18900 -7.38900  0.560 51.04000  ?  18  GLY A N   1 
ATOM   254  N  N   B GLY A 1 18  ? 43.13100 40.33300 -7.48000  0.440 51.45000  ?  18  GLY A N   1 
ATOM   255  C  CA  A GLY A 1 18  ? 42.77000 41.30600 -6.72400  0.560 47.32000  ?  18  GLY A CA  1 
ATOM   256  C  CA  B GLY A 1 18  ? 42.52400 41.40400 -6.72100  0.440 48.09000  ?  18  GLY A CA  1 
ATOM   257  C  C   A GLY A 1 18  ? 43.65300 41.91500 -5.65400  0.560 53.17000  ?  18  GLY A C   1 
ATOM   258  C  C   B GLY A 1 18  ? 43.46100 41.93900 -5.68200  0.440 53.26000  ?  18  GLY A C   1 
ATOM   259  O  O   A GLY A 1 18  ? 43.79900 43.13600 -5.57000  0.560 55.78000  ?  18  GLY A O   1 
ATOM   260  O  O   B GLY A 1 18  ? 43.73600 43.13500 -5.64700  0.440 55.79000  ?  18  GLY A O   1 
ATOM   261  N  N   A THR A 1 19  ? 44.27400 41.06300 -4.83700  0.560 50.56000  ?  19  THR A N   1 
ATOM   262  N  N   B THR A 1 19  ? 44.03000 41.04500 -4.87300  0.440 50.89000  ?  19  THR A N   1 
ATOM   263  C  CA  A THR A 1 19  ? 45.10100 41.54500 -3.73600  0.560 55.87000  ?  19  THR A CA  1 
ATOM   264  C  CA  B THR A 1 19  ? 44.90200 41.48500 -3.79800  0.440 55.77000  ?  19  THR A CA  1 
ATOM   265  C  C   A THR A 1 19  ? 46.23800 42.42600 -4.24200  0.560 60.92000  ?  19  THR A C   1 
ATOM   266  C  C   B THR A 1 19  ? 46.07600 42.28300 -4.34000  0.440 60.68000  ?  19  THR A C   1 
ATOM   267  O  O   A THR A 1 19  ? 46.47100 43.52200 -3.71800  0.560 63.04000  ?  19  THR A O   1 
ATOM   268  O  O   B THR A 1 19  ? 46.49400 43.27700 -3.74600  0.440 63.23000  ?  19  THR A O   1 
ATOM   269  C  CB  A THR A 1 19  ? 45.66100 40.35900 -2.94900  0.560 50.98000  ?  19  THR A CB  1 
ATOM   270  C  CB  B THR A 1 19  ? 45.39900 40.28500 -3.01800  0.440 52.02000  ?  19  THR A CB  1 
ATOM   271  O  OG1 A THR A 1 19  ? 44.59000 39.61300 -2.35700  0.560 49.90000  ?  19  THR A OG1 1 
ATOM   272  O  OG1 B THR A 1 19  ? 44.27100 39.51500 -2.54800  0.440 50.55000  ?  19  THR A OG1 1 
ATOM   273  C  CG2 A THR A 1 19  ? 46.60900 40.84300 -1.86000  0.560 50.51000  ?  19  THR A CG2 1 
ATOM   274  C  CG2 B THR A 1 19  ? 46.17200 40.79600 -1.86500  0.440 50.33000  ?  19  THR A CG2 1 
ATOM   275  N  N   A LEU A 1 20  ? 46.96900 41.95500 -5.25500  0.560 63.75000  ?  20  LEU A N   1 
ATOM   276  N  N   B LEU A 1 20  ? 46.60000 41.88800 -5.48900  0.440 63.03000  ?  20  LEU A N   1 
ATOM   277  C  CA  A LEU A 1 20  ? 48.08500 42.73500 -5.78000  0.560 75.93000  ?  20  LEU A CA  1 
ATOM   278  C  CA  B LEU A 1 20  ? 47.68500 42.66100 -6.07400  0.440 73.77000  ?  20  LEU A CA  1 
ATOM   279  C  C   A LEU A 1 20  ? 47.59800 44.02700 -6.42100  0.560 80.13000  ?  20  LEU A C   1 
ATOM   280  C  C   B LEU A 1 20  ? 47.17700 43.98400 -6.63500  0.440 78.08000  ?  20  LEU A C   1 
ATOM   281  O  O   A LEU A 1 20  ? 48.24500 45.07400 -6.29700  0.560 90.29000  ?  20  LEU A O   1 
ATOM   282  O  O   B LEU A 1 20  ? 47.64500 45.05700 -6.23300  0.440 85.44000  ?  20  LEU A O   1 
ATOM   283  C  CB  A LEU A 1 20  ? 48.87200 41.90400 -6.79000  0.560 73.76000  ?  20  LEU A CB  1 
ATOM   284  C  CB  B LEU A 1 20  ? 48.40900 41.82800 -7.13300  0.440 71.49000  ?  20  LEU A CB  1 
ATOM   285  C  CG  A LEU A 1 20  ? 49.45800 40.59500 -6.26300  0.560 75.97000  ?  20  LEU A CG  1 
ATOM   286  C  CG  B LEU A 1 20  ? 49.05400 40.64700 -6.40900  0.440 75.24000  ?  20  LEU A CG  1 
ATOM   287  C  CD1 A LEU A 1 20  ? 50.16200 39.83700 -7.38000  0.560 77.27000  ?  20  LEU A CD1 1 
ATOM   288  C  CD1 B LEU A 1 20  ? 49.91600 39.81800 -7.32900  0.440 76.79000  ?  20  LEU A CD1 1 
ATOM   289  C  CD2 A LEU A 1 20  ? 50.41000 40.86100 -5.10900  0.560 82.21000  ?  20  LEU A CD2 1 
ATOM   290  C  CD2 B LEU A 1 20  ? 49.84700 41.13000 -5.17200  0.440 81.56000  ?  20  LEU A CD2 1 
ATOM   291  N  N   A ALA A 1 21  ? 46.46100 43.97200 -7.11700  0.560 71.60000  ?  21  ALA A N   1 
ATOM   292  N  N   B ALA A 1 21  ? 46.22000 43.92400 -7.56900  0.440 66.94000  ?  21  ALA A N   1 
ATOM   293  C  CA  A ALA A 1 21  ? 45.91400 45.17700 -7.73200  0.560 60.24000  ?  21  ALA A CA  1 
ATOM   294  C  CA  B ALA A 1 21  ? 45.64300 45.11700 -8.18400  0.440 57.94000  ?  21  ALA A CA  1 
ATOM   295  C  C   A ALA A 1 21  ? 45.58600 46.22500 -6.67600  0.560 71.12000  ?  21  ALA A C   1 
ATOM   296  C  C   B ALA A 1 21  ? 45.28100 46.21600 -7.20000  0.440 67.73000  ?  21  ALA A C   1 
ATOM   297  O  O   A ALA A 1 21  ? 45.93000 47.40300 -6.82500  0.560 74.88000  ?  21  ALA A O   1 
ATOM   298  O  O   B ALA A 1 21  ? 45.68400 47.37600 -7.35400  0.440 70.54000  ?  21  ALA A O   1 
ATOM   299  C  CB  A ALA A 1 21  ? 44.67100 44.83100 -8.55200  0.560 60.15000  ?  21  ALA A CB  1 
ATOM   300  C  CB  B ALA A 1 21  ? 44.39500 44.71000 -8.95100  0.440 61.76000  ?  21  ALA A CB  1 
ATOM   301  N  N   A PHE A 1 22  ? 44.91500 45.81400 -5.59500  0.560 65.12000  ?  22  PHE A N   1 
ATOM   302  N  N   B PHE A 1 22  ? 44.43900 45.87200 -6.23500  0.440 63.92000  ?  22  PHE A N   1 
ATOM   303  C  CA  A PHE A 1 22  ? 44.55000 46.77200 -4.55600  0.560 69.20000  ?  22  PHE A CA  1 
ATOM   304  C  CA  B PHE A 1 22  ? 44.18900 46.75600 -5.11700  0.440 65.71000  ?  22  PHE A CA  1 
ATOM   305  C  C   A PHE A 1 22  ? 45.79000 47.31900 -3.85400  0.560 75.02000  ?  22  PHE A C   1 
ATOM   306  C  C   B PHE A 1 22  ? 45.49600 47.22000 -4.47700  0.440 74.72000  ?  22  PHE A C   1 
ATOM   307  O  O   A PHE A 1 22  ? 45.87300 48.52300 -3.58500  0.560 79.93000  ?  22  PHE A O   1 
ATOM   308  O  O   B PHE A 1 22  ? 45.67300 48.41600 -4.21200  0.440 80.12000  ?  22  PHE A O   1 
ATOM   309  C  CB  A PHE A 1 22  ? 43.59500 46.13100 -3.54400  0.560 61.45000  ?  22  PHE A CB  1 
ATOM   310  C  CB  B PHE A 1 22  ? 43.29800 46.04900 -4.08900  0.440 61.23000  ?  22  PHE A CB  1 
ATOM   311  C  CG  A PHE A 1 22  ? 42.37300 45.50700 -4.16900  0.560 58.10000  ?  22  PHE A CG  1 
ATOM   312  C  CG  B PHE A 1 22  ? 41.98500 45.54300 -4.63900  0.440 58.55000  ?  22  PHE A CG  1 
ATOM   313  C  CD1 A PHE A 1 22  ? 41.72300 46.12400 -5.22900  0.560 58.03000  ?  22  PHE A CD1 1 
ATOM   314  C  CD1 B PHE A 1 22  ? 41.32600 46.23500 -5.65100  0.440 54.10000  ?  22  PHE A CD1 1 
ATOM   315  C  CD2 A PHE A 1 22  ? 41.87800 44.29900 -3.70100  0.560 52.61000  ?  22  PHE A CD2 1 
ATOM   316  C  CD2 B PHE A 1 22  ? 41.36700 44.40900 -4.08500  0.440 53.13000  ?  22  PHE A CD2 1 
ATOM   317  C  CE1 A PHE A 1 22  ? 40.60500 45.54900 -5.80700  0.560 51.85000  ?  22  PHE A CE1 1 
ATOM   318  C  CE1 B PHE A 1 22  ? 40.10300 45.78900 -6.13700  0.440 51.60000  ?  22  PHE A CE1 1 
ATOM   319  C  CE2 A PHE A 1 22  ? 40.76100 43.72000 -4.27600  0.560 51.43000  ?  22  PHE A CE2 1 
ATOM   320  C  CE2 B PHE A 1 22  ? 40.12800 43.94000 -4.56200  0.440 51.27000  ?  22  PHE A CE2 1 
ATOM   321  C  CZ  A PHE A 1 22  ? 40.12600 44.34500 -5.33100  0.560 52.78000  ?  22  PHE A CZ  1 
ATOM   322  C  CZ  B PHE A 1 22  ? 39.49300 44.63200 -5.58700  0.440 51.58000  ?  22  PHE A CZ  1 
ATOM   323  N  N   A ALA A 1 23  ? 46.76600 46.45700 -3.55600  0.560 78.05000  ?  23  ALA A N   1 
ATOM   324  N  N   B ALA A 1 23  ? 46.43200 46.29300 -4.22600  0.440 71.38000  ?  23  ALA A N   1 
ATOM   325  C  CA  A ALA A 1 23  ? 47.97800 46.92500 -2.88800  0.560 81.33000  ?  23  ALA A CA  1 
ATOM   326  C  CA  B ALA A 1 23  ? 47.66400 46.69800 -3.55300  0.440 80.66000  ?  23  ALA A CA  1 
ATOM   327  C  C   A ALA A 1 23  ? 48.69900 47.96000 -3.73900  0.560 97.56000  ?  23  ALA A C   1 
ATOM   328  C  C   B ALA A 1 23  ? 48.37700 47.76400 -4.36100  0.440 93.86000  ?  23  ALA A C   1 
ATOM   329  O  O   A ALA A 1 23  ? 49.19000 48.97500 -3.22400  0.560 107.62000 ?  23  ALA A O   1 
ATOM   330  O  O   B ALA A 1 23  ? 48.87900 48.74600 -3.80500  0.440 103.59000 ?  23  ALA A O   1 
ATOM   331  C  CB  A ALA A 1 23  ? 48.89900 45.74300 -2.58400  0.560 72.65000  ?  23  ALA A CB  1 
ATOM   332  C  CB  B ALA A 1 23  ? 48.58400 45.49900 -3.31100  0.440 77.25000  ?  23  ALA A CB  1 
ATOM   333  N  N   A TRP A 1 24  ? 48.76400 47.72200 -5.04900  0.560 99.40000  ?  24  TRP A N   1 
ATOM   334  N  N   B TRP A 1 24  ? 48.37500 47.61900 -5.68400  0.440 98.22000  ?  24  TRP A N   1 
ATOM   335  C  CA  A TRP A 1 24  ? 49.41500 48.66800 -5.94700  0.560 109.42000 ?  24  TRP A CA  1 
ATOM   336  C  CA  B TRP A 1 24  ? 49.13200 48.54300 -6.50800  0.440 108.26000 ?  24  TRP A CA  1 
ATOM   337  C  C   A TRP A 1 24  ? 48.71200 50.02000 -5.93600  0.560 115.80000 ?  24  TRP A C   1 
ATOM   338  C  C   B TRP A 1 24  ? 48.50500 49.92900 -6.49900  0.440 114.87000 ?  24  TRP A C   1 
ATOM   339  O  O   A TRP A 1 24  ? 49.34600 51.06500 -5.78100  0.560 129.79000 ?  24  TRP A O   1 
ATOM   340  O  O   B TRP A 1 24  ? 49.19100 50.93300 -6.27300  0.440 128.98000 ?  24  TRP A O   1 
ATOM   341  C  CB  A TRP A 1 24  ? 49.41600 48.12500 -7.36700  0.560 108.21000 ?  24  TRP A CB  1 
ATOM   342  C  CB  B TRP A 1 24  ? 49.26400 48.01900 -7.93500  0.440 110.20000 ?  24  TRP A CB  1 
ATOM   343  C  CG  A TRP A 1 24  ? 50.41600 48.79300 -8.22600  0.560 127.84000 ?  24  TRP A CG  1 
ATOM   344  C  CG  B TRP A 1 24  ? 50.34700 48.77100 -8.59000  0.440 128.34000 ?  24  TRP A CG  1 
ATOM   345  C  CD1 A TRP A 1 24  ? 50.19000 49.48300 -9.37600  0.560 131.55000 ?  24  TRP A CD1 1 
ATOM   346  C  CD1 B TRP A 1 24  ? 50.23300 49.61700 -9.65000  0.440 132.19000 ?  24  TRP A CD1 1 
ATOM   347  C  CD2 A TRP A 1 24  ? 51.82100 48.85500 -7.98800  0.560 141.67000 ?  24  TRP A CD2 1 
ATOM   348  C  CD2 B TRP A 1 24  ? 51.72500 48.82700 -8.17200  0.440 141.19000 ?  24  TRP A CD2 1 
ATOM   349  N  NE1 A TRP A 1 24  ? 51.37700 49.94700 -9.89000  0.560 140.55000 ?  24  TRP A NE1 1 
ATOM   350  N  NE1 B TRP A 1 24  ? 51.45600 50.17600 -9.94200  0.440 140.38000 ?  24  TRP A NE1 1 
ATOM   351  C  CE2 A TRP A 1 24  ? 52.39300 49.58500 -9.04500  0.560 146.26000 ?  24  TRP A CE2 1 
ATOM   352  C  CE2 B TRP A 1 24  ? 52.38900 49.70900 -9.05000  0.440 146.12000 ?  24  TRP A CE2 1 
ATOM   353  C  CE3 A TRP A 1 24  ? 52.65200 48.36300 -6.97900  0.560 145.66000 ?  24  TRP A CE3 1 
ATOM   354  C  CE3 B TRP A 1 24  ? 52.46500 48.20500 -7.15100  0.440 144.54000 ?  24  TRP A CE3 1 
ATOM   355  C  CZ2 A TRP A 1 24  ? 53.76000 49.83200 -9.12400  0.560 149.04000 ?  24  TRP A CZ2 1 
ATOM   356  C  CZ2 B TRP A 1 24  ? 53.77000 49.98900 -8.93900  0.440 148.86000 ?  24  TRP A CZ2 1 
ATOM   357  C  CZ3 A TRP A 1 24  ? 54.00700 48.60900 -7.05800  0.560 153.80000 ?  24  TRP A CZ3 1 
ATOM   358  C  CZ3 B TRP A 1 24  ? 53.83400 48.48600 -7.04000  0.440 153.51000 ?  24  TRP A CZ3 1 
ATOM   359  C  CH2 A TRP A 1 24  ? 54.54900 49.33600 -8.12300  0.560 151.68000 ?  24  TRP A CH2 1 
ATOM   360  C  CH2 B TRP A 1 24  ? 54.46900 49.36900 -7.93000  0.440 151.61000 ?  24  TRP A CH2 1 
ATOM   361  N  N   A ALA A 1 25  ? 47.39200 50.01700 -6.10900  0.560 93.30000  ?  25  ALA A N   1 
ATOM   362  N  N   B ALA A 1 25  ? 47.20100 50.00900 -6.72900  0.440 92.95000  ?  25  ALA A N   1 
ATOM   363  C  CA  A ALA A 1 25  ? 46.63900 51.26400 -6.13400  0.560 91.94000  ?  25  ALA A CA  1 
ATOM   364  C  CA  B ALA A 1 25  ? 46.57500 51.31800 -6.76800  0.440 89.78000  ?  25  ALA A CA  1 
ATOM   365  C  C   A ALA A 1 25  ? 46.74100 52.01200 -4.81700  0.560 104.77000 ?  25  ALA A C   1 
ATOM   366  C  C   B ALA A 1 25  ? 46.72300 52.05600 -5.45300  0.440 102.87000 ?  25  ALA A C   1 
ATOM   367  O  O   A ALA A 1 25  ? 46.56500 53.23300 -4.79400  0.560 111.44000 ?  25  ALA A O   1 
ATOM   368  O  O   B ALA A 1 25  ? 46.48700 53.26700 -5.40400  0.440 107.22000 ?  25  ALA A O   1 
ATOM   369  C  CB  A ALA A 1 25  ? 45.17300 50.97100 -6.46100  0.560 83.22000  ?  25  ALA A CB  1 
ATOM   370  C  CB  B ALA A 1 25  ? 45.10700 51.18200 -7.13200  0.440 80.21000  ?  25  ALA A CB  1 
ATOM   371  N  N   A GLY A 1 26  ? 47.01500 51.30900 -3.72200  0.560 106.19000 ?  26  GLY A N   1 
ATOM   372  N  N   B GLY A 1 26  ? 47.12200 51.35600 -4.39700  0.440 104.13000 ?  26  GLY A N   1 
ATOM   373  C  CA  A GLY A 1 26  ? 47.15100 51.95500 -2.43100  0.560 119.64000 ?  26  GLY A CA  1 
ATOM   374  C  CA  B GLY A 1 26  ? 47.29600 51.90300 -3.06900  0.440 115.29000 ?  26  GLY A CA  1 
ATOM   375  C  C   A GLY A 1 26  ? 48.48700 52.60700 -2.16400  0.560 135.56000 ?  26  GLY A C   1 
ATOM   376  C  C   B GLY A 1 26  ? 48.70900 52.27400 -2.68600  0.440 132.28000 ?  26  GLY A C   1 
ATOM   377  O  O   A GLY A 1 26  ? 48.60400 53.36200 -1.19400  0.560 147.89000 ?  26  GLY A O   1 
ATOM   378  O  O   B GLY A 1 26  ? 48.98300 52.44700 -1.49200  0.440 142.05000 ?  26  GLY A O   1 
ATOM   379  N  N   A GLU A 1 33  ? 43.14800 58.19900 2.79100   0.560 128.35000 ?  33  GLU A N   1 
ATOM   380  N  N   B GLU A 1 33  ? 43.07700 58.22000 2.43800   0.440 127.07000 ?  33  GLU A N   1 
ATOM   381  C  CA  A GLU A 1 33  ? 42.47600 57.18500 1.99000   0.560 115.43000 ?  33  GLU A CA  1 
ATOM   382  C  CA  B GLU A 1 33  ? 42.36000 57.27900 1.58500   0.440 114.02000 ?  33  GLU A CA  1 
ATOM   383  C  C   A GLU A 1 33  ? 43.17300 55.83200 2.06200   0.560 115.99000 ?  33  GLU A C   1 
ATOM   384  C  C   B GLU A 1 33  ? 43.04700 55.91600 1.53300   0.440 114.77000 ?  33  GLU A C   1 
ATOM   385  O  O   A GLU A 1 33  ? 42.64600 54.85200 1.52500   0.560 103.99000 ?  33  GLU A O   1 
ATOM   386  O  O   B GLU A 1 33  ? 42.55000 55.00700 0.86000   0.440 103.42000 ?  33  GLU A O   1 
ATOM   387  C  CB  A GLU A 1 33  ? 42.38400 57.64200 0.53200   0.560 109.89000 ?  33  GLU A CB  1 
ATOM   388  C  CB  B GLU A 1 33  ? 42.20600 57.85800 0.17600   0.440 108.67000 ?  33  GLU A CB  1 
ATOM   389  N  N   A ARG A 1 35  ? 43.19400 53.87700 4.38000   0.560 98.25000  ?  35  ARG A N   1 
ATOM   390  N  N   B ARG A 1 35  ? 42.85600 53.88800 3.72900   0.440 96.87000  ?  35  ARG A N   1 
ATOM   391  C  CA  A ARG A 1 35  ? 42.33400 52.93500 5.09100   0.560 88.99000  ?  35  ARG A CA  1 
ATOM   392  C  CA  B ARG A 1 35  ? 41.93600 52.95700 4.37900   0.440 88.15000  ?  35  ARG A CA  1 
ATOM   393  C  C   A ARG A 1 35  ? 41.56700 52.04500 4.12100   0.560 83.55000  ?  35  ARG A C   1 
ATOM   394  C  C   B ARG A 1 35  ? 41.09000 52.17300 3.39600   0.440 79.54000  ?  35  ARG A C   1 
ATOM   395  O  O   A ARG A 1 35  ? 41.52100 50.82000 4.28600   0.560 76.30000  ?  35  ARG A O   1 
ATOM   396  O  O   B ARG A 1 35  ? 40.74300 51.02100 3.67200   0.440 73.22000  ?  35  ARG A O   1 
ATOM   397  C  CB  A ARG A 1 35  ? 41.35900 53.69400 5.99000   0.560 94.28000  ?  35  ARG A CB  1 
ATOM   398  C  CB  B ARG A 1 35  ? 41.01200 53.67800 5.35200   0.440 89.80000  ?  35  ARG A CB  1 
ATOM   399  C  CG  A ARG A 1 35  ? 41.81700 53.86500 7.42500   0.560 107.50000 ?  35  ARG A CG  1 
ATOM   400  C  CG  B ARG A 1 35  ? 41.32300 53.40400 6.81600   0.440 99.42000  ?  35  ARG A CG  1 
ATOM   401  C  CD  A ARG A 1 35  ? 40.88600 54.80200 8.18900   0.560 114.44000 ?  35  ARG A CD  1 
ATOM   402  C  CD  B ARG A 1 35  ? 40.49100 54.31000 7.69500   0.440 106.58000 ?  35  ARG A CD  1 
ATOM   403  N  NE  A ARG A 1 35  ? 40.48600 55.95800 7.38700   0.560 123.41000 ?  35  ARG A NE  1 
ATOM   404  N  NE  B ARG A 1 35  ? 40.25700 55.55900 6.98000   0.440 117.48000 ?  35  ARG A NE  1 
ATOM   405  C  CZ  A ARG A 1 35  ? 39.52600 56.81300 7.72300   0.560 123.05000 ?  35  ARG A CZ  1 
ATOM   406  C  CZ  B ARG A 1 35  ? 39.50200 56.56000 7.41100   0.440 121.98000 ?  35  ARG A CZ  1 
ATOM   407  N  NH1 A ARG A 1 35  ? 38.85600 56.65100 8.85500   0.560 124.30000 ?  35  ARG A NH1 1 
ATOM   408  N  NH1 B ARG A 1 35  ? 38.96300 56.54900 8.62100   0.440 124.14000 ?  35  ARG A NH1 1 
ATOM   409  N  NH2 A ARG A 1 35  ? 39.23700 57.83100 6.92400   0.560 121.26000 ?  35  ARG A NH2 1 
ATOM   410  N  NH2 B ARG A 1 35  ? 39.31500 57.61500 6.61900   0.440 120.55000 ?  35  ARG A NH2 1 
ATOM   411  N  N   A TYR A 1 36  ? 40.94000 52.65000 3.11100   0.560 79.73000  ?  36  TYR A N   1 
ATOM   412  N  N   B TYR A 1 36  ? 40.69900 52.77100 2.28300   0.440 78.63000  ?  36  TYR A N   1 
ATOM   413  C  CA  A TYR A 1 36  ? 40.12900 51.88000 2.17500   0.560 76.12000  ?  36  TYR A CA  1 
ATOM   414  C  CA  B TYR A 1 36  ? 39.87800 51.98000 1.38600   0.440 74.95000  ?  36  TYR A CA  1 
ATOM   415  C  C   A TYR A 1 36  ? 40.97400 50.84000 1.45000   0.560 76.28000  ?  36  TYR A C   1 
ATOM   416  C  C   B TYR A 1 36  ? 40.70400 50.91500 0.68800   0.440 74.55000  ?  36  TYR A C   1 
ATOM   417  O  O   A TYR A 1 36  ? 40.60200 49.66300 1.37200   0.560 70.36000  ?  36  TYR A O   1 
ATOM   418  O  O   B TYR A 1 36  ? 40.32100 49.73400 0.66900   0.440 70.02000  ?  36  TYR A O   1 
ATOM   419  C  CB  A TYR A 1 36  ? 39.45700 52.81800 1.17200   0.560 74.31000  ?  36  TYR A CB  1 
ATOM   420  C  CB  B TYR A 1 36  ? 39.17000 52.85100 0.35900   0.440 73.98000  ?  36  TYR A CB  1 
ATOM   421  C  CG  A TYR A 1 36  ? 38.56800 53.86300 1.80400   0.560 74.87000  ?  36  TYR A CG  1 
ATOM   422  C  CG  B TYR A 1 36  ? 38.16500 53.83300 0.92200   0.440 74.79000  ?  36  TYR A CG  1 
ATOM   423  C  CD1 A TYR A 1 36  ? 37.22700 53.60500 2.05000   0.560 71.02000  ?  36  TYR A CD1 1 
ATOM   424  C  CD1 B TYR A 1 36  ? 36.83900 53.43700 1.18400   0.440 63.96000  ?  36  TYR A CD1 1 
ATOM   425  C  CD2 A TYR A 1 36  ? 39.07000 55.11000 2.15400   0.560 79.20000  ?  36  TYR A CD2 1 
ATOM   426  C  CD2 B TYR A 1 36  ? 38.50400 55.18200 1.07500   0.440 75.08000  ?  36  TYR A CD2 1 
ATOM   427  C  CE1 A TYR A 1 36  ? 36.41000 54.55600 2.62800   0.560 77.58000  ?  36  TYR A CE1 1 
ATOM   428  C  CE1 B TYR A 1 36  ? 35.90300 54.32900 1.66500   0.440 68.98000  ?  36  TYR A CE1 1 
ATOM   429  C  CE2 A TYR A 1 36  ? 38.26000 56.06900 2.73300   0.560 88.04000  ?  36  TYR A CE2 1 
ATOM   430  C  CE2 B TYR A 1 36  ? 37.58600 56.09200 1.53000   0.440 78.08000  ?  36  TYR A CE2 1 
ATOM   431  C  CZ  A TYR A 1 36  ? 36.93100 55.78600 2.96700   0.560 81.04000  ?  36  TYR A CZ  1 
ATOM   432  C  CZ  B TYR A 1 36  ? 36.29000 55.67000 1.83000   0.440 78.05000  ?  36  TYR A CZ  1 
ATOM   433  O  OH  A TYR A 1 36  ? 36.11500 56.73200 3.54200   0.560 80.18000  ?  36  TYR A OH  1 
ATOM   434  O  OH  B TYR A 1 36  ? 35.38500 56.59500 2.29500   0.440 75.39000  ?  36  TYR A OH  1 
ATOM   435  N  N   A TYR A 1 37  ? 42.12100 51.25800 0.91100   0.560 78.60000  ?  37  TYR A N   1 
ATOM   436  N  N   B TYR A 1 37  ? 41.84100 51.31700 0.11600   0.440 77.01000  ?  37  TYR A N   1 
ATOM   437  C  CA  A TYR A 1 37  ? 42.95500 50.33300 0.15300   0.560 76.35000  ?  37  TYR A CA  1 
ATOM   438  C  CA  B TYR A 1 37  ? 42.66400 50.36800 -0.62000  0.440 76.73000  ?  37  TYR A CA  1 
ATOM   439  C  C   A TYR A 1 37  ? 43.48500 49.21200 1.03900   0.560 74.64000  ?  37  TYR A C   1 
ATOM   440  C  C   B TYR A 1 37  ? 43.10900 49.21900 0.27500   0.440 71.75000  ?  37  TYR A C   1 
ATOM   441  O  O   A TYR A 1 37  ? 43.57600 48.05800 0.60400   0.560 71.28000  ?  37  TYR A O   1 
ATOM   442  O  O   B TYR A 1 37  ? 42.96200 48.05000 -0.10100  0.440 67.21000  ?  37  TYR A O   1 
ATOM   443  C  CB  A TYR A 1 37  ? 44.10600 51.09200 -0.50600  0.560 88.22000  ?  37  TYR A CB  1 
ATOM   444  C  CB  B TYR A 1 37  ? 43.86200 51.08100 -1.24000  0.440 89.36000  ?  37  TYR A CB  1 
ATOM   445  C  CG  A TYR A 1 37  ? 43.67500 52.01300 -1.62600  0.560 93.15000  ?  37  TYR A CG  1 
ATOM   446  C  CG  B TYR A 1 37  ? 43.49300 52.11700 -2.28700  0.440 92.26000  ?  37  TYR A CG  1 
ATOM   447  C  CD1 A TYR A 1 37  ? 43.49100 51.53000 -2.91500  0.560 88.03000  ?  37  TYR A CD1 1 
ATOM   448  C  CD1 B TYR A 1 37  ? 43.11200 51.74200 -3.55900  0.440 87.44000  ?  37  TYR A CD1 1 
ATOM   449  C  CD2 A TYR A 1 37  ? 43.45300 53.36300 -1.39500  0.560 101.13000 ?  37  TYR A CD2 1 
ATOM   450  C  CD2 B TYR A 1 37  ? 43.58000 53.47600 -2.01000  0.440 101.27000 ?  37  TYR A CD2 1 
ATOM   451  C  CE1 A TYR A 1 37  ? 43.09900 52.36700 -3.94200  0.560 90.59000  ?  37  TYR A CE1 1 
ATOM   452  C  CE1 B TYR A 1 37  ? 42.79900 52.69100 -4.50500  0.440 92.43000  ?  37  TYR A CE1 1 
ATOM   453  C  CE2 A TYR A 1 37  ? 43.06100 54.20900 -2.41500  0.560 102.12000 ?  37  TYR A CE2 1 
ATOM   454  C  CE2 B TYR A 1 37  ? 43.26600 54.42000 -2.96000  0.440 102.11000 ?  37  TYR A CE2 1 
ATOM   455  C  CZ  A TYR A 1 37  ? 42.88600 53.70500 -3.68700  0.560 91.92000  ?  37  TYR A CZ  1 
ATOM   456  C  CZ  B TYR A 1 37  ? 42.87900 54.01800 -4.20300  0.440 93.16000  ?  37  TYR A CZ  1 
ATOM   457  O  OH  A TYR A 1 37  ? 42.49400 54.54200 -4.70700  0.560 96.56000  ?  37  TYR A OH  1 
ATOM   458  O  OH  B TYR A 1 37  ? 42.56600 54.94400 -5.17000  0.440 99.79000  ?  37  TYR A OH  1 
ATOM   459  N  N   A VAL A 1 38  ? 43.83700 49.52700 2.28600   0.560 72.24000  ?  38  VAL A N   1 
ATOM   460  N  N   B VAL A 1 38  ? 43.61200 49.53800 1.47800   0.440 75.90000  ?  38  VAL A N   1 
ATOM   461  C  CA  A VAL A 1 38  ? 44.33500 48.49300 3.18800   0.560 70.59000  ?  38  VAL A CA  1 
ATOM   462  C  CA  B VAL A 1 38  ? 43.95800 48.52700 2.47400   0.440 68.44000  ?  38  VAL A CA  1 
ATOM   463  C  C   A VAL A 1 38  ? 43.23000 47.49700 3.51700   0.560 59.22000  ?  38  VAL A C   1 
ATOM   464  C  C   B VAL A 1 38  ? 42.78200 47.57800 2.73000   0.440 58.93000  ?  38  VAL A C   1 
ATOM   465  O  O   A VAL A 1 38  ? 43.48200 46.29600 3.66700   0.560 63.38000  ?  38  VAL A O   1 
ATOM   466  O  O   B VAL A 1 38  ? 42.95600 46.36100 2.73600   0.440 56.33000  ?  38  VAL A O   1 
ATOM   467  C  CB  A VAL A 1 38  ? 44.92400 49.13000 4.46000   0.560 76.13000  ?  38  VAL A CB  1 
ATOM   468  C  CB  B VAL A 1 38  ? 44.43800 49.21600 3.76600   0.440 73.65000  ?  38  VAL A CB  1 
ATOM   469  C  CG1 A VAL A 1 38  ? 45.22100 48.06300 5.50300   0.560 71.62000  ?  38  VAL A CG1 1 
ATOM   470  C  CG1 B VAL A 1 38  ? 44.53500 48.20600 4.91100   0.440 75.19000  ?  38  VAL A CG1 1 
ATOM   471  C  CG2 A VAL A 1 38  ? 46.17700 49.92500 4.11700   0.560 81.22000  ?  38  VAL A CG2 1 
ATOM   472  C  CG2 B VAL A 1 38  ? 45.76000 49.86300 3.54400   0.440 77.92000  ?  38  VAL A CG2 1 
ATOM   473  N  N   A THR A 1 39  ? 41.98900 47.97700 3.63800   0.560 55.51000  ?  39  THR A N   1 
ATOM   474  N  N   B THR A 1 39  ? 41.57700 48.11200 2.95000   0.440 59.63000  ?  39  THR A N   1 
ATOM   475  C  CA  A THR A 1 39  ? 40.87700 47.07300 3.91300   0.560 56.95000  ?  39  THR A CA  1 
ATOM   476  C  CA  B THR A 1 39  ? 40.40700 47.26100 3.16900   0.440 56.83000  ?  39  THR A CA  1 
ATOM   477  C  C   A THR A 1 39  ? 40.64800 46.12000 2.74700   0.560 56.13000  ?  39  THR A C   1 
ATOM   478  C  C   B THR A 1 39  ? 40.24400 46.23500 2.06000   0.440 57.76000  ?  39  THR A C   1 
ATOM   479  O  O   A THR A 1 39  ? 40.44200 44.91900 2.95000   0.560 52.88000  ?  39  THR A O   1 
ATOM   480  O  O   B THR A 1 39  ? 40.02900 45.04400 2.31700   0.440 54.90000  ?  39  THR A O   1 
ATOM   481  C  CB  A THR A 1 39  ? 39.60800 47.87500 4.20700   0.560 57.33000  ?  39  THR A CB  1 
ATOM   482  C  CB  B THR A 1 39  ? 39.14900 48.10600 3.24400   0.440 57.18000  ?  39  THR A CB  1 
ATOM   483  O  OG1 A THR A 1 39  ? 39.87300 48.82200 5.25000   0.560 67.08000  ?  39  THR A OG1 1 
ATOM   484  O  OG1 B THR A 1 39  ? 39.41600 49.30300 3.97000   0.440 61.25000  ?  39  THR A OG1 1 
ATOM   485  C  CG2 A THR A 1 39  ? 38.47000 46.95600 4.63600   0.560 55.25000  ?  39  THR A CG2 1 
ATOM   486  C  CG2 B THR A 1 39  ? 38.03500 47.33300 3.97400   0.440 52.96000  ?  39  THR A CG2 1 
ATOM   487  N  N   A LEU A 1 40  ? 40.69700 46.63200 1.51800   0.560 59.04000  ?  40  LEU A N   1 
ATOM   488  N  N   B LEU A 1 40  ? 40.32700 46.68800 0.81300   0.440 57.14000  ?  40  LEU A N   1 
ATOM   489  C  CA  A LEU A 1 40  ? 40.48200 45.77000 0.36100   0.560 51.49000  ?  40  LEU A CA  1 
ATOM   490  C  CA  B LEU A 1 40  ? 40.16300 45.78300 -0.30900  0.440 52.32000  ?  40  LEU A CA  1 
ATOM   491  C  C   A LEU A 1 40  ? 41.58100 44.72000 0.24900   0.560 51.09000  ?  40  LEU A C   1 
ATOM   492  C  C   B LEU A 1 40  ? 41.27400 44.75100 -0.35400  0.440 50.31000  ?  40  LEU A C   1 
ATOM   493  O  O   A LEU A 1 40  ? 41.32000 43.57600 -0.14600  0.560 49.82000  ?  40  LEU A O   1 
ATOM   494  O  O   B LEU A 1 40  ? 41.01900 43.56100 -0.58500  0.440 45.95000  ?  40  LEU A O   1 
ATOM   495  C  CB  A LEU A 1 40  ? 40.39200 46.62000 -0.90500  0.560 57.53000  ?  40  LEU A CB  1 
ATOM   496  C  CB  B LEU A 1 40  ? 40.12500 46.57600 -1.60600  0.440 57.24000  ?  40  LEU A CB  1 
ATOM   497  C  CG  A LEU A 1 40  ? 39.10200 47.44700 -0.94200  0.560 55.24000  ?  40  LEU A CG  1 
ATOM   498  C  CG  B LEU A 1 40  ? 38.87700 47.44200 -1.68100  0.440 54.66000  ?  40  LEU A CG  1 
ATOM   499  C  CD1 A LEU A 1 40  ? 39.22500 48.54900 -1.97600  0.560 58.17000  ?  40  LEU A CD1 1 
ATOM   500  C  CD1 B LEU A 1 40  ? 39.06300 48.47800 -2.77000  0.440 56.06000  ?  40  LEU A CD1 1 
ATOM   501  C  CD2 A LEU A 1 40  ? 37.89800 46.55900 -1.21400  0.560 54.25000  ?  40  LEU A CD2 1 
ATOM   502  C  CD2 B LEU A 1 40  ? 37.64900 46.59300 -1.94600  0.440 53.03000  ?  40  LEU A CD2 1 
ATOM   503  N  N   A VAL A 1 41  ? 42.81900 45.08200 0.58900   0.560 55.54000  ?  41  VAL A N   1 
ATOM   504  N  N   B VAL A 1 41  ? 42.52200 45.19000 -0.15700  0.440 53.75000  ?  41  VAL A N   1 
ATOM   505  C  CA  A VAL A 1 41  ? 43.88300 44.08100 0.59500   0.560 53.84000  ?  41  VAL A CA  1 
ATOM   506  C  CA  B VAL A 1 41  ? 43.63800 44.24600 -0.18300  0.440 56.63000  ?  41  VAL A CA  1 
ATOM   507  C  C   A VAL A 1 41  ? 43.56000 42.97900 1.59800   0.560 54.39000  ?  41  VAL A C   1 
ATOM   508  C  C   B VAL A 1 41  ? 43.44000 43.17700 0.87500   0.440 51.77000  ?  41  VAL A C   1 
ATOM   509  O  O   A VAL A 1 41  ? 43.76400 41.78900 1.32700   0.560 58.51000  ?  41  VAL A O   1 
ATOM   510  O  O   B VAL A 1 41  ? 43.79200 42.00400 0.67300   0.440 48.48000  ?  41  VAL A O   1 
ATOM   511  C  CB  A VAL A 1 41  ? 45.24900 44.73000 0.88900   0.560 50.25000  ?  41  VAL A CB  1 
ATOM   512  C  CB  B VAL A 1 41  ? 44.98400 44.96600 0.01800   0.440 58.63000  ?  41  VAL A CB  1 
ATOM   513  C  CG1 A VAL A 1 41  ? 46.30800 43.65500 1.13200   0.560 56.68000  ?  41  VAL A CG1 1 
ATOM   514  C  CG1 B VAL A 1 41  ? 46.07600 43.92600 0.05800   0.440 58.31000  ?  41  VAL A CG1 1 
ATOM   515  C  CG2 A VAL A 1 41  ? 45.66100 45.63500 -0.26000  0.560 57.24000  ?  41  VAL A CG2 1 
ATOM   516  C  CG2 B VAL A 1 41  ? 45.26300 45.93200 -1.09700  0.440 58.97000  ?  41  VAL A CG2 1 
ATOM   517  N  N   A GLY A 1 42  ? 43.04400 43.35600 2.76900   0.560 49.61000  ?  42  GLY A N   1 
ATOM   518  N  N   B GLY A 1 42  ? 42.89300 43.58700 2.02600   0.440 49.66000  ?  42  GLY A N   1 
ATOM   519  C  CA  A GLY A 1 42  ? 42.67900 42.35600 3.75800   0.560 41.65000  ?  42  GLY A CA  1 
ATOM   520  C  CA  B GLY A 1 42  ? 42.64200 42.66200 3.12100   0.440 47.97000  ?  42  GLY A CA  1 
ATOM   521  C  C   A GLY A 1 42  ? 41.53700 41.47100 3.29800   0.560 48.61000  ?  42  GLY A C   1 
ATOM   522  C  C   B GLY A 1 42  ? 41.42600 41.80400 2.85500   0.440 48.76000  ?  42  GLY A C   1 
ATOM   523  O  O   A GLY A 1 42  ? 41.55500 40.25500 3.51300   0.560 47.00000  ?  42  GLY A O   1 
ATOM   524  O  O   B GLY A 1 42  ? 41.43300 40.59100 3.14300   0.440 49.02000  ?  42  GLY A O   1 
ATOM   525  N  N   A ILE A 1 43  ? 40.53900 42.06600 2.64000   0.560 45.32000  ?  43  ILE A N   1 
ATOM   526  N  N   B ILE A 1 43  ? 40.38700 42.40800 2.25700   0.440 42.21000  ?  43  ILE A N   1 
ATOM   527  C  CA  A ILE A 1 43  ? 39.37700 41.30400 2.19000   0.560 49.72000  ?  43  ILE A CA  1 
ATOM   528  C  CA  B ILE A 1 43  ? 39.25900 41.60500 1.81300   0.440 50.42000  ?  43  ILE A CA  1 
ATOM   529  C  C   A ILE A 1 43  ? 39.79800 40.20100 1.22800   0.560 48.20000  ?  43  ILE A C   1 
ATOM   530  C  C   B ILE A 1 43  ? 39.73900 40.44300 0.94700   0.440 48.24000  ?  43  ILE A C   1 
ATOM   531  O  O   A ILE A 1 43  ? 39.42700 39.03500 1.39300   0.560 47.18000  ?  43  ILE A O   1 
ATOM   532  O  O   B ILE A 1 43  ? 39.40900 39.28100 1.20300   0.440 46.02000  ?  43  ILE A O   1 
ATOM   533  C  CB  A ILE A 1 43  ? 38.33900 42.24000 1.54500   0.560 48.71000  ?  43  ILE A CB  1 
ATOM   534  C  CB  B ILE A 1 43  ? 38.21800 42.44400 1.05800   0.440 47.56000  ?  43  ILE A CB  1 
ATOM   535  C  CG1 A ILE A 1 43  ? 37.66500 43.10100 2.61100   0.560 42.06000  ?  43  ILE A CG1 1 
ATOM   536  C  CG1 B ILE A 1 43  ? 37.41400 43.32600 2.02400   0.440 44.75000  ?  43  ILE A CG1 1 
ATOM   537  C  CG2 A ILE A 1 43  ? 37.31600 41.44000 0.75800   0.560 41.85000  ?  43  ILE A CG2 1 
ATOM   538  C  CG2 B ILE A 1 43  ? 37.30500 41.46400 0.25300   0.440 42.82000  ?  43  ILE A CG2 1 
ATOM   539  C  CD1 A ILE A 1 43  ? 37.05800 44.37300 2.07100   0.560 42.58000  ?  43  ILE A CD1 1 
ATOM   540  C  CD1 B ILE A 1 43  ? 36.76100 44.46900 1.35800   0.440 43.13000  ?  43  ILE A CD1 1 
ATOM   541  N  N   A SER A 1 44  ? 40.54500 40.55200 0.18600   0.560 43.43000  ?  44  SER A N   1 
ATOM   542  N  N   B SER A 1 44  ? 40.45200 40.74000 -0.14600  0.440 44.49000  ?  44  SER A N   1 
ATOM   543  C  CA  A SER A 1 44  ? 40.93600 39.54700 -0.79500  0.560 47.78000  ?  44  SER A CA  1 
ATOM   544  C  CA  B SER A 1 44  ? 40.67300 39.62400 -1.05400  0.440 47.84000  ?  44  SER A CA  1 
ATOM   545  C  C   A SER A 1 44  ? 42.17700 38.77300 -0.37800  0.560 46.63000  ?  44  SER A C   1 
ATOM   546  C  C   B SER A 1 44  ? 41.94400 38.91300 -0.70400  0.440 47.20000  ?  44  SER A C   1 
ATOM   547  O  O   A SER A 1 44  ? 42.32100 37.60100 -0.74800  0.560 47.66000  ?  44  SER A O   1 
ATOM   548  O  O   B SER A 1 44  ? 42.07200 37.72900 -1.02700  0.440 46.18000  ?  44  SER A O   1 
ATOM   549  C  CB  A SER A 1 44  ? 41.16800 40.19500 -2.16200  0.560 50.76000  ?  44  SER A CB  1 
ATOM   550  C  CB  B SER A 1 44  ? 40.66100 40.03900 -2.54400  0.440 49.16000  ?  44  SER A CB  1 
ATOM   551  O  OG  A SER A 1 44  ? 42.02900 41.31200 -2.06600  0.560 53.57000  ?  44  SER A OG  1 
ATOM   552  O  OG  B SER A 1 44  ? 41.34700 41.24100 -2.77500  0.440 47.78000  ?  44  SER A OG  1 
ATOM   553  N  N   A GLY A 1 45  ? 43.05900 39.39100 0.40900   0.560 42.97000  ?  45  GLY A N   1 
ATOM   554  N  N   B GLY A 1 45  ? 42.82200 39.58300 0.03900   0.440 42.74000  ?  45  GLY A N   1 
ATOM   555  C  CA  A GLY A 1 45  ? 44.24200 38.68600 0.86800   0.560 47.41000  ?  45  GLY A CA  1 
ATOM   556  C  CA  B GLY A 1 45  ? 43.97600 38.89800 0.58700   0.440 45.92000  ?  45  GLY A CA  1 
ATOM   557  C  C   A GLY A 1 45  ? 43.91300 37.52600 1.78500   0.560 48.02000  ?  45  GLY A C   1 
ATOM   558  C  C   B GLY A 1 45  ? 43.60100 37.84500 1.61000   0.440 47.06000  ?  45  GLY A C   1 
ATOM   559  O  O   A GLY A 1 45  ? 44.49900 36.44800 1.67000   0.560 47.22000  ?  45  GLY A O   1 
ATOM   560  O  O   B GLY A 1 45  ? 44.12000 36.72600 1.57600   0.440 49.25000  ?  45  GLY A O   1 
ATOM   561  N  N   A ILE A 1 46  ? 42.97700 37.73100 2.71400   0.560 39.10000  ?  46  ILE A N   1 
ATOM   562  N  N   B ILE A 1 46  ? 42.70300 38.17000 2.52900   0.440 40.84000  ?  46  ILE A N   1 
ATOM   563  C  CA  A ILE A 1 46  ? 42.57400 36.64400 3.59700   0.560 44.95000  ?  46  ILE A CA  1 
ATOM   564  C  CA  B ILE A 1 46  ? 42.22900 37.09400 3.37700   0.440 47.37000  ?  46  ILE A CA  1 
ATOM   565  C  C   A ILE A 1 46  ? 41.90200 35.53600 2.79600   0.560 43.13000  ?  46  ILE A C   1 
ATOM   566  C  C   B ILE A 1 46  ? 41.63800 36.02900 2.48500   0.440 44.31000  ?  46  ILE A C   1 
ATOM   567  O  O   A ILE A 1 46  ? 42.18500 34.34900 2.99500   0.560 43.52000  ?  46  ILE A O   1 
ATOM   568  O  O   B ILE A 1 46  ? 41.86800 34.83600 2.68300   0.440 43.07000  ?  46  ILE A O   1 
ATOM   569  C  CB  A ILE A 1 46  ? 41.65600 37.17700 4.71200   0.560 38.66000  ?  46  ILE A CB  1 
ATOM   570  C  CB  B ILE A 1 46  ? 41.23400 37.62300 4.42400   0.440 40.34000  ?  46  ILE A CB  1 
ATOM   571  C  CG1 A ILE A 1 46  ? 42.45700 38.03800 5.69300   0.560 40.18000  ?  46  ILE A CG1 1 
ATOM   572  C  CG1 B ILE A 1 46  ? 42.03200 38.36500 5.46700   0.440 40.82000  ?  46  ILE A CG1 1 
ATOM   573  C  CG2 A ILE A 1 46  ? 40.98600 36.02400 5.44700   0.560 36.85000  ?  46  ILE A CG2 1 
ATOM   574  C  CG2 B ILE A 1 46  ? 40.52800 36.47400 5.10600   0.440 37.84000  ?  46  ILE A CG2 1 
ATOM   575  C  CD1 A ILE A 1 46  ? 41.61500 38.95800 6.55400   0.560 48.45000  ?  46  ILE A CD1 1 
ATOM   576  C  CD1 B ILE A 1 46  ? 41.28500 39.47000 6.14100   0.440 48.80000  ?  46  ILE A CD1 1 
ATOM   577  N  N   A ALA A 1 47  ? 41.01400 35.90400 1.86900   0.560 45.34000  ?  47  ALA A N   1 
ATOM   578  N  N   B ALA A 1 47  ? 41.01000 36.45600 1.39300   0.440 44.01000  ?  47  ALA A N   1 
ATOM   579  C  CA  A ALA A 1 47  ? 40.34600 34.89600 1.05200   0.560 44.00000  ?  47  ALA A CA  1 
ATOM   580  C  CA  B ALA A 1 47  ? 40.26200 35.51100 0.56300   0.440 43.37000  ?  47  ALA A CA  1 
ATOM   581  C  C   A ALA A 1 47  ? 41.35100 34.11700 0.21100   0.560 44.24000  ?  47  ALA A C   1 
ATOM   582  C  C   B ALA A 1 47  ? 41.18600 34.61400 -0.24200  0.440 39.39000  ?  47  ALA A C   1 
ATOM   583  O  O   A ALA A 1 47  ? 41.22100 32.89800 0.05200   0.560 45.40000  ?  47  ALA A O   1 
ATOM   584  O  O   B ALA A 1 47  ? 40.96500 33.40700 -0.34900  0.440 43.68000  ?  47  ALA A O   1 
ATOM   585  C  CB  A ALA A 1 47  ? 39.28900 35.55700 0.16700   0.560 41.54000  ?  47  ALA A CB  1 
ATOM   586  C  CB  B ALA A 1 47  ? 39.31500 36.25500 -0.36900  0.440 43.75000  ?  47  ALA A CB  1 
ATOM   587  N  N   A ALA A 1 48  ? 42.36400 34.79800 -0.33100  0.560 40.55000  ?  48  ALA A N   1 
ATOM   588  N  N   B ALA A 1 48  ? 42.23400 35.17100 -0.82400  0.440 46.65000  ?  48  ALA A N   1 
ATOM   589  C  CA  A ALA A 1 48  ? 43.40900 34.09000 -1.06400  0.560 47.59000  ?  48  ALA A CA  1 
ATOM   590  C  CA  B ALA A 1 48  ? 43.20400 34.29000 -1.47600  0.440 49.11000  ?  48  ALA A CA  1 
ATOM   591  C  C   A ALA A 1 48  ? 43.96600 32.94200 -0.22900  0.560 53.80000  ?  48  ALA A C   1 
ATOM   592  C  C   B ALA A 1 48  ? 43.70700 33.25100 -0.49400  0.440 50.89000  ?  48  ALA A C   1 
ATOM   593  O  O   A ALA A 1 48  ? 44.02600 31.79400 -0.68400  0.560 49.06000  ?  48  ALA A O   1 
ATOM   594  O  O   B ALA A 1 48  ? 43.72500 32.04900 -0.80500  0.440 49.26000  ?  48  ALA A O   1 
ATOM   595  C  CB  A ALA A 1 48  ? 44.52800 35.05500 -1.45900  0.560 46.52000  ?  48  ALA A CB  1 
ATOM   596  C  CB  B ALA A 1 48  ? 44.37800 35.09100 -2.06900  0.440 46.40000  ?  48  ALA A CB  1 
ATOM   597  N  N   A VAL A 1 49  ? 44.35900 33.23400 1.01200   0.560 53.47000  ?  49  VAL A N   1 
ATOM   598  N  N   B VAL A 1 49  ? 44.02200 33.69500 0.74100   0.440 54.41000  ?  49  VAL A N   1 
ATOM   599  C  CA  A VAL A 1 49  ? 44.95600 32.21000 1.86500   0.560 49.26000  ?  49  VAL A CA  1 
ATOM   600  C  CA  B VAL A 1 49  ? 44.60200 32.80600 1.74300   0.440 47.98000  ?  49  VAL A CA  1 
ATOM   601  C  C   A VAL A 1 49  ? 43.97500 31.06500 2.09400   0.560 52.76000  ?  49  VAL A C   1 
ATOM   602  C  C   B VAL A 1 49  ? 43.66700 31.63700 2.02700   0.440 49.03000  ?  49  VAL A C   1 
ATOM   603  O  O   A VAL A 1 49  ? 44.33500 29.88700 1.99300   0.560 55.09000  ?  49  VAL A O   1 
ATOM   604  O  O   B VAL A 1 49  ? 44.07400 30.46900 1.99000   0.440 53.85000  ?  49  VAL A O   1 
ATOM   605  C  CB  A VAL A 1 49  ? 45.42500 32.82800 3.19600   0.560 65.10000  ?  49  VAL A CB  1 
ATOM   606  C  CB  B VAL A 1 49  ? 44.95300 33.59000 3.01600   0.440 57.46000  ?  49  VAL A CB  1 
ATOM   607  C  CG1 A VAL A 1 49  ? 45.82000 31.73600 4.18300   0.560 52.62000  ?  49  VAL A CG1 1 
ATOM   608  C  CG1 B VAL A 1 49  ? 45.36600 32.61100 4.14000   0.440 53.49000  ?  49  VAL A CG1 1 
ATOM   609  C  CG2 A VAL A 1 49  ? 46.58300 33.78700 2.95300   0.560 53.00000  ?  49  VAL A CG2 1 
ATOM   610  C  CG2 B VAL A 1 49  ? 46.05200 34.53300 2.69400   0.440 55.03000  ?  49  VAL A CG2 1 
ATOM   611  N  N   A ALA A 1 50  ? 42.72000 31.39200 2.41000   0.560 49.83000  ?  50  ALA A N   1 
ATOM   612  N  N   B ALA A 1 50  ? 42.40100 31.92800 2.31800   0.440 48.66000  ?  50  ALA A N   1 
ATOM   613  C  CA  A ALA A 1 50  ? 41.73900 30.33900 2.66000   0.560 42.28000  ?  50  ALA A CA  1 
ATOM   614  C  CA  B ALA A 1 50  ? 41.45400 30.83900 2.54600   0.440 46.71000  ?  50  ALA A CA  1 
ATOM   615  C  C   A ALA A 1 50  ? 41.60500 29.41600 1.45600   0.560 49.11000  ?  50  ALA A C   1 
ATOM   616  C  C   B ALA A 1 50  ? 41.30300 29.95900 1.29300   0.440 51.30000  ?  50  ALA A C   1 
ATOM   617  O  O   A ALA A 1 50  ? 41.52800 28.19200 1.60500   0.560 47.05000  ?  50  ALA A O   1 
ATOM   618  O  O   B ALA A 1 50  ? 40.99400 28.76500 1.41400   0.440 47.92000  ?  50  ALA A O   1 
ATOM   619  C  CB  A ALA A 1 50  ? 40.38600 30.95200 3.02000   0.560 41.59000  ?  50  ALA A CB  1 
ATOM   620  C  CB  B ALA A 1 50  ? 40.10600 31.40000 3.01300   0.440 43.01000  ?  50  ALA A CB  1 
ATOM   621  N  N   A TYR A 1 51  ? 41.59300 29.98000 0.24900   0.560 51.01000  ?  51  TYR A N   1 
ATOM   622  N  N   B TYR A 1 51  ? 41.55300 30.50100 0.08000   0.440 48.97000  ?  51  TYR A N   1 
ATOM   623  C  CA  A TYR A 1 51  ? 41.41100 29.15100 -0.93800  0.560 45.71000  ?  51  TYR A CA  1 
ATOM   624  C  CA  B TYR A 1 51  ? 41.40500 29.63900 -1.10000  0.440 45.94000  ?  51  TYR A CA  1 
ATOM   625  C  C   A TYR A 1 51  ? 42.63500 28.28500 -1.21500  0.560 46.99000  ?  51  TYR A C   1 
ATOM   626  C  C   B TYR A 1 51  ? 42.61800 28.78100 -1.33400  0.440 46.36000  ?  51  TYR A C   1 
ATOM   627  O  O   A TYR A 1 51  ? 42.49700 27.12500 -1.62100  0.560 47.41000  ?  51  TYR A O   1 
ATOM   628  O  O   B TYR A 1 51  ? 42.47500 27.69000 -1.88500  0.440 44.86000  ?  51  TYR A O   1 
ATOM   629  C  CB  A TYR A 1 51  ? 41.07200 30.03600 -2.13300  0.560 43.63000  ?  51  TYR A CB  1 
ATOM   630  C  CB  B TYR A 1 51  ? 41.06600 30.42600 -2.37800  0.440 43.21000  ?  51  TYR A CB  1 
