data_9IN9
# 
_entry.id   9IN9 
# 
_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   9IN9         pdb_00009in9 10.2210/pdb9in9/pdb 
WWPDB D_1300049193 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IN9 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              valentin.gordeliy@gmail.com 
_pdbx_contact_author.name_first         Valentin 
_pdbx_contact_author.name_last          Gordeliy 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5782-5896 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bukhdruker, S.' 1 0000-0002-0157-532X 
'Zabelskii, D.'  2 0000-0001-6906-975X 
'Astashkin, R.'  3 0000-0001-9065-8225 
'Gordeliy, V.'   4 0000-0001-5782-5896 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01488-7 
_citation.pdbx_database_id_PubMed   40205223 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zabelskii, D.'   1  ?                   
primary 'Bukhdruker, S.'  2  0000-0002-0157-532X 
primary 'Bukhalovich, S.' 3  0000-0002-0770-6597 
primary 'Tsybrov, F.'     4  0000-0001-7422-0899 
primary 'Lamm, G.H.U.'    5  0009-0006-6743-2344 
primary 'Astashkin, R.'   6  ?                   
primary 'Doroginin, D.'   7  ?                   
primary 'Matveev, G.'     8  ?                   
primary 'Sudarev, V.'     9  ?                   
primary 'Kuzmin, A.'      10 0000-0003-3945-3691 
primary 'Zinovev, E.'     11 ?                   
primary 'Vlasova, A.'     12 ?                   
primary 'Ryzhykau, Y.'    13 0000-0003-3719-1464 
primary 'Ilyinsky, N.'    14 0000-0002-8812-5849 
primary 'Gushchin, I.'    15 0000-0002-5348-6070 
primary 'Bourenkov, G.'   16 ?                   
primary 'Alekseev, A.'    17 ?                   
primary 'Round, A.'       18 0000-0002-0723-8228 
primary 'Wachtveitl, J.'  19 0000-0002-8496-8240 
primary 'Bamberg, E.'     20 0000-0002-5411-6207 
primary 'Gordeliy, V.'    21 0000-0001-5782-5896 
# 
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 'Viral rhodopsin OLPVR1'                         28127.299 1   ? ? ? ? 
2 non-polymer syn RETINAL                                          284.436   1   ? ? ? ? 
3 non-polymer syn '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' 328.487   1   ? ? ? ? 
4 non-polymer syn EICOSANE                                         282.547   20  ? ? ? ? 
5 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   4   ? ? ? ? 
6 water       nat water                                            18.015    111 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(FME)DNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFD
WVLTTPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLL
YVKYTKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLLLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFDWVLT
TPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLLYVKY
TKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLLLEHHHHHH
;
_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 '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' 97N 
4 EICOSANE                                         LFA 
5 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
6 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   FME n 
1 2   ASP n 
1 3   ASN n 
1 4   ILE n 
1 5   ILE n 
1 6   MET n 
1 7   THR n 
1 8   ALA n 
1 9   TYR n 
1 10  ILE n 
1 11  SER n 
1 12  ILE n 
1 13  PHE n 
1 14  VAL n 
1 15  GLN n 
1 16  ILE n 
1 17  ILE n 
1 18  THR n 
1 19  ALA n 
1 20  ILE n 
1 21  ILE n 
1 22  SER n 
1 23  VAL n 
1 24  TYR n 
1 25  GLY n 
1 26  LEU n 
1 27  PHE n 
1 28  ILE n 
1 29  PRO n 
1 30  LEU n 
1 31  ASN n 
1 32  PHE n 
1 33  LYS n 
1 34  ASP n 
1 35  ILE n 
1 36  ILE n 
1 37  LEU n 
1 38  ARG n 
1 39  GLU n 
1 40  ILE n 
1 41  LEU n 
1 42  ILE n 
1 43  LEU n 
1 44  GLU n 
1 45  LEU n 
1 46  ILE n 
1 47  VAL n 
1 48  GLN n 
1 49  ILE n 
1 50  ILE n 
1 51  GLU n 
1 52  PHE n 
1 53  ILE n 
1 54  PHE n 
1 55  TYR n 
1 56  ILE n 
1 57  TRP n 
1 58  LEU n 
1 59  ILE n 
1 60  ILE n 
1 61  THR n 
1 62  LEU n 
1 63  GLN n 
1 64  SER n 
1 65  ILE n 
1 66  ASN n 
1 67  GLU n 
1 68  ASP n 
1 69  ILE n 
1 70  THR n 
1 71  TYR n 
1 72  VAL n 
1 73  ARG n 
1 74  TYR n 
1 75  PHE n 
1 76  ASP n 
1 77  TRP n 
1 78  VAL n 
1 79  LEU n 
1 80  THR n 
1 81  THR n 
1 82  PRO n 
1 83  VAL n 
1 84  MET n 
1 85  LEU n 
1 86  LEU n 
1 87  THR n 
1 88  THR n 
1 89  VAL n 
1 90  TYR n 
1 91  PHE n 
1 92  PHE n 
1 93  GLU n 
1 94  TYR n 
1 95  MET n 
1 96  ASN n 
1 97  SER n 
1 98  ASP n 
1 99  ASP n 
1 100 GLY n 
1 101 ILE n 
1 102 ARG n 
1 103 LYS n 
1 104 LYS n 
1 105 GLU n 
1 106 ILE n 
1 107 ASN n 
1 108 ASP n 
1 109 ARG n 
1 110 ASP n 
1 111 TYR n 
1 112 VAL n 
1 113 TYR n 
1 114 LEU n 
1 115 PHE n 
1 116 TYR n 
1 117 ILE n 
1 118 CYS n 
1 119 LEU n 
1 120 SER n 
1 121 ASN n 
1 122 PHE n 
1 123 PHE n 
1 124 MET n 
1 125 LEU n 
1 126 LEU n 
1 127 ILE n 
1 128 GLY n 
1 129 TYR n 
1 130 LEU n 
1 131 GLY n 
1 132 GLU n 
1 133 THR n 
1 134 LYS n 
1 135 GLN n 
1 136 ILE n 
1 137 ASN n 
1 138 LYS n 
1 139 MET n 
1 140 LEU n 
1 141 THR n 
1 142 LEU n 
1 143 PHE n 
1 144 GLY n 
1 145 GLY n 
1 146 SER n 
1 147 PHE n 
1 148 PHE n 
1 149 LEU n 
1 150 PHE n 
1 151 LEU n 
1 152 THR n 
1 153 PHE n 
1 154 TYR n 
1 155 LEU n 
1 156 LEU n 
1 157 TYR n 
1 158 VAL n 
1 159 LYS n 
1 160 TYR n 
1 161 THR n 
1 162 LYS n 
1 163 GLU n 
1 164 ASN n 
1 165 TRP n 
1 166 MET n 
1 167 ASN n 
1 168 TYR n 
1 169 ILE n 
1 170 VAL n 
1 171 PHE n 
1 172 TYR n 
1 173 PHE n 
1 174 MET n 
1 175 PHE n 
1 176 LEU n 
1 177 VAL n 
1 178 TRP n 
1 179 PHE n 
1 180 LEU n 
1 181 TYR n 
1 182 GLY n 
1 183 PHE n 
1 184 ALA n 
1 185 PHE n 
1 186 MET n 
1 187 PHE n 
1 188 PRO n 
1 189 PHE n 
1 190 SER n 
1 191 ILE n 
1 192 LYS n 
1 193 ASN n 
1 194 GLN n 
1 195 MET n 
1 196 TYR n 
1 197 ASN n 
1 198 ILE n 
1 199 LEU n 
1 200 ASP n 
1 201 ILE n 
1 202 VAL n 
1 203 SER n 
1 204 LYS n 
1 205 ASN n 
1 206 ILE n 
1 207 TYR n 
1 208 SER n 
1 209 ILE n 
1 210 PHE n 
1 211 ILE n 
1 212 PHE n 
1 213 ILE n 
1 214 VAL n 
1 215 ILE n 
1 216 LEU n 
1 217 ASN n 
1 218 GLN n 
1 219 SER n 
1 220 TYR n 
1 221 LYS n 
1 222 LEU n 
1 223 LEU n 
1 224 LEU n 
1 225 GLU n 
1 226 HIS n 
1 227 HIS n 
1 228 HIS n 
1 229 HIS n 
1 230 HIS n 
1 231 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                   231 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 162281038 
_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      'Organic Lake phycodnavirus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     938083 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              C41 
_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 
97N non-polymer         . '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' ?                   'C19 H36 O4'     328.487 
ALA 'L-peptide linking' y ALANINE                                          ?                   'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                         ?                   'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ?                   'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ?                   'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ?                   'C3 H7 N O2 S'   121.158 
FME 'L-peptide linking' n N-FORMYLMETHIONINE                               ?                   'C6 H11 N O3 S'  177.221 
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 
LFA non-polymer         . EICOSANE                                         'LIPID FRAGMENT'    'C20 H42'        282.547 
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 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol 'C21 H40 O4'     356.540 
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   FME 1   1   1   FME FME A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  TRP 57  57  57  TRP TRP A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  TRP 77  77  77  TRP TRP A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  MET 84  84  84  MET MET A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 MET 124 124 124 MET MET A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 TRP 178 178 178 TRP TRP A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 ILE 209 209 209 ILE ILE 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 PHE 212 212 212 PHE PHE A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ASN 217 217 217 ASN ASN A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 HIS 226 226 ?   ?   ?   A . n 
A 1 227 HIS 227 227 ?   ?   ?   A . n 
A 1 228 HIS 228 228 ?   ?   ?   A . n 
A 1 229 HIS 229 229 ?   ?   ?   A . n 
A 1 230 HIS 230 230 ?   ?   ?   A . n 
A 1 231 HIS 231 231 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RET 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RET 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B  2 RET 1   301 301 RET RET A . 
C  3 97N 1   302 303 97N 97N A . 
D  4 LFA 1   303 401 LFA LFA A . 
E  4 LFA 1   304 402 LFA LFA A . 
F  4 LFA 1   305 403 LFA LFA A . 
G  4 LFA 1   306 404 LFA LFA A . 
H  4 LFA 1   307 405 LFA LFA A . 
I  4 LFA 1   308 406 LFA LFA A . 
J  4 LFA 1   309 407 LFA LFA A . 
K  4 LFA 1   310 408 LFA LFA A . 
L  4 LFA 1   311 409 LFA LFA A . 
M  4 LFA 1   312 410 LFA LFA A . 
N  4 LFA 1   313 411 LFA LFA A . 
O  4 LFA 1   314 412 LFA LFA A . 
P  4 LFA 1   315 413 LFA LFA A . 
Q  4 LFA 1   316 414 LFA LFA A . 
R  4 LFA 1   317 415 LFA LFA A . 
S  4 LFA 1   318 416 LFA LFA A . 
T  5 OLC 1   319 417 OLC OLA A . 
U  5 OLC 1   320 418 OLC OLA A . 
V  5 OLC 1   321 419 OLC OLC A . 
W  5 OLC 1   322 420 OLC OLC A . 
X  4 LFA 1   323 421 LFA LFA A . 
Y  4 LFA 1   324 422 LFA LFA A . 
Z  4 LFA 1   325 423 LFA LFA A . 
AA 4 LFA 1   326 424 LFA LFA A . 
BA 6 HOH 1   401 518 HOH HOH A . 
BA 6 HOH 2   402 522 HOH HOH A . 
BA 6 HOH 3   403 530 HOH HOH A . 
BA 6 HOH 4   404 544 HOH HOH A . 
BA 6 HOH 5   405 548 HOH HOH A . 
BA 6 HOH 6   406 573 HOH HOH A . 
BA 6 HOH 7   407 605 HOH HOH A . 
BA 6 HOH 8   408 505 HOH HOH A . 
BA 6 HOH 9   409 596 HOH HOH A . 
BA 6 HOH 10  410 574 HOH HOH A . 
BA 6 HOH 11  411 602 HOH HOH A . 
BA 6 HOH 12  412 553 HOH HOH A . 
BA 6 HOH 13  413 540 HOH HOH A . 
BA 6 HOH 14  414 504 HOH HOH A . 
BA 6 HOH 15  415 588 HOH HOH A . 
BA 6 HOH 16  416 512 HOH HOH A . 
BA 6 HOH 17  417 545 HOH HOH A . 
BA 6 HOH 18  418 523 HOH HOH A . 
BA 6 HOH 19  419 532 HOH HOH A . 
BA 6 HOH 20  420 526 HOH HOH A . 
BA 6 HOH 21  421 529 HOH HOH A . 
BA 6 HOH 22  422 536 HOH HOH A . 
BA 6 HOH 23  423 515 HOH HOH A . 
BA 6 HOH 24  424 579 HOH HOH A . 
BA 6 HOH 25  425 547 HOH HOH A . 
BA 6 HOH 26  426 577 HOH HOH A . 
BA 6 HOH 27  427 606 HOH HOH A . 
BA 6 HOH 28  428 513 HOH HOH A . 
BA 6 HOH 29  429 521 HOH HOH A . 
BA 6 HOH 30  430 550 HOH HOH A . 
BA 6 HOH 31  431 567 HOH HOH A . 
BA 6 HOH 32  432 561 HOH HOH A . 
BA 6 HOH 33  433 520 HOH HOH A . 
BA 6 HOH 34  434 570 HOH HOH A . 
BA 6 HOH 35  435 552 HOH HOH A . 
BA 6 HOH 36  436 527 HOH HOH A . 
BA 6 HOH 37  437 506 HOH HOH A . 
BA 6 HOH 38  438 594 HOH HOH A . 
BA 6 HOH 39  439 507 HOH HOH A . 
BA 6 HOH 40  440 514 HOH HOH A . 
BA 6 HOH 41  441 560 HOH HOH A . 
BA 6 HOH 42  442 580 HOH HOH A . 
BA 6 HOH 43  443 502 HOH HOH A . 
BA 6 HOH 44  444 534 HOH HOH A . 
BA 6 HOH 45  445 537 HOH HOH A . 
BA 6 HOH 46  446 556 HOH HOH A . 
BA 6 HOH 47  447 555 HOH HOH A . 
BA 6 HOH 48  448 525 HOH HOH A . 
BA 6 HOH 49  449 542 HOH HOH A . 
BA 6 HOH 50  450 510 HOH HOH A . 
BA 6 HOH 51  451 539 HOH HOH A . 
BA 6 HOH 52  452 564 HOH HOH A . 
BA 6 HOH 53  453 528 HOH HOH A . 
BA 6 HOH 54  454 503 HOH HOH A . 
BA 6 HOH 55  455 546 HOH HOH A . 
BA 6 HOH 56  456 563 HOH HOH A . 
BA 6 HOH 57  457 519 HOH HOH A . 
BA 6 HOH 58  458 609 HOH HOH A . 
BA 6 HOH 59  459 535 HOH HOH A . 
BA 6 HOH 60  460 589 HOH HOH A . 
BA 6 HOH 61  461 595 HOH HOH A . 
BA 6 HOH 62  462 543 HOH HOH A . 
BA 6 HOH 63  463 549 HOH HOH A . 
BA 6 HOH 64  464 516 HOH HOH A . 
BA 6 HOH 65  465 583 HOH HOH A . 
BA 6 HOH 66  466 610 HOH HOH A . 
BA 6 HOH 67  467 509 HOH HOH A . 
BA 6 HOH 68  468 599 HOH HOH A . 
BA 6 HOH 69  469 558 HOH HOH A . 
BA 6 HOH 70  470 593 HOH HOH A . 
BA 6 HOH 71  471 575 HOH HOH A . 
BA 6 HOH 72  472 541 HOH HOH A . 
BA 6 HOH 73  473 517 HOH HOH A . 
BA 6 HOH 74  474 601 HOH HOH A . 
BA 6 HOH 75  475 557 HOH HOH A . 
BA 6 HOH 76  476 586 HOH HOH A . 
BA 6 HOH 77  477 554 HOH HOH A . 
BA 6 HOH 78  478 538 HOH HOH A . 
BA 6 HOH 79  479 508 HOH HOH A . 
BA 6 HOH 80  480 578 HOH HOH A . 
BA 6 HOH 81  481 597 HOH HOH A . 
BA 6 HOH 82  482 608 HOH HOH A . 
BA 6 HOH 83  483 568 HOH HOH A . 
BA 6 HOH 84  484 600 HOH HOH A . 
BA 6 HOH 85  485 598 HOH HOH A . 
BA 6 HOH 86  486 524 HOH HOH A . 
BA 6 HOH 87  487 571 HOH HOH A . 
BA 6 HOH 88  488 566 HOH HOH A . 
BA 6 HOH 89  489 501 HOH HOH A . 
BA 6 HOH 90  490 565 HOH HOH A . 
BA 6 HOH 91  491 562 HOH HOH A . 
BA 6 HOH 92  492 511 HOH HOH A . 
BA 6 HOH 93  493 572 HOH HOH A . 
BA 6 HOH 94  494 584 HOH HOH A . 
BA 6 HOH 95  495 559 HOH HOH A . 
BA 6 HOH 96  496 592 HOH HOH A . 
BA 6 HOH 97  497 581 HOH HOH A . 
BA 6 HOH 98  498 551 HOH HOH A . 
BA 6 HOH 99  499 607 HOH HOH A . 
BA 6 HOH 100 500 569 HOH HOH A . 
BA 6 HOH 101 501 587 HOH HOH A . 
BA 6 HOH 102 502 582 HOH HOH A . 
BA 6 HOH 103 503 533 HOH HOH A . 
BA 6 HOH 104 504 611 HOH HOH A . 
BA 6 HOH 105 505 604 HOH HOH A . 
BA 6 HOH 106 506 531 HOH HOH A . 
BA 6 HOH 107 507 603 HOH HOH A . 
BA 6 HOH 108 508 576 HOH HOH A . 
BA 6 HOH 109 509 585 HOH HOH A . 
BA 6 HOH 110 510 591 HOH HOH A . 
BA 6 HOH 111 511 590 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 ASP 2   ? CG  ? A  ASP 2   CG  
2   1 Y 1 A ASP 2   ? OD1 ? A  ASP 2   OD1 
3   1 Y 1 A ASP 2   ? OD2 ? A  ASP 2   OD2 
4   1 Y 1 A ILE 65  ? CG1 ? A  ILE 65  CG1 
5   1 Y 1 A ILE 65  ? CG2 ? A  ILE 65  CG2 
6   1 Y 1 A ILE 65  ? CD1 ? A  ILE 65  CD1 
7   1 Y 1 A GLU 67  ? CG  ? A  GLU 67  CG  
8   1 Y 1 A GLU 67  ? CD  ? A  GLU 67  CD  
9   1 Y 1 A GLU 67  ? OE1 ? A  GLU 67  OE1 
10  1 Y 1 A GLU 67  ? OE2 ? A  GLU 67  OE2 
11  1 Y 1 A ASP 98  ? CG  ? A  ASP 98  CG  
12  1 Y 1 A ASP 98  ? OD1 ? A  ASP 98  OD1 
13  1 Y 1 A ASP 98  ? OD2 ? A  ASP 98  OD2 
14  1 Y 1 A ASP 99  ? CG  ? A  ASP 99  CG  
15  1 Y 1 A ASP 99  ? OD1 ? A  ASP 99  OD1 
16  1 Y 1 A ASP 99  ? OD2 ? A  ASP 99  OD2 
17  1 Y 1 A ARG 102 ? NE  ? A  ARG 102 NE  
18  1 Y 1 A ARG 102 ? CZ  ? A  ARG 102 CZ  
19  1 Y 1 A ARG 102 ? NH1 ? A  ARG 102 NH1 
20  1 Y 1 A ARG 102 ? NH2 ? A  ARG 102 NH2 
21  1 Y 1 A LYS 103 ? CE  ? A  LYS 103 CE  
22  1 Y 1 A LYS 103 ? NZ  ? A  LYS 103 NZ  
23  1 Y 1 A LYS 134 ? CE  ? A  LYS 134 CE  
24  1 Y 1 A LYS 134 ? NZ  ? A  LYS 134 NZ  
25  1 Y 1 A LYS 138 ? CD  ? A  LYS 138 CD  
26  1 Y 1 A LYS 138 ? CE  ? A  LYS 138 CE  
27  1 Y 1 A LYS 138 ? NZ  ? A  LYS 138 NZ  
28  1 Y 1 A LYS 221 ? CD  ? A  LYS 221 CD  
29  1 Y 1 A LYS 221 ? CE  ? A  LYS 221 CE  
30  1 Y 1 A LYS 221 ? NZ  ? A  LYS 221 NZ  
31  1 Y 1 A GLU 225 ? CG  ? A  GLU 225 CG  
32  1 Y 1 A GLU 225 ? CD  ? A  GLU 225 CD  
33  1 Y 1 A GLU 225 ? OE1 ? A  GLU 225 OE1 
34  1 Y 1 A GLU 225 ? OE2 ? A  GLU 225 OE2 
35  1 N 1 A 97N 302 ? C   ? C  97N 1   C   
36  1 N 1 A 97N 302 ? C1  ? C  97N 1   C1  
37  1 N 1 A 97N 302 ? C2  ? C  97N 1   C2  
38  1 N 1 A 97N 302 ? C3  ? C  97N 1   C3  
39  1 N 1 A 97N 302 ? C4  ? C  97N 1   C4  
40  1 N 1 A 97N 302 ? C5  ? C  97N 1   C5  
41  1 N 1 A 97N 302 ? C6  ? C  97N 1   C6  
42  1 N 1 A 97N 302 ? C7  ? C  97N 1   C7  
43  1 N 1 A 97N 302 ? C8  ? C  97N 1   C8  
44  1 N 1 A 97N 302 ? C9  ? C  97N 1   C9  
45  1 N 1 A 97N 302 ? C10 ? C  97N 1   C10 
46  1 N 1 A 97N 302 ? C11 ? C  97N 1   C11 
47  1 N 1 A LFA 303 ? C1  ? D  LFA 1   C1  
48  1 N 1 A LFA 303 ? C16 ? D  LFA 1   C16 
49  1 N 1 A LFA 303 ? C17 ? D  LFA 1   C17 
50  1 N 1 A LFA 303 ? C18 ? D  LFA 1   C18 
51  1 N 1 A LFA 303 ? C19 ? D  LFA 1   C19 
52  1 N 1 A LFA 303 ? C20 ? D  LFA 1   C20 
53  1 N 1 A LFA 304 ? C9  ? E  LFA 1   C9  
54  1 N 1 A LFA 304 ? C10 ? E  LFA 1   C10 
55  1 N 1 A LFA 304 ? C11 ? E  LFA 1   C11 
56  1 N 1 A LFA 304 ? C12 ? E  LFA 1   C12 
57  1 N 1 A LFA 304 ? C13 ? E  LFA 1   C13 
58  1 N 1 A LFA 304 ? C14 ? E  LFA 1   C14 
59  1 N 1 A LFA 304 ? C15 ? E  LFA 1   C15 
60  1 N 1 A LFA 304 ? C16 ? E  LFA 1   C16 
61  1 N 1 A LFA 304 ? C17 ? E  LFA 1   C17 
62  1 N 1 A LFA 304 ? C18 ? E  LFA 1   C18 
63  1 N 1 A LFA 304 ? C19 ? E  LFA 1   C19 
64  1 N 1 A LFA 304 ? C20 ? E  LFA 1   C20 
65  1 N 1 A LFA 305 ? C8  ? F  LFA 1   C8  
66  1 N 1 A LFA 305 ? C9  ? F  LFA 1   C9  
67  1 N 1 A LFA 305 ? C10 ? F  LFA 1   C10 
68  1 N 1 A LFA 305 ? C11 ? F  LFA 1   C11 
69  1 N 1 A LFA 305 ? C12 ? F  LFA 1   C12 
70  1 N 1 A LFA 305 ? C13 ? F  LFA 1   C13 
71  1 N 1 A LFA 305 ? C14 ? F  LFA 1   C14 
72  1 N 1 A LFA 305 ? C15 ? F  LFA 1   C15 
73  1 N 1 A LFA 305 ? C16 ? F  LFA 1   C16 
74  1 N 1 A LFA 305 ? C17 ? F  LFA 1   C17 
75  1 N 1 A LFA 305 ? C18 ? F  LFA 1   C18 
76  1 N 1 A LFA 305 ? C19 ? F  LFA 1   C19 
77  1 N 1 A LFA 305 ? C20 ? F  LFA 1   C20 
78  1 N 1 A LFA 306 ? C8  ? G  LFA 1   C8  
79  1 N 1 A LFA 306 ? C9  ? G  LFA 1   C9  
80  1 N 1 A LFA 306 ? C10 ? G  LFA 1   C10 
81  1 N 1 A LFA 306 ? C11 ? G  LFA 1   C11 
82  1 N 1 A LFA 306 ? C12 ? G  LFA 1   C12 
83  1 N 1 A LFA 306 ? C13 ? G  LFA 1   C13 
84  1 N 1 A LFA 306 ? C14 ? G  LFA 1   C14 
85  1 N 1 A LFA 306 ? C15 ? G  LFA 1   C15 
86  1 N 1 A LFA 306 ? C16 ? G  LFA 1   C16 
87  1 N 1 A LFA 306 ? C17 ? G  LFA 1   C17 
88  1 N 1 A LFA 306 ? C18 ? G  LFA 1   C18 
89  1 N 1 A LFA 306 ? C19 ? G  LFA 1   C19 
90  1 N 1 A LFA 306 ? C20 ? G  LFA 1   C20 
91  1 N 1 A LFA 307 ? C1  ? H  LFA 1   C1  
92  1 N 1 A LFA 307 ? C2  ? H  LFA 1   C2  
93  1 N 1 A LFA 307 ? C3  ? H  LFA 1   C3  
94  1 N 1 A LFA 307 ? C4  ? H  LFA 1   C4  
95  1 N 1 A LFA 307 ? C5  ? H  LFA 1   C5  
96  1 N 1 A LFA 307 ? C6  ? H  LFA 1   C6  
97  1 N 1 A LFA 307 ? C7  ? H  LFA 1   C7  
98  1 N 1 A LFA 307 ? C8  ? H  LFA 1   C8  
99  1 N 1 A LFA 307 ? C9  ? H  LFA 1   C9  
100 1 N 1 A LFA 307 ? C10 ? H  LFA 1   C10 
101 1 N 1 A LFA 307 ? C20 ? H  LFA 1   C20 
102 1 N 1 A LFA 308 ? C1  ? I  LFA 1   C1  
103 1 N 1 A LFA 308 ? C5  ? I  LFA 1   C5  
104 1 N 1 A LFA 308 ? C6  ? I  LFA 1   C6  
105 1 N 1 A LFA 308 ? C7  ? I  LFA 1   C7  
106 1 N 1 A LFA 308 ? C8  ? I  LFA 1   C8  
107 1 N 1 A LFA 308 ? C9  ? I  LFA 1   C9  
108 1 N 1 A LFA 308 ? C10 ? I  LFA 1   C10 
109 1 N 1 A LFA 308 ? C11 ? I  LFA 1   C11 
110 1 N 1 A LFA 308 ? C12 ? I  LFA 1   C12 
111 1 N 1 A LFA 308 ? C13 ? I  LFA 1   C13 
112 1 N 1 A LFA 308 ? C14 ? I  LFA 1   C14 
113 1 N 1 A LFA 308 ? C15 ? I  LFA 1   C15 
114 1 N 1 A LFA 308 ? C16 ? I  LFA 1   C16 
115 1 N 1 A LFA 308 ? C17 ? I  LFA 1   C17 
116 1 N 1 A LFA 308 ? C18 ? I  LFA 1   C18 
117 1 N 1 A LFA 308 ? C19 ? I  LFA 1   C19 
118 1 N 1 A LFA 308 ? C20 ? I  LFA 1   C20 
119 1 N 1 A LFA 309 ? C8  ? J  LFA 1   C8  
120 1 N 1 A LFA 309 ? C9  ? J  LFA 1   C9  
121 1 N 1 A LFA 309 ? C10 ? J  LFA 1   C10 
122 1 N 1 A LFA 309 ? C11 ? J  LFA 1   C11 
123 1 N 1 A LFA 309 ? C12 ? J  LFA 1   C12 
124 1 N 1 A LFA 309 ? C13 ? J  LFA 1   C13 
125 1 N 1 A LFA 309 ? C14 ? J  LFA 1   C14 
126 1 N 1 A LFA 309 ? C15 ? J  LFA 1   C15 
127 1 N 1 A LFA 309 ? C16 ? J  LFA 1   C16 
128 1 N 1 A LFA 309 ? C17 ? J  LFA 1   C17 
129 1 N 1 A LFA 309 ? C18 ? J  LFA 1   C18 
130 1 N 1 A LFA 309 ? C19 ? J  LFA 1   C19 
131 1 N 1 A LFA 309 ? C20 ? J  LFA 1   C20 
132 1 N 1 A LFA 310 ? C1  ? K  LFA 1   C1  
133 1 N 1 A LFA 310 ? C2  ? K  LFA 1   C2  
134 1 N 1 A LFA 310 ? C3  ? K  LFA 1   C3  
135 1 N 1 A LFA 310 ? C8  ? K  LFA 1   C8  
136 1 N 1 A LFA 310 ? C9  ? K  LFA 1   C9  
137 1 N 1 A LFA 310 ? C10 ? K  LFA 1   C10 
138 1 N 1 A LFA 310 ? C11 ? K  LFA 1   C11 
139 1 N 1 A LFA 310 ? C12 ? K  LFA 1   C12 
140 1 N 1 A LFA 310 ? C13 ? K  LFA 1   C13 
141 1 N 1 A LFA 310 ? C14 ? K  LFA 1   C14 
142 1 N 1 A LFA 310 ? C15 ? K  LFA 1   C15 
143 1 N 1 A LFA 310 ? C16 ? K  LFA 1   C16 
144 1 N 1 A LFA 310 ? C17 ? K  LFA 1   C17 
145 1 N 1 A LFA 310 ? C18 ? K  LFA 1   C18 
146 1 N 1 A LFA 310 ? C19 ? K  LFA 1   C19 
147 1 N 1 A LFA 310 ? C20 ? K  LFA 1   C20 
148 1 N 1 A LFA 311 ? C1  ? L  LFA 1   C1  
149 1 N 1 A LFA 311 ? C2  ? L  LFA 1   C2  
150 1 N 1 A LFA 311 ? C3  ? L  LFA 1   C3  
151 1 N 1 A LFA 311 ? C4  ? L  LFA 1   C4  
152 1 N 1 A LFA 311 ? C5  ? L  LFA 1   C5  
153 1 N 1 A LFA 311 ? C6  ? L  LFA 1   C6  
154 1 N 1 A LFA 311 ? C7  ? L  LFA 1   C7  
155 1 N 1 A LFA 311 ? C8  ? L  LFA 1   C8  
156 1 N 1 A LFA 311 ? C9  ? L  LFA 1   C9  
157 1 N 1 A LFA 311 ? C10 ? L  LFA 1   C10 
158 1 N 1 A LFA 311 ? C11 ? L  LFA 1   C11 
159 1 N 1 A LFA 311 ? C12 ? L  LFA 1   C12 
160 1 N 1 A LFA 311 ? C13 ? L  LFA 1   C13 
161 1 N 1 A LFA 311 ? C14 ? L  LFA 1   C14 
162 1 N 1 A LFA 311 ? C15 ? L  LFA 1   C15 
163 1 N 1 A LFA 312 ? C1  ? M  LFA 1   C1  
164 1 N 1 A LFA 312 ? C2  ? M  LFA 1   C2  
165 1 N 1 A LFA 312 ? C3  ? M  LFA 1   C3  
166 1 N 1 A LFA 312 ? C4  ? M  LFA 1   C4  
167 1 N 1 A LFA 312 ? C5  ? M  LFA 1   C5  
168 1 N 1 A LFA 312 ? C6  ? M  LFA 1   C6  
169 1 N 1 A LFA 312 ? C7  ? M  LFA 1   C7  
170 1 N 1 A LFA 312 ? C8  ? M  LFA 1   C8  
171 1 N 1 A LFA 312 ? C9  ? M  LFA 1   C9  
172 1 N 1 A LFA 312 ? C10 ? M  LFA 1   C10 
173 1 N 1 A LFA 312 ? C11 ? M  LFA 1   C11 
174 1 N 1 A LFA 312 ? C12 ? M  LFA 1   C12 
175 1 N 1 A LFA 313 ? C1  ? N  LFA 1   C1  
176 1 N 1 A LFA 313 ? C2  ? N  LFA 1   C2  
177 1 N 1 A LFA 313 ? C9  ? N  LFA 1   C9  
178 1 N 1 A LFA 313 ? C10 ? N  LFA 1   C10 
179 1 N 1 A LFA 313 ? C11 ? N  LFA 1   C11 
180 1 N 1 A LFA 313 ? C12 ? N  LFA 1   C12 
181 1 N 1 A LFA 313 ? C13 ? N  LFA 1   C13 
182 1 N 1 A LFA 313 ? C14 ? N  LFA 1   C14 
183 1 N 1 A LFA 313 ? C15 ? N  LFA 1   C15 
184 1 N 1 A LFA 313 ? C16 ? N  LFA 1   C16 
185 1 N 1 A LFA 313 ? C17 ? N  LFA 1   C17 
186 1 N 1 A LFA 313 ? C18 ? N  LFA 1   C18 
187 1 N 1 A LFA 313 ? C19 ? N  LFA 1   C19 
188 1 N 1 A LFA 313 ? C20 ? N  LFA 1   C20 
189 1 N 1 A LFA 314 ? C1  ? O  LFA 1   C1  
190 1 N 1 A LFA 314 ? C2  ? O  LFA 1   C2  
191 1 N 1 A LFA 314 ? C15 ? O  LFA 1   C15 
192 1 N 1 A LFA 314 ? C16 ? O  LFA 1   C16 
193 1 N 1 A LFA 314 ? C17 ? O  LFA 1   C17 
194 1 N 1 A LFA 314 ? C18 ? O  LFA 1   C18 
195 1 N 1 A LFA 314 ? C19 ? O  LFA 1   C19 
196 1 N 1 A LFA 314 ? C20 ? O  LFA 1   C20 
197 1 N 1 A LFA 315 ? C1  ? P  LFA 1   C1  
198 1 N 1 A LFA 315 ? C2  ? P  LFA 1   C2  
199 1 N 1 A LFA 315 ? C3  ? P  LFA 1   C3  
200 1 N 1 A LFA 315 ? C4  ? P  LFA 1   C4  
201 1 N 1 A LFA 315 ? C5  ? P  LFA 1   C5  
202 1 N 1 A LFA 315 ? C6  ? P  LFA 1   C6  
203 1 N 1 A LFA 315 ? C7  ? P  LFA 1   C7  
204 1 N 1 A LFA 315 ? C8  ? P  LFA 1   C8  
205 1 N 1 A LFA 316 ? C1  ? Q  LFA 1   C1  
206 1 N 1 A LFA 316 ? C2  ? Q  LFA 1   C2  
207 1 N 1 A LFA 316 ? C3  ? Q  LFA 1   C3  
208 1 N 1 A LFA 316 ? C4  ? Q  LFA 1   C4  
209 1 N 1 A LFA 316 ? C5  ? Q  LFA 1   C5  
210 1 N 1 A LFA 316 ? C6  ? Q  LFA 1   C6  
211 1 N 1 A LFA 316 ? C7  ? Q  LFA 1   C7  
212 1 N 1 A LFA 316 ? C8  ? Q  LFA 1   C8  
213 1 N 1 A LFA 316 ? C9  ? Q  LFA 1   C9  
214 1 N 1 A LFA 317 ? C7  ? R  LFA 1   C7  
215 1 N 1 A LFA 317 ? C8  ? R  LFA 1   C8  
216 1 N 1 A LFA 317 ? C9  ? R  LFA 1   C9  
217 1 N 1 A LFA 317 ? C10 ? R  LFA 1   C10 
218 1 N 1 A LFA 317 ? C11 ? R  LFA 1   C11 
219 1 N 1 A LFA 317 ? C12 ? R  LFA 1   C12 
220 1 N 1 A LFA 317 ? C13 ? R  LFA 1   C13 
221 1 N 1 A LFA 317 ? C14 ? R  LFA 1   C14 
222 1 N 1 A LFA 317 ? C15 ? R  LFA 1   C15 
223 1 N 1 A LFA 317 ? C16 ? R  LFA 1   C16 
224 1 N 1 A LFA 317 ? C17 ? R  LFA 1   C17 
225 1 N 1 A LFA 317 ? C18 ? R  LFA 1   C18 
226 1 N 1 A LFA 317 ? C19 ? R  LFA 1   C19 
227 1 N 1 A LFA 317 ? C20 ? R  LFA 1   C20 
228 1 N 1 A LFA 318 ? C1  ? S  LFA 1   C1  
229 1 N 1 A LFA 318 ? C2  ? S  LFA 1   C2  
230 1 N 1 A LFA 318 ? C3  ? S  LFA 1   C3  
231 1 N 1 A LFA 318 ? C4  ? S  LFA 1   C4  
232 1 N 1 A LFA 318 ? C5  ? S  LFA 1   C5  
233 1 N 1 A LFA 318 ? C6  ? S  LFA 1   C6  
234 1 N 1 A LFA 318 ? C7  ? S  LFA 1   C7  
235 1 N 1 A LFA 318 ? C8  ? S  LFA 1   C8  
236 1 N 1 A LFA 318 ? C9  ? S  LFA 1   C9  
237 1 N 1 A LFA 318 ? C10 ? S  LFA 1   C10 
238 1 N 1 A LFA 318 ? C11 ? S  LFA 1   C11 
239 1 N 1 A LFA 318 ? C12 ? S  LFA 1   C12 
240 1 N 1 A LFA 318 ? C13 ? S  LFA 1   C13 
241 1 N 1 A LFA 318 ? C14 ? S  LFA 1   C14 
242 1 N 1 A LFA 318 ? C15 ? S  LFA 1   C15 
243 1 N 1 A LFA 318 ? C16 ? S  LFA 1   C16 
244 1 N 1 A OLC 319 ? C18 ? T  OLC 1   C18 
245 1 N 1 A OLC 319 ? C10 ? T  OLC 1   C10 
246 1 N 1 A OLC 319 ? C9  ? T  OLC 1   C9  
247 1 N 1 A OLC 319 ? C17 ? T  OLC 1   C17 
248 1 N 1 A OLC 319 ? C11 ? T  OLC 1   C11 
249 1 N 1 A OLC 319 ? C24 ? T  OLC 1   C24 
250 1 N 1 A OLC 319 ? C16 ? T  OLC 1   C16 
251 1 N 1 A OLC 319 ? C12 ? T  OLC 1   C12 
252 1 N 1 A OLC 319 ? C15 ? T  OLC 1   C15 
253 1 N 1 A OLC 319 ? C13 ? T  OLC 1   C13 
254 1 N 1 A OLC 319 ? C14 ? T  OLC 1   C14 
255 1 N 1 A OLC 319 ? C21 ? T  OLC 1   C21 
256 1 N 1 A OLC 319 ? C22 ? T  OLC 1   C22 
257 1 N 1 A OLC 319 ? O25 ? T  OLC 1   O25 
258 1 N 1 A OLC 319 ? O23 ? T  OLC 1   O23 
259 1 N 1 A OLC 320 ? C18 ? U  OLC 1   C18 
260 1 N 1 A OLC 320 ? C10 ? U  OLC 1   C10 
261 1 N 1 A OLC 320 ? C9  ? U  OLC 1   C9  
262 1 N 1 A OLC 320 ? C17 ? U  OLC 1   C17 
263 1 N 1 A OLC 320 ? C11 ? U  OLC 1   C11 
264 1 N 1 A OLC 320 ? C8  ? U  OLC 1   C8  
265 1 N 1 A OLC 320 ? C24 ? U  OLC 1   C24 
266 1 N 1 A OLC 320 ? C16 ? U  OLC 1   C16 
267 1 N 1 A OLC 320 ? C12 ? U  OLC 1   C12 
268 1 N 1 A OLC 320 ? C7  ? U  OLC 1   C7  
269 1 N 1 A OLC 320 ? C15 ? U  OLC 1   C15 
270 1 N 1 A OLC 320 ? C13 ? U  OLC 1   C13 
271 1 N 1 A OLC 320 ? C6  ? U  OLC 1   C6  
272 1 N 1 A OLC 320 ? C14 ? U  OLC 1   C14 
273 1 N 1 A OLC 320 ? C5  ? U  OLC 1   C5  
274 1 N 1 A OLC 320 ? C4  ? U  OLC 1   C4  
275 1 N 1 A OLC 320 ? C21 ? U  OLC 1   C21 
276 1 N 1 A OLC 320 ? C22 ? U  OLC 1   C22 
277 1 N 1 A OLC 320 ? O25 ? U  OLC 1   O25 
278 1 N 1 A OLC 320 ? O23 ? U  OLC 1   O23 
279 1 N 1 A OLC 321 ? C18 ? V  OLC 1   C18 
280 1 N 1 A OLC 321 ? C17 ? V  OLC 1   C17 
281 1 N 1 A OLC 321 ? C24 ? V  OLC 1   C24 
282 1 N 1 A OLC 321 ? C16 ? V  OLC 1   C16 
283 1 N 1 A OLC 321 ? C15 ? V  OLC 1   C15 
284 1 N 1 A OLC 321 ? C13 ? V  OLC 1   C13 
285 1 N 1 A OLC 321 ? C14 ? V  OLC 1   C14 
286 1 N 1 A OLC 321 ? O25 ? V  OLC 1   O25 
287 1 N 1 A OLC 322 ? C18 ? W  OLC 1   C18 
288 1 N 1 A OLC 322 ? C17 ? W  OLC 1   C17 
289 1 N 1 A OLC 322 ? C24 ? W  OLC 1   C24 
290 1 N 1 A OLC 322 ? C16 ? W  OLC 1   C16 
291 1 N 1 A OLC 322 ? C15 ? W  OLC 1   C15 
292 1 N 1 A OLC 322 ? C13 ? W  OLC 1   C13 
293 1 N 1 A OLC 322 ? C14 ? W  OLC 1   C14 
294 1 N 1 A OLC 322 ? C21 ? W  OLC 1   C21 
295 1 N 1 A OLC 322 ? C22 ? W  OLC 1   C22 
296 1 N 1 A OLC 322 ? O25 ? W  OLC 1   O25 
297 1 N 1 A OLC 322 ? O23 ? W  OLC 1   O23 
298 1 N 1 A LFA 323 ? C7  ? X  LFA 1   C7  
299 1 N 1 A LFA 323 ? C8  ? X  LFA 1   C8  
300 1 N 1 A LFA 323 ? C9  ? X  LFA 1   C9  
301 1 N 1 A LFA 323 ? C10 ? X  LFA 1   C10 
302 1 N 1 A LFA 323 ? C11 ? X  LFA 1   C11 
303 1 N 1 A LFA 323 ? C12 ? X  LFA 1   C12 
304 1 N 1 A LFA 323 ? C13 ? X  LFA 1   C13 
305 1 N 1 A LFA 323 ? C14 ? X  LFA 1   C14 
306 1 N 1 A LFA 323 ? C15 ? X  LFA 1   C15 
307 1 N 1 A LFA 323 ? C16 ? X  LFA 1   C16 
308 1 N 1 A LFA 323 ? C17 ? X  LFA 1   C17 
309 1 N 1 A LFA 323 ? C18 ? X  LFA 1   C18 
310 1 N 1 A LFA 323 ? C19 ? X  LFA 1   C19 
311 1 N 1 A LFA 323 ? C20 ? X  LFA 1   C20 
312 1 N 1 A LFA 324 ? C4  ? Y  LFA 1   C4  
313 1 N 1 A LFA 324 ? C5  ? Y  LFA 1   C5  
314 1 N 1 A LFA 324 ? C6  ? Y  LFA 1   C6  
315 1 N 1 A LFA 324 ? C7  ? Y  LFA 1   C7  
316 1 N 1 A LFA 324 ? C8  ? Y  LFA 1   C8  
317 1 N 1 A LFA 324 ? C9  ? Y  LFA 1   C9  
318 1 N 1 A LFA 324 ? C10 ? Y  LFA 1   C10 
319 1 N 1 A LFA 324 ? C11 ? Y  LFA 1   C11 
320 1 N 1 A LFA 324 ? C12 ? Y  LFA 1   C12 
321 1 N 1 A LFA 324 ? C13 ? Y  LFA 1   C13 
322 1 N 1 A LFA 324 ? C14 ? Y  LFA 1   C14 
323 1 N 1 A LFA 324 ? C15 ? Y  LFA 1   C15 
324 1 N 1 A LFA 324 ? C16 ? Y  LFA 1   C16 
325 1 N 1 A LFA 324 ? C17 ? Y  LFA 1   C17 
326 1 N 1 A LFA 324 ? C18 ? Y  LFA 1   C18 
327 1 N 1 A LFA 324 ? C19 ? Y  LFA 1   C19 
328 1 N 1 A LFA 324 ? C20 ? Y  LFA 1   C20 
329 1 N 1 A LFA 325 ? C8  ? Z  LFA 1   C8  
330 1 N 1 A LFA 325 ? C9  ? Z  LFA 1   C9  
331 1 N 1 A LFA 325 ? C10 ? Z  LFA 1   C10 
332 1 N 1 A LFA 325 ? C11 ? Z  LFA 1   C11 
333 1 N 1 A LFA 325 ? C12 ? Z  LFA 1   C12 
334 1 N 1 A LFA 325 ? C13 ? Z  LFA 1   C13 
335 1 N 1 A LFA 325 ? C14 ? Z  LFA 1   C14 
336 1 N 1 A LFA 325 ? C15 ? Z  LFA 1   C15 
337 1 N 1 A LFA 325 ? C16 ? Z  LFA 1   C16 
338 1 N 1 A LFA 325 ? C17 ? Z  LFA 1   C17 
339 1 N 1 A LFA 325 ? C18 ? Z  LFA 1   C18 
340 1 N 1 A LFA 325 ? C19 ? Z  LFA 1   C19 
341 1 N 1 A LFA 325 ? C20 ? Z  LFA 1   C20 
342 1 N 1 A LFA 326 ? C5  ? AA LFA 1   C5  
343 1 N 1 A LFA 326 ? C6  ? AA LFA 1   C6  
344 1 N 1 A LFA 326 ? C7  ? AA LFA 1   C7  
345 1 N 1 A LFA 326 ? C8  ? AA LFA 1   C8  
346 1 N 1 A LFA 326 ? C9  ? AA LFA 1   C9  
347 1 N 1 A LFA 326 ? C10 ? AA LFA 1   C10 
348 1 N 1 A LFA 326 ? C11 ? AA LFA 1   C11 
349 1 N 1 A LFA 326 ? C12 ? AA LFA 1   C12 
350 1 N 1 A LFA 326 ? C13 ? AA LFA 1   C13 
351 1 N 1 A LFA 326 ? C14 ? AA LFA 1   C14 
352 1 N 1 A LFA 326 ? C15 ? AA LFA 1   C15 
353 1 N 1 A LFA 326 ? C16 ? AA LFA 1   C16 
354 1 N 1 A LFA 326 ? C17 ? AA LFA 1   C17 
355 1 N 1 A LFA 326 ? C18 ? AA LFA 1   C18 
356 1 N 1 A LFA 326 ? C19 ? AA LFA 1   C19 
357 1 N 1 A LFA 326 ? C20 ? AA LFA 1   C20 
# 
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 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE    ? ? ? 3           1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 5 
# 
_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                     9IN9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.235 
_cell.length_a_esd                 ? 
_cell.length_b                     115.755 
_cell.length_b_esd                 ? 
_cell.length_c                     53.214 
_cell.length_c_esd                 ? 
_cell.volume                       284797.732 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9IN9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   9IN9 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.10 
_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              8.0 
_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    
'100 mM Tris, 900 mM NaCl, and 24% (w/v) PEG 6000; Soaked: 100 mM sodium citrate pH 2.5, 900 mM NaCl, and 24% (w/v) PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X CdTe 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         2022-10-06 
_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   0.8856 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          24.97 
_reflns.entry_id                                       9IN9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.41 
_reflns.d_resolution_low                               33.42 
_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                                     36461 
_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                           92.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_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                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.41 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1824 
_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                               6.6 
_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                               0.952 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.316 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          75.9 
_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                               31.74 
_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                                 9IN9 
_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                            1.41 
_refine.ls_d_res_low                             33.42 
_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                     36424 
_refine.ls_number_reflns_R_free                  1781 
_refine.ls_number_reflns_R_work                  34643 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    64.55 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1892 
_refine.ls_R_factor_R_free                       0.2180 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1877 
_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                          1.34 
_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                      7AKY 
_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                 34.9591 
_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                            0.1651 
_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                       1.41 
_refine_hist.d_res_low                        33.42 
_refine_hist.number_atoms_solvent             111 
_refine_hist.number_atoms_total               2231 
_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        1900 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         220 
_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' ? 0.0082  ? 2952 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9312  ? 3979 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0745  ? 427  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0060  ? 478  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7115 ? 1097 ? 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' 1.41 1.44  . . 5   165  4.06  . . . . 0.3946 . . . . . . . . . . . 0.2906 
'X-RAY DIFFRACTION' 1.44 1.49  . . 25  391  9.78  . . . . 0.3294 . . . . . . . . . . . 0.3796 
'X-RAY DIFFRACTION' 1.49 1.53  . . 48  851  20.99 . . . . 0.2904 . . . . . . . . . . . 0.3186 
'X-RAY DIFFRACTION' 1.53 1.59  . . 66  1258 30.93 . . . . 0.3102 . . . . . . . . . . . 0.3152 
'X-RAY DIFFRACTION' 1.59 1.65  . . 104 1868 45.88 . . . . 0.3125 . . . . . . . . . . . 0.3463 
'X-RAY DIFFRACTION' 1.65 1.73  . . 116 2527 61.48 . . . . 0.2932 . . . . . . . . . . . 0.3330 
'X-RAY DIFFRACTION' 1.73 1.82  . . 147 3291 80.61 . . . . 0.2773 . . . . . . . . . . . 0.3112 
'X-RAY DIFFRACTION' 1.82 1.93  . . 186 3794 91.49 . . . . 0.2404 . . . . . . . . . . . 0.2781 
'X-RAY DIFFRACTION' 1.93 2.08  . . 207 4070 98.89 . . . . 0.1916 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.08 2.29  . . 204 4083 98.42 . . . . 0.1712 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 2.29 2.62  . . 234 4048 97.94 . . . . 0.1628 . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 2.62 3.30  . . 202 4120 97.32 . . . . 0.1669 . . . . . . . . . . . 0.1928 
'X-RAY DIFFRACTION' 3.30 33.42 . . 237 4177 95.75 . . . . 0.1847 . . . . . . . . . . . 0.2136 
# 
_struct.entry_id                     9IN9 
_struct.title                        'Structure of the viral channelrhodopsin OLPVR1 at low pH obtained by soaking' 
_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        9IN9 
_struct_keywords.text            'rhodopsin, ChR2, open state, open channel, ChRMine, cation-conducting ChR, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 3 ? 
D  N N 4 ? 
E  N N 4 ? 
F  N N 4 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 5 ? 
U  N N 5 ? 
V  N N 5 ? 
W  N N 5 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    F2Y337_9PHYC 
_struct_ref.pdbx_db_accession          F2Y337 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFDWVLT
TPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLLYVKY
TKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLL
;
_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              9IN9 
_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                 223 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             F2Y337 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  223 
_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       223 
# 
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 9IN9 LEU A 224 ? UNP F2Y337 ? ? 'expression tag' 224 1 
1 9IN9 GLU A 225 ? UNP F2Y337 ? ? 'expression tag' 225 2 
1 9IN9 HIS A 226 ? UNP F2Y337 ? ? 'expression tag' 226 3 
1 9IN9 HIS A 227 ? UNP F2Y337 ? ? 'expression tag' 227 4 
1 9IN9 HIS A 228 ? UNP F2Y337 ? ? 'expression tag' 228 5 
1 9IN9 HIS A 229 ? UNP F2Y337 ? ? 'expression tag' 229 6 
1 9IN9 HIS A 230 ? UNP F2Y337 ? ? 'expression tag' 230 7 
1 9IN9 HIS A 231 ? UNP F2Y337 ? ? 'expression tag' 231 8 
# 
_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)' 5680  ? 
1 MORE         26    ? 
1 'SSA (A^2)'  12250 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 FME A 1   ? PHE A 27  ? FME A 1   PHE A 27  1 ? 27 
HELX_P HELX_P2  AA2 ASP A 34  ? LEU A 62  ? ASP A 34  LEU A 62  1 ? 29 
HELX_P HELX_P3  AA3 GLN A 63  ? ILE A 65  ? GLN A 63  ILE A 65  5 ? 3  
HELX_P HELX_P4  AA4 ILE A 69  ? TYR A 71  ? ILE A 69  TYR A 71  5 ? 3  
HELX_P HELX_P5  AA5 VAL A 72  ? SER A 97  ? VAL A 72  SER A 97  1 ? 26 
HELX_P HELX_P6  AA6 ARG A 102 ? THR A 133 ? ARG A 102 THR A 133 1 ? 32 
HELX_P HELX_P7  AA7 ASN A 137 ? THR A 161 ? ASN A 137 THR A 161 1 ? 25 
HELX_P HELX_P8  AA8 ASN A 164 ? MET A 186 ? ASN A 164 MET A 186 1 ? 23 
HELX_P HELX_P9  AA9 PRO A 188 ? LYS A 204 ? PRO A 188 LYS A 204 1 ? 17 
HELX_P HELX_P10 AB1 LYS A 204 ? LEU A 224 ? LYS A 204 LEU A 224 1 ? 21 
# 
_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 both ? A FME 1   C  ? ? ? 1_555 A ASP 2 N   A ? A FME 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2 covale both ? A FME 1   C  ? ? ? 1_555 A ASP 2 N   B ? A FME 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale3 covale one  ? A LYS 204 NZ A ? ? 1_555 B RET . C15 A ? A LYS 204 A RET 301 1_555 ? ? ? ? ? ? ? 1.483 ? ? 
covale4 covale one  ? A LYS 204 NZ B ? ? 1_555 B RET . C15 B ? A LYS 204 A RET 301 1_555 ? ? ? ? ? ? ? 1.436 ? ? 
# 
_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 FME A 1 ? .   . .   . FME A 1   ? 1_555 .   . .   . .     .   .  MET 1 FME Formylation   'Named protein modification' 
2 RET B . A LYS A 204 A RET A 301 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
3 RET B . B LYS A 204 B RET A 301 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
# 
_pdbx_entry_details.entry_id                   9IN9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 SER A 64  ? A -115.86 65.75  
2 1 LYS A 204 ? A -96.55  -65.39 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    FME 
_pdbx_struct_mod_residue.label_seq_id     1 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     FME 
_pdbx_struct_mod_residue.auth_seq_id      1 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   MET 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_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     449 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   BA 
_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+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 1.15778489854  29.2224467102 -1.30915513773  0.220853231135 ? -0.0548852148503   ? 
-0.00454753351951 ? 0.231608057989 ? 0.000514978828993 ? 0.243809292095 ? 0.536372574531 ? -0.318507649023 ? -0.115415134073  ? 
0.683107870356 ? 0.33404860595   ? 0.0969142258576 ? 0.0624852460324   ? 0.0127405479509   ? 0.0570924694871  ? -0.0636265442362 ? 
0.0148860843828  ? -0.0120857562194 ? -0.296988023083 ? 0.15552431515    ? 0.000219490225942  ? 
2 'X-RAY DIFFRACTION' ? refined 2.9325036334   21.0196635712 1.60541148831   0.194414768443 ? -0.0426485537214   ? 
-0.0164371988112  ? 0.17164471487  ? -0.0190153038666  ? 0.22663416917  ? 0.914522879862 ? -0.461623915218 ? 0.250062147873   ? 
0.673038142045 ? -0.135306463059 ? 0.303121105984  ? 0.205036319864    ? -0.00690056115137 ? 0.0739972587763  ? 0.0820171248247  ? 
0.0942417983042  ? -0.10636749197   ? -0.627688828535 ? 0.310903249867   ? 0.00787432786621   ? 
3 'X-RAY DIFFRACTION' ? refined -8.68497376911 10.6627132748 -0.167743050647 0.148687375791 ? -0.000387000517556 ? 
-0.0136722223262  ? 0.135730567342 ? -0.0136680741842  ? 0.16696153901  ? 1.08836430501  ? -0.347747114579 ? 0.01304828128    ? 
1.20070059474  ? 0.0291759715083 ? 1.17987615073   ? -0.00204893376409 ? 0.0535141874122   ? -0.0958705501935 ? -0.0377656196093 ? 
-0.0133009586041 ? 0.0803283666243  ? 0.137324139721  ? -0.0402677552439 ? -0.000195955326803 ? 
4 'X-RAY DIFFRACTION' ? refined -5.76645468941 24.9408548336 -0.20015078963  0.161951893052 ? -0.00560601369458  ? 
-0.0153858596996  ? 0.166559975867 ? -0.00321750775008 ? 0.200301626202 ? 0.960326061623 ? -0.345969641773 ? -0.0338519650549 ? 
0.853000909864 ? -0.509525668255 ? 0.317046319306  ? 0.126288207809    ? -0.0945334977893  ? -0.0191470987415 ? 0.00501355109052 ? 
0.118154438782   ? -0.152885736675  ? -0.148201659997 ? 0.125071089424   ? 0.000498057596561  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 2   A 2   ? A 31  A 31  ? ? 
;chain 'A' and (resid 2 through 31 )
;
2 'X-RAY DIFFRACTION' 2 A 32  A 32  ? A 64  A 64  ? ? 
;chain 'A' and (resid 32 through 64 )
;
3 'X-RAY DIFFRACTION' 3 A 65  A 65  ? A 186 A 186 ? ? 
;chain 'A' and (resid 65 through 186 )
;
4 'X-RAY DIFFRACTION' 4 A 187 A 187 ? A 225 A 225 ? ? 
;chain 'A' and (resid 187 through 225 )
;
# 
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 HIS 226 ? A HIS 226 
2 1 Y 1 A HIS 227 ? A HIS 227 
3 1 Y 1 A HIS 228 ? A HIS 228 
4 1 Y 1 A HIS 229 ? A HIS 229 
5 1 Y 1 A HIS 230 ? A HIS 230 
6 1 Y 1 A HIS 231 ? A HIS 231 
# 
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 
97N C    C N N 1   
97N O    O N N 2   
97N C1   C N N 3   
97N O1   O N N 4   
97N C2   C N N 5   
97N O2   O N N 6   
97N C3   C N N 7   
97N O3   O N N 8   
97N C4   C N N 9   
97N C5   C N N 10  
97N C6   C N N 11  
97N C7   C N N 12  
97N C8   C N N 13  
97N C9   C N N 14  
97N C10  C N N 15  
97N C11  C N N 16  
97N C12  C N N 17  
97N C13  C N N 18  
97N C14  C N N 19  
97N C15  C N N 20  
97N C16  C N N 21  
97N C17  C N S 22  
97N C18  C N N 23  
97N H1   H N N 24  
97N H2   H N N 25  
97N H3   H N N 26  
97N H4   H N N 27  
97N H5   H N N 28  
97N H6   H N N 29  
97N H7   H N N 30  
97N H8   H N N 31  
97N H9   H N N 32  
97N H10  H N N 33  
97N H11  H N N 34  
97N H12  H N N 35  
97N H13  H N N 36  
97N H14  H N N 37  
97N H15  H N N 38  
97N H16  H N N 39  
97N H17  H N N 40  
97N H18  H N N 41  
97N H19  H N N 42  
97N H20  H N N 43  
97N H21  H N N 44  
97N H22  H N N 45  
97N H23  H N N 46  
97N H24  H N N 47  
97N H25  H N N 48  
97N H26  H N N 49  
97N H27  H N N 50  
97N H28  H N N 51  
97N H29  H N N 52  
97N H30  H N N 53  
97N H31  H N N 54  
97N H32  H N N 55  
97N H33  H N N 56  
97N H34  H N N 57  
97N H35  H N N 58  
97N H36  H N N 59  
ALA N    N N N 60  
ALA CA   C N S 61  
ALA C    C N N 62  
ALA O    O N N 63  
ALA CB   C N N 64  
ALA OXT  O N N 65  
ALA H    H N N 66  
ALA H2   H N N 67  
ALA HA   H N N 68  
ALA HB1  H N N 69  
ALA HB2  H N N 70  
ALA HB3  H N N 71  
ALA HXT  H N N 72  
ARG N    N N N 73  
ARG CA   C N S 74  
ARG C    C N N 75  
ARG O    O N N 76  
ARG CB   C N N 77  
ARG CG   C N N 78  
ARG CD   C N N 79  
ARG NE   N N N 80  
ARG CZ   C N N 81  
ARG NH1  N N N 82  
ARG NH2  N N N 83  
ARG OXT  O N N 84  
ARG H    H N N 85  
ARG H2   H N N 86  
ARG HA   H N N 87  
ARG HB2  H N N 88  
ARG HB3  H N N 89  
ARG HG2  H N N 90  
ARG HG3  H N N 91  
ARG HD2  H N N 92  
ARG HD3  H N N 93  
ARG HE   H N N 94  
ARG HH11 H N N 95  
ARG HH12 H N N 96  
ARG HH21 H N N 97  
ARG HH22 H N N 98  
ARG HXT  H N N 99  
ASN N    N N N 100 
ASN CA   C N S 101 
ASN C    C N N 102 
ASN O    O N N 103 
ASN CB   C N N 104 
ASN CG   C N N 105 
ASN OD1  O N N 106 
ASN ND2  N N N 107 
ASN OXT  O N N 108 
ASN H    H N N 109 
ASN H2   H N N 110 
ASN HA   H N N 111 
ASN HB2  H N N 112 
ASN HB3  H N N 113 
ASN HD21 H N N 114 
ASN HD22 H N N 115 
ASN HXT  H N N 116 
ASP N    N N N 117 
ASP CA   C N S 118 
ASP C    C N N 119 
ASP O    O N N 120 
ASP CB   C N N 121 
ASP CG   C N N 122 
ASP OD1  O N N 123 
ASP OD2  O N N 124 
ASP OXT  O N N 125 
ASP H    H N N 126 
ASP H2   H N N 127 
ASP HA   H N N 128 
ASP HB2  H N N 129 
ASP HB3  H N N 130 
ASP HD2  H N N 131 
ASP HXT  H N N 132 
CYS N    N N N 133 
CYS CA   C N R 134 
CYS C    C N N 135 
CYS O    O N N 136 
CYS CB   C N N 137 
CYS SG   S N N 138 
CYS OXT  O N N 139 
CYS H    H N N 140 
CYS H2   H N N 141 
CYS HA   H N N 142 
CYS HB2  H N N 143 
CYS HB3  H N N 144 
CYS HG   H N N 145 
CYS HXT  H N N 146 
FME N    N N N 147 
FME CN   C N N 148 
FME O1   O N N 149 
FME CA   C N S 150 
FME CB   C N N 151 
FME CG   C N N 152 
FME SD   S N N 153 
FME CE   C N N 154 
FME C    C N N 155 
FME O    O N N 156 
FME OXT  O N N 157 
FME H    H N N 158 
FME HCN  H N N 159 
FME HA   H N N 160 
FME HB2  H N N 161 
FME HB3  H N N 162 
FME HG2  H N N 163 
FME HG3  H N N 164 
FME HE1  H N N 165 
FME HE2  H N N 166 
FME HE3  H N N 167 
FME HXT  H N N 168 
GLN N    N N N 169 
GLN CA   C N S 170 
GLN C    C N N 171 
GLN O    O N N 172 
GLN CB   C N N 173 
GLN CG   C N N 174 
GLN CD   C N N 175 
GLN OE1  O N N 176 
GLN NE2  N N N 177 
GLN OXT  O N N 178 
GLN H    H N N 179 
GLN H2   H N N 180 
GLN HA   H N N 181 
GLN HB2  H N N 182 
GLN HB3  H N N 183 
GLN HG2  H N N 184 
GLN HG3  H N N 185 
GLN HE21 H N N 186 
GLN HE22 H N N 187 
GLN HXT  H N N 188 
GLU N    N N N 189 
GLU CA   C N S 190 
GLU C    C N N 191 
GLU O    O N N 192 
GLU CB   C N N 193 
GLU CG   C N N 194 
GLU CD   C N N 195 
GLU OE1  O N N 196 
GLU OE2  O N N 197 
GLU OXT  O N N 198 
GLU H    H N N 199 
GLU H2   H N N 200 
GLU HA   H N N 201 
GLU HB2  H N N 202 
GLU HB3  H N N 203 
GLU HG2  H N N 204 
GLU HG3  H N N 205 
GLU HE2  H N N 206 
GLU HXT  H N N 207 
GLY N    N N N 208 
GLY CA   C N N 209 
GLY C    C N N 210 
GLY O    O N N 211 
GLY OXT  O N N 212 
GLY H    H N N 213 
GLY H2   H N N 214 
GLY HA2  H N N 215 
GLY HA3  H N N 216 
GLY HXT  H N N 217 
HIS N    N N N 218 
HIS CA   C N S 219 
HIS C    C N N 220 
HIS O    O N N 221 
HIS CB   C N N 222 
HIS CG   C Y N 223 
HIS ND1  N Y N 224 
HIS CD2  C Y N 225 
HIS CE1  C Y N 226 
HIS NE2  N Y N 227 
HIS OXT  O N N 228 
HIS H    H N N 229 
HIS H2   H N N 230 
HIS HA   H N N 231 
HIS HB2  H N N 232 
HIS HB3  H N N 233 
HIS HD1  H N N 234 
HIS HD2  H N N 235 
HIS HE1  H N N 236 
HIS HE2  H N N 237 
HIS HXT  H N N 238 
HOH O    O N N 239 
HOH H1   H N N 240 
HOH H2   H N N 241 
ILE N    N N N 242 
ILE CA   C N S 243 
ILE C    C N N 244 
ILE O    O N N 245 
ILE CB   C N S 246 
ILE CG1  C N N 247 
ILE CG2  C N N 248 
ILE CD1  C N N 249 
ILE OXT  O N N 250 
ILE H    H N N 251 
ILE H2   H N N 252 
ILE HA   H N N 253 
ILE HB   H N N 254 
ILE HG12 H N N 255 
ILE HG13 H N N 256 
ILE HG21 H N N 257 
ILE HG22 H N N 258 
ILE HG23 H N N 259 
ILE HD11 H N N 260 
ILE HD12 H N N 261 
ILE HD13 H N N 262 
ILE HXT  H N N 263 
LEU N    N N N 264 
LEU CA   C N S 265 
LEU C    C N N 266 
LEU O    O N N 267 
LEU CB   C N N 268 
LEU CG   C N N 269 
LEU CD1  C N N 270 
LEU CD2  C N N 271 
LEU OXT  O N N 272 
LEU H    H N N 273 
LEU H2   H N N 274 
LEU HA   H N N 275 
LEU HB2  H N N 276 
LEU HB3  H N N 277 
LEU HG   H N N 278 
LEU HD11 H N N 279 
LEU HD12 H N N 280 
LEU HD13 H N N 281 
LEU HD21 H N N 282 
LEU HD22 H N N 283 
LEU HD23 H N N 284 
LEU HXT  H N N 285 
LFA C1   C N N 286 
LFA C2   C N N 287 
LFA C3   C N N 288 
LFA C4   C N N 289 
LFA C5   C N N 290 
LFA C6   C N N 291 
LFA C7   C N N 292 
LFA C8   C N N 293 
LFA C9   C N N 294 
LFA C10  C N N 295 
LFA C11  C N N 296 
LFA C12  C N N 297 
LFA C13  C N N 298 
LFA C14  C N N 299 
LFA C15  C N N 300 
LFA C16  C N N 301 
LFA C17  C N N 302 
LFA C18  C N N 303 
LFA C19  C N N 304 
LFA C20  C N N 305 
LFA H11  H N N 306 
LFA H12  H N N 307 
LFA H13  H N N 308 
LFA H21  H N N 309 
LFA H22  H N N 310 
LFA H31  H N N 311 
LFA H32  H N N 312 
LFA H41  H N N 313 
LFA H42  H N N 314 
LFA H51  H N N 315 
LFA H52  H N N 316 
LFA H61  H N N 317 
LFA H62  H N N 318 
LFA H71  H N N 319 
LFA H72  H N N 320 
LFA H81  H N N 321 
LFA H82  H N N 322 
LFA H91  H N N 323 
LFA H92  H N N 324 
LFA H101 H N N 325 
LFA H102 H N N 326 
LFA H111 H N N 327 
LFA H112 H N N 328 
LFA H121 H N N 329 
LFA H122 H N N 330 
LFA H131 H N N 331 
LFA H132 H N N 332 
LFA H141 H N N 333 
LFA H142 H N N 334 
LFA H151 H N N 335 
LFA H152 H N N 336 
LFA H161 H N N 337 
LFA H162 H N N 338 
LFA H171 H N N 339 
LFA H172 H N N 340 
LFA H181 H N N 341 
LFA H182 H N N 342 
LFA H191 H N N 343 
LFA H192 H N N 344 
LFA H201 H N N 345 
LFA H202 H N N 346 
LFA H203 H N N 347 
LYS N    N N N 348 
LYS CA   C N S 349 
LYS C    C N N 350 
LYS O    O N N 351 
LYS CB   C N N 352 
LYS CG   C N N 353 
LYS CD   C N N 354 
LYS CE   C N N 355 
LYS NZ   N N N 356 
LYS OXT  O N N 357 
LYS H    H N N 358 
LYS H2   H N N 359 
LYS HA   H N N 360 
LYS HB2  H N N 361 
LYS HB3  H N N 362 
LYS HG2  H N N 363 
LYS HG3  H N N 364 
LYS HD2  H N N 365 
LYS HD3  H N N 366 
LYS HE2  H N N 367 
LYS HE3  H N N 368 
LYS HZ1  H N N 369 
LYS HZ2  H N N 370 
LYS HZ3  H N N 371 
LYS HXT  H N N 372 
MET N    N N N 373 
MET CA   C N S 374 
MET C    C N N 375 
MET O    O N N 376 
MET CB   C N N 377 
MET CG   C N N 378 
MET SD   S N N 379 
MET CE   C N N 380 
MET OXT  O N N 381 
MET H    H N N 382 
MET H2   H N N 383 
MET HA   H N N 384 
MET HB2  H N N 385 
MET HB3  H N N 386 
MET HG2  H N N 387 
MET HG3  H N N 388 
MET HE1  H N N 389 
MET HE2  H N N 390 
MET HE3  H N N 391 
MET HXT  H N N 392 
OLC C18  C N N 393 
OLC C10  C N N 394 
OLC C9   C N N 395 
OLC C17  C N N 396 
OLC C11  C N N 397 
OLC C8   C N N 398 
OLC C24  C N N 399 
OLC C16  C N N 400 
OLC C12  C N N 401 
OLC C7   C N N 402 
OLC C15  C N N 403 
OLC C13  C N N 404 
OLC C6   C N N 405 
OLC C14  C N N 406 
OLC C5   C N N 407 
OLC C4   C N N 408 
OLC C3   C N N 409 
OLC C2   C N N 410 
OLC C21  C N N 411 
OLC C1   C N N 412 
OLC C22  C N R 413 
OLC O19  O N N 414 
OLC O25  O N N 415 
OLC O23  O N N 416 
OLC O20  O N N 417 
OLC H18  H N N 418 
OLC H18A H N N 419 
OLC H18B H N N 420 
OLC H10  H N N 421 
OLC H9   H N N 422 
OLC H17  H N N 423 
OLC H17A H N N 424 
OLC H11  H N N 425 
OLC H11A H N N 426 
OLC H8   H N N 427 
OLC H8A  H N N 428 
OLC H24  H N N 429 
OLC H24A H N N 430 
OLC H16  H N N 431 
OLC H16A H N N 432 
OLC H12  H N N 433 
OLC H12A H N N 434 
OLC H7   H N N 435 
OLC H7A  H N N 436 
OLC H15  H N N 437 
OLC H15A H N N 438 
OLC H13  H N N 439 
OLC H13A H N N 440 
OLC H6   H N N 441 
OLC H6A  H N N 442 
OLC H14  H N N 443 
OLC H14A H N N 444 
OLC H5   H N N 445 
OLC H5A  H N N 446 
OLC H4   H N N 447 
OLC H4A  H N N 448 
OLC H3   H N N 449 
OLC H3A  H N N 450 
OLC H2   H N N 451 
OLC H2A  H N N 452 
OLC H21  H N N 453 
OLC H21A H N N 454 
OLC H22  H N N 455 
OLC HO25 H N N 456 
OLC HO23 H N N 457 
PHE N    N N N 458 
PHE CA   C N S 459 
PHE C    C N N 460 
PHE O    O N N 461 
PHE CB   C N N 462 
PHE CG   C Y N 463 
PHE CD1  C Y N 464 
PHE CD2  C Y N 465 
PHE CE1  C Y N 466 
PHE CE2  C Y N 467 
PHE CZ   C Y N 468 
PHE OXT  O N N 469 
PHE H    H N N 470 
PHE H2   H N N 471 
PHE HA   H N N 472 
PHE HB2  H N N 473 
PHE HB3  H N N 474 
PHE HD1  H N N 475 
PHE HD2  H N N 476 
PHE HE1  H N N 477 
PHE HE2  H N N 478 
PHE HZ   H N N 479 
PHE HXT  H N N 480 
PRO N    N N N 481 
PRO CA   C N S 482 
PRO C    C N N 483 
PRO O    O N N 484 
PRO CB   C N N 485 
PRO CG   C N N 486 
PRO CD   C N N 487 
PRO OXT  O N N 488 
PRO H    H N N 489 
PRO HA   H N N 490 
PRO HB2  H N N 491 
PRO HB3  H N N 492 
PRO HG2  H N N 493 
PRO HG3  H N N 494 
PRO HD2  H N N 495 
PRO HD3  H N N 496 
PRO HXT  H N N 497 
RET C1   C N N 498 
RET C2   C N N 499 
RET C3   C N N 500 
RET C4   C N N 501 
RET C5   C N N 502 
RET C6   C N N 503 
RET C7   C N N 504 
RET C8   C N N 505 
RET C9   C N N 506 
RET C10  C N N 507 
RET C11  C N N 508 
RET C12  C N N 509 
RET C13  C N N 510 
RET C14  C N N 511 
RET C15  C N N 512 
RET O1   O N N 513 
RET C16  C N N 514 
RET C17  C N N 515 
RET C18  C N N 516 
RET C19  C N N 517 
RET C20  C N N 518 
RET H21  H N N 519 
RET H22  H N N 520 
RET H31  H N N 521 
RET H32  H N N 522 
RET H41  H N N 523 
RET H42  H N N 524 
RET H7   H N N 525 
RET H8   H N N 526 
RET H10  H N N 527 
RET H11  H N N 528 
RET H12  H N N 529 
RET H14  H N N 530 
RET H15  H N N 531 
RET H161 H N N 532 
RET H162 H N N 533 
RET H163 H N N 534 
RET H171 H N N 535 
RET H172 H N N 536 
RET H173 H N N 537 
RET H181 H N N 538 
RET H182 H N N 539 
RET H183 H N N 540 
RET H191 H N N 541 
RET H192 H N N 542 
RET H193 H N N 543 
RET H201 H N N 544 
RET H202 H N N 545 
RET H203 H N N 546 
SER N    N N N 547 
SER CA   C N S 548 
SER C    C N N 549 
SER O    O N N 550 
SER CB   C N N 551 
SER OG   O N N 552 
SER OXT  O N N 553 
SER H    H N N 554 
SER H2   H N N 555 
SER HA   H N N 556 
SER HB2  H N N 557 
SER HB3  H N N 558 
SER HG   H N N 559 
SER HXT  H N N 560 
THR N    N N N 561 
THR CA   C N S 562 
THR C    C N N 563 
THR O    O N N 564 
THR CB   C N R 565 
THR OG1  O N N 566 
THR CG2  C N N 567 
THR OXT  O N N 568 
THR H    H N N 569 
THR H2   H N N 570 
THR HA   H N N 571 
THR HB   H N N 572 
THR HG1  H N N 573 
THR HG21 H N N 574 
THR HG22 H N N 575 
THR HG23 H N N 576 
THR HXT  H N N 577 
TRP N    N N N 578 
TRP CA   C N S 579 
TRP C    C N N 580 
TRP O    O N N 581 
TRP CB   C N N 582 
TRP CG   C Y N 583 
TRP CD1  C Y N 584 
TRP CD2  C Y N 585 
TRP NE1  N Y N 586 
TRP CE2  C Y N 587 
TRP CE3  C Y N 588 
TRP CZ2  C Y N 589 
TRP CZ3  C Y N 590 
TRP CH2  C Y N 591 
TRP OXT  O N N 592 
TRP H    H N N 593 
TRP H2   H N N 594 
TRP HA   H N N 595 
TRP HB2  H N N 596 
TRP HB3  H N N 597 
TRP HD1  H N N 598 
TRP HE1  H N N 599 
TRP HE3  H N N 600 
TRP HZ2  H N N 601 
TRP HZ3  H N N 602 
TRP HH2  H N N 603 
TRP HXT  H N N 604 
TYR N    N N N 605 
TYR CA   C N S 606 
TYR C    C N N 607 
TYR O    O N N 608 
TYR CB   C N N 609 
TYR CG   C Y N 610 
TYR CD1  C Y N 611 
TYR CD2  C Y N 612 
TYR CE1  C Y N 613 
TYR CE2  C Y N 614 
TYR CZ   C Y N 615 
TYR OH   O N N 616 
TYR OXT  O N N 617 
TYR H    H N N 618 
TYR H2   H N N 619 
TYR HA   H N N 620 
TYR HB2  H N N 621 
TYR HB3  H N N 622 
TYR HD1  H N N 623 
TYR HD2  H N N 624 
TYR HE1  H N N 625 
TYR HE2  H N N 626 
TYR HH   H N N 627 
TYR HXT  H N N 628 
VAL N    N N N 629 
VAL CA   C N S 630 
VAL C    C N N 631 
VAL O    O N N 632 
VAL CB   C N N 633 
VAL CG1  C N N 634 
VAL CG2  C N N 635 
VAL OXT  O N N 636 
VAL H    H N N 637 
VAL H2   H N N 638 
VAL HA   H N N 639 
VAL HB   H N N 640 
VAL HG11 H N N 641 
VAL HG12 H N N 642 
VAL HG13 H N N 643 
VAL HG21 H N N 644 
VAL HG22 H N N 645 
VAL HG23 H N N 646 
VAL HXT  H N N 647 
# 
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 
97N C   C1   sing N N 1   
97N C1  C2   sing N N 2   
97N C2  C3   sing N N 3   
97N C3  C4   sing N N 4   
97N C4  C5   sing N N 5   
97N C5  C6   sing N N 6   
97N C6  C7   doub N Z 7   
97N C7  C8   sing N N 8   
97N C8  C9   sing N N 9   
97N C9  C10  sing N N 10  
97N C10 C11  sing N N 11  
97N C11 C12  sing N N 12  
97N C12 C13  sing N N 13  
97N C13 C14  sing N N 14  
97N C14 C15  sing N N 15  
97N O   C15  doub N N 16  
97N C15 O1   sing N N 17  
97N O1  C16  sing N N 18  
97N O2  C17  sing N N 19  
97N C16 C17  sing N N 20  
97N C17 C18  sing N N 21  
97N C18 O3   sing N N 22  
97N C   H1   sing N N 23  
97N C   H2   sing N N 24  
97N C   H3   sing N N 25  
97N C1  H4   sing N N 26  
97N C1  H5   sing N N 27  
97N C2  H6   sing N N 28  
97N C2  H7   sing N N 29  
97N O2  H8   sing N N 30  
97N C3  H9   sing N N 31  
97N C3  H10  sing N N 32  
97N O3  H11  sing N N 33  
97N C4  H12  sing N N 34  
97N C4  H13  sing N N 35  
97N C5  H14  sing N N 36  
97N C5  H15  sing N N 37  
97N C6  H16  sing N N 38  
97N C7  H17  sing N N 39  
97N C8  H18  sing N N 40  
97N C8  H19  sing N N 41  
97N C9  H20  sing N N 42  
97N C9  H21  sing N N 43  
97N C10 H22  sing N N 44  
97N C10 H23  sing N N 45  
97N C11 H24  sing N N 46  
97N C11 H25  sing N N 47  
97N C12 H26  sing N N 48  
97N C12 H27  sing N N 49  
97N C13 H28  sing N N 50  
97N C13 H29  sing N N 51  
97N C14 H30  sing N N 52  
97N C14 H31  sing N N 53  
97N C16 H32  sing N N 54  
97N C16 H33  sing N N 55  
97N C17 H34  sing N N 56  
97N C18 H35  sing N N 57  
97N C18 H36  sing N N 58  
ALA N   CA   sing N N 59  
ALA N   H    sing N N 60  
ALA N   H2   sing N N 61  
ALA CA  C    sing N N 62  
ALA CA  CB   sing N N 63  
ALA CA  HA   sing N N 64  
ALA C   O    doub N N 65  
ALA C   OXT  sing N N 66  
ALA CB  HB1  sing N N 67  
ALA CB  HB2  sing N N 68  
ALA CB  HB3  sing N N 69  
ALA OXT HXT  sing N N 70  
ARG N   CA   sing N N 71  
ARG N   H    sing N N 72  
ARG N   H2   sing N N 73  
ARG CA  C    sing N N 74  
ARG CA  CB   sing N N 75  
ARG CA  HA   sing N N 76  
ARG C   O    doub N N 77  
ARG C   OXT  sing N N 78  
ARG CB  CG   sing N N 79  
ARG CB  HB2  sing N N 80  
ARG CB  HB3  sing N N 81  
ARG CG  CD   sing N N 82  
ARG CG  HG2  sing N N 83  
ARG CG  HG3  sing N N 84  
ARG CD  NE   sing N N 85  
ARG CD  HD2  sing N N 86  
ARG CD  HD3  sing N N 87  
ARG NE  CZ   sing N N 88  
ARG NE  HE   sing N N 89  
ARG CZ  NH1  sing N N 90  
ARG CZ  NH2  doub N N 91  
ARG NH1 HH11 sing N N 92  
ARG NH1 HH12 sing N N 93  
ARG NH2 HH21 sing N N 94  
ARG NH2 HH22 sing N N 95  
ARG OXT HXT  sing N N 96  
ASN N   CA   sing N N 97  
ASN N   H    sing N N 98  
ASN N   H2   sing N N 99  
ASN CA  C    sing N N 100 
ASN CA  CB   sing N N 101 
ASN CA  HA   sing N N 102 
ASN C   O    doub N N 103 
ASN C   OXT  sing N N 104 
ASN CB  CG   sing N N 105 
ASN CB  HB2  sing N N 106 
ASN CB  HB3  sing N N 107 
ASN CG  OD1  doub N N 108 
ASN CG  ND2  sing N N 109 
ASN ND2 HD21 sing N N 110 
ASN ND2 HD22 sing N N 111 
ASN OXT HXT  sing N N 112 
ASP N   CA   sing N N 113 
ASP N   H    sing N N 114 
ASP N   H2   sing N N 115 
ASP CA  C    sing N N 116 
ASP CA  CB   sing N N 117 
ASP CA  HA   sing N N 118 
ASP C   O    doub N N 119 
ASP C   OXT  sing N N 120 
ASP CB  CG   sing N N 121 
ASP CB  HB2  sing N N 122 
ASP CB  HB3  sing N N 123 
ASP CG  OD1  doub N N 124 
ASP CG  OD2  sing N N 125 
ASP OD2 HD2  sing N N 126 
ASP OXT HXT  sing N N 127 
CYS N   CA   sing N N 128 
CYS N   H    sing N N 129 
CYS N   H2   sing N N 130 
CYS CA  C    sing N N 131 
CYS CA  CB   sing N N 132 
CYS CA  HA   sing N N 133 
CYS C   O    doub N N 134 
CYS C   OXT  sing N N 135 
CYS CB  SG   sing N N 136 
CYS CB  HB2  sing N N 137 
CYS CB  HB3  sing N N 138 
CYS SG  HG   sing N N 139 
CYS OXT HXT  sing N N 140 
FME N   CN   sing N N 141 
FME N   CA   sing N N 142 
FME N   H    sing N N 143 
FME CN  O1   doub N N 144 
FME CN  HCN  sing N N 145 
FME CA  CB   sing N N 146 
FME CA  C    sing N N 147 
FME CA  HA   sing N N 148 
FME CB  CG   sing N N 149 
FME CB  HB2  sing N N 150 
FME CB  HB3  sing N N 151 
FME CG  SD   sing N N 152 
FME CG  HG2  sing N N 153 
FME CG  HG3  sing N N 154 
FME SD  CE   sing N N 155 
FME CE  HE1  sing N N 156 
FME CE  HE2  sing N N 157 
FME CE  HE3  sing N N 158 
FME C   O    doub N N 159 
FME C   OXT  sing N N 160 
FME OXT HXT  sing N N 161 
GLN N   CA   sing N N 162 
GLN N   H    sing N N 163 
GLN N   H2   sing N N 164 
GLN CA  C    sing N N 165 
GLN CA  CB   sing N N 166 
GLN CA  HA   sing N N 167 
GLN C   O    doub N N 168 
GLN C   OXT  sing N N 169 
GLN CB  CG   sing N N 170 
GLN CB  HB2  sing N N 171 
GLN CB  HB3  sing N N 172 
GLN CG  CD   sing N N 173 
GLN CG  HG2  sing N N 174 
GLN CG  HG3  sing N N 175 
GLN CD  OE1  doub N N 176 
GLN CD  NE2  sing N N 177 
GLN NE2 HE21 sing N N 178 
GLN NE2 HE22 sing N N 179 
GLN OXT HXT  sing N N 180 
GLU N   CA   sing N N 181 
GLU N   H    sing N N 182 
GLU N   H2   sing N N 183 
GLU CA  C    sing N N 184 
GLU CA  CB   sing N N 185 
GLU CA  HA   sing N N 186 
GLU C   O    doub N N 187 
GLU C   OXT  sing N N 188 
GLU CB  CG   sing N N 189 
GLU CB  HB2  sing N N 190 
GLU CB  HB3  sing N N 191 
GLU CG  CD   sing N N 192 
GLU CG  HG2  sing N N 193 
GLU CG  HG3  sing N N 194 
GLU CD  OE1  doub N N 195 
GLU CD  OE2  sing N N 196 
GLU OE2 HE2  sing N N 197 
GLU OXT HXT  sing N N 198 
GLY N   CA   sing N N 199 
GLY N   H    sing N N 200 
GLY N   H2   sing N N 201 
GLY CA  C    sing N N 202 
GLY CA  HA2  sing N N 203 
GLY CA  HA3  sing N N 204 
GLY C   O    doub N N 205 
GLY C   OXT  sing N N 206 
GLY OXT HXT  sing N N 207 
HIS N   CA   sing N N 208 
HIS N   H    sing N N 209 
HIS N   H2   sing N N 210 
HIS CA  C    sing N N 211 
HIS CA  CB   sing N N 212 
HIS CA  HA   sing N N 213 
HIS C   O    doub N N 214 
HIS C   OXT  sing N N 215 
HIS CB  CG   sing N N 216 
HIS CB  HB2  sing N N 217 
HIS CB  HB3  sing N N 218 
HIS CG  ND1  sing Y N 219 
HIS CG  CD2  doub Y N 220 
HIS ND1 CE1  doub Y N 221 
HIS ND1 HD1  sing N N 222 
HIS CD2 NE2  sing Y N 223 
HIS CD2 HD2  sing N N 224 
HIS CE1 NE2  sing Y N 225 
HIS CE1 HE1  sing N N 226 
HIS NE2 HE2  sing N N 227 
HIS OXT HXT  sing N N 228 
HOH O   H1   sing N N 229 
HOH O   H2   sing N N 230 
ILE N   CA   sing N N 231 
ILE N   H    sing N N 232 
ILE N   H2   sing N N 233 
ILE CA  C    sing N N 234 
ILE CA  CB   sing N N 235 
ILE CA  HA   sing N N 236 
ILE C   O    doub N N 237 
ILE C   OXT  sing N N 238 
ILE CB  CG1  sing N N 239 
ILE CB  CG2  sing N N 240 
ILE CB  HB   sing N N 241 
ILE CG1 CD1  sing N N 242 
ILE CG1 HG12 sing N N 243 
ILE CG1 HG13 sing N N 244 
ILE CG2 HG21 sing N N 245 
ILE CG2 HG22 sing N N 246 
ILE CG2 HG23 sing N N 247 
ILE CD1 HD11 sing N N 248 
ILE CD1 HD12 sing N N 249 
ILE CD1 HD13 sing N N 250 
ILE OXT HXT  sing N N 251 
LEU N   CA   sing N N 252 
LEU N   H    sing N N 253 
LEU N   H2   sing N N 254 
LEU CA  C    sing N N 255 
LEU CA  CB   sing N N 256 
LEU CA  HA   sing N N 257 
LEU C   O    doub N N 258 
LEU C   OXT  sing N N 259 
LEU CB  CG   sing N N 260 
LEU CB  HB2  sing N N 261 
LEU CB  HB3  sing N N 262 
LEU CG  CD1  sing N N 263 
LEU CG  CD2  sing N N 264 
LEU CG  HG   sing N N 265 
LEU CD1 HD11 sing N N 266 
LEU CD1 HD12 sing N N 267 
LEU CD1 HD13 sing N N 268 
LEU CD2 HD21 sing N N 269 
LEU CD2 HD22 sing N N 270 
LEU CD2 HD23 sing N N 271 
LEU OXT HXT  sing N N 272 
LFA C1  C2   sing N N 273 
LFA C1  H11  sing N N 274 
LFA C1  H12  sing N N 275 
LFA C1  H13  sing N N 276 
LFA C2  C3   sing N N 277 
LFA C2  H21  sing N N 278 
LFA C2  H22  sing N N 279 
LFA C3  C4   sing N N 280 
LFA C3  H31  sing N N 281 
LFA C3  H32  sing N N 282 
LFA C4  C5   sing N N 283 
LFA C4  H41  sing N N 284 
LFA C4  H42  sing N N 285 
LFA C5  C6   sing N N 286 
LFA C5  H51  sing N N 287 
LFA C5  H52  sing N N 288 
LFA C6  C7   sing N N 289 
LFA C6  H61  sing N N 290 
LFA C6  H62  sing N N 291 
LFA C7  C8   sing N N 292 
LFA C7  H71  sing N N 293 
LFA C7  H72  sing N N 294 
LFA C8  C9   sing N N 295 
LFA C8  H81  sing N N 296 
LFA C8  H82  sing N N 297 
LFA C9  C10  sing N N 298 
LFA C9  H91  sing N N 299 
LFA C9  H92  sing N N 300 
LFA C10 C11  sing N N 301 
LFA C10 H101 sing N N 302 
LFA C10 H102 sing N N 303 
LFA C11 C12  sing N N 304 
LFA C11 H111 sing N N 305 
LFA C11 H112 sing N N 306 
LFA C12 C13  sing N N 307 
LFA C12 H121 sing N N 308 
LFA C12 H122 sing N N 309 
LFA C13 C14  sing N N 310 
LFA C13 H131 sing N N 311 
LFA C13 H132 sing N N 312 
LFA C14 C15  sing N N 313 
LFA C14 H141 sing N N 314 
LFA C14 H142 sing N N 315 
LFA C15 C16  sing N N 316 
LFA C15 H151 sing N N 317 
LFA C15 H152 sing N N 318 
LFA C16 C17  sing N N 319 
LFA C16 H161 sing N N 320 
LFA C16 H162 sing N N 321 
LFA C17 C18  sing N N 322 
LFA C17 H171 sing N N 323 
LFA C17 H172 sing N N 324 
LFA C18 C19  sing N N 325 
LFA C18 H181 sing N N 326 
LFA C18 H182 sing N N 327 
LFA C19 C20  sing N N 328 
LFA C19 H191 sing N N 329 
LFA C19 H192 sing N N 330 
LFA C20 H201 sing N N 331 
LFA C20 H202 sing N N 332 
LFA C20 H203 sing N N 333 
LYS N   CA   sing N N 334 
LYS N   H    sing N N 335 
LYS N   H2   sing N N 336 
LYS CA  C    sing N N 337 
LYS CA  CB   sing N N 338 
LYS CA  HA   sing N N 339 
LYS C   O    doub N N 340 
LYS C   OXT  sing N N 341 
LYS CB  CG   sing N N 342 
LYS CB  HB2  sing N N 343 
LYS CB  HB3  sing N N 344 
LYS CG  CD   sing N N 345 
LYS CG  HG2  sing N N 346 
LYS CG  HG3  sing N N 347 
LYS CD  CE   sing N N 348 
LYS CD  HD2  sing N N 349 
LYS CD  HD3  sing N N 350 
LYS CE  NZ   sing N N 351 
LYS CE  HE2  sing N N 352 
LYS CE  HE3  sing N N 353 
LYS NZ  HZ1  sing N N 354 
LYS NZ  HZ2  sing N N 355 
LYS NZ  HZ3  sing N N 356 
LYS OXT HXT  sing N N 357 
MET N   CA   sing N N 358 
MET N   H    sing N N 359 
MET N   H2   sing N N 360 
MET CA  C    sing N N 361 
MET CA  CB   sing N N 362 
MET CA  HA   sing N N 363 
MET C   O    doub N N 364 
MET C   OXT  sing N N 365 
MET CB  CG   sing N N 366 
MET CB  HB2  sing N N 367 
MET CB  HB3  sing N N 368 
MET CG  SD   sing N N 369 
MET CG  HG2  sing N N 370 
MET CG  HG3  sing N N 371 
MET SD  CE   sing N N 372 
MET CE  HE1  sing N N 373 
MET CE  HE2  sing N N 374 
MET CE  HE3  sing N N 375 
MET OXT HXT  sing N N 376 
OLC C18 C17  sing N N 377 
OLC C10 C9   doub N N 378 
OLC C10 C11  sing N N 379 
OLC C9  C8   sing N N 380 
OLC C17 C16  sing N Z 381 
OLC C11 C12  sing N N 382 
OLC C8  C7   sing N N 383 
OLC C24 C22  sing N N 384 
OLC C24 O25  sing N N 385 
OLC C16 C15  sing N N 386 
OLC C12 C13  sing N N 387 
OLC C7  C6   sing N N 388 
OLC C15 C14  sing N N 389 
OLC C13 C14  sing N N 390 
OLC C6  C5   sing N N 391 
OLC C5  C4   sing N N 392 
OLC C4  C3   sing N N 393 
OLC C3  C2   sing N N 394 
OLC C2  C1   sing N N 395 
OLC C21 C22  sing N N 396 
OLC C21 O20  sing N N 397 
OLC C1  O19  doub N N 398 
OLC C1  O20  sing N N 399 
OLC C22 O23  sing N N 400 
OLC C18 H18  sing N N 401 
OLC C18 H18A sing N N 402 
OLC C18 H18B sing N N 403 
OLC C10 H10  sing N N 404 
OLC C9  H9   sing N N 405 
OLC C17 H17  sing N N 406 
OLC C17 H17A sing N N 407 
OLC C11 H11  sing N N 408 
OLC C11 H11A sing N N 409 
OLC C8  H8   sing N N 410 
OLC C8  H8A  sing N N 411 
OLC C24 H24  sing N N 412 
OLC C24 H24A sing N N 413 
OLC C16 H16  sing N N 414 
OLC C16 H16A sing N N 415 
OLC C12 H12  sing N N 416 
OLC C12 H12A sing N N 417 
OLC C7  H7   sing N N 418 
OLC C7  H7A  sing N N 419 
OLC C15 H15  sing N N 420 
OLC C15 H15A sing N N 421 
OLC C13 H13  sing N N 422 
OLC C13 H13A sing N N 423 
OLC C6  H6   sing N N 424 
OLC C6  H6A  sing N N 425 
OLC C14 H14  sing N N 426 
OLC C14 H14A sing N N 427 
OLC C5  H5   sing N N 428 
OLC C5  H5A  sing N N 429 
OLC C4  H4   sing N N 430 
OLC C4  H4A  sing N N 431 
OLC C3  H3   sing N N 432 
OLC C3  H3A  sing N N 433 
OLC C2  H2   sing N N 434 
OLC C2  H2A  sing N N 435 
OLC C21 H21  sing N N 436 
OLC C21 H21A sing N N 437 
OLC C22 H22  sing N N 438 
OLC O25 HO25 sing N N 439 
OLC O23 HO23 sing N N 440 
PHE N   CA   sing N N 441 
PHE N   H    sing N N 442 
PHE N   H2   sing N N 443 
PHE CA  C    sing N N 444 
PHE CA  CB   sing N N 445 
PHE CA  HA   sing N N 446 
PHE C   O    doub N N 447 
PHE C   OXT  sing N N 448 
PHE CB  CG   sing N N 449 
PHE CB  HB2  sing N N 450 
PHE CB  HB3  sing N N 451 
PHE CG  CD1  doub Y N 452 
PHE CG  CD2  sing Y N 453 
PHE CD1 CE1  sing Y N 454 
PHE CD1 HD1  sing N N 455 
PHE CD2 CE2  doub Y N 456 
PHE CD2 HD2  sing N N 457 
PHE CE1 CZ   doub Y N 458 
PHE CE1 HE1  sing N N 459 
PHE CE2 CZ   sing Y N 460 
PHE CE2 HE2  sing N N 461 
PHE CZ  HZ   sing N N 462 
PHE OXT HXT  sing N N 463 
PRO N   CA   sing N N 464 
PRO N   CD   sing N N 465 
PRO N   H    sing N N 466 
PRO CA  C    sing N N 467 
PRO CA  CB   sing N N 468 
PRO CA  HA   sing N N 469 
PRO C   O    doub N N 470 
PRO C   OXT  sing N N 471 
PRO CB  CG   sing N N 472 
PRO CB  HB2  sing N N 473 
PRO CB  HB3  sing N N 474 
PRO CG  CD   sing N N 475 
PRO CG  HG2  sing N N 476 
PRO CG  HG3  sing N N 477 
PRO CD  HD2  sing N N 478 
PRO CD  HD3  sing N N 479 
PRO OXT HXT  sing N N 480 
RET C1  C2   sing N N 481 
RET C1  C6   sing N N 482 
RET C1  C16  sing N N 483 
RET C1  C17  sing N N 484 
RET C2  C3   sing N N 485 
RET C2  H21  sing N N 486 
RET C2  H22  sing N N 487 
RET C3  C4   sing N N 488 
RET C3  H31  sing N N 489 
RET C3  H32  sing N N 490 
RET C4  C5   sing N N 491 
RET C4  H41  sing N N 492 
RET C4  H42  sing N N 493 
RET C5  C6   doub N N 494 
RET C5  C18  sing N N 495 
RET C6  C7   sing N N 496 
RET C7  C8   doub N E 497 
RET C7  H7   sing N N 498 
RET C8  C9   sing N N 499 
RET C8  H8   sing N N 500 
RET C9  C10  doub N E 501 
RET C9  C19  sing N N 502 
RET C10 C11  sing N N 503 
RET C10 H10  sing N N 504 
RET C11 C12  doub N E 505 
RET C11 H11  sing N N 506 
RET C12 C13  sing N N 507 
RET C12 H12  sing N N 508 
RET C13 C14  doub N E 509 
RET C13 C20  sing N N 510 
RET C14 C15  sing N N 511 
RET C14 H14  sing N N 512 
RET C15 O1   doub N N 513 
RET C15 H15  sing N N 514 
RET C16 H161 sing N N 515 
RET C16 H162 sing N N 516 
RET C16 H163 sing N N 517 
RET C17 H171 sing N N 518 
RET C17 H172 sing N N 519 
RET C17 H173 sing N N 520 
RET C18 H181 sing N N 521 
RET C18 H182 sing N N 522 
RET C18 H183 sing N N 523 
RET C19 H191 sing N N 524 
RET C19 H192 sing N N 525 
RET C19 H193 sing N N 526 
RET C20 H201 sing N N 527 
RET C20 H202 sing N N 528 
RET C20 H203 sing N N 529 
SER N   CA   sing N N 530 
SER N   H    sing N N 531 
SER N   H2   sing N N 532 
SER CA  C    sing N N 533 
SER CA  CB   sing N N 534 
SER CA  HA   sing N N 535 
SER C   O    doub N N 536 
SER C   OXT  sing N N 537 
SER CB  OG   sing N N 538 
SER CB  HB2  sing N N 539 
SER CB  HB3  sing N N 540 
SER OG  HG   sing N N 541 
SER OXT HXT  sing N N 542 
THR N   CA   sing N N 543 
THR N   H    sing N N 544 
THR N   H2   sing N N 545 
THR CA  C    sing N N 546 
THR CA  CB   sing N N 547 
THR CA  HA   sing N N 548 
THR C   O    doub N N 549 
THR C   OXT  sing N N 550 
THR CB  OG1  sing N N 551 
THR CB  CG2  sing N N 552 
THR CB  HB   sing N N 553 
THR OG1 HG1  sing N N 554 
THR CG2 HG21 sing N N 555 
THR CG2 HG22 sing N N 556 
THR CG2 HG23 sing N N 557 
THR OXT HXT  sing N N 558 
TRP N   CA   sing N N 559 
TRP N   H    sing N N 560 
TRP N   H2   sing N N 561 
TRP CA  C    sing N N 562 
TRP CA  CB   sing N N 563 
TRP CA  HA   sing N N 564 
TRP C   O    doub N N 565 
TRP C   OXT  sing N N 566 
TRP CB  CG   sing N N 567 
TRP CB  HB2  sing N N 568 
TRP CB  HB3  sing N N 569 
TRP CG  CD1  doub Y N 570 
TRP CG  CD2  sing Y N 571 
TRP CD1 NE1  sing Y N 572 
TRP CD1 HD1  sing N N 573 
TRP CD2 CE2  doub Y N 574 
TRP CD2 CE3  sing Y N 575 
TRP NE1 CE2  sing Y N 576 
TRP NE1 HE1  sing N N 577 
TRP CE2 CZ2  sing Y N 578 
TRP CE3 CZ3  doub Y N 579 
TRP CE3 HE3  sing N N 580 
TRP CZ2 CH2  doub Y N 581 
TRP CZ2 HZ2  sing N N 582 
TRP CZ3 CH2  sing Y N 583 
TRP CZ3 HZ3  sing N N 584 
TRP CH2 HH2  sing N N 585 
TRP OXT HXT  sing N N 586 
TYR N   CA   sing N N 587 
TYR N   H    sing N N 588 
TYR N   H2   sing N N 589 
TYR CA  C    sing N N 590 
TYR CA  CB   sing N N 591 
TYR CA  HA   sing N N 592 
TYR C   O    doub N N 593 
TYR C   OXT  sing N N 594 
TYR CB  CG   sing N N 595 
TYR CB  HB2  sing N N 596 
TYR CB  HB3  sing N N 597 
TYR CG  CD1  doub Y N 598 
TYR CG  CD2  sing Y N 599 
TYR CD1 CE1  sing Y N 600 
TYR CD1 HD1  sing N N 601 
TYR CD2 CE2  doub Y N 602 
TYR CD2 HD2  sing N N 603 
TYR CE1 CZ   doub Y N 604 
TYR CE1 HE1  sing N N 605 
TYR CE2 CZ   sing Y N 606 
TYR CE2 HE2  sing N N 607 
TYR CZ  OH   sing N N 608 
TYR OH  HH   sing N N 609 
TYR OXT HXT  sing N N 610 
VAL N   CA   sing N N 611 
VAL N   H    sing N N 612 
VAL N   H2   sing N N 613 
VAL CA  C    sing N N 614 
VAL CA  CB   sing N N 615 
VAL CA  HA   sing N N 616 
VAL C   O    doub N N 617 
VAL C   OXT  sing N N 618 
VAL CB  CG1  sing N N 619 
VAL CB  CG2  sing N N 620 
VAL CB  HB   sing N N 621 
VAL CG1 HG11 sing N N 622 
VAL CG1 HG12 sing N N 623 
VAL CG1 HG13 sing N N 624 
VAL CG2 HG21 sing N N 625 
VAL CG2 HG22 sing N N 626 
VAL CG2 HG23 sing N N 627 
VAL OXT HXT  sing N N 628 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Agence Nationale de la Recherche (ANR)' France ANR-15-CE11-0029-02 1 
'Agence Nationale de la Recherche (ANR)' France ANR-19-CE11-0026    2 
'Agence Nationale de la Recherche (ANR)' France ANR-11-LABX-0015-01 3 
# 
_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   7AKY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9IN9 
_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]   0.021629 
_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]   0.008639 
_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]   0.018792 
_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.