ATOM   631  C  CG  A TYR A 1 51  ? 39.58200 30.22800 -2.28600  0.560 47.67000  ?  51  TYR A CG  1 
ATOM   632  C  CG  B TYR A 1 51  ? 39.56700 30.41800 -2.47100  0.440 47.25000  ?  51  TYR A CG  1 
ATOM   633  C  CD1 A TYR A 1 51  ? 38.78400 29.20800 -2.78500  0.560 43.71000  ?  51  TYR A CD1 1 
ATOM   634  C  CD1 B TYR A 1 51  ? 38.91200 29.28600 -2.85400  0.440 44.16000  ?  51  TYR A CD1 1 
ATOM   635  C  CD2 A TYR A 1 51  ? 38.96800 31.41500 -1.91000  0.560 43.86000  ?  51  TYR A CD2 1 
ATOM   636  C  CD2 B TYR A 1 51  ? 38.80400 31.47900 -1.99800  0.440 43.20000  ?  51  TYR A CD2 1 
ATOM   637  C  CE1 A TYR A 1 51  ? 37.42300 29.36800 -2.91600  0.560 43.29000  ?  51  TYR A CE1 1 
ATOM   638  C  CE1 B TYR A 1 51  ? 37.54300 29.23400 -2.86900  0.440 43.38000  ?  51  TYR A CE1 1 
ATOM   639  C  CE2 A TYR A 1 51  ? 37.60200 31.58400 -2.04200  0.560 39.83000  ?  51  TYR A CE2 1 
ATOM   640  C  CE2 B TYR A 1 51  ? 37.42900 31.41300 -2.00100  0.440 40.63000  ?  51  TYR A CE2 1 
ATOM   641  C  CZ  A TYR A 1 51  ? 36.83600 30.55500 -2.54400  0.560 42.33000  ?  51  TYR A CZ  1 
ATOM   642  C  CZ  B TYR A 1 51  ? 36.81800 30.27500 -2.44400  0.440 42.97000  ?  51  TYR A CZ  1 
ATOM   643  O  OH  A TYR A 1 51  ? 35.47600 30.70700 -2.68200  0.560 44.76000  ?  51  TYR A OH  1 
ATOM   644  O  OH  B TYR A 1 51  ? 35.46100 30.13400 -2.44700  0.440 42.47000  ?  51  TYR A OH  1 
ATOM   645  N  N   A VAL A 1 52  ? 43.83900 28.81200 -0.98700  0.560 46.50000  ?  52  VAL A N   1 
ATOM   646  N  N   B VAL A 1 52  ? 43.79700 29.22000 -0.89600  0.440 46.77000  ?  52  VAL A N   1 
ATOM   647  C  CA  A VAL A 1 52  ? 45.03700 27.99100 -1.15800  0.560 47.84000  ?  52  VAL A CA  1 
ATOM   648  C  CA  B VAL A 1 52  ? 44.91100 28.29000 -0.97300  0.440 47.54000  ?  52  VAL A CA  1 
ATOM   649  C  C   A VAL A 1 52  ? 45.00000 26.80600 -0.20000  0.560 56.57000  ?  52  VAL A C   1 
ATOM   650  C  C   B VAL A 1 52  ? 44.84200 27.25600 0.15800   0.440 54.93000  ?  52  VAL A C   1 
ATOM   651  O  O   A VAL A 1 52  ? 45.21900 25.65500 -0.59700  0.560 58.99000  ?  52  VAL A O   1 
ATOM   652  O  O   B VAL A 1 52  ? 45.19500 26.08400 -0.04100  0.440 55.83000  ?  52  VAL A O   1 
ATOM   653  C  CB  A VAL A 1 52  ? 46.30800 28.83500 -0.95500  0.560 51.22000  ?  52  VAL A CB  1 
ATOM   654  C  CB  B VAL A 1 52  ? 46.24300 29.03100 -0.97100  0.440 51.04000  ?  52  VAL A CB  1 
ATOM   655  C  CG1 A VAL A 1 52  ? 47.53300 27.92600 -0.90800  0.560 55.88000  ?  52  VAL A CG1 1 
ATOM   656  C  CG1 B VAL A 1 52  ? 47.39800 28.02000 -0.99900  0.440 56.05000  ?  52  VAL A CG1 1 
ATOM   657  C  CG2 A VAL A 1 52  ? 46.45200 29.87100 -2.05400  0.560 52.95000  ?  52  VAL A CG2 1 
ATOM   658  C  CG2 B VAL A 1 52  ? 46.33900 29.94800 -2.15700  0.440 52.63000  ?  52  VAL A CG2 1 
ATOM   659  N  N   A VAL A 1 53  ? 44.71800 27.07200 1.07700   0.560 51.08000  ?  53  VAL A N   1 
ATOM   660  N  N   B VAL A 1 53  ? 44.40000 27.64700 1.35200   0.440 49.16000  ?  53  VAL A N   1 
ATOM   661  C  CA  A VAL A 1 53  ? 44.63900 26.00100 2.06900   0.560 53.10000  ?  53  VAL A CA  1 
ATOM   662  C  CA  B VAL A 1 53  ? 44.12100 26.64700 2.37300   0.440 52.56000  ?  53  VAL A CA  1 
ATOM   663  C  C   A VAL A 1 53  ? 43.66400 24.92900 1.60300   0.560 52.89000  ?  53  VAL A C   1 
ATOM   664  C  C   B VAL A 1 53  ? 43.23200 25.54800 1.80700   0.440 50.86000  ?  53  VAL A C   1 
ATOM   665  O  O   A VAL A 1 53  ? 43.94800 23.72700 1.66700   0.560 50.49000  ?  53  VAL A O   1 
ATOM   666  O  O   B VAL A 1 53  ? 43.58300 24.36200 1.85100   0.440 51.00000  ?  53  VAL A O   1 
ATOM   667  C  CB  A VAL A 1 53  ? 44.23300 26.57400 3.43900   0.560 54.51000  ?  53  VAL A CB  1 
ATOM   668  C  CB  B VAL A 1 53  ? 43.47900 27.29700 3.61000   0.440 53.06000  ?  53  VAL A CB  1 
ATOM   669  C  CG1 A VAL A 1 53  ? 43.90400 25.45900 4.41700   0.560 55.18000  ?  53  VAL A CG1 1 
ATOM   670  C  CG1 B VAL A 1 53  ? 42.68200 26.29600 4.34600   0.440 48.01000  ?  53  VAL A CG1 1 
ATOM   671  C  CG2 A VAL A 1 53  ? 45.33900 27.45900 3.98700   0.560 52.03000  ?  53  VAL A CG2 1 
ATOM   672  C  CG2 B VAL A 1 53  ? 44.52300 27.87600 4.50100   0.440 56.20000  ?  53  VAL A CG2 1 
ATOM   673  N  N   A MET A 1 54  ? 42.49100 25.35500 1.13400   0.560 45.94000  ?  54  MET A N   1 
ATOM   674  N  N   B MET A 1 54  ? 42.08100 25.92200 1.25000   0.440 45.96000  ?  54  MET A N   1 
ATOM   675  C  CA  A MET A 1 54  ? 41.50400 24.40000 0.64700   0.560 56.16000  ?  54  MET A CA  1 
ATOM   676  C  CA  B MET A 1 54  ? 41.17600 24.89800 0.74200   0.440 54.05000  ?  54  MET A CA  1 
ATOM   677  C  C   A MET A 1 54  ? 41.99800 23.70100 -0.61400  0.560 59.01000  ?  54  MET A C   1 
ATOM   678  C  C   B MET A 1 54  ? 41.81700 24.18100 -0.40400  0.440 57.40000  ?  54  MET A C   1 
ATOM   679  O  O   A MET A 1 54  ? 41.81700 22.48700 -0.76500  0.560 61.33000  ?  54  MET A O   1 
ATOM   680  O  O   B MET A 1 54  ? 41.71700 22.95700 -0.50800  0.440 60.55000  ?  54  MET A O   1 
ATOM   681  C  CB  A MET A 1 54  ? 40.17400 25.11300 0.40200   0.560 49.10000  ?  54  MET A CB  1 
ATOM   682  C  CB  B MET A 1 54  ? 39.84500 25.46100 0.24600   0.440 49.21000  ?  54  MET A CB  1 
ATOM   683  C  CG  A MET A 1 54  ? 39.44100 25.45000 1.68700   0.560 52.09000  ?  54  MET A CG  1 
ATOM   684  C  CG  B MET A 1 54  ? 38.90200 25.84300 1.33900   0.440 50.14000  ?  54  MET A CG  1 
ATOM   685  S  SD  A MET A 1 54  ? 37.71600 25.91700 1.45500   0.560 51.30000  ?  54  MET A SD  1 
ATOM   686  S  SD  B MET A 1 54  ? 37.29200 26.45900 0.80500   0.440 47.38000  ?  54  MET A SD  1 
ATOM   687  C  CE  A MET A 1 54  ? 37.88500 27.65600 1.00900   0.560 49.67000  ?  54  MET A CE  1 
ATOM   688  C  CE  B MET A 1 54  ? 37.80900 28.03500 0.13300   0.440 46.27000  ?  54  MET A CE  1 
ATOM   689  N  N   A ALA A 1 55  ? 42.63900 24.44300 -1.52000  0.560 55.81000  ?  55  ALA A N   1 
ATOM   690  N  N   B ALA A 1 55  ? 42.45200 24.94000 -1.29500  0.440 54.82000  ?  55  ALA A N   1 
ATOM   691  C  CA  A ALA A 1 55  ? 43.18200 23.82400 -2.72500  0.560 58.73000  ?  55  ALA A CA  1 
ATOM   692  C  CA  B ALA A 1 55  ? 43.05300 24.34300 -2.47200  0.440 57.75000  ?  55  ALA A CA  1 
ATOM   693  C  C   A ALA A 1 55  ? 44.16800 22.71800 -2.37600  0.560 62.95000  ?  55  ALA A C   1 
ATOM   694  C  C   B ALA A 1 55  ? 43.82700 23.11300 -2.03100  0.440 62.88000  ?  55  ALA A C   1 
ATOM   695  O  O   A ALA A 1 55  ? 44.23200 21.69100 -3.06200  0.560 66.59000  ?  55  ALA A O   1 
ATOM   696  O  O   B ALA A 1 55  ? 43.57100 21.99500 -2.49100  0.440 58.65000  ?  55  ALA A O   1 
ATOM   697  C  CB  A ALA A 1 55  ? 43.85600 24.88000 -3.60100  0.560 53.33000  ?  55  ALA A CB  1 
ATOM   698  C  CB  B ALA A 1 55  ? 43.94100 25.36700 -3.18100  0.440 52.64000  ?  55  ALA A CB  1 
ATOM   699  N  N   A LEU A 1 56  ? 44.94300 22.90500 -1.31100  0.560 58.55000  ?  56  LEU A N   1 
ATOM   700  N  N   B LEU A 1 56  ? 44.65300 23.29600 -1.00400  0.440 59.34000  ?  56  LEU A N   1 
ATOM   701  C  CA  A LEU A 1 56  ? 45.90000 21.89700 -0.87800  0.560 61.66000  ?  56  LEU A CA  1 
ATOM   702  C  CA  B LEU A 1 56  ? 45.50500 22.23400 -0.51800  0.440 60.31000  ?  56  LEU A CA  1 
ATOM   703  C  C   A LEU A 1 56  ? 45.24600 20.73700 -0.13900  0.560 59.79000  ?  56  LEU A C   1 
ATOM   704  C  C   B LEU A 1 56  ? 44.71000 21.27300 0.34200   0.440 59.85000  ?  56  LEU A C   1 
ATOM   705  O  O   A LEU A 1 56  ? 45.95600 19.82400 0.29500   0.560 61.59000  ?  56  LEU A O   1 
ATOM   706  O  O   B LEU A 1 56  ? 45.28500 20.50800 1.11200   0.440 55.80000  ?  56  LEU A O   1 
ATOM   707  C  CB  A LEU A 1 56  ? 46.96600 22.53800 0.01400   0.560 63.35000  ?  56  LEU A CB  1 
ATOM   708  C  CB  B LEU A 1 56  ? 46.69800 22.83400 0.23200   0.440 62.81000  ?  56  LEU A CB  1 
ATOM   709  C  CG  A LEU A 1 56  ? 47.90400 23.51500 -0.69600  0.560 65.74000  ?  56  LEU A CG  1 
ATOM   710  C  CG  B LEU A 1 56  ? 47.63400 23.53400 -0.75600  0.440 65.01000  ?  56  LEU A CG  1 
ATOM   711  C  CD1 A LEU A 1 56  ? 48.75800 24.28500 0.29800   0.560 62.80000  ?  56  LEU A CD1 1 
ATOM   712  C  CD1 B LEU A 1 56  ? 48.61700 24.43400 -0.06400  0.440 63.94000  ?  56  LEU A CD1 1 
ATOM   713  C  CD2 A LEU A 1 56  ? 48.78300 22.77400 -1.70000  0.560 76.08000  ?  56  LEU A CD2 1 
ATOM   714  C  CD2 B LEU A 1 56  ? 48.38600 22.45200 -1.46700  0.440 72.87000  ?  56  LEU A CD2 1 
ATOM   715  N  N   A GLY A 1 57  ? 43.92500 20.74400 0.01500   0.560 55.94000  ?  57  GLY A N   1 
ATOM   716  N  N   B GLY A 1 57  ? 43.39100 21.28900 0.21200   0.440 56.51000  ?  57  GLY A N   1 
ATOM   717  C  CA  A GLY A 1 57  ? 43.24200 19.67500 0.70900   0.560 61.44000  ?  57  GLY A CA  1 
ATOM   718  C  CA  B GLY A 1 57  ? 42.60600 20.27400 0.89000   0.440 63.36000  ?  57  GLY A CA  1 
ATOM   719  C  C   A GLY A 1 57  ? 43.20600 19.80700 2.21100   0.560 71.15000  ?  57  GLY A C   1 
ATOM   720  C  C   B GLY A 1 57  ? 42.76900 20.24000 2.40400   0.440 69.24000  ?  57  GLY A C   1 
ATOM   721  O  O   A GLY A 1 57  ? 42.89900 18.82400 2.89600   0.560 70.42000  ?  57  GLY A O   1 
ATOM   722  O  O   B GLY A 1 57  ? 42.62400 19.18100 3.02800   0.440 70.38000  ?  57  GLY A O   1 
ATOM   723  N  N   A VAL A 1 58  ? 43.50100 20.97300 2.74500   0.560 66.67000  ?  58  VAL A N   1 
ATOM   724  N  N   B VAL A 1 58  ? 43.06900 21.34500 3.00500   0.440 66.58000  ?  58  VAL A N   1 
ATOM   725  C  CA  A VAL A 1 58  ? 43.53100 21.18000 4.18600   0.560 68.17000  ?  58  VAL A CA  1 
ATOM   726  C  CA  B VAL A 1 58  ? 43.13800 21.45400 4.45700   0.440 68.03000  ?  58  VAL A CA  1 
ATOM   727  C  C   A VAL A 1 58  ? 42.18600 21.73200 4.63400   0.560 65.54000  ?  58  VAL A C   1 
ATOM   728  C  C   B VAL A 1 58  ? 41.75700 21.87900 4.94800   0.440 65.64000  ?  58  VAL A C   1 
ATOM   729  O  O   A VAL A 1 58  ? 41.59600 22.59400 3.97200   0.560 64.02000  ?  58  VAL A O   1 
ATOM   730  O  O   B VAL A 1 58  ? 41.01600 22.59600 4.25200   0.440 62.89000  ?  58  VAL A O   1 
ATOM   731  C  CB  A VAL A 1 58  ? 44.68400 22.12200 4.57900   0.560 64.16000  ?  58  VAL A CB  1 
ATOM   732  C  CB  B VAL A 1 58  ? 44.24000 22.45400 4.87900   0.440 65.79000  ?  58  VAL A CB  1 
ATOM   733  C  CG1 A VAL A 1 58  ? 44.53400 22.55700 6.02800   0.560 70.28000  ?  58  VAL A CG1 1 
ATOM   734  C  CG1 B VAL A 1 58  ? 44.19400 22.69600 6.33900   0.440 71.86000  ?  58  VAL A CG1 1 
ATOM   735  C  CG2 A VAL A 1 58  ? 46.02600 21.43700 4.35100   0.560 67.81000  ?  58  VAL A CG2 1 
ATOM   736  C  CG2 B VAL A 1 58  ? 45.60400 21.94800 4.46200   0.440 66.58000  ?  58  VAL A CG2 1 
ATOM   737  N  N   A GLY A 1 59  ? 41.69300 21.22000 5.75700   0.560 67.41000  ?  59  GLY A N   1 
ATOM   738  N  N   B GLY A 1 59  ? 41.37400 21.39300 6.12300   0.440 67.28000  ?  59  GLY A N   1 
ATOM   739  C  CA  A GLY A 1 59  ? 40.46900 21.73200 6.33600   0.560 63.89000  ?  59  GLY A CA  1 
ATOM   740  C  CA  B GLY A 1 59  ? 40.12400 21.83200 6.70000   0.440 63.28000  ?  59  GLY A CA  1 
ATOM   741  C  C   A GLY A 1 59  ? 39.19300 21.15700 5.77300   0.560 64.22000  ?  59  GLY A C   1 
ATOM   742  C  C   B GLY A 1 59  ? 38.87200 21.41800 5.96000   0.440 63.42000  ?  59  GLY A C   1 
ATOM   743  O  O   A GLY A 1 59  ? 38.13100 21.76500 5.93700   0.560 60.30000  ?  59  GLY A O   1 
ATOM   744  O  O   B GLY A 1 59  ? 37.83100 22.08000 6.08900   0.440 58.99000  ?  59  GLY A O   1 
ATOM   745  N  N   A TRP A 1 60  ? 39.25800 20.00700 5.11100   0.560 71.00000  ?  60  TRP A N   1 
ATOM   746  N  N   B TRP A 1 60  ? 38.93200 20.34800 5.18200   0.440 70.04000  ?  60  TRP A N   1 
ATOM   747  C  CA  A TRP A 1 60  ? 38.06200 19.33400 4.61000   0.560 67.03000  ?  60  TRP A CA  1 
ATOM   748  C  CA  B TRP A 1 60  ? 37.71300 19.74000 4.66600   0.440 66.49000  ?  60  TRP A CA  1 
ATOM   749  C  C   A TRP A 1 60  ? 37.57000 18.42800 5.73200   0.560 76.71000  ?  60  TRP A C   1 
ATOM   750  C  C   B TRP A 1 60  ? 37.17200 18.84400 5.76000   0.440 73.79000  ?  60  TRP A C   1 
ATOM   751  O  O   A TRP A 1 60  ? 38.13100 17.35700 5.96100   0.560 76.31000  ?  60  TRP A O   1 
ATOM   752  O  O   B TRP A 1 60  ? 37.77300 17.82800 6.10700   0.440 77.95000  ?  60  TRP A O   1 
ATOM   753  C  CB  A TRP A 1 60  ? 38.36500 18.52700 3.35500   0.560 65.71000  ?  60  TRP A CB  1 
ATOM   754  C  CB  B TRP A 1 60  ? 37.99500 18.94900 3.39400   0.440 64.71000  ?  60  TRP A CB  1 
ATOM   755  C  CG  A TRP A 1 60  ? 38.89200 19.30600 2.18700   0.560 67.97000  ?  60  TRP A CG  1 
ATOM   756  C  CG  B TRP A 1 60  ? 38.60900 19.75000 2.25300   0.440 68.93000  ?  60  TRP A CG  1 
ATOM   757  C  CD1 A TRP A 1 60  ? 39.54100 20.50600 2.21400   0.560 66.51000  ?  60  TRP A CD1 1 
ATOM   758  C  CD1 B TRP A 1 60  ? 39.24900 20.98300 2.32500   0.440 67.25000  ?  60  TRP A CD1 1 
ATOM   759  C  CD2 A TRP A 1 60  ? 38.81700 18.92200 0.80900   0.560 61.76000  ?  60  TRP A CD2 1 
ATOM   760  C  CD2 B TRP A 1 60  ? 38.69800 19.34300 0.89000   0.440 64.12000  ?  60  TRP A CD2 1 
ATOM   761  N  NE1 A TRP A 1 60  ? 39.87500 20.89300 0.93800   0.560 70.84000  ?  60  TRP A NE1 1 
ATOM   762  N  NE1 B TRP A 1 60  ? 39.69500 21.35500 1.09100   0.440 68.24000  ?  60  TRP A NE1 1 
ATOM   763  C  CE2 A TRP A 1 60  ? 39.44100 19.93700 0.05700   0.560 72.19000  ?  60  TRP A CE2 1 
ATOM   764  C  CE2 B TRP A 1 60  ? 39.37500 20.37200 0.18900   0.440 70.68000  ?  60  TRP A CE2 1 
ATOM   765  C  CE3 A TRP A 1 60  ? 38.28200 17.81800 0.13900   0.560 62.22000  ?  60  TRP A CE3 1 
ATOM   766  C  CE3 B TRP A 1 60  ? 38.27200 18.21400 0.18800   0.440 62.55000  ?  60  TRP A CE3 1 
ATOM   767  C  CZ2 A TRP A 1 60  ? 39.54400 19.88100 -1.33100  0.560 67.81000  ?  60  TRP A CZ2 1 
ATOM   768  C  CZ2 B TRP A 1 60  ? 39.62800 20.30300 -1.17900  0.440 66.71000  ?  60  TRP A CZ2 1 
ATOM   769  C  CZ3 A TRP A 1 60  ? 38.38300 17.76300 -1.23700  0.560 66.76000  ?  60  TRP A CZ3 1 
ATOM   770  C  CZ3 B TRP A 1 60  ? 38.53600 18.14600 -1.17700  0.440 66.60000  ?  60  TRP A CZ3 1 
ATOM   771  C  CH2 A TRP A 1 60  ? 39.01000 18.78800 -1.95900  0.560 68.14000  ?  60  TRP A CH2 1 
ATOM   772  C  CH2 B TRP A 1 60  ? 39.20100 19.18700 -1.84200  0.440 67.93000  ?  60  TRP A CH2 1 
ATOM   773  N  N   A VAL A 1 61  ? 36.53200 18.84600 6.45000   0.560 70.44000  ?  61  VAL A N   1 
ATOM   774  N  N   B VAL A 1 61  ? 36.00200 19.21700 6.31500   0.440 67.77000  ?  61  VAL A N   1 
ATOM   775  C  CA  A VAL A 1 61  ? 36.08300 18.15200 7.65500   0.560 70.54000  ?  61  VAL A CA  1 
ATOM   776  C  CA  B VAL A 1 61  ? 35.43800 18.60600 7.49600   0.440 66.08000  ?  61  VAL A CA  1 
ATOM   777  C  C   A VAL A 1 61  ? 34.86300 17.29400 7.31000   0.560 71.33000  ?  61  VAL A C   1 
ATOM   778  C  C   B VAL A 1 61  ? 34.39000 17.60100 7.08800   0.440 67.64000  ?  61  VAL A C   1 
ATOM   779  O  O   A VAL A 1 61  ? 33.83700 17.84700 6.89300   0.560 63.77000  ?  61  VAL A O   1 
ATOM   780  O  O   B VAL A 1 61  ? 33.38000 17.97800 6.46300   0.440 63.55000  ?  61  VAL A O   1 
ATOM   781  C  CB  A VAL A 1 61  ? 35.76000 19.12200 8.80300   0.560 66.52000  ?  61  VAL A CB  1 
ATOM   782  C  CB  B VAL A 1 61  ? 34.84200 19.68100 8.42700   0.440 61.62000  ?  61  VAL A CB  1 
ATOM   783  C  CG1 A VAL A 1 61  ? 35.42700 18.30300 10.05200  0.560 74.83000  ?  61  VAL A CG1 1 
ATOM   784  C  CG1 B VAL A 1 61  ? 34.18100 19.04300 9.67800   0.440 61.71000  ?  61  VAL A CG1 1 
ATOM   785  C  CG2 A VAL A 1 61  ? 36.92700 20.04400 9.05000   0.560 66.68000  ?  61  VAL A CG2 1 
ATOM   786  C  CG2 B VAL A 1 61  ? 35.93100 20.64200 8.84400   0.440 51.12000  ?  61  VAL A CG2 1 
ATOM   787  N  N   A PRO A 1 62  ? 34.92500 15.97700 7.46700   0.560 81.69000  ?  62  PRO A N   1 
ATOM   788  N  N   B PRO A 1 62  ? 34.52600 16.30300 7.40300   0.440 79.30000  ?  62  PRO A N   1 
ATOM   789  C  CA  A PRO A 1 62  ? 33.73200 15.14800 7.25400   0.560 77.30000  ?  62  PRO A CA  1 
ATOM   790  C  CA  B PRO A 1 62  ? 33.40200 15.41500 7.15600   0.440 76.77000  ?  62  PRO A CA  1 
ATOM   791  C  C   A PRO A 1 62  ? 32.75800 15.30200 8.41100   0.560 73.19000  ?  62  PRO A C   1 
ATOM   792  C  C   B PRO A 1 62  ? 32.38900 15.67900 8.24000   0.440 72.52000  ?  62  PRO A C   1 
ATOM   793  O  O   A PRO A 1 62  ? 33.14700 15.30500 9.58200   0.560 80.44000  ?  62  PRO A O   1 
ATOM   794  O  O   B PRO A 1 62  ? 32.72900 15.74100 9.42700   0.440 78.68000  ?  62  PRO A O   1 
ATOM   795  C  CB  A PRO A 1 62  ? 34.30400 13.72900 7.18900   0.560 81.95000  ?  62  PRO A CB  1 
ATOM   796  C  CB  B PRO A 1 62  ? 34.01200 14.01900 7.26800   0.440 81.08000  ?  62  PRO A CB  1 
ATOM   797  C  CG  A PRO A 1 62  ? 35.48700 13.78700 8.12800   0.560 86.84000  ?  62  PRO A CG  1 
ATOM   798  C  CG  B PRO A 1 62  ? 35.07900 14.19500 8.27200   0.440 84.76000  ?  62  PRO A CG  1 
ATOM   799  C  CD  A PRO A 1 62  ? 36.03800 15.20200 8.03900   0.560 83.02000  ?  62  PRO A CD  1 
ATOM   800  C  CD  B PRO A 1 62  ? 35.58300 15.62100 8.17700   0.440 81.53000  ?  62  PRO A CD  1 
ATOM   801  N  N   A VAL A 1 63  ? 31.48100 15.44000 8.07000   0.560 69.42000  ?  63  VAL A N   1 
ATOM   802  N  N   B VAL A 1 63  ? 31.15900 15.92700 7.83500   0.440 68.52000  ?  63  VAL A N   1 
ATOM   803  C  CA  A VAL A 1 63  ? 30.42500 15.63300 9.05500   0.560 69.76000  ?  63  VAL A CA  1 
ATOM   804  C  CA  B VAL A 1 63  ? 30.09200 16.26500 8.74600   0.440 68.99000  ?  63  VAL A CA  1 
ATOM   805  C  C   A VAL A 1 63  ? 29.23000 14.80100 8.60900   0.560 77.21000  ?  63  VAL A C   1 
ATOM   806  C  C   B VAL A 1 63  ? 28.92200 15.40300 8.32400   0.440 76.06000  ?  63  VAL A C   1 
ATOM   807  O  O   A VAL A 1 63  ? 28.60200 15.11200 7.58900   0.560 77.99000  ?  63  VAL A O   1 
ATOM   808  O  O   B VAL A 1 63  ? 28.21400 15.72900 7.36800   0.440 76.39000  ?  63  VAL A O   1 
ATOM   809  C  CB  A VAL A 1 63  ? 30.03500 17.10900 9.21000   0.560 66.17000  ?  63  VAL A CB  1 
ATOM   810  C  CB  B VAL A 1 63  ? 29.74100 17.75300 8.73100   0.440 63.07000  ?  63  VAL A CB  1 
ATOM   811  C  CG1 A VAL A 1 63  ? 28.88200 17.25000 10.18600  0.560 73.52000  ?  63  VAL A CG1 1 
ATOM   812  C  CG1 B VAL A 1 63  ? 28.41100 17.97800 9.28300   0.440 64.39000  ?  63  VAL A CG1 1 
ATOM   813  C  CG2 A VAL A 1 63  ? 31.23700 17.92700 9.67000   0.560 64.72000  ?  63  VAL A CG2 1 
ATOM   814  C  CG2 B VAL A 1 63  ? 30.74500 18.50300 9.55400   0.440 62.43000  ?  63  VAL A CG2 1 
ATOM   815  N  N   A ALA A 1 64  ? 28.91300 13.75000 9.37200   0.560 85.22000  ?  64  ALA A N   1 
ATOM   816  N  N   B ALA A 1 64  ? 28.73600 14.28800 9.01700   0.440 78.24000  ?  64  ALA A N   1 
ATOM   817  C  CA  A ALA A 1 64  ? 27.87000 12.80600 8.99000   0.560 88.51000  ?  64  ALA A CA  1 
ATOM   818  C  CA  B ALA A 1 64  ? 27.78600 13.27500 8.61700   0.440 85.93000  ?  64  ALA A CA  1 
ATOM   819  C  C   A ALA A 1 64  ? 28.18200 12.25500 7.60400   0.560 95.54000  ?  64  ALA A C   1 
ATOM   820  C  C   B ALA A 1 64  ? 28.25400 12.69700 7.31100   0.440 92.69000  ?  64  ALA A C   1 
ATOM   821  O  O   A ALA A 1 64  ? 29.10700 11.45100 7.44700   0.560 104.64000 ?  64  ALA A O   1 
ATOM   822  O  O   B ALA A 1 64  ? 29.35800 12.15300 7.19200   0.440 97.10000  ?  64  ALA A O   1 
ATOM   823  C  CB  A ALA A 1 64  ? 26.49800 13.47500 9.03200   0.560 90.83000  ?  64  ALA A CB  1 
ATOM   824  C  CB  B ALA A 1 64  ? 26.38200 13.85600 8.45000   0.440 84.54000  ?  64  ALA A CB  1 
ATOM   825  N  N   A GLU A 1 65  ? 27.42800 12.68500 6.59000   0.560 93.71000  ?  65  GLU A N   1 
ATOM   826  N  N   B GLU A 1 65  ? 27.41000 12.88100 6.31900   0.440 93.28000  ?  65  GLU A N   1 
ATOM   827  C  CA  A GLU A 1 65  ? 27.61500 12.19600 5.22800   0.560 97.24000  ?  65  GLU A CA  1 
ATOM   828  C  CA  B GLU A 1 65  ? 27.63900 12.37300 4.99200   0.440 96.65000  ?  65  GLU A CA  1 
ATOM   829  C  C   A GLU A 1 65  ? 28.06000 13.29100 4.26300   0.560 95.80000  ?  65  GLU A C   1 
ATOM   830  C  C   B GLU A 1 65  ? 28.16300 13.45700 4.05700   0.440 95.94000  ?  65  GLU A C   1 
ATOM   831  O  O   A GLU A 1 65  ? 28.14600 13.04200 3.05300   0.560 98.97000  ?  65  GLU A O   1 
ATOM   832  O  O   B GLU A 1 65  ? 28.61300 13.14100 2.95000   0.440 97.68000  ?  65  GLU A O   1 
ATOM   833  C  CB  A GLU A 1 65  ? 26.32300 11.55300 4.71600   0.560 109.34000 ?  65  GLU A CB  1 
ATOM   834  C  CB  B GLU A 1 65  ? 26.33400 11.77800 4.48400   0.440 108.34000 ?  65  GLU A CB  1 
ATOM   835  C  CG  A GLU A 1 65  ? 26.03500 10.18500 5.29600   0.560 124.98000 ?  65  GLU A CG  1 
ATOM   836  C  CG  B GLU A 1 65  ? 25.88400 10.59200 5.34700   0.440 122.46000 ?  65  GLU A CG  1 
ATOM   837  C  CD  A GLU A 1 65  ? 26.59600 9.05900  4.44200   0.560 139.52000 ?  65  GLU A CD  1 
ATOM   838  C  CD  B GLU A 1 65  ? 26.49600 9.26300  4.92400   0.440 136.46000 ?  65  GLU A CD  1 
ATOM   839  O  OE1 A GLU A 1 65  ? 27.34500 9.34200  3.48300   0.560 145.53000 ?  65  GLU A OE1 1 
ATOM   840  O  OE1 B GLU A 1 65  ? 27.41400 9.26600  4.07600   0.440 142.68000 ?  65  GLU A OE1 1 
ATOM   841  O  OE2 A GLU A 1 65  ? 26.28500 7.88400  4.73200   0.560 145.05000 -1 65  GLU A OE2 1 
ATOM   842  O  OE2 B GLU A 1 65  ? 26.06800 8.21100  5.44700   0.440 142.95000 -1 65  GLU A OE2 1 
ATOM   843  N  N   A ARG A 1 66  ? 28.35300 14.48500 4.76200   0.560 87.81000  ?  66  ARG A N   1 
ATOM   844  N  N   B ARG A 1 66  ? 28.13700 14.72600 4.48900   0.440 86.10000  ?  66  ARG A N   1 
ATOM   845  C  CA  A ARG A 1 66  ? 28.75700 15.61600 3.94100   0.560 73.45000  ?  66  ARG A CA  1 
ATOM   846  C  CA  B ARG A 1 66  ? 28.63700 15.87900 3.74500   0.440 73.97000  ?  66  ARG A CA  1 
ATOM   847  C  C   A ARG A 1 66  ? 30.21800 15.95500 4.20600   0.560 73.12000  ?  66  ARG A C   1 
ATOM   848  C  C   B ARG A 1 66  ? 30.09300 16.19200 4.06300   0.440 72.64000  ?  66  ARG A C   1 
ATOM   849  O  O   A ARG A 1 66  ? 30.83500 15.47300 5.15800   0.560 74.24000  ?  66  ARG A O   1 
ATOM   850  O  O   B ARG A 1 66  ? 30.69400 15.67400 5.00700   0.440 73.62000  ?  66  ARG A O   1 
ATOM   851  C  CB  A ARG A 1 66  ? 27.87200 16.83600 4.22800   0.560 77.11000  ?  66  ARG A CB  1 
ATOM   852  C  CB  B ARG A 1 66  ? 27.85300 17.16900 4.05100   0.440 76.72000  ?  66  ARG A CB  1 
ATOM   853  C  CG  A ARG A 1 66  ? 26.38800 16.59700 4.05100   0.560 87.14000  ?  66  ARG A CG  1 
ATOM   854  C  CG  B ARG A 1 66  ? 26.38200 17.21200 3.74100   0.440 79.13000  ?  66  ARG A CG  1 
ATOM   855  C  CD  A ARG A 1 66  ? 25.61000 16.80000 5.34900   0.560 87.98000  ?  66  ARG A CD  1 
ATOM   856  C  CD  B ARG A 1 66  ? 25.59500 17.63700 4.97800   0.440 78.43000  ?  66  ARG A CD  1 
ATOM   857  N  NE  A ARG A 1 66  ? 26.06300 17.95900 6.11500   0.560 73.67000  ?  66  ARG A NE  1 
ATOM   858  N  NE  B ARG A 1 66  ? 26.25700 18.68900 5.73900   0.440 72.17000  ?  66  ARG A NE  1 
ATOM   859  C  CZ  A ARG A 1 66  ? 25.70200 18.22000 7.36700   0.560 83.10000  ?  66  ARG A CZ  1 
ATOM   860  C  CZ  B ARG A 1 66  ? 25.80300 19.13800 6.89800   0.440 77.84000  ?  66  ARG A CZ  1 
ATOM   861  N  NH1 A ARG A 1 66  ? 24.86900 17.40800 8.00100   0.560 82.99000  ?  66  ARG A NH1 1 
ATOM   862  N  NH1 B ARG A 1 66  ? 24.67800 18.67700 7.42300   0.440 81.43000  ?  66  ARG A NH1 1 
ATOM   863  N  NH2 A ARG A 1 66  ? 26.16900 19.29600 7.98500   0.560 75.40000  ?  66  ARG A NH2 1 
ATOM   864  N  NH2 B ARG A 1 66  ? 26.47000 20.09800 7.53000   0.440 73.98000  ?  66  ARG A NH2 1 
ATOM   865  N  N   A THR A 1 67  ? 30.77200 16.79800 3.34200   0.560 66.63000  ?  67  THR A N   1 
ATOM   866  N  N   B THR A 1 67  ? 30.63500 17.11400 3.27100   0.440 65.70000  ?  67  THR A N   1 
ATOM   867  C  CA  A THR A 1 67  ? 32.09800 17.36700 3.54100   0.560 66.64000  ?  67  THR A CA  1 
ATOM   868  C  CA  B THR A 1 67  ? 31.86100 17.83900 3.57900   0.440 66.14000  ?  67  THR A CA  1 
ATOM   869  C  C   A THR A 1 67  ? 31.95000 18.86800 3.74700   0.560 61.34000  ?  67  THR A C   1 
ATOM   870  C  C   B THR A 1 67  ? 31.49600 19.29500 3.90300   0.440 60.35000  ?  67  THR A C   1 
ATOM   871  O  O   A THR A 1 67  ? 31.31300 19.54800 2.93700   0.560 55.36000  ?  67  THR A O   1 
ATOM   872  O  O   B THR A 1 67  ? 30.48600 19.79900 3.41500   0.440 54.43000  ?  67  THR A O   1 
ATOM   873  C  CB  A THR A 1 67  ? 33.02000 17.07800 2.35700   0.560 65.12000  ?  67  THR A CB  1 
ATOM   874  C  CB  B THR A 1 67  ? 32.84800 17.74600 2.40100   0.440 62.69000  ?  67  THR A CB  1 
ATOM   875  O  OG1 A THR A 1 67  ? 33.08500 15.66400 2.14000   0.560 57.92000  ?  67  THR A OG1 1 
ATOM   876  O  OG1 B THR A 1 67  ? 32.99700 16.37000 1.99900   0.440 65.28000  ?  67  THR A OG1 1 
ATOM   877  C  CG2 A THR A 1 67  ? 34.42000 17.60700 2.64000   0.560 59.89000  ?  67  THR A CG2 1 
ATOM   878  C  CG2 B THR A 1 67  ? 34.19000 18.29500 2.77200   0.440 59.29000  ?  67  THR A CG2 1 
ATOM   879  N  N   A VAL A 1 68  ? 32.52700 19.37500 4.83300   0.560 62.44000  ?  68  VAL A N   1 
ATOM   880  N  N   B VAL A 1 68  ? 32.26400 19.94100 4.79500   0.440 57.86000  ?  68  VAL A N   1 
ATOM   881  C  CA  A VAL A 1 68  ? 32.45000 20.78700 5.19600   0.560 53.37000  ?  68  VAL A CA  1 
ATOM   882  C  CA  B VAL A 1 68  ? 32.12600 21.36200 5.13800   0.440 50.07000  ?  68  VAL A CA  1 
ATOM   883  C  C   A VAL A 1 68  ? 33.83800 21.40200 5.06000   0.560 54.38000  ?  68  VAL A C   1 
ATOM   884  C  C   B VAL A 1 68  ? 33.49200 22.00600 4.91000   0.440 51.73000  ?  68  VAL A C   1 
ATOM   885  O  O   A VAL A 1 68  ? 34.83700 20.80600 5.47500   0.560 56.71000  ?  68  VAL A O   1 
ATOM   886  O  O   B VAL A 1 68  ? 34.52000 21.44400 5.31200   0.440 56.43000  ?  68  VAL A O   1 
ATOM   887  C  CB  A VAL A 1 68  ? 31.90900 20.98500 6.62500   0.560 57.66000  ?  68  VAL A CB  1 
ATOM   888  C  CB  B VAL A 1 68  ? 31.65400 21.58200 6.59200   0.440 56.39000  ?  68  VAL A CB  1 
ATOM   889  C  CG1 A VAL A 1 68  ? 32.42200 22.29900 7.20300   0.560 56.29000  ?  68  VAL A CG1 1 
ATOM   890  C  CG1 B VAL A 1 68  ? 31.97000 23.00000 7.06200   0.440 52.31000  ?  68  VAL A CG1 1 
ATOM   891  C  CG2 A VAL A 1 68  ? 30.39200 20.95800 6.61600   0.560 58.45000  ?  68  VAL A CG2 1 
ATOM   892  C  CG2 B VAL A 1 68  ? 30.18600 21.24100 6.75300   0.440 58.51000  ?  68  VAL A CG2 1 
ATOM   893  N  N   A PHE A 1 69  ? 33.89400 22.60000 4.48600   0.560 50.36000  ?  69  PHE A N   1 
ATOM   894  N  N   B PHE A 1 69  ? 33.51400 23.14300 4.20800   0.440 52.08000  ?  69  PHE A N   1 
ATOM   895  C  CA  A PHE A 1 69  ? 35.14800 23.29300 4.19100   0.560 50.61000  ?  69  PHE A CA  1 
ATOM   896  C  CA  B PHE A 1 69  ? 34.78400 23.81700 3.93200   0.440 52.31000  ?  69  PHE A CA  1 
ATOM   897  C  C   A PHE A 1 69  ? 35.34800 24.37500 5.24300   0.560 49.75000  ?  69  PHE A C   1 
ATOM   898  C  C   B PHE A 1 69  ? 34.85900 24.94500 4.91300   0.440 51.67000  ?  69  PHE A C   1 
ATOM   899  O  O   A PHE A 1 69  ? 34.79500 25.47300 5.14000   0.560 53.42000  ?  69  PHE A O   1 
ATOM   900  O  O   B PHE A 1 69  ? 34.50300 26.08000 4.61100   0.440 52.36000  ?  69  PHE A O   1 
ATOM   901  C  CB  A PHE A 1 69  ? 35.10100 23.86200 2.78000   0.560 52.97000  ?  69  PHE A CB  1 
ATOM   902  C  CB  B PHE A 1 69  ? 34.90800 24.28400 2.48900   0.440 52.17000  ?  69  PHE A CB  1 
ATOM   903  C  CG  A PHE A 1 69  ? 34.87600 22.81700 1.72800   0.560 52.58000  ?  69  PHE A CG  1 
ATOM   904  C  CG  B PHE A 1 69  ? 34.80700 23.17100 1.54800   0.440 50.84000  ?  69  PHE A CG  1 
ATOM   905  C  CD1 A PHE A 1 69  ? 35.90300 21.96900 1.35500   0.560 54.76000  ?  69  PHE A CD1 1 
ATOM   906  C  CD1 B PHE A 1 69  ? 35.89600 22.31800 1.36800   0.440 54.66000  ?  69  PHE A CD1 1 
ATOM   907  C  CD2 A PHE A 1 69  ? 33.63900 22.67100 1.12500   0.560 46.70000  ?  69  PHE A CD2 1 
ATOM   908  C  CD2 B PHE A 1 69  ? 33.61200 22.91100 0.92600   0.440 45.86000  ?  69  PHE A CD2 1 
ATOM   909  C  CE1 A PHE A 1 69  ? 35.70300 20.99700 0.39200   0.560 51.40000  ?  69  PHE A CE1 1 
ATOM   910  C  CE1 B PHE A 1 69  ? 35.80600 21.23700 0.56000   0.440 51.45000  ?  69  PHE A CE1 1 
ATOM   911  C  CE2 A PHE A 1 69  ? 33.43200 21.70400 0.16300   0.560 47.58000  ?  69  PHE A CE2 1 
ATOM   912  C  CE2 B PHE A 1 69  ? 33.49800 21.84700 0.12000   0.440 47.54000  ?  69  PHE A CE2 1 
ATOM   913  C  CZ  A PHE A 1 69  ? 34.46600 20.86400 -0.20400  0.560 47.92000  ?  69  PHE A CZ  1 
ATOM   914  C  CZ  B PHE A 1 69  ? 34.59300 20.99100 -0.08900  0.440 48.32000  ?  69  PHE A CZ  1 
ATOM   915  N  N   A ALA A 1 70  ? 36.15100 24.05900 6.25100   0.560 49.52000  ?  70  ALA A N   1 
ATOM   916  N  N   B ALA A 1 70  ? 35.26400 24.57400 6.12000   0.440 52.72000  ?  70  ALA A N   1 
ATOM   917  C  CA  A ALA A 1 70  ? 36.29500 24.92500 7.40900   0.560 52.10000  ?  70  ALA A CA  1 
ATOM   918  C  CA  B ALA A 1 70  ? 35.52200 25.53600 7.17400   0.440 49.02000  ?  70  ALA A CA  1 
ATOM   919  C  C   A ALA A 1 70  ? 36.98400 26.23800 7.06100   0.560 45.98000  ?  70  ALA A C   1 
ATOM   920  C  C   B ALA A 1 70  ? 36.27700 26.75800 6.67400   0.440 46.07000  ?  70  ALA A C   1 
ATOM   921  O  O   A ALA A 1 70  ? 36.59600 27.28500 7.59300   0.560 39.35000  ?  70  ALA A O   1 
ATOM   922  O  O   B ALA A 1 70  ? 35.86100 27.87300 7.03100   0.440 49.36000  ?  70  ALA A O   1 
ATOM   923  C  CB  A ALA A 1 70  ? 37.06800 24.20400 8.51400   0.560 42.80000  ?  70  ALA A CB  1 
ATOM   924  C  CB  B ALA A 1 70  ? 36.23800 24.79900 8.32100   0.440 45.61000  ?  70  ALA A CB  1 
ATOM   925  N  N   A PRO A 1 71  ? 38.00700 26.24300 6.20100   0.560 48.59000  ?  71  PRO A N   1 
ATOM   926  N  N   B PRO A 1 71  ? 37.31300 26.64900 5.80700   0.440 50.86000  ?  71  PRO A N   1 
ATOM   927  C  CA  A PRO A 1 71  ? 38.64900 27.52900 5.87300   0.560 50.54000  ?  71  PRO A CA  1 
ATOM   928  C  CA  B PRO A 1 71  ? 37.97500 27.87500 5.26500   0.440 49.85000  ?  71  PRO A CA  1 
ATOM   929  C  C   A PRO A 1 71  ? 37.68300 28.54100 5.28200   0.560 48.54000  ?  71  PRO A C   1 
ATOM   930  C  C   B PRO A 1 71  ? 37.06300 28.85000 4.55500   0.440 39.72000  ?  71  PRO A C   1 
ATOM   931  O  O   A PRO A 1 71  ? 37.85100 29.74900 5.49800   0.560 47.33000  ?  71  PRO A O   1 
ATOM   932  O  O   B PRO A 1 71  ? 37.30500 30.06300 4.58100   0.440 38.51000  ?  71  PRO A O   1 
ATOM   933  C  CB  A PRO A 1 71  ? 39.74900 27.13200 4.87800   0.560 51.95000  ?  71  PRO A CB  1 
ATOM   934  C  CB  B PRO A 1 71  ? 38.99600 27.31300 4.28300   0.440 47.77000  ?  71  PRO A CB  1 
ATOM   935  C  CG  A PRO A 1 71  ? 40.07500 25.71100 5.24300   0.560 53.64000  ?  71  PRO A CG  1 
ATOM   936  C  CG  B PRO A 1 71  ? 39.18900 25.90400 4.72100   0.440 48.69000  ?  71  PRO A CG  1 
ATOM   937  C  CD  A PRO A 1 71  ? 38.74200 25.09900 5.62400   0.560 51.57000  ?  71  PRO A CD  1 
ATOM   938  C  CD  B PRO A 1 71  ? 37.91500 25.42500 5.24100   0.440 49.96000  ?  71  PRO A CD  1 
ATOM   939  N  N   A ARG A 1 72  ? 36.66300 28.07900 4.55600   0.560 40.77000  ?  72  ARG A N   1 
ATOM   940  N  N   B ARG A 1 72  ? 36.02700 28.33200 3.90300   0.440 46.69000  ?  72  ARG A N   1 
ATOM   941  C  CA  A ARG A 1 72  ? 35.67900 28.99800 3.99600   0.560 44.70000  ?  72  ARG A CA  1 
ATOM   942  C  CA  B ARG A 1 72  ? 34.98200 29.15100 3.30200   0.440 42.95000  ?  72  ARG A CA  1 
ATOM   943  C  C   A ARG A 1 72  ? 35.02800 29.84300 5.08400   0.560 45.82000  ?  72  ARG A C   1 
ATOM   944  C  C   B ARG A 1 72  ? 34.25600 29.99400 4.34700   0.440 42.49000  ?  72  ARG A C   1 
ATOM   945  O  O   A ARG A 1 72  ? 34.82100 31.04800 4.90200   0.560 48.06000  ?  72  ARG A O   1 
ATOM   946  O  O   B ARG A 1 72  ? 34.06300 31.19700 4.14600   0.440 44.22000  ?  72  ARG A O   1 
ATOM   947  C  CB  A ARG A 1 72  ? 34.62300 28.21300 3.21500   0.560 46.67000  ?  72  ARG A CB  1 
ATOM   948  C  CB  B ARG A 1 72  ? 34.03200 28.21800 2.54500   0.440 43.40000  ?  72  ARG A CB  1 
ATOM   949  C  CG  A ARG A 1 72  ? 33.29000 28.91800 3.06800   0.560 42.90000  ?  72  ARG A CG  1 
ATOM   950  C  CG  B ARG A 1 72  ? 32.57500 28.57100 2.63600   0.440 44.27000  ?  72  ARG A CG  1 
ATOM   951  C  CD  A ARG A 1 72  ? 32.22300 27.96400 2.53700   0.560 42.33000  ?  72  ARG A CD  1 
ATOM   952  C  CD  B ARG A 1 72  ? 31.62800 27.42700 2.19000   0.440 41.62000  ?  72  ARG A CD  1 
ATOM   953  N  NE  A ARG A 1 72  ? 32.43400 27.64800 1.12300   0.560 44.56000  ?  72  ARG A NE  1 
ATOM   954  N  NE  B ARG A 1 72  ? 31.83100 27.01700 0.81000   0.440 43.59000  ?  72  ARG A NE  1 
ATOM   955  C  CZ  A ARG A 1 72  ? 31.81300 26.67200 0.46700   0.560 44.24000  ?  72  ARG A CZ  1 
ATOM   956  C  CZ  B ARG A 1 72  ? 31.07200 26.12900 0.17600   0.440 45.00000  ?  72  ARG A CZ  1 
ATOM   957  N  NH1 A ARG A 1 72  ? 30.93500 25.90300 1.09300   0.560 48.57000  ?  72  ARG A NH1 1 
ATOM   958  N  NH1 B ARG A 1 72  ? 29.87300 25.80900 0.59900   0.440 39.15000  ?  72  ARG A NH1 1 
ATOM   959  N  NH2 A ARG A 1 72  ? 32.07500 26.46600 -0.81500  0.560 52.15000  ?  72  ARG A NH2 1 
ATOM   960  N  NH2 B ARG A 1 72  ? 31.50900 25.58400 -0.94400  0.440 44.20000  ?  72  ARG A NH2 1 
ATOM   961  N  N   A TYR A 1 73  ? 34.66900 29.22900 6.21200   0.560 43.45000  ?  73  TYR A N   1 
ATOM   962  N  N   B TYR A 1 73  ? 33.88900 29.41100 5.49500   0.440 43.83000  ?  73  TYR A N   1 
ATOM   963  C  CA  A TYR A 1 73  ? 33.93600 29.97100 7.23200   0.560 37.46000  ?  73  TYR A CA  1 
ATOM   964  C  CA  B TYR A 1 73  ? 33.23700 30.21700 6.53400   0.440 37.80000  ?  73  TYR A CA  1 
ATOM   965  C  C   A TYR A 1 73  ? 34.85100 30.87900 8.04300   0.560 41.45000  ?  73  TYR A C   1 
ATOM   966  C  C   B TYR A 1 73  ? 34.20600 31.14100 7.27300   0.440 38.41000  ?  73  TYR A C   1 
ATOM   967  O  O   A TYR A 1 73  ? 34.44200 31.98000 8.42500   0.560 44.31000  ?  73  TYR A O   1 
ATOM   968  O  O   B TYR A 1 73  ? 33.82600 32.24100 7.66700   0.440 39.98000  ?  73  TYR A O   1 
ATOM   969  C  CB  A TYR A 1 73  ? 33.18000 29.00100 8.13500   0.560 50.46000  ?  73  TYR A CB  1 
ATOM   970  C  CB  B TYR A 1 73  ? 32.50000 29.31000 7.53300   0.440 45.99000  ?  73  TYR A CB  1 
ATOM   971  C  CG  A TYR A 1 73  ? 32.10800 28.25500 7.38000   0.560 40.77000  ?  73  TYR A CG  1 
ATOM   972  C  CG  B TYR A 1 73  ? 31.33900 28.53000 6.91600   0.440 42.04000  ?  73  TYR A CG  1 
ATOM   973  C  CD1 A TYR A 1 73  ? 30.86800 28.83100 7.13900   0.560 45.43000  ?  73  TYR A CD1 1 
ATOM   974  C  CD1 B TYR A 1 73  ? 31.54900 27.32900 6.26000   0.440 40.84000  ?  73  TYR A CD1 1 
ATOM   975  C  CD2 A TYR A 1 73  ? 32.34500 26.98400 6.88100   0.560 49.10000  ?  73  TYR A CD2 1 
ATOM   976  C  CD2 B TYR A 1 73  ? 30.04200 29.06400 6.92600   0.440 47.82000  ?  73  TYR A CD2 1 
ATOM   977  C  CE1 A TYR A 1 73  ? 29.89100 28.15400 6.43700   0.560 47.78000  ?  73  TYR A CE1 1 
ATOM   978  C  CE1 B TYR A 1 73  ? 30.48800 26.64100 5.66200   0.440 45.78000  ?  73  TYR A CE1 1 
ATOM   979  C  CE2 A TYR A 1 73  ? 31.37500 26.30000 6.17700   0.560 46.55000  ?  73  TYR A CE2 1 
ATOM   980  C  CE2 B TYR A 1 73  ? 28.95800 28.39200 6.35100   0.440 44.26000  ?  73  TYR A CE2 1 
ATOM   981  C  CZ  A TYR A 1 73  ? 30.15100 26.89000 5.95900   0.560 46.40000  ?  73  TYR A CZ  1 
ATOM   982  C  CZ  B TYR A 1 73  ? 29.19500 27.17800 5.71900   0.440 48.86000  ?  73  TYR A CZ  1 
ATOM   983  O  OH  A TYR A 1 73  ? 29.18300 26.20900 5.25700   0.560 53.51000  ?  73  TYR A OH  1 
ATOM   984  O  OH  B TYR A 1 73  ? 28.14400 26.50700 5.15000   0.440 55.82000  ?  73  TYR A OH  1 
ATOM   985  N  N   A ILE A 1 74  ? 36.09100 30.46000 8.30100   0.560 41.05000  ?  74  ILE A N   1 
ATOM   986  N  N   B ILE A 1 74  ? 35.44400 30.73700 7.52500   0.440 36.84000  ?  74  ILE A N   1 
ATOM   987  C  CA  A ILE A 1 74  ? 37.04400 31.37400 8.92600   0.560 48.25000  ?  74  ILE A CA  1 
ATOM   988  C  CA  B ILE A 1 74  ? 36.33300 31.67100 8.19000   0.440 37.14000  ?  74  ILE A CA  1 
ATOM   989  C  C   A ILE A 1 74  ? 37.24000 32.60000 8.04000   0.560 42.53000  ?  74  ILE A C   1 
ATOM   990  C  C   B ILE A 1 74  ? 36.44200 32.90500 7.35200   0.440 38.67000  ?  74  ILE A C   1 
ATOM   991  O  O   A ILE A 1 74  ? 37.22300 33.74200 8.51200   0.560 54.28000  ?  74  ILE A O   1 
ATOM   992  O  O   B ILE A 1 74  ? 36.31800 34.03400 7.85200   0.440 41.76000  ?  74  ILE A O   1 
ATOM   993  C  CB  A ILE A 1 74  ? 38.37700 30.66000 9.20500   0.560 45.03000  ?  74  ILE A CB  1 
ATOM   994  C  CB  B ILE A 1 74  ? 37.70600 31.02400 8.47700   0.440 48.37000  ?  74  ILE A CB  1 
ATOM   995  C  CG1 A ILE A 1 74  ? 38.22500 29.67300 10.36500  0.560 50.98000  ?  74  ILE A CG1 1 
ATOM   996  C  CG1 B ILE A 1 74  ? 37.62100 30.08900 9.68200   0.440 51.46000  ?  74  ILE A CG1 1 
ATOM   997  C  CG2 A ILE A 1 74  ? 39.45800 31.67200 9.55200   0.560 38.41000  ?  74  ILE A CG2 1 
ATOM   998  C  CG2 B ILE A 1 74  ? 38.77700 32.04200 8.82800   0.440 45.21000  ?  74  ILE A CG2 1 
ATOM   999  C  CD1 A ILE A 1 74  ? 37.63700 28.34600 9.97000   0.560 55.28000  ?  74  ILE A CD1 1 
ATOM   1000 C  CD1 B ILE A 1 74  ? 37.28800 28.72100 9.36700   0.440 52.67000  ?  74  ILE A CD1 1 
ATOM   1001 N  N   A ASP A 1 75  ? 37.43000 32.37200 6.73800   0.560 41.95000  ?  75  ASP A N   1 
ATOM   1002 N  N   B ASP A 1 75  ? 36.63200 32.68100 6.04900   0.440 41.40000  ?  75  ASP A N   1 
ATOM   1003 C  CA  A ASP A 1 75  ? 37.48100 33.45200 5.75600   0.560 43.87000  ?  75  ASP A CA  1 
ATOM   1004 C  CA  B ASP A 1 75  ? 36.68800 33.71900 5.03400   0.440 40.41000  ?  75  ASP A CA  1 
ATOM   1005 C  C   A ASP A 1 75  ? 36.29000 34.38800 5.91100   0.560 40.27000  ?  75  ASP A C   1 
ATOM   1006 C  C   B ASP A 1 75  ? 35.56700 34.70800 5.26600   0.440 36.57000  ?  75  ASP A C   1 
ATOM   1007 O  O   A ASP A 1 75  ? 36.45400 35.59400 6.12600   0.560 41.18000  ?  75  ASP A O   1 
ATOM   1008 O  O   B ASP A 1 75  ? 35.79700 35.90000 5.49700   0.440 37.02000  ?  75  ASP A O   1 