;
? 
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.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 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.
;
? 
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 
HETATM 1    N N   . FME A  1 1   ? -2.64694  26.39471 -23.50654 1.000 43.31225  ?  1   FME A N   1 
HETATM 2    C CN  B FME A  1 1   ? -3.84001  26.30629 -22.83994 0.400 27.87590  ?  1   FME A CN  1 
HETATM 3    O O1  B FME A  1 1   ? -3.90564  26.23218 -21.61617 0.400 22.59936  ?  1   FME A O1  1 
HETATM 4    C CA  . FME A  1 1   ? -1.34691  26.40751 -22.88108 1.000 48.35252  ?  1   FME A CA  1 
HETATM 5    C CB  . FME A  1 1   ? -0.18894  26.63306 -23.88125 1.000 47.76157  ?  1   FME A CB  1 
HETATM 6    C CG  B FME A  1 1   ? 1.10560   26.93872 -23.16638 0.400 46.31879  ?  1   FME A CG  1 
HETATM 7    S SD  B FME A  1 1   ? 1.95155   25.40186 -22.93283 0.400 55.88606  ?  1   FME A SD  1 
HETATM 8    C CE  B FME A  1 1   ? 1.50970   24.95799 -21.30127 0.400 49.97276  ?  1   FME A CE  1 
HETATM 9    C C   . FME A  1 1   ? -1.24147  27.54309 -21.86709 1.000 48.30231  ?  1   FME A C   1 
HETATM 10   O O   . FME A  1 1   ? -0.79239  27.38128 -20.71538 1.000 39.60185  ?  1   FME A O   1 
ATOM   11   N N   A ASP A  1 2   ? -1.71731  28.70559 -22.31319 0.600 43.41533  ?  2   ASP A N   1 
ATOM   12   N N   B ASP A  1 2   ? -1.65963  28.72737 -22.30594 0.400 43.42537  ?  2   ASP A N   1 
ATOM   13   C CA  A ASP A  1 2   ? -1.69506  29.93412 -21.52945 0.600 40.66359  ?  2   ASP A CA  1 
ATOM   14   C CA  B ASP A  1 2   ? -1.55441  29.93416 -21.48973 0.400 40.50271  ?  2   ASP A CA  1 
ATOM   15   C C   A ASP A  1 2   ? -2.51625  29.80675 -20.23925 0.600 31.78535  ?  2   ASP A C   1 
ATOM   16   C C   B ASP A  1 2   ? -2.37356  29.83132 -20.19802 0.400 31.78407  ?  2   ASP A C   1 
ATOM   17   O O   A ASP A  1 2   ? -1.99621  30.04157 -19.14599 0.600 29.59909  ?  2   ASP A O   1 
ATOM   18   O O   B ASP A  1 2   ? -2.13144  30.56395 -19.23478 0.400 30.24095  ?  2   ASP A O   1 
ATOM   19   C CB  A ASP A  1 2   ? -2.18648  31.12223 -22.36802 0.600 46.36478  ?  2   ASP A CB  1 
ATOM   20   C CB  B ASP A  1 2   ? -1.97780  31.17024 -22.29136 0.400 46.27612  ?  2   ASP A CB  1 
ATOM   21   N N   A ASN A  1 3   ? -3.79012  29.41292 -20.36704 0.600 34.53674  ?  3   ASN A N   1 
ATOM   22   N N   B ASN A  1 3   ? -3.33934  28.91220 -20.17397 0.400 30.00009  ?  3   ASN A N   1 
ATOM   23   C CA  A ASN A  1 3   ? -4.64980  29.36511 -19.18797 0.600 32.80730  ?  3   ASN A CA  1 
ATOM   24   C CA  B ASN A  1 3   ? -4.19458  28.80044 -19.00018 0.400 42.59592  ?  3   ASN A CA  1 
ATOM   25   C C   A ASN A  1 3   ? -4.20846  28.28881 -18.20273 0.600 31.22781  ?  3   ASN A C   1 
ATOM   26   C C   B ASN A  1 3   ? -3.70008  27.75538 -18.00349 0.400 34.06687  ?  3   ASN A C   1 
ATOM   27   O O   A ASN A  1 3   ? -4.41708  28.44579 -16.99859 0.600 23.13105  ?  3   ASN A O   1 
ATOM   28   O O   B ASN A  1 3   ? -3.73429  28.00083 -16.79396 0.400 26.88113  ?  3   ASN A O   1 
ATOM   29   C CB  A ASN A  1 3   ? -6.11453  29.16288 -19.56879 0.600 33.83766  ?  3   ASN A CB  1 
ATOM   30   C CB  B ASN A  1 3   ? -5.64780  28.55667 -19.41078 0.400 34.81651  ?  3   ASN A CB  1 
ATOM   31   C CG  A ASN A  1 3   ? -6.76498  30.43319 -20.07196 0.600 35.83185  ?  3   ASN A CG  1 
ATOM   32   C CG  B ASN A  1 3   ? -6.28778  29.78286 -20.04029 0.400 48.75947  ?  3   ASN A CG  1 
ATOM   33   O OD1 A ASN A  1 3   ? -6.25486  31.53423 -19.85966 0.600 36.62003  ?  3   ASN A OD1 1 
ATOM   34   O OD1 B ASN A  1 3   ? -7.02111  29.67933 -21.02723 0.400 36.91448  ?  3   ASN A OD1 1 
ATOM   35   N ND2 A ASN A  1 3   ? -7.90135  30.28610 -20.73285 0.600 40.85505  ?  3   ASN A ND2 1 
ATOM   36   N ND2 B ASN A  1 3   ? -5.99888  30.95529 -19.47982 0.400 42.61059  ?  3   ASN A ND2 1 
ATOM   37   N N   A ILE A  1 4   ? -3.61498  27.18617 -18.67664 0.600 27.28007  ?  4   ILE A N   1 
ATOM   38   N N   B ILE A  1 4   ? -3.24328  26.58841 -18.47274 0.400 28.61656  ?  4   ILE A N   1 
ATOM   39   C CA  A ILE A  1 4   ? -3.03571  26.23413 -17.72750 0.600 22.12287  ?  4   ILE A CA  1 
ATOM   40   C CA  B ILE A  1 4   ? -2.53864  25.67551 -17.57498 0.400 23.30929  ?  4   ILE A CA  1 
ATOM   41   C C   A ILE A  1 4   ? -1.91916  26.89960 -16.93788 0.600 27.86292  ?  4   ILE A C   1 
ATOM   42   C C   B ILE A  1 4   ? -1.43043  26.41555 -16.84595 0.400 27.06629  ?  4   ILE A C   1 
ATOM   43   O O   A ILE A  1 4   ? -1.85071  26.78648 -15.71033 0.600 25.94795  ?  4   ILE A O   1 
ATOM   44   O O   B ILE A  1 4   ? -1.27602  26.29830 -15.62306 0.400 22.44642  ?  4   ILE A O   1 
ATOM   45   C CB  A ILE A  1 4   ? -2.53521  24.96088 -18.42584 0.600 27.48340  ?  4   ILE A CB  1 
ATOM   46   C CB  B ILE A  1 4   ? -1.97471  24.47542 -18.35590 0.400 23.91154  ?  4   ILE A CB  1 
ATOM   47   C CG1 A ILE A  1 4   ? -3.63503  24.33469 -19.27283 0.600 26.02214  ?  4   ILE A CG1 1 
ATOM   48   C CG1 B ILE A  1 4   ? -3.09258  23.51002 -18.73150 0.400 20.00906  ?  4   ILE A CG1 1 
ATOM   49   C CG2 A ILE A  1 4   ? -2.00566  23.98030 -17.35515 0.600 24.22754  ?  4   ILE A CG2 1 
ATOM   50   C CG2 B ILE A  1 4   ? -0.92304  23.77020 -17.51727 0.400 27.19355  ?  4   ILE A CG2 1 
ATOM   51   C CD1 A ILE A  1 4   ? -3.12252  23.17918 -20.12243 0.600 29.90921  ?  4   ILE A CD1 1 
ATOM   52   C CD1 B ILE A  1 4   ? -2.62447  22.31521 -19.53639 0.400 30.67661  ?  4   ILE A CD1 1 
ATOM   53   N N   A ILE A  1 5   ? -1.02547  27.61146 -17.63168 0.600 24.63949  ?  5   ILE A N   1 
ATOM   54   N N   B ILE A  1 5   ? -0.63729  27.18378 -17.59576 0.400 26.25242  ?  5   ILE A N   1 
ATOM   55   C CA  A ILE A  1 5   ? 0.11066   28.21718 -16.93751 0.600 29.33129  ?  5   ILE A CA  1 
ATOM   56   C CA  B ILE A  1 5   ? 0.40679   28.01654 -17.00488 0.400 25.90160  ?  5   ILE A CA  1 
ATOM   57   C C   A ILE A  1 5   ? -0.35318  29.33570 -16.00599 0.600 23.53078  ?  5   ILE A C   1 
ATOM   58   C C   B ILE A  1 5   ? -0.19534  28.99452 -16.00097 0.400 22.66883  ?  5   ILE A C   1 
ATOM   59   O O   A ILE A  1 5   ? 0.13526   29.45881 -14.87612 0.600 26.50526  ?  5   ILE A O   1 
ATOM   60   O O   B ILE A  1 5   ? 0.24992   29.07749 -14.85193 0.400 25.22738  ?  5   ILE A O   1 
ATOM   61   C CB  A ILE A  1 5   ? 1.20703   28.65541 -17.93152 0.600 31.23367  ?  5   ILE A CB  1 
ATOM   62   C CB  B ILE A  1 5   ? 1.20065   28.72910 -18.11860 0.400 29.97705  ?  5   ILE A CB  1 
ATOM   63   C CG1 A ILE A  1 5   ? 1.77853   27.42413 -18.63466 0.600 37.83525  ?  5   ILE A CG1 1 
ATOM   64   C CG1 B ILE A  1 5   ? 2.01819   27.70412 -18.90564 0.400 41.02932  ?  5   ILE A CG1 1 
ATOM   65   C CG2 A ILE A  1 5   ? 2.33421   29.35925 -17.21075 0.600 33.10228  ?  5   ILE A CG2 1 
ATOM   66   C CG2 B ILE A  1 5   ? 2.10213   29.79311 -17.55057 0.400 33.90335  ?  5   ILE A CG2 1 
ATOM   67   C CD1 A ILE A  1 5   ? 2.75532   27.73333 -19.75771 0.600 55.03002  ?  5   ILE A CD1 1 
ATOM   68   C CD1 B ILE A  1 5   ? 2.77169   28.28435 -20.08862 0.400 49.41656  ?  5   ILE A CD1 1 
ATOM   69   N N   A MET A  1 6   ? -1.31714  30.15411 -16.44872 0.600 25.82049  ?  6   MET A N   1 
ATOM   70   N N   B MET A  1 6   ? -1.22871  29.73727 -16.41763 0.400 26.81085  ?  6   MET A N   1 
ATOM   71   C CA  A MET A  1 6   ? -1.81519  31.20955 -15.57068 0.600 25.58072  ?  6   MET A CA  1 
ATOM   72   C CA  B MET A  1 6   ? -1.80902  30.76907 -15.55843 0.400 23.67478  ?  6   MET A CA  1 
ATOM   73   C C   A MET A  1 6   ? -2.42524  30.63264 -14.29613 0.600 27.43171  ?  6   MET A C   1 
ATOM   74   C C   B MET A  1 6   ? -2.33775  30.17770 -14.25457 0.400 30.33059  ?  6   MET A C   1 
ATOM   75   O O   A MET A  1 6   ? -2.25274  31.19305 -13.20395 0.600 22.29522  ?  6   MET A O   1 
ATOM   76   O O   B MET A  1 6   ? -1.91969  30.57164 -13.15404 0.400 22.99929  ?  6   MET A O   1 
ATOM   77   C CB  A MET A  1 6   ? -2.82787  32.10155 -16.29230 0.600 28.80808  ?  6   MET A CB  1 
ATOM   78   C CB  B MET A  1 6   ? -2.92460  31.51391 -16.30058 0.400 33.10508  ?  6   MET A CB  1 
ATOM   79   C CG  A MET A  1 6   ? -3.45467  33.15730 -15.35464 0.600 35.10600  ?  6   MET A CG  1 
ATOM   80   C CG  B MET A  1 6   ? -3.67753  32.50997 -15.41721 0.400 33.07146  ?  6   MET A CG  1 
ATOM   81   S SD  A MET A  1 6   ? -4.63447  34.24450 -16.18365 0.600 44.27039  ?  6   MET A SD  1 
ATOM   82   S SD  B MET A  1 6   ? -4.90801  33.52199 -16.28229 0.400 46.86431  ?  6   MET A SD  1 
ATOM   83   C CE  A MET A  1 6   ? -3.78564  34.53490 -17.72326 0.600 31.06578  ?  6   MET A CE  1 
ATOM   84   C CE  B MET A  1 6   ? -5.40181  34.60998 -14.95298 0.400 29.07726  ?  6   MET A CE  1 
ATOM   85   N N   A THR A  1 7   ? -3.14840  29.51117 -14.40906 0.600 23.83323  ?  7   THR A N   1 
ATOM   86   N N   B THR A  1 7   ? -3.26183  29.21456 -14.36050 0.400 24.55672  ?  7   THR A N   1 
ATOM   87   C CA  A THR A  1 7   ? -3.68197  28.89407 -13.19500 0.600 23.92445  ?  7   THR A CA  1 
ATOM   88   C CA  B THR A  1 7   ? -3.80510  28.58758 -13.15853 0.400 22.47692  ?  7   THR A CA  1 
ATOM   89   C C   A THR A  1 7   ? -2.57993  28.27046 -12.33159 0.600 20.66379  ?  7   THR A C   1 
ATOM   90   C C   B THR A  1 7   ? -2.70496  27.94872 -12.33029 0.400 22.31194  ?  7   THR A C   1 
ATOM   91   O O   A THR A  1 7   ? -2.65184  28.34732 -11.09303 0.600 21.37225  ?  7   THR A O   1 
ATOM   92   O O   B THR A  1 7   ? -2.88813  27.70940 -11.13076 0.400 21.15592  ?  7   THR A O   1 
ATOM   93   C CB  A THR A  1 7   ? -4.82351  27.90793 -13.49924 0.600 22.76453  ?  7   THR A CB  1 
ATOM   94   C CB  B THR A  1 7   ? -4.83528  27.52448 -13.51907 0.400 24.06613  ?  7   THR A CB  1 
ATOM   95   O OG1 A THR A  1 7   ? -4.42619  26.96709 -14.51067 0.600 21.37502  ?  7   THR A OG1 1 
ATOM   96   O OG1 B THR A  1 7   ? -4.15550  26.38591 -14.05494 0.400 19.29288  ?  7   THR A OG1 1 
ATOM   97   C CG2 A THR A  1 7   ? -6.11238  28.64984 -13.94106 0.600 20.54723  ?  7   THR A CG2 1 
ATOM   98   C CG2 B THR A  1 7   ? -5.82985  28.06651 -14.54183 0.400 26.62456  ?  7   THR A CG2 1 
ATOM   99   N N   . ALA A  1 8   ? -1.56308  27.65177 -12.95600 1.000 25.20984  ?  8   ALA A N   1 
ATOM   100  C CA  . ALA A  1 8   ? -0.43008  27.15003 -12.19221 1.000 27.06049  ?  8   ALA A CA  1 
ATOM   101  C C   . ALA A  1 8   ? 0.22196   28.27879 -11.41211 1.000 20.85535  ?  8   ALA A C   1 
ATOM   102  O O   . ALA A  1 8   ? 0.53541   28.10894 -10.23226 1.000 21.65271  ?  8   ALA A O   1 
ATOM   103  C CB  . ALA A  1 8   ? 0.58041   26.42460 -13.08791 1.000 22.92190  ?  8   ALA A CB  1 
ATOM   104  N N   . TYR A  1 9   ? 0.38240   29.45193 -12.03917 1.000 22.69662  ?  9   TYR A N   1 
ATOM   105  C CA  . TYR A  1 9   ? 0.92761   30.59780 -11.31771 1.000 26.42207  ?  9   TYR A CA  1 
ATOM   106  C C   . TYR A  1 9   ? 0.05570   31.00010 -10.13583 1.000 24.22708  ?  9   TYR A C   1 
ATOM   107  O O   . TYR A  1 9   ? 0.57675   31.28772 -9.04824  1.000 26.06916  ?  9   TYR A O   1 
ATOM   108  C CB  . TYR A  1 9   ? 1.09739   31.77302 -12.25796 1.000 28.44374  ?  9   TYR A CB  1 
ATOM   109  C CG  . TYR A  1 9   ? 2.25730   31.62770 -13.22338 1.000 34.19529  ?  9   TYR A CG  1 
ATOM   110  C CD1 . TYR A  1 9   ? 3.46206   31.05188 -12.82119 1.000 29.63936  ?  9   TYR A CD1 1 
ATOM   111  C CD2 . TYR A  1 9   ? 2.15889   32.10986 -14.51015 1.000 34.96343  ?  9   TYR A CD2 1 
ATOM   112  C CE1 . TYR A  1 9   ? 4.53256   30.93493 -13.70482 1.000 38.54509  ?  9   TYR A CE1 1 
ATOM   113  C CE2 . TYR A  1 9   ? 3.21492   31.99734 -15.39380 1.000 43.93841  ?  9   TYR A CE2 1 
ATOM   114  C CZ  . TYR A  1 9   ? 4.40351   31.40679 -14.98704 1.000 37.22520  ?  9   TYR A CZ  1 
ATOM   115  O OH  . TYR A  1 9   ? 5.46567   31.30869 -15.86320 1.000 44.11535  ?  9   TYR A OH  1 
ATOM   116  N N   . ILE A  1 10  ? -1.27248  31.06054 -10.33533 1.000 25.60842  ?  10  ILE A N   1 
ATOM   117  C CA  . ILE A  1 10  ? -2.15634  31.42569 -9.23276  1.000 23.92431  ?  10  ILE A CA  1 
ATOM   118  C C   . ILE A  1 10  ? -1.99706  30.42740 -8.09700  1.000 25.76848  ?  10  ILE A C   1 
ATOM   119  O O   . ILE A  1 10  ? -1.86544  30.80722 -6.92426  1.000 25.09599  ?  10  ILE A O   1 
ATOM   120  C CB  . ILE A  1 10  ? -3.61901  31.50171 -9.71509  1.000 29.64082  ?  10  ILE A CB  1 
ATOM   121  C CG1 . ILE A  1 10  ? -3.79611  32.64181 -10.72093 1.000 27.68788  ?  10  ILE A CG1 1 
ATOM   122  C CG2 . ILE A  1 10  ? -4.58363  31.66138 -8.52556  1.000 24.63223  ?  10  ILE A CG2 1 
ATOM   123  C CD1 . ILE A  1 10  ? -5.05603  32.48922 -11.53339 1.000 30.13484  ?  10  ILE A CD1 1 
ATOM   124  N N   . SER A  1 11  ? -1.94894  29.13248 -8.43870  1.000 24.23549  ?  11  SER A N   1 
ATOM   125  C CA  . SER A  1 11  ? -1.78159  28.08609 -7.43217  1.000 24.46624  ?  11  SER A CA  1 
ATOM   126  C C   . SER A  1 11  ? -0.46235  28.24475 -6.69057  1.000 20.81176  ?  11  SER A C   1 
ATOM   127  O O   . SER A  1 11  ? -0.41517  28.14538 -5.46318  1.000 22.73063  ?  11  SER A O   1 
ATOM   128  C CB  . SER A  1 11  ? -1.85626  26.71875 -8.10425  1.000 21.49918  ?  11  SER A CB  1 
ATOM   129  O OG  . SER A  1 11  ? -1.90391  25.68032 -7.14567  1.000 22.25132  ?  11  SER A OG  1 
ATOM   130  N N   . ILE A  1 12  ? 0.62186   28.48898 -7.43194  1.000 23.85916  ?  12  ILE A N   1 
ATOM   131  C CA  . ILE A  1 12  ? 1.93764   28.67884 -6.82760  1.000 26.21643  ?  12  ILE A CA  1 
ATOM   132  C C   . ILE A  1 12  ? 1.93788   29.88956 -5.89817  1.000 22.46811  ?  12  ILE A C   1 
ATOM   133  O O   . ILE A  1 12  ? 2.54160   29.85788 -4.81446  1.000 23.50220  ?  12  ILE A O   1 
ATOM   134  C CB  . ILE A  1 12  ? 2.98464   28.83443 -7.94494  1.000 23.70648  ?  12  ILE A CB  1 
ATOM   135  C CG1 . ILE A  1 12  ? 3.28756   27.49460 -8.59380  1.000 24.96909  ?  12  ILE A CG1 1 
ATOM   136  C CG2 . ILE A  1 12  ? 4.27295   29.50930 -7.41472  1.000 31.38155  ?  12  ILE A CG2 1 
ATOM   137  C CD1 . ILE A  1 12  ? 4.12918   27.68359 -9.87577  1.000 27.62496  ?  12  ILE A CD1 1 
ATOM   138  N N   . PHE A  1 13  ? 1.25999   30.97320 -6.30643  1.000 23.48668  ?  13  PHE A N   1 
ATOM   139  C CA  . PHE A  1 13  ? 1.16913   32.17379 -5.47455  1.000 25.15798  ?  13  PHE A CA  1 
ATOM   140  C C   . PHE A  1 13  ? 0.55619   31.83885 -4.11553  1.000 24.00392  ?  13  PHE A C   1 
ATOM   141  O O   . PHE A  1 13  ? 1.15341   32.11541 -3.06410  1.000 27.31501  ?  13  PHE A O   1 
ATOM   142  C CB  . PHE A  1 13  ? 0.36143   33.22875 -6.24196  1.000 26.26513  ?  13  PHE A CB  1 
ATOM   143  C CG  . PHE A  1 13  ? 0.20388   34.54474 -5.52286  1.000 27.12863  ?  13  PHE A CG  1 
ATOM   144  C CD1 . PHE A  1 13  ? -0.81453  34.72411 -4.58975  1.000 26.86327  ?  13  PHE A CD1 1 
ATOM   145  C CD2 . PHE A  1 13  ? 1.01075   35.61776 -5.84330  1.000 28.86110  ?  13  PHE A CD2 1 
ATOM   146  C CE1 . PHE A  1 13  ? -0.98878  35.93952 -3.96086  1.000 30.00356  ?  13  PHE A CE1 1 
ATOM   147  C CE2 . PHE A  1 13  ? 0.84638   36.86963 -5.19444  1.000 31.25488  ?  13  PHE A CE2 1 
ATOM   148  C CZ  . PHE A  1 13  ? -0.16033  37.01077 -4.25435  1.000 31.50545  ?  13  PHE A CZ  1 
ATOM   149  N N   . VAL A  1 14  ? -0.60705  31.19018 -4.11559  1.000 25.26176  ?  14  VAL A N   1 
ATOM   150  C CA  . VAL A  1 14  ? -1.23032  30.79226 -2.85457  1.000 24.36777  ?  14  VAL A CA  1 
ATOM   151  C C   . VAL A  1 14  ? -0.33693  29.81559 -2.08364  1.000 22.84880  ?  14  VAL A C   1 
ATOM   152  O O   . VAL A  1 14  ? -0.17498  29.93091 -0.85761  1.000 24.92377  ?  14  VAL A O   1 
ATOM   153  C CB  . VAL A  1 14  ? -2.65296  30.26152 -3.10034  1.000 22.92981  ?  14  VAL A CB  1 
ATOM   154  C CG1 . VAL A  1 14  ? -3.30041  29.91022 -1.75070  1.000 24.71527  ?  14  VAL A CG1 1 
ATOM   155  C CG2 . VAL A  1 14  ? -3.45997  31.31110 -3.84009  1.000 21.69767  ?  14  VAL A CG2 1 
ATOM   156  N N   . GLN A  1 15  ? 0.32839   28.89406 -2.78164  1.000 22.01164  ?  15  GLN A N   1 
ATOM   157  C CA  . GLN A  1 15  ? 1.20385   27.96030 -2.07494  1.000 26.06257  ?  15  GLN A CA  1 
ATOM   158  C C   . GLN A  1 15  ? 2.32106   28.68487 -1.32621  1.000 26.49618  ?  15  GLN A C   1 
ATOM   159  O O   . GLN A  1 15  ? 2.62092   28.35838 -0.17064  1.000 25.60735  ?  15  GLN A O   1 
ATOM   160  C CB  . GLN A  1 15  ? 1.82705   26.99840 -3.06466  1.000 23.61408  ?  15  GLN A CB  1 
ATOM   161  C CG  . GLN A  1 15  ? 0.88007   25.91282 -3.57773  1.000 21.57429  ?  15  GLN A CG  1 
ATOM   162  C CD  . GLN A  1 15  ? 1.52348   25.13189 -4.68155  1.000 27.73585  ?  15  GLN A CD  1 
ATOM   163  O OE1 . GLN A  1 15  ? 2.61537   24.58175 -4.49741  1.000 25.64335  ?  15  GLN A OE1 1 
ATOM   164  N NE2 . GLN A  1 15  ? 0.89610   25.10030 -5.84020  1.000 25.61217  ?  15  GLN A NE2 1 
ATOM   165  N N   A ILE A  1 16  ? 2.94095   29.68618 -1.94083  0.600 25.49432  ?  16  ILE A N   1 
ATOM   166  N N   B ILE A  1 16  ? 2.97416   29.64459 -2.00803  0.400 25.56112  ?  16  ILE A N   1 
ATOM   167  C CA  A ILE A  1 16  ? 4.06939   30.31242 -1.26055  0.600 26.29974  ?  16  ILE A CA  1 
ATOM   168  C CA  B ILE A  1 16  ? 4.03995   30.45993 -1.41503  0.400 24.77136  ?  16  ILE A CA  1 
ATOM   169  C C   A ILE A  1 16  ? 3.60558   31.09683 -0.03284  0.600 24.19189  ?  16  ILE A C   1 
ATOM   170  C C   B ILE A  1 16  ? 3.57269   31.04326 -0.09026  0.400 24.14770  ?  16  ILE A C   1 
ATOM   171  O O   A ILE A  1 16  ? 4.24633   31.06146 1.02678   0.600 28.04691  ?  16  ILE A O   1 
ATOM   172  O O   B ILE A  1 16  ? 4.17349   30.82156 0.96763   0.400 28.99378  ?  16  ILE A O   1 
ATOM   173  C CB  A ILE A  1 16  ? 4.90230   31.14937 -2.23495  0.600 22.32443  ?  16  ILE A CB  1 
ATOM   174  C CB  B ILE A  1 16  ? 4.45981   31.58768 -2.37718  0.400 29.53048  ?  16  ILE A CB  1 
ATOM   175  C CG1 A ILE A  1 16  ? 5.65176   30.23341 -3.21400  0.600 20.93441  ?  16  ILE A CG1 1 
ATOM   176  C CG1 B ILE A  1 16  ? 5.25932   31.06047 -3.56210  0.400 27.04095  ?  16  ILE A CG1 1 
ATOM   177  C CG2 A ILE A  1 16  ? 5.85603   32.04917 -1.44462  0.600 22.77345  ?  16  ILE A CG2 1 
ATOM   178  C CG2 B ILE A  1 16  ? 5.24986   32.66460 -1.63387  0.400 28.40707  ?  16  ILE A CG2 1 
ATOM   179  C CD1 A ILE A  1 16  ? 6.11524   30.95371 -4.47404  0.600 33.43044  ?  16  ILE A CD1 1 
ATOM   180  C CD1 B ILE A  1 16  ? 5.92862   32.14530 -4.35373  0.400 26.79504  ?  16  ILE A CD1 1 
ATOM   181  N N   . ILE A  1 17  ? 2.47631   31.79428 -0.14041  1.000 25.73962  ?  17  ILE A N   1 
ATOM   182  C CA  A ILE A  1 17  ? 1.97263   32.53159 1.01710   0.600 30.74030  ?  17  ILE A CA  1 
ATOM   183  C CA  B ILE A  1 17  ? 2.01732   32.52697 1.02952   0.400 30.68974  ?  17  ILE A CA  1 
ATOM   184  C C   . ILE A  1 17  ? 1.57616   31.57406 2.13117   1.000 27.46570  ?  17  ILE A C   1 
ATOM   185  O O   . ILE A  1 17  ? 1.86415   31.80581 3.31311   1.000 28.32404  ?  17  ILE A O   1 
ATOM   186  C CB  A ILE A  1 17  ? 0.81317   33.44784 0.58780   0.600 36.33385  ?  17  ILE A CB  1 
ATOM   187  C CB  B ILE A  1 17  ? 0.93528   33.54511 0.62524   0.400 36.23105  ?  17  ILE A CB  1 
ATOM   188  C CG1 A ILE A  1 17  ? 1.32775   34.51969 -0.36698  0.600 39.45740  ?  17  ILE A CG1 1 
ATOM   189  C CG1 B ILE A  1 17  ? 1.39735   34.31352 -0.61479  0.400 37.06790  ?  17  ILE A CG1 1 
ATOM   190  C CG2 A ILE A  1 17  ? 0.13191   34.07413 1.80025   0.600 34.66733  ?  17  ILE A CG2 1 
ATOM   191  C CG2 B ILE A  1 17  ? 0.65372   34.51681 1.75911   0.400 33.57804  ?  17  ILE A CG2 1 
ATOM   192  C CD1 A ILE A  1 17  ? 0.22621   35.33739 -0.97034  0.600 41.58099  ?  17  ILE A CD1 1 
ATOM   193  C CD1 B ILE A  1 17  ? 2.69494   35.09153 -0.42131  0.400 30.13206  ?  17  ILE A CD1 1 
ATOM   194  N N   A THR A  1 18  ? 0.91292   30.47131 1.76514   0.600 27.69785  ?  18  THR A N   1 
ATOM   195  N N   B THR A  1 18  ? 0.92755   30.45704 1.78156   0.400 27.69207  ?  18  THR A N   1 
ATOM   196  C CA  A THR A  1 18  ? 0.48515   29.46830 2.72911   0.600 27.13531  ?  18  THR A CA  1 
ATOM   197  C CA  B THR A  1 18  ? 0.49591   29.52058 2.81654   0.400 27.15616  ?  18  THR A CA  1 
ATOM   198  C C   A THR A  1 18  ? 1.67836   28.81554 3.41033   0.600 25.24624  ?  18  THR A C   1 
ATOM   199  C C   B THR A  1 18  ? 1.66363   28.74027 3.41075   0.400 25.27650  ?  18  THR A C   1 
ATOM   200  O O   A THR A  1 18  ? 1.64347   28.55379 4.61808   0.600 29.01602  ?  18  THR A O   1 
ATOM   201  O O   B THR A  1 18  ? 1.58248   28.28561 4.55781   0.400 27.78364  ?  18  THR A O   1 
ATOM   202  C CB  A THR A  1 18  ? -0.35966  28.41684 2.01034   0.600 27.13617  ?  18  THR A CB  1 
ATOM   203  C CB  B THR A  1 18  ? -0.56819  28.56463 2.27936   0.400 30.31136  ?  18  THR A CB  1 
ATOM   204  O OG1 A THR A  1 18  ? -1.46677  29.05653 1.35354   0.600 25.90799  ?  18  THR A OG1 1 
ATOM   205  O OG1 B THR A  1 18  ? -0.11520  27.96930 1.05769   0.400 25.68193  ?  18  THR A OG1 1 
ATOM   206  C CG2 A THR A  1 18  ? -0.90280  27.39735 2.99650   0.600 27.68988  ?  18  THR A CG2 1 
ATOM   207  C CG2 B THR A  1 18  ? -1.87450  29.30102 2.03491   0.400 22.94747  ?  18  THR A CG2 1 
ATOM   208  N N   . ALA A  1 19  ? 2.74489   28.55068 2.65496   1.000 24.71598  ?  19  ALA A N   1 
ATOM   209  C CA  . ALA A  1 19  ? 3.91567   27.92747 3.25290   1.000 25.09588  ?  19  ALA A CA  1 
ATOM   210  C C   . ALA A  1 19  ? 4.52564   28.84559 4.30998   1.000 27.03113  ?  19  ALA A C   1 
ATOM   211  O O   . ALA A  1 19  ? 4.87595   28.39744 5.40605   1.000 28.17891  ?  19  ALA A O   1 
ATOM   212  C CB  . ALA A  1 19  ? 4.94335   27.59766 2.18021   1.000 28.16716  ?  19  ALA A CB  1 
ATOM   213  N N   . ILE A  1 20  ? 4.64350   30.13836 3.99890   1.000 25.44939  ?  20  ILE A N   1 
ATOM   214  C CA  . ILE A  1 20  ? 5.18613   31.09575 4.96490   1.000 30.61088  ?  20  ILE A CA  1 
ATOM   215  C C   . ILE A  1 20  ? 4.34949   31.08710 6.23305   1.000 31.78625  ?  20  ILE A C   1 
ATOM   216  O O   . ILE A  1 20  ? 4.87608   30.95570 7.34511   1.000 28.38982  ?  20  ILE A O   1 
ATOM   217  C CB  . ILE A  1 20  ? 5.28003   32.49859 4.34645   1.000 26.34575  ?  20  ILE A CB  1 
ATOM   218  C CG1 . ILE A  1 20  ? 6.34141   32.50812 3.24145   1.000 26.19978  ?  20  ILE A CG1 1 
ATOM   219  C CG2 . ILE A  1 20  ? 5.59684   33.53758 5.45175   1.000 29.09253  ?  20  ILE A CG2 1 
ATOM   220  C CD1 . ILE A  1 20  ? 6.28530   33.72792 2.34877   1.000 34.32511  ?  20  ILE A CD1 1 
ATOM   221  N N   . ILE A  1 21  ? 3.02969   31.18575 6.07856   1.000 26.97267  ?  21  ILE A N   1 
ATOM   222  C CA  . ILE A  1 21  ? 2.11614   31.19896 7.22375   1.000 32.56464  ?  21  ILE A CA  1 
ATOM   223  C C   . ILE A  1 21  ? 2.26155   29.92836 8.05810   1.000 33.00511  ?  21  ILE A C   1 
ATOM   224  O O   . ILE A  1 21  ? 2.30038   29.97404 9.29724   1.000 28.99062  ?  21  ILE A O   1 
ATOM   225  C CB  . ILE A  1 21  ? 0.68020   31.38875 6.69975   1.000 32.61266  ?  21  ILE A CB  1 
ATOM   226  C CG1 . ILE A  1 21  ? 0.48871   32.83307 6.22119   1.000 31.28750  ?  21  ILE A CG1 1 
ATOM   227  C CG2 . ILE A  1 21  ? -0.34732  31.03361 7.73932   1.000 35.72857  ?  21  ILE A CG2 1 
ATOM   228  C CD1 . ILE A  1 21  ? -0.64723  32.96853 5.23984   1.000 34.37353  ?  21  ILE A CD1 1 
ATOM   229  N N   . SER A  1 22  ? 2.33994   28.77640 7.39327   1.000 29.57174  ?  22  SER A N   1 
ATOM   230  C CA  . SER A  1 22  ? 2.44399   27.51609 8.11401   1.000 30.86445  ?  22  SER A CA  1 
ATOM   231  C C   . SER A  1 22  ? 3.73739   27.44659 8.90847   1.000 27.53708  ?  22  SER A C   1 
ATOM   232  O O   . SER A  1 22  ? 3.74617   26.94461 10.03588  1.000 27.16810  ?  22  SER A O   1 
ATOM   233  C CB  . SER A  1 22  ? 2.34018   26.35220 7.13879   1.000 34.26615  ?  22  SER A CB  1 
ATOM   234  O OG  . SER A  1 22  ? 1.05987   26.35127 6.53518   1.000 35.82094  ?  22  SER A OG  1 
ATOM   235  N N   . VAL A  1 23  ? 4.84281   27.90932 8.32101   1.000 25.36617  ?  23  VAL A N   1 
ATOM   236  C CA  . VAL A  1 23  ? 6.11164   27.88875 9.04045   1.000 27.60240  ?  23  VAL A CA  1 
ATOM   237  C C   . VAL A  1 23  ? 6.00635   28.68807 10.33677  1.000 26.65098  ?  23  VAL A C   1 
ATOM   238  O O   . VAL A  1 23  ? 6.40785   28.21048 11.40678  1.000 27.53363  ?  23  VAL A O   1 
ATOM   239  C CB  . VAL A  1 23  ? 7.26613   28.33677 8.13042   1.000 26.79396  ?  23  VAL A CB  1 
ATOM   240  C CG1 . VAL A  1 23  ? 8.52233   28.51879 8.91197   1.000 28.86075  ?  23  VAL A CG1 1 
ATOM   241  C CG2 . VAL A  1 23  ? 7.50832   27.27234 7.04423   1.000 28.47862  ?  23  VAL A CG2 1 
ATOM   242  N N   . TYR A  1 24  ? 5.45568   29.91469 10.26981  1.000 22.22360  ?  24  TYR A N   1 
ATOM   243  C CA  . TYR A  1 24  ? 5.29680   30.69772 11.49892  1.000 23.56135  ?  24  TYR A CA  1 
ATOM   244  C C   . TYR A  1 24  ? 4.38758   29.98641 12.49160  1.000 22.50328  ?  24  TYR A C   1 
ATOM   245  O O   . TYR A  1 24  ? 4.62656   30.04164 13.71734  1.000 24.91798  ?  24  TYR A O   1 
ATOM   246  C CB  . TYR A  1 24  ? 4.77077   32.10712 11.19340  1.000 27.64442  ?  24  TYR A CB  1 
ATOM   247  C CG  . TYR A  1 24  ? 5.83154   33.08388 10.75284  1.000 25.27205  ?  24  TYR A CG  1 
ATOM   248  C CD1 . TYR A  1 24  ? 6.20268   33.16411 9.41209   1.000 22.21383  ?  24  TYR A CD1 1 
ATOM   249  C CD2 . TYR A  1 24  ? 6.46507   33.92269 11.66292  1.000 27.01368  ?  24  TYR A CD2 1 
ATOM   250  C CE1 . TYR A  1 24  ? 7.15835   34.02182 8.99417   1.000 26.78101  ?  24  TYR A CE1 1 
ATOM   251  C CE2 . TYR A  1 24  ? 7.43370   34.81953 11.24169  1.000 24.05070  ?  24  TYR A CE2 1 
ATOM   252  C CZ  . TYR A  1 24  ? 7.78009   34.85043 9.88788   1.000 25.77050  ?  24  TYR A CZ  1 
ATOM   253  O OH  . TYR A  1 24  ? 8.74704   35.73312 9.45883   1.000 24.73465  ?  24  TYR A OH  1 
ATOM   254  N N   . GLY A  1 25  ? 3.35670   29.30227 11.98166  1.000 24.10222  ?  25  GLY A N   1 
ATOM   255  C CA  . GLY A  1 25  ? 2.43921   28.55591 12.82669  1.000 26.69259  ?  25  GLY A CA  1 
ATOM   256  C C   . GLY A  1 25  ? 3.11930   27.48233 13.66057  1.000 24.02387  ?  25  GLY A C   1 
ATOM   257  O O   . GLY A  1 25  ? 2.67717   27.18845 14.77578  1.000 27.14383  ?  25  GLY A O   1 
ATOM   258  N N   A LEU A  1 26  ? 4.23169   26.92451 13.16386  0.600 25.70623  ?  26  LEU A N   1 
ATOM   259  N N   B LEU A  1 26  ? 4.17333   26.86176 13.11648  0.400 25.99875  ?  26  LEU A N   1 
ATOM   260  C CA  A LEU A  1 26  ? 4.97759   25.93304 13.93642  0.600 26.47219  ?  26  LEU A CA  1 
ATOM   261  C CA  B LEU A  1 26  ? 4.91115   25.76958 13.74631  0.400 25.37967  ?  26  LEU A CA  1 
ATOM   262  C C   A LEU A  1 26  ? 5.48560   26.50379 15.24834  0.600 25.43277  ?  26  LEU A C   1 
ATOM   263  C C   B LEU A  1 26  ? 5.66685   26.19545 14.99003  0.400 29.70481  ?  26  LEU A C   1 
ATOM   264  O O   A LEU A  1 26  ? 5.60597   25.77514 16.24542  0.600 26.97061  ?  26  LEU A O   1 
ATOM   265  O O   B LEU A  1 26  ? 6.27735   25.34400 15.65172  0.400 30.60544  ?  26  LEU A O   1 
ATOM   266  C CB  A LEU A  1 26  ? 6.18425   25.44725 13.14076  0.600 25.42474  ?  26  LEU A CB  1 
ATOM   267  C CB  B LEU A  1 26  ? 5.90585   25.18084 12.75159  0.400 32.35780  ?  26  LEU A CB  1 
ATOM   268  C CG  A LEU A  1 26  ? 5.84844   24.76922 11.82223  0.600 27.40057  ?  26  LEU A CG  1 
ATOM   269  C CG  B LEU A  1 26  ? 5.29269   24.49728 11.54029  0.400 27.73989  ?  26  LEU A CG  1 
ATOM   270  C CD1 A LEU A  1 26  ? 7.13824   24.29245 11.17288  0.600 29.33158  ?  26  LEU A CD1 1 
ATOM   271  C CD1 B LEU A  1 26  ? 6.38819   23.92223 10.67139  0.400 28.10413  ?  26  LEU A CD1 1 
ATOM   272  C CD2 A LEU A  1 26  ? 4.89721   23.61441 12.09125  0.600 33.15562  ?  26  LEU A CD2 1 
ATOM   273  C CD2 B LEU A  1 26  ? 4.37577   23.39903 12.01650  0.400 32.81741  ?  26  LEU A CD2 1 
ATOM   274  N N   A PHE A  1 27  ? 5.80643   27.78728 15.26845  0.600 25.39482  ?  27  PHE A N   1 
ATOM   275  N N   B PHE A  1 27  ? 5.65290   27.47721 15.31614  0.400 21.91430  ?  27  PHE A N   1 
ATOM   276  C CA  A PHE A  1 27  ? 6.44808   28.39546 16.41850  0.600 27.76289  ?  27  PHE A CA  1 
ATOM   277  C CA  B PHE A  1 27  ? 6.35678   27.99144 16.47526  0.400 27.21126  ?  27  PHE A CA  1 
ATOM   278  C C   A PHE A  1 27  ? 5.46587   29.06493 17.36827  0.600 26.82208  ?  27  PHE A C   1 
ATOM   279  C C   B PHE A  1 27  ? 5.45100   28.67476 17.48576  0.400 25.55677  ?  27  PHE A C   1 
ATOM   280  O O   A PHE A  1 27  ? 5.88793   29.74019 18.31862  0.600 25.36345  ?  27  PHE A O   1 
ATOM   281  O O   B PHE A  1 27  ? 5.93218   29.04077 18.56571  0.400 28.42509  ?  27  PHE A O   1 
ATOM   282  C CB  A PHE A  1 27  ? 7.56788   29.31730 15.94528  0.600 28.12478  ?  27  PHE A CB  1 
ATOM   283  C CB  B PHE A  1 27  ? 7.47317   28.95254 16.04227  0.400 30.26606  ?  27  PHE A CB  1 
ATOM   284  C CG  A PHE A  1 27  ? 8.63039   28.57855 15.19565  0.600 32.39412  ?  27  PHE A CG  1 
ATOM   285  C CG  B PHE A  1 27  ? 8.52587   28.30003 15.20561  0.400 32.70223  ?  27  PHE A CG  1 
ATOM   286  C CD1 A PHE A  1 27  ? 9.57967   27.82525 15.87997  0.600 42.36310  ?  27  PHE A CD1 1 
ATOM   287  C CD1 B PHE A  1 27  ? 9.53329   27.54942 15.79552  0.400 41.19888  ?  27  PHE A CD1 1 
ATOM   288  C CD2 A PHE A  1 27  ? 8.63630   28.56619 13.81573  0.600 35.11864  ?  27  PHE A CD2 1 
ATOM   289  C CD2 B PHE A  1 27  ? 8.50400   28.42350 13.82900  0.400 35.18461  ?  27  PHE A CD2 1 
ATOM   290  C CE1 A PHE A  1 27  ? 10.54782  27.10612 15.19216  0.600 40.66299  ?  27  PHE A CE1 1 
ATOM   291  C CE1 B PHE A  1 27  ? 10.50682  26.93891 15.02315  0.400 40.04164  ?  27  PHE A CE1 1 
ATOM   292  C CE2 A PHE A  1 27  ? 9.59414   27.84466 13.11572  0.600 39.54998  ?  27  PHE A CE2 1 
ATOM   293  C CE2 B PHE A  1 27  ? 9.47311   27.81165 13.04616  0.400 39.27249  ?  27  PHE A CE2 1 
ATOM   294  C CZ  A PHE A  1 27  ? 10.55512  27.11290 13.81028  0.600 43.98620  ?  27  PHE A CZ  1 
ATOM   295  C CZ  B PHE A  1 27  ? 10.47670  27.06688 13.64855  0.400 43.95406  ?  27  PHE A CZ  1 
ATOM   296  N N   . ILE A  1 28  ? 4.17078   28.86119 17.16682  1.000 26.38257  ?  28  ILE A N   1 
ATOM   297  C CA  . ILE A  1 28  ? 3.18556   29.39498 18.10277  1.000 28.40542  ?  28  ILE A CA  1 
ATOM   298  C C   . ILE A  1 28  ? 3.08862   28.42305 19.30807  1.000 25.20818  ?  28  ILE A C   1 
ATOM   299  O O   . ILE A  1 28  ? 2.83103   27.22991 19.09260  1.000 28.15093  ?  28  ILE A O   1 
ATOM   300  C CB  . ILE A  1 28  ? 1.82872   29.53207 17.40618  1.000 26.60468  ?  28  ILE A CB  1 
ATOM   301  C CG1 . ILE A  1 28  ? 1.94532   30.56795 16.27547  1.000 26.08916  ?  28  ILE A CG1 1 
ATOM   302  C CG2 . ILE A  1 28  ? 0.71518   29.87626 18.40834  1.000 27.97410  ?  28  ILE A CG2 1 
ATOM   303  C CD1 . ILE A  1 28  ? 0.71081   30.68309 15.41246  1.000 25.41042  ?  28  ILE A CD1 1 
ATOM   304  N N   . PRO A  1 29  ? 3.28278   28.89443 20.53016  1.000 26.60177  ?  29  PRO A N   1 
ATOM   305  C CA  . PRO A  1 29  ? 3.20045   27.96650 21.67003  1.000 23.53960  ?  29  PRO A CA  1 
ATOM   306  C C   . PRO A  1 29  ? 1.78292   27.41503 21.81348  1.000 31.26524  ?  29  PRO A C   1 
ATOM   307  O O   . PRO A  1 29  ? 0.79751   28.08752 21.50483  1.000 28.95393  ?  29  PRO A O   1 
ATOM   308  C CB  . PRO A  1 29  ? 3.57625   28.84440 22.86003  1.000 29.92972  ?  29  PRO A CB  1 
ATOM   309  C CG  . PRO A  1 29  ? 3.18580   30.24742 22.43052  1.000 39.49762  ?  29  PRO A CG  1 
ATOM   310  C CD  . PRO A  1 29  ? 3.45333   30.29879 20.94205  1.000 35.79791  ?  29  PRO A CD  1 
ATOM   311  N N   . LEU A  1 30  ? 1.68001   26.17065 22.26052  1.000 31.51518  ?  30  LEU A N   1 
ATOM   312  C CA  . LEU A  1 30  ? 0.38980   25.48979 22.32209  1.000 28.67446  ?  30  LEU A CA  1 
ATOM   313  C C   . LEU A  1 30  ? 0.07235   25.03772 23.73868  1.000 27.33696  ?  30  LEU A C   1 
ATOM   314  O O   . LEU A  1 30  ? 0.96289   24.61290 24.46905  1.000 29.94902  ?  30  LEU A O   1 
ATOM   315  C CB  . LEU A  1 30  ? 0.39768   24.25267 21.42695  1.000 31.94023  ?  30  LEU A CB  1 
ATOM   316  C CG  . LEU A  1 30  ? 0.56060   24.50935 19.93391  1.000 37.26347  ?  30  LEU A CG  1 
ATOM   317  C CD1 . LEU A  1 30  ? 0.59148   23.18831 19.16192  1.000 35.22649  ?  30  LEU A CD1 1 
ATOM   318  C CD2 . LEU A  1 30  ? -0.58688  25.38013 19.43612  1.000 27.63999  ?  30  LEU A CD2 1 
ATOM   319  N N   . ASN A  1 31  ? -1.20548  25.13891 24.11932  1.000 25.37777  ?  31  ASN A N   1 
ATOM   320  C CA  . ASN A  1 31  ? -1.71326  24.47845 25.31557  1.000 28.43588  ?  31  ASN A CA  1 
ATOM   321  C C   . ASN A  1 31  ? -1.71850  22.95452 25.10885  1.000 24.93814  ?  31  ASN A C   1 
ATOM   322  O O   . ASN A  1 31  ? -1.67783  22.45896 23.97794  1.000 29.01300  ?  31  ASN A O   1 
ATOM   323  C CB  . ASN A  1 31  ? -3.12631  24.98836 25.61879  1.000 31.14789  ?  31  ASN A CB  1 
ATOM   324  C CG  . ASN A  1 31  ? -3.14566  26.47522 25.93040  1.000 45.47731  ?  31  ASN A CG  1 
ATOM   325  O OD1 . ASN A  1 31  ? -3.65507  27.28762 25.15057  1.000 51.98619  ?  31  ASN A OD1 1 
ATOM   326  N ND2 . ASN A  1 31  ? -2.57715  26.84173 27.06973  1.000 35.27668  ?  31  ASN A ND2 1 
ATOM   327  N N   A PHE A  1 32  ? -1.75777  22.22274 26.22919  0.600 33.11975  ?  32  PHE A N   1 
ATOM   328  N N   B PHE A  1 32  ? -1.78292  22.21333 26.22536  0.400 33.04121  ?  32  PHE A N   1 
ATOM   329  C CA  A PHE A  1 32  ? -1.82244  20.76176 26.19610  0.600 28.22100  ?  32  PHE A CA  1 
ATOM   330  C CA  B PHE A  1 32  ? -1.58522  20.76088 26.18647  0.400 27.32543  ?  32  PHE A CA  1 
ATOM   331  C C   A PHE A  1 32  ? -2.85390  20.26500 25.19284  0.600 26.18011  ?  32  PHE A C   1 
ATOM   332  C C   B PHE A  1 32  ? -2.59158  20.05830 25.28715  0.400 27.16929  ?  32  PHE A C   1 
ATOM   333  O O   A PHE A  1 32  ? -2.54786  19.45250 24.31541  0.600 25.09817  ?  32  PHE A O   1 
ATOM   334  O O   B PHE A  1 32  ? -2.24187  19.10700 24.58328  0.400 28.97386  ?  32  PHE A O   1 
ATOM   335  C CB  A PHE A  1 32  ? -2.16949  20.24003 27.59847  0.600 27.68684  ?  32  PHE A CB  1 
ATOM   336  C CB  B PHE A  1 32  ? -1.66953  20.15340 27.59127  0.400 32.85644  ?  32  PHE A CB  1 
ATOM   337  C CG  A PHE A  1 32  ? -2.47246  18.76428 27.64641  0.600 31.69278  ?  32  PHE A CG  1 
ATOM   338  C CG  B PHE A  1 32  ? -1.86464  18.65799 27.58088  0.400 26.91665  ?  32  PHE A CG  1 
ATOM   339  C CD1 A PHE A  1 32  ? -1.45312  17.83574 27.80711  0.600 32.22221  ?  32  PHE A CD1 1 
ATOM   340  C CD1 B PHE A  1 32  ? -0.80818  17.81698 27.28353  0.400 33.32694  ?  32  PHE A CD1 1 
ATOM   341  C CD2 A PHE A  1 32  ? -3.78251  18.31037 27.54046  0.600 27.75733  ?  32  PHE A CD2 1 
ATOM   342  C CD2 B PHE A  1 32  ? -3.11024  18.09846 27.83306  0.400 32.93217  ?  32  PHE A CD2 1 
ATOM   343  C CE1 A PHE A  1 32  ? -1.73006  16.47248 27.85752  0.600 35.05035  ?  32  PHE A CE1 1 
ATOM   344  C CE1 B PHE A  1 32  ? -0.97833  16.44740 27.25453  0.400 32.15702  ?  32  PHE A CE1 1 
ATOM   345  C CE2 A PHE A  1 32  ? -4.07577  16.95899 27.59356  0.600 26.55701  ?  32  PHE A CE2 1 
ATOM   346  C CE2 B PHE A  1 32  ? -3.29148  16.72652 27.81249  0.400 27.65091  ?  32  PHE A CE2 1 
ATOM   347  C CZ  A PHE A  1 32  ? -3.05238  16.03301 27.74088  0.600 29.42792  ?  32  PHE A CZ  1 
ATOM   348  C CZ  B PHE A  1 32  ? -2.21909  15.89715 27.52030  0.400 36.30891  ?  32  PHE A CZ  1 
ATOM   349  N N   A LYS A  1 33  ? -4.09064  20.75684 25.29621  0.600 26.81291  ?  33  LYS A N   1 
ATOM   350  N N   B LYS A  1 33  ? -3.85048  20.47826 25.32860  0.400 27.35815  ?  33  LYS A N   1 
ATOM   351  C CA  A LYS A  1 33  ? -5.15104  20.18904 24.46528  0.600 31.29694  ?  33  LYS A CA  1 
ATOM   352  C CA  B LYS A  1 33  ? -4.89361  19.83825 24.51860  0.400 28.31877  ?  33  LYS A CA  1 
ATOM   353  C C   A LYS A  1 33  ? -4.87787  20.34320 22.96969  0.600 30.76089  ?  33  LYS A C   1 
ATOM   354  C C   B LYS A  1 33  ? -4.82229  20.19476 23.00427  0.400 30.41031  ?  33  LYS A C   1 
ATOM   355  O O   A LYS A  1 33  ? -5.19994  19.43571 22.18753  0.600 29.79728  ?  33  LYS A O   1 
ATOM   356  O O   B LYS A  1 33  ? -5.75577  19.82285 22.23797  0.400 28.88610  ?  33  LYS A O   1 
ATOM   357  C CB  A LYS A  1 33  ? -6.51582  20.75027 24.85811  0.600 30.00592  ?  33  LYS A CB  1 
ATOM   358  C CB  B LYS A  1 33  ? -6.27586  20.15335 25.09762  0.400 30.92644  ?  33  LYS A CB  1 
ATOM   359  C CG  A LYS A  1 33  ? -6.72146  22.23245 24.60584  0.600 35.85810  ?  33  LYS A CG  1 
ATOM   360  C CG  B LYS A  1 33  ? -6.99726  21.38060 24.52362  0.400 40.56521  ?  33  LYS A CG  1 
ATOM   361  C CD  A LYS A  1 33  ? -8.08987  22.65178 25.15320  0.600 32.87813  ?  33  LYS A CD  1 
ATOM   362  C CD  B LYS A  1 33  ? -6.35055  22.71987 24.86736  0.400 38.56601  ?  33  LYS A CD  1 
ATOM   363  C CE  A LYS A  1 33  ? -8.51735  24.00872 24.64342  0.600 40.96364  ?  33  LYS A CE  1 
ATOM   364  C CE  B LYS A  1 33  ? -7.41846  23.83089 24.90423  0.400 41.49225  ?  33  LYS A CE  1 
ATOM   365  N NZ  A LYS A  1 33  ? -8.68443  24.01518 23.16700  0.600 43.67255  ?  33  LYS A NZ  1 
ATOM   366  N NZ  B LYS A  1 33  ? -6.94889  25.15485 24.38818  0.400 45.56661  ?  33  LYS A NZ  1 
ATOM   367  N N   A ASP A  1 34  ? -4.24333  21.44706 22.56038  0.600 22.64237  ?  34  ASP A N   1 
ATOM   368  N N   B ASP A  1 34  ? -3.75461  20.87494 22.57071  0.400 28.06551  ?  34  ASP A N   1 
ATOM   369  C CA  A ASP A  1 34  ? -4.08001  21.80057 21.15036  0.600 21.26902  ?  34  ASP A CA  1 
ATOM   370  C CA  B ASP A  1 34  ? -3.63049  21.34777 21.19893  0.400 25.80147  ?  34  ASP A CA  1 
ATOM   371  C C   A ASP A  1 34  ? -2.78242  21.30729 20.51885  0.600 24.33993  ?  34  ASP A C   1 
ATOM   372  C C   B ASP A  1 34  ? -2.37925  20.84815 20.48283  0.400 21.67820  ?  34  ASP A C   1 
ATOM   373  O O   A ASP A  1 34  ? -2.47753  21.71472 19.39205  0.600 22.76515  ?  34  ASP A O   1 
ATOM   374  O O   B ASP A  1 34  ? -2.20809  21.14358 19.29608  0.400 23.89398  ?  34  ASP A O   1 
ATOM   375  C CB  A ASP A  1 34  ? -4.12814  23.31954 21.00256  0.600 28.63344  ?  34  ASP A CB  1 
ATOM   376  C CB  B ASP A  1 34  ? -3.66707  22.88414 21.15527  0.400 25.50591  ?  34  ASP A CB  1 
ATOM   377  C CG  A ASP A  1 34  ? -5.36065  23.91276 21.63646  0.600 34.44744  ?  34  ASP A CG  1 
ATOM   378  C CG  B ASP A  1 34  ? -5.01143  23.45678 21.60417  0.400 30.43131  ?  34  ASP A CG  1 
ATOM   379  O OD1 A ASP A  1 34  ? -6.47837  23.49826 21.23495  0.600 28.31193  ?  34  ASP A OD1 1 
ATOM   380  O OD1 B ASP A  1 34  ? -6.01713  22.70649 21.61256  0.400 24.37992  ?  34  ASP A OD1 1 
ATOM   381  O OD2 A ASP A  1 34  ? -5.20821  24.77187 22.53172  0.600 30.02661  -1 34  ASP A OD2 1 
ATOM   382  O OD2 B ASP A  1 34  ? -5.06581  24.67489 21.90449  0.400 28.08176  -1 34  ASP A OD2 1 
ATOM   383  N N   A ILE A  1 35  ? -2.01694  20.45737 21.21276  0.600 21.66414  ?  35  ILE A N   1 
ATOM   384  N N   B ILE A  1 35  ? -1.49851  20.10932 21.16741  0.400 27.87933  ?  35  ILE A N   1 
ATOM   385  C CA  A ILE A  1 35  ? -0.69381  20.04599 20.72386  0.600 26.70782  ?  35  ILE A CA  1 
ATOM   386  C CA  B ILE A  1 35  ? -0.23685  19.68817 20.55008  0.400 21.26640  ?  35  ILE A CA  1 
ATOM   387  C C   A ILE A  1 35  ? -0.76712  19.45514 19.31377  0.600 21.14623  ?  35  ILE A C   1 
ATOM   388  C C   B ILE A  1 35  ? -0.47324  18.88209 19.27973  0.400 24.75736  ?  35  ILE A C   1 
ATOM   389  O O   A ILE A  1 35  ? 0.12126   19.67944 18.48020  0.600 24.96218  ?  35  ILE A O   1 
ATOM   390  O O   B ILE A  1 35  ? 0.31994   18.95634 18.33044  0.400 22.38551  ?  35  ILE A O   1 
ATOM   391  C CB  A ILE A  1 35  ? -0.03600  19.08713 21.74223  0.600 28.46807  ?  35  ILE A CB  1 
ATOM   392  C CB  B ILE A  1 35  ? 0.64218   18.91770 21.55518  0.400 32.70743  ?  35  ILE A CB  1 
ATOM   393  C CG1 A ILE A  1 35  ? 0.64178   19.88588 22.86941  0.600 29.79086  ?  35  ILE A CG1 1 
ATOM   394  C CG1 B ILE A  1 35  ? 0.42531   19.44680 22.97189  0.400 29.60121  ?  35  ILE A CG1 1 
ATOM   395  C CG2 A ILE A  1 35  ? 0.93071   18.11259 21.05288  0.600 30.89109  ?  35  ILE A CG2 1 
ATOM   396  C CG2 B ILE A  1 35  ? 2.11307   19.04066 21.15647  0.400 36.08198  ?  35  ILE A CG2 1 
ATOM   397  C CD1 A ILE A  1 35  ? 1.05984   19.04306 24.09066  0.600 44.39832  ?  35  ILE A CD1 1 
ATOM   398  C CD1 B ILE A  1 35  ? 1.08564   18.60065 24.05732  0.400 40.15268  ?  35  ILE A CD1 1 
ATOM   399  N N   A ILE A  1 36  ? -1.84323  18.72210 19.00591  0.600 21.92552  ?  36  ILE A N   1 
ATOM   400  N N   B ILE A  1 36  ? -1.55593  18.09992 19.23051  0.400 19.35880  ?  36  ILE A N   1 
ATOM   401  C CA  A ILE A  1 36  ? -1.92610  17.98996 17.74577  0.600 19.91725  ?  36  ILE A CA  1 
ATOM   402  C CA  B ILE A  1 36  ? -1.83275  17.32472 18.02400  0.400 19.44085  ?  36  ILE A CA  1 
ATOM   403  C C   A ILE A  1 36  ? -2.05408  18.91209 16.53552  0.600 20.72734  ?  36  ILE A C   1 
ATOM   404  C C   B ILE A  1 36  ? -1.83093  18.21818 16.79182  0.400 20.46878  ?  36  ILE A C   1 
ATOM   405  O O   A ILE A  1 36  ? -1.80997  18.48218 15.40799  0.600 19.66956  ?  36  ILE A O   1 
ATOM   406  O O   B ILE A  1 36  ? -1.51024  17.77458 15.68796  0.400 24.46098  ?  36  ILE A O   1 
ATOM   407  C CB  A ILE A  1 36  ? -3.10453  16.99393 17.78892  0.600 20.42199  ?  36  ILE A CB  1 
ATOM   408  C CB  B ILE A  1 36  ? -3.15057  16.52393 18.17133  0.400 18.37600  ?  36  ILE A CB  1 
ATOM   409  C CG1 A ILE A  1 36  ? -2.96604  15.93096 16.69023  0.600 22.83667  ?  36  ILE A CG1 1 
ATOM   410  C CG1 B ILE A  1 36  ? -3.35582  15.60711 16.96439  0.400 32.60040  ?  36  ILE A CG1 1 
ATOM   411  C CG2 A ILE A  1 36  ? -4.41471  17.73212 17.63789  0.600 18.99868  ?  36  ILE A CG2 1 
ATOM   412  C CG2 B ILE A  1 36  ? -4.35370  17.44102 18.29449  0.400 16.49887  ?  36  ILE A CG2 1 
ATOM   413  C CD1 A ILE A  1 36  ? -4.00991  14.79054 16.79880  0.600 22.99336  ?  36  ILE A CD1 1 
ATOM   414  C CD1 B ILE A  1 36  ? -2.21842  14.67895 16.73995  0.400 27.03589  ?  36  ILE A CD1 1 
ATOM   415  N N   A LEU A  1 37  ? -2.46428  20.16324 16.73780  0.600 20.69710  ?  37  LEU A N   1 
ATOM   416  N N   B LEU A  1 37  ? -2.15283  19.49839 16.96981  0.400 21.13949  ?  37  LEU A N   1 
ATOM   417  C CA  A LEU A  1 37  ? -2.53851  21.08226 15.60627  0.600 21.57110  ?  37  LEU A CA  1 
ATOM   418  C CA  B LEU A  1 37  ? -2.22035  20.41596 15.84092  0.400 19.92045  ?  37  LEU A CA  1 
ATOM   419  C C   A LEU A  1 37  ? -1.16349  21.37563 15.02209  0.600 20.55402  ?  37  LEU A C   1 
ATOM   420  C C   B LEU A  1 37  ? -0.85393  20.64109 15.20463  0.400 24.08599  ?  37  LEU A C   1 
ATOM   421  O O   A LEU A  1 37  ? -1.05080  21.62054 13.82191  0.600 21.45715  ?  37  LEU A O   1 
ATOM   422  O O   B LEU A  1 37  ? -0.75647  20.79393 13.98248  0.400 23.37265  ?  37  LEU A O   1 
ATOM   423  C CB  A LEU A  1 37  ? -3.21440  22.39529 16.00070  0.600 19.07163  ?  37  LEU A CB  1 
ATOM   424  C CB  B LEU A  1 37  ? -2.83312  21.74069 16.29411  0.400 19.61151  ?  37  LEU A CB  1 
ATOM   425  C CG  A LEU A  1 37  ? -4.67524  22.37278 16.48001  0.600 20.38774  ?  37  LEU A CG  1 
ATOM   426  C CG  B LEU A  1 37  ? -4.24394  21.61803 16.85064  0.400 22.14282  ?  37  LEU A CG  1 
ATOM   427  C CD1 A LEU A  1 37  ? -5.05002  23.68684 17.11882  0.600 21.26923  ?  37  LEU A CD1 1 
ATOM   428  C CD1 B LEU A  1 37  ? -4.69945  22.91694 17.47826  0.400 24.47234  ?  37  LEU A CD1 1 
ATOM   429  C CD2 A LEU A  1 37  ? -5.61700  22.02783 15.35484  0.600 22.57863  ?  37  LEU A CD2 1 
ATOM   430  C CD2 B LEU A  1 37  ? -5.18645  21.22632 15.72997  0.400 20.45112  ?  37  LEU A CD2 1 
ATOM   431  N N   A ARG A  1 38  ? -0.11733  21.41685 15.84583  0.600 23.40600  ?  38  ARG A N   1 
ATOM   432  N N   B ARG A  1 38  ? 0.21436   20.66658 16.00660  0.400 22.79484  ?  38  ARG A N   1 
ATOM   433  C CA  A ARG A  1 38  ? 1.20675   21.59221 15.26068  0.600 25.31006  ?  38  ARG A CA  1 
ATOM   434  C CA  B ARG A  1 38  ? 1.54874   20.77912 15.42353  0.400 23.77307  ?  38  ARG A CA  1 
ATOM   435  C C   A ARG A  1 38  ? 1.62018   20.34907 14.49577  0.600 23.61558  ?  38  ARG A C   1 
ATOM   436  C C   B ARG A  1 38  ? 1.83367   19.59926 14.50023  0.400 21.41651  ?  38  ARG A C   1 
ATOM   437  O O   A ARG A  1 38  ? 2.27549   20.45085 13.45390  0.600 22.16734  ?  38  ARG A O   1 
ATOM   438  O O   B ARG A  1 38  ? 2.35938   19.77059 13.39128  0.400 23.18095  ?  38  ARG A O   1 
ATOM   439  C CB  A ARG A  1 38  ? 2.25560   21.94721 16.30712  0.600 31.34550  ?  38  ARG A CB  1 
ATOM   440  C CB  B ARG A  1 38  ? 2.61144   20.91697 16.52012  0.400 23.77317  ?  38  ARG A CB  1 
ATOM   441  C CG  A ARG A  1 38  ? 3.65043   22.00817 15.69584  0.600 30.67010  ?  38  ARG A CG  1 
ATOM   442  C CG  B ARG A  1 38  ? 3.74120   21.89075 16.13245  0.400 34.24029  ?  38  ARG A CG  1 
ATOM   443  C CD  A ARG A  1 38  ? 4.69298   22.23061 16.74451  0.600 36.05375  ?  38  ARG A CD  1 
ATOM   444  C CD  B ARG A  1 38  ? 4.67901   22.21119 17.29873  0.400 28.58369  ?  38  ARG A CD  1 
ATOM   445  N NE  A ARG A  1 38  ? 4.41697   23.43420 17.50193  0.600 30.44415  ?  38  ARG A NE  1 
ATOM   446  N NE  B ARG A  1 38  ? 4.27249   23.40280 18.03055  0.400 39.59495  ?  38  ARG A NE  1 
ATOM   447  C CZ  A ARG A  1 38  ? 4.65073   23.55806 18.80235  0.600 49.88825  ?  38  ARG A CZ  1 
ATOM   448  C CZ  B ARG A  1 38  ? 4.29338   23.49661 19.35385  0.400 42.82352  ?  38  ARG A CZ  1 
ATOM   449  N NH1 A ARG A  1 38  ? 5.09843   22.53970 19.52601  0.600 48.25671  ?  38  ARG A NH1 1 
ATOM   450  N NH1 B ARG A  1 38  ? 4.63185   22.46406 20.11391  0.400 37.88572  ?  38  ARG A NH1 1 
ATOM   451  N NH2 A ARG A  1 38  ? 4.41401   24.72425 19.39525  0.600 36.55646  ?  38  ARG A NH2 1 
ATOM   452  N NH2 B ARG A  1 38  ? 3.93527   24.64113 19.93017  0.400 34.01025  ?  38  ARG A NH2 1 
ATOM   453  N N   A GLU A  1 39  ? 1.22778   19.17059 14.99930  0.600 19.58717  ?  39  GLU A N   1 
ATOM   454  N N   B GLU A  1 39  ? 1.44969   18.39167 14.91874  0.400 25.89287  ?  39  GLU A N   1 
ATOM   455  C CA  A GLU A  1 39  ? 1.50852   17.90594 14.31442  0.600 25.25967  ?  39  GLU A CA  1 
ATOM   456  C CA  B GLU A  1 39  ? 1.54780   17.26509 14.00084  0.400 23.76887  ?  39  GLU A CA  1 
ATOM   457  C C   A GLU A  1 39  ? 0.89789   17.90685 12.90691  0.600 22.01347  ?  39  GLU A C   1 
ATOM   458  C C   B GLU A  1 39  ? 0.73256   17.49656 12.73470  0.400 21.69570  ?  39  GLU A C   1 
ATOM   459  O O   A GLU A  1 39  ? 1.58717   17.65563 11.91030  0.600 22.95249  ?  39  GLU A O   1 
ATOM   460  O O   B GLU A  1 39  ? 1.14693   17.06469 11.64718  0.400 21.16875  ?  39  GLU A O   1 
ATOM   461  C CB  A GLU A  1 39  ? 0.96247   16.73636 15.16872  0.600 25.52360  ?  39  GLU A CB  1 
ATOM   462  C CB  B GLU A  1 39  ? 1.14043   15.95248 14.67163  0.400 25.26961  ?  39  GLU A CB  1 
ATOM   463  C CG  A GLU A  1 39  ? 1.74312   16.47256 16.50640  0.600 24.58411  ?  39  GLU A CG  1 
ATOM   464  C CG  B GLU A  1 39  ? 1.12012   14.76166 13.72828  0.400 32.98642  ?  39  GLU A CG  1 
ATOM   465  C CD  A GLU A  1 39  ? 1.17485   15.33792 17.41765  0.600 27.75159  ?  39  GLU A CD  1 
ATOM   466  C CD  B GLU A  1 39  ? 2.45881   14.49483 13.04987  0.400 35.29978  ?  39  GLU A CD  1 
ATOM   467  O OE1 A GLU A  1 39  ? -0.02352  15.00991 17.33357  0.600 32.53447  ?  39  GLU A OE1 1 
ATOM   468  O OE1 B GLU A  1 39  ? 3.47242   15.09525 13.44736  0.400 25.04819  ?  39  GLU A OE1 1 
ATOM   469  O OE2 A GLU A  1 39  ? 1.94043   14.79780 18.23375  0.600 37.88002  -1 39  GLU A OE2 1 
ATOM   470  O OE2 B GLU A  1 39  ? 2.48510   13.68150 12.09825  0.400 36.49265  -1 39  GLU A OE2 1 
ATOM   471  N N   . ILE A  1 40  ? -0.40569  18.19617 12.82577  1.000 27.38438  ?  40  ILE A N   1 
ATOM   472  C CA  . ILE A  1 40  ? -1.14941  18.44349 11.58770  1.000 23.55845  ?  40  ILE A CA  1 
ATOM   473  C C   . ILE A  1 40  ? -0.42008  19.43618 10.69086  1.000 24.68765  ?  40  ILE A C   1 
ATOM   474  O O   . ILE A  1 40  ? -0.27150  19.20898 9.48633   1.000 25.08205  ?  40  ILE A O   1 
ATOM   475  C CB  . ILE A  1 40  ? -2.58628  18.90384 11.91151  1.000 23.71015  ?  40  ILE A CB  1 
ATOM   476  C CG1 . ILE A  1 40  ? -3.34707  17.73934 12.57716  1.000 23.82674  ?  40  ILE A CG1 1 
ATOM   477  C CG2 . ILE A  1 40  ? -3.33145  19.46215 10.66645  1.000 25.79939  ?  40  ILE A CG2 1 
ATOM   478  C CD1 . ILE A  1 40  ? -4.73903  18.15029 13.08763  1.000 28.53880  ?  40  ILE A CD1 1 
ATOM   479  N N   A LEU A  1 41  ? 0.08976   20.53099 11.25815  0.600 23.35645  ?  41  LEU A N   1 
ATOM   480  N N   B LEU A  1 41  ? -0.00642  20.56908 11.25401  0.400 23.60607  ?  41  LEU A N   1 
ATOM   481  C CA  A LEU A  1 41  ? 0.66901   21.56013 10.39653  0.600 24.23556  ?  41  LEU A CA  1 
ATOM   482  C CA  B LEU A  1 41  ? 0.67814   21.57061 10.45126  0.400 24.36783  ?  41  LEU A CA  1 
ATOM   483  C C   A LEU A  1 41  ? 2.02549   21.14041 9.83333   0.600 25.77422  ?  41  LEU A C   1 
ATOM   484  C C   B LEU A  1 41  ? 1.89548   20.96046 9.76759   0.400 25.80856  ?  41  LEU A C   1 
ATOM   485  O O   A LEU A  1 41  ? 2.42136   21.60372 8.75213   0.600 27.95215  ?  41  LEU A O   1 
ATOM   486  O O   B LEU A  1 41  ? 2.04087   21.05400 8.54276   0.400 19.32483  ?  41  LEU A O   1 
ATOM   487  C CB  A LEU A  1 41  ? 0.74343   22.90449 11.12472  0.600 32.09016  ?  41  LEU A CB  1 
ATOM   488  C CB  B LEU A  1 41  ? 1.05646   22.76317 11.33089  0.400 32.44162  ?  41  LEU A CB  1 
ATOM   489  C CG  A LEU A  1 41  ? 0.94337   24.09042 10.18571  0.600 34.74413  ?  41  LEU A CG  1 
ATOM   490  C CG  B LEU A  1 41  ? 1.13264   24.15445 10.70017  0.400 34.27692  ?  41  LEU A CG  1 
ATOM   491  C CD1 A LEU A  1 41  ? -0.16094  24.13284 9.13330   0.600 32.30857  ?  41  LEU A CD1 1 
ATOM   492  C CD1 B LEU A  1 41  ? -0.04377  24.41638 9.77765   0.400 32.49647  ?  41  LEU A CD1 1 
ATOM   493  C CD2 A LEU A  1 41  ? 1.00112   25.38760 10.97193  0.600 27.64081  ?  41  LEU A CD2 1 
ATOM   494  C CD2 B LEU A  1 41  ? 1.17879   25.20066 11.79880  0.400 27.24694  ?  41  LEU A CD2 1 
ATOM   495  N N   . ILE A  1 42  ? 2.73696   20.25800 10.53923  1.000 24.99449  ?  42  ILE A N   1 
ATOM   496  C CA  . ILE A  1 42  ? 3.95295   19.63769 9.98462   1.000 25.43924  ?  42  ILE A CA  1 
ATOM   497  C C   . ILE A  1 42  ? 3.61837   18.76705 8.77454   1.000 23.99156  ?  42  ILE A C   1 
ATOM   498  O O   . ILE A  1 42  ? 4.31063   18.80950 7.74417   1.000 28.39997  ?  42  ILE A O   1 
ATOM   499  C CB  . ILE A  1 42  ? 4.69032   18.82125 11.06837  1.000 31.92352  ?  42  ILE A CB  1 
ATOM   500  C CG1 . ILE A  1 42  ? 5.34978   19.74355 12.07155  1.000 35.05750  ?  42  ILE A CG1 1 
ATOM   501  C CG2 . ILE A  1 42  ? 5.76981   17.90949 10.41179  1.000 33.26580  ?  42  ILE A CG2 1 
ATOM   502  C CD1 . ILE A  1 42  ? 5.82957   19.03061 13.34084  1.000 47.39200  ?  42  ILE A CD1 1 
ATOM   503  N N   A LEU A  1 43  ? 2.55875   17.96846 8.87304   0.600 22.41135  ?  43  LEU A N   1 
ATOM   504  N N   B LEU A  1 43  ? 2.57501   17.93198 8.88822   0.400 22.44167  ?  43  LEU A N   1 
ATOM   505  C CA  A LEU A  1 43  ? 2.19875   17.09489 7.77366   0.600 23.76751  ?  43  LEU A CA  1 
ATOM   506  C CA  B LEU A  1 43  ? 2.15048   17.12533 7.74605   0.400 23.86021  ?  43  LEU A CA  1 
ATOM   507  C C   A LEU A  1 43  ? 1.56160   17.85109 6.61301   0.600 23.23822  ?  43  LEU A C   1 
ATOM   508  C C   B LEU A  1 43  ? 1.80280   18.01790 6.56076   0.400 24.26010  ?  43  LEU A C   1 
ATOM   509  O O   A LEU A  1 43  ? 1.61785   17.37038 5.47086   0.600 21.74575  ?  43  LEU A O   1 
ATOM   510  O O   B LEU A  1 43  ? 2.35729   17.86122 5.46288   0.400 17.75546  ?  43  LEU A O   1 
ATOM   511  C CB  A LEU A  1 43  ? 1.29454   15.96267 8.26543   0.600 25.69066  ?  43  LEU A CB  1 
ATOM   512  C CB  B LEU A  1 43  ? 0.95858   16.22706 8.10623   0.400 18.13898  ?  43  LEU A CB  1 
ATOM   513  C CG  A LEU A  1 43  ? 1.95021   15.01611 9.28831   0.600 19.16862  ?  43  LEU A CG  1 
ATOM   514  C CG  B LEU A  1 43  ? 1.17927   14.99627 9.00655   0.400 26.34821  ?  43  LEU A CG  1 
ATOM   515  C CD1 A LEU A  1 43  ? 0.95931   14.00256 9.81911   0.600 25.71032  ?  43  LEU A CD1 1 
ATOM   516  C CD1 B LEU A  1 43  ? -0.17010  14.39511 9.40302   0.400 26.94995  ?  43  LEU A CD1 1 
ATOM   517  C CD2 A LEU A  1 43  ? 3.13023   14.29454 8.64456   0.600 21.55406  ?  43  LEU A CD2 1 
ATOM   518  C CD2 B LEU A  1 43  ? 2.08977   13.92043 8.38865   0.400 22.34699  ?  43  LEU A CD2 1 
ATOM   519  N N   A GLU A  1 44  ? 0.96984   19.02885 6.86193   0.600 23.12367  ?  44  GLU A N   1 
ATOM   520  N N   B GLU A  1 44  ? 0.89330   18.98065 6.77534   0.400 23.71998  ?  44  GLU A N   1 
ATOM   521  C CA  A GLU A  1 44  ? 0.49132   19.84384 5.74326   0.600 21.97758  ?  44  GLU A CA  1 
ATOM   522  C CA  B GLU A  1 44  ? 0.49920   19.90442 5.71267   0.400 21.99369  ?  44  GLU A CA  1 
ATOM   523  C C   A GLU A  1 44  ? 1.64545   20.55126 5.04903   0.600 24.03501  ?  44  GLU A C   1 
ATOM   524  C C   B GLU A  1 44  ? 1.72274   20.44146 4.99086   0.400 24.13431  ?  44  GLU A C   1 
ATOM   525  O O   A GLU A  1 44  ? 1.57024   20.83898 3.84175   0.600 24.45884  ?  44  GLU A O   1 
ATOM   526  O O   B GLU A  1 44  ? 1.79566   20.41896 3.75355   0.400 22.82952  ?  44  GLU A O   1 
ATOM   527  C CB  A GLU A  1 44  ? -0.52141  20.87625 6.23545   0.600 27.08358  ?  44  GLU A CB  1 
ATOM   528  C CB  B GLU A  1 44  ? -0.30372  21.06297 6.30762   0.400 27.83022  ?  44  GLU A CB  1 
ATOM   529  C CG  A GLU A  1 44  ? -1.87309  20.31604 6.58134   0.600 32.23441  ?  44  GLU A CG  1 
ATOM   530  C CG  B GLU A  1 44  ? -1.55416  20.64616 7.05572   0.400 24.40019  ?  44  GLU A CG  1 
ATOM   531  C CD  A GLU A  1 44  ? -2.57881  19.69740 5.38374   0.600 41.36884  ?  44  GLU A CD  1 
ATOM   532  C CD  B GLU A  1 44  ? -2.48794  21.80748 7.33574   0.400 37.90618  ?  44  GLU A CD  1 
ATOM   533  O OE1 A GLU A  1 44  ? -2.64630  20.35564 4.32040   0.600 38.17807  ?  44  GLU A OE1 1 
ATOM   534  O OE1 B GLU A  1 44  ? -2.12276  22.70114 8.13989   0.400 28.74155  ?  44  GLU A OE1 1 
ATOM   535  O OE2 A GLU A  1 44  ? -3.04814  18.54212 5.50609   0.600 40.56917  ?  44  GLU A OE2 1 
ATOM   536  O OE2 B GLU A  1 44  ? -3.59228  21.82852 6.74915   0.400 39.27169  ?  44  GLU A OE2 1 
ATOM   537  N N   A LEU A  1 45  ? 2.72006   20.83382 5.79578   0.600 24.61282  ?  45  LEU A N   1 
ATOM   538  N N   B LEU A  1 45  ? 2.72038   20.88093 5.76394   0.400 24.66778  ?  45  LEU A N   1 
ATOM   539  C CA  A LEU A  1 45  ? 3.92321   21.41390 5.20529   0.600 24.34364  ?  45  LEU A CA  1 
ATOM   540  C CA  B LEU A  1 45  ? 3.93970   21.43591 5.18894   0.400 24.41728  ?  45  LEU A CA  1 
ATOM   541  C C   A LEU A  1 45  ? 4.67404   20.38465 4.37478   0.600 26.45956  ?  45  LEU A C   1 
ATOM   542  C C   B LEU A  1 45  ? 4.70297   20.39071 4.38287   0.400 26.45871  ?  45  LEU A C   1 
ATOM   543  O O   A LEU A  1 45  ? 5.25193   20.72083 3.33288   0.600 27.31530  ?  45  LEU A O   1 
ATOM   544  O O   B LEU A  1 45  ? 5.31799   20.72029 3.36127   0.400 27.48273  ?  45  LEU A O   1 
ATOM   545  C CB  A LEU A  1 45  ? 4.82952   21.99994 6.29801   0.600 26.94270  ?  45  LEU A CB  1 
ATOM   546  C CB  B LEU A  1 45  ? 4.81724   22.02515 6.29625   0.400 26.90674  ?  45  LEU A CB  1 
ATOM   547  C CG  A LEU A  1 45  ? 4.50572   23.41928 6.76255   0.600 26.57525  ?  45  LEU A CG  1 
ATOM   548  C CG  B LEU A  1 45  ? 5.90853   22.97402 5.81111   0.400 28.39737  ?  45  LEU A CG  1 
ATOM   549  C CD1 A LEU A  1 45  ? 5.26985   23.74969 8.03671   0.600 26.05426  ?  45  LEU A CD1 1 
ATOM   550  C CD1 B LEU A  1 45  ? 5.30037   24.18343 5.09755   0.400 27.63294  ?  45  LEU A CD1 1 
ATOM   551  C CD2 A LEU A  1 45  ? 4.86303   24.42765 5.66444   0.600 31.04792  ?  45  LEU A CD2 1 
ATOM   552  C CD2 B LEU A  1 45  ? 6.79090   23.42077 6.97444   0.400 30.36973  ?  45  LEU A CD2 1 
ATOM   553  N N   . ILE A  1 46  ? 4.68688   19.12889 4.82504   1.000 23.50409  ?  46  ILE A N   1 
ATOM   554  C CA  . ILE A  1 46  ? 5.25511   18.06405 4.00731   1.000 22.78520  ?  46  ILE A CA  1 
ATOM   555  C C   . ILE A  1 46  ? 4.50215   17.96099 2.68795   1.000 25.43124  ?  46  ILE A C   1 
ATOM   556  O O   . ILE A  1 46  ? 5.09986   17.88453 1.60245   1.000 25.04543  ?  46  ILE A O   1 
ATOM   557  C CB  . ILE A  1 46  ? 5.28664   16.73604 4.77308   1.000 25.05446  ?  46  ILE A CB  1 
ATOM   558  C CG1 . ILE A  1 46  ? 6.33930   16.81414 5.87769   1.000 27.29857  ?  46  ILE A CG1 1 
ATOM   559  C CG2 . ILE A  1 46  ? 5.55054   15.59770 3.78913   1.000 31.80615  ?  46  ILE A CG2 1 
ATOM   560  C CD1 . ILE A  1 46  ? 6.22976   15.68185 6.88791   1.000 39.12245  ?  46  ILE A CD1 1 
ATOM   561  N N   . VAL A  1 47  ? 3.17346   17.96813 2.75843   1.000 21.28407  ?  47  VAL A N   1 
ATOM   562  C CA  . VAL A  1 47  ? 2.36486   17.94857 1.54236   1.000 22.85544  ?  47  VAL A CA  1 
ATOM   563  C C   . VAL A  1 47  ? 2.72284   19.14453 0.65706   1.000 25.75434  ?  47  VAL A C   1 
ATOM   564  O O   . VAL A  1 47  ? 2.83896   19.01504 -0.56969  1.000 25.23839  ?  47  VAL A O   1 
ATOM   565  C CB  . VAL A  1 47  ? 0.85776   17.89479 1.87456   1.000 22.15286  ?  47  VAL A CB  1 
ATOM   566  C CG1 . VAL A  1 47  ? 0.01248   18.23900 0.63169   1.000 25.37146  ?  47  VAL A CG1 1 
ATOM   567  C CG2 . VAL A  1 47  ? 0.46729   16.50950 2.41401   1.000 21.67193  ?  47  VAL A CG2 1 
ATOM   568  N N   A GLN A  1 48  ? 2.95380   20.31660 1.25633   0.600 22.75648  ?  48  GLN A N   1 
ATOM   569  N N   B GLN A  1 48  ? 2.90465   20.32172 1.27791   0.400 22.78951  ?  48  GLN A N   1 
ATOM   570  C CA  A GLN A  1 48  ? 3.31187   21.47827 0.43712   0.600 26.07749  ?  48  GLN A CA  1 
ATOM   571  C CA  B GLN A  1 48  ? 3.19974   21.56095 0.55343   0.400 25.68891  ?  48  GLN A CA  1 
ATOM   572  C C   A GLN A  1 48  ? 4.62948   21.26381 -0.29875  0.600 28.72700  ?  48  GLN A C   1 
ATOM   573  C C   B GLN A  1 48  ? 4.55637   21.51395 -0.13386  0.400 29.34268  ?  48  GLN A C   1 
ATOM   574  O O   A GLN A  1 48  ? 4.75970   21.63893 -1.47058  0.600 29.00214  ?  48  GLN A O   1 
ATOM   575  O O   B GLN A  1 48  ? 4.77207   22.21502 -1.13395  0.400 26.65813  ?  48  GLN A O   1 
ATOM   576  C CB  A GLN A  1 48  ? 3.35287   22.76455 1.26396   0.600 27.30803  ?  48  GLN A CB  1 
ATOM   577  C CB  B GLN A  1 48  ? 3.15388   22.75211 1.51486   0.400 28.90508  ?  48  GLN A CB  1 
ATOM   578  C CG  A GLN A  1 48  ? 1.96812   23.32696 1.57784   0.600 30.07422  ?  48  GLN A CG  1 
ATOM   579  C CG  B GLN A  1 48  ? 1.76282   23.03701 2.04112   0.400 29.34587  ?  48  GLN A CG  1 
ATOM   580  C CD  A GLN A  1 48  ? 1.94185   24.84626 1.67901   0.600 30.50797  ?  48  GLN A CD  1 
ATOM   581  C CD  B GLN A  1 48  ? 1.70975   24.06004 3.17583   0.400 31.17132  ?  48  GLN A CD  1 
ATOM   582  O OE1 A GLN A  1 48  ? 1.44530   25.40561 2.66249   0.600 30.20109  ?  48  GLN A OE1 1 
ATOM   583  O OE1 B GLN A  1 48  ? 1.27350   23.74696 4.28386   0.400 28.98312  ?  48  GLN A OE1 1 
ATOM   584  N NE2 A GLN A  1 48  ? 2.44315   25.52521 0.64743   0.600 28.61390  ?  48  GLN A NE2 1 
ATOM   585  N NE2 B GLN A  1 48  ? 2.14180   25.28649 2.89863   0.400 25.27128  ?  48  GLN A NE2 1 
ATOM   586  N N   A ILE A  1 49  ? 5.62541   20.67901 0.36911   0.600 26.36797  ?  49  ILE A N   1 
ATOM   587  N N   B ILE A  1 49  ? 5.49013   20.72702 0.39595   0.400 26.55776  ?  49  ILE A N   1 
ATOM   588  C CA  A ILE A  1 49  ? 6.90730   20.45660 -0.29343  0.600 31.10507  ?  49  ILE A CA  1 
ATOM   589  C CA  B ILE A  1 49  ? 6.75424   20.51863 -0.29976  0.400 30.93825  ?  49  ILE A CA  1 
ATOM   590  C C   A ILE A  1 49  ? 6.73163   19.58412 -1.53064  0.600 29.98183  ?  49  ILE A C   1 
ATOM   591  C C   B ILE A  1 49  ? 6.52485   19.72229 -1.57516  0.400 30.02727  ?  49  ILE A C   1 
ATOM   592  O O   A ILE A  1 49  ? 7.34455   19.83552 -2.57652  0.600 29.85249  ?  49  ILE A O   1 
ATOM   593  O O   B ILE A  1 49  ? 6.91282   20.14249 -2.67328  0.400 29.07751  ?  49  ILE A O   1 
ATOM   594  C CB  A ILE A  1 49  ? 7.95014   19.89442 0.69005   0.600 33.16872  ?  49  ILE A CB  1 
ATOM   595  C CB  B ILE A  1 49  ? 7.76899   19.82387 0.62368   0.400 32.68767  ?  49  ILE A CB  1 
ATOM   596  C CG1 A ILE A  1 49  ? 8.25377   20.92930 1.77779   0.600 32.00184  ?  49  ILE A CG1 1 
ATOM   597  C CG1 B ILE A  1 49  ? 8.12575   20.72560 1.80490   0.400 31.89090  ?  49  ILE A CG1 1 
ATOM   598  C CG2 A ILE A  1 49  ? 9.22188   19.50318 -0.06202  0.600 32.51951  ?  49  ILE A CG2 1 
ATOM   599  C CG2 B ILE A  1 49  ? 9.00724   19.43129 -0.16859  0.400 31.60493  ?  49  ILE A CG2 1 
ATOM   600  C CD1 A ILE A  1 49  ? 9.11471   20.42574 2.92175   0.600 32.49941  ?  49  ILE A CD1 1 
ATOM   601  C CD1 B ILE A  1 49  ? 8.86341   20.01371 2.92295   0.400 31.34625  ?  49  ILE A CD1 1 
ATOM   602  N N   . ILE A  1 50  ? 5.87767   18.55886 -1.44748  1.000 24.44650  ?  50  ILE A N   1 
ATOM   603  C CA  A ILE A  1 50  ? 5.64461   17.68842 -2.59190  0.600 25.57959  ?  50  ILE A CA  1 
ATOM   604  C CA  B ILE A  1 50  ? 5.64304   17.68492 -2.58898  0.400 25.71404  ?  50  ILE A CA  1 
ATOM   605  C C   . ILE A  1 50  ? 4.85735   18.40316 -3.66682  1.000 28.84181  ?  50  ILE A C   1 
ATOM   606  O O   . ILE A  1 50  ? 5.17441   18.33601 -4.85978  1.000 25.91625  ?  50  ILE A O   1 
ATOM   607  C CB  A ILE A  1 50  ? 4.95965   16.37951 -2.16173  0.600 25.42693  ?  50  ILE A CB  1 
ATOM   608  C CB  B ILE A  1 50  ? 4.93411   16.40370 -2.11535  0.400 25.23263  ?  50  ILE A CB  1 
ATOM   609  C CG1 A ILE A  1 50  ? 5.97877   15.49024 -1.43480  0.600 26.56994  ?  50  ILE A CG1 1 
ATOM   610  C CG1 B ILE A  1 50  ? 5.62331   15.89440 -0.84138  0.400 24.78205  ?  50  ILE A CG1 1 
ATOM   611  C CG2 A ILE A  1 50  ? 4.36937   15.67840 -3.39792  0.600 22.26158  ?  50  ILE A CG2 1 
ATOM   612  C CG2 B ILE A  1 50  ? 4.97181   15.33955 -3.20743  0.400 28.82682  ?  50  ILE A CG2 1 
ATOM   613  C CD1 A ILE A  1 50  ? 5.35813   14.43844 -0.53173  0.600 32.28170  ?  50  ILE A CD1 1 
ATOM   614  C CD1 B ILE A  1 50  ? 4.72169   15.10900 0.09525   0.400 22.30645  ?  50  ILE A CD1 1 
ATOM   615  N N   A GLU A  1 51  ? 3.78289   19.11397 -3.27083  0.300 22.59091  ?  51  GLU A N   1 
ATOM   616  N N   B GLU A  1 51  ? 3.75822   19.06759 -3.25427  0.300 22.55856  ?  51  GLU A N   1 
ATOM   617  N N   C GLU A  1 51  ? 4.26336   19.49275 -3.16810  0.400 22.29990  ?  51  GLU A N   1 
ATOM   618  C CA  A GLU A  1 51  ? 2.98584   19.84796 -4.24698  0.300 24.46614  ?  51  GLU A CA  1 
ATOM   619  C CA  B GLU A  1 51  ? 2.97488   19.91786 -4.13904  0.300 24.60134  ?  51  GLU A CA  1 
ATOM   620  C CA  C GLU A  1 51  ? 3.37728   20.30640 -3.99493  0.400 28.47943  ?  51  GLU A CA  1 
ATOM   621  C C   A GLU A  1 51  ? 3.84229   20.84289 -5.02574  0.300 26.92578  ?  51  GLU A C   1 
ATOM   622  C C   B GLU A  1 51  ? 3.86784   20.90236 -4.88752  0.300 26.75406  ?  51  GLU A C   1 
ATOM   623  C C   C GLU A  1 51  ? 4.11813   21.38358 -4.78243  0.400 28.19252  ?  51  GLU A C   1 
ATOM   624  O O   A GLU A  1 51  ? 3.75626   20.91456 -6.25884  0.300 23.69335  ?  51  GLU A O   1 
ATOM   625  O O   B GLU A  1 51  ? 3.75660   21.04893 -6.11138  0.300 24.39136  ?  51  GLU A O   1 
ATOM   626  O O   C GLU A  1 51  ? 3.98788   21.47242 -6.01036  0.400 26.92646  ?  51  GLU A O   1 
ATOM   627  C CB  A GLU A  1 51  ? 1.82137   20.56471 -3.56048  0.300 26.11296  ?  51  GLU A CB  1 
ATOM   628  C CB  B GLU A  1 51  ? 1.92475   20.66094 -3.30116  0.300 25.64581  ?  51  GLU A CB  1 
ATOM   629  C CB  C GLU A  1 51  ? 2.27455   20.93165 -3.14343  0.400 27.17390  ?  51  GLU A CB  1 
ATOM   630  C CG  A GLU A  1 51  ? 0.99115   21.36990 -4.53575  0.300 25.95373  ?  51  GLU A CG  1 
ATOM   631  C CG  B GLU A  1 51  ? 1.08309   21.67740 -4.05922  0.300 24.84458  ?  51  GLU A CG  1 
ATOM   632  C CG  C GLU A  1 51  ? 1.07083   20.04049 -3.01972  0.400 23.70867  ?  51  GLU A CG  1 
ATOM   633  C CD  A GLU A  1 51  ? 0.05711   22.38464 -3.89949  0.300 25.20126  ?  51  GLU A CD  1 
ATOM   634  C CD  B GLU A  1 51  ? 0.14628   22.49063 -3.15612  0.300 23.63110  ?  51  GLU A CD  1 
ATOM   635  C CD  C GLU A  1 51  ? 0.35003   19.87894 -4.34498  0.400 31.20670  ?  51  GLU A CD  1 
ATOM   636  O OE1 A GLU A  1 51  ? 0.24961   22.78163 -2.73251  0.300 22.05594  ?  51  GLU A OE1 1 
ATOM   637  O OE1 B GLU A  1 51  ? 0.42854   22.64061 -1.94218  0.300 26.24431  ?  51  GLU A OE1 1 
ATOM   638  O OE1 C GLU A  1 51  ? -0.34446  20.83016 -4.75745  0.400 30.21361  ?  51  GLU A OE1 1 
ATOM   639  O OE2 A GLU A  1 51  ? -0.87476  22.81228 -4.59497  0.300 19.04595  ?  51  GLU A OE2 1 
ATOM   640  O OE2 B GLU A  1 51  ? -0.88056  22.98337 -3.66057  0.300 20.38626  ?  51  GLU A OE2 1 
ATOM   641  O OE2 C GLU A  1 51  ? 0.47429   18.80457 -4.97732  0.400 34.17128  ?  51  GLU A OE2 1 
ATOM   642  N N   A PHE A  1 52  ? 4.68326   21.61376 -4.31685  0.600 27.10901  ?  52  PHE A N   1 
ATOM   643  N N   B PHE A  1 52  ? 4.78530   21.56558 -4.16377  0.400 27.48766  ?  52  PHE A N   1 
ATOM   644  C CA  A PHE A  1 52  ? 5.50954   22.64030 -4.95789  0.600 28.87635  ?  52  PHE A CA  1 
ATOM   645  C CA  B PHE A  1 52  ? 5.60427   22.62607 -4.75501  0.400 28.75821  ?  52  PHE A CA  1 
ATOM   646  C C   A PHE A  1 52  ? 6.45326   22.04416 -5.99839  0.600 29.43882  ?  52  PHE A C   1 
ATOM   647  C C   B PHE A  1 52  ? 6.62095   22.08064 -5.75500  0.400 28.77873  ?  52  PHE A C   1 
ATOM   648  O O   A PHE A  1 52  ? 6.56635   22.56220 -7.11869  0.600 28.81449  ?  52  PHE A O   1 
ATOM   649  O O   B PHE A  1 52  ? 6.95550   22.75775 -6.73713  0.400 30.43003  ?  52  PHE A O   1 
ATOM   650  C CB  A PHE A  1 52  ? 6.29521   23.42608 -3.90162  0.600 32.41292  ?  52  PHE A CB  1 
ATOM   651  C CB  B PHE A  1 52  ? 6.30786   23.43472 -3.66054  0.400 31.00338  ?  52  PHE A CB  1 
ATOM   652  C CG  A PHE A  1 52  ? 7.01158   24.63473 -4.44707  0.600 35.14205  ?  52  PHE A CG  1 
ATOM   653  C CG  B PHE A  1 52  ? 6.31169   24.91624 -3.91279  0.400 29.70247  ?  52  PHE A CG  1 
ATOM   654  C CD1 A PHE A  1 52  ? 6.29888   25.74427 -4.88960  0.600 29.38108  ?  52  PHE A CD1 1 
ATOM   655  C CD1 B PHE A  1 52  ? 7.15718   25.47082 -4.86043  0.400 35.19019  ?  52  PHE A CD1 1 
ATOM   656  C CD2 A PHE A  1 52  ? 8.40106   24.66351 -4.51862  0.600 28.45142  ?  52  PHE A CD2 1 
ATOM   657  C CD2 B PHE A  1 52  ? 5.46621   25.75035 -3.20982  0.400 36.21165  ?  52  PHE A CD2 1 
ATOM   658  C CE1 A PHE A  1 52  ? 6.96610   26.85874 -5.39633  0.600 35.53775  ?  52  PHE A CE1 1 
ATOM   659  C CE1 B PHE A  1 52  ? 7.15838   26.83273 -5.09643  0.400 37.10312  ?  52  PHE A CE1 1 
ATOM   660  C CE2 A PHE A  1 52  ? 9.07230   25.77999 -5.01428  0.600 28.60310  ?  52  PHE A CE2 1 
ATOM   661  C CE2 B PHE A  1 52  ? 5.46175   27.10562 -3.43534  0.400 36.91034  ?  52  PHE A CE2 1 
ATOM   662  C CZ  A PHE A  1 52  ? 8.35672   26.87672 -5.44725  0.600 24.67318  ?  52  PHE A CZ  1 
ATOM   663  C CZ  B PHE A  1 52  ? 6.30637   27.65208 -4.38267  0.400 47.67152  ?  52  PHE A CZ  1 
ATOM   664  N N   A ILE A  1 53  ? 7.17286   20.97996 -5.62972  0.600 26.45399  ?  53  ILE A N   1 
ATOM   665  N N   B ILE A  1 53  ? 7.15833   20.88498 -5.50305  0.400 27.02690  ?  53  ILE A N   1 
ATOM   666  C CA  A ILE A  1 53  ? 8.04668   20.28667 -6.57724  0.600 32.37574  ?  53  ILE A CA  1 
ATOM   667  C CA  B ILE A  1 53  ? 8.00198   20.22067 -6.49593  0.400 32.31175  ?  53  ILE A CA  1 
ATOM   668  C C   A ILE A  1 53  ? 7.28082   19.91379 -7.84330  0.600 29.40855  ?  53  ILE A C   1 
ATOM   669  C C   B ILE A  1 53  ? 7.23093   20.03168 -7.79237  0.400 28.84801  ?  53  ILE A C   1 
ATOM   670  O O   A ILE A  1 53  ? 7.78789   20.06591 -8.96655  0.600 27.84726  ?  53  ILE A O   1 
ATOM   671  O O   B ILE A  1 53  ? 7.69323   20.41082 -8.88026  0.400 26.41936  ?  53  ILE A O   1 
ATOM   672  C CB  A ILE A  1 53  ? 8.70796   19.06260 -5.90937  0.600 28.08643  ?  53  ILE A CB  1 
ATOM   673  C CB  B ILE A  1 53  ? 8.50550   18.86953 -5.95312  0.400 30.11339  ?  53  ILE A CB  1 
ATOM   674  C CG1 A ILE A  1 53  ? 9.65806   19.49145 -4.78935  0.600 36.54329  ?  53  ILE A CG1 1 
ATOM   675  C CG1 B ILE A  1 53  ? 9.51526   19.06415 -4.82755  0.400 35.06953  ?  53  ILE A CG1 1 
ATOM   676  C CG2 A ILE A  1 53  ? 9.45663   18.21967 -6.93828  0.600 32.08928  ?  53  ILE A CG2 1 
ATOM   677  C CG2 B ILE A  1 53  ? 9.09306   18.02238 -7.07887  0.400 32.50888  ?  53  ILE A CG2 1 
ATOM   678  C CD1 A ILE A  1 53  ? 10.21240  18.32478 -3.96273  0.600 31.15659  ?  53  ILE A CD1 1 
ATOM   679  C CD1 B ILE A  1 53  ? 9.86532   17.77051 -4.11289  0.400 27.14382  ?  53  ILE A CD1 1 
ATOM   680  N N   . PHE A  1 54  ? 6.03873   19.43637 -7.68864  1.000 24.34298  ?  54  PHE A N   1 
ATOM   681  C CA  . PHE A  1 54  ? 5.21722   19.15640 -8.86268  1.000 27.77356  ?  54  PHE A CA  1 
ATOM   682  C C   . PHE A  1 54  ? 4.95714   20.41896 -9.67963  1.000 28.12250  ?  54  PHE A C   1 
ATOM   683  O O   . PHE A  1 54  ? 5.06889   20.40311 -10.91175 1.000 25.86273  ?  54  PHE A O   1 
ATOM   684  C CB  . PHE A  1 54  ? 3.87371   18.51453 -8.49230  1.000 28.84059  ?  54  PHE A CB  1 
ATOM   685  C CG  . PHE A  1 54  ? 2.92142   18.45976 -9.66490  1.000 27.21865  ?  54  PHE A CG  1 
ATOM   686  C CD1 . PHE A  1 54  ? 3.05370   17.47758 -10.63341 1.000 28.57100  ?  54  PHE A CD1 1 
ATOM   687  C CD2 . PHE A  1 54  ? 1.95253   19.43131 -9.83787  1.000 25.99395  ?  54  PHE A CD2 1 
ATOM   688  C CE1 . PHE A  1 54  ? 2.20868   17.44841 -11.72791 1.000 26.43403  ?  54  PHE A CE1 1 
ATOM   689  C CE2 . PHE A  1 54  ? 1.11722   19.43130 -10.92612 1.000 27.71448  ?  54  PHE A CE2 1 
ATOM   690  C CZ  . PHE A  1 54  ? 1.24316   18.42835 -11.89168 1.000 30.40091  ?  54  PHE A CZ  1 
ATOM   691  N N   A TYR A  1 55  ? 4.57343   21.50864 -9.01007  0.500 23.34176  ?  55  TYR A N   1 
ATOM   692  N N   B TYR A  1 55  ? 4.62464   21.53279 -9.01733  0.500 23.32110  ?  55  TYR A N   1 
ATOM   693  C CA  A TYR A  1 55  ? 4.25125   22.72924 -9.74311  0.500 25.66870  ?  55  TYR A CA  1 
ATOM   694  C CA  B TYR A  1 55  ? 4.24103   22.72445 -9.77923  0.500 25.66686  ?  55  TYR A CA  1 
ATOM   695  C C   A TYR A  1 55  ? 5.46589   23.26286 -10.48577 0.500 21.59464  ?  55  TYR A C   1 
ATOM   696  C C   B TYR A  1 55  ? 5.43530   23.44664 -10.39274 0.500 23.22684  ?  55  TYR A C   1 
ATOM   697  O O   A TYR A  1 55  ? 5.36254   23.65367 -11.65428 0.500 22.58437  ?  55  TYR A O   1 
ATOM   698  O O   B TYR A  1 55  ? 5.27335   24.17591 -11.38105 0.500 25.01802  ?  55  TYR A O   1 
ATOM   699  C CB  A TYR A  1 55  ? 3.61682   23.77654 -8.81967  0.500 25.29051  ?  55  TYR A CB  1 
ATOM   700  C CB  B TYR A  1 55  ? 3.32589   23.64860 -8.95966  0.500 25.00305  ?  55  TYR A CB  1 
ATOM   701  C CG  A TYR A  1 55  ? 2.11735   23.58630 -8.70030  0.500 23.88883  ?  55  TYR A CG  1 
ATOM   702  C CG  B TYR A  1 55  ? 1.88995   23.16964 -8.93949  0.500 19.80878  ?  55  TYR A CG  1 
ATOM   703  C CD1 A TYR A  1 55  ? 1.57868   22.68160 -7.79652  0.500 19.09751  ?  55  TYR A CD1 1 
ATOM   704  C CD1 B TYR A  1 55  ? 0.98880   23.60295 -9.90091  0.500 20.27034  ?  55  TYR A CD1 1 
ATOM   705  C CD2 A TYR A  1 55  ? 1.24627   24.29428 -9.51605  0.500 22.56026  ?  55  TYR A CD2 1 
ATOM   706  C CD2 B TYR A  1 55  ? 1.44782   22.26444 -7.98232  0.500 22.32966  ?  55  TYR A CD2 1 
ATOM   707  C CE1 A TYR A  1 55  ? 0.20786   22.48960 -7.70932  0.500 20.74798  ?  55  TYR A CE1 1 
ATOM   708  C CE1 B TYR A  1 55  ? -0.29643  23.16955 -9.91713  0.500 21.68770  ?  55  TYR A CE1 1 
ATOM   709  C CE2 A TYR A  1 55  ? -0.11341  24.11075 -9.43766  0.500 21.98613  ?  55  TYR A CE2 1 
ATOM   710  C CE2 B TYR A  1 55  ? 0.14277   21.81866 -7.99167  0.500 19.29407  ?  55  TYR A CE2 1 
ATOM   711  C CZ  A TYR A  1 55  ? -0.63001  23.21000 -8.53312  0.500 25.65641  ?  55  TYR A CZ  1 
ATOM   712  C CZ  B TYR A  1 55  ? -0.72235  22.27394 -8.97198  0.500 18.40160  ?  55  TYR A CZ  1 
ATOM   713  O OH  A TYR A  1 55  ? -1.99681  23.03100 -8.44941  0.500 31.35434  ?  55  TYR A OH  1 
ATOM   714  O OH  B TYR A  1 55  ? -2.02243  21.84889 -8.98967  0.500 19.61529  ?  55  TYR A OH  1 
ATOM   715  N N   . ILE A  1 56  ? 6.63828   23.26738 -9.83978  1.000 29.43273  ?  56  ILE A N   1 
ATOM   716  C CA  . ILE A  1 56  ? 7.83919   23.77001 -10.51847 1.000 30.89093  ?  56  ILE A CA  1 
ATOM   717  C C   . ILE A  1 56  ? 8.14639   22.92281 -11.74897 1.000 26.07626  ?  56  ILE A C   1 
ATOM   718  O O   . ILE A  1 56  ? 8.36217   23.44792 -12.85170 1.000 29.55916  ?  56  ILE A O   1 
ATOM   719  C CB  . ILE A  1 56  ? 9.04178   23.83620 -9.55900  1.000 31.34221  ?  56  ILE A CB  1 
ATOM   720  C CG1 . ILE A  1 56  ? 8.77590   24.84378 -8.42630  1.000 34.17536  ?  56  ILE A CG1 1 
ATOM   721  C CG2 . ILE A  1 56  ? 10.32675  24.13816 -10.35823 1.000 31.50720  ?  56  ILE A CG2 1 
ATOM   722  C CD1 . ILE A  1 56  ? 8.11517   26.16367 -8.88576  1.000 36.73463  ?  56  ILE A CD1 1 
ATOM   723  N N   . TRP A  1 57  ? 8.15904   21.59424 -11.58211 1.000 25.65324  ?  57  TRP A N   1 
ATOM   724  C CA  . TRP A  1 57  ? 8.25544   20.67992 -12.72422 1.000 26.22249  ?  57  TRP A CA  1 
ATOM   725  C C   . TRP A  1 57  ? 7.22070   21.02103 -13.79551 1.000 30.19678  ?  57  TRP A C   1 
ATOM   726  O O   . TRP A  1 57  ? 7.52985   21.04532 -14.99490 1.000 30.73892  ?  57  TRP A O   1 
ATOM   727  C CB  . TRP A  1 57  ? 8.04053   19.23929 -12.24724 1.000 27.09703  ?  57  TRP A CB  1 
ATOM   728  C CG  . TRP A  1 57  ? 7.95447   18.25301 -13.38496 1.000 28.01935  ?  57  TRP A CG  1 
ATOM   729  C CD1 . TRP A  1 57  ? 8.99914   17.59269 -13.96650 1.000 44.39246  ?  57  TRP A CD1 1 
ATOM   730  C CD2 . TRP A  1 57  ? 6.77601   17.86155 -14.12222 1.000 26.04513  ?  57  TRP A CD2 1 
ATOM   731  N NE1 . TRP A  1 57  ? 8.54632   16.80059 -14.99694 1.000 38.97897  ?  57  TRP A NE1 1 
ATOM   732  C CE2 . TRP A  1 57  ? 7.19167   16.94404 -15.11678 1.000 38.32218  ?  57  TRP A CE2 1 
ATOM   733  C CE3 . TRP A  1 57  ? 5.42071   18.17919 -14.02925 1.000 29.91611  ?  57  TRP A CE3 1 
ATOM   734  C CZ2 . TRP A  1 57  ? 6.30439   16.35186 -16.01616 1.000 34.36719  ?  57  TRP A CZ2 1 
ATOM   735  C CZ3 . TRP A  1 57  ? 4.52390   17.57457 -14.94409 1.000 30.35361  ?  57  TRP A CZ3 1 
ATOM   736  C CH2 . TRP A  1 57  ? 4.98281   16.67967 -15.92062 1.000 33.78250  ?  57  TRP A CH2 1 
ATOM   737  N N   . LEU A  1 58  ? 5.97441   21.26511 -13.37631 1.000 26.53740  ?  58  LEU A N   1 
ATOM   738  C CA  . LEU A  1 58  ? 4.91139   21.55535 -14.33544 1.000 27.41955  ?  58  LEU A CA  1 
ATOM   739  C C   . LEU A  1 58  ? 5.21668   22.80421 -15.14782 1.000 30.31771  ?  58  LEU A C   1 
ATOM   740  O O   . LEU A  1 58  ? 5.10629   22.79056 -16.37761 1.000 32.26848  ?  58  LEU A O   1 
ATOM   741  C CB  . LEU A  1 58  ? 3.55663   21.68392 -13.63164 1.000 27.70569  ?  58  LEU A CB  1 
ATOM   742  C CG  . LEU A  1 58  ? 2.36665   22.05980 -14.53561 1.000 29.14780  ?  58  LEU A CG  1 
ATOM   743  C CD1 . LEU A  1 58  ? 2.12174   20.96872 -15.57379 1.000 32.95797  ?  58  LEU A CD1 1 
ATOM   744  C CD2 . LEU A  1 58  ? 1.08799   22.29524 -13.74181 1.000 32.20438  ?  58  LEU A CD2 1 
ATOM   745  N N   A ILE A  1 59  ? 5.56634   23.90979 -14.47877 0.600 28.95696  ?  59  ILE A N   1 
ATOM   746  N N   B ILE A  1 59  ? 5.60094   23.90046 -14.48350 0.400 29.01881  ?  59  ILE A N   1 
ATOM   747  C CA  A ILE A  1 59  ? 5.72558   25.14012 -15.24700 0.600 34.55248  ?  59  ILE A CA  1 
ATOM   748  C CA  B ILE A  1 59  ? 5.83311   25.12937 -15.23696 0.400 34.44133  ?  59  ILE A CA  1 
ATOM   749  C C   A ILE A  1 59  ? 6.97729   25.08960 -16.10191 0.600 30.53391  ?  59  ILE A C   1 
ATOM   750  C C   B ILE A  1 59  ? 7.00688   24.95965 -16.19276 0.400 31.28902  ?  59  ILE A C   1 
ATOM   751  O O   A ILE A  1 59  ? 7.03160   25.72276 -17.15911 0.600 36.91698  ?  59  ILE A O   1 
ATOM   752  O O   B ILE A  1 59  ? 6.96989   25.44440 -17.32847 0.400 33.94583  ?  59  ILE A O   1 
ATOM   753  C CB  A ILE A  1 59  ? 5.61782   26.42248 -14.40148 0.600 38.04147  ?  59  ILE A CB  1 
ATOM   754  C CB  B ILE A  1 59  ? 5.97264   26.36401 -14.32316 0.400 37.25771  ?  59  ILE A CB  1 
ATOM   755  C CG1 A ILE A  1 59  ? 6.53339   26.35457 -13.18566 0.600 26.57206  ?  59  ILE A CG1 1 
ATOM   756  C CG1 B ILE A  1 59  ? 7.27557   26.31691 -13.52799 0.400 34.29439  ?  59  ILE A CG1 1 
ATOM   757  C CG2 A ILE A  1 59  ? 4.16914   26.68104 -13.99071 0.600 27.41290  ?  59  ILE A CG2 1 
ATOM   758  C CG2 B ILE A  1 59  ? 4.75676   26.50553 -13.39587 0.400 31.17827  ?  59  ILE A CG2 1 
ATOM   759  C CD1 A ILE A  1 59  ? 6.59111   27.65646 -12.42292 0.600 40.45256  ?  59  ILE A CD1 1 
ATOM   760  C CD1 B ILE A  1 59  ? 7.55197   27.57327 -12.74750 0.400 32.43799  ?  59  ILE A CD1 1 
ATOM   761  N N   A ILE A  1 60  ? 7.98872   24.32262 -15.68998 0.600 31.55137  ?  60  ILE A N   1 
ATOM   762  N N   B ILE A  1 60  ? 8.04207   24.22645 -15.77509 0.400 31.94057  ?  60  ILE A N   1 
ATOM   763  C CA  A ILE A  1 60  ? 9.13399   24.09532 -16.57025 0.600 35.15965  ?  60  ILE A CA  1 
ATOM   764  C CA  B ILE A  1 60  ? 9.21917   24.05691 -16.62580 0.400 34.85249  ?  60  ILE A CA  1 
ATOM   765  C C   A ILE A  1 60  ? 8.73395   23.21199 -17.74651 0.600 37.34042  ?  60  ILE A C   1 
ATOM   766  C C   B ILE A  1 60  ? 8.90246   23.16022 -17.81637 0.400 38.17495  ?  60  ILE A C   1 
ATOM   767  O O   A ILE A  1 60  ? 9.10969   23.47445 -18.89608 0.600 40.10736  ?  60  ILE A O   1 
ATOM   768  O O   B ILE A  1 60  ? 9.12422   23.53787 -18.97338 0.400 40.12752  ?  60  ILE A O   1 
ATOM   769  C CB  A ILE A  1 60  ? 10.31852  23.50077 -15.78757 0.600 35.71818  ?  60  ILE A CB  1 
ATOM   770  C CB  B ILE A  1 60  ? 10.40747  23.52005 -15.80913 0.400 35.75872  ?  60  ILE A CB  1 
ATOM   771  C CG1 A ILE A  1 60  ? 10.79426  24.46715 -14.70975 0.600 32.91780  ?  60  ILE A CG1 1 
ATOM   772  C CG1 B ILE A  1 60  ? 10.86393  24.55105 -14.78079 0.400 33.08726  ?  60  ILE A CG1 1 
ATOM   773  C CG2 A ILE A  1 60  ? 11.45759  23.13812 -16.74314 0.600 36.08649  ?  60  ILE A CG2 1 
ATOM   774  C CG2 B ILE A  1 60  ? 11.54970  23.12280 -16.73941 0.400 36.13037  ?  60  ILE A CG2 1 
ATOM   775  C CD1 A ILE A  1 60  ? 11.81386  23.86337 -13.77176 0.600 36.84565  ?  60  ILE A CD1 1 
ATOM   776  C CD1 B ILE A  1 60  ? 11.87520  24.00911 -13.79479 0.400 36.97830  ?  60  ILE A CD1 1 
ATOM   777  N N   A THR A  1 61  ? 7.97202   22.14392 -17.47789 0.600 33.22638  ?  61  THR A N   1 
ATOM   778  N N   B THR A  1 61  ? 8.39166   21.95342 -17.55150 0.400 37.71717  ?  61  THR A N   1 
ATOM   779  C CA  A THR A  1 61  ? 7.65387   21.18882 -18.53750 0.600 35.22582  ?  61  THR A CA  1 
ATOM   780  C CA  B THR A  1 61  ? 8.22924   20.97243 -18.62032 0.400 36.31176  ?  61  THR A CA  1 
ATOM   781  C C   A THR A  1 61  ? 6.70223   21.79578 -19.55997 0.600 42.35941  ?  61  THR A C   1 
ATOM   782  C C   B THR A  1 61  ? 7.16845   21.40341 -19.62135 0.400 40.67860  ?  61  THR A C   1 
ATOM   783  O O   A THR A  1 61  ? 6.82765   21.53501 -20.76305 0.600 48.89436  ?  61  THR A O   1 
ATOM   784  O O   B THR A  1 61  ? 7.32815   21.18931 -20.82662 0.400 48.12663  ?  61  THR A O   1 
ATOM   785  C CB  A THR A  1 61  ? 7.08062   19.90064 -17.94057 0.600 39.71901  ?  61  THR A CB  1 
ATOM   786  C CB  B THR A  1 61  ? 7.90056   19.60158 -18.03792 0.400 42.82938  ?  61  THR A CB  1 
ATOM   787  O OG1 A THR A  1 61  ? 8.06980   19.27395 -17.10425 0.600 27.52964  ?  61  THR A OG1 1 
ATOM   788  O OG1 B THR A  1 61  ? 6.86348   19.73665 -17.05771 0.400 47.67078  ?  61  THR A OG1 1 
ATOM   789  C CG2 A THR A  1 61  ? 6.65170   18.92403 -19.04008 0.600 31.38200  ?  61  THR A CG2 1 
ATOM   790  C CG2 B THR A  1 61  ? 9.13499   18.99579 -17.39491 0.400 47.02204  ?  61  THR A CG2 1 
ATOM   791  N N   A LEU A  1 62  ? 5.76148   22.63087 -19.10572 0.600 35.39947  ?  62  LEU A N   1 
ATOM   792  N N   B LEU A  1 62  ? 6.08035   22.01242 -19.14719 0.400 41.38405  ?  62  LEU A N   1 
ATOM   793  C CA  A LEU A  1 62  ? 4.77898   23.22460 -20.00851 0.600 49.72233  ?  62  LEU A CA  1 
ATOM   794  C CA  B LEU A  1 62  ? 5.04611   22.47017 -20.06762 0.400 45.83398  ?  62  LEU A CA  1 
ATOM   795  C C   A LEU A  1 62  ? 5.39933   24.16678 -21.03577 0.600 53.61300  ?  62  LEU A C   1 
ATOM   796  C C   B LEU A  1 62  ? 5.58064   23.55391 -20.99790 0.400 52.88491  ?  62  LEU A C   1 
ATOM   797  O O   A LEU A  1 62  ? 4.67002   24.67168 -21.89736 0.600 61.05883  ?  62  LEU A O   1 
ATOM   798  O O   B LEU A  1 62  ? 5.25297   23.57485 -22.18967 0.400 56.51956  ?  62  LEU A O   1 
ATOM   799  C CB  A LEU A  1 62  ? 3.68047   23.95414 -19.22257 0.600 51.00698  ?  62  LEU A CB  1 
ATOM   800  C CB  B LEU A  1 62  ? 3.82819   22.96723 -19.28709 0.400 43.26375  ?  62  LEU A CB  1 
ATOM   801  C CG  A LEU A  1 62  ? 2.56816   23.12799 -18.56318 0.600 42.43327  ?  62  LEU A CG  1 
ATOM   802  C CD1 A LEU A  1 62  ? 1.74799   23.99830 -17.62797 0.600 35.73154  ?  62  LEU A CD1 1 
ATOM   803  C CD2 A LEU A  1 62  ? 1.66781   22.47129 -19.58932 0.600 31.33929  ?  62  LEU A CD2 1 
ATOM   804  N N   A GLN A  1 63  ? 6.70921   24.43012 -20.95888 0.600 50.32338  ?  63  GLN A N   1 
ATOM   805  N N   B GLN A  1 63  ? 6.42380   24.45193 -20.47458 0.400 49.81525  ?  63  GLN A N   1 
ATOM   806  C CA  A GLN A  1 63  ? 7.37482   25.18307 -22.01929 0.600 57.21822  ?  63  GLN A CA  1 
ATOM   807  C CA  B GLN A  1 63  ? 6.97719   25.52966 -21.28914 0.400 52.11545  ?  63  GLN A CA  1 
ATOM   808  C C   A GLN A  1 63  ? 7.39653   24.39356 -23.32262 0.600 62.43165  ?  63  GLN A C   1 
ATOM   809  C C   B GLN A  1 63  ? 7.83884   25.01346 -22.43827 0.400 59.02410  ?  63  GLN A C   1 
ATOM   810  O O   A GLN A  1 63  ? 7.06156   24.92662 -24.38571 0.600 63.17134  ?  63  GLN A O   1 
ATOM   811  O O   B GLN A  1 63  ? 8.04148   25.73642 -23.41985 0.400 66.35317  ?  63  GLN A O   1 
ATOM   812  C CB  A GLN A  1 63  ? 8.80751   25.51727 -21.60938 0.600 56.46559  ?  63  GLN A CB  1 
ATOM   813  C CB  B GLN A  1 63  ? 7.75205   26.52265 -20.41550 0.400 45.18710  ?  63  GLN A CB  1 
ATOM   814  C CG  A GLN A  1 63  ? 8.94379   26.33835 -20.35349 0.600 48.66095  ?  63  GLN A CG  1 
ATOM   815  C CG  B GLN A  1 63  ? 6.94651   27.75563 -20.02669 0.400 47.62869  ?  63  GLN A CG  1 
ATOM   816  C CD  A GLN A  1 63  ? 10.37687  26.37798 -19.89062 0.600 51.95808  ?  63  GLN A CD  1 
ATOM   817  C CD  B GLN A  1 63  ? 7.13564   28.15233 -18.57321 0.400 43.94249  ?  63  GLN A CD  1 
ATOM   818  O OE1 A GLN A  1 63  ? 10.94015  27.45143 -19.67542 0.600 64.62618  ?  63  GLN A OE1 1 
ATOM   819  O OE1 B GLN A  1 63  ? 6.21158   28.64076 -17.92973 0.400 45.33341  ?  63  GLN A OE1 1 
ATOM   820  N NE2 A GLN A  1 63  ? 10.99068  25.20129 -19.76023 0.600 36.11841  ?  63  GLN A NE2 1 
ATOM   821  N NE2 B GLN A  1 63  ? 8.33343   27.93552 -18.04864 0.400 49.31561  ?  63  GLN A NE2 1 
ATOM   822  N N   A SER A  1 64  ? 7.80461   23.12821 -23.26182 0.600 71.17659  ?  64  SER A N   1 
ATOM   823  N N   B SER A  1 64  ? 8.34148   23.78021 -22.35185 0.400 62.14488  ?  64  SER A N   1 
ATOM   824  C CA  A SER A  1 64  ? 7.87143   22.27869 -24.44235 0.600 72.58250  ?  64  SER A CA  1 
ATOM   825  C CA  B SER A  1 64  ? 9.15023   23.20689 -23.42094 0.400 67.13238  ?  64  SER A CA  1 
ATOM   826  C C   A SER A  1 64  ? 6.88972   21.12268 -24.30471 0.600 67.49754  ?  64  SER A C   1 
ATOM   827  C C   B SER A  1 64  ? 8.68155   21.84060 -23.91670 0.400 71.68973  ?  64  SER A C   1 
ATOM   828  O O   A SER A  1 64  ? 7.29331   19.95944 -24.21036 0.600 67.01941  ?  64  SER A O   1 
ATOM   829  O O   B SER A  1 64  ? 9.22213   21.35209 -24.91637 0.400 75.53541  ?  64  SER A O   1 
ATOM   830  C CB  A SER A  1 64  ? 9.29681   21.76181 -24.63700 0.600 72.59565  ?  64  SER A CB  1 
ATOM   831  C CB  B SER A  1 64  ? 10.63175  23.13083 -23.00976 0.400 66.98420  ?  64  SER A CB  1 
ATOM   832  O OG  A SER A  1 64  ? 9.77103   21.13712 -23.45507 0.600 85.69600  ?  64  SER A OG  1 
ATOM   833  O OG  B SER A  1 64  ? 10.79351  22.42578 -21.79204 0.400 64.14648  ?  64  SER A OG  1 
ATOM   834  N N   A ILE A  1 65  ? 5.59620   21.43395 -24.28732 0.600 60.02298  ?  65  ILE A N   1 
ATOM   835  N N   B ILE A  1 65  ? 7.70572   21.21098 -23.25984 0.400 63.99448  ?  65  ILE A N   1 
ATOM   836  C CA  A ILE A  1 65  ? 4.56014   20.42674 -24.06413 0.600 74.54159  ?  65  ILE A CA  1 
ATOM   837  C CA  B ILE A  1 65  ? 7.19083   19.89911 -23.64100 0.400 66.46809  ?  65  ILE A CA  1 
ATOM   838  C C   A ILE A  1 65  ? 4.34162   19.66469 -25.36959 0.600 67.24609  ?  65  ILE A C   1 
ATOM   839  C C   B ILE A  1 65  ? 5.67096   19.91055 -23.50331 0.400 70.13769  ?  65  ILE A C   1 
ATOM   840  O O   A ILE A  1 65  ? 3.69902   20.15977 -26.29585 0.600 60.75035  ?  65  ILE A O   1 
ATOM   841  O O   B ILE A  1 65  ? 5.06555   20.93548 -23.17869 0.400 59.06937  ?  65  ILE A O   1 
ATOM   842  C CB  A ILE A  1 65  ? 3.26352   21.04029 -23.53218 0.600 68.38672  ?  65  ILE A CB  1 
ATOM   843  C CB  B ILE A  1 65  ? 7.81403   18.75898 -22.80940 0.400 59.05807  ?  65  ILE A CB  1 
ATOM   844  N N   A ASN A  1 66  ? 4.88204   18.44879 -25.44148 0.600 77.02343  ?  66  ASN A N   1 
ATOM   845  N N   B ASN A  1 66  ? 5.04946   18.75105 -23.73937 0.400 79.78669  ?  66  ASN A N   1 
ATOM   846  C CA  A ASN A  1 66  ? 4.65679   17.56614 -26.57469 0.600 73.53350  ?  66  ASN A CA  1 
ATOM   847  C CA  B ASN A  1 66  ? 3.59444   18.66002 -23.81312 0.400 67.05909  ?  66  ASN A CA  1 
ATOM   848  C C   A ASN A  1 66  ? 3.60233   16.50347 -26.30057 0.600 71.34771  ?  66  ASN A C   1 
ATOM   849  C C   B ASN A  1 66  ? 3.09829   17.32423 -23.27414 0.400 65.81880  ?  66  ASN A C   1 
ATOM   850  O O   A ASN A  1 66  ? 2.98625   16.00945 -27.25064 0.600 82.40097  ?  66  ASN A O   1 
ATOM   851  O O   B ASN A  1 66  ? 3.52699   16.26308 -23.73774 0.400 71.31160  ?  66  ASN A O   1 
ATOM   852  C CB  A ASN A  1 66  ? 5.97175   16.89100 -26.98961 0.600 72.24051  ?  66  ASN A CB  1 
ATOM   853  C CB  B ASN A  1 66  ? 3.10938   18.84366 -25.25766 0.400 59.33043  ?  66  ASN A CB  1 
ATOM   854  C CG  A ASN A  1 66  ? 5.81011   15.99670 -28.19505 0.600 66.86263  ?  66  ASN A CG  1 
ATOM   855  O OD1 A ASN A  1 66  ? 6.04823   14.79594 -28.12441 0.600 80.12803  ?  66  ASN A OD1 1 
ATOM   856  N ND2 A ASN A  1 66  ? 5.38923   16.58067 -29.31385 0.600 68.17488  ?  66  ASN A ND2 1 
ATOM   857  N N   A GLU A  1 67  ? 3.37862   16.14294 -25.03504 0.600 64.81659  ?  67  GLU A N   1 
ATOM   858  N N   B GLU A  1 67  ? 2.19873   17.39109 -22.28709 0.400 44.59998  ?  67  GLU A N   1 
ATOM   859  C CA  A GLU A  1 67  ? 2.38448   15.13359 -24.70369 0.600 50.77630  ?  67  GLU A CA  1 
ATOM   860  C CA  B GLU A  1 67  ? 1.34455   16.26423 -21.88590 0.400 48.44953  ?  67  GLU A CA  1 
ATOM   861  C C   A GLU A  1 67  ? 1.49516   15.56711 -23.54611 0.600 52.30143  ?  67  GLU A C   1 
ATOM   862  C C   B GLU A  1 67  ? 2.11025   15.05882 -21.33452 0.400 53.68059  ?  67  GLU A C   1 
ATOM   863  O O   A GLU A  1 67  ? 1.58553   16.69167 -23.03810 0.600 47.57045  ?  67  GLU A O   1 
ATOM   864  O O   B GLU A  1 67  ? 1.72450   13.90835 -21.55561 0.400 49.55024  ?  67  GLU A O   1 
ATOM   865  C CB  A GLU A  1 67  ? 3.05203   13.78984 -24.39684 0.600 64.35881  ?  67  GLU A CB  1 
ATOM   866  C CB  B GLU A  1 67  ? 0.37344   15.84881 -22.99004 0.400 41.97239  ?  67  GLU A CB  1 
ATOM   867  N N   A ASP A  1 68  ? 0.62844   14.66020 -23.12960 0.600 40.35050  ?  68  ASP A N   1 
ATOM   868  N N   B ASP A  1 68  ? 3.18684   15.31022 -20.59778 0.400 36.23487  ?  68  ASP A N   1 
ATOM   869  C CA  A ASP A  1 68  ? -0.38678  14.93137 -22.12597 0.600 34.80973  ?  68  ASP A CA  1 
ATOM   870  C CA  B ASP A  1 68  ? 3.72242   14.29585 -19.69884 0.400 42.14446  ?  68  ASP A CA  1 
ATOM   871  C C   A ASP A  1 68  ? 0.20169   14.52608 -20.77871 0.600 33.12189  ?  68  ASP A C   1 
ATOM   872  C C   B ASP A  1 68  ? 3.02534   14.33589 -18.34768 0.400 41.55245  ?  68  ASP A C   1 
ATOM   873  O O   A ASP A  1 68  ? 0.29926   13.34151 -20.45819 0.600 34.27858  ?  68  ASP A O   1 
ATOM   874  O O   B ASP A  1 68  ? 3.38863   13.58271 -17.43739 0.400 34.90286  ?  68  ASP A O   1 
ATOM   875  C CB  A ASP A  1 68  ? -1.62719  14.13623 -22.50491 0.600 32.48284  ?  68  ASP A CB  1 
ATOM   876  C CB  B ASP A  1 68  ? 5.23686   14.47836 -19.52584 0.400 57.47441  ?  68  ASP A CB  1 
ATOM   877  C CG  A ASP A  1 68  ? -2.72931  14.23174 -21.49470 0.600 28.44708  ?  68  ASP A CG  1 
ATOM   878  O OD1 A ASP A  1 68  ? -2.51309  14.70165 -20.36084 0.600 27.48563  ?  68  ASP A OD1 1 
ATOM   879  O OD2 A ASP A  1 68  ? -3.84001  13.81259 -21.86742 0.600 31.95017  -1 68  ASP A OD2 1 
ATOM   880  N N   A ILE A  1 69  ? 0.60126   15.51685 -19.98478 0.600 33.96947  ?  69  ILE A N   1 
ATOM   881  N N   B ILE A  1 69  ? 1.99572   15.17495 -18.22418 0.400 36.55255  ?  69  ILE A N   1 
ATOM   882  C CA  A ILE A  1 69  ? 1.26645   15.24378 -18.71140 0.600 34.44126  ?  69  ILE A CA  1 
ATOM   883  C CA  B ILE A  1 69  ? 1.49537   15.57986 -16.92421 0.400 32.47355  ?  69  ILE A CA  1 
ATOM   884  C C   A ILE A  1 69  ? 0.32113   15.21277 -17.51117 0.600 28.14366  ?  69  ILE A C   1 
ATOM   885  C C   B ILE A  1 69  ? 0.81265   14.44733 -16.17423 0.400 27.41282  ?  69  ILE A C   1 
ATOM   886  O O   A ILE A  1 69  ? 0.77111   15.29845 -16.36332 0.600 26.97275  ?  69  ILE A O   1 
ATOM   887  O O   B ILE A  1 69  ? 0.69122   14.51936 -14.95084 0.400 25.44881  ?  69  ILE A O   1 
ATOM   888  C CB  A ILE A  1 69  ? 2.46255   16.18753 -18.46762 0.600 39.75149  ?  69  ILE A CB  1 
ATOM   889  C CB  B ILE A  1 69  ? 0.58045   16.81374 -17.06580 0.400 42.46803  ?  69  ILE A CB  1 
ATOM   890  C CG1 A ILE A  1 69  ? 2.12637   17.63808 -18.81977 0.600 40.38494  ?  69  ILE A CG1 1 
ATOM   891  C CG2 A ILE A  1 69  ? 3.67620   15.72591 -19.27832 0.600 40.11318  ?  69  ILE A CG2 1 
ATOM   892  C CD1 A ILE A  1 69  ? 1.08205   18.26844 -17.96749 0.600 27.46205  ?  69  ILE A CD1 1 
ATOM   893  N N   A THR A  1 70  ? -0.98626  15.08680 -17.75005 0.600 21.84091  ?  70  THR A N   1 
ATOM   894  N N   B THR A  1 70  ? 0.36159   13.39724 -16.86204 0.400 33.88441  ?  70  THR A N   1 
ATOM   895  C CA  A THR A  1 70  ? -1.92694  15.03064 -16.63143 0.600 22.98665  ?  70  THR A CA  1 
ATOM   896  C CA  B THR A  1 70  ? -0.44949  12.38649 -16.18788 0.400 30.73226  ?  70  THR A CA  1 
ATOM   897  C C   A THR A  1 70  ? -1.59037  13.89433 -15.66425 0.600 19.77647  ?  70  THR A C   1 
ATOM   898  C C   B THR A  1 70  ? 0.37549   11.58393 -15.18670 0.400 26.96799  ?  70  THR A C   1 
ATOM   899  O O   A THR A  1 70  ? -1.65485  14.05993 -14.44380 0.600 22.95896  ?  70  THR A O   1 
ATOM   900  O O   B THR A  1 70  ? -0.04179  11.38575 -14.04099 0.400 24.90612  ?  70  THR A O   1 
ATOM   901  C CB  A THR A  1 70  ? -3.36010  14.87373 -17.14252 0.600 31.91924  ?  70  THR A CB  1 
ATOM   902  C CB  B THR A  1 70  ? -1.12272  11.47089 -17.21092 0.400 39.93410  ?  70  THR A CB  1 
ATOM   903  O OG1 A THR A  1 70  ? -3.60639  15.81436 -18.20021 0.600 27.88034  ?  70  THR A OG1 1 
ATOM   904  C CG2 A THR A  1 70  ? -4.33645  15.11069 -16.01979 0.600 27.50660  ?  70  THR A CG2 1 
ATOM   905  N N   A TYR A  1 71  ? -1.21404  12.73625 -16.20344 0.600 27.02558  ?  71  TYR A N   1 
ATOM   906  N N   B TYR A  1 71  ? 1.55149   11.11540 -15.59697 0.400 29.99315  ?  71  TYR A N   1 
ATOM   907  C CA  A TYR A  1 71  ? -0.95374  11.56164 -15.38068 0.600 24.86461  ?  71  TYR A CA  1 
ATOM   908  C CA  B TYR A  1 71  ? 2.35815   10.29508 -14.70074 0.400 29.29089  ?  71  TYR A CA  1 
ATOM   909  C C   A TYR A  1 71  ? 0.16894   11.79213 -14.36764 0.600 24.04745  ?  71  TYR A C   1 
ATOM   910  C C   B TYR A  1 71  ? 2.85818   11.08773 -13.49267 0.400 33.08564  ?  71  TYR A C   1 
ATOM   911  O O   A TYR A  1 71  ? 0.18716   11.14502 -13.31338 0.600 22.05634  ?  71  TYR A O   1 
ATOM   912  O O   B TYR A  1 71  ? 3.09840   10.50440 -12.42775 0.400 40.05750  ?  71  TYR A O   1 
ATOM   913  C CB  A TYR A  1 71  ? -0.61925  10.37618 -16.28761 0.600 24.63797  ?  71  TYR A CB  1 
ATOM   914  C CB  B TYR A  1 71  ? 3.51746   9.66104  -15.47227 0.400 44.10233  ?  71  TYR A CB  1 
ATOM   915  C CG  A TYR A  1 71  ? 0.78017   10.44039 -16.87507 0.600 25.16053  ?  71  TYR A CG  1 
ATOM   916  C CD1 A TYR A  1 71  ? 1.04861   11.15626 -18.04181 0.600 27.87900  ?  71  TYR A CD1 1 
ATOM   917  C CD2 A TYR A  1 71  ? 1.83608   9.78837  -16.25036 0.600 23.80933  ?  71  TYR A CD2 1 
ATOM   918  C CE1 A TYR A  1 71  ? 2.34669   11.21451 -18.56875 0.600 29.69423  ?  71  TYR A CE1 1 
ATOM   919  C CE2 A TYR A  1 71  ? 3.12409   9.83503  -16.76883 0.600 24.16411  ?  71  TYR A CE2 1 
ATOM   920  C CZ  A TYR A  1 71  ? 3.37213   10.54858 -17.91830 0.600 40.49272  ?  71  TYR A CZ  1 
ATOM   921  O OH  A TYR A  1 71  ? 4.66559   10.59115 -18.40672 0.600 36.07729  ?  71  TYR A OH  1 
ATOM   922  N N   A VAL A  1 72  ? 1.10375   12.70579 -14.64995 0.600 22.98298  ?  72  VAL A N   1 
ATOM   923  N N   B VAL A  1 72  ? 3.02067   12.40413 -13.62485 0.400 24.68483  ?  72  VAL A N   1 
ATOM   924  C CA  A VAL A  1 72  ? 2.17275   12.96693 -13.68183 0.600 24.95230  ?  72  VAL A CA  1 
ATOM   925  C CA  B VAL A  1 72  ? 3.58238   13.18861 -12.52523 0.400 34.14125  ?  72  VAL A CA  1 
ATOM   926  C C   A VAL A  1 72  ? 1.62798   13.43708 -12.33535 0.600 25.32122  ?  72  VAL A C   1 
ATOM   927  C C   B VAL A  1 72  ? 2.49868   13.74943 -11.61487 0.400 24.70490  ?  72  VAL A C   1 
ATOM   928  O O   A VAL A  1 72  ? 2.25514   13.19937 -11.29173 0.600 21.51341  ?  72  VAL A O   1 
ATOM   929  O O   B VAL A  1 72  ? 2.65482   13.75134 -10.38846 0.400 25.00494  ?  72  VAL A O   1 
ATOM   930  C CB  A VAL A  1 72  ? 3.23314   13.91156 -14.28702 0.600 25.50282  ?  72  VAL A CB  1 
ATOM   931  C CB  B VAL A  1 72  ? 4.52816   14.28178 -13.05573 0.400 27.96663  ?  72  VAL A CB  1 
ATOM   932  C CG1 A VAL A  1 72  ? 4.34563   14.22220 -13.30880 0.600 27.01448  ?  72  VAL A CG1 1 
ATOM   933  C CG1 B VAL A  1 72  ? 5.20684   14.98824 -11.89803 0.400 41.88113  ?  72  VAL A CG1 1 
ATOM   934  C CG2 A VAL A  1 72  ? 3.80787   13.29627 -15.55426 0.600 27.05888  ?  72  VAL A CG2 1 
ATOM   935  C CG2 B VAL A  1 72  ? 5.54872   13.66089 -13.98975 0.400 43.63343  ?  72  VAL A CG2 1 
ATOM   936  N N   A ARG A  1 73  ? 0.43683   14.05902 -12.31195 0.600 21.17097  ?  73  ARG A N   1 
ATOM   937  N N   B ARG A  1 73  ? 1.40057   14.23458 -12.20070 0.400 23.97537  ?  73  ARG A N   1 
ATOM   938  C CA  A ARG A  1 73  ? -0.11505  14.53209 -11.03265 0.600 23.26404  ?  73  ARG A CA  1 
ATOM   939  C CA  B ARG A  1 73  ? 0.21430   14.54932 -11.41573 0.400 25.28185  ?  73  ARG A CA  1 
ATOM   940  C C   A ARG A  1 73  ? -0.33846  13.39363 -10.03880 0.600 19.67745  ?  73  ARG A C   1 
ATOM   941  C C   B ARG A  1 73  ? -0.19428  13.36623 -10.55335 0.400 21.09375  ?  73  ARG A C   1 
ATOM   942  O O   A ARG A  1 73  ? -0.35508  13.62296 -8.82095  0.600 21.93667  ?  73  ARG A O   1 
ATOM   943  O O   B ARG A  1 73  ? -0.36046  13.50712 -9.33914  0.400 20.76632  ?  73  ARG A O   1 
ATOM   944  C CB  A ARG A  1 73  ? -1.44730  15.26162 -11.22496 0.600 23.09815  ?  73  ARG A CB  1 
ATOM   945  C CB  B ARG A  1 73  ? -0.93738  14.93469 -12.33704 0.400 28.98618  ?  73  ARG A CB  1 
ATOM   946  C CG  A ARG A  1 73  ? -1.42218  16.51870 -12.07431 0.600 24.97566  ?  73  ARG A CG  1 
ATOM   947  C CG  B ARG A  1 73  ? -2.23235  15.22593 -11.61461 0.400 27.90477  ?  73  ARG A CG  1 
ATOM   948  C CD  A ARG A  1 73  ? -2.82743  17.15587 -12.16404 0.600 22.96331  ?  73  ARG A CD  1 
ATOM   949  C CD  B ARG A  1 73  ? -2.23861  16.65789 -11.08277 0.400 24.19269  ?  73  ARG A CD  1 
ATOM   950  N NE  A ARG A  1 73  ? -2.83781  18.27877 -13.09059 0.600 21.03278  ?  73  ARG A NE  1 
ATOM   951  N NE  B ARG A  1 73  ? -2.21836  17.64878 -12.15867 0.400 27.40587  ?  73  ARG A NE  1 
ATOM   952  C CZ  A ARG A  1 73  ? -2.53096  19.53255 -12.78399 0.600 25.50702  ?  73  ARG A CZ  1 
ATOM   953  C CZ  B ARG A  1 73  ? -2.28756  18.96068 -11.96878 0.400 20.80565  ?  73  ARG A CZ  1 
ATOM   954  N NH1 A ARG A  1 73  ? -2.23496  19.89185 -11.54173 0.600 20.60743  ?  73  ARG A NH1 1 
ATOM   955  N NH1 B ARG A  1 73  ? -2.42410  19.47726 -10.75762 0.400 22.85598  ?  73  ARG A NH1 1 
ATOM   956  N NH2 A ARG A  1 73  ? -2.51014  20.44763 -13.75136 0.600 23.51083  ?  73  ARG A NH2 1 
ATOM   957  N NH2 B ARG A  1 73  ? -2.18915  19.77743 -13.01850 0.400 22.02868  ?  73  ARG A NH2 1 
ATOM   958  N N   A TYR A  1 74  ? -0.53848  12.16867 -10.53472 0.600 19.20867  ?  74  TYR A N   1 
ATOM   959  N N   B TYR A  1 74  ? -0.35031  12.18342 -11.16273 0.400 16.31657  ?  74  TYR A N   1 
ATOM   960  C CA  A TYR A  1 74  ? -0.75192  11.01810 -9.66616  0.600 15.75686  ?  74  TYR A CA  1 
ATOM   961  C CA  B TYR A  1 74  ? -0.78053  11.01461 -10.39329 0.400 17.83348  ?  74  TYR A CA  1 
ATOM   962  C C   A TYR A  1 74  ? 0.48614   10.69978 -8.82939  0.600 16.39121  ?  74  TYR A C   1 
ATOM   963  C C   B TYR A  1 74  ? 0.26869   10.54528 -9.38731  0.400 24.32622  ?  74  TYR A C   1 
ATOM   964  O O   A TYR A  1 74  ? 0.35831   10.20485 -7.70544  0.600 18.84928  ?  74  TYR A O   1 
ATOM   965  O O   B TYR A  1 74  ? -0.08266  9.92866  -8.37821  0.400 23.06370  ?  74  TYR A O   1 
ATOM   966  C CB  A TYR A  1 74  ? -1.20238  9.80950  -10.50279 0.600 17.60798  ?  74  TYR A CB  1 
ATOM   967  C CB  B TYR A  1 74  ? -1.21694  9.87373  -11.31269 0.400 19.40981  ?  74  TYR A CB  1 
ATOM   968  C CG  A TYR A  1 74  ? -2.64391  9.95028  -10.94009 0.600 16.45000  ?  74  TYR A CG  1 
ATOM   969  C CG  B TYR A  1 74  ? -2.66345  9.99743  -11.73704 0.400 19.09386  ?  74  TYR A CG  1 
ATOM   970  C CD1 A TYR A  1 74  ? -2.98742  10.77445 -12.00721 0.600 22.36085  ?  74  TYR A CD1 1 
ATOM   971  C CD1 B TYR A  1 74  ? -3.66022  9.30651  -11.06447 0.400 21.16543  ?  74  TYR A CD1 1 
ATOM   972  C CD2 A TYR A  1 74  ? -3.66474  9.27901  -10.27222 0.600 20.77718  ?  74  TYR A CD2 1 
ATOM   973  C CD2 B TYR A  1 74  ? -3.03357  10.83243 -12.78233 0.400 18.51178  ?  74  TYR A CD2 1 
ATOM   974  C CE1 A TYR A  1 74  ? -4.31803  10.93220 -12.40081 0.600 21.19257  ?  74  TYR A CE1 1 
ATOM   975  C CE1 B TYR A  1 74  ? -4.99079  9.41980  -11.44138 0.400 21.70718  ?  74  TYR A CE1 1 
ATOM   976  C CE2 A TYR A  1 74  ? -4.98259  9.43124  -10.65134 0.600 18.99944  ?  74  TYR A CE2 1 
ATOM   977  C CE2 B TYR A  1 74  ? -4.36430  10.95178 -13.16915 0.400 23.29405  ?  74  TYR A CE2 1 
ATOM   978  C CZ  A TYR A  1 74  ? -5.30763  10.26354 -11.71476 0.600 21.81687  ?  74  TYR A CZ  1 
ATOM   979  C CZ  B TYR A  1 74  ? -5.33743  10.24211 -12.49336 0.400 19.77853  ?  74  TYR A CZ  1 
ATOM   980  O OH  A TYR A  1 74  ? -6.60649  10.41585 -12.10975 0.600 22.41501  ?  74  TYR A OH  1 
ATOM   981  O OH  B TYR A  1 74  ? -6.66467  10.34385 -12.85413 0.400 25.23012  ?  74  TYR A OH  1 
ATOM   982  N N   A PHE A  1 75  ? 1.68491   10.98211 -9.35989  0.600 23.40676  ?  75  PHE A N   1 
ATOM   983  N N   B PHE A  1 75  ? 1.55301   10.80152 -9.63504  0.400 24.27450  ?  75  PHE A N   1 
ATOM   984  C CA  A PHE A  1 75  ? 2.90301   10.79563 -8.57871  0.600 24.15265  ?  75  PHE A CA  1 
ATOM   985  C CA  B PHE A  1 75  ? 2.55391   10.45837 -8.62897  0.400 24.10518  ?  75  PHE A CA  1 
ATOM   986  C C   A PHE A  1 75  ? 2.95341   11.78338 -7.41778  0.600 23.43544  ?  75  PHE A C   1 
ATOM   987  C C   B PHE A  1 75  ? 2.45233   11.39995 -7.43783  0.400 22.65112  ?  75  PHE A C   1 
ATOM   988  O O   A PHE A  1 75  ? 3.52459   11.48003 -6.35505  0.600 22.72487  ?  75  PHE A O   1 
ATOM   989  O O   B PHE A  1 75  ? 2.44081   10.96007 -6.27688  0.400 26.31737  ?  75  PHE A O   1 
ATOM   990  C CB  A PHE A  1 75  ? 4.13592   10.86524 -9.50516  0.600 23.70416  ?  75  PHE A CB  1 
ATOM   991  C CB  B PHE A  1 75  ? 3.94629   10.51651 -9.25868  0.400 28.64357  ?  75  PHE A CB  1 
ATOM   992  C CG  A PHE A  1 75  ? 4.06403   9.92345  -10.70617 0.600 26.45667  ?  75  PHE A CG  1 
ATOM   993  C CG  B PHE A  1 75  ? 5.07081   10.22744 -8.30383  0.400 35.57123  ?  75  PHE A CG  1 
ATOM   994  C CD1 A PHE A  1 75  ? 3.42705   8.68646  -10.60969 0.600 34.92609  ?  75  PHE A CD1 1 
ATOM   995  C CD1 B PHE A  1 75  ? 5.10994   9.03832  -7.59088  0.400 38.34649  ?  75  PHE A CD1 1 
ATOM   996  C CD2 A PHE A  1 75  ? 4.60676   10.28952 -11.92585 0.600 34.60257  ?  75  PHE A CD2 1 
ATOM   997  C CD2 B PHE A  1 75  ? 6.11043   11.13109 -8.14896  0.400 38.83344  ?  75  PHE A CD2 1 
ATOM   998  C CE1 A PHE A  1 75  ? 3.33927   7.82315  -11.71814 0.600 31.81417  ?  75  PHE A CE1 1 
ATOM   999  C CE1 B PHE A  1 75  ? 6.15511   8.76861  -6.72219  0.400 40.26549  ?  75  PHE A CE1 1 
ATOM   1000 C CE2 A PHE A  1 75  ? 4.52731   9.43102  -13.02555 0.600 40.89303  ?  75  PHE A CE2 1 
ATOM   1001 C CE2 B PHE A  1 75  ? 7.15439   10.86081 -7.28838  0.400 35.59565  ?  75  PHE A CE2 1 
ATOM   1002 C CZ  A PHE A  1 75  ? 3.88580   8.20371  -12.91823 0.600 31.55873  ?  75  PHE A CZ  1 
ATOM   1003 C CZ  B PHE A  1 75  ? 7.17257   9.68179  -6.57516  0.400 27.13403  ?  75  PHE A CZ  1 
ATOM   1004 N N   A ASP A  1 76  ? 2.33787   12.95630 -7.59143  0.600 22.06648  ?  76  ASP A N   1 
ATOM   1005 N N   B ASP A  1 76  ? 2.35622   12.70419 -7.71342  0.400 21.70723  ?  76  ASP A N   1 
ATOM   1006 C CA  A ASP A  1 76  ? 2.02635   13.83448 -6.46833  0.600 22.58832  ?  76  ASP A CA  1 
ATOM   1007 C CA  B ASP A  1 76  ? 2.19299   13.69124 -6.65105  0.400 23.88077  ?  76  ASP A CA  1 
ATOM   1008 C C   A ASP A  1 76  ? 1.00227   13.18196 -5.52917  0.600 21.27256  ?  76  ASP A C   1 
ATOM   1009 C C   B ASP A  1 76  ? 0.90207   13.45390 -5.87211  0.400 23.05961  ?  76  ASP A C   1 
ATOM   1010 O O   A ASP A  1 76  ? 1.30102   12.90574 -4.36191  0.600 19.94920  ?  76  ASP A O   1 
ATOM   1011 O O   B ASP A  1 76  ? 0.83673   13.71456 -4.66349  0.400 25.45915  ?  76  ASP A O   1 
ATOM   1012 C CB  A ASP A  1 76  ? 1.53375   15.17120 -7.05752  0.600 23.47105  ?  76  ASP A CB  1 
ATOM   1013 C CB  B ASP A  1 76  ? 2.20781   15.09032 -7.26508  0.400 23.76467  ?  76  ASP A CB  1 
ATOM   1014 C CG  A ASP A  1 76  ? 0.98405   16.13974 -6.03182  0.600 23.92301  ?  76  ASP A CG  1 
ATOM   1015 C CG  B ASP A  1 76  ? 2.73244   16.14668 -6.30675  0.400 28.79873  ?  76  ASP A CG  1 
ATOM   1016 O OD1 A ASP A  1 76  ? 0.48613   15.73080 -4.97599  0.600 27.34803  ?  76  ASP A OD1 1 
ATOM   1017 O OD1 B ASP A  1 76  ? 3.97045   16.22701 -6.13390  0.400 28.63612  ?  76  ASP A OD1 1 
ATOM   1018 O OD2 A ASP A  1 76  ? 1.01524   17.35782 -6.30793  0.600 28.51917  -1 76  ASP A OD2 1 
ATOM   1019 O OD2 B ASP A  1 76  ? 1.93147   16.90349 -5.73611  0.400 26.77311  -1 76  ASP A OD2 1 
ATOM   1020 N N   A TRP A  1 77  ? -0.21441  12.93152 -6.03834  0.600 19.50184  ?  77  TRP A N   1 
ATOM   1021 N N   B TRP A  1 77  ? -0.13922  12.96016 -6.55326  0.400 18.70657  ?  77  TRP A N   1 
ATOM   1022 C CA  A TRP A  1 77  ? -1.35904  12.51910 -5.22159  0.600 20.63565  ?  77  TRP A CA  1 
ATOM   1023 C CA  B TRP A  1 77  ? -1.39161  12.64022 -5.87014  0.400 20.41975  ?  77  TRP A CA  1 
ATOM   1024 C C   A TRP A  1 77  ? -1.11536  11.19911 -4.47397  0.600 16.85640  ?  77  TRP A C   1 
ATOM   1025 C C   B TRP A  1 77  ? -1.21868  11.51272 -4.85321  0.400 19.03033  ?  77  TRP A C   1 
ATOM   1026 O O   A TRP A  1 77  ? -1.55677  11.05249 -3.32134  0.600 16.58665  ?  77  TRP A O   1 
ATOM   1027 O O   B TRP A  1 77  ? -1.77492  11.58655 -3.74757  0.400 18.70507  ?  77  TRP A O   1 
ATOM   1028 C CB  A TRP A  1 77  ? -2.60520  12.38476 -6.10998  0.600 15.87692  ?  77  TRP A CB  1 
ATOM   1029 C CB  B TRP A  1 77  ? -2.45226  12.23891 -6.88544  0.400 17.91950  ?  77  TRP A CB  1 
ATOM   1030 C CG  A TRP A  1 77  ? -3.02858  13.64404 -6.82464  0.600 16.28647  ?  77  TRP A CG  1 
ATOM   1031 C CG  B TRP A  1 77  ? -3.13720  13.37980 -7.56509  0.400 18.87732  ?  77  TRP A CG  1 
ATOM   1032 C CD1 A TRP A  1 77  ? -2.62075  14.92389 -6.55801  0.600 18.32727  ?  77  TRP A CD1 1 
ATOM   1033 C CD1 B TRP A  1 77  ? -2.83778  14.71052 -7.46053  0.400 17.40330  ?  77  TRP A CD1 1 
ATOM   1034 C CD2 A TRP A  1 77  ? -3.93597  13.73413 -7.92991  0.600 19.22551  ?  77  TRP A CD2 1 
ATOM   1035 C CD2 B TRP A  1 77  ? -4.25284  13.28608 -8.45510  0.400 17.47756  ?  77  TRP A CD2 1 
ATOM   1036 N NE1 A TRP A  1 77  ? -3.22776  15.80590 -7.42398  0.600 20.02277  ?  77  TRP A NE1 1 
ATOM   1037 N NE1 B TRP A  1 77  ? -3.70566  15.45324 -8.23576  0.400 20.43425  ?  77  TRP A NE1 1 
ATOM   1038 C CE2 A TRP A  1 77  ? -4.04034  15.10206 -8.27908  0.600 22.08053  ?  77  TRP A CE2 1 
ATOM   1039 C CE2 B TRP A  1 77  ? -4.58160  14.60168 -8.85802  0.400 15.30888  ?  77  TRP A CE2 1 
ATOM   1040 C CE3 A TRP A  1 77  ? -4.66547  12.78906 -8.66223  0.600 19.51980  ?  77  TRP A CE3 1 
ATOM   1041 C CE3 B TRP A  1 77  ? -5.00228  12.21464 -8.95730  0.400 18.03388  ?  77  TRP A CE3 1 
ATOM   1042 C CZ2 A TRP A  1 77  ? -4.84209  15.54998 -9.34215  0.600 20.23401  ?  77  TRP A CZ2 1 
ATOM   1043 C CZ2 B TRP A  1 77  ? -5.62369  14.87560 -9.73962  0.400 23.17569  ?  77  TRP A CZ2 1 
ATOM   1044 C CZ3 A TRP A  1 77  ? -5.47652  13.23963 -9.72187  0.600 18.87615  ?  77  TRP A CZ3 1 
ATOM   1045 C CZ3 B TRP A  1 77  ? -6.03715  12.48692 -9.82798  0.400 17.00012  ?  77  TRP A CZ3 1 
ATOM   1046 C CH2 A TRP A  1 77  ? -5.54935  14.60677 -10.04985 0.600 24.29095  ?  77  TRP A CH2 1 
ATOM   1047 C CH2 B TRP A  1 77  ? -6.33504  13.80942 -10.21835 0.400 25.69535  ?  77  TRP A CH2 1 
ATOM   1048 N N   A VAL A  1 78  ? -0.43532  10.22939 -5.10317  0.600 19.96129  ?  78  VAL A N   1 
ATOM   1049 N N   B VAL A  1 78  ? -0.43675  10.48334 -5.20252  0.400 19.88926  ?  78  VAL A N   1 
ATOM   1050 C CA  A VAL A  1 78  ? -0.14326  8.97347  -4.40568  0.600 21.21979  ?  78  VAL A CA  1 
ATOM   1051 C CA  B VAL A  1 78  ? -0.35211  9.24837  -4.41612  0.400 22.09299  ?  78  VAL A CA  1 
ATOM   1052 C C   A VAL A  1 78  ? 0.67550   9.23227  -3.14549  0.600 23.41392  ?  78  VAL A C   1 
ATOM   1053 C C   B VAL A  1 78  ? 0.40717   9.45563  -3.10521  0.400 22.20980  ?  78  VAL A C   1 
ATOM   1054 O O   A VAL A  1 78  ? 0.66345   8.42196  -2.20412  0.600 24.12360  ?  78  VAL A O   1 
ATOM   1055 O O   B VAL A  1 78  ? 0.13217   8.77688  -2.10657  0.400 22.02566  ?  78  VAL A O   1 
ATOM   1056 C CB  A VAL A  1 78  ? 0.52043   7.93689  -5.34121  0.600 24.03515  ?  78  VAL A CB  1 
ATOM   1057 C CB  B VAL A  1 78  ? 0.24440   8.11481  -5.28346  0.400 27.75518  ?  78  VAL A CB  1 
ATOM   1058 C CG1 A VAL A  1 78  ? 1.93114   8.36516  -5.70155  0.600 21.23471  ?  78  VAL A CG1 1 
ATOM   1059 C CG1 B VAL A  1 78  ? 1.69332   7.84746  -4.91470  0.400 23.15959  ?  78  VAL A CG1 1 
ATOM   1060 C CG2 A VAL A  1 78  ? 0.50974   6.53887  -4.68670  0.600 25.06741  ?  78  VAL A CG2 1 
ATOM   1061 C CG2 B VAL A  1 78  ? -0.58529  6.83146  -5.18148  0.400 25.08535  ?  78  VAL A CG2 1 
ATOM   1062 N N   . LEU A  1 79  ? 1.38468   10.36442 -3.09292  1.000 21.40152  ?  79  LEU A N   1 
ATOM   1063 C CA  . LEU A  1 79  ? 2.11332   10.73172 -1.88334  1.000 25.45857  ?  79  LEU A CA  1 
ATOM   1064 C C   . LEU A  1 79  ? 1.30892   11.66240 -0.98645  1.000 24.36163  ?  79  LEU A C   1 
ATOM   1065 O O   . LEU A  1 79  ? 1.29965   11.50351 0.24605   1.000 24.47537  ?  79  LEU A O   1 
ATOM   1066 C CB  . LEU A  1 79  ? 3.41310   11.43751 -2.28818  1.000 23.29650  ?  79  LEU A CB  1 
ATOM   1067 C CG  . LEU A  1 79  ? 4.37436   10.58478 -3.12895  1.000 27.07407  ?  79  LEU A CG  1 
ATOM   1068 C CD1 . LEU A  1 79  ? 5.66438   11.32844 -3.40734  1.000 29.67447  ?  79  LEU A CD1 1 
ATOM   1069 C CD2 . LEU A  1 79  ? 4.66405   9.26562  -2.41171  1.000 33.27892  ?  79  LEU A CD2 1 
ATOM   1070 N N   . THR A  1 80  ? 0.64567   12.66033 -1.56576  1.000 21.79195  ?  80  THR A N   1 
ATOM   1071 C CA  . THR A  1 80  ? 0.04288   13.70209 -0.73758  1.000 20.52276  ?  80  THR A CA  1 
ATOM   1072 C C   . THR A  1 80  ? -1.30996  13.29392 -0.18228  1.000 24.22050  ?  80  THR A C   1 
ATOM   1073 O O   . THR A  1 80  ? -1.61246  13.62365 0.97056   1.000 23.10025  ?  80  THR A O   1 
ATOM   1074 C CB  . THR A  1 80  ? -0.13739  15.01498 -1.50605  1.000 22.25501  ?  80  THR A CB  1 
ATOM   1075 O OG1 . THR A  1 80  ? -0.88163  14.75855 -2.71652  1.000 23.26978  ?  80  THR A OG1 1 
ATOM   1076 C CG2 . THR A  1 80  ? 1.22058   15.66194 -1.80111  1.000 26.03188  ?  80  THR A CG2 1 
ATOM   1077 N N   . THR A  1 81  ? -2.14919  12.62231 -0.97560  1.000 20.56198  ?  81  THR A N   1 
ATOM   1078 C CA  . THR A  1 81  ? -3.50030  12.33286 -0.49629  1.000 21.36007  ?  81  THR A CA  1 
ATOM   1079 C C   . THR A  1 81  ? -3.54963  11.42903 0.74153   1.000 20.43581  ?  81  THR A C   1 
ATOM   1080 O O   . THR A  1 81  ? -4.37231  11.70128 1.62843   1.000 21.69051  ?  81  THR A O   1 
ATOM   1081 C CB  . THR A  1 81  ? -4.42246  11.83128 -1.62403  1.000 26.39589  ?  81  THR A CB  1 
ATOM   1082 O OG1 . THR A  1 81  ? -3.95263  10.59752 -2.17782  1.000 20.26121  ?  81  THR A OG1 1 
ATOM   1083 C CG2 . THR A  1 81  ? -4.56159  12.88461 -2.75697  1.000 22.54317  ?  81  THR A CG2 1 
ATOM   1084 N N   . PRO A  1 82  ? -2.70916  10.40475 0.89792   1.000 20.49137  ?  82  PRO A N   1 
ATOM   1085 C CA  . PRO A  1 82  ? -2.76660  9.66182  2.17340   1.000 20.74038  ?  82  PRO A CA  1 
ATOM   1086 C C   . PRO A  1 82  ? -2.37558  10.51957 3.35801   1.000 19.85143  ?  82  PRO A C   1 
ATOM   1087 O O   . PRO A  1 82  ? -2.97870  10.41100 4.44223   1.000 22.31345  ?  82  PRO A O   1 
ATOM   1088 C CB  . PRO A  1 82  ? -1.77872  8.51024  1.97249   1.000 22.64849  ?  82  PRO A CB  1 
ATOM   1089 C CG  . PRO A  1 82  ? -0.96537  8.89692  0.76968   1.000 27.59793  ?  82  PRO A CG  1 
ATOM   1090 C CD  . PRO A  1 82  ? -1.85759  9.71187  -0.08361  1.000 24.51330  ?  82  PRO A CD  1 
ATOM   1091 N N   . VAL A  1 83  ? -1.38196  11.40003 3.17568   1.000 20.59576  ?  83  VAL A N   1 
ATOM   1092 C CA  . VAL A  1 83  ? -1.01072  12.30708 4.26068   1.000 20.54365  ?  83  VAL A CA  1 
ATOM   1093 C C   . VAL A  1 83  ? -2.18184  13.21783 4.61695   1.000 17.82668  ?  83  VAL A C   1 
ATOM   1094 O O   . VAL A  1 83  ? -2.51000  13.40683 5.81456   1.000 21.28693  ?  83  VAL A O   1 
ATOM   1095 C CB  . VAL A  1 83  ? 0.24900   13.10641 3.89340   1.000 22.14881  ?  83  VAL A CB  1 
ATOM   1096 C CG1 . VAL A  1 83  ? 0.54348   14.12497 4.96435   1.000 22.89376  ?  83  VAL A CG1 1 
ATOM   1097 C CG2 . VAL A  1 83  ? 1.44676   12.15389 3.67771   1.000 24.50171  ?  83  VAL A CG2 1 
ATOM   1098 N N   . MET A  1 84  ? -2.84986  13.76334 3.58431   1.000 20.22764  ?  84  MET A N   1 
ATOM   1099 C CA  . MET A  1 84  ? -4.01845  14.60968 3.80242   1.000 20.23934  ?  84  MET A CA  1 
ATOM   1100 C C   . MET A  1 84  ? -5.12945  13.86846 4.54632   1.000 24.05826  ?  84  MET A C   1 
ATOM   1101 O O   . MET A  1 84  ? -5.79175  14.44739 5.42378   1.000 22.82872  ?  84  MET A O   1 
ATOM   1102 C CB  . MET A  1 84  ? -4.51083  15.11608 2.45852   1.000 20.20026  ?  84  MET A CB  1 
ATOM   1103 C CG  . MET A  1 84  ? -3.51368  16.03332 1.81236   1.000 23.30356  ?  84  MET A CG  1 
ATOM   1104 S SD  . MET A  1 84  ? -3.95326  16.47223 0.15052   1.000 23.66520  ?  84  MET A SD  1 
ATOM   1105 C CE  . MET A  1 84  ? -5.25759  17.61081 0.44351   1.000 23.05200  ?  84  MET A CE  1 
ATOM   1106 N N   . LEU A  1 85  ? -5.36540  12.59462 4.20307   1.000 19.79672  ?  85  LEU A N   1 
ATOM   1107 C CA  . LEU A  1 85  ? -6.39782  11.83719 4.90516   1.000 19.77511  ?  85  LEU A CA  1 
ATOM   1108 C C   . LEU A  1 85  ? -6.01957  11.63756 6.36582   1.000 23.36125  ?  85  LEU A C   1 
ATOM   1109 O O   . LEU A  1 85  ? -6.86837  11.75857 7.26215   1.000 23.58060  ?  85  LEU A O   1 
ATOM   1110 C CB  . LEU A  1 85  ? -6.60758  10.49810 4.22165   1.000 23.02734  ?  85  LEU A CB  1 
ATOM   1111 C CG  . LEU A  1 85  ? -7.32184  10.63409 2.87713   1.000 20.93171  ?  85  LEU A CG  1 
ATOM   1112 C CD1 . LEU A  1 85  ? -7.13367  9.34010  2.01394   1.000 22.67802  ?  85  LEU A CD1 1 
ATOM   1113 C CD2 . LEU A  1 85  ? -8.79008  10.98969 3.08713   1.000 23.67917  ?  85  LEU A CD2 1 
ATOM   1114 N N   A LEU A  1 86  ? -4.74095  11.38493 6.64526   0.600 20.51216  ?  86  LEU A N   1 
ATOM   1115 N N   B LEU A  1 86  ? -4.75187  11.29540 6.60938   0.400 20.38176  ?  86  LEU A N   1 
ATOM   1116 C CA  A LEU A  1 86  ? -4.32806  11.19791 8.03534   0.600 20.91869  ?  86  LEU A CA  1 
ATOM   1117 C CA  B LEU A  1 86  ? -4.22402  11.22177 7.96587   0.400 21.35578  ?  86  LEU A CA  1 
ATOM   1118 C C   A LEU A  1 86  ? -4.53160  12.46824 8.85610   0.600 23.95694  ?  86  LEU A C   1 
ATOM   1119 C C   B LEU A  1 86  ? -4.28764  12.58036 8.64670   0.400 23.66220  ?  86  LEU A C   1 
ATOM   1120 O O   A LEU A  1 86  ? -5.01885  12.40519 9.99283   0.600 21.32721  ?  86  LEU A O   1 
ATOM   1121 O O   B LEU A  1 86  ? -4.58138  12.67577 9.84629   0.400 22.95882  ?  86  LEU A O   1 
ATOM   1122 C CB  A LEU A  1 86  ? -2.88381  10.71020 8.09888   0.600 22.17967  ?  86  LEU A CB  1 
ATOM   1123 C CB  B LEU A  1 86  ? -2.78120  10.73328 7.90038   0.400 21.52624  ?  86  LEU A CB  1 
ATOM   1124 C CG  A LEU A  1 86  ? -2.53337  9.28292  7.65932   0.600 26.16986  ?  86  LEU A CG  1 
ATOM   1125 C CG  B LEU A  1 86  ? -2.16703  10.58098 9.28644   0.400 18.35922  ?  86  LEU A CG  1 
ATOM   1126 C CD1 A LEU A  1 86  ? -1.01768  9.09318  7.78425   0.600 36.67729  ?  86  LEU A CD1 1 
ATOM   1127 C CD1 B LEU A  1 86  ? -2.92317  9.51040  10.05919  0.400 23.73182  ?  86  LEU A CD1 1 
ATOM   1128 C CD2 A LEU A  1 86  ? -3.25294  8.20061  8.49137   0.600 31.85839  ?  86  LEU A CD2 1 
ATOM   1129 C CD2 B LEU A  1 86  ? -0.66791  10.27319 9.22888   0.400 26.03459  ?  86  LEU A CD2 1 
ATOM   1130 N N   A THR A  1 87  ? -4.17811  13.63663 8.29819   0.600 22.54169  ?  87  THR A N   1 
ATOM   1131 N N   B THR A  1 87  ? -4.01292  13.64981 7.89495   0.400 20.85404  ?  87  THR A N   1 
ATOM   1132 C CA  A THR A  1 87  ? -4.37135  14.87946 9.04112   0.600 22.55130  ?  87  THR A CA  1 
ATOM   1133 C CA  B THR A  1 87  ? -4.12078  14.98728 8.46204   0.400 21.31888  ?  87  THR A CA  1 
ATOM   1134 C C   A THR A  1 87  ? -5.84622  15.14007 9.28186   0.600 18.35713  ?  87  THR A C   1 
ATOM   1135 C C   B THR A  1 87  ? -5.55321  15.29385 8.89829   0.400 20.69691  ?  87  THR A C   1 
ATOM   1136 O O   A THR A  1 87  ? -6.23009  15.57533 10.37133  0.600 20.39754  ?  87  THR A O   1 
ATOM   1137 O O   B THR A  1 87  ? -5.76472  16.02883 9.87251   0.400 20.48217  ?  87  THR A O   1 
ATOM   1138 C CB  A THR A  1 87  ? -3.73616  16.08186 8.33057   0.600 28.82529  ?  87  THR A CB  1 
ATOM   1139 C CB  B THR A  1 87  ? -3.58083  16.01766 7.46470   0.400 25.59773  ?  87  THR A CB  1 
ATOM   1140 O OG1 A THR A  1 87  ? -4.23790  16.20325 6.99157   0.600 26.42723  ?  87  THR A OG1 1 
ATOM   1141 O OG1 B THR A  1 87  ? -2.17897  15.80692 7.28140   0.400 20.73968  ?  87  THR A OG1 1 
ATOM   1142 C CG2 A THR A  1 87  ? -2.24624  15.95366 8.31313   0.600 23.23132  ?  87  THR A CG2 1 
ATOM   1143 C CG2 B THR A  1 87  ? -3.77513  17.40922 7.97564   0.400 33.38992  ?  87  THR A CG2 1 
ATOM   1144 N N   A THR A  1 88  ? -6.67859  14.91414 8.26433   0.600 20.89109  ?  88  THR A N   1 
ATOM   1145 N N   B THR A  1 88  ? -6.54589  14.70716 8.22631   0.400 19.79789  ?  88  THR A N   1 
ATOM   1146 C CA  A THR A  1 88  ? -8.11565  14.99059 8.47971   0.600 24.19564  ?  88  THR A CA  1 
ATOM   1147 C CA  B THR A  1 88  ? -7.94043  15.02474 8.52623   0.400 23.72313  ?  88  THR A CA  1 
ATOM   1148 C C   A THR A  1 88  ? -8.51040  14.14208 9.68089   0.600 21.27827  ?  88  THR A C   1 
ATOM   1149 C C   B THR A  1 88  ? -8.53932  14.11475 9.59903   0.400 21.59159  ?  88  THR A C   1 
ATOM   1150 O O   A THR A  1 88  ? -9.19188  14.62872 10.60029  0.600 20.71902  ?  88  THR A O   1 
ATOM   1151 O O   B THR A  1 88  ? -9.45944  14.52912 10.31421  0.400 24.65311  ?  88  THR A O   1 
ATOM   1152 C CB  A THR A  1 88  ? -8.87155  14.53889 7.23261   0.600 21.90252  ?  88  THR A CB  1 
ATOM   1153 C CB  B THR A  1 88  ? -8.77617  15.01126 7.23759   0.400 28.72845  ?  88  THR A CB  1 
ATOM   1154 O OG1 A THR A  1 88  ? -8.55066  15.39274 6.12504   0.600 25.87196  ?  88  THR A OG1 1 
ATOM   1155 O OG1 B THR A  1 88  ? -9.83768  15.97056 7.33857   0.400 25.65394  ?  88  THR A OG1 1 
ATOM   1156 C CG2 A THR A  1 88  ? -10.36223 14.60243 7.48756   0.600 20.08884  ?  88  THR A CG2 1 
ATOM   1157 C CG2 B THR A  1 88  ? -9.36177  13.62604 6.95038   0.400 16.06027  ?  88  THR A CG2 1 
ATOM   1158 N N   . VAL A  1 89  ? -8.04327  12.88334 9.71784   1.000 21.68893  ?  89  VAL A N   1 
ATOM   1159 C CA  . VAL A  1 89  ? -8.35003  12.03622 10.87212  1.000 18.50926  ?  89  VAL A CA  1 
ATOM   1160 C C   . VAL A  1 89  ? -7.90064  12.72649 12.16262  1.000 23.29500  ?  89  VAL A C   1 
ATOM   1161 O O   . VAL A  1 89  ? -8.65573  12.80349 13.14125  1.000 22.92175  ?  89  VAL A O   1 
ATOM   1162 C CB  . VAL A  1 89  ? -7.73352  10.64132 10.72265  1.000 23.25865  ?  89  VAL A CB  1 
ATOM   1163 C CG1 . VAL A  1 89  ? -7.80218  9.89295  12.05162  1.000 23.84642  ?  89  VAL A CG1 1 
ATOM   1164 C CG2 . VAL A  1 89  ? -8.51288  9.84714  9.62975   1.000 22.16631  ?  89  VAL A CG2 1 
ATOM   1165 N N   A TYR A  1 90  ? -6.68260  13.28472 12.16185  0.600 21.18017  ?  90  TYR A N   1 
ATOM   1166 N N   B TYR A  1 90  ? -6.64764  13.20367 12.18975  0.400 21.12563  ?  90  TYR A N   1 
ATOM   1167 C CA  A TYR A  1 90  ? -6.17278  13.90090 13.38666  0.600 21.36257  ?  90  TYR A CA  1 
ATOM   1168 C CA  B TYR A  1 90  ? -6.16568  13.89063 13.38569  0.400 21.51722  ?  90  TYR A CA  1 
ATOM   1169 C C   A TYR A  1 90  ? -6.95261  15.15644 13.74102  0.600 20.97882  ?  90  TYR A C   1 
ATOM   1170 C C   B TYR A  1 90  ? -7.08077  15.06148 13.72943  0.400 20.94087  ?  90  TYR A C   1 
ATOM   1171 O O   A TYR A  1 90  ? -7.11753  15.47078 14.93225  0.600 20.98659  ?  90  TYR A O   1 
ATOM   1172 O O   B TYR A  1 90  ? -7.52267  15.19273 14.87837  0.400 20.48899  ?  90  TYR A O   1 
ATOM   1173 C CB  A TYR A  1 90  ? -4.70173  14.25536 13.22092  0.600 23.63125  ?  90  TYR A CB  1 
ATOM   1174 C CB  B TYR A  1 90  ? -4.71076  14.35410 13.22255  0.400 23.60264  ?  90  TYR A CB  1 
ATOM   1175 C CG  A TYR A  1 90  ? -3.80711  13.10446 12.83705  0.600 22.39741  ?  90  TYR A CG  1 
ATOM   1176 C CG  B TYR A  1 90  ? -3.61899  13.27110 13.14651  0.400 23.56063  ?  90  TYR A CG  1 
ATOM   1177 C CD1 A TYR A  1 90  ? -4.09462  11.79227 13.22359  0.600 22.19068  ?  90  TYR A CD1 1 
ATOM   1178 C CD1 B TYR A  1 90  ? -3.86752  11.93558 13.47239  0.400 21.87695  ?  90  TYR A CD1 1 
ATOM   1179 C CD2 A TYR A  1 90  ? -2.66427  13.33440 12.07975  0.600 25.87756  ?  90  TYR A CD2 1 
ATOM   1180 C CD2 B TYR A  1 90  ? -2.32034  13.60796 12.75214  0.400 23.69039  ?  90  TYR A CD2 1 
ATOM   1181 C CE1 A TYR A  1 90  ? -3.25363  10.74319 12.86697  0.600 25.34265  ?  90  TYR A CE1 1 
ATOM   1182 C CE1 B TYR A  1 90  ? -2.84778  10.96530 13.38288  0.400 24.84271  ?  90  TYR A CE1 1 
ATOM   1183 C CE2 A TYR A  1 90  ? -1.82700  12.30622 11.72735  0.600 23.99934  ?  90  TYR A CE2 1 
ATOM   1184 C CE2 B TYR A  1 90  ? -1.31156  12.65124 12.66446  0.400 19.36087  ?  90  TYR A CE2 1 
ATOM   1185 C CZ  A TYR A  1 90  ? -2.11951  11.01674 12.12267  0.600 25.76646  ?  90  TYR A CZ  1 
ATOM   1186 C CZ  B TYR A  1 90  ? -1.57361  11.33658 12.97622  0.400 22.19135  ?  90  TYR A CZ  1 
ATOM   1187 O OH  A TYR A  1 90  ? -1.27274  10.00506 11.73487  0.600 28.80756  ?  90  TYR A OH  1 
ATOM   1188 O OH  B TYR A  1 90  ? -0.55252  10.40244 12.88507  0.400 17.03492  ?  90  TYR A OH  1 
ATOM   1189 N N   . PHE A  1 91  ? -7.43581  15.88886 12.72683  1.000 20.38336  ?  91  PHE A N   1 
ATOM   1190 C CA  . PHE A  1 91  ? -8.26334  17.06669 13.02093  1.000 22.56741  ?  91  PHE A CA  1 
ATOM   1191 C C   . PHE A  1 91  ? -9.63119  16.67079 13.56971  1.000 23.71533  ?  91  PHE A C   1 
ATOM   1192 O O   . PHE A  1 91  ? -10.13703 17.29103 14.51850  1.000 22.87695  ?  91  PHE A O   1 
ATOM   1193 C CB  . PHE A  1 91  ? -8.44191  17.98905 11.82553  1.000 23.67195  ?  91  PHE A CB  1 
ATOM   1194 C CG  . PHE A  1 91  ? -9.09924  19.25425 12.22936  1.000 23.91043  ?  91  PHE A CG  1 
ATOM   1195 C CD1 . PHE A  1 91  ? -8.40631  20.16306 13.01962  1.000 24.96934  ?  91  PHE A CD1 1 
ATOM   1196 C CD2 . PHE A  1 91  ? -10.44074 19.48433 11.95802  1.000 23.78165  ?  91  PHE A CD2 1 
ATOM   1197 C CE1 . PHE A  1 91  ? -9.00242  21.32658 13.46500  1.000 25.85645  ?  91  PHE A CE1 1 
ATOM   1198 C CE2 . PHE A  1 91  ? -11.05087 20.64549 12.41336  1.000 26.18909  ?  91  PHE A CE2 1 
ATOM   1199 C CZ  . PHE A  1 91  ? -10.33496 21.56039 13.18097  1.000 26.51257  ?  91  PHE A CZ  1 
ATOM   1200 N N   . PHE A  1 92  ? -10.23666 15.61747 13.01108  1.000 22.61887  ?  92  PHE A N   1 
ATOM   1201 C CA  . PHE A  1 92  ? -11.51061 15.15545 13.55535  1.000 20.97037  ?  92  PHE A CA  1 
ATOM   1202 C C   . PHE A  1 92  ? -11.34023 14.69108 14.98652  1.000 24.05454  ?  92  PHE A C   1 
ATOM   1203 O O   . PHE A  1 92  ? -12.17237 14.99116 15.84634  1.000 24.70695  ?  92  PHE A O   1 
ATOM   1204 C CB  . PHE A  1 92  ? -12.12348 14.07119 12.67332  1.000 23.36668  ?  92  PHE A CB  1 
ATOM   1205 C CG  . PHE A  1 92  ? -12.90668 14.61950 11.51855  1.000 21.58095  ?  92  PHE A CG  1 
ATOM   1206 C CD1 . PHE A  1 92  ? -14.10418 15.27417 11.73424  1.000 24.75063  ?  92  PHE A CD1 1 
ATOM   1207 C CD2 . PHE A  1 92  ? -12.45424 14.48963 10.22258  1.000 30.09992  ?  92  PHE A CD2 1 
ATOM   1208 C CE1 . PHE A  1 92  ? -14.83367 15.79209 10.67737  1.000 29.21923  ?  92  PHE A CE1 1 
ATOM   1209 C CE2 . PHE A  1 92  ? -13.20442 15.01112 9.14699   1.000 33.55733  ?  92  PHE A CE2 1 
ATOM   1210 C CZ  . PHE A  1 92  ? -14.37959 15.67459 9.39505   1.000 32.52793  ?  92  PHE A CZ  1 
ATOM   1211 N N   A GLU A  1 93  ? -10.25143 13.96745 15.25892  0.600 22.27447  ?  93  GLU A N   1 
ATOM   1212 N N   B GLU A  1 93  ? -10.27175 13.93332 15.25873  0.400 22.27199  ?  93  GLU A N   1 
ATOM   1213 C CA  A GLU A  1 93  ? -9.97489  13.50651 16.61339  0.600 24.77125  ?  93  GLU A CA  1 
ATOM   1214 C CA  B GLU A  1 93  ? -10.00288 13.50961 16.62718  0.400 24.70781  ?  93  GLU A CA  1 
ATOM   1215 C C   A GLU A  1 93  ? -9.76523  14.68192 17.55505  0.600 23.49874  ?  93  GLU A C   1 
ATOM   1216 C C   B GLU A  1 93  ? -9.82714  14.71413 17.53818  0.400 23.65507  ?  93  GLU A C   1 
ATOM   1217 O O   A GLU A  1 93  ? -10.24147 14.66876 18.69028  0.600 25.58231  ?  93  GLU A O   1 
ATOM   1218 O O   B GLU A  1 93  ? -10.39677 14.75851 18.63071  0.400 25.05842  ?  93  GLU A O   1 
ATOM   1219 C CB  A GLU A  1 93  ? -8.74691  12.60506 16.58795  0.600 24.16056  ?  93  GLU A CB  1 
ATOM   1220 C CB  B GLU A  1 93  ? -8.77161  12.60435 16.67307  0.400 24.17183  ?  93  GLU A CB  1 
ATOM   1221 C CG  A GLU A  1 93  ? -9.01976  11.25721 15.97394  0.600 24.66046  ?  93  GLU A CG  1 
ATOM   1222 C CG  B GLU A  1 93  ? -9.00202  11.18216 16.17522  0.400 25.37102  ?  93  GLU A CG  1 
ATOM   1223 C CD  A GLU A  1 93  ? -9.72843  10.32687 16.94833  0.600 28.33123  ?  93  GLU A CD  1 
ATOM   1224 C CD  B GLU A  1 93  ? -9.78013  10.32760 17.16802  0.400 28.04792  ?  93  GLU A CD  1 
ATOM   1225 O OE1 A GLU A  1 93  ? -9.09744  9.92442  17.93631  0.600 40.80259  ?  93  GLU A OE1 1 
ATOM   1226 O OE1 B GLU A  1 93  ? -10.11826 10.83977 18.25631  0.400 19.90533  ?  93  GLU A OE1 1 
ATOM   1227 O OE2 A GLU A  1 93  ? -10.92878 10.01703 16.74526  0.600 37.46342  -1 93  GLU A OE2 1 
ATOM   1228 O OE2 B GLU A  1 93  ? -10.06473 9.14708  16.85820  0.400 20.87561  -1 93  GLU A OE2 1 
ATOM   1229 N N   . TYR A  1 94  ? -9.07032  15.71906 17.08957  1.000 26.28231  ?  94  TYR A N   1 
ATOM   1230 C CA  . TYR A  1 94  ? -8.90694  16.92816 17.89023  1.000 24.55919  ?  94  TYR A CA  1 
ATOM   1231 C C   . TYR A  1 94  ? -10.25712 17.57720 18.18966  1.000 23.24408  ?  94  TYR A C   1 
ATOM   1232 O O   . TYR A  1 94  ? -10.55124 17.93702 19.33695  1.000 25.21961  ?  94  TYR A O   1 
ATOM   1233 C CB  . TYR A  1 94  ? -8.02240  17.90530 17.13559  1.000 22.95572  ?  94  TYR A CB  1 
ATOM   1234 C CG  . TYR A  1 94  ? -8.02782  19.30191 17.72320  1.000 26.13754  ?  94  TYR A CG  1 
ATOM   1235 C CD1 . TYR A  1 94  ? -7.39622  19.57292 18.93340  1.000 26.85660  ?  94  TYR A CD1 1 
ATOM   1236 C CD2 . TYR A  1 94  ? -8.65249  20.34741 17.06134  1.000 23.71364  ?  94  TYR A CD2 1 
ATOM   1237 C CE1 . TYR A  1 94  ? -7.38400  20.84739 19.46049  1.000 27.25204  ?  94  TYR A CE1 1 
ATOM   1238 C CE2 . TYR A  1 94  ? -8.64676  21.62708 17.56828  1.000 29.16323  ?  94  TYR A CE2 1 
ATOM   1239 C CZ  . TYR A  1 94  ? -8.01855  21.87139 18.78486  1.000 30.55118  ?  94  TYR A CZ  1 
ATOM   1240 O OH  . TYR A  1 94  ? -8.00966  23.13739 19.32245  1.000 31.58718  ?  94  TYR A OH  1 
ATOM   1241 N N   . MET A  1 95  ? -11.07345 17.76930 17.15030  1.000 23.23036  ?  95  MET A N   1 
ATOM   1242 C CA  . MET A  1 95  ? -12.37036 18.41466 17.33818  1.000 27.89171  ?  95  MET A CA  1 
ATOM   1243 C C   . MET A  1 95  ? -13.26118 17.62433 18.27606  1.000 29.30384  ?  95  MET A C   1 
ATOM   1244 O O   . MET A  1 95  ? -14.05272 18.21508 19.02791  1.000 29.94165  ?  95  MET A O   1 
ATOM   1245 C CB  . MET A  1 95  ? -13.09154 18.51824 15.98956  1.000 26.07217  ?  95  MET A CB  1 
ATOM   1246 C CG  . MET A  1 95  ? -12.95286 19.82095 15.27167  1.000 39.70477  ?  95  MET A CG  1 
ATOM   1247 S SD  . MET A  1 95  ? -14.35912 20.07376 14.13279  1.000 34.92551  ?  95  MET A SD  1 
ATOM   1248 C CE  . MET A  1 95  ? -14.28172 18.56466 13.19271  1.000 29.56534  ?  95  MET A CE  1 
ATOM   1249 N N   . ASN A  1 96  ? -13.15379 16.29459 18.25304  1.000 24.26958  ?  96  ASN A N   1 
ATOM   1250 C CA  . ASN A  1 96  ? -14.18414 15.41917 18.80091  1.000 25.95088  ?  96  ASN A CA  1 
ATOM   1251 C C   . ASN A  1 96  ? -13.81294 14.74569 20.11230  1.000 30.88127  ?  96  ASN A C   1 
ATOM   1252 O O   . ASN A  1 96  ? -14.70717 14.25451 20.80567  1.000 34.20751  ?  96  ASN A O   1 
ATOM   1253 C CB  . ASN A  1 96  ? -14.62896 14.38013 17.74946  1.000 28.66108  ?  96  ASN A CB  1 
ATOM   1254 C CG  . ASN A  1 96  ? -15.39546 15.02917 16.59150  1.000 27.47208  ?  96  ASN A CG  1 
ATOM   1255 O OD1 . ASN A  1 96  ? -15.97190 16.11018 16.75624  1.000 27.52665  ?  96  ASN A OD1 1 
ATOM   1256 N ND2 . ASN A  1 96  ? -15.38071 14.39650 15.42023  1.000 24.75882  ?  96  ASN A ND2 1 
ATOM   1257 N N   . SER A  1 97  ? -12.53504 14.71729 20.47923  1.000 33.51969  ?  97  SER A N   1 
ATOM   1258 C CA  A SER A  1 97  ? -12.13313 14.13337 21.75198  0.600 32.79043  ?  97  SER A CA  1 
ATOM   1259 C CA  B SER A  1 97  ? -12.12789 14.13479 21.75088  0.400 32.83098  ?  97  SER A CA  1 
ATOM   1260 C C   . SER A  1 97  ? -12.30281 15.15692 22.86619  1.000 32.79954  ?  97  SER A C   1 
ATOM   1261 O O   . SER A  1 97  ? -11.82629 16.29233 22.75912  1.000 39.87403  ?  97  SER A O   1 
ATOM   1262 C CB  A SER A  1 97  ? -10.67695 13.67182 21.69464  0.600 37.13126  ?  97  SER A CB  1 
ATOM   1263 C CB  B SER A  1 97  ? -10.66487 13.69907 21.68564  0.400 37.14112  ?  97  SER A CB  1 
ATOM   1264 O OG  A SER A  1 97  ? -10.40207 12.99435 20.48374  0.600 41.60320  ?  97  SER A OG  1 
ATOM   1265 O OG  B SER A  1 97  ? -9.80699  14.82836 21.63288  0.400 41.32608  ?  97  SER A OG  1 
ATOM   1266 N N   . ASP A  1 98  ? -12.99135 14.75360 23.94068  1.000 45.67007  ?  98  ASP A N   1 
ATOM   1267 C CA  . ASP A  1 98  ? -13.16601 15.63284 25.09621  1.000 72.71434  ?  98  ASP A CA  1 
ATOM   1268 C C   . ASP A  1 98  ? -11.84710 15.86179 25.82602  1.000 54.77170  ?  98  ASP A C   1 
ATOM   1269 O O   . ASP A  1 98  ? -11.62106 16.94488 26.38329  1.000 63.78668  ?  98  ASP A O   1 
ATOM   1270 C CB  . ASP A  1 98  ? -14.20777 15.04874 26.05630  1.000 62.97231  ?  98  ASP A CB  1 
ATOM   1271 N N   . ASP A  1 99  ? -10.97154 14.86537 25.82350  1.000 38.57903  ?  99  ASP A N   1 
ATOM   1272 C CA  . ASP A  1 99  ? -9.63907  14.97777 26.39886  1.000 54.60649  ?  99  ASP A CA  1 
ATOM   1273 C C   . ASP A  1 99  ? -8.61322  15.22300 25.29563  1.000 52.55488  ?  99  ASP A C   1 
ATOM   1274 O O   . ASP A  1 99  ? -8.85050  14.92648 24.12139  1.000 43.49409  ?  99  ASP A O   1 