ATOM   1009 C  CB  A ASP A 1 75  ? 37.54300 32.82400 4.35500   0.560 42.87000  ?  75  ASP A CB  1 
ATOM   1010 C  CB  B ASP A 1 75  ? 36.56400 33.03300 3.66300   0.440 40.54000  ?  75  ASP A CB  1 
ATOM   1011 C  CG  A ASP A 1 75  ? 37.21300 33.79700 3.22100   0.560 40.49000  ?  75  ASP A CG  1 
ATOM   1012 C  CG  B ASP A 1 75  ? 36.78600 33.97200 2.46800   0.440 41.49000  ?  75  ASP A CG  1 
ATOM   1013 O  OD1 A ASP A 1 75  ? 36.92900 34.98800 3.46200   0.560 46.35000  ?  75  ASP A OD1 1 
ATOM   1014 O  OD1 B ASP A 1 75  ? 37.47900 35.01300 2.56200   0.440 45.29000  ?  75  ASP A OD1 1 
ATOM   1015 O  OD2 A ASP A 1 75  ? 37.24200 33.34600 2.05200   0.560 46.91000  -1 75  ASP A OD2 1 
ATOM   1016 O  OD2 B ASP A 1 75  ? 36.25200 33.68000 1.40300   0.440 41.48000  -1 75  ASP A OD2 1 
ATOM   1017 N  N   A TRP A 1 76  ? 35.07600 33.84300 5.81400   0.560 36.34000  ?  76  TRP A N   1 
ATOM   1018 N  N   B TRP A 1 76  ? 34.35300 34.19200 5.35500   0.440 30.45000  ?  76  TRP A N   1 
ATOM   1019 C  CA  A TRP A 1 76  ? 33.88800 34.68900 5.84900   0.560 32.05000  ?  76  TRP A CA  1 
ATOM   1020 C  CA  B TRP A 1 76  ? 33.20000 35.05400 5.48800   0.440 32.99000  ?  76  TRP A CA  1 
ATOM   1021 C  C   A TRP A 1 76  ? 33.81800 35.49200 7.14400   0.560 39.95000  ?  76  TRP A C   1 
ATOM   1022 C  C   B TRP A 1 76  ? 33.20400 35.76000 6.82500   0.440 37.13000  ?  76  TRP A C   1 
ATOM   1023 O  O   A TRP A 1 76  ? 33.44500 36.67000 7.13100   0.560 37.94000  ?  76  TRP A O   1 
ATOM   1024 O  O   B TRP A 1 76  ? 32.90200 36.95300 6.89400   0.440 37.93000  ?  76  TRP A O   1 
ATOM   1025 C  CB  A TRP A 1 76  ? 32.63400 33.83000 5.67500   0.560 31.67000  ?  76  TRP A CB  1 
ATOM   1026 C  CB  B TRP A 1 76  ? 31.93200 34.22400 5.32500   0.440 33.70000  ?  76  TRP A CB  1 
ATOM   1027 C  CG  A TRP A 1 76  ? 32.44500 33.27600 4.28100   0.560 46.08000  ?  76  TRP A CG  1 
ATOM   1028 C  CG  B TRP A 1 76  ? 31.74700 33.68000 3.91600   0.440 43.78000  ?  76  TRP A CG  1 
ATOM   1029 C  CD1 A TRP A 1 76  ? 33.23900 33.49400 3.19500   0.560 40.36000  ?  76  TRP A CD1 1 
ATOM   1030 C  CD1 B TRP A 1 76  ? 32.47700 33.99500 2.81400   0.440 36.29000  ?  76  TRP A CD1 1 
ATOM   1031 C  CD2 A TRP A 1 76  ? 31.39100 32.41200 3.83900   0.560 36.32000  ?  76  TRP A CD2 1 
ATOM   1032 C  CD2 B TRP A 1 76  ? 30.82400 32.66100 3.50300   0.440 36.25000  ?  76  TRP A CD2 1 
ATOM   1033 N  NE1 A TRP A 1 76  ? 32.74300 32.82600 2.10200   0.560 37.52000  ?  76  TRP A NE1 1 
ATOM   1034 N  NE1 B TRP A 1 76  ? 32.05200 33.26500 1.71600   0.440 39.45000  ?  76  TRP A NE1 1 
ATOM   1035 C  CE2 A TRP A 1 76  ? 31.61000 32.14900 2.47200   0.560 41.01000  ?  76  TRP A CE2 1 
ATOM   1036 C  CE2 B TRP A 1 76  ? 31.02800 32.44600 2.11200   0.440 40.82000  ?  76  TRP A CE2 1 
ATOM   1037 C  CE3 A TRP A 1 76  ? 30.28300 31.83300 4.46700   0.560 34.08000  ?  76  TRP A CE3 1 
ATOM   1038 C  CE3 B TRP A 1 76  ? 29.82100 31.93300 4.16400   0.440 33.86000  ?  76  TRP A CE3 1 
ATOM   1039 C  CZ2 A TRP A 1 76  ? 30.76100 31.33400 1.72200   0.560 40.84000  ?  76  TRP A CZ2 1 
ATOM   1040 C  CZ2 B TRP A 1 76  ? 30.26700 31.54500 1.36900   0.440 39.45000  ?  76  TRP A CZ2 1 
ATOM   1041 C  CZ3 A TRP A 1 76  ? 29.44200 31.02300 3.72000   0.560 40.87000  ?  76  TRP A CZ3 1 
ATOM   1042 C  CZ3 B TRP A 1 76  ? 29.06600 31.00200 3.42600   0.440 41.57000  ?  76  TRP A CZ3 1 
ATOM   1043 C  CH2 A TRP A 1 76  ? 29.68600 30.78200 2.36400   0.560 38.07000  ?  76  TRP A CH2 1 
ATOM   1044 C  CH2 B TRP A 1 76  ? 29.28200 30.83400 2.03000   0.440 35.95000  ?  76  TRP A CH2 1 
ATOM   1045 N  N   A ILE A 1 77  ? 34.17600 34.87300 8.27200   0.560 36.66000  ?  77  ILE A N   1 
ATOM   1046 N  N   B ILE A 1 77  ? 33.44800 35.02100 7.92000   0.440 40.72000  ?  77  ILE A N   1 
ATOM   1047 C  CA  A ILE A 1 77  ? 34.04600 35.54200 9.56500   0.560 40.45000  ?  77  ILE A CA  1 
ATOM   1048 C  CA  B ILE A 1 77  ? 33.41300 35.69400 9.21500   0.440 39.79000  ?  77  ILE A CA  1 
ATOM   1049 C  C   A ILE A 1 77  ? 34.96800 36.74900 9.65500   0.560 38.57000  ?  77  ILE A C   1 
ATOM   1050 C  C   B ILE A 1 77  ? 34.35700 36.85900 9.19400   0.440 35.83000  ?  77  ILE A C   1 
ATOM   1051 O  O   A ILE A 1 77  ? 34.66900 37.71900 10.36500  0.560 46.18000  ?  77  ILE A O   1 
ATOM   1052 O  O   B ILE A 1 77  ? 34.02800 37.94500 9.65400   0.440 30.81000  ?  77  ILE A O   1 
ATOM   1053 C  CB  A ILE A 1 77  ? 34.34100 34.55300 10.71200  0.560 33.73000  ?  77  ILE A CB  1 
ATOM   1054 C  CB  B ILE A 1 77  ? 33.78100 34.75200 10.36100  0.440 41.42000  ?  77  ILE A CB  1 
ATOM   1055 C  CG1 A ILE A 1 77  ? 33.25200 33.48500 10.82700  0.560 40.83000  ?  77  ILE A CG1 1 
ATOM   1056 C  CG1 B ILE A 1 77  ? 32.91800 33.50900 10.31100  0.440 41.55000  ?  77  ILE A CG1 1 
ATOM   1057 C  CG2 A ILE A 1 77  ? 34.48500 35.30100 12.04300  0.560 38.99000  ?  77  ILE A CG2 1 
ATOM   1058 C  CG2 B ILE A 1 77  ? 33.56700 35.50200 11.64300  0.440 40.13000  ?  77  ILE A CG2 1 
ATOM   1059 C  CD1 A ILE A 1 77  ? 33.66200 32.27300 11.66000  0.560 53.06000  ?  77  ILE A CD1 1 
ATOM   1060 C  CD1 B ILE A 1 77  ? 33.65200 32.31400 10.79400  0.440 42.30000  ?  77  ILE A CD1 1 
ATOM   1061 N  N   A LEU A 1 78  ? 36.10700 36.70600 8.96700   0.560 37.23000  ?  78  LEU A N   1 
ATOM   1062 N  N   B LEU A 1 78  ? 35.52500 36.66000 8.59100   0.440 35.91000  ?  78  LEU A N   1 
ATOM   1063 C  CA  A LEU A 1 78  ? 37.06000 37.80400 9.03000   0.560 40.63000  ?  78  LEU A CA  1 
ATOM   1064 C  CA  B LEU A 1 78  ? 36.52000 37.71200 8.58900   0.440 37.72000  ?  78  LEU A CA  1 
ATOM   1065 C  C   A LEU A 1 78  ? 36.87200 38.81000 7.91000   0.560 41.75000  ?  78  LEU A C   1 
ATOM   1066 C  C   B LEU A 1 78  ? 36.19900 38.79900 7.57200   0.440 44.07000  ?  78  LEU A C   1 
ATOM   1067 O  O   A LEU A 1 78  ? 37.12500 40.00400 8.11300   0.560 41.93000  ?  78  LEU A O   1 
ATOM   1068 O  O   B LEU A 1 78  ? 36.20300 39.98700 7.90900   0.440 47.12000  ?  78  LEU A O   1 
ATOM   1069 C  CB  A LEU A 1 78  ? 38.49000 37.26600 8.97400   0.560 48.19000  ?  78  LEU A CB  1 
ATOM   1070 C  CB  B LEU A 1 78  ? 37.90100 37.12300 8.31800   0.440 41.17000  ?  78  LEU A CB  1 
ATOM   1071 C  CG  A LEU A 1 78  ? 38.90800 36.33500 10.11100  0.560 40.69000  ?  78  LEU A CG  1 
ATOM   1072 C  CG  B LEU A 1 78  ? 38.57600 36.38700 9.47300   0.440 42.29000  ?  78  LEU A CG  1 
ATOM   1073 C  CD1 A LEU A 1 78  ? 40.23100 35.67100 9.76900   0.560 42.83000  ?  78  LEU A CD1 1 
ATOM   1074 C  CD1 B LEU A 1 78  ? 40.07900 36.07800 9.15900   0.440 41.38000  ?  78  LEU A CD1 1 
ATOM   1075 C  CD2 A LEU A 1 78  ? 38.98800 37.10000 11.41200  0.560 51.48000  ?  78  LEU A CD2 1 
ATOM   1076 C  CD2 B LEU A 1 78  ? 38.39800 37.16000 10.77300  0.440 43.13000  ?  78  LEU A CD2 1 
ATOM   1077 N  N   A THR A 1 79  ? 36.44300 38.35900 6.73200   0.560 42.28000  ?  79  THR A N   1 
ATOM   1078 N  N   B THR A 1 79  ? 35.96000 38.43400 6.31500   0.440 36.98000  ?  79  THR A N   1 
ATOM   1079 C  CA  A THR A 1 79  ? 36.37400 39.24600 5.57900   0.560 37.33000  ?  79  THR A CA  1 
ATOM   1080 C  CA  B THR A 1 79  ? 36.01000 39.49500 5.31100   0.440 39.21000  ?  79  THR A CA  1 
ATOM   1081 C  C   A THR A 1 79  ? 35.04700 39.99000 5.48900   0.560 43.48000  ?  79  THR A C   1 
ATOM   1082 C  C   B THR A 1 79  ? 34.74400 40.32200 5.33900   0.440 44.38000  ?  79  THR A C   1 
ATOM   1083 O  O   A THR A 1 79  ? 35.02800 41.16300 5.09800   0.560 45.07000  ?  79  THR A O   1 
ATOM   1084 O  O   B THR A 1 79  ? 34.80400 41.52400 5.09500   0.440 45.36000  ?  79  THR A O   1 
ATOM   1085 C  CB  A THR A 1 79  ? 36.61300 38.46800 4.27700   0.560 39.68000  ?  79  THR A CB  1 
ATOM   1086 C  CB  B THR A 1 79  ? 36.21600 38.97500 3.85200   0.440 38.52000  ?  79  THR A CB  1 
ATOM   1087 O  OG1 A THR A 1 79  ? 35.61000 37.46200 4.10700   0.560 43.63000  ?  79  THR A OG1 1 
ATOM   1088 O  OG1 B THR A 1 79  ? 35.08700 38.20000 3.43800   0.440 32.47000  ?  79  THR A OG1 1 
ATOM   1089 C  CG2 A THR A 1 79  ? 37.98900 37.81800 4.28400   0.560 30.64000  ?  79  THR A CG2 1 
ATOM   1090 C  CG2 B THR A 1 79  ? 37.53200 38.19300 3.66000   0.440 29.93000  ?  79  THR A CG2 1 
ATOM   1091 N  N   A THR A 1 80  ? 33.93100 39.35000 5.84400   0.560 42.57000  ?  80  THR A N   1 
ATOM   1092 N  N   B THR A 1 80  ? 33.58900 39.71800 5.64600   0.440 42.49000  ?  80  THR A N   1 
ATOM   1093 C  CA  A THR A 1 80  ? 32.65200 40.04700 5.73700   0.560 40.85000  ?  80  THR A CA  1 
ATOM   1094 C  CA  B THR A 1 80  ? 32.35000 40.48700 5.55900   0.440 41.42000  ?  80  THR A CA  1 
ATOM   1095 C  C   A THR A 1 80  ? 32.55800 41.25500 6.66400   0.560 45.14000  ?  80  THR A C   1 
ATOM   1096 C  C   B THR A 1 80  ? 32.26500 41.66900 6.53900   0.440 44.24000  ?  80  THR A C   1 
ATOM   1097 O  O   A THR A 1 80  ? 31.98900 42.27500 6.23600   0.560 42.78000  ?  80  THR A O   1 
ATOM   1098 O  O   B THR A 1 80  ? 31.53500 42.62300 6.24600   0.440 43.53000  ?  80  THR A O   1 
ATOM   1099 C  CB  A THR A 1 80  ? 31.47500 39.08800 5.98000   0.560 36.90000  ?  80  THR A CB  1 
ATOM   1100 C  CB  B THR A 1 80  ? 31.12300 39.56800 5.71200   0.440 39.62000  ?  80  THR A CB  1 
ATOM   1101 O  OG1 A THR A 1 80  ? 31.57900 38.47200 7.27100   0.560 43.37000  ?  80  THR A OG1 1 
ATOM   1102 O  OG1 B THR A 1 80  ? 31.06400 39.04700 7.01900   0.440 42.70000  ?  80  THR A OG1 1 
ATOM   1103 C  CG2 A THR A 1 80  ? 31.42100 38.02100 4.89000   0.560 38.61000  ?  80  THR A CG2 1 
ATOM   1104 C  CG2 B THR A 1 80  ? 31.13100 38.37700 4.69500   0.440 38.92000  ?  80  THR A CG2 1 
ATOM   1105 N  N   A PRO A 1 81  ? 33.06400 41.23400 7.90700   0.560 46.58000  ?  81  PRO A N   1 
ATOM   1106 N  N   B PRO A 1 81  ? 32.95400 41.68500 7.70100   0.440 47.10000  ?  81  PRO A N   1 
ATOM   1107 C  CA  A PRO A 1 81  ? 33.03500 42.47900 8.69800   0.560 47.90000  ?  81  PRO A CA  1 
ATOM   1108 C  CA  B PRO A 1 81  ? 33.00600 42.94800 8.44900   0.440 47.13000  ?  81  PRO A CA  1 
ATOM   1109 C  C   A PRO A 1 81  ? 33.88400 43.57800 8.08400   0.560 45.92000  ?  81  PRO A C   1 
ATOM   1110 C  C   B PRO A 1 81  ? 33.88300 43.95000 7.76100   0.440 45.80000  ?  81  PRO A C   1 
ATOM   1111 O  O   A PRO A 1 81  ? 33.57700 44.76200 8.26700   0.560 47.67000  ?  81  PRO A O   1 
ATOM   1112 O  O   B PRO A 1 81  ? 33.62700 45.15200 7.88200   0.440 45.51000  ?  81  PRO A O   1 
ATOM   1113 C  CB  A PRO A 1 81  ? 33.55900 42.05200 10.07800  0.560 45.39000  ?  81  PRO A CB  1 
ATOM   1114 C  CB  B PRO A 1 81  ? 33.56400 42.55500 9.82300   0.440 45.14000  ?  81  PRO A CB  1 
ATOM   1115 C  CG  A PRO A 1 81  ? 34.34100 40.80500 9.82500   0.560 49.11000  ?  81  PRO A CG  1 
ATOM   1116 C  CG  B PRO A 1 81  ? 34.20400 41.26600 9.62600   0.440 47.88000  ?  81  PRO A CG  1 
ATOM   1117 C  CD  A PRO A 1 81  ? 33.66900 40.11500 8.65700   0.560 41.58000  ?  81  PRO A CD  1 
ATOM   1118 C  CD  B PRO A 1 81  ? 33.31200 40.56600 8.57100   0.440 42.01000  ?  81  PRO A CD  1 
ATOM   1119 N  N   A LEU A 1 82  ? 34.93700 43.21600 7.34800   0.560 47.78000  ?  82  LEU A N   1 
ATOM   1120 N  N   B LEU A 1 82  ? 34.92400 43.48400 7.06400   0.440 47.97000  ?  82  LEU A N   1 
ATOM   1121 C  CA  A LEU A 1 82  ? 35.74900 44.21600 6.66600   0.560 49.00000  ?  82  LEU A CA  1 
ATOM   1122 C  CA  B LEU A 1 82  ? 35.70200 44.40500 6.23300   0.440 49.17000  ?  82  LEU A CA  1 
ATOM   1123 C  C   A LEU A 1 82  ? 34.98200 44.85200 5.51400   0.560 48.48000  ?  82  LEU A C   1 
ATOM   1124 C  C   B LEU A 1 82  ? 34.81600 45.07500 5.16600   0.440 47.78000  ?  82  LEU A C   1 
ATOM   1125 O  O   A LEU A 1 82  ? 35.15500 46.04300 5.22800   0.560 44.63000  ?  82  LEU A O   1 
ATOM   1126 O  O   B LEU A 1 82  ? 34.94500 46.27200 4.88000   0.440 46.09000  ?  82  LEU A O   1 
ATOM   1127 C  CB  A LEU A 1 82  ? 37.03800 43.57300 6.16100   0.560 47.58000  ?  82  LEU A CB  1 
ATOM   1128 C  CB  B LEU A 1 82  ? 36.88100 43.67400 5.59200   0.440 44.35000  ?  82  LEU A CB  1 
ATOM   1129 C  CG  A LEU A 1 82  ? 38.07600 43.18700 7.21900   0.560 47.57000  ?  82  LEU A CG  1 
ATOM   1130 C  CG  B LEU A 1 82  ? 37.96900 43.21300 6.55000   0.440 49.56000  ?  82  LEU A CG  1 
ATOM   1131 C  CD1 A LEU A 1 82  ? 39.19300 42.38500 6.57000   0.560 44.43000  ?  82  LEU A CD1 1 
ATOM   1132 C  CD1 B LEU A 1 82  ? 39.24000 42.73100 5.79400   0.440 41.64000  ?  82  LEU A CD1 1 
ATOM   1133 C  CD2 A LEU A 1 82  ? 38.61100 44.42300 7.91000   0.560 47.86000  ?  82  LEU A CD2 1 
ATOM   1134 C  CD2 B LEU A 1 82  ? 38.26200 44.37300 7.45400   0.440 45.52000  ?  82  LEU A CD2 1 
ATOM   1135 N  N   A ILE A 1 83  ? 34.13800 44.07400 4.83700   0.560 41.60000  ?  83  ILE A N   1 
ATOM   1136 N  N   B ILE A 1 83  ? 33.90300 44.30900 4.57200   0.440 41.89000  ?  83  ILE A N   1 
ATOM   1137 C  CA  A ILE A 1 83  ? 33.28700 44.63900 3.79700   0.560 44.66000  ?  83  ILE A CA  1 
ATOM   1138 C  CA  B ILE A 1 83  ? 33.02800 44.83800 3.52500   0.440 45.39000  ?  83  ILE A CA  1 
ATOM   1139 C  C   A ILE A 1 83  ? 32.27200 45.59500 4.41000   0.560 48.73000  ?  83  ILE A C   1 
ATOM   1140 C  C   B ILE A 1 83  ? 32.04100 45.82400 4.11600   0.440 48.94000  ?  83  ILE A C   1 
ATOM   1141 O  O   A ILE A 1 83  ? 32.01700 46.68100 3.87500   0.560 48.48000  ?  83  ILE A O   1 
ATOM   1142 O  O   B ILE A 1 83  ? 31.91800 46.96900 3.66200   0.440 46.64000  ?  83  ILE A O   1 
ATOM   1143 C  CB  A ILE A 1 83  ? 32.59100 43.51600 3.00800   0.560 45.43000  ?  83  ILE A CB  1 
ATOM   1144 C  CB  B ILE A 1 83  ? 32.30700 43.67700 2.81100   0.440 43.58000  ?  83  ILE A CB  1 
ATOM   1145 C  CG1 A ILE A 1 83  ? 33.61300 42.68600 2.23200   0.560 45.43000  ?  83  ILE A CG1 1 
ATOM   1146 C  CG1 B ILE A 1 83  ? 33.34200 42.83400 2.07200   0.440 44.16000  ?  83  ILE A CG1 1 
ATOM   1147 C  CG2 A ILE A 1 83  ? 31.55600 44.10400 2.06200   0.560 43.10000  ?  83  ILE A CG2 1 
ATOM   1148 C  CG2 B ILE A 1 83  ? 31.28600 44.15700 1.83500   0.440 43.27000  ?  83  ILE A CG2 1 
ATOM   1149 C  CD1 A ILE A 1 83  ? 33.03300 41.43900 1.58600   0.560 42.09000  ?  83  ILE A CD1 1 
ATOM   1150 C  CD1 B ILE A 1 83  ? 32.81400 41.44800 1.63400   0.440 42.31000  ?  83  ILE A CD1 1 
ATOM   1151 N  N   A VAL A 1 84  ? 31.66900 45.20200 5.53500   0.560 49.77000  ?  84  VAL A N   1 
ATOM   1152 N  N   B VAL A 1 84  ? 31.28200 45.37100 5.11000   0.440 49.30000  ?  84  VAL A N   1 
ATOM   1153 C  CA  A VAL A 1 84  ? 30.72500 46.07900 6.22100   0.560 48.74000  ?  84  VAL A CA  1 
ATOM   1154 C  CA  B VAL A 1 84  ? 30.41700 46.27100 5.85800   0.440 47.99000  ?  84  VAL A CA  1 
ATOM   1155 C  C   A VAL A 1 84  ? 31.44100 47.31400 6.74900   0.560 47.73000  ?  84  VAL A C   1 
ATOM   1156 C  C   B VAL A 1 84  ? 31.20900 47.48800 6.35200   0.440 48.64000  ?  84  VAL A C   1 
ATOM   1157 O  O   A VAL A 1 84  ? 30.89700 48.42500 6.72300   0.560 49.18000  ?  84  VAL A O   1 
ATOM   1158 O  O   B VAL A 1 84  ? 30.73400 48.63100 6.29700   0.440 50.51000  ?  84  VAL A O   1 
ATOM   1159 C  CB  A VAL A 1 84  ? 30.01000 45.30700 7.34600   0.560 49.72000  ?  84  VAL A CB  1 
ATOM   1160 C  CB  B VAL A 1 84  ? 29.75100 45.49900 7.02000   0.440 50.39000  ?  84  VAL A CB  1 
ATOM   1161 C  CG1 A VAL A 1 84  ? 29.25100 46.25400 8.25600   0.560 41.86000  ?  84  VAL A CG1 1 
ATOM   1162 C  CG1 B VAL A 1 84  ? 28.99900 46.43500 7.94000   0.440 39.75000  ?  84  VAL A CG1 1 
ATOM   1163 C  CG2 A VAL A 1 84  ? 29.08200 44.25300 6.75100   0.560 44.59000  ?  84  VAL A CG2 1 
ATOM   1164 C  CG2 B VAL A 1 84  ? 28.82200 44.38800 6.47500   0.440 45.38000  ?  84  VAL A CG2 1 
ATOM   1165 N  N   A TYR A 1 85  ? 32.67400 47.14600 7.22500   0.560 49.16000  ?  85  TYR A N   1 
ATOM   1166 N  N   B TYR A 1 85  ? 32.41900 47.27400 6.84700   0.440 47.98000  ?  85  TYR A N   1 
ATOM   1167 C  CA  A TYR A 1 85  ? 33.46200 48.29500 7.65800   0.560 54.32000  ?  85  TYR A CA  1 
ATOM   1168 C  CA  B TYR A 1 85  ? 33.22100 48.43100 7.21900   0.440 51.18000  ?  85  TYR A CA  1 
ATOM   1169 C  C   A TYR A 1 85  ? 33.69000 49.26400 6.50400   0.560 47.42000  ?  85  TYR A C   1 
ATOM   1170 C  C   B TYR A 1 85  ? 33.43400 49.34600 6.01900   0.440 51.20000  ?  85  TYR A C   1 
ATOM   1171 O  O   A TYR A 1 85  ? 33.49100 50.47600 6.64600   0.560 49.95000  ?  85  TYR A O   1 
ATOM   1172 O  O   B TYR A 1 85  ? 33.23300 50.56400 6.10200   0.440 48.41000  ?  85  TYR A O   1 
ATOM   1173 C  CB  A TYR A 1 85  ? 34.79100 47.81400 8.24000   0.560 52.47000  ?  85  TYR A CB  1 
ATOM   1174 C  CB  B TYR A 1 85  ? 34.55700 47.97800 7.80500   0.440 53.68000  ?  85  TYR A CB  1 
ATOM   1175 C  CG  A TYR A 1 85  ? 35.72500 48.92400 8.64700   0.560 57.23000  ?  85  TYR A CG  1 
ATOM   1176 C  CG  B TYR A 1 85  ? 35.50600 49.11100 8.04600   0.440 56.61000  ?  85  TYR A CG  1 
ATOM   1177 C  CD1 A TYR A 1 85  ? 35.36500 49.83700 9.62700   0.560 61.48000  ?  85  TYR A CD1 1 
ATOM   1178 C  CD1 B TYR A 1 85  ? 35.23700 50.10900 9.00900   0.440 61.50000  ?  85  TYR A CD1 1 
ATOM   1179 C  CD2 A TYR A 1 85  ? 36.97100 49.05800 8.05000   0.560 61.68000  ?  85  TYR A CD2 1 
ATOM   1180 C  CD2 B TYR A 1 85  ? 36.65900 49.23400 7.29200   0.440 55.00000  ?  85  TYR A CD2 1 
ATOM   1181 C  CE1 A TYR A 1 85  ? 36.22000 50.85400 10.00100  0.560 63.80000  ?  85  TYR A CE1 1 
ATOM   1182 C  CE1 B TYR A 1 85  ? 36.13300 51.19600 9.22900   0.440 60.77000  ?  85  TYR A CE1 1 
ATOM   1183 C  CE2 A TYR A 1 85  ? 37.83000 50.06800 8.41500   0.560 69.72000  ?  85  TYR A CE2 1 
ATOM   1184 C  CE2 B TYR A 1 85  ? 37.55600 50.30600 7.51300   0.440 64.41000  ?  85  TYR A CE2 1 
ATOM   1185 C  CZ  A TYR A 1 85  ? 37.45300 50.96500 9.39100   0.560 60.68000  ?  85  TYR A CZ  1 
ATOM   1186 C  CZ  B TYR A 1 85  ? 37.28600 51.27700 8.48000   0.440 61.64000  ?  85  TYR A CZ  1 
ATOM   1187 O  OH  A TYR A 1 85  ? 38.31300 51.97600 9.75700   0.560 70.26000  ?  85  TYR A OH  1 
ATOM   1188 O  OH  B TYR A 1 85  ? 38.18400 52.30700 8.66400   0.440 72.19000  ?  85  TYR A OH  1 
ATOM   1189 N  N   A PHE A 1 86  ? 34.09900 48.74500 5.34400   0.560 55.76000  ?  86  PHE A N   1 
ATOM   1190 N  N   B PHE A 1 86  ? 33.82700 48.76700 4.87500   0.440 55.39000  ?  86  PHE A N   1 
ATOM   1191 C  CA  A PHE A 1 86  ? 34.29000 49.59200 4.17000   0.560 52.19000  ?  86  PHE A CA  1 
ATOM   1192 C  CA  B PHE A 1 86  ? 34.01300 49.57500 3.67300   0.440 52.34000  ?  86  PHE A CA  1 
ATOM   1193 C  C   A PHE A 1 86  ? 33.02800 50.38900 3.86200   0.560 49.81000  ?  86  PHE A C   1 
ATOM   1194 C  C   B PHE A 1 86  ? 32.78700 50.43500 3.40700   0.440 48.61000  ?  86  PHE A C   1 
ATOM   1195 O  O   A PHE A 1 86  ? 33.07900 51.60700 3.65500   0.560 50.38000  ?  86  PHE A O   1 
ATOM   1196 O  O   B PHE A 1 86  ? 32.90000 51.63700 3.17400   0.440 52.16000  ?  86  PHE A O   1 
ATOM   1197 C  CB  A PHE A 1 86  ? 34.69700 48.72200 2.97600   0.560 52.85000  ?  86  PHE A CB  1 
ATOM   1198 C  CB  B PHE A 1 86  ? 34.32900 48.68300 2.46100   0.440 49.48000  ?  86  PHE A CB  1 
ATOM   1199 C  CG  A PHE A 1 86  ? 35.12400 49.50100 1.76300   0.560 45.24000  ?  86  PHE A CG  1 
ATOM   1200 C  CG  B PHE A 1 86  ? 34.72500 49.44700 1.21000   0.440 41.68000  ?  86  PHE A CG  1 
ATOM   1201 C  CD1 A PHE A 1 86  ? 34.18600 50.12800 0.96100   0.560 45.18000  ?  86  PHE A CD1 1 
ATOM   1202 C  CD1 B PHE A 1 86  ? 36.04100 49.79700 1.01600   0.440 44.81000  ?  86  PHE A CD1 1 
ATOM   1203 C  CD2 A PHE A 1 86  ? 36.46300 49.58800 1.41200   0.560 45.95000  ?  86  PHE A CD2 1 
ATOM   1204 C  CD2 B PHE A 1 86  ? 33.78900 49.82900 0.24700   0.440 53.20000  ?  86  PHE A CD2 1 
ATOM   1205 C  CE1 A PHE A 1 86  ? 34.57400 50.84000 -0.15600  0.560 52.25000  ?  86  PHE A CE1 1 
ATOM   1206 C  CE1 B PHE A 1 86  ? 36.43800 50.47500 -0.12100  0.440 56.38000  ?  86  PHE A CE1 1 
ATOM   1207 C  CE2 A PHE A 1 86  ? 36.85400 50.29600 0.29500   0.560 56.38000  ?  86  PHE A CE2 1 
ATOM   1208 C  CE2 B PHE A 1 86  ? 34.18900 50.51800 -0.91600  0.440 49.13000  ?  86  PHE A CE2 1 
ATOM   1209 C  CZ  A PHE A 1 86  ? 35.90900 50.92100 -0.49000  0.560 53.79000  ?  86  PHE A CZ  1 
ATOM   1210 C  CZ  B PHE A 1 86  ? 35.51300 50.84400 -1.08900  0.440 49.43000  ?  86  PHE A CZ  1 
ATOM   1211 N  N   A LEU A 1 87  ? 31.87700 49.71100 3.83500   0.560 49.06000  ?  87  LEU A N   1 
ATOM   1212 N  N   B LEU A 1 87  ? 31.60600 49.82800 3.43800   0.440 47.16000  ?  87  LEU A N   1 
ATOM   1213 C  CA  A LEU A 1 87  ? 30.62100 50.40700 3.58100   0.560 47.39000  ?  87  LEU A CA  1 
ATOM   1214 C  CA  B LEU A 1 87  ? 30.38100 50.58300 3.21200   0.440 47.69000  ?  87  LEU A CA  1 
ATOM   1215 C  C   A LEU A 1 87  ? 30.31400 51.42700 4.66900   0.560 56.11000  ?  87  LEU A C   1 
ATOM   1216 C  C   B LEU A 1 87  ? 30.20700 51.66800 4.26800   0.440 56.63000  ?  87  LEU A C   1 
ATOM   1217 O  O   A LEU A 1 87  ? 29.75100 52.49000 4.38500   0.560 59.75000  ?  87  LEU A O   1 
ATOM   1218 O  O   B LEU A 1 87  ? 30.21700 52.86700 3.94700   0.440 57.57000  ?  87  LEU A O   1 
ATOM   1219 C  CB  A LEU A 1 87  ? 29.47500 49.40300 3.48100   0.560 46.00000  ?  87  LEU A CB  1 
ATOM   1220 C  CB  B LEU A 1 87  ? 29.17000 49.64100 3.17400   0.440 45.46000  ?  87  LEU A CB  1 
ATOM   1221 C  CG  A LEU A 1 87  ? 29.61000 48.33300 2.40200   0.560 45.51000  ?  87  LEU A CG  1 
ATOM   1222 C  CG  B LEU A 1 87  ? 29.07400 48.62200 2.03400   0.440 44.56000  ?  87  LEU A CG  1 
ATOM   1223 C  CD1 A LEU A 1 87  ? 28.65400 47.18200 2.66200   0.560 49.73000  ?  87  LEU A CD1 1 
ATOM   1224 C  CD1 B LEU A 1 87  ? 27.89000 47.66900 2.22700   0.440 39.85000  ?  87  LEU A CD1 1 
ATOM   1225 C  CD2 A LEU A 1 87  ? 29.35100 48.94600 1.03300   0.560 44.72000  ?  87  LEU A CD2 1 
ATOM   1226 C  CD2 B LEU A 1 87  ? 28.94200 49.33200 0.68700   0.440 43.36000  ?  87  LEU A CD2 1 
ATOM   1227 N  N   A GLY A 1 88  ? 30.65900 51.11800 5.91900   0.560 55.83000  ?  88  GLY A N   1 
ATOM   1228 N  N   B GLY A 1 88  ? 30.06700 51.26400 5.53700   0.440 57.97000  ?  88  GLY A N   1 
ATOM   1229 C  CA  A GLY A 1 88  ? 30.39000 52.04300 7.00300   0.560 58.98000  ?  88  GLY A CA  1 
ATOM   1230 C  CA  B GLY A 1 88  ? 29.94700 52.22800 6.62100   0.440 60.20000  ?  88  GLY A CA  1 
ATOM   1231 C  C   A GLY A 1 88  ? 31.21800 53.30400 6.93000   0.560 61.52000  ?  88  GLY A C   1 
ATOM   1232 C  C   B GLY A 1 88  ? 30.89200 53.40300 6.48800   0.440 59.99000  ?  88  GLY A C   1 
ATOM   1233 O  O   A GLY A 1 88  ? 30.74800 54.37700 7.31900   0.560 63.76000  ?  88  GLY A O   1 
ATOM   1234 O  O   B GLY A 1 88  ? 30.50300 54.53100 6.78600   0.440 61.75000  ?  88  GLY A O   1 
ATOM   1235 N  N   A LEU A 1 89  ? 32.45300 53.19900 6.43900   0.560 56.15000  ?  89  LEU A N   1 
ATOM   1236 N  N   B LEU A 1 89  ? 32.14400 53.15500 6.05000   0.440 55.64000  ?  89  LEU A N   1 
ATOM   1237 C  CA  A LEU A 1 89  ? 33.26100 54.39200 6.22700   0.560 59.97000  ?  89  LEU A CA  1 
ATOM   1238 C  CA  B LEU A 1 89  ? 33.06600 54.24800 5.72600   0.440 60.76000  ?  89  LEU A CA  1 
ATOM   1239 C  C   A LEU A 1 89  ? 32.64300 55.27900 5.15400   0.560 68.29000  ?  89  LEU A C   1 
ATOM   1240 C  C   B LEU A 1 89  ? 32.56400 55.09300 4.57300   0.440 68.60000  ?  89  LEU A C   1 
ATOM   1241 O  O   A LEU A 1 89  ? 32.54300 56.49900 5.32400   0.560 75.51000  ?  89  LEU A O   1 
ATOM   1242 O  O   B LEU A 1 89  ? 32.76100 56.31200 4.56500   0.440 67.49000  ?  89  LEU A O   1 
ATOM   1243 C  CB  A LEU A 1 89  ? 34.68500 53.99900 5.84000   0.560 62.02000  ?  89  LEU A CB  1 
ATOM   1244 C  CB  B LEU A 1 89  ? 34.46200 53.75800 5.35300   0.440 62.50000  ?  89  LEU A CB  1 
ATOM   1245 C  CG  A LEU A 1 89  ? 35.56200 53.36000 6.91700   0.560 73.55000  ?  89  LEU A CG  1 
ATOM   1246 C  CG  B LEU A 1 89  ? 35.54500 53.25400 6.28700   0.440 69.30000  ?  89  LEU A CG  1 
ATOM   1247 C  CD1 A LEU A 1 89  ? 36.88100 52.90100 6.29400   0.560 69.61000  ?  89  LEU A CD1 1 
ATOM   1248 C  CD1 B LEU A 1 89  ? 36.85400 53.03700 5.50400   0.440 60.96000  ?  89  LEU A CD1 1 
ATOM   1249 C  CD2 A LEU A 1 89  ? 35.81200 54.31400 8.06600   0.560 77.99000  ?  89  LEU A CD2 1 
ATOM   1250 C  CD2 B LEU A 1 89  ? 35.74800 54.25400 7.42100   0.440 77.17000  ?  89  LEU A CD2 1 
ATOM   1251 N  N   A LEU A 1 90  ? 32.23200 54.68000 4.03300   0.560 68.17000  ?  90  LEU A N   1 
ATOM   1252 N  N   B LEU A 1 90  ? 31.99500 54.46100 3.54700   0.440 65.36000  ?  90  LEU A N   1 
ATOM   1253 C  CA  A LEU A 1 90  ? 31.59300 55.45500 2.97600   0.560 67.92000  ?  90  LEU A CA  1 
ATOM   1254 C  CA  B LEU A 1 90  ? 31.33300 55.26700 2.53400   0.440 66.16000  ?  90  LEU A CA  1 
ATOM   1255 C  C   A LEU A 1 90  ? 30.37600 56.20000 3.50500   0.560 62.78000  ?  90  LEU A C   1 
ATOM   1256 C  C   B LEU A 1 90  ? 30.03800 55.86100 3.07900   0.440 64.68000  ?  90  LEU A C   1 
ATOM   1257 O  O   A LEU A 1 90  ? 30.16800 57.37600 3.18400   0.560 75.91000  ?  90  LEU A O   1 
ATOM   1258 O  O   B LEU A 1 90  ? 29.56200 56.87600 2.57700   0.440 65.02000  ?  90  LEU A O   1 
ATOM   1259 C  CB  A LEU A 1 90  ? 31.18100 54.54000 1.82700   0.560 62.90000  ?  90  LEU A CB  1 
ATOM   1260 C  CB  B LEU A 1 90  ? 31.05400 54.42000 1.31100   0.440 64.23000  ?  90  LEU A CB  1 
ATOM   1261 C  CG  A LEU A 1 90  ? 32.19100 54.20100 0.73300   0.560 68.70000  ?  90  LEU A CG  1 
ATOM   1262 C  CG  B LEU A 1 90  ? 32.27100 54.23400 0.43500   0.440 68.54000  ?  90  LEU A CG  1 
ATOM   1263 C  CD1 A LEU A 1 90  ? 31.49800 53.32300 -0.31300  0.560 60.84000  ?  90  LEU A CD1 1 
ATOM   1264 C  CD1 B LEU A 1 90  ? 31.85900 53.47000 -0.76600  0.440 62.43000  ?  90  LEU A CD1 1 
ATOM   1265 C  CD2 A LEU A 1 90  ? 32.77400 55.43600 0.09800   0.560 72.18000  ?  90  LEU A CD2 1 
ATOM   1266 C  CD2 B LEU A 1 90  ? 32.83000 55.56800 0.03200   0.440 72.36000  ?  90  LEU A CD2 1 
ATOM   1267 N  N   A ALA A 1 91  ? 29.55400 55.52800 4.31000   0.560 64.62000  ?  91  ALA A N   1 
ATOM   1268 N  N   B ALA A 1 91  ? 29.42800 55.21200 4.07500   0.440 63.96000  ?  91  ALA A N   1 
ATOM   1269 C  CA  A ALA A 1 91  ? 28.33500 56.12700 4.83200   0.560 66.98000  ?  91  ALA A CA  1 
ATOM   1270 C  CA  B ALA A 1 91  ? 28.17400 55.68800 4.63900   0.440 65.14000  ?  91  ALA A CA  1 
ATOM   1271 C  C   A ALA A 1 91  ? 28.59100 57.09000 5.98200   0.560 69.23000  ?  91  ALA A C   1 
ATOM   1272 C  C   B ALA A 1 91  ? 28.40700 56.73000 5.71300   0.440 68.95000  ?  91  ALA A C   1 
ATOM   1273 O  O   A ALA A 1 91  ? 27.69100 57.86200 6.33100   0.560 74.84000  ?  91  ALA A O   1 
ATOM   1274 O  O   B ALA A 1 91  ? 27.62000 57.67700 5.81800   0.440 71.02000  ?  91  ALA A O   1 
ATOM   1275 C  CB  A ALA A 1 91  ? 27.37200 55.02800 5.28900   0.560 64.92000  ?  91  ALA A CB  1 
ATOM   1276 C  CB  B ALA A 1 91  ? 27.36500 54.52300 5.21900   0.440 64.23000  ?  91  ALA A CB  1 
ATOM   1277 N  N   A GLY A 1 92  ? 29.78200 57.06600 6.57400   0.560 72.44000  ?  92  GLY A N   1 
ATOM   1278 N  N   B GLY A 1 92  ? 29.48800 56.57900 6.49000   0.440 71.50000  ?  92  GLY A N   1 
ATOM   1279 C  CA  A GLY A 1 92  ? 30.10000 57.96300 7.66600   0.560 81.87000  ?  92  GLY A CA  1 
ATOM   1280 C  CA  B GLY A 1 92  ? 29.79100 57.47700 7.58500   0.440 80.05000  ?  92  GLY A CA  1 
ATOM   1281 C  C   A GLY A 1 92  ? 29.41300 57.60300 8.96500   0.560 81.11000  ?  92  GLY A C   1 
ATOM   1282 C  C   B GLY A 1 92  ? 29.10800 57.06300 8.87500   0.440 79.60000  ?  92  GLY A C   1 
ATOM   1283 O  O   A GLY A 1 92  ? 28.80900 58.46200 9.61600   0.560 94.96000  ?  92  GLY A O   1 
ATOM   1284 O  O   B GLY A 1 92  ? 28.50200 57.89100 9.56300   0.440 89.13000  ?  92  GLY A O   1 
ATOM   1285 N  N   A LEU A 1 93  ? 29.50100 56.33800 9.36000   0.560 78.91000  ?  93  LEU A N   1 
ATOM   1286 N  N   B LEU A 1 93  ? 29.18200 55.78600 9.22200   0.440 76.02000  ?  93  LEU A N   1 
ATOM   1287 C  CA  A LEU A 1 93  ? 28.88000 55.89300 10.59700  0.560 85.79000  ?  93  LEU A CA  1 
ATOM   1288 C  CA  B LEU A 1 93  ? 28.53800 55.34600 10.44000  0.440 83.69000  ?  93  LEU A CA  1 
ATOM   1289 C  C   A LEU A 1 93  ? 29.70400 56.32600 11.80200  0.560 83.74000  ?  93  LEU A C   1 
ATOM   1290 C  C   B LEU A 1 93  ? 29.30900 55.83600 11.64600  0.440 84.20000  ?  93  LEU A C   1 
ATOM   1291 O  O   A LEU A 1 93  ? 30.93800 56.33900 11.75900  0.560 85.53000  ?  93  LEU A O   1 
ATOM   1292 O  O   B LEU A 1 93  ? 30.54200 55.90300 11.62400  0.440 85.97000  ?  93  LEU A O   1 
ATOM   1293 C  CB  A LEU A 1 93  ? 28.73600 54.37400 10.60400  0.560 77.96000  ?  93  LEU A CB  1 
ATOM   1294 C  CB  B LEU A 1 93  ? 28.43100 53.83300 10.45400  0.440 76.11000  ?  93  LEU A CB  1 
ATOM   1295 C  CG  A LEU A 1 93  ? 27.61900 53.76200 9.76300   0.560 77.69000  ?  93  LEU A CG  1 
ATOM   1296 C  CG  B LEU A 1 93  ? 27.22800 53.51800 9.57400   0.440 77.41000  ?  93  LEU A CG  1 
ATOM   1297 C  CD1 A LEU A 1 93  ? 27.63300 52.24800 9.94800   0.560 68.95000  ?  93  LEU A CD1 1 
ATOM   1298 C  CD1 B LEU A 1 93  ? 26.96100 52.04000 9.59100   0.440 70.34000  ?  93  LEU A CD1 1 
ATOM   1299 C  CD2 A LEU A 1 93  ? 26.27200 54.34400 10.12900  0.560 78.50000  ?  93  LEU A CD2 1 
ATOM   1300 C  CD2 B LEU A 1 93  ? 25.98900 54.33600 10.00100  0.440 77.21000  ?  93  LEU A CD2 1 
ATOM   1301 N  N   A ASP A 1 94  ? 29.01400 56.67900 12.88200  0.560 93.11000  ?  94  ASP A N   1 
ATOM   1302 N  N   B ASP A 1 94  ? 28.58000 56.21500 12.68500  0.440 85.23000  ?  94  ASP A N   1 
ATOM   1303 C  CA  A ASP A 1 94  ? 29.68600 56.87000 14.15600  0.560 96.50000  ?  94  ASP A CA  1 
ATOM   1304 C  CA  B ASP A 1 94  ? 29.24300 56.43300 13.96400  0.440 96.84000  ?  94  ASP A CA  1 
ATOM   1305 C  C   A ASP A 1 94  ? 30.08900 55.51400 14.73100  0.560 89.55000  ?  94  ASP A C   1 
ATOM   1306 C  C   B ASP A 1 94  ? 29.91100 55.13300 14.36800  0.440 88.42000  ?  94  ASP A C   1 
ATOM   1307 O  O   A ASP A 1 94  ? 29.50500 54.47200 14.41100  0.560 87.08000  ?  94  ASP A O   1 
ATOM   1308 O  O   B ASP A 1 94  ? 29.50900 54.06300 13.91900  0.440 85.93000  ?  94  ASP A O   1 
ATOM   1309 C  CB  A ASP A 1 94  ? 28.78600 57.62500 15.13300  0.560 98.47000  ?  94  ASP A CB  1 
ATOM   1310 C  CB  B ASP A 1 94  ? 28.23200 56.87500 15.01600  0.440 97.74000  ?  94  ASP A CB  1 
ATOM   1311 C  CG  A ASP A 1 94  ? 27.55500 56.83800 15.51900  0.560 101.80000 ?  94  ASP A CG  1 
ATOM   1312 C  CG  B ASP A 1 94  ? 26.97600 56.03800 14.96900  0.440 102.44000 ?  94  ASP A CG  1 
ATOM   1313 O  OD1 A ASP A 1 94  ? 26.80700 56.41200 14.61500  0.560 106.95000 ?  94  ASP A OD1 1 
ATOM   1314 O  OD1 B ASP A 1 94  ? 26.40100 55.93800 13.86000  0.440 101.50000 ?  94  ASP A OD1 1 
ATOM   1315 O  OD2 A ASP A 1 94  ? 27.33600 56.64700 16.73200  0.560 110.57000 -1 94  ASP A OD2 1 
ATOM   1316 O  OD2 B ASP A 1 94  ? 26.55900 55.49200 15.99400  0.440 102.16000 -1 94  ASP A OD2 1 
ATOM   1317 N  N   A SER A 1 95  ? 31.10500 55.53800 15.59700  0.560 90.08000  ?  95  SER A N   1 
ATOM   1318 N  N   B SER A 1 95  ? 30.96300 55.21000 15.18100  0.440 88.96000  ?  95  SER A N   1 
ATOM   1319 C  CA  A SER A 1 95  ? 31.67300 54.30100 16.12200  0.560 87.68000  ?  95  SER A CA  1 
ATOM   1320 C  CA  B SER A 1 95  ? 31.54900 53.95100 15.61900  0.440 85.92000  ?  95  SER A CA  1 
ATOM   1321 C  C   A SER A 1 95  ? 30.64000 53.40700 16.79500  0.560 83.20000  ?  95  SER A C   1 
ATOM   1322 C  C   B SER A 1 95  ? 30.52500 53.07300 16.33300  0.440 81.77000  ?  95  SER A C   1 
ATOM   1323 O  O   A SER A 1 95  ? 30.90700 52.21800 17.00100  0.560 78.57000  ?  95  SER A O   1 
ATOM   1324 O  O   B SER A 1 95  ? 30.72400 51.85300 16.41700  0.440 67.61000  ?  95  SER A O   1 
ATOM   1325 C  CB  A SER A 1 95  ? 32.77800 54.62100 17.12800  0.560 91.90000  ?  95  SER A CB  1 
ATOM   1326 C  CB  B SER A 1 95  ? 32.75900 54.20300 16.51500  0.440 89.77000  ?  95  SER A CB  1 
ATOM   1327 O  OG  A SER A 1 95  ? 32.29100 54.54100 18.46100  0.560 106.50000 ?  95  SER A OG  1 
ATOM   1328 O  OG  B SER A 1 95  ? 32.40200 54.10200 17.87500  0.440 98.68000  ?  95  SER A OG  1 
ATOM   1329 N  N   A ARG A 1 96  ? 29.46400 53.93800 17.12700  0.560 86.04000  ?  96  ARG A N   1 
ATOM   1330 N  N   B ARG A 1 96  ? 29.41100 53.65400 16.78600  0.440 84.55000  ?  96  ARG A N   1 
ATOM   1331 C  CA  A ARG A 1 96  ? 28.44300 53.13400 17.78900  0.560 90.79000  ?  96  ARG A CA  1 
ATOM   1332 C  CA  B ARG A 1 96  ? 28.38800 52.88900 17.47900  0.440 87.68000  ?  96  ARG A CA  1 
ATOM   1333 C  C   A ARG A 1 96  ? 27.61400 52.35200 16.77900  0.560 81.06000  ?  96  ARG A C   1 
ATOM   1334 C  C   B ARG A 1 96  ? 27.48600 52.13900 16.51900  0.440 81.49000  ?  96  ARG A C   1 
ATOM   1335 O  O   A ARG A 1 96  ? 27.29500 51.18000 17.00600  0.560 72.92000  ?  96  ARG A O   1 
ATOM   1336 O  O   B ARG A 1 96  ? 27.25600 50.93800 16.70800  0.440 72.52000  ?  96  ARG A O   1 
ATOM   1337 C  CB  A ARG A 1 96  ? 27.54800 54.03700 18.63700  0.560 108.59000 ?  96  ARG A CB  1 
ATOM   1338 C  CB  B ARG A 1 96  ? 27.56000 53.80500 18.37600  0.440 105.66000 ?  96  ARG A CB  1 
ATOM   1339 C  CG  A ARG A 1 96  ? 26.32900 53.35400 19.23100  0.560 111.43000 ?  96  ARG A CG  1 
ATOM   1340 C  CG  B ARG A 1 96  ? 26.36600 53.12600 19.06700  0.440 110.12000 ?  96  ARG A CG  1 
ATOM   1341 C  CD  A ARG A 1 96  ? 25.40300 54.38400 19.88100  0.560 128.58000 ?  96  ARG A CD  1 
ATOM   1342 C  CD  B ARG A 1 96  ? 25.53200 54.10500 19.94300  0.440 127.18000 ?  96  ARG A CD  1 
ATOM   1343 N  NE  A ARG A 1 96  ? 26.13200 55.33800 20.71700  0.560 141.04000 ?  96  ARG A NE  1 
ATOM   1344 N  NE  B ARG A 1 96  ? 26.30500 54.92700 20.88200  0.440 139.08000 ?  96  ARG A NE  1 
ATOM   1345 C  CZ  A ARG A 1 96  ? 26.49300 56.55900 20.33100  0.560 146.78000 ?  96  ARG A CZ  1 
ATOM   1346 C  CZ  B ARG A 1 96  ? 26.55800 56.22600 20.73400  0.440 145.39000 ?  96  ARG A CZ  1 
ATOM   1347 N  NH1 A ARG A 1 96  ? 26.19700 56.99700 19.11400  0.560 149.71000 ?  96  ARG A NH1 1 
ATOM   1348 N  NH1 B ARG A 1 96  ? 26.10700 56.90700 19.69300  0.440 150.12000 ?  96  ARG A NH1 1 
ATOM   1349 N  NH2 A ARG A 1 96  ? 27.15300 57.34700 21.16800  0.560 149.45000 ?  96  ARG A NH2 1 
ATOM   1350 N  NH2 B ARG A 1 96  ? 27.27100 56.86300 21.66100  0.440 149.01000 ?  96  ARG A NH2 1 
ATOM   1351 N  N   A GLU A 1 97  ? 27.24600 52.98900 15.66500  0.560 95.64000  ?  97  GLU A N   1 
ATOM   1352 N  N   B GLU A 1 97  ? 26.95900 52.83800 15.49500  0.440 93.86000  ?  97  GLU A N   1 
ATOM   1353 C  CA  A GLU A 1 97  ? 26.50900 52.28300 14.62200  0.560 79.03000  ?  97  GLU A CA  1 
ATOM   1354 C  CA  B GLU A 1 97  ? 26.15000 52.16200 14.48200  0.440 77.15000  ?  97  GLU A CA  1 
ATOM   1355 C  C   A GLU A 1 97  ? 27.33800 51.14300 14.04400  0.560 69.29000  ?  97  GLU A C   1 
ATOM   1356 C  C   B GLU A 1 97  ? 26.95700 51.09000 13.75500  0.440 68.52000  ?  97  GLU A C   1 
ATOM   1357 O  O   A GLU A 1 97  ? 26.80000 50.07900 13.71000  0.560 64.04000  ?  97  GLU A O   1 
ATOM   1358 O  O   B GLU A 1 97  ? 26.39700 50.06800 13.33600  0.440 65.95000  ?  97  GLU A O   1 
ATOM   1359 C  CB  A GLU A 1 97  ? 26.10100 53.25800 13.51800  0.560 79.89000  ?  97  GLU A CB  1 
ATOM   1360 C  CB  B GLU A 1 97  ? 25.54500 53.16700 13.51600  0.440 79.63000  ?  97  GLU A CB  1 
ATOM   1361 N  N   A PHE A 1 98  ? 28.65200 51.34800 13.91900  0.560 70.80000  ?  98  PHE A N   1 
ATOM   1362 N  N   B PHE A 1 98  ? 28.27800 51.25900 13.67000  0.440 70.41000  ?  98  PHE A N   1 
ATOM   1363 C  CA  A PHE A 1 98  ? 29.54300 50.27100 13.50100  0.560 67.13000  ?  98  PHE A CA  1 
ATOM   1364 C  CA  B PHE A 1 98  ? 29.15500 50.19300 13.19200  0.440 66.72000  ?  98  PHE A CA  1 
ATOM   1365 C  C   A PHE A 1 98  ? 29.32500 49.02600 14.35600  0.560 61.83000  ?  98  PHE A C   1 
ATOM   1366 C  C   B PHE A 1 98  ? 28.94600 48.92300 13.98300  0.440 61.32000  ?  98  PHE A C   1 
ATOM   1367 O  O   A PHE A 1 98  ? 29.25400 47.90300 13.84500  0.560 61.25000  ?  98  PHE A O   1 
ATOM   1368 O  O   B PHE A 1 98  ? 28.60300 47.87300 13.42200  0.440 55.72000  ?  98  PHE A O   1 
ATOM   1369 C  CB  A PHE A 1 98  ? 31.00000 50.73100 13.60800  0.560 73.85000  ?  98  PHE A CB  1 
ATOM   1370 C  CB  B PHE A 1 98  ? 30.61500 50.62100 13.32400  0.440 73.27000  ?  98  PHE A CB  1 
ATOM   1371 C  CG  A PHE A 1 98  ? 31.52200 51.42200 12.37900  0.560 77.64000  ?  98  PHE A CG  1 
ATOM   1372 C  CG  B PHE A 1 98  ? 31.12100 51.40300 12.17100  0.440 77.05000  ?  98  PHE A CG  1 
ATOM   1373 C  CD1 A PHE A 1 98  ? 31.68100 50.73200 11.19000  0.560 72.51000  ?  98  PHE A CD1 1 
ATOM   1374 C  CD1 B PHE A 1 98  ? 31.03000 50.87900 10.88900  0.440 69.95000  ?  98  PHE A CD1 1 
ATOM   1375 C  CD2 A PHE A 1 98  ? 31.86800 52.76300 12.42100  0.560 81.49000  ?  98  PHE A CD2 1 
ATOM   1376 C  CD2 B PHE A 1 98  ? 31.72200 52.64900 12.36900  0.440 81.16000  ?  98  PHE A CD2 1 
ATOM   1377 C  CE1 A PHE A 1 98  ? 32.16600 51.36900 10.06300  0.560 70.09000  ?  98  PHE A CE1 1 
ATOM   1378 C  CE1 B PHE A 1 98  ? 31.50800 51.58500 9.80500   0.440 70.48000  ?  98  PHE A CE1 1 
ATOM   1379 C  CE2 A PHE A 1 98  ? 32.35200 53.40600 11.30000  0.560 74.95000  ?  98  PHE A CE2 1 
ATOM   1380 C  CE2 B PHE A 1 98  ? 32.22000 53.38100 11.29700  0.440 75.01000  ?  98  PHE A CE2 1 
ATOM   1381 C  CZ  A PHE A 1 98  ? 32.50100 52.70700 10.11700  0.560 76.89000  ?  98  PHE A CZ  1 
ATOM   1382 C  CZ  B PHE A 1 98  ? 32.10700 52.85300 10.00600  0.440 77.06000  ?  98  PHE A CZ  1 
ATOM   1383 N  N   A GLY A 1 99  ? 29.22100 49.21300 15.67200  0.560 68.31000  ?  99  GLY A N   1 
ATOM   1384 N  N   B GLY A 1 99  ? 29.14100 49.02400 15.31900  0.440 67.96000  ?  99  GLY A N   1 
ATOM   1385 C  CA  A GLY A 1 99  ? 29.11000 48.06900 16.56400  0.560 50.93000  ?  99  GLY A CA  1 
ATOM   1386 C  CA  B GLY A 1 99  ? 29.16600 47.85300 16.19100  0.440 51.58000  ?  99  GLY A CA  1 
ATOM   1387 C  C   A GLY A 1 99  ? 27.88900 47.21700 16.28100  0.560 54.50000  ?  99  GLY A C   1 
ATOM   1388 C  C   B GLY A 1 99  ? 27.85000 47.09100 16.21900  0.440 54.60000  ?  99  GLY A C   1 
ATOM   1389 O  O   A GLY A 1 99  ? 27.96100 45.98500 16.29600  0.560 53.68000  ?  99  GLY A O   1 
ATOM   1390 O  O   B GLY A 1 99  ? 27.83400 45.89100 16.45100  0.440 54.14000  ?  99  GLY A O   1 
ATOM   1391 N  N   A ILE A 1 100 ? 26.75300 47.86100 16.01600  0.560 54.32000  ?  100 ILE A N   1 
ATOM   1392 N  N   B ILE A 1 100 ? 26.73100 47.77300 16.03600  0.440 54.21000  ?  100 ILE A N   1 
ATOM   1393 C  CA  A ILE A 1 100 ? 25.52600 47.11900 15.74900  0.560 56.85000  ?  100 ILE A CA  1 
ATOM   1394 C  CA  B ILE A 1 100 ? 25.49400 47.11500 15.63900  0.440 57.27000  ?  100 ILE A CA  1 
ATOM   1395 C  C   A ILE A 1 100 ? 25.68900 46.25100 14.50700  0.560 56.06000  ?  100 ILE A C   1 
ATOM   1396 C  C   B ILE A 1 100 ? 25.77400 46.22900 14.42600  0.440 56.00000  ?  100 ILE A C   1 
ATOM   1397 O  O   A ILE A 1 100 ? 25.45900 45.03700 14.54400  0.560 56.42000  ?  100 ILE A O   1 
ATOM   1398 O  O   B ILE A 1 100 ? 25.95300 45.01400 14.58700  0.440 56.04000  ?  100 ILE A O   1 
ATOM   1399 C  CB  A ILE A 1 100 ? 24.33400 48.08300 15.60700  0.560 62.99000  ?  100 ILE A CB  1 
ATOM   1400 C  CB  B ILE A 1 100 ? 24.40200 48.16300 15.35200  0.440 63.33000  ?  100 ILE A CB  1 
ATOM   1401 C  CG1 A ILE A 1 100 ? 24.03600 48.77100 16.94100  0.560 78.24000  ?  100 ILE A CG1 1 
ATOM   1402 C  CG1 B ILE A 1 100 ? 24.17500 48.99400 16.61400  0.440 74.96000  ?  100 ILE A CG1 1 
ATOM   1403 C  CG2 A ILE A 1 100 ? 23.10800 47.33500 15.10100  0.560 60.63000  ?  100 ILE A CG2 1 
ATOM   1404 C  CG2 B ILE A 1 100 ? 23.10200 47.52100 14.92800  0.440 60.58000  ?  100 ILE A CG2 1 
ATOM   1405 C  CD1 A ILE A 1 100 ? 23.79700 50.26600 16.82300  0.560 71.66000  ?  100 ILE A CD1 1 
ATOM   1406 C  CD1 B ILE A 1 100 ? 24.04900 50.45900 16.39200  0.440 68.12000  ?  100 ILE A CD1 1 
ATOM   1407 N  N   A VAL A 1 101 ? 26.08700 46.85600 13.38500  0.560 54.87000  ?  101 VAL A N   1 
ATOM   1408 N  N   B VAL A 1 101 ? 25.87900 46.82600 13.22000  0.440 54.90000  ?  101 VAL A N   1 
ATOM   1409 C  CA  A VAL A 1 101 ? 26.09800 46.10900 12.12900  0.560 54.53000  ?  101 VAL A CA  1 
ATOM   1410 C  CA  B VAL A 1 101 ? 25.81300 46.01800 11.99100  0.440 54.21000  ?  101 VAL A CA  1 
ATOM   1411 C  C   A VAL A 1 101 ? 27.17000 45.02700 12.15600  0.560 45.51000  ?  101 VAL A C   1 
ATOM   1412 C  C   B VAL A 1 101 ? 26.88500 44.95400 11.95500  0.440 47.08000  ?  101 VAL A C   1 
ATOM   1413 O  O   A VAL A 1 101 ? 26.95700 43.91500 11.65900  0.560 50.64000  ?  101 VAL A O   1 
ATOM   1414 O  O   B VAL A 1 101 ? 26.61900 43.84200 11.49200  0.440 49.51000  ?  101 VAL A O   1 
ATOM   1415 C  CB  A VAL A 1 101 ? 26.27700 47.05500 10.92500  0.560 56.53000  ?  101 VAL A CB  1 
ATOM   1416 C  CB  B VAL A 1 101 ? 25.87800 46.84700 10.69100  0.440 55.42000  ?  101 VAL A CB  1 
ATOM   1417 C  CG1 A VAL A 1 101 ? 25.12100 48.04700 10.86000  0.560 57.99000  ?  101 VAL A CG1 1 
ATOM   1418 C  CG1 B VAL A 1 101 ? 24.70600 47.76800 10.61000  0.440 58.76000  ?  101 VAL A CG1 1 
ATOM   1419 C  CG2 A VAL A 1 101 ? 27.61500 47.77100 10.96900  0.560 60.08000  ?  101 VAL A CG2 1 
ATOM   1420 C  CG2 B VAL A 1 101 ? 27.16200 47.61700 10.59600  0.440 57.24000  ?  101 VAL A CG2 1 
ATOM   1421 N  N   A ILE A 1 102 ? 28.33500 45.32300 12.73800  0.560 45.45000  ?  102 ILE A N   1 
ATOM   1422 N  N   B ILE A 1 102 ? 28.09000 45.24600 12.45000  0.440 45.02000  ?  102 ILE A N   1 
ATOM   1423 C  CA  A ILE A 1 102 ? 29.37700 44.30500 12.81000  0.560 52.92000  ?  102 ILE A CA  1 
ATOM   1424 C  CA  B ILE A 1 102 ? 29.10700 44.19800 12.46000  0.440 52.99000  ?  102 ILE A CA  1 
ATOM   1425 C  C   A ILE A 1 102 ? 28.95900 43.18400 13.75400  0.560 53.57000  ?  102 ILE A C   1 
ATOM   1426 C  C   B ILE A 1 102 ? 28.67300 43.04400 13.35900  0.440 52.67000  ?  102 ILE A C   1 
ATOM   1427 O  O   A ILE A 1 102 ? 29.30200 42.01700 13.52900  0.560 48.10000  ?  102 ILE A O   1 
ATOM   1428 O  O   B ILE A 1 102 ? 28.77900 41.87900 12.96100  0.440 44.21000  ?  102 ILE A O   1 
ATOM   1429 C  CB  A ILE A 1 102 ? 30.71900 44.94100 13.22000  0.560 55.68000  ?  102 ILE A CB  1 
ATOM   1430 C  CB  B ILE A 1 102 ? 30.49200 44.75300 12.83400  0.440 56.31000  ?  102 ILE A CB  1 
ATOM   1431 C  CG1 A ILE A 1 102 ? 31.36000 45.62900 12.01000  0.560 59.00000  ?  102 ILE A CG1 1 
ATOM   1432 C  CG1 B ILE A 1 102 ? 31.15700 45.32100 11.56600  0.440 53.41000  ?  102 ILE A CG1 1 
ATOM   1433 C  CG2 A ILE A 1 102 ? 31.66400 43.89300 13.78400  0.560 51.41000  ?  102 ILE A CG2 1 
ATOM   1434 C  CG2 B ILE A 1 102 ? 31.33000 43.68400 13.47200  0.440 52.37000  ?  102 ILE A CG2 1 
ATOM   1435 C  CD1 A ILE A 1 102 ? 32.12300 46.89000 12.32800  0.560 64.34000  ?  102 ILE A CD1 1 
ATOM   1436 C  CD1 B ILE A 1 102 ? 32.12700 46.51800 11.80900  0.440 64.38000  ?  102 ILE A CD1 1 
ATOM   1437 N  N   A THR A 1 103 ? 28.20500 43.50100 14.81100  0.560 50.85000  ?  103 THR A N   1 
ATOM   1438 N  N   B THR A 1 103 ? 28.08200 43.33700 14.53400  0.440 52.71000  ?  103 THR A N   1 
ATOM   1439 C  CA  A THR A 1 103 ? 27.68500 42.44800 15.67900  0.560 49.71000  ?  103 THR A CA  1 
ATOM   1440 C  CA  B THR A 1 103 ? 27.63900 42.24000 15.40600  0.440 50.15000  ?  103 THR A CA  1 
ATOM   1441 C  C   A THR A 1 103 ? 26.68300 41.57700 14.93000  0.560 50.55000  ?  103 THR A C   1 
ATOM   1442 C  C   B THR A 1 103 ? 26.57600 41.36700 14.71000  0.440 49.83000  ?  103 THR A C   1 
ATOM   1443 O  O   A THR A 1 103 ? 26.77000 40.34300 14.96100  0.560 50.24000  ?  103 THR A O   1 
ATOM   1444 O  O   B THR A 1 103 ? 26.60100 40.13200 14.85200  0.440 49.37000  ?  103 THR A O   1 
ATOM   1445 C  CB  A THR A 1 103 ? 27.03900 43.05600 16.92600  0.560 54.18000  ?  103 THR A CB  1 
ATOM   1446 C  CB  B THR A 1 103 ? 27.11300 42.77200 16.75600  0.440 53.77000  ?  103 THR A CB  1 
ATOM   1447 O  OG1 A THR A 1 103 ? 28.04400 43.66900 17.74300  0.560 41.01000  ?  103 THR A OG1 1 
ATOM   1448 O  OG1 B THR A 1 103 ? 27.99800 43.77000 17.29100  0.440 49.51000  ?  103 THR A OG1 1 
ATOM   1449 C  CG2 A THR A 1 103 ? 26.31800 41.98100 17.73600  0.560 50.94000  ?  103 THR A CG2 1 
ATOM   1450 C  CG2 B THR A 1 103 ? 27.06400 41.62400 17.76000  0.440 50.46000  ?  103 THR A CG2 1 
ATOM   1451 N  N   A LEU A 1 104 ? 25.72500 42.20600 14.24000  0.560 43.57000  ?  104 LEU A N   1 
ATOM   1452 N  N   B LEU A 1 104 ? 25.66700 41.98600 13.91200  0.440 44.37000  ?  104 LEU A N   1 
ATOM   1453 C  CA  A LEU A 1 104 ? 24.76400 41.45000 13.44000  0.560 47.00000  ?  104 LEU A CA  1 
ATOM   1454 C  CA  B LEU A 1 104 ? 24.64100 41.22200 13.17600  0.440 47.19000  ?  104 LEU A CA  1 
ATOM   1455 C  C   A LEU A 1 104 ? 25.46700 40.58400 12.40200  0.560 46.78000  ?  104 LEU A C   1 
ATOM   1456 C  C   B LEU A 1 104 ? 25.24200 40.40600 12.02700  0.440 44.42000  ?  104 LEU A C   1 
ATOM   1457 O  O   A LEU A 1 104 ? 25.09500 39.42300 12.19400  0.560 44.32000  ?  104 LEU A O   1 
ATOM   1458 O  O   B LEU A 1 104 ? 24.90000 39.23100 11.85000  0.440 44.72000  ?  104 LEU A O   1 
ATOM   1459 C  CB  A LEU A 1 104 ? 23.78900 42.40200 12.74500  0.560 48.22000  ?  104 LEU A CB  1 
ATOM   1460 C  CB  B LEU A 1 104 ? 23.57600 42.14100 12.60300  0.440 46.52000  ?  104 LEU A CB  1 
ATOM   1461 C  CG  A LEU A 1 104 ? 22.61900 42.97900 13.53800  0.560 47.68000  ?  104 LEU A CG  1 
ATOM   1462 C  CG  B LEU A 1 104 ? 22.40000 42.61700 13.38700  0.440 48.04000  ?  104 LEU A CG  1 
ATOM   1463 C  CD1 A LEU A 1 104 ? 21.79200 43.92400 12.66200  0.560 46.38000  ?  104 LEU A CD1 1 
ATOM   1464 C  CD1 B LEU A 1 104 ? 21.55300 43.43200 12.47000  0.440 44.37000  ?  104 LEU A CD1 1 
ATOM   1465 C  CD2 A LEU A 1 104 ? 21.73700 41.87700 14.09200  0.560 51.16000  ?  104 LEU A CD2 1 
ATOM   1466 C  CD2 B LEU A 1 104 ? 21.65500 41.39100 13.83600  0.440 50.36000  ?  104 LEU A CD2 1 
ATOM   1467 N  N   A ASN A 1 105 ? 26.48200 41.13300 11.73200  0.560 40.11000  ?  105 ASN A N   1 
ATOM   1468 N  N   B ASN A 1 105 ? 26.06800 41.03900 11.19200  0.440 38.69000  ?  105 ASN A N   1 
ATOM   1469 C  CA  A ASN A 1 105 ? 27.20800 40.35400 10.73500  0.560 45.68000  ?  105 ASN A CA  1 
ATOM   1470 C  CA  B ASN A 1 105 ? 26.85500 40.31200 10.20900  0.440 46.22000  ?  105 ASN A CA  1 
ATOM   1471 C  C   A ASN A 1 105 ? 27.84100 39.11700 11.36100  0.560 42.86000  ?  105 ASN A C   1 
ATOM   1472 C  C   B ASN A 1 105 ? 27.53600 39.11200 10.83500  0.440 42.99000  ?  105 ASN A C   1 
ATOM   1473 O  O   A ASN A 1 105 ? 27.75300 38.01300 10.81000  0.560 47.45000  ?  105 ASN A O   1 
ATOM   1474 O  O   B ASN A 1 105 ? 27.60900 38.03600 10.23100  0.440 46.04000  ?  105 ASN A O   1 
ATOM   1475 C  CB  A ASN A 1 105 ? 28.27700 41.21900 10.06500  0.560 52.97000  ?  105 ASN A CB  1 
ATOM   1476 C  CB  B ASN A 1 105 ? 27.90800 41.26000 9.63000   0.440 53.20000  ?  105 ASN A CB  1 
ATOM   1477 C  CG  A ASN A 1 105 ? 28.93000 40.52500 8.88900   0.560 49.22000  ?  105 ASN A CG  1 
ATOM   1478 C  CG  B ASN A 1 105 ? 28.96300 40.54900 8.74300   0.440 49.71000  ?  105 ASN A CG  1 
ATOM   1479 O  OD1 A ASN A 1 105 ? 28.44000 40.59800 7.76200   0.560 49.47000  ?  105 ASN A OD1 1 
ATOM   1480 O  OD1 B ASN A 1 105 ? 28.88000 40.57800 7.52200   0.440 49.86000  ?  105 ASN A OD1 1 
ATOM   1481 N  ND2 A ASN A 1 105 ? 30.04000 39.84000 9.14600   0.560 49.62000  ?  105 ASN A ND2 1 
ATOM   1482 N  ND2 B ASN A 1 105 ? 29.96700 39.92500 9.37700   0.440 49.22000  ?  105 ASN A ND2 1 
ATOM   1483 N  N   A THR A 1 106 ? 28.47700 39.27800 12.52400  0.560 46.63000  ?  106 THR A N   1 
ATOM   1484 N  N   B THR A 1 106 ? 28.05600 39.28800 12.04800  0.440 46.47000  ?  106 THR A N   1 
ATOM   1485 C  CA  A THR A 1 106 ? 29.16800 38.14900 13.14200  0.560 45.21000  ?  106 THR A CA  1 
ATOM   1486 C  CA  B THR A 1 106 ? 28.79700 38.24500 12.74000  0.440 45.13000  ?  106 THR A CA  1 
ATOM   1487 C  C   A THR A 1 106 ? 28.18800 37.04500 13.52700  0.560 41.86000  ?  106 THR A C   1 
ATOM   1488 C  C   B THR A 1 106 ? 27.85300 37.18100 13.27300  0.440 42.31000  ?  106 THR A C   1 
ATOM   1489 O  O   A THR A 1 106 ? 28.51800 35.85400 13.45700  0.560 43.34000  ?  106 THR A O   1 
ATOM   1490 O  O   B THR A 1 106 ? 28.21600 36.01800 13.30500  0.440 41.49000  ?  106 THR A O   1 
ATOM   1491 C  CB  A THR A 1 106 ? 29.95900 38.61700 14.36400  0.560 43.91000  ?  106 THR A CB  1 
ATOM   1492 C  CB  B THR A 1 106 ? 29.64500 38.86700 13.83800  0.440 44.08000  ?  106 THR A CB  1 
ATOM   1493 O  OG1 A THR A 1 106 ? 30.91900 39.60300 13.96400  0.560 50.29000  ?  106 THR A OG1 1 
ATOM   1494 O  OG1 B THR A 1 106 ? 30.41800 39.89000 13.22900  0.440 50.60000  ?  106 THR A OG1 1 
ATOM   1495 C  CG2 A THR A 1 106 ? 30.67800 37.44200 15.01700  0.560 35.97000  ?  106 THR A CG2 1 
ATOM   1496 C  CG2 B THR A 1 106 ? 30.63300 37.85000 14.42500  0.440 40.48000  ?  106 THR A CG2 1 
ATOM   1497 N  N   A VAL A 1 107 ? 26.97200 37.41800 13.93200  0.560 42.48000  ?  107 VAL A N   1 
ATOM   1498 N  N   B VAL A 1 107 ? 26.61700 37.53900 13.65400  0.440 42.88000  ?  107 VAL A N   1 
ATOM   1499 C  CA  A VAL A 1 107 ? 25.97300 36.40900 14.27500  0.560 39.37000  ?  107 VAL A CA  1 
ATOM   1500 C  CA  B VAL A 1 107 ? 25.63400 36.50900 14.03600  0.440 39.95000  ?  107 VAL A CA  1 
ATOM   1501 C  C   A VAL A 1 107 ? 25.63200 35.56700 13.05300  0.560 43.15000  ?  107 VAL A C   1 
ATOM   1502 C  C   B VAL A 1 107 ? 25.22400 35.63400 12.84300  0.440 43.00000  ?  107 VAL A C   1 
ATOM   1503 O  O   A VAL A 1 107 ? 25.48600 34.34200 13.14400  0.560 39.11000  ?  107 VAL A O   1 
ATOM   1504 O  O   B VAL A 1 107 ? 24.92200 34.43700 13.02400  0.440 40.90000  ?  107 VAL A O   1 
ATOM   1505 C  CB  A VAL A 1 107 ? 24.71400 37.07300 14.86800  0.560 40.17000  ?  107 VAL A CB  1 
ATOM   1506 C  CB  B VAL A 1 107 ? 24.38300 37.12800 14.70600  0.440 38.89000  ?  107 VAL A CB  1 
ATOM   1507 C  CG1 A VAL A 1 107 ? 23.63200 36.02700 15.11300  0.560 37.64000  ?  107 VAL A CG1 1 
ATOM   1508 C  CG1 B VAL A 1 107 ? 23.29500 36.02200 15.06400  0.440 36.95000  ?  107 VAL A CG1 1 
ATOM   1509 C  CG2 A VAL A 1 107 ? 25.04900 37.82000 16.14000  0.560 41.29000  ?  107 VAL A CG2 1 
ATOM   1510 C  CG2 B VAL A 1 107 ? 24.78200 37.90200 15.99600  0.440 42.09000  ?  107 VAL A CG2 1 
ATOM   1511 N  N   A VAL A 1 108 ? 25.48700 36.21100 11.89300  0.560 44.34000  ?  108 VAL A N   1 
ATOM   1512 N  N   B VAL A 1 108 ? 25.21400 36.19900 11.61200  0.440 43.50000  ?  108 VAL A N   1 
ATOM   1513 C  CA  A VAL A 1 108 ? 25.21100 35.47600 10.66100  0.560 35.81000  ?  108 VAL A CA  1 
ATOM   1514 C  CA  B VAL A 1 108 ? 24.76400 35.43600 10.44400  0.440 34.72000  ?  108 VAL A CA  1 
ATOM   1515 C  C   A VAL A 1 108 ? 26.32100 34.47300 10.39200  0.560 37.17000  ?  108 VAL A C   1 
ATOM   1516 C  C   B VAL A 1 108 ? 25.80000 34.37200 10.07900  0.440 38.20000  ?  108 VAL A C   1 
ATOM   1517 O  O   A VAL A 1 108 ? 26.07500 33.28000 10.16300  0.560 40.50000  ?  108 VAL A O   1 
ATOM   1518 O  O   B VAL A 1 108 ? 25.47500 33.19800 9.83000   0.440 41.28000  ?  108 VAL A O   1 
ATOM   1519 C  CB  A VAL A 1 108 ? 25.05800 36.45300 9.48100   0.560 39.91000  ?  108 VAL A CB  1 
ATOM   1520 C  CB  B VAL A 1 108 ? 24.47400 36.36300 9.26200   0.440 40.07000  ?  108 VAL A CB  1 
ATOM   1521 C  CG1 A VAL A 1 108 ? 24.88000 35.68200 8.18200   0.560 33.21000  ?  108 VAL A CG1 1 
ATOM   1522 C  CG1 B VAL A 1 108 ? 24.06700 35.46400 8.07400   0.440 36.18000  ?  108 VAL A CG1 1 
ATOM   1523 C  CG2 A VAL A 1 108 ? 23.90900 37.41600 9.71600   0.560 32.67000  ?  108 VAL A CG2 1 
ATOM   1524 C  CG2 B VAL A 1 108 ? 23.42000 37.41700 9.62600   0.440 32.46000  ?  108 VAL A CG2 1 
ATOM   1525 N  N   A MET A 1 109 ? 27.56600 34.95100 10.41800  0.560 37.02000  ?  109 MET A N   1 
ATOM   1526 N  N   B MET A 1 109 ? 27.07300 34.76900 10.02700  0.440 36.98000  ?  109 MET A N   1 
ATOM   1527 C  CA  A MET A 1 109 ? 28.71100 34.12200 10.06300  0.560 38.60000  ?  109 MET A CA  1 
ATOM   1528 C  CA  B MET A 1 109 ? 28.12600 33.83200 9.60800   0.440 39.38000  ?  109 MET A CA  1 
ATOM   1529 C  C   A MET A 1 109 ? 28.90900 32.97700 11.05000  0.560 43.77000  ?  109 MET A C   1 
ATOM   1530 C  C   B MET A 1 109 ? 28.29900 32.73900 10.62900  0.440 45.63000  ?  109 MET A C   1 
ATOM   1531 O  O   A MET A 1 109 ? 29.12500 31.83300 10.64500  0.560 46.15000  ?  109 MET A O   1 
ATOM   1532 O  O   B MET A 1 109 ? 28.21000 31.54300 10.30700  0.440 46.48000  ?  109 MET A O   1 
ATOM   1533 C  CB  A MET A 1 109 ? 29.96200 34.99200 10.02200  0.560 34.32000  ?  109 MET A CB  1 
ATOM   1534 C  CB  B MET A 1 109 ? 29.46100 34.53700 9.45700   0.440 32.54000  ?  109 MET A CB  1 
ATOM   1535 C  CG  A MET A 1 109 ? 29.95100 36.01300 8.90500   0.560 46.85000  ?  109 MET A CG  1 
ATOM   1536 C  CG  B MET A 1 109 ? 29.30200 35.75800 8.58800   0.440 44.36000  ?  109 MET A CG  1 
ATOM   1537 S  SD  A MET A 1 109 ? 29.72500 35.17500 7.32300   0.560 61.34000  ?  109 MET A SD  1 
ATOM   1538 S  SD  B MET A 1 109 ? 28.46000 35.36800 7.00500   0.440 28.65000  ?  109 MET A SD  1 
ATOM   1539 C  CE  A MET A 1 109 ? 28.38000 36.06300 6.56500   0.560 39.06000  ?  109 MET A CE  1 
ATOM   1540 C  CE  B MET A 1 109 ? 27.51600 36.88400 6.92100   0.440 38.60000  ?  109 MET A CE  1 
ATOM   1541 N  N   A LEU A 1 110 ? 28.81900 33.25700 12.34900  0.560 38.58000  ?  110 LEU A N   1 
ATOM   1542 N  N   B LEU A 1 110 ? 28.54600 33.17200 11.88400  0.440 40.83000  ?  110 LEU A N   1 
ATOM   1543 C  CA  A LEU A 1 110 ? 28.99800 32.20600 13.34400  0.560 45.60000  ?  110 LEU A CA  1 
ATOM   1544 C  CA  B LEU A 1 110 ? 28.54700 32.34000 13.08200  0.440 46.95000  ?  110 LEU A CA  1 
ATOM   1545 C  C   A LEU A 1 110 ? 27.89400 31.16200 13.24700  0.560 43.92000  ?  110 LEU A C   1 
ATOM   1546 C  C   B LEU A 1 110 ? 27.44000 31.29100 13.05000  0.440 44.70000  ?  110 LEU A C   1 
ATOM   1547 O  O   A LEU A 1 110 ? 28.16200 29.95900 13.32900  0.560 39.72000  ?  110 LEU A O   1 
ATOM   1548 O  O   B LEU A 1 110 ? 27.71700 30.08200 13.06200  0.440 41.30000  ?  110 LEU A O   1 
ATOM   1549 C  CB  A LEU A 1 110 ? 29.03500 32.83000 14.73700  0.560 46.44000  ?  110 LEU A CB  1 
ATOM   1550 C  CB  B LEU A 1 110 ? 28.44100 33.27700 14.27900  0.440 40.43000  ?  110 LEU A CB  1 
ATOM   1551 C  CG  A LEU A 1 110 ? 30.29500 33.64000 15.05000  0.560 48.35000  ?  110 LEU A CG  1 
ATOM   1552 C  CG  B LEU A 1 110 ? 29.83100 33.87000 14.33600  0.440 42.51000  ?  110 LEU A CG  1 
ATOM   1553 C  CD1 A LEU A 1 110 ? 30.26100 34.13300 16.48900  0.560 42.78000  ?  110 LEU A CD1 1 
ATOM   1554 C  CD1 B LEU A 1 110 ? 29.92800 34.79400 15.54200  0.440 39.25000  ?  110 LEU A CD1 1 
ATOM   1555 C  CD2 A LEU A 1 110 ? 31.55900 32.83600 14.79200  0.560 52.69000  ?  110 LEU A CD2 1 
ATOM   1556 C  CD2 B LEU A 1 110 ? 30.75900 32.66300 14.45800  0.440 45.59000  ?  110 LEU A CD2 1 
ATOM   1557 N  N   A ALA A 1 111 ? 26.64500 31.60200 13.06700  0.560 43.63000  ?  111 ALA A N   1 
ATOM   1558 N  N   B ALA A 1 111 ? 26.18200 31.74800 12.96000  0.440 41.10000  ?  111 ALA A N   1 
ATOM   1559 C  CA  A ALA A 1 111 ? 25.54500 30.65000 12.95300  0.560 42.35000  ?  111 ALA A CA  1 
ATOM   1560 C  CA  B ALA A 1 111 ? 25.05200 30.83500 12.84600  0.440 40.78000  ?  111 ALA A CA  1 
ATOM   1561 C  C   A ALA A 1 111 ? 25.74000 29.72700 11.75800  0.560 41.56000  ?  111 ALA A C   1 
ATOM   1562 C  C   B ALA A 1 111 ? 25.19800 29.90300 11.65300  0.440 41.21000  ?  111 ALA A C   1 
ATOM   1563 O  O   A ALA A 1 111 ? 25.49200 28.51900 11.85300  0.560 46.93000  ?  111 ALA A O   1 
ATOM   1564 O  O   B ALA A 1 111 ? 25.06300 28.68400 11.79100  0.440 45.22000  ?  111 ALA A O   1 
ATOM   1565 C  CB  A ALA A 1 111 ? 24.21200 31.38800 12.84200  0.560 36.36000  ?  111 ALA A CB  1 
ATOM   1566 C  CB  B ALA A 1 111 ? 23.75500 31.63100 12.74700  0.440 36.76000  ?  111 ALA A CB  1 
ATOM   1567 N  N   A GLY A 1 112 ? 26.17000 30.27400 10.62200  0.560 46.39000  ?  112 GLY A N   1 
ATOM   1568 N  N   B GLY A 1 112 ? 25.45100 30.44900 10.46700  0.440 46.00000  ?  112 GLY A N   1 
ATOM   1569 C  CA  A GLY A 1 112 ? 26.43200 29.42800 9.47000   0.560 42.11000  ?  112 GLY A CA  1 
ATOM   1570 C  CA  B GLY A 1 112 ? 25.57800 29.58500 9.30100   0.440 41.43000  ?  112 GLY A CA  1 
ATOM   1571 C  C   A GLY A 1 112 ? 27.54500 28.43400 9.73200   0.560 42.35000  ?  112 GLY A C   1 
ATOM   1572 C  C   B GLY A 1 112 ? 26.66000 28.54900 9.48800   0.440 41.51000  ?  112 GLY A C   1 
ATOM   1573 O  O   A GLY A 1 112 ? 27.43200 27.25300 9.39300   0.560 41.03000  ?  112 GLY A O   1 
ATOM   1574 O  O   B GLY A 1 112 ? 26.47000 27.37700 9.16800   0.440 42.64000  ?  112 GLY A O   1 
ATOM   1575 N  N   A PHE A 1 113 ? 28.63200 28.89900 10.34900  0.560 38.40000  ?  113 PHE A N   1 
ATOM   1576 N  N   B PHE A 1 113 ? 27.81600 28.96700 10.00800  0.440 41.00000  ?  113 PHE A N   1 
ATOM   1577 C  CA  A PHE A 1 113 ? 29.75000 28.02000 10.66800  0.560 49.10000  ?  113 PHE A CA  1 
ATOM   1578 C  CA  B PHE A 1 113 ? 28.92000 28.02800 10.13200  0.440 46.53000  ?  113 PHE A CA  1 
ATOM   1579 C  C   A PHE A 1 113 ? 29.32100 26.90200 11.60400  0.560 49.51000  ?  113 PHE A C   1 
ATOM   1580 C  C   B PHE A 1 113 ? 28.55500 26.88700 11.07300  0.440 50.65000  ?  113 PHE A C   1 
ATOM   1581 O  O   A PHE A 1 113 ? 29.70000 25.74200 11.41000  0.560 54.33000  ?  113 PHE A O   1 
ATOM   1582 O  O   B PHE A 1 113 ? 28.91200 25.72500 10.82600  0.440 53.79000  ?  113 PHE A O   1 
ATOM   1583 C  CB  A PHE A 1 113 ? 30.87600 28.84400 11.29000  0.560 51.79000  ?  113 PHE A CB  1 
ATOM   1584 C  CB  B PHE A 1 113 ? 30.16600 28.77200 10.60500  0.440 47.87000  ?  113 PHE A CB  1 
ATOM   1585 C  CG  A PHE A 1 113 ? 32.18000 28.10900 11.42700  0.560 57.44000  ?  113 PHE A CG  1 
ATOM   1586 C  CG  B PHE A 1 113 ? 31.40800 27.92600 10.68000  0.440 54.75000  ?  113 PHE A CG  1 
ATOM   1587 C  CD1 A PHE A 1 113 ? 32.41900 26.93700 10.73000  0.560 57.77000  ?  113 PHE A CD1 1 
ATOM   1588 C  CD1 B PHE A 1 113 ? 31.56200 26.77600 9.89800   0.440 52.34000  ?  113 PHE A CD1 1 
ATOM   1589 C  CD2 A PHE A 1 113 ? 33.17600 28.60400 12.25400  0.560 54.06000  ?  113 PHE A CD2 1 
ATOM   1590 C  CD2 B PHE A 1 113 ? 32.43700 28.31100 11.52800  0.440 57.45000  ?  113 PHE A CD2 1 
ATOM   1591 C  CE1 A PHE A 1 113 ? 33.62400 26.27000 10.85900  0.560 60.07000  ?  113 PHE A CE1 1 
ATOM   1592 C  CE1 B PHE A 1 113 ? 32.68800 26.04900 9.96500   0.440 52.87000  ?  113 PHE A CE1 1 
ATOM   1593 C  CE2 A PHE A 1 113 ? 34.37900 27.94400 12.38600  0.560 65.41000  ?  113 PHE A CE2 1 
ATOM   1594 C  CE2 B PHE A 1 113 ? 33.57900 27.58200 11.59700  0.440 61.40000  ?  113 PHE A CE2 1 
ATOM   1595 C  CZ  A PHE A 1 113 ? 34.60400 26.77500 11.68900  0.560 69.05000  ?  113 PHE A CZ  1 
ATOM   1596 C  CZ  B PHE A 1 113 ? 33.70900 26.44900 10.80800  0.440 59.86000  ?  113 PHE A CZ  1 
ATOM   1597 N  N   A ALA A 1 114 ? 28.52300 27.23000 12.62300  0.560 44.31000  ?  114 ALA A N   1 
ATOM   1598 N  N   B ALA A 1 114 ? 27.79300 27.20200 12.13200  0.440 46.11000  ?  114 ALA A N   1 
ATOM   1599 C  CA  A ALA A 1 114 ? 28.08800 26.21600 13.57600  0.560 45.11000  ?  114 ALA A CA  1 
ATOM   1600 C  CA  B ALA A 1 114 ? 27.47900 26.22700 13.16900  0.440 47.17000  ?  114 ALA A CA  1 
ATOM   1601 C  C   A ALA A 1 114 ? 27.10800 25.24300 12.93600  0.560 46.21000  ?  114 ALA A C   1 
ATOM   1602 C  C   B ALA A 1 114 ? 26.39400 25.25200 12.72800  0.440 50.12000  ?  114 ALA A C   1 
ATOM   1603 O  O   A ALA A 1 114 ? 27.20400 24.02800 13.14800  0.560 50.19000  ?  114 ALA A O   1 
ATOM   1604 O  O   B ALA A 1 114 ? 26.42800 24.08300 13.09100  0.440 53.05000  ?  114 ALA A O   1 
ATOM   1605 C  CB  A ALA A 1 114 ? 27.46100 26.88500 14.79700  0.560 42.63000  ?  114 ALA A CB  1 
ATOM   1606 C  CB  B ALA A 1 114 ? 27.06600 26.97100 14.44100  0.440 43.55000  ?  114 ALA A CB  1 
ATOM   1607 N  N   A GLY A 1 115 ? 26.16400 25.75600 12.14300  0.560 46.57000  ?  115 GLY A N   1 
ATOM   1608 N  N   B GLY A 1 115 ? 25.42400 25.69300 11.94300  0.440 47.63000  ?  115 GLY A N   1 
ATOM   1609 C  CA  A GLY A 1 115 ? 25.21300 24.87900 11.48200  0.560 50.00000  ?  115 GLY A CA  1 
ATOM   1610 C  CA  B GLY A 1 115 ? 24.46200 24.73800 11.44200  0.440 48.18000  ?  115 GLY A CA  1 
ATOM   1611 C  C   A GLY A 1 115 ? 25.88500 23.90800 10.53300  0.560 57.46000  ?  115 GLY A C   1 
ATOM   1612 C  C   B GLY A 1 115 ? 25.10100 23.76100 10.48200  0.440 56.37000  ?  115 GLY A C   1 
ATOM   1613 O  O   A GLY A 1 115 ? 25.50800 22.73700 10.45600  0.560 59.76000  ?  115 GLY A O   1 
ATOM   1614 O  O   B GLY A 1 115 ? 24.79400 22.56900 10.51400  0.440 52.14000  ?  115 GLY A O   1 
ATOM   1615 N  N   A ALA A 1 116 ? 26.88800 24.38100 9.79400   0.560 49.84000  ?  116 ALA A N   1 
ATOM   1616 N  N   B ALA A 1 116 ? 26.02300 24.24800 9.63800   0.440 53.48000  ?  116 ALA A N   1 
ATOM   1617 C  CA  A ALA A 1 116 ? 27.61700 23.49200 8.89900   0.560 58.89000  ?  116 ALA A CA  1 
ATOM   1618 C  CA  B ALA A 1 116 ? 26.70900 23.37200 8.68600   0.440 55.33000  ?  116 ALA A CA  1 
ATOM   1619 C  C   A ALA A 1 116 ? 28.31200 22.37200 9.66300   0.560 62.87000  ?  116 ALA A C   1 
ATOM   1620 C  C   B ALA A 1 116 ? 27.56100 22.32200 9.40900   0.440 61.43000  ?  116 ALA A C   1 
ATOM   1621 O  O   A ALA A 1 116 ? 28.43600 21.25500 9.14900   0.560 63.57000  ?  116 ALA A O   1 
ATOM   1622 O  O   B ALA A 1 116 ? 27.52100 21.14000 9.05700   0.440 65.55000  ?  116 ALA A O   1 
ATOM   1623 C  CB  A ALA A 1 116 ? 28.64100 24.28800 8.08800   0.560 47.28000  ?  116 ALA A CB  1 
ATOM   1624 C  CB  B ALA A 1 116 ? 27.55100 24.21600 7.71900   0.440 49.50000  ?  116 ALA A CB  1 
ATOM   1625 N  N   A MET A 1 117 ? 28.76200 22.64200 10.88800  0.560 61.87000  ?  117 MET A N   1 
ATOM   1626 N  N   B MET A 1 117 ? 28.32300 22.73000 10.44400  0.440 61.14000  ?  117 MET A N   1 
ATOM   1627 C  CA  A MET A 1 117 ? 29.54600 21.68000 11.65200  0.560 61.38000  ?  117 MET A CA  1 
ATOM   1628 C  CA  B MET A 1 117 ? 29.04400 21.76500 11.28000  0.440 61.72000  ?  117 MET A CA  1 
ATOM   1629 C  C   A MET A 1 117 ? 28.69700 20.75400 12.51600  0.560 62.07000  ?  117 MET A C   1 
ATOM   1630 C  C   B MET A 1 117 ? 28.08400 20.83400 12.01800  0.440 65.60000  ?  117 MET A C   1 
ATOM   1631 O  O   A MET A 1 117 ? 29.25600 19.88800 13.19700  0.560 70.93000  ?  117 MET A O   1 
ATOM   1632 O  O   B MET A 1 117 ? 28.52100 19.81400 12.55900  0.440 63.53000  ?  117 MET A O   1 
ATOM   1633 C  CB  A MET A 1 117 ? 30.55300 22.41500 12.54600  0.560 60.48000  ?  117 MET A CB  1 
ATOM   1634 C  CB  B MET A 1 117 ? 29.90500 22.44900 12.35300  0.440 62.18000  ?  117 MET A CB  1 
ATOM   1635 C  CG  A MET A 1 117 ? 31.67800 23.10700 11.79600  0.560 65.72000  ?  117 MET A CG  1 
ATOM   1636 C  CG  B MET A 1 117 ? 31.04500 23.34400 11.91600  0.440 61.70000  ?  117 MET A CG  1 
ATOM   1637 S  SD  A MET A 1 117 ? 32.83500 21.94400 11.05100  0.560 77.63000  ?  117 MET A SD  1 
ATOM   1638 S  SD  B MET A 1 117 ? 32.38800 22.46000 11.15000  0.440 73.85000  ?  117 MET A SD  1 
ATOM   1639 C  CE  A MET A 1 117 ? 33.63400 21.27000 12.51100  0.560 74.67000  ?  117 MET A CE  1 
ATOM   1640 C  CE  B MET A 1 117 ? 33.02200 21.50800 12.53300  0.440 74.02000  ?  117 MET A CE  1 
ATOM   1641 N  N   A VAL A 1 118 ? 27.38100 20.90700 12.50700  0.560 69.20000  ?  118 VAL A N   1 
ATOM   1642 N  N   B VAL A 1 118 ? 26.79300 21.16800 12.06700  0.440 67.21000  ?  118 VAL A N   1 
ATOM   1643 C  CA  A VAL A 1 118 ? 26.47900 20.10400 13.33200  0.560 72.85000  ?  118 VAL A CA  1 
ATOM   1644 C  CA  B VAL A 1 118 ? 25.80500 20.38600 12.81100  0.440 73.54000  ?  118 VAL A CA  1 
ATOM   1645 C  C   A VAL A 1 118 ? 25.81700 19.06200 12.44400  0.560 71.19000  ?  118 VAL A C   1 
ATOM   1646 C  C   B VAL A 1 118 ? 25.18300 19.35900 11.87500  0.440 69.62000  ?  118 VAL A C   1 
ATOM   1647 O  O   A VAL A 1 118 ? 25.21000 19.42800 11.42600  0.560 66.21000  ?  118 VAL A O   1 
ATOM   1648 O  O   B VAL A 1 118 ? 24.52300 19.70800 10.88400  0.440 65.83000  ?  118 VAL A O   1 
ATOM   1649 C  CB  A VAL A 1 118 ? 25.41800 20.98200 14.02300  0.560 64.30000  ?  118 VAL A CB  1 
ATOM   1650 C  CB  B VAL A 1 118 ? 24.70700 21.26000 13.45100  0.440 62.67000  ?  118 VAL A CB  1 
ATOM   1651 C  CG1 A VAL A 1 118 ? 24.24900 20.13100 14.49200  0.560 68.93000  ?  118 VAL A CG1 1 
ATOM   1652 C  CG1 B VAL A 1 118 ? 23.45800 20.45000 13.62400  0.440 69.77000  ?  118 VAL A CG1 1 
ATOM   1653 C  CG2 A VAL A 1 118 ? 26.03700 21.75100 15.18200  0.560 67.18000  ?  118 VAL A CG2 1 
ATOM   1654 C  CG2 B VAL A 1 118 ? 25.14100 21.76700 14.78700  0.440 61.69000  ?  118 VAL A CG2 1 
ATOM   1655 N  N   A PRO A 1 119 ? 25.87800 17.76800 12.79300  0.560 78.82000  ?  119 PRO A N   1 
ATOM   1656 N  N   B PRO A 1 119 ? 25.27600 18.08400 12.23000  0.440 73.96000  ?  119 PRO A N   1 
ATOM   1657 C  CA  A PRO A 1 119 ? 25.33800 16.74200 11.88800  0.560 79.90000  ?  119 PRO A CA  1 
ATOM   1658 C  CA  B PRO A 1 119 ? 24.82700 17.03900 11.30300  0.440 74.92000  ?  119 PRO A CA  1 
ATOM   1659 C  C   A PRO A 1 119 ? 23.81800 16.65600 11.88400  0.560 74.44000  ?  119 PRO A C   1 
ATOM   1660 C  C   B PRO A 1 119 ? 23.32600 16.99500 11.11300  0.440 75.81000  ?  119 PRO A C   1 
ATOM   1661 O  O   A PRO A 1 119 ? 23.21700 16.35600 10.84800  0.560 72.66000  ?  119 PRO A O   1 
ATOM   1662 O  O   B PRO A 1 119 ? 22.84100 16.88400 9.97900   0.440 74.43000  ?  119 PRO A O   1 
ATOM   1663 C  CB  A PRO A 1 119 ? 25.96100 15.43400 12.40300  0.560 81.22000  ?  119 PRO A CB  1 
ATOM   1664 C  CB  B PRO A 1 119 ? 25.33700 15.75200 11.96600  0.440 83.29000  ?  119 PRO A CB  1 
ATOM   1665 C  CG  A PRO A 1 119 ? 26.64800 15.75800 13.70300  0.560 77.76000  ?  119 PRO A CG  1 
ATOM   1666 C  CG  B PRO A 1 119 ? 25.77300 16.12900 13.39200  0.440 79.19000  ?  119 PRO A CG  1 
ATOM   1667 C  CD  A PRO A 1 119 ? 26.41900 17.20000 14.04200  0.560 80.21000  ?  119 PRO A CD  1 
ATOM   1668 C  CD  B PRO A 1 119 ? 25.48900 17.58800 13.60000  0.440 77.87000  ?  119 PRO A CD  1 
ATOM   1669 N  N   A GLY A 1 120 ? 23.18500 16.90700 13.02900  0.560 78.67000  ?  120 GLY A N   1 
ATOM   1670 N  N   B GLY A 1 120 ? 22.57100 17.04500 12.19700  0.440 82.34000  ?  120 GLY A N   1 
ATOM   1671 C  CA  A GLY A 1 120 ? 21.75200 16.74600 13.15500  0.560 88.02000  ?  120 GLY A CA  1 
ATOM   1672 C  CA  B GLY A 1 120 ? 21.15100 16.82200 12.11000  0.440 89.38000  ?  120 GLY A CA  1 
ATOM   1673 C  C   A GLY A 1 120 ? 20.96100 17.91500 12.60200  0.560 92.97000  ?  120 GLY A C   1 
ATOM   1674 C  C   B GLY A 1 120 ? 20.33700 18.03600 11.70200  0.440 88.08000  ?  120 GLY A C   1 
ATOM   1675 O  O   A GLY A 1 120 ? 21.50000 18.91300 12.12300  0.560 89.64000  ?  120 GLY A O   1 
ATOM   1676 O  O   B GLY A 1 120 ? 20.81800 19.16300 11.57100  0.440 85.76000  ?  120 GLY A O   1 
ATOM   1677 N  N   A ILE A 1 121 ? 19.63400 17.78300 12.70000  0.560 97.84000  ?  121 ILE A N   1 
ATOM   1678 N  N   B ILE A 1 121 ? 19.04500 17.76800 11.52400  0.440 86.11000  ?  121 ILE A N   1 
ATOM   1679 C  CA  A ILE A 1 121 ? 18.73100 18.82400 12.22700  0.560 89.44000  ?  121 ILE A CA  1 
ATOM   1680 C  CA  B ILE A 1 121 ? 18.06900 18.77300 11.15900  0.440 83.97000  ?  121 ILE A CA  1 
ATOM   1681 C  C   A ILE A 1 121 ? 18.82600 20.09900 13.04100  0.560 79.80000  ?  121 ILE A C   1 
ATOM   1682 C  C   B ILE A 1 121 ? 18.10000 20.01300 12.06100  0.440 80.83000  ?  121 ILE A C   1 
ATOM   1683 O  O   A ILE A 1 121 ? 18.32000 21.14100 12.60500  0.560 72.31000  ?  121 ILE A O   1 
ATOM   1684 O  O   B ILE A 1 121 ? 17.65400 21.08400 11.63600  0.440 78.91000  ?  121 ILE A O   1 
ATOM   1685 C  CB  A ILE A 1 121 ? 17.27800 18.33300 12.25900  0.560 95.42000  ?  121 ILE A CB  1 
ATOM   1686 C  CB  B ILE A 1 121 ? 16.67900 18.12400 11.17800  0.440 95.54000  ?  121 ILE A CB  1 
ATOM   1687 C  CG1 A ILE A 1 121 ? 16.35700 19.25200 11.47300  0.560 97.14000  ?  121 ILE A CG1 1 
ATOM   1688 C  CG1 B ILE A 1 121 ? 15.77100 18.79200 10.16000  0.440 96.80000  ?  121 ILE A CG1 1 
ATOM   1689 C  CG2 A ILE A 1 121 ? 16.76400 18.34900 13.69700  0.560 95.93000  ?  121 ILE A CG2 1 
ATOM   1690 C  CG2 B ILE A 1 121 ? 16.06600 18.28900 12.55200  0.440 95.59000  ?  121 ILE A CG2 1 
ATOM   1691 C  CD1 A ILE A 1 121 ? 15.32800 18.51600 10.64500  0.560 102.69000 ?  121 ILE A CD1 1 
ATOM   1692 C  CD1 B ILE A 1 121 ? 14.93600 17.82300 9.40200   0.440 102.80000 ?  121 ILE A CD1 1 
ATOM   1693 N  N   A GLU A 1 122 ? 19.41800 20.05000 14.24000  0.560 86.25000  ?  122 GLU A N   1 
ATOM   1694 N  N   B GLU A 1 122 ? 18.60500 19.91100 13.29900  0.440 77.89000  ?  122 GLU A N   1 
ATOM   1695 C  CA  A GLU A 1 122 ? 19.62400 21.30300 14.95800  0.560 83.89000  ?  122 GLU A CA  1 
ATOM   1696 C  CA  B GLU A 1 122 ? 18.72100 21.12600 14.10500  0.440 81.49000  ?  122 GLU A CA  1 
ATOM   1697 C  C   A GLU A 1 122 ? 20.32600 22.32200 14.06600  0.560 69.95000  ?  122 GLU A C   1 
ATOM   1698 C  C   B GLU A 1 122 ? 19.40300 22.23800 13.32700  0.440 67.67000  ?  122 GLU A C   1 
ATOM   1699 O  O   A GLU A 1 122 ? 20.24700 23.53000 14.31900  0.560 65.33000  ?  122 GLU A O   1 
ATOM   1700 O  O   B GLU A 1 122 ? 19.10800 23.41400 13.54400  0.440 61.33000  ?  122 GLU A O   1 
ATOM   1701 C  CB  A GLU A 1 122 ? 20.46500 21.13400 16.23000  0.560 76.09000  ?  122 GLU A CB  1 
ATOM   1702 C  CB  B GLU A 1 122 ? 19.51500 20.91300 15.40800  0.440 81.42000  ?  122 GLU A CB  1 
ATOM   1703 C  CG  A GLU A 1 122 ? 20.20400 19.89900 17.03600  0.560 81.52000  ?  122 GLU A CG  1 
ATOM   1704 C  CG  B GLU A 1 122 ? 19.39100 19.58000 16.11500  0.440 82.89000  ?  122 GLU A CG  1 
ATOM   1705 C  CD  A GLU A 1 122 ? 21.21100 18.81500 16.72000  0.560 90.23000  ?  122 GLU A CD  1 
ATOM   1706 C  CD  B GLU A 1 122 ? 20.64700 18.71300 16.05800  0.440 90.56000  ?  122 GLU A CD  1 
ATOM   1707 O  OE1 A GLU A 1 122 ? 22.42300 19.12800 16.60500  0.560 98.70000  ?  122 GLU A OE1 1 
ATOM   1708 O  OE1 B GLU A 1 122 ? 21.78100 19.26800 16.09900  0.440 98.54000  ?  122 GLU A OE1 1 
ATOM   1709 O  OE2 A GLU A 1 122 ? 20.78700 17.64700 16.59100  0.560 87.51000  -1 122 GLU A OE2 1 
ATOM   1710 O  OE2 B GLU A 1 122 ? 20.49000 17.47200 15.95900  0.440 88.34000  -1 122 GLU A OE2 1 
ATOM   1711 N  N   A ARG A 1 123 ? 21.04500 21.85100 13.04000  0.560 64.44000  ?  123 ARG A N   1 
ATOM   1712 N  N   B ARG A 1 123 ? 20.29500 21.87900 12.39900  0.440 63.11000  ?  123 ARG A N   1 
ATOM   1713 C  CA  A ARG A 1 123 ? 21.76700 22.75700 12.15500  0.560 55.78000  ?  123 ARG A CA  1 
ATOM   1714 C  CA  B ARG A 1 123 ? 21.08100 22.86100 11.66600  0.440 58.00000  ?  123 ARG A CA  1 
ATOM   1715 C  C   A ARG A 1 123 ? 20.82000 23.67600 11.39700  0.560 57.24000  ?  123 ARG A C   1 
ATOM   1716 C  C   B ARG A 1 123 ? 20.20600 23.91700 11.00900  0.440 53.17000  ?  123 ARG A C   1 
ATOM   1717 O  O   A ARG A 1 123 ? 21.20700 24.78800 11.02400  0.560 50.80000  ?  123 ARG A O   1 
ATOM   1718 O  O   B ARG A 1 123 ? 20.64700 25.05300 10.77700  0.440 48.95000  ?  123 ARG A O   1 
ATOM   1719 C  CB  A ARG A 1 123 ? 22.63000 21.95800 11.17700  0.560 65.67000  ?  123 ARG A CB  1 
ATOM   1720 C  CB  B ARG A 1 123 ? 21.92200 22.14800 10.62300  0.440 61.47000  ?  123 ARG A CB  1 
ATOM   1721 C  CG  A ARG A 1 123 ? 21.86200 21.28700 10.04100  0.560 59.87000  ?  123 ARG A CG  1 
ATOM   1722 C  CG  B ARG A 1 123 ? 21.19800 21.68500 9.40900   0.440 59.69000  ?  123 ARG A CG  1 
ATOM   1723 C  CD  A ARG A 1 123 ? 22.76500 20.31500 9.28700   0.560 74.39000  ?  123 ARG A CD  1 
ATOM   1724 C  CD  B ARG A 1 123 ? 22.11100 20.76500 8.62000   0.440 70.64000  ?  123 ARG A CD  1 
ATOM   1725 N  NE  A ARG A 1 123 ? 22.18100 19.83800 8.03600   0.560 70.14000  ?  123 ARG A NE  1 
ATOM   1726 N  NE  B ARG A 1 123 ? 21.46400 20.33100 7.39400   0.440 66.51000  ?  123 ARG A NE  1 
ATOM   1727 C  CZ  A ARG A 1 123 ? 21.27900 18.86600 7.95100   0.560 78.61000  ?  123 ARG A CZ  1 
ATOM   1728 C  CZ  B ARG A 1 123 ? 20.47100 19.45200 7.35300   0.440 72.09000  ?  123 ARG A CZ  1 
ATOM   1729 N  NH1 A ARG A 1 123 ? 20.84400 18.26300 9.04800   0.560 78.25000  ?  123 ARG A NH1 1 
ATOM   1730 N  NH1 B ARG A 1 123 ? 20.02300 18.86400 8.45200   0.440 77.30000  ?  123 ARG A NH1 1 
ATOM   1731 N  NH2 A ARG A 1 123 ? 20.80900 18.49800 6.76700   0.560 74.19000  ?  123 ARG A NH2 1 
ATOM   1732 N  NH2 B ARG A 1 123 ? 19.90200 19.16300 6.18300   0.440 66.97000  ?  123 ARG A NH2 1 
ATOM   1733 N  N   A TYR A 1 124 ? 19.58300 23.24000 11.15400  0.560 52.06000  ?  124 TYR A N   1 
ATOM   1734 N  N   B TYR A 1 124 ? 18.96200 23.57100 10.73400  0.440 48.87000  ?  124 TYR A N   1 
ATOM   1735 C  CA  A TYR A 1 124 ? 18.62300 24.13900 10.52300  0.560 46.34000  ?  124 TYR A CA  1 
ATOM   1736 C  CA  B TYR A 1 124 ? 18.00900 24.54400 10.24600  0.440 50.30000  ?  124 TYR A CA  1 
ATOM   1737 C  C   A TYR A 1 124 ? 18.16400 25.21400 11.49900  0.560 50.16000  ?  124 TYR A C   1 
ATOM   1738 C  C   B TYR A 1 124 ? 17.57900 25.56800 11.31100  0.440 47.77000  ?  124 TYR A C   1 
ATOM   1739 O  O   A TYR A 1 124 ? 17.84500 26.33400 11.08300  0.560 38.15000  ?  124 TYR A O   1 
ATOM   1740 O  O   B TYR A 1 124 ? 17.36400 26.73200 10.95800  0.440 35.40000  ?  124 TYR A O   1 
ATOM   1741 C  CB  A TYR A 1 124 ? 17.43400 23.34900 9.98300   0.560 48.78000  ?  124 TYR A CB  1 
ATOM   1742 C  CB  B TYR A 1 124 ? 16.79800 23.80600 9.69000   0.440 42.29000  ?  124 TYR A CB  1 
ATOM   1743 C  CG  A TYR A 1 124 ? 17.75400 22.53900 8.74100   0.560 60.00000  ?  124 TYR A CG  1 
ATOM   1744 C  CG  B TYR A 1 124 ? 17.12600 23.00700 8.46300   0.440 58.13000  ?  124 TYR A CG  1 
ATOM   1745 C  CD1 A TYR A 1 124 ? 18.05900 23.16100 7.53400   0.560 62.14000  ?  124 TYR A CD1 1 
ATOM   1746 C  CD1 B TYR A 1 124 ? 17.24000 23.60100 7.21600   0.440 58.23000  ?  124 TYR A CD1 1 
ATOM   1747 C  CD2 A TYR A 1 124 ? 17.74900 21.15200 8.77700   0.560 67.03000  ?  124 TYR A CD2 1 
ATOM   1748 C  CD2 B TYR A 1 124 ? 17.33300 21.63900 8.56300   0.440 66.38000  ?  124 TYR A CD2 1 
ATOM   1749 C  CE1 A TYR A 1 124 ? 18.35100 22.41800 6.39900   0.560 63.88000  ?  124 TYR A CE1 1 
ATOM   1750 C  CE1 B TYR A 1 124 ? 17.52400 22.82400 6.06700   0.440 60.58000  ?  124 TYR A CE1 1 
ATOM   1751 C  CE2 A TYR A 1 124 ? 18.03800 20.40500 7.65100   0.560 70.36000  ?  124 TYR A CE2 1 
ATOM   1752 C  CE2 B TYR A 1 124 ? 17.60900 20.85900 7.44400   0.440 70.59000  ?  124 TYR A CE2 1 
ATOM   1753 C  CZ  A TYR A 1 124 ? 18.33800 21.04100 6.46700   0.560 71.73000  ?  124 TYR A CZ  1 
ATOM   1754 C  CZ  B TYR A 1 124 ? 17.70700 21.45500 6.19400   0.440 65.22000  ?  124 TYR A CZ  1 
ATOM   1755 O  OH  A TYR A 1 124 ? 18.62400 20.28900 5.35100   0.560 72.77000  ?  124 TYR A OH  1 
ATOM   1756 O  OH  B TYR A 1 124 ? 17.98600 20.64100 5.12000   0.440 68.99000  ?  124 TYR A OH  1 
ATOM   1757 N  N   A ALA A 1 125 ? 18.13700 24.89900 12.79600  0.560 47.44000  ?  125 ALA A N   1 
ATOM   1758 N  N   B ALA A 1 125 ? 17.41300 25.19000 12.58500  0.440 41.44000  ?  125 ALA A N   1 
ATOM   1759 C  CA  A ALA A 1 125 ? 17.84200 25.91800 13.79800  0.560 43.97000  ?  125 ALA A CA  1 
ATOM   1760 C  CA  B ALA A 1 125 ? 17.30800 26.22600 13.60400  0.440 40.08000  ?  125 ALA A CA  1 
ATOM   1761 C  C   A ALA A 1 125 ? 18.92200 26.99300 13.81500  0.560 42.72000  ?  125 ALA A C   1 
ATOM   1762 C  C   B ALA A 1 125 ? 18.43900 27.23700 13.44300  0.440 42.20000  ?  125 ALA A C   1 
ATOM   1763 O  O   A ALA A 1 125 ? 18.62500 28.18400 13.96600  0.560 38.67000  ?  125 ALA A O   1 