ATOM   1275 C CB  . ASP A  1 99  ? -9.28044  13.69254 27.15001  1.000 49.79280  ?  99  ASP A CB  1 
ATOM   1276 N N   . GLY A  1 100 ? -7.45401  15.76122 25.68817  1.000 39.81799  ?  100 GLY A N   1 
ATOM   1277 C CA  . GLY A  1 100 ? -6.38654  15.98529 24.73224  1.000 27.63501  ?  100 GLY A CA  1 
ATOM   1278 C C   . GLY A  1 100 ? -5.91247  14.67066 24.14224  1.000 37.54904  ?  100 GLY A C   1 
ATOM   1279 O O   . GLY A  1 100 ? -5.69733  13.70325 24.88284  1.000 41.78555  ?  100 GLY A O   1 
ATOM   1280 N N   . ILE A  1 101 ? -5.76554  14.61507 22.82459  1.000 32.69996  ?  101 ILE A N   1 
ATOM   1281 C CA  . ILE A  1 101 ? -5.32983  13.41329 22.12068  1.000 28.05073  ?  101 ILE A CA  1 
ATOM   1282 C C   . ILE A  1 101 ? -4.17433  13.79678 21.20746  1.000 27.96407  ?  101 ILE A C   1 
ATOM   1283 O O   . ILE A  1 101 ? -4.13569  14.91460 20.66965  1.000 28.81051  ?  101 ILE A O   1 
ATOM   1284 C CB  . ILE A  1 101 ? -6.49883  12.79587 21.32021  1.000 29.11702  ?  101 ILE A CB  1 
ATOM   1285 C CG1 . ILE A  1 101 ? -6.06240  11.49843 20.63986  1.000 35.01524  ?  101 ILE A CG1 1 
ATOM   1286 C CG2 . ILE A  1 101 ? -7.00593  13.75688 20.27353  1.000 34.88378  ?  101 ILE A CG2 1 
ATOM   1287 C CD1 . ILE A  1 101 ? -6.90321  10.33081 20.99751  1.000 36.59029  ?  101 ILE A CD1 1 
ATOM   1288 N N   A ARG A  1 102 ? -3.23737  12.87193 20.99784  0.600 29.03847  ?  102 ARG A N   1 
ATOM   1289 N N   B ARG A  1 102 ? -3.21657  12.88045 21.08109  0.400 29.33630  ?  102 ARG A N   1 
ATOM   1290 C CA  A ARG A  1 102 ? -2.13769  13.13209 20.07585  0.600 30.11329  ?  102 ARG A CA  1 
ATOM   1291 C CA  B ARG A  1 102 ? -1.95455  13.06010 20.37582  0.400 29.60024  ?  102 ARG A CA  1 
ATOM   1292 C C   A ARG A  1 102 ? -2.03288  12.01767 19.04676  0.600 29.68138  ?  102 ARG A C   1 
ATOM   1293 C C   B ARG A  1 102 ? -1.91303  12.14036 19.15596  0.400 30.25293  ?  102 ARG A C   1 
ATOM   1294 O O   A ARG A  1 102 ? -2.46917  10.88293 19.28332  0.600 21.92282  ?  102 ARG A O   1 
ATOM   1295 O O   B ARG A  1 102 ? -2.87757  11.43960 18.83544  0.400 26.54810  ?  102 ARG A O   1 
ATOM   1296 C CB  A ARG A  1 102 ? -0.78762  13.33787 20.78523  0.600 36.15755  ?  102 ARG A CB  1 
ATOM   1297 C CB  B ARG A  1 102 ? -0.77008  12.77916 21.30969  0.400 31.03142  ?  102 ARG A CB  1 
ATOM   1298 C CG  A ARG A  1 102 ? -0.73123  14.58286 21.67352  0.600 37.58878  ?  102 ARG A CG  1 
ATOM   1299 C CG  B ARG A  1 102 ? -0.59522  13.79432 22.43754  0.400 33.13521  ?  102 ARG A CG  1 
ATOM   1300 C CD  A ARG A  1 102 ? 0.65270   14.80068 22.25639  0.600 33.89763  ?  102 ARG A CD  1 
ATOM   1301 C CD  B ARG A  1 102 ? -0.40596  15.19785 21.88910  0.400 37.39506  ?  102 ARG A CD  1 
ATOM   1302 N N   A LYS A  1 103 ? -1.43795  12.37258 17.89425  0.600 24.17663  ?  103 LYS A N   1 
ATOM   1303 N N   B LYS A  1 103 ? -0.78221  12.14220 18.45243  0.400 23.46149  ?  103 LYS A N   1 
ATOM   1304 C CA  A LYS A  1 103 ? -1.44435  11.47280 16.74838  0.600 28.27803  ?  103 LYS A CA  1 
ATOM   1305 C CA  B LYS A  1 103 ? -0.70904  11.29269 17.26847  0.400 29.88952  ?  103 LYS A CA  1 
ATOM   1306 C C   A LYS A  1 103 ? -0.83833  10.11558 17.07125  0.600 24.93308  ?  103 LYS A C   1 
ATOM   1307 C C   B LYS A  1 103 ? -0.43371  9.84320  17.64776  0.400 26.92273  ?  103 LYS A C   1 
ATOM   1308 O O   A LYS A  1 103 ? -1.17556  9.13950  16.39735  0.600 27.02236  ?  103 LYS A O   1 
ATOM   1309 O O   B LYS A  1 103 ? -1.04865  8.92637  17.09303  0.400 20.74930  ?  103 LYS A O   1 
ATOM   1310 C CB  A LYS A  1 103 ? -0.74927  12.09541 15.52790  0.600 26.67933  ?  103 LYS A CB  1 
ATOM   1311 C CB  B LYS A  1 103 ? 0.28118   11.85017 16.23463  0.400 29.99655  ?  103 LYS A CB  1 
ATOM   1312 C CG  A LYS A  1 103 ? 0.76082   11.92504 15.51093  0.600 31.10942  ?  103 LYS A CG  1 
ATOM   1313 C CG  B LYS A  1 103 ? 1.68354   11.25815 16.25777  0.400 41.03606  ?  103 LYS A CG  1 
ATOM   1314 C CD  A LYS A  1 103 ? 1.42402   12.64513 14.32736  0.600 38.82117  ?  103 LYS A CD  1 
ATOM   1315 C CD  B LYS A  1 103 ? 2.47385   11.69470 15.01893  0.400 41.53469  ?  103 LYS A CD  1 
ATOM   1316 N N   A LYS A  1 104 ? 0.04363   10.01860 18.07279  0.600 25.87650  ?  104 LYS A N   1 
ATOM   1317 N N   B LYS A  1 104 ? 0.43059   9.61597  18.64183  0.400 28.66989  ?  104 LYS A N   1 
ATOM   1318 C CA  A LYS A  1 104 ? 0.62599   8.71055  18.37926  0.600 31.85493  ?  104 LYS A CA  1 
ATOM   1319 C CA  B LYS A  1 104 ? 0.80464   8.24434  18.98249  0.400 32.56352  ?  104 LYS A CA  1 
ATOM   1320 C C   A LYS A  1 104 ? -0.42639  7.75378  18.93276  0.600 25.50581  ?  104 LYS A C   1 
ATOM   1321 C C   B LYS A  1 104 ? -0.40011  7.41785  19.42029  0.400 35.69374  ?  104 LYS A C   1 
ATOM   1322 O O   A LYS A  1 104 ? -0.48423  6.58370  18.52740  0.600 24.46513  ?  104 LYS A O   1 
ATOM   1323 O O   B LYS A  1 104 ? -0.45997  6.21217  19.15370  0.400 25.92993  ?  104 LYS A O   1 
ATOM   1324 C CB  A LYS A  1 104 ? 1.82639   8.82169  19.33098  0.600 30.62286  ?  104 LYS A CB  1 
ATOM   1325 C CB  B LYS A  1 104 ? 1.87541   8.24559  20.07756  0.400 28.43553  ?  104 LYS A CB  1 
ATOM   1326 C CG  A LYS A  1 104 ? 2.26284   7.45357  19.91119  0.600 36.93586  ?  104 LYS A CG  1 
ATOM   1327 C CG  B LYS A  1 104 ? 2.10799   6.87284  20.70448  0.400 28.58880  ?  104 LYS A CG  1 
ATOM   1328 C CD  A LYS A  1 104 ? 3.55530   7.53764  20.72440  0.600 41.71750  ?  104 LYS A CD  1 
ATOM   1329 C CD  B LYS A  1 104 ? 3.36762   6.83121  21.54814  0.400 52.33541  ?  104 LYS A CD  1 
ATOM   1330 C CE  A LYS A  1 104 ? 3.76083   6.31227  21.64233  0.600 57.28994  ?  104 LYS A CE  1 
ATOM   1331 C CE  B LYS A  1 104 ? 4.53290   6.26798  20.74464  0.400 53.26282  ?  104 LYS A CE  1 
ATOM   1332 N NZ  A LYS A  1 104 ? 4.07442   5.03156  20.92967  0.600 48.78073  ?  104 LYS A NZ  1 
ATOM   1333 N NZ  B LYS A  1 104 ? 4.24007   4.88532  20.25299  0.400 46.98981  ?  104 LYS A NZ  1 
ATOM   1334 N N   A GLU A  1 105 ? -1.25699  8.22707  19.87264  0.600 26.07925  ?  105 GLU A N   1 
ATOM   1335 N N   B GLU A  1 105 ? -1.36720  8.03716  20.09166  0.400 26.57456  ?  105 GLU A N   1 
ATOM   1336 C CA  A GLU A  1 105 ? -2.32554  7.38828  20.41546  0.600 27.82309  ?  105 GLU A CA  1 
ATOM   1337 C CA  B GLU A  1 105 ? -2.52539  7.28124  20.55030  0.400 28.50881  ?  105 GLU A CA  1 
ATOM   1338 C C   A GLU A  1 105 ? -3.23365  6.91863  19.29559  0.600 26.06135  ?  105 GLU A C   1 
ATOM   1339 C C   B GLU A  1 105 ? -3.50436  6.97696  19.42146  0.400 26.59955  ?  105 GLU A C   1 
ATOM   1340 O O   A GLU A  1 105 ? -3.59228  5.73183  19.21734  0.600 25.02783  ?  105 GLU A O   1 
ATOM   1341 O O   B GLU A  1 105 ? -4.18880  5.94318  19.47016  0.400 29.45871  ?  105 GLU A O   1 
ATOM   1342 C CB  A GLU A  1 105 ? -3.13625  8.16128  21.47193  0.600 32.18436  ?  105 GLU A CB  1 
ATOM   1343 C CB  B GLU A  1 105 ? -3.21390  8.02846  21.68929  0.400 34.08101  ?  105 GLU A CB  1 
ATOM   1344 C CG  A GLU A  1 105 ? -4.51181  7.52056  21.84459  0.600 29.47143  ?  105 GLU A CG  1 
ATOM   1345 C CG  B GLU A  1 105 ? -3.34163  9.50439  21.43002  0.400 45.73424  ?  105 GLU A CG  1 
ATOM   1346 C CD  A GLU A  1 105 ? -5.23437  8.21624  23.01815  0.600 47.34924  ?  105 GLU A CD  1 
ATOM   1347 C CD  B GLU A  1 105 ? -3.49966  10.30225 22.70545  0.400 43.54119  ?  105 GLU A CD  1 
ATOM   1348 O OE1 A GLU A  1 105 ? -4.59633  8.97862  23.76316  0.600 37.00628  ?  105 GLU A OE1 1 
ATOM   1349 O OE1 B GLU A  1 105 ? -4.54061  10.14904 23.37731  0.400 44.35672  ?  105 GLU A OE1 1 
ATOM   1350 O OE2 A GLU A  1 105 ? -6.45586  8.00352  23.19299  0.600 46.94974  -1 105 GLU A OE2 1 
ATOM   1351 O OE2 B GLU A  1 105 ? -2.57430  11.07479 23.03875  0.400 38.82467  -1 105 GLU A OE2 1 
ATOM   1352 N N   . ILE A  1 106 ? -3.58889  7.84977  18.41226  1.000 23.86958  ?  106 ILE A N   1 
ATOM   1353 C CA  . ILE A  1 106 ? -4.42058  7.56299  17.24397  1.000 24.00060  ?  106 ILE A CA  1 
ATOM   1354 C C   . ILE A  1 106 ? -3.75971  6.49928  16.37906  1.000 25.82450  ?  106 ILE A C   1 
ATOM   1355 O O   . ILE A  1 106 ? -4.38068  5.48352  16.02620  1.000 28.11129  ?  106 ILE A O   1 
ATOM   1356 C CB  . ILE A  1 106 ? -4.69306  8.86152  16.45046  1.000 19.89257  ?  106 ILE A CB  1 
ATOM   1357 C CG1 . ILE A  1 106 ? -5.52748  9.82723  17.31060  1.000 23.81486  ?  106 ILE A CG1 1 
ATOM   1358 C CG2 . ILE A  1 106 ? -5.47366  8.56364  15.13254  1.000 24.10326  ?  106 ILE A CG2 1 
ATOM   1359 C CD1 . ILE A  1 106 ? -5.49817  11.27835 16.84437  1.000 26.19317  ?  106 ILE A CD1 1 
ATOM   1360 N N   A ASN A  1 107 ? -2.48183  6.69426  16.05538  0.600 24.53005  ?  107 ASN A N   1 
ATOM   1361 N N   B ASN A  1 107 ? -2.51233  6.74333  15.96885  0.400 24.71719  ?  107 ASN A N   1 
ATOM   1362 C CA  A ASN A  1 107 ? -1.80981  5.77647  15.13594  0.600 25.74700  ?  107 ASN A CA  1 
ATOM   1363 C CA  B ASN A  1 107 ? -1.79126  5.76547  15.15944  0.400 25.86589  ?  107 ASN A CA  1 
ATOM   1364 C C   A ASN A  1 107 ? -1.62859  4.38807  15.75121  0.600 28.13722  ?  107 ASN A C   1 
ATOM   1365 C C   B ASN A  1 107 ? -1.83320  4.39064  15.81667  0.400 26.71323  ?  107 ASN A C   1 
ATOM   1366 O O   A ASN A  1 107 ? -1.74328  3.37574  15.05038  0.600 27.46657  ?  107 ASN A O   1 
ATOM   1367 O O   B ASN A  1 107 ? -2.31597  3.41112  15.23204  0.400 23.55373  ?  107 ASN A O   1 
ATOM   1368 C CB  A ASN A  1 107 ? -0.46119  6.35654  14.72184  0.600 24.42100  ?  107 ASN A CB  1 
ATOM   1369 C CB  B ASN A  1 107 ? -0.33220  6.19710  15.00129  0.400 22.99035  ?  107 ASN A CB  1 
ATOM   1370 C CG  A ASN A  1 107 ? -0.59554  7.52622  13.78297  0.600 26.09292  ?  107 ASN A CG  1 
ATOM   1371 C CG  B ASN A  1 107 ? -0.18187  7.58074  14.39865  0.400 25.79928  ?  107 ASN A CG  1 
ATOM   1372 O OD1 A ASN A  1 107 ? -1.61105  7.69210  13.09334  0.600 26.20086  ?  107 ASN A OD1 1 
ATOM   1373 O OD1 B ASN A  1 107 ? 0.71179   8.33694  14.78632  0.400 34.21965  ?  107 ASN A OD1 1 
ATOM   1374 N ND2 A ASN A  1 107 ? 0.44939   8.34462  13.72943  0.600 28.22718  ?  107 ASN A ND2 1 
ATOM   1375 N ND2 B ASN A  1 107 ? -1.04539  7.91654  13.42875  0.400 24.25128  ?  107 ASN A ND2 1 
ATOM   1376 N N   . ASP A  1 108 ? -1.33718  4.30874  17.05585  1.000 25.05782  ?  108 ASP A N   1 
ATOM   1377 C CA  . ASP A  1 108 ? -1.13233  3.01049  17.68382  1.000 24.07625  ?  108 ASP A CA  1 
ATOM   1378 C C   . ASP A  1 108 ? -2.44765  2.26388  17.82887  1.000 29.35105  ?  108 ASP A C   1 
ATOM   1379 O O   . ASP A  1 108 ? -2.46128  1.03390  17.86900  1.000 30.55070  ?  108 ASP A O   1 
ATOM   1380 C CB  . ASP A  1 108 ? -0.52252  3.16154  19.07076  1.000 26.71610  ?  108 ASP A CB  1 
ATOM   1381 C CG  . ASP A  1 108 ? 0.92691   3.61374  19.03669  1.000 33.48552  ?  108 ASP A CG  1 
ATOM   1382 O OD1 . ASP A  1 108 ? 1.55299   3.60951  17.96548  1.000 33.90877  ?  108 ASP A OD1 1 
ATOM   1383 O OD2 . ASP A  1 108 ? 1.41964   4.01430  20.11198  1.000 33.72135  -1 108 ASP A OD2 1 
ATOM   1384 N N   . ARG A  1 109 ? -3.55180  2.99129  17.93839  1.000 26.80377  ?  109 ARG A N   1 
ATOM   1385 C CA  . ARG A  1 109 ? -4.84338  2.35463  18.14955  1.000 29.07218  ?  109 ARG A CA  1 
ATOM   1386 C C   . ARG A  1 109 ? -5.48238  1.98155  16.82679  1.000 27.80567  ?  109 ARG A C   1 
ATOM   1387 O O   . ARG A  1 109 ? -6.09982  0.90920  16.71115  1.000 30.87289  ?  109 ARG A O   1 
ATOM   1388 C CB  . ARG A  1 109 ? -5.77805  3.32168  18.87953  1.000 28.43169  ?  109 ARG A CB  1 
ATOM   1389 C CG  . ARG A  1 109 ? -7.14520  2.74948  19.21751  1.000 32.56098  ?  109 ARG A CG  1 
ATOM   1390 C CD  . ARG A  1 109 ? -8.08634  3.85132  19.74034  1.000 30.33252  ?  109 ARG A CD  1 
ATOM   1391 N NE  . ARG A  1 109 ? -8.41804  4.80734  18.68802  1.000 32.99571  ?  109 ARG A NE  1 
ATOM   1392 C CZ  . ARG A  1 109 ? -8.79994  6.06455  18.89102  1.000 42.65048  ?  109 ARG A CZ  1 
ATOM   1393 N NH1 . ARG A  1 109 ? -8.86987  6.58315  20.11402  1.000 36.55649  ?  109 ARG A NH1 1 
ATOM   1394 N NH2 . ARG A  1 109 ? -9.12765  6.81744  17.84223  1.000 35.41946  ?  109 ARG A NH2 1 
ATOM   1395 N N   . ASP A  1 110 ? -5.33628  2.83597  15.82431  1.000 25.69799  ?  110 ASP A N   1 
ATOM   1396 C CA  . ASP A  1 110 ? -6.15101  2.74739  14.62370  1.000 25.67894  ?  110 ASP A CA  1 
ATOM   1397 C C   . ASP A  1 110 ? -5.38520  2.34201  13.36932  1.000 25.37396  ?  110 ASP A C   1 
ATOM   1398 O O   . ASP A  1 110 ? -5.93703  2.47157  12.27939  1.000 24.94462  ?  110 ASP A O   1 
ATOM   1399 C CB  . ASP A  1 110 ? -6.85350  4.07903  14.35440  1.000 26.67556  ?  110 ASP A CB  1 
ATOM   1400 C CG  . ASP A  1 110 ? -7.93788  4.38689  15.36762  1.000 24.63429  ?  110 ASP A CG  1 
ATOM   1401 O OD1 . ASP A  1 110 ? -8.32476  3.49585  16.17424  1.000 29.40729  ?  110 ASP A OD1 1 
ATOM   1402 O OD2 . ASP A  1 110 ? -8.38382  5.55120  15.36349  1.000 29.57020  -1 110 ASP A OD2 1 
ATOM   1403 N N   . TYR A  1 111 ? -4.14216  1.85015  13.47831  1.000 23.84677  ?  111 TYR A N   1 
ATOM   1404 C CA  . TYR A  1 111 ? -3.33858  1.68824  12.26219  1.000 23.70454  ?  111 TYR A CA  1 
ATOM   1405 C C   . TYR A  1 111 ? -4.00339  0.76907  11.23499  1.000 23.36496  ?  111 TYR A C   1 
ATOM   1406 O O   . TYR A  1 111 ? -3.92229  1.04277  10.02124  1.000 24.59790  ?  111 TYR A O   1 
ATOM   1407 C CB  . TYR A  1 111 ? -1.89297  1.26327  12.56571  1.000 25.57626  ?  111 TYR A CB  1 
ATOM   1408 C CG  . TYR A  1 111 ? -1.79395  -0.03087 13.33488  1.000 26.01592  ?  111 TYR A CG  1 
ATOM   1409 C CD1 . TYR A  1 111 ? -1.81040  -0.04622 14.73356  1.000 26.30236  ?  111 TYR A CD1 1 
ATOM   1410 C CD2 . TYR A  1 111 ? -1.67189  -1.25438 12.66273  1.000 26.40591  ?  111 TYR A CD2 1 
ATOM   1411 C CE1 . TYR A  1 111 ? -1.71258  -1.23308 15.43408  1.000 30.96644  ?  111 TYR A CE1 1 
ATOM   1412 C CE2 . TYR A  1 111 ? -1.56480  -2.45247 13.35787  1.000 27.43585  ?  111 TYR A CE2 1 
ATOM   1413 C CZ  . TYR A  1 111 ? -1.59256  -2.44831 14.74261  1.000 28.86006  ?  111 TYR A CZ  1 
ATOM   1414 O OH  . TYR A  1 111 ? -1.50395  -3.62617 15.44383  1.000 29.25326  ?  111 TYR A OH  1 
ATOM   1415 N N   . VAL A  1 112 ? -4.69061  -0.29374 11.68552  1.000 25.09780  ?  112 VAL A N   1 
ATOM   1416 C CA  . VAL A  1 112 ? -5.36791  -1.16402 10.71771  1.000 28.60198  ?  112 VAL A CA  1 
ATOM   1417 C C   . VAL A  1 112 ? -6.43711  -0.38432 9.96235   1.000 27.50901  ?  112 VAL A C   1 
ATOM   1418 O O   . VAL A  1 112 ? -6.50109  -0.42494 8.73132   1.000 25.88163  ?  112 VAL A O   1 
ATOM   1419 C CB  . VAL A  1 112 ? -5.97174  -2.40465 11.39157  1.000 29.42896  ?  112 VAL A CB  1 
ATOM   1420 C CG1 . VAL A  1 112 ? -6.80739  -3.20004 10.35851  1.000 31.00070  ?  112 VAL A CG1 1 
ATOM   1421 C CG2 . VAL A  1 112 ? -4.86743  -3.29258 11.98109  1.000 30.55843  ?  112 VAL A CG2 1 
ATOM   1422 N N   . TYR A  1 113 ? -7.30900  0.32318  10.69191  1.000 23.48049  ?  113 TYR A N   1 
ATOM   1423 C CA  . TYR A  1 113 ? -8.36300  1.10285  10.04091  1.000 25.28435  ?  113 TYR A CA  1 
ATOM   1424 C C   . TYR A  1 113 ? -7.78111  2.15973  9.11489   1.000 22.02443  ?  113 TYR A C   1 
ATOM   1425 O O   . TYR A  1 113 ? -8.27629  2.36311  8.00195   1.000 26.31361  ?  113 TYR A O   1 
ATOM   1426 C CB  . TYR A  1 113 ? -9.23009  1.76567  11.10635  1.000 27.52029  ?  113 TYR A CB  1 
ATOM   1427 C CG  . TYR A  1 113 ? -10.56516 2.21216  10.60227  1.000 30.19011  ?  113 TYR A CG  1 
ATOM   1428 C CD1 . TYR A  1 113 ? -11.64033 1.32807  10.58771  1.000 29.55410  ?  113 TYR A CD1 1 
ATOM   1429 C CD2 . TYR A  1 113 ? -10.76737 3.51554  10.16101  1.000 28.96567  ?  113 TYR A CD2 1 
ATOM   1430 C CE1 . TYR A  1 113 ? -12.87734 1.71959  10.14256  1.000 33.89041  ?  113 TYR A CE1 1 
ATOM   1431 C CE2 . TYR A  1 113 ? -12.02852 3.93131  9.71095   1.000 26.25963  ?  113 TYR A CE2 1 
ATOM   1432 C CZ  . TYR A  1 113 ? -13.07063 3.01081  9.70309   1.000 31.55903  ?  113 TYR A CZ  1 
ATOM   1433 O OH  . TYR A  1 113 ? -14.33581 3.35313  9.29606   1.000 26.20708  ?  113 TYR A OH  1 
ATOM   1434 N N   . LEU A  1 114 ? -6.72682  2.83748  9.55644   1.000 22.49548  ?  114 LEU A N   1 
ATOM   1435 C CA  . LEU A  1 114 ? -6.07359  3.83526  8.72981   1.000 24.81435  ?  114 LEU A CA  1 
ATOM   1436 C C   . LEU A  1 114 ? -5.53655  3.21381  7.44735   1.000 26.35271  ?  114 LEU A C   1 
ATOM   1437 O O   . LEU A  1 114 ? -5.64257  3.81099  6.36851   1.000 24.40163  ?  114 LEU A O   1 
ATOM   1438 C CB  . LEU A  1 114 ? -4.98232  4.51604  9.54597   1.000 23.74869  ?  114 LEU A CB  1 
ATOM   1439 C CG  . LEU A  1 114 ? -5.57878  5.34567  10.69430  1.000 26.35430  ?  114 LEU A CG  1 
ATOM   1440 C CD1 . LEU A  1 114 ? -4.48898  5.95512  11.57127  1.000 31.44383  ?  114 LEU A CD1 1 
ATOM   1441 C CD2 . LEU A  1 114 ? -6.44285  6.45846  10.14368  1.000 30.17769  ?  114 LEU A CD2 1 
ATOM   1442 N N   . PHE A  1 115 ? -4.99490  1.99691  7.53825   1.000 27.38074  ?  115 PHE A N   1 
ATOM   1443 C CA  . PHE A  1 115 ? -4.54048  1.31233  6.33213   1.000 26.37999  ?  115 PHE A CA  1 
ATOM   1444 C C   . PHE A  1 115 ? -5.69333  1.05586  5.36781   1.000 24.92503  ?  115 PHE A C   1 
ATOM   1445 O O   . PHE A  1 115 ? -5.53287  1.22371  4.15072   1.000 27.68466  ?  115 PHE A O   1 
ATOM   1446 C CB  . PHE A  1 115 ? -3.78389  0.03314  6.67982   1.000 29.55127  ?  115 PHE A CB  1 
ATOM   1447 C CG  . PHE A  1 115 ? -3.50039  -0.82001 5.48345   1.000 31.97859  ?  115 PHE A CG  1 
ATOM   1448 C CD1 . PHE A  1 115 ? -2.43251  -0.53083 4.64063   1.000 51.77148  ?  115 PHE A CD1 1 
ATOM   1449 C CD2 . PHE A  1 115 ? -4.31866  -1.87436 5.17484   1.000 32.32163  ?  115 PHE A CD2 1 
ATOM   1450 C CE1 . PHE A  1 115 ? -2.17791  -1.32418 3.51683   1.000 47.16762  ?  115 PHE A CE1 1 
ATOM   1451 C CE2 . PHE A  1 115 ? -4.06798  -2.68176 4.06020   1.000 49.99410  ?  115 PHE A CE2 1 
ATOM   1452 C CZ  . PHE A  1 115 ? -3.00786  -2.40018 3.22999   1.000 40.47705  ?  115 PHE A CZ  1 
ATOM   1453 N N   . TYR A  1 116 ? -6.87820  0.68541  5.88670   1.000 25.20680  ?  116 TYR A N   1 
ATOM   1454 C CA  . TYR A  1 116 ? -8.04627  0.50379  5.00612   1.000 27.73767  ?  116 TYR A CA  1 
ATOM   1455 C C   . TYR A  1 116 ? -8.42949  1.79564  4.28033   1.000 26.01850  ?  116 TYR A C   1 
ATOM   1456 O O   . TYR A  1 116 ? -8.75029  1.76776  3.08169   1.000 25.76272  ?  116 TYR A O   1 
ATOM   1457 C CB  . TYR A  1 116 ? -9.26903  0.06426  5.79483   1.000 25.69195  ?  116 TYR A CB  1 
ATOM   1458 C CG  . TYR A  1 116 ? -9.21078  -1.27213 6.45238   1.000 36.20393  ?  116 TYR A CG  1 
ATOM   1459 C CD1 . TYR A  1 116 ? -8.37949  -2.26923 5.98083   1.000 37.40789  ?  116 TYR A CD1 1 
ATOM   1460 C CD2 . TYR A  1 116 ? -10.01596 -1.54175 7.55695   1.000 51.40722  ?  116 TYR A CD2 1 
ATOM   1461 C CE1 . TYR A  1 116 ? -8.35582  -3.52700 6.59475   1.000 46.20655  ?  116 TYR A CE1 1 
ATOM   1462 C CE2 . TYR A  1 116 ? -9.99928  -2.76867 8.17089   1.000 52.29403  ?  116 TYR A CE2 1 
ATOM   1463 C CZ  . TYR A  1 116 ? -9.16825  -3.75866 7.68674   1.000 39.43084  ?  116 TYR A CZ  1 
ATOM   1464 O OH  . TYR A  1 116 ? -9.13727  -4.98548 8.30948   1.000 64.88670  ?  116 TYR A OH  1 
ATOM   1465 N N   . ILE A  1 117 ? -8.45535  2.92501  5.00355   1.000 24.06785  ?  117 ILE A N   1 
ATOM   1466 C CA  . ILE A  1 117 ? -8.71589  4.22221  4.37885   1.000 23.11864  ?  117 ILE A CA  1 
ATOM   1467 C C   . ILE A  1 117 ? -7.69754  4.49418  3.27938   1.000 25.67120  ?  117 ILE A C   1 
ATOM   1468 O O   . ILE A  1 117 ? -8.05101  4.85831  2.14953   1.000 24.86733  ?  117 ILE A O   1 
ATOM   1469 C CB  . ILE A  1 117 ? -8.71213  5.34286  5.43686   1.000 26.16014  ?  117 ILE A CB  1 
ATOM   1470 C CG1 . ILE A  1 117 ? -9.88489  5.16297  6.42382   1.000 22.43757  ?  117 ILE A CG1 1 
ATOM   1471 C CG2 . ILE A  1 117 ? -8.68806  6.73241  4.76317   1.000 22.07379  ?  117 ILE A CG2 1 
ATOM   1472 C CD1 . ILE A  1 117 ? -9.95242  6.23388  7.52597   1.000 23.18136  ?  117 ILE A CD1 1 
ATOM   1473 N N   A CYS A  1 118 ? -6.41544  4.30048  3.56560   0.600 24.08116  ?  118 CYS A N   1 
ATOM   1474 N N   B CYS A  1 118 ? -6.41233  4.35426  3.61574   0.400 24.54953  ?  118 CYS A N   1 
ATOM   1475 C CA  A CYS A  1 118 ? -5.43376  4.62205  2.54069   0.600 25.10143  ?  118 CYS A CA  1 
ATOM   1476 C CA  B CYS A  1 118 ? -5.34363  4.53288  2.64431   0.400 25.21403  ?  118 CYS A CA  1 
ATOM   1477 C C   A CYS A  1 118 ? -5.40345  3.59730  1.41687   0.600 24.91478  ?  118 CYS A C   1 
ATOM   1478 C C   B CYS A  1 118 ? -5.58029  3.64823  1.43169   0.400 24.78196  ?  118 CYS A C   1 
ATOM   1479 O O   A CYS A  1 118 ? -4.98965  3.93982  0.30336   0.600 23.48338  ?  118 CYS A O   1 
ATOM   1480 O O   B CYS A  1 118 ? -5.59029  4.12563  0.28983   0.400 23.35012  ?  118 CYS A O   1 
ATOM   1481 C CB  A CYS A  1 118 ? -4.05159  4.80900  3.15830   0.600 28.16811  ?  118 CYS A CB  1 
ATOM   1482 C CB  B CYS A  1 118 ? -4.00538  4.18692  3.30545   0.400 24.84184  ?  118 CYS A CB  1 
ATOM   1483 S SG  A CYS A  1 118 ? -3.98536  6.19932  4.29694   0.600 35.47591  ?  118 CYS A SG  1 
ATOM   1484 S SG  B CYS A  1 118 ? -2.55354  4.66782  2.33795   0.400 34.56701  ?  118 CYS A SG  1 
ATOM   1485 N N   . LEU A  1 119 ? -5.82063  2.35580  1.67633   1.000 23.41862  ?  119 LEU A N   1 
ATOM   1486 C CA  . LEU A  1 119 ? -5.93503  1.38275  0.59187   1.000 26.64055  ?  119 LEU A CA  1 
ATOM   1487 C C   . LEU A  1 119 ? -7.07150  1.75298  -0.35630  1.000 27.05555  ?  119 LEU A C   1 
ATOM   1488 O O   . LEU A  1 119 ? -6.91794  1.70121  -1.58342  1.000 26.61009  ?  119 LEU A O   1 
ATOM   1489 C CB  . LEU A  1 119 ? -6.17382  -0.01039 1.16802   1.000 26.87892  ?  119 LEU A CB  1 
ATOM   1490 C CG  . LEU A  1 119 ? -6.15550  -1.09373 0.10300   1.000 28.87719  ?  119 LEU A CG  1 
ATOM   1491 C CD1 . LEU A  1 119 ? -4.77662  -1.10460 -0.58383  1.000 28.78015  ?  119 LEU A CD1 1 
ATOM   1492 C CD2 . LEU A  1 119 ? -6.46599  -2.47099 0.72963   1.000 31.54559  ?  119 LEU A CD2 1 
ATOM   1493 N N   . SER A  1 120 ? -8.23717  2.09026  0.20368   1.000 23.45296  ?  120 SER A N   1 
ATOM   1494 C CA  . SER A  1 120 ? -9.36559  2.54980  -0.60835  1.000 26.28410  ?  120 SER A CA  1 
ATOM   1495 C C   . SER A  1 120 ? -8.96366  3.74306  -1.46466  1.000 22.16960  ?  120 SER A C   1 
ATOM   1496 O O   . SER A  1 120 ? -9.27807  3.79307  -2.66381  1.000 24.19633  ?  120 SER A O   1 
ATOM   1497 C CB  . SER A  1 120 ? -10.51579 2.95002  0.31512   1.000 28.81719  ?  120 SER A CB  1 
ATOM   1498 O OG  . SER A  1 120 ? -11.65112 3.38806  -0.41696  1.000 26.78044  ?  120 SER A OG  1 
ATOM   1499 N N   . ASN A  1 121 ? -8.20889  4.67085  -0.87404  1.000 20.67599  ?  121 ASN A N   1 
ATOM   1500 C CA  . ASN A  1 121 ? -7.78172  5.86615  -1.58716  1.000 22.42430  ?  121 ASN A CA  1 
ATOM   1501 C C   . ASN A  1 121 ? -6.76469  5.52063  -2.67050  1.000 23.75745  ?  121 ASN A C   1 
ATOM   1502 O O   . ASN A  1 121 ? -6.81791  6.06048  -3.77820  1.000 22.91313  ?  121 ASN A O   1 
ATOM   1503 C CB  . ASN A  1 121 ? -7.20380  6.86176  -0.59079  1.000 21.27056  ?  121 ASN A CB  1 
ATOM   1504 C CG  . ASN A  1 121 ? -6.72370  8.12602  -1.26111  1.000 20.42773  ?  121 ASN A CG  1 
ATOM   1505 O OD1 . ASN A  1 121 ? -7.53108  8.95513  -1.64762  1.000 23.97630  ?  121 ASN A OD1 1 
ATOM   1506 N ND2 . ASN A  1 121 ? -5.39719  8.30080  -1.37507  1.000 20.98949  ?  121 ASN A ND2 1 
ATOM   1507 N N   . PHE A  1 122 ? -5.84415  4.60403  -2.37348  1.000 25.58156  ?  122 PHE A N   1 
ATOM   1508 C CA  . PHE A  1 122 ? -4.92277  4.12096  -3.39687  1.000 25.53228  ?  122 PHE A CA  1 
ATOM   1509 C C   . PHE A  1 122 ? -5.66725  3.50635  -4.58873  1.000 25.71295  ?  122 PHE A C   1 
ATOM   1510 O O   . PHE A  1 122 ? -5.30315  3.73879  -5.75281  1.000 26.09145  ?  122 PHE A O   1 
ATOM   1511 C CB  . PHE A  1 122 ? -3.91307  3.14691  -2.79839  1.000 27.09299  ?  122 PHE A CB  1 
ATOM   1512 C CG  . PHE A  1 122 ? -2.98863  2.58537  -3.82695  1.000 27.57537  ?  122 PHE A CG  1 
ATOM   1513 C CD1 . PHE A  1 122 ? -1.92240  3.35209  -4.29984  1.000 29.31092  ?  122 PHE A CD1 1 
ATOM   1514 C CD2 . PHE A  1 122 ? -3.21875  1.33526  -4.37690  1.000 31.09648  ?  122 PHE A CD2 1 
ATOM   1515 C CE1 . PHE A  1 122 ? -1.07841  2.83971  -5.29477  1.000 29.92912  ?  122 PHE A CE1 1 
ATOM   1516 C CE2 . PHE A  1 122 ? -2.38026  0.82337  -5.35893  1.000 29.28239  ?  122 PHE A CE2 1 
ATOM   1517 C CZ  . PHE A  1 122 ? -1.32382  1.57759  -5.81899  1.000 34.28375  ?  122 PHE A CZ  1 
ATOM   1518 N N   . PHE A  1 123 ? -6.72587  2.72759  -4.32880  1.000 23.31787  ?  123 PHE A N   1 
ATOM   1519 C CA  . PHE A  1 123 ? -7.47385  2.13672  -5.43161  1.000 25.58060  ?  123 PHE A CA  1 
ATOM   1520 C C   . PHE A  1 123 ? -8.17232  3.20323  -6.26648  1.000 25.18090  ?  123 PHE A C   1 
ATOM   1521 O O   . PHE A  1 123 ? -8.24281  3.08766  -7.50318  1.000 24.78757  ?  123 PHE A O   1 
ATOM   1522 C CB  . PHE A  1 123 ? -8.46115  1.09175  -4.91648  1.000 26.35156  ?  123 PHE A CB  1 
ATOM   1523 C CG  . PHE A  1 123 ? -7.79978  -0.17292 -4.46299  1.000 30.18891  ?  123 PHE A CG  1 
ATOM   1524 C CD1 . PHE A  1 123 ? -6.65509  -0.62264 -5.10036  1.000 39.28326  ?  123 PHE A CD1 1 
ATOM   1525 C CD2 . PHE A  1 123 ? -8.31044  -0.91829 -3.41014  1.000 35.74803  ?  123 PHE A CD2 1 
ATOM   1526 C CE1 . PHE A  1 123 ? -6.01490  -1.80206 -4.68805  1.000 57.62638  ?  123 PHE A CE1 1 
ATOM   1527 C CE2 . PHE A  1 123 ? -7.68064  -2.09222 -2.99719  1.000 39.80707  ?  123 PHE A CE2 1 
ATOM   1528 C CZ  . PHE A  1 123 ? -6.52765  -2.52863 -3.63840  1.000 37.87871  ?  123 PHE A CZ  1 
ATOM   1529 N N   . MET A  1 124 ? -8.71284  4.23576  -5.61081  1.000 23.60037  ?  124 MET A N   1 
ATOM   1530 C CA  . MET A  1 124 ? -9.25658  5.36386  -6.36168  1.000 23.79525  ?  124 MET A CA  1 
ATOM   1531 C C   . MET A  1 124 ? -8.21769  5.94340  -7.32865  1.000 19.84310  ?  124 MET A C   1 
ATOM   1532 O O   . MET A  1 124 ? -8.48370  6.10234  -8.52042  1.000 23.67849  ?  124 MET A O   1 
ATOM   1533 C CB  . MET A  1 124 ? -9.74996  6.40881  -5.36776  1.000 20.46556  ?  124 MET A CB  1 
ATOM   1534 C CG  . MET A  1 124 ? -10.42993 7.64324  -6.03865  1.000 27.03510  ?  124 MET A CG  1 
ATOM   1535 S SD  . MET A  1 124 ? -10.56069 9.02663  -4.91197  1.000 24.72140  ?  124 MET A SD  1 
ATOM   1536 C CE  . MET A  1 124 ? -8.83762  9.45194  -4.65440  1.000 21.91616  ?  124 MET A CE  1 
ATOM   1537 N N   . LEU A  1 125 ? -7.00877  6.23051  -6.81698  1.000 21.49149  ?  125 LEU A N   1 
ATOM   1538 C CA  . LEU A  1 125 ? -5.96536  6.82889  -7.64965  1.000 23.61133  ?  125 LEU A CA  1 
ATOM   1539 C C   . LEU A  1 125 ? -5.51425  5.87607  -8.75605  1.000 24.91444  ?  125 LEU A C   1 
ATOM   1540 O O   . LEU A  1 125 ? -5.30262  6.29575  -9.90562  1.000 24.60100  ?  125 LEU A O   1 
ATOM   1541 C CB  . LEU A  1 125 ? -4.77001  7.24342  -6.79451  1.000 22.16798  ?  125 LEU A CB  1 
ATOM   1542 C CG  . LEU A  1 125 ? -5.04488  8.32846  -5.76509  1.000 22.86424  ?  125 LEU A CG  1 
ATOM   1543 C CD1 . LEU A  1 125 ? -3.80571  8.60925  -4.85130  1.000 24.18249  ?  125 LEU A CD1 1 
ATOM   1544 C CD2 . LEU A  1 125 ? -5.54454  9.57961  -6.43008  1.000 23.88849  ?  125 LEU A CD2 1 
ATOM   1545 N N   . LEU A  1 126 ? -5.33371  4.59186  -8.41818  1.000 24.51141  ?  126 LEU A N   1 
ATOM   1546 C CA  . LEU A  1 126 ? -4.96148  3.59400  -9.42162  1.000 25.39464  ?  126 LEU A CA  1 
ATOM   1547 C C   . LEU A  1 126 ? -5.96400  3.55120  -10.57240 1.000 23.51027  ?  126 LEU A C   1 
ATOM   1548 O O   . LEU A  1 126 ? -5.58479  3.54724  -11.75515 1.000 25.41981  ?  126 LEU A O   1 
ATOM   1549 C CB  . LEU A  1 126 ? -4.85961  2.23115  -8.74291  1.000 23.75244  ?  126 LEU A CB  1 
ATOM   1550 C CG  . LEU A  1 126 ? -4.63723  1.06261  -9.70018  1.000 31.96029  ?  126 LEU A CG  1 
ATOM   1551 C CD1 . LEU A  1 126 ? -3.34956  1.27024  -10.48266 1.000 33.27818  ?  126 LEU A CD1 1 
ATOM   1552 C CD2 . LEU A  1 126 ? -4.64213  -0.26572 -8.90106  1.000 32.47566  ?  126 LEU A CD2 1 
ATOM   1553 N N   . ILE A  1 127 ? -7.25983  3.53398  -10.25113 1.000 26.19961  ?  127 ILE A N   1 
ATOM   1554 C CA  . ILE A  1 127 ? -8.27814  3.50448  -11.29397 1.000 28.99229  ?  127 ILE A CA  1 
ATOM   1555 C C   . ILE A  1 127 ? -8.23375  4.79128  -12.12163 1.000 24.81669  ?  127 ILE A C   1 
ATOM   1556 O O   . ILE A  1 127 ? -8.26532  4.74459  -13.36489 1.000 26.93252  ?  127 ILE A O   1 
ATOM   1557 C CB  . ILE A  1 127 ? -9.65165  3.25033  -10.64565 1.000 25.52715  ?  127 ILE A CB  1 
ATOM   1558 C CG1 . ILE A  1 127 ? -9.67814  1.82161  -10.08426 1.000 28.56345  ?  127 ILE A CG1 1 
ATOM   1559 C CG2 . ILE A  1 127 ? -10.78371 3.51035  -11.63965 1.000 29.26496  ?  127 ILE A CG2 1 
ATOM   1560 C CD1 . ILE A  1 127 ? -10.89315 1.56011  -9.18637  1.000 31.99419  ?  127 ILE A CD1 1 
ATOM   1561 N N   . GLY A  1 128 ? -8.11544  5.94734  -11.44731 1.000 23.96810  ?  128 GLY A N   1 
ATOM   1562 C CA  . GLY A  1 128 ? -7.89189  7.19554  -12.16884 1.000 24.80327  ?  128 GLY A CA  1 
ATOM   1563 C C   . GLY A  1 128 ? -6.69935  7.13196  -13.09102 1.000 24.30135  ?  128 GLY A C   1 
ATOM   1564 O O   . GLY A  1 128 ? -6.76845  7.54695  -14.25616 1.000 29.29616  ?  128 GLY A O   1 
ATOM   1565 N N   A TYR A  1 129 ? -5.57457  6.60348  -12.59838 0.600 24.62907  ?  129 TYR A N   1 
ATOM   1566 N N   B TYR A  1 129 ? -5.56561  6.60754  -12.60606 0.400 24.85865  ?  129 TYR A N   1 
ATOM   1567 C CA  A TYR A  1 129 ? -4.36798  6.54975  -13.40821 0.600 26.97554  ?  129 TYR A CA  1 
ATOM   1568 C CA  B TYR A  1 129 ? -4.37104  6.55896  -13.44248 0.400 26.96223  ?  129 TYR A CA  1 
ATOM   1569 C C   A TYR A  1 129 ? -4.57615  5.68284  -14.64238 0.600 26.22639  ?  129 TYR A C   1 
ATOM   1570 C C   B TYR A  1 129 ? -4.59595  5.68505  -14.66484 0.400 26.35798  ?  129 TYR A C   1 
ATOM   1571 O O   A TYR A  1 129 ? -4.14589  6.04317  -15.75173 0.600 29.90221  ?  129 TYR A O   1 
ATOM   1572 O O   B TYR A  1 129 ? -4.17663  6.03168  -15.78033 0.400 30.03982  ?  129 TYR A O   1 
ATOM   1573 C CB  A TYR A  1 129 ? -3.20239  6.05377  -12.55773 0.600 25.80078  ?  129 TYR A CB  1 
ATOM   1574 C CB  B TYR A  1 129 ? -3.16679  6.06377  -12.64612 0.400 25.92854  ?  129 TYR A CB  1 
ATOM   1575 C CG  A TYR A  1 129 ? -1.87562  6.09048  -13.27827 0.600 29.42317  ?  129 TYR A CG  1 
ATOM   1576 C CG  B TYR A  1 129 ? -1.96031  5.75857  -13.51900 0.400 26.43581  ?  129 TYR A CG  1 
ATOM   1577 C CD1 A TYR A  1 129 ? -1.07130  7.22773  -13.24164 0.600 29.35956  ?  129 TYR A CD1 1 
ATOM   1578 C CD1 B TYR A  1 129 ? -1.09507  6.77303  -13.92656 0.400 24.01986  ?  129 TYR A CD1 1 
ATOM   1579 C CD2 A TYR A  1 129 ? -1.42071  4.98969  -13.99101 0.600 29.08673  ?  129 TYR A CD2 1 
ATOM   1580 C CD2 B TYR A  1 129 ? -1.68626  4.45887  -13.93433 0.400 31.71434  ?  129 TYR A CD2 1 
ATOM   1581 C CE1 A TYR A  1 129 ? 0.14212   7.26099  -13.89820 0.600 25.55159  ?  129 TYR A CE1 1 
ATOM   1582 C CE1 B TYR A  1 129 ? 0.00600   6.50043  -14.70450 0.400 34.72721  ?  129 TYR A CE1 1 
ATOM   1583 C CE2 A TYR A  1 129 ? -0.20824  5.01792  -14.64761 0.600 36.10186  ?  129 TYR A CE2 1 
ATOM   1584 C CE2 B TYR A  1 129 ? -0.59194  4.17630  -14.72989 0.400 34.74046  ?  129 TYR A CE2 1 
ATOM   1585 C CZ  A TYR A  1 129 ? 0.57194   6.15687  -14.59167 0.600 27.39082  ?  129 TYR A CZ  1 
ATOM   1586 C CZ  B TYR A  1 129 ? 0.25258   5.19977  -15.11315 0.400 38.55014  ?  129 TYR A CZ  1 
ATOM   1587 O OH  A TYR A  1 129 ? 1.77948   6.19329  -15.24990 0.600 38.51766  ?  129 TYR A OH  1 
ATOM   1588 O OH  B TYR A  1 129 ? 1.34481   4.92420  -15.90306 0.400 42.91053  ?  129 TYR A OH  1 
ATOM   1589 N N   . LEU A  1 130 ? -5.25887  4.54241  -14.47493 1.000 25.99451  ?  130 LEU A N   1 
ATOM   1590 C CA  . LEU A  1 130 ? -5.58495  3.67959  -15.59964 1.000 27.13416  ?  130 LEU A CA  1 
ATOM   1591 C C   . LEU A  1 130 ? -6.47543  4.39771  -16.61037 1.000 28.89961  ?  130 LEU A C   1 
ATOM   1592 O O   . LEU A  1 130 ? -6.28638  4.25731  -17.82170 1.000 33.86457  ?  130 LEU A O   1 
ATOM   1593 C CB  . LEU A  1 130 ? -6.22861  2.38074  -15.10231 1.000 28.70815  ?  130 LEU A CB  1 
ATOM   1594 C CG  . LEU A  1 130 ? -5.28356  1.53996  -14.21426 1.000 29.93443  ?  130 LEU A CG  1 
ATOM   1595 C CD1 . LEU A  1 130 ? -6.00255  0.39635  -13.55854 1.000 34.36262  ?  130 LEU A CD1 1 
ATOM   1596 C CD2 . LEU A  1 130 ? -4.08495  1.05535  -14.97521 1.000 34.92048  ?  130 LEU A CD2 1 
ATOM   1597 N N   . GLY A  1 131 ? -7.43933  5.18814  -16.13067 1.000 28.61185  ?  131 GLY A N   1 
ATOM   1598 C CA  . GLY A  1 131 ? -8.26283  5.95602  -17.04967 1.000 35.64082  ?  131 GLY A CA  1 
ATOM   1599 C C   . GLY A  1 131 ? -7.52565  7.11185  -17.69311 1.000 31.56458  ?  131 GLY A C   1 
ATOM   1600 O O   . GLY A  1 131 ? -7.74301  7.41348  -18.87338 1.000 35.61709  ?  131 GLY A O   1 
ATOM   1601 N N   A GLU A  1 132 ? -6.72084  7.82648  -16.89475 0.600 30.14493  ?  132 GLU A N   1 
ATOM   1602 N N   B GLU A  1 132 ? -6.57905  7.72885  -16.99529 0.400 30.15936  ?  132 GLU A N   1 
ATOM   1603 C CA  A GLU A  1 132 ? -6.02066  9.02411  -17.35143 0.600 30.53489  ?  132 GLU A CA  1 
ATOM   1604 C CA  B GLU A  1 132 ? -5.82068  8.78026  -17.66918 0.400 33.69434  ?  132 GLU A CA  1 
ATOM   1605 C C   A GLU A  1 132 ? -4.97922  8.67958  -18.40295 0.600 33.42784  ?  132 GLU A C   1 
ATOM   1606 C C   B GLU A  1 132 ? -4.91052  8.19942  -18.74555 0.400 39.06339  ?  132 GLU A C   1 
ATOM   1607 O O   A GLU A  1 132 ? -4.65284  9.52043  -19.24812 0.600 31.79308  ?  132 GLU A O   1 
ATOM   1608 O O   B GLU A  1 132 ? -4.92158  8.65724  -19.89747 0.400 32.00071  ?  132 GLU A O   1 
ATOM   1609 C CB  A GLU A  1 132 ? -5.36256  9.72467  -16.15326 0.600 34.05336  ?  132 GLU A CB  1 
ATOM   1610 C CB  B GLU A  1 132 ? -5.04172  9.63326  -16.67584 0.400 30.30484  ?  132 GLU A CB  1 
ATOM   1611 C CG  A GLU A  1 132 ? -4.71073  11.06597 -16.46902 0.600 30.55702  ?  132 GLU A CG  1 
ATOM   1612 C CG  B GLU A  1 132 ? -4.88201  11.05303 -17.16457 0.400 37.97534  ?  132 GLU A CG  1 
ATOM   1613 C CD  A GLU A  1 132 ? -5.70989  12.06598 -17.02982 0.600 27.54367  ?  132 GLU A CD  1 
ATOM   1614 C CD  B GLU A  1 132 ? -6.14612  11.56683 -17.83965 0.400 29.91541  ?  132 GLU A CD  1 
ATOM   1615 O OE1 A GLU A  1 132 ? -6.73787  12.31419 -16.36400 0.600 21.86497  ?  132 GLU A OE1 1 
ATOM   1616 O OE1 B GLU A  1 132 ? -7.17779  11.75049 -17.14482 0.400 27.00302  ?  132 GLU A OE1 1 
ATOM   1617 O OE2 A GLU A  1 132 ? -5.46748  12.58060 -18.14310 0.600 27.80033  -1 132 GLU A OE2 1 
ATOM   1618 O OE2 B GLU A  1 132 ? -6.11261  11.77661 -19.06620 0.400 31.20421  -1 132 GLU A OE2 1 
ATOM   1619 N N   A THR A  1 133 ? -4.45307  7.45141  -18.36649 0.600 38.94957  ?  133 THR A N   1 
ATOM   1620 N N   B THR A  1 133 ? -4.13696  7.16518  -18.40045 0.400 38.40524  ?  133 THR A N   1 
ATOM   1621 C CA  A THR A  1 133 ? -3.49296  6.95417  -19.34378 0.600 38.36789  ?  133 THR A CA  1 
ATOM   1622 C CA  B THR A  1 133 ? -3.30221  6.48895  -19.38616 0.400 39.23326  ?  133 THR A CA  1 
ATOM   1623 C C   A THR A  1 133 ? -4.13788  6.03221  -20.37485 0.600 40.09112  ?  133 THR A C   1 
ATOM   1624 C C   B THR A  1 133 ? -4.15996  5.66500  -20.32651 0.400 38.46647  ?  133 THR A C   1 
ATOM   1625 O O   A THR A  1 133 ? -3.42494  5.41426  -21.17174 0.600 37.57447  ?  133 THR A O   1 
ATOM   1626 O O   B THR A  1 133 ? -3.64114  4.76679  -21.00095 0.400 45.78369  ?  133 THR A O   1 
ATOM   1627 C CB  A THR A  1 133 ? -2.30113  6.27357  -18.64306 0.600 42.92525  ?  133 THR A CB  1 
ATOM   1628 C CB  B THR A  1 133 ? -2.29052  5.54534  -18.73038 0.400 37.45144  ?  133 THR A CB  1 
ATOM   1629 O OG1 A THR A  1 133 ? -2.75680  5.14562  -17.88652 0.600 31.46809  ?  133 THR A OG1 1 
ATOM   1630 O OG1 B THR A  1 133 ? -2.98994  4.54470  -17.97709 0.400 37.12274  ?  133 THR A OG1 1 
ATOM   1631 C CG2 A THR A  1 133 ? -1.61664  7.24522  -17.67990 0.600 32.45330  ?  133 THR A CG2 1 
ATOM   1632 C CG2 B THR A  1 133 ? -1.34683  6.31416  -17.82428 0.400 33.81851  ?  133 THR A CG2 1 
ATOM   1633 N N   . LYS A  1 134 ? -5.47002  5.92608  -20.35197 1.000 42.82622  ?  134 LYS A N   1 
ATOM   1634 C CA  . LYS A  1 134 ? -6.33286  5.31986  -21.35762 1.000 38.73377  ?  134 LYS A CA  1 
ATOM   1635 C C   . LYS A  1 134 ? -6.25654  3.80177  -21.38211 1.000 36.77077  ?  134 LYS A C   1 
ATOM   1636 O O   . LYS A  1 134 ? -6.43758  3.19037  -22.43722 1.000 48.38010  ?  134 LYS A O   1 
ATOM   1637 C CB  . LYS A  1 134 ? -6.06730  5.89242  -22.76175 1.000 41.30959  ?  134 LYS A CB  1 
ATOM   1638 C CG  . LYS A  1 134 ? -6.11417  7.43483  -22.84659 1.000 52.40821  ?  134 LYS A CG  1 
ATOM   1639 C CD  . LYS A  1 134 ? -7.51297  7.98237  -22.66272 1.000 56.21723  ?  134 LYS A CD  1 
ATOM   1640 N N   . GLN A  1 135 ? -5.97314  3.19562  -20.22569 1.000 40.13042  ?  135 GLN A N   1 
ATOM   1641 C CA  . GLN A  1 135 ? -5.92013  1.74832  -20.09339 1.000 35.70920  ?  135 GLN A CA  1 
ATOM   1642 C C   . GLN A  1 135 ? -7.27896  1.12541  -19.80714 1.000 45.91159  ?  135 GLN A C   1 
ATOM   1643 O O   . GLN A  1 135 ? -7.44545  -0.07992 -20.01613 1.000 45.53855  ?  135 GLN A O   1 
ATOM   1644 C CB  . GLN A  1 135 ? -4.91558  1.37105  -18.99867 1.000 36.82837  ?  135 GLN A CB  1 
ATOM   1645 C CG  . GLN A  1 135 ? -3.47935  1.62823  -19.41074 1.000 42.91922  ?  135 GLN A CG  1 
ATOM   1646 C CD  . GLN A  1 135 ? -2.50857  0.58385  -18.86822 1.000 78.46853  ?  135 GLN A CD  1 
ATOM   1647 O OE1 . GLN A  1 135 ? -2.81259  -0.13558 -17.92024 1.000 55.27266  ?  135 GLN A OE1 1 
ATOM   1648 N NE2 . GLN A  1 135 ? -1.33658  0.49435  -19.48131 1.000 74.74954  ?  135 GLN A NE2 1 
ATOM   1649 N N   . ILE A  1 136 ? -8.23632  1.91192  -19.30992 1.000 45.05270  ?  136 ILE A N   1 
ATOM   1650 C CA  . ILE A  1 136 ? -9.63450  1.51946  -19.16006 1.000 37.15028  ?  136 ILE A CA  1 
ATOM   1651 C C   . ILE A  1 136 ? -10.46023 2.70403  -19.63788 1.000 39.05494  ?  136 ILE A C   1 
ATOM   1652 O O   . ILE A  1 136 ? -9.96023  3.82390  -19.74049 1.000 40.59557  ?  136 ILE A O   1 
ATOM   1653 C CB  . ILE A  1 136 ? -9.99329  1.19811  -17.69416 1.000 37.77184  ?  136 ILE A CB  1 
ATOM   1654 C CG1 . ILE A  1 136 ? -9.71995  2.42265  -16.80127 1.000 36.01255  ?  136 ILE A CG1 1 
ATOM   1655 C CG2 . ILE A  1 136 ? -9.21252  -0.02040 -17.21488 1.000 43.18097  ?  136 ILE A CG2 1 
ATOM   1656 C CD1 . ILE A  1 136 ? -10.00665 2.22662  -15.29739 1.000 44.97267  ?  136 ILE A CD1 1 
ATOM   1657 N N   . ASN A  1 137 ? -11.74080 2.46248  -19.91447 1.000 38.42842  ?  137 ASN A N   1 
ATOM   1658 C CA  . ASN A  1 137 ? -12.53748 3.54888  -20.47686 1.000 52.37028  ?  137 ASN A CA  1 
ATOM   1659 C C   . ASN A  1 137 ? -12.90075 4.58602  -19.41167 1.000 45.80413  ?  137 ASN A C   1 
ATOM   1660 O O   . ASN A  1 137 ? -12.77534 4.35445  -18.20543 1.000 41.77553  ?  137 ASN A O   1 
ATOM   1661 C CB  . ASN A  1 137 ? -13.77662 3.02567  -21.20786 1.000 50.34804  ?  137 ASN A CB  1 
ATOM   1662 C CG  . ASN A  1 137 ? -14.76871 2.35931  -20.28316 1.000 97.39905  ?  137 ASN A CG  1 
ATOM   1663 O OD1 . ASN A  1 137 ? -15.32856 2.99444  -19.40378 1.000 44.45376  ?  137 ASN A OD1 1 
ATOM   1664 N ND2 . ASN A  1 137 ? -15.01173 1.08125  -20.49690 1.000 66.81276  ?  137 ASN A ND2 1 
ATOM   1665 N N   . LYS A  1 138 ? -13.33459 5.76271  -19.87925 1.000 45.21987  ?  138 LYS A N   1 
ATOM   1666 C CA  . LYS A  1 138 ? -13.62664 6.86299  -18.96248 1.000 45.04128  ?  138 LYS A CA  1 
ATOM   1667 C C   . LYS A  1 138 ? -14.79342 6.52108  -18.04228 1.000 50.03885  ?  138 LYS A C   1 
ATOM   1668 O O   . LYS A  1 138 ? -14.79172 6.89380  -16.86003 1.000 36.63483  ?  138 LYS A O   1 
ATOM   1669 C CB  . LYS A  1 138 ? -13.93812 8.14057  -19.75205 1.000 50.95858  ?  138 LYS A CB  1 
ATOM   1670 C CG  . LYS A  1 138 ? -12.71048 8.90087  -20.27401 1.000 50.20192  ?  138 LYS A CG  1 
ATOM   1671 N N   A MET A  1 139 ? -15.76819 5.75655  -18.54889 0.600 41.96352  ?  139 MET A N   1 
ATOM   1672 N N   B MET A  1 139 ? -15.82765 5.87013  -18.57822 0.400 42.18727  ?  139 MET A N   1 
ATOM   1673 C CA  A MET A  1 139 ? -16.93298 5.40224  -17.74213 0.600 45.08567  ?  139 MET A CA  1 
ATOM   1674 C CA  B MET A  1 139 ? -17.00521 5.60267  -17.76036 0.400 44.86479  ?  139 MET A CA  1 
ATOM   1675 C C   A MET A  1 139 ? -16.56057 4.44770  -16.61393 0.600 34.64340  ?  139 MET A C   1 
ATOM   1676 C C   B MET A  1 139 ? -16.67928 4.63954  -16.62866 0.400 35.26610  ?  139 MET A C   1 
ATOM   1677 O O   A MET A  1 139 ? -17.01648 4.61731  -15.47533 0.600 41.75601  ?  139 MET A O   1 
ATOM   1678 O O   B MET A  1 139 ? -17.13015 4.83226  -15.49175 0.400 40.41668  ?  139 MET A O   1 
ATOM   1679 C CB  A MET A  1 139 ? -18.02522 4.79905  -18.62632 0.600 49.11167  ?  139 MET A CB  1 
ATOM   1680 C CB  B MET A  1 139 ? -18.15935 5.08942  -18.62067 0.400 49.70460  ?  139 MET A CB  1 
ATOM   1681 C CG  A MET A  1 139 ? -19.40423 4.81144  -17.99109 0.600 53.37102  ?  139 MET A CG  1 
ATOM   1682 C CG  B MET A  1 139 ? -19.31236 6.07353  -18.72038 0.400 46.88608  ?  139 MET A CG  1 
ATOM   1683 S SD  A MET A  1 139 ? -20.70678 4.28493  -19.13164 0.600 86.55374  ?  139 MET A SD  1 
ATOM   1684 S SD  B MET A  1 139 ? -20.90340 5.24987  -18.90750 0.400 78.78148  ?  139 MET A SD  1 
ATOM   1685 C CE  A MET A  1 139 ? -22.14564 5.05504  -18.37693 0.600 57.36998  ?  139 MET A CE  1 
ATOM   1686 C CE  B MET A  1 139 ? -20.73046 3.92406  -17.70676 0.400 56.55272  ?  139 MET A CE  1 
ATOM   1687 N N   A LEU A  1 140 ? -15.73565 3.43603  -16.90590 0.600 37.14901  ?  140 LEU A N   1 
ATOM   1688 N N   B LEU A  1 140 ? -15.87654 3.61236  -16.91522 0.400 38.28173  ?  140 LEU A N   1 
ATOM   1689 C CA  A LEU A  1 140 ? -15.25803 2.55718  -15.84371 0.600 39.18989  ?  140 LEU A CA  1 
ATOM   1690 C CA  B LEU A  1 140 ? -15.41486 2.72258  -15.85773 0.400 39.52416  ?  140 LEU A CA  1 
ATOM   1691 C C   A LEU A  1 140 ? -14.38118 3.31037  -14.84773 0.600 33.56722  ?  140 LEU A C   1 
ATOM   1692 C C   B LEU A  1 140 ? -14.56581 3.47695  -14.84020 0.400 35.15950  ?  140 LEU A C   1 
ATOM   1693 O O   A LEU A  1 140 ? -14.38684 2.99205  -13.65006 0.600 33.74710  ?  140 LEU A O   1 
ATOM   1694 O O   B LEU A  1 140 ? -14.75179 3.31277  -13.62776 0.400 37.49107  ?  140 LEU A O   1 
ATOM   1695 C CB  A LEU A  1 140 ? -14.50847 1.36379  -16.43927 0.600 47.01670  ?  140 LEU A CB  1 
ATOM   1696 C CB  B LEU A  1 140 ? -14.63045 1.55743  -16.46052 0.400 46.70325  ?  140 LEU A CB  1 
ATOM   1697 C CG  A LEU A  1 140 ? -13.76478 0.43386  -15.47257 0.600 48.68923  ?  140 LEU A CG  1 
ATOM   1698 C CG  B LEU A  1 140 ? -14.24970 0.42240  -15.50735 0.400 43.03536  ?  140 LEU A CG  1 
ATOM   1699 C CD1 A LEU A  1 140 ? -14.66561 -0.06491 -14.34556 0.600 46.39955  ?  140 LEU A CD1 1 
ATOM   1700 C CD1 B LEU A  1 140 ? -15.48770 -0.25324 -14.94841 0.400 43.04270  ?  140 LEU A CD1 1 
ATOM   1701 C CD2 A LEU A  1 140 ? -13.14990 -0.74181 -16.23293 0.600 50.17327  ?  140 LEU A CD2 1 
ATOM   1702 C CD2 B LEU A  1 140 ? -13.36285 -0.59164 -16.21579 0.400 49.95569  ?  140 LEU A CD2 1 
ATOM   1703 N N   . THR A  1 141 ? -13.63247 4.31334  -15.31478 1.000 35.54047  ?  141 THR A N   1 
ATOM   1704 C CA  . THR A  1 141 ? -12.79662 5.09296  -14.40405 1.000 30.19877  ?  141 THR A CA  1 
ATOM   1705 C C   . THR A  1 141 ? -13.65748 5.91320  -13.46831 1.000 28.54729  ?  141 THR A C   1 
ATOM   1706 O O   . THR A  1 141 ? -13.41322 5.95920  -12.25937 1.000 29.44852  ?  141 THR A O   1 
ATOM   1707 C CB  . THR A  1 141 ? -11.87846 6.03643  -15.19051 1.000 31.85016  ?  141 THR A CB  1 
ATOM   1708 O OG1 . THR A  1 141 ? -11.14442 5.30431  -16.17912 1.000 32.13689  ?  141 THR A OG1 1 
ATOM   1709 C CG2 . THR A  1 141 ? -10.89087 6.75683  -14.21824 1.000 26.90430  ?  141 THR A CG2 1 
ATOM   1710 N N   A LEU A  1 142 ? -14.69112 6.56208  -14.00302 0.600 32.18341  ?  142 LEU A N   1 
ATOM   1711 N N   B LEU A  1 142 ? -14.68136 6.57697  -14.01337 0.400 32.17067  ?  142 LEU A N   1 
ATOM   1712 C CA  A LEU A  1 142 ? -15.50416 7.43126  -13.16151 0.600 33.79506  ?  142 LEU A CA  1 
ATOM   1713 C CA  B LEU A  1 142 ? -15.54148 7.42321  -13.19211 0.400 33.95170  ?  142 LEU A CA  1 
ATOM   1714 C C   A LEU A  1 142 ? -16.31858 6.63191  -12.15143 0.600 37.93453  ?  142 LEU A C   1 
ATOM   1715 C C   B LEU A  1 142 ? -16.29355 6.59640  -12.15741 0.400 37.92543  ?  142 LEU A C   1 
ATOM   1716 O O   A LEU A  1 142 ? -16.49435 7.07037  -11.01158 0.600 35.21087  ?  142 LEU A O   1 
ATOM   1717 O O   B LEU A  1 142 ? -16.30719 6.93672  -10.97019 0.400 35.30038  ?  142 LEU A O   1 
ATOM   1718 C CB  A LEU A  1 142 ? -16.39691 8.32481  -14.02032 0.600 34.33861  ?  142 LEU A CB  1 
ATOM   1719 C CB  B LEU A  1 142 ? -16.50847 8.21678  -14.07642 0.400 34.63601  ?  142 LEU A CB  1 
ATOM   1720 C CG  A LEU A  1 142 ? -15.68748 9.49255  -14.70869 0.600 31.56134  ?  142 LEU A CG  1 
ATOM   1721 C CG  B LEU A  1 142 ? -17.37585 9.29547  -13.41022 0.400 37.02536  ?  142 LEU A CG  1 
ATOM   1722 C CD1 A LEU A  1 142 ? -16.60018 10.07682 -15.76574 0.600 38.38262  ?  142 LEU A CD1 1 
ATOM   1723 C CD1 B LEU A  1 142 ? -16.54387 10.47974 -12.90671 0.400 31.83111  ?  142 LEU A CD1 1 
ATOM   1724 C CD2 A LEU A  1 142 ? -15.27354 10.56909 -13.70840 0.600 25.68520  ?  142 LEU A CD2 1 
ATOM   1725 C CD2 B LEU A  1 142 ? -18.45411 9.75849  -14.37847 0.400 49.83352  ?  142 LEU A CD2 1 
ATOM   1726 N N   A PHE A  1 143 ? -16.81118 5.45240  -12.53523 0.600 40.99642  ?  143 PHE A N   1 
ATOM   1727 N N   B PHE A  1 143 ? -16.91950 5.49781  -12.58730 0.400 40.89188  ?  143 PHE A N   1 
ATOM   1728 C CA  A PHE A  1 143 ? -17.59463 4.66112  -11.58669 0.600 45.10434  ?  143 PHE A CA  1 
ATOM   1729 C CA  B PHE A  1 143 ? -17.58807 4.61224  -11.63700 0.400 44.89354  ?  143 PHE A CA  1 
ATOM   1730 C C   A PHE A  1 143 ? -16.70253 3.96857  -10.55772 0.600 34.00283  ?  143 PHE A C   1 
ATOM   1731 C C   B PHE A  1 143 ? -16.60924 4.12192  -10.57702 0.400 33.95815  ?  143 PHE A C   1 
ATOM   1732 O O   A PHE A  1 143 ? -17.00671 3.97738  -9.35935  0.600 33.81746  ?  143 PHE A O   1 
ATOM   1733 O O   B PHE A  1 143 ? -16.74039 4.44384  -9.38889  0.400 31.60735  ?  143 PHE A O   1 
ATOM   1734 C CB  A PHE A  1 143 ? -18.48717 3.65354  -12.31323 0.600 42.37259  ?  143 PHE A CB  1 
ATOM   1735 C CB  B PHE A  1 143 ? -18.21755 3.41922  -12.36257 0.400 39.54854  ?  143 PHE A CB  1 
ATOM   1736 C CG  A PHE A  1 143 ? -19.74733 4.25730  -12.88219 0.600 49.71661  ?  143 PHE A CG  1 
ATOM   1737 C CG  B PHE A  1 143 ? -18.80654 2.39289  -11.43192 0.400 45.39249  ?  143 PHE A CG  1 
ATOM   1738 C CD1 A PHE A  1 143 ? -20.73252 4.75324  -12.04334 0.600 48.68477  ?  143 PHE A CD1 1 
ATOM   1739 C CD1 B PHE A  1 143 ? -20.06192 2.58411  -10.87622 0.400 50.11653  ?  143 PHE A CD1 1 
ATOM   1740 C CD2 A PHE A  1 143 ? -19.94990 4.32064  -14.25229 0.600 59.11404  ?  143 PHE A CD2 1 
ATOM   1741 C CD2 B PHE A  1 143 ? -18.09929 1.24753  -11.09996 0.400 39.34775  ?  143 PHE A CD2 1 
ATOM   1742 C CE1 A PHE A  1 143 ? -21.89313 5.30400  -12.56554 0.600 47.07605  ?  143 PHE A CE1 1 
ATOM   1743 C CE1 B PHE A  1 143 ? -20.60374 1.65095  -10.01072 0.400 46.93590  ?  143 PHE A CE1 1 
ATOM   1744 C CE2 A PHE A  1 143 ? -21.10665 4.87153  -14.77799 0.600 42.09654  ?  143 PHE A CE2 1 
ATOM   1745 C CE2 B PHE A  1 143 ? -18.63309 0.31341  -10.23492 0.400 44.14484  ?  143 PHE A CE2 1 
ATOM   1746 C CZ  A PHE A  1 143 ? -22.07689 5.36395  -13.93133 0.600 47.63784  ?  143 PHE A CZ  1 
ATOM   1747 C CZ  B PHE A  1 143 ? -19.88679 0.51393  -9.69030  0.400 49.65105  ?  143 PHE A CZ  1 
ATOM   1748 N N   . GLY A  1 144 ? -15.60779 3.35012  -11.00571 1.000 34.22462  ?  144 GLY A N   1 
ATOM   1749 C CA  . GLY A  1 144 ? -14.70343 2.71176  -10.06178 1.000 29.29720  ?  144 GLY A CA  1 
ATOM   1750 C C   . GLY A  1 144 ? -14.03970 3.71589  -9.14570  1.000 30.26677  ?  144 GLY A C   1 
ATOM   1751 O O   . GLY A  1 144 ? -13.98395 3.53276  -7.93163  1.000 29.98278  ?  144 GLY A O   1 
ATOM   1752 N N   . GLY A  1 145 ? -13.55439 4.81273  -9.71275  1.000 28.14875  ?  145 GLY A N   1 
ATOM   1753 C CA  . GLY A  1 145 ? -12.93959 5.83692  -8.88210  1.000 25.58105  ?  145 GLY A CA  1 
ATOM   1754 C C   . GLY A  1 145 ? -13.92036 6.46636  -7.90477  1.000 24.76705  ?  145 GLY A C   1 
ATOM   1755 O O   . GLY A  1 145 ? -13.57171 6.74478  -6.75980  1.000 28.63149  ?  145 GLY A O   1 
ATOM   1756 N N   . SER A  1 146 ? -15.16324 6.69232  -8.34257  1.000 27.04244  ?  146 SER A N   1 
ATOM   1757 C CA  . SER A  1 146 ? -16.15341 7.28138  -7.44900  1.000 28.97449  ?  146 SER A CA  1 
ATOM   1758 C C   . SER A  1 146 ? -16.51476 6.31889  -6.33418  1.000 29.62518  ?  146 SER A C   1 
ATOM   1759 O O   . SER A  1 146 ? -16.65527 6.73908  -5.17626  1.000 29.03702  ?  146 SER A O   1 
ATOM   1760 C CB  . SER A  1 146 ? -17.40651 7.70994  -8.20976  1.000 35.88931  ?  146 SER A CB  1 
ATOM   1761 O OG  . SER A  1 146 ? -17.11829 8.79789  -9.07419  1.000 37.25901  ?  146 SER A OG  1 
ATOM   1762 N N   . PHE A  1 147 ? -16.68297 5.03186  -6.66241  1.000 29.65736  ?  147 PHE A N   1 
ATOM   1763 C CA  . PHE A  1 147 ? -16.91815 4.03752  -5.61762  1.000 28.55027  ?  147 PHE A CA  1 
ATOM   1764 C C   . PHE A  1 147 ? -15.87694 4.13801  -4.50157  1.000 26.75038  ?  147 PHE A C   1 
ATOM   1765 O O   . PHE A  1 147 ? -16.22030 4.22132  -3.31162  1.000 25.88138  ?  147 PHE A O   1 
ATOM   1766 C CB  . PHE A  1 147 ? -16.91933 2.62924  -6.19309  1.000 34.83011  ?  147 PHE A CB  1 
ATOM   1767 C CG  . PHE A  1 147 ? -17.00951 1.56987  -5.13124  1.000 31.98098  ?  147 PHE A CG  1 
ATOM   1768 C CD1 . PHE A  1 147 ? -18.24816 1.18365  -4.63530  1.000 41.26574  ?  147 PHE A CD1 1 
ATOM   1769 C CD2 . PHE A  1 147 ? -15.86422 1.00121  -4.59842  1.000 30.61256  ?  147 PHE A CD2 1 
ATOM   1770 C CE1 . PHE A  1 147 ? -18.33856 0.22840  -3.63797  1.000 49.02669  ?  147 PHE A CE1 1 
ATOM   1771 C CE2 . PHE A  1 147 ? -15.94471 0.04800  -3.60654  1.000 38.50032  ?  147 PHE A CE2 1 
ATOM   1772 C CZ  . PHE A  1 147 ? -17.18251 -0.33786 -3.12263  1.000 37.09596  ?  147 PHE A CZ  1 
ATOM   1773 N N   . PHE A  1 148 ? -14.58837 4.13773  -4.86756  1.000 25.32386  ?  148 PHE A N   1 
ATOM   1774 C CA  . PHE A  1 148 ? -13.55833 4.19610  -3.83719  1.000 21.93202  ?  148 PHE A CA  1 
ATOM   1775 C C   . PHE A  1 148 ? -13.52686 5.53836  -3.11366  1.000 21.75298  ?  148 PHE A C   1 
ATOM   1776 O O   . PHE A  1 148 ? -13.33308 5.56838  -1.89151  1.000 23.42586  ?  148 PHE A O   1 
ATOM   1777 C CB  . PHE A  1 148 ? -12.20162 3.76379  -4.38908  1.000 27.20723  ?  148 PHE A CB  1 
ATOM   1778 C CG  . PHE A  1 148 ? -12.11028 2.25336  -4.56855  1.000 23.80440  ?  148 PHE A CG  1 
ATOM   1779 C CD1 . PHE A  1 148 ? -12.05775 1.42417  -3.45666  1.000 27.50566  ?  148 PHE A CD1 1 
ATOM   1780 C CD2 . PHE A  1 148 ? -12.16363 1.67072  -5.83016  1.000 27.82178  ?  148 PHE A CD2 1 
ATOM   1781 C CE1 . PHE A  1 148 ? -11.99981 0.05306  -3.59807  1.000 30.58793  ?  148 PHE A CE1 1 
ATOM   1782 C CE2 . PHE A  1 148 ? -12.12351 0.27611  -5.97565  1.000 28.50953  ?  148 PHE A CE2 1 
ATOM   1783 C CZ  . PHE A  1 148 ? -12.03752 -0.52007 -4.85666  1.000 28.27894  ?  148 PHE A CZ  1 
ATOM   1784 N N   . LEU A  1 149 ? -13.66329 6.65664  -3.83722  1.000 23.10960  ?  149 LEU A N   1 
ATOM   1785 C CA  . LEU A  1 149 ? -13.85162 7.94325  -3.16421  1.000 22.49211  ?  149 LEU A CA  1 
ATOM   1786 C C   . LEU A  1 149 ? -14.92645 7.85752  -2.07541  1.000 22.76760  ?  149 LEU A C   1 
ATOM   1787 O O   . LEU A  1 149 ? -14.70053 8.26537  -0.92752  1.000 23.17571  ?  149 LEU A O   1 
ATOM   1788 C CB  . LEU A  1 149 ? -14.23664 9.01058  -4.18018  1.000 21.64689  ?  149 LEU A CB  1 
ATOM   1789 C CG  . LEU A  1 149 ? -14.39526 10.37760 -3.48038  1.000 23.38821  ?  149 LEU A CG  1 
ATOM   1790 C CD1 . LEU A  1 149 ? -13.07754 11.00713 -2.96749  1.000 23.06091  ?  149 LEU A CD1 1 
ATOM   1791 C CD2 . LEU A  1 149 ? -15.15102 11.36317 -4.41626  1.000 29.95309  ?  149 LEU A CD2 1 
ATOM   1792 N N   . PHE A  1 150 ? -16.09375 7.29939  -2.42184  1.000 22.82161  ?  150 PHE A N   1 
ATOM   1793 C CA  A PHE A  1 150 ? -17.18733 7.17382  -1.45427  0.600 27.89203  ?  150 PHE A CA  1 
ATOM   1794 C CA  B PHE A  1 150 ? -17.18217 7.18111  -1.45309  0.400 27.84892  ?  150 PHE A CA  1 
ATOM   1795 C C   . PHE A  1 150 ? -16.81838 6.24195  -0.30736  1.000 26.73438  ?  150 PHE A C   1 
ATOM   1796 O O   . PHE A  1 150 ? -17.13658 6.52959  0.85087   1.000 26.17355  ?  150 PHE A O   1 
ATOM   1797 C CB  A PHE A  1 150 ? -18.47110 6.67267  -2.12546  0.600 26.64834  ?  150 PHE A CB  1 
ATOM   1798 C CB  B PHE A  1 150 ? -18.47899 6.74586  -2.14754  0.400 26.73828  ?  150 PHE A CB  1 
ATOM   1799 C CG  A PHE A  1 150 ? -19.02198 7.59325  -3.18324  0.600 28.08465  ?  150 PHE A CG  1 
ATOM   1800 C CG  B PHE A  1 150 ? -19.21929 7.87536  -2.82279  0.400 31.11706  ?  150 PHE A CG  1 
ATOM   1801 C CD1 A PHE A  1 150 ? -18.65503 8.94099  -3.23193  0.600 27.36149  ?  150 PHE A CD1 1 
ATOM   1802 C CD1 B PHE A  1 150 ? -18.64164 8.57967  -3.87111  0.400 33.21014  ?  150 PHE A CD1 1 
ATOM   1803 C CD2 A PHE A  1 150 ? -19.90499 7.11191  -4.12290  0.600 33.52680  ?  150 PHE A CD2 1 
ATOM   1804 C CD2 B PHE A  1 150 ? -20.48249 8.23500  -2.40561  0.400 31.08132  ?  150 PHE A CD2 1 
ATOM   1805 C CE1 A PHE A  1 150 ? -19.17266 9.77593  -4.20583  0.600 32.91557  ?  150 PHE A CE1 1 
ATOM   1806 C CE1 B PHE A  1 150 ? -19.31685 9.61429  -4.48405  0.400 34.26675  ?  150 PHE A CE1 1 
ATOM   1807 C CE2 A PHE A  1 150 ? -20.42302 7.94132  -5.09790  0.600 37.22694  ?  150 PHE A CE2 1 
ATOM   1808 C CE2 B PHE A  1 150 ? -21.16464 9.26666  -3.01461  0.400 27.68308  ?  150 PHE A CE2 1 
ATOM   1809 C CZ  A PHE A  1 150 ? -20.05785 9.27053  -5.14212  0.600 35.60115  ?  150 PHE A CZ  1 
ATOM   1810 C CZ  B PHE A  1 150 ? -20.57918 9.95928  -4.05246  0.400 29.59014  ?  150 PHE A CZ  1 
ATOM   1811 N N   . LEU A  1 151 ? -16.15771 5.12133  -0.60552  1.000 24.62069  ?  151 LEU A N   1 
ATOM   1812 C CA  . LEU A  1 151 ? -15.72654 4.21928  0.45849   1.000 22.98860  ?  151 LEU A CA  1 
ATOM   1813 C C   . LEU A  1 151 ? -14.76731 4.93338  1.41817   1.000 25.29792  ?  151 LEU A C   1 
ATOM   1814 O O   . LEU A  1 151 ? -14.90772 4.82900  2.65312   1.000 23.02410  ?  151 LEU A O   1 
ATOM   1815 C CB  . LEU A  1 151 ? -15.04110 2.99672  -0.14815  1.000 24.61860  ?  151 LEU A CB  1 
ATOM   1816 C CG  . LEU A  1 151 ? -14.48071 2.02958  0.88633   1.000 28.70908  ?  151 LEU A CG  1 
ATOM   1817 C CD1 . LEU A  1 151 ? -15.56739 1.62762  1.85803   1.000 26.82606  ?  151 LEU A CD1 1 
ATOM   1818 C CD2 . LEU A  1 151 ? -13.92036 0.77104  0.20340   1.000 30.48779  ?  151 LEU A CD2 1 
ATOM   1819 N N   . THR A  1 152 ? -13.77617 5.65097  0.86040   1.000 24.68911  ?  152 THR A N   1 
ATOM   1820 C CA  . THR A  1 152 ? -12.79473 6.35493  1.68929   1.000 23.79327  ?  152 THR A CA  1 
ATOM   1821 C C   . THR A  1 152 ? -13.49029 7.31057  2.64582   1.000 24.53242  ?  152 THR A C   1 
ATOM   1822 O O   . THR A  1 152 ? -13.24298 7.29714  3.86753   1.000 22.55057  ?  152 THR A O   1 
ATOM   1823 C CB  . THR A  1 152 ? -11.84572 7.15456  0.80400   1.000 24.10868  ?  152 THR A CB  1 
ATOM   1824 O OG1 . THR A  1 152 ? -11.04923 6.25108  0.03930   1.000 23.09280  ?  152 THR A OG1 1 
ATOM   1825 C CG2 . THR A  1 152 ? -10.94728 8.06837  1.66964   1.000 22.69647  ?  152 THR A CG2 1 
ATOM   1826 N N   . PHE A  1 153 ? -14.40484 8.12207  2.10497   1.000 22.76498  ?  153 PHE A N   1 
ATOM   1827 C CA  . PHE A  1 153 ? -15.10192 9.11467  2.91499   1.000 24.00884  ?  153 PHE A CA  1 
ATOM   1828 C C   . PHE A  1 153 ? -16.10072 8.47321  3.87174   1.000 21.18394  ?  153 PHE A C   1 
ATOM   1829 O O   . PHE A  1 153 ? -16.26623 8.95992  5.00048   1.000 24.58504  ?  153 PHE A O   1 
ATOM   1830 C CB  . PHE A  1 153 ? -15.68665 10.21660 2.02049   1.000 23.79396  ?  153 PHE A CB  1 
ATOM   1831 C CG  . PHE A  1 153 ? -14.67267 11.27576 1.70852   1.000 24.78381  ?  153 PHE A CG  1 
ATOM   1832 C CD1 . PHE A  1 153 ? -13.71404 11.05957 0.72424   1.000 24.73741  ?  153 PHE A CD1 1 
ATOM   1833 C CD2 . PHE A  1 153 ? -14.59197 12.43116 2.47940   1.000 21.35293  ?  153 PHE A CD2 1 
ATOM   1834 C CE1 . PHE A  1 153 ? -12.72564 12.03385 0.50006   1.000 24.29733  ?  153 PHE A CE1 1 
ATOM   1835 C CE2 . PHE A  1 153 ? -13.63149 13.39648 2.24040   1.000 23.89795  ?  153 PHE A CE2 1 
ATOM   1836 C CZ  . PHE A  1 153 ? -12.69384 13.19222 1.25356   1.000 25.92230  ?  153 PHE A CZ  1 
ATOM   1837 N N   . TYR A  1 154 ? -16.72735 7.36731  3.46167   1.000 22.26436  ?  154 TYR A N   1 
ATOM   1838 C CA  . TYR A  1 154 ? -17.59360 6.62801  4.37715   1.000 25.22222  ?  154 TYR A CA  1 
ATOM   1839 C C   . TYR A  1 154 ? -16.81135 6.10361  5.58253   1.000 23.38152  ?  154 TYR A C   1 
ATOM   1840 O O   . TYR A  1 154 ? -17.21910 6.29208  6.73889   1.000 25.74847  ?  154 TYR A O   1 
ATOM   1841 C CB  . TYR A  1 154 ? -18.27940 5.47661  3.63546   1.000 27.37980  ?  154 TYR A CB  1 
ATOM   1842 C CG  . TYR A  1 154 ? -19.14030 4.66188  4.57372   1.000 28.51172  ?  154 TYR A CG  1 
ATOM   1843 C CD1 . TYR A  1 154 ? -20.35448 5.15885  5.02659   1.000 40.30175  ?  154 TYR A CD1 1 
ATOM   1844 C CD2 . TYR A  1 154 ? -18.72947 3.41440  5.02649   1.000 36.39197  ?  154 TYR A CD2 1 
ATOM   1845 C CE1 . TYR A  1 154 ? -21.15483 4.42797  5.88936   1.000 41.80966  ?  154 TYR A CE1 1 
ATOM   1846 C CE2 . TYR A  1 154 ? -19.52921 2.67285  5.90282   1.000 39.42274  ?  154 TYR A CE2 1 
ATOM   1847 C CZ  . TYR A  1 154 ? -20.73790 3.19969  6.33078   1.000 42.49292  ?  154 TYR A CZ  1 
ATOM   1848 O OH  . TYR A  1 154 ? -21.55162 2.49850  7.20011   1.000 42.97657  ?  154 TYR A OH  1 
ATOM   1849 N N   . LEU A  1 155 ? -15.67993 5.43387  5.33334   1.000 24.03978  ?  155 LEU A N   1 
ATOM   1850 C CA  . LEU A  1 155 ? -14.83778 4.95177  6.43335   1.000 24.06099  ?  155 LEU A CA  1 
ATOM   1851 C C   . LEU A  1 155 ? -14.41530 6.08909  7.35747   1.000 22.92474  ?  155 LEU A C   1 
ATOM   1852 O O   . LEU A  1 155 ? -14.44544 5.94475  8.59432   1.000 24.54181  ?  155 LEU A O   1 
ATOM   1853 C CB  . LEU A  1 155 ? -13.59013 4.29243  5.86492   1.000 25.37068  ?  155 LEU A CB  1 
ATOM   1854 C CG  . LEU A  1 155 ? -13.79926 2.97988  5.10768   1.000 25.50993  ?  155 LEU A CG  1 
ATOM   1855 C CD1 . LEU A  1 155 ? -12.50677 2.58037  4.35029   1.000 26.35495  ?  155 LEU A CD1 1 
ATOM   1856 C CD2 . LEU A  1 155 ? -14.30443 1.87559  6.07787   1.000 29.34789  ?  155 LEU A CD2 1 
ATOM   1857 N N   . LEU A  1 156 ? -14.00091 7.22788  6.78139   1.000 22.32518  ?  156 LEU A N   1 
ATOM   1858 C CA  . LEU A  1 156 ? -13.66023 8.39752  7.58385   1.000 21.66775  ?  156 LEU A CA  1 
ATOM   1859 C C   . LEU A  1 156 ? -14.84684 8.85452  8.42885   1.000 24.13073  ?  156 LEU A C   1 
ATOM   1860 O O   . LEU A  1 156 ? -14.71031 9.10698  9.63786   1.000 24.19728  ?  156 LEU A O   1 
ATOM   1861 C CB  . LEU A  1 156 ? -13.21072 9.51085  6.63448   1.000 26.02346  ?  156 LEU A CB  1 
ATOM   1862 C CG  . LEU A  1 156 ? -12.97344 10.89193 7.23905   1.000 42.74425  ?  156 LEU A CG  1 
ATOM   1863 C CD1 . LEU A  1 156 ? -11.93453 10.80205 8.32621   1.000 32.97259  ?  156 LEU A CD1 1 
ATOM   1864 C CD2 . LEU A  1 156 ? -12.49645 11.86954 6.13718   1.000 29.11549  ?  156 LEU A CD2 1 
ATOM   1865 N N   . TYR A  1 157 ? -16.03365 8.90289  7.82058   1.000 24.97907  ?  157 TYR A N   1 
ATOM   1866 C CA  . TYR A  1 157 ? -17.20664 9.45119  8.49203   1.000 25.06015  ?  157 TYR A CA  1 
ATOM   1867 C C   . TYR A  1 157 ? -17.61378 8.59173  9.67433   1.000 25.33714  ?  157 TYR A C   1 
ATOM   1868 O O   . TYR A  1 157 ? -17.77992 9.10269  10.79460  1.000 27.16544  ?  157 TYR A O   1 
ATOM   1869 C CB  . TYR A  1 157 ? -18.38203 9.53792  7.52326   1.000 27.40626  ?  157 TYR A CB  1 
ATOM   1870 C CG  . TYR A  1 157 ? -19.55394 10.33376 8.08588   1.000 28.47865  ?  157 TYR A CG  1 
ATOM   1871 C CD1 . TYR A  1 157 ? -20.51333 9.73446  8.89880   1.000 26.78688  ?  157 TYR A CD1 1 
ATOM   1872 C CD2 . TYR A  1 157 ? -19.67215 11.69885 7.82285   1.000 25.65634  ?  157 TYR A CD2 1 
ATOM   1873 C CE1 . TYR A  1 157 ? -21.58757 10.48617 9.41982   1.000 27.60256  ?  157 TYR A CE1 1 
ATOM   1874 C CE2 . TYR A  1 157 ? -20.75327 12.46079 8.33092   1.000 30.32014  ?  157 TYR A CE2 1 
ATOM   1875 C CZ  . TYR A  1 157 ? -21.70083 11.84404 9.12792   1.000 34.49062  ?  157 TYR A CZ  1 
ATOM   1876 O OH  . TYR A  1 157 ? -22.77206 12.57736 9.63117   1.000 29.62661  ?  157 TYR A OH  1 
ATOM   1877 N N   . VAL A  1 158 ? -17.78749 7.27971  9.44567   1.000 23.18972  ?  158 VAL A N   1 
ATOM   1878 C CA  . VAL A  1 158 ? -18.37201 6.44191  10.48648  1.000 27.54745  ?  158 VAL A CA  1 
ATOM   1879 C C   . VAL A  1 158 ? -17.43274 6.20917  11.65618  1.000 27.45759  ?  158 VAL A C   1 
ATOM   1880 O O   . VAL A  1 158 ? -17.88954 5.79616  12.72627  1.000 34.74576  ?  158 VAL A O   1 
ATOM   1881 C CB  . VAL A  1 158 ? -18.92297 5.11134  9.94310   1.000 28.76524  ?  158 VAL A CB  1 
ATOM   1882 C CG1 . VAL A  1 158 ? -20.02650 5.38956  8.94598   1.000 38.89135  ?  158 VAL A CG1 1 
ATOM   1883 C CG2 . VAL A  1 158 ? -17.80119 4.29043  9.30810   1.000 29.39055  ?  158 VAL A CG2 1 
ATOM   1884 N N   . LYS A  1 159 ? -16.13301 6.44281  11.49703  1.000 28.51215  ?  159 LYS A N   1 
ATOM   1885 C CA  . LYS A  1 159 ? -15.23121 6.23883  12.62741  1.000 25.63435  ?  159 LYS A CA  1 
ATOM   1886 C C   . LYS A  1 159 ? -14.89526 7.53516  13.35932  1.000 24.70416  ?  159 LYS A C   1 
ATOM   1887 O O   . LYS A  1 159 ? -14.76224 7.53489  14.59041  1.000 26.26499  ?  159 LYS A O   1 
ATOM   1888 C CB  . LYS A  1 159 ? -13.93291 5.56044  12.16887  1.000 29.43284  ?  159 LYS A CB  1 
ATOM   1889 C CG  . LYS A  1 159 ? -12.95728 5.25547  13.32598  1.000 33.70606  ?  159 LYS A CG  1 
ATOM   1890 C CD  . LYS A  1 159 ? -12.30489 3.89988  13.17101  1.000 46.99016  ?  159 LYS A CD  1 
ATOM   1891 C CE  . LYS A  1 159 ? -11.50149 3.49570  14.38020  1.000 44.16671  ?  159 LYS A CE  1 
ATOM   1892 N NZ  . LYS A  1 159 ? -12.23485 2.49798  15.20783  1.000 48.93724  ?  159 LYS A NZ  1 
ATOM   1893 N N   . TYR A  1 160 ? -14.73979 8.64877  12.63072  1.000 23.21016  ?  160 TYR A N   1 
ATOM   1894 C CA  . TYR A  1 160 ? -14.11004 9.82550  13.20597  1.000 25.63622  ?  160 TYR A CA  1 
ATOM   1895 C C   . TYR A  1 160 ? -15.00378 11.05356 13.37604  1.000 30.33570  ?  160 TYR A C   1 
ATOM   1896 O O   . TYR A  1 160 ? -14.60888 11.96943 14.10495  1.000 26.15835  ?  160 TYR A O   1 
ATOM   1897 C CB  . TYR A  1 160 ? -12.84473 10.20647 12.41857  1.000 24.17105  ?  160 TYR A CB  1 
ATOM   1898 C CG  . TYR A  1 160 ? -11.79029 9.12291  12.48285  1.000 23.78914  ?  160 TYR A CG  1 
ATOM   1899 C CD1 . TYR A  1 160 ? -11.09546 8.89063  13.66018  1.000 24.27915  ?  160 TYR A CD1 1 
ATOM   1900 C CD2 . TYR A  1 160 ? -11.52225 8.30831  11.37463  1.000 23.25796  ?  160 TYR A CD2 1 
ATOM   1901 C CE1 . TYR A  1 160 ? -10.16050 7.89270  13.74949  1.000 24.61063  ?  160 TYR A CE1 1 
ATOM   1902 C CE2 . TYR A  1 160 ? -10.56568 7.31083  11.44831  1.000 24.05335  ?  160 TYR A CE2 1 
ATOM   1903 C CZ  . TYR A  1 160 ? -9.88540  7.12583  12.63618  1.000 25.65595  ?  160 TYR A CZ  1 
ATOM   1904 O OH  . TYR A  1 160 ? -8.94632  6.14609  12.75423  1.000 25.24519  ?  160 TYR A OH  1 
ATOM   1905 N N   . THR A  1 161 ? -16.17407 11.11749 12.74339  1.000 26.15882  ?  161 THR A N   1 
ATOM   1906 C CA  . THR A  1 161 ? -17.01430 12.30644 12.90864  1.000 27.02338  ?  161 THR A CA  1 
ATOM   1907 C C   . THR A  1 161 ? -17.96782 12.20329 14.10287  1.000 29.70301  ?  161 THR A C   1 
ATOM   1908 O O   . THR A  1 161 ? -18.19354 11.13797 14.68669  1.000 27.80551  ?  161 THR A O   1 
ATOM   1909 C CB  . THR A  1 161 ? -17.84339 12.60534 11.64512  1.000 23.10530  ?  161 THR A CB  1 
ATOM   1910 O OG1 . THR A  1 161 ? -18.80642 11.55056 11.40843  1.000 28.42523  ?  161 THR A OG1 1 
ATOM   1911 C CG2 . THR A  1 161 ? -16.96419 12.83654 10.43222  1.000 21.67918  ?  161 THR A CG2 1 
ATOM   1912 N N   . LYS A  1 162 ? -18.54309 13.35087 14.45373  1.000 25.03287  ?  162 LYS A N   1 