ATOM   1764 O  O   B ALA A 1 125 ? 18.19300 28.43300 13.26800  0.440 35.18000  ?  125 ALA A O   1 
ATOM   1765 C  CB  A ALA A 1 125 ? 17.70700 25.27200 15.17600  0.560 49.36000  ?  125 ALA A CB  1 
ATOM   1766 C  CB  B ALA A 1 125 ? 17.36500 25.62000 15.00700  0.440 47.18000  ?  125 ALA A CB  1 
ATOM   1767 N  N   A LEU A 1 126 ? 20.18700 26.59200 13.67500  0.560 41.55000  ?  126 LEU A N   1 
ATOM   1768 N  N   B LEU A 1 126 ? 19.69000 26.74600 13.45200  0.440 42.21000  ?  126 LEU A N   1 
ATOM   1769 C  CA  A LEU A 1 126 ? 21.26200 27.57600 13.59500  0.560 44.94000  ?  126 LEU A CA  1 
ATOM   1770 C  CA  B LEU A 1 126 ? 20.86600 27.61500 13.38200  0.440 45.01000  ?  126 LEU A CA  1 
ATOM   1771 C  C   A LEU A 1 126 ? 21.16700 28.38400 12.30500  0.560 44.15000  ?  126 LEU A C   1 
ATOM   1772 C  C   B LEU A 1 126 ? 20.89100 28.41600 12.08000  0.440 44.31000  ?  126 LEU A C   1 
ATOM   1773 O  O   A LEU A 1 126 ? 21.35200 29.60700 12.31500  0.560 46.68000  ?  126 LEU A O   1 
ATOM   1774 O  O   B LEU A 1 126 ? 21.14000 29.62700 12.09300  0.440 45.85000  ?  126 LEU A O   1 
ATOM   1775 C  CB  A LEU A 1 126 ? 22.61800 26.87700 13.70100  0.560 39.40000  ?  126 LEU A CB  1 
ATOM   1776 C  CB  B LEU A 1 126 ? 22.15100 26.78500 13.50700  0.440 42.55000  ?  126 LEU A CB  1 
ATOM   1777 C  CG  A LEU A 1 126 ? 22.87500 26.20500 15.05100  0.560 52.37000  ?  126 LEU A CG  1 
ATOM   1778 C  CG  B LEU A 1 126 ? 22.25900 25.85600 14.74500  0.440 53.45000  ?  126 LEU A CG  1 
ATOM   1779 C  CD1 A LEU A 1 126 ? 23.98500 25.17100 14.99200  0.560 51.16000  ?  126 LEU A CD1 1 
ATOM   1780 C  CD1 B LEU A 1 126 ? 23.52200 24.97800 14.73300  0.440 53.14000  ?  126 LEU A CD1 1 
ATOM   1781 C  CD2 A LEU A 1 126 ? 23.18500 27.26700 16.11500  0.560 40.94000  ?  126 LEU A CD2 1 
ATOM   1782 C  CD2 B LEU A 1 126 ? 22.20900 26.63000 16.05300  0.440 48.81000  ?  126 LEU A CD2 1 
ATOM   1783 N  N   A PHE A 1 127 ? 20.85500 27.72100 11.18900  0.560 43.13000  ?  127 PHE A N   1 
ATOM   1784 N  N   B PHE A 1 127 ? 20.66200 27.75500 10.93000  0.440 42.36000  ?  127 PHE A N   1 
ATOM   1785 C  CA  A PHE A 1 127 ? 20.69500 28.43900 9.93000   0.560 37.72000  ?  127 PHE A CA  1 
ATOM   1786 C  CA  B PHE A 1 127 ? 20.48100 28.53200 9.70800   0.440 38.38000  ?  127 PHE A CA  1 
ATOM   1787 C  C   A PHE A 1 127 ? 19.59300 29.48800 10.02900  0.560 39.62000  ?  127 PHE A C   1 
ATOM   1788 C  C   B PHE A 1 127 ? 19.33300 29.53000 9.88900   0.440 39.59000  ?  127 PHE A C   1 
ATOM   1789 O  O   A PHE A 1 127 ? 19.75100 30.61500 9.54500   0.560 38.55000  ?  127 PHE A O   1 
ATOM   1790 O  O   B PHE A 1 127 ? 19.45900 30.72300 9.55400   0.440 39.10000  ?  127 PHE A O   1 
ATOM   1791 C  CB  A PHE A 1 127 ? 20.39400 27.45800 8.79900   0.560 47.13000  ?  127 PHE A CB  1 
ATOM   1792 C  CB  B PHE A 1 127 ? 20.24200 27.62500 8.48600   0.440 46.21000  ?  127 PHE A CB  1 
ATOM   1793 C  CG  A PHE A 1 127 ? 19.94500 28.12300 7.53400   0.560 42.41000  ?  127 PHE A CG  1 
ATOM   1794 C  CG  B PHE A 1 127 ? 19.76200 28.39000 7.25000   0.440 42.45000  ?  127 PHE A CG  1 
ATOM   1795 C  CD1 A PHE A 1 127 ? 20.87200 28.62200 6.63200   0.560 46.15000  ?  127 PHE A CD1 1 
ATOM   1796 C  CD1 B PHE A 1 127 ? 18.39100 28.66900 7.03900   0.440 40.10000  ?  127 PHE A CD1 1 
ATOM   1797 C  CD2 A PHE A 1 127 ? 18.59800 28.25800 7.24600   0.560 39.04000  ?  127 PHE A CD2 1 
ATOM   1798 C  CD2 B PHE A 1 127 ? 20.68300 28.84500 6.31200   0.440 47.55000  ?  127 PHE A CD2 1 
ATOM   1799 C  CE1 A PHE A 1 127 ? 20.46400 29.24000 5.46900   0.560 47.93000  ?  127 PHE A CE1 1 
ATOM   1800 C  CE1 B PHE A 1 127 ? 17.95800 29.37900 5.88700   0.440 53.80000  ?  127 PHE A CE1 1 
ATOM   1801 C  CE2 A PHE A 1 127 ? 18.18400 28.87700 6.07800   0.560 52.71000  ?  127 PHE A CE2 1 
ATOM   1802 C  CE2 B PHE A 1 127 ? 20.28100 29.57100 5.16500   0.440 46.77000  ?  127 PHE A CE2 1 
ATOM   1803 C  CZ  A PHE A 1 127 ? 19.11700 29.36600 5.19300   0.560 51.93000  ?  127 PHE A CZ  1 
ATOM   1804 C  CZ  B PHE A 1 127 ? 18.92100 29.83100 4.93300   0.440 49.37000  ?  127 PHE A CZ  1 
ATOM   1805 N  N   A GLY A 1 128 ? 18.47100 29.13500 10.65800  0.560 35.15000  ?  128 GLY A N   1 
ATOM   1806 N  N   B GLY A 1 128 ? 18.20400 29.05600 10.41400  0.440 34.19000  ?  128 GLY A N   1 
ATOM   1807 C  CA  A GLY A 1 128 ? 17.38700 30.09100 10.81100  0.560 38.74000  ?  128 GLY A CA  1 
ATOM   1808 C  CA  B GLY A 1 128 ? 17.08600 29.90400 10.75100  0.440 37.28000  ?  128 GLY A CA  1 
ATOM   1809 C  C   A GLY A 1 128 ? 17.79200 31.31600 11.60300  0.560 40.97000  ?  128 GLY A C   1 
ATOM   1810 C  C   B GLY A 1 128 ? 17.47500 31.09300 11.63500  0.440 40.92000  ?  128 GLY A C   1 
ATOM   1811 O  O   A GLY A 1 128 ? 17.36900 32.43400 11.29500  0.560 41.64000  ?  128 GLY A O   1 
ATOM   1812 O  O   B GLY A 1 128 ? 16.98700 32.20100 11.39700  0.440 43.43000  ?  128 GLY A O   1 
ATOM   1813 N  N   A MET A 1 129 ? 18.61300 31.12900 12.63800  0.560 39.85000  ?  129 MET A N   1 
ATOM   1814 N  N   B MET A 1 129 ? 18.35000 30.94600 12.63400  0.440 39.87000  ?  129 MET A N   1 
ATOM   1815 C  CA  A MET A 1 129 ? 19.03400 32.27700 13.43200  0.560 42.89000  ?  129 MET A CA  1 
ATOM   1816 C  CA  B MET A 1 129 ? 18.76400 32.13400 13.39000  0.440 41.61000  ?  129 MET A CA  1 
ATOM   1817 C  C   A MET A 1 129 ? 19.90000 33.22600 12.61700  0.560 36.81000  ?  129 MET A C   1 
ATOM   1818 C  C   B MET A 1 129 ? 19.56000 33.08400 12.50900  0.440 38.25000  ?  129 MET A C   1 
ATOM   1819 O  O   A MET A 1 129 ? 19.76500 34.45000 12.72600  0.560 33.61000  ?  129 MET A O   1 
ATOM   1820 O  O   B MET A 1 129 ? 19.35100 34.29400 12.52800  0.440 34.09000  ?  129 MET A O   1 
ATOM   1821 C  CB  A MET A 1 129 ? 19.79800 31.82700 14.67000  0.560 41.48000  ?  129 MET A CB  1 
ATOM   1822 C  CB  B MET A 1 129 ? 19.61800 31.75200 14.58100  0.440 41.28000  ?  129 MET A CB  1 
ATOM   1823 C  CG  A MET A 1 129 ? 19.46700 32.67900 15.86300  0.560 56.10000  ?  129 MET A CG  1 
ATOM   1824 C  CG  B MET A 1 129 ? 19.74700 32.88400 15.56400  0.440 53.13000  ?  129 MET A CG  1 
ATOM   1825 S  SD  A MET A 1 129 ? 20.42500 32.32800 17.35100  0.560 63.47000  ?  129 MET A SD  1 
ATOM   1826 S  SD  B MET A 1 129 ? 21.01700 32.54900 16.74700  0.440 54.42000  ?  129 MET A SD  1 
ATOM   1827 C  CE  A MET A 1 129 ? 22.04800 32.94500 16.86700  0.560 52.39000  ?  129 MET A CE  1 
ATOM   1828 C  CE  B MET A 1 129 ? 22.43400 32.58200 15.70300  0.440 56.94000  ?  129 MET A CE  1 
ATOM   1829 N  N   A GLY A 1 130 ? 20.80900 32.68000 11.81100  0.560 34.36000  ?  130 GLY A N   1 
ATOM   1830 N  N   B GLY A 1 130 ? 20.48300 32.54800 11.73200  0.440 35.87000  ?  130 GLY A N   1 
ATOM   1831 C  CA  A GLY A 1 130 ? 21.58200 33.52300 10.91700  0.560 39.14000  ?  130 GLY A CA  1 
ATOM   1832 C  CA  B GLY A 1 130 ? 21.20200 33.37600 10.77800  0.440 39.65000  ?  130 GLY A CA  1 
ATOM   1833 C  C   A GLY A 1 130 ? 20.70500 34.25200 9.92000   0.560 39.18000  ?  130 GLY A C   1 
ATOM   1834 C  C   B GLY A 1 130 ? 20.30700 34.19900 9.86100   0.440 38.45000  ?  130 GLY A C   1 
ATOM   1835 O  O   A GLY A 1 130 ? 20.96000 35.41200 9.58700   0.560 39.91000  ?  130 GLY A O   1 
ATOM   1836 O  O   B GLY A 1 130 ? 20.45900 35.42200 9.76500   0.440 39.83000  ?  130 GLY A O   1 
ATOM   1837 N  N   A ALA A 1 131 ? 19.65700 33.58500 9.43100   0.560 33.89000  ?  131 ALA A N   1 
ATOM   1838 N  N   B ALA A 1 131 ? 19.37600 33.53600 9.17800   0.440 33.51000  ?  131 ALA A N   1 
ATOM   1839 C  CA  A ALA A 1 131 ? 18.74100 34.24300 8.50600   0.560 33.50000  ?  131 ALA A CA  1 
ATOM   1840 C  CA  B ALA A 1 131 ? 18.44200 34.24900 8.32300   0.440 35.46000  ?  131 ALA A CA  1 
ATOM   1841 C  C   A ALA A 1 131 ? 18.06700 35.43900 9.16300   0.560 43.68000  ?  131 ALA A C   1 
ATOM   1842 C  C   B ALA A 1 131 ? 17.90800 35.46300 9.03600   0.440 43.83000  ?  131 ALA A C   1 
ATOM   1843 O  O   A ALA A 1 131 ? 17.94200 36.50600 8.55200   0.560 46.20000  ?  131 ALA A O   1 
ATOM   1844 O  O   B ALA A 1 131 ? 18.01100 36.59400 8.53300   0.440 45.84000  ?  131 ALA A O   1 
ATOM   1845 C  CB  A ALA A 1 131 ? 17.69000 33.25400 8.00700   0.560 38.27000  ?  131 ALA A CB  1 
ATOM   1846 C  CB  B ALA A 1 131 ? 17.28400 33.34300 7.90100   0.440 37.49000  ?  131 ALA A CB  1 
ATOM   1847 N  N   A VAL A 1 132 ? 17.62200 35.28000 10.41000  0.560 38.76000  ?  132 VAL A N   1 
ATOM   1848 N  N   B VAL A 1 132 ? 17.33800 35.23700 10.22000  0.440 39.27000  ?  132 VAL A N   1 
ATOM   1849 C  CA  A VAL A 1 132 ? 16.95800 36.38200 11.09900  0.560 39.20000  ?  132 VAL A CA  1 
ATOM   1850 C  CA  B VAL A 1 132 ? 16.77400 36.30800 11.03300  0.440 39.26000  ?  132 VAL A CA  1 
ATOM   1851 C  C   A VAL A 1 132 ? 17.91600 37.55700 11.25900  0.560 39.77000  ?  132 VAL A C   1 
ATOM   1852 C  C   B VAL A 1 132 ? 17.77500 37.42900 11.19900  0.440 39.92000  ?  132 VAL A C   1 
ATOM   1853 O  O   A VAL A 1 132 ? 17.56600 38.71100 10.98400  0.560 34.85000  ?  132 VAL A O   1 
ATOM   1854 O  O   B VAL A 1 132 ? 17.47400 38.60500 10.95600  0.440 35.20000  ?  132 VAL A O   1 
ATOM   1855 C  CB  A VAL A 1 132 ? 16.40600 35.91400 12.45700  0.560 45.54000  ?  132 VAL A CB  1 
ATOM   1856 C  CB  B VAL A 1 132 ? 16.35400 35.72900 12.39200  0.440 45.22000  ?  132 VAL A CB  1 
ATOM   1857 C  CG1 A VAL A 1 132 ? 15.95100 37.11100 13.27500  0.560 44.55000  ?  132 VAL A CG1 1 
ATOM   1858 C  CG1 B VAL A 1 132 ? 15.95900 36.85200 13.39500  0.440 43.69000  ?  132 VAL A CG1 1 
ATOM   1859 C  CG2 A VAL A 1 132 ? 15.26400 34.93300 12.25500  0.560 37.53000  ?  132 VAL A CG2 1 
ATOM   1860 C  CG2 B VAL A 1 132 ? 15.22300 34.72100 12.16400  0.440 37.15000  ?  132 VAL A CG2 1 
ATOM   1861 N  N   A ALA A 1 133 ? 19.14500 37.27600 11.70000  0.560 35.24000  ?  133 ALA A N   1 
ATOM   1862 N  N   B ALA A 1 133 ? 19.00300 37.07800 11.54000  0.440 34.78000  ?  133 ALA A N   1 
ATOM   1863 C  CA  A ALA A 1 133 ? 20.12800 38.33900 11.87800  0.560 41.23000  ?  133 ALA A CA  1 
ATOM   1864 C  CA  B ALA A 1 133 ? 19.97400 38.12000 11.79800  0.440 40.78000  ?  133 ALA A CA  1 
ATOM   1865 C  C   A ALA A 1 133 ? 20.50700 38.98000 10.55100  0.560 42.00000  ?  133 ALA A C   1 
ATOM   1866 C  C   B ALA A 1 133 ? 20.27100 38.87000 10.51100  0.440 41.90000  ?  133 ALA A C   1 
ATOM   1867 O  O   A ALA A 1 133 ? 20.81000 40.17700 10.50800  0.560 39.55000  ?  133 ALA A O   1 
ATOM   1868 O  O   B ALA A 1 133 ? 20.48300 40.08800 10.51300  0.440 39.24000  ?  133 ALA A O   1 
ATOM   1869 C  CB  A ALA A 1 133 ? 21.37500 37.79300 12.57400  0.560 39.92000  ?  133 ALA A CB  1 
ATOM   1870 C  CB  B ALA A 1 133 ? 21.23100 37.50400 12.43300  0.440 39.30000  ?  133 ALA A CB  1 
ATOM   1871 N  N   A PHE A 1 134 ? 20.50200 38.20300 9.46700   0.560 44.97000  ?  134 PHE A N   1 
ATOM   1872 N  N   B PHE A 1 134 ? 20.17200 38.16900 9.38900   0.440 43.62000  ?  134 PHE A N   1 
ATOM   1873 C  CA  A PHE A 1 134 ? 20.79900 38.76300 8.15500   0.560 35.75000  ?  134 PHE A CA  1 
ATOM   1874 C  CA  B PHE A 1 134 ? 20.50700 38.73700 8.10300   0.440 35.67000  ?  134 PHE A CA  1 
ATOM   1875 C  C   A PHE A 1 134 ? 19.75000 39.79100 7.75100   0.560 41.74000  ?  134 PHE A C   1 
ATOM   1876 C  C   B PHE A 1 134 ? 19.46000 39.70500 7.61900   0.440 42.13000  ?  134 PHE A C   1 
ATOM   1877 O  O   A PHE A 1 134 ? 20.08500 40.84500 7.19600   0.560 41.54000  ?  134 PHE A O   1 
ATOM   1878 O  O   B PHE A 1 134 ? 19.79700 40.65100 6.87900   0.440 43.71000  ?  134 PHE A O   1 
ATOM   1879 C  CB  A PHE A 1 134 ? 20.88500 37.63800 7.12400   0.560 42.02000  ?  134 PHE A CB  1 
ATOM   1880 C  CB  B PHE A 1 134 ? 20.64100 37.61300 7.08700   0.440 42.41000  ?  134 PHE A CB  1 
ATOM   1881 C  CG  A PHE A 1 134 ? 21.23500 38.10600 5.74600   0.560 36.79000  ?  134 PHE A CG  1 
ATOM   1882 C  CG  B PHE A 1 134 ? 21.04000 38.08200 5.79500   0.440 36.47000  ?  134 PHE A CG  1 
ATOM   1883 C  CD1 A PHE A 1 134 ? 22.49400 38.60900 5.47100   0.560 41.58000  ?  134 PHE A CD1 1 
ATOM   1884 C  CD1 B PHE A 1 134 ? 22.35700 38.39900 5.56000   0.440 41.48000  ?  134 PHE A CD1 1 
ATOM   1885 C  CD2 A PHE A 1 134 ? 20.30100 38.04900 4.72400   0.560 41.61000  ?  134 PHE A CD2 1 
ATOM   1886 C  CD2 B PHE A 1 134 ? 20.11000 38.33200 4.83900   0.440 40.38000  ?  134 PHE A CD2 1 
ATOM   1887 C  CE1 A PHE A 1 134 ? 22.81600 39.04300 4.19500   0.560 43.58000  ?  134 PHE A CE1 1 
ATOM   1888 C  CE1 B PHE A 1 134 ? 22.73900 38.87900 4.35600   0.440 43.28000  ?  134 PHE A CE1 1 
ATOM   1889 C  CE2 A PHE A 1 134 ? 20.61900 38.48100 3.45300   0.560 43.51000  ?  134 PHE A CE2 1 
ATOM   1890 C  CE2 B PHE A 1 134 ? 20.50000 38.79800 3.56300   0.440 42.92000  ?  134 PHE A CE2 1 
ATOM   1891 C  CZ  A PHE A 1 134 ? 21.87800 38.97800 3.19100   0.560 44.06000  ?  134 PHE A CZ  1 
ATOM   1892 C  CZ  B PHE A 1 134 ? 21.80400 39.07800 3.33800   0.440 43.71000  ?  134 PHE A CZ  1 
ATOM   1893 N  N   A LEU A 1 135 ? 18.47400 39.51000 8.02400   0.560 37.34000  ?  135 LEU A N   1 
ATOM   1894 N  N   B LEU A 1 135 ? 18.18400 39.45000 7.95200   0.440 37.75000  ?  135 LEU A N   1 
ATOM   1895 C  CA  A LEU A 1 135 ? 17.43400 40.48100 7.70300   0.560 38.34000  ?  135 LEU A CA  1 
ATOM   1896 C  CA  B LEU A 1 135 ? 17.17000 40.42700 7.60600   0.440 38.99000  ?  135 LEU A CA  1 
ATOM   1897 C  C   A LEU A 1 135 ? 17.66300 41.78900 8.45000   0.560 46.08000  ?  135 LEU A C   1 
ATOM   1898 C  C   B LEU A 1 135 ? 17.39700 41.71700 8.36500   0.440 45.99000  ?  135 LEU A C   1 
ATOM   1899 O  O   A LEU A 1 135 ? 17.44800 42.87400 7.89800   0.560 49.47000  ?  135 LEU A O   1 
ATOM   1900 O  O   B LEU A 1 135 ? 17.01500 42.79500 7.88400   0.440 48.10000  ?  135 LEU A O   1 
ATOM   1901 C  CB  A LEU A 1 135 ? 16.05700 39.90700 8.02700   0.560 38.11000  ?  135 LEU A CB  1 
ATOM   1902 C  CB  B LEU A 1 135 ? 15.77200 39.89200 7.88900   0.440 38.27000  ?  135 LEU A CB  1 
ATOM   1903 C  CG  A LEU A 1 135 ? 15.62300 38.76600 7.10700   0.560 43.52000  ?  135 LEU A CG  1 
ATOM   1904 C  CG  B LEU A 1 135 ? 15.53000 38.76500 6.86300   0.440 43.91000  ?  135 LEU A CG  1 
ATOM   1905 C  CD1 A LEU A 1 135 ? 14.36800 38.09500 7.63500   0.560 44.66000  ?  135 LEU A CD1 1 
ATOM   1906 C  CD1 B LEU A 1 135 ? 14.30300 38.03200 7.27000   0.440 42.48000  ?  135 LEU A CD1 1 
ATOM   1907 C  CD2 A LEU A 1 135 ? 15.40800 39.26500 5.68300   0.560 50.16000  ?  135 LEU A CD2 1 
ATOM   1908 C  CD2 B LEU A 1 135 ? 15.37100 39.32600 5.44800   0.440 49.58000  ?  135 LEU A CD2 1 
ATOM   1909 N  N   A GLY A 1 136 ? 18.10200 41.70700 9.70700   0.560 46.55000  ?  136 GLY A N   1 
ATOM   1910 N  N   B GLY A 1 136 ? 18.03200 41.62900 9.53000   0.440 46.48000  ?  136 GLY A N   1 
ATOM   1911 C  CA  A GLY A 1 136 ? 18.43000 42.91900 10.44000  0.560 44.27000  ?  136 GLY A CA  1 
ATOM   1912 C  CA  B GLY A 1 136 ? 18.33600 42.81800 10.27000  0.440 44.37000  ?  136 GLY A CA  1 
ATOM   1913 C  C   A GLY A 1 136 ? 19.60500 43.65800 9.83100   0.560 44.12000  ?  136 GLY A C   1 
ATOM   1914 C  C   B GLY A 1 136 ? 19.42500 43.57200 9.55300   0.440 44.13000  ?  136 GLY A C   1 
ATOM   1915 O  O   A GLY A 1 136 ? 19.62300 44.89100 9.79200   0.560 47.94000  ?  136 GLY A O   1 
ATOM   1916 O  O   B GLY A 1 136 ? 19.23300 44.72400 9.14100   0.440 47.52000  ?  136 GLY A O   1 
ATOM   1917 N  N   A LEU A 1 137 ? 20.60200 42.91600 9.34700   0.560 45.21000  ?  137 LEU A N   1 
ATOM   1918 N  N   B LEU A 1 137 ? 20.57700 42.91200 9.39100   0.440 45.05000  ?  137 LEU A N   1 
ATOM   1919 C  CA  A LEU A 1 137 ? 21.73600 43.54700 8.68200   0.560 45.69000  ?  137 LEU A CA  1 
ATOM   1920 C  CA  B LEU A 1 137 ? 21.68700 43.42800 8.59000   0.440 45.57000  ?  137 LEU A CA  1 
ATOM   1921 C  C   A LEU A 1 137 ? 21.29700 44.26300 7.41300   0.560 49.97000  ?  137 LEU A C   1 
ATOM   1922 C  C   B LEU A 1 137 ? 21.23200 44.03100 7.27000   0.440 49.69000  ?  137 LEU A C   1 
ATOM   1923 O  O   A LEU A 1 137 ? 21.74000 45.38500 7.13900   0.560 52.75000  ?  137 LEU A O   1 
ATOM   1924 O  O   B LEU A 1 137 ? 21.85100 44.96600 6.75700   0.440 50.85000  ?  137 LEU A O   1 
ATOM   1925 C  CB  A LEU A 1 137 ? 22.79800 42.49800 8.36500   0.560 42.59000  ?  137 LEU A CB  1 
ATOM   1926 C  CB  B LEU A 1 137 ? 22.69100 42.32900 8.34200   0.440 43.11000  ?  137 LEU A CB  1 
ATOM   1927 C  CG  A LEU A 1 137 ? 24.06100 42.99000 7.66300   0.560 49.76000  ?  137 LEU A CG  1 
ATOM   1928 C  CG  B LEU A 1 137 ? 23.72700 42.69300 7.30500   0.440 50.65000  ?  137 LEU A CG  1 
ATOM   1929 C  CD1 A LEU A 1 137 ? 24.82700 43.94500 8.56200   0.560 40.68000  ?  137 LEU A CD1 1 
ATOM   1930 C  CD1 B LEU A 1 137 ? 24.57300 43.81400 7.84900   0.440 41.79000  ?  137 LEU A CD1 1 
ATOM   1931 C  CD2 A LEU A 1 137 ? 24.93700 41.81800 7.25700   0.560 47.29000  ?  137 LEU A CD2 1 
ATOM   1932 C  CD2 B LEU A 1 137 ? 24.51900 41.41700 6.93400   0.440 38.22000  ?  137 LEU A CD2 1 
ATOM   1933 N  N   A VAL A 1 138 ? 20.42800 43.62800 6.62300   0.560 48.59000  ?  138 VAL A N   1 
ATOM   1934 N  N   B VAL A 1 138 ? 20.10900 43.55000 6.74000   0.440 48.64000  ?  138 VAL A N   1 
ATOM   1935 C  CA  A VAL A 1 138 ? 19.94100 44.25700 5.39800   0.560 46.13000  ?  138 VAL A CA  1 
ATOM   1936 C  CA  B VAL A 1 138 ? 19.62700 44.09900 5.48400   0.440 46.52000  ?  138 VAL A CA  1 
ATOM   1937 C  C   A VAL A 1 138 ? 19.19500 45.54000 5.72500   0.560 53.00000  ?  138 VAL A C   1 
ATOM   1938 C  C   B VAL A 1 138 ? 18.86300 45.38900 5.70900   0.440 53.29000  ?  138 VAL A C   1 
ATOM   1939 O  O   A VAL A 1 138 ? 19.30900 46.54400 5.00900   0.560 56.25000  ?  138 VAL A O   1 
ATOM   1940 O  O   B VAL A 1 138 ? 18.98400 46.32700 4.90700   0.440 54.88000  ?  138 VAL A O   1 
ATOM   1941 C  CB  A VAL A 1 138 ? 19.05200 43.27700 4.60800   0.560 51.74000  ?  138 VAL A CB  1 
ATOM   1942 C  CB  B VAL A 1 138 ? 18.80600 43.02900 4.75900   0.440 51.31000  ?  138 VAL A CB  1 
ATOM   1943 C  CG1 A VAL A 1 138 ? 18.30600 44.00400 3.49500   0.560 48.15000  ?  138 VAL A CG1 1 
ATOM   1944 C  CG1 B VAL A 1 138 ? 17.93500 43.64600 3.72400   0.440 47.95000  ?  138 VAL A CG1 1 
ATOM   1945 C  CG2 A VAL A 1 138 ? 19.88900 42.14000 4.05000   0.560 42.61000  ?  138 VAL A CG2 1 
ATOM   1946 C  CG2 B VAL A 1 138 ? 19.77200 42.05500 4.10900   0.440 42.90000  ?  138 VAL A CG2 1 
ATOM   1947 N  N   A TYR A 1 139 ? 18.40800 45.52900 6.80300   0.560 56.46000  ?  139 TYR A N   1 
ATOM   1948 N  N   B TYR A 1 139 ? 18.11400 45.50400 6.82200   0.440 55.60000  ?  139 TYR A N   1 
ATOM   1949 C  CA  A TYR A 1 139 ? 17.69300 46.73900 7.18700   0.560 54.67000  ?  139 TYR A CA  1 
ATOM   1950 C  CA  B TYR A 1 139 ? 17.51900 46.80600 7.12600   0.440 54.75000  ?  139 TYR A CA  1 
ATOM   1951 C  C   A TYR A 1 139 ? 18.66200 47.88500 7.44600   0.560 56.17000  ?  139 TYR A C   1 
ATOM   1952 C  C   B TYR A 1 139 ? 18.57200 47.83800 7.51200   0.440 56.25000  ?  139 TYR A C   1 
ATOM   1953 O  O   A TYR A 1 139 ? 18.41400 49.02300 7.03600   0.560 57.88000  ?  139 TYR A O   1 
ATOM   1954 O  O   B TYR A 1 139 ? 18.46700 49.00100 7.10400   0.440 57.79000  ?  139 TYR A O   1 
ATOM   1955 C  CB  A TYR A 1 139 ? 16.83200 46.49800 8.42700   0.560 61.55000  ?  139 TYR A CB  1 
ATOM   1956 C  CB  B TYR A 1 139 ? 16.45700 46.72900 8.21800   0.440 62.65000  ?  139 TYR A CB  1 
ATOM   1957 C  CG  A TYR A 1 139 ? 16.31500 47.79100 9.02900   0.560 69.17000  ?  139 TYR A CG  1 
ATOM   1958 C  CG  B TYR A 1 139 ? 16.26100 48.09100 8.91200   0.440 69.56000  ?  139 TYR A CG  1 
ATOM   1959 C  CD1 A TYR A 1 139 ? 15.16600 48.39700 8.53800   0.560 78.90000  ?  139 TYR A CD1 1 
ATOM   1960 C  CD1 B TYR A 1 139 ? 15.58500 49.14800 8.26300   0.440 75.32000  ?  139 TYR A CD1 1 
ATOM   1961 C  CD2 A TYR A 1 139 ? 16.98900 48.41700 10.07200  0.560 64.85000  ?  139 TYR A CD2 1 
ATOM   1962 C  CD2 B TYR A 1 139 ? 16.74600 48.32700 10.20700  0.440 65.20000  ?  139 TYR A CD2 1 
ATOM   1963 C  CE1 A TYR A 1 139 ? 14.69400 49.58400 9.07600   0.560 74.55000  ?  139 TYR A CE1 1 
ATOM   1964 C  CE1 B TYR A 1 139 ? 15.39500 50.41200 8.88500   0.440 75.10000  ?  139 TYR A CE1 1 
ATOM   1965 C  CE2 A TYR A 1 139 ? 16.52500 49.60600 10.61400  0.560 74.21000  ?  139 TYR A CE2 1 
ATOM   1966 C  CE2 B TYR A 1 139 ? 16.56800 49.59500 10.84300  0.440 74.25000  ?  139 TYR A CE2 1 
ATOM   1967 C  CZ  A TYR A 1 139 ? 15.37700 50.18300 10.11300  0.560 79.92000  ?  139 TYR A CZ  1 
ATOM   1968 C  CZ  B TYR A 1 139 ? 15.88000 50.63000 10.18500  0.440 80.97000  ?  139 TYR A CZ  1 
ATOM   1969 O  OH  A TYR A 1 139 ? 14.91000 51.36300 10.64800  0.560 91.73000  ?  139 TYR A OH  1 
ATOM   1970 O  OH  B TYR A 1 139 ? 15.70900 51.87500 10.81300  0.440 84.39000  ?  139 TYR A OH  1 
ATOM   1971 N  N   A TYR A 1 140 ? 19.77200 47.60900 8.13400   0.560 51.95000  ?  140 TYR A N   1 
ATOM   1972 N  N   B TYR A 1 140 ? 19.57800 47.47300 8.31600   0.440 51.54000  ?  140 TYR A N   1 
ATOM   1973 C  CA  A TYR A 1 140 ? 20.70600 48.68200 8.45800   0.560 55.58000  ?  140 TYR A CA  1 
ATOM   1974 C  CA  B TYR A 1 140 ? 20.57200 48.50400 8.56900   0.440 55.26000  ?  140 TYR A CA  1 
ATOM   1975 C  C   A TYR A 1 140 ? 21.41100 49.19200 7.20900   0.560 62.90000  ?  140 TYR A C   1 
ATOM   1976 C  C   B TYR A 1 140 ? 21.22800 48.95900 7.26200   0.440 61.77000  ?  140 TYR A C   1 
ATOM   1977 O  O   A TYR A 1 140 ? 21.65600 50.39600 7.07800   0.560 62.96000  ?  140 TYR A O   1 
ATOM   1978 O  O   B TYR A 1 140 ? 21.57500 50.13800 7.11400   0.440 63.00000  ?  140 TYR A O   1 
ATOM   1979 C  CB  A TYR A 1 140 ? 21.70600 48.20400 9.50900   0.560 53.95000  ?  140 TYR A CB  1 
ATOM   1980 C  CB  B TYR A 1 140 ? 21.58200 48.05000 9.60500   0.440 54.59000  ?  140 TYR A CB  1 
ATOM   1981 C  CG  A TYR A 1 140 ? 21.18300 48.41400 10.91300  0.560 63.23000  ?  140 TYR A CG  1 
ATOM   1982 C  CG  B TYR A 1 140 ? 21.06700 48.37600 10.99500  0.440 63.25000  ?  140 TYR A CG  1 
ATOM   1983 C  CD1 A TYR A 1 140 ? 20.41800 47.44100 11.54100  0.560 69.94000  ?  140 TYR A CD1 1 
ATOM   1984 C  CD1 B TYR A 1 140 ? 21.00500 49.69300 11.44100  0.440 63.26000  ?  140 TYR A CD1 1 
ATOM   1985 C  CD2 A TYR A 1 140 ? 21.42400 49.60000 11.59500  0.560 60.38000  ?  140 TYR A CD2 1 
ATOM   1986 C  CD2 B TYR A 1 140 ? 20.51000 47.38800 11.81100  0.440 69.59000  ?  140 TYR A CD2 1 
ATOM   1987 C  CE1 A TYR A 1 140 ? 19.92400 47.63400 12.81800  0.560 71.56000  ?  140 TYR A CE1 1 
ATOM   1988 C  CE1 B TYR A 1 140 ? 20.46600 50.03100 12.68800  0.440 71.31000  ?  140 TYR A CE1 1 
ATOM   1989 C  CE2 A TYR A 1 140 ? 20.93400 49.80200 12.87300  0.560 73.82000  ?  140 TYR A CE2 1 
ATOM   1990 C  CE2 B TYR A 1 140 ? 19.98700 47.70400 13.08700  0.440 71.67000  ?  140 TYR A CE2 1 
ATOM   1991 C  CZ  A TYR A 1 140 ? 20.18400 48.81600 13.48000  0.560 82.27000  ?  140 TYR A CZ  1 
ATOM   1992 C  CZ  B TYR A 1 140 ? 19.95900 49.03600 13.52200  0.440 81.74000  ?  140 TYR A CZ  1 
ATOM   1993 O  OH  A TYR A 1 140 ? 19.69100 49.01000 14.75200  0.560 81.28000  ?  140 TYR A OH  1 
ATOM   1994 O  OH  B TYR A 1 140 ? 19.42600 49.37300 14.77300  0.440 80.02000  ?  140 TYR A OH  1 
ATOM   1995 N  N   A LEU A 1 141 ? 21.72100 48.30100 6.26800   0.560 53.85000  ?  141 LEU A N   1 
ATOM   1996 N  N   B LEU A 1 141 ? 21.30600 48.07300 6.26600   0.440 54.55000  ?  141 LEU A N   1 
ATOM   1997 C  CA  A LEU A 1 141 ? 22.34900 48.73700 5.02600   0.560 54.09000  ?  141 LEU A CA  1 
ATOM   1998 C  CA  B LEU A 1 141 ? 21.80600 48.46600 4.95100   0.440 55.40000  ?  141 LEU A CA  1 
ATOM   1999 C  C   A LEU A 1 141 ? 21.40700 49.61500 4.21400   0.560 57.56000  ?  141 LEU A C   1 
ATOM   2000 C  C   B LEU A 1 141 ? 20.82200 49.39000 4.23300   0.440 58.63000  ?  141 LEU A C   1 
ATOM   2001 O  O   A LEU A 1 141 ? 21.80100 50.67500 3.71300   0.560 56.38000  ?  141 LEU A O   1 
ATOM   2002 O  O   B LEU A 1 141 ? 21.22000 50.36100 3.58600   0.440 58.67000  ?  141 LEU A O   1 
ATOM   2003 C  CB  A LEU A 1 141 ? 22.77800 47.52100 4.20900   0.560 50.43000  ?  141 LEU A CB  1 
ATOM   2004 C  CB  B LEU A 1 141 ? 22.07800 47.22800 4.09100   0.440 48.27000  ?  141 LEU A CB  1 
ATOM   2005 C  CG  A LEU A 1 141 ? 24.00500 46.76700 4.71800   0.560 47.15000  ?  141 LEU A CG  1 
ATOM   2006 C  CG  B LEU A 1 141 ? 23.43000 46.57300 4.31500   0.440 45.82000  ?  141 LEU A CG  1 
ATOM   2007 C  CD1 A LEU A 1 141 ? 24.03600 45.37900 4.10500   0.560 44.33000  ?  141 LEU A CD1 1 
ATOM   2008 C  CD1 B LEU A 1 141 ? 23.44700 45.19600 3.72800   0.440 44.58000  ?  141 LEU A CD1 1 
ATOM   2009 C  CD2 A LEU A 1 141 ? 25.26200 47.54900 4.40400   0.560 51.16000  ?  141 LEU A CD2 1 
ATOM   2010 C  CD2 B LEU A 1 141 ? 24.54000 47.41000 3.72600   0.440 49.62000  ?  141 LEU A CD2 1 
ATOM   2011 N  N   A VAL A 1 142 ? 20.15200 49.18800 4.07400   0.560 60.93000  ?  142 VAL A N   1 
ATOM   2012 N  N   B VAL A 1 142 ? 19.53500 49.10300 4.34400   0.440 59.42000  ?  142 VAL A N   1 
ATOM   2013 C  CA  A VAL A 1 142 ? 19.20400 49.90100 3.22800   0.560 56.77000  ?  142 VAL A CA  1 
ATOM   2014 C  CA  B VAL A 1 142 ? 18.51100 49.79000 3.58400   0.440 55.80000  ?  142 VAL A CA  1 
ATOM   2015 C  C   A VAL A 1 142 ? 18.62000 51.12700 3.90900   0.560 56.38000  ?  142 VAL A C   1 
ATOM   2016 C  C   B VAL A 1 142 ? 17.92000 50.98100 4.33000   0.440 58.29000  ?  142 VAL A C   1 
ATOM   2017 O  O   A VAL A 1 142 ? 18.18500 52.05500 3.21600   0.560 64.20000  ?  142 VAL A O   1 
ATOM   2018 O  O   B VAL A 1 142 ? 17.44000 51.93500 3.70000   0.440 65.26000  ?  142 VAL A O   1 
ATOM   2019 C  CB  A VAL A 1 142 ? 18.08600 48.93600 2.79900   0.560 57.94000  ?  142 VAL A CB  1 
ATOM   2020 C  CB  B VAL A 1 142 ? 17.45900 48.73600 3.20300   0.440 55.99000  ?  142 VAL A CB  1 
ATOM   2021 C  CG1 A VAL A 1 142 ? 16.89500 49.68700 2.24500   0.560 50.82000  ?  142 VAL A CG1 1 
ATOM   2022 C  CG1 B VAL A 1 142 ? 16.11100 49.32400 3.01300   0.440 56.20000  ?  142 VAL A CG1 1 
ATOM   2023 C  CG2 A VAL A 1 142 ? 18.62300 47.93800 1.77700   0.560 46.26000  ?  142 VAL A CG2 1 
ATOM   2024 C  CG2 B VAL A 1 142 ? 17.89300 48.07000 1.89900   0.440 50.70000  ?  142 VAL A CG2 1 
ATOM   2025 N  N   A GLY A 1 143 ? 18.61500 51.16900 5.23800   0.560 58.11000  ?  143 GLY A N   1 
ATOM   2026 N  N   B GLY A 1 143 ? 17.95900 50.97500 5.65400   0.440 60.03000  ?  143 GLY A N   1 
ATOM   2027 C  CA  A GLY A 1 143 ? 17.99600 52.25300 5.95900   0.560 62.97000  ?  143 GLY A CA  1 
ATOM   2028 C  CA  B GLY A 1 143 ? 17.50500 52.11400 6.41200   0.440 63.32000  ?  143 GLY A CA  1 
ATOM   2029 C  C   A GLY A 1 143 ? 18.99200 53.17800 6.62400   0.560 64.93000  ?  143 GLY A C   1 
ATOM   2030 C  C   B GLY A 1 143 ? 18.66400 53.01000 6.78200   0.440 64.48000  ?  143 GLY A C   1 
ATOM   2031 O  O   A GLY A 1 143 ? 19.54400 54.09000 5.99900   0.560 69.51000  ?  143 GLY A O   1 
ATOM   2032 O  O   B GLY A 1 143 ? 19.25600 53.69500 5.94200   0.440 65.61000  ?  143 GLY A O   1 
ATOM   2033 N  N   A PRO A 1 144 ? 19.23100 52.96100 7.92200   0.560 66.96000  ?  144 PRO A N   1 
ATOM   2034 N  N   B PRO A 1 144 ? 19.04000 52.94900 8.05100   0.440 66.78000  ?  144 PRO A N   1 
ATOM   2035 C  CA  A PRO A 1 144 ? 20.10700 53.88500 8.66600   0.560 64.86000  ?  144 PRO A CA  1 
ATOM   2036 C  CA  B PRO A 1 144 ? 20.09500 53.80200 8.62600   0.440 64.92000  ?  144 PRO A CA  1 
ATOM   2037 C  C   A PRO A 1 144 ? 21.41200 54.22200 7.96000   0.560 62.89000  ?  144 PRO A C   1 
ATOM   2038 C  C   B PRO A 1 144 ? 21.27200 54.19800 7.75600   0.440 63.96000  ?  144 PRO A C   1 
ATOM   2039 O  O   A PRO A 1 144 ? 21.80500 55.39500 7.93500   0.560 65.14000  ?  144 PRO A O   1 
ATOM   2040 O  O   B PRO A 1 144 ? 21.45600 55.39100 7.48000   0.440 65.60000  ?  144 PRO A O   1 
ATOM   2041 C  CB  A PRO A 1 144 ? 20.35200 53.13900 9.98500   0.560 65.47000  ?  144 PRO A CB  1 
ATOM   2042 C  CB  B PRO A 1 144 ? 20.57100 52.95700 9.81200   0.440 64.81000  ?  144 PRO A CB  1 
ATOM   2043 C  CG  A PRO A 1 144 ? 19.11600 52.31200 10.18200  0.560 66.48000  ?  144 PRO A CG  1 
ATOM   2044 C  CG  B PRO A 1 144 ? 19.34800 52.29200 10.25100  0.440 66.44000  ?  144 PRO A CG  1 
ATOM   2045 C  CD  A PRO A 1 144 ? 18.61400 51.94500 8.80300   0.560 61.74000  ?  144 PRO A CD  1 
ATOM   2046 C  CD  B PRO A 1 144 ? 18.46500 52.05500 9.05800   0.440 62.48000  ?  144 PRO A CD  1 
ATOM   2047 N  N   A MET A 1 145 ? 22.10400 53.23300 7.39200   0.560 68.00000  ?  145 MET A N   1 
ATOM   2048 N  N   B MET A 1 145 ? 22.09400 53.22600 7.34800   0.440 67.77000  ?  145 MET A N   1 
ATOM   2049 C  CA  A MET A 1 145 ? 23.36700 53.52600 6.72300   0.560 66.93000  ?  145 MET A CA  1 
ATOM   2050 C  CA  B MET A 1 145 ? 23.23500 53.56300 6.50300   0.440 66.78000  ?  145 MET A CA  1 
ATOM   2051 C  C   A MET A 1 145 ? 23.15000 54.35400 5.46500   0.560 67.52000  ?  145 MET A C   1 
ATOM   2052 C  C   B MET A 1 145 ? 22.77900 54.28000 5.24100   0.440 64.87000  ?  145 MET A C   1 
ATOM   2053 O  O   A MET A 1 145 ? 24.00200 55.17800 5.11300   0.560 66.33000  ?  145 MET A O   1 
ATOM   2054 O  O   B MET A 1 145 ? 23.46300 55.19700 4.77900   0.440 66.54000  ?  145 MET A O   1 
ATOM   2055 C  CB  A MET A 1 145 ? 24.09800 52.22200 6.40500   0.560 55.37000  ?  145 MET A CB  1 
ATOM   2056 C  CB  B MET A 1 145 ? 24.03200 52.32100 6.12900   0.440 55.48000  ?  145 MET A CB  1 
ATOM   2057 C  CG  A MET A 1 145 ? 24.49200 51.45400 7.66000   0.560 60.73000  ?  145 MET A CG  1 
ATOM   2058 C  CG  B MET A 1 145 ? 24.37200 51.42100 7.29000   0.440 60.97000  ?  145 MET A CG  1 
ATOM   2059 S  SD  A MET A 1 145 ? 25.43000 49.94200 7.37200   0.560 57.57000  ?  145 MET A SD  1 
ATOM   2060 S  SD  B MET A 1 145 ? 25.27100 49.99700 6.70400   0.440 61.88000  ?  145 MET A SD  1 
ATOM   2061 C  CE  A MET A 1 145 ? 26.77800 50.56000 6.37300   0.560 55.90000  ?  145 MET A CE  1 
ATOM   2062 C  CE  B MET A 1 145 ? 26.69800 50.77600 5.96800   0.440 58.49000  ?  145 MET A CE  1 
ATOM   2063 N  N   A THR A 1 146 ? 22.01700 54.16700 4.78400   0.560 60.37000  ?  146 THR A N   1 
ATOM   2064 N  N   B THR A 1 146 ? 21.61500 53.90800 4.68700   0.440 60.10000  ?  146 THR A N   1 
ATOM   2065 C  CA  A THR A 1 146 ? 21.73500 54.97700 3.60400   0.560 66.73000  ?  146 THR A CA  1 
ATOM   2066 C  CA  B THR A 1 146 ? 21.10300 54.65100 3.53400   0.440 65.73000  ?  146 THR A CA  1 
ATOM   2067 C  C   A THR A 1 146 ? 21.37000 56.40500 3.99400   0.560 70.10000  ?  146 THR A C   1 
ATOM   2068 C  C   B THR A 1 146 ? 20.80000 56.09100 3.91800   0.440 69.00000  ?  146 THR A C   1 
ATOM   2069 O  O   A THR A 1 146 ? 21.80400 57.36200 3.34300   0.560 73.66000  ?  146 THR A O   1 
ATOM   2070 O  O   B THR A 1 146 ? 21.26700 57.02600 3.26000   0.440 71.92000  ?  146 THR A O   1 
ATOM   2071 C  CB  A THR A 1 146 ? 20.62000 54.33800 2.77800   0.560 60.31000  ?  146 THR A CB  1 
ATOM   2072 C  CB  B THR A 1 146 ? 19.85300 53.99900 2.94500   0.440 59.55000  ?  146 THR A CB  1 
ATOM   2073 O  OG1 A THR A 1 146 ? 21.03700 53.03300 2.35700   0.560 56.50000  ?  146 THR A OG1 1 
ATOM   2074 O  OG1 B THR A 1 146 ? 20.19000 52.72500 2.39600   0.440 55.35000  ?  146 THR A OG1 1 
ATOM   2075 C  CG2 A THR A 1 146 ? 20.30300 55.19200 1.55600   0.560 55.11000  ?  146 THR A CG2 1 
ATOM   2076 C  CG2 B THR A 1 146 ? 19.27100 54.88700 1.85100   0.440 61.17000  ?  146 THR A CG2 1 
ATOM   2077 N  N   A GLU A 1 147 ? 20.57500 56.57300 5.05500   0.560 66.61000  ?  147 GLU A N   1 
ATOM   2078 N  N   B GLU A 1 147 ? 20.02200 56.29200 4.97600   0.440 65.97000  ?  147 GLU A N   1 
ATOM   2079 C  CA  A GLU A 1 147 ? 20.33500 57.91300 5.58100   0.560 81.87000  ?  147 GLU A CA  1 
ATOM   2080 C  CA  B GLU A 1 147 ? 19.88900 57.63900 5.51100   0.440 81.18000  ?  147 GLU A CA  1 
ATOM   2081 C  C   A GLU A 1 147 ? 21.65800 58.60600 5.87700   0.560 74.93000  ?  147 GLU A C   1 
ATOM   2082 C  C   B GLU A 1 147 ? 21.27500 58.22300 5.72000   0.440 76.80000  ?  147 GLU A C   1 
ATOM   2083 O  O   A GLU A 1 147 ? 21.86500 59.77100 5.51200   0.560 81.92000  ?  147 GLU A O   1 
ATOM   2084 O  O   B GLU A 1 147 ? 21.65300 59.22600 5.10500   0.440 79.16000  ?  147 GLU A O   1 
ATOM   2085 C  CB  A GLU A 1 147 ? 19.45800 57.84800 6.83900   0.560 83.17000  ?  147 GLU A CB  1 
ATOM   2086 C  CB  B GLU A 1 147 ? 19.13600 57.64100 6.83900   0.440 82.87000  ?  147 GLU A CB  1 
ATOM   2087 C  CG  A GLU A 1 147 ? 18.07900 57.22000 6.63600   0.560 92.35000  ?  147 GLU A CG  1 
ATOM   2088 C  CG  B GLU A 1 147 ? 17.72800 57.10300 6.79700   0.440 92.66000  ?  147 GLU A CG  1 
ATOM   2089 C  CD  A GLU A 1 147 ? 16.99900 57.87700 7.48400   0.560 115.14000 ?  147 GLU A CD  1 
ATOM   2090 C  CD  B GLU A 1 147 ? 16.84700 57.73500 7.87700   0.440 115.37000 ?  147 GLU A CD  1 
ATOM   2091 O  OE1 A GLU A 1 147 ? 16.49500 58.94500 7.08000   0.560 125.63000 ?  147 GLU A OE1 1 
ATOM   2092 O  OE1 B GLU A 1 147 ? 16.32900 58.85600 7.67100   0.440 123.66000 ?  147 GLU A OE1 1 
ATOM   2093 O  OE2 A GLU A 1 147 ? 16.65500 57.32900 8.55300   0.560 116.16000 -1 147 GLU A OE2 1 
ATOM   2094 O  OE2 B GLU A 1 147 ? 16.69700 57.11000 8.95300   0.440 114.37000 -1 147 GLU A OE2 1 
ATOM   2095 N  N   A SER A 1 148 ? 22.57200 57.89400 6.54400   0.560 73.09000  ?  148 SER A N   1 
ATOM   2096 N  N   B SER A 1 148 ? 22.04700 57.54700 6.56200   0.440 73.82000  ?  148 SER A N   1 
ATOM   2097 C  CA  A SER A 1 148 ? 23.84000 58.49700 6.94200   0.560 76.09000  ?  148 SER A CA  1 
ATOM   2098 C  CA  B SER A 1 148 ? 23.33200 58.07500 6.97800   0.440 74.05000  ?  148 SER A CA  1 
ATOM   2099 C  C   A SER A 1 148 ? 24.68400 58.86200 5.72300   0.560 75.87000  ?  148 SER A C   1 
ATOM   2100 C  C   B SER A 1 148 ? 24.16200 58.50200 5.77300   0.440 75.46000  ?  148 SER A C   1 
ATOM   2101 O  O   A SER A 1 148 ? 25.23700 59.96600 5.64500   0.560 75.62000  ?  148 SER A O   1 
ATOM   2102 O  O   B SER A 1 148 ? 24.82700 59.53700 5.79600   0.440 76.24000  ?  148 SER A O   1 
ATOM   2103 C  CB  A SER A 1 148 ? 24.59800 57.54600 7.87100   0.560 66.05000  ?  148 SER A CB  1 
ATOM   2104 C  CB  B SER A 1 148 ? 24.04200 57.01800 7.83000   0.440 66.87000  ?  148 SER A CB  1 
ATOM   2105 O  OG  A SER A 1 148 ? 25.98200 57.84700 7.90800   0.560 74.65000  ?  148 SER A OG  1 
ATOM   2106 O  OG  B SER A 1 148 ? 25.37700 57.35600 8.06500   0.440 68.75000  ?  148 SER A OG  1 
ATOM   2107 N  N   A ALA A 1 149 ? 24.79400 57.94700 4.75700   0.560 76.26000  ?  149 ALA A N   1 
ATOM   2108 N  N   B ALA A 1 149 ? 24.10700 57.75000 4.69400   0.440 76.15000  ?  149 ALA A N   1 
ATOM   2109 C  CA  A ALA A 1 149 ? 25.55800 58.23700 3.54800   0.560 75.80000  ?  149 ALA A CA  1 
ATOM   2110 C  CA  B ALA A 1 149 ? 24.96100 58.11400 3.57600   0.440 75.64000  ?  149 ALA A CA  1 
ATOM   2111 C  C   A ALA A 1 149 ? 25.01600 59.44800 2.80100   0.560 80.57000  ?  149 ALA A C   1 
ATOM   2112 C  C   B ALA A 1 149 ? 24.35200 59.17600 2.68100   0.440 79.10000  ?  149 ALA A C   1 
ATOM   2113 O  O   A ALA A 1 149 ? 25.74400 60.05000 2.00300   0.560 84.44000  ?  149 ALA A O   1 
ATOM   2114 O  O   B ALA A 1 149 ? 25.05800 59.72800 1.83100   0.440 84.12000  ?  149 ALA A O   1 
ATOM   2115 C  CB  A ALA A 1 149 ? 25.55800 57.02300 2.61600   0.560 60.33000  ?  149 ALA A CB  1 
ATOM   2116 C  CB  B ALA A 1 149 ? 25.29000 56.88200 2.74200   0.440 61.07000  ?  149 ALA A CB  1 
ATOM   2117 N  N   A SER A 1 150 ? 23.75600 59.81600 3.03700   0.560 77.87000  ?  150 SER A N   1 
ATOM   2118 N  N   B SER A 1 150 ? 23.06800 59.46900 2.81900   0.440 75.97000  ?  150 SER A N   1 
ATOM   2119 C  CA  A SER A 1 150 ? 23.17200 60.94300 2.32100   0.560 85.15000  ?  150 SER A CA  1 
ATOM   2120 C  CA  B SER A 1 150 ? 22.55100 60.58400 2.06000   0.440 84.52000  ?  150 SER A CA  1 
ATOM   2121 C  C   A SER A 1 150 ? 23.86100 62.25400 2.67200   0.560 94.01000  ?  150 SER A C   1 
ATOM   2122 C  C   B SER A 1 150 ? 23.18300 61.90100 2.50200   0.440 92.36000  ?  150 SER A C   1 
ATOM   2123 O  O   A SER A 1 150 ? 23.88000 63.18000 1.85200   0.560 117.54000 ?  150 SER A O   1 
ATOM   2124 O  O   B SER A 1 150 ? 22.99700 62.91600 1.82000   0.440 110.62000 ?  150 SER A O   1 
ATOM   2125 C  CB  A SER A 1 150 ? 21.67700 61.03600 2.62600   0.560 89.02000  ?  150 SER A CB  1 
ATOM   2126 C  CB  B SER A 1 150 ? 21.03900 60.61800 2.19600   0.440 89.11000  ?  150 SER A CB  1 
ATOM   2127 O  OG  A SER A 1 150 ? 21.43800 61.91600 3.71100   0.560 92.98000  ?  150 SER A OG  1 
ATOM   2128 O  OG  B SER A 1 150 ? 20.66500 61.43300 3.28600   0.440 93.15000  ?  150 SER A OG  1 
ATOM   2129 N  N   A GLN A 1 151 ? 24.43200 62.35500 3.87300   0.560 99.04000  ?  151 GLN A N   1 
ATOM   2130 N  N   B GLN A 1 151 ? 23.93800 61.89900 3.61900   0.440 97.12000  ?  151 GLN A N   1 
ATOM   2131 C  CA  A GLN A 1 151 ? 25.08000 63.59000 4.29700   0.560 97.96000  ?  151 GLN A CA  1 
ATOM   2132 C  CA  B GLN A 1 151 ? 24.60500 63.09800 4.14000   0.440 98.26000  ?  151 GLN A CA  1 
ATOM   2133 C  C   A GLN A 1 151 ? 26.40200 63.84600 3.58200   0.560 91.20000  ?  151 GLN A C   1 
ATOM   2134 C  C   B GLN A 1 151 ? 25.84100 63.51500 3.33700   0.440 92.27000  ?  151 GLN A C   1 
ATOM   2135 O  O   A GLN A 1 151 ? 27.01200 64.89600 3.80200   0.560 91.38000  ?  151 GLN A O   1 
ATOM   2136 O  O   B GLN A 1 151 ? 26.26600 64.66800 3.46100   0.440 90.91000  ?  151 GLN A O   1 
ATOM   2137 C  CB  A GLN A 1 151 ? 25.32100 63.56700 5.80900   0.560 99.84000  ?  151 GLN A CB  1 
ATOM   2138 C  CB  B GLN A 1 151 ? 25.10800 62.91200 5.58600   0.440 99.63000  ?  151 GLN A CB  1 
ATOM   2139 C  CG  A GLN A 1 151 ? 24.12000 63.13900 6.64200   0.560 104.26000 ?  151 GLN A CG  1 
ATOM   2140 C  CG  B GLN A 1 151 ? 24.20400 62.28800 6.66600   0.440 102.82000 ?  151 GLN A CG  1 
ATOM   2141 C  CD  A GLN A 1 151 ? 22.90300 64.01100 6.40700   0.560 109.63000 ?  151 GLN A CD  1 
ATOM   2142 C  CD  B GLN A 1 151 ? 22.99300 63.09100 7.03100   0.440 107.88000 ?  151 GLN A CD  1 
ATOM   2143 O  OE1 A GLN A 1 151 ? 22.36500 64.05800 5.30100   0.560 114.41000 ?  151 GLN A OE1 1 
ATOM   2144 O  OE1 B GLN A 1 151 ? 22.11800 63.33800 6.20600   0.440 111.69000 ?  151 GLN A OE1 1 
ATOM   2145 N  NE2 A GLN A 1 151 ? 22.45800 64.70400 7.45000   0.560 120.41000 ?  151 GLN A NE2 1 
ATOM   2146 N  NE2 B GLN A 1 151 ? 22.90500 63.45700 8.30100   0.440 114.21000 ?  151 GLN A NE2 1 
ATOM   2147 N  N   A ARG A 1 152 ? 26.86600 62.93400 2.74100   0.560 87.12000  ?  152 ARG A N   1 
ATOM   2148 N  N   B ARG A 1 152 ? 26.47700 62.60800 2.58100   0.440 86.71000  ?  152 ARG A N   1 
ATOM   2149 C  CA  A ARG A 1 152 ? 28.15700 63.07500 2.08800   0.560 91.29000  ?  152 ARG A CA  1 
ATOM   2150 C  CA  B ARG A 1 152 ? 27.77200 62.92100 1.96400   0.440 91.41000  ?  152 ARG A CA  1 
ATOM   2151 C  C   A ARG A 1 152 ? 27.98000 63.64000 0.68200   0.560 87.65000  ?  152 ARG A C   1 
ATOM   2152 C  C   B ARG A 1 152 ? 27.59600 63.75800 0.68000   0.440 88.14000  ?  152 ARG A C   1 
ATOM   2153 O  O   A ARG A 1 152 ? 26.86500 63.82300 0.18900   0.560 85.14000  ?  152 ARG A O   1 
ATOM   2154 O  O   B ARG A 1 152 ? 26.48400 64.17000 0.30400   0.440 83.27000  ?  152 ARG A O   1 
ATOM   2155 C  CB  A ARG A 1 152 ? 28.88400 61.72600 2.04600   0.560 95.77000  ?  152 ARG A CB  1 
ATOM   2156 C  CB  B ARG A 1 152 ? 28.58400 61.63300 1.69600   0.440 94.83000  ?  152 ARG A CB  1 
ATOM   2157 C  CG  A ARG A 1 152 ? 28.89900 60.99300 3.38300   0.560 86.77000  ?  152 ARG A CG  1 
ATOM   2158 C  CG  B ARG A 1 152 ? 28.83600 60.65500 2.88700   0.440 85.49000  ?  152 ARG A CG  1 
ATOM   2159 C  CD  A ARG A 1 152 ? 30.18000 61.26600 4.16700   0.560 89.59000  ?  152 ARG A CD  1 
ATOM   2160 C  CD  B ARG A 1 152 ? 30.20100 60.86200 3.59800   0.440 88.53000  ?  152 ARG A CD  1 
ATOM   2161 N  NE  A ARG A 1 152 ? 31.22200 60.28700 3.86500   0.560 98.22000  ?  152 ARG A NE  1 
ATOM   2162 N  NE  B ARG A 1 152 ? 31.27200 59.95000 3.19100   0.440 97.65000  ?  152 ARG A NE  1 
ATOM   2163 C  CZ  A ARG A 1 152 ? 32.47900 60.37100 4.28700   0.560 109.42000 ?  152 ARG A CZ  1 
ATOM   2164 C  CZ  B ARG A 1 152 ? 32.53300 59.99500 3.62800   0.440 105.59000 ?  152 ARG A CZ  1 
ATOM   2165 N  NH1 A ARG A 1 152 ? 32.86500 61.39200 5.03900   0.560 122.33000 ?  152 ARG A NH1 1 
ATOM   2166 N  NH1 B ARG A 1 152 ? 32.93500 60.89300 4.51700   0.440 114.53000 ?  152 ARG A NH1 1 
ATOM   2167 N  NH2 A ARG A 1 152 ? 33.35300 59.43100 3.95500   0.560 104.68000 ?  152 ARG A NH2 1 
ATOM   2168 N  NH2 B ARG A 1 152 ? 33.41800 59.11000 3.16700   0.440 101.13000 ?  152 ARG A NH2 1 
ATOM   2169 N  N   A SER A 1 153 ? 29.11200 63.93100 0.04100   0.560 85.24000  ?  153 SER A N   1 
ATOM   2170 N  N   B SER A 1 153 ? 28.71000 64.03400 -0.00000  0.440 86.18000  ?  153 SER A N   1 
ATOM   2171 C  CA  A SER A 1 153 ? 29.10800 64.46600 -1.31500  0.560 88.48000  ?  153 SER A CA  1 
ATOM   2172 C  CA  B SER A 1 153 ? 28.57100 64.51900 -1.36000  0.440 87.34000  ?  153 SER A CA  1 
ATOM   2173 C  C   A SER A 1 153 ? 28.27400 63.57200 -2.22300  0.560 89.27000  ?  153 SER A C   1 
ATOM   2174 C  C   B SER A 1 153 ? 27.72400 63.52800 -2.15600  0.440 90.78000  ?  153 SER A C   1 
ATOM   2175 O  O   A SER A 1 153 ? 28.02400 62.41000 -1.89700  0.560 92.61000  ?  153 SER A O   1 
ATOM   2176 O  O   B SER A 1 153 ? 27.53300 62.36300 -1.77700  0.440 92.66000  ?  153 SER A O   1 
ATOM   2177 C  CB  A SER A 1 153 ? 30.53300 64.58300 -1.85100  0.560 91.91000  ?  153 SER A CB  1 
ATOM   2178 C  CB  B SER A 1 153 ? 29.93800 64.68600 -2.02600  0.440 90.70000  ?  153 SER A CB  1 
ATOM   2179 O  OG  A SER A 1 153 ? 31.02300 63.31700 -2.25600  0.560 93.13000  ?  153 SER A OG  1 
ATOM   2180 O  OG  B SER A 1 153 ? 30.40300 63.46700 -2.58700  0.440 88.55000  ?  153 SER A OG  1 
ATOM   2181 N  N   A SER A 1 154 ? 27.83600 64.09700 -3.36600  0.560 98.76000  ?  154 SER A N   1 
ATOM   2182 N  N   B SER A 1 154 ? 27.17700 64.00300 -3.26000  0.440 96.10000  ?  154 SER A N   1 
ATOM   2183 C  CA  A SER A 1 154 ? 26.99000 63.30400 -4.24900  0.560 100.63000 ?  154 SER A CA  1 
ATOM   2184 C  CA  B SER A 1 154 ? 26.32200 63.11300 -4.02900  0.440 100.44000 ?  154 SER A CA  1 
ATOM   2185 C  C   A SER A 1 154 ? 27.75800 62.13000 -4.83900  0.560 92.40000  ?  154 SER A C   1 
ATOM   2186 C  C   B SER A 1 154 ? 27.13900 62.03900 -4.76100  0.440 93.79000  ?  154 SER A C   1 
ATOM   2187 O  O   A SER A 1 154 ? 27.15900 61.08300 -5.12600  0.560 87.36000  ?  154 SER A O   1 
ATOM   2188 O  O   B SER A 1 154 ? 26.63200 60.93400 -5.01500  0.440 86.93000  ?  154 SER A O   1 
ATOM   2189 C  CB  A SER A 1 154 ? 26.39900 64.19700 -5.34300  0.560 107.43000 ?  154 SER A CB  1 
ATOM   2190 C  CB  B SER A 1 154 ? 25.48100 63.93600 -4.99200  0.440 106.93000 ?  154 SER A CB  1 
ATOM   2191 O  OG  A SER A 1 154 ? 25.17900 63.65100 -5.82300  0.560 112.89000 ?  154 SER A OG  1 
ATOM   2192 O  OG  B SER A 1 154 ? 24.23400 63.32700 -5.17300  0.440 111.80000 ?  154 SER A OG  1 
ATOM   2193 N  N   A GLY A 1 155 ? 29.07100 62.27900 -5.03400  0.560 88.66000  ?  155 GLY A N   1 
ATOM   2194 N  N   B GLY A 1 155 ? 28.40100 62.33900 -5.09100  0.440 91.46000  ?  155 GLY A N   1 
ATOM   2195 C  CA  A GLY A 1 155 ? 29.84400 61.18100 -5.59100  0.560 85.87000  ?  155 GLY A CA  1 
ATOM   2196 C  CA  B GLY A 1 155 ? 29.30100 61.30500 -5.58000  0.440 86.85000  ?  155 GLY A CA  1 
ATOM   2197 C  C   A GLY A 1 155 ? 30.07000 60.05300 -4.59600  0.560 91.99000  ?  155 GLY A C   1 
ATOM   2198 C  C   B GLY A 1 155 ? 29.50400 60.20000 -4.56300  0.440 90.57000  ?  155 GLY A C   1 
ATOM   2199 O  O   A GLY A 1 155 ? 30.03200 58.87400 -4.95800  0.560 86.47000  ?  155 GLY A O   1 
ATOM   2200 O  O   B GLY A 1 155 ? 29.31100 59.02100 -4.86900  0.440 85.08000  ?  155 GLY A O   1 
ATOM   2201 N  N   A ILE A 1 156 ? 30.32400 60.39700 -3.33200  0.560 94.00000  ?  156 ILE A N   1 
ATOM   2202 N  N   B ILE A 1 156 ? 29.85700 60.57000 -3.32700  0.440 94.36000  ?  156 ILE A N   1 
ATOM   2203 C  CA  A ILE A 1 156 ? 30.46500 59.37500 -2.29700  0.560 93.72000  ?  156 ILE A CA  1 
ATOM   2204 C  CA  B ILE A 1 156 ? 29.99400 59.56000 -2.29000  0.440 93.88000  ?  156 ILE A CA  1 
ATOM   2205 C  C   A ILE A 1 156 ? 29.14500 58.64000 -2.09900  0.560 94.00000  ?  156 ILE A C   1 
ATOM   2206 C  C   B ILE A 1 156 ? 28.63900 58.94500 -1.97200  0.440 93.66000  ?  156 ILE A C   1 
ATOM   2207 O  O   A ILE A 1 156 ? 29.10600 57.40700 -2.02100  0.560 86.59000  ?  156 ILE A O   1 
ATOM   2208 O  O   B ILE A 1 156 ? 28.54600 57.73900 -1.71400  0.440 89.07000  ?  156 ILE A O   1 
ATOM   2209 C  CB  A ILE A 1 156 ? 30.95800 60.00900 -0.98400  0.560 96.35000  ?  156 ILE A CB  1 
ATOM   2210 C  CB  B ILE A 1 156 ? 30.68200 60.13700 -1.04100  0.440 95.94000  ?  156 ILE A CB  1 
ATOM   2211 C  CG1 A ILE A 1 156 ? 32.39200 60.52200 -1.14600  0.560 102.31000 ?  156 ILE A CG1 1 
ATOM   2212 C  CG1 B ILE A 1 156 ? 32.15800 60.38900 -1.33700  0.440 101.53000 ?  156 ILE A CG1 1 
ATOM   2213 C  CG2 A ILE A 1 156 ? 30.86100 59.01000 0.16300   0.560 94.38000  ?  156 ILE A CG2 1 
ATOM   2214 C  CG2 B ILE A 1 156 ? 30.55100 59.18000 0.13000   0.440 94.55000  ?  156 ILE A CG2 1 
ATOM   2215 C  CD1 A ILE A 1 156 ? 33.45900 59.50500 -0.79400  0.560 110.22000 ?  156 ILE A CD1 1 
ATOM   2216 C  CD1 B ILE A 1 156 ? 33.09800 59.23300 -0.96200  0.440 107.49000 ?  156 ILE A CD1 1 
ATOM   2217 N  N   A LYS A 1 157 ? 28.04400 59.38900 -2.01200  0.560 82.60000  ?  157 LYS A N   1 
ATOM   2218 N  N   B LYS A 1 157 ? 27.55700 59.71400 -2.04600  0.440 78.38000  ?  157 LYS A N   1 
ATOM   2219 C  CA  A LYS A 1 157 ? 26.73500 58.76100 -1.87400  0.560 81.89000  ?  157 LYS A CA  1 
ATOM   2220 C  CA  B LYS A 1 157 ? 26.27400 59.07000 -1.79400  0.440 79.51000  ?  157 LYS A CA  1 
ATOM   2221 C  C   A LYS A 1 157 ? 26.46800 57.80400 -3.02700  0.560 79.80000  ?  157 LYS A C   1 
ATOM   2222 C  C   B LYS A 1 157 ? 25.86100 58.14300 -2.92300  0.440 80.00000  ?  157 LYS A C   1 
ATOM   2223 O  O   A LYS A 1 157 ? 25.94500 56.70300 -2.82200  0.560 65.54000  ?  157 LYS A O   1 
ATOM   2224 O  O   B LYS A 1 157 ? 25.21300 57.12200 -2.66500  0.440 71.04000  ?  157 LYS A O   1 
ATOM   2225 C  CB  A LYS A 1 157 ? 25.65300 59.83700 -1.79700  0.560 80.82000  ?  157 LYS A CB  1 
ATOM   2226 C  CB  B LYS A 1 157 ? 25.16700 60.07000 -1.58000  0.440 84.51000  ?  157 LYS A CB  1 
ATOM   2227 C  CG  A LYS A 1 157 ? 24.23400 59.30200 -1.73800  0.560 78.55000  ?  157 LYS A CG  1 
ATOM   2228 C  CG  B LYS A 1 157 ? 23.87200 59.35400 -1.22900  0.440 81.30000  ?  157 LYS A CG  1 
ATOM   2229 C  CD  A LYS A 1 157 ? 23.30200 60.11600 -2.63200  0.560 93.77000  ?  157 LYS A CD  1 
ATOM   2230 C  CD  B LYS A 1 157 ? 22.77900 59.86800 -2.09500  0.440 89.13000  ?  157 LYS A CD  1 
ATOM   2231 C  CE  A LYS A 1 157 ? 23.07600 61.51800 -2.08200  0.560 109.09000 ?  157 LYS A CE  1 
ATOM   2232 C  CE  B LYS A 1 157 ? 22.79600 61.39700 -1.94100  0.440 109.82000 ?  157 LYS A CE  1 
ATOM   2233 N  NZ  A LYS A 1 157 ? 21.70800 62.02300 -2.39000  0.560 122.14000 ?  157 LYS A NZ  1 
ATOM   2234 N  NZ  B LYS A 1 157 ? 21.47500 62.06500 -1.97800  0.440 119.71000 ?  157 LYS A NZ  1 
ATOM   2235 N  N   A SER A 1 158 ? 26.83000 58.20400 -4.24900  0.560 85.95000  ?  158 SER A N   1 
ATOM   2236 N  N   B SER A 1 158 ? 26.24200 58.45100 -4.17100  0.440 86.10000  ?  158 SER A N   1 
ATOM   2237 C  CA  A SER A 1 158 ? 26.60100 57.35000 -5.41000  0.560 73.45000  ?  158 SER A CA  1 
ATOM   2238 C  CA  B SER A 1 158 ? 25.81400 57.60600 -5.28700  0.440 78.23000  ?  158 SER A CA  1 
ATOM   2239 C  C   A SER A 1 158 ? 27.42000 56.06800 -5.32200  0.560 65.56000  ?  158 SER A C   1 
ATOM   2240 C  C   B SER A 1 158 ? 26.62000 56.31500 -5.36700  0.440 65.65000  ?  158 SER A C   1 
ATOM   2241 O  O   A SER A 1 158 ? 26.92000 54.97800 -5.62500  0.560 63.21000  ?  158 SER A O   1 
ATOM   2242 O  O   B SER A 1 158 ? 26.05200 55.25300 -5.64300  0.440 61.86000  ?  158 SER A O   1 
ATOM   2243 C  CB  A SER A 1 158 ? 26.93900 58.11900 -6.68800  0.560 73.58000  ?  158 SER A CB  1 
ATOM   2244 C  CB  B SER A 1 158 ? 25.89500 58.37200 -6.61300  0.440 70.67000  ?  158 SER A CB  1 
ATOM   2245 O  OG  A SER A 1 158 ? 26.76800 57.31300 -7.84100  0.560 78.28000  ?  158 SER A OG  1 
ATOM   2246 O  OG  B SER A 1 158 ? 25.50100 57.52300 -7.67700  0.440 81.63000  ?  158 SER A OG  1 
ATOM   2247 N  N   A LEU A 1 159 ? 28.68500 56.17900 -4.91100  0.560 61.09000  ?  159 LEU A N   1 
ATOM   2248 N  N   B LEU A 1 159 ? 27.94700 56.39700 -5.17500  0.440 66.96000  ?  159 LEU A N   1 
ATOM   2249 C  CA  A LEU A 1 159 ? 29.51400 54.99200 -4.73900  0.560 65.16000  ?  159 LEU A CA  1 
ATOM   2250 C  CA  B LEU A 1 159 ? 28.75200 55.19700 -4.97000  0.440 61.52000  ?  159 LEU A CA  1 
ATOM   2251 C  C   A LEU A 1 159 ? 28.93900 54.07200 -3.67200  0.560 68.79000  ?  159 LEU A C   1 
ATOM   2252 C  C   B LEU A 1 159 ? 28.13800 54.31100 -3.86800  0.440 67.14000  ?  159 LEU A C   1 
ATOM   2253 O  O   A LEU A 1 159 ? 28.90400 52.84900 -3.85200  0.560 56.41000  ?  159 LEU A O   1 
ATOM   2254 O  O   B LEU A 1 159 ? 28.06100 53.08300 -4.02300  0.440 60.67000  ?  159 LEU A O   1 
ATOM   2255 C  CB  A LEU A 1 159 ? 30.94100 55.40200 -4.38000  0.560 71.33000  ?  159 LEU A CB  1 
ATOM   2256 C  CB  B LEU A 1 159 ? 30.21200 55.59200 -4.65100  0.440 66.26000  ?  159 LEU A CB  1 
ATOM   2257 C  CG  A LEU A 1 159 ? 31.96400 54.28300 -4.19400  0.560 73.52000  ?  159 LEU A CG  1 
ATOM   2258 C  CG  B LEU A 1 159 ? 31.35200 54.56200 -4.35600  0.440 73.71000  ?  159 LEU A CG  1 
ATOM   2259 C  CD1 A LEU A 1 159 ? 31.97600 53.37300 -5.41400  0.560 71.45000  ?  159 LEU A CD1 1 
ATOM   2260 C  CD1 B LEU A 1 159 ? 31.64400 53.51700 -5.47800  0.440 71.21000  ?  159 LEU A CD1 1 
ATOM   2261 C  CD2 A LEU A 1 159 ? 33.34700 54.86200 -3.93600  0.560 70.54000  ?  159 LEU A CD2 1 
ATOM   2262 C  CD2 B LEU A 1 159 ? 32.69400 55.17600 -3.84200  0.440 74.50000  ?  159 LEU A CD2 1 
ATOM   2263 N  N   A TYR A 1 160 ? 28.47900 54.63800 -2.55400  0.560 65.65000  ?  160 TYR A N   1 
ATOM   2264 N  N   B TYR A 1 160 ? 27.64100 54.92100 -2.76600  0.440 68.42000  ?  160 TYR A N   1 
ATOM   2265 C  CA  A TYR A 1 160 ? 27.90700 53.80400 -1.50300  0.560 64.72000  ?  160 TYR A CA  1 
ATOM   2266 C  CA  B TYR A 1 160 ? 27.04900 54.11900 -1.68100  0.440 63.63000  ?  160 TYR A CA  1 
ATOM   2267 C  C   A TYR A 1 160 ? 26.70400 53.02300 -2.02100  0.560 59.43000  ?  160 TYR A C   1 
ATOM   2268 C  C   B TYR A 1 160 ? 25.77700 53.42000 -2.10000  0.440 59.71000  ?  160 TYR A C   1 
ATOM   2269 O  O   A TYR A 1 160 ? 26.58100 51.81500 -1.78400  0.560 59.92000  ?  160 TYR A O   1 
ATOM   2270 O  O   B TYR A 1 160 ? 25.52000 52.30100 -1.65500  0.440 52.47000  ?  160 TYR A O   1 
ATOM   2271 C  CB  A TYR A 1 160 ? 27.49500 54.64900 -0.29800  0.560 63.48000  ?  160 TYR A CB  1 
ATOM   2272 C  CB  B TYR A 1 160 ? 26.67300 54.90500 -0.41100  0.440 59.21000  ?  160 TYR A CB  1 
ATOM   2273 C  CG  A TYR A 1 160 ? 26.69000 53.82800 0.68500   0.560 59.93000  ?  160 TYR A CG  1 
ATOM   2274 C  CG  B TYR A 1 160 ? 25.94600 53.94600 0.55600   0.440 55.36000  ?  160 TYR A CG  1 
ATOM   2275 C  CD1 A TYR A 1 160 ? 27.32300 52.97600 1.57800   0.560 49.95000  ?  160 TYR A CD1 1 
ATOM   2276 C  CD1 B TYR A 1 160 ? 26.66800 52.95600 1.24000   0.440 53.00000  ?  160 TYR A CD1 1 
ATOM   2277 C  CD2 A TYR A 1 160 ? 25.29900 53.86500 0.68900   0.560 54.57000  ?  160 TYR A CD2 1 
ATOM   2278 C  CD2 B TYR A 1 160 ? 24.55600 53.97300 0.74600   0.440 53.33000  ?  160 TYR A CD2 1 
ATOM   2279 C  CE1 A TYR A 1 160 ? 26.60500 52.20400 2.46200   0.560 51.07000  ?  160 TYR A CE1 1 
ATOM   2280 C  CE1 B TYR A 1 160 ? 26.06300 52.04000 2.06700   0.440 47.41000  ?  160 TYR A CE1 1 
ATOM   2281 C  CE2 A TYR A 1 160 ? 24.56800 53.08900 1.57600   0.560 55.17000  ?  160 TYR A CE2 1 
ATOM   2282 C  CE2 B TYR A 1 160 ? 23.92700 53.03200 1.64100   0.440 55.30000  ?  160 TYR A CE2 1 
ATOM   2283 C  CZ  A TYR A 1 160 ? 25.23200 52.26000 2.45900   0.560 53.69000  ?  160 TYR A CZ  1 
ATOM   2284 C  CZ  B TYR A 1 160 ? 24.72800 52.06700 2.28800   0.440 56.95000  ?  160 TYR A CZ  1 
ATOM   2285 O  OH  A TYR A 1 160 ? 24.53900 51.47900 3.35300   0.560 60.00000  ?  160 TYR A OH  1 
ATOM   2286 O  OH  B TYR A 1 160 ? 24.24500 51.09700 3.16300   0.440 56.52000  ?  160 TYR A OH  1 
ATOM   2287 N  N   A VAL A 1 161 ? 25.79800 53.70400 -2.72700  0.560 57.79000  ?  161 VAL A N   1 
ATOM   2288 N  N   B VAL A 1 161 ? 24.91000 54.07500 -2.85700  0.440 58.99000  ?  161 VAL A N   1 
ATOM   2289 C  CA  A VAL A 1 161 ? 24.58000 53.05200 -3.19900  0.560 62.25000  ?  161 VAL A CA  1 
ATOM   2290 C  CA  B VAL A 1 161 ? 23.75700 53.28900 -3.25600  0.440 60.60000  ?  161 VAL A CA  1 
ATOM   2291 C  C   A VAL A 1 161 ? 24.91800 51.90600 -4.14200  0.560 63.78000  ?  161 VAL A C   1 
ATOM   2292 C  C   B VAL A 1 161 ? 24.14300 52.31500 -4.35800  0.440 64.06000  ?  161 VAL A C   1 
ATOM   2293 O  O   A VAL A 1 161 ? 24.26500 50.85600 -4.12500  0.560 60.74000  ?  161 VAL A O   1 
ATOM   2294 O  O   B VAL A 1 161 ? 23.55600 51.22900 -4.44800  0.440 65.75000  ?  161 VAL A O   1 
ATOM   2295 C  CB  A VAL A 1 161 ? 23.65200 54.08300 -3.87000  0.560 65.84000  ?  161 VAL A CB  1 
ATOM   2296 C  CB  B VAL A 1 161 ? 22.55400 54.15900 -3.62000  0.440 66.12000  ?  161 VAL A CB  1 
ATOM   2297 C  CG1 A VAL A 1 161 ? 22.58900 53.38600 -4.70900  0.560 58.27000  ?  161 VAL A CG1 1 
ATOM   2298 C  CG1 B VAL A 1 161 ? 21.70200 53.46100 -4.63100  0.440 63.53000  ?  161 VAL A CG1 1 
ATOM   2299 C  CG2 A VAL A 1 161 ? 23.01100 54.98300 -2.82100  0.560 66.12000  ?  161 VAL A CG2 1 
ATOM   2300 C  CG2 B VAL A 1 161 ? 21.72700 54.35300 -2.37000  0.440 65.03000  ?  161 VAL A CG2 1 
ATOM   2301 N  N   A ARG A 1 162 ? 25.93600 52.08300 -4.98300  0.560 66.01000  ?  162 ARG A N   1 
ATOM   2302 N  N   B ARG A 1 162 ? 25.18200 52.60000 -5.14500  0.440 62.13000  ?  162 ARG A N   1 
ATOM   2303 C  CA  A ARG A 1 162 ? 26.26800 51.03300 -5.94000  0.560 68.48000  ?  162 ARG A CA  1 
ATOM   2304 C  CA  B ARG A 1 162 ? 25.59700 51.53200 -6.05300  0.440 67.69000  ?  162 ARG A CA  1 
ATOM   2305 C  C   A ARG A 1 162 ? 26.91700 49.83900 -5.24400  0.560 57.73000  ?  162 ARG A C   1 
ATOM   2306 C  C   B ARG A 1 162 ? 26.05700 50.32700 -5.22000  0.440 58.78000  ?  162 ARG A C   1 
ATOM   2307 O  O   A ARG A 1 162 ? 26.57800 48.68700 -5.53700  0.560 47.24000  ?  162 ARG A O   1 
ATOM   2308 O  O   B ARG A 1 162 ? 25.39200 49.27900 -5.23900  0.440 57.03000  ?  162 ARG A O   1 
ATOM   2309 C  CB  A ARG A 1 162 ? 27.15100 51.60900 -7.04800  0.560 63.68000  ?  162 ARG A CB  1 
ATOM   2310 C  CB  B ARG A 1 162 ? 26.67200 52.00700 -7.06000  0.440 67.62000  ?  162 ARG A CB  1 
ATOM   2311 C  CG  A ARG A 1 162 ? 26.37300 52.51800 -7.99900  0.560 76.77000  ?  162 ARG A CG  1 
ATOM   2312 C  CG  B ARG A 1 162 ? 26.16600 53.07500 -8.07900  0.440 78.66000  ?  162 ARG A CG  1 
ATOM   2313 C  CD  A ARG A 1 162 ? 26.81200 52.35500 -9.46200  0.560 90.70000  ?  162 ARG A CD  1 
ATOM   2314 C  CD  B ARG A 1 162 ? 26.57000 52.79500 -9.52400  0.440 91.21000  ?  162 ARG A CD  1 
ATOM   2315 N  NE  A ARG A 1 162 ? 26.31100 51.10900 -10.02300 0.560 105.10000 ?  162 ARG A NE  1 
ATOM   2316 N  NE  B ARG A 1 162 ? 25.88200 51.60900 -10.02400 0.440 102.48000 ?  162 ARG A NE  1 
ATOM   2317 C  CZ  A ARG A 1 162 ? 27.08200 50.17400 -10.56600 0.560 110.04000 ?  162 ARG A CZ  1 
ATOM   2318 C  CZ  B ARG A 1 162 ? 26.48800 50.55100 -10.54800 0.440 107.81000 ?  162 ARG A CZ  1 
ATOM   2319 N  NH1 A ARG A 1 162 ? 28.39100 50.34400 -10.64800 0.560 112.49000 ?  162 ARG A NH1 1 
ATOM   2320 N  NH1 B ARG A 1 162 ? 27.78300 50.56100 -10.82300 0.440 112.17000 ?  162 ARG A NH1 1 
ATOM   2321 N  NH2 A ARG A 1 162 ? 26.54500 49.06600 -11.03700 0.560 101.26000 ?  162 ARG A NH2 1 
ATOM   2322 N  NH2 B ARG A 1 162 ? 25.77900 49.45400 -10.80400 0.440 102.04000 ?  162 ARG A NH2 1 
ATOM   2323 N  N   A LEU A 1 163 ? 27.81200 50.08400 -4.28500  0.560 54.66000  ?  163 LEU A N   1 
ATOM   2324 N  N   B LEU A 1 163 ? 27.14100 50.48700 -4.44400  0.440 53.78000  ?  163 LEU A N   1 
ATOM   2325 C  CA  A LEU A 1 163 ? 28.38800 48.96800 -3.53800  0.560 61.29000  ?  163 LEU A CA  1 
ATOM   2326 C  CA  B LEU A 1 163 ? 27.71600 49.36500 -3.71000  0.440 59.80000  ?  163 LEU A CA  1 
ATOM   2327 C  C   A LEU A 1 163 ? 27.34600 48.31700 -2.63500  0.560 54.22000  ?  163 LEU A C   1 
ATOM   2328 C  C   B LEU A 1 163 ? 26.69000 48.65200 -2.79300  0.440 53.74000  ?  163 LEU A C   1 
ATOM   2329 O  O   A LEU A 1 163 ? 27.32400 47.08900 -2.48200  0.560 48.21000  ?  163 LEU A O   1 
ATOM   2330 O  O   B LEU A 1 163 ? 26.84300 47.44400 -2.53200  0.440 50.57000  ?  163 LEU A O   1 
ATOM   2331 C  CB  A LEU A 1 163 ? 29.58600 49.44600 -2.72300  0.560 55.76000  ?  163 LEU A CB  1 
ATOM   2332 C  CB  B LEU A 1 163 ? 28.96800 49.85500 -2.95800  0.440 56.36000  ?  163 LEU A CB  1 
ATOM   2333 C  CG  A LEU A 1 163 ? 30.81900 49.82400 -3.54500  0.560 58.95000  ?  163 LEU A CG  1 
ATOM   2334 C  CG  B LEU A 1 163 ? 30.18500 50.13000 -3.83200  0.440 57.75000  ?  163 LEU A CG  1 
ATOM   2335 C  CD1 A LEU A 1 163 ? 31.90000 50.42800 -2.66300  0.560 63.02000  ?  163 LEU A CD1 1 
ATOM   2336 C  CD1 B LEU A 1 163 ? 31.30200 50.77800 -3.04100  0.440 60.67000  ?  163 LEU A CD1 1 
ATOM   2337 C  CD2 A LEU A 1 163 ? 31.36000 48.62100 -4.30800  0.560 51.60000  ?  163 LEU A CD2 1 
ATOM   2338 C  CD2 B LEU A 1 163 ? 30.69400 48.88500 -4.47200  0.440 53.50000  ?  163 LEU A CD2 1 
ATOM   2339 N  N   A ARG A 1 164 ? 26.46800 49.12400 -2.03600  0.560 49.78000  ?  164 ARG A N   1 
ATOM   2340 N  N   B ARG A 1 164 ? 25.60400 49.33600 -2.39600  0.440 52.83000  ?  164 ARG A N   1 
ATOM   2341 C  CA  A ARG A 1 164 ? 25.41400 48.57500 -1.19100  0.560 49.99000  ?  164 ARG A CA  1 
ATOM   2342 C  CA  B ARG A 1 164 ? 24.60200 48.74900 -1.50300  0.440 53.16000  ?  164 ARG A CA  1 
ATOM   2343 C  C   A ARG A 1 164 ? 24.52200 47.61400 -1.97100  0.560 47.98000  ?  164 ARG A C   1 
ATOM   2344 C  C   B ARG A 1 164 ? 23.68100 47.77900 -2.24400  0.440 49.95000  ?  164 ARG A C   1 
ATOM   2345 O  O   A ARG A 1 164 ? 24.20900 46.52200 -1.49500  0.560 47.35000  ?  164 ARG A O   1 
ATOM   2346 O  O   B ARG A 1 164 ? 23.45200 46.64500 -1.78700  0.440 44.71000  ?  164 ARG A O   1 
ATOM   2347 C  CB  A ARG A 1 164 ? 24.58500 49.70900 -0.58700  0.560 50.25000  ?  164 ARG A CB  1 
ATOM   2348 C  CB  B ARG A 1 164 ? 23.80400 49.87100 -0.81600  0.440 53.18000  ?  164 ARG A CB  1 
ATOM   2349 C  CG  A ARG A 1 164 ? 23.36700 49.26000 0.21000   0.560 45.75000  ?  164 ARG A CG  1 
ATOM   2350 C  CG  B ARG A 1 164 ? 22.67200 49.46900 0.15100   0.440 45.39000  ?  164 ARG A CG  1 
ATOM   2351 C  CD  A ARG A 1 164 ? 22.30200 50.35500 0.21400   0.560 51.17000  ?  164 ARG A CD  1 
ATOM   2352 C  CD  B ARG A 1 164 ? 21.55200 50.52100 0.26300   0.440 56.36000  ?  164 ARG A CD  1 
ATOM   2353 N  NE  A ARG A 1 164 ? 21.58700 50.41500 -1.05800  0.560 67.91000  ?  164 ARG A NE  1 
ATOM   2354 N  NE  B ARG A 1 164 ? 20.61500 50.45600 -0.86500  0.440 64.43000  ?  164 ARG A NE  1 
ATOM   2355 C  CZ  A ARG A 1 164 ? 20.59000 51.25300 -1.32100  0.560 71.48000  ?  164 ARG A CZ  1 
ATOM   2356 C  CZ  B ARG A 1 164 ? 19.59100 51.28300 -1.08400  0.440 72.25000  ?  164 ARG A CZ  1 
ATOM   2357 N  NH1 A ARG A 1 164 ? 20.18000 52.11200 -0.39800  0.560 71.67000  ?  164 ARG A NH1 1 
ATOM   2358 N  NH1 B ARG A 1 164 ? 19.33300 52.31400 -0.28000  0.440 61.59000  ?  164 ARG A NH1 1 
ATOM   2359 N  NH2 A ARG A 1 164 ? 20.00000 51.23100 -2.50800  0.560 63.88000  ?  164 ARG A NH2 1 
ATOM   2360 N  NH2 B ARG A 1 164 ? 18.82800 51.09700 -2.16200  0.440 73.98000  ?  164 ARG A NH2 1 
ATOM   2361 N  N   A ASN A 1 165 ? 24.08500 48.00500 -3.16500  0.560 48.27000  ?  165 ASN A N   1 
ATOM   2362 N  N   B ASN A 1 165 ? 23.14900 48.21100 -3.38900  0.440 52.48000  ?  165 ASN A N   1 
ATOM   2363 C  CA  A ASN A 1 165 ? 23.17900 47.12800 -3.89800  0.560 53.20000  ?  165 ASN A CA  1 
ATOM   2364 C  CA  B ASN A 1 165 ? 22.26000 47.36100 -4.17800  0.440 51.42000  ?  165 ASN A CA  1 
ATOM   2365 C  C   A ASN A 1 165 ? 23.90600 45.88700 -4.38000  0.560 47.42000  ?  165 ASN A C   1 
ATOM   2366 C  C   B ASN A 1 165 ? 22.96300 46.07400 -4.57600  0.440 49.46000  ?  165 ASN A C   1 
ATOM   2367 O  O   A ASN A 1 165 ? 23.34000 44.78200 -4.31200  0.560 46.41000  ?  165 ASN A O   1 
ATOM   2368 O  O   B ASN A 1 165 ? 22.43400 44.97200 -4.36200  0.440 46.98000  ?  165 ASN A O   1 
ATOM   2369 C  CB  A ASN A 1 165 ? 22.47900 47.91400 -5.01000  0.560 57.07000  ?  165 ASN A CB  1 
ATOM   2370 C  CB  B ASN A 1 165 ? 21.79200 48.09900 -5.43900  0.440 59.85000  ?  165 ASN A CB  1 
ATOM   2371 C  CG  A ASN A 1 165 ? 21.53100 48.97900 -4.43500  0.560 63.19000  ?  165 ASN A CG  1 
ATOM   2372 C  CG  B ASN A 1 165 ? 20.84600 49.23700 -5.14300  0.440 63.54000  ?  165 ASN A CG  1 
ATOM   2373 O  OD1 A ASN A 1 165 ? 20.98000 48.83800 -3.33500  0.560 66.17000  ?  165 ASN A OD1 1 
ATOM   2374 O  OD1 B ASN A 1 165 ? 20.15700 49.26100 -4.12600  0.440 56.79000  ?  165 ASN A OD1 1 
ATOM   2375 N  ND2 A ASN A 1 165 ? 21.36600 50.05600 -5.17300  0.560 64.60000  ?  165 ASN A ND2 1 
ATOM   2376 N  ND2 B ASN A 1 165 ? 20.77500 50.17200 -6.06700  0.440 65.49000  ?  165 ASN A ND2 1 
ATOM   2377 N  N   A LEU A 1 166 ? 25.14300 46.03700 -4.87500  0.560 46.87000  ?  166 LEU A N   1 
ATOM   2378 N  N   B LEU A 1 166 ? 24.15100 46.20700 -5.19400  0.440 49.51000  ?  166 LEU A N   1 
ATOM   2379 C  CA  A LEU A 1 166 ? 25.93100 44.84700 -5.17000  0.560 52.31000  ?  166 LEU A CA  1 
ATOM   2380 C  CA  B LEU A 1 166 ? 25.01600 45.05900 -5.43100  0.440 50.12000  ?  166 LEU A CA  1 
ATOM   2381 C  C   A LEU A 1 166 ? 25.95400 43.91200 -3.95900  0.560 47.95000  ?  166 LEU A C   1 
ATOM   2382 C  C   B LEU A 1 166 ? 25.03200 44.16600 -4.19000  0.440 48.96000  ?  166 LEU A C   1 
ATOM   2383 O  O   A LEU A 1 166 ? 25.75200 42.69700 -4.08100  0.560 33.75000  ?  166 LEU A O   1 
ATOM   2384 O  O   B LEU A 1 166 ? 24.50600 43.04400 -4.20300  0.440 41.46000  ?  166 LEU A O   1 
ATOM   2385 C  CB  A LEU A 1 166 ? 27.35700 45.21500 -5.57800  0.560 56.52000  ?  166 LEU A CB  1 
ATOM   2386 C  CB  B LEU A 1 166 ? 26.43400 45.53100 -5.73400  0.440 52.83000  ?  166 LEU A CB  1 
ATOM   2387 C  CG  A LEU A 1 166 ? 28.28000 44.04200 -5.93000  0.560 61.89000  ?  166 LEU A CG  1 
ATOM   2388 C  CG  B LEU A 1 166 ? 27.54800 44.59600 -6.19300  0.440 54.62000  ?  166 LEU A CG  1 
ATOM   2389 C  CD1 A LEU A 1 166 ? 27.99000 43.56200 -7.34700  0.560 46.77000  ?  166 LEU A CD1 1 
ATOM   2390 C  CD1 B LEU A 1 166 ? 28.02600 44.94700 -7.54200  0.440 49.80000  ?  166 LEU A CD1 1 
ATOM   2391 C  CD2 A LEU A 1 166 ? 29.74400 44.42500 -5.78700  0.560 63.81000  ?  166 LEU A CD2 1 
ATOM   2392 C  CD2 B LEU A 1 166 ? 28.71100 44.38100 -5.16700  0.440 55.72000  ?  166 LEU A CD2 1 
ATOM   2393 N  N   A THR A 1 167 ? 26.19100 44.47400 -2.77300  0.560 42.90000  ?  167 THR A N   1 
ATOM   2394 N  N   B THR A 1 167 ? 25.56000 44.71500 -3.07600  0.440 46.32000  ?  167 THR A N   1 
ATOM   2395 C  CA  A THR A 1 167 ? 26.33900 43.65700 -1.57200  0.560 42.79000  ?  167 THR A CA  1 
ATOM   2396 C  CA  B THR A 1 167 ? 25.72100 44.00100 -1.80900  0.440 41.30000  ?  167 THR A CA  1 
ATOM   2397 C  C   A THR A 1 167 ? 25.02500 42.98100 -1.19400  0.560 39.19000  ?  167 THR A C   1 
ATOM   2398 C  C   B THR A 1 167 ? 24.44400 43.25300 -1.41100  0.440 41.12000  ?  167 THR A C   1 
ATOM   2399 O  O   A THR A 1 167 ? 24.98100 41.76600 -0.96500  0.560 31.86000  ?  167 THR A O   1 
ATOM   2400 O  O   B THR A 1 167 ? 24.44400 42.02000 -1.24700  0.440 34.37000  ?  167 THR A O   1 
ATOM   2401 C  CB  A THR A 1 167 ? 26.85600 44.52600 -0.42200  0.560 44.19000  ?  167 THR A CB  1 
ATOM   2402 C  CB  B THR A 1 167 ? 26.17400 45.01500 -0.74500  0.440 42.62000  ?  167 THR A CB  1 
ATOM   2403 O  OG1 A THR A 1 167 ? 28.23000 44.86600 -0.65700  0.560 43.55000  ?  167 THR A OG1 1 
ATOM   2404 O  OG1 B THR A 1 167 ? 27.53000 45.40500 -1.01900  0.440 39.89000  ?  167 THR A OG1 1 
ATOM   2405 C  CG2 A THR A 1 167 ? 26.73400 43.79600 0.90600   0.560 37.22000  ?  167 THR A CG2 1 
ATOM   2406 C  CG2 B THR A 1 167 ? 26.10800 44.45300 0.59700   0.440 39.98000  ?  167 THR A CG2 1 
ATOM   2407 N  N   A VAL A 1 168 ? 23.93900 43.75500 -1.13000  0.560 41.12000  ?  168 VAL A N   1 
ATOM   2408 N  N   B VAL A 1 168 ? 23.31500 43.97100 -1.34100  0.440 40.76000  ?  168 VAL A N   1 
ATOM   2409 C  CA  A VAL A 1 168 ? 22.66700 43.21500 -0.65700  0.560 40.38000  ?  168 VAL A CA  1 
ATOM   2410 C  CA  B VAL A 1 168 ? 22.07200 43.30800 -0.92700  0.440 41.92000  ?  168 VAL A CA  1 
ATOM   2411 C  C   A VAL A 1 168 ? 22.16300 42.12200 -1.59000  0.560 41.86000  ?  168 VAL A C   1 
ATOM   2412 C  C   B VAL A 1 168 ? 21.70400 42.18800 -1.89300  0.440 43.35000  ?  168 VAL A C   1 
ATOM   2413 O  O   A VAL A 1 168 ? 21.71100 41.06300 -1.14000  0.560 41.60000  ?  168 VAL A O   1 
ATOM   2414 O  O   B VAL A 1 168 ? 21.21800 41.12200 -1.48700  0.440 40.79000  ?  168 VAL A O   1 
ATOM   2415 C  CB  A VAL A 1 168 ? 21.63400 44.34800 -0.50700  0.560 49.33000  ?  168 VAL A CB  1 
ATOM   2416 C  CB  B VAL A 1 168 ? 20.92900 44.32900 -0.80200  0.440 44.79000  ?  168 VAL A CB  1 
ATOM   2417 C  CG1 A VAL A 1 168 ? 20.22500 43.77700 -0.38800  0.560 44.12000  ?  168 VAL A CG1 1 
ATOM   2418 C  CG1 B VAL A 1 168 ? 19.58700 43.59100 -0.60400  0.440 43.36000  ?  168 VAL A CG1 1 
ATOM   2419 C  CG2 A VAL A 1 168 ? 21.96700 45.22800 0.69000   0.560 41.04000  ?  168 VAL A CG2 1 
ATOM   2420 C  CG2 B VAL A 1 168 ? 21.23600 45.30600 0.31300   0.440 47.07000  ?  168 VAL A CG2 1 
ATOM   2421 N  N   A ILE A 1 169 ? 22.23300 42.35500 -2.90100  0.560 44.58000  ?  169 ILE A N   1 
ATOM   2422 N  N   B ILE A 1 169 ? 21.90100 42.42500 -3.18900  0.440 44.17000  ?  169 ILE A N   1 
ATOM   2423 C  CA  A ILE A 1 169 ? 21.66600 41.40100 -3.84800  0.560 34.74000  ?  169 ILE A CA  1 
ATOM   2424 C  CA  B ILE A 1 169 ? 21.60300 41.41800 -4.19200  0.440 35.73000  ?  169 ILE A CA  1 
ATOM   2425 C  C   A ILE A 1 169 ? 22.45300 40.09600 -3.82500  0.560 38.33000  ?  169 ILE A C   1 
ATOM   2426 C  C   B ILE A 1 169 ? 22.54200 40.23800 -4.02700  0.440 38.26000  ?  169 ILE A C   1 
ATOM   2427 O  O   A ILE A 1 169 ? 21.87300 39.00600 -3.75500  0.560 38.04000  ?  169 ILE A O   1 
ATOM   2428 O  O   B ILE A 1 169 ? 22.10200 39.09500 -3.87400  0.440 38.03000  ?  169 ILE A O   1 
ATOM   2429 C  CB  A ILE A 1 169 ? 21.61200 42.01400 -5.25900  0.560 43.67000  ?  169 ILE A CB  1 
ATOM   2430 C  CB  B ILE A 1 169 ? 21.72300 42.04500 -5.58500  0.440 43.40000  ?  169 ILE A CB  1 
ATOM   2431 C  CG1 A ILE A 1 169 ? 20.54600 43.11300 -5.30200  0.560 44.88000  ?  169 ILE A CG1 1 
ATOM   2432 C  CG1 B ILE A 1 169 ? 20.51700 42.96100 -5.83600  0.440 46.97000  ?  169 ILE A CG1 1 
ATOM   2433 C  CG2 A ILE A 1 169 ? 21.32600 40.94700 -6.29500  0.560 41.99000  ?  169 ILE A CG2 1 
ATOM   2434 C  CG2 B ILE A 1 169 ? 21.80600 40.98900 -6.59500  0.440 41.31000  ?  169 ILE A CG2 1 
ATOM   2435 C  CD1 A ILE A 1 169 ? 20.67600 44.05600 -6.46700  0.560 64.73000  ?  169 ILE A CD1 1 
ATOM   2436 C  CD1 B ILE A 1 169 ? 20.77500 43.96700 -6.90600  0.440 65.41000  ?  169 ILE A CD1 1 
ATOM   2437 N  N   A LEU A 1 170 ? 23.78600 40.18600 -3.85300  0.560 32.51000  ?  170 LEU A N   1 
ATOM   2438 N  N   B LEU A 1 170 ? 23.85900 40.50100 -3.99400  0.440 33.85000  ?  170 LEU A N   1 
ATOM   2439 C  CA  A LEU A 1 170 ? 24.59400 38.97300 -3.92600  0.560 33.90000  ?  170 LEU A CA  1 
ATOM   2440 C  CA  B LEU A 1 170 ? 24.78400 39.38700 -3.88200  0.440 35.39000  ?  170 LEU A CA  1 
ATOM   2441 C  C   A LEU A 1 170 ? 24.65000 38.25300 -2.58300  0.560 39.15000  ?  170 LEU A C   1 
ATOM   2442 C  C   B LEU A 1 170 ? 24.60100 38.67800 -2.56200  0.440 40.66000  ?  170 LEU A C   1 
ATOM   2443 O  O   A LEU A 1 170 ? 24.59200 37.02000 -2.53800  0.560 36.37000  ?  170 LEU A O   1 
ATOM   2444 O  O   B LEU A 1 170 ? 24.30500 37.48100 -2.54800  0.440 35.81000  ?  170 LEU A O   1 
ATOM   2445 C  CB  A LEU A 1 170 ? 26.00300 39.30400 -4.41600  0.560 40.69000  ?  170 LEU A CB  1 
ATOM   2446 C  CB  B LEU A 1 170 ? 26.23400 39.83400 -4.05900  0.440 37.11000  ?  170 LEU A CB  1 
ATOM   2447 C  CG  A LEU A 1 170 ? 26.05300 39.83600 -5.84500  0.560 44.56000  ?  170 LEU A CG  1 
ATOM   2448 C  CG  B LEU A 1 170 ? 26.46500 40.20900 -5.53300  0.440 47.50000  ?  170 LEU A CG  1 
ATOM   2449 C  CD1 A LEU A 1 170 ? 27.48300 40.01200 -6.31800  0.560 47.83000  ?  170 LEU A CD1 1 
ATOM   2450 C  CD1 B LEU A 1 170 ? 27.92600 40.62600 -5.73500  0.440 48.74000  ?  170 LEU A CD1 1 
ATOM   2451 C  CD2 A LEU A 1 170 ? 25.29900 38.90800 -6.79300  0.560 43.54000  ?  170 LEU A CD2 1 
ATOM   2452 C  CD2 B LEU A 1 170 ? 26.08000 39.05100 -6.46700  0.440 41.95000  ?  170 LEU A CD2 1 
ATOM   2453 N  N   A TRP A 1 171 ? 24.78100 38.99100 -1.47800  0.560 39.54000  ?  171 TRP A N   1 
ATOM   2454 N  N   B TRP A 1 171 ? 24.68800 39.42600 -1.43700  0.440 38.11000  ?  171 TRP A N   1 
ATOM   2455 C  CA  A TRP A 1 171 ? 24.82300 38.32200 -0.18000  0.560 40.02000  ?  171 TRP A CA  1 
ATOM   2456 C  CA  B TRP A 1 171 ? 24.64900 38.77800 -0.11900  0.440 42.25000  ?  171 TRP A CA  1 
ATOM   2457 C  C   A TRP A 1 171 ? 23.54600 37.52700 0.06700   0.560 37.10000  ?  171 TRP A C   1 
ATOM   2458 C  C   B TRP A 1 171 ? 23.46900 37.86200 0.01800   0.440 38.59000  ?  171 TRP A C   1 
ATOM   2459 O  O   A TRP A 1 171 ? 23.58400 36.47000 0.70900   0.560 30.71000  ?  171 TRP A O   1 
ATOM   2460 O  O   B TRP A 1 171 ? 23.56900 36.84700 0.70700   0.440 32.51000  ?  171 TRP A O   1 
ATOM   2461 C  CB  A TRP A 1 171 ? 25.03900 39.33600 0.94500   0.560 35.62000  ?  171 TRP A CB  1 
ATOM   2462 C  CB  B TRP A 1 171 ? 24.60800 39.77800 1.04500   0.440 33.43000  ?  171 TRP A CB  1 
ATOM   2463 C  CG  A TRP A 1 171 ? 26.44100 39.86000 1.04400   0.560 33.03000  ?  171 TRP A CG  1 
ATOM   2464 C  CG  B TRP A 1 171 ? 25.93300 40.35100 1.21700   0.440 36.97000  ?  171 TRP A CG  1 
ATOM   2465 C  CD1 A TRP A 1 171 ? 27.30800 40.08300 0.01300   0.560 39.78000  ?  171 TRP A CD1 1 
ATOM   2466 C  CD1 B TRP A 1 171 ? 26.85800 40.50500 0.24100   0.440 39.50000  ?  171 TRP A CD1 1 
ATOM   2467 C  CD2 A TRP A 1 171 ? 27.13700 40.23700 2.24000   0.560 45.90000  ?  171 TRP A CD2 1 
ATOM   2468 C  CD2 B TRP A 1 171 ? 26.53200 40.84600 2.40600   0.440 44.48000  ?  171 TRP A CD2 1 
ATOM   2469 N  NE1 A TRP A 1 171 ? 28.49700 40.57400 0.49100   0.560 40.16000  ?  171 TRP A NE1 1 
ATOM   2470 N  NE1 B TRP A 1 171 ? 27.98000 41.06500 0.72700   0.440 38.10000  ?  171 TRP A NE1 1 
ATOM   2471 C  CE2 A TRP A 1 171 ? 28.41900 40.67800 1.85400   0.560 41.85000  ?  171 TRP A CE2 1 
ATOM   2472 C  CE2 B TRP A 1 171 ? 27.80900 41.29000 2.05900   0.440 42.02000  ?  171 TRP A CE2 1 
ATOM   2473 C  CE3 A TRP A 1 171 ? 26.80300 40.24200 3.60000   0.560 38.25000  ?  171 TRP A CE3 1 
ATOM   2474 C  CE3 B TRP A 1 171 ? 26.13100 40.93200 3.73200   0.440 41.29000  ?  171 TRP A CE3 1 
ATOM   2475 C  CZ2 A TRP A 1 171 ? 29.36600 41.12100 2.77800   0.560 42.55000  ?  171 TRP A CZ2 1 
ATOM   2476 C  CZ2 B TRP A 1 171 ? 28.68600 41.81400 2.97100   0.440 44.29000  ?  171 TRP A CZ2 1 
ATOM   2477 C  CZ3 A TRP A 1 171 ? 27.74500 40.68200 4.51400   0.560 38.75000  ?  171 TRP A CZ3 1 
ATOM   2478 C  CZ3 B TRP A 1 171 ? 27.01100 41.46500 4.63600   0.440 49.11000  ?  171 TRP A CZ3 1 
ATOM   2479 C  CH2 A TRP A 1 171 ? 29.01000 41.11400 4.10000   0.560 43.71000  ?  171 TRP A CH2 1 
ATOM   2480 C  CH2 B TRP A 1 171 ? 28.26900 41.91500 4.24200   0.440 48.36000  ?  171 TRP A CH2 1 
ATOM   2481 N  N   A ALA A 1 172 ? 22.41100 38.01000 -0.44700  0.560 35.50000  ?  172 ALA A N   1 
ATOM   2482 N  N   B ALA A 1 172 ? 22.34700 38.18900 -0.62500  0.440 34.66000  ?  172 ALA A N   1 
ATOM   2483 C  CA  A ALA A 1 172 ? 21.13700 37.32700 -0.25400  0.560 35.00000  ?  172 ALA A CA  1 
ATOM   2484 C  CA  B ALA A 1 172 ? 21.16200 37.37900 -0.40300  0.440 35.23000  ?  172 ALA A CA  1 
ATOM   2485 C  C   A ALA A 1 172 ? 21.08200 35.98800 -0.97200  0.560 45.43000  ?  172 ALA A C   1 
ATOM   2486 C  C   B ALA A 1 172 ? 21.18700 36.07500 -1.17300  0.440 45.19000  ?  172 ALA A C   1 
ATOM   2487 O  O   A ALA A 1 172 ? 20.21100 35.16900 -0.66100  0.560 46.95000  ?  172 ALA A O   1 
ATOM   2488 O  O   B ALA A 1 172 ? 20.40500 35.17600 -0.84400  0.440 47.21000  ?  172 ALA A O   1 
ATOM   2489 C  CB  A ALA A 1 172 ? 19.98900 38.21600 -0.73600  0.560 36.53000  ?  172 ALA A CB  1 
ATOM   2490 C  CB  B ALA A 1 172 ? 19.90900 38.18000 -0.74400  0.440 32.36000  ?  172 ALA A CB  1 
ATOM   2491 N  N   A ILE A 1 173 ? 21.99000 35.74800 -1.91600  0.560 36.99000  ?  173 ILE A N   1 
ATOM   2492 N  N   B ILE A 1 173 ? 22.07000 35.92500 -2.16100  0.440 36.24000  ?  173 ILE A N   1 
ATOM   2493 C  CA  A ILE A 1 173 ? 21.99800 34.48700 -2.64500  0.560 38.00000  ?  173 ILE A CA  1 
ATOM   2494 C  CA  B ILE A 1 173 ? 22.10600 34.67900 -2.91800  0.440 39.44000  ?  173 ILE A CA  1 
ATOM   2495 C  C   A ILE A 1 173 ? 22.70500 33.39800 -1.85100  0.560 39.99000  ?  173 ILE A C   1 
ATOM   2496 C  C   B ILE A 1 173 ? 22.65800 33.53500 -2.07300  0.440 40.43000  ?  173 ILE A C   1 
ATOM   2497 O  O   A ILE A 1 173 ? 22.33900 32.22000 -1.94800  0.560 40.38000  ?  173 ILE A O   1 
ATOM   2498 O  O   B ILE A 1 173 ? 22.11500 32.41700 -2.07100  0.440 41.69000  ?  173 ILE A O   1 
ATOM   2499 C  CB  A ILE A 1 173 ? 22.65700 34.69000 -4.02000  0.560 42.86000  ?  173 ILE A CB  1 
ATOM   2500 C  CB  B ILE A 1 173 ? 22.90400 34.91700 -4.21400  0.440 41.58000  ?  173 ILE A CB  1 
ATOM   2501 C  CG1 A ILE A 1 173 ? 21.79900 35.61000 -4.89400  0.560 39.84000  ?  173 ILE A CG1 1 
ATOM   2502 C  CG1 B ILE A 1 173 ? 22.03400 35.68800 -5.22000  0.440 39.72000  ?  173 ILE A CG1 1 
ATOM   2503 C  CG2 A ILE A 1 173 ? 22.89000 33.35100 -4.70800  0.560 32.93000  ?  173 ILE A CG2 1 
ATOM   2504 C  CG2 B ILE A 1 173 ? 23.37100 33.65200 -4.85400  0.440 33.85000  ?  173 ILE A CG2 1 
ATOM   2505 C  CD1 A ILE A 1 173 ? 22.54600 36.22500 -6.05500  0.560 46.19000  ?  173 ILE A CD1 1 
ATOM   2506 C  CD1 B ILE A 1 173 ? 22.77600 36.10800 -6.38800  0.440 45.45000  ?  173 ILE A CD1 1 
ATOM   2507 N  N   A TYR A 1 174 ? 23.70800 33.76000 -1.05500  0.560 37.57000  ?  174 TYR A N   1 
ATOM   2508 N  N   B TYR A 1 174 ? 23.71500 33.79900 -1.31700  0.440 37.39000  ?  174 TYR A N   1 
ATOM   2509 C  CA  A TYR A 1 174 ? 24.47000 32.75600 -0.31500  0.560 41.41000  ?  174 TYR A CA  1 
ATOM   2510 C  CA  B TYR A 1 174 ? 24.32700 32.77100 -0.47200  0.440 41.29000  ?  174 TYR A CA  1 
ATOM   2511 C  C   A TYR A 1 174 ? 23.60000 31.82600 0.52000   0.560 40.67000  ?  174 TYR A C   1 
ATOM   2512 C  C   B TYR A 1 174 ? 23.32700 31.93300 0.34600   0.440 41.53000  ?  174 TYR A C   1 
ATOM   2513 O  O   A TYR A 1 174 ? 23.81700 30.60400 0.46400   0.560 38.77000  ?  174 TYR A O   1 
ATOM   2514 O  O   B TYR A 1 174 ? 23.38700 30.69500 0.26100   0.440 43.15000  ?  174 TYR A O   1 
ATOM   2515 C  CB  A TYR A 1 174 ? 25.48600 33.43700 0.61100   0.560 36.23000  ?  174 TYR A CB  1 
ATOM   2516 C  CB  B TYR A 1 174 ? 25.34000 33.48100 0.43400   0.440 37.28000  ?  174 TYR A CB  1 
ATOM   2517 C  CG  A TYR A 1 174 ? 26.76800 33.90500 -0.03400  0.560 32.77000  ?  174 TYR A CG  1 
ATOM   2518 C  CG  B TYR A 1 174 ? 26.65600 33.96300 -0.17100  0.440 33.02000  ?  174 TYR A CG  1 
ATOM   2519 C  CD1 A TYR A 1 174 ? 26.82700 35.12600 -0.68800  0.560 37.72000  ?  174 TYR A CD1 1 