ATOM   1913 C CA  . LYS A  1 162 ? -19.65307 13.45522 15.39063  1.000 26.37041  ?  162 LYS A CA  1 
ATOM   1914 C C   . LYS A  1 162 ? -20.76503 14.23504 14.69414  1.000 28.85615  ?  162 LYS A C   1 
ATOM   1915 O O   . LYS A  1 162 ? -20.52626 14.93122 13.70598  1.000 27.90519  ?  162 LYS A O   1 
ATOM   1916 C CB  . LYS A  1 162 ? -19.24294 14.13315 16.70440  1.000 30.26371  ?  162 LYS A CB  1 
ATOM   1917 C CG  . LYS A  1 162 ? -18.42617 13.21243 17.61485  1.000 33.36478  ?  162 LYS A CG  1 
ATOM   1918 C CD  . LYS A  1 162 ? -18.03086 13.92531 18.90576  1.000 53.42668  ?  162 LYS A CD  1 
ATOM   1919 C CE  . LYS A  1 162 ? -17.73171 12.93435 20.03613  1.000 47.20971  ?  162 LYS A CE  1 
ATOM   1920 N NZ  . LYS A  1 162 ? -17.42222 13.64380 21.31904  1.000 62.30521  ?  162 LYS A NZ  1 
ATOM   1921 N N   . GLU A  1 163 ? -21.99180 14.09770 15.19372  1.000 28.13597  ?  163 GLU A N   1 
ATOM   1922 C CA  . GLU A  1 163 ? -23.14378 14.68072 14.50888  1.000 28.59648  ?  163 GLU A CA  1 
ATOM   1923 C C   . GLU A  1 163 ? -23.34445 16.13033 14.94567  1.000 30.35838  ?  163 GLU A C   1 
ATOM   1924 O O   . GLU A  1 163 ? -24.16066 16.42849 15.82672  1.000 29.70498  ?  163 GLU A O   1 
ATOM   1925 C CB  . GLU A  1 163 ? -24.38942 13.82964 14.74425  1.000 35.38838  ?  163 GLU A CB  1 
ATOM   1926 C CG  . GLU A  1 163 ? -24.34440 12.44699 14.11260  1.000 32.28426  ?  163 GLU A CG  1 
ATOM   1927 C CD  . GLU A  1 163 ? -24.24370 12.49423 12.58993  1.000 30.21979  ?  163 GLU A CD  1 
ATOM   1928 O OE1 . GLU A  1 163 ? -24.94235 13.32426 11.95239  1.000 33.91825  ?  163 GLU A OE1 1 
ATOM   1929 O OE2 . GLU A  1 163 ? -23.46686 11.68675 12.02650  1.000 33.24544  -1 163 GLU A OE2 1 
ATOM   1930 N N   . ASN A  1 164 ? -22.61787 17.05231 14.30082  1.000 26.64723  ?  164 ASN A N   1 
ATOM   1931 C CA  . ASN A  1 164 ? -22.82801 18.47697 14.56647  1.000 30.19653  ?  164 ASN A CA  1 
ATOM   1932 C C   . ASN A  1 164 ? -22.28371 19.29623 13.40587  1.000 25.95425  ?  164 ASN A C   1 
ATOM   1933 O O   . ASN A  1 164 ? -21.59901 18.77832 12.51955  1.000 24.87368  ?  164 ASN A O   1 
ATOM   1934 C CB  . ASN A  1 164 ? -22.25769 18.92075 15.91837  1.000 30.74262  ?  164 ASN A CB  1 
ATOM   1935 C CG  . ASN A  1 164 ? -20.76557 18.71188 16.01996  1.000 28.80210  ?  164 ASN A CG  1 
ATOM   1936 O OD1 . ASN A  1 164 ? -20.00002 19.07395 15.11182  1.000 26.87897  ?  164 ASN A OD1 1 
ATOM   1937 N ND2 . ASN A  1 164 ? -20.33768 18.10143 17.12412  1.000 29.60551  ?  164 ASN A ND2 1 
ATOM   1938 N N   . TRP A  1 165 ? -22.60135 20.59356 13.42192  1.000 26.37395  ?  165 TRP A N   1 
ATOM   1939 C CA  . TRP A  1 165 ? -22.35757 21.40921 12.23464  1.000 23.91062  ?  165 TRP A CA  1 
ATOM   1940 C C   . TRP A  1 165 ? -20.87520 21.67067 11.99367  1.000 28.56858  ?  165 TRP A C   1 
ATOM   1941 O O   . TRP A  1 165 ? -20.45556 21.78275 10.83276  1.000 27.85524  ?  165 TRP A O   1 
ATOM   1942 C CB  . TRP A  1 165 ? -23.22890 22.66926 12.24320  1.000 31.70934  ?  165 TRP A CB  1 
ATOM   1943 C CG  . TRP A  1 165 ? -24.61767 22.32596 11.80006  1.000 37.92139  ?  165 TRP A CG  1 
ATOM   1944 C CD1 . TRP A  1 165 ? -25.70576 22.07728 12.59593  1.000 37.09698  ?  165 TRP A CD1 1 
ATOM   1945 C CD2 . TRP A  1 165 ? -25.05683 22.13008 10.44677  1.000 28.26768  ?  165 TRP A CD2 1 
ATOM   1946 N NE1 . TRP A  1 165 ? -26.79501 21.74162 11.81147  1.000 35.38012  ?  165 TRP A NE1 1 
ATOM   1947 C CE2 . TRP A  1 165 ? -26.41931 21.77411 10.49377  1.000 34.06714  ?  165 TRP A CE2 1 
ATOM   1948 C CE3 . TRP A  1 165 ? -24.42284 22.22437 9.19625   1.000 30.72217  ?  165 TRP A CE3 1 
ATOM   1949 C CZ2 . TRP A  1 165 ? -27.16420 21.52556 9.34088   1.000 30.09972  ?  165 TRP A CZ2 1 
ATOM   1950 C CZ3 . TRP A  1 165 ? -25.16617 21.98419 8.05548   1.000 34.02782  ?  165 TRP A CZ3 1 
ATOM   1951 C CH2 . TRP A  1 165 ? -26.51464 21.62714 8.13534   1.000 33.25163  ?  165 TRP A CH2 1 
ATOM   1952 N N   A MET A  1 166 ? -20.05864 21.74771 13.04905  0.600 25.47870  ?  166 MET A N   1 
ATOM   1953 N N   B MET A  1 166 ? -20.08109 21.77272 13.06758  0.400 25.58664  ?  166 MET A N   1 
ATOM   1954 C CA  A MET A  1 166 ? -18.62221 21.88346 12.82015  0.600 25.97584  ?  166 MET A CA  1 
ATOM   1955 C CA  B MET A  1 166 ? -18.63092 21.86521 12.91795  0.400 26.15449  ?  166 MET A CA  1 
ATOM   1956 C C   A MET A  1 166 ? -18.07169 20.66398 12.09906  0.600 24.48133  ?  166 MET A C   1 
ATOM   1957 C C   B MET A  1 166 ? -18.09330 20.68205 12.12355  0.400 24.50804  ?  166 MET A C   1 
ATOM   1958 O O   A MET A  1 166 ? -17.25998 20.79305 11.17640  0.600 28.44660  ?  166 MET A O   1 
ATOM   1959 O O   B MET A  1 166 ? -17.31021 20.85292 11.18260  0.400 28.61011  ?  166 MET A O   1 
ATOM   1960 C CB  A MET A  1 166 ? -17.88242 22.08469 14.13278  0.600 27.27557  ?  166 MET A CB  1 
ATOM   1961 C CB  B MET A  1 166 ? -17.97087 21.91110 14.29454  0.400 28.47497  ?  166 MET A CB  1 
ATOM   1962 C CG  A MET A  1 166 ? -18.51392 23.11126 15.02783  0.600 48.03133  ?  166 MET A CG  1 
ATOM   1963 C CG  B MET A  1 166 ? -17.80463 23.30133 14.88145  0.400 42.81813  ?  166 MET A CG  1 
ATOM   1964 S SD  A MET A  1 166 ? -19.26571 22.46606 16.55305  0.600 67.23128  ?  166 MET A SD  1 
ATOM   1965 S SD  B MET A  1 166 ? -17.35893 23.20654 16.63235  0.400 37.92498  ?  166 MET A SD  1 
ATOM   1966 C CE  A MET A  1 166 ? -20.98116 22.29590 16.05755  0.600 31.18069  ?  166 MET A CE  1 
ATOM   1967 C CE  B MET A  1 166 ? -16.29273 21.78478 16.54680  0.400 26.06045  ?  166 MET A CE  1 
ATOM   1968 N N   . ASN A  1 167 ? -18.52893 19.46949 12.47063  1.000 23.62624  ?  167 ASN A N   1 
ATOM   1969 C CA  . ASN A  1 167 ? -18.11934 18.27857 11.71912  1.000 21.24135  ?  167 ASN A CA  1 
ATOM   1970 C C   . ASN A  1 167 ? -18.65336 18.30180 10.29058  1.000 27.27919  ?  167 ASN A C   1 
ATOM   1971 O O   . ASN A  1 167 ? -17.92717 17.97625 9.34248   1.000 27.08026  ?  167 ASN A O   1 
ATOM   1972 C CB  . ASN A  1 167 ? -18.65404 17.04377 12.41060  1.000 20.81485  ?  167 ASN A CB  1 
ATOM   1973 C CG  . ASN A  1 167 ? -17.73792 16.55544 13.51972  1.000 21.29461  ?  167 ASN A CG  1 
ATOM   1974 O OD1 . ASN A  1 167 ? -16.98942 15.59803 13.31660  1.000 24.88312  ?  167 ASN A OD1 1 
ATOM   1975 N ND2 . ASN A  1 167 ? -17.78719 17.19996 14.67186  1.000 25.20833  ?  167 ASN A ND2 1 
ATOM   1976 N N   . TYR A  1 168 ? -19.91560 18.68376 10.10445  1.000 22.99811  ?  168 TYR A N   1 
ATOM   1977 C CA  . TYR A  1 168 ? -20.47860 18.65717 8.74919   1.000 25.77638  ?  168 TYR A CA  1 
ATOM   1978 C C   . TYR A  1 168 ? -19.71796 19.59758 7.82750   1.000 22.99344  ?  168 TYR A C   1 
ATOM   1979 O O   . TYR A  1 168 ? -19.41701 19.24688 6.67733   1.000 25.15955  ?  168 TYR A O   1 
ATOM   1980 C CB  . TYR A  1 168 ? -21.96639 19.01124 8.75159   1.000 30.13234  ?  168 TYR A CB  1 
ATOM   1981 C CG  . TYR A  1 168 ? -22.83903 18.15675 9.64163   1.000 26.50851  ?  168 TYR A CG  1 
ATOM   1982 C CD1 . TYR A  1 168 ? -22.56556 16.80431 9.83294   1.000 28.09031  ?  168 TYR A CD1 1 
ATOM   1983 C CD2 . TYR A  1 168 ? -23.90560 18.71639 10.32539  1.000 30.51886  ?  168 TYR A CD2 1 
ATOM   1984 C CE1 . TYR A  1 168 ? -23.37684 16.02373 10.67389  1.000 26.28392  ?  168 TYR A CE1 1 
ATOM   1985 C CE2 . TYR A  1 168 ? -24.70712 17.95403 11.16514  1.000 28.34613  ?  168 TYR A CE2 1 
ATOM   1986 C CZ  . TYR A  1 168 ? -24.43540 16.61990 11.33330  1.000 26.82389  ?  168 TYR A CZ  1 
ATOM   1987 O OH  . TYR A  1 168 ? -25.22000 15.89232 12.17327  1.000 28.61137  ?  168 TYR A OH  1 
ATOM   1988 N N   . ILE A  1 169 ? -19.38325 20.79616 8.31827   1.000 21.89050  ?  169 ILE A N   1 
ATOM   1989 C CA  . ILE A  1 169 ? -18.63835 21.74659 7.49737   1.000 22.21796  ?  169 ILE A CA  1 
ATOM   1990 C C   . ILE A  1 169 ? -17.32471 21.13534 7.03914   1.000 21.81530  ?  169 ILE A C   1 
ATOM   1991 O O   . ILE A  1 169 ? -17.03267 21.08007 5.84075   1.000 23.02289  ?  169 ILE A O   1 
ATOM   1992 C CB  . ILE A  1 169 ? -18.41139 23.06818 8.25726   1.000 21.95868  ?  169 ILE A CB  1 
ATOM   1993 C CG1 . ILE A  1 169 ? -19.72663 23.83079 8.46673   1.000 21.50760  ?  169 ILE A CG1 1 
ATOM   1994 C CG2 . ILE A  1 169 ? -17.37105 23.93765 7.48776   1.000 24.73459  ?  169 ILE A CG2 1 
ATOM   1995 C CD1 . ILE A  1 169 ? -19.54532 24.96476 9.45723   1.000 28.85505  ?  169 ILE A CD1 1 
ATOM   1996 N N   . VAL A  1 170 ? -16.52694 20.63155 7.98498   1.000 23.88855  ?  170 VAL A N   1 
ATOM   1997 C CA  . VAL A  1 170 ? -15.21737 20.09023 7.64677   1.000 25.08235  ?  170 VAL A CA  1 
ATOM   1998 C C   . VAL A  1 170 ? -15.34844 18.86129 6.76002   1.000 22.47841  ?  170 VAL A C   1 
ATOM   1999 O O   . VAL A  1 170 ? -14.66954 18.74156 5.73184   1.000 24.92545  ?  170 VAL A O   1 
ATOM   2000 C CB  . VAL A  1 170 ? -14.41104 19.79776 8.92590   1.000 28.76819  ?  170 VAL A CB  1 
ATOM   2001 C CG1 . VAL A  1 170 ? -13.07547 19.19702 8.54809   1.000 29.41774  ?  170 VAL A CG1 1 
ATOM   2002 C CG2 . VAL A  1 170 ? -14.22746 21.08084 9.72341   1.000 25.20808  ?  170 VAL A CG2 1 
ATOM   2003 N N   . PHE A  1 171 ? -16.27081 17.96233 7.08937   1.000 21.37532  ?  171 PHE A N   1 
ATOM   2004 C CA  . PHE A  1 171 ? -16.36052 16.72631 6.33427   1.000 25.18630  ?  171 PHE A CA  1 
ATOM   2005 C C   . PHE A  1 171 ? -16.84541 16.99025 4.91998   1.000 21.85524  ?  171 PHE A C   1 
ATOM   2006 O O   . PHE A  1 171 ? -16.23913 16.52495 3.94580   1.000 23.64331  ?  171 PHE A O   1 
ATOM   2007 C CB  . PHE A  1 171 ? -17.28179 15.72502 7.03213   1.000 21.38286  ?  171 PHE A CB  1 
ATOM   2008 C CG  . PHE A  1 171 ? -17.38955 14.42275 6.29855   1.000 22.54108  ?  171 PHE A CG  1 
ATOM   2009 C CD1 . PHE A  1 171 ? -16.42247 13.43272 6.46496   1.000 25.24077  ?  171 PHE A CD1 1 
ATOM   2010 C CD2 . PHE A  1 171 ? -18.43061 14.19529 5.40756   1.000 25.40812  ?  171 PHE A CD2 1 
ATOM   2011 C CE1 . PHE A  1 171 ? -16.51250 12.22038 5.76658   1.000 24.65403  ?  171 PHE A CE1 1 
ATOM   2012 C CE2 . PHE A  1 171 ? -18.51695 12.99842 4.69179   1.000 28.87778  ?  171 PHE A CE2 1 
ATOM   2013 C CZ  . PHE A  1 171 ? -17.56377 12.00199 4.88223   1.000 26.12572  ?  171 PHE A CZ  1 
ATOM   2014 N N   . TYR A  1 172 ? -17.96049 17.72326 4.78519   1.000 22.86033  ?  172 TYR A N   1 
ATOM   2015 C CA  . TYR A  1 172 ? -18.60131 17.83623 3.48060   1.000 21.46656  ?  172 TYR A CA  1 
ATOM   2016 C C   . TYR A  1 172 ? -17.84932 18.79600 2.56372   1.000 20.80439  ?  172 TYR A C   1 
ATOM   2017 O O   . TYR A  1 172 ? -17.84065 18.59175 1.34346   1.000 23.16539  ?  172 TYR A O   1 
ATOM   2018 C CB  . TYR A  1 172 ? -20.08558 18.17307 3.61884   1.000 26.19178  ?  172 TYR A CB  1 
ATOM   2019 C CG  . TYR A  1 172 ? -20.88275 16.96364 4.06400   1.000 22.74699  ?  172 TYR A CG  1 
ATOM   2020 C CD1 . TYR A  1 172 ? -21.13287 15.92146 3.18065   1.000 23.99378  ?  172 TYR A CD1 1 
ATOM   2021 C CD2 . TYR A  1 172 ? -21.35012 16.85381 5.37095   1.000 24.93857  ?  172 TYR A CD2 1 
ATOM   2022 C CE1 . TYR A  1 172 ? -21.83076 14.80416 3.56667   1.000 24.59074  ?  172 TYR A CE1 1 
ATOM   2023 C CE2 . TYR A  1 172 ? -22.05222 15.72984 5.78252   1.000 28.68463  ?  172 TYR A CE2 1 
ATOM   2024 C CZ  . TYR A  1 172 ? -22.28309 14.69912 4.87885   1.000 27.35616  ?  172 TYR A CZ  1 
ATOM   2025 O OH  . TYR A  1 172 ? -22.98131 13.58471 5.26752   1.000 31.40381  ?  172 TYR A OH  1 
ATOM   2026 N N   A PHE A  1 173 ? -17.22600 19.84119 3.11159   0.600 21.80424  ?  173 PHE A N   1 
ATOM   2027 N N   B PHE A  1 173 ? -17.20783 19.82057 3.12387   0.400 21.87311  ?  173 PHE A N   1 
ATOM   2028 C CA  A PHE A  1 173 ? -16.34857 20.66729 2.28558   0.600 22.21992  ?  173 PHE A CA  1 
ATOM   2029 C CA  B PHE A  1 173 ? -16.35654 20.66712 2.29928   0.400 22.35663  ?  173 PHE A CA  1 
ATOM   2030 C C   A PHE A  1 173 ? -15.26630 19.79424 1.65958   0.600 25.47575  ?  173 PHE A C   1 
ATOM   2031 C C   B PHE A  1 173 ? -15.22689 19.85172 1.68867   0.400 25.37877  ?  173 PHE A C   1 
ATOM   2032 O O   A PHE A  1 173 ? -15.11480 19.75545 0.43016   0.600 21.58495  ?  173 PHE A O   1 
ATOM   2033 O O   B PHE A  1 173 ? -14.94643 19.96212 0.49061   0.400 23.53585  ?  173 PHE A O   1 
ATOM   2034 C CB  A PHE A  1 173 ? -15.75154 21.78733 3.14124   0.600 25.25192  ?  173 PHE A CB  1 
ATOM   2035 C CB  B PHE A  1 173 ? -15.80244 21.82704 3.11391   0.400 25.18627  ?  173 PHE A CB  1 
ATOM   2036 C CG  A PHE A  1 173 ? -15.02730 22.86983 2.35842   0.600 23.58824  ?  173 PHE A CG  1 
ATOM   2037 C CG  B PHE A  1 173 ? -14.66556 22.53595 2.44082   0.400 27.15437  ?  173 PHE A CG  1 
ATOM   2038 C CD1 A PHE A  1 173 ? -15.21658 23.03288 1.00287   0.600 28.43142  ?  173 PHE A CD1 1 
ATOM   2039 C CD1 B PHE A  1 173 ? -14.91499 23.47763 1.47257   0.400 25.63070  ?  173 PHE A CD1 1 
ATOM   2040 C CD2 A PHE A  1 173 ? -14.15584 23.73106 3.01873   0.600 28.72805  ?  173 PHE A CD2 1 
ATOM   2041 C CD2 B PHE A  1 173 ? -13.35436 22.25422 2.77963   0.400 26.16118  ?  173 PHE A CD2 1 
ATOM   2042 C CE1 A PHE A  1 173 ? -14.54427 24.04027 0.30352   0.600 36.50357  ?  173 PHE A CE1 1 
ATOM   2043 C CE1 B PHE A  1 173 ? -13.88613 24.13997 0.84690   0.400 37.97872  ?  173 PHE A CE1 1 
ATOM   2044 C CE2 A PHE A  1 173 ? -13.48057 24.72864 2.33785   0.600 37.09054  ?  173 PHE A CE2 1 
ATOM   2045 C CE2 B PHE A  1 173 ? -12.31171 22.91222 2.15137   0.400 34.91971  ?  173 PHE A CE2 1 
ATOM   2046 C CZ  A PHE A  1 173 ? -13.67421 24.88721 0.97578   0.600 36.53237  ?  173 PHE A CZ  1 
ATOM   2047 C CZ  B PHE A  1 173 ? -12.58455 23.85648 1.18679   0.400 32.45981  ?  173 PHE A CZ  1 
ATOM   2048 N N   . MET A  1 174 ? -14.58317 18.99904 2.49034   1.000 20.68767  ?  174 MET A N   1 
ATOM   2049 C CA  A MET A  1 174 ? -13.54502 18.08895 1.99970   0.600 22.36714  ?  174 MET A CA  1 
ATOM   2050 C CA  B MET A  1 174 ? -13.54524 18.15227 1.93166   0.400 22.40241  ?  174 MET A CA  1 
ATOM   2051 C C   . MET A  1 174 ? -14.11324 17.11714 0.96521   1.000 24.29989  ?  174 MET A C   1 
ATOM   2052 O O   . MET A  1 174 ? -13.55078 16.91697 -0.11385  1.000 23.36604  ?  174 MET A O   1 
ATOM   2053 C CB  A MET A  1 174 ? -12.94579 17.31053 3.18016   0.600 22.60349  ?  174 MET A CB  1 
ATOM   2054 C CB  B MET A  1 174 ? -12.75071 17.49285 3.03459   0.400 23.09195  ?  174 MET A CB  1 
ATOM   2055 C CG  A MET A  1 174 ? -11.61130 17.84551 3.71255   0.600 51.25973  ?  174 MET A CG  1 
ATOM   2056 C CG  B MET A  1 174 ? -11.60072 16.69600 2.49804   0.400 11.53748  ?  174 MET A CG  1 
ATOM   2057 S SD  A MET A  1 174 ? -10.60499 16.65666 4.66034   0.600 35.87817  ?  174 MET A SD  1 
ATOM   2058 S SD  B MET A  1 174 ? -10.98444 15.77876 3.87897   0.400 17.43976  ?  174 MET A SD  1 
ATOM   2059 C CE  A MET A  1 174 ? -11.10367 15.09827 3.92206   0.600 18.54506  ?  174 MET A CE  1 
ATOM   2060 C CE  B MET A  1 174 ? -9.56784  14.98072 3.12441   0.400 14.52075  ?  174 MET A CE  1 
ATOM   2061 N N   . PHE A  1 175 ? -15.24668 16.48483 1.29438   1.000 21.02489  ?  175 PHE A N   1 
ATOM   2062 C CA  . PHE A  1 175 ? -15.82925 15.49204 0.39684   1.000 22.67972  ?  175 PHE A CA  1 
ATOM   2063 C C   . PHE A  1 175 ? -16.15060 16.10923 -0.95588  1.000 24.93827  ?  175 PHE A C   1 
ATOM   2064 O O   . PHE A  1 175 ? -15.81379 15.54256 -2.00473  1.000 24.21720  ?  175 PHE A O   1 
ATOM   2065 C CB  . PHE A  1 175 ? -17.08084 14.91688 1.05398   1.000 23.06575  ?  175 PHE A CB  1 
ATOM   2066 C CG  . PHE A  1 175 ? -17.68416 13.72625 0.34736   1.000 26.78362  ?  175 PHE A CG  1 
ATOM   2067 C CD1 . PHE A  1 175 ? -16.94446 12.90299 -0.49209  1.000 25.58967  ?  175 PHE A CD1 1 
ATOM   2068 C CD2 . PHE A  1 175 ? -19.00928 13.39695 0.57782   1.000 31.15571  ?  175 PHE A CD2 1 
ATOM   2069 C CE1 . PHE A  1 175 ? -17.53773 11.81005 -1.11665  1.000 26.70210  ?  175 PHE A CE1 1 
ATOM   2070 C CE2 . PHE A  1 175 ? -19.60298 12.30815 -0.04407  1.000 52.06016  ?  175 PHE A CE2 1 
ATOM   2071 C CZ  . PHE A  1 175 ? -18.85877 11.51455 -0.89641  1.000 37.33678  ?  175 PHE A CZ  1 
ATOM   2072 N N   . LEU A  1 176 ? -16.80762 17.27165 -0.95066  1.000 22.34857  ?  176 LEU A N   1 
ATOM   2073 C CA  . LEU A  1 176 ? -17.17992 17.91241 -2.21169  1.000 24.63463  ?  176 LEU A CA  1 
ATOM   2074 C C   . LEU A  1 176 ? -15.94590 18.26089 -3.04200  1.000 23.53341  ?  176 LEU A C   1 
ATOM   2075 O O   . LEU A  1 176 ? -15.90082 18.00447 -4.25937  1.000 24.39168  ?  176 LEU A O   1 
ATOM   2076 C CB  . LEU A  1 176 ? -18.00741 19.16208 -1.93065  1.000 24.17429  ?  176 LEU A CB  1 
ATOM   2077 C CG  . LEU A  1 176 ? -18.32621 20.05111 -3.13262  1.000 28.70466  ?  176 LEU A CG  1 
ATOM   2078 C CD1 . LEU A  1 176 ? -19.04489 19.26682 -4.24565  1.000 27.31186  ?  176 LEU A CD1 1 
ATOM   2079 C CD2 . LEU A  1 176 ? -19.15780 21.27513 -2.66001  1.000 28.08489  ?  176 LEU A CD2 1 
ATOM   2080 N N   . VAL A  1 177 ? -14.94141 18.85933 -2.39934  1.000 19.79617  ?  177 VAL A N   1 
ATOM   2081 C CA  . VAL A  1 177 ? -13.74204 19.28110 -3.12044  1.000 20.32702  ?  177 VAL A CA  1 
ATOM   2082 C C   . VAL A  1 177 ? -13.05330 18.07808 -3.75176  1.000 18.58233  ?  177 VAL A C   1 
ATOM   2083 O O   . VAL A  1 177 ? -12.68138 18.11138 -4.93426  1.000 19.55519  ?  177 VAL A O   1 
ATOM   2084 C CB  . VAL A  1 177 ? -12.80254 20.02791 -2.17796  1.000 19.97320  ?  177 VAL A CB  1 
ATOM   2085 C CG1 . VAL A  1 177 ? -11.43489 20.15600 -2.82063  1.000 25.70415  ?  177 VAL A CG1 1 
ATOM   2086 C CG2 . VAL A  1 177 ? -13.39605 21.41142 -1.83656  1.000 20.86882  ?  177 VAL A CG2 1 
ATOM   2087 N N   . TRP A  1 178 ? -12.88188 16.98773 -2.96736  1.000 19.22863  ?  178 TRP A N   1 
ATOM   2088 C CA  . TRP A  1 178 ? -12.30635 15.76981 -3.55325  1.000 22.57487  ?  178 TRP A CA  1 
ATOM   2089 C C   . TRP A  1 178 ? -13.14852 15.24204 -4.72044  1.000 21.39085  ?  178 TRP A C   1 
ATOM   2090 O O   . TRP A  1 178 ? -12.60551 14.88278 -5.77185  1.000 21.47903  ?  178 TRP A O   1 
ATOM   2091 C CB  . TRP A  1 178 ? -12.03979 14.71351 -2.47862  1.000 19.78753  ?  178 TRP A CB  1 
ATOM   2092 C CG  . TRP A  1 178 ? -10.86228 15.06330 -1.58851  1.000 19.81020  ?  178 TRP A CG  1 
ATOM   2093 C CD1 . TRP A  1 178 ? -10.55848 16.28865 -1.04234  1.000 22.35948  ?  178 TRP A CD1 1 
ATOM   2094 C CD2 . TRP A  1 178 ? -9.81554  14.18011 -1.18449  1.000 21.79025  ?  178 TRP A CD2 1 
ATOM   2095 N NE1 . TRP A  1 178 ? -9.38354  16.21713 -0.30465  1.000 20.98595  ?  178 TRP A NE1 1 
ATOM   2096 C CE2 . TRP A  1 178 ? -8.91512  14.93281 -0.37162  1.000 24.78900  ?  178 TRP A CE2 1 
ATOM   2097 C CE3 . TRP A  1 178 ? -9.55805  12.82553 -1.40014  1.000 22.47076  ?  178 TRP A CE3 1 
ATOM   2098 C CZ2 . TRP A  1 178 ? -7.75939  14.36360 0.21553   1.000 23.49327  ?  178 TRP A CZ2 1 
ATOM   2099 C CZ3 . TRP A  1 178 ? -8.41125  12.25901 -0.80559  1.000 20.53291  ?  178 TRP A CZ3 1 
ATOM   2100 C CH2 . TRP A  1 178 ? -7.51609  13.04093 -0.02782  1.000 19.02220  ?  178 TRP A CH2 1 
ATOM   2101 N N   A PHE A  1 179 ? -14.47046 15.18778 -4.56332  0.600 22.74874  ?  179 PHE A N   1 
ATOM   2102 N N   B PHE A  1 179 ? -14.48071 15.25067 -4.55508  0.400 22.80458  ?  179 PHE A N   1 
ATOM   2103 C CA  A PHE A  1 179 ? -15.30870 14.74765 -5.67305  0.600 24.27886  ?  179 PHE A CA  1 
ATOM   2104 C CA  B PHE A  1 179 ? -15.44706 14.84581 -5.57911  0.400 23.34243  ?  179 PHE A CA  1 
ATOM   2105 C C   A PHE A  1 179 ? -15.05233 15.57964 -6.92949  0.600 22.75909  ?  179 PHE A C   1 
ATOM   2106 C C   B PHE A  1 179 ? -15.29462 15.65137 -6.87154  0.400 22.05089  ?  179 PHE A C   1 
ATOM   2107 O O   A PHE A  1 179 ? -14.99812 15.03203 -8.03809  0.600 19.15595  ?  179 PHE A O   1 
ATOM   2108 O O   B PHE A  1 179 ? -15.62525 15.16337 -7.95831  0.400 25.02304  ?  179 PHE A O   1 
ATOM   2109 C CB  A PHE A  1 179 ? -16.77597 14.79602 -5.27418  0.600 24.47427  ?  179 PHE A CB  1 
ATOM   2110 C CB  B PHE A  1 179 ? -16.84061 15.07020 -4.98559  0.400 22.72114  ?  179 PHE A CB  1 
ATOM   2111 C CG  A PHE A  1 179 ? -17.70906 14.32983 -6.35630  0.600 30.90956  ?  179 PHE A CG  1 
ATOM   2112 C CG  B PHE A  1 179 ? -17.98231 14.66141 -5.87824  0.400 25.16059  ?  179 PHE A CG  1 
ATOM   2113 C CD1 A PHE A  1 179 ? -18.01873 12.98182 -6.48352  0.600 33.97712  ?  179 PHE A CD1 1 
ATOM   2114 C CD1 B PHE A  1 179 ? -18.48880 15.53105 -6.83900  0.400 31.71021  ?  179 PHE A CD1 1 
ATOM   2115 C CD2 A PHE A  1 179 ? -18.24724 15.23081 -7.26729  0.600 33.56677  ?  179 PHE A CD2 1 
ATOM   2116 C CD2 B PHE A  1 179 ? -18.58257 13.42716 -5.71411  0.400 30.62079  ?  179 PHE A CD2 1 
ATOM   2117 C CE1 A PHE A  1 179 ? -18.87844 12.54830 -7.48422  0.600 41.18608  ?  179 PHE A CE1 1 
ATOM   2118 C CE1 B PHE A  1 179 ? -19.54844 15.15133 -7.64728  0.400 37.04141  ?  179 PHE A CE1 1 
ATOM   2119 C CE2 A PHE A  1 179 ? -19.09859 14.80069 -8.26942  0.600 35.91651  ?  179 PHE A CE2 1 
ATOM   2120 C CE2 B PHE A  1 179 ? -19.64288 13.04356 -6.51614  0.400 44.02145  ?  179 PHE A CE2 1 
ATOM   2121 C CZ  A PHE A  1 179 ? -19.41334 13.46108 -8.37688  0.600 32.02787  ?  179 PHE A CZ  1 
ATOM   2122 C CZ  B PHE A  1 179 ? -20.12471 13.90622 -7.48184  0.400 30.78953  ?  179 PHE A CZ  1 
ATOM   2123 N N   . LEU A  1 180 ? -14.82398 16.89407 -6.76090  1.000 20.08570  ?  180 LEU A N   1 
ATOM   2124 C CA  . LEU A  1 180 ? -14.59752 17.76818 -7.90557  1.000 22.76211  ?  180 LEU A CA  1 
ATOM   2125 C C   . LEU A  1 180 ? -13.33797 17.40912 -8.70140  1.000 20.35390  ?  180 LEU A C   1 
ATOM   2126 O O   . LEU A  1 180 ? -13.25248 17.75728 -9.88654  1.000 22.52897  ?  180 LEU A O   1 
ATOM   2127 C CB  . LEU A  1 180 ? -14.57556 19.22610 -7.42565  1.000 22.15487  ?  180 LEU A CB  1 
ATOM   2128 C CG  . LEU A  1 180 ? -16.01541 19.70863 -7.10564  1.000 24.23105  ?  180 LEU A CG  1 
ATOM   2129 C CD1 . LEU A  1 180 ? -15.97891 21.00057 -6.26531  1.000 26.79459  ?  180 LEU A CD1 1 
ATOM   2130 C CD2 . LEU A  1 180 ? -16.88446 19.89204 -8.39072  1.000 28.68124  ?  180 LEU A CD2 1 
ATOM   2131 N N   . TYR A  1 181 ? -12.37458 16.70927 -8.09585  1.000 19.98595  ?  181 TYR A N   1 
ATOM   2132 C CA  . TYR A  1 181 ? -11.29420 16.14642 -8.92610  1.000 24.42994  ?  181 TYR A CA  1 
ATOM   2133 C C   . TYR A  1 181 ? -11.81549 15.09345 -9.91285  1.000 24.86271  ?  181 TYR A C   1 
ATOM   2134 O O   . TYR A  1 181 ? -11.34853 15.00799 -11.06189 1.000 25.46368  ?  181 TYR A O   1 
ATOM   2135 C CB  . TYR A  1 181 ? -10.22649 15.52005 -8.03994  1.000 21.27276  ?  181 TYR A CB  1 
ATOM   2136 C CG  . TYR A  1 181 ? -9.32469  16.50661 -7.34296  1.000 21.95438  ?  181 TYR A CG  1 
ATOM   2137 C CD1 . TYR A  1 181 ? -9.75531  17.18022 -6.19376  1.000 19.72605  ?  181 TYR A CD1 1 
ATOM   2138 C CD2 . TYR A  1 181 ? -8.03435  16.75698 -7.83193  1.000 19.10046  ?  181 TYR A CD2 1 
ATOM   2139 C CE1 . TYR A  1 181 ? -8.90903  18.08012 -5.55370  1.000 24.05314  ?  181 TYR A CE1 1 
ATOM   2140 C CE2 . TYR A  1 181 ? -7.18381  17.67335 -7.19252  1.000 20.73646  ?  181 TYR A CE2 1 
ATOM   2141 C CZ  . TYR A  1 181 ? -7.63825  18.30215 -6.04955  1.000 20.66675  ?  181 TYR A CZ  1 
ATOM   2142 O OH  . TYR A  1 181 ? -6.85975  19.18947 -5.34777  1.000 22.03668  ?  181 TYR A OH  1 
ATOM   2143 N N   . GLY A  1 182 ? -12.76439 14.25941 -9.47396  1.000 21.65277  ?  182 GLY A N   1 
ATOM   2144 C CA  . GLY A  1 182 ? -13.43654 13.36552 -10.39803 1.000 23.04882  ?  182 GLY A CA  1 
ATOM   2145 C C   . GLY A  1 182 ? -14.19141 14.11032 -11.48623 1.000 23.43363  ?  182 GLY A C   1 
ATOM   2146 O O   . GLY A  1 182 ? -14.19781 13.69004 -12.64714 1.000 27.23218  ?  182 GLY A O   1 
ATOM   2147 N N   . PHE A  1 183 ? -14.84336 15.22467 -11.12861 1.000 23.24730  ?  183 PHE A N   1 
ATOM   2148 C CA  . PHE A  1 183 ? -15.54956 16.01599 -12.12955 1.000 23.81347  ?  183 PHE A CA  1 
ATOM   2149 C C   . PHE A  1 183 ? -14.59092 16.54263 -13.20405 1.000 26.44874  ?  183 PHE A C   1 
ATOM   2150 O O   . PHE A  1 183 ? -14.86333 16.45420 -14.40765 1.000 24.80023  ?  183 PHE A O   1 
ATOM   2151 C CB  . PHE A  1 183 ? -16.24415 17.17452 -11.41876 1.000 23.83368  ?  183 PHE A CB  1 
ATOM   2152 C CG  . PHE A  1 183 ? -17.14357 17.98898 -12.30650 1.000 27.09324  ?  183 PHE A CG  1 
ATOM   2153 C CD1 . PHE A  1 183 ? -18.28885 17.43323 -12.85855 1.000 31.60255  ?  183 PHE A CD1 1 
ATOM   2154 C CD2 . PHE A  1 183 ? -16.84074 19.31881 -12.58369 1.000 26.26128  ?  183 PHE A CD2 1 
ATOM   2155 C CE1 . PHE A  1 183 ? -19.11858 18.18646 -13.66636 1.000 33.32512  ?  183 PHE A CE1 1 
ATOM   2156 C CE2 . PHE A  1 183 ? -17.66718 20.07316 -13.38823 1.000 30.40264  ?  183 PHE A CE2 1 
ATOM   2157 C CZ  . PHE A  1 183 ? -18.80852 19.51705 -13.94001 1.000 31.54088  ?  183 PHE A CZ  1 
ATOM   2158 N N   . ALA A  1 184 ? -13.46993 17.11099 -12.76594 1.000 22.65832  ?  184 ALA A N   1 
ATOM   2159 C CA  . ALA A  1 184 ? -12.42653 17.58573 -13.66790 1.000 25.05162  ?  184 ALA A CA  1 
ATOM   2160 C C   . ALA A  1 184 ? -11.94870 16.50789 -14.64079 1.000 20.79798  ?  184 ALA A C   1 
ATOM   2161 O O   . ALA A  1 184 ? -11.60346 16.81282 -15.78907 1.000 24.03021  ?  184 ALA A O   1 
ATOM   2162 C CB  . ALA A  1 184 ? -11.25601 18.08872 -12.82353 1.000 24.77954  ?  184 ALA A CB  1 
ATOM   2163 N N   . PHE A  1 185 ? -11.87920 15.24923 -14.18411 1.000 23.72682  ?  185 PHE A N   1 
ATOM   2164 C CA  . PHE A  1 185 ? -11.40230 14.15137 -15.02914 1.000 24.88909  ?  185 PHE A CA  1 
ATOM   2165 C C   . PHE A  1 185 ? -12.16403 14.07566 -16.34734 1.000 27.31890  ?  185 PHE A C   1 
ATOM   2166 O O   . PHE A  1 185 ? -11.60436 13.66087 -17.36970 1.000 28.55425  ?  185 PHE A O   1 
ATOM   2167 C CB  . PHE A  1 185 ? -11.50621 12.83719 -14.23996 1.000 26.89701  ?  185 PHE A CB  1 
ATOM   2168 C CG  . PHE A  1 185 ? -11.14324 11.61980 -15.03283 1.000 25.84679  ?  185 PHE A CG  1 
ATOM   2169 C CD1 . PHE A  1 185 ? -9.83983  11.12795 -15.00775 1.000 31.63059  ?  185 PHE A CD1 1 
ATOM   2170 C CD2 . PHE A  1 185 ? -12.09451 10.93850 -15.76590 1.000 29.31156  ?  185 PHE A CD2 1 
ATOM   2171 C CE1 . PHE A  1 185 ? -9.49071  9.99565  -15.75274 1.000 29.45396  ?  185 PHE A CE1 1 
ATOM   2172 C CE2 . PHE A  1 185 ? -11.75326 9.81102  -16.50368 1.000 28.60552  ?  185 PHE A CE2 1 
ATOM   2173 C CZ  . PHE A  1 185 ? -10.44364 9.34750  -16.49413 1.000 30.58155  ?  185 PHE A CZ  1 
ATOM   2174 N N   . MET A  1 186 ? -13.43492 14.48543 -16.35526 1.000 27.12535  ?  186 MET A N   1 
ATOM   2175 C CA  . MET A  1 186 ? -14.27545 14.43676 -17.54707 1.000 33.14736  ?  186 MET A CA  1 
ATOM   2176 C C   . MET A  1 186 ? -13.88073 15.43215 -18.63913 1.000 35.06156  ?  186 MET A C   1 
ATOM   2177 O O   . MET A  1 186 ? -14.40398 15.33016 -19.75337 1.000 32.55359  ?  186 MET A O   1 
ATOM   2178 C CB  . MET A  1 186 ? -15.72933 14.71804 -17.15094 1.000 29.15681  ?  186 MET A CB  1 
ATOM   2179 C CG  . MET A  1 186 ? -16.26224 13.79429 -16.04268 1.000 36.86883  ?  186 MET A CG  1 
ATOM   2180 S SD  . MET A  1 186 ? -18.07551 13.73386 -16.01196 1.000 52.48295  ?  186 MET A SD  1 
ATOM   2181 C CE  . MET A  1 186 ? -18.45058 15.47236 -15.88186 1.000 43.74888  ?  186 MET A CE  1 
ATOM   2182 N N   . PHE A  1 187 ? -13.00373 16.39241 -18.35996 1.000 26.06684  ?  187 PHE A N   1 
ATOM   2183 C CA  . PHE A  1 187 ? -12.84597 17.49949 -19.29934 1.000 25.68527  ?  187 PHE A CA  1 
ATOM   2184 C C   . PHE A  1 187 ? -11.59620 17.32036 -20.15691 1.000 25.57311  ?  187 PHE A C   1 
ATOM   2185 O O   . PHE A  1 187 ? -10.69477 16.54997 -19.80950 1.000 26.83388  ?  187 PHE A O   1 
ATOM   2186 C CB  . PHE A  1 187 ? -12.77253 18.82727 -18.51980 1.000 28.69399  ?  187 PHE A CB  1 
ATOM   2187 C CG  . PHE A  1 187 ? -14.10523 19.28827 -17.99057 1.000 26.33074  ?  187 PHE A CG  1 
ATOM   2188 C CD1 . PHE A  1 187 ? -14.85847 20.19457 -18.70525 1.000 32.88591  ?  187 PHE A CD1 1 
ATOM   2189 C CD2 . PHE A  1 187 ? -14.59804 18.80931 -16.77781 1.000 27.34406  ?  187 PHE A CD2 1 
ATOM   2190 C CE1 . PHE A  1 187 ? -16.08982 20.63023 -18.24158 1.000 27.21384  ?  187 PHE A CE1 1 
ATOM   2191 C CE2 . PHE A  1 187 ? -15.83300 19.22209 -16.31353 1.000 29.94631  ?  187 PHE A CE2 1 
ATOM   2192 C CZ  . PHE A  1 187 ? -16.58933 20.13804 -17.05003 1.000 26.46361  ?  187 PHE A CZ  1 
ATOM   2193 N N   . PRO A  1 188 ? -11.50889 18.02010 -21.29703 1.000 29.12422  ?  188 PRO A N   1 
ATOM   2194 C CA  . PRO A  1 188 ? -10.29737 17.93039 -22.12442 1.000 31.27247  ?  188 PRO A CA  1 
ATOM   2195 C C   . PRO A  1 188 ? -9.08406  18.49811 -21.39444 1.000 31.36804  ?  188 PRO A C   1 
ATOM   2196 O O   . PRO A  1 188 ? -9.20738  19.19600 -20.38208 1.000 25.59315  ?  188 PRO A O   1 
ATOM   2197 C CB  . PRO A  1 188 ? -10.64568 18.75910 -23.37232 1.000 31.13814  ?  188 PRO A CB  1 
ATOM   2198 C CG  . PRO A  1 188 ? -12.12970 18.92315 -23.34983 1.000 37.47222  ?  188 PRO A CG  1 
ATOM   2199 C CD  . PRO A  1 188 ? -12.51664 18.90802 -21.89830 1.000 28.67401  ?  188 PRO A CD  1 
ATOM   2200 N N   A PHE A  1 189 ? -7.89704  18.13179 -21.89477 0.600 26.84661  ?  189 PHE A N   1 
ATOM   2201 N N   B PHE A  1 189 ? -7.91589  18.25890 -22.00102 0.400 26.80481  ?  189 PHE A N   1 
ATOM   2202 C CA  A PHE A  1 189 ? -6.61668  18.47050 -21.26708 0.600 26.17469  ?  189 PHE A CA  1 
ATOM   2203 C CA  B PHE A  1 189 ? -6.60593  18.45739 -21.37573 0.400 26.05819  ?  189 PHE A CA  1 
ATOM   2204 C C   A PHE A  1 189 ? -6.58198  19.83931 -20.58744 0.600 23.80973  ?  189 PHE A C   1 
ATOM   2205 C C   B PHE A  1 189 ? -6.45382  19.80802 -20.66765 0.400 23.36882  ?  189 PHE A C   1 
ATOM   2206 O O   A PHE A  1 189 ? -6.39285  19.94117 -19.36658 0.600 22.60671  ?  189 PHE A O   1 
ATOM   2207 O O   B PHE A  1 189 ? -6.02121  19.86511 -19.51053 0.400 23.66211  ?  189 PHE A O   1 
ATOM   2208 C CB  A PHE A  1 189 ? -5.51201  18.39765 -22.32098 0.600 25.50256  ?  189 PHE A CB  1 
ATOM   2209 C CB  B PHE A  1 189 ? -5.53148  18.28649 -22.44979 0.400 25.67130  ?  189 PHE A CB  1 
ATOM   2210 C CG  A PHE A  1 189 ? -4.16232  18.85122 -21.83350 0.600 24.36462  ?  189 PHE A CG  1 
ATOM   2211 C CG  B PHE A  1 189 ? -4.13076  18.28116 -21.92095 0.400 24.10880  ?  189 PHE A CG  1 
ATOM   2212 C CD1 A PHE A  1 189 ? -3.43825  18.08746 -20.92072 0.600 21.62714  ?  189 PHE A CD1 1 
ATOM   2213 C CD1 B PHE A  1 189 ? -3.66022  17.22104 -21.16858 0.400 24.02763  ?  189 PHE A CD1 1 
ATOM   2214 C CD2 A PHE A  1 189 ? -3.59753  20.02212 -22.31898 0.600 23.92043  ?  189 PHE A CD2 1 
ATOM   2215 C CD2 B PHE A  1 189 ? -3.27453  19.33581 -22.19779 0.400 29.27106  ?  189 PHE A CD2 1 
ATOM   2216 C CE1 A PHE A  1 189 ? -2.17672  18.49131 -20.48572 0.600 27.74516  ?  189 PHE A CE1 1 
ATOM   2217 C CE1 B PHE A  1 189 ? -2.35682  17.21953 -20.68777 0.400 27.34456  ?  189 PHE A CE1 1 
ATOM   2218 C CE2 A PHE A  1 189 ? -2.32300  20.43278 -21.90087 0.600 25.88266  ?  189 PHE A CE2 1 
ATOM   2219 C CE2 B PHE A  1 189 ? -1.97105  19.33580 -21.72654 0.400 25.37235  ?  189 PHE A CE2 1 
ATOM   2220 C CZ  A PHE A  1 189 ? -1.61416  19.67022 -20.97981 0.600 25.50040  ?  189 PHE A CZ  1 
ATOM   2221 C CZ  B PHE A  1 189 ? -1.51607  18.27507 -20.96958 0.400 29.76628  ?  189 PHE A CZ  1 
ATOM   2222 N N   . SER A  1 190 ? -6.75380  20.91338 -21.36240 1.000 25.18751  ?  190 SER A N   1 
ATOM   2223 C CA  . SER A  1 190 ? -6.49886  22.24440 -20.79869 1.000 25.23808  ?  190 SER A CA  1 
ATOM   2224 C C   . SER A  1 190 ? -7.44912  22.56745 -19.64792 1.000 24.41866  ?  190 SER A C   1 
ATOM   2225 O O   . SER A  1 190 ? -7.02100  22.99923 -18.56809 1.000 24.70152  ?  190 SER A O   1 
ATOM   2226 C CB  . SER A  1 190 ? -6.59347  23.31370 -21.87689 1.000 26.76740  ?  190 SER A CB  1 
ATOM   2227 O OG  . SER A  1 190 ? -6.39026  24.58887 -21.29698 1.000 30.21628  ?  190 SER A OG  1 
ATOM   2228 N N   . ILE A  1 191 ? -8.74112  22.31474 -19.84685 1.000 24.86686  ?  191 ILE A N   1 
ATOM   2229 C CA  . ILE A  1 191 ? -9.73706  22.62055 -18.82174 1.000 22.81011  ?  191 ILE A CA  1 
ATOM   2230 C C   . ILE A  1 191 ? -9.53252  21.73692 -17.59748 1.000 22.83934  ?  191 ILE A C   1 
ATOM   2231 O O   . ILE A  1 191 ? -9.57674  22.22620 -16.45524 1.000 23.62620  ?  191 ILE A O   1 
ATOM   2232 C CB  . ILE A  1 191 ? -11.14527 22.47007 -19.42357 1.000 25.24175  ?  191 ILE A CB  1 
ATOM   2233 C CG1 . ILE A  1 191 ? -11.37472 23.59285 -20.44446 1.000 29.35839  ?  191 ILE A CG1 1 
ATOM   2234 C CG2 . ILE A  1 191 ? -12.21679 22.51160 -18.33883 1.000 27.35853  ?  191 ILE A CG2 1 
ATOM   2235 C CD1 . ILE A  1 191 ? -12.57402 23.33930 -21.34030 1.000 35.05060  ?  191 ILE A CD1 1 
ATOM   2236 N N   A LYS A  1 192 ? -9.40129  20.42076 -17.81231 0.600 21.84875  ?  192 LYS A N   1 
ATOM   2237 N N   B LYS A  1 192 ? -9.26055  20.43955 -17.81798 0.400 22.44281  ?  192 LYS A N   1 
ATOM   2238 C CA  A LYS A  1 192 ? -9.01462  19.49992 -16.74923 0.600 22.19417  ?  192 LYS A CA  1 
ATOM   2239 C CA  B LYS A  1 192 ? -9.08312  19.47547 -16.72816 0.400 22.35080  ?  192 LYS A CA  1 
ATOM   2240 C C   A LYS A  1 192 ? -7.84111  20.05281 -15.92892 0.600 19.63757  ?  192 LYS A C   1 
ATOM   2241 C C   B LYS A  1 192 ? -7.87792  19.81037 -15.84286 0.400 21.39806  ?  192 LYS A C   1 
ATOM   2242 O O   A LYS A  1 192 ? -7.93663  20.23016 -14.70663 0.600 18.24286  ?  192 LYS A O   1 
ATOM   2243 O O   B LYS A  1 192 ? -7.90705  19.58509 -14.62439 0.400 21.33157  ?  192 LYS A O   1 
ATOM   2244 C CB  A LYS A  1 192 ? -8.68263  18.14815 -17.38552 0.600 22.05714  ?  192 LYS A CB  1 
ATOM   2245 C CB  B LYS A  1 192 ? -8.96739  18.06446 -17.31440 0.400 22.12703  ?  192 LYS A CB  1 
ATOM   2246 C CG  A LYS A  1 192 ? -8.17671  17.10839 -16.40322 0.600 21.27758  ?  192 LYS A CG  1 
ATOM   2247 C CG  B LYS A  1 192 ? -8.37624  17.01823 -16.36415 0.400 21.70580  ?  192 LYS A CG  1 
ATOM   2248 C CD  A LYS A  1 192 ? -8.14982  15.70113 -16.99131 0.600 24.26917  ?  192 LYS A CD  1 
ATOM   2249 C CD  B LYS A  1 192 ? -8.24811  15.65005 -17.03878 0.400 24.17329  ?  192 LYS A CD  1 
ATOM   2250 C CE  A LYS A  1 192 ? -7.23541  15.63510 -18.22073 0.600 28.29334  ?  192 LYS A CE  1 
ATOM   2251 C CE  B LYS A  1 192 ? -7.21770  15.69333 -18.17225 0.400 28.13438  ?  192 LYS A CE  1 
ATOM   2252 N NZ  A LYS A  1 192 ? -7.09291  14.24423 -18.74623 0.600 34.31401  ?  192 LYS A NZ  1 
ATOM   2253 N NZ  B LYS A  1 192 ? -7.34597  14.56098 -19.13770 0.400 36.32961  ?  192 LYS A NZ  1 
ATOM   2254 N N   A ASN A  1 193 ? -6.72310  20.35087 -16.60739 0.600 20.86203  ?  193 ASN A N   1 
ATOM   2255 N N   B ASN A  1 193 ? -6.78830  20.30199 -16.43655 0.400 21.68034  ?  193 ASN A N   1 
ATOM   2256 C CA  A ASN A  1 193 ? -5.51350  20.71911 -15.87825 0.600 24.93784  ?  193 ASN A CA  1 
ATOM   2257 C CA  B ASN A  1 193 ? -5.62765  20.63238 -15.61545 0.400 24.20589  ?  193 ASN A CA  1 
ATOM   2258 C C   A ASN A  1 193 ? -5.66886  22.03212 -15.12847 0.600 22.97167  ?  193 ASN A C   1 
ATOM   2259 C C   B ASN A  1 193 ? -5.71043  22.04526 -15.03980 0.400 23.22155  ?  193 ASN A C   1 
ATOM   2260 O O   A ASN A  1 193 ? -5.14649  22.18541 -14.01159 0.600 23.47255  ?  193 ASN A O   1 
ATOM   2261 O O   B ASN A  1 193 ? -5.15435  22.30172 -13.95828 0.400 22.97628  ?  193 ASN A O   1 
ATOM   2262 C CB  A ASN A  1 193 ? -4.31739  20.69759 -16.81505 0.600 22.68804  ?  193 ASN A CB  1 
ATOM   2263 C CB  B ASN A  1 193 ? -4.31919  20.37627 -16.37426 0.400 24.57213  ?  193 ASN A CB  1 
ATOM   2264 C CG  A ASN A  1 193 ? -3.66707  19.33389 -16.83442 0.600 20.91238  ?  193 ASN A CG  1 
ATOM   2265 C CG  B ASN A  1 193 ? -4.14506  18.90283 -16.77065 0.400 23.26598  ?  193 ASN A CG  1 
ATOM   2266 O OD1 A ASN A  1 193 ? -2.99661  18.96753 -15.87457 0.600 18.46453  ?  193 ASN A OD1 1 
ATOM   2267 O OD1 B ASN A  1 193 ? -3.47923  18.13983 -16.07198 0.400 25.05941  ?  193 ASN A OD1 1 
ATOM   2268 N ND2 A ASN A  1 193 ? -3.92039  18.54507 -17.88302 0.600 22.83968  ?  193 ASN A ND2 1 
ATOM   2269 N ND2 B ASN A  1 193 ? -4.74426  18.50329 -17.89515 0.400 19.59614  ?  193 ASN A ND2 1 
ATOM   2270 N N   . GLN A  1 194 ? -6.39672  22.97678 -15.72176 1.000 21.24587  ?  194 GLN A N   1 
ATOM   2271 C CA  . GLN A  1 194 ? -6.76373  24.22093 -15.03454 1.000 21.81850  ?  194 GLN A CA  1 
ATOM   2272 C C   . GLN A  1 194 ? -7.56249  23.92874 -13.76689 1.000 23.20598  ?  194 GLN A C   1 
ATOM   2273 O O   . GLN A  1 194 ? -7.28948  24.49944 -12.70245 1.000 22.39896  ?  194 GLN A O   1 
ATOM   2274 C CB  . GLN A  1 194 ? -7.59231  25.09764 -15.95948 1.000 22.53574  ?  194 GLN A CB  1 
ATOM   2275 C CG  . GLN A  1 194 ? -6.81270  25.77907 -17.04326 1.000 22.39534  ?  194 GLN A CG  1 
ATOM   2276 C CD  . GLN A  1 194 ? -7.75102  26.55440 -17.93141 1.000 29.36416  ?  194 GLN A CD  1 
ATOM   2277 O OE1 . GLN A  1 194 ? -8.36542  27.54043 -17.51702 1.000 30.64522  ?  194 GLN A OE1 1 
ATOM   2278 N NE2 . GLN A  1 194 ? -7.88255  26.09460 -19.16866 1.000 29.65246  ?  194 GLN A NE2 1 
ATOM   2279 N N   A MET A  1 195 ? -8.58026  23.08379 -13.84062 0.600 19.83413  ?  195 MET A N   1 
ATOM   2280 N N   B MET A  1 195 ? -8.48948  22.96376 -13.87889 0.400 20.22492  ?  195 MET A N   1 
ATOM   2281 C CA  A MET A  1 195 ? -9.35081  22.82156 -12.63017 0.600 21.88829  ?  195 MET A CA  1 
ATOM   2282 C CA  B MET A  1 195 ? -9.30723  22.48480 -12.77063 0.400 20.91481  ?  195 MET A CA  1 
ATOM   2283 C C   A MET A  1 195 ? -8.46349  22.26755 -11.51797 0.600 19.25126  ?  195 MET A C   1 
ATOM   2284 C C   B MET A  1 195 ? -8.46710  21.79601 -11.70578 0.400 21.25230  ?  195 MET A C   1 
ATOM   2285 O O   A MET A  1 195 ? -8.48590  22.76125 -10.38199 0.600 15.93616  ?  195 MET A O   1 
ATOM   2286 O O   B MET A  1 195 ? -8.68558  21.99534 -10.50022 0.400 16.38599  ?  195 MET A O   1 
ATOM   2287 C CB  A MET A  1 195 ? -10.52939 21.89935 -12.93558 0.600 23.52852  ?  195 MET A CB  1 
ATOM   2288 C CB  B MET A  1 195 ? -10.34130 21.48654 -13.29911 0.400 18.54806  ?  195 MET A CB  1 
ATOM   2289 C CG  A MET A  1 195 ? -11.50749 22.53808 -13.93690 0.600 18.12618  ?  195 MET A CG  1 
ATOM   2290 C CG  B MET A  1 195 ? -11.69801 22.07475 -13.70463 0.400 26.72429  ?  195 MET A CG  1 
ATOM   2291 S SD  A MET A  1 195 ? -12.75052 21.39031 -14.54448 0.600 19.52072  ?  195 MET A SD  1 
ATOM   2292 S SD  B MET A  1 195 ? -12.97739 20.80124 -13.84474 0.400 21.79086  ?  195 MET A SD  1 
ATOM   2293 C CE  A MET A  1 195 ? -13.91568 22.50933 -15.24399 0.600 21.67992  ?  195 MET A CE  1 
ATOM   2294 C CE  B MET A  1 195 ? -14.35228 21.83578 -14.33874 0.400 29.37330  ?  195 MET A CE  1 
ATOM   2295 N N   A TYR A  1 196 ? -7.65071  21.24806 -11.83505 0.600 19.91820  ?  196 TYR A N   1 
ATOM   2296 N N   B TYR A  1 196 ? -7.56115  20.90331 -12.12155 0.400 17.71750  ?  196 TYR A N   1 
ATOM   2297 C CA  A TYR A  1 196 ? -6.75281  20.66707 -10.83498 0.600 17.57223  ?  196 TYR A CA  1 
ATOM   2298 C CA  B TYR A  1 196 ? -6.69518  20.25668 -11.14066 0.400 18.20025  ?  196 TYR A CA  1 
ATOM   2299 C C   A TYR A  1 196 ? -5.81621  21.72586 -10.23994 0.600 21.28756  ?  196 TYR A C   1 
ATOM   2300 C C   B TYR A  1 196 ? -5.89192  21.29509 -10.36300 0.400 24.06385  ?  196 TYR A C   1 
ATOM   2301 O O   A TYR A  1 196 ? -5.44158  21.63582 -9.06449  0.600 23.72605  ?  196 TYR A O   1 
ATOM   2302 O O   B TYR A  1 196 ? -5.96208  21.35346 -9.13102  0.400 20.76462  ?  196 TYR A O   1 
ATOM   2303 C CB  A TYR A  1 196 ? -5.91881  19.53755 -11.46084 0.600 19.70323  ?  196 TYR A CB  1 
ATOM   2304 C CB  B TYR A  1 196 ? -5.76313  19.25086 -11.81949 0.400 18.92474  ?  196 TYR A CB  1 
ATOM   2305 C CG  A TYR A  1 196 ? -6.68694  18.28682 -11.81618 0.600 19.98388  ?  196 TYR A CG  1 
ATOM   2306 C CG  B TYR A  1 196 ? -6.43461  17.96077 -12.22128 0.400 26.05380  ?  196 TYR A CG  1 
ATOM   2307 C CD1 A TYR A  1 196 ? -7.64931  17.77836 -10.96002 0.600 21.09206  ?  196 TYR A CD1 1 
ATOM   2308 C CD1 B TYR A  1 196 ? -7.71075  17.64461 -11.76355 0.400 18.49913  ?  196 TYR A CD1 1 
ATOM   2309 C CD2 A TYR A  1 196 ? -6.45578  17.61025 -13.01440 0.600 23.26066  ?  196 TYR A CD2 1 
ATOM   2310 C CD2 B TYR A  1 196 ? -5.80202  17.05787 -13.07017 0.400 24.02100  ?  196 TYR A CD2 1 
ATOM   2311 C CE1 A TYR A  1 196 ? -8.34204  16.62073 -11.25087 0.600 20.31371  ?  196 TYR A CE1 1 
ATOM   2312 C CE1 B TYR A  1 196 ? -8.32907  16.46105 -12.13538 0.400 22.89181  ?  196 TYR A CE1 1 
ATOM   2313 C CE2 A TYR A  1 196 ? -7.15969  16.45961 -13.32445 0.600 22.28303  ?  196 TYR A CE2 1 
ATOM   2314 C CE2 B TYR A  1 196 ? -6.41874  15.87359 -13.45766 0.400 25.71298  ?  196 TYR A CE2 1 
ATOM   2315 C CZ  A TYR A  1 196 ? -8.11041  15.96863 -12.43814 0.600 23.28376  ?  196 TYR A CZ  1 
ATOM   2316 C CZ  B TYR A  1 196 ? -7.68363  15.57542 -12.98338 0.400 21.39380  ?  196 TYR A CZ  1 
ATOM   2317 O OH  A TYR A  1 196 ? -8.83304  14.81994 -12.73101 0.600 24.83415  ?  196 TYR A OH  1 
ATOM   2318 O OH  B TYR A  1 196 ? -8.32148  14.40384 -13.35851 0.400 20.12814  ?  196 TYR A OH  1 
ATOM   2319 N N   A ASN A  1 197 ? -5.39926  22.70884 -11.04831 0.600 17.99552  ?  197 ASN A N   1 
ATOM   2320 N N   B ASN A  1 197 ? -5.14417  22.14197 -11.08496 0.400 21.11577  ?  197 ASN A N   1 
ATOM   2321 C CA  A ASN A  1 197 ? -4.54130  23.76718 -10.53214 0.600 18.21945  ?  197 ASN A CA  1 
ATOM   2322 C CA  B ASN A  1 197 ? -4.26124  23.12289 -10.45452 0.400 18.87450  ?  197 ASN A CA  1 
ATOM   2323 C C   A ASN A  1 197 ? -5.26509  24.56897 -9.46137  0.600 19.04561  ?  197 ASN A C   1 
ATOM   2324 C C   B ASN A  1 197 ? -4.98826  23.94961 -9.40008  0.400 16.04370  ?  197 ASN A C   1 
ATOM   2325 O O   A ASN A  1 197 ? -4.68358  24.90275 -8.42806  0.600 18.42497  ?  197 ASN A O   1 
ATOM   2326 O O   B ASN A  1 197 ? -4.50021  24.11556 -8.27785  0.400 23.12024  ?  197 ASN A O   1 
ATOM   2327 C CB  A ASN A  1 197 ? -4.07295  24.68859 -11.66483 0.600 19.54898  ?  197 ASN A CB  1 
ATOM   2328 C CB  B ASN A  1 197 ? -3.62524  24.02697 -11.51932 0.400 20.34814  ?  197 ASN A CB  1 
ATOM   2329 C CG  A ASN A  1 197 ? -2.98007  24.06663 -12.54090 0.600 18.03489  ?  197 ASN A CG  1 
ATOM   2330 C CG  B ASN A  1 197 ? -2.78522  23.25287 -12.54310 0.400 21.14336  ?  197 ASN A CG  1 
ATOM   2331 O OD1 A ASN A  1 197 ? -2.43362  23.00370 -12.23453 0.600 18.62435  ?  197 ASN A OD1 1 
ATOM   2332 O OD1 B ASN A  1 197 ? -2.31658  22.14355 -12.27696 0.400 23.30852  ?  197 ASN A OD1 1 
ATOM   2333 N ND2 A ASN A  1 197 ? -2.64569  24.74069 -13.62803 0.600 18.90365  ?  197 ASN A ND2 1 
ATOM   2334 N ND2 B ASN A  1 197 ? -2.59214  23.84625 -13.71801 0.400 25.29679  ?  197 ASN A ND2 1 
ATOM   2335 N N   A ILE A  1 198 ? -6.54597  24.87388 -9.69020  0.600 20.53492  ?  198 ILE A N   1 
ATOM   2336 N N   B ILE A  1 198 ? -6.18919  24.43427 -9.72890  0.400 19.95007  ?  198 ILE A N   1 
ATOM   2337 C CA  A ILE A  1 198 ? -7.31259  25.63007 -8.70408  0.600 20.33526  ?  198 ILE A CA  1 
ATOM   2338 C CA  B ILE A  1 198 ? -6.89564  25.33391 -8.81794  0.400 20.35275  ?  198 ILE A CA  1 
ATOM   2339 C C   A ILE A  1 198 ? -7.84897  24.73362 -7.57920  0.600 20.56551  ?  198 ILE A C   1 
ATOM   2340 C C   B ILE A  1 198 ? -7.42922  24.57392 -7.61113  0.400 21.87822  ?  198 ILE A C   1 
ATOM   2341 O O   A ILE A  1 198 ? -8.01158  25.18975 -6.43416  0.600 21.10675  ?  198 ILE A O   1 
ATOM   2342 O O   B ILE A  1 198 ? -7.24164  24.99731 -6.46387  0.400 20.53306  ?  198 ILE A O   1 
ATOM   2343 C CB  A ILE A  1 198 ? -8.42727  26.42939 -9.40257  0.600 24.67056  ?  198 ILE A CB  1 
ATOM   2344 C CB  B ILE A  1 198 ? -8.01776  26.08539 -9.55119  0.400 19.05916  ?  198 ILE A CB  1 
ATOM   2345 C CG1 A ILE A  1 198 ? -7.84451  27.24102 -10.55166 0.600 20.78564  ?  198 ILE A CG1 1 
ATOM   2346 C CG1 B ILE A  1 198 ? -7.40765  27.15491 -10.45089 0.400 24.91571  ?  198 ILE A CG1 1 
ATOM   2347 C CG2 A ILE A  1 198 ? -9.10114  27.36180 -8.41339  0.600 21.61930  ?  198 ILE A CG2 1 
ATOM   2348 C CG2 B ILE A  1 198 ? -8.99762  26.68816 -8.51618  0.400 21.35755  ?  198 ILE A CG2 1 
ATOM   2349 C CD1 A ILE A  1 198 ? -6.64264  28.16810 -10.15707 0.600 19.68463  ?  198 ILE A CD1 1 
ATOM   2350 C CD1 B ILE A  1 198 ? -8.38673  27.90748 -11.28838 0.400 34.96612  ?  198 ILE A CD1 1 
ATOM   2351 N N   . LEU A  1 199 ? -8.12181  23.45440 -7.86047  1.000 20.27969  ?  199 LEU A N   1 
ATOM   2352 C CA  . LEU A  1 199 ? -8.60154  22.57183 -6.79556  1.000 22.22282  ?  199 LEU A CA  1 
ATOM   2353 C C   . LEU A  1 199 ? -7.52599  22.35162 -5.73699  1.000 19.95756  ?  199 LEU A C   1 
ATOM   2354 O O   . LEU A  1 199 ? -7.82560  22.32561 -4.53520  1.000 24.06726  ?  199 LEU A O   1 
ATOM   2355 C CB  . LEU A  1 199 ? -9.14637  21.25944 -7.38417  1.000 21.19189  ?  199 LEU A CB  1 
ATOM   2356 C CG  . LEU A  1 199 ? -10.52816 21.26860 -8.08014  1.000 21.72986  ?  199 LEU A CG  1 
ATOM   2357 C CD1 . LEU A  1 199 ? -10.76363 19.98571 -8.92595  1.000 22.06424  ?  199 LEU A CD1 1 
ATOM   2358 C CD2 . LEU A  1 199 ? -11.65324 21.41604 -7.04592  1.000 22.85589  ?  199 LEU A CD2 1 
ATOM   2359 N N   A ASP A  1 200 ? -6.25841  22.23431 -6.16159  0.600 21.16371  ?  200 ASP A N   1 
ATOM   2360 N N   B ASP A  1 200 ? -6.25730  22.21728 -6.15725  0.400 21.19255  ?  200 ASP A N   1 
ATOM   2361 C CA  A ASP A  1 200 ? -5.16841  22.05801 -5.20201  0.600 23.88086  ?  200 ASP A CA  1 
ATOM   2362 C CA  B ASP A  1 200 ? -5.16431  22.05013 -5.19501  0.400 23.87146  ?  200 ASP A CA  1 
ATOM   2363 C C   A ASP A  1 200 ? -5.12266  23.20606 -4.20012  0.600 22.43044  ?  200 ASP A C   1 
ATOM   2364 C C   B ASP A  1 200 ? -5.08312  23.21532 -4.21033  0.400 22.54695  ?  200 ASP A C   1 
ATOM   2365 O O   A ASP A  1 200 ? -4.83953  22.99250 -3.01899  0.600 22.78188  ?  200 ASP A O   1 
ATOM   2366 O O   B ASP A  1 200 ? -4.69635  23.02115 -3.05433  0.400 23.07350  ?  200 ASP A O   1 
ATOM   2367 C CB  A ASP A  1 200 ? -3.82978  21.93936 -5.92254  0.600 24.05553  ?  200 ASP A CB  1 
ATOM   2368 C CB  B ASP A  1 200 ? -3.82435  21.88546 -5.91915  0.400 24.00156  ?  200 ASP A CB  1 
ATOM   2369 C CG  A ASP A  1 200 ? -3.68789  20.65209 -6.71388  0.600 21.58465  ?  200 ASP A CG  1 
ATOM   2370 C CG  B ASP A  1 200 ? -3.49588  20.43814 -6.26278  0.400 24.47710  ?  200 ASP A CG  1 
ATOM   2371 O OD1 A ASP A  1 200 ? -4.45556  19.67780 -6.47888  0.600 23.96379  ?  200 ASP A OD1 1 
ATOM   2372 O OD1 B ASP A  1 200 ? -4.30835  19.52562 -5.99923  0.400 20.89471  ?  200 ASP A OD1 1 
ATOM   2373 O OD2 A ASP A  1 200 ? -2.78131  20.59345 -7.58036  0.600 26.26154  -1 200 ASP A OD2 1 
ATOM   2374 O OD2 B ASP A  1 200 ? -2.40287  20.20651 -6.82245  0.400 25.87562  -1 200 ASP A OD2 1 
ATOM   2375 N N   . ILE A  1 201 ? -5.42675  24.42974 -4.65195  1.000 21.26575  ?  201 ILE A N   1 
ATOM   2376 C CA  . ILE A  1 201 ? -5.47147  25.58088 -3.73803  1.000 22.89655  ?  201 ILE A CA  1 
ATOM   2377 C C   . ILE A  1 201 ? -6.47433  25.32377 -2.63086  1.000 26.71731  ?  201 ILE A C   1 
ATOM   2378 O O   . ILE A  1 201 ? -6.20252  25.58989 -1.45925  1.000 25.66464  ?  201 ILE A O   1 
ATOM   2379 C CB  . ILE A  1 201 ? -5.83885  26.87245 -4.49161  1.000 23.88435  ?  201 ILE A CB  1 
ATOM   2380 C CG1 . ILE A  1 201 ? -4.79816  27.22025 -5.53975  1.000 23.05826  ?  201 ILE A CG1 1 
ATOM   2381 C CG2 . ILE A  1 201 ? -6.02291  28.04310 -3.47703  1.000 25.88007  ?  201 ILE A CG2 1 
ATOM   2382 C CD1 . ILE A  1 201 ? -5.25003  28.36834 -6.47720  1.000 26.14730  ?  201 ILE A CD1 1 
ATOM   2383 N N   . VAL A  1 202 ? -7.65658  24.82467 -3.00509  1.000 22.49469  ?  202 VAL A N   1 
ATOM   2384 C CA  . VAL A  1 202 ? -8.74960  24.56987 -2.07141  1.000 24.21018  ?  202 VAL A CA  1 
ATOM   2385 C C   . VAL A  1 202 ? -8.45364  23.36139 -1.19264  1.000 22.03523  ?  202 VAL A C   1 
ATOM   2386 O O   . VAL A  1 202 ? -8.56412  23.43228 0.03266   1.000 26.37477  ?  202 VAL A O   1 
ATOM   2387 C CB  . VAL A  1 202 ? -10.08127 24.41897 -2.82906  1.000 27.50093  ?  202 VAL A CB  1 
ATOM   2388 C CG1 . VAL A  1 202 ? -11.22826 24.25375 -1.84826  1.000 30.49568  ?  202 VAL A CG1 1 
ATOM   2389 C CG2 . VAL A  1 202 ? -10.34461 25.60376 -3.71374  1.000 27.90076  ?  202 VAL A CG2 1 
ATOM   2390 N N   . SER A  1 203 ? -8.06513  22.23276 -1.80074  1.000 18.64030  ?  203 SER A N   1 
ATOM   2391 C CA  . SER A  1 203 ? -7.85835  21.00472 -1.03563  1.000 18.76984  ?  203 SER A CA  1 
ATOM   2392 C C   . SER A  1 203 ? -6.63033  21.06624 -0.11216  1.000 23.65613  ?  203 SER A C   1 
ATOM   2393 O O   . SER A  1 203 ? -6.66538  20.52670 1.00659   1.000 23.99803  ?  203 SER A O   1 
ATOM   2394 C CB  . SER A  1 203 ? -7.79657  19.79429 -1.98307  1.000 23.06424  ?  203 SER A CB  1 
ATOM   2395 O OG  . SER A  1 203 ? -6.52547  19.75173 -2.61324  1.000 22.97743  ?  203 SER A OG  1 
ATOM   2396 N N   A LYS A  1 204 ? -5.53954  21.69730 -0.55058  0.600 23.98015  ?  204 LYS A N   1 
ATOM   2397 N N   B LYS A  1 204 ? -5.55002  21.73131 -0.53178  0.400 24.21284  ?  204 LYS A N   1 
ATOM   2398 C CA  A LYS A  1 204 ? -4.35008  21.79756 0.30291   0.600 24.50268  ?  204 LYS A CA  1 
ATOM   2399 C CA  B LYS A  1 204 ? -4.28357  21.70161 0.19843   0.400 24.70907  ?  204 LYS A CA  1 
ATOM   2400 C C   A LYS A  1 204 ? -4.32677  23.13213 1.03400   0.600 19.61658  ?  204 LYS A C   1 
ATOM   2401 C C   B LYS A  1 204 ? -3.96526  23.00258 0.92401   0.400 22.92827  ?  204 LYS A C   1 
ATOM   2402 O O   A LYS A  1 204 ? -4.44982  23.17976 2.26127   0.600 22.67669  ?  204 LYS A O   1 
ATOM   2403 O O   B LYS A  1 204 ? -3.54830  22.98617 2.09890   0.400 21.16699  ?  204 LYS A O   1 
ATOM   2404 C CB  A LYS A  1 204 ? -3.06035  21.54481 -0.49531  0.600 23.58686  ?  204 LYS A CB  1 
ATOM   2405 C CB  B LYS A  1 204 ? -3.12929  21.34191 -0.76378  0.400 25.89756  ?  204 LYS A CB  1 
ATOM   2406 C CG  A LYS A  1 204 ? -2.87630  20.06973 -0.93617  0.600 24.33627  ?  204 LYS A CG  1 
ATOM   2407 C CG  B LYS A  1 204 ? -3.30241  19.98594 -1.46192  0.400 22.12125  ?  204 LYS A CG  1 
ATOM   2408 C CD  A LYS A  1 204 ? -1.77489  19.91370 -1.96378  0.600 22.17261  ?  204 LYS A CD  1 
ATOM   2409 C CD  B LYS A  1 204 ? -2.22727  19.72864 -2.51202  0.400 21.95799  ?  204 LYS A CD  1 
ATOM   2410 C CE  A LYS A  1 204 ? -1.75396  18.50564 -2.56397  0.600 26.07339  ?  204 LYS A CE  1 
ATOM   2411 C CE  B LYS A  1 204 ? -1.80348  18.24833 -2.53430  0.400 25.94682  ?  204 LYS A CE  1 
ATOM   2412 N NZ  A LYS A  1 204 ? -2.80221  18.20689 -3.60533  0.600 23.57400  ?  204 LYS A NZ  1 
ATOM   2413 N NZ  B LYS A  1 204 ? -2.62774  17.36781 -3.42640  0.400 22.05776  ?  204 LYS A NZ  1 
ATOM   2414 N N   A ASN A  1 205 ? -4.19251  24.23122 0.29006   0.600 21.45609  ?  205 ASN A N   1 
ATOM   2415 N N   B ASN A  1 205 ? -4.10901  24.14436 0.24332   0.400 22.08115  ?  205 ASN A N   1 
ATOM   2416 C CA  A ASN A  1 205 ? -3.71929  25.47899 0.87313   0.600 24.59094  ?  205 ASN A CA  1 
ATOM   2417 C CA  B ASN A  1 205 ? -3.75478  25.42164 0.84705   0.400 24.52441  ?  205 ASN A CA  1 
ATOM   2418 C C   A ASN A  1 205 ? -4.78937  26.19451 1.69810   0.600 24.76164  ?  205 ASN A C   1 
ATOM   2419 C C   B ASN A  1 205 ? -4.80343  25.88754 1.84354   0.400 24.15695  ?  205 ASN A C   1 
ATOM   2420 O O   A ASN A  1 205 ? -4.45690  26.93783 2.63010   0.600 22.76769  ?  205 ASN A O   1 
ATOM   2421 O O   B ASN A  1 205 ? -4.47028  26.20107 2.99311   0.400 20.98930  ?  205 ASN A O   1 
ATOM   2422 C CB  A ASN A  1 205 ? -3.08588  26.33262 -0.23488  0.600 23.07206  ?  205 ASN A CB  1 
ATOM   2423 C CB  B ASN A  1 205 ? -3.54140  26.47581 -0.23657  0.400 23.89028  ?  205 ASN A CB  1 
ATOM   2424 C CG  A ASN A  1 205 ? -2.07624  25.54336 -1.05341  0.600 26.86738  ?  205 ASN A CG  1 
ATOM   2425 C CG  B ASN A  1 205 ? -2.41335  26.11773 -1.16636  0.400 21.95549  ?  205 ASN A CG  1 
ATOM   2426 O OD1 A ASN A  1 205 ? -2.27885  25.27747 -2.23927  0.600 32.20380  ?  205 ASN A OD1 1 
ATOM   2427 O OD1 B ASN A  1 205 ? -1.58430  25.26235 -0.85663  0.400 27.21338  ?  205 ASN A OD1 1 
ATOM   2428 N ND2 A ASN A  1 205 ? -0.98456  25.13952 -0.40722  0.600 29.30764  ?  205 ASN A ND2 1 
ATOM   2429 N ND2 B ASN A  1 205 ? -2.37985  26.75129 -2.31869  0.400 15.68838  ?  205 ASN A ND2 1 
ATOM   2430 N N   . ILE A  1 206 ? -6.07071  25.96048 1.41847   1.000 23.37078  ?  206 ILE A N   1 
ATOM   2431 C CA  . ILE A  1 206 ? -7.11004  26.49698 2.30648   1.000 22.98393  ?  206 ILE A CA  1 
ATOM   2432 C C   . ILE A  1 206 ? -7.14312  25.71514 3.61045   1.000 25.60663  ?  206 ILE A C   1 
ATOM   2433 O O   . ILE A  1 206 ? -7.32296  26.28917 4.69188   1.000 25.12315  ?  206 ILE A O   1 
ATOM   2434 C CB  . ILE A  1 206 ? -8.47825  26.52350 1.60082   1.000 29.60987  ?  206 ILE A CB  1 
ATOM   2435 C CG1 . ILE A  1 206 ? -8.54156  27.71342 0.65429   1.000 34.26188  ?  206 ILE A CG1 1 
ATOM   2436 C CG2 . ILE A  1 206 ? -9.66090  26.50679 2.62205   1.000 27.45741  ?  206 ILE A CG2 1 
ATOM   2437 C CD1 . ILE A  1 206 ? -9.82009  27.80416 -0.13559  1.000 38.02213  ?  206 ILE A CD1 1 
ATOM   2438 N N   A TYR A  1 207 ? -6.88732  24.40544 3.53925   0.600 28.23454  ?  207 TYR A N   1 
ATOM   2439 N N   B TYR A  1 207 ? -7.00708  24.38323 3.53190   0.400 27.87059  ?  207 TYR A N   1 
ATOM   2440 C CA  A TYR A  1 207 ? -6.77739  23.59306 4.74780   0.600 28.07071  ?  207 TYR A CA  1 
ATOM   2441 C CA  B TYR A  1 207 ? -6.94523  23.57452 4.74838   0.400 27.95873  ?  207 TYR A CA  1 
ATOM   2442 C C   A TYR A  1 207 ? -5.69016  24.11966 5.67721   0.600 26.88209  ?  207 TYR A C   1 
ATOM   2443 C C   B TYR A  1 207 ? -5.78183  24.00018 5.63556   0.400 26.19632  ?  207 TYR A C   1 
ATOM   2444 O O   A TYR A  1 207 ? -5.94097  24.37397 6.86289   0.600 28.24297  ?  207 TYR A O   1 
ATOM   2445 O O   B TYR A  1 207 ? -5.84902  23.86177 6.86282   0.400 28.66234  ?  207 TYR A O   1 
ATOM   2446 C CB  A TYR A  1 207 ? -6.48966  22.13398 4.38379   0.600 31.81934  ?  207 TYR A CB  1 
ATOM   2447 C CB  B TYR A  1 207 ? -6.84352  22.07825 4.40679   0.400 35.17613  ?  207 TYR A CB  1 
ATOM   2448 C CG  A TYR A  1 207 ? -6.73797  21.19280 5.54122   0.600 30.39266  ?  207 TYR A CG  1 
ATOM   2449 C CG  B TYR A  1 207 ? -7.41352  21.14627 5.48120   0.400 41.42464  ?  207 TYR A CG  1 
ATOM   2450 C CD1 A TYR A  1 207 ? -8.03895  20.84807 5.89826   0.600 42.74688  ?  207 TYR A CD1 1 
ATOM   2451 C CD1 B TYR A  1 207 ? -6.89167  21.13147 6.77242   0.400 42.06761  ?  207 TYR A CD1 1 
ATOM   2452 C CD2 A TYR A  1 207 ? -5.69269  20.67907 6.29625   0.600 30.02696  ?  207 TYR A CD2 1 
ATOM   2453 C CD2 B TYR A  1 207 ? -8.46196  20.26898 5.19460   0.400 40.85956  ?  207 TYR A CD2 1 
ATOM   2454 C CE1 A TYR A  1 207 ? -8.29129  19.99595 6.95456   0.600 42.65812  ?  207 TYR A CE1 1 
ATOM   2455 C CE1 B TYR A  1 207 ? -7.40486  20.29382 7.75271   0.400 36.84645  ?  207 TYR A CE1 1 
ATOM   2456 C CE2 A TYR A  1 207 ? -5.93616  19.81559 7.35490   0.600 31.06014  ?  207 TYR A CE2 1 
ATOM   2457 C CE2 B TYR A  1 207 ? -8.98320  19.41570 6.17645   0.400 30.34511  ?  207 TYR A CE2 1 
ATOM   2458 C CZ  A TYR A  1 207 ? -7.23957  19.48081 7.67954   0.600 30.03339  ?  207 TYR A CZ  1 
ATOM   2459 C CZ  B TYR A  1 207 ? -8.44687  19.43613 7.45158   0.400 34.95702  ?  207 TYR A CZ  1 
ATOM   2460 O OH  A TYR A  1 207 ? -7.50055  18.64097 8.74244   0.600 38.06670  ?  207 TYR A OH  1 
ATOM   2461 O OH  B TYR A  1 207 ? -8.94896  18.60844 8.43512   0.400 27.74017  ?  207 TYR A OH  1 
ATOM   2462 N N   A SER A  1 208 ? -4.46919  24.28973 5.15564   0.600 26.01940  ?  208 SER A N   1 
ATOM   2463 N N   B SER A  1 208 ? -4.71526  24.53583 5.04031   0.400 28.47725  ?  208 SER A N   1 
ATOM   2464 C CA  A SER A  1 208 ? -3.36145  24.76031 5.98200   0.600 29.25348  ?  208 SER A CA  1 
ATOM   2465 C CA  B SER A  1 208 ? -3.58144  24.99170 5.83441   0.400 28.35162  ?  208 SER A CA  1 
ATOM   2466 C C   A SER A  1 208 ? -3.70163  26.06577 6.68526   0.600 33.35967  ?  208 SER A C   1 
ATOM   2467 C C   B SER A  1 208 ? -3.80761  26.39231 6.40519   0.400 32.36915  ?  208 SER A C   1 
ATOM   2468 O O   A SER A  1 208 ? -3.49759  26.19842 7.89563   0.600 26.03416  ?  208 SER A O   1 
ATOM   2469 O O   B SER A  1 208 ? -3.36397  26.68808 7.51954   0.400 28.22045  ?  208 SER A O   1 
ATOM   2470 C CB  A SER A  1 208 ? -2.10220  24.94014 5.13845   0.600 32.25455  ?  208 SER A CB  1 
ATOM   2471 C CB  B SER A  1 208 ? -2.28821  24.90252 5.01800   0.400 32.37816  ?  208 SER A CB  1 
ATOM   2472 O OG  A SER A  1 208 ? -1.60895  23.72171 4.63232   0.600 24.63798  ?  208 SER A OG  1 
ATOM   2473 O OG  B SER A  1 208 ? -1.99932  26.13569 4.37579   0.400 45.71435  ?  208 SER A OG  1 
ATOM   2474 N N   A ILE A  1 209 ? -4.22565  27.04117 5.93877   0.600 26.11396  ?  209 ILE A N   1 
ATOM   2475 N N   B ILE A  1 209 ? -4.49259  27.26781 5.66367   0.400 24.74866  ?  209 ILE A N   1 
ATOM   2476 C CA  A ILE A  1 209 ? -4.58961  28.32397 6.53375   0.600 24.65139  ?  209 ILE A CA  1 
ATOM   2477 C CA  B ILE A  1 209 ? -4.92131  28.54657 6.23015   0.400 28.33327  ?  209 ILE A CA  1 
ATOM   2478 C C   A ILE A  1 209 ? -5.64549  28.13117 7.61660   0.600 25.75573  ?  209 ILE A C   1 
ATOM   2479 C C   B ILE A  1 209 ? -5.80508  28.30680 7.44021   0.400 25.45703  ?  209 ILE A C   1 
ATOM   2480 O O   A ILE A  1 209 ? -5.55171  28.71545 8.70257   0.600 23.01848  ?  209 ILE A O   1 
ATOM   2481 O O   B ILE A  1 209 ? -5.73843  29.02747 8.44035   0.400 24.69412  ?  209 ILE A O   1 
ATOM   2482 C CB  A ILE A  1 209 ? -5.04213  29.30687 5.43840   0.600 34.45952  ?  209 ILE A CB  1 
ATOM   2483 C CB  B ILE A  1 209 ? -5.68276  29.36807 5.17418   0.400 20.23704  ?  209 ILE A CB  1 
ATOM   2484 C CG1 A ILE A  1 209 ? -3.86368  29.62991 4.50862   0.600 27.91323  ?  209 ILE A CG1 1 
ATOM   2485 C CG1 B ILE A  1 209 ? -4.77879  29.72282 3.99720   0.400 31.48812  ?  209 ILE A CG1 1 
ATOM   2486 C CG2 A ILE A  1 209 ? -5.63152  30.56327 6.06364   0.600 27.61837  ?  209 ILE A CG2 1 
ATOM   2487 C CG2 B ILE A  1 209 ? -6.25510  30.60939 5.80674   0.400 28.47568  ?  209 ILE A CG2 1 
ATOM   2488 C CD1 A ILE A  1 209 ? -4.27842  30.11868 3.14186   0.600 41.29799  ?  209 ILE A CD1 1 
ATOM   2489 C CD1 B ILE A  1 209 ? -5.53510  30.33895 2.82874   0.400 23.72231  ?  209 ILE A CD1 1 
ATOM   2490 N N   . PHE A  1 210 ? -6.64320  27.27791 7.35131   1.000 24.37173  ?  210 PHE A N   1 
ATOM   2491 C CA  . PHE A  1 210 ? -7.63769  26.97310 8.37046   1.000 28.36886  ?  210 PHE A CA  1 
ATOM   2492 C C   . PHE A  1 210 ? -6.96773  26.50757 9.65900   1.000 27.27282  ?  210 PHE A C   1 
ATOM   2493 O O   . PHE A  1 210 ? -7.21781  27.05473 10.74377  1.000 24.76443  ?  210 PHE A O   1 
ATOM   2494 C CB  . PHE A  1 210 ? -8.57085  25.89355 7.79728   1.000 23.84490  ?  210 PHE A CB  1 
ATOM   2495 C CG  . PHE A  1 210 ? -9.45430  25.23632 8.82632   1.000 23.64904  ?  210 PHE A CG  1 
ATOM   2496 C CD1 . PHE A  1 210 ? -10.47646 25.95905 9.45908   1.000 26.91721  ?  210 PHE A CD1 1 
ATOM   2497 C CD2 . PHE A  1 210 ? -9.26825  23.89849 9.17039   1.000 29.15148  ?  210 PHE A CD2 1 
ATOM   2498 C CE1 . PHE A  1 210 ? -11.27365 25.36182 10.43129  1.000 31.73263  ?  210 PHE A CE1 1 
ATOM   2499 C CE2 . PHE A  1 210 ? -10.07694 23.29667 10.14274  1.000 26.49491  ?  210 PHE A CE2 1 
ATOM   2500 C CZ  . PHE A  1 210 ? -11.08370 24.03597 10.76180  1.000 28.56498  ?  210 PHE A CZ  1 
ATOM   2501 N N   . ILE A  1 211 ? -6.10824  25.48815 9.55934   1.000 24.59587  ?  211 ILE A N   1 
ATOM   2502 C CA  . ILE A  1 211 ? -5.35912  25.00156 10.71216  1.000 21.09728  ?  211 ILE A CA  1 
ATOM   2503 C C   . ILE A  1 211 ? -4.56426  26.13072 11.34868  1.000 20.69489  ?  211 ILE A C   1 
ATOM   2504 O O   . ILE A  1 211 ? -4.48613  26.23318 12.57359  1.000 22.68330  ?  211 ILE A O   1 
ATOM   2505 C CB  . ILE A  1 211 ? -4.43916  23.83991 10.29357  1.000 24.18520  ?  211 ILE A CB  1 
ATOM   2506 C CG1 . ILE A  1 211 ? -5.25850  22.62004 9.83107   1.000 29.02802  ?  211 ILE A CG1 1 
ATOM   2507 C CG2 . ILE A  1 211 ? -3.51124  23.48525 11.41040  1.000 25.11741  ?  211 ILE A CG2 1 
ATOM   2508 C CD1 . ILE A  1 211 ? -6.16013  22.02931 10.93174  1.000 26.54477  ?  211 ILE A CD1 1 
ATOM   2509 N N   . PHE A  1 212 ? -3.94309  26.98987 10.52137  1.000 23.18524  ?  212 PHE A N   1 
ATOM   2510 C CA  . PHE A  1 212 ? -3.19789  28.11263 11.08331  1.000 26.32452  ?  212 PHE A CA  1 
ATOM   2511 C C   . PHE A  1 212 ? -4.10530  29.00946 11.91431  1.000 24.73862  ?  212 PHE A C   1 
ATOM   2512 O O   . PHE A  1 212 ? -3.75536  29.41697 13.02392  1.000 25.86865  ?  212 PHE A O   1 
ATOM   2513 C CB  . PHE A  1 212 ? -2.52640  28.93685 9.98155   1.000 28.79791  ?  212 PHE A CB  1 
ATOM   2514 C CG  . PHE A  1 212 ? -1.89894  30.19115 10.50802  1.000 25.62397  ?  212 PHE A CG  1 
ATOM   2515 C CD1 . PHE A  1 212 ? -0.60924  30.16884 11.03933  1.000 27.00935  ?  212 PHE A CD1 1 
ATOM   2516 C CD2 . PHE A  1 212 ? -2.59663  31.38601 10.52383  1.000 30.06367  ?  212 PHE A CD2 1 
ATOM   2517 C CE1 . PHE A  1 212 ? -0.02367  31.32390 11.55390  1.000 27.49608  ?  212 PHE A CE1 1 
ATOM   2518 C CE2 . PHE A  1 212 ? -2.02255  32.54248 11.01666  1.000 34.63776  ?  212 PHE A CE2 1 
ATOM   2519 C CZ  . PHE A  1 212 ? -0.73586  32.51851 11.54257  1.000 30.50703  ?  212 PHE A CZ  1 
ATOM   2520 N N   . ILE A  1 213 ? -5.28408  29.33069 11.38038  1.000 23.11842  ?  213 ILE A N   1 
ATOM   2521 C CA  . ILE A  1 213 ? -6.20609  30.19390 12.11403  1.000 27.53679  ?  213 ILE A CA  1 
ATOM   2522 C C   . ILE A  1 213 ? -6.68031  29.51422 13.39785  1.000 25.02823  ?  213 ILE A C   1 
ATOM   2523 O O   . ILE A  1 213 ? -6.78215  30.14581 14.46023  1.000 25.07107  ?  213 ILE A O   1 
ATOM   2524 C CB  . ILE A  1 213 ? -7.36384  30.62668 11.19580  1.000 27.36383  ?  213 ILE A CB  1 
ATOM   2525 C CG1 . ILE A  1 213 ? -6.83400  31.54479 10.09250  1.000 27.58989  ?  213 ILE A CG1 1 
ATOM   2526 C CG2 . ILE A  1 213 ? -8.46193  31.35822 12.01253  1.000 28.40538  ?  213 ILE A CG2 1 
ATOM   2527 C CD1 . ILE A  1 213 ? -7.84429  31.83793 8.99073   1.000 31.04971  ?  213 ILE A CD1 1 
ATOM   2528 N N   . VAL A  1 214 ? -6.96572  28.20910 13.32738  1.000 25.32658  ?  214 VAL A N   1 
ATOM   2529 C CA  . VAL A  1 214 ? -7.30707  27.48790 14.55381  1.000 27.37839  ?  214 VAL A CA  1 
ATOM   2530 C C   . VAL A  1 214 ? -6.18757  27.59182 15.58992  1.000 28.60443  ?  214 VAL A C   1 
ATOM   2531 O O   . VAL A  1 214 ? -6.43241  27.87721 16.76610  1.000 25.97367  ?  214 VAL A O   1 
ATOM   2532 C CB  . VAL A  1 214 ? -7.70891  26.03248 14.26450  1.000 26.20188  ?  214 VAL A CB  1 
ATOM   2533 C CG1 . VAL A  1 214 ? -7.93166  25.30369 15.59908  1.000 24.08573  ?  214 VAL A CG1 1 
ATOM   2534 C CG2 . VAL A  1 214 ? -8.99042  25.99305 13.38655  1.000 25.25754  ?  214 VAL A CG2 1 
ATOM   2535 N N   . ILE A  1 215 ? -4.93891  27.39843 15.17080  1.000 21.21800  ?  215 ILE A N   1 
ATOM   2536 C CA  . ILE A  1 215 ? -3.83561  27.49721 16.11281  1.000 23.08479  ?  215 ILE A CA  1 
ATOM   2537 C C   . ILE A  1 215 ? -3.77504  28.89240 16.71374  1.000 22.06070  ?  215 ILE A C   1 
ATOM   2538 O O   . ILE A  1 215 ? -3.67432  29.06047 17.92836  1.000 24.66056  ?  215 ILE A O   1 
ATOM   2539 C CB  . ILE A  1 215 ? -2.52001  27.12270 15.41356  1.000 30.56370  ?  215 ILE A CB  1 
ATOM   2540 C CG1 . ILE A  1 215 ? -2.48346  25.62420 15.16575  1.000 26.29872  ?  215 ILE A CG1 1 
ATOM   2541 C CG2 . ILE A  1 215 ? -1.34295  27.55557 16.28196  1.000 25.50419  ?  215 ILE A CG2 1 
ATOM   2542 C CD1 . ILE A  1 215 ? -1.30668  25.17814 14.32193  1.000 29.38660  ?  215 ILE A CD1 1 
ATOM   2543 N N   A LEU A  1 216 ? -3.81149  29.91371 15.85666  0.600 25.45638  ?  216 LEU A N   1 
ATOM   2544 N N   B LEU A  1 216 ? -3.82260  29.91574 15.85841  0.400 25.64556  ?  216 LEU A N   1 
ATOM   2545 C CA  A LEU A  1 216 ? -3.72564  31.28305 16.35036  0.600 25.54008  ?  216 LEU A CA  1 
ATOM   2546 C CA  B LEU A  1 216 ? -3.72497  31.28620 16.34832  0.400 25.65303  ?  216 LEU A CA  1 
ATOM   2547 C C   A LEU A  1 216 ? -4.86131  31.58450 17.31376  0.600 26.81232  ?  216 LEU A C   1 
ATOM   2548 C C   B LEU A  1 216 ? -4.86720  31.60904 17.29859  0.400 26.87215  ?  216 LEU A C   1 
ATOM   2549 O O   A LEU A  1 216 ? -4.64335  32.17240 18.37971  0.600 31.90890  ?  216 LEU A O   1 
ATOM   2550 O O   B LEU A  1 216 ? -4.66102  32.24423 18.33883  0.400 31.94528  ?  216 LEU A O   1 
ATOM   2551 C CB  A LEU A  1 216 ? -3.75054  32.24606 15.16298  0.600 26.22177  ?  216 LEU A CB  1 