ATOM   2520 C  CD1 B TYR A 1 174 ? 27.73600 33.14400 -0.20500  0.440 33.54000  ?  174 TYR A CD1 1 
ATOM   2521 C  CD2 A TYR A 1 174 ? 27.93000 33.14700 0.04800   0.560 34.74000  ?  174 TYR A CD2 1 
ATOM   2522 C  CD2 B TYR A 1 174 ? 26.82000 35.29200 -0.61600  0.440 37.43000  ?  174 TYR A CD2 1 
ATOM   2523 C  CE1 A TYR A 1 174 ? 27.99700 35.57200 -1.26500  0.560 32.18000  ?  174 TYR A CE1 1 
ATOM   2524 C  CE1 B TYR A 1 174 ? 28.94800 33.58300 -0.69400  0.440 35.34000  ?  174 TYR A CE1 1 
ATOM   2525 C  CE2 A TYR A 1 174 ? 29.10900 33.58400 -0.52400  0.560 35.43000  ?  174 TYR A CE2 1 
ATOM   2526 C  CE2 B TYR A 1 174 ? 28.03200 35.74800 -1.08600  0.440 31.97000  ?  174 TYR A CE2 1 
ATOM   2527 C  CZ  A TYR A 1 174 ? 29.13500 34.80000 -1.17900  0.560 34.72000  ?  174 TYR A CZ  1 
ATOM   2528 C  CZ  B TYR A 1 174 ? 29.10900 34.85900 -1.13400  0.440 32.71000  ?  174 TYR A CZ  1 
ATOM   2529 O  OH  A TYR A 1 174 ? 30.29800 35.25500 -1.75700  0.560 36.40000  ?  174 TYR A OH  1 
ATOM   2530 O  OH  B TYR A 1 174 ? 30.37400 35.24100 -1.59200  0.440 35.44000  ?  174 TYR A OH  1 
ATOM   2531 N  N   A PRO A 1 175 ? 22.65700 32.31000 1.33800   0.560 39.52000  ?  175 PRO A N   1 
ATOM   2532 N  N   B PRO A 1 175 ? 22.41800 32.50600 1.16100   0.440 39.58000  ?  175 PRO A N   1 
ATOM   2533 C  CA  A PRO A 1 175 ? 21.86900 31.36000 2.14400   0.560 42.38000  ?  175 PRO A CA  1 
ATOM   2534 C  CA  B PRO A 1 175 ? 21.39400 31.65900 1.81000   0.440 44.51000  ?  175 PRO A CA  1 
ATOM   2535 C  C   A PRO A 1 175 ? 21.11800 30.35200 1.29500   0.560 46.30000  ?  175 PRO A C   1 
ATOM   2536 C  C   B PRO A 1 175 ? 20.65700 30.73100 0.87000   0.440 46.63000  ?  175 PRO A C   1 
ATOM   2537 O  O   A PRO A 1 175 ? 20.90700 29.21500 1.73400   0.560 37.97000  ?  175 PRO A O   1 
ATOM   2538 O  O   B PRO A 1 175 ? 20.18600 29.67200 1.32100   0.440 42.10000  ?  175 PRO A O   1 
ATOM   2539 C  CB  A PRO A 1 175 ? 20.91500 32.26000 2.94700   0.560 37.76000  ?  175 PRO A CB  1 
ATOM   2540 C  CB  B PRO A 1 175 ? 20.42300 32.67200 2.43000   0.440 40.93000  ?  175 PRO A CB  1 
ATOM   2541 C  CG  A PRO A 1 175 ? 20.96600 33.60300 2.29900   0.560 39.92000  ?  175 PRO A CG  1 
ATOM   2542 C  CG  B PRO A 1 175 ? 20.87100 33.97600 1.94300   0.440 39.29000  ?  175 PRO A CG  1 
ATOM   2543 C  CD  A PRO A 1 175 ? 22.30000 33.71600 1.61800   0.560 37.37000  ?  175 PRO A CD  1 
ATOM   2544 C  CD  B PRO A 1 175 ? 22.33000 33.86000 1.70300   0.440 37.54000  ?  175 PRO A CD  1 
ATOM   2545 N  N   A PHE A 1 176 ? 20.72600 30.72400 0.07700   0.560 47.06000  ?  176 PHE A N   1 
ATOM   2546 N  N   B PHE A 1 176 ? 20.56000 31.05200 -0.42700  0.440 45.42000  ?  176 PHE A N   1 
ATOM   2547 C  CA  A PHE A 1 176 ? 20.05800 29.76700 -0.79600  0.560 46.91000  ?  176 PHE A CA  1 
ATOM   2548 C  CA  B PHE A 1 176 ? 19.83300 30.09700 -1.25300  0.440 44.57000  ?  176 PHE A CA  1 
ATOM   2549 C  C   A PHE A 1 176 ? 21.03300 28.71800 -1.31500  0.560 45.46000  ?  176 PHE A C   1 
ATOM   2550 C  C   B PHE A 1 176 ? 20.70000 28.94500 -1.64600  0.440 45.30000  ?  176 PHE A C   1 
ATOM   2551 O  O   A PHE A 1 176 ? 20.70000 27.52800 -1.36200  0.560 46.97000  ?  176 PHE A O   1 
ATOM   2552 O  O   B PHE A 1 176 ? 20.21300 27.81200 -1.71600  0.440 44.51000  ?  176 PHE A O   1 
ATOM   2553 C  CB  A PHE A 1 176 ? 19.37700 30.50600 -1.94400  0.560 39.23000  ?  176 PHE A CB  1 
ATOM   2554 C  CB  B PHE A 1 176 ? 19.24200 30.76100 -2.45200  0.440 39.63000  ?  176 PHE A CB  1 
ATOM   2555 C  CG  A PHE A 1 176 ? 18.28300 31.42500 -1.49200  0.560 43.39000  ?  176 PHE A CG  1 
ATOM   2556 C  CG  B PHE A 1 176 ? 18.13700 31.64100 -2.06500  0.440 44.40000  ?  176 PHE A CG  1 
ATOM   2557 C  CD1 A PHE A 1 176 ? 17.00300 30.94400 -1.26900  0.560 44.56000  ?  176 PHE A CD1 1 
ATOM   2558 C  CD1 B PHE A 1 176 ? 16.90900 31.10500 -1.81200  0.440 44.04000  ?  176 PHE A CD1 1 
ATOM   2559 C  CD2 A PHE A 1 176 ? 18.53900 32.76500 -1.26600  0.560 41.72000  ?  176 PHE A CD2 1 
ATOM   2560 C  CD2 B PHE A 1 176 ? 18.33500 32.99100 -1.86700  0.440 44.07000  ?  176 PHE A CD2 1 
ATOM   2561 C  CE1 A PHE A 1 176 ? 15.99800 31.78700 -0.84300  0.560 49.49000  ?  176 PHE A CE1 1 
ATOM   2562 C  CE1 B PHE A 1 176 ? 15.88100 31.92300 -1.39800  0.440 47.95000  ?  176 PHE A CE1 1 
ATOM   2563 C  CE2 A PHE A 1 176 ? 17.53400 33.61300 -0.83700  0.560 47.66000  ?  176 PHE A CE2 1 
ATOM   2564 C  CE2 B PHE A 1 176 ? 17.30700 33.81100 -1.48200  0.440 48.43000  ?  176 PHE A CE2 1 
ATOM   2565 C  CZ  A PHE A 1 176 ? 16.26500 33.12400 -0.62600  0.560 44.80000  ?  176 PHE A CZ  1 
ATOM   2566 C  CZ  B PHE A 1 176 ? 16.08200 33.26800 -1.23000  0.440 49.18000  ?  176 PHE A CZ  1 
ATOM   2567 N  N   A ILE A 1 177 ? 22.24600 29.12900 -1.69500  0.560 37.67000  ?  177 ILE A N   1 
ATOM   2568 N  N   B ILE A 1 177 ? 21.99700 29.20100 -1.84600  0.440 40.43000  ?  177 ILE A N   1 
ATOM   2569 C  CA  A ILE A 1 177 ? 23.23600 28.15700 -2.15200  0.560 42.57000  ?  177 ILE A CA  1 
ATOM   2570 C  CA  B ILE A 1 177 ? 22.87600 28.09600 -2.17700  0.440 43.58000  ?  177 ILE A CA  1 
ATOM   2571 C  C   A ILE A 1 177 ? 23.59900 27.20000 -1.02100  0.560 50.35000  ?  177 ILE A C   1 
ATOM   2572 C  C   B ILE A 1 177 ? 23.01700 27.18300 -0.95300  0.440 50.10000  ?  177 ILE A C   1 
ATOM   2573 O  O   A ILE A 1 177 ? 23.74900 25.98900 -1.22900  0.560 55.08000  ?  177 ILE A O   1 
ATOM   2574 O  O   B ILE A 1 177 ? 22.61300 26.01700 -0.99600  0.440 50.31000  ?  177 ILE A O   1 
ATOM   2575 C  CB  A ILE A 1 177 ? 24.48800 28.87000 -2.69400  0.560 49.99000  ?  177 ILE A CB  1 
ATOM   2576 C  CB  B ILE A 1 177 ? 24.22000 28.59800 -2.72800  0.440 49.11000  ?  177 ILE A CB  1 
ATOM   2577 C  CG1 A ILE A 1 177 ? 24.12700 29.88400 -3.78000  0.560 46.72000  ?  177 ILE A CG1 1 
ATOM   2578 C  CG1 B ILE A 1 177 ? 24.01000 29.65000 -3.82500  0.440 47.13000  ?  177 ILE A CG1 1 
ATOM   2579 C  CG2 A ILE A 1 177 ? 25.48200 27.83800 -3.22700  0.560 50.17000  ?  177 ILE A CG2 1 
ATOM   2580 C  CG2 B ILE A 1 177 ? 24.92000 27.48900 -3.42000  0.440 48.31000  ?  177 ILE A CG2 1 
ATOM   2581 C  CD1 A ILE A 1 177 ? 23.09000 29.40700 -4.76600  0.560 42.93000  ?  177 ILE A CD1 1 
ATOM   2582 C  CD1 B ILE A 1 177 ? 22.90500 29.35600 -4.81700  0.440 42.46000  ?  177 ILE A CD1 1 
ATOM   2583 N  N   A TRP A 1 178 ? 23.78900 27.73800 0.18600   0.560 50.91000  ?  178 TRP A N   1 
ATOM   2584 N  N   B TRP A 1 178 ? 23.43600 27.73800 0.19400   0.440 50.14000  ?  178 TRP A N   1 
ATOM   2585 C  CA  A TRP A 1 178 ? 24.08400 26.91100 1.35400   0.560 48.03000  ?  178 TRP A CA  1 
ATOM   2586 C  CA  B TRP A 1 178 ? 23.44600 26.96900 1.43900   0.440 45.95000  ?  178 TRP A CA  1 
ATOM   2587 C  C   A TRP A 1 178 ? 22.98400 25.88300 1.57900   0.560 52.11000  ?  178 TRP A C   1 
ATOM   2588 C  C   B TRP A 1 178 ? 22.17600 26.17800 1.57300   0.440 49.93000  ?  178 TRP A C   1 
ATOM   2589 O  O   A TRP A 1 178 ? 23.25300 24.68400 1.71900   0.560 53.67000  ?  178 TRP A O   1 
ATOM   2590 O  O   B TRP A 1 178 ? 22.18600 24.97300 1.87900   0.440 50.71000  ?  178 TRP A O   1 
ATOM   2591 C  CB  A TRP A 1 178 ? 24.25000 27.82700 2.57200   0.560 52.32000  ?  178 TRP A CB  1 
ATOM   2592 C  CB  B TRP A 1 178 ? 23.56100 27.87100 2.66400   0.440 49.67000  ?  178 TRP A CB  1 
ATOM   2593 C  CG  A TRP A 1 178 ? 24.74800 27.21300 3.85400   0.560 41.27000  ?  178 TRP A CG  1 
ATOM   2594 C  CG  B TRP A 1 178 ? 24.01900 27.20100 3.95600   0.440 39.17000  ?  178 TRP A CG  1 
ATOM   2595 C  CD1 A TRP A 1 178 ? 26.02500 27.24900 4.34000   0.560 47.03000  ?  178 TRP A CD1 1 
ATOM   2596 C  CD1 B TRP A 1 178 ? 25.27500 27.28200 4.47400   0.440 45.06000  ?  178 TRP A CD1 1 
ATOM   2597 C  CD2 A TRP A 1 178 ? 23.96600 26.52600 4.83800   0.560 43.56000  ?  178 TRP A CD2 1 
ATOM   2598 C  CD2 B TRP A 1 178 ? 23.24400 26.43200 4.92000   0.440 48.05000  ?  178 TRP A CD2 1 
ATOM   2599 N  NE1 A TRP A 1 178 ? 26.08900 26.61200 5.55500   0.560 48.04000  ?  178 TRP A NE1 1 
ATOM   2600 N  NE1 B TRP A 1 178 ? 25.35500 26.60800 5.67300   0.440 48.70000  ?  178 TRP A NE1 1 
ATOM   2601 C  CE2 A TRP A 1 178 ? 24.83800 26.15900 5.88400   0.560 48.92000  ?  178 TRP A CE2 1 
ATOM   2602 C  CE2 B TRP A 1 178 ? 24.12100 26.09500 5.98800   0.440 50.10000  ?  178 TRP A CE2 1 
ATOM   2603 C  CE3 A TRP A 1 178 ? 22.61500 26.18200 4.93400   0.560 49.00000  ?  178 TRP A CE3 1 
ATOM   2604 C  CE3 B TRP A 1 178 ? 21.90900 25.97300 4.98500   0.440 51.97000  ?  178 TRP A CE3 1 
ATOM   2605 C  CZ2 A TRP A 1 178 ? 24.40200 25.45900 7.00800   0.560 57.59000  ?  178 TRP A CZ2 1 
ATOM   2606 C  CZ2 B TRP A 1 178 ? 23.70200 25.30700 7.11100   0.440 57.41000  ?  178 TRP A CZ2 1 
ATOM   2607 C  CZ3 A TRP A 1 178 ? 22.18700 25.48400 6.04800   0.560 54.10000  ?  178 TRP A CZ3 1 
ATOM   2608 C  CZ3 B TRP A 1 178 ? 21.48400 25.19300 6.15500   0.440 53.35000  ?  178 TRP A CZ3 1 
ATOM   2609 C  CH2 A TRP A 1 178 ? 23.07700 25.13200 7.07100   0.560 56.39000  ?  178 TRP A CH2 1 
ATOM   2610 C  CH2 B TRP A 1 178 ? 22.38400 24.87900 7.17000   0.440 52.02000  ?  178 TRP A CH2 1 
ATOM   2611 N  N   A LEU A 1 179 ? 21.73000 26.33400 1.57200   0.560 49.64000  ?  179 LEU A N   1 
ATOM   2612 N  N   B LEU A 1 179 ? 21.05600 26.85300 1.36400   0.440 48.11000  ?  179 LEU A N   1 
ATOM   2613 C  CA  A LEU A 1 179 ? 20.61700 25.44600 1.88900   0.560 48.46000  ?  179 LEU A CA  1 
ATOM   2614 C  CA  B LEU A 1 179 ? 19.83500 26.10700 1.53900   0.440 49.35000  ?  179 LEU A CA  1 
ATOM   2615 C  C   A LEU A 1 179 ? 20.41700 24.38900 0.81200   0.560 48.93000  ?  179 LEU A C   1 
ATOM   2616 C  C   B LEU A 1 179 ? 19.66400 25.01900 0.46600   0.440 51.62000  ?  179 LEU A C   1 
ATOM   2617 O  O   A LEU A 1 179 ? 20.05700 23.24800 1.12000   0.560 52.18000  ?  179 LEU A O   1 
ATOM   2618 O  O   B LEU A 1 179 ? 18.89800 24.06700 0.69500   0.440 52.05000  ?  179 LEU A O   1 
ATOM   2619 C  CB  A LEU A 1 179 ? 19.34700 26.26900 2.07400   0.560 44.92000  ?  179 LEU A CB  1 
ATOM   2620 C  CB  B LEU A 1 179 ? 18.67200 27.06400 1.56500   0.440 49.58000  ?  179 LEU A CB  1 
ATOM   2621 C  CG  A LEU A 1 179 ? 18.25900 25.69900 2.97900   0.560 54.74000  ?  179 LEU A CG  1 
ATOM   2622 C  CG  B LEU A 1 179 ? 17.93700 26.64100 2.77500   0.440 54.70000  ?  179 LEU A CG  1 
ATOM   2623 C  CD1 A LEU A 1 179 ? 18.77900 25.45300 4.37600   0.560 61.08000  ?  179 LEU A CD1 1 
ATOM   2624 C  CD1 B LEU A 1 179 ? 18.89600 26.74000 3.91000   0.440 55.34000  ?  179 LEU A CD1 1 
ATOM   2625 C  CD2 A LEU A 1 179 ? 17.07400 26.65700 2.99000   0.560 58.54000  ?  179 LEU A CD2 1 
ATOM   2626 C  CD2 B LEU A 1 179 ? 16.82300 27.58800 2.94600   0.440 53.90000  ?  179 LEU A CD2 1 
ATOM   2627 N  N   A LEU A 1 180 ? 20.63200 24.74300 -0.45400  0.560 53.49000  ?  180 LEU A N   1 
ATOM   2628 N  N   B LEU A 1 180 ? 20.38600 25.11700 -0.67300  0.440 53.25000  ?  180 LEU A N   1 
ATOM   2629 C  CA  A LEU A 1 180 ? 20.45800 23.77800 -1.53200  0.560 53.95000  ?  180 LEU A CA  1 
ATOM   2630 C  CA  B LEU A 1 180 ? 20.25600 24.18600 -1.80500  0.440 54.18000  ?  180 LEU A CA  1 
ATOM   2631 C  C   A LEU A 1 180 ? 21.66300 22.86400 -1.70400  0.560 56.24000  ?  180 LEU A C   1 
ATOM   2632 C  C   B LEU A 1 180 ? 21.41500 23.22700 -1.91600  0.440 55.70000  ?  180 LEU A C   1 
ATOM   2633 O  O   A LEU A 1 180 ? 21.56100 21.85800 -2.41500  0.560 57.94000  ?  180 LEU A O   1 
ATOM   2634 O  O   B LEU A 1 180 ? 21.25500 22.15000 -2.48300  0.440 56.51000  ?  180 LEU A O   1 
ATOM   2635 C  CB  A LEU A 1 180 ? 20.18100 24.50200 -2.84900  0.560 53.57000  ?  180 LEU A CB  1 
ATOM   2636 C  CB  B LEU A 1 180 ? 20.19200 24.93100 -3.14900  0.440 51.78000  ?  180 LEU A CB  1 
ATOM   2637 C  CG  A LEU A 1 180 ? 18.79600 25.13600 -2.98800  0.560 57.38000  ?  180 LEU A CG  1 
ATOM   2638 C  CG  B LEU A 1 180 ? 18.96700 25.69000 -3.63300  0.440 55.40000  ?  180 LEU A CG  1 
ATOM   2639 C  CD1 A LEU A 1 180 ? 18.73700 26.06700 -4.18900  0.560 54.99000  ?  180 LEU A CD1 1 
ATOM   2640 C  CD1 B LEU A 1 180 ? 19.45500 26.68900 -4.69500  0.440 41.12000  ?  180 LEU A CD1 1 
ATOM   2641 C  CD2 A LEU A 1 180 ? 17.72300 24.06100 -3.10000  0.560 49.97000  ?  180 LEU A CD2 1 
ATOM   2642 C  CD2 B LEU A 1 180 ? 17.85500 24.79000 -4.12400  0.440 44.87000  ?  180 LEU A CD2 1 
ATOM   2643 N  N   A GLY A 1 181 ? 22.78400 23.18100 -1.06500  0.560 57.01000  ?  181 GLY A N   1 
ATOM   2644 N  N   B GLY A 1 181 ? 22.59100 23.61300 -1.45400  0.440 55.05000  ?  181 GLY A N   1 
ATOM   2645 C  CA  A GLY A 1 181 ? 23.99400 22.41400 -1.21400  0.560 56.09000  ?  181 GLY A CA  1 
ATOM   2646 C  CA  B GLY A 1 181 ? 23.73700 22.76500 -1.61000  0.440 55.75000  ?  181 GLY A CA  1 
ATOM   2647 C  C   A GLY A 1 181 ? 24.15500 21.36300 -0.13800  0.560 58.24000  ?  181 GLY A C   1 
ATOM   2648 C  C   B GLY A 1 181 ? 23.68300 21.67100 -0.58000  0.440 59.45000  ?  181 GLY A C   1 
ATOM   2649 O  O   A GLY A 1 181 ? 23.21500 21.02800 0.58900   0.560 59.78000  ?  181 GLY A O   1 
ATOM   2650 O  O   B GLY A 1 181 ? 22.63000 21.36000 -0.01500  0.440 58.01000  ?  181 GLY A O   1 
ATOM   2651 N  N   A PRO A 1 182 ? 25.36600 20.82400 -0.01900  0.560 58.43000  ?  182 PRO A N   1 
ATOM   2652 N  N   B PRO A 1 182 ? 24.84300 21.09700 -0.30000  0.440 57.78000  ?  182 PRO A N   1 
ATOM   2653 C  CA  A PRO A 1 182 ? 25.61700 19.74300 0.94800   0.560 62.64000  ?  182 PRO A CA  1 
ATOM   2654 C  CA  B PRO A 1 182 ? 24.95500 20.05300 0.73400   0.440 60.02000  ?  182 PRO A CA  1 
ATOM   2655 C  C   A PRO A 1 182 ? 25.25100 20.13300 2.36900   0.560 59.11000  ?  182 PRO A C   1 
ATOM   2656 C  C   B PRO A 1 182 ? 24.31800 20.43800 2.06400   0.440 60.71000  ?  182 PRO A C   1 
ATOM   2657 O  O   A PRO A 1 182 ? 24.70500 19.30400 3.11500   0.560 63.17000  ?  182 PRO A O   1 
ATOM   2658 O  O   B PRO A 1 182 ? 23.51200 19.65200 2.60000   0.440 58.78000  ?  182 PRO A O   1 
ATOM   2659 C  CB  A PRO A 1 182 ? 27.12700 19.49000 0.80900   0.560 58.53000  ?  182 PRO A CB  1 
ATOM   2660 C  CB  B PRO A 1 182 ? 26.48200 19.86400 0.85000   0.440 59.71000  ?  182 PRO A CB  1 
ATOM   2661 C  CG  A PRO A 1 182 ? 27.43400 19.88100 -0.60900  0.560 57.37000  ?  182 PRO A CG  1 
ATOM   2662 C  CG  B PRO A 1 182 ? 26.99400 20.17400 -0.53200  0.440 57.30000  ?  182 PRO A CG  1 
ATOM   2663 C  CD  A PRO A 1 182 ? 26.51400 21.04300 -0.92200  0.560 56.25000  ?  182 PRO A CD  1 
ATOM   2664 C  CD  B PRO A 1 182 ? 26.10000 21.28700 -1.05400  0.440 56.08000  ?  182 PRO A CD  1 
ATOM   2665 N  N   A PRO A 1 183 ? 25.54700 21.36500 2.80400   0.560 53.40000  ?  183 PRO A N   1 
ATOM   2666 N  N   B PRO A 1 183 ? 24.60800 21.62900 2.64100   0.440 57.40000  ?  183 PRO A N   1 
ATOM   2667 C  CA  A PRO A 1 183 ? 25.22400 21.71600 4.20100   0.560 58.73000  ?  183 PRO A CA  1 
ATOM   2668 C  CA  B PRO A 1 183 ? 24.19500 21.86600 4.03900   0.440 58.34000  ?  183 PRO A CA  1 
ATOM   2669 C  C   A PRO A 1 183 ? 23.74900 21.57400 4.53000   0.560 58.33000  ?  183 PRO A C   1 
ATOM   2670 C  C   B PRO A 1 183 ? 22.69600 21.77500 4.25800   0.440 57.82000  ?  183 PRO A C   1 
ATOM   2671 O  O   A PRO A 1 183 ? 23.40200 21.28800 5.68300   0.560 63.02000  ?  183 PRO A O   1 
ATOM   2672 O  O   B PRO A 1 183 ? 22.24300 21.41300 5.35700   0.440 63.83000  ?  183 PRO A O   1 
ATOM   2673 C  CB  A PRO A 1 183 ? 25.68500 23.17600 4.32400   0.560 51.12000  ?  183 PRO A CB  1 
ATOM   2674 C  CB  B PRO A 1 183 ? 24.69900 23.28800 4.32600   0.440 50.89000  ?  183 PRO A CB  1 
ATOM   2675 C  CG  A PRO A 1 183 ? 26.67300 23.37000 3.22100   0.560 56.48000  ?  183 PRO A CG  1 
ATOM   2676 C  CG  B PRO A 1 183 ? 25.69100 23.57500 3.31500   0.440 53.55000  ?  183 PRO A CG  1 
ATOM   2677 C  CD  A PRO A 1 183 ? 26.21900 22.47400 2.09900   0.560 52.49000  ?  183 PRO A CD  1 
ATOM   2678 C  CD  B PRO A 1 183 ? 25.25700 22.83000 2.08900   0.440 53.57000  ?  183 PRO A CD  1 
ATOM   2679 N  N   A GLY A 1 184 ? 22.87100 21.77400 3.55000   0.560 54.44000  ?  184 GLY A N   1 
ATOM   2680 N  N   B GLY A 1 184 ? 21.91000 22.14100 3.25100   0.440 56.00000  ?  184 GLY A N   1 
ATOM   2681 C  CA  A GLY A 1 184 ? 21.44100 21.71300 3.77500   0.560 58.10000  ?  184 GLY A CA  1 
ATOM   2682 C  CA  B GLY A 1 184 ? 20.46800 22.08900 3.38700   0.440 60.72000  ?  184 GLY A CA  1 
ATOM   2683 C  C   A GLY A 1 184 ? 20.81400 20.45700 3.21300   0.560 63.60000  ?  184 GLY A C   1 
ATOM   2684 C  C   B GLY A 1 184 ? 19.87200 20.88000 2.68200   0.440 61.49000  ?  184 GLY A C   1 
ATOM   2685 O  O   A GLY A 1 184 ? 21.18000 19.34800 3.60900   0.560 72.78000  ?  184 GLY A O   1 
ATOM   2686 O  O   B GLY A 1 184 ? 20.25800 19.74300 2.96900   0.440 62.25000  ?  184 GLY A O   1 
ATOM   2687 N  N   A VAL A 1 185 ? 19.89400 20.60500 2.26300   0.560 62.43000  ?  185 VAL A N   1 
ATOM   2688 N  N   B VAL A 1 185 ? 18.95900 21.11900 1.72900   0.440 64.04000  ?  185 VAL A N   1 
ATOM   2689 C  CA  A VAL A 1 185 ? 19.16600 19.45100 1.74200   0.560 73.58000  ?  185 VAL A CA  1 
ATOM   2690 C  CA  B VAL A 1 185 ? 18.28300 20.05600 0.98500   0.440 68.13000  ?  185 VAL A CA  1 
ATOM   2691 C  C   A VAL A 1 185 ? 20.06800 18.58100 0.87000   0.560 86.29000  ?  185 VAL A C   1 
ATOM   2692 C  C   B VAL A 1 185 ? 19.22600 19.27600 0.08500   0.440 69.37000  ?  185 VAL A C   1 
ATOM   2693 O  O   A VAL A 1 185 ? 19.64100 17.53500 0.36600   0.560 85.74000  ?  185 VAL A O   1 
ATOM   2694 O  O   B VAL A 1 185 ? 18.76300 18.43200 -0.68400  0.440 69.63000  ?  185 VAL A O   1 
ATOM   2695 C  CB  A VAL A 1 185 ? 17.91700 19.87800 0.94600   0.560 69.55000  ?  185 VAL A CB  1 
ATOM   2696 C  CB  B VAL A 1 185 ? 17.10600 20.58000 0.14400   0.440 50.52000  ?  185 VAL A CB  1 
ATOM   2697 C  CG1 A VAL A 1 185 ? 16.88600 20.51700 1.85200   0.560 76.70000  ?  185 VAL A CG1 1 
ATOM   2698 C  CG1 B VAL A 1 185 ? 16.13100 21.26600 1.03400   0.440 69.30000  ?  185 VAL A CG1 1 
ATOM   2699 C  CG2 A VAL A 1 185 ? 18.30600 20.82300 -0.19200  0.560 64.96000  ?  185 VAL A CG2 1 
ATOM   2700 C  CG2 B VAL A 1 185 ? 17.56500 21.52200 -0.89600  0.440 61.20000  ?  185 VAL A CG2 1 
ATOM   2701 N  N   A ALA A 1 186 ? 21.31400 19.00500 0.66700   0.560 94.64000  ?  186 ALA A N   1 
ATOM   2702 N  N   B ALA A 1 186 ? 20.54300 19.51400 0.19400   0.440 92.39000  ?  186 ALA A N   1 
ATOM   2703 C  CA  A ALA A 1 186 ? 22.28600 18.21200 -0.09400  0.560 91.39000  ?  186 ALA A CA  1 
ATOM   2704 C  CA  B ALA A 1 186 ? 21.59400 18.68200 -0.42200  0.440 89.63000  ?  186 ALA A CA  1 
ATOM   2705 C  C   A ALA A 1 186 ? 21.77400 17.90200 -1.50100  0.560 93.20000  ?  186 ALA A C   1 
ATOM   2706 C  C   B ALA A 1 186 ? 21.30500 18.36600 -1.88300  0.440 91.14000  ?  186 ALA A C   1 
ATOM   2707 O  O   A ALA A 1 186 ? 22.02100 16.82600 -2.05400  0.560 103.02000 ?  186 ALA A O   1 
ATOM   2708 O  O   B ALA A 1 186 ? 21.81100 17.37200 -2.43500  0.440 100.25000 ?  186 ALA A O   1 
ATOM   2709 C  CB  A ALA A 1 186 ? 22.63600 16.91700 0.64400   0.560 93.62000  ?  186 ALA A CB  1 
ATOM   2710 C  CB  B ALA A 1 186 ? 21.82400 17.38500 0.36800   0.440 93.32000  ?  186 ALA A CB  1 
ATOM   2711 N  N   A LEU A 1 187 ? 21.04100 18.85100 -2.08000  0.560 78.73000  ?  187 LEU A N   1 
ATOM   2712 N  N   B LEU A 1 187 ? 20.48900 19.20700 -2.51700  0.440 74.34000  ?  187 LEU A N   1 
ATOM   2713 C  CA  A LEU A 1 187 ? 20.52600 18.69000 -3.43900  0.560 69.38000  ?  187 LEU A CA  1 
ATOM   2714 C  CA  B LEU A 1 187 ? 20.14600 19.06900 -3.92200  0.440 66.02000  ?  187 LEU A CA  1 
ATOM   2715 C  C   A LEU A 1 187 ? 21.63800 18.94100 -4.45300  0.560 78.86000  ?  187 LEU A C   1 
ATOM   2716 C  C   B LEU A 1 187 ? 21.38600 19.28000 -4.74600  0.440 77.67000  ?  187 LEU A C   1 
ATOM   2717 O  O   A LEU A 1 187 ? 22.10400 18.01600 -5.12400  0.560 87.94000  ?  187 LEU A O   1 
ATOM   2718 O  O   B LEU A 1 187 ? 22.02500 18.29600 -5.15100  0.440 87.09000  ?  187 LEU A O   1 
ATOM   2719 C  CB  A LEU A 1 187 ? 19.34500 19.64100 -3.65200  0.560 65.33000  ?  187 LEU A CB  1 
ATOM   2720 C  CB  B LEU A 1 187 ? 19.12100 20.09700 -4.33000  0.440 65.05000  ?  187 LEU A CB  1 
ATOM   2721 C  CG  A LEU A 1 187 ? 18.35900 19.38700 -4.79000  0.560 63.04000  ?  187 LEU A CG  1 
ATOM   2722 C  CG  B LEU A 1 187 ? 18.29000 19.88800 -5.56500  0.440 59.89000  ?  187 LEU A CG  1 
ATOM   2723 C  CD1 A LEU A 1 187 ? 17.92600 17.94500 -4.89000  0.560 65.52000  ?  187 LEU A CD1 1 
ATOM   2724 C  CD1 B LEU A 1 187 ? 17.61400 18.55700 -5.53300  0.440 55.54000  ?  187 LEU A CD1 1 
ATOM   2725 C  CD2 A LEU A 1 187 ? 17.13500 20.30000 -4.60600  0.560 62.15000  ?  187 LEU A CD2 1 
ATOM   2726 C  CD2 B LEU A 1 187 ? 17.30800 20.96000 -5.52100  0.440 60.13000  ?  187 LEU A CD2 1 
ATOM   2727 N  N   A LEU A 1 188 ? 22.08200 20.19200 -4.56500  0.560 70.01000  ?  188 LEU A N   1 
ATOM   2728 N  N   B LEU A 1 188 ? 21.71300 20.56000 -4.99900  0.440 69.77000  ?  188 LEU A N   1 
ATOM   2729 C  CA  A LEU A 1 188 ? 23.22000 20.50300 -5.41700  0.560 64.18000  ?  188 LEU A CA  1 
ATOM   2730 C  CA  B LEU A 1 188 ? 22.95900 20.90100 -5.66600  0.440 63.70000  ?  188 LEU A CA  1 
ATOM   2731 C  C   A LEU A 1 188 ? 24.43300 19.68400 -4.99500  0.560 66.40000  ?  188 LEU A C   1 
ATOM   2732 C  C   B LEU A 1 188 ? 24.05200 19.98200 -5.19200  0.440 65.23000  ?  188 LEU A C   1 
ATOM   2733 O  O   A LEU A 1 188 ? 24.66100 19.44700 -3.80500  0.560 68.46000  ?  188 LEU A O   1 
ATOM   2734 O  O   B LEU A 1 188 ? 24.13500 19.63400 -4.01000  0.440 65.61000  ?  188 LEU A O   1 
ATOM   2735 C  CB  A LEU A 1 188 ? 23.55100 21.99100 -5.33900  0.560 56.53000  ?  188 LEU A CB  1 
ATOM   2736 C  CB  B LEU A 1 188 ? 23.40500 22.33700 -5.38700  0.440 55.58000  ?  188 LEU A CB  1 
ATOM   2737 C  CG  A LEU A 1 188 ? 22.54500 22.95800 -5.95300  0.560 54.54000  ?  188 LEU A CG  1 
ATOM   2738 C  CG  B LEU A 1 188 ? 22.49400 23.40100 -5.89500  0.440 54.65000  ?  188 LEU A CG  1 
ATOM   2739 C  CD1 A LEU A 1 188 ? 22.91000 24.38600 -5.58400  0.560 54.03000  ?  188 LEU A CD1 1 
ATOM   2740 C  CD1 B LEU A 1 188 ? 23.12900 24.66300 -5.46700  0.440 54.25000  ?  188 LEU A CD1 1 
ATOM   2741 C  CD2 A LEU A 1 188 ? 22.50100 22.79200 -7.46000  0.560 68.14000  ?  188 LEU A CD2 1 
ATOM   2742 C  CD2 B LEU A 1 188 ? 22.39600 23.32500 -7.39300  0.440 64.74000  ?  188 LEU A CD2 1 
ATOM   2743 N  N   A THR A 1 189 ? 25.21900 19.25600 -5.97700  0.560 59.46000  ?  189 THR A N   1 
ATOM   2744 N  N   B THR A 1 189 ? 24.85100 19.63800 -6.08600  0.440 62.26000  ?  189 THR A N   1 
ATOM   2745 C  CA  A THR A 1 189 ? 26.41200 18.47400 -5.70000  0.560 53.80000  ?  189 THR A CA  1 
ATOM   2746 C  CA  B THR A 1 189 ? 25.99200 18.76600 -5.99300  0.440 56.93000  ?  189 THR A CA  1 
ATOM   2747 C  C   A THR A 1 189 ? 27.53200 19.37400 -5.19300  0.560 54.76000  ?  189 THR A C   1 
ATOM   2748 C  C   B THR A 1 189 ? 27.20300 19.56300 -5.49200  0.440 54.41000  ?  189 THR A C   1 
ATOM   2749 O  O   A THR A 1 189 ? 27.52300 20.58600 -5.42400  0.560 53.61000  ?  189 THR A O   1 
ATOM   2750 O  O   B THR A 1 189 ? 27.36100 20.74700 -5.82200  0.440 56.52000  ?  189 THR A O   1 
ATOM   2751 C  CB  A THR A 1 189 ? 26.86500 17.74000 -6.95700  0.560 59.28000  ?  189 THR A CB  1 
ATOM   2752 C  CB  B THR A 1 189 ? 26.24500 18.18100 -7.38000  0.440 60.05000  ?  189 THR A CB  1 
ATOM   2753 O  OG1 A THR A 1 189 ? 27.19300 18.69400 -7.97500  0.560 58.68000  ?  189 THR A OG1 1 
ATOM   2754 O  OG1 B THR A 1 189 ? 26.77100 19.19700 -8.22500  0.440 58.25000  ?  189 THR A OG1 1 
ATOM   2755 C  CG2 A THR A 1 189 ? 25.76600 16.81600 -7.46100  0.560 68.11000  ?  189 THR A CG2 1 
ATOM   2756 C  CG2 B THR A 1 189 ? 24.90100 17.81300 -8.01400  0.440 57.91000  ?  189 THR A CG2 1 
ATOM   2757 N  N   A PRO A 1 190 ? 28.51800 18.80200 -4.49600  0.560 58.19000  ?  190 PRO A N   1 
ATOM   2758 N  N   B PRO A 1 190 ? 28.03100 18.97200 -4.68400  0.440 54.15000  ?  190 PRO A N   1 
ATOM   2759 C  CA  A PRO A 1 190 ? 29.61400 19.64500 -3.98300  0.560 50.91000  ?  190 PRO A CA  1 
ATOM   2760 C  CA  B PRO A 1 190 ? 29.19000 19.70400 -4.15400  0.440 52.11000  ?  190 PRO A CA  1 
ATOM   2761 C  C   A PRO A 1 190 ? 30.30700 20.44400 -5.07300  0.560 50.62000  ?  190 PRO A C   1 
ATOM   2762 C  C   B PRO A 1 190 ? 30.08000 20.35400 -5.20500  0.440 50.61000  ?  190 PRO A C   1 
ATOM   2763 O  O   A PRO A 1 190 ? 30.63500 21.61900 -4.86600  0.560 50.27000  ?  190 PRO A O   1 
ATOM   2764 O  O   B PRO A 1 190 ? 30.59200 21.45200 -4.97800  0.440 50.00000  ?  190 PRO A O   1 
ATOM   2765 C  CB  A PRO A 1 190 ? 30.56100 18.63000 -3.32200  0.560 51.85000  ?  190 PRO A CB  1 
ATOM   2766 C  CB  B PRO A 1 190 ? 29.93200 18.62000 -3.37100  0.440 52.49000  ?  190 PRO A CB  1 
ATOM   2767 C  CG  A PRO A 1 190 ? 29.70200 17.42700 -3.03000  0.560 51.78000  ?  190 PRO A CG  1 
ATOM   2768 C  CG  B PRO A 1 190 ? 28.82600 17.72700 -2.86400  0.440 54.75000  ?  190 PRO A CG  1 
ATOM   2769 C  CD  A PRO A 1 190 ? 28.68500 17.38000 -4.14100  0.560 53.09000  ?  190 PRO A CD  1 
ATOM   2770 C  CD  B PRO A 1 190 ? 27.77200 17.71300 -3.96200  0.440 49.19000  ?  190 PRO A CD  1 
ATOM   2771 N  N   A THR A 1 191 ? 30.52800 19.84200 -6.24200  0.560 55.06000  ?  191 THR A N   1 
ATOM   2772 N  N   B THR A 1 191 ? 30.30900 19.70100 -6.34400  0.440 54.63000  ?  191 THR A N   1 
ATOM   2773 C  CA  A THR A 1 191 ? 31.27000 20.52900 -7.29400  0.560 53.13000  ?  191 THR A CA  1 
ATOM   2774 C  CA  B THR A 1 191 ? 31.04100 20.38100 -7.41000  0.440 53.32000  ?  191 THR A CA  1 
ATOM   2775 C  C   A THR A 1 191 ? 30.51100 21.75200 -7.79400  0.560 42.77000  ?  191 THR A C   1 
ATOM   2776 C  C   B THR A 1 191 ? 30.32200 21.66300 -7.78500  0.440 43.07000  ?  191 THR A C   1 
ATOM   2777 O  O   A THR A 1 191 ? 31.08600 22.83800 -7.93400  0.560 46.37000  ?  191 THR A O   1 
ATOM   2778 O  O   B THR A 1 191 ? 30.91700 22.74600 -7.80000  0.440 46.48000  ?  191 THR A O   1 
ATOM   2779 C  CB  A THR A 1 191 ? 31.55800 19.57000 -8.44900  0.560 49.23000  ?  191 THR A CB  1 
ATOM   2780 C  CB  B THR A 1 191 ? 31.20800 19.48000 -8.63700  0.440 48.41000  ?  191 THR A CB  1 
ATOM   2781 O  OG1 A THR A 1 191 ? 32.44200 18.53500 -8.00100  0.560 58.42000  ?  191 THR A OG1 1 
ATOM   2782 O  OG1 B THR A 1 191 ? 31.99300 18.34100 -8.28400  0.440 56.92000  ?  191 THR A OG1 1 
ATOM   2783 C  CG2 A THR A 1 191 ? 32.19300 20.31800 -9.60900  0.560 50.11000  ?  191 THR A CG2 1 
ATOM   2784 C  CG2 B THR A 1 191 ? 31.93200 20.23500 -9.74300  0.440 50.20000  ?  191 THR A CG2 1 
ATOM   2785 N  N   A VAL A 1 192 ? 29.22000 21.59100 -8.08500  0.560 47.63000  ?  192 VAL A N   1 
ATOM   2786 N  N   B VAL A 1 192 ? 29.01300 21.55400 -8.02100  0.440 47.99000  ?  192 VAL A N   1 
ATOM   2787 C  CA  A VAL A 1 192 ? 28.42400 22.72800 -8.53100  0.560 42.41000  ?  192 VAL A CA  1 
ATOM   2788 C  CA  B VAL A 1 192 ? 28.18800 22.69000 -8.42200  0.440 43.12000  ?  192 VAL A CA  1 
ATOM   2789 C  C   A VAL A 1 192 ? 28.30000 23.75700 -7.41600  0.560 46.16000  ?  192 VAL A C   1 
ATOM   2790 C  C   B VAL A 1 192 ? 28.03300 23.63400 -7.25700  0.440 47.21000  ?  192 VAL A C   1 
ATOM   2791 O  O   A VAL A 1 192 ? 28.43200 24.96500 -7.64800  0.560 46.52000  ?  192 VAL A O   1 
ATOM   2792 O  O   B VAL A 1 192 ? 27.95800 24.86400 -7.41800  0.440 46.13000  ?  192 VAL A O   1 
ATOM   2793 C  CB  A VAL A 1 192 ? 27.04300 22.25300 -9.02200  0.560 48.96000  ?  192 VAL A CB  1 
ATOM   2794 C  CB  B VAL A 1 192 ? 26.81900 22.17900 -8.91800  0.440 49.32000  ?  192 VAL A CB  1 
ATOM   2795 C  CG1 A VAL A 1 192 ? 26.18400 23.44100 -9.42700  0.560 50.16000  ?  192 VAL A CG1 1 
ATOM   2796 C  CG1 B VAL A 1 192 ? 25.78900 23.31200 -8.97400  0.440 51.74000  ?  192 VAL A CG1 1 
ATOM   2797 C  CG2 A VAL A 1 192 ? 27.20200 21.27300 -10.17400 0.560 44.52000  ?  192 VAL A CG2 1 
ATOM   2798 C  CG2 B VAL A 1 192 ? 26.97200 21.47800 -10.25900 0.440 44.74000  ?  192 VAL A CG2 1 
ATOM   2799 N  N   A ASP A 1 193 ? 28.05100 23.29900 -6.18700  0.560 50.40000  ?  193 ASP A N   1 
ATOM   2800 N  N   B ASP A 1 193 ? 27.97100 23.07000 -6.05200  0.440 50.58000  ?  193 ASP A N   1 
ATOM   2801 C  CA  A ASP A 1 193 ? 27.89200 24.23100 -5.07600  0.560 44.84000  ?  193 ASP A CA  1 
ATOM   2802 C  CA  B ASP A 1 193 ? 27.99900 23.92200 -4.89000  0.440 45.54000  ?  193 ASP A CA  1 
ATOM   2803 C  C   A ASP A 1 193 ? 29.15500 25.05500 -4.86300  0.560 42.00000  ?  193 ASP A C   1 
ATOM   2804 C  C   B ASP A 1 193 ? 29.23600 24.78700 -4.91900  0.440 41.87000  ?  193 ASP A C   1 
ATOM   2805 O  O   A ASP A 1 193 ? 29.08600 26.27100 -4.64600  0.560 47.80000  ?  193 ASP A O   1 
ATOM   2806 O  O   B ASP A 1 193 ? 29.15400 26.00900 -4.79700  0.440 46.37000  ?  193 ASP A O   1 
ATOM   2807 C  CB  A ASP A 1 193 ? 27.53400 23.47000 -3.80400  0.560 46.60000  ?  193 ASP A CB  1 
ATOM   2808 C  CB  B ASP A 1 193 ? 27.95700 23.11700 -3.60900  0.440 47.81000  ?  193 ASP A CB  1 
ATOM   2809 C  CG  A ASP A 1 193 ? 26.88200 24.35400 -2.77200  0.560 55.56000  ?  193 ASP A CG  1 
ATOM   2810 C  CG  B ASP A 1 193 ? 27.75700 24.01700 -2.40600  0.440 51.43000  ?  193 ASP A CG  1 
ATOM   2811 O  OD1 A ASP A 1 193 ? 25.71000 24.73100 -2.97700  0.560 56.55000  ?  193 ASP A OD1 1 
ATOM   2812 O  OD1 B ASP A 1 193 ? 26.61400 24.50800 -2.23600  0.440 59.90000  ?  193 ASP A OD1 1 
ATOM   2813 O  OD2 A ASP A 1 193 ? 27.54100 24.68000 -1.76500  0.560 54.11000  -1 193 ASP A OD2 1 
ATOM   2814 O  OD2 B ASP A 1 193 ? 28.76200 24.30900 -1.69700  0.440 41.63000  -1 193 ASP A OD2 1 
ATOM   2815 N  N   A VAL A 1 194 ? 30.31800 24.40600 -4.92500  0.560 40.27000  ?  194 VAL A N   1 
ATOM   2816 N  N   B VAL A 1 194 ? 30.39500 24.17200 -5.12000  0.440 42.13000  ?  194 VAL A N   1 
ATOM   2817 C  CA  A VAL A 1 194 ? 31.58400 25.11500 -4.77200  0.560 41.17000  ?  194 VAL A CA  1 
ATOM   2818 C  CA  B VAL A 1 194 ? 31.65100 24.88600 -4.92300  0.440 41.79000  ?  194 VAL A CA  1 
ATOM   2819 C  C   A VAL A 1 194 ? 31.78100 26.09800 -5.91800  0.560 45.86000  ?  194 VAL A C   1 
ATOM   2820 C  C   B VAL A 1 194 ? 31.89100 25.88900 -6.05400  0.440 46.67000  ?  194 VAL A C   1 
ATOM   2821 O  O   A VAL A 1 194 ? 32.17500 27.25100 -5.70800  0.560 37.49000  ?  194 VAL A O   1 
ATOM   2822 O  O   B VAL A 1 194 ? 32.36500 27.00800 -5.80500  0.440 39.76000  ?  194 VAL A O   1 
ATOM   2823 C  CB  A VAL A 1 194 ? 32.74400 24.10800 -4.67900  0.560 42.71000  ?  194 VAL A CB  1 
ATOM   2824 C  CB  B VAL A 1 194 ? 32.81900 23.88700 -4.73500  0.440 42.86000  ?  194 VAL A CB  1 
ATOM   2825 C  CG1 A VAL A 1 194 ? 34.06700 24.77000 -4.99400  0.560 42.28000  ?  194 VAL A CG1 1 
ATOM   2826 C  CG1 B VAL A 1 194 ? 34.14900 24.52500 -5.02100  0.440 42.63000  ?  194 VAL A CG1 1 
ATOM   2827 C  CG2 A VAL A 1 194 ? 32.77100 23.46000 -3.29600  0.560 45.79000  ?  194 VAL A CG2 1 
ATOM   2828 C  CG2 B VAL A 1 194 ? 32.82300 23.35200 -3.29100  0.440 45.71000  ?  194 VAL A CG2 1 
ATOM   2829 N  N   A ALA A 1 195 ? 31.50600 25.65800 -7.14900  0.560 48.06000  ?  195 ALA A N   1 
ATOM   2830 N  N   B ALA A 1 195 ? 31.55000 25.54300 -7.31100  0.440 47.75000  ?  195 ALA A N   1 
ATOM   2831 C  CA  A ALA A 1 195 ? 31.66500 26.54500 -8.29800  0.560 44.75000  ?  195 ALA A CA  1 
ATOM   2832 C  CA  B ALA A 1 195 ? 31.81300 26.49700 -8.41100  0.440 44.59000  ?  195 ALA A CA  1 
ATOM   2833 C  C   A ALA A 1 195 ? 30.84200 27.81400 -8.13000  0.560 36.89000  ?  195 ALA A C   1 
ATOM   2834 C  C   B ALA A 1 195 ? 31.00600 27.78800 -8.23700  0.440 37.43000  ?  195 ALA A C   1 
ATOM   2835 O  O   A ALA A 1 195 ? 31.32100 28.91800 -8.41500  0.560 30.01000  ?  195 ALA A O   1 
ATOM   2836 O  O   B ALA A 1 195 ? 31.52400 28.89900 -8.45100  0.440 29.72000  ?  195 ALA A O   1 
ATOM   2837 C  CB  A ALA A 1 195 ? 31.26800 25.81800 -9.58300  0.560 41.96000  ?  195 ALA A CB  1 
ATOM   2838 C  CB  B ALA A 1 195 ? 31.50600 25.87400 -9.77000  0.440 41.72000  ?  195 ALA A CB  1 
ATOM   2839 N  N   A LEU A 1 196 ? 29.60000 27.68100 -7.66200  0.560 30.19000  ?  196 LEU A N   1 
ATOM   2840 N  N   B LEU A 1 196 ? 29.74800 27.64500 -7.81200  0.440 30.19000  ?  196 LEU A N   1 
ATOM   2841 C  CA  A LEU A 1 196 ? 28.76200 28.85900 -7.47500  0.560 35.47000  ?  196 LEU A CA  1 
ATOM   2842 C  CA  B LEU A 1 196 ? 28.83000 28.75500 -7.63200  0.440 35.26000  ?  196 LEU A CA  1 
ATOM   2843 C  C   A LEU A 1 196 ? 29.32600 29.77300 -6.39100  0.560 43.30000  ?  196 LEU A C   1 
ATOM   2844 C  C   B LEU A 1 196 ? 29.20500 29.62200 -6.45500  0.440 43.76000  ?  196 LEU A C   1 
ATOM   2845 O  O   A LEU A 1 196 ? 29.28400 31.00000 -6.52700  0.560 42.05000  ?  196 LEU A O   1 
ATOM   2846 O  O   B LEU A 1 196 ? 28.72800 30.75000 -6.36900  0.440 44.06000  ?  196 LEU A O   1 
ATOM   2847 C  CB  A LEU A 1 196 ? 27.33100 28.43400 -7.14600  0.560 37.41000  ?  196 LEU A CB  1 
ATOM   2848 C  CB  B LEU A 1 196 ? 27.40200 28.27100 -7.36700  0.440 38.50000  ?  196 LEU A CB  1 
ATOM   2849 C  CG  A LEU A 1 196 ? 26.56900 27.79000 -8.30800  0.560 39.93000  ?  196 LEU A CG  1 
ATOM   2850 C  CG  B LEU A 1 196 ? 26.55400 27.74500 -8.49400  0.440 40.48000  ?  196 LEU A CG  1 
ATOM   2851 C  CD1 A LEU A 1 196 ? 25.26800 27.16800 -7.82900  0.560 40.55000  ?  196 LEU A CD1 1 
ATOM   2852 C  CD1 B LEU A 1 196 ? 25.16900 27.27900 -7.97100  0.440 40.50000  ?  196 LEU A CD1 1 
ATOM   2853 C  CD2 A LEU A 1 196 ? 26.30300 28.81300 -9.40600  0.560 46.34000  ?  196 LEU A CD2 1 
ATOM   2854 C  CD2 B LEU A 1 196 ? 26.42600 28.89300 -9.49600  0.440 45.98000  ?  196 LEU A CD2 1 
ATOM   2855 N  N   A ILE A 1 197 ? 29.88000 29.20400 -5.31900  0.560 36.87000  ?  197 ILE A N   1 
ATOM   2856 N  N   B ILE A 1 197 ? 29.95800 29.10300 -5.49100  0.440 37.79000  ?  197 ILE A N   1 
ATOM   2857 C  CA  A ILE A 1 197 ? 30.37700 30.04800 -4.23600  0.560 39.63000  ?  197 ILE A CA  1 
ATOM   2858 C  CA  B ILE A 1 197 ? 30.39300 29.96100 -4.39900  0.440 39.34000  ?  197 ILE A CA  1 
ATOM   2859 C  C   A ILE A 1 197 ? 31.70500 30.69700 -4.61700  0.560 40.43000  ?  197 ILE A C   1 
ATOM   2860 C  C   B ILE A 1 197 ? 31.75800 30.56800 -4.69600  0.440 40.04000  ?  197 ILE A C   1 
ATOM   2861 O  O   A ILE A 1 197 ? 31.97600 31.84100 -4.23400  0.560 37.54000  ?  197 ILE A O   1 
ATOM   2862 O  O   B ILE A 1 197 ? 32.03100 31.71300 -4.29800  0.440 37.92000  ?  197 ILE A O   1 
ATOM   2863 C  CB  A ILE A 1 197 ? 30.48600 29.24300 -2.92800  0.560 38.25000  ?  197 ILE A CB  1 
ATOM   2864 C  CB  B ILE A 1 197 ? 30.33700 29.19800 -3.03700  0.440 39.39000  ?  197 ILE A CB  1 
ATOM   2865 C  CG1 A ILE A 1 197 ? 29.08900 29.01700 -2.34500  0.560 42.18000  ?  197 ILE A CG1 1 
ATOM   2866 C  CG1 B ILE A 1 197 ? 28.90100 29.36500 -2.50600  0.440 41.46000  ?  197 ILE A CG1 1 
ATOM   2867 C  CG2 A ILE A 1 197 ? 31.35600 29.98300 -1.91500  0.560 33.13000  ?  197 ILE A CG2 1 
ATOM   2868 C  CG2 B ILE A 1 197 ? 31.42800 29.68800 -2.05500  0.440 34.18000  ?  197 ILE A CG2 1 
ATOM   2869 C  CD1 A ILE A 1 197 ? 28.93500 27.72300 -1.58600  0.560 46.98000  ?  197 ILE A CD1 1 
ATOM   2870 C  CD1 B ILE A 1 197 ? 28.25900 28.18400 -1.99000  0.440 44.38000  ?  197 ILE A CD1 1 
ATOM   2871 N  N   A VAL A 1 198 ? 32.55900 29.99500 -5.36600  0.560 38.22000  ?  198 VAL A N   1 
ATOM   2872 N  N   B VAL A 1 198 ? 32.66600 29.82900 -5.35900  0.440 37.93000  ?  198 VAL A N   1 
ATOM   2873 C  CA  A VAL A 1 198 ? 33.77900 30.64500 -5.84100  0.560 38.86000  ?  198 VAL A CA  1 
ATOM   2874 C  CA  B VAL A 1 198 ? 33.89700 30.48700 -5.81600  0.440 39.21000  ?  198 VAL A CA  1 
ATOM   2875 C  C   A VAL A 1 198 ? 33.42200 31.87200 -6.67000  0.560 36.19000  ?  198 VAL A C   1 
ATOM   2876 C  C   B VAL A 1 198 ? 33.53400 31.66000 -6.67200  0.440 36.33000  ?  198 VAL A C   1 
ATOM   2877 O  O   A VAL A 1 198 ? 34.05800 32.92800 -6.55500  0.560 42.30000  ?  198 VAL A O   1 
ATOM   2878 O  O   B VAL A 1 198 ? 34.07500 32.75900 -6.51400  0.440 42.28000  ?  198 VAL A O   1 
ATOM   2879 C  CB  A VAL A 1 198 ? 34.66100 29.67000 -6.64400  0.560 42.18000  ?  198 VAL A CB  1 
ATOM   2880 C  CB  B VAL A 1 198 ? 34.82600 29.55100 -6.59700  0.440 42.17000  ?  198 VAL A CB  1 
ATOM   2881 C  CG1 A VAL A 1 198 ? 35.76000 30.44600 -7.36900  0.560 43.07000  ?  198 VAL A CG1 1 
ATOM   2882 C  CG1 B VAL A 1 198 ? 35.94200 30.37100 -7.19700  0.440 43.26000  ?  198 VAL A CG1 1 
ATOM   2883 C  CG2 A VAL A 1 198 ? 35.25800 28.61500 -5.73900  0.560 40.19000  ?  198 VAL A CG2 1 
ATOM   2884 C  CG2 B VAL A 1 198 ? 35.39800 28.51100 -5.69600  0.440 40.45000  ?  198 VAL A CG2 1 
ATOM   2885 N  N   A TYR A 1 199 ? 32.40200 31.75300 -7.52300  0.560 34.58000  ?  199 TYR A N   1 
ATOM   2886 N  N   B TYR A 1 199 ? 32.53600 31.48000 -7.52500  0.440 35.47000  ?  199 TYR A N   1 
ATOM   2887 C  CA  A TYR A 1 199 ? 31.98300 32.89700 -8.32300  0.560 37.74000  ?  199 TYR A CA  1 
ATOM   2888 C  CA  B TYR A 1 199 ? 32.06900 32.63900 -8.26800  0.440 37.39000  ?  199 TYR A CA  1 
ATOM   2889 C  C   A TYR A 1 199 ? 31.51800 34.04200 -7.43300  0.560 38.47000  ?  199 TYR A C   1 
ATOM   2890 C  C   B TYR A 1 199 ? 31.62900 33.75400 -7.30800  0.440 37.86000  ?  199 TYR A C   1 
ATOM   2891 O  O   A TYR A 1 199 ? 31.89400 35.20100 -7.64000  0.560 34.02000  ?  199 TYR A O   1 
ATOM   2892 O  O   B TYR A 1 199 ? 32.28500 34.80500 -7.25100  0.440 40.51000  ?  199 TYR A O   1 
ATOM   2893 C  CB  A TYR A 1 199 ? 30.86600 32.50200 -9.28600  0.560 32.56000  ?  199 TYR A CB  1 
ATOM   2894 C  CB  B TYR A 1 199 ? 30.97300 32.24400 -9.28700  0.440 32.77000  ?  199 TYR A CB  1 
ATOM   2895 C  CG  A TYR A 1 199 ? 30.30500 33.70200 -10.02200 0.560 32.30000  ?  199 TYR A CG  1 
ATOM   2896 C  CG  B TYR A 1 199 ? 30.50000 33.40300 -10.11600 0.440 32.19000  ?  199 TYR A CG  1 
ATOM   2897 C  CD1 A TYR A 1 199 ? 30.95400 34.21600 -11.13700 0.560 32.57000  ?  199 TYR A CD1 1 
ATOM   2898 C  CD1 B TYR A 1 199 ? 31.30000 33.94900 -11.10700 0.440 31.57000  ?  199 TYR A CD1 1 
ATOM   2899 C  CD2 A TYR A 1 199 ? 29.14600 34.33700 -9.58700  0.560 37.52000  ?  199 TYR A CD2 1 
ATOM   2900 C  CD2 B TYR A 1 199 ? 29.26000 33.97400 -9.89600  0.440 36.50000  ?  199 TYR A CD2 1 
ATOM   2901 C  CE1 A TYR A 1 199 ? 30.46400 35.31300 -11.80800 0.560 36.12000  ?  199 TYR A CE1 1 
ATOM   2902 C  CE1 B TYR A 1 199 ? 30.86300 35.07700 -11.85000 0.440 35.40000  ?  199 TYR A CE1 1 
ATOM   2903 C  CE2 A TYR A 1 199 ? 28.64500 35.44200 -10.25300 0.560 31.92000  ?  199 TYR A CE2 1 
ATOM   2904 C  CE2 B TYR A 1 199 ? 28.84200 35.08500 -10.61900 0.440 34.01000  ?  199 TYR A CE2 1 
ATOM   2905 C  CZ  A TYR A 1 199 ? 29.30900 35.92500 -11.36700 0.560 37.12000  ?  199 TYR A CZ  1 
ATOM   2906 C  CZ  B TYR A 1 199 ? 29.64200 35.61600 -11.60200 0.440 37.08000  ?  199 TYR A CZ  1 
ATOM   2907 O  OH  A TYR A 1 199 ? 28.83200 37.02500 -12.04800 0.560 35.32000  ?  199 TYR A OH  1 
ATOM   2908 O  OH  B TYR A 1 199 ? 29.17300 36.68100 -12.34000 0.440 34.84000  ?  199 TYR A OH  1 
ATOM   2909 N  N   A LEU A 1 200 ? 30.69500 33.73200 -6.42700  0.560 35.89000  ?  200 LEU A N   1 
ATOM   2910 N  N   B LEU A 1 200 ? 30.52600 33.54200 -6.54800  0.440 35.41000  ?  200 LEU A N   1 
ATOM   2911 C  CA  A LEU A 1 200 ? 30.15300 34.78000 -5.56400  0.560 32.98000  ?  200 LEU A CA  1 
ATOM   2912 C  CA  B LEU A 1 200 ? 30.03200 34.55600 -5.61200  0.440 33.71000  ?  200 LEU A CA  1 
ATOM   2913 C  C   A LEU A 1 200 ? 31.25400 35.43200 -4.73200  0.560 31.91000  ?  200 LEU A C   1 
ATOM   2914 C  C   B LEU A 1 200 ? 31.15700 35.24900 -4.86000  0.440 31.59000  ?  200 LEU A C   1 
ATOM   2915 O  O   A LEU A 1 200 ? 31.30300 36.66200 -4.60200  0.560 37.79000  ?  200 LEU A O   1 
ATOM   2916 O  O   B LEU A 1 200 ? 31.20600 36.47700 -4.77500  0.440 36.47000  ?  200 LEU A O   1 
ATOM   2917 C  CB  A LEU A 1 200 ? 29.06200 34.20600 -4.65600  0.560 38.93000  ?  200 LEU A CB  1 
ATOM   2918 C  CB  B LEU A 1 200 ? 29.07600 33.92000 -4.60900  0.440 38.42000  ?  200 LEU A CB  1 
ATOM   2919 C  CG  A LEU A 1 200 ? 27.73800 33.83500 -5.32300  0.560 42.98000  ?  200 LEU A CG  1 
ATOM   2920 C  CG  B LEU A 1 200 ? 27.66000 33.61500 -5.09100  0.440 42.36000  ?  200 LEU A CG  1 
ATOM   2921 C  CD1 A LEU A 1 200 ? 26.87000 33.00800 -4.36900  0.560 37.23000  ?  200 LEU A CD1 1 
ATOM   2922 C  CD1 B LEU A 1 200 ? 26.76200 32.97300 -4.01800  0.440 35.74000  ?  200 LEU A CD1 1 
ATOM   2923 C  CD2 A LEU A 1 200 ? 26.97400 35.05900 -5.79400  0.560 35.08000  ?  200 LEU A CD2 1 
ATOM   2924 C  CD2 B LEU A 1 200 ? 26.96500 34.86400 -5.62800  0.440 36.11000  ?  200 LEU A CD2 1 
ATOM   2925 N  N   A ASP A 1 201 ? 32.14400 34.62200 -4.15200  0.560 31.16000  ?  201 ASP A N   1 
ATOM   2926 N  N   B ASP A 1 201 ? 32.07200 34.47700 -4.29900  0.440 31.61000  ?  201 ASP A N   1 
ATOM   2927 C  CA  A ASP A 1 201 ? 33.26200 35.17900 -3.39300  0.560 39.04000  ?  201 ASP A CA  1 
ATOM   2928 C  CA  B ASP A 1 201 ? 33.14100 35.06900 -3.50800  0.440 38.99000  ?  201 ASP A CA  1 
ATOM   2929 C  C   A ASP A 1 201 ? 34.05700 36.16100 -4.24300  0.560 40.77000  ?  201 ASP A C   1 
ATOM   2930 C  C   B ASP A 1 201 ? 34.03000 35.96800 -4.36300  0.440 40.82000  ?  201 ASP A C   1 
ATOM   2931 O  O   A ASP A 1 201 ? 34.37500 37.27100 -3.80300  0.560 37.63000  ?  201 ASP A O   1 
ATOM   2932 O  O   B ASP A 1 201 ? 34.49100 37.02700 -3.90700  0.440 38.20000  ?  201 ASP A O   1 
ATOM   2933 C  CB  A ASP A 1 201 ? 34.17700 34.06100 -2.88800  0.560 33.64000  ?  201 ASP A CB  1 
ATOM   2934 C  CB  B ASP A 1 201 ? 33.95700 33.95100 -2.84000  0.440 34.63000  ?  201 ASP A CB  1 
ATOM   2935 C  CG  A ASP A 1 201 ? 33.61300 33.33700 -1.67700  0.560 37.07000  ?  201 ASP A CG  1 
ATOM   2936 C  CG  B ASP A 1 201 ? 33.21500 33.30100 -1.69300  0.440 38.48000  ?  201 ASP A CG  1 
ATOM   2937 O  OD1 A ASP A 1 201 ? 32.54200 33.74200 -1.17700  0.560 37.01000  ?  201 ASP A OD1 1 
ATOM   2938 O  OD1 B ASP A 1 201 ? 32.16100 33.85800 -1.25100  0.440 35.73000  ?  201 ASP A OD1 1 
ATOM   2939 O  OD2 A ASP A 1 201 ? 34.24900 32.36000 -1.22700  0.560 41.12000  -1 201 ASP A OD2 1 
ATOM   2940 O  OD2 B ASP A 1 201 ? 33.65400 32.20300 -1.27000  0.440 38.76000  -1 201 ASP A OD2 1 
ATOM   2941 N  N   A LEU A 1 202 ? 34.39300 35.76200 -5.47100  0.560 38.22000  ?  202 LEU A N   1 
ATOM   2942 N  N   B LEU A 1 202 ? 34.34000 35.53800 -5.58300  0.440 37.98000  ?  202 LEU A N   1 
ATOM   2943 C  CA  A LEU A 1 202 ? 35.18200 36.63200 -6.33600  0.560 37.89000  ?  202 LEU A CA  1 
ATOM   2944 C  CA  B LEU A 1 202 ? 35.05800 36.43400 -6.49500  0.440 38.66000  ?  202 LEU A CA  1 
ATOM   2945 C  C   A LEU A 1 202 ? 34.45500 37.94200 -6.61800  0.560 36.44000  ?  202 LEU A C   1 
ATOM   2946 C  C   B LEU A 1 202 ? 34.27700 37.73300 -6.73100  0.440 36.57000  ?  202 LEU A C   1 
ATOM   2947 O  O   A LEU A 1 202 ? 35.07400 39.01200 -6.61800  0.560 38.55000  ?  202 LEU A O   1 
ATOM   2948 O  O   B LEU A 1 202 ? 34.84700 38.82500 -6.65200  0.440 37.76000  ?  202 LEU A O   1 
ATOM   2949 C  CB  A LEU A 1 202 ? 35.51700 35.90700 -7.63800  0.560 38.01000  ?  202 LEU A CB  1 
ATOM   2950 C  CB  B LEU A 1 202 ? 35.33600 35.71100 -7.81100  0.440 37.72000  ?  202 LEU A CB  1 
ATOM   2951 C  CG  A LEU A 1 202 ? 36.60500 34.83600 -7.54200  0.560 44.19000  ?  202 LEU A CG  1 
ATOM   2952 C  CG  B LEU A 1 202 ? 36.41500 34.65600 -7.55000  0.440 43.61000  ?  202 LEU A CG  1 
ATOM   2953 C  CD1 A LEU A 1 202 ? 36.70700 34.03400 -8.83300  0.560 42.77000  ?  202 LEU A CD1 1 
ATOM   2954 C  CD1 B LEU A 1 202 ? 36.36200 33.59600 -8.58900  0.440 42.02000  ?  202 LEU A CD1 1 
ATOM   2955 C  CD2 A LEU A 1 202 ? 37.95800 35.44900 -7.18700  0.560 41.14000  ?  202 LEU A CD2 1 
ATOM   2956 C  CD2 B LEU A 1 202 ? 37.81700 35.26900 -7.47100  0.440 41.50000  ?  202 LEU A CD2 1 
ATOM   2957 N  N   A VAL A 1 203 ? 33.14100 37.89000 -6.84700  0.560 32.99000  ?  203 VAL A N   1 
ATOM   2958 N  N   B VAL A 1 203 ? 32.95600 37.63800 -6.99700  0.440 33.77000  ?  203 VAL A N   1 
ATOM   2959 C  CA  A VAL A 1 203 ? 32.42800 39.11500 -7.20300  0.560 37.00000  ?  203 VAL A CA  1 
ATOM   2960 C  CA  B VAL A 1 203 ? 32.14500 38.82700 -7.29600  0.440 36.38000  ?  203 VAL A CA  1 
ATOM   2961 C  C   A VAL A 1 203 ? 32.22500 40.00000 -5.97500  0.560 40.79000  ?  203 VAL A C   1 
ATOM   2962 C  C   B VAL A 1 203 ? 32.02300 39.72300 -6.08200  0.440 41.09000  ?  203 VAL A C   1 
ATOM   2963 O  O   A VAL A 1 203 ? 32.38500 41.22500 -6.04600  0.560 39.17000  ?  203 VAL A O   1 
ATOM   2964 O  O   B VAL A 1 203 ? 31.85800 40.94900 -6.20400  0.440 41.49000  ?  203 VAL A O   1 
ATOM   2965 C  CB  A VAL A 1 203 ? 31.09000 38.79200 -7.89300  0.560 35.28000  ?  203 VAL A CB  1 
ATOM   2966 C  CB  B VAL A 1 203 ? 30.73000 38.47100 -7.78100  0.440 33.98000  ?  203 VAL A CB  1 
ATOM   2967 C  CG1 A VAL A 1 203 ? 30.29200 40.07400 -8.11700  0.560 44.49000  ?  203 VAL A CG1 1 
ATOM   2968 C  CG1 B VAL A 1 203 ? 30.16100 39.65800 -8.50800  0.440 42.02000  ?  203 VAL A CG1 1 
ATOM   2969 C  CG2 A VAL A 1 203 ? 31.32100 38.07800 -9.21700  0.560 39.40000  ?  203 VAL A CG2 1 
ATOM   2970 C  CG2 B VAL A 1 203 ? 30.74100 37.26700 -8.61000  0.440 39.28000  ?  203 VAL A CG2 1 
ATOM   2971 N  N   A THR A 1 204 ? 31.86800 39.40600 -4.83200  0.560 38.63000  ?  204 THR A N   1 
ATOM   2972 N  N   B THR A 1 204 ? 32.04800 39.12900 -4.89000  0.440 38.17000  ?  204 THR A N   1 
ATOM   2973 C  CA  A THR A 1 204 ? 31.61600 40.21700 -3.64400  0.560 39.32000  ?  204 THR A CA  1 
ATOM   2974 C  CA  B THR A 1 204 ? 31.78200 39.89300 -3.69600  0.440 38.02000  ?  204 THR A CA  1 
ATOM   2975 C  C   A THR A 1 204 ? 32.89200 40.77100 -3.02200  0.560 42.24000  ?  204 THR A C   1 
ATOM   2976 C  C   B THR A 1 204 ? 33.04600 40.43600 -3.07100  0.440 41.50000  ?  204 THR A C   1 
ATOM   2977 O  O   A THR A 1 204 ? 32.80400 41.64300 -2.15000  0.560 41.49000  ?  204 THR A O   1 
ATOM   2978 O  O   B THR A 1 204 ? 33.00000 41.52200 -2.48500  0.440 42.67000  ?  204 THR A O   1 
ATOM   2979 C  CB  A THR A 1 204 ? 30.86000 39.42100 -2.57300  0.560 38.59000  ?  204 THR A CB  1 
ATOM   2980 C  CB  B THR A 1 204 ? 31.01900 39.05500 -2.67700  0.440 38.60000  ?  204 THR A CB  1 
ATOM   2981 O  OG1 A THR A 1 204 ? 31.65700 38.30900 -2.14900  0.560 45.21000  ?  204 THR A OG1 1 
ATOM   2982 O  OG1 B THR A 1 204 ? 31.66500 37.80100 -2.54900  0.440 46.46000  ?  204 THR A OG1 1 
ATOM   2983 C  CG2 A THR A 1 204 ? 29.52800 38.92900 -3.10600  0.560 36.77000  ?  204 THR A CG2 1 
ATOM   2984 C  CG2 B THR A 1 204 ? 29.67900 38.76000 -3.17600  0.440 36.33000  ?  204 THR A CG2 1 
ATOM   2985 N  N   A LYS A 1 205 ? 34.06200 40.27900 -3.42400  0.560 39.53000  ?  205 LYS A N   1 
ATOM   2986 N  N   B LYS A 1 205 ? 34.18400 39.77600 -3.27100  0.440 38.34000  ?  205 LYS A N   1 
ATOM   2987 C  CA  A LYS A 1 205 ? 35.33400 40.77600 -2.91600  0.560 41.02000  ?  205 LYS A CA  1 
ATOM   2988 C  CA  B LYS A 1 205 ? 35.45000 40.20700 -2.67600  0.440 41.99000  ?  205 LYS A CA  1 
ATOM   2989 C  C   A LYS A 1 205 ? 36.13000 41.49900 -3.99500  0.560 43.70000  ?  205 LYS A C   1 
ATOM   2990 C  C   B LYS A 1 205 ? 36.35300 40.96200 -3.63200  0.440 43.99000  ?  205 LYS A C   1 
ATOM   2991 O  O   A LYS A 1 205 ? 36.37500 42.70200 -3.87900  0.560 45.57000  ?  205 LYS A O   1 
ATOM   2992 O  O   B LYS A 1 205 ? 36.96200 41.96500 -3.23900  0.440 48.68000  ?  205 LYS A O   1 
ATOM   2993 C  CB  A LYS A 1 205 ? 36.15400 39.61900 -2.32700  0.560 42.76000  ?  205 LYS A CB  1 
ATOM   2994 C  CB  B LYS A 1 205 ? 36.19800 39.00500 -2.10400  0.440 41.38000  ?  205 LYS A CB  1 
ATOM   2995 C  CG  A LYS A 1 205 ? 35.55600 39.01100 -1.06400  0.560 33.11000  ?  205 LYS A CG  1 
ATOM   2996 C  CG  B LYS A 1 205 ? 35.39500 38.38600 -1.01400  0.440 34.47000  ?  205 LYS A CG  1 
ATOM   2997 C  CD  A LYS A 1 205 ? 36.43200 37.89500 -0.51000  0.560 38.81000  ?  205 LYS A CD  1 
ATOM   2998 C  CD  B LYS A 1 205 ? 35.99800 37.13900 -0.48200  0.440 39.38000  ?  205 LYS A CD  1 
ATOM   2999 C  CE  A LYS A 1 205 ? 36.01400 37.51400 0.90200   0.560 45.41000  ?  205 LYS A CE  1 
ATOM   3000 C  CE  B LYS A 1 205 ? 35.17400 36.66600 0.67000   0.440 34.00000  ?  205 LYS A CE  1 
ATOM   3001 N  NZ  A LYS A 1 205 ? 34.86100 36.56600 0.89700   0.560 31.07000  ?  205 LYS A NZ  1 
ATOM   3002 N  NZ  B LYS A 1 205 ? 34.08100 35.79800 0.27300   0.440 38.59000  ?  205 LYS A NZ  1 
ATOM   3003 N  N   A VAL A 1 206 ? 36.54300 40.79600 -5.05200  0.560 43.15000  ?  206 VAL A N   1 
ATOM   3004 N  N   B VAL A 1 206 ? 36.44400 40.53500 -4.88400  0.440 43.63000  ?  206 VAL A N   1 
ATOM   3005 C  CA  A VAL A 1 206 ? 37.37000 41.42300 -6.07900  0.560 39.37000  ?  206 VAL A CA  1 
ATOM   3006 C  CA  B VAL A 1 206 ? 37.20700 41.26000 -5.87700  0.440 40.45000  ?  206 VAL A CA  1 
ATOM   3007 C  C   A VAL A 1 206 ? 36.54200 42.35500 -6.95200  0.560 42.29000  ?  206 VAL A C   1 
ATOM   3008 C  C   B VAL A 1 206 ? 36.28400 42.09300 -6.76400  0.440 42.33000  ?  206 VAL A C   1 
ATOM   3009 O  O   A VAL A 1 206 ? 36.97800 43.46400 -7.27300  0.560 44.28000  ?  206 VAL A O   1 
ATOM   3010 O  O   B VAL A 1 206 ? 36.52400 43.26700 -7.00300  0.440 39.16000  ?  206 VAL A O   1 
ATOM   3011 C  CB  A VAL A 1 206 ? 38.08300 40.34600 -6.91700  0.560 51.95000  ?  206 VAL A CB  1 
ATOM   3012 C  CB  B VAL A 1 206 ? 38.06100 40.26000 -6.69200  0.440 50.87000  ?  206 VAL A CB  1 
ATOM   3013 C  CG1 A VAL A 1 206 ? 38.93500 40.98300 -8.00500  0.560 50.96000  ?  206 VAL A CG1 1 
ATOM   3014 C  CG1 B VAL A 1 206 ? 38.94700 40.99900 -7.66000  0.440 51.71000  ?  206 VAL A CG1 1 
ATOM   3015 C  CG2 A VAL A 1 206 ? 38.92400 39.44800 -6.01300  0.560 43.90000  ?  206 VAL A CG2 1 
ATOM   3016 C  CG2 B VAL A 1 206 ? 38.90300 39.41300 -5.74000  0.440 44.25000  ?  206 VAL A CG2 1 
ATOM   3017 N  N   A GLY A 1 207 ? 35.34600 41.92900 -7.35800  0.560 37.94000  ?  207 GLY A N   1 
ATOM   3018 N  N   B GLY A 1 207 ? 35.16600 41.54300 -7.19100  0.440 39.65000  ?  207 GLY A N   1 
ATOM   3019 C  CA  A GLY A 1 207 ? 34.48300 42.82500 -8.11200  0.560 41.09000  ?  207 GLY A CA  1 
ATOM   3020 C  CA  B GLY A 1 207 ? 34.31800 42.23100 -8.14200  0.440 43.27000  ?  207 GLY A CA  1 
ATOM   3021 C  C   A GLY A 1 207 ? 34.13700 44.07100 -7.32300  0.560 44.79000  ?  207 GLY A C   1 
ATOM   3022 C  C   B GLY A 1 207 ? 33.79800 43.53700 -7.59100  0.440 42.01000  ?  207 GLY A C   1 
ATOM   3023 O  O   A GLY A 1 207 ? 34.28600 45.19400 -7.80900  0.560 51.43000  ?  207 GLY A O   1 
ATOM   3024 O  O   B GLY A 1 207 ? 34.11600 44.59500 -8.13600  0.440 47.88000  ?  207 GLY A O   1 
ATOM   3025 N  N   A PHE A 1 208 ? 33.65400 43.88200 -6.09400  0.560 53.44000  ?  208 PHE A N   1 
ATOM   3026 N  N   B PHE A 1 208 ? 32.92600 43.46100 -6.58100  0.440 46.65000  ?  208 PHE A N   1 
ATOM   3027 C  CA  A PHE A 1 208 ? 33.49600 44.96500 -5.12900  0.560 45.10000  ?  208 PHE A CA  1 
ATOM   3028 C  CA  B PHE A 1 208 ? 32.64500 44.57500 -5.68000  0.440 47.96000  ?  208 PHE A CA  1 
ATOM   3029 C  C   A PHE A 1 208 ? 34.68300 45.91600 -5.16100  0.560 50.00000  ?  208 PHE A C   1 
ATOM   3030 C  C   B PHE A 1 208 ? 33.75800 45.61100 -5.66600  0.440 46.83000  ?  208 PHE A C   1 
ATOM   3031 O  O   A PHE A 1 208 ? 34.52200 47.12600 -5.35500  0.560 50.53000  ?  208 PHE A O   1 
ATOM   3032 O  O   B PHE A 1 208 ? 33.54200 46.75900 -6.05100  0.440 58.04000  ?  208 PHE A O   1 
ATOM   3033 C  CB  A PHE A 1 208 ? 33.31700 44.32400 -3.74500  0.560 43.70000  ?  208 PHE A CB  1 
ATOM   3034 C  CB  B PHE A 1 208 ? 32.43000 44.05900 -4.26300  0.440 44.73000  ?  208 PHE A CB  1 
ATOM   3035 C  CG  A PHE A 1 208 ? 32.99000 45.28000 -2.63600  0.560 43.78000  ?  208 PHE A CG  1 
ATOM   3036 C  CG  B PHE A 1 208 ? 32.24500 45.16900 -3.22300  0.440 45.35000  ?  208 PHE A CG  1 
ATOM   3037 C  CD1 A PHE A 1 208 ? 33.99800 45.91700 -1.93200  0.560 44.90000  ?  208 PHE A CD1 1 
ATOM   3038 C  CD1 B PHE A 1 208 ? 31.01000 45.72700 -2.98800  0.440 37.92000  ?  208 PHE A CD1 1 
ATOM   3039 C  CD2 A PHE A 1 208 ? 31.67600 45.49000 -2.25300  0.560 43.29000  ?  208 PHE A CD2 1 
ATOM   3040 C  CD2 B PHE A 1 208 ? 33.31900 45.60100 -2.46000  0.440 43.14000  ?  208 PHE A CD2 1 
ATOM   3041 C  CE1 A PHE A 1 208 ? 33.70000 46.77700 -0.89300  0.560 46.18000  ?  208 PHE A CE1 1 
ATOM   3042 C  CE1 B PHE A 1 208 ? 30.82900 46.70600 -2.04400  0.440 48.83000  ?  208 PHE A CE1 1 
ATOM   3043 C  CE2 A PHE A 1 208 ? 31.37100 46.34900 -1.21400  0.560 49.86000  ?  208 PHE A CE2 1 
ATOM   3044 C  CE2 B PHE A 1 208 ? 33.15700 46.58000 -1.50200  0.440 49.08000  ?  208 PHE A CE2 1 
ATOM   3045 C  CZ  A PHE A 1 208 ? 32.38500 46.99300 -0.53200  0.560 50.39000  ?  208 PHE A CZ  1 
ATOM   3046 C  CZ  B PHE A 1 208 ? 31.90000 47.13600 -1.28500  0.440 52.54000  ?  208 PHE A CZ  1 
ATOM   3047 N  N   A GLY A 1 209 ? 35.88800 45.37500 -4.99500  0.560 52.69000  ?  209 GLY A N   1 
ATOM   3048 N  N   B GLY A 1 209 ? 34.96500 45.20900 -5.26800  0.440 47.07000  ?  209 GLY A N   1 
ATOM   3049 C  CA  A GLY A 1 209 ? 37.06300 46.22400 -4.93400  0.560 47.74000  ?  209 GLY A CA  1 
ATOM   3050 C  CA  B GLY A 1 209 ? 36.04800 46.17800 -5.14000  0.440 50.23000  ?  209 GLY A CA  1 
ATOM   3051 C  C   A GLY A 1 209 ? 37.27200 47.03700 -6.19600  0.560 57.54000  ?  209 GLY A C   1 
ATOM   3052 C  C   B GLY A 1 209 ? 36.49100 46.76100 -6.46900  0.440 54.83000  ?  209 GLY A C   1 
ATOM   3053 O  O   A GLY A 1 209 ? 37.56800 48.23300 -6.13200  0.560 60.99000  ?  209 GLY A O   1 
ATOM   3054 O  O   B GLY A 1 209 ? 36.89900 47.91900 -6.54800  0.440 59.90000  ?  209 GLY A O   1 
ATOM   3055 N  N   A PHE A 1 210 ? 37.11800 46.40600 -7.36100  0.560 57.13000  ?  210 PHE A N   1 
ATOM   3056 N  N   B PHE A 1 210 ? 36.46200 45.96600 -7.53400  0.440 55.42000  ?  210 PHE A N   1 
ATOM   3057 C  CA  A PHE A 1 210 ? 37.39500 47.11600 -8.60300  0.560 59.38000  ?  210 PHE A CA  1 
ATOM   3058 C  CA  B PHE A 1 210 ? 36.75100 46.58700 -8.81000  0.440 56.28000  ?  210 PHE A CA  1 
ATOM   3059 C  C   A PHE A 1 210 ? 36.36600 48.20600 -8.86900  0.560 59.62000  ?  210 PHE A C   1 
ATOM   3060 C  C   B PHE A 1 210 ? 35.60300 47.45900 -9.25000  0.440 59.57000  ?  210 PHE A C   1 
ATOM   3061 O  O   A PHE A 1 210 ? 36.70500 49.24000 -9.45500  0.560 66.08000  ?  210 PHE A O   1 
ATOM   3062 O  O   B PHE A 1 210 ? 35.77000 48.26300 -10.16000 0.440 60.26000  ?  210 PHE A O   1 
ATOM   3063 C  CB  A PHE A 1 210 ? 37.46400 46.12800 -9.76500  0.560 51.91000  ?  210 PHE A CB  1 
ATOM   3064 C  CB  B PHE A 1 210 ? 37.12400 45.54200 -9.84800  0.440 51.34000  ?  210 PHE A CB  1 
ATOM   3065 C  CG  A PHE A 1 210 ? 38.81200 45.48200 -9.91900  0.560 52.40000  ?  210 PHE A CG  1 
ATOM   3066 C  CG  B PHE A 1 210 ? 38.57900 45.21800 -9.82700  0.440 52.43000  ?  210 PHE A CG  1 
ATOM   3067 C  CD1 A PHE A 1 210 ? 39.94500 46.25100 -10.14300 0.560 68.17000  ?  210 PHE A CD1 1 
ATOM   3068 C  CD1 B PHE A 1 210 ? 39.49400 46.04100 -10.44400 0.440 65.63000  ?  210 PHE A CD1 1 
ATOM   3069 C  CD2 A PHE A 1 210 ? 38.95100 44.11000 -9.82600  0.560 56.55000  ?  210 PHE A CD2 1 
ATOM   3070 C  CD2 B PHE A 1 210 ? 39.04900 44.15400 -9.08800  0.440 58.78000  ?  210 PHE A CD2 1 
ATOM   3071 C  CE1 A PHE A 1 210 ? 41.18400 45.66200 -10.28000 0.560 68.49000  ?  210 PHE A CE1 1 
ATOM   3072 C  CE1 B PHE A 1 210 ? 40.85200 45.75200 -10.38600 0.440 68.88000  ?  210 PHE A CE1 1 
ATOM   3073 C  CE2 A PHE A 1 210 ? 40.19100 43.51400 -9.96200  0.560 56.18000  ?  210 PHE A CE2 1 
ATOM   3074 C  CE2 B PHE A 1 210 ? 40.40100 43.86300 -9.01800  0.440 56.42000  ?  210 PHE A CE2 1 
ATOM   3075 C  CZ  A PHE A 1 210 ? 41.30900 44.29200 -10.18900 0.560 63.12000  ?  210 PHE A CZ  1 
ATOM   3076 C  CZ  B PHE A 1 210 ? 41.29100 44.65900 -9.66100  0.440 60.02000  ?  210 PHE A CZ  1 
ATOM   3077 N  N   A ILE A 1 211 ? 35.11600 48.01000 -8.44400  0.560 62.29000  ?  211 ILE A N   1 
ATOM   3078 N  N   B ILE A 1 211 ? 34.44800 47.35300 -8.60500  0.440 59.24000  ?  211 ILE A N   1 
ATOM   3079 C  CA  A ILE A 1 211 ? 34.14100 49.09000 -8.56000  0.560 64.52000  ?  211 ILE A CA  1 
ATOM   3080 C  CA  B ILE A 1 211 ? 33.46800 48.40300 -8.83300  0.440 60.44000  ?  211 ILE A CA  1 
ATOM   3081 C  C   A ILE A 1 211 ? 34.57000 50.28100 -7.71500  0.560 70.67000  ?  211 ILE A C   1 
ATOM   3082 C  C   B ILE A 1 211 ? 33.76500 49.61300 -7.95900  0.440 66.90000  ?  211 ILE A C   1 
ATOM   3083 O  O   A ILE A 1 211 ? 34.33600 51.43500 -8.09100  0.560 77.18000  ?  211 ILE A O   1 
ATOM   3084 O  O   B ILE A 1 211 ? 33.64700 50.75100 -8.41400  0.440 74.28000  ?  211 ILE A O   1 
ATOM   3085 C  CB  A ILE A 1 211 ? 32.73600 48.60000 -8.16400  0.560 60.46000  ?  211 ILE A CB  1 
ATOM   3086 C  CB  B ILE A 1 211 ? 32.02700 47.89100 -8.66000  0.440 55.89000  ?  211 ILE A CB  1 
ATOM   3087 C  CG1 A ILE A 1 211 ? 32.18400 47.64300 -9.22000  0.560 56.10000  ?  211 ILE A CG1 1 
ATOM   3088 C  CG1 B ILE A 1 211 ? 31.64600 47.07000 -9.89400  0.440 56.46000  ?  211 ILE A CG1 1 
ATOM   3089 C  CG2 A ILE A 1 211 ? 31.79900 49.78600 -7.97800  0.560 53.26000  ?  211 ILE A CG2 1 
ATOM   3090 C  CG2 B ILE A 1 211 ? 31.08800 49.06300 -8.47200  0.440 53.68000  ?  211 ILE A CG2 1 
ATOM   3091 C  CD1 A ILE A 1 211 ? 31.10600 46.71800 -8.69400  0.560 58.54000  ?  211 ILE A CD1 1 
ATOM   3092 C  CD1 B ILE A 1 211 ? 30.63400 46.00000 -9.75200  0.440 54.27000  ?  211 ILE A CD1 1 
ATOM   3093 N  N   A ALA A 1 212 ? 35.20300 50.02800 -6.56600  0.560 73.53000  ?  212 ALA A N   1 
ATOM   3094 N  N   B ALA A 1 212 ? 34.20000 49.41400 -6.71800  0.440 59.67000  ?  212 ALA A N   1 
ATOM   3095 C  CA  A ALA A 1 212 ? 35.68800 51.12400 -5.73600  0.560 77.88000  ?  212 ALA A CA  1 
ATOM   3096 C  CA  B ALA A 1 212 ? 34.69300 50.56000 -5.95600  0.440 75.02000  ?  212 ALA A CA  1 
ATOM   3097 C  C   A ALA A 1 212 ? 36.86400 51.82900 -6.40000  0.560 76.33000  ?  212 ALA A C   1 
ATOM   3098 C  C   B ALA A 1 212 ? 35.76400 51.34000 -6.74400  0.440 73.01000  ?  212 ALA A C   1 
ATOM   3099 O  O   A ALA A 1 212 ? 36.91000 53.06300 -6.45600  0.560 83.12000  ?  212 ALA A O   1 
ATOM   3100 O  O   B ALA A 1 212 ? 35.54600 52.49400 -7.11300  0.440 75.54000  ?  212 ALA A O   1 
ATOM   3101 C  CB  A ALA A 1 212 ? 36.07800 50.60100 -4.35300  0.560 55.89000  ?  212 ALA A CB  1 
ATOM   3102 C  CB  B ALA A 1 212 ? 35.20700 50.10000 -4.58000  0.440 63.50000  ?  212 ALA A CB  1 
ATOM   3103 N  N   A LEU A 1 213 ? 37.82200 51.05800 -6.92200  0.560 70.15000  ?  213 LEU A N   1 
ATOM   3104 N  N   B LEU A 1 213 ? 36.91500 50.70700 -7.04100  0.440 73.01000  ?  213 LEU A N   1 
ATOM   3105 C  CA  A LEU A 1 213 ? 38.95200 51.66100 -7.62200  0.560 71.44000  ?  213 LEU A CA  1 
ATOM   3106 C  CA  B LEU A 1 213 ? 38.06100 51.40600 -7.63100  0.440 69.96000  ?  213 LEU A CA  1 
ATOM   3107 C  C   A LEU A 1 213 ? 38.47200 52.54500 -8.76700  0.560 89.14000  ?  213 LEU A C   1 
ATOM   3108 C  C   B LEU A 1 213 ? 37.66100 52.17900 -8.87600  0.440 83.01000  ?  213 LEU A C   1 
ATOM   3109 O  O   A LEU A 1 213 ? 38.95300 53.67100 -8.94500  0.560 92.04000  ?  213 LEU A O   1 
ATOM   3110 O  O   B LEU A 1 213 ? 38.27600 53.19900 -9.22400  0.440 89.96000  ?  213 LEU A O   1 
ATOM   3111 C  CB  A LEU A 1 213 ? 39.88400 50.57600 -8.15700  0.560 68.57000  ?  213 LEU A CB  1 
ATOM   3112 C  CB  B LEU A 1 213 ? 39.16600 50.40500 -7.97700  0.440 68.21000  ?  213 LEU A CB  1 
ATOM   3113 C  CG  A LEU A 1 213 ? 40.71700 49.75700 -7.17500  0.560 74.78000  ?  213 LEU A CG  1 
ATOM   3114 C  CG  B LEU A 1 213 ? 40.00700 49.79700 -6.84700  0.440 73.11000  ?  213 LEU A CG  1 
ATOM   3115 C  CD1 A LEU A 1 213 ? 41.74000 48.92500 -7.96300  0.560 69.72000  ?  213 LEU A CD1 1 
ATOM   3116 C  CD1 B LEU A 1 213 ? 41.33700 49.12700 -7.31700  0.440 69.01000  ?  213 LEU A CD1 1 
ATOM   3117 C  CD2 A LEU A 1 213 ? 41.41100 50.62200 -6.15400  0.560 82.64000  ?  213 LEU A CD2 1 
ATOM   3118 C  CD2 B LEU A 1 213 ? 40.28900 50.86700 -5.79100  0.440 74.54000  ?  213 LEU A CD2 1 
ATOM   3119 N  N   A ASP A 1 214 ? 37.52600 52.04000 -9.56300  0.560 84.84000  ?  214 ASP A N   1 
ATOM   3120 N  N   B ASP A 1 214 ? 36.61400 51.71300 -9.54600  0.440 84.61000  ?  214 ASP A N   1 
ATOM   3121 C  CA  A ASP A 1 214 ? 37.03500 52.80000 -10.70700 0.560 88.24000  ?  214 ASP A CA  1 
ATOM   3122 C  CA  B ASP A 1 214 ? 36.04700 52.35400 -10.71700 0.440 84.74000  ?  214 ASP A CA  1 
ATOM   3123 C  C   A ASP A 1 214 ? 36.52600 54.17000 -10.28200 0.560 103.61000 ?  214 ASP A C   1 
ATOM   3124 C  C   B ASP A 1 214 ? 35.51500 53.73600 -10.40000 0.440 94.95000  ?  214 ASP A C   1 
ATOM   3125 O  O   A ASP A 1 214 ? 36.76800 55.17200 -10.96600 0.560 117.83000 ?  214 ASP A O   1 
ATOM   3126 O  O   B ASP A 1 214 ? 35.15000 54.46000 -11.32900 0.440 108.42000 ?  214 ASP A O   1 
ATOM   3127 C  CB  A ASP A 1 214 ? 35.93000 52.01600 -11.41500 0.560 84.23000  ?  214 ASP A CB  1 
ATOM   3128 C  CB  B ASP A 1 214 ? 34.96000 51.43700 -11.27700 0.440 85.08000  ?  214 ASP A CB  1 
ATOM   3129 C  CG  A ASP A 1 214 ? 35.55600 52.61800 -12.75200 0.560 98.36000  ?  214 ASP A CG  1 
ATOM   3130 C  CG  B ASP A 1 214 ? 34.54600 51.78900 -12.67800 0.440 93.22000  ?  214 ASP A CG  1 
ATOM   3131 O  OD1 A ASP A 1 214 ? 36.46600 52.86300 -13.56900 0.560 99.61000  ?  214 ASP A OD1 1 
ATOM   3132 O  OD1 B ASP A 1 214 ? 35.42600 51.97300 -13.54300 0.440 96.30000  ?  214 ASP A OD1 1 
ATOM   3133 O  OD2 A ASP A 1 214 ? 34.35000 52.84900 -12.98400 0.560 102.68000 -1 214 ASP A OD2 1 
ATOM   3134 O  OD2 B ASP A 1 214 ? 33.33300 51.78600 -12.93700 0.440 89.98000  -1 214 ASP A OD2 1 
ATOM   3135 N  N   A ALA A 1 215 ? 35.81800 54.23600 -9.15300  0.560 98.74000  ?  215 ALA A N   1 
ATOM   3136 N  N   B ALA A 1 215 ? 35.52600 54.13400 -9.12400  0.440 97.81000  ?  215 ALA A N   1 
ATOM   3137 C  CA  A ALA A 1 215 ? 35.27600 55.51000 -8.69900  0.560 104.66000 ?  215 ALA A CA  1 
ATOM   3138 C  CA  B ALA A 1 215 ? 35.08900 55.45200 -8.68100  0.440 104.27000 ?  215 ALA A CA  1 
ATOM   3139 C  C   A ALA A 1 215 ? 36.36200 56.41100 -8.12500  0.560 123.21000 ?  215 ALA A C   1 
ATOM   3140 C  C   B ALA A 1 215 ? 36.21400 56.32100 -8.11900  0.440 122.89000 ?  215 ALA A C   1 
ATOM   3141 O  O   A ALA A 1 215 ? 36.25600 57.64000 -8.21400  0.560 127.80000 ?  215 ALA A O   1 
ATOM   3142 O  O   B ALA A 1 215 ? 36.15900 57.54800 -8.27200  0.440 127.68000 ?  215 ALA A O   1 
ATOM   3143 C  CB  A ALA A 1 215 ? 34.17700 55.27200 -7.66300  0.560 89.90000  ?  215 ALA A CB  1 
ATOM   3144 C  CB  B ALA A 1 215 ? 33.99500 55.30900 -7.62300  0.440 89.98000  ?  215 ALA A CB  1 
ATOM   3145 N  N   A ALA A 1 216 ? 37.41100 55.82700 -7.54200  0.560 132.13000 ?  216 ALA A N   1 
ATOM   3146 N  N   B ALA A 1 216 ? 37.23000 55.73000 -7.46400  0.440 131.46000 ?  216 ALA A N   1 
ATOM   3147 C  CA  A ALA A 1 216 ? 38.47900 56.63000 -6.95800  0.560 136.82000 ?  216 ALA A CA  1 
ATOM   3148 C  CA  B ALA A 1 216 ? 38.33500 56.49200 -6.87100  0.440 136.29000 ?  216 ALA A CA  1 
ATOM   3149 C  C   A ALA A 1 216 ? 39.26400 57.40400 -8.01000  0.560 144.55000 ?  216 ALA A C   1 
ATOM   3150 C  C   B ALA A 1 216 ? 39.30100 57.04900 -7.91000  0.440 144.00000 ?  216 ALA A C   1 
ATOM   3151 O  O   A ALA A 1 216 ? 39.90500 58.40600 -7.67300  0.560 150.77000 ?  216 ALA A O   1 
ATOM   3152 O  O   B ALA A 1 216 ? 40.24000 57.76900 -7.54300  0.440 146.38000 ?  216 ALA A O   1 
ATOM   3153 C  CB  A ALA A 1 216 ? 39.43100 55.74100 -6.15500  0.560 125.52000 ?  216 ALA A CB  1 
ATOM   3154 C  CB  B ALA A 1 216 ? 39.10400 55.62900 -5.86500  0.440 123.88000 ?  216 ALA A CB  1 
ATOM   3155 N  N   A ALA A 1 217 ? 39.23700 56.96100 -9.26700  0.560 158.30000 ?  217 ALA A N   1 
ATOM   3156 N  N   B ALA A 1 217 ? 39.10200 56.70000 -9.18400  0.440 157.53000 ?  217 ALA A N   1 
ATOM   3157 C  CA  A ALA A 1 217 ? 39.88900 57.69100 -10.34600 0.560 170.73000 ?  217 ALA A CA  1 
ATOM   3158 C  CA  B ALA A 1 217 ? 39.76000 57.35800 -10.29700 0.440 169.72000 ?  217 ALA A CA  1 
ATOM   3159 C  C   A ALA A 1 217 ? 38.96500 58.71200 -10.99400 0.560 180.66000 ?  217 ALA A C   1 
ATOM   3160 C  C   B ALA A 1 217 ? 38.85400 58.37000 -10.98900 0.440 179.55000 ?  217 ALA A C   1 
ATOM   3161 O  O   A ALA A 1 217 ? 39.44600 59.71200 -11.54200 0.560 190.80000 ?  217 ALA A O   1 
ATOM   3162 O  O   B ALA A 1 217 ? 39.37100 59.28300 -11.64000 0.440 189.38000 ?  217 ALA A O   1 
ATOM   3163 C  CB  A ALA A 1 217 ? 40.39800 56.71900 -11.41200 0.560 170.34000 ?  217 ALA A CB  1 
ATOM   3164 C  CB  B ALA A 1 217 ? 40.26200 56.32300 -11.31700 0.440 169.54000 ?  217 ALA A CB  1 
ATOM   3165 N  N   A THR A 1 218 ? 37.65100 58.48600 -10.94000 0.560 149.01000 ?  218 THR A N   1 
ATOM   3166 N  N   B THR A 1 218 ? 37.52500 58.26100 -10.83600 0.440 147.87000 ?  218 THR A N   1 
ATOM   3167 C  CA  A THR A 1 218 ? 36.70100 59.41200 -11.54300 0.560 148.02000 ?  218 THR A CA  1 
ATOM   3168 C  CA  B THR A 1 218 ? 36.59200 59.20700 -11.45200 0.440 147.20000 ?  218 THR A CA  1 
ATOM   3169 C  C   A THR A 1 218 ? 36.54000 60.69900 -10.74400 0.560 154.16000 ?  218 THR A C   1 
ATOM   3170 C  C   B THR A 1 218 ? 36.27200 60.41600 -10.56800 0.440 152.94000 ?  218 THR A C   1 
ATOM   3171 O  O   A THR A 1 218 ? 35.85600 61.61400 -11.21500 0.560 159.38000 ?  218 THR A O   1 
ATOM   3172 O  O   B THR A 1 218 ? 35.43900 61.24200 -10.96000 0.440 157.96000 ?  218 THR A O   1 
ATOM   3173 C  CB  A THR A 1 218 ? 35.33100 58.74400 -11.69600 0.560 137.58000 ?  218 THR A CB  1 
ATOM   3174 C  CB  B THR A 1 218 ? 35.27600 58.51100 -11.84600 0.440 137.60000 ?  218 THR A CB  1 
ATOM   3175 O  OG1 A THR A 1 218 ? 34.88600 58.25600 -10.42300 0.560 138.52000 ?  218 THR A OG1 1 
ATOM   3176 O  OG1 B THR A 1 218 ? 34.57500 58.09000 -10.67400 0.440 137.17000 ?  218 THR A OG1 1 
ATOM   3177 C  CG2 A THR A 1 218 ? 35.40200 57.58900 -12.68600 0.560 132.55000 ?  218 THR A CG2 1 
ATOM   3178 C  CG2 B THR A 1 218 ? 35.55000 57.29600 -12.71000 0.440 133.00000 ?  218 THR A CG2 1 
ATOM   3179 N  N   A LEU A 1 219 ? 37.13800 60.79400 -9.56100  0.560 149.81000 ?  219 LEU A N   1 
ATOM   3180 N  N   B LEU A 1 219 ? 36.90600 60.54400 -9.40000  0.440 149.46000 ?  219 LEU A N   1 
ATOM   3181 C  CA  A LEU A 1 219 ? 37.03300 61.99900 -8.74600  0.560 147.99000 ?  219 LEU A CA  1 
ATOM   3182 C  CA  B LEU A 1 219 ? 36.76200 61.72700 -8.55600  0.440 146.91000 ?  219 LEU A CA  1 
ATOM   3183 C  C   A LEU A 1 219 ? 37.43400 63.22900 -9.55800  0.560 155.69000 ?  219 LEU A C   1 
ATOM   3184 C  C   B LEU A 1 219 ? 37.20200 62.98500 -9.31700  0.440 155.19000 ?  219 LEU A C   1 
ATOM   3185 O  O   A LEU A 1 219 ? 37.05400 64.35400 -9.23300  0.560 161.22000 ?  219 LEU A O   1 
ATOM   3186 O  O   B LEU A 1 219 ? 36.50800 64.00600 -9.34000  0.440 160.66000 ?  219 LEU A O   1 
ATOM   3187 C  CB  A LEU A 1 219 ? 37.91000 61.89000 -7.50100  0.560 146.02000 ?  219 LEU A CB  1 
ATOM   3188 C  CB  B LEU A 1 219 ? 37.58600 61.57600 -7.26200  0.440 144.87000 ?  219 LEU A CB  1 
ATOM   3189 C  CG  A LEU A 1 219 ? 37.64500 60.73300 -6.53900  0.560 138.65000 ?  219 LEU A CG  1 
ATOM   3190 C  CG  B LEU A 1 219 ? 37.32800 60.46000 -6.23600  0.440 136.47000 ?  219 LEU A CG  1 
ATOM   3191 C  CD1 A LEU A 1 219 ? 38.18200 61.08300 -5.14800  0.560 137.24000 ?  219 LEU A CD1 1 
ATOM   3192 C  CD1 B LEU A 1 219 ? 37.98900 60.80800 -4.91500  0.440 137.86000 ?  219 LEU A CD1 1 
ATOM   3193 C  CD2 A LEU A 1 219 ? 36.17300 60.37700 -6.46500  0.560 131.21000 ?  219 LEU A CD2 1 
ATOM   3194 C  CD2 B LEU A 1 219 ? 35.85000 60.22700 -6.02100  0.440 128.55000 ?  219 LEU A CD2 1 
HETATM 3195 C  C1  A RET B 2 .   ? 25.06100 31.73800 5.61700   0.670 40.73000  ?  301 RET A C1  1 
HETATM 3196 C  C1  B RET B 2 .   ? 24.45900 31.91500 5.24700   0.330 39.00000  ?  301 RET A C1  1 
HETATM 3197 C  C2  A RET B 2 .   ? 24.20700 30.70600 6.36900   0.670 38.31000  ?  301 RET A C2  1 
HETATM 3198 C  C2  B RET B 2 .   ? 23.47800 30.94700 5.89700   0.330 38.97000  ?  301 RET A C2  1 
HETATM 3199 C  C3  A RET B 2 .   ? 23.32200 31.28700 7.45900   0.670 39.90000  ?  301 RET A C3  1 
HETATM 3200 C  C3  B RET B 2 .   ? 22.58100 31.57200 6.94300   0.330 40.31000  ?  301 RET A C3  1 
HETATM 3201 C  C4  A RET B 2 .   ? 22.41300 32.36800 6.91000   0.670 41.57000  ?  301 RET A C4  1 
HETATM 3202 C  C4  B RET B 2 .   ? 21.83700 32.77800 6.41500   0.330 38.87000  ?  301 RET A C4  1 
HETATM 3203 C  C5  A RET B 2 .   ? 23.06800 33.26700 5.89500   0.670 35.44000  ?  301 RET A C5  1 
HETATM 3204 C  C5  B RET B 2 .   ? 22.68900 33.69500 5.60100   0.330 36.79000  ?  301 RET A C5  1 
HETATM 3205 C  C6  A RET B 2 .   ? 24.32800 33.07800 5.46400   0.670 39.66000  ?  301 RET A C6  1 
HETATM 3206 C  C6  B RET B 2 .   ? 23.92300 33.37000 5.16900   0.330 38.23000  ?  301 RET A C6  1 
HETATM 3207 C  C7  A RET B 2 .   ? 25.02200 34.13200 4.73900   0.670 31.70000  ?  301 RET A C7  1 
HETATM 3208 C  C7  B RET B 2 .   ? 24.72300 34.41800 4.52800   0.330 34.16000  ?  301 RET A C7  1 
HETATM 3209 C  C8  A RET B 2 .   ? 26.22600 34.09700 4.11300   0.670 34.60000  ?  301 RET A C8  1 
HETATM 3210 C  C8  B RET B 2 .   ? 25.98500 34.48100 3.80200   0.330 36.45000  ?  301 RET A C8  1 
HETATM 3211 C  C9  A RET B 2 .   ? 26.86500 35.20400 3.41500   0.670 40.24000  ?  301 RET A C9  1 
HETATM 3212 C  C9  B RET B 2 .   ? 26.62600 35.69600 3.19200   0.330 37.53000  ?  301 RET A C9  1 
HETATM 3213 C  C10 A RET B 2 .   ? 28.14100 35.05500 2.98000   0.670 35.66000  ?  301 RET A C10 1 
HETATM 3214 C  C10 B RET B 2 .   ? 27.95200 35.68300 2.84300   0.330 35.17000  ?  301 RET A C10 1 
HETATM 3215 C  C11 A RET B 2 .   ? 28.96200 36.03200 2.32100   0.670 30.86000  ?  301 RET A C11 1 
HETATM 3216 C  C11 B RET B 2 .   ? 28.74700 36.76500 2.31800   0.330 33.48000  ?  301 RET A C11 1 
HETATM 3217 C  C12 A RET B 2 .   ? 30.25100 35.80400 2.02800   0.670 37.33000  ?  301 RET A C12 1 
HETATM 3218 C  C12 B RET B 2 .   ? 30.04100 36.65700 1.89200   0.330 36.50000  ?  301 RET A C12 1 
HETATM 3219 C  C13 A RET B 2 .   ? 31.18500 36.73800 1.42300   0.670 35.98000  ?  301 RET A C13 1 
HETATM 3220 C  C13 B RET B 2 .   ? 30.89200 37.74600 1.42200   0.330 38.65000  ?  301 RET A C13 1 
HETATM 3221 C  C14 A RET B 2 .   ? 32.49100 36.39000 1.32400   0.670 36.61000  ?  301 RET A C14 1 
HETATM 3222 C  C14 B RET B 2 .   ? 32.19700 37.54100 1.06900   0.330 33.04000  ?  301 RET A C14 1 
HETATM 3223 C  C15 A RET B 2 .   ? 33.57000 37.18400 0.79500   0.670 30.56000  ?  301 RET A C15 1 
HETATM 3224 C  C15 B RET B 2 .   ? 32.94400 36.31100 0.98800   0.330 37.26000  ?  301 RET A C15 1 
HETATM 3225 C  C16 A RET B 2 .   ? 26.36500 31.92600 6.40300   0.670 29.14000  ?  301 RET A C16 1 
HETATM 3226 C  C16 B RET B 2 .   ? 25.74700 31.87400 6.07700   0.330 35.77000  ?  301 RET A C16 1 
HETATM 3227 C  C17 A RET B 2 .   ? 25.39300 31.14200 4.24200   0.670 36.18000  ?  301 RET A C17 1 
HETATM 3228 C  C17 B RET B 2 .   ? 24.74100 31.34700 3.84900   0.330 34.97000  ?  301 RET A C17 1 
HETATM 3229 C  C18 A RET B 2 .   ? 22.29300 34.53900 5.68700   0.670 36.47000  ?  301 RET A C18 1 
HETATM 3230 C  C18 B RET B 2 .   ? 21.94300 34.94000 5.18700   0.330 39.72000  ?  301 RET A C18 1 
HETATM 3231 C  C19 A RET B 2 .   ? 26.07100 36.46500 3.20800   0.670 36.56000  ?  301 RET A C19 1 
HETATM 3232 C  C19 B RET B 2 .   ? 25.74800 36.89700 2.99600   0.330 37.83000  ?  301 RET A C19 1 
HETATM 3233 C  C20 A RET B 2 .   ? 30.66200 38.08100 0.99400   0.670 39.40000  ?  301 RET A C20 1 
HETATM 3234 C  C20 B RET B 2 .   ? 30.29900 39.12400 1.43400   0.330 40.50000  ?  301 RET A C20 1 
HETATM 3235 CL CL  A CL  C 3 .   ? 30.63000 24.32800 3.68100   0.560 30.00000  ?  302 CL  A CL  1 
HETATM 3236 O  O   A HOH D 4 .   ? 24.66300 55.77400 13.47900  0.560 81.05000  ?  401 HOH A O   1 
HETATM 3237 O  O   B HOH D 4 .   ? 25.18800 56.33200 12.49400  0.440 80.36000  ?  401 HOH A O   1 
HETATM 3238 O  O   A HOH D 4 .   ? 29.95900 24.55900 -1.06700  0.560 54.95000  ?  402 HOH A O   1 
HETATM 3239 O  O   B HOH D 4 .   ? 30.39100 23.68800 -1.14300  0.440 61.03000  ?  402 HOH A O   1 
HETATM 3240 O  O   A HOH D 4 .   ? 36.99200 31.01200 1.13000   0.560 50.26000  ?  403 HOH A O   1 
HETATM 3241 O  O   B HOH D 4 .   ? 35.03400 31.75100 1.34900   0.440 27.87000  ?  403 HOH A O   1 
HETATM 3242 O  O   A HOH D 4 .   ? 35.95200 34.23200 -0.16400  0.560 60.16000  ?  404 HOH A O   1 
HETATM 3243 O  O   A HOH D 4 .   ? 41.41300 17.93700 5.00500   0.560 75.93000  ?  405 HOH A O   1 
HETATM 3244 O  O   B HOH D 4 .   ? 41.06200 18.45200 4.70300   0.440 64.02000  ?  405 HOH A O   1 
HETATM 3245 O  O   A HOH D 4 .   ? 23.87200 16.74500 15.74500  0.560 86.08000  ?  406 HOH A O   1 
HETATM 3246 O  O   B HOH D 4 .   ? 23.42100 16.63500 16.64100  0.440 76.23000  ?  406 HOH A O   1 
HETATM 3247 O  O   A HOH D 4 .   ? 34.53000 30.05600 0.39700   0.560 55.21000  ?  407 HOH A O   1 
HETATM 3248 O  O   A HOH D 4 .   ? 30.22200 42.51800 -1.17800  0.560 40.89000  ?  408 HOH A O   1 
HETATM 3249 O  O   B HOH D 4 .   ? 30.10100 42.67300 -0.87900  0.440 40.58000  ?  408 HOH A O   1 
HETATM 3250 O  O   A HOH D 4 .   ? 31.97500 38.23800 11.34100  0.560 46.09000  ?  409 HOH A O   1 
HETATM 3251 O  O   B HOH D 4 .   ? 32.31000 39.27900 11.23100  0.440 50.96000  ?  409 HOH A O   1 
HETATM 3252 O  O   A HOH D 4 .   ? 30.34800 16.61500 -7.05300  0.560 52.52000  ?  410 HOH A O   1 
HETATM 3253 O  O   B HOH D 4 .   ? 29.86600 17.08200 -7.18100  0.440 55.11000  ?  410 HOH A O   1 
HETATM 3254 O  O   A HOH D 4 .   ? 39.65100 17.24900 -6.53800  0.560 70.17000  ?  411 HOH A O   1 
HETATM 3255 O  O   B HOH D 4 .   ? 40.20500 17.28600 -5.95200  0.440 64.94000  ?  411 HOH A O   1 
HETATM 3256 O  O   A HOH D 4 .   ? 34.00600 27.96400 -2.63400  0.560 55.04000  ?  412 HOH A O   1 
HETATM 3257 O  O   B HOH D 4 .   ? 34.20200 27.61300 -3.15900  0.440 53.42000  ?  412 HOH A O   1 
HETATM 3258 O  O   A HOH D 4 .   ? 18.49000 51.82700 14.79800  0.560 81.42000  ?  413 HOH A O   1 
HETATM 3259 O  O   B HOH D 4 .   ? 18.83200 52.82200 14.25100  0.440 82.62000  ?  413 HOH A O   1 
HETATM 3260 O  O   A HOH D 4 .   ? 22.01200 14.41100 -5.08800  0.560 93.41000  ?  414 HOH A O   1 
HETATM 3261 O  O   B HOH D 4 .   ? 22.14300 14.86300 -5.23400  0.440 89.89000  ?  414 HOH A O   1 
HETATM 3262 O  O   . HOH D 4 .   ? 49.49300 18.61000 -1.57200  1.000 78.81000  ?  415 HOH A O   1 
HETATM 3263 O  O   A HOH D 4 .   ? 37.24900 55.22800 -2.42100  0.560 78.63000  ?  416 HOH A O   1 
HETATM 3264 O  O   B HOH D 4 .   ? 36.88900 55.00200 -2.39700  0.440 77.76000  ?  416 HOH A O   1 
HETATM 3265 O  O   A HOH D 4 .   ? 36.54300 45.36400 11.93600  0.560 65.76000  ?  417 HOH A O   1 
HETATM 3266 O  O   B HOH D 4 .   ? 37.09000 43.66400 12.08000  0.440 47.77000  ?  417 HOH A O   1 
HETATM 3267 O  O   A HOH D 4 .   ? 49.02400 34.31600 -0.12400  0.560 75.32000  ?  418 HOH A O   1 
HETATM 3268 O  O   B HOH D 4 .   ? 48.35600 35.01300 -0.39700  0.440 69.05000  ?  418 HOH A O   1 
HETATM 3269 O  O   A HOH D 4 .   ? 17.18600 34.36500 3.65200   0.560 64.82000  ?  419 HOH A O   1 
HETATM 3270 O  O   B HOH D 4 .   ? 16.84600 33.76900 4.06700   0.440 57.33000  ?  419 HOH A O   1 
HETATM 3271 O  O   A HOH D 4 .   ? 44.87500 26.01700 -12.75000 0.28  102.46000 ?  420 HOH A O   1 
HETATM 3272 O  O   B HOH D 4 .   ? 44.79100 26.78800 -12.87500 0.440 100.33000 ?  420 HOH A O   1 
HETATM 3273 O  O   A HOH D 4 .   ? 35.33100 32.33700 -12.23600 0.560 47.73000  ?  421 HOH A O   1 
HETATM 3274 O  O   B HOH D 4 .   ? 34.52900 30.44300 -11.79300 0.440 25.94000  ?  421 HOH A O   1 
# 