ATOM   2552 C CB  B LEU A  1 216 ? -3.72809  32.24966 15.16395  0.400 26.27060  ?  216 LEU A CB  1 
ATOM   2553 C CG  A LEU A  1 216 ? -2.67335  33.33114 15.15847  0.600 41.37551  ?  216 LEU A CG  1 
ATOM   2554 C CG  B LEU A  1 216 ? -3.42631  33.69900 15.53490  0.400 28.81588  ?  216 LEU A CG  1 
ATOM   2555 C CD1 A LEU A  1 216 ? -3.08476  34.46513 14.22586  0.600 40.80653  ?  216 LEU A CD1 1 
ATOM   2556 C CD1 B LEU A  1 216 ? -2.04153  33.78160 16.15196  0.400 39.53888  ?  216 LEU A CD1 1 
ATOM   2557 C CD2 A LEU A  1 216 ? -2.38455  33.83361 16.57881  0.600 39.77485  ?  216 LEU A CD2 1 
ATOM   2558 C CD2 B LEU A  1 216 ? -3.52932  34.57840 14.29849  0.400 38.93769  ?  216 LEU A CD2 1 
ATOM   2559 N N   . ASN A  1 217 ? -6.08264  31.16997 16.95755  1.000 28.62531  ?  217 ASN A N   1 
ATOM   2560 C CA  . ASN A  1 217 ? -7.23755  31.43401 17.81527  1.000 31.23943  ?  217 ASN A CA  1 
ATOM   2561 C C   . ASN A  1 217 ? -7.10357  30.72443 19.15789  1.000 28.66333  ?  217 ASN A C   1 
ATOM   2562 O O   . ASN A  1 217 ? -7.38784  31.30555 20.21135  1.000 33.07697  ?  217 ASN A O   1 
ATOM   2563 C CB  . ASN A  1 217 ? -8.51196  31.00258 17.07544  1.000 30.65888  ?  217 ASN A CB  1 
ATOM   2564 C CG  . ASN A  1 217 ? -9.76335  31.11259 17.93526  1.000 47.93224  ?  217 ASN A CG  1 
ATOM   2565 O OD1 . ASN A  1 217 ? -10.19178 32.20715 18.29442  1.000 52.39681  ?  217 ASN A OD1 1 
ATOM   2566 N ND2 . ASN A  1 217 ? -10.36290 29.97419 18.25240  1.000 42.69427  ?  217 ASN A ND2 1 
ATOM   2567 N N   . GLN A  1 218 ? -6.60926  29.48834 19.14632  1.000 27.54446  ?  218 GLN A N   1 
ATOM   2568 C CA  . GLN A  1 218 ? -6.49507  28.74828 20.39548  1.000 32.81101  ?  218 GLN A CA  1 
ATOM   2569 C C   . GLN A  1 218 ? -5.39094  29.30242 21.28061  1.000 36.86979  ?  218 GLN A C   1 
ATOM   2570 O O   . GLN A  1 218 ? -5.50096  29.26004 22.51102  1.000 35.72115  ?  218 GLN A O   1 
ATOM   2571 C CB  . GLN A  1 218 ? -6.24383  27.25784 20.12443  1.000 33.12561  ?  218 GLN A CB  1 
ATOM   2572 C CG  . GLN A  1 218 ? -7.42965  26.54268 19.51320  1.000 30.77385  ?  218 GLN A CG  1 
ATOM   2573 C CD  . GLN A  1 218 ? -8.65466  26.59399 20.40176  1.000 37.50366  ?  218 GLN A CD  1 
ATOM   2574 O OE1 . GLN A  1 218 ? -8.58714  26.25586 21.58188  1.000 47.48440  ?  218 GLN A OE1 1 
ATOM   2575 N NE2 . GLN A  1 218 ? -9.77731  27.02586 19.84404  1.000 56.21304  ?  218 GLN A NE2 1 
ATOM   2576 N N   . SER A  1 219 ? -4.33172  29.83386 20.68246  1.000 32.61979  ?  219 SER A N   1 
ATOM   2577 C CA  . SER A  1 219 ? -3.11262  30.09608 21.41588  1.000 31.99351  ?  219 SER A CA  1 
ATOM   2578 C C   . SER A  1 219 ? -2.83945  31.57120 21.58610  1.000 34.85994  ?  219 SER A C   1 
ATOM   2579 O O   . SER A  1 219 ? -1.78686  31.92313 22.12820  1.000 40.35055  ?  219 SER A O   1 
ATOM   2580 C CB  . SER A  1 219 ? -1.91987  29.44718 20.71280  1.000 30.40839  ?  219 SER A CB  1 
ATOM   2581 O OG  . SER A  1 219 ? -2.21069  28.11538 20.31608  1.000 39.73923  ?  219 SER A OG  1 
ATOM   2582 N N   . TYR A  1 220 ? -3.74389  32.43705 21.12080  1.000 34.48419  ?  220 TYR A N   1 
ATOM   2583 C CA  . TYR A  1 220 ? -3.43726  33.86154 21.06528  1.000 44.05819  ?  220 TYR A CA  1 
ATOM   2584 C C   . TYR A  1 220 ? -3.04146  34.40748 22.43278  1.000 56.62261  ?  220 TYR A C   1 
ATOM   2585 O O   . TYR A  1 220 ? -2.07625  35.17630 22.54232  1.000 43.29872  ?  220 TYR A O   1 
ATOM   2586 C CB  . TYR A  1 220 ? -4.61767  34.63564 20.48837  1.000 38.79670  ?  220 TYR A CB  1 
ATOM   2587 C CG  . TYR A  1 220 ? -4.32573  36.11365 20.39043  1.000 64.20953  ?  220 TYR A CG  1 
ATOM   2588 C CD1 . TYR A  1 220 ? -3.52863  36.61885 19.36458  1.000 60.42476  ?  220 TYR A CD1 1 
ATOM   2589 C CD2 . TYR A  1 220 ? -4.83076  37.00832 21.33180  1.000 58.31614  ?  220 TYR A CD2 1 
ATOM   2590 C CE1 . TYR A  1 220 ? -3.25030  37.98273 19.27464  1.000 74.21711  ?  220 TYR A CE1 1 
ATOM   2591 C CE2 . TYR A  1 220 ? -4.55888  38.37536 21.25045  1.000 78.71774  ?  220 TYR A CE2 1 
ATOM   2592 C CZ  . TYR A  1 220 ? -3.76893  38.85529 20.21894  1.000 84.79504  ?  220 TYR A CZ  1 
ATOM   2593 O OH  . TYR A  1 220 ? -3.49816  40.20688 20.13016  1.000 95.08611  ?  220 TYR A OH  1 
ATOM   2594 N N   . LYS A  1 221 ? -3.76642  34.01389 23.48944  1.000 42.61109  ?  221 LYS A N   1 
ATOM   2595 C CA  . LYS A  1 221 ? -3.43208  34.48120 24.83257  1.000 42.16760  ?  221 LYS A CA  1 
ATOM   2596 C C   . LYS A  1 221 ? -2.06081  33.97013 25.26370  1.000 58.12203  ?  221 LYS A C   1 
ATOM   2597 O O   . LYS A  1 221 ? -1.24406  34.72099 25.81560  1.000 53.11861  ?  221 LYS A O   1 
ATOM   2598 C CB  . LYS A  1 221 ? -4.50937  34.04167 25.82984  1.000 48.19251  ?  221 LYS A CB  1 
ATOM   2599 C CG  . LYS A  1 221 ? -5.84579  34.75901 25.68527  1.000 51.23295  ?  221 LYS A CG  1 
ATOM   2600 N N   . LEU A  1 222 ? -1.80181  32.68061 25.03665  1.000 48.32881  ?  222 LEU A N   1 
ATOM   2601 C CA  . LEU A  1 222 ? -0.49401  32.11733 25.35125  1.000 58.50967  ?  222 LEU A CA  1 
ATOM   2602 C C   . LEU A  1 222 ? 0.59353   32.82536 24.55595  1.000 58.65429  ?  222 LEU A C   1 
ATOM   2603 O O   . LEU A  1 222 ? 1.66831   33.13210 25.08673  1.000 61.38560  ?  222 LEU A O   1 
ATOM   2604 C CB  . LEU A  1 222 ? -0.50483  30.61237 25.05368  1.000 44.17534  ?  222 LEU A CB  1 
ATOM   2605 C CG  . LEU A  1 222 ? 0.53988   29.70874 25.71186  1.000 65.40542  ?  222 LEU A CG  1 
ATOM   2606 C CD1 . LEU A  1 222 ? 0.40814   29.76243 27.22345  1.000 55.01815  ?  222 LEU A CD1 1 
ATOM   2607 C CD2 . LEU A  1 222 ? 0.39749   28.27423 25.20586  1.000 55.57531  ?  222 LEU A CD2 1 
ATOM   2608 N N   . LEU A  1 223 ? 0.30735   33.13055 23.28923  1.000 60.92755  ?  223 LEU A N   1 
ATOM   2609 C CA  . LEU A  1 223 ? 1.27636   33.78860 22.41843  1.000 61.40235  ?  223 LEU A CA  1 
ATOM   2610 C C   . LEU A  1 223 ? 1.58816   35.19941 22.90120  1.000 73.26743  ?  223 LEU A C   1 
ATOM   2611 O O   . LEU A  1 223 ? 2.75936   35.58182 23.01444  1.000 103.06850 ?  223 LEU A O   1 
ATOM   2612 C CB  . LEU A  1 223 ? 0.72928   33.81958 20.98898  1.000 53.21931  ?  223 LEU A CB  1 
ATOM   2613 C CG  . LEU A  1 223 ? 1.54628   34.49554 19.89065  1.000 62.20362  ?  223 LEU A CG  1 
ATOM   2614 C CD1 . LEU A  1 223 ? 2.85593   33.74812 19.62830  1.000 49.22445  ?  223 LEU A CD1 1 
ATOM   2615 C CD2 . LEU A  1 223 ? 0.71004   34.57321 18.62745  1.000 53.07622  ?  223 LEU A CD2 1 
ATOM   2616 N N   . LEU A  1 224 ? 0.55390   35.98992 23.18322  1.000 81.34396  ?  224 LEU A N   1 
ATOM   2617 C CA  . LEU A  1 224 ? 0.75367   37.37847 23.57900  1.000 81.21106  ?  224 LEU A CA  1 
ATOM   2618 C C   . LEU A  1 224 ? 1.39651   37.45457 24.96253  1.000 86.76708  ?  224 LEU A C   1 
ATOM   2619 O O   . LEU A  1 224 ? 0.93410   36.81661 25.91520  1.000 86.90171  ?  224 LEU A O   1 
ATOM   2620 C CB  . LEU A  1 224 ? -0.58073  38.12071 23.56090  1.000 65.46070  ?  224 LEU A CB  1 
ATOM   2621 C CG  . LEU A  1 224 ? -0.59892  39.38994 22.70545  1.000 87.70137  ?  224 LEU A CG  1 
ATOM   2622 C CD1 . LEU A  1 224 ? -0.31268  39.07398 21.23640  1.000 62.68887  ?  224 LEU A CD1 1 
ATOM   2623 C CD2 . LEU A  1 224 ? -1.92605  40.12399 22.86882  1.000 91.01547  ?  224 LEU A CD2 1 
ATOM   2624 N N   . GLU A  1 225 ? 2.47386   38.22982 25.06568  1.000 92.86568  ?  225 GLU A N   1 
ATOM   2625 C CA  . GLU A  1 225 ? 3.22382   38.35046 26.31242  1.000 93.61472  ?  225 GLU A CA  1 
ATOM   2626 C C   . GLU A  1 225 ? 4.01777   39.65354 26.34423  1.000 75.62790  ?  225 GLU A C   1 
ATOM   2627 O O   . GLU A  1 225 ? 4.13663   40.33955 25.32958  1.000 79.88323  ?  225 GLU A O   1 
ATOM   2628 C CB  . GLU A  1 225 ? 4.16347   37.15278 26.48853  1.000 83.46557  ?  225 GLU A CB  1 
HETATM 2629 C C1  A RET B  2 .   ? -10.01743 10.54504 -10.03475 0.600 25.52013  ?  301 RET A C1  1 
HETATM 2630 C C1  B RET B  2 .   ? -9.96742  10.57013 -10.11811 0.400 25.45563  ?  301 RET A C1  1 
HETATM 2631 C C2  A RET B  2 .   ? -10.62479 9.58496  -11.06378 0.600 25.44267  ?  301 RET A C2  1 
HETATM 2632 C C2  B RET B  2 .   ? -10.65246 9.82273  -11.26143 0.400 24.55744  ?  301 RET A C2  1 
HETATM 2633 C C3  A RET B  2 .   ? -12.07364 9.92452  -11.38136 0.600 24.05161  ?  301 RET A C3  1 
HETATM 2634 C C3  B RET B  2 .   ? -11.58349 8.72540  -10.77061 0.400 25.67069  ?  301 RET A C3  1 
HETATM 2635 C C4  A RET B  2 .   ? -12.93309 9.85951  -10.13367 0.600 25.43491  ?  301 RET A C4  1 
HETATM 2636 C C4  B RET B  2 .   ? -12.64620 9.26841  -9.83281  0.400 26.09427  ?  301 RET A C4  1 
HETATM 2637 C C5  A RET B  2 .   ? -12.27515 10.45478 -8.90182  0.600 22.71418  ?  301 RET A C5  1 
HETATM 2638 C C5  B RET B  2 .   ? -12.13440 10.29032 -8.84928  0.400 22.63558  ?  301 RET A C5  1 
HETATM 2639 C C6  A RET B  2 .   ? -10.94973 10.68642 -8.82164  0.600 24.57558  ?  301 RET A C6  1 
HETATM 2640 C C6  B RET B  2 .   ? -10.98516 10.96467 -9.03944  0.400 25.21773  ?  301 RET A C6  1 
HETATM 2641 C C7  A RET B  2 .   ? -10.40744 11.34585 -7.64473  0.600 19.94058  ?  301 RET A C7  1 
HETATM 2642 C C7  B RET B  2 .   ? -10.55401 11.94542 -8.06133  0.400 21.22034  ?  301 RET A C7  1 
HETATM 2643 C C8  A RET B  2 .   ? -9.38847  12.21558 -7.44748  0.600 20.74482  ?  301 RET A C8  1 
HETATM 2644 C C8  B RET B  2 .   ? -9.43836  11.98182 -7.35675  0.400 21.44771  ?  301 RET A C8  1 
HETATM 2645 C C9  A RET B  2 .   ? -9.02515  12.78067 -6.15840  0.600 20.76637  ?  301 RET A C9  1 
HETATM 2646 C C9  B RET B  2 .   ? -9.11256  12.96752 -6.36308  0.400 22.53113  ?  301 RET A C9  1 
HETATM 2647 C C10 A RET B  2 .   ? -7.84012  13.44299 -6.03378  0.600 23.40071  ?  301 RET A C10 1 
HETATM 2648 C C10 B RET B  2 .   ? -7.94279  13.64608 -6.44022  0.400 20.18335  ?  301 RET A C10 1 
HETATM 2649 C C11 A RET B  2 .   ? -7.30724  14.10402 -4.87401  0.600 18.97647  ?  301 RET A C11 1 
HETATM 2650 C C11 B RET B  2 .   ? -7.47087  14.64373 -5.52612  0.400 19.52958  ?  301 RET A C11 1 
HETATM 2651 C C12 A RET B  2 .   ? -6.34931  15.04697 -4.96054  0.600 21.38121  ?  301 RET A C12 1 
HETATM 2652 C C12 B RET B  2 .   ? -6.23055  15.13505 -5.46322  0.400 20.02942  ?  301 RET A C12 1 
HETATM 2653 C C13 A RET B  2 .   ? -5.75023  15.80919 -3.88767  0.600 20.21029  ?  301 RET A C13 1 
HETATM 2654 C C13 B RET B  2 .   ? -5.77920  16.13453 -4.51855  0.400 16.98448  ?  301 RET A C13 1 
HETATM 2655 C C14 A RET B  2 .   ? -4.54015  16.37917 -4.08977  0.600 23.13142  ?  301 RET A C14 1 
HETATM 2656 C C14 B RET B  2 .   ? -4.57481  16.71770 -4.68616  0.400 17.66574  ?  301 RET A C14 1 
HETATM 2657 C C15 A RET B  2 .   ? -3.78046  17.18191 -3.16788  0.600 21.60029  ?  301 RET A C15 1 
HETATM 2658 C C15 B RET B  2 .   ? -3.96146  17.70472 -3.83764  0.400 20.05109  ?  301 RET A C15 1 
HETATM 2659 C C16 A RET B  2 .   ? -9.79995  11.90103 -10.72436 0.600 24.79450  ?  301 RET A C16 1 
HETATM 2660 C C16 B RET B  2 .   ? -9.27484  11.80323 -10.71370 0.400 20.54416  ?  301 RET A C16 1 
HETATM 2661 C C17 A RET B  2 .   ? -8.65458  9.97525  -9.62164  0.600 24.22766  ?  301 RET A C17 1 
HETATM 2662 C C17 B RET B  2 .   ? -8.90382  9.63076  -9.53254  0.400 23.23091  ?  301 RET A C17 1 
HETATM 2663 C C18 A RET B  2 .   ? -13.26741 10.86927 -7.85129  0.600 22.98149  ?  301 RET A C18 1 
HETATM 2664 C C18 B RET B  2 .   ? -12.88476 10.25977 -7.54578  0.400 25.68862  ?  301 RET A C18 1 
HETATM 2665 C C19 A RET B  2 .   ? -10.02003 12.64163 -5.03689  0.600 21.52791  ?  301 RET A C19 1 
HETATM 2666 C C19 B RET B  2 .   ? -10.11815 13.20690 -5.27138  0.400 22.16497  ?  301 RET A C19 1 
HETATM 2667 C C20 A RET B  2 .   ? -6.54938  15.99778 -2.62780  0.600 23.17698  ?  301 RET A C20 1 
HETATM 2668 C C20 B RET B  2 .   ? -6.69223  16.48052 -3.37377  0.400 24.48500  ?  301 RET A C20 1 
HETATM 2669 O O   A 97N C  3 .   ? -12.57217 21.36964 5.90425   0.600 57.39854  ?  302 97N A O   1 
HETATM 2670 O O1  A 97N C  3 .   ? -11.02166 22.18018 4.54464   0.600 48.72933  ?  302 97N A O1  1 
HETATM 2671 O O2  A 97N C  3 .   ? -9.41614  21.66095 2.19121   0.600 37.31746  ?  302 97N A O2  1 
HETATM 2672 O O3  A 97N C  3 .   ? -10.90530 19.86715 0.82398   0.600 39.76160  ?  302 97N A O3  1 
HETATM 2673 C C12 A 97N C  3 .   ? -12.82282 25.59438 5.94377   0.600 36.19613  ?  302 97N A C12 1 
HETATM 2674 C C13 A 97N C  3 .   ? -12.79368 24.27390 6.70516   0.600 24.80821  ?  302 97N A C13 1 
HETATM 2675 C C14 A 97N C  3 .   ? -11.52970 23.48905 6.39746   0.600 37.05425  ?  302 97N A C14 1 
HETATM 2676 C C15 A 97N C  3 .   ? -11.77853 22.23307 5.62479   0.600 51.18973  ?  302 97N A C15 1 
HETATM 2677 C C16 A 97N C  3 .   ? -11.41033 21.27374 3.52107   0.600 35.37612  ?  302 97N A C16 1 
HETATM 2678 C C17 A 97N C  3 .   ? -10.82256 21.79918 2.22994   0.600 37.43989  ?  302 97N A C17 1 
HETATM 2679 C C18 A 97N C  3 .   ? -11.54347 21.09479 1.09573   0.600 36.22849  ?  302 97N A C18 1 
HETATM 2680 C C2  . LFA D  4 .   ? 2.49212   35.69236 8.40866   1.000 50.84064  ?  303 LFA A C2  1 
HETATM 2681 C C3  . LFA D  4 .   ? 3.06517   35.57283 9.80407   1.000 33.36417  ?  303 LFA A C3  1 
HETATM 2682 C C4  . LFA D  4 .   ? 2.04743   35.33344 10.89132  1.000 51.12058  ?  303 LFA A C4  1 
HETATM 2683 C C5  . LFA D  4 .   ? 2.65160   34.96077 12.21888  1.000 43.97816  ?  303 LFA A C5  1 
HETATM 2684 C C6  . LFA D  4 .   ? 1.70555   35.05205 13.38926  1.000 46.13386  ?  303 LFA A C6  1 
HETATM 2685 C C7  . LFA D  4 .   ? 2.19416   34.30494 14.60345  1.000 41.77806  ?  303 LFA A C7  1 
HETATM 2686 C C8  . LFA D  4 .   ? 3.61621   34.62079 15.00057  1.000 40.88128  ?  303 LFA A C8  1 
HETATM 2687 C C9  . LFA D  4 .   ? 4.30286   33.49319 15.71315  1.000 41.19398  ?  303 LFA A C9  1 
HETATM 2688 C C10 . LFA D  4 .   ? 5.71810   33.78047 16.15414  1.000 37.57619  ?  303 LFA A C10 1 
HETATM 2689 C C11 . LFA D  4 .   ? 6.18504   32.81646 17.20805  1.000 54.23181  ?  303 LFA A C11 1 
HETATM 2690 C C12 . LFA D  4 .   ? 7.46905   33.17133 17.90080  1.000 53.24007  ?  303 LFA A C12 1 
HETATM 2691 C C13 . LFA D  4 .   ? 7.56554   32.62318 19.30600  1.000 45.81187  ?  303 LFA A C13 1 
HETATM 2692 C C14 . LFA D  4 .   ? 6.48848   33.14193 20.23109  1.000 41.49909  ?  303 LFA A C14 1 
HETATM 2693 C C15 . LFA D  4 .   ? 6.67087   32.75859 21.67891  1.000 53.92611  ?  303 LFA A C15 1 
HETATM 2694 C C1  A LFA E  4 .   ? 7.94505   13.93541 -5.26861  0.600 35.18609  ?  304 LFA A C1  1 
HETATM 2695 C C2  A LFA E  4 .   ? 7.18127   14.80593 -6.23371  0.600 42.34859  ?  304 LFA A C2  1 
HETATM 2696 C C3  A LFA E  4 .   ? 6.28122   14.03267 -7.15918  0.600 42.75818  ?  304 LFA A C3  1 
HETATM 2697 C C4  A LFA E  4 .   ? 5.51699   14.88420 -8.13798  0.600 31.41137  ?  304 LFA A C4  1 
HETATM 2698 C C5  A LFA E  4 .   ? 6.38434   15.73036 -9.02547  0.600 44.51923  ?  304 LFA A C5  1 
HETATM 2699 C C6  A LFA E  4 .   ? 7.14872   14.95685 -10.06397 0.600 50.99018  ?  304 LFA A C6  1 
HETATM 2700 C C7  A LFA E  4 .   ? 8.34081   15.68991 -10.62399 0.600 48.34226  ?  304 LFA A C7  1 
HETATM 2701 C C8  A LFA E  4 .   ? 9.20705   14.85731 -11.53436 0.600 45.67946  ?  304 LFA A C8  1 
HETATM 2702 C C1  . LFA F  4 .   ? 12.98688  18.32159 -17.43701 1.000 59.14898  ?  305 LFA A C1  1 
HETATM 2703 C C2  . LFA F  4 .   ? 12.47912  19.28675 -16.38716 1.000 50.59403  ?  305 LFA A C2  1 
HETATM 2704 C C3  . LFA F  4 .   ? 12.64221  18.83027 -14.95891 1.000 45.17116  ?  305 LFA A C3  1 
HETATM 2705 C C4  . LFA F  4 .   ? 12.18895  19.85526 -13.94085 1.000 50.97928  ?  305 LFA A C4  1 
HETATM 2706 C C5  . LFA F  4 .   ? 12.33834  19.42874 -12.49901 1.000 50.93404  ?  305 LFA A C5  1 
HETATM 2707 C C6  . LFA F  4 .   ? 11.98857  20.51354 -11.50859 1.000 47.43332  ?  305 LFA A C6  1 
HETATM 2708 C C7  . LFA F  4 .   ? 12.07907  20.11034 -10.05597 1.000 45.90307  ?  305 LFA A C7  1 
HETATM 2709 C C1  . LFA G  4 .   ? 16.22819  21.96453 -10.57951 1.000 50.99363  ?  306 LFA A C1  1 
HETATM 2710 C C2  . LFA G  4 .   ? 16.51822  21.62204 -12.01969 1.000 52.33382  ?  306 LFA A C2  1 
HETATM 2711 C C3  . LFA G  4 .   ? 15.78101  22.41223 -13.07590 1.000 47.97955  ?  306 LFA A C3  1 
HETATM 2712 C C4  . LFA G  4 .   ? 16.21536  22.00074 -14.46492 1.000 70.92810  ?  306 LFA A C4  1 
HETATM 2713 C C5  . LFA G  4 .   ? 15.40118  22.57081 -15.60473 1.000 59.88593  ?  306 LFA A C5  1 
HETATM 2714 C C6  . LFA G  4 .   ? 15.80042  22.03497 -16.96363 1.000 55.55483  ?  306 LFA A C6  1 
HETATM 2715 C C7  . LFA G  4 .   ? 14.91276  22.47896 -18.10372 1.000 58.95235  ?  306 LFA A C7  1 
HETATM 2716 C C11 . LFA H  4 .   ? -13.92052 -2.06430 6.77152   1.000 58.79097  ?  307 LFA A C11 1 
HETATM 2717 C C12 . LFA H  4 .   ? -12.77197 -2.35867 5.84244   1.000 56.83381  ?  307 LFA A C12 1 
HETATM 2718 C C13 . LFA H  4 .   ? -12.92215 -1.79519 4.45108   1.000 49.56417  ?  307 LFA A C13 1 
HETATM 2719 C C14 . LFA H  4 .   ? -11.65271 -1.85727 3.63567   1.000 65.06298  ?  307 LFA A C14 1 
HETATM 2720 C C15 . LFA H  4 .   ? -11.78132 -1.35621 2.22027   1.000 52.96220  ?  307 LFA A C15 1 
HETATM 2721 C C16 . LFA H  4 .   ? -10.46034 -1.15323 1.50699   1.000 47.85706  ?  307 LFA A C16 1 
HETATM 2722 C C17 . LFA H  4 .   ? -10.51335 -1.43197 0.03018   1.000 37.16140  ?  307 LFA A C17 1 
HETATM 2723 C C18 . LFA H  4 .   ? -10.94222 -2.84167 -0.30270  1.000 53.94888  ?  307 LFA A C18 1 
HETATM 2724 C C19 . LFA H  4 .   ? -11.05996 -3.16943 -1.76867  1.000 56.85468  ?  307 LFA A C19 1 
HETATM 2725 C C2  . LFA I  4 .   ? -1.86936  5.57844  -8.59030  1.000 33.83147  ?  308 LFA A C2  1 
HETATM 2726 C C3  . LFA I  4 .   ? -0.93216  5.88004  -9.72726  1.000 41.28852  ?  308 LFA A C3  1 
HETATM 2727 C C4  . LFA I  4 .   ? 0.45040   6.24933  -9.26472  1.000 44.21715  ?  308 LFA A C4  1 
HETATM 2728 C C1  A LFA J  4 .   ? 5.98759   26.48896 -1.56348  0.600 30.21223  ?  309 LFA A C1  1 
HETATM 2729 C C2  A LFA J  4 .   ? 6.24296   25.32502 -0.63967  0.600 33.54471  ?  309 LFA A C2  1 
HETATM 2730 C C3  . LFA J  4 .   ? 7.34954   25.63007 0.32980   1.000 70.79523  ?  309 LFA A C3  1 
HETATM 2731 C C4  . LFA J  4 .   ? 7.48121   24.72159 1.53049   1.000 47.06512  ?  309 LFA A C4  1 
HETATM 2732 C C5  . LFA J  4 .   ? 8.54206   25.17101 2.51220   1.000 59.81429  ?  309 LFA A C5  1 
HETATM 2733 C C6  . LFA J  4 .   ? 8.65556   24.31477 3.74954   1.000 56.39606  ?  309 LFA A C6  1 
HETATM 2734 C C7  . LFA J  4 .   ? 9.63156   24.83426 4.77813   1.000 61.82663  ?  309 LFA A C7  1 
HETATM 2735 C C4  . LFA K  4 .   ? 9.64527   23.62482 15.64208  1.000 58.17998  ?  310 LFA A C4  1 
HETATM 2736 C C5  . LFA K  4 .   ? 9.07764   22.25579 15.35360  1.000 68.68773  ?  310 LFA A C5  1 
HETATM 2737 C C6  . LFA K  4 .   ? 9.68741   21.58341 14.14813  1.000 76.43881  ?  310 LFA A C6  1 
HETATM 2738 C C7  . LFA K  4 .   ? 9.61560   22.40190 12.88317  1.000 54.59690  ?  310 LFA A C7  1 
HETATM 2739 C C16 . LFA L  4 .   ? -21.02607 3.43008  -3.19680  1.000 55.03403  ?  311 LFA A C16 1 
HETATM 2740 C C17 . LFA L  4 .   ? -20.73894 2.80448  -1.84831  1.000 66.51795  ?  311 LFA A C17 1 
HETATM 2741 C C18 . LFA L  4 .   ? -19.50896 3.34892  -1.15250  1.000 46.00321  ?  311 LFA A C18 1 
HETATM 2742 C C19 . LFA L  4 .   ? -19.24959 2.83126  0.24325   1.000 55.64987  ?  311 LFA A C19 1 
HETATM 2743 C C20 . LFA L  4 .   ? -20.40517 3.00395  1.21122   1.000 51.54389  ?  311 LFA A C20 1 
HETATM 2744 C C13 . LFA M  4 .   ? -10.60450 30.80056 -8.52322  1.000 52.37505  ?  312 LFA A C13 1 
HETATM 2745 C C14 . LFA M  4 .   ? -9.52500  31.17200 -9.52322  1.000 44.55363  ?  312 LFA A C14 1 
HETATM 2746 C C15 . LFA M  4 .   ? -9.91218  31.01177 -10.98337 1.000 49.73723  ?  312 LFA A C15 1 
HETATM 2747 C C16 . LFA M  4 .   ? -8.80430  31.38695 -11.96313 1.000 41.83800  ?  312 LFA A C16 1 
HETATM 2748 C C17 . LFA M  4 .   ? -9.12595  31.19893 -13.42991 1.000 38.38327  ?  312 LFA A C17 1 
HETATM 2749 C C18 . LFA M  4 .   ? -7.99785  31.59811 -14.36171 1.000 47.86176  ?  312 LFA A C18 1 
HETATM 2750 C C19 . LFA M  4 .   ? -8.16097  31.24123 -15.82625 1.000 62.81082  ?  312 LFA A C19 1 
HETATM 2751 C C20 . LFA M  4 .   ? -9.11771  32.13682 -16.57712 1.000 55.75340  ?  312 LFA A C20 1 
HETATM 2752 C C3  . LFA N  4 .   ? -13.80832 28.25666 0.46723   1.000 57.03015  ?  313 LFA A C3  1 
HETATM 2753 C C4  . LFA N  4 .   ? -14.49681 28.34821 -0.86884  1.000 40.98692  ?  313 LFA A C4  1 
HETATM 2754 C C5  . LFA N  4 .   ? -13.57254 28.26275 -2.05938  1.000 51.26782  ?  313 LFA A C5  1 
HETATM 2755 C C6  . LFA N  4 .   ? -14.27369 28.33565 -3.39761  1.000 55.92782  ?  313 LFA A C6  1 
HETATM 2756 C C7  . LFA N  4 .   ? -13.39155 28.05368 -4.59670  1.000 45.72734  ?  313 LFA A C7  1 
HETATM 2757 C C8  . LFA N  4 .   ? -12.19618 28.97105 -4.72927  1.000 57.04928  ?  313 LFA A C8  1 
HETATM 2758 C C3  . LFA O  4 .   ? -12.93366 25.33233 -6.71271  1.000 33.84011  ?  314 LFA A C3  1 
HETATM 2759 C C4  . LFA O  4 .   ? -12.64125 24.77915 -8.08223  1.000 41.38180  ?  314 LFA A C4  1 
HETATM 2760 C C5  . LFA O  4 .   ? -12.74873 25.80235 -9.17800  1.000 34.74634  ?  314 LFA A C5  1 
HETATM 2761 C C6  . LFA O  4 .   ? -12.70831 25.21050 -10.56976 1.000 35.79188  ?  314 LFA A C6  1 
HETATM 2762 C C7  . LFA O  4 .   ? -12.68917 26.22756 -11.67316 1.000 42.05968  ?  314 LFA A C7  1 
HETATM 2763 C C8  . LFA O  4 .   ? -11.33037 26.38353 -12.29794 1.000 53.76136  ?  314 LFA A C8  1 
HETATM 2764 C C9  . LFA O  4 .   ? -11.23520 27.48085 -13.31853 1.000 58.61481  ?  314 LFA A C9  1 
HETATM 2765 C C10 . LFA O  4 .   ? -10.90166 27.01781 -14.70458 1.000 56.44222  ?  314 LFA A C10 1 
HETATM 2766 C C11 . LFA O  4 .   ? -11.88954 26.04288 -15.28054 1.000 40.29264  ?  314 LFA A C11 1 
HETATM 2767 C C12 . LFA O  4 .   ? -11.86882 25.99814 -16.78072 1.000 55.91636  ?  314 LFA A C12 1 
HETATM 2768 C C13 . LFA O  4 .   ? -12.05173 27.35157 -17.42384 1.000 51.86231  ?  314 LFA A C13 1 
HETATM 2769 C C14 . LFA O  4 .   ? -12.16977 27.32438 -18.92379 1.000 52.84711  ?  314 LFA A C14 1 
HETATM 2770 C C9  . LFA P  4 .   ? -26.46437 17.91413 7.23488   1.000 40.71722  ?  315 LFA A C9  1 
HETATM 2771 C C10 . LFA P  4 .   ? -25.80202 18.46177 5.99375   1.000 53.86237  ?  315 LFA A C10 1 
HETATM 2772 C C11 . LFA P  4 .   ? -25.60145 17.45402 4.88304   1.000 44.22578  ?  315 LFA A C11 1 
HETATM 2773 C C12 . LFA P  4 .   ? -25.31625 18.07265 3.52924   1.000 56.82588  ?  315 LFA A C12 1 
HETATM 2774 C C13 . LFA P  4 .   ? -24.72119 17.12027 2.51029   1.000 51.09480  ?  315 LFA A C13 1 
HETATM 2775 C C14 . LFA P  4 .   ? -24.81686 17.57844 1.06704   1.000 65.57179  ?  315 LFA A C14 1 
HETATM 2776 C C15 . LFA P  4 .   ? -24.21687 18.93904 0.76555   1.000 64.22891  ?  315 LFA A C15 1 
HETATM 2777 C C16 . LFA P  4 .   ? -22.70362 19.01387 0.79338   1.000 57.29211  ?  315 LFA A C16 1 
HETATM 2778 C C17 . LFA P  4 .   ? -22.00403 18.59640 -0.48170  1.000 48.72220  ?  315 LFA A C17 1 
HETATM 2779 C C18 . LFA P  4 .   ? -21.77737 17.10849 -0.65286  1.000 55.69531  ?  315 LFA A C18 1 
HETATM 2780 C C19 . LFA P  4 .   ? -20.87924 16.76076 -1.82320  1.000 54.96870  ?  315 LFA A C19 1 
HETATM 2781 C C20 . LFA P  4 .   ? -20.58922 15.28723 -2.02403  1.000 54.71865  ?  315 LFA A C20 1 
HETATM 2782 C C10 . LFA Q  4 .   ? -24.19254 7.83478  8.24019   1.000 66.33659  ?  316 LFA A C10 1 
HETATM 2783 C C11 . LFA Q  4 .   ? -23.95693 8.85436  7.14586   1.000 53.71424  ?  316 LFA A C11 1 
HETATM 2784 C C12 . LFA Q  4 .   ? -22.74154 8.57178  6.29131   1.000 57.86407  ?  316 LFA A C12 1 
HETATM 2785 C C13 . LFA Q  4 .   ? -22.44111 9.61742  5.24262   1.000 49.37194  ?  316 LFA A C13 1 
HETATM 2786 C C14 . LFA Q  4 .   ? -21.24324 9.28194  4.38735   1.000 53.58298  ?  316 LFA A C14 1 
HETATM 2787 C C15 . LFA Q  4 .   ? -20.90419 10.30374 3.32795   1.000 49.81255  ?  316 LFA A C15 1 
HETATM 2788 C C16 . LFA Q  4 .   ? -19.84594 9.82457  2.36891   1.000 49.62365  ?  316 LFA A C16 1 
HETATM 2789 C C17 . LFA Q  4 .   ? -20.21416 8.53133  1.69219   1.000 50.99440  ?  316 LFA A C17 1 
HETATM 2790 C C18 . LFA Q  4 .   ? -21.40168 8.65612  0.76653   1.000 66.26014  ?  316 LFA A C18 1 
HETATM 2791 C C19 . LFA Q  4 .   ? -22.22961 7.41074  0.58011   1.000 56.14997  ?  316 LFA A C19 1 
HETATM 2792 C C20 . LFA Q  4 .   ? -21.44668 6.18098  0.19926   1.000 67.52295  ?  316 LFA A C20 1 
HETATM 2793 C C1  . LFA R  4 .   ? -3.03625  -3.80280 -3.58153  1.000 62.77551  ?  317 LFA A C1  1 
HETATM 2794 C C2  . LFA R  4 .   ? -2.44050  -4.22437 -2.25729  1.000 53.26522  ?  317 LFA A C2  1 
HETATM 2795 C C3  . LFA R  4 .   ? -3.24873  -5.24740 -1.48803  1.000 55.21442  ?  317 LFA A C3  1 
HETATM 2796 C C4  . LFA R  4 .   ? -2.61348  -5.66907 -0.17630  1.000 71.06649  ?  317 LFA A C4  1 
HETATM 2797 C C5  . LFA R  4 .   ? -3.33037  -6.79015 0.54639   1.000 60.52532  ?  317 LFA A C5  1 
HETATM 2798 C C6  . LFA R  4 .   ? -2.68730  -7.21029 1.84733   1.000 43.28865  ?  317 LFA A C6  1 
HETATM 2799 C C17 . LFA S  4 .   ? -1.76961  37.67190 11.82640  1.000 57.57606  ?  318 LFA A C17 1 
HETATM 2800 C C18 . LFA S  4 .   ? -2.64595  36.97619 10.80467  1.000 62.16352  ?  318 LFA A C18 1 
HETATM 2801 C C19 . LFA S  4 .   ? -1.96796  36.50410 9.53595   1.000 50.65579  ?  318 LFA A C19 1 
HETATM 2802 C C20 . LFA S  4 .   ? -2.89381  35.77146 8.58316   1.000 60.30078  ?  318 LFA A C20 1 
HETATM 2803 C C8  . OLC T  5 .   ? -1.30123  3.69735  9.07168   1.000 54.11064  ?  319 OLC A C8  1 
HETATM 2804 C C7  . OLC T  5 .   ? -0.05355  4.39222  9.53901   1.000 66.57100  ?  319 OLC A C7  1 
HETATM 2805 C C6  . OLC T  5 .   ? -0.27722  5.46494  10.60037  1.000 44.72210  ?  319 OLC A C6  1 
HETATM 2806 C C5  . OLC T  5 .   ? 0.99663   6.07695  11.15550  1.000 48.60296  ?  319 OLC A C5  1 
HETATM 2807 C C4  . OLC T  5 .   ? 1.78130   6.93187  10.18289  1.000 55.24312  ?  319 OLC A C4  1 
HETATM 2808 C C3  . OLC T  5 .   ? 3.19339   7.27966  10.64239  1.000 65.34441  ?  319 OLC A C3  1 
HETATM 2809 C C2  . OLC T  5 .   ? 3.23178   8.29452  11.74453  1.000 60.23055  ?  319 OLC A C2  1 
HETATM 2810 C C1  . OLC T  5 .   ? 2.85322   9.70828  11.33034  1.000 74.28332  ?  319 OLC A C1  1 
HETATM 2811 O O19 . OLC T  5 .   ? 1.92269   10.27712 11.94223  1.000 63.87445  ?  319 OLC A O19 1 
HETATM 2812 O O20 . OLC T  5 .   ? 3.48838   10.24145 10.39387  1.000 68.16667  ?  319 OLC A O20 1 
HETATM 2813 C C3  . OLC U  5 .   ? 0.00691   -0.35543 -13.11758 0.500 43.41705  ?  320 OLC A C3  1 
HETATM 2814 C C2  . OLC U  5 .   ? -0.53476  0.58932  -14.14684 0.500 46.78214  ?  320 OLC A C2  1 
HETATM 2815 C C1  . OLC U  5 .   ? -0.29081  0.17557  -15.58769 0.500 55.98167  ?  320 OLC A C1  1 
HETATM 2816 O O19 . OLC U  5 .   ? 0.32961   0.96630  -16.33320 0.500 58.55753  ?  320 OLC A O19 1 
HETATM 2817 O O20 . OLC U  5 .   ? -0.71801  -0.93824 -15.96237 0.500 58.24077  ?  320 OLC A O20 1 
HETATM 2818 C C10 . OLC V  5 .   ? -15.32567 26.53636 10.58797  1.000 52.23703  ?  321 OLC A C10 1 
HETATM 2819 C C9  . OLC V  5 .   ? -16.14237 25.60449 11.02722  1.000 55.25937  ?  321 OLC A C9  1 
HETATM 2820 C C11 . OLC V  5 .   ? -15.58013 27.49927 9.46995   1.000 40.32504  ?  321 OLC A C11 1 
HETATM 2821 C C8  . OLC V  5 .   ? -15.95433 24.70555 12.21355  1.000 54.00998  ?  321 OLC A C8  1 
HETATM 2822 C C12 . OLC V  5 .   ? -14.68508 27.31131 8.28479   1.000 39.42878  ?  321 OLC A C12 1 
HETATM 2823 C C7  . OLC V  5 .   ? -14.66748 23.94635 12.21301  1.000 39.02956  ?  321 OLC A C7  1 
HETATM 2824 C C6  . OLC V  5 .   ? -13.61867 24.45934 13.19570  1.000 55.69210  ?  321 OLC A C6  1 
HETATM 2825 C C5  . OLC V  5 .   ? -13.64509 23.79772 14.55235  1.000 47.17190  ?  321 OLC A C5  1 
HETATM 2826 C C4  . OLC V  5 .   ? -12.43010 24.09722 15.39934  1.000 52.42590  ?  321 OLC A C4  1 
HETATM 2827 C C3  . OLC V  5 .   ? -12.40937 23.40330 16.74605  1.000 41.34971  ?  321 OLC A C3  1 
HETATM 2828 C C2  . OLC V  5 .   ? -11.36227 23.97422 17.65909  1.000 56.55863  ?  321 OLC A C2  1 
HETATM 2829 C C21 . OLC V  5 .   ? -10.90149 22.83293 21.15285  1.000 62.84808  ?  321 OLC A C21 1 
HETATM 2830 C C1  . OLC V  5 .   ? -11.67277 23.79570 19.12226  1.000 72.86648  ?  321 OLC A C1  1 
HETATM 2831 C C22 . OLC V  5 .   ? -11.89376 21.69551 21.27583  1.000 79.30734  ?  321 OLC A C22 1 
HETATM 2832 O O19 . OLC V  5 .   ? -12.65945 24.22332 19.66857  1.000 90.91206  ?  321 OLC A O19 1 
HETATM 2833 O O23 . OLC V  5 .   ? -11.38835 20.53216 20.61996  1.000 42.98599  ?  321 OLC A O23 1 
HETATM 2834 O O20 . OLC V  5 .   ? -10.70107 23.13742 19.75401  1.000 76.24283  ?  321 OLC A O20 1 
HETATM 2835 C C10 . OLC W  5 .   ? 12.69693  28.30745 -6.05326  1.000 45.09126  ?  322 OLC A C10 1 
HETATM 2836 C C9  . OLC W  5 .   ? 12.60027  27.56674 -7.12772  1.000 52.28858  ?  322 OLC A C9  1 
HETATM 2837 C C11 . OLC W  5 .   ? 13.63466  28.11314 -4.90483  1.000 48.99863  ?  322 OLC A C11 1 
HETATM 2838 C C8  . OLC W  5 .   ? 11.60160  27.76479 -8.22888  1.000 45.63473  ?  322 OLC A C8  1 
HETATM 2839 C C12 . OLC W  5 .   ? 13.34935  26.89709 -4.07965  1.000 54.99918  ?  322 OLC A C12 1 
HETATM 2840 C C7  . OLC W  5 .   ? 12.20624  28.12396 -9.54954  1.000 45.40174  ?  322 OLC A C7  1 
HETATM 2841 C C6  . OLC W  5 .   ? 11.24805  28.02016 -10.72828 1.000 42.87061  ?  322 OLC A C6  1 
HETATM 2842 C C5  . OLC W  5 .   ? 11.65316  28.83609 -11.92843 1.000 37.53212  ?  322 OLC A C5  1 
HETATM 2843 C C4  . OLC W  5 .   ? 11.22028  28.25815 -13.24459 1.000 45.43433  ?  322 OLC A C4  1 
HETATM 2844 C C3  . OLC W  5 .   ? 10.70017  29.27823 -14.23805 1.000 50.52940  ?  322 OLC A C3  1 
HETATM 2845 C C2  . OLC W  5 .   ? 10.52667  28.68992 -15.60035 1.000 53.70870  ?  322 OLC A C2  1 
HETATM 2846 C C1  A OLC W  5 .   ? 9.64944   29.50160 -16.51941 0.600 53.02232  ?  322 OLC A C1  1 
HETATM 2847 O O19 A OLC W  5 .   ? 9.96741   30.50885 -17.09690 0.600 49.87056  ?  322 OLC A O19 1 
HETATM 2848 O O20 A OLC W  5 .   ? 8.43568   28.96531 -16.61768 0.600 67.45886  ?  322 OLC A O20 1 
HETATM 2849 C C1  A LFA X  4 .   ? 8.51269   11.57367 -12.94994 0.600 45.19503  ?  323 LFA A C1  1 
HETATM 2850 C C2  A LFA X  4 .   ? 7.85002   12.39384 -14.03634 0.600 50.69103  ?  323 LFA A C2  1 
HETATM 2851 C C3  A LFA X  4 .   ? 8.19588   11.99423 -15.45136 0.600 48.45669  ?  323 LFA A C3  1 
HETATM 2852 C C4  A LFA X  4 .   ? 7.49901   12.84074 -16.49075 0.600 51.95320  ?  323 LFA A C4  1 
HETATM 2853 C C5  A LFA X  4 .   ? 8.04826   12.69573 -17.88804 0.600 37.70072  ?  323 LFA A C5  1 
HETATM 2854 C C6  A LFA X  4 .   ? 7.41217   13.61018 -18.90496 0.600 45.21708  ?  323 LFA A C6  1 
HETATM 2855 C C1  B LFA Y  4 .   ? -17.92323 13.55191 -11.32325 0.400 27.03631  ?  324 LFA A C1  1 
HETATM 2856 C C2  B LFA Y  4 .   ? -19.17014 12.97522 -11.93330 0.400 31.66118  ?  324 LFA A C2  1 
HETATM 2857 C C3  B LFA Y  4 .   ? -20.26556 12.83831 -10.91507 0.400 35.69877  ?  324 LFA A C3  1 
HETATM 2858 C C1  . LFA Z  4 .   ? -17.63100 -0.71978 5.38114   1.000 50.82113  ?  325 LFA A C1  1 
HETATM 2859 C C2  . LFA Z  4 .   ? -17.25763 -1.11220 6.79384   1.000 53.06007  ?  325 LFA A C2  1 
HETATM 2860 C C3  . LFA Z  4 .   ? -17.33739 0.01268  7.80161   1.000 58.50649  ?  325 LFA A C3  1 
HETATM 2861 C C4  . LFA Z  4 .   ? -16.87341 -0.33370 9.20684   1.000 64.86637  ?  325 LFA A C4  1 
HETATM 2862 C C5  . LFA Z  4 .   ? -16.80622 0.84487  10.15823  1.000 47.89366  ?  325 LFA A C5  1 
HETATM 2863 C C6  . LFA Z  4 .   ? -16.27225 0.51537  11.53830  1.000 66.43937  ?  325 LFA A C6  1 
HETATM 2864 C C7  . LFA Z  4 .   ? -16.17821 1.70161  12.47806  1.000 50.91591  ?  325 LFA A C7  1 
HETATM 2865 C C1  . LFA AA 4 .   ? -8.39873  35.32110 -9.68529  1.000 37.83376  ?  326 LFA A C1  1 
HETATM 2866 C C2  . LFA AA 4 .   ? -7.73589  35.66853 -11.00200 1.000 55.26546  ?  326 LFA A C2  1 
HETATM 2867 C C3  . LFA AA 4 .   ? -8.71329  36.03715 -12.09498 1.000 67.82773  ?  326 LFA A C3  1 
HETATM 2868 C C4  . LFA AA 4 .   ? -8.10429  36.26987 -13.45844 1.000 65.80874  ?  326 LFA A C4  1 
HETATM 2869 O O   A HOH BA 6 .   ? -1.98527  24.51776 -4.45095  0.500 26.12532  ?  401 HOH A O   1 
HETATM 2870 O O   B HOH BA 6 .   ? -2.16776  25.32648 -4.23971  0.500 25.60048  ?  401 HOH A O   1 
HETATM 2871 O O   . HOH BA 6 .   ? -9.26652  12.29795 -18.17331 1.000 37.00506  ?  402 HOH A O   1 
HETATM 2872 O O   . HOH BA 6 .   ? -12.76019 11.48359 16.26703  1.000 35.68023  ?  403 HOH A O   1 
HETATM 2873 O O   A HOH BA 6 .   ? -4.28999  11.86732 -20.12045 0.600 24.01345  ?  404 HOH A O   1 
HETATM 2874 O O   . HOH BA 6 .   ? -9.78317  14.40859 -20.44907 1.000 45.01046  ?  405 HOH A O   1 
HETATM 2875 O O   . HOH BA 6 .   ? 1.36344   35.36533 27.82396  1.000 56.15345  ?  406 HOH A O   1 
HETATM 2876 O O   B HOH BA 6 .   ? -3.66455  21.34035 3.90607   0.400 31.71090  ?  407 HOH A O   1 
HETATM 2877 O O   . HOH BA 6 .   ? 3.27304   24.03665 -1.85016  1.000 28.63949  ?  408 HOH A O   1 
HETATM 2878 O O   . HOH BA 6 .   ? -19.21881 15.37516 21.33055  1.000 72.91822  ?  409 HOH A O   1 
HETATM 2879 O O   . HOH BA 6 .   ? -7.22720  27.62293 24.04027  1.000 52.77291  ?  410 HOH A O   1 
HETATM 2880 O O   . HOH BA 6 .   ? 4.25275   4.36098  17.77816  1.000 46.95481  ?  411 HOH A O   1 
HETATM 2881 O O   . HOH BA 6 .   ? -6.53756  17.32473 21.64346  1.000 34.23202  ?  412 HOH A O   1 
HETATM 2882 O O   . HOH BA 6 .   ? 3.02786   8.20848  15.88853  1.000 38.54071  ?  413 HOH A O   1 
HETATM 2883 O O   . HOH BA 6 .   ? 9.51119   37.52165 11.13960  1.000 25.20518  ?  414 HOH A O   1 
HETATM 2884 O O   B HOH BA 6 .   ? -2.68911  16.10315 -14.71695 0.400 28.75294  ?  415 HOH A O   1 
HETATM 2885 O O   . HOH BA 6 .   ? -24.04911 13.75458 7.73560   1.000 32.81612  ?  416 HOH A O   1 
HETATM 2886 O O   . HOH BA 6 .   ? -9.39306  17.45642 21.58414  1.000 34.42162  ?  417 HOH A O   1 
HETATM 2887 O O   A HOH BA 6 .   ? 0.94042   24.20900 5.10583   0.600 25.80840  ?  418 HOH A O   1 
HETATM 2888 O O   . HOH BA 6 .   ? -0.54614  21.03008 2.37953   1.000 31.36204  ?  419 HOH A O   1 
HETATM 2889 O O   . HOH BA 6 .   ? -1.02198  23.91542 1.87780   1.000 34.17166  ?  420 HOH A O   1 
HETATM 2890 O O   . HOH BA 6 .   ? -10.53804 9.10311  20.16863  1.000 37.03150  ?  421 HOH A O   1 
HETATM 2891 O O   A HOH BA 6 .   ? -6.07533  15.19556 -21.54813 0.600 30.14618  ?  422 HOH A O   1 
HETATM 2892 O O   A HOH BA 6 .   ? -7.00333  12.54978 -13.73732 0.600 20.99327  ?  423 HOH A O   1 
HETATM 2893 O O   B HOH BA 6 .   ? -6.65902  12.48885 -14.68881 0.400 22.18765  ?  423 HOH A O   1 
HETATM 2894 O O   . HOH BA 6 .   ? -0.30254  9.84900  22.41232  1.000 45.10177  ?  424 HOH A O   1 
HETATM 2895 O O   . HOH BA 6 .   ? -6.93905  -0.81762 18.55578  1.000 38.38636  ?  425 HOH A O   1 
HETATM 2896 O O   . HOH BA 6 .   ? -10.26133 27.54582 17.15991  1.000 51.11290  ?  426 HOH A O   1 
HETATM 2897 O O   B HOH BA 6 .   ? -1.81555  17.33595 5.12569   0.400 25.08890  ?  427 HOH A O   1 
HETATM 2898 O O   . HOH BA 6 .   ? 2.44580   25.55898 16.87902  1.000 29.09602  ?  428 HOH A O   1 
HETATM 2899 O O   . HOH BA 6 .   ? -9.40257  1.13646  15.53756  1.000 32.54750  ?  429 HOH A O   1 
HETATM 2900 O O   . HOH BA 6 .   ? -18.79111 8.73082  13.68396  1.000 43.54588  ?  430 HOH A O   1 
HETATM 2901 O O   . HOH BA 6 .   ? -15.99952 13.31351 -20.50205 1.000 48.02413  ?  431 HOH A O   1 
HETATM 2902 O O   . HOH BA 6 .   ? -5.29283  13.50553 27.53145  1.000 54.25049  ?  432 HOH A O   1 
HETATM 2903 O O   A HOH BA 6 .   ? -1.37207  18.54688 -5.96198  0.600 32.17512  ?  433 HOH A O   1 
HETATM 2904 O O   B HOH BA 6 .   ? -1.35364  17.62161 -6.11162  0.400 25.89037  ?  433 HOH A O   1 
HETATM 2905 O O   A HOH BA 6 .   ? -0.26423  17.30169 -8.67608  0.600 33.92855  ?  434 HOH A O   1 
HETATM 2906 O O   . HOH BA 6 .   ? -2.58203  16.51807 23.91956  1.000 33.79515  ?  435 HOH A O   1 
HETATM 2907 O O   . HOH BA 6 .   ? -25.75816 12.42378 9.53901   1.000 44.27263  ?  436 HOH A O   1 
HETATM 2908 O O   . HOH BA 6 .   ? -3.11897  26.48232 22.41050  1.000 27.82562  ?  437 HOH A O   1 
HETATM 2909 O O   . HOH BA 6 .   ? -20.42228 5.88517  13.71691  1.000 48.86440  ?  438 HOH A O   1 
HETATM 2910 O O   . HOH BA 6 .   ? -3.39263  17.46302 21.29188  1.000 28.17577  ?  439 HOH A O   1 
HETATM 2911 O O   . HOH BA 6 .   ? -21.04093 11.04385 13.09467  1.000 32.96523  ?  440 HOH A O   1 
HETATM 2912 O O   . HOH BA 6 .   ? -5.09005  28.97479 -22.82378 1.000 40.23562  ?  441 HOH A O   1 
HETATM 2913 O O   . HOH BA 6 .   ? -0.00935  4.97809  22.25215  1.000 43.71749  ?  442 HOH A O   1 
HETATM 2914 O O   . HOH BA 6 .   ? -10.28858 8.20782  -1.76354  1.000 25.02360  ?  443 HOH A O   1 
HETATM 2915 O O   . HOH BA 6 .   ? -3.41121  -5.38565 14.48232  1.000 40.43771  ?  444 HOH A O   1 
HETATM 2916 O O   . HOH BA 6 .   ? -17.47656 18.13491 17.91216  1.000 35.32135  ?  445 HOH A O   1 
HETATM 2917 O O   . HOH BA 6 .   ? -12.07082 -0.27407 -20.27215 1.000 51.93086  ?  446 HOH A O   1 
HETATM 2918 O O   . HOH BA 6 .   ? -10.11302 6.75191  -20.17990 1.000 44.08991  ?  447 HOH A O   1 
HETATM 2919 O O   . HOH BA 6 .   ? -3.39349  4.11286  21.47999  1.000 34.02005  ?  448 HOH A O   1 
HETATM 2920 O O   . HOH BA 6 .   ? -0.00000  0.00000  18.69321  0.500 33.67482  ?  449 HOH A O   1 
HETATM 2921 O O   . HOH BA 6 .   ? -3.63799  6.30168  -0.33394  1.000 28.50276  ?  450 HOH A O   1 
HETATM 2922 O O   A HOH BA 6 .   ? -2.87957  11.23541 23.24755  0.600 39.64505  ?  451 HOH A O   1 
HETATM 2923 O O   . HOH BA 6 .   ? -14.76066 20.93725 19.21854  1.000 47.17519  ?  452 HOH A O   1 
HETATM 2924 O O   . HOH BA 6 .   ? 1.96519   12.14415 19.18630  1.000 36.42559  ?  453 HOH A O   1 
HETATM 2925 O O   . HOH BA 6 .   ? -8.56127  18.41302 1.51156   1.000 23.69830  ?  454 HOH A O   1 
HETATM 2926 O O   A HOH BA 6 .   ? -5.05627  19.28523 3.23482   0.600 31.77688  ?  455 HOH A O   1 
HETATM 2927 O O   . HOH BA 6 .   ? -4.04310  30.67407 24.51818  1.000 53.15463  ?  456 HOH A O   1 
HETATM 2928 O O   . HOH BA 6 .   ? -1.91564  23.51409 28.77356  1.000 39.18267  ?  457 HOH A O   1 
HETATM 2929 O O   B HOH BA 6 .   ? 2.12845   25.54225 -0.05395  0.400 31.82662  ?  458 HOH A O   1 
HETATM 2930 O O   A HOH BA 6 .   ? -2.42271  18.12077 -8.98904  0.600 28.56600  ?  459 HOH A O   1 
HETATM 2931 O O   B HOH BA 6 .   ? -3.55281  18.61817 -8.68406  0.400 26.18925  ?  459 HOH A O   1 
HETATM 2932 O O   . HOH BA 6 .   ? -22.11081 16.88882 19.05586  1.000 50.78613  ?  460 HOH A O   1 
HETATM 2933 O O   . HOH BA 6 .   ? -24.15852 8.86609  12.12391  1.000 60.25000  ?  461 HOH A O   1 
HETATM 2934 O O   . HOH BA 6 .   ? -1.14664  6.17729  -1.74664  1.000 31.20895  ?  462 HOH A O   1 
HETATM 2935 O O   . HOH BA 6 .   ? -9.72913  19.11970 25.90541  1.000 39.17796  ?  463 HOH A O   1 
HETATM 2936 O O   . HOH BA 6 .   ? -22.38703 12.11735 17.32249  1.000 32.62409  ?  464 HOH A O   1 
HETATM 2937 O O   . HOH BA 6 .   ? -14.44383 3.13643  17.07579  1.000 59.60059  ?  465 HOH A O   1 
HETATM 2938 O O   A HOH BA 6 .   ? -5.91018  17.58200 4.96284   0.600 37.82655  ?  466 HOH A O   1 
HETATM 2939 O O   . HOH BA 6 .   ? -7.36547  20.91817 -24.26787 1.000 26.34339  ?  467 HOH A O   1 
HETATM 2940 O O   A HOH BA 6 .   ? 3.18302   15.21795 12.48559  0.600 27.63720  ?  468 HOH A O   1 
HETATM 2941 O O   . HOH BA 6 .   ? -16.35686 5.38362  -21.46162 1.000 55.46582  ?  469 HOH A O   1 
HETATM 2942 O O   . HOH BA 6 .   ? -12.66668 7.60841  16.88239  1.000 42.09804  ?  470 HOH A O   1 
HETATM 2943 O O   B HOH BA 6 .   ? -20.99285 22.15131 15.87232  0.400 27.87890  ?  471 HOH A O   1 
HETATM 2944 O O   . HOH BA 6 .   ? 4.34056   24.65348 22.88610  1.000 37.31285  ?  472 HOH A O   1 
HETATM 2945 O O   . HOH BA 6 .   ? -5.42255  -1.00266 14.49914  1.000 29.43938  ?  473 HOH A O   1 
HETATM 2946 O O   . HOH BA 6 .   ? -6.32528  32.29306 22.83296  1.000 52.85903  ?  474 HOH A O   1 
HETATM 2947 O O   . HOH BA 6 .   ? -13.23578 6.18871  -22.85565 1.000 42.50759  ?  475 HOH A O   1 
HETATM 2948 O O   . HOH BA 6 .   ? -14.88036 12.40038 23.97341  1.000 52.64528  ?  476 HOH A O   1 
HETATM 2949 O O   . HOH BA 6 .   ? -8.79632  10.07241 -19.88731 1.000 40.64975  ?  477 HOH A O   1 
HETATM 2950 O O   A HOH BA 6 .   ? -2.05545  11.94325 -19.08472 0.600 26.68692  ?  478 HOH A O   1 
HETATM 2951 O O   . HOH BA 6 .   ? -7.82935  -0.28450 13.65619  1.000 30.68718  ?  479 HOH A O   1 
HETATM 2952 O O   B HOH BA 6 .   ? 0.62850   14.90682 18.49982  0.400 20.04707  ?  480 HOH A O   1 
HETATM 2953 O O   A HOH BA 6 .   ? 4.79945   16.61285 -22.29053 0.600 39.99042  ?  481 HOH A O   1 
HETATM 2954 O O   B HOH BA 6 .   ? -3.46320  15.64469 -17.98249 0.400 29.83205  ?  482 HOH A O   1 
HETATM 2955 O O   . HOH BA 6 .   ? -13.31289 15.41503 -22.70313 1.000 44.80283  ?  483 HOH A O   1 
HETATM 2956 O O   . HOH BA 6 .   ? -10.00331 27.26382 -21.21101 1.000 49.67145  ?  484 HOH A O   1 
HETATM 2957 O O   . HOH BA 6 .   ? -9.57283  20.12081 23.20011  1.000 57.16963  ?  485 HOH A O   1 
HETATM 2958 O O   . HOH BA 6 .   ? -7.46352  18.42761 27.49719  1.000 29.06113  ?  486 HOH A O   1 
HETATM 2959 O O   . HOH BA 6 .   ? -7.554    15.852   -24.147   1.000 26.67220  ?  487 HOH A O   1 
HETATM 2960 O O   A HOH BA 6 .   ? -8.34491  17.85092 4.04887   0.600 41.80678  ?  488 HOH A O   1 
HETATM 2961 O O   B HOH BA 6 .   ? -7.03333  16.94342 4.02219   0.400 30.50785  ?  488 HOH A O   1 
HETATM 2962 O O   . HOH BA 6 .   ? -4.85827  22.52579 27.94247  1.000 22.57384  ?  489 HOH A O   1 
HETATM 2963 O O   A HOH BA 6 .   ? -24.75956 21.01814 15.92030  0.600 27.54909  ?  490 HOH A O   1 
HETATM 2964 O O   B HOH BA 6 .   ? -24.20849 22.13457 15.73869  0.400 26.55941  ?  490 HOH A O   1 
HETATM 2965 O O   A HOH BA 6 .   ? -6.66575  11.57389 -21.10490 0.600 36.06746  ?  491 HOH A O   1 
HETATM 2966 O O   . HOH BA 6 .   ? -9.51813  22.24159 -23.10549 1.000 35.20864  ?  492 HOH A O   1 
HETATM 2967 O O   . HOH BA 6 .   ? -11.20250 15.03499 29.19117  1.000 54.28372  ?  493 HOH A O   1 
HETATM 2968 O O   . HOH BA 6 .   ? -21.23175 9.85713  15.65489  1.000 43.32649  ?  494 HOH A O   1 
HETATM 2969 O O   . HOH BA 6 .   ? -25.71362 12.22025 6.85340   1.000 71.88058  ?  495 HOH A O   1 
HETATM 2970 O O   B HOH BA 6 .   ? -21.01658 21.34290 18.34659  0.500 39.97529  ?  496 HOH A O   1 
HETATM 2971 O O   . HOH BA 6 .   ? 0.09431   7.14575  23.26425  1.000 43.37000  ?  497 HOH A O   1 
HETATM 2972 O O   . HOH BA 6 .   ? -3.28724  1.34476  21.37639  1.000 41.13580  ?  498 HOH A O   1 
HETATM 2973 O O   B HOH BA 6 .   ? -2.21697  19.65643 2.78941   0.400 37.80000  ?  499 HOH A O   1 
HETATM 2974 O O   . HOH BA 6 .   ? -1.06253  9.73630  -20.38714 1.000 52.14131  ?  500 HOH A O   1 
HETATM 2975 O O   B HOH BA 6 .   ? -4.10346  13.76624 -15.68185 0.400 23.07047  ?  501 HOH A O   1 
HETATM 2976 O O   . HOH BA 6 .   ? -9.82587  -2.21521 12.48395  1.000 43.01729  ?  502 HOH A O   1 
HETATM 2977 O O   . HOH BA 6 .   ? -5.54705  -3.69160 15.36457  1.000 37.58217  ?  503 HOH A O   1 
HETATM 2978 O O   B HOH BA 6 .   ? -1.73028  2.40184  1.07837   0.400 29.12133  ?  504 HOH A O   1 
HETATM 2979 O O   . HOH BA 6 .   ? 0.21132   0.17302  21.25198  0.500 47.09384  ?  505 HOH A O   1 
HETATM 2980 O O   . HOH BA 6 .   ? 2.06342   11.35958 22.18632  1.000 48.74814  ?  506 HOH A O   1 
HETATM 2981 O O   . HOH BA 6 .   ? -21.76000 7.62430  11.85401  1.000 49.94244  ?  507 HOH A O   1 
HETATM 2982 O O   B HOH BA 6 .   ? -22.95916 23.84923 16.36528  0.400 26.15435  ?  508 HOH A O   1 
HETATM 2983 O O   . HOH BA 6 .   ? 0.037     22.650   30.298    1.000 50.41226  ?  509 HOH A O   1 
HETATM 2984 O O   A HOH BA 6 .   ? -16.65672 21.58758 16.77022  0.500 34.47373  ?  510 HOH A O   1 
HETATM 2985 O O   . HOH BA 6 .   ? -24.28994 20.00722 18.74134  1.000 61.65559  ?  511 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
11   N N   A ASP A 2   ? 0.60251 0.55268 0.49439 0.02739  -0.01803 0.01743  2   ASP A N   
12   N N   B ASP A 2   ? 0.60275 0.55285 0.49437 0.02689  -0.01762 0.01757  2   ASP A N   
13   C CA  A ASP A 2   ? 0.57525 0.51030 0.45949 0.02087  -0.01251 0.02141  2   ASP A CA  
14   C CA  B ASP A 2   ? 0.57287 0.50860 0.45745 0.01965  -0.01174 0.02150  2   ASP A CA  
15   C C   A ASP A 2   ? 0.45649 0.39463 0.35658 0.02060  -0.01681 0.01918  2   ASP A C   
16   C C   B ASP A 2   ? 0.45637 0.39485 0.35643 0.01933  -0.01597 0.01937  2   ASP A C   
17   O O   A ASP A 2   ? 0.42550 0.36599 0.33313 0.01124  -0.01282 0.01956  2   ASP A O   
18   O O   B ASP A 2   ? 0.43877 0.37108 0.33917 0.01157  -0.01147 0.02123  2   ASP A O   
19   C CB  A ASP A 2   ? 0.66297 0.57568 0.52299 0.02658  -0.01047 0.02610  2   ASP A CB  
20   C CB  B ASP A 2   ? 0.66168 0.57476 0.52184 0.02454  -0.00906 0.02641  2   ASP A CB  
21   N N   A ASN A 3   ? 0.48942 0.42786 0.39496 0.03107  -0.02492 0.01650  3   ASN A N   
22   N N   B ASN A 3   ? 0.42620 0.37409 0.33958 0.02785  -0.02440 0.01519  3   ASN A N   
23   C CA  A ASN A 3   ? 0.46254 0.40202 0.38197 0.03138  -0.02832 0.01465  3   ASN A CA  
24   C CA  B ASN A 3   ? 0.58034 0.53002 0.50810 0.02837  -0.02798 0.01327  3   ASN A CA  
25   C C   A ASN A 3   ? 0.42856 0.38750 0.37045 0.02571  -0.02908 0.01130  3   ASN A C   
26   C C   B ASN A 3   ? 0.45863 0.42743 0.40832 0.02237  -0.02845 0.01012  3   ASN A C   
27   O O   A ASN A 3   ? 0.32292 0.28212 0.27383 0.02138  -0.02825 0.01116  3   ASN A O   
28   O O   B ASN A 3   ? 0.36529 0.33376 0.32231 0.01678  -0.02663 0.01046  3   ASN A O   
29   C CB  A ASN A 3   ? 0.47608 0.41175 0.39784 0.04395  -0.03661 0.01195  3   ASN A CB  
30   C CB  B ASN A 3   ? 0.48206 0.42844 0.41236 0.04101  -0.03624 0.01057  3   ASN A CB  
31   C CG  A ASN A 3   ? 0.51545 0.42922 0.41677 0.04885  -0.03609 0.01548  3   ASN A CG  
32   C CG  B ASN A 3   ? 0.67288 0.59774 0.58202 0.04647  -0.03591 0.01398  3   ASN A CG  
33   O OD1 A ASN A 3   ? 0.53434 0.43496 0.42210 0.04207  -0.02923 0.02013  3   ASN A OD1 
34   O OD1 B ASN A 3   ? 0.52651 0.44720 0.42888 0.05721  -0.04141 0.01258  3   ASN A OD1 
35   N ND2 A ASN A 3   ? 0.58094 0.49068 0.48068 0.06084  -0.04347 0.01298  3   ASN A ND2 
36   N ND2 B ASN A 3   ? 0.60311 0.51418 0.50172 0.03934  -0.02959 0.01828  3   ASN A ND2 
37   N N   A ILE A 4   ? 0.37010 0.34529 0.32113 0.02598  -0.03070 0.00857  4   ILE A N   
38   N N   B ILE A 4   ? 0.38059 0.36598 0.34073 0.02367  -0.03093 0.00702  4   ILE A N   
39   C CA  A ILE A 4   ? 0.29227 0.28511 0.26319 0.01967  -0.03053 0.00604  4   ILE A CA  
40   C CA  B ILE A 4   ? 0.30139 0.30413 0.28012 0.01679  -0.03021 0.00477  4   ILE A CA  
41   C C   A ILE A 4   ? 0.36709 0.35744 0.33413 0.00746  -0.02295 0.00871  4   ILE A C   
42   C C   B ILE A 4   ? 0.35198 0.35107 0.32535 0.00482  -0.02258 0.00758  4   ILE A C   
43   O O   A ILE A 4   ? 0.33754 0.33264 0.31572 0.00237  -0.02226 0.00805  4   ILE A O   
44   O O   B ILE A 4   ? 0.28814 0.29231 0.27241 -0.00070 -0.02165 0.00698  4   ILE A O   
45   C CB  A ILE A 4   ? 0.35081 0.36135 0.33208 0.02187  -0.03343 0.00258  4   ILE A CB  
46   C CB  B ILE A 4   ? 0.30051 0.32005 0.28798 0.01874  -0.03268 0.00157  4   ILE A CB  
47   C CG1 A ILE A 4   ? 0.33018 0.34315 0.31539 0.03444  -0.04122 -0.00081 4   ILE A CG1 
48   C CG1 B ILE A 4   ? 0.24420 0.27162 0.24444 0.02990  -0.04098 -0.00269 4   ILE A CG1 
49   C CG2 A ILE A 4   ? 0.29668 0.32477 0.29908 0.01577  -0.03354 0.00016  4   ILE A CG2 
50   C CG2 B ILE A 4   ? 0.33201 0.36707 0.33415 0.00964  -0.03014 0.00025  4   ILE A CG2 
51   C CD1 A ILE A 4   ? 0.37135 0.40054 0.36453 0.03711  -0.04395 -0.00435 4   ILE A CD1 
52   C CD1 B ILE A 4   ? 0.37062 0.41470 0.38026 0.03266  -0.04399 -0.00640 4   ILE A CD1 
53   N N   A ILE A 5   ? 0.33412 0.31674 0.28533 0.00281  -0.01698 0.01157  5   ILE A N   
54   N N   B ILE A 5   ? 0.35024 0.34039 0.30684 0.00092  -0.01687 0.01046  5   ILE A N   
55   C CA  A ILE A 5   ? 0.39471 0.37587 0.34387 -0.00897 -0.00965 0.01325  5   ILE A CA  
56   C CA  B ILE A 5   ? 0.34942 0.33436 0.30037 -0.01027 -0.00916 0.01277  5   ILE A CA  
57   C C   A ILE A 5   ? 0.32776 0.29466 0.27164 -0.01187 -0.00733 0.01551  5   ILE A C   
58   C C   B ILE A 5   ? 0.31376 0.28592 0.26164 -0.01221 -0.00794 0.01461  5   ILE A C   
59   O O   A ILE A 5   ? 0.36155 0.33233 0.31319 -0.01957 -0.00484 0.01481  5   ILE A O   
60   O O   B ILE A 5   ? 0.34201 0.31837 0.29815 -0.01956 -0.00579 0.01384  5   ILE A O   
61   C CB  A ILE A 5   ? 0.42486 0.40174 0.36013 -0.01340 -0.00311 0.01541  5   ILE A CB  
62   C CB  B ILE A 5   ? 0.41035 0.38560 0.34304 -0.01275 -0.00281 0.01580  5   ILE A CB  
63   C CG1 A ILE A 5   ? 0.49984 0.49392 0.44381 -0.01186 -0.00538 0.01233  5   ILE A CG1 
64   C CG1 B ILE A 5   ? 0.54345 0.53385 0.48162 -0.01300 -0.00308 0.01340  5   ILE A CG1 
65   C CG2 A ILE A 5   ? 0.44968 0.42413 0.38393 -0.02544 0.00457  0.01652  5   ILE A CG2 
66   C CG2 B ILE A 5   ? 0.46524 0.43162 0.39131 -0.02349 0.00548  0.01820  5   ILE A CG2 
67   C CD1 A ILE A 5   ? 0.72341 0.71382 0.65367 -0.01467 0.00079  0.01419  5   ILE A CD1 
68   C CD1 B ILE A 5   ? 0.65854 0.64017 0.57889 -0.01454 0.00339  0.01627  5   ILE A CD1 
69   N N   A MET A 6   ? 0.36658 0.31703 0.29745 -0.00539 -0.00846 0.01792  6   MET A N   
70   N N   B MET A 6   ? 0.37539 0.33193 0.31137 -0.00524 -0.00962 0.01676  6   MET A N   
71   C CA  A MET A 6   ? 0.36949 0.30644 0.29601 -0.00780 -0.00653 0.01978  6   MET A CA  
72   C CA  B MET A 6   ? 0.34167 0.28457 0.27330 -0.00696 -0.00810 0.01860  6   MET A CA  
73   C C   A MET A 6   ? 0.38414 0.33008 0.32806 -0.00746 -0.01070 0.01689  6   MET A C   
74   C C   B MET A 6   ? 0.41689 0.36928 0.36625 -0.00721 -0.01189 0.01576  6   MET A C   
75   O O   A MET A 6   ? 0.31948 0.26214 0.26550 -0.01380 -0.00773 0.01724  6   MET A O   
76   O O   B MET A 6   ? 0.32286 0.27514 0.27587 -0.01475 -0.00857 0.01583  6   MET A O   
77   C CB  A MET A 6   ? 0.42191 0.34017 0.33249 0.00012  -0.00790 0.02254  6   MET A CB  
78   C CB  B MET A 6   ? 0.47156 0.39737 0.38891 0.00203  -0.01049 0.02084  6   MET A CB  
79   C CG  A MET A 6   ? 0.50723 0.41186 0.41477 -0.00178 -0.00652 0.02403  6   MET A CG  
80   C CG  B MET A 6   ? 0.47665 0.38884 0.39107 0.00133  -0.00985 0.02223  6   MET A CG  
81   S SD  A MET A 6   ? 0.63705 0.51909 0.52594 0.00758  -0.00834 0.02723  6   MET A SD  
82   S SD  B MET A 6   ? 0.66457 0.55503 0.56103 0.01135  -0.01229 0.02504  6   MET A SD  
83   C CE  A MET A 6   ? 0.47833 0.35382 0.34821 0.00819  -0.00371 0.03082  6   MET A CE  
84   C CE  B MET A 6   ? 0.44309 0.32157 0.34014 0.00662  -0.00987 0.02606  6   MET A CE  
85   N N   A THR A 7   ? 0.33053 0.28772 0.28731 0.00009  -0.01736 0.01387  7   THR A N   
86   N N   B THR A 7   ? 0.33718 0.29788 0.29799 0.00128  -0.01873 0.01303  7   THR A N   
87   C CA  A THR A 7   ? 0.32306 0.28904 0.29692 0.00034  -0.02040 0.01142  7   THR A CA  
88   C CA  B THR A 7   ? 0.30220 0.27165 0.28017 0.00166  -0.02174 0.01062  7   THR A CA  
89   C C   A THR A 7   ? 0.27298 0.25372 0.25843 -0.00826 -0.01789 0.01005  7   THR A C   
90   C C   B THR A 7   ? 0.29138 0.27561 0.28076 -0.00677 -0.01928 0.00932  7   THR A C   
91   O O   A THR A 7   ? 0.27908 0.26134 0.27162 -0.01195 -0.01707 0.00959  7   THR A O   
92   O O   B THR A 7   ? 0.27164 0.26059 0.27160 -0.00895 -0.01967 0.00832  7   THR A O   
93   C CB  A THR A 7   ? 0.30201 0.27502 0.28792 0.01085  -0.02769 0.00839  7   THR A CB  
94   C CB  B THR A 7   ? 0.31534 0.29315 0.30590 0.01181  -0.02887 0.00745  7   THR A CB  
95   O OG1 A THR A 7   ? 0.27933 0.26392 0.26890 0.01414  -0.03024 0.00653  7   THR A OG1 
96   O OG1 B THR A 7   ? 0.24644 0.24057 0.24603 0.01188  -0.03047 0.00526  7   THR A OG1 
97   C CG2 A THR A 7   ? 0.28227 0.23941 0.25902 0.01930  -0.03073 0.00906  7   THR A CG2 
98   C CG2 B THR A 7   ? 0.35608 0.32057 0.33496 0.02109  -0.03219 0.00797  7   THR A CG2 
99   N N   . ALA A 8   ? 0.32632 0.31793 0.31361 -0.01123 -0.01679 0.00919  8   ALA A N   
100  C CA  . ALA A 8   ? 0.34209 0.34684 0.33924 -0.01963 -0.01437 0.00772  8   ALA A CA  
101  C C   . ALA A 8   ? 0.26922 0.26477 0.25842 -0.02858 -0.00853 0.00928  8   ALA A C   
102  O O   . ALA A 8   ? 0.27426 0.27616 0.27229 -0.03330 -0.00808 0.00793  8   ALA A O   
103  C CB  . ALA A 8   ? 0.28507 0.30154 0.28432 -0.02157 -0.01371 0.00642  8   ALA A CB  
104  N N   . TYR A 9   ? 0.30326 0.28333 0.27578 -0.03047 -0.00409 0.01205  9   TYR A N   
105  C CA  . TYR A 9   ? 0.35598 0.32628 0.32165 -0.03866 0.00156  0.01320  9   TYR A CA  
106  C C   . TYR A 9   ? 0.32900 0.29362 0.29790 -0.03751 -0.00016 0.01305  9   TYR A C   
107  O O   . TYR A 9   ? 0.35029 0.31701 0.32321 -0.04418 0.00212  0.01180  9   TYR A O   
108  C CB  . TYR A 9   ? 0.39330 0.34665 0.34077 -0.03972 0.00671  0.01659  9   TYR A CB  
109  C CG  . TYR A 9   ? 0.46630 0.42369 0.40928 -0.04385 0.01104  0.01689  9   TYR A CG  
110  C CD1 . TYR A 9   ? 0.40026 0.37209 0.35381 -0.05146 0.01302  0.01401  9   TYR A CD1 
111  C CD2 . TYR A 9   ? 0.48486 0.43098 0.41261 -0.04013 0.01343  0.02001  9   TYR A CD2 
112  C CE1 . TYR A 9   ? 0.51300 0.48843 0.46310 -0.05550 0.01745  0.01398  9   TYR A CE1 
113  C CE2 . TYR A 9   ? 0.59906 0.54824 0.52215 -0.04388 0.01815  0.02042  9   TYR A CE2 
114  C CZ  . TYR A 9   ? 0.50517 0.46921 0.44002 -0.05180 0.02030  0.01727  9   TYR A CZ  
115  O OH  . TYR A 9   ? 0.59275 0.55977 0.52366 -0.05581 0.02546  0.01738  9   TYR A OH  
116  N N   . ILE A 10  ? 0.34965 0.30672 0.31663 -0.02893 -0.00415 0.01397  10  ILE A N   
117  C CA  . ILE A 10  ? 0.32903 0.28055 0.29944 -0.02751 -0.00552 0.01368  10  ILE A CA  
118  C C   . ILE A 10  ? 0.34175 0.30886 0.32848 -0.02911 -0.00768 0.01101  10  ILE A C   
119  O O   . ILE A 10  ? 0.33285 0.29896 0.32173 -0.03361 -0.00592 0.01038  10  ILE A O   
120  C CB  . ILE A 10  ? 0.40525 0.34780 0.37316 -0.01739 -0.00994 0.01439  10  ILE A CB  
121  C CG1 . ILE A 10  ? 0.39248 0.31732 0.34221 -0.01570 -0.00761 0.01746  10  ILE A CG1 
122  C CG2 . ILE A 10  ? 0.34067 0.27996 0.31528 -0.01545 -0.01158 0.01349  10  ILE A CG2 
123  C CD1 . ILE A 10  ? 0.42631 0.34512 0.37355 -0.00467 -0.01299 0.01751  10  ILE A CD1 
124  N N   . SER A 11  ? 0.31360 0.29546 0.31178 -0.02546 -0.01136 0.00936  11  SER A N   
125  C CA  . SER A 11  ? 0.30627 0.30320 0.32014 -0.02635 -0.01333 0.00722  11  SER A CA  
126  C C   . SER A 11  ? 0.25775 0.26072 0.27228 -0.03590 -0.00973 0.00624  11  SER A C   
127  O O   . SER A 11  ? 0.27887 0.28551 0.29928 -0.03823 -0.00963 0.00527  11  SER A O   
128  C CB  . SER A 11  ? 0.26002 0.27122 0.28563 -0.02108 -0.01750 0.00563  11  SER A CB  
129  O OG  . SER A 11  ? 0.25997 0.28430 0.30118 -0.02048 -0.01954 0.00403  11  SER A OG  
130  N N   . ILE A 12  ? 0.29797 0.30201 0.30656 -0.04123 -0.00670 0.00622  12  ILE A N   
131  C CA  . ILE A 12  ? 0.32546 0.33524 0.33540 -0.05044 -0.00327 0.00452  12  ILE A CA  
132  C C   . ILE A 12  ? 0.28426 0.28237 0.28705 -0.05516 0.00003  0.00475  12  ILE A C   
133  O O   . ILE A 12  ? 0.29359 0.29775 0.30164 -0.06012 0.00061  0.00253  12  ILE A O   
134  C CB  . ILE A 12  ? 0.29529 0.30599 0.29946 -0.05482 0.00014  0.00454  12  ILE A CB  
135  C CG1 . ILE A 12  ? 0.30266 0.32910 0.31695 -0.05195 -0.00313 0.00308  12  ILE A CG1 
136  C CG2 . ILE A 12  ? 0.39306 0.40383 0.39546 -0.06502 0.00512  0.00276  12  ILE A CG2 
137  C CD1 . ILE A 12  ? 0.33915 0.36458 0.34590 -0.05479 0.00044  0.00350  12  ILE A CD1 
138  N N   . PHE A 13  ? 0.30681 0.28807 0.29752 -0.05334 0.00197  0.00719  13  PHE A N   
139  C CA  . PHE A 13  ? 0.33418 0.30347 0.31824 -0.05738 0.00506  0.00732  13  PHE A CA  
140  C C   . PHE A 13  ? 0.31549 0.28895 0.30760 -0.05530 0.00220  0.00592  13  PHE A C   
141  O O   . PHE A 13  ? 0.35579 0.33199 0.35006 -0.06078 0.00366  0.00374  13  PHE A O   
142  C CB  . PHE A 13  ? 0.35880 0.30965 0.32950 -0.05398 0.00673  0.01050  13  PHE A CB  
143  C CG  . PHE A 13  ? 0.37679 0.31382 0.34015 -0.05782 0.01009  0.01079  13  PHE A CG  
144  C CD1 . PHE A 13  ? 0.37412 0.30683 0.33973 -0.05421 0.00775  0.01049  13  PHE A CD1 
145  C CD2 . PHE A 13  ? 0.40486 0.33248 0.35925 -0.06461 0.01587  0.01140  13  PHE A CD2 
146  C CE1 . PHE A 13  ? 0.42032 0.34034 0.37934 -0.05748 0.01069  0.01050  13  PHE A CE1 
147  C CE2 . PHE A 13  ? 0.44155 0.35608 0.38991 -0.06810 0.01904  0.01140  13  PHE A CE2 
148  C CZ  . PHE A 13  ? 0.44510 0.35621 0.39576 -0.06440 0.01613  0.01086  13  PHE A CZ  
149  N N   . VAL A 14  ? 0.32932 0.30396 0.32655 -0.04718 -0.00182 0.00682  14  VAL A N   
150  C CA  . VAL A 14  ? 0.31406 0.29258 0.31923 -0.04468 -0.00387 0.00584  14  VAL A CA  
151  C C   . VAL A 14  ? 0.28575 0.28088 0.30151 -0.04789 -0.00487 0.00359  14  VAL A C   
152  O O   . VAL A 14  ? 0.31074 0.30777 0.32848 -0.05030 -0.00438 0.00223  14  VAL A O   
153  C CB  . VAL A 14  ? 0.29491 0.27138 0.30493 -0.03528 -0.00747 0.00697  14  VAL A CB  
154  C CG1 . VAL A 14  ? 0.31398 0.29326 0.33182 -0.03296 -0.00840 0.00623  14  VAL A CG1 
155  C CG2 . VAL A 14  ? 0.28876 0.24826 0.28740 -0.03223 -0.00679 0.00884  14  VAL A CG2 
156  N N   . GLN A 15  ? 0.26908 0.27623 0.29103 -0.04816 -0.00623 0.00297  15  GLN A N   
157  C CA  . GLN A 15  ? 0.31176 0.33461 0.34388 -0.05104 -0.00745 0.00077  15  GLN A CA  
158  C C   . GLN A 15  ? 0.31866 0.34130 0.34677 -0.05943 -0.00461 -0.00158 15  GLN A C   
159  O O   . GLN A 15  ? 0.30341 0.33298 0.33657 -0.06070 -0.00563 -0.00334 15  GLN A O   
160  C CB  . GLN A 15  ? 0.27463 0.30939 0.31321 -0.05077 -0.00897 0.00017  15  GLN A CB  
161  C CG  . GLN A 15  ? 0.24385 0.28440 0.29148 -0.04231 -0.01284 0.00116  15  GLN A CG  
162  C CD  . GLN A 15  ? 0.31689 0.36777 0.36918 -0.04234 -0.01406 0.00028  15  GLN A CD  
163  O OE1 . GLN A 15  ? 0.28443 0.34720 0.34269 -0.04700 -0.01398 -0.00163 15  GLN A OE1 
164  N NE2 . GLN A 15  ? 0.29244 0.33893 0.34177 -0.03715 -0.01530 0.00132  15  GLN A NE2 
165  N N   A ILE A 16  ? 0.31170 0.32614 0.33083 -0.06495 -0.00095 -0.00182 16  ILE A N   
166  N N   B ILE A 16  ? 0.31232 0.32724 0.33165 -0.06496 -0.00098 -0.00181 16  ILE A N   
167  C CA  A ILE A 16  ? 0.32199 0.33757 0.33970 -0.07306 0.00167  -0.00498 16  ILE A CA  
168  C CA  B ILE A 16  ? 0.30383 0.31737 0.32000 -0.07323 0.00219  -0.00466 16  ILE A CA  
169  C C   A ILE A 16  ? 0.29924 0.30682 0.31312 -0.07346 0.00218  -0.00575 16  ILE A C   
170  C C   B ILE A 16  ? 0.29853 0.30635 0.31262 -0.07312 0.00206  -0.00558 16  ILE A C   
171  O O   A ILE A 16  ? 0.34480 0.35873 0.36213 -0.07688 0.00166  -0.00895 16  ILE A O   
172  O O   B ILE A 16  ? 0.35571 0.37149 0.37444 -0.07582 0.00102  -0.00861 16  ILE A O   
173  C CB  A ILE A 16  ? 0.27616 0.28528 0.28678 -0.07918 0.00627  -0.00522 16  ILE A CB  
174  C CB  B ILE A 16  ? 0.37149 0.37310 0.37744 -0.07792 0.00709  -0.00384 16  ILE A CB  
175  C CG1 A ILE A 16  ? 0.25283 0.27353 0.26906 -0.07993 0.00578  -0.00567 16  ILE A CG1 
176  C CG1 B ILE A 16  ? 0.33699 0.34564 0.34480 -0.07979 0.00818  -0.00384 16  ILE A CG1 
177  C CG2 A ILE A 16  ? 0.28305 0.29006 0.29218 -0.08724 0.00940  -0.00888 16  ILE A CG2 
178  C CG2 B ILE A 16  ? 0.36004 0.35657 0.36273 -0.08567 0.01070  -0.00687 16  ILE A CG2 
179  C CD1 A ILE A 16  ? 0.41688 0.42895 0.42438 -0.08334 0.01063  -0.00431 16  ILE A CD1 
180  C CD1 B ILE A 16  ? 0.34046 0.33858 0.33904 -0.08570 0.01413  -0.00343 16  ILE A CD1 
181  N N   . ILE A 17  ? 0.32578 0.31962 0.33258 -0.06959 0.00291  -0.00314 17  ILE A N   
182  C CA  A ILE A 17  ? 0.39284 0.37900 0.39616 -0.06966 0.00346  -0.00398 17  ILE A CA  
183  C CA  B ILE A 17  ? 0.39205 0.37853 0.39549 -0.06987 0.00348  -0.00410 17  ILE A CA  
184  C C   . ILE A 17  ? 0.34551 0.34133 0.35674 -0.06531 0.00014  -0.00458 17  ILE A C   
185  O O   . ILE A 17  ? 0.35581 0.35335 0.36703 -0.06747 0.00015  -0.00704 17  ILE A O   
186  C CB  A ILE A 17  ? 0.47217 0.44152 0.46683 -0.06610 0.00482  -0.00109 17  ILE A CB  
187  C CB  B ILE A 17  ? 0.47109 0.44022 0.46530 -0.06702 0.00519  -0.00139 17  ILE A CB  
188  C CG1 A ILE A 17  ? 0.51836 0.47695 0.50389 -0.07103 0.00893  -0.00039 17  ILE A CG1 
189  C CG1 B ILE A 17  ? 0.48722 0.44767 0.47352 -0.07062 0.00866  -0.00007 17  ILE A CG1 
190  C CG2 A ILE A 17  ? 0.45426 0.41642 0.44652 -0.06509 0.00502  -0.00194 17  ILE A CG2 
191  C CG2 B ILE A 17  ? 0.44181 0.40234 0.43166 -0.06893 0.00663  -0.00299 17  ILE A CG2 
192  C CD1 A ILE A 17  ? 0.55369 0.49592 0.53028 -0.06686 0.00987  0.00284  17  ILE A CD1 
193  C CD1 B ILE A 17  ? 0.40023 0.36024 0.38441 -0.07976 0.01264  -0.00308 17  ILE A CD1 
194  N N   A THR A 18  ? 0.34400 0.34620 0.36220 -0.05885 -0.00261 -0.00243 18  THR A N   
195  N N   B THR A 18  ? 0.34380 0.34625 0.36213 -0.05888 -0.00264 -0.00247 18  THR A N   
196  C CA  A THR A 18  ? 0.33118 0.34220 0.35764 -0.05415 -0.00509 -0.00231 18  THR A CA  
197  C CA  B THR A 18  ? 0.33166 0.34237 0.35778 -0.05435 -0.00499 -0.00244 18  THR A CA  
198  C C   A THR A 18  ? 0.30073 0.32570 0.33281 -0.05792 -0.00630 -0.00506 18  THR A C   
199  C C   B THR A 18  ? 0.30072 0.32632 0.33335 -0.05763 -0.00645 -0.00499 18  THR A C   
200  O O   A THR A 18  ? 0.34665 0.37532 0.38050 -0.05666 -0.00712 -0.00597 18  THR A O   
201  O O   B THR A 18  ? 0.32972 0.36041 0.36553 -0.05562 -0.00760 -0.00557 18  THR A O   
202  C CB  A THR A 18  ? 0.32708 0.34250 0.36148 -0.04698 -0.00744 0.00012  18  THR A CB  
203  C CB  B THR A 18  ? 0.36836 0.38152 0.40181 -0.04647 -0.00718 0.00022  18  THR A CB  
204  O OG1 A THR A 18  ? 0.31767 0.31993 0.34678 -0.04306 -0.00689 0.00208  18  THR A OG1 
205  O OG1 B THR A 18  ? 0.30619 0.32616 0.34345 -0.04656 -0.00839 0.00048  18  THR A OG1 
206  C CG2 A THR A 18  ? 0.32848 0.35159 0.37202 -0.04177 -0.00909 0.00072  18  THR A CG2 
207  C CG2 B THR A 18  ? 0.28178 0.28031 0.30982 -0.04211 -0.00637 0.00210  18  THR A CG2 
208  N N   . ALA A 19  ? 0.29061 0.32325 0.32523 -0.06229 -0.00640 -0.00653 19  ALA A N   
209  C CA  . ALA A 19  ? 0.28889 0.33507 0.32957 -0.06584 -0.00796 -0.00966 19  ALA A CA  
210  C C   . ALA A 19  ? 0.31639 0.35914 0.35153 -0.07089 -0.00677 -0.01319 19  ALA A C   
211  O O   . ALA A 19  ? 0.32735 0.37777 0.36556 -0.07030 -0.00880 -0.01516 19  ALA A O   
212  C CB  . ALA A 19  ? 0.32398 0.37790 0.36834 -0.07009 -0.00778 -0.01102 19  ALA A CB  
213  N N   . ILE A 20  ? 0.30302 0.33399 0.32995 -0.07550 -0.00353 -0.01412 20  ILE A N   
214  C CA  . ILE A 20  ? 0.37118 0.39831 0.39359 -0.08031 -0.00233 -0.01810 20  ILE A CA  
215  C C   . ILE A 20  ? 0.38772 0.41208 0.40793 -0.07546 -0.00369 -0.01760 20  ILE A C   
216  O O   . ILE A 20  ? 0.34227 0.37291 0.36350 -0.07623 -0.00540 -0.02092 20  ILE A O   
217  C CB  . ILE A 20  ? 0.32437 0.33775 0.33890 -0.08542 0.00194  -0.01852 20  ILE A CB  
218  C CG1 . ILE A 20  ? 0.32050 0.33767 0.33731 -0.09107 0.00402  -0.01970 20  ILE A CG1 
219  C CG2 . ILE A 20  ? 0.36226 0.37042 0.37270 -0.08933 0.00302  -0.02277 20  ILE A CG2 
220  C CD1 . ILE A 20  ? 0.43094 0.43357 0.43969 -0.09479 0.00894  -0.01838 20  ILE A CD1 
221  N N   . ILE A 21  ? 0.33080 0.34596 0.34807 -0.06997 -0.00301 -0.01362 21  ILE A N   
222  C CA  . ILE A 21  ? 0.40363 0.41492 0.41876 -0.06506 -0.00347 -0.01280 21  ILE A CA  
223  C C   . ILE A 21  ? 0.40264 0.42688 0.42452 -0.06099 -0.00627 -0.01267 21  ILE A C   
224  O O   . ILE A 21  ? 0.35220 0.37768 0.37163 -0.05982 -0.00687 -0.01437 21  ILE A O   
225  C CB  . ILE A 21  ? 0.40863 0.40882 0.42169 -0.05969 -0.00231 -0.00867 21  ILE A CB  
226  C CG1 . ILE A 21  ? 0.39973 0.38507 0.40399 -0.06337 0.00056  -0.00902 21  ILE A CG1 
227  C CG2 . ILE A 21  ? 0.44834 0.44691 0.46227 -0.05345 -0.00262 -0.00717 21  ILE A CG2 
228  C CD1 . ILE A 21  ? 0.44256 0.41824 0.44524 -0.05884 0.00110  -0.00523 21  ILE A CD1 
229  N N   . SER A 22  ? 0.35319 0.38703 0.38337 -0.05849 -0.00797 -0.01065 22  SER A N   
230  C CA  . SER A 22  ? 0.36323 0.40897 0.40051 -0.05427 -0.01035 -0.00997 22  SER A CA  
231  C C   . SER A 22  ? 0.31809 0.37300 0.35520 -0.05834 -0.01225 -0.01432 22  SER A C   
232  O O   . SER A 22  ? 0.31179 0.37146 0.34901 -0.05499 -0.01365 -0.01457 22  SER A O   
233  C CB  . SER A 22  ? 0.40015 0.45446 0.44735 -0.05135 -0.01180 -0.00748 22  SER A CB  
234  O OG  . SER A 22  ? 0.42220 0.46849 0.47035 -0.04643 -0.01066 -0.00404 22  SER A OG  
235  N N   . VAL A 23  ? 0.28968 0.34729 0.32683 -0.06523 -0.01228 -0.01790 23  VAL A N   
236  C CA  . VAL A 23  ? 0.31469 0.38123 0.35285 -0.06925 -0.01442 -0.02306 23  VAL A CA  
237  C C   . VAL A 23  ? 0.30724 0.36787 0.33752 -0.06904 -0.01432 -0.02578 23  VAL A C   
238  O O   . VAL A 23  ? 0.31591 0.38387 0.34637 -0.06682 -0.01702 -0.02783 23  VAL A O   
239  C CB  . VAL A 23  ? 0.30275 0.37206 0.34324 -0.07702 -0.01363 -0.02676 23  VAL A CB  
240  C CG1 . VAL A 23  ? 0.32595 0.40288 0.36775 -0.08144 -0.01572 -0.03315 23  VAL A CG1 
241  C CG2 . VAL A 23  ? 0.31807 0.39673 0.36725 -0.07634 -0.01460 -0.02462 23  VAL A CG2 
242  N N   . TYR A 24  ? 0.25811 0.30526 0.28102 -0.07096 -0.01134 -0.02591 24  TYR A N   
243  C CA  . TYR A 24  ? 0.27944 0.32080 0.29498 -0.07052 -0.01122 -0.02877 24  TYR A CA  
244  C C   . TYR A 24  ? 0.26642 0.30836 0.28024 -0.06259 -0.01203 -0.02546 24  TYR A C   
245  O O   . TYR A 24  ? 0.29766 0.34186 0.30726 -0.06088 -0.01359 -0.02825 24  TYR A O   
246  C CB  . TYR A 24  ? 0.33842 0.36476 0.34718 -0.07364 -0.00768 -0.02909 24  TYR A CB  
247  C CG  . TYR A 24  ? 0.30898 0.33364 0.31761 -0.08193 -0.00637 -0.03411 24  TYR A CG  
248  C CD1 . TYR A 24  ? 0.26945 0.29333 0.28125 -0.08606 -0.00437 -0.03286 24  TYR A CD1 
249  C CD2 . TYR A 24  ? 0.33230 0.35609 0.33800 -0.08548 -0.00684 -0.04030 24  TYR A CD2 
250  C CE1 . TYR A 24  ? 0.32777 0.34970 0.34009 -0.09357 -0.00226 -0.03710 24  TYR A CE1 
251  C CE2 . TYR A 24  ? 0.29479 0.31691 0.30212 -0.09324 -0.00509 -0.04522 24  TYR A CE2 
252  C CZ  . TYR A 24  ? 0.31576 0.33681 0.32659 -0.09740 -0.00246 -0.04332 24  TYR A CZ  
253  O OH  . TYR A 24  ? 0.30267 0.32153 0.31561 -0.10520 0.00021  -0.04797 24  TYR A OH  
254  N N   . GLY A 25  ? 0.28618 0.32617 0.30342 -0.05747 -0.01088 -0.01976 25  GLY A N   
255  C CA  . GLY A 25  ? 0.31893 0.35912 0.33614 -0.04987 -0.01066 -0.01614 25  GLY A CA  
256  C C   . GLY A 25  ? 0.27993 0.33273 0.30014 -0.04702 -0.01360 -0.01681 25  GLY A C   
257  O O   . GLY A 25  ? 0.32098 0.37308 0.33728 -0.04177 -0.01330 -0.01556 25  GLY A O   
258  N N   A LEU A 26  ? 0.29535 0.35944 0.32193 -0.05038 -0.01636 -0.01896 26  LEU A N   
259  N N   B LEU A 26  ? 0.29887 0.36303 0.32593 -0.05007 -0.01628 -0.01857 26  LEU A N   
260  C CA  A LEU A 26  ? 0.30003 0.37631 0.32948 -0.04781 -0.01970 -0.02006 26  LEU A CA  
261  C CA  B LEU A 26  ? 0.28539 0.36238 0.31654 -0.04752 -0.01960 -0.01927 26  LEU A CA  
262  C C   A LEU A 26  ? 0.28994 0.36574 0.31065 -0.04787 -0.02135 -0.02465 26  LEU A C   
263  C C   B LEU A 26  ? 0.34187 0.42102 0.36576 -0.04819 -0.02194 -0.02432 26  LEU A C   
264  O O   A LEU A 26  ? 0.30811 0.38956 0.32709 -0.04274 -0.02325 -0.02407 26  LEU A O   
265  O O   B LEU A 26  ? 0.34939 0.43846 0.37502 -0.04534 -0.02508 -0.02514 26  LEU A O   
266  C CB  A LEU A 26  ? 0.28016 0.36800 0.31787 -0.05257 -0.02248 -0.02285 26  LEU A CB  
267  C CB  B LEU A 26  ? 0.36703 0.45491 0.40751 -0.05167 -0.02186 -0.02085 26  LEU A CB  
268  C CG  A LEU A 26  ? 0.30127 0.39177 0.34806 -0.05235 -0.02155 -0.01904 26  LEU A CG  
269  C CG  B LEU A 26  ? 0.30543 0.39428 0.35428 -0.05003 -0.02057 -0.01629 26  LEU A CG  
270  C CD1 A LEU A 26  ? 0.31912 0.42172 0.37363 -0.05713 -0.02428 -0.02244 26  LEU A CD1 
271  C CD1 B LEU A 26  ? 0.30332 0.40375 0.36076 -0.05421 -0.02292 -0.01854 26  LEU A CD1 
272  C CD2 A LEU A 26  ? 0.37181 0.46449 0.42346 -0.04440 -0.02107 -0.01337 26  LEU A CD2 
273  C CD2 B LEU A 26  ? 0.36769 0.45854 0.42068 -0.04196 -0.02011 -0.01112 26  LEU A CD2 
274  N N   A PHE A 27  ? 0.29350 0.36269 0.30870 -0.05332 -0.02072 -0.02936 27  PHE A N   
275  N N   B PHE A 27  ? 0.24877 0.31905 0.26483 -0.05159 -0.02075 -0.02797 27  PHE A N   
276  C CA  A PHE A 27  ? 0.32559 0.39550 0.33377 -0.05411 -0.02294 -0.03525 27  PHE A CA  
277  C CA  B PHE A 27  ? 0.31755 0.38954 0.32682 -0.05221 -0.02324 -0.03377 27  PHE A CA  
278  C C   A PHE A 27  ? 0.32068 0.37964 0.31880 -0.05015 -0.02061 -0.03426 27  PHE A C   
279  C C   B PHE A 27  ? 0.30356 0.36501 0.30247 -0.04835 -0.02110 -0.03319 27  PHE A C   
280  O O   A PHE A 27  ? 0.30482 0.36278 0.29610 -0.05072 -0.02222 -0.03958 27  PHE A O   
281  O O   B PHE A 27  ? 0.34164 0.40446 0.33392 -0.04752 -0.02336 -0.03792 27  PHE A O   
282  C CB  A PHE A 27  ? 0.32905 0.40028 0.33929 -0.06264 -0.02395 -0.04218 27  PHE A CB  
283  C CB  B PHE A 27  ? 0.35535 0.42848 0.36614 -0.06073 -0.02437 -0.04087 27  PHE A CB  
284  C CG  A PHE A 27  ? 0.37583 0.45912 0.39588 -0.06609 -0.02641 -0.04385 27  PHE A CG  
285  C CG  B PHE A 27  ? 0.37911 0.46361 0.39982 -0.06471 -0.02660 -0.04261 27  PHE A CG  
286  C CD1 A PHE A 27  ? 0.49708 0.59269 0.51983 -0.06444 -0.03115 -0.04741 27  PHE A CD1 
287  C CD1 B PHE A 27  ? 0.48141 0.57852 0.50544 -0.06358 -0.03130 -0.04626 27  PHE A CD1 
288  C CD2 A PHE A 27  ? 0.40855 0.49092 0.43487 -0.07023 -0.02409 -0.04162 27  PHE A CD2 
289  C CD2 B PHE A 27  ? 0.40932 0.49182 0.43572 -0.06922 -0.02408 -0.04067 27  PHE A CD2 
290  C CE1 A PHE A 27  ? 0.46844 0.57551 0.50105 -0.06752 -0.03349 -0.04912 27  PHE A CE1 
291  C CE1 B PHE A 27  ? 0.45987 0.56771 0.49381 -0.06736 -0.03333 -0.04819 27  PHE A CE1 
292  C CE2 A PHE A 27  ? 0.45782 0.55153 0.49337 -0.07324 -0.02610 -0.04314 27  PHE A CE2 
293  C CE2 B PHE A 27  ? 0.45453 0.54759 0.49006 -0.07288 -0.02578 -0.04239 27  PHE A CE2 
294  C CZ  A PHE A 27  ? 0.50860 0.61485 0.54783 -0.07209 -0.03078 -0.04701 27  PHE A CZ  
295  C CZ  B PHE A 27  ? 0.50810 0.61402 0.54793 -0.07215 -0.03037 -0.04626 27  PHE A CZ  
296  N N   . ILE A 28  ? 0.31786 0.36910 0.31545 -0.04582 -0.01702 -0.02802 28  ILE A N   
297  C CA  . ILE A 28  ? 0.34981 0.39099 0.33848 -0.04155 -0.01445 -0.02685 28  ILE A CA  
298  C C   . ILE A 28  ? 0.30870 0.35538 0.29371 -0.03393 -0.01552 -0.02481 28  ILE A C   
299  O O   . ILE A 28  ? 0.34205 0.39427 0.33329 -0.02971 -0.01522 -0.01979 28  ILE A O   
300  C CB  . ILE A 28  ? 0.32979 0.36063 0.32044 -0.03970 -0.01015 -0.02136 28  ILE A CB  
301  C CG1 . ILE A 28  ? 0.32497 0.34921 0.31709 -0.04668 -0.00910 -0.02329 28  ILE A CG1 
302  C CG2 . ILE A 28  ? 0.35294 0.37416 0.33579 -0.03436 -0.00705 -0.01954 28  ILE A CG2 
303  C CD1 . ILE A 28  ? 0.31868 0.33346 0.31334 -0.04490 -0.00581 -0.01837 28  ILE A CD1 
304  N N   . PRO A 29  ? 0.33014 0.37524 0.30536 -0.03188 -0.01662 -0.02851 29  PRO A N   
305  C CA  . PRO A 29  ? 0.29154 0.34112 0.26174 -0.02406 -0.01736 -0.02612 29  PRO A CA  
306  C C   . PRO A 29  ? 0.39173 0.43422 0.36198 -0.01758 -0.01210 -0.01851 29  PRO A C   
307  O O   . PRO A 29  ? 0.36616 0.39811 0.33585 -0.01833 -0.00822 -0.01689 29  PRO A O   
308  C CB  . PRO A 29  ? 0.37723 0.42427 0.33569 -0.02350 -0.01925 -0.03229 29  PRO A CB  
309  C CG  . PRO A 29  ? 0.50238 0.53893 0.45942 -0.02924 -0.01693 -0.03532 29  PRO A CG  
310  C CD  . PRO A 29  ? 0.45140 0.48944 0.41931 -0.03587 -0.01672 -0.03461 29  PRO A CD  
311  N N   . LEU A 30  ? 0.39246 0.44068 0.36430 -0.01116 -0.01181 -0.01390 30  LEU A N   
312  C CA  . LEU A 30  ? 0.35735 0.40003 0.33212 -0.00505 -0.00638 -0.00661 30  LEU A CA  
313  C C   . LEU A 30  ? 0.34432 0.38529 0.30908 0.00295  -0.00435 -0.00414 30  LEU A C   
314  O O   . LEU A 30  ? 0.37674 0.42515 0.33604 0.00533  -0.00804 -0.00602 30  LEU A O   
315  C CB  . LEU A 30  ? 0.39158 0.44208 0.37992 -0.00409 -0.00651 -0.00207 30  LEU A CB  
316  C CG  . LEU A 30  ? 0.45505 0.50707 0.45372 -0.01072 -0.00777 -0.00328 30  LEU A CG  
317  C CD1 . LEU A 30  ? 0.42187 0.48272 0.43385 -0.00886 -0.00820 0.00084  30  LEU A CD1 
318  C CD2 . LEU A 30  ? 0.33732 0.37694 0.33593 -0.01197 -0.00377 -0.00221 30  LEU A CD2 
319  N N   . ASN A 31  ? 0.32373 0.35457 0.28594 0.00731  0.00164  -0.00004 31  ASN A N   
320  C CA  . ASN A 31  ? 0.36574 0.39419 0.32050 0.01579  0.00541  0.00429  31  ASN A CA  
321  C C   . ASN A 31  ? 0.31573 0.35162 0.28019 0.02036  0.00648  0.01038  31  ASN A C   
322  O O   . ASN A 31  ? 0.36110 0.40195 0.33931 0.01735  0.00553  0.01179  31  ASN A O   
323  C CB  . ASN A 31  ? 0.40530 0.42081 0.35736 0.01853  0.01222  0.00696  31  ASN A CB  
324  C CG  . ASN A 31  ? 0.59260 0.60055 0.53478 0.01459  0.01134  0.00099  31  ASN A CG  
325  O OD1 . ASN A 31  ? 0.67558 0.67717 0.62250 0.00983  0.01235  -0.00050 31  ASN A OD1 
326  N ND2 . ASN A 31  ? 0.46778 0.47639 0.39618 0.01683  0.00922  -0.00269 31  ASN A ND2 
327  N N   A PHE A 32  ? 0.52128 0.41834 0.31878 0.04739  -0.02521 -0.01028 32  PHE A N   
328  N N   B PHE A 32  ? 0.52020 0.41732 0.31790 0.04770  -0.02509 -0.00994 32  PHE A N   
329  C CA  A PHE A 32  ? 0.43663 0.36833 0.26732 0.05255  -0.03274 0.00115  32  PHE A CA  
330  C CA  B PHE A 32  ? 0.42460 0.35779 0.25585 0.04967  -0.03427 -0.00138 32  PHE A CA  
331  C C   A PHE A 32  ? 0.40200 0.33734 0.25539 0.06133  -0.02832 0.01622  32  PHE A C   
332  C C   B PHE A 32  ? 0.41099 0.35303 0.26830 0.05932  -0.03122 0.01486  32  PHE A C   
333  O O   A PHE A 32  ? 0.37177 0.32670 0.25514 0.05613  -0.03457 0.01879  32  PHE A O   
334  O O   B PHE A 32  ? 0.41564 0.38108 0.30416 0.05487  -0.03865 0.01790  32  PHE A O   
335  C CB  A PHE A 32  ? 0.42787 0.37258 0.25152 0.06577  -0.03442 0.00822  32  PHE A CB  
336  C CB  B PHE A 32  ? 0.49071 0.44048 0.31721 0.06002  -0.03825 0.00340  32  PHE A CB  
337  C CG  A PHE A 32  ? 0.45624 0.43434 0.31360 0.07401  -0.04067 0.02303  32  PHE A CG  
338  C CG  B PHE A 32  ? 0.39242 0.37651 0.25378 0.06679  -0.04530 0.01709  32  PHE A CG  
339  C CD1 A PHE A 32  ? 0.44651 0.45293 0.32486 0.06564  -0.05288 0.01891  32  PHE A CD1 
340  C CD1 B PHE A 32  ? 0.45669 0.46643 0.34315 0.05536  -0.05696 0.01181  32  PHE A CD1 
341  C CD2 A PHE A 32  ? 0.40154 0.38255 0.27056 0.09020  -0.03454 0.04124  32  PHE A CD2 
342  C CD2 B PHE A 32  ? 0.46342 0.45395 0.33390 0.08448  -0.04030 0.03545  32  PHE A CD2 
343  C CE1 A PHE A 32  ? 0.46153 0.49824 0.37198 0.07325  -0.05909 0.03263  32  PHE A CE1 
344  C CE1 B PHE A 32  ? 0.42060 0.46114 0.34008 0.06147  -0.06397 0.02404  32  PHE A CE1 
345  C CE2 A PHE A 32  ? 0.36542 0.37656 0.26707 0.09772  -0.04064 0.05525  32  PHE A CE2 
346  C CE2 B PHE A 32  ? 0.37488 0.39643 0.27929 0.09042  -0.04721 0.04832  32  PHE A CE2 
347  C CZ  A PHE A 32  ? 0.38555 0.42439 0.30818 0.08925  -0.05301 0.05099  32  PHE A CZ  
348  C CZ  B PHE A 32  ? 0.46811 0.51443 0.39702 0.07886  -0.05931 0.04237  32  PHE A CZ  
349  N N   A LYS A 33  ? 0.42098 0.33732 0.26047 0.07504  -0.01777 0.02596  33  LYS A N   
350  N N   B LYS A 33  ? 0.42308 0.34755 0.26886 0.07318  -0.02091 0.02538  33  LYS A N   
351  C CA  A LYS A 33  ? 0.46820 0.39009 0.33085 0.08524  -0.01439 0.04156  33  LYS A CA  
352  C CA  B LYS A 33  ? 0.42459 0.35639 0.29500 0.08349  -0.01809 0.04127  33  LYS A CA  
353  C C   A LYS A 33  ? 0.45830 0.37535 0.33512 0.07475  -0.01488 0.03752  33  LYS A C   
354  C C   B LYS A 33  ? 0.45152 0.37247 0.33146 0.07470  -0.01614 0.03793  33  LYS A C   
355  O O   A LYS A 33  ? 0.43001 0.36494 0.33721 0.07803  -0.01877 0.04678  33  LYS A O   
356  O O   B LYS A 33  ? 0.42584 0.34840 0.32329 0.08354  -0.01315 0.05014  33  LYS A O   
357  C CB  A LYS A 33  ? 0.46467 0.36629 0.30914 0.10173  -0.00264 0.05239  33  LYS A CB  
358  C CB  B LYS A 33  ? 0.46719 0.38486 0.32301 0.10174  -0.00767 0.05419  33  LYS A CB  
359  C CG  A LYS A 33  ? 0.56185 0.42634 0.37426 0.09880  0.00733  0.04384  33  LYS A CG  
360  C CG  B LYS A 33  ? 0.60816 0.49134 0.44179 0.10406  0.00404  0.05303  33  LYS A CG  
361  C CD  A LYS A 33  ? 0.53505 0.38329 0.33088 0.11697  0.01834  0.05551  33  LYS A CD  
362  C CD  B LYS A 33  ? 0.60403 0.45940 0.40189 0.09430  0.00777  0.03619  33  LYS A CD  
363  C CE  A LYS A 33  ? 0.65804 0.46994 0.42845 0.11593  0.02862  0.05022  33  LYS A CE  
364  C CE  B LYS A 33  ? 0.66085 0.48350 0.43217 0.10439  0.02070  0.03951  33  LYS A CE  
365  N NZ  A LYS A 33  ? 0.68778 0.49543 0.47615 0.11050  0.02955  0.05271  33  LYS A NZ  
366  N NZ  B LYS A 33  ? 0.73054 0.52234 0.47845 0.09233  0.02510  0.02525  33  LYS A NZ  
367  N N   A ASP A 34  ? 0.36992 0.26418 0.22621 0.06203  -0.01162 0.02369  34  ASP A N   
368  N N   B ASP A 34  ? 0.42856 0.33949 0.29831 0.05812  -0.01793 0.02233  34  ASP A N   
369  C CA  A ASP A 34  ? 0.35298 0.23795 0.21719 0.05318  -0.00968 0.02044  34  ASP A CA  
370  C CA  B ASP A 34  ? 0.40240 0.30111 0.27682 0.04955  -0.01499 0.01862  34  ASP A CA  
371  C C   A ASP A 34  ? 0.37880 0.28345 0.26255 0.03715  -0.01938 0.01068  34  ASP A C   
372  C C   B ASP A 34  ? 0.33682 0.25502 0.23184 0.03388  -0.02442 0.00934  34  ASP A C   
373  O O   A ASP A 34  ? 0.36061 0.25683 0.24754 0.02820  -0.01749 0.00609  34  ASP A O   
374  O O   B ASP A 34  ? 0.36513 0.27661 0.26612 0.02677  -0.02247 0.00665  34  ASP A O   
375  C CB  A ASP A 34  ? 0.46926 0.31759 0.30110 0.04816  -0.00002 0.01180  34  ASP A CB  
376  C CB  B ASP A 34  ? 0.42223 0.28419 0.26269 0.04470  -0.00530 0.00969  34  ASP A CB  
377  C CG  A ASP A 34  ? 0.55729 0.38423 0.36733 0.06367  0.00997  0.01995  34  ASP A CG  
378  C CG  B ASP A 34  ? 0.49841 0.33848 0.31936 0.06077  0.00532  0.01931  34  ASP A CG  
379  O OD1 A ASP A 34  ? 0.47447 0.30388 0.29738 0.07670  0.01393  0.03427  34  ASP A OD1 
380  O OD1 B ASP A 34  ? 0.41253 0.26429 0.24950 0.07519  0.00645  0.03434  34  ASP A OD1 
381  O OD2 A ASP A 34  ? 0.51721 0.32552 0.29814 0.06311  0.01347  0.01190  34  ASP A OD2 
382  O OD2 B ASP A 34  ? 0.48857 0.29929 0.27912 0.05887  0.01254  0.01183  34  ASP A OD2 
383  N N   A ILE A 35  ? 0.33199 0.26262 0.22852 0.03367  -0.02939 0.00766  35  ILE A N   
384  N N   B ILE A 35  ? 0.40375 0.34610 0.30943 0.02866  -0.03438 0.00453  35  ILE A N   
385  C CA  A ILE A 35  ? 0.38409 0.33328 0.29740 0.01790  -0.03870 -0.00294 35  ILE A CA  
386  C CA  B ILE A 35  ? 0.30776 0.26848 0.23178 0.01330  -0.04324 -0.00535 35  ILE A CA  
387  C C   A ILE A 35  ? 0.30042 0.26172 0.24133 0.01628  -0.04088 0.00165  35  ILE A C   
388  C C   B ILE A 35  ? 0.33645 0.31313 0.29109 0.01494  -0.04618 0.00183  35  ILE A C   
389  O O   A ILE A 35  ? 0.34671 0.30915 0.29258 0.00272  -0.04292 -0.00776 35  ILE A O   
390  O O   B ILE A 35  ? 0.30209 0.28264 0.26581 0.00284  -0.04864 -0.00597 35  ILE A O   
391  C CB  A ILE A 35  ? 0.39313 0.37030 0.31822 0.01741  -0.04937 -0.00435 35  ILE A CB  
392  C CB  B ILE A 35  ? 0.44150 0.42739 0.37384 0.00948  -0.05397 -0.01011 35  ILE A CB  
393  C CG1 A ILE A 35  ? 0.42378 0.38827 0.31986 0.01099  -0.04944 -0.01663 35  ILE A CG1 
394  C CG1 B ILE A 35  ? 0.41574 0.38906 0.31991 0.01552  -0.05100 -0.01175 35  ILE A CG1 
395  C CG2 A ILE A 35  ? 0.40369 0.40990 0.36014 0.00739  -0.06022 -0.00820 35  ILE A CG2 
396  C CG2 B ILE A 35  ? 0.47982 0.47371 0.41742 -0.00943 -0.06062 -0.02522 35  ILE A CG2 
397  C CD1 A ILE A 35  ? 0.59895 0.58744 0.50054 0.01422  -0.05847 -0.01623 35  ILE A CD1 
398  C CD1 B ILE A 35  ? 0.53821 0.53718 0.45023 0.01534  -0.06126 -0.01359 35  ILE A CD1 
399  N N   A ILE A 36  ? 0.30135 0.27132 0.26040 0.03043  -0.04032 0.01619  36  ILE A N   
400  N N   B ILE A 36  ? 0.25919 0.24568 0.23067 0.03010  -0.04617 0.01669  36  ILE A N   
401  C CA  A ILE A 36  ? 0.26130 0.24633 0.24913 0.03059  -0.04447 0.02062  36  ILE A CA  
402  C CA  B ILE A 36  ? 0.24561 0.24662 0.24643 0.03274  -0.04981 0.02313  36  ILE A CA  
403  C C   A ILE A 36  ? 0.28257 0.24493 0.26004 0.02559  -0.03665 0.01727  36  ILE A C   
404  C C   B ILE A 36  ? 0.26882 0.24878 0.26011 0.02631  -0.04280 0.01840  36  ILE A C   
405  O O   A ILE A 36  ? 0.25889 0.23241 0.25605 0.02209  -0.04025 0.01684  36  ILE A O   
406  O O   B ILE A 36  ? 0.30873 0.30066 0.32002 0.02205  -0.04693 0.01714  36  ILE A O   
407  C CB  A ILE A 36  ? 0.25560 0.25447 0.26588 0.04769  -0.04632 0.03727  36  ILE A CB  
408  C CB  B ILE A 36  ? 0.22356 0.23307 0.24158 0.05090  -0.04959 0.04044  36  ILE A CB  
409  C CG1 A ILE A 36  ? 0.26651 0.28911 0.31207 0.04746  -0.05496 0.04024  36  ILE A CG1 
410  C CG1 B ILE A 36  ? 0.38679 0.41396 0.43792 0.05359  -0.05573 0.04595  36  ILE A CG1 
411  C CG2 A ILE A 36  ? 0.25170 0.22437 0.24580 0.05943  -0.03488 0.04645  36  ILE A CG2 
412  C CG2 B ILE A 36  ? 0.21715 0.19761 0.21212 0.06154  -0.03721 0.04782  36  ILE A CG2 
413  C CD1 A ILE A 36  ? 0.25656 0.29411 0.32298 0.06140  -0.05623 0.05181  36  ILE A CD1 
414  C CD1 B ILE A 36  ? 0.29864 0.35459 0.37402 0.04402  -0.06790 0.03886  36  ILE A CD1 
415  N N   A LEU A 37  ? 0.30291 0.23363 0.24985 0.02601  -0.02602 0.01526  37  LEU A N   
416  N N   B LEU A 37  ? 0.29819 0.24664 0.25838 0.02553  -0.03226 0.01541  37  LEU A N   
417  C CA  A LEU A 37  ? 0.32489 0.23344 0.26128 0.02069  -0.01845 0.01221  37  LEU A CA  
418  C CA  B LEU A 37  ? 0.29364 0.22006 0.24319 0.02013  -0.02471 0.01210  37  LEU A CA  
419  C C   A LEU A 37  ? 0.31031 0.22287 0.24778 0.00242  -0.02170 -0.00128 37  LEU A C   
420  C C   B LEU A 37  ? 0.34359 0.27555 0.29601 0.00219  -0.02838 -0.00115 37  LEU A C   
421  O O   A LEU A 37  ? 0.32166 0.22968 0.26394 -0.00212 -0.01911 -0.00224 37  LEU A O   
422  O O   B LEU A 37  ? 0.33312 0.26251 0.29242 -0.00181 -0.02641 -0.00181 37  LEU A O   
423  C CB  A LEU A 37  ? 0.31613 0.18917 0.21933 0.02447  -0.00669 0.01229  37  LEU A CB  
424  C CB  B LEU A 37  ? 0.31281 0.20407 0.22827 0.02322  -0.01310 0.01154  37  LEU A CB  
425  C CG  A LEU A 37  ? 0.33802 0.20107 0.23555 0.04285  -0.00060 0.02577  37  LEU A CG  
426  C CG  B LEU A 37  ? 0.34865 0.23265 0.26003 0.04153  -0.00790 0.02515  37  LEU A CG  
427  C CD1 A LEU A 37  ? 0.37200 0.20187 0.23427 0.04439  0.00957  0.02235  37  LEU A CD1 
428  C CD1 B LEU A 37  ? 0.40097 0.25173 0.27714 0.04402  0.00264  0.02262  37  LEU A CD1 
429  C CD2 A LEU A 37  ? 0.35993 0.22356 0.27440 0.05224  0.00158  0.03685  37  LEU A CD2 
430  C CD2 B LEU A 37  ? 0.32065 0.20620 0.25020 0.05102  -0.00605 0.03638  37  LEU A CD2 
431  N N   A ARG A 38  ? 0.34577 0.26577 0.27778 -0.00808 -0.02687 -0.01169 38  ARG A N   
432  N N   B ARG A 38  ? 0.32622 0.26623 0.27365 -0.00850 -0.03370 -0.01160 38  ARG A N   
433  C CA  A ARG A 38  ? 0.36581 0.29287 0.30298 -0.02538 -0.03053 -0.02368 38  ARG A CA  
434  C CA  B ARG A 38  ? 0.33361 0.28226 0.28740 -0.02555 -0.03786 -0.02361 38  ARG A CA  
435  C C   A ARG A 38  ? 0.32235 0.28186 0.29308 -0.02624 -0.03978 -0.02164 38  ARG A C   
436  C C   B ARG A 38  ? 0.28271 0.26115 0.26987 -0.02541 -0.04604 -0.02069 38  ARG A C   
437  O O   A ARG A 38  ? 0.29993 0.26351 0.27881 -0.03576 -0.04000 -0.02672 38  ARG A O   
438  O O   B ARG A 38  ? 0.30239 0.28221 0.29617 -0.03376 -0.04518 -0.02503 38  ARG A O   
439  C CB  A ARG A 38  ? 0.44646 0.37373 0.37079 -0.03679 -0.03451 -0.03589 38  ARG A CB  
440  C CB  B ARG A 38  ? 0.33476 0.28888 0.27963 -0.03606 -0.04338 -0.03495 38  ARG A CB  
441  C CG  A ARG A 38  ? 0.43099 0.36928 0.36506 -0.05463 -0.03906 -0.04749 38  ARG A CG  
442  C CG  B ARG A 38  ? 0.47550 0.41701 0.40846 -0.05424 -0.04117 -0.04853 38  ARG A CG  
443  C CD  A ARG A 38  ? 0.50110 0.44265 0.42612 -0.06545 -0.04465 -0.05937 38  ARG A CD  
444  C CD  B ARG A 38  ? 0.40813 0.34961 0.32832 -0.06386 -0.04603 -0.06020 38  ARG A CD  
445  N NE  A ARG A 38  ? 0.45112 0.36137 0.34425 -0.06560 -0.03765 -0.06368 38  ARG A NE  
446  N NE  B ARG A 38  ? 0.56905 0.47844 0.45694 -0.06231 -0.03845 -0.06340 38  ARG A NE  
447  C CZ  A ARG A 38  ? 0.70264 0.61114 0.58175 -0.06521 -0.04135 -0.06919 38  ARG A CZ  
448  C CZ  B ARG A 38  ? 0.61586 0.52252 0.48871 -0.05898 -0.04127 -0.06689 38  ARG A CZ  
449  N NH1 A ARG A 38  ? 0.66787 0.60399 0.56167 -0.06395 -0.05153 -0.06982 38  ARG A NH1 
450  N NH1 B ARG A 38  ? 0.53962 0.47339 0.42648 -0.05621 -0.05098 -0.06633 38  ARG A NH1 
451  N NH2 A ARG A 38  ? 0.55377 0.43203 0.40319 -0.06545 -0.03492 -0.07417 38  ARG A NH2 
452  N NH2 B ARG A 38  ? 0.52445 0.40048 0.36730 -0.05754 -0.03426 -0.07076 38  ARG A NH2 
453  N N   A GLU A 39  ? 0.25692 0.23972 0.24759 -0.01585 -0.04736 -0.01391 39  GLU A N   
454  N N   B GLU A 39  ? 0.32425 0.32655 0.33302 -0.01518 -0.05388 -0.01280 39  GLU A N   
455  C CA  A GLU A 39  ? 0.30718 0.32105 0.33152 -0.01469 -0.05705 -0.01128 39  GLU A CA  
456  C CA  B GLU A 39  ? 0.27785 0.30644 0.31882 -0.01279 -0.06174 -0.00921 39  GLU A CA  
457  C C   A GLU A 39  ? 0.26460 0.27360 0.29822 -0.00968 -0.05324 -0.00558 39  GLU A C   
458  C C   B GLU A 39  ? 0.25466 0.27140 0.29827 -0.00623 -0.05569 -0.00270 39  GLU A C   
459  O O   A GLU A 39  ? 0.26776 0.28898 0.31534 -0.01714 -0.05658 -0.01065 39  GLU A O   
460  O O   B GLU A 39  ? 0.23748 0.26793 0.29891 -0.00980 -0.05956 -0.00499 39  GLU A O   
461  C CB  A GLU A 39  ? 0.29736 0.33255 0.33988 -0.00229 -0.06460 -0.00174 39  GLU A CB  
462  C CB  B GLU A 39  ? 0.28051 0.33457 0.34505 -0.00170 -0.07095 -0.00041 39  GLU A CB  
463  C CG  A GLU A 39  ? 0.28254 0.33026 0.32129 -0.00747 -0.07106 -0.00771 39  GLU A CG  
464  C CG  B GLU A 39  ? 0.35811 0.43810 0.45712 0.00247  -0.07971 0.00375  39  GLU A CG  
465  C CD  A GLU A 39  ? 0.31003 0.37855 0.36586 0.00540  -0.07783 0.00314  39  GLU A CD  
466  C CD  B GLU A 39  ? 0.37984 0.47497 0.48642 -0.01116 -0.08206 -0.00762 39  GLU A CD  
467  O OE1 A GLU A 39  ? 0.36902 0.43515 0.43198 0.01979  -0.07496 0.01628  39  GLU A OE1 
468  O OE1 B GLU A 39  ? 0.25347 0.34722 0.35102 -0.02491 -0.08533 -0.01889 39  GLU A OE1 
469  O OE2 A GLU A 39  ? 0.43000 0.51709 0.49218 0.00094  -0.08592 -0.00128 39  GLU A OE2 
470  O OE2 B GLU A 39  ? 0.39180 0.49380 0.50095 -0.00761 -0.07351 -0.00504 39  GLU A OE2 
471  N N   . ILE A 40  ? 0.34122 0.33254 0.36672 0.00351  -0.04620 0.00503  40  ILE A N   
472  C CA  . ILE A 40  ? 0.29592 0.27570 0.32349 0.00951  -0.04077 0.01082  40  ILE A CA  
473  C C   . ILE A 40  ? 0.32023 0.28466 0.33313 -0.00362 -0.03458 0.00163  40  ILE A C   
474  O O   . ILE A 40  ? 0.31858 0.29029 0.34413 -0.00481 -0.03572 0.00142  40  ILE A O   
475  C CB  . ILE A 40  ? 0.31001 0.26736 0.32351 0.02390  -0.03239 0.02205  40  ILE A CB  
476  C CG1 . ILE A 40  ? 0.29770 0.27485 0.33276 0.03785  -0.03917 0.03325  40  ILE A CG1 
477  C CG2 . ILE A 40  ? 0.34423 0.28310 0.35293 0.02881  -0.02497 0.02677  40  ILE A CG2 
478  C CD1 . ILE A 40  ? 0.36843 0.32568 0.39023 0.05239  -0.03087 0.04486  40  ILE A CD1 
479  N N   A LEU A 41  ? 0.31889 0.26281 0.30574 -0.01377 -0.02838 -0.00629 41  LEU A N   
480  N N   B LEU A 41  ? 0.32295 0.26517 0.30880 -0.01286 -0.02775 -0.00558 41  LEU A N   
481  C CA  A LEU A 41  ? 0.34052 0.26707 0.31325 -0.02562 -0.02132 -0.01330 41  LEU A CA  
482  C CA  B LEU A 41  ? 0.34245 0.26878 0.31463 -0.02574 -0.02135 -0.01346 41  LEU A CA  
483  C C   A LEU A 41  ? 0.34696 0.29624 0.33610 -0.03936 -0.02796 -0.02263 41  LEU A C   
484  C C   B LEU A 41  ? 0.34521 0.29741 0.33798 -0.03708 -0.02883 -0.02105 41  LEU A C   
485  O O   A LEU A 41  ? 0.37672 0.32083 0.36451 -0.04636 -0.02368 -0.02547 41  LEU A O   
486  O O   B LEU A 41  ? 0.26082 0.21397 0.25947 -0.03944 -0.02650 -0.02102 41  LEU A O   
487  C CB  A LEU A 41  ? 0.46092 0.35661 0.40175 -0.03195 -0.01274 -0.01869 41  LEU A CB  
488  C CB  B LEU A 41  ? 0.46260 0.36415 0.40589 -0.03472 -0.01520 -0.02116 41  LEU A CB  
489  C CG  A LEU A 41  ? 0.50814 0.37934 0.43264 -0.04048 -0.00316 -0.02205 41  LEU A CG  
490  C CG  B LEU A 41  ? 0.50369 0.37448 0.42420 -0.04253 -0.00432 -0.02471 41  LEU A CG  
491  C CD1 A LEU A 41  ? 0.47986 0.34134 0.40638 -0.02861 0.00256  -0.01146 41  LEU A CD1 
492  C CD1 B LEU A 41  ? 0.48743 0.34259 0.40469 -0.03084 0.00317  -0.01425 41  LEU A CD1 
493  C CD2 A LEU A 41  ? 0.43847 0.27889 0.33286 -0.04633 0.00424  -0.02772 41  LEU A CD2 
494  C CD2 B LEU A 41  ? 0.43238 0.27777 0.32511 -0.04656 0.00059  -0.03043 41  LEU A CD2 
495  N N   . ILE A 42  ? 0.32322 0.29824 0.32821 -0.04289 -0.03818 -0.02696 42  ILE A N   
496  C CA  . ILE A 42  ? 0.31325 0.31460 0.33872 -0.05376 -0.04583 -0.03472 42  ILE A CA  
497  C C   . ILE A 42  ? 0.28107 0.30024 0.33025 -0.04587 -0.04962 -0.02900 42  ILE A C   
498  O O   . ILE A 42  ? 0.33197 0.35881 0.38828 -0.05343 -0.04933 -0.03371 42  ILE A O   
499  C CB  . ILE A 42  ? 0.38324 0.40851 0.42119 -0.05760 -0.05657 -0.03976 42  ILE A CB  
500  C CG1 . ILE A 42  ? 0.43573 0.44540 0.45090 -0.06882 -0.05387 -0.04881 42  ILE A CG1 
501  C CG2 . ILE A 42  ? 0.38063 0.43771 0.44561 -0.06528 -0.06587 -0.04573 42  ILE A CG2 
502  C CD1 . ILE A 42  ? 0.58319 0.61195 0.60554 -0.06957 -0.06363 -0.05220 42  ILE A CD1 
503  N N   A LEU A 43  ? 0.25440 0.28065 0.31648 -0.03031 -0.05333 -0.01881 43  LEU A N   
504  N N   B LEU A 43  ? 0.25423 0.28142 0.31704 -0.03031 -0.05370 -0.01887 43  LEU A N   
505  C CA  A LEU A 43  ? 0.25806 0.30126 0.34374 -0.02181 -0.05834 -0.01385 43  LEU A CA  
506  C CA  B LEU A 43  ? 0.25981 0.30191 0.34486 -0.02143 -0.05793 -0.01351 43  LEU A CA  
507  C C   A LEU A 43  ? 0.26239 0.28448 0.33607 -0.01792 -0.04897 -0.00989 43  LEU A C   
508  C C   B LEU A 43  ? 0.27664 0.29756 0.34758 -0.02133 -0.04803 -0.01205 43  LEU A C   
509  O O   A LEU A 43  ? 0.23413 0.26888 0.32322 -0.01513 -0.05204 -0.00946 43  LEU A O   
510  O O   B LEU A 43  ? 0.18751 0.21913 0.26798 -0.02558 -0.04924 -0.01581 43  LEU A O   
511  C CB  A LEU A 43  ? 0.27054 0.32892 0.37667 -0.00679 -0.06628 -0.00410 43  LEU A CB  
512  C CB  B LEU A 43  ? 0.17967 0.22931 0.28022 -0.00436 -0.06299 -0.00191 43  LEU A CB  
513  C CG  A LEU A 43  ? 0.17672 0.25787 0.29373 -0.00927 -0.07341 -0.00675 43  LEU A CG  
514  C CG  B LEU A 43  ? 0.26880 0.34405 0.38826 -0.00117 -0.07236 -0.00061 43  LEU A CG  
515  C CD1 A LEU A 43  ? 0.25966 0.34243 0.37479 0.00485  -0.06782 0.00354  43  LEU A CD1 
516  C CD1 B LEU A 43  ? 0.27977 0.34865 0.39556 0.01411  -0.06628 0.01107  43  LEU A CD1 
517  C CD2 A LEU A 43  ? 0.20362 0.29944 0.31590 -0.01606 -0.06699 -0.01209 43  LEU A CD2 
518  C CD2 B LEU A 43  ? 0.21470 0.30516 0.32922 -0.00469 -0.06490 -0.00467 43  LEU A CD2 
519  N N   A GLU A 44  ? 0.28073 0.27095 0.32691 -0.01736 -0.03779 -0.00726 44  GLU A N   
520  N N   B GLU A 44  ? 0.28772 0.27838 0.33516 -0.01624 -0.03791 -0.00653 44  GLU A N   
521  C CA  A GLU A 44  ? 0.27752 0.24679 0.31073 -0.01534 -0.02844 -0.00421 44  GLU A CA  
522  C CA  B GLU A 44  ? 0.27850 0.24656 0.31061 -0.01570 -0.02791 -0.00434 44  GLU A CA  
523  C C   A GLU A 44  ? 0.30734 0.27365 0.33223 -0.03099 -0.02402 -0.01338 44  GLU A C   
524  C C   B GLU A 44  ? 0.30660 0.27622 0.33418 -0.03124 -0.02502 -0.01377 44  GLU A C   
525  O O   A GLU A 44  ? 0.31468 0.27625 0.33839 -0.03029 -0.01956 -0.01189 44  GLU A O   
526  O O   B GLU A 44  ? 0.28698 0.26031 0.32013 -0.03050 -0.02346 -0.01310 44  GLU A O   
527  C CB  A GLU A 44  ? 0.36199 0.29791 0.36915 -0.00941 -0.01800 0.00171  44  GLU A CB  
528  C CB  B GLU A 44  ? 0.37341 0.30714 0.37687 -0.01276 -0.01706 -0.00036 44  GLU A CB  
529  C CG  A GLU A 44  ? 0.42492 0.36020 0.43964 0.00808  -0.01977 0.01320  44  GLU A CG  
530  C CG  B GLU A 44  ? 0.33029 0.26064 0.33617 0.00287  -0.01820 0.00977  44  GLU A CG  
531  C CD  A GLU A 44  ? 0.53183 0.47559 0.56441 0.01941  -0.02266 0.02024  44  GLU A CD  
532  C CD  B GLU A 44  ? 0.52214 0.41769 0.50043 0.00801  -0.00652 0.01471  44  GLU A CD  
533  O OE1 A GLU A 44  ? 0.49931 0.42926 0.52202 0.01800  -0.01616 0.02007  44  GLU A OE1 
534  O OE1 B GLU A 44  ? 0.41944 0.29720 0.37540 -0.00004 -0.00117 0.00905  44  GLU A OE1 
535  O OE2 A GLU A 44  ? 0.50660 0.47119 0.56365 0.02977  -0.03186 0.02590  44  GLU A OE2 
536  O OE2 B GLU A 44  ? 0.54237 0.42817 0.52160 0.02040  -0.00306 0.02397  44  GLU A OE2 
537  N N   A LEU A 45  ? 0.31539 0.28489 0.33490 -0.04497 -0.02526 -0.02260 45  LEU A N   
538  N N   B LEU A 45  ? 0.31667 0.28519 0.33540 -0.04519 -0.02482 -0.02262 45  LEU A N   
539  C CA  A LEU A 45  ? 0.31305 0.28332 0.32858 -0.06086 -0.02203 -0.03134 45  LEU A CA  
540  C CA  B LEU A 45  ? 0.31416 0.28416 0.32942 -0.06114 -0.02185 -0.03146 45  LEU A CA  
541  C C   A LEU A 45  ? 0.32012 0.32312 0.36211 -0.06279 -0.03039 -0.03462 45  LEU A C   
542  C C   B LEU A 45  ? 0.32006 0.32322 0.36203 -0.06315 -0.03041 -0.03485 45  LEU A C   
543  O O   A LEU A 45  ? 0.33043 0.33499 0.37244 -0.06950 -0.02632 -0.03739 45  LEU A O   
544  O O   B LEU A 45  ? 0.33226 0.33748 0.37448 -0.07027 -0.02651 -0.03789 45  LEU A O   
545  C CB  A LEU A 45  ? 0.35204 0.31620 0.35546 -0.07492 -0.02186 -0.04047 45  LEU A CB  
546  C CB  B LEU A 45  ? 0.35199 0.31546 0.35489 -0.07491 -0.02162 -0.04041 45  LEU A CB  
547  C CG  A LEU A 45  ? 0.36968 0.29729 0.34277 -0.07888 -0.01114 -0.04097 45  LEU A CG  
548  C CG  B LEU A 45  ? 0.37693 0.33179 0.37025 -0.09193 -0.01556 -0.04836 45  LEU A CG  
549  C CD1 A LEU A 45  ? 0.36694 0.29197 0.33103 -0.08956 -0.01407 -0.05000 45  LEU A CD1 
550  C CD1 B LEU A 45  ? 0.38519 0.30796 0.35677 -0.09099 -0.00278 -0.04361 45  LEU A CD1 
551  C CD2 A LEU A 45  ? 0.43550 0.34652 0.39766 -0.08770 -0.00145 -0.04223 45  LEU A CD2 
552  C CD2 B LEU A 45  ? 0.40608 0.35724 0.39060 -0.10500 -0.01767 -0.05792 45  LEU A CD2 
553  N N   . ILE A 46  ? 0.26621 0.29582 0.33101 -0.05677 -0.04201 -0.03422 46  ILE A N   
554  C CA  . ILE A 46  ? 0.23790 0.29864 0.32919 -0.05603 -0.05076 -0.03682 46  ILE A CA  
555  C C   . ILE A 46  ? 0.27112 0.32903 0.36612 -0.04505 -0.04801 -0.03041 46  ILE A C   
556  O O   . ILE A 46  ? 0.26029 0.32927 0.36205 -0.04875 -0.04760 -0.03385 46  ILE A O   
557  C CB  . ILE A 46  ? 0.25315 0.33776 0.36105 -0.04890 -0.06049 -0.03396 46  ILE A CB  
558  C CG1 . ILE A 46  ? 0.28465 0.37086 0.38171 -0.05998 -0.06085 -0.03716 46  ILE A CG1 
559  C CG2 . ILE A 46  ? 0.33275 0.43292 0.44283 -0.04067 -0.05831 -0.02680 46  ILE A CG2 
560  C CD1 . ILE A 46  ? 0.42987 0.52864 0.52797 -0.05189 -0.06291 -0.02987 46  ILE A CD1 
561  N N   . VAL A 47  ? 0.22506 0.26823 0.31541 -0.03098 -0.04602 -0.02090 47  VAL A N   
562  C CA  . VAL A 47  ? 0.24627 0.28393 0.33821 -0.01979 -0.04336 -0.01458 47  VAL A CA  
563  C C   . VAL A 47  ? 0.29654 0.31463 0.36738 -0.02813 -0.03146 -0.01662 47  VAL A C   
564  O O   . VAL A 47  ? 0.28573 0.31116 0.36205 -0.02557 -0.03088 -0.01655 47  VAL A O   
565  C CB  . VAL A 47  ? 0.24362 0.26575 0.33234 -0.00411 -0.04225 -0.00375 47  VAL A CB  
566  C CG1 . VAL A 47  ? 0.29084 0.29935 0.37381 0.00579  -0.03681 0.00245  47  VAL A CG1 
567  C CG2 . VAL A 47  ? 0.22022 0.26674 0.33647 0.00614  -0.05519 -0.00019 47  VAL A CG2 
568  N N   A GLN A 48  ? 0.27466 0.26839 0.32159 -0.03835 -0.02208 -0.01869 48  GLN A N   
569  N N   B GLN A 48  ? 0.27543 0.26845 0.32202 -0.03789 -0.02200 -0.01838 48  GLN A N   
570  C CA  A GLN A 48  ? 0.32942 0.30399 0.35741 -0.04688 -0.01063 -0.01994 48  GLN A CA  
571  C CA  B GLN A 48  ? 0.32640 0.29758 0.35209 -0.04637 -0.00999 -0.01935 48  GLN A CA  
572  C C   A GLN A 48  ? 0.35196 0.34831 0.39123 -0.05831 -0.01248 -0.02751 48  GLN A C   
573  C C   B GLN A 48  ? 0.36381 0.35334 0.39774 -0.05935 -0.01053 -0.02718 48  GLN A C   
574  O O   A GLN A 48  ? 0.35776 0.35130 0.39289 -0.05877 -0.00655 -0.02612 48  GLN A O   
575  O O   B GLN A 48  ? 0.33628 0.31623 0.36038 -0.06318 -0.00217 -0.02633 48  GLN A O   
576  C CB  A GLN A 48  ? 0.36381 0.30808 0.36568 -0.05615 -0.00120 -0.02142 48  GLN A CB  
577  C CB  B GLN A 48  ? 0.38537 0.32702 0.38587 -0.05434 -0.00156 -0.02055 48  GLN A CB  
578  C CG  A GLN A 48  ? 0.41404 0.32992 0.39873 -0.04435 0.00499  -0.01275 48  GLN A CG  
579  C CG  B GLN A 48  ? 0.40272 0.32168 0.39062 -0.04129 0.00195  -0.01208 48  GLN A CG  
580  C CD  A GLN A 48  ? 0.44059 0.32176 0.39680 -0.05233 0.01754  -0.01308 48  GLN A CD  
581  C CD  B GLN A 48  ? 0.44242 0.33502 0.40693 -0.04765 0.00833  -0.01429 48  GLN A CD  
582  O OE1 A GLN A 48  ? 0.44881 0.30940 0.38930 -0.05102 0.02081  -0.01217 48  GLN A OE1 
583  O OE1 B GLN A 48  ? 0.41478 0.30739 0.37906 -0.04229 0.00447  -0.01305 48  GLN A OE1 
584  N NE2 A GLN A 48  ? 0.42118 0.29539 0.37062 -0.05990 0.02475  -0.01398 48  GLN A NE2 
585  N NE2 B GLN A 48  ? 0.38178 0.25175 0.32667 -0.05863 0.01804  -0.01739 48  GLN A NE2 
586  N N   A ILE A 49  ? 0.31007 0.32848 0.36332 -0.06744 -0.02034 -0.03529 49  ILE A N   
587  N N   B ILE A 49  ? 0.31390 0.32962 0.36555 -0.06631 -0.01982 -0.03444 49  ILE A N   
588  C CA  A ILE A 49  ? 0.35876 0.39920 0.42390 -0.07836 -0.02209 -0.04255 49  ILE A CA  
589  C CA  B ILE A 49  ? 0.35833 0.39563 0.42155 -0.07705 -0.02136 -0.04153 49  ILE A CA  
590  C C   A ILE A 49  ? 0.33175 0.39320 0.41422 -0.06769 -0.02681 -0.04028 49  ILE A C   
591  C C   B ILE A 49  ? 0.33525 0.39142 0.41423 -0.06618 -0.02527 -0.03879 49  ILE A C   
592  O O   A ILE A 49  ? 0.32821 0.39559 0.41046 -0.07239 -0.02222 -0.04216 49  ILE A O   
593  O O   B ILE A 49  ? 0.32479 0.38068 0.39934 -0.06934 -0.01886 -0.03899 49  ILE A O   
594  C CB  A ILE A 49  ? 0.37329 0.43491 0.45206 -0.08883 -0.03089 -0.05119 49  ILE A CB  
595  C CB  B ILE A 49  ? 0.36717 0.42839 0.44642 -0.08629 -0.03113 -0.04996 49  ILE A CB  
596  C CG1 A ILE A 49  ? 0.37268 0.41167 0.43158 -0.10078 -0.02534 -0.05477 49  ILE A CG1 
597  C CG1 B ILE A 49  ? 0.36938 0.41122 0.43111 -0.09823 -0.02698 -0.05404 49  ILE A CG1 
598  C CG2 A ILE A 49  ? 0.35382 0.43684 0.44493 -0.09356 -0.03320 -0.05467 49  ILE A CG2 
599  C CG2 B ILE A 49  ? 0.34157 0.42535 0.43392 -0.09193 -0.03345 -0.05422 49  ILE A CG2 
600  C CD1 A ILE A 49  ? 0.37168 0.42424 0.43891 -0.10391 -0.03395 -0.05911 49  ILE A CD1 
601  C CD1 B ILE A 49  ? 0.35338 0.41149 0.42614 -0.09894 -0.03696 -0.05733 49  ILE A CD1 
602  N N   . ILE A 50  ? 0.25276 0.32555 0.35055 -0.05273 -0.03602 -0.03603 50  ILE A N   
603  C CA  A ILE A 50  ? 0.25492 0.34711 0.36988 -0.04132 -0.04195 -0.03450 50  ILE A CA  
604  C CA  B ILE A 50  ? 0.25659 0.34882 0.37161 -0.04129 -0.04199 -0.03450 50  ILE A CA  
605  C C   . ILE A 50  ? 0.30854 0.37997 0.40735 -0.03350 -0.03261 -0.02776 50  ILE A C   
606  O O   . ILE A 50  ? 0.26738 0.34834 0.36898 -0.03179 -0.03103 -0.02879 50  ILE A O   
607  C CB  A ILE A 50  ? 0.24223 0.34898 0.37489 -0.02734 -0.05337 -0.03021 50  ILE A CB  
608  C CB  B ILE A 50  ? 0.23992 0.34615 0.37266 -0.02744 -0.05344 -0.03025 50  ILE A CB  
609  C CG1 A ILE A 50  ? 0.25743 0.37189 0.38022 -0.03195 -0.05299 -0.02674 50  ILE A CG1 
610  C CG1 B ILE A 50  ? 0.23643 0.34512 0.36006 -0.03338 -0.05356 -0.02855 50  ILE A CG1 
611  C CG2 A ILE A 50  ? 0.20056 0.31100 0.33429 -0.01267 -0.05363 -0.02416 50  ILE A CG2 
612  C CG2 B ILE A 50  ? 0.28346 0.39868 0.41315 -0.01687 -0.05284 -0.02418 50  ILE A CG2 
613  C CD1 A ILE A 50  ? 0.33184 0.44532 0.44940 -0.02269 -0.05321 -0.01909 50  ILE A CD1 
614  C CD1 B ILE A 50  ? 0.20695 0.31226 0.32834 -0.02239 -0.05485 -0.02150 50  ILE A CD1 
615  N N   A GLU A 51  ? 0.24504 0.28738 0.32593 -0.02782 -0.02604 -0.02043 51  GLU A N   
616  N N   B GLU A 51  ? 0.24415 0.28713 0.32585 -0.02735 -0.02651 -0.02035 51  GLU A N   
617  N N   C GLU A 51  ? 0.24412 0.28376 0.31941 -0.03550 -0.02274 -0.02303 51  GLU A N   
618  C CA  A GLU A 51  ? 0.28148 0.30218 0.34595 -0.02020 -0.01696 -0.01355 51  GLU A CA  
619  C CA  B GLU A 51  ? 0.28432 0.30305 0.34737 -0.02089 -0.01646 -0.01349 51  GLU A CA  
620  C CA  C GLU A 51  ? 0.33680 0.35150 0.39378 -0.02797 -0.01303 -0.01553 51  GLU A CA  
621  C C   A GLU A 51  ? 0.32052 0.33301 0.36953 -0.03230 -0.00591 -0.01613 51  GLU A C   
622  C C   B GLU A 51  ? 0.31917 0.33019 0.36717 -0.03346 -0.00561 -0.01637 51  GLU A C   
623  C C   C GLU A 51  ? 0.34257 0.34591 0.38271 -0.03943 -0.00122 -0.01715 51  GLU A C   
624  O O   A GLU A 51  ? 0.27947 0.29410 0.32667 -0.02686 -0.00273 -0.01380 51  GLU A O   
625  O O   B GLU A 51  ? 0.29027 0.30146 0.33503 -0.02830 -0.00170 -0.01373 51  GLU A O   
626  O O   C GLU A 51  ? 0.32684 0.33143 0.36482 -0.03376 0.00227  -0.01431 51  GLU A O   
627  C CB  A GLU A 51  ? 0.31868 0.30836 0.36513 -0.01437 -0.01080 -0.00603 51  GLU A CB  
628  C CB  B GLU A 51  ? 0.31391 0.30189 0.35862 -0.01689 -0.01033 -0.00683 51  GLU A CB  
629  C CB  C GLU A 51  ? 0.33544 0.32109 0.37596 -0.02271 -0.00816 -0.00889 51  GLU A CB  
630  C CG  A GLU A 51  ? 0.33040 0.29646 0.35927 -0.00669 -0.00130 0.00123  51  GLU A CG  
631  C CG  B GLU A 51  ? 0.32067 0.27962 0.34369 -0.01109 0.00091  0.00054  51  GLU A CG  
632  C CG  C GLU A 51  ? 0.28533 0.27605 0.33944 -0.00517 -0.01635 -0.00233 51  GLU A CG  
633  C CD  A GLU A 51  ? 0.33990 0.27148 0.34616 -0.00451 0.00774  0.00759  51  GLU A CD  
634  C CD  B GLU A 51  ? 0.32201 0.25000 0.32586 -0.00841 0.00761  0.00619  51  GLU A CD  
635  C CD  C GLU A 51  ? 0.37979 0.36979 0.43613 0.00793  -0.01606 0.00299  51  GLU A CD  
636  O OE1 A GLU A 51  ? 0.30613 0.22764 0.30425 -0.01241 0.00961  0.00523  51  GLU A OE1 
637  O OE1 B GLU A 51  ? 0.35755 0.28178 0.35783 -0.01581 0.00696  0.00287  51  GLU A OE1 
638  O OE1 C GLU A 51  ? 0.38296 0.34615 0.41887 0.01145  -0.00607 0.00895  51  GLU A OE1 
639  O OE2 A GLU A 51  ? 0.27123 0.18532 0.26711 0.00554  0.01306  0.01478  51  GLU A OE2 
640  O OE2 B GLU A 51  ? 0.29173 0.19918 0.28367 0.00163  0.01343  0.01382  51  GLU A OE2 
641  O OE2 C GLU A 51  ? 0.40134 0.41732 0.47969 0.01507  -0.02616 0.00096  51  GLU A OE2 
642  N N   A PHE A 52  ? 0.32943 0.33287 0.36771 -0.04860 -0.00017 -0.02082 52  PHE A N   
643  N N   B PHE A 52  ? 0.33324 0.33837 0.37279 -0.04997 -0.00100 -0.02176 52  PHE A N   
644  C CA  A PHE A 52  ? 0.35965 0.35354 0.38398 -0.06142 0.01091  -0.02250 52  PHE A CA  
645  C CA  B PHE A 52  ? 0.35772 0.35225 0.38272 -0.06312 0.01023  -0.02349 52  PHE A CA  
646  C C   A PHE A 52  ? 0.35193 0.37488 0.39173 -0.06377 0.00801  -0.02678 52  PHE A C   
647  C C   B PHE A 52  ? 0.34337 0.36660 0.38349 -0.06680 0.00770  -0.02812 52  PHE A C   
648  O O   A PHE A 52  ? 0.34848 0.36676 0.37958 -0.06349 0.01611  -0.02371 52  PHE A O   
649  O O   B PHE A 52  ? 0.36955 0.38688 0.39977 -0.07060 0.01699  -0.02612 52  PHE A O   
650  C CB  A PHE A 52  ? 0.41165 0.39374 0.42616 -0.07863 0.01504  -0.02791 52  PHE A CB  
651  C CB  B PHE A 52  ? 0.39423 0.37530 0.40846 -0.07964 0.01442  -0.02856 52  PHE A CB  
652  C CG  A PHE A 52  ? 0.45646 0.42321 0.45557 -0.09211 0.02731  -0.02827 52  PHE A CG  
653  C CG  B PHE A 52  ? 0.39647 0.34597 0.38612 -0.08794 0.02841  -0.02548 52  PHE A CG  
654  C CD1 A PHE A 52  ? 0.40143 0.33665 0.37826 -0.08958 0.03883  -0.02102 52  PHE A CD1 
655  C CD1 B PHE A 52  ? 0.46610 0.41804 0.45293 -0.09750 0.03606  -0.02619 52  PHE A CD1 
656  C CD2 A PHE A 52  ? 0.36300 0.34703 0.37099 -0.10737 0.02735  -0.03543 52  PHE A CD2 
657  C CD2 B PHE A 52  ? 0.49608 0.41375 0.46604 -0.08584 0.03402  -0.02153 52  PHE A CD2 
658  C CE1 A PHE A 52  ? 0.48840 0.40946 0.45241 -0.10221 0.05015  -0.02055 52  PHE A CE1 
659  C CE1 B PHE A 52  ? 0.50716 0.42982 0.47277 -0.10528 0.04882  -0.02264 52  PHE A CE1 
660  C CE2 A PHE A 52  ? 0.37357 0.34389 0.36932 -0.12020 0.03880  -0.03493 52  PHE A CE2 
661  C CE2 B PHE A 52  ? 0.52203 0.41009 0.47030 -0.09329 0.04634  -0.01883 52  PHE A CE2 
662  C CZ  A PHE A 52  ? 0.34162 0.28032 0.31553 -0.11773 0.05017  -0.02735 52  PHE A CZ  
663  C CZ  B PHE A 52  ? 0.65822 0.54842 0.60466 -0.10324 0.05368  -0.01917 52  PHE A CZ  
664  N N   A ILE A 53  ? 0.29652 0.34977 0.35885 -0.06623 -0.00317 -0.03383 53  ILE A N   
665  N N   B ILE A 53  ? 0.30281 0.35735 0.36674 -0.06600 -0.00443 -0.03419 53  ILE A N   
666  C CA  A ILE A 53  ? 0.35591 0.43933 0.43490 -0.06693 -0.00717 -0.03848 53  ILE A CA  
667  C CA  B ILE A 53  ? 0.35463 0.43849 0.43457 -0.06640 -0.00806 -0.03855 53  ILE A CA  
668  C C   A ILE A 53  ? 0.31666 0.40369 0.39704 -0.05053 -0.00780 -0.03326 53  ILE A C   
669  C C   B ILE A 53  ? 0.31145 0.39512 0.38953 -0.05102 -0.00676 -0.03275 53  ILE A C   
670  O O   A ILE A 53  ? 0.29444 0.39028 0.37334 -0.05119 -0.00293 -0.03357 53  ILE A O   
671  O O   B ILE A 53  ? 0.28145 0.36840 0.35396 -0.05295 0.00028  -0.03214 53  ILE A O   
672  C CB  A ILE A 53  ? 0.28260 0.39737 0.38718 -0.06888 -0.02098 -0.04622 53  ILE A CB  
673  C CB  B ILE A 53  ? 0.30697 0.42333 0.41388 -0.06530 -0.02282 -0.04551 53  ILE A CB  
674  C CG1 A ILE A 53  ? 0.39088 0.50406 0.49354 -0.08645 -0.01996 -0.05236 53  ILE A CG1 
675  C CG1 B ILE A 53  ? 0.36755 0.48805 0.47688 -0.08200 -0.02398 -0.05243 53  ILE A CG1 
676  C CG2 A ILE A 53  ? 0.31641 0.46329 0.43954 -0.06634 -0.02634 -0.05092 53  ILE A CG2 
677  C CG2 B ILE A 53  ? 0.32130 0.46806 0.44584 -0.06058 -0.02813 -0.04932 53  ILE A CG2 
678  C CD1 A ILE A 53  ? 0.31318 0.44086 0.42977 -0.08055 -0.03236 -0.05254 53  ILE A CD1 
679  C CD1 B ILE A 53  ? 0.25955 0.39096 0.38083 -0.07206 -0.03651 -0.04966 53  ILE A CD1 
680  N N   . PHE A 54  ? 0.25387 0.33407 0.33698 -0.03520 -0.01370 -0.02817 54  PHE A N   
681  C CA  . PHE A 54  ? 0.29719 0.37775 0.38032 -0.01905 -0.01460 -0.02314 54  PHE A CA  
682  C C   . PHE A 54  ? 0.31880 0.37338 0.37635 -0.02027 0.00008  -0.01687 54  PHE A C   
683  O O   . PHE A 54  ? 0.28826 0.35036 0.34404 -0.01466 0.00274  -0.01575 54  PHE A O   
684  C CB  . PHE A 54  ? 0.30997 0.38514 0.40070 -0.00297 -0.02308 -0.01799 54  PHE A CB  
685  C CG  . PHE A 54  ? 0.29279 0.36188 0.37952 0.01321  -0.02261 -0.01213 54  PHE A CG  
686  C CD1 . PHE A 54  ? 0.29557 0.39033 0.39967 0.02338  -0.03180 -0.01551 54  PHE A CD1 
687  C CD2 . PHE A 54  ? 0.29506 0.33274 0.35986 0.01803  -0.01288 -0.00380 54  PHE A CD2 
688  C CE1 . PHE A 54  ? 0.27189 0.36103 0.37146 0.03843  -0.03183 -0.01080 54  PHE A CE1 
689  C CE2 . PHE A 54  ? 0.32038 0.35209 0.38056 0.03248  -0.01233 0.00144  54  PHE A CE2 
690  C CZ  . PHE A 54  ? 0.33995 0.39770 0.41745 0.04296  -0.02206 -0.00217 54  PHE A CZ  
691  N N   A TYR A 55  ? 0.27524 0.29900 0.31264 -0.02666 0.00947  -0.01257 55  TYR A N   
692  N N   B TYR A 55  ? 0.27499 0.29892 0.31218 -0.02732 0.00977  -0.01275 55  TYR A N   
693  C CA  A TYR A 55  ? 0.32164 0.31872 0.33493 -0.02739 0.02327  -0.00587 55  TYR A CA  
694  C CA  B TYR A 55  ? 0.32158 0.31880 0.33485 -0.02706 0.02330  -0.00576 55  TYR A CA  
695  C C   A TYR A 55  ? 0.26881 0.27387 0.27781 -0.03996 0.03160  -0.00851 55  TYR A C   
696  C C   B TYR A 55  ? 0.29210 0.29238 0.29803 -0.04133 0.03317  -0.00795 55  TYR A C   
697  O O   A TYR A 55  ? 0.28580 0.28708 0.28523 -0.03512 0.03861  -0.00391 55  TYR A O   
698  O O   B TYR A 55  ? 0.32403 0.31156 0.31498 -0.03914 0.04303  -0.00222 55  TYR A O   
699  C CB  A TYR A 55  ? 0.33503 0.29741 0.32848 -0.03173 0.03105  -0.00141 55  TYR A CB  
700  C CB  B TYR A 55  ? 0.33125 0.29336 0.32538 -0.02714 0.02994  0.00002  55  TYR A CB  
701  C CG  A TYR A 55  ? 0.32335 0.27069 0.31362 -0.01495 0.02803  0.00564  55  TYR A CG  
702  C CG  B TYR A 55  ? 0.26721 0.22171 0.26372 -0.00884 0.02423  0.00615  55  TYR A CG  
703  C CD1 A TYR A 55  ? 0.25456 0.21110 0.25997 -0.00773 0.01705  0.00469  55  TYR A CD1 
704  C CD1 B TYR A 55  ? 0.28268 0.22090 0.26661 0.00277  0.02974  0.01379  55  TYR A CD1 
705  C CD2 A TYR A 55  ? 0.31972 0.24457 0.29290 -0.00608 0.03613  0.01374  55  TYR A CD2 
706  C CD2 B TYR A 55  ? 0.29045 0.25507 0.30291 -0.00300 0.01316  0.00469  55  TYR A CD2 
707  C CE1 A TYR A 55  ? 0.27994 0.22395 0.28444 0.00772  0.01442  0.01180  55  TYR A CE1 
708  C CE1 B TYR A 55  ? 0.30151 0.23348 0.28904 0.01923  0.02429  0.01935  55  TYR A CE1 
709  C CE2 A TYR A 55  ? 0.31724 0.22927 0.28886 0.00933  0.03320  0.02024  55  TYR A CE2 
710  C CE2 B TYR A 55  ? 0.25259 0.21119 0.26932 0.01361  0.00804  0.01097  55  TYR A CE2 
711  C CZ  A TYR A 55  ? 0.35510 0.27688 0.34284 0.01609  0.02244  0.01932  55  TYR A CZ  
712  C CZ  B TYR A 55  ? 0.25075 0.19309 0.25534 0.02459  0.01348  0.01806  55  TYR A CZ  
713  O OH  A TYR A 55  ? 0.43138 0.34084 0.41910 0.03143  0.01977  0.02649  55  TYR A OH  
714  O OH  B TYR A 55  ? 0.26640 0.20265 0.27624 0.04095  0.00821  0.02436  55  TYR A OH  
715  N N   . ILE A 56  ? 0.36147 0.37870 0.37814 -0.05587 0.03087  -0.01563 56  ILE A N   
716  C CA  . ILE A 56  ? 0.37760 0.40376 0.39235 -0.06855 0.03901  -0.01771 56  ILE A CA  
717  C C   . ILE A 56  ? 0.30268 0.35781 0.33028 -0.05918 0.03481  -0.01906 56  ILE A C   
718  O O   . ILE A 56  ? 0.35071 0.40397 0.36844 -0.05862 0.04404  -0.01489 56  ILE A O   
719  C CB  . ILE A 56  ? 0.37716 0.41311 0.40059 -0.08692 0.03743  -0.02570 56  ILE A CB  
720  C CG1 . ILE A 56  ? 0.42893 0.43339 0.43619 -0.09643 0.04286  -0.02461 56  ILE A CG1 
721  C CG2 . ILE A 56  ? 0.37283 0.42458 0.39972 -0.09864 0.04433  -0.02788 56  ILE A CG2 
722  C CD1 . ILE A 56  ? 0.48157 0.45071 0.46346 -0.09591 0.05652  -0.01586 56  ILE A CD1 
723  N N   . TRP A 57  ? 0.28087 0.36322 0.33062 -0.05108 0.02067  -0.02479 57  TRP A N   
724  C CA  . TRP A 57  ? 0.27500 0.38394 0.33739 -0.03885 0.01457  -0.02663 57  TRP A CA  
725  C C   . TRP A 57  ? 0.33555 0.42888 0.38291 -0.02378 0.01957  -0.01853 57  TRP A C   
726  O O   . TRP A 57  ? 0.33991 0.44389 0.38414 -0.01920 0.02373  -0.01742 57  TRP A O   
727  C CB  . TRP A 57  ? 0.26978 0.40275 0.35704 -0.02954 -0.00253 -0.03253 57  TRP A CB  
728  C CG  . TRP A 57  ? 0.26877 0.42662 0.36922 -0.01452 -0.01056 -0.03480 57  TRP A CG  
729  C CD1 . TRP A 57  ? 0.46075 0.64988 0.57608 -0.01643 -0.01455 -0.04181 57  TRP A CD1 
730  C CD2 . TRP A 57  ? 0.24575 0.39888 0.34497 0.00497  -0.01539 -0.03037 57  TRP A CD2 
731  N NE1 . TRP A 57  ? 0.38465 0.58875 0.50762 0.00097  -0.02191 -0.04253 57  TRP A NE1 
732  C CE2 . TRP A 57  ? 0.38662 0.56916 0.50028 0.01419  -0.02289 -0.03573 57  TRP A CE2 
733  C CE3 . TRP A 57  ? 0.30700 0.43454 0.39513 0.01575  -0.01457 -0.02276 57  TRP A CE3 
734  C CZ2 . TRP A 57  ? 0.33414 0.52059 0.45106 0.03365  -0.03003 -0.03414 57  TRP A CZ2 
735  C CZ3 . TRP A 57  ? 0.30963 0.44161 0.40206 0.03506  -0.02161 -0.02065 57  TRP A CZ3 
736  C CH2 . TRP A 57  ? 0.33870 0.49967 0.44521 0.04362  -0.02943 -0.02658 57  TRP A CH2 
737  N N   . LEU A 58  ? 0.30049 0.36925 0.33856 -0.01524 0.01901  -0.01272 58  LEU A N   
738  C CA  . LEU A 58  ? 0.32130 0.37460 0.34591 -0.00012 0.02264  -0.00503 58  LEU A CA  
739  C C   . LEU A 58  ? 0.37135 0.40733 0.37326 -0.00657 0.03874  0.00095  58  LEU A C   
740  O O   . LEU A 58  ? 0.39595 0.43764 0.39246 0.00301  0.04152  0.00392  58  LEU A O   
741  C CB  . LEU A 58  ? 0.33503 0.36379 0.35387 0.00860  0.02013  0.00050  58  LEU A CB  
742  C CG  . LEU A 58  ? 0.36449 0.37420 0.36879 0.02415  0.02392  0.00895  58  LEU A CG  
743  C CD1 . LEU A 58  ? 0.39971 0.43388 0.41866 0.04072  0.01319  0.00657  58  LEU A CD1 
744  C CD2 . LEU A 58  ? 0.41367 0.39796 0.41199 0.03099  0.02284  0.01475  58  LEU A CD2 
745  N N   A ILE A 59  ? 0.36609 0.37994 0.35419 -0.02220 0.04936  0.00309  59  ILE A N   
746  N N   B ILE A 59  ? 0.36653 0.38108 0.35496 -0.02247 0.04934  0.00292  59  ILE A N   
747  C CA  A ILE A 59  ? 0.45058 0.44497 0.41728 -0.02749 0.06477  0.01023  59  ILE A CA  
748  C CA  B ILE A 59  ? 0.44834 0.44439 0.41589 -0.02863 0.06482  0.00973  59  ILE A CA  
749  C C   A ILE A 59  ? 0.38996 0.40824 0.36195 -0.03477 0.06935  0.00766  59  ILE A C   
750  C C   B ILE A 59  ? 0.39767 0.41969 0.37147 -0.03354 0.06834  0.00715  59  ILE A C   
751  O O   A ILE A 59  ? 0.47736 0.48963 0.43569 -0.03261 0.07963  0.01406  59  ILE A O   
752  O O   B ILE A 59  ? 0.43670 0.45507 0.39802 -0.02875 0.07711  0.01330  59  ILE A O   
753  C CB  A ILE A 59  ? 0.51192 0.47238 0.46111 -0.04056 0.07514  0.01410  59  ILE A CB  
754  C CB  B ILE A 59  ? 0.49895 0.46512 0.45155 -0.04446 0.07488  0.01218  59  ILE A CB  
755  C CG1 A ILE A 59  ? 0.36077 0.32825 0.32060 -0.05727 0.07188  0.00618  59  ILE A CG1 
756  C CG1 B ILE A 59  ? 0.45264 0.43324 0.41715 -0.06303 0.07373  0.00417  59  ILE A CG1 
757  C CG2 A ILE A 59  ? 0.39036 0.32315 0.32806 -0.02913 0.07422  0.01986  59  ILE A CG2 
758  C CG2 B ILE A 59  ? 0.43259 0.37379 0.37825 -0.03781 0.07156  0.01484  59  ILE A CG2 
759  C CD1 A ILE A 59  ? 0.55292 0.48837 0.49572 -0.07116 0.08204  0.00873  59  ILE A CD1 
760  C CD1 B ILE A 59  ? 0.44329 0.39571 0.39350 -0.07932 0.08358  0.00572  59  ILE A CD1 
761  N N   A ILE A 60  ? 0.38677 0.43324 0.37879 -0.04274 0.06195  -0.00127 60  ILE A N   
762  N N   B ILE A 60  ? 0.39010 0.43989 0.38361 -0.04204 0.06133  -0.00171 60  ILE A N   
763  C CA  A ILE A 60  ? 0.42087 0.49443 0.42060 -0.04705 0.06496  -0.00404 60  ILE A CA  
764  C CA  B ILE A 60  ? 0.41586 0.49185 0.41653 -0.04727 0.06494  -0.00439 60  ILE A CA  
765  C C   A ILE A 60  ? 0.44006 0.53377 0.44494 -0.02780 0.05857  -0.00417 60  ILE A C   
766  C C   B ILE A 60  ? 0.44875 0.54650 0.45522 -0.02864 0.05866  -0.00486 60  ILE A C   
767  O O   A ILE A 60  ? 0.47491 0.57648 0.47250 -0.02491 0.06634  -0.00070 60  ILE A O   
768  O O   B ILE A 60  ? 0.47578 0.57678 0.47211 -0.02494 0.06735  -0.00015 60  ILE A O   
769  C CB  A ILE A 60  ? 0.41271 0.51119 0.43322 -0.06054 0.05830  -0.01385 60  ILE A CB  
770  C CB  B ILE A 60  ? 0.41278 0.51232 0.43357 -0.06146 0.05876  -0.01400 60  ILE A CB  
771  C CG1 A ILE A 60  ? 0.38617 0.46433 0.40023 -0.08000 0.06513  -0.01404 60  ILE A CG1 
772  C CG1 B ILE A 60  ? 0.38871 0.46659 0.40186 -0.08090 0.06639  -0.01363 60  ILE A CG1 
773  C CG2 A ILE A 60  ? 0.40371 0.53325 0.43416 -0.06290 0.06052  -0.01693 60  ILE A CG2 
774  C CG2 B ILE A 60  ? 0.40338 0.53462 0.43479 -0.06376 0.06055  -0.01734 60  ILE A CG2 
775  C CD1 A ILE A 60  ? 0.42194 0.52191 0.45611 -0.09243 0.05692  -0.02394 60  ILE A CD1 
776  C CD1 B ILE A 60  ? 0.42486 0.52280 0.45734 -0.09401 0.05859  -0.02338 60  ILE A CD1 
777  N N   A THR A 61  ? 0.38057 0.48333 0.39855 -0.01404 0.04408  -0.00814 61  THR A N   
778  N N   B THR A 61  ? 0.43218 0.54550 0.45540 -0.01640 0.04321  -0.01058 61  THR A N   
779  C CA  A THR A 61  ? 0.39604 0.52029 0.42209 0.00430  0.03563  -0.01015 61  THR A CA  
780  C CA  B THR A 61  ? 0.40318 0.54089 0.43562 0.00073  0.03495  -0.01333 61  THR A CA  
781  C C   A THR A 61  ? 0.49998 0.60433 0.50515 0.01753  0.04279  -0.00106 61  THR A C   
782  C C   B THR A 61  ? 0.47074 0.59035 0.48450 0.01620  0.03979  -0.00496 61  THR A C   
783  O O   A THR A 61  ? 0.57855 0.69782 0.58140 0.02802  0.04343  -0.00070 61  THR A O   
784  O O   B THR A 61  ? 0.56121 0.69537 0.57201 0.02612  0.04113  -0.00448 61  THR A O   
785  C CB  A THR A 61  ? 0.44116 0.57930 0.48869 0.01494  0.01770  -0.01646 61  THR A CB  
786  C CB  B THR A 61  ? 0.47140 0.62817 0.52776 0.00966  0.01666  -0.02115 61  THR A CB  
787  O OG1 A THR A 61  ? 0.27275 0.43290 0.34035 0.00322  0.01083  -0.02510 61  THR A OG1 
788  O OG1 B THR A 61  ? 0.54151 0.67454 0.59522 0.01163  0.01305  -0.01786 61  THR A OG1 
789  C CG2 A THR A 61  ? 0.32608 0.48408 0.38222 0.03502  0.00777  -0.01892 61  THR A CG2 
790  C CG2 B THR A 61  ? 0.50890 0.69212 0.58560 -0.00316 0.01110  -0.03034 61  THR A CG2 
791  N N   A LEU A 62  ? 0.42842 0.49909 0.41751 0.01744  0.04846  0.00632  62  LEU A N   
792  N N   B LEU A 62  ? 0.49452 0.58273 0.49515 0.01900  0.04241  0.00162  62  LEU A N   
793  C CA  A LEU A 62  ? 0.62337 0.67324 0.59261 0.03028  0.05480  0.01529  62  LEU A CA  
794  C CA  B LEU A 62  ? 0.56313 0.63268 0.54567 0.03350  0.04707  0.00990  62  LEU A CA  
795  C C   A LEU A 62  ? 0.67982 0.72598 0.63125 0.02527  0.07016  0.02145  62  LEU A C   
796  C C   B LEU A 62  ? 0.66197 0.72316 0.62425 0.02763  0.06360  0.01686  62  LEU A C   
797  O O   A LEU A 62  ? 0.78507 0.81574 0.71915 0.03618  0.07602  0.02923  62  LEU A O   
798  O O   B LEU A 62  ? 0.71040 0.77419 0.66289 0.04079  0.06603  0.02085  62  LEU A O   
799  C CB  A LEU A 62  ? 0.65581 0.67006 0.61216 0.03029  0.05803  0.02180  62  LEU A CB  
800  C CB  B LEU A 62  ? 0.54459 0.58169 0.51754 0.03626  0.04741  0.01571  62  LEU A CB  
801  C CG  A LEU A 62  ? 0.54393 0.55580 0.51254 0.04263  0.04425  0.02004  62  LEU A CG  
802  C CD1 A LEU A 62  ? 0.47506 0.45237 0.43020 0.03840  0.05004  0.02615  62  LEU A CD1 
803  C CD2 A LEU A 62  ? 0.40041 0.41914 0.37120 0.06420  0.03624  0.02160  62  LEU A CD2 
804  N N   A GLN A 63  ? 0.63226 0.69194 0.58786 0.00916  0.07694  0.01877  63  GLN A N   
805  N N   B GLN A 63  ? 0.62821 0.67991 0.58463 0.00803  0.07484  0.01848  63  GLN A N   
806  C CA  A GLN A 63  ? 0.72349 0.78502 0.66552 0.00539  0.09097  0.02486  63  GLN A CA  
807  C CA  B GLN A 63  ? 0.66602 0.70917 0.60496 0.00081  0.09118  0.02608  63  GLN A CA  
808  C C   A GLN A 63  ? 0.77990 0.86740 0.72482 0.02251  0.08630  0.02316  63  GLN A C   
809  C C   B GLN A 63  ? 0.74086 0.81604 0.68575 0.00545  0.09199  0.02368  63  GLN A C   
810  O O   A GLN A 63  ? 0.79795 0.87712 0.72515 0.03137  0.09475  0.03103  63  GLN A O   
811  O O   B GLN A 63  ? 0.84042 0.91100 0.76970 0.00630  0.10435  0.03142  63  GLN A O   
812  C CB  A GLN A 63  ? 0.70727 0.78093 0.65723 -0.01551 0.09785  0.02177  63  GLN A CB  
813  C CB  B GLN A 63  ? 0.58460 0.61248 0.51983 -0.02184 0.10138  0.02732  63  GLN A CB  
814  C CG  A GLN A 63  ? 0.61747 0.66691 0.56451 -0.03350 0.10255  0.02244  63  GLN A CG  
815  C CG  B GLN A 63  ? 0.63616 0.62305 0.55046 -0.02556 0.11099  0.03607  63  GLN A CG  
816  C CD  A GLN A 63  ? 0.64878 0.71609 0.60930 -0.05260 0.10515  0.01688  63  GLN A CD  
817  C CD  B GLN A 63  ? 0.59361 0.56475 0.51126 -0.04136 0.11030  0.03235  63  GLN A CD  
818  O OE1 A GLN A 63  ? 0.81716 0.86883 0.76950 -0.06860 0.11713  0.02135  63  GLN A OE1 
819  O OE1 B GLN A 63  ? 0.62419 0.56698 0.53130 -0.03949 0.11083  0.03560  63  GLN A OE1 
820  N NE2 A GLN A 63  ? 0.42980 0.53043 0.41210 -0.05093 0.09364  0.00707  63  GLN A NE2 
821  N NE2 B GLN A 63  ? 0.65052 0.64044 0.58280 -0.05645 0.10889  0.02528  63  GLN A NE2 
822  N N   A SER A 64  ? 0.87278 0.99194 0.83966 0.02763  0.07276  0.01279  64  SER A N   
823  N N   B SER A 64  ? 0.76220 0.86988 0.72914 0.00907  0.07927  0.01343  64  SER A N   
824  C CA  A SER A 64  ? 0.88017 1.02603 0.85161 0.04442  0.06654  0.00926  64  SER A CA  
825  C CA  B SER A 64  ? 0.81249 0.95232 0.78592 0.01482  0.07905  0.01010  64  SER A CA  
826  C C   A SER A 64  ? 0.80902 0.96155 0.79403 0.06193  0.04828  0.00309  64  SER A C   
827  C C   B SER A 64  ? 0.85772 1.02126 0.84490 0.03488  0.06272  0.00255  64  SER A C   
828  O O   A SER A 64  ? 0.78622 0.96727 0.79295 0.06612  0.03525  -0.00686 64  SER A O   
829  O O   B SER A 64  ? 0.89681 1.08608 0.88712 0.04285  0.06207  -0.00030 64  SER A O   
830  C CB  A SER A 64  ? 0.86376 1.04400 0.85054 0.03615  0.06645  0.00202  64  SER A CB  
831  C CB  B SER A 64  ? 0.79838 0.96024 0.78647 -0.00330 0.08197  0.00445  64  SER A CB  
832  O OG  A SER A 64  ? 1.01874 1.21019 1.02713 0.02533  0.05685  -0.00672 64  SER A OG  
833  O OG  B SER A 64  ? 0.75328 0.92288 0.76111 -0.01012 0.06985  -0.00454 64  SER A OG  
834  N N   A ILE A 65  ? 0.79678 0.83846 0.64536 0.04839  0.11307  0.08459  65  ILE A N   
835  N N   B ILE A 65  ? 0.82589 0.89015 0.71545 0.04086  0.12689  0.08489  65  ILE A N   
836  C CA  A ILE A 65  ? 0.98553 1.02151 0.82519 0.05318  0.09984  0.07193  65  ILE A CA  
837  C CA  B ILE A 65  ? 0.86391 0.92599 0.73558 0.05026  0.12131  0.07332  65  ILE A CA  
838  C C   A ILE A 65  ? 0.90358 0.93802 0.71344 0.06342  0.10167  0.06803  65  ILE A C   
839  C C   B ILE A 65  ? 0.91954 0.96709 0.77829 0.05124  0.10649  0.06883  65  ILE A C   
840  O O   A ILE A 65  ? 0.83132 0.85835 0.61856 0.06728  0.10029  0.07332  65  ILE A O   
841  O O   B ILE A 65  ? 0.78067 0.82050 0.64319 0.04588  0.10162  0.07507  65  ILE A O   
842  C CB  A ILE A 65  ? 0.91107 0.93574 0.75157 0.04995  0.08676  0.07209  65  ILE A CB  
843  C CB  B ILE A 65  ? 0.76108 0.83263 0.65023 0.05154  0.11998  0.06272  65  ILE A CB  
844  N N   A ASN A 66  ? 1.02552 1.06644 0.83458 0.06843  0.10443  0.05845  66  ASN A N   
845  N N   B ASN A 66  ? 1.04771 1.09163 0.89219 0.05814  0.09921  0.05758  66  ASN A N   
846  C CA  A ASN A 66  ? 0.99148 1.02993 0.77253 0.07854  0.10480  0.05181  66  ASN A CA  
847  C CA  B ASN A 66  ? 0.89508 0.92722 0.72564 0.05991  0.08569  0.05288  66  ASN A CA  
848  C C   A ASN A 66  ? 0.96849 0.99910 0.74329 0.08139  0.09013  0.03777  66  ASN A C   
849  C C   B ASN A 66  ? 0.87934 0.90956 0.71191 0.06239  0.07609  0.03873  66  ASN A C   
850  O O   A ASN A 66  ? 1.11907 1.14375 0.86805 0.08855  0.08582  0.03237  66  ASN A O   
851  O O   B ASN A 66  ? 0.95096 0.98390 0.77465 0.06863  0.07937  0.03143  66  ASN A O   
852  C CB  A ASN A 66  ? 0.97113 1.02098 0.75270 0.08363  0.11863  0.05008  66  ASN A CB  
853  C CB  B ASN A 66  ? 0.80939 0.83597 0.60892 0.06712  0.08701  0.05643  66  ASN A CB  
854  C CG  A ASN A 66  ? 0.91433 0.96095 0.66519 0.09482  0.11997  0.04270  66  ASN A CG  
855  O OD1 A ASN A 66  ? 1.08221 1.13008 0.83220 0.10011  0.11895  0.03103  66  ASN A OD1 
856  N ND2 A ASN A 66  ? 0.94155 0.98293 0.66585 0.09895  0.12185  0.04934  66  ASN A ND2 
857  N N   A GLU A 67  ? 0.87833 0.90867 0.67573 0.07580  0.08238  0.03180  67  GLU A N   
858  N N   B GLU A 67  ? 0.60843 0.63342 0.45275 0.05755  0.06474  0.03513  67  GLU A N   
859  C CA  A GLU A 67  ? 0.70414 0.72701 0.49811 0.07724  0.06919  0.01923  67  GLU A CA  
860  C CA  B GLU A 67  ? 0.65935 0.67939 0.50212 0.05921  0.05372  0.02297  67  GLU A CA  
861  C C   A GLU A 67  ? 0.71883 0.73768 0.53071 0.06943  0.05831  0.01939  67  GLU A C   
862  C C   B GLU A 67  ? 0.72073 0.74508 0.57381 0.06074  0.05621  0.01463  67  GLU A C   
863  O O   A GLU A 67  ? 0.65401 0.67446 0.47899 0.06347  0.06013  0.02873  67  GLU A O   
864  O O   B GLU A 67  ? 0.67313 0.69289 0.51666 0.06510  0.05126  0.00455  67  GLU A O   
865  C CB  A GLU A 67  ? 0.87330 0.89897 0.67307 0.08087  0.07147  0.00875  67  GLU A CB  
866  C CB  B GLU A 67  ? 0.58820 0.60146 0.40510 0.06543  0.04719  0.01811  67  GLU A CB  
867  N N   A ASP A 68  ? 0.56919 0.58239 0.38156 0.06946  0.04727  0.00876  68  ASP A N   
868  N N   B ASP A 68  ? 0.49033 0.52304 0.36339 0.05720  0.06327  0.01856  68  ASP A N   
869  C CA  A ASP A 68  ? 0.49561 0.50500 0.32200 0.06317  0.03653  0.00763  68  ASP A CA  
870  C CA  B ASP A 68  ? 0.55922 0.59517 0.44691 0.05751  0.06252  0.01126  68  ASP A CA  
871  C C   A ASP A 68  ? 0.46494 0.47787 0.31567 0.05839  0.03779  0.00513  68  ASP A C   
872  C C   B ASP A 68  ? 0.54779 0.57961 0.45140 0.05123  0.05271  0.00884  68  ASP A C   
873  O O   A ASP A 68  ? 0.47937 0.49061 0.33245 0.06014  0.03561  -0.00392 68  ASP A O   
874  O O   B ASP A 68  ? 0.45875 0.49220 0.37520 0.05086  0.05107  0.00385  68  ASP A O   
875  C CB  A ASP A 68  ? 0.47284 0.47526 0.28611 0.06569  0.02466  -0.00219 68  ASP A CB  
876  C CB  B ASP A 68  ? 0.74411 0.79295 0.64671 0.05738  0.07401  0.01599  68  ASP A CB  
877  C CG  A ASP A 68  ? 0.41769 0.41745 0.24572 0.05969  0.01393  -0.00458 68  ASP A CG  
878  O OD1 A ASP A 68  ? 0.39791 0.40015 0.24627 0.05401  0.01524  -0.00060 68  ASP A OD1 
879  O OD2 A ASP A 68  ? 0.46653 0.46217 0.28527 0.06089  0.00393  -0.01096 68  ASP A OD2 
880  N N   A ILE A 69  ? 0.46849 0.48548 0.33671 0.05255  0.04100  0.01315  69  ILE A N   
881  N N   B ILE A 69  ? 0.48697 0.51317 0.38869 0.04711  0.04620  0.01229  69  ILE A N   
882  C CA  A ILE A 69  ? 0.46553 0.48698 0.35610 0.04839  0.04231  0.01157  69  ILE A CA  
883  C CA  B ILE A 69  ? 0.43035 0.45471 0.34878 0.04067  0.03952  0.01264  69  ILE A CA  
884  C C   A ILE A 69  ? 0.38308 0.40007 0.28618 0.04324  0.03234  0.00822  69  ILE A C   
885  C C   B ILE A 69  ? 0.36695 0.38622 0.28839 0.04081  0.03128  0.00336  69  ILE A C   
886  O O   A ILE A 69  ? 0.36113 0.38133 0.28237 0.03909  0.03272  0.00878  69  ILE A O   
887  O O   B ILE A 69  ? 0.33702 0.35636 0.27355 0.03639  0.02761  0.00283  69  ILE A O   
888  C CB  A ILE A 69  ? 0.52538 0.55536 0.42964 0.04493  0.05209  0.02072  69  ILE A CB  
889  C CB  B ILE A 69  ? 0.55962 0.57930 0.47467 0.03742  0.03551  0.01894  69  ILE A CB  
890  C CG1 A ILE A 69  ? 0.53524 0.56268 0.43652 0.04153  0.05320  0.03080  69  ILE A CG1 
891  C CG2 A ILE A 69  ? 0.52914 0.56695 0.42802 0.05026  0.06325  0.02126  69  ILE A CG2 
892  C CD1 A ILE A 69  ? 0.37103 0.39222 0.28019 0.03664  0.04386  0.03128  69  ILE A CD1 
893  N N   A THR A 70  ? 0.30852 0.31900 0.20233 0.04362  0.02338  0.00463  70  THR A N   
894  N N   B THR A 70  ? 0.45540 0.46959 0.36247 0.04560  0.02832  -0.00402 70  THR A N   
895  C CA  A THR A 70  ? 0.32001 0.32743 0.22596 0.03894  0.01487  0.00158  70  THR A CA  
896  C CA  B THR A 70  ? 0.41671 0.42433 0.32664 0.04451  0.02007  -0.01216 70  THR A CA  
897  C C   A THR A 70  ? 0.27578 0.28297 0.19266 0.03795  0.01398  -0.00514 70  THR A C   
898  C C   B THR A 70  ? 0.36398 0.37328 0.28740 0.04456  0.02227  -0.01510 70  THR A C   
899  O O   A THR A 70  ? 0.31080 0.31867 0.24287 0.03357  0.01193  -0.00450 70  THR A O   
900  O O   B THR A 70  ? 0.33488 0.34171 0.26973 0.04060  0.01733  -0.01650 70  THR A O   
901  C CB  A THR A 70  ? 0.43843 0.44091 0.33345 0.04004  0.00552  -0.00237 70  THR A CB  
902  C CB  B THR A 70  ? 0.54167 0.54249 0.43315 0.04903  0.01582  -0.01991 70  THR A CB  
903  O OG1 A THR A 70  ? 0.39192 0.39411 0.27329 0.04281  0.00629  0.00388  70  THR A OG1 
904  C CG2 A THR A 70  ? 0.37829 0.37963 0.28721 0.03505  -0.00161 -0.00328 70  THR A CG2 
905  N N   A TYR A 71  ? 0.37112 0.37649 0.27924 0.04260  0.01560  -0.01155 71  TYR A N   
906  N N   B TYR A 71  ? 0.40124 0.41512 0.32324 0.04962  0.02985  -0.01581 71  TYR A N   
907  C CA  A TYR A 71  ? 0.34189 0.34470 0.25815 0.04268  0.01435  -0.01793 71  TYR A CA  
908  C CA  B TYR A 71  ? 0.38768 0.40335 0.32189 0.05110  0.03144  -0.01868 71  TYR A CA  
909  C C   A TYR A 71  ? 0.32375 0.33310 0.25684 0.04100  0.01968  -0.01397 71  TYR A C   
910  C C   B TYR A 71  ? 0.42679 0.44984 0.38047 0.04585  0.03203  -0.01279 71  TYR A C   
911  O O   A TYR A 71  ? 0.29589 0.30311 0.23903 0.03950  0.01697  -0.01700 71  TYR A O   
912  O O   B TYR A 71  ? 0.51177 0.53417 0.47606 0.04547  0.02957  -0.01502 71  TYR A O   
913  C CB  A TYR A 71  ? 0.34501 0.34378 0.24734 0.04913  0.01618  -0.02522 71  TYR A CB  
914  C CB  B TYR A 71  ? 0.57547 0.59587 0.50435 0.05877  0.03979  -0.02078 71  TYR A CB  
915  C CG  A TYR A 71  ? 0.35017 0.35598 0.24984 0.05436  0.02664  -0.02238 71  TYR A CG  
916  C CD1 A TYR A 71  ? 0.38756 0.39737 0.27435 0.05733  0.03214  -0.01772 71  TYR A CD1 
917  C CD2 A TYR A 71  ? 0.32834 0.33750 0.23881 0.05663  0.03129  -0.02389 71  TYR A CD2 
918  C CE1 A TYR A 71  ? 0.40827 0.42605 0.29392 0.06189  0.04301  -0.01461 71  TYR A CE1 
919  C CE2 A TYR A 71  ? 0.32995 0.34780 0.24038 0.06161  0.04125  -0.02138 71  TYR A CE2 
920  C CZ  A TYR A 71  ? 0.53915 0.56166 0.43773 0.06389  0.04748  -0.01674 71  TYR A CZ  
921  O OH  A TYR A 71  ? 0.47938 0.51198 0.37941 0.06857  0.05849  -0.01380 71  TYR A OH  
922  N N   A VAL A 72  ? 0.30641 0.32381 0.24303 0.04101  0.02700  -0.00704 72  VAL A N   
923  N N   B VAL A 72  ? 0.31695 0.34608 0.27488 0.04190  0.03491  -0.00539 72  VAL A N   
924  C CA  A VAL A 72  ? 0.32291 0.34799 0.27718 0.03884  0.03101  -0.00378 72  VAL A CA  
925  C CA  B VAL A 72  ? 0.42834 0.46426 0.40460 0.03679  0.03532  -0.00066 72  VAL A CA  
926  C C   A VAL A 72  ? 0.32381 0.34714 0.29114 0.03282  0.02492  -0.00263 72  VAL A C   
927  C C   B VAL A 72  ? 0.30943 0.33928 0.28996 0.03103  0.02755  -0.00005 72  VAL A C   
928  O O   A VAL A 72  ? 0.27007 0.29695 0.25039 0.03174  0.02489  -0.00315 72  VAL A O   
929  O O   B VAL A 72  ? 0.30869 0.33980 0.30158 0.02829  0.02454  -0.00048 72  VAL A O   
930  C CB  A VAL A 72  ? 0.32578 0.36036 0.28285 0.03876  0.04011  0.00363  72  VAL A CB  
931  C CB  B VAL A 72  ? 0.34510 0.39089 0.32661 0.03507  0.04347  0.00690  72  VAL A CB  
932  C CG1 A VAL A 72  ? 0.33506 0.37916 0.31221 0.03584  0.04336  0.00651  72  VAL A CG1 
933  C CG1 B VAL A 72  ? 0.51220 0.56522 0.51388 0.02958  0.04316  0.01030  72  VAL A CG1 
934  C CG2 A VAL A 72  ? 0.34931 0.38618 0.29263 0.04581  0.04705  0.00183  72  VAL A CG2 
935  C CG2 B VAL A 72  ? 0.54274 0.59563 0.51950 0.04154  0.05211  0.00607  72  VAL A CG2 
936  N N   A ARG A 73  ? 0.27425 0.29229 0.23786 0.02959  0.01940  -0.00146 73  ARG A N   
937  N N   B ARG A 73  ? 0.30569 0.32951 0.27575 0.02980  0.02423  0.00092  73  ARG A N   
938  C CA  A ARG A 73  ? 0.29746 0.31394 0.27253 0.02460  0.01431  -0.00067 73  ARG A CA  
939  C CA  B ARG A 73  ? 0.32319 0.34127 0.29613 0.02579  0.01673  0.00012  73  ARG A CA  
940  C C   A ARG A 73  ? 0.25161 0.26464 0.23140 0.02477  0.01032  -0.00632 73  ARG A C   
941  C C   B ARG A 73  ? 0.27071 0.28428 0.24647 0.02618  0.01194  -0.00617 73  ARG A C   
942  O O   A ARG A 73  ? 0.27652 0.29015 0.26683 0.02168  0.00805  -0.00561 73  ARG A O   
943  O O   B ARG A 73  ? 0.26329 0.27657 0.24916 0.02298  0.00896  -0.00598 73  ARG A O   
944  C CB  A ARG A 73  ? 0.29860 0.31037 0.26866 0.02244  0.00907  0.00075  73  ARG A CB  
945  C CB  B ARG A 73  ? 0.37606 0.38916 0.33612 0.02632  0.01329  0.00065  73  ARG A CB  
946  C CG  A ARG A 73  ? 0.32378 0.33646 0.28872 0.02216  0.01190  0.00749  73  ARG A CG  
947  C CG  B ARG A 73  ? 0.36258 0.37137 0.32630 0.02297  0.00587  -0.00044 73  ARG A CG  
948  C CD  A ARG A 73  ? 0.30123 0.30919 0.26208 0.02121  0.00552  0.00837  73  ARG A CD  
949  C CD  B ARG A 73  ? 0.31234 0.32240 0.28447 0.01926  0.00632  0.00582  73  ARG A CD  
950  N NE  A ARG A 73  ? 0.27959 0.28661 0.23295 0.02214  0.00798  0.01525  73  ARG A NE  
951  N NE  B ARG A 73  ? 0.35590 0.36563 0.31977 0.02035  0.00910  0.01182  73  ARG A NE  
952  C CZ  A ARG A 73  ? 0.33418 0.34055 0.29442 0.01918  0.01043  0.02179  73  ARG A CZ  
953  C CZ  B ARG A 73  ? 0.27125 0.27962 0.23965 0.01771  0.00966  0.01785  73  ARG A CZ  
954  N NH1 A ARG A 73  ? 0.26702 0.27412 0.24184 0.01503  0.00997  0.02159  73  ARG A NH1 
955  N NH1 B ARG A 73  ? 0.29340 0.30092 0.27410 0.01398  0.00725  0.01782  73  ARG A NH1 
956  N NH2 A ARG A 73  ? 0.31262 0.31663 0.26406 0.02051  0.01330  0.02868  73  ARG A NH2 
957  N NH2 B ARG A 73  ? 0.29020 0.29710 0.24969 0.01912  0.01296  0.02413  73  ARG A NH2 
958  N N   A TYR A 74  ? 0.25014 0.25840 0.22130 0.02840  0.00935  -0.01195 74  TYR A N   
959  N N   B TYR A 74  ? 0.21491 0.22400 0.18104 0.03019  0.01134  -0.01179 74  TYR A N   
960  C CA  A TYR A 74  ? 0.20709 0.20993 0.18167 0.02860  0.00607  -0.01671 74  TYR A CA  
961  C CA  B TYR A 74  ? 0.23556 0.23821 0.20383 0.03016  0.00706  -0.01729 74  TYR A CA  
962  C C   A TYR A 74  ? 0.21028 0.21766 0.19486 0.03044  0.00931  -0.01577 74  TYR A C   
963  C C   B TYR A 74  ? 0.31329 0.31883 0.29216 0.03145  0.00941  -0.01706 74  TYR A C   
964  O O   A TYR A 74  ? 0.24043 0.24469 0.23106 0.02936  0.00639  -0.01685 74  TYR A O   
965  O O   B TYR A 74  ? 0.29739 0.29810 0.28082 0.03013  0.00585  -0.01899 74  TYR A O   
966  C CB  A TYR A 74  ? 0.23710 0.23219 0.19973 0.03193  0.00432  -0.02327 74  TYR A CB  
967  C CB  B TYR A 74  ? 0.26228 0.25756 0.21764 0.03372  0.00532  -0.02394 74  TYR A CB  
968  C CG  A TYR A 74  ? 0.22604 0.21672 0.18226 0.02900  -0.00163 -0.02533 74  TYR A CG  
969  C CG  B TYR A 74  ? 0.26200 0.25273 0.21075 0.03088  -0.00109 -0.02615 74  TYR A CG  
970  C CD1 A TYR A 74  ? 0.30286 0.29632 0.25043 0.02969  -0.00173 -0.02323 74  TYR A CD1 
971  C CD1 B TYR A 74  ? 0.28908 0.27360 0.24151 0.02744  -0.00683 -0.03001 74  TYR A CD1 
972  C CD2 A TYR A 74  ? 0.28184 0.26628 0.24132 0.02557  -0.00711 -0.02887 74  TYR A CD2 
973  C CD2 B TYR A 74  ? 0.25676 0.25016 0.19645 0.03162  -0.00137 -0.02381 74  TYR A CD2 
974  C CE1 A TYR A 74  ? 0.29050 0.28150 0.23322 0.02761  -0.00813 -0.02511 74  TYR A CE1 
975  C CE1 B TYR A 74  ? 0.29770 0.28037 0.24670 0.02461  -0.01296 -0.03222 74  TYR A CE1 
976  C CE2 A TYR A 74  ? 0.26090 0.24376 0.21723 0.02267  -0.01277 -0.03082 74  TYR A CE2 
977  C CE2 B TYR A 74  ? 0.31988 0.31066 0.25452 0.02967  -0.00818 -0.02596 74  TYR A CE2 
978  C CZ  A TYR A 74  ? 0.29805 0.28465 0.24625 0.02398  -0.01375 -0.02918 74  TYR A CZ  
979  C CZ  B TYR A 74  ? 0.27495 0.26124 0.21531 0.02601  -0.01409 -0.03046 74  TYR A CZ  
980  O OH  A TYR A 74  ? 0.30652 0.29292 0.25223 0.02185  -0.02021 -0.03123 74  TYR A OH  
981  O OH  B TYR A 74  ? 0.34493 0.33078 0.28292 0.02379  -0.02109 -0.03285 74  TYR A OH  
982  N N   A PHE A 75  ? 0.29575 0.31123 0.28237 0.03340  0.01538  -0.01344 75  PHE A N   
983  N N   B PHE A 75  ? 0.30844 0.32231 0.29156 0.03422  0.01536  -0.01448 75  PHE A N   
984  C CA  A PHE A 75  ? 0.29888 0.32149 0.29732 0.03520  0.01791  -0.01232 75  PHE A CA  
985  C CA  B PHE A 75  ? 0.30079 0.31943 0.29566 0.03564  0.01651  -0.01403 75  PHE A CA  
986  C C   A PHE A 75  ? 0.28428 0.31128 0.29488 0.02982  0.01533  -0.00845 75  PHE A C   
987  C C   B PHE A 75  ? 0.27747 0.29951 0.28366 0.03016  0.01351  -0.01029 75  PHE A C   
988  O O   A PHE A 75  ? 0.27137 0.30111 0.29096 0.03044  0.01371  -0.00876 75  PHE A O   
989  O O   B PHE A 75  ? 0.32277 0.34265 0.33452 0.02984  0.01009  -0.01133 75  PHE A O   
990  C CB  A PHE A 75  ? 0.28982 0.32195 0.28888 0.03955  0.02564  -0.01083 75  PHE A CB  
991  C CB  B PHE A 75  ? 0.35363 0.38265 0.35205 0.03997  0.02379  -0.01240 75  PHE A CB  
992  C CG  A PHE A 75  ? 0.33124 0.35824 0.31576 0.04571  0.02841  -0.01545 75  PHE A CG  
993  C CG  B PHE A 75  ? 0.43423 0.47095 0.44636 0.04206  0.02463  -0.01183 75  PHE A CG  
994  C CD1 A PHE A 75  ? 0.44504 0.46029 0.42170 0.04842  0.02412  -0.02177 75  PHE A CD1 
995  C CD1 B PHE A 75  ? 0.47139 0.50192 0.48368 0.04602  0.02147  -0.01564 75  PHE A CD1 
996  C CD2 A PHE A 75  ? 0.43454 0.46761 0.41258 0.04857  0.03537  -0.01353 75  PHE A CD2 
997  C CD2 B PHE A 75  ? 0.46674 0.51691 0.49185 0.04016  0.02840  -0.00736 75  PHE A CD2 
998  C CE1 A PHE A 75  ? 0.41243 0.42150 0.37486 0.05400  0.02591  -0.02722 75  PHE A CE1 
999  C CE1 B PHE A 75  ? 0.48918 0.52727 0.51346 0.04898  0.02149  -0.01486 75  PHE A CE1 
1000 C CE2 A PHE A 75  ? 0.52109 0.54890 0.48376 0.05485  0.03769  -0.01860 75  PHE A CE2 
1001 C CE2 B PHE A 75  ? 0.41831 0.47724 0.45692 0.04235  0.02815  -0.00728 75  PHE A CE2 
1002 C CZ  A PHE A 75  ? 0.40959 0.42508 0.36442 0.05755  0.03249  -0.02596 75  PHE A CZ  
1003 C CZ  B PHE A 75  ? 0.31339 0.36651 0.35108 0.04725  0.02445  -0.01099 75  PHE A CZ  
1004 N N   A ASP A 76  ? 0.26716 0.29402 0.27725 0.02506  0.01443  -0.00510 76  ASP A N   
1005 N N   B ASP A 76  ? 0.26336 0.28958 0.27183 0.02612  0.01469  -0.00593 76  ASP A N   
1006 C CA  A ASP A 76  ? 0.27088 0.29797 0.28941 0.02007  0.01065  -0.00300 76  ASP A CA  
1007 C CA  B ASP A 76  ? 0.28721 0.31505 0.30510 0.02099  0.01162  -0.00319 76  ASP A CA  
1008 C C   A ASP A 76  ? 0.25764 0.27673 0.27389 0.01941  0.00505  -0.00620 76  ASP A C   
1009 C C   B ASP A 76  ? 0.28067 0.30002 0.29547 0.01895  0.00570  -0.00545 76  ASP A C   
1010 O O   A ASP A 76  ? 0.23862 0.25828 0.26108 0.01935  0.00284  -0.00684 76  ASP A O   
1011 O O   B ASP A 76  ? 0.30881 0.32822 0.33030 0.01672  0.00271  -0.00519 76  ASP A O   
1012 C CB  A ASP A 76  ? 0.28286 0.30954 0.29939 0.01635  0.01140  0.00114  76  ASP A CB  
1013 C CB  B ASP A 76  ? 0.28443 0.31522 0.30330 0.01742  0.01417  0.00178  76  ASP A CB  
1014 C CG  A ASP A 76  ? 0.28724 0.31169 0.31003 0.01177  0.00731  0.00250  76  ASP A CG  
1015 C CG  B ASP A 76  ? 0.34234 0.37771 0.37417 0.01277  0.01322  0.00457  76  ASP A CG  
1016 O OD1 A ASP A 76  ? 0.33111 0.35232 0.35567 0.01135  0.00311  -0.00021 76  ASP A OD1 
1017 O OD1 B ASP A 76  ? 0.33387 0.37830 0.37587 0.01269  0.01625  0.00574  76  ASP A OD1 
1018 O OD2 A ASP A 76  ? 0.34450 0.36953 0.36957 0.00873  0.00862  0.00652  76  ASP A OD2 
1019 O OD2 B ASP A 76  ? 0.31815 0.34855 0.35056 0.00935  0.00936  0.00520  76  ASP A OD2 
1020 N N   A TRP A 77  ? 0.24048 0.25263 0.24787 0.01891  0.00274  -0.00801 77  TRP A N   
1021 N N   B TRP A 77  ? 0.23110 0.24379 0.23587 0.01968  0.00398  -0.00786 77  TRP A N   
1022 C CA  A TRP A 77  ? 0.25722 0.26295 0.26389 0.01692  -0.00185 -0.01012 77  TRP A CA  
1023 C CA  B TRP A 77  ? 0.25542 0.26155 0.25889 0.01745  -0.00094 -0.00999 77  TRP A CA  
1024 C C   A TRP A 77  ? 0.21064 0.21205 0.21777 0.01918  -0.00268 -0.01286 77  TRP A C   
1025 C C   B TRP A 77  ? 0.23821 0.24064 0.24422 0.01874  -0.00231 -0.01242 77  TRP A C   
1026 O O   A TRP A 77  ? 0.20712 0.20577 0.21732 0.01744  -0.00514 -0.01267 77  TRP A O   
1027 O O   B TRP A 77  ? 0.23362 0.23390 0.24318 0.01636  -0.00497 -0.01202 77  TRP A O   
1028 C CB  A TRP A 77  ? 0.20122 0.20236 0.19967 0.01618  -0.00414 -0.01203 77  TRP A CB  
1029 C CB  B TRP A 77  ? 0.22864 0.22984 0.22239 0.01781  -0.00295 -0.01268 77  TRP A CB  
1030 C CG  A TRP A 77  ? 0.20621 0.20998 0.20262 0.01479  -0.00419 -0.00884 77  TRP A CG  
1031 C CG  B TRP A 77  ? 0.24121 0.24405 0.23198 0.01621  -0.00397 -0.00994 77  TRP A CG  
1032 C CD1 A TRP A 77  ? 0.22892 0.23650 0.23093 0.01298  -0.00271 -0.00444 77  TRP A CD1 
1033 C CD1 B TRP A 77  ? 0.21980 0.22643 0.21501 0.01454  -0.00240 -0.00507 77  TRP A CD1 
1034 C CD2 A TRP A 77  ? 0.24694 0.24882 0.23472 0.01540  -0.00626 -0.00975 77  TRP A CD2 
1035 C CD2 B TRP A 77  ? 0.22710 0.22719 0.20977 0.01639  -0.00735 -0.01190 77  TRP A CD2 
1036 N NE1 A TRP A 77  ? 0.25223 0.25929 0.24926 0.01272  -0.00323 -0.00186 77  TRP A NE1 
1037 N NE1 B TRP A 77  ? 0.26043 0.26594 0.25003 0.01431  -0.00425 -0.00326 77  TRP A NE1 
1038 C CE2 A TRP A 77  ? 0.28221 0.28655 0.27020 0.01454  -0.00563 -0.00495 77  TRP A CE2 
1039 C CE2 B TRP A 77  ? 0.19908 0.20158 0.18101 0.01566  -0.00760 -0.00744 77  TRP A CE2 
1040 C CE3 A TRP A 77  ? 0.25466 0.25258 0.23442 0.01661  -0.00912 -0.01439 77  TRP A CE3 
1041 C CE3 B TRP A 77  ? 0.23783 0.23334 0.21404 0.01704  -0.01071 -0.01723 77  TRP A CE3 
1042 C CZ2 A TRP A 77  ? 0.26192 0.26536 0.24153 0.01573  -0.00777 -0.00399 77  TRP A CZ2 
1043 C CZ2 B TRP A 77  ? 0.30147 0.30303 0.27607 0.01644  -0.01132 -0.00778 77  TRP A CZ2 
1044 C CZ3 A TRP A 77  ? 0.24905 0.24719 0.22097 0.01732  -0.01187 -0.01429 77  TRP A CZ3 
1045 C CZ3 B TRP A 77  ? 0.22691 0.22231 0.19671 0.01699  -0.01477 -0.01830 77  TRP A CZ3 
1046 C CH2 A TRP A 77  ? 0.31676 0.31789 0.28829 0.01731  -0.01115 -0.00879 77  TRP A CH2 
1047 C CH2 B TRP A 77  ? 0.33619 0.33513 0.30498 0.01714  -0.01515 -0.01340 77  TRP A CH2 
1048 N N   A VAL A 78  ? 0.25172 0.25173 0.25499 0.02356  -0.00039 -0.01522 78  VAL A N   
1049 N N   B VAL A 78  ? 0.25029 0.25156 0.25385 0.02310  -0.00016 -0.01465 78  VAL A N   
1050 C CA  A VAL A 78  ? 0.26953 0.26380 0.27293 0.02653  -0.00113 -0.01731 78  VAL A CA  
1051 C CA  B VAL A 78  ? 0.28031 0.27520 0.28392 0.02528  -0.00151 -0.01684 78  VAL A CA  
1052 C C   A VAL A 78  ? 0.29273 0.29215 0.30475 0.02715  -0.00163 -0.01460 78  VAL A C   
1053 C C   B VAL A 78  ? 0.27756 0.27682 0.28950 0.02577  -0.00214 -0.01429 78  VAL A C   
1054 O O   A VAL A 78  ? 0.30351 0.29749 0.31559 0.02866  -0.00341 -0.01485 78  VAL A O   
1055 O O   B VAL A 78  ? 0.27723 0.27064 0.28900 0.02604  -0.00430 -0.01442 78  VAL A O   
1056 C CB  A VAL A 78  ? 0.30807 0.29945 0.30570 0.03226  0.00164  -0.02075 78  VAL A CB  
1057 C CB  B VAL A 78  ? 0.35528 0.34639 0.35290 0.03082  0.00091  -0.02042 78  VAL A CB  
1058 C CG1 A VAL A 78  ? 0.26720 0.26960 0.27002 0.03607  0.00617  -0.01886 78  VAL A CG1 
1059 C CG1 B VAL A 78  ? 0.29295 0.29024 0.29677 0.03594  0.00368  -0.01934 78  VAL A CG1 
1060 C CG2 A VAL A 78  ? 0.32518 0.30625 0.32102 0.03514  0.00012  -0.02316 78  VAL A CG2 
1061 C CG2 B VAL A 78  ? 0.32780 0.30596 0.31937 0.03085  -0.00172 -0.02436 78  VAL A CG2 
1062 N N   . LEU A 79  ? 0.26155 0.27098 0.28063 0.02584  -0.00039 -0.01189 79  LEU A N   
1063 C CA  . LEU A 79  ? 0.30822 0.32331 0.33578 0.02576  -0.00219 -0.01011 79  LEU A CA  
1064 C C   . LEU A 79  ? 0.29428 0.30809 0.32326 0.02083  -0.00537 -0.00882 79  LEU A C   
1065 O O   . LEU A 79  ? 0.29580 0.30815 0.32600 0.02109  -0.00824 -0.00860 79  LEU A O   
1066 C CB  . LEU A 79  ? 0.27378 0.30110 0.31028 0.02644  0.00073  -0.00844 79  LEU A CB  
1067 C CG  . LEU A 79  ? 0.32028 0.35153 0.35688 0.03239  0.00492  -0.00967 79  LEU A CG  
1068 C CD1 . LEU A 79  ? 0.34455 0.39021 0.39273 0.03237  0.00836  -0.00744 79  LEU A CD1 
1069 C CD2 . LEU A 79  ? 0.40097 0.42725 0.43622 0.03805  0.00286  -0.01158 79  LEU A CD2 
1070 N N   . THR A 80  ? 0.26193 0.27605 0.29001 0.01704  -0.00487 -0.00787 80  THR A N   
1071 C CA  . THR A 80  ? 0.24518 0.25889 0.27570 0.01323  -0.00744 -0.00689 80  THR A CA  
1072 C C   . THR A 80  ? 0.29624 0.30260 0.32143 0.01217  -0.00944 -0.00793 80  THR A C   
1073 O O   . THR A 80  ? 0.28198 0.28743 0.30829 0.01112  -0.01146 -0.00779 80  THR A O   
1074 C CB  . THR A 80  ? 0.26581 0.28181 0.29797 0.01012  -0.00618 -0.00493 80  THR A CB  
1075 O OG1 . THR A 80  ? 0.28215 0.29487 0.30713 0.01068  -0.00475 -0.00505 80  THR A OG1 
1076 C CG2 . THR A 80  ? 0.30826 0.33242 0.34841 0.00950  -0.00383 -0.00303 80  THR A CG2 
1077 N N   . THR A 81  ? 0.25331 0.25497 0.27299 0.01223  -0.00889 -0.00917 81  THR A N   
1078 C CA  . THR A 81  ? 0.26591 0.26251 0.28317 0.01016  -0.01048 -0.00991 81  THR A CA  
1079 C C   . THR A 81  ? 0.25597 0.24818 0.27232 0.01100  -0.01099 -0.00981 81  THR A C   
1080 O O   . THR A 81  ? 0.27213 0.26326 0.28875 0.00913  -0.01162 -0.00912 81  THR A O   
1081 C CB  . THR A 81  ? 0.33218 0.32562 0.34513 0.00931  -0.01077 -0.01180 81  THR A CB  
1082 O OG1 . THR A 81  ? 0.25725 0.24642 0.26616 0.01176  -0.00989 -0.01396 81  THR A OG1 
1083 C CG2 . THR A 81  ? 0.28238 0.27979 0.29436 0.00887  -0.01068 -0.01094 81  THR A CG2 
1084 N N   . PRO A 82  ? 0.25806 0.24760 0.27292 0.01427  -0.01048 -0.01004 82  PRO A N   
1085 C CA  . PRO A 82  ? 0.26357 0.24810 0.27637 0.01546  -0.01106 -0.00875 82  PRO A CA  
1086 C C   . PRO A 82  ? 0.25006 0.23930 0.26490 0.01578  -0.01262 -0.00729 82  PRO A C   
1087 O O   . PRO A 82  ? 0.28334 0.26934 0.29513 0.01520  -0.01288 -0.00603 82  PRO A O   
1088 C CB  . PRO A 82  ? 0.28952 0.27048 0.30054 0.02017  -0.01053 -0.00917 82  PRO A CB  
1089 C CG  . PRO A 82  ? 0.34914 0.33653 0.36292 0.02174  -0.00934 -0.01069 82  PRO A CG  
1090 C CD  . PRO A 82  ? 0.30954 0.29880 0.32305 0.01763  -0.00903 -0.01148 82  PRO A CD  
1091 N N   . VAL A 83  ? 0.25526 0.25217 0.27512 0.01645  -0.01354 -0.00759 83  VAL A N   
1092 C CA  . VAL A 83  ? 0.25247 0.25356 0.27454 0.01617  -0.01600 -0.00737 83  VAL A CA  
1093 C C   . VAL A 83  ? 0.21903 0.21859 0.23972 0.01283  -0.01601 -0.00768 83  VAL A C   
1094 O O   . VAL A 83  ? 0.26449 0.26249 0.28183 0.01326  -0.01718 -0.00763 83  VAL A O   
1095 C CB  . VAL A 83  ? 0.26727 0.27710 0.29718 0.01621  -0.01698 -0.00788 83  VAL A CB  
1096 C CG1 . VAL A 83  ? 0.27474 0.28793 0.30718 0.01495  -0.02041 -0.00877 83  VAL A CG1 
1097 C CG2 . VAL A 83  ? 0.29509 0.30831 0.32756 0.02069  -0.01679 -0.00766 83  VAL A CG2 
1098 N N   . MET A 84  ? 0.24872 0.24870 0.27114 0.01027  -0.01462 -0.00798 84  MET A N   
1099 C CA  . MET A 84  ? 0.24929 0.24833 0.27137 0.00807  -0.01456 -0.00828 84  MET A CA  
1100 C C   . MET A 84  ? 0.30034 0.29538 0.31839 0.00793  -0.01336 -0.00786 84  MET A C   
1101 O O   . MET A 84  ? 0.28512 0.28021 0.30206 0.00771  -0.01319 -0.00809 84  MET A O   
1102 C CB  . MET A 84  ? 0.24783 0.24793 0.27175 0.00642  -0.01375 -0.00815 84  MET A CB  
1103 C CG  . MET A 84  ? 0.28467 0.28832 0.31244 0.00596  -0.01386 -0.00749 84  MET A CG  
1104 S SD  . MET A 84  ? 0.28942 0.29342 0.31632 0.00513  -0.01251 -0.00621 84  MET A SD  
1105 C CE  . MET A 84  ? 0.28210 0.28421 0.30956 0.00411  -0.01386 -0.00608 84  MET A CE  
1106 N N   . LEU A 85  ? 0.24833 0.23956 0.26430 0.00795  -0.01210 -0.00730 85  LEU A N   
1107 C CA  . LEU A 85  ? 0.25026 0.23745 0.26365 0.00681  -0.01027 -0.00618 85  LEU A CA  
1108 C C   . LEU A 85  ? 0.29802 0.28313 0.30647 0.00917  -0.01008 -0.00450 85  LEU A C   
1109 O O   . LEU A 85  ? 0.30176 0.28632 0.30787 0.00856  -0.00818 -0.00345 85  LEU A O   
1110 C CB  . LEU A 85  ? 0.29359 0.27531 0.30603 0.00586  -0.00936 -0.00620 85  LEU A CB  
1111 C CG  . LEU A 85  ? 0.26532 0.24896 0.28103 0.00329  -0.01001 -0.00835 85  LEU A CG  
1112 C CD1 . LEU A 85  ? 0.29028 0.26760 0.30378 0.00323  -0.01015 -0.00991 85  LEU A CD1 
1113 C CD2 . LEU A 85  ? 0.29788 0.28447 0.31735 0.00009  -0.00927 -0.00829 85  LEU A CD2 
1114 N N   A LEU A 86  ? 0.26261 0.24752 0.26924 0.01239  -0.01207 -0.00423 86  LEU A N   
1115 N N   B LEU A 86  ? 0.26111 0.24564 0.26766 0.01238  -0.01195 -0.00414 86  LEU A N   
1116 C CA  A LEU A 86  ? 0.27036 0.25355 0.27090 0.01545  -0.01298 -0.00266 86  LEU A CA  
1117 C CA  B LEU A 86  ? 0.27563 0.25918 0.27661 0.01555  -0.01323 -0.00282 86  LEU A CA  
1118 C C   A LEU A 86  ? 0.30789 0.29502 0.30734 0.01539  -0.01421 -0.00430 86  LEU A C   
1119 C C   B LEU A 86  ? 0.30330 0.29147 0.30428 0.01538  -0.01491 -0.00478 86  LEU A C   
1120 O O   A LEU A 86  ? 0.27760 0.26248 0.27025 0.01667  -0.01299 -0.00312 86  LEU A O   
1121 O O   B LEU A 86  ? 0.29712 0.28373 0.29148 0.01700  -0.01465 -0.00413 86  LEU A O   
1122 C CB  A LEU A 86  ? 0.28614 0.27009 0.28649 0.01949  -0.01585 -0.00240 86  LEU A CB  
1123 C CB  B LEU A 86  ? 0.27728 0.26185 0.27877 0.01940  -0.01597 -0.00269 86  LEU A CB  
1124 C CG  A LEU A 86  ? 0.33929 0.31702 0.33803 0.02178  -0.01477 -0.00067 86  LEU A CG  
1125 C CG  B LEU A 86  ? 0.23950 0.22350 0.23457 0.02353  -0.01856 -0.00132 86  LEU A CG  
1126 C CD1 A LEU A 86  ? 0.47044 0.45218 0.47096 0.02684  -0.01809 -0.00089 86  LEU A CD1 
1127 C CD1 B LEU A 86  ? 0.31351 0.28851 0.29968 0.02455  -0.01555 0.00259  86  LEU A CD1 
1128 C CD2 A LEU A 86  ? 0.41721 0.38517 0.40809 0.02228  -0.01229 0.00301  86  LEU A CD2 
1129 C CD2 B LEU A 86  ? 0.33433 0.32243 0.33243 0.02784  -0.02229 -0.00165 86  LEU A CD2 
1130 N N   A THR A 87  ? 0.28633 0.27846 0.29169 0.01406  -0.01627 -0.00699 87  THR A N   
1131 N N   B THR A 87  ? 0.26400 0.25690 0.27146 0.01363  -0.01644 -0.00716 87  THR A N   
1132 C CA  A THR A 87  ? 0.28623 0.28013 0.29049 0.01406  -0.01775 -0.00934 87  THR A CA  
1133 C CA  B THR A 87  ? 0.26901 0.26419 0.27682 0.01319  -0.01814 -0.00956 87  THR A CA  
1134 C C   A THR A 87  ? 0.23419 0.22668 0.23661 0.01301  -0.01417 -0.00914 87  THR A C   
1135 C C   B THR A 87  ? 0.26271 0.25609 0.26760 0.01251  -0.01509 -0.00956 87  THR A C   
1136 O O   A THR A 87  ? 0.26216 0.25392 0.25894 0.01475  -0.01371 -0.01013 87  THR A O   
1137 O O   B THR A 87  ? 0.26143 0.25456 0.26224 0.01393  -0.01571 -0.01138 87  THR A O   
1138 C CB  A THR A 87  ? 0.36197 0.35962 0.37364 0.01218  -0.02028 -0.01175 87  THR A CB  
1139 C CB  B THR A 87  ? 0.31935 0.31818 0.33507 0.01097  -0.01968 -0.01114 87  THR A CB  
1140 O OG1 A THR A 87  ? 0.32970 0.32789 0.34652 0.00977  -0.01814 -0.01089 87  THR A OG1 
1141 O OG1 B THR A 87  ? 0.25531 0.25787 0.27483 0.01179  -0.02210 -0.01123 87  THR A OG1 
1142 C CG2 A THR A 87  ? 0.28870 0.29014 0.30385 0.01314  -0.02368 -0.01221 87  THR A CG2 
1143 C CG2 B THR A 87  ? 0.41789 0.41659 0.43418 0.01022  -0.02140 -0.01382 87  THR A CG2 
1144 N N   A THR A 88  ? 0.26449 0.25747 0.27181 0.01051  -0.01180 -0.00826 88  THR A N   
1145 N N   B THR A 88  ? 0.25084 0.24347 0.25792 0.01058  -0.01187 -0.00794 88  THR A N   
1146 C CA  A THR A 88  ? 0.30595 0.29964 0.31373 0.00955  -0.00831 -0.00779 88  THR A CA  
1147 C CA  B THR A 88  ? 0.30017 0.29369 0.30751 0.00980  -0.00875 -0.00792 88  THR A CA  
1148 C C   A THR A 88  ? 0.27225 0.26325 0.27298 0.01075  -0.00511 -0.00539 88  THR A C   
1149 C C   B THR A 88  ? 0.27603 0.26709 0.27726 0.01054  -0.00507 -0.00536 88  THR A C   
1150 O O   A THR A 88  ? 0.26597 0.25809 0.26317 0.01220  -0.00272 -0.00579 88  THR A O   
1151 O O   B THR A 88  ? 0.31479 0.30756 0.31435 0.01122  -0.00207 -0.00550 88  THR A O   
1152 C CB  A THR A 88  ? 0.27435 0.26942 0.28843 0.00660  -0.00720 -0.00713 88  THR A CB  
1153 C CB  B THR A 88  ? 0.36040 0.35626 0.37489 0.00707  -0.00791 -0.00787 88  THR A CB  
1154 O OG1 A THR A 88  ? 0.32240 0.31961 0.34101 0.00612  -0.00974 -0.00861 88  THR A OG1 
1155 O OG1 B THR A 88  ? 0.31932 0.31850 0.33691 0.00736  -0.00674 -0.00906 88  THR A OG1 
1156 C CG2 A THR A 88  ? 0.24936 0.24750 0.26643 0.00545  -0.00386 -0.00671 88  THR A CG2 
1157 C CG2 B THR A 88  ? 0.20035 0.19433 0.21554 0.00480  -0.00556 -0.00582 88  THR A CG2 
1158 N N   . VAL A 89  ? 0.27989 0.26661 0.27757 0.01075  -0.00472 -0.00268 89  VAL A N   
1159 C CA  . VAL A 89  ? 0.24370 0.22622 0.23335 0.01205  -0.00135 0.00084  89  VAL A CA  
1160 C C   . VAL A 89  ? 0.30719 0.29011 0.28780 0.01623  -0.00273 -0.00018 89  VAL A C   
1161 O O   . VAL A 89  ? 0.30458 0.28732 0.27902 0.01743  0.00118  0.00113  89  VAL A O   
1162 C CB  . VAL A 89  ? 0.30702 0.28281 0.29389 0.01240  -0.00154 0.00398  89  VAL A CB  
1163 C CG1 . VAL A 89  ? 0.31994 0.29004 0.29608 0.01491  0.00132  0.00847  89  VAL A CG1 
1164 C CG2 . VAL A 89  ? 0.29138 0.26522 0.28562 0.00773  0.00065  0.00452  89  VAL A CG2 
1165 N N   A TYR A 90  ? 0.28017 0.26434 0.26024 0.01840  -0.00830 -0.00294 90  TYR A N   
1166 N N   B TYR A 90  ? 0.27971 0.26358 0.25938 0.01852  -0.00829 -0.00269 90  TYR A N   
1167 C CA  A TYR A 90  ? 0.28542 0.26973 0.25653 0.02226  -0.01107 -0.00489 90  TYR A CA  
1168 C CA  B TYR A 90  ? 0.28739 0.27168 0.25849 0.02227  -0.01108 -0.00486 90  TYR A CA  
1169 C C   A TYR A 90  ? 0.27989 0.26652 0.25069 0.02235  -0.00984 -0.00860 90  TYR A C   
1170 C C   B TYR A 90  ? 0.27945 0.26595 0.25025 0.02218  -0.00911 -0.00813 90  TYR A C   
1171 O O   A TYR A 90  ? 0.28382 0.26928 0.24430 0.02573  -0.00930 -0.00970 90  TYR A O   
1172 O O   B TYR A 90  ? 0.27745 0.26274 0.23830 0.02514  -0.00684 -0.00812 90  TYR A O   
1173 C CB  A TYR A 90  ? 0.31250 0.29916 0.28622 0.02357  -0.01789 -0.00760 90  TYR A CB  
1174 C CB  B TYR A 90  ? 0.31199 0.29888 0.28592 0.02349  -0.01802 -0.00793 90  TYR A CB  
1175 C CG  A TYR A 90  ? 0.29685 0.28227 0.27189 0.02479  -0.01945 -0.00460 90  TYR A CG  
1176 C CG  B TYR A 90  ? 0.31204 0.29794 0.28521 0.02574  -0.02072 -0.00525 90  TYR A CG  
1177 C CD1 A TYR A 90  ? 0.29853 0.27794 0.26667 0.02652  -0.01626 0.00040  90  TYR A CD1 
1178 C CD1 B TYR A 90  ? 0.29486 0.27491 0.26145 0.02753  -0.01759 -0.00015 90  TYR A CD1 
1179 C CD2 A TYR A 90  ? 0.33655 0.32653 0.32014 0.02441  -0.02367 -0.00659 90  TYR A CD2 
1180 C CD2 B TYR A 90  ? 0.30979 0.30066 0.28968 0.02623  -0.02623 -0.00773 90  TYR A CD2 
1181 C CE1 A TYR A 90  ? 0.33898 0.31585 0.30808 0.02860  -0.01784 0.00283  90  TYR A CE1 
1182 C CE1 B TYR A 90  ? 0.33325 0.31146 0.29920 0.03069  -0.02027 0.00217  90  TYR A CE1 
1183 C CE2 A TYR A 90  ? 0.31237 0.30191 0.29759 0.02661  -0.02479 -0.00430 90  TYR A CE2 
1184 C CE2 B TYR A 90  ? 0.25459 0.24594 0.23509 0.02928  -0.02862 -0.00556 90  TYR A CE2 
1185 C CZ  A TYR A 90  ? 0.33963 0.32209 0.31729 0.02908  -0.02218 0.00015  90  TYR A CZ  
1186 C CZ  B TYR A 90  ? 0.29517 0.27973 0.26827 0.03199  -0.02585 -0.00076 90  TYR A CZ  
1187 O OH  A TYR A 90  ? 0.37813 0.35897 0.35746 0.03209  -0.02338 0.00208  90  TYR A OH  
1188 O OH  B TYR A 90  ? 0.22979 0.21400 0.20346 0.03610  -0.02842 0.00128  90  TYR A OH  
1189 N N   . PHE A 91  ? 0.26806 0.25744 0.24897 0.01943  -0.00944 -0.01062 91  PHE A N   
1190 C CA  . PHE A 91  ? 0.29520 0.28593 0.27632 0.02037  -0.00797 -0.01399 91  PHE A CA  
1191 C C   . PHE A 91  ? 0.31023 0.30232 0.28852 0.02112  -0.00104 -0.01156 91  PHE A C   
1192 O O   . PHE A 91  ? 0.30177 0.29404 0.27341 0.02441  0.00118  -0.01370 91  PHE A O   
1193 C CB  . PHE A 91  ? 0.30500 0.29757 0.29686 0.01796  -0.00949 -0.01607 91  PHE A CB  
1194 C CG  . PHE A 91  ? 0.30838 0.30058 0.29952 0.02016  -0.00890 -0.01989 91  PHE A CG  
1195 C CD1 . PHE A 91  ? 0.32488 0.31365 0.31019 0.02237  -0.01284 -0.02451 91  PHE A CD1 
1196 C CD2 . PHE A 91  ? 0.30418 0.29949 0.29993 0.02060  -0.00450 -0.01931 91  PHE A CD2 
1197 C CE1 . PHE A 91  ? 0.33752 0.32406 0.32085 0.02511  -0.01231 -0.02881 91  PHE A CE1 
1198 C CE2 . PHE A 91  ? 0.33532 0.32988 0.32987 0.02398  -0.00365 -0.02311 91  PHE A CE2 
1199 C CZ  . PHE A 91  ? 0.34353 0.33275 0.33108 0.02642  -0.00734 -0.02797 91  PHE A CZ  
1200 N N   . PHE A 92  ? 0.29430 0.28745 0.27767 0.01803  0.00267  -0.00730 92  PHE A N   
1201 C CA  . PHE A 92  ? 0.27284 0.26842 0.25551 0.01772  0.00980  -0.00438 92  PHE A CA  
1202 C C   . PHE A 92  ? 0.31783 0.30983 0.28630 0.02116  0.01269  -0.00196 92  PHE A C   
1203 O O   . PHE A 92  ? 0.32691 0.32134 0.29050 0.02352  0.01804  -0.00181 92  PHE A O   
1204 C CB  . PHE A 92  ? 0.29978 0.29650 0.29154 0.01271  0.01239  -0.00070 92  PHE A CB  
1205 C CG  . PHE A 92  ? 0.27083 0.27367 0.27548 0.01020  0.01166  -0.00286 92  PHE A CG  
1206 C CD1 . PHE A 92  ? 0.30693 0.31670 0.31678 0.01116  0.01551  -0.00388 92  PHE A CD1 
1207 C CD2 . PHE A 92  ? 0.37683 0.37897 0.38786 0.00766  0.00717  -0.00381 92  PHE A CD2 
1208 C CE1 . PHE A 92  ? 0.35755 0.37349 0.37916 0.00977  0.01403  -0.00565 92  PHE A CE1 
1209 C CE2 . PHE A 92  ? 0.41533 0.42308 0.43661 0.00605  0.00594  -0.00551 92  PHE A CE2 
1210 C CZ  . PHE A 92  ? 0.39823 0.41283 0.42485 0.00726  0.00895  -0.00636 92  PHE A CZ  
1211 N N   A GLU A 93  ? 0.29956 0.28607 0.26070 0.02221  0.00927  0.00006  93  GLU A N   
1212 N N   B GLU A 93  ? 0.29953 0.28601 0.26070 0.02214  0.00944  0.00023  93  GLU A N   
1213 C CA  A GLU A 93  ? 0.33776 0.32010 0.28334 0.02637  0.01094  0.00286  93  GLU A CA  
1214 C CA  B GLU A 93  ? 0.33695 0.31935 0.28248 0.02638  0.01111  0.00290  93  GLU A CA  
1215 C C   A GLU A 93  ? 0.32452 0.30789 0.26044 0.03131  0.00860  -0.00241 93  GLU A C   
1216 C C   B GLU A 93  ? 0.32628 0.30989 0.26261 0.03122  0.00886  -0.00250 93  GLU A C   
1217 O O   A GLU A 93  ? 0.35525 0.33783 0.27893 0.03495  0.01314  -0.00113 93  GLU A O   
1218 O O   B GLU A 93  ? 0.34793 0.33123 0.27295 0.03467  0.01380  -0.00142 93  GLU A O   
1219 C CB  A GLU A 93  ? 0.33334 0.31020 0.27445 0.02744  0.00610  0.00547  93  GLU A CB  
1220 C CB  B GLU A 93  ? 0.33381 0.31056 0.27405 0.02768  0.00635  0.00559  93  GLU A CB  
1221 C CG  A GLU A 93  ? 0.33936 0.31206 0.28557 0.02372  0.00951  0.01112  93  GLU A CG  
1222 C CG  B GLU A 93  ? 0.34936 0.32135 0.29328 0.02435  0.00987  0.01174  93  GLU A CG  
1223 C CD  A GLU A 93  ? 0.39070 0.35856 0.32720 0.02424  0.01688  0.01793  93  GLU A CD  
1224 C CD  B GLU A 93  ? 0.38796 0.35556 0.32217 0.02486  0.01757  0.01841  93  GLU A CD  
1225 O OE1 A GLU A 93  ? 0.55516 0.51776 0.47739 0.02904  0.01581  0.02095  93  GLU A OE1 
1226 O OE1 B GLU A 93  ? 0.28791 0.25706 0.21134 0.02851  0.02047  0.01831  93  GLU A OE1 
1227 O OE2 A GLU A 93  ? 0.50347 0.47325 0.44672 0.01986  0.02381  0.02051  93  GLU A OE2 
1228 O OE2 B GLU A 93  ? 0.29806 0.26008 0.23504 0.02154  0.02108  0.02375  93  GLU A OE2 
1229 N N   . TYR A 94  ? 0.35767 0.34229 0.29865 0.03139  0.00180  -0.00850 94  TYR A N   
1230 C CA  . TYR A 94  ? 0.33858 0.32284 0.27172 0.03539  -0.00109 -0.01480 94  TYR A CA  
1231 C C   . TYR A 94  ? 0.32102 0.30798 0.25417 0.03695  0.00575  -0.01637 94  TYR A C   
1232 O O   . TYR A 94  ? 0.35078 0.33662 0.27083 0.04184  0.00819  -0.01844 94  TYR A O   
1233 C CB  . TYR A 94  ? 0.31519 0.29970 0.25733 0.03348  -0.00881 -0.02037 94  TYR A CB  
1234 C CG  . TYR A 94  ? 0.35764 0.34036 0.29511 0.03633  -0.01170 -0.02780 94  TYR A CG  
1235 C CD1 . TYR A 94  ? 0.37248 0.35233 0.29562 0.04063  -0.01599 -0.03174 94  TYR A CD1 
1236 C CD2 . TYR A 94  ? 0.32374 0.30678 0.27049 0.03511  -0.01069 -0.03116 94  TYR A CD2 
1237 C CE1 . TYR A 94  ? 0.38010 0.35684 0.29851 0.04310  -0.01920 -0.03961 94  TYR A CE1 
1238 C CE2 . TYR A 94  ? 0.39541 0.37469 0.33797 0.03788  -0.01343 -0.03827 94  TYR A CE2 
1239 C CZ  . TYR A 94  ? 0.41892 0.39472 0.34717 0.04169  -0.01762 -0.04289 94  TYR A CZ  
1240 O OH  . TYR A 94  ? 0.43547 0.40610 0.35859 0.04447  -0.02080 -0.05104 94  TYR A OH  
1241 N N   . MET A 95  ? 0.31463 0.30573 0.26229 0.03347  0.00862  -0.01579 95  MET A N   
1242 C CA  . MET A 95  ? 0.37127 0.36675 0.32174 0.03549  0.01482  -0.01737 95  MET A CA  
1243 C C   . MET A 95  ? 0.39079 0.38892 0.33370 0.03716  0.02385  -0.01253 95  MET A C   
1244 O O   . MET A 95  ? 0.39968 0.40056 0.33741 0.04155  0.02915  -0.01475 95  MET A O   
1245 C CB  . MET A 95  ? 0.34060 0.34130 0.30872 0.03137  0.01573  -0.01635 95  MET A CB  
1246 C CG  . MET A 95  ? 0.51122 0.51095 0.48643 0.03206  0.01082  -0.02163 95  MET A CG  
1247 S SD  . MET A 95  ? 0.44224 0.45029 0.43448 0.03049  0.01437  -0.02031 95  MET A SD  
1248 C CE  . MET A 95  ? 0.37093 0.38155 0.37088 0.02369  0.01450  -0.01427 95  MET A CE  
1249 N N   . ASN A 96  ? 0.32774 0.32460 0.26980 0.03391  0.02627  -0.00577 96  ASN A N   
1250 C CA  . ASN A 96  ? 0.34851 0.34852 0.28899 0.03300  0.03613  0.00053  96  ASN A CA  
1251 C C   . ASN A 96  ? 0.41931 0.41367 0.34037 0.03671  0.03915  0.00476  96  ASN A C   
1252 O O   . ASN A 96  ? 0.46202 0.45891 0.37880 0.03713  0.04865  0.00977  96  ASN A O   
1253 C CB  . ASN A 96  ? 0.37709 0.37924 0.33266 0.02573  0.03805  0.00561  96  ASN A CB  
1254 C CG  . ASN A 96  ? 0.35330 0.36341 0.32710 0.02288  0.03712  0.00223  96  ASN A CG  
1255 O OD1 . ASN A 96  ? 0.35153 0.36686 0.32749 0.02653  0.03847  -0.00204 96  ASN A OD1 
1256 N ND2 . ASN A 96  ? 0.31480 0.32524 0.30068 0.01716  0.03437  0.00382  96  ASN A ND2 
1257 N N   . SER A 97  ? 0.45891 0.44640 0.36829 0.03957  0.03151  0.00321  97  SER A N   
1258 C CA  A SER A 97  ? 0.45833 0.44027 0.34729 0.04431  0.03316  0.00716  97  SER A CA  
1259 C CA  B SER A 97  ? 0.45885 0.44077 0.34780 0.04432  0.03312  0.00714  97  SER A CA  
1260 C C   . SER A 97  ? 0.46319 0.44599 0.33704 0.05129  0.03416  0.00159  97  SER A C   
1261 O O   . SER A 97  ? 0.55256 0.53544 0.42703 0.05345  0.02708  -0.00694 97  SER A O   
1262 C CB  A SER A 97  ? 0.51731 0.49289 0.40062 0.04532  0.02362  0.00747  97  SER A CB  
1263 C CB  B SER A 97  ? 0.51737 0.49301 0.40081 0.04534  0.02345  0.00727  97  SER A CB  
1264 O OG  A SER A 97  ? 0.56906 0.54399 0.46769 0.03957  0.02125  0.00996  97  SER A OG  
1265 O OG  B SER A 97  ? 0.57029 0.54666 0.45325 0.04774  0.01410  -0.00141 97  SER A OG  
1266 N N   . ASP A 98  ? 0.63089 0.61368 0.49069 0.05480  0.04335  0.00640  98  ASP A N   
1267 C CA  . ASP A 98  ? 0.97928 0.96219 0.82134 0.06251  0.04509  0.00110  98  ASP A CA  
1268 C C   . ASP A 98  ? 0.76051 0.73644 0.58413 0.06787  0.03460  -0.00315 98  ASP A C   
1269 O O   . ASP A 98  ? 0.87822 0.85329 0.69209 0.07305  0.03023  -0.01203 98  ASP A O   
1270 C CB  . ASP A 98  ? 0.85895 0.84408 0.68963 0.06503  0.05862  0.00839  98  ASP A CB  
1271 N N   . ASP A 99  ? 0.55854 0.52948 0.37781 0.06690  0.02999  0.00260  99  ASP A N   
1272 C CA  . ASP A 99  ? 0.76785 0.73404 0.57290 0.07162  0.01865  -0.00101 99  ASP A CA  
1273 C C   . ASP A 99  ? 0.73567 0.70286 0.55831 0.06703  0.00764  -0.00546 99  ASP A C   
1274 O O   . ASP A 99  ? 0.61357 0.58309 0.45591 0.06057  0.00940  -0.00304 99  ASP A O   
1275 C CB  . ASP A 99  ? 0.71442 0.67470 0.50278 0.07483  0.02044  0.00885  99  ASP A CB  
1276 N N   . GLY A 100 ? 0.57723 0.54318 0.39250 0.07044  -0.00381 -0.01209 100 GLY A N   
1277 C CA  . GLY A 100 ? 0.41676 0.38480 0.24844 0.06629  -0.01384 -0.01588 100 GLY A CA  
1278 C C   . GLY A 100 ? 0.54036 0.50732 0.37901 0.06390  -0.01392 -0.00733 100 GLY A C   
1279 O O   . GLY A 100 ? 0.60025 0.56307 0.42434 0.06817  -0.01290 -0.00064 100 GLY A O   
1280 N N   . ILE A 101 ? 0.47109 0.44077 0.33059 0.05768  -0.01485 -0.00731 101 ILE A N   
1281 C CA  . ILE A 101 ? 0.41008 0.37816 0.27756 0.05543  -0.01484 -0.00044 101 ILE A CA  
1282 C C   . ILE A 101 ? 0.40246 0.37501 0.28504 0.05287  -0.02396 -0.00527 101 ILE A C   
1283 O O   . ILE A 101 ? 0.40837 0.38485 0.30144 0.04965  -0.02671 -0.01208 101 ILE A O   
1284 C CB  . ILE A 101 ? 0.42037 0.38748 0.29847 0.04997  -0.00477 0.00518  101 ILE A CB  
1285 C CG1 . ILE A 101 ? 0.49425 0.45745 0.37872 0.04803  -0.00481 0.01164  101 ILE A CG1 
1286 C CG2 . ILE A 101 ? 0.48596 0.45836 0.38111 0.04475  -0.00409 -0.00034 101 ILE A CG2 
1287 C CD1 . ILE A 101 ? 0.51861 0.47527 0.39638 0.04747  0.00422  0.02063  101 ILE A CD1 
1288 N N   A ARG A 102 ? 0.41572 0.38755 0.30006 0.05441  -0.02812 -0.00140 102 ARG A N   
1289 N N   B ARG A 102 ? 0.41989 0.39164 0.30312 0.05480  -0.02835 -0.00146 102 ARG A N   
1290 C CA  A ARG A 102 ? 0.42216 0.39974 0.32227 0.05204  -0.03538 -0.00514 102 ARG A CA  
1291 C CA  B ARG A 102 ? 0.41702 0.39435 0.31331 0.05373  -0.03683 -0.00500 102 ARG A CA  
1292 C C   A ARG A 102 ? 0.41390 0.38958 0.32428 0.04984  -0.03219 0.00055  102 ARG A C   
1293 C C   B ARG A 102 ? 0.42115 0.39752 0.33081 0.05032  -0.03337 -0.00026 102 ARG A C   
1294 O O   A ARG A 102 ? 0.32045 0.28915 0.22337 0.05152  -0.02703 0.00763  102 ARG A O   
1295 O O   B ARG A 102 ? 0.37600 0.34709 0.28562 0.04802  -0.02533 0.00489  102 ARG A O   
1296 C CB  A ARG A 102 ? 0.49898 0.48073 0.39411 0.05691  -0.04620 -0.00874 102 ARG A CB  
1297 C CB  B ARG A 102 ? 0.43811 0.41694 0.32400 0.06039  -0.04585 -0.00536 102 ARG A CB  
1298 C CG  A ARG A 102 ? 0.51924 0.50292 0.40604 0.05835  -0.05139 -0.01671 102 ARG A CG  
1299 C CG  B ARG A 102 ? 0.46837 0.44894 0.34168 0.06370  -0.05180 -0.01220 102 ARG A CG  
1300 C CD  A ARG A 102 ? 0.47120 0.46059 0.35617 0.06211  -0.06347 -0.02118 102 ARG A CD  
1301 C CD  B ARG A 102 ? 0.51597 0.50191 0.40296 0.05837  -0.05580 -0.02135 102 ARG A CD  
1302 N N   A LYS A 103 ? 0.33670 0.31799 0.26391 0.04603  -0.03514 -0.00275 103 LYS A N   
1303 N N   B LYS A 103 ? 0.32926 0.31117 0.25100 0.04988  -0.03945 -0.00241 103 LYS A N   
1304 C CA  A LYS A 103 ? 0.38583 0.36536 0.32325 0.04356  -0.03163 0.00105  103 LYS A CA  
1305 C CA  B LYS A 103 ? 0.40729 0.38796 0.34041 0.04743  -0.03615 0.00117  103 LYS A CA  
1306 C C   A LYS A 103 ? 0.34729 0.32182 0.27824 0.04884  -0.03268 0.00682  103 LYS A C   
1307 C C   B LYS A 103 ? 0.37491 0.34858 0.29945 0.05261  -0.03529 0.00814  103 LYS A C   
1308 O O   A LYS A 103 ? 0.37462 0.34331 0.30880 0.04747  -0.02797 0.01102  103 LYS A O   
1309 O O   B LYS A 103 ? 0.29858 0.26518 0.22462 0.05068  -0.02908 0.01281  103 LYS A O   
1310 C CB  A LYS A 103 ? 0.35741 0.34441 0.31187 0.03976  -0.03472 -0.00326 103 LYS A CB  
1311 C CB  B LYS A 103 ? 0.40007 0.38955 0.35011 0.04477  -0.04089 -0.00334 103 LYS A CB  
1312 C CG  A LYS A 103 ? 0.40957 0.40303 0.36941 0.04321  -0.04201 -0.00453 103 LYS A CG  
1313 C CG  B LYS A 103 ? 0.53699 0.53138 0.49082 0.04957  -0.04726 -0.00266 103 LYS A CG  
1314 C CD  A LYS A 103 ? 0.49870 0.50054 0.47578 0.03886  -0.04376 -0.00838 103 LYS A CD  
1315 C CD  B LYS A 103 ? 0.53413 0.53750 0.50650 0.04596  -0.04888 -0.00592 103 LYS A CD  
1316 N N   A LYS A 104 ? 0.36183 0.33786 0.28350 0.05513  -0.03919 0.00695  104 LYS A N   
1317 N N   B LYS A 104 ? 0.40007 0.37460 0.31465 0.05938  -0.04169 0.00897  104 LYS A N   
1318 C CA  A LYS A 104 ? 0.44162 0.41202 0.35670 0.06128  -0.04044 0.01307  104 LYS A CA  
1319 C CA  B LYS A 104 ? 0.45462 0.42165 0.36099 0.06542  -0.04162 0.01607  104 LYS A CA  
1320 C C   A LYS A 104 ? 0.37003 0.32777 0.27131 0.06207  -0.03262 0.02071  104 LYS A C   
1321 C C   B LYS A 104 ? 0.50266 0.45707 0.39648 0.06484  -0.03267 0.02338  104 LYS A C   
1322 O O   A LYS A 104 ? 0.35945 0.30879 0.26133 0.06284  -0.02918 0.02622  104 LYS A O   
1323 O O   B LYS A 104 ? 0.38249 0.32764 0.27509 0.06618  -0.02923 0.02955  104 LYS A O   
1324 C CB  A LYS A 104 ? 0.42641 0.40235 0.33477 0.06859  -0.05019 0.01163  104 LYS A CB  
1325 C CB  B LYS A 104 ? 0.40442 0.37529 0.30071 0.07355  -0.05086 0.01571  104 LYS A CB  
1326 C CG  A LYS A 104 ? 0.51286 0.48078 0.40976 0.07669  -0.05126 0.01928  104 LYS A CG  
1327 C CG  B LYS A 104 ? 0.41419 0.37502 0.29703 0.08126  -0.05058 0.02428  104 LYS A CG  
1328 C CD  A LYS A 104 ? 0.57230 0.54788 0.46489 0.08465  -0.06236 0.01756  104 LYS A CD  
1329 C CD  B LYS A 104 ? 0.71498 0.68201 0.59152 0.09009  -0.06150 0.02350  104 LYS A CD  
1330 C CE  A LYS A 104 ? 0.77883 0.74428 0.65365 0.09399  -0.06336 0.02610  104 LYS A CE  
1331 C CE  B LYS A 104 ? 0.71963 0.69259 0.61152 0.09339  -0.06626 0.02323  104 LYS A CE  
1332 N NZ  A LYS A 104 ? 0.67153 0.62969 0.55223 0.09699  -0.06061 0.03189  104 LYS A NZ  
1333 N NZ  B LYS A 104 ? 0.64518 0.60472 0.53550 0.09541  -0.05960 0.03094  104 LYS A NZ  
1334 N N   A GLU A 105 ? 0.38211 0.33792 0.27087 0.06194  -0.02940 0.02116  105 GLU A N   
1335 N N   B GLU A 105 ? 0.39039 0.34402 0.27531 0.06282  -0.02844 0.02282  105 GLU A N   
1336 C CA  A GLU A 105 ? 0.41178 0.35682 0.28855 0.06177  -0.02059 0.02893  105 GLU A CA  
1337 C CA  B GLU A 105 ? 0.42184 0.36520 0.29616 0.06174  -0.01902 0.03021  105 GLU A CA  
1338 C C   A GLU A 105 ? 0.38647 0.32774 0.27600 0.05434  -0.01298 0.03070  105 GLU A C   
1339 C C   B GLU A 105 ? 0.39393 0.33480 0.28193 0.05372  -0.01137 0.03113  105 GLU A C   
1340 O O   A GLU A 105 ? 0.37778 0.30862 0.26454 0.05388  -0.00794 0.03761  105 GLU A O   
1341 O O   B GLU A 105 ? 0.43466 0.36568 0.31896 0.05211  -0.00450 0.03814  105 GLU A O   
1342 C CB  A GLU A 105 ? 0.47103 0.41726 0.33456 0.06235  -0.01725 0.02788  105 GLU A CB  
1343 C CB  B GLU A 105 ? 0.49680 0.44145 0.35668 0.06320  -0.01642 0.02928  105 GLU A CB  
1344 C CG  A GLU A 105 ? 0.44190 0.38008 0.29780 0.05967  -0.00553 0.03531  105 GLU A CG  
1345 C CG  B GLU A 105 ? 0.63833 0.59290 0.50646 0.05993  -0.01914 0.01985  105 GLU A CG  
1346 C CD  A GLU A 105 ? 0.67295 0.61276 0.51334 0.06208  -0.00150 0.03476  105 GLU A CD  
1347 C CD  B GLU A 105 ? 0.61566 0.57174 0.46696 0.06441  -0.02060 0.01678  105 GLU A CD  
1348 O OE1 A GLU A 105 ? 0.54393 0.48789 0.37425 0.06738  -0.00851 0.02967  105 GLU A OE1 
1349 O OE1 B GLU A 105 ? 0.63121 0.58314 0.47100 0.06487  -0.01220 0.02083  105 GLU A OE1 
1350 O OE2 A GLU A 105 ? 0.66929 0.60666 0.50792 0.05865  0.00881  0.03906  105 GLU A OE2 
1351 O OE2 B GLU A 105 ? 0.55460 0.51625 0.40431 0.06743  -0.03009 0.01009  105 GLU A OE2 
1352 N N   . ILE A 106 ? 0.35143 0.30061 0.25489 0.04856  -0.01266 0.02435  106 ILE A N   
1353 C CA  . ILE A 106 ? 0.34920 0.29698 0.26573 0.04155  -0.00710 0.02452  106 ILE A CA  
1354 C C   . ILE A 106 ? 0.37199 0.31430 0.29492 0.04207  -0.00872 0.02650  106 ILE A C   
1355 O O   . ILE A 106 ? 0.40363 0.33689 0.32758 0.03919  -0.00347 0.03091  106 ILE A O   
1356 C CB  . ILE A 106 ? 0.28969 0.24740 0.21874 0.03696  -0.00837 0.01718  106 ILE A CB  
1357 C CG1 . ILE A 106 ? 0.34045 0.30162 0.26278 0.03690  -0.00550 0.01527  106 ILE A CG1 
1358 C CG2 . ILE A 106 ? 0.33873 0.29593 0.28116 0.03036  -0.00411 0.01690  106 ILE A CG2 
1359 C CD1 . ILE A 106 ? 0.36486 0.33439 0.29597 0.03482  -0.00883 0.00767  106 ILE A CD1 
1360 N N   A ASN A 107 ? 0.35230 0.29990 0.27983 0.04587  -0.01590 0.02312  107 ASN A N   
1361 N N   B ASN A 107 ? 0.35417 0.30222 0.28275 0.04540  -0.01580 0.02274  107 ASN A N   
1362 C CA  A ASN A 107 ? 0.36663 0.31040 0.30124 0.04717  -0.01716 0.02391  107 ASN A CA  
1363 C CA  B ASN A 107 ? 0.36824 0.31194 0.30261 0.04734  -0.01724 0.02399  107 ASN A CA  
1364 C C   A ASN A 107 ? 0.40491 0.33561 0.32857 0.05235  -0.01585 0.03123  107 ASN A C   
1365 C C   B ASN A 107 ? 0.38743 0.31733 0.31022 0.05157  -0.01482 0.03169  107 ASN A C   
1366 O O   A ASN A 107 ? 0.39835 0.31983 0.32542 0.05135  -0.01310 0.03341  107 ASN A O   
1367 O O   B ASN A 107 ? 0.35006 0.26973 0.27515 0.04891  -0.01035 0.03460  107 ASN A O   
1368 C CB  A ASN A 107 ? 0.34340 0.29799 0.28650 0.05042  -0.02445 0.01888  107 ASN A CB  
1369 C CB  B ASN A 107 ? 0.32669 0.28007 0.26677 0.05215  -0.02512 0.01999  107 ASN A CB  
1370 C CG  A ASN A 107 ? 0.35701 0.32163 0.31278 0.04462  -0.02474 0.01266  107 ASN A CG  
1371 C CG  B ASN A 107 ? 0.35434 0.32018 0.30574 0.04778  -0.02753 0.01310  107 ASN A CG  
1372 O OD1 A ASN A 107 ? 0.35746 0.32038 0.31767 0.03873  -0.01988 0.01188  107 ASN A OD1 
1373 O OD1 B ASN A 107 ? 0.45731 0.43218 0.41069 0.05022  -0.03373 0.00965  107 ASN A OD1 
1374 N ND2 A ASN A 107 ? 0.37830 0.35361 0.34059 0.04622  -0.03069 0.00840  107 ASN A ND2 
1375 N ND2 B ASN A 107 ? 0.33203 0.29815 0.29125 0.04122  -0.02299 0.01111  107 ASN A ND2 
1376 N N   . ASP A 108 ? 0.37135 0.29993 0.28081 0.05827  -0.01802 0.03510  108 ASP A N   
1377 C CA  . ASP A 108 ? 0.36742 0.28240 0.26497 0.06402  -0.01693 0.04310  108 ASP A CA  
1378 C C   . ASP A 108 ? 0.44025 0.34234 0.33262 0.05866  -0.00757 0.04939  108 ASP A C   
1379 O O   . ASP A 108 ? 0.46187 0.34958 0.34934 0.06053  -0.00492 0.05574  108 ASP A O   
1380 C CB  . ASP A 108 ? 0.40567 0.32196 0.28746 0.07216  -0.02196 0.04597  108 ASP A CB  
1381 C CG  . ASP A 108 ? 0.48569 0.41373 0.37288 0.07845  -0.03225 0.04092  108 ASP A CG  
1382 O OD1 . ASP A 108 ? 0.48411 0.41778 0.38649 0.07756  -0.03455 0.03672  108 ASP A OD1 
1383 O OD2 . ASP A 108 ? 0.49087 0.42340 0.36698 0.08417  -0.03800 0.04093  108 ASP A OD2 
1384 N N   . ARG A 109 ? 0.40583 0.31283 0.29976 0.05212  -0.00244 0.04784  109 ARG A N   
1385 C CA  . ARG A 109 ? 0.43873 0.33623 0.32965 0.04642  0.00689  0.05388  109 ARG A CA  
1386 C C   . ARG A 109 ? 0.41820 0.31345 0.32484 0.03833  0.01008  0.05121  109 ARG A C   
1387 O O   . ARG A 109 ? 0.46133 0.34389 0.36781 0.03461  0.01554  0.05656  109 ARG A O   
1388 C CB  . ARG A 109 ? 0.42938 0.33501 0.31588 0.04372  0.01133  0.05313  109 ARG A CB  
1389 C CG  . ARG A 109 ? 0.48464 0.38346 0.36907 0.03778  0.02190  0.05977  109 ARG A CG  
1390 C CD  . ARG A 109 ? 0.45297 0.36297 0.33656 0.03537  0.02649  0.05726  109 ARG A CD  
1391 N NE  . ARG A 109 ? 0.47709 0.39886 0.37774 0.03026  0.02442  0.04861  109 ARG A NE  
1392 C CZ  . ARG A 109 ? 0.59507 0.52820 0.49726 0.03028  0.02437  0.04316  109 ARG A CZ  
1393 N NH1 . ARG A 109 ? 0.52215 0.45726 0.40956 0.03526  0.02596  0.04420  109 ARG A NH1 
1394 N NH2 . ARG A 109 ? 0.49537 0.43719 0.41322 0.02571  0.02266  0.03646  109 ARG A NH2 
1395 N N   . ASP A 110 ? 0.38335 0.28999 0.30307 0.03549  0.00653  0.04308  110 ASP A N   
1396 C CA  . ASP A 110 ? 0.37830 0.28563 0.31176 0.02747  0.00941  0.03966  110 ASP A CA  
1397 C C   . ASP A 110 ? 0.37219 0.27767 0.31423 0.02824  0.00508  0.03527  110 ASP A C   
1398 O O   . ASP A 110 ? 0.36224 0.27053 0.31501 0.02240  0.00590  0.03091  110 ASP A O   
1399 C CB  . ASP A 110 ? 0.38358 0.30501 0.32497 0.02305  0.01001  0.03420  110 ASP A CB  
1400 C CG  . ASP A 110 ? 0.35899 0.28232 0.29468 0.02091  0.01639  0.03791  110 ASP A CG  
1401 O OD1 . ASP A 110 ? 0.42569 0.33921 0.35244 0.02103  0.02168  0.04536  110 ASP A OD1 
1402 O OD2 . ASP A 110 ? 0.41639 0.35091 0.35624 0.01952  0.01643  0.03351  110 ASP A OD2 
1403 N N   . TYR A 111 ? 0.35574 0.25716 0.29317 0.03581  0.00053  0.03617  111 TYR A N   
1404 C CA  . TYR A 111 ? 0.35041 0.25361 0.29664 0.03744  -0.00323 0.03092  111 TYR A CA  
1405 C C   . TYR A 111 ? 0.34780 0.24039 0.29958 0.03209  0.00003  0.02988  111 TYR A C   
1406 O O   . TYR A 111 ? 0.35868 0.25652 0.31941 0.02977  -0.00147 0.02375  111 TYR A O   
1407 C CB  . TYR A 111 ? 0.37600 0.27791 0.31787 0.04720  -0.00836 0.03211  111 TYR A CB  
1408 C CG  . TYR A 111 ? 0.39093 0.27603 0.32153 0.05201  -0.00680 0.03968  111 TYR A CG  
1409 C CD1 . TYR A 111 ? 0.39980 0.28218 0.31739 0.05589  -0.00667 0.04604  111 TYR A CD1 
1410 C CD2 . TYR A 111 ? 0.40035 0.27093 0.33203 0.05319  -0.00546 0.04057  111 TYR A CD2 
1411 C CE1 . TYR A 111 ? 0.46827 0.33403 0.37428 0.06072  -0.00502 0.05406  111 TYR A CE1 
1412 C CE2 . TYR A 111 ? 0.42281 0.27576 0.34387 0.05790  -0.00398 0.04806  111 TYR A CE2 
1413 C CZ  . TYR A 111 ? 0.44599 0.29639 0.35417 0.06160  -0.00359 0.05537  111 TYR A CZ  
1414 O OH  . TYR A 111 ? 0.46110 0.29293 0.35746 0.06652  -0.00181 0.06391  111 TYR A OH  
1415 N N   . VAL A 112 ? 0.37658 0.25407 0.32295 0.02968  0.00448  0.03565  112 VAL A N   
1416 C CA  . VAL A 112 ? 0.42253 0.28929 0.37493 0.02357  0.00689  0.03376  112 VAL A CA  
1417 C C   . VAL A 112 ? 0.40153 0.27916 0.36453 0.01480  0.00819  0.02863  112 VAL A C   
1418 O O   . VAL A 112 ? 0.37808 0.25692 0.34838 0.01218  0.00625  0.02247  112 VAL A O   
1419 C CB  . VAL A 112 ? 0.44143 0.28944 0.38729 0.02124  0.01183  0.04138  112 VAL A CB  
1420 C CG1 . VAL A 112 ? 0.46198 0.29980 0.41610 0.01299  0.01377  0.03809  112 VAL A CG1 
1421 C CG2 . VAL A 112 ? 0.46372 0.29863 0.39873 0.03109  0.00986  0.04649  112 VAL A CG2 
1422 N N   . TYR A 113 ? 0.34771 0.23339 0.31105 0.01080  0.01148  0.03110  113 TYR A N   
1423 C CA  . TYR A 113 ? 0.36323 0.26025 0.33721 0.00345  0.01250  0.02664  113 TYR A CA  
1424 C C   . TYR A 113 ? 0.31587 0.22567 0.29528 0.00563  0.00746  0.01962  113 TYR A C   
1425 O O   . TYR A 113 ? 0.36604 0.28002 0.35373 0.00120  0.00623  0.01457  113 TYR A O   
1426 C CB  . TYR A 113 ? 0.38955 0.29409 0.36200 0.00111  0.01708  0.03054  113 TYR A CB  
1427 C CG  . TYR A 113 ? 0.41650 0.32994 0.40064 -0.00691 0.01966  0.02787  113 TYR A CG  
1428 C CD1 . TYR A 113 ? 0.40877 0.31564 0.39852 -0.01449 0.02445  0.03082  113 TYR A CD1 
1429 C CD2 . TYR A 113 ? 0.39392 0.32236 0.38429 -0.00696 0.01722  0.02267  113 TYR A CD2 
1430 C CE1 . TYR A 113 ? 0.45611 0.37315 0.45842 -0.02171 0.02633  0.02828  113 TYR A CE1 
1431 C CE2 . TYR A 113 ? 0.35286 0.29038 0.35451 -0.01338 0.01916  0.02044  113 TYR A CE2 
1432 C CZ  . TYR A 113 ? 0.41947 0.35211 0.42752 -0.02064 0.02350  0.02310  113 TYR A CZ  
1433 O OH  . TYR A 113 ? 0.34388 0.28703 0.36485 -0.02703 0.02513  0.02099  113 TYR A OH  
1434 N N   . LEU A 114 ? 0.32129 0.23736 0.29608 0.01229  0.00434  0.01939  114 LEU A N   
1435 C CA  . LEU A 114 ? 0.34506 0.27253 0.32524 0.01409  0.00019  0.01370  114 LEU A CA  
1436 C C   . LEU A 114 ? 0.36484 0.28800 0.34844 0.01499  -0.00185 0.00978  114 LEU A C   
1437 O O   . LEU A 114 ? 0.33570 0.26607 0.32538 0.01282  -0.00332 0.00497  114 LEU A O   
1438 C CB  . LEU A 114 ? 0.33106 0.26486 0.30642 0.02052  -0.00293 0.01447  114 LEU A CB  
1439 C CG  . LEU A 114 ? 0.36363 0.30283 0.33488 0.01969  -0.00126 0.01652  114 LEU A CG  
1440 C CD1 . LEU A 114 ? 0.42830 0.37270 0.39372 0.02597  -0.00544 0.01654  114 LEU A CD1 
1441 C CD2 . LEU A 114 ? 0.40617 0.35510 0.38535 0.01469  -0.00048 0.01262  114 LEU A CD2 
1442 N N   . PHE A 115 ? 0.38368 0.29422 0.36244 0.01862  -0.00171 0.01186  115 PHE A N   
1443 C CA  . PHE A 115 ? 0.37223 0.27706 0.35302 0.02010  -0.00310 0.00754  115 PHE A CA  
1444 C C   . PHE A 115 ? 0.35321 0.25488 0.33895 0.01246  -0.00207 0.00380  115 PHE A C   
1445 O O   . PHE A 115 ? 0.38602 0.29109 0.37479 0.01231  -0.00395 -0.00182 115 PHE A O   
1446 C CB  . PHE A 115 ? 0.41940 0.30969 0.39373 0.02624  -0.00309 0.01047  115 PHE A CB  
1447 C CG  . PHE A 115 ? 0.45279 0.33419 0.42807 0.02764  -0.00374 0.00559  115 PHE A CG  
1448 C CD1 . PHE A 115 ? 0.70021 0.58920 0.67766 0.03344  -0.00583 0.00108  115 PHE A CD1 
1449 C CD2 . PHE A 115 ? 0.46263 0.32851 0.43693 0.02286  -0.00204 0.00509  115 PHE A CD2 
1450 C CE1 . PHE A 115 ? 0.64495 0.52550 0.62170 0.03557  -0.00593 -0.00403 115 PHE A CE1 
1451 C CE2 . PHE A 115 ? 0.68986 0.54601 0.66369 0.02446  -0.00307 -0.00055 115 PHE A CE2 
1452 C CZ  . PHE A 115 ? 0.56674 0.43023 0.54098 0.03124  -0.00489 -0.00525 115 PHE A CZ  
1453 N N   . TYR A 116 ? 0.35818 0.25451 0.34505 0.00596  0.00088  0.00681  116 TYR A N   
1454 C CA  . TYR A 116 ? 0.38812 0.28390 0.38189 -0.00202 0.00098  0.00287  116 TYR A CA  
1455 C C   . TYR A 116 ? 0.35882 0.27093 0.35883 -0.00412 -0.00115 -0.00143 116 TYR A C   
1456 O O   . TYR A 116 ? 0.35402 0.26742 0.35743 -0.00664 -0.00363 -0.00696 116 TYR A O   
1457 C CB  . TYR A 116 ? 0.36278 0.25400 0.35939 -0.00915 0.00510  0.00746  116 TYR A CB  
1458 C CG  . TYR A 116 ? 0.50380 0.37676 0.49503 -0.00929 0.00802  0.01258  116 TYR A CG  
1459 C CD1 . TYR A 116 ? 0.52559 0.38404 0.51170 -0.00483 0.00611  0.01084  116 TYR A CD1 
1460 C CD2 . TYR A 116 ? 0.69755 0.56718 0.68851 -0.01365 0.01329  0.01959  116 TYR A CD2 
1461 C CE1 . TYR A 116 ? 0.64522 0.48445 0.62596 -0.00474 0.00884  0.01612  116 TYR A CE1 
1462 C CE2 . TYR A 116 ? 0.71669 0.56811 0.70213 -0.01414 0.01654  0.02543  116 TYR A CE2 
1463 C CZ  . TYR A 116 ? 0.56079 0.39631 0.54109 -0.00968 0.01402  0.02374  116 TYR A CZ  
1464 O OH  . TYR A 116 ? 0.89198 0.70727 0.86616 -0.00963 0.01721  0.03009  116 TYR A OH  
1465 N N   . ILE A 117 ? 0.33003 0.25368 0.33076 -0.00297 -0.00037 0.00101  117 ILE A N   
1466 C CA  . ILE A 117 ? 0.31166 0.24924 0.31750 -0.00388 -0.00237 -0.00237 117 ILE A CA  
1467 C C   . ILE A 117 ? 0.34364 0.28370 0.34805 0.00036  -0.00551 -0.00651 117 ILE A C   
1468 O O   . ILE A 117 ? 0.33094 0.27559 0.33831 -0.00155 -0.00752 -0.01061 117 ILE A O   
1469 C CB  . ILE A 117 ? 0.34733 0.29405 0.35259 -0.00214 -0.00111 0.00063  117 ILE A CB  
1470 C CG1 . ILE A 117 ? 0.29976 0.24608 0.30668 -0.00641 0.00312  0.00449  117 ILE A CG1 
1471 C CG2 . ILE A 117 ? 0.29017 0.24894 0.29960 -0.00163 -0.00357 -0.00266 117 ILE A CG2 
1472 C CD1 . ILE A 117 ? 0.30730 0.26164 0.31184 -0.00402 0.00477  0.00677  117 ILE A CD1 
1473 N N   A CYS A 118 ? 0.32584 0.26348 0.32565 0.00649  -0.00588 -0.00535 118 CYS A N   
1474 N N   B CYS A 118 ? 0.33161 0.26971 0.33145 0.00653  -0.00586 -0.00519 118 CYS A N   
1475 C CA  A CYS A 118 ? 0.33731 0.27941 0.33701 0.01048  -0.00770 -0.00883 118 CYS A CA  
1476 C CA  B CYS A 118 ? 0.33917 0.28044 0.33841 0.01098  -0.00761 -0.00848 118 CYS A CA  
1477 C C   A CYS A 118 ? 0.33863 0.27193 0.33609 0.01080  -0.00826 -0.01300 118 CYS A C   
1478 C C   B CYS A 118 ? 0.33668 0.27031 0.33461 0.00991  -0.00827 -0.01297 118 CYS A C   
1479 O O   A CYS A 118 ? 0.31906 0.25701 0.31620 0.01261  -0.00924 -0.01667 118 CYS A O   
1480 O O   B CYS A 118 ? 0.31648 0.25560 0.31512 0.00964  -0.00956 -0.01678 118 CYS A O   
1481 C CB  A CYS A 118 ? 0.37570 0.32090 0.37366 0.01693  -0.00813 -0.00673 118 CYS A CB  
1482 C CB  B CYS A 118 ? 0.33618 0.27555 0.33215 0.01782  -0.00775 -0.00614 118 CYS A CB  
1483 S SG  A CYS A 118 ? 0.46393 0.42010 0.46389 0.01662  -0.00879 -0.00391 118 CYS A SG  
1484 S SG  B CYS A 118 ? 0.45566 0.40396 0.45377 0.02356  -0.00879 -0.00914 118 CYS A SG  
1485 N N   . LEU A 119 ? 0.32491 0.24481 0.32008 0.00918  -0.00747 -0.01256 119 LEU A N   
1486 C CA  . LEU A 119 ? 0.36986 0.27974 0.36262 0.00876  -0.00856 -0.01774 119 LEU A CA  
1487 C C   . LEU A 119 ? 0.37235 0.28696 0.36867 0.00243  -0.01068 -0.02210 119 LEU A C   
1488 O O   . LEU A 119 ? 0.36757 0.28239 0.36110 0.00376  -0.01266 -0.02756 119 LEU A O   
1489 C CB  . LEU A 119 ? 0.37953 0.27213 0.36962 0.00766  -0.00731 -0.01594 119 LEU A CB  
1490 C CG  . LEU A 119 ? 0.41034 0.28989 0.39697 0.00805  -0.00878 -0.02212 119 LEU A CG  
1491 C CD1 . LEU A 119 ? 0.41019 0.29138 0.39194 0.01734  -0.00899 -0.02517 119 LEU A CD1 
1492 C CD2 . LEU A 119 ? 0.45135 0.31134 0.43589 0.00606  -0.00739 -0.01979 119 LEU A CD2 
1493 N N   . SER A 120 ? 0.32339 0.24211 0.32560 -0.00403 -0.01030 -0.01981 120 SER A N   
1494 C CA  . SER A 120 ? 0.35513 0.28105 0.36249 -0.00958 -0.01298 -0.02352 120 SER A CA  
1495 C C   . SER A 120 ? 0.29949 0.23739 0.30547 -0.00614 -0.01483 -0.02545 120 SER A C   
1496 O O   . SER A 120 ? 0.32513 0.26469 0.32953 -0.00687 -0.01799 -0.03039 120 SER A O   
1497 C CB  . SER A 120 ? 0.38250 0.31464 0.39779 -0.01536 -0.01125 -0.01962 120 SER A CB  
1498 O OG  . SER A 120 ? 0.35161 0.29225 0.37367 -0.02029 -0.01425 -0.02303 120 SER A OG  
1499 N N   . ASN A 121 ? 0.27820 0.22348 0.28391 -0.00223 -0.01302 -0.02159 121 ASN A N   
1500 C CA  . ASN A 121 ? 0.29711 0.25275 0.30216 0.00047  -0.01399 -0.02222 121 ASN A CA  
1501 C C   . ASN A 121 ? 0.31704 0.26999 0.31565 0.00531  -0.01415 -0.02553 121 ASN A C   
1502 O O   . ASN A 121 ? 0.30557 0.26345 0.30158 0.00604  -0.01556 -0.02793 121 ASN A O   
1503 C CB  . ASN A 121 ? 0.27945 0.24205 0.28668 0.00262  -0.01218 -0.01769 121 ASN A CB  
1504 C CG  . ASN A 121 ? 0.26563 0.23745 0.27308 0.00465  -0.01272 -0.01763 121 ASN A CG  
1505 O OD1 . ASN A 121 ? 0.30789 0.28536 0.31774 0.00240  -0.01414 -0.01784 121 ASN A OD1 
1506 N ND2 . ASN A 121 ? 0.27270 0.24638 0.27842 0.00899  -0.01142 -0.01690 121 ASN A ND2 
1507 N N   . PHE A 122 ? 0.34385 0.28890 0.33923 0.00930  -0.01247 -0.02550 122 PHE A N   
1508 C CA  . PHE A 122 ? 0.34626 0.28825 0.33559 0.01459  -0.01192 -0.02924 122 PHE A CA  
1509 C C   . PHE A 122 ? 0.35227 0.28806 0.33664 0.01252  -0.01458 -0.03548 122 PHE A C   
1510 O O   . PHE A 122 ? 0.35799 0.29681 0.33656 0.01565  -0.01476 -0.03880 122 PHE A O   
1511 C CB  . PHE A 122 ? 0.36934 0.30320 0.35687 0.01987  -0.00998 -0.02827 122 PHE A CB  
1512 C CG  . PHE A 122 ? 0.37841 0.30919 0.36013 0.02620  -0.00877 -0.03255 122 PHE A CG  
1513 C CD1 . PHE A 122 ? 0.39639 0.33856 0.37873 0.03094  -0.00642 -0.03169 122 PHE A CD1 
1514 C CD2 . PHE A 122 ? 0.42967 0.34637 0.40549 0.02714  -0.00968 -0.03774 122 PHE A CD2 
1515 C CE1 . PHE A 122 ? 0.40659 0.34718 0.38340 0.03734  -0.00423 -0.03567 122 PHE A CE1 
1516 C CE2 . PHE A 122 ? 0.40991 0.32352 0.37917 0.03389  -0.00818 -0.04246 122 PHE A CE2 
1517 C CZ  . PHE A 122 ? 0.46893 0.39514 0.43855 0.03923  -0.00513 -0.04129 122 PHE A CZ  
1518 N N   . PHE A 123 ? 0.32407 0.25142 0.31049 0.00703  -0.01671 -0.03724 123 PHE A N   
1519 C CA  . PHE A 123 ? 0.35590 0.27756 0.33849 0.00433  -0.02047 -0.04409 123 PHE A CA  
1520 C C   . PHE A 123 ? 0.34675 0.28032 0.32969 0.00226  -0.02355 -0.04535 123 PHE A C   
1521 O O   . PHE A 123 ? 0.34453 0.27729 0.32000 0.00389  -0.02632 -0.05089 123 PHE A O   
1522 C CB  . PHE A 123 ? 0.36784 0.27844 0.35495 -0.00231 -0.02208 -0.04541 123 PHE A CB  
1523 C CG  . PHE A 123 ? 0.42300 0.31753 0.40651 0.00052  -0.01991 -0.04561 123 PHE A CG  
1524 C CD1 . PHE A 123 ? 0.54296 0.43171 0.51791 0.00846  -0.01877 -0.04897 123 PHE A CD1 
1525 C CD2 . PHE A 123 ? 0.49497 0.37992 0.48338 -0.00418 -0.01856 -0.04206 123 PHE A CD2 
1526 C CE1 . PHE A 123 ? 0.78162 0.65476 0.75316 0.01238  -0.01693 -0.04914 123 PHE A CE1 
1527 C CE2 . PHE A 123 ? 0.55335 0.42168 0.53746 -0.00082 -0.01665 -0.04154 123 PHE A CE2 
1528 C CZ  . PHE A 123 ? 0.53372 0.39599 0.50951 0.00781  -0.01617 -0.04526 123 PHE A CZ  
1529 N N   . MET A 124 ? 0.32071 0.26474 0.31126 -0.00069 -0.02329 -0.04041 124 MET A N   
1530 C CA  . MET A 124 ? 0.31947 0.27459 0.31005 -0.00113 -0.02598 -0.04051 124 MET A CA  
1531 C C   . MET A 124 ? 0.27126 0.22990 0.25279 0.00515  -0.02443 -0.04068 124 MET A C   
1532 O O   . MET A 124 ? 0.32161 0.28195 0.29611 0.00639  -0.02738 -0.04426 124 MET A O   
1533 C CB  . MET A 124 ? 0.27121 0.23555 0.27084 -0.00353 -0.02477 -0.03479 124 MET A CB  
1534 C CG  . MET A 124 ? 0.35045 0.32557 0.35119 -0.00362 -0.02775 -0.03415 124 MET A CG  
1535 S SD  . MET A 124 ? 0.31553 0.29957 0.32421 -0.00371 -0.02512 -0.02761 124 MET A SD  
1536 C CE  . MET A 124 ? 0.28204 0.26485 0.28582 0.00137  -0.02053 -0.02426 124 MET A CE  
1537 N N   . LEU A 125 ? 0.29159 0.25174 0.27325 0.00919  -0.01973 -0.03674 125 LEU A N   
1538 C CA  . LEU A 125 ? 0.31889 0.28398 0.29425 0.01452  -0.01695 -0.03587 125 LEU A CA  
1539 C C   . LEU A 125 ? 0.34125 0.29942 0.30596 0.01872  -0.01679 -0.04182 125 LEU A C   
1540 O O   . LEU A 125 ? 0.33892 0.30066 0.29515 0.02179  -0.01643 -0.04312 125 LEU A O   
1541 C CB  . LEU A 125 ? 0.29756 0.26677 0.27796 0.01722  -0.01242 -0.03095 125 LEU A CB  
1542 C CG  . LEU A 125 ? 0.30127 0.27721 0.29025 0.01404  -0.01244 -0.02572 125 LEU A CG  
1543 C CD1 . LEU A 125 ? 0.31507 0.29463 0.30913 0.01654  -0.00917 -0.02200 125 LEU A CD1 
1544 C CD2 . LEU A 125 ? 0.31215 0.29508 0.30042 0.01284  -0.01361 -0.02385 125 LEU A CD2 
1545 N N   . LEU A 126 ? 0.34000 0.28734 0.30398 0.01948  -0.01671 -0.04532 126 LEU A N   
1546 C CA  . LEU A 126 ? 0.35766 0.29621 0.31101 0.02387  -0.01680 -0.05216 126 LEU A CA  
1547 C C   . LEU A 126 ? 0.33685 0.27402 0.28241 0.02164  -0.02216 -0.05803 126 LEU A C   
1548 O O   . LEU A 126 ? 0.36489 0.30225 0.29869 0.02648  -0.02171 -0.06186 126 LEU A O   
1549 C CB  . LEU A 126 ? 0.34094 0.26564 0.29591 0.02392  -0.01684 -0.05473 126 LEU A CB  
1550 C CG  . LEU A 126 ? 0.45271 0.36487 0.39676 0.02805  -0.01775 -0.06311 126 LEU A CG  
1551 C CD1 . LEU A 126 ? 0.47031 0.38754 0.40657 0.03700  -0.01269 -0.06377 126 LEU A CD1 
1552 C CD2 . LEU A 126 ? 0.46371 0.35980 0.41041 0.02736  -0.01800 -0.06469 126 LEU A CD2 
1553 N N   . ILE A 127 ? 0.36891 0.30570 0.32085 0.01458  -0.02736 -0.05885 127 ILE A N   
1554 C CA  . ILE A 127 ? 0.40606 0.34319 0.35232 0.01218  -0.03384 -0.06471 127 ILE A CA  
1555 C C   . ILE A 127 ? 0.35124 0.30016 0.29153 0.01524  -0.03397 -0.06164 127 ILE A C   
1556 O O   . ILE A 127 ? 0.38255 0.33083 0.30993 0.01865  -0.03651 -0.06639 127 ILE A O   
1557 C CB  . ILE A 127 ? 0.35838 0.29515 0.31638 0.00360  -0.03883 -0.06541 127 ILE A CB  
1558 C CG1 . ILE A 127 ? 0.40086 0.32274 0.36168 0.00066  -0.03867 -0.06910 127 ILE A CG1 
1559 C CG2 . ILE A 127 ? 0.40486 0.34684 0.36024 0.00089  -0.04653 -0.07033 127 ILE A CG2 
1560 C CD1 . ILE A 127 ? 0.43961 0.36157 0.41446 -0.00841 -0.04114 -0.06765 127 ILE A CD1 
1561 N N   . GLY A 128 ? 0.33458 0.29319 0.28291 0.01448  -0.03108 -0.05363 128 GLY A N   
1562 C CA  . GLY A 128 ? 0.34404 0.31174 0.28663 0.01776  -0.02992 -0.04939 128 GLY A CA  
1563 C C   . GLY A 128 ? 0.34226 0.30893 0.27216 0.02459  -0.02497 -0.05007 128 GLY A C   
1564 O O   . GLY A 128 ? 0.40871 0.37790 0.32652 0.02789  -0.02608 -0.05094 128 GLY A O   
1565 N N   A TYR A 129 ? 0.34673 0.31025 0.27881 0.02742  -0.01920 -0.04947 129 TYR A N   
1566 N N   B TYR A 129 ? 0.34966 0.31321 0.28165 0.02747  -0.01915 -0.04946 129 TYR A N   
1567 C CA  A TYR A 129 ? 0.37939 0.34397 0.30159 0.03433  -0.01323 -0.04974 129 TYR A CA  
1568 C CA  B TYR A 129 ? 0.37932 0.34396 0.30116 0.03441  -0.01324 -0.04979 129 TYR A CA  
1569 C C   A TYR A 129 ? 0.37771 0.33480 0.28397 0.03811  -0.01591 -0.05831 129 TYR A C   
1570 C C   B TYR A 129 ? 0.37946 0.33653 0.28548 0.03810  -0.01603 -0.05840 129 TYR A C   
1571 O O   A TYR A 129 ? 0.42751 0.38786 0.32078 0.04323  -0.01315 -0.05843 129 TYR A O   
1572 O O   B TYR A 129 ? 0.42943 0.38962 0.32232 0.04322  -0.01337 -0.05864 129 TYR A O   
1573 C CB  A TYR A 129 ? 0.36232 0.32585 0.29214 0.03691  -0.00754 -0.04807 129 TYR A CB  
1574 C CB  B TYR A 129 ? 0.36418 0.32787 0.29312 0.03729  -0.00734 -0.04819 129 TYR A CB  
1575 C CG  A TYR A 129 ? 0.40896 0.37677 0.33222 0.04414  -0.00023 -0.04742 129 TYR A CG  
1576 C CG  B TYR A 129 ? 0.37335 0.33816 0.29292 0.04510  -0.00096 -0.04996 129 TYR A CG  
1577 C CD1 A TYR A 129 ? 0.40260 0.38200 0.33093 0.04481  0.00543  -0.03991 129 TYR A CD1 
1578 C CD1 B TYR A 129 ? 0.33915 0.31501 0.25848 0.04772  0.00543  -0.04384 129 TYR A CD1 
1579 C CD2 A TYR A 129 ? 0.41074 0.37103 0.32339 0.05022  0.00138  -0.05446 129 TYR A CD2 
1580 C CD2 B TYR A 129 ? 0.44634 0.40095 0.35771 0.04989  -0.00082 -0.05771 129 TYR A CD2 
1581 C CE1 A TYR A 129 ? 0.35386 0.33893 0.27805 0.05095  0.01300  -0.03886 129 TYR A CE1 
1582 C CE1 B TYR A 129 ? 0.47629 0.45492 0.38827 0.05488  0.01235  -0.04503 129 TYR A CE1 
1583 C CE2 A TYR A 129 ? 0.49959 0.46525 0.40686 0.05745  0.00901  -0.05386 129 TYR A CE2 
1584 C CE2 B TYR A 129 ? 0.48695 0.44331 0.38973 0.05797  0.00568  -0.05967 129 TYR A CE2 
1585 C CZ  A TYR A 129 ? 0.38266 0.36162 0.29644 0.05757  0.01508  -0.04571 129 TYR A CZ  
1586 C CZ  B TYR A 129 ? 0.53066 0.50002 0.43406 0.06048  0.01258  -0.05313 129 TYR A CZ  
1587 O OH  A TYR A 129 ? 0.52243 0.50847 0.43259 0.06429  0.02353  -0.04463 129 TYR A OH  
1588 O OH  B TYR A 129 ? 0.58726 0.56005 0.48309 0.06858  0.02014  -0.05468 129 TYR A OH  
1589 N N   . LEU A 130 ? 0.37826 0.32471 0.28470 0.03547  -0.02130 -0.06564 130 LEU A N   
1590 C CA  . LEU A 130 ? 0.40056 0.33833 0.29208 0.03818  -0.02545 -0.07529 130 LEU A CA  
1591 C C   . LEU A 130 ? 0.42418 0.36764 0.30623 0.03744  -0.03127 -0.07633 130 LEU A C   
1592 O O   . LEU A 130 ? 0.49343 0.43511 0.35816 0.04294  -0.03169 -0.08111 130 LEU A O   
1593 C CB  . LEU A 130 ? 0.42333 0.34780 0.31965 0.03372  -0.03061 -0.08242 130 LEU A CB  
1594 C CG  . LEU A 130 ? 0.43950 0.35590 0.34197 0.03625  -0.02506 -0.08164 130 LEU A CG  
1595 C CD1 . LEU A 130 ? 0.49798 0.40070 0.40694 0.03058  -0.02965 -0.08627 130 LEU A CD1 
1596 C CD2 . LEU A 130 ? 0.50802 0.42068 0.39811 0.04586  -0.01940 -0.08543 130 LEU A CD2 
1597 N N   . GLY A 131 ? 0.41469 0.36529 0.30714 0.03150  -0.03573 -0.07178 131 GLY A N   
1598 C CA  . GLY A 131 ? 0.50433 0.46131 0.38855 0.03179  -0.04155 -0.07170 131 GLY A CA  
1599 C C   . GLY A 131 ? 0.45325 0.41799 0.32807 0.03742  -0.03565 -0.06424 131 GLY A C   
1600 O O   . GLY A 131 ? 0.50944 0.47564 0.36820 0.04151  -0.03835 -0.06584 131 GLY A O   
1601 N N   A GLU A 132 ? 0.43011 0.40002 0.31524 0.03715  -0.02806 -0.05563 132 GLU A N   
1602 N N   B GLU A 132 ? 0.43112 0.40036 0.31444 0.03800  -0.02734 -0.05619 132 GLU A N   
1603 C CA  A GLU A 132 ? 0.43436 0.41159 0.31423 0.04077  -0.02180 -0.04718 132 GLU A CA  
1604 C CA  B GLU A 132 ? 0.47656 0.45235 0.35132 0.04266  -0.02097 -0.04899 132 GLU A CA  
1605 C C   A GLU A 132 ? 0.47703 0.45270 0.34038 0.04809  -0.01539 -0.04916 132 GLU A C   
1606 C C   B GLU A 132 ? 0.55143 0.52408 0.40872 0.05004  -0.01579 -0.05307 132 GLU A C   
1607 O O   A GLU A 132 ? 0.45845 0.43876 0.31078 0.05184  -0.01163 -0.04388 132 GLU A O   
1608 O O   B GLU A 132 ? 0.46689 0.44149 0.30750 0.05454  -0.01536 -0.05208 132 GLU A O   
1609 C CB  A GLU A 132 ? 0.47164 0.45390 0.36833 0.03783  -0.01580 -0.03909 132 GLU A CB  
1610 C CB  B GLU A 132 ? 0.42669 0.40860 0.31616 0.04061  -0.01394 -0.03983 132 GLU A CB  
1611 C CG  A GLU A 132 ? 0.42558 0.41485 0.32060 0.03959  -0.00962 -0.02967 132 GLU A CG  
1612 C CG  B GLU A 132 ? 0.52291 0.51148 0.40850 0.04181  -0.01076 -0.03092 132 GLU A CG  
1613 C CD  A GLU A 132 ? 0.38852 0.38010 0.27791 0.03912  -0.01489 -0.02599 132 GLU A CD  
1614 C CD  B GLU A 132 ? 0.42341 0.41234 0.30089 0.04160  -0.01893 -0.03112 132 GLU A CD  
1615 O OE1 A GLU A 132 ? 0.31301 0.30532 0.21244 0.03487  -0.02121 -0.02606 132 GLU A OE1 
1616 O OE1 B GLU A 132 ? 0.38249 0.37237 0.27113 0.03697  -0.02549 -0.03149 132 GLU A OE1 
1617 O OE2 A GLU A 132 ? 0.39632 0.38911 0.27085 0.04356  -0.01249 -0.02286 132 GLU A OE2 
1618 O OE2 B GLU A 132 ? 0.44566 0.43454 0.30541 0.04656  -0.01878 -0.03088 132 GLU A OE2 
1619 N N   A THR A 133 ? 0.55003 0.51879 0.41109 0.05059  -0.01361 -0.05643 133 THR A N   
1620 N N   B THR A 133 ? 0.54401 0.51137 0.40384 0.05208  -0.01179 -0.05777 133 THR A N   
1621 C CA  A THR A 133 ? 0.54861 0.51534 0.39385 0.05849  -0.00735 -0.05997 133 THR A CA  
1622 C CA  B THR A 133 ? 0.56113 0.52493 0.40463 0.05995  -0.00673 -0.06301 133 THR A CA  
1623 C C   A THR A 133 ? 0.57952 0.53723 0.40653 0.06160  -0.01418 -0.07109 133 THR A C   
1624 C C   B THR A 133 ? 0.55994 0.51474 0.38688 0.06167  -0.01504 -0.07381 133 THR A C   
1625 O O   A THR A 133 ? 0.55383 0.50765 0.36618 0.06877  -0.00968 -0.07629 133 THR A O   
1626 O O   B THR A 133 ? 0.65933 0.60729 0.47294 0.06787  -0.01275 -0.08145 133 THR A O   
1627 C CB  A THR A 133 ? 0.60355 0.56916 0.45825 0.06096  0.00019  -0.06035 133 THR A CB  
1628 C CB  B THR A 133 ? 0.53724 0.49709 0.38866 0.06257  -0.00097 -0.06572 133 THR A CB  
1629 O OG1 A THR A 133 ? 0.45928 0.41480 0.32157 0.05789  -0.00528 -0.06723 133 THR A OG1 
1630 O OG1 B THR A 133 ? 0.53385 0.48345 0.39319 0.05811  -0.00793 -0.07214 133 THR A OG1 
1631 C CG2 A THR A 133 ? 0.46175 0.43742 0.33390 0.05790  0.00615  -0.04990 133 THR A CG2 
1632 C CG2 B THR A 133 ? 0.48240 0.45227 0.35028 0.06126  0.00663  -0.05594 133 THR A CG2 
1633 N N   . LYS A 134 ? 0.61465 0.56949 0.44306 0.05639  -0.02503 -0.07523 134 LYS A N   
1634 C CA  . LYS A 134 ? 0.57027 0.51881 0.38263 0.05774  -0.03420 -0.08529 134 LYS A CA  
1635 C C   . LYS A 134 ? 0.55102 0.48622 0.35988 0.05856  -0.03664 -0.09728 134 LYS A C   
1636 O O   . LYS A 134 ? 0.70656 0.63500 0.49666 0.06291  -0.04084 -0.10677 134 LYS A O   
1637 C CB  . LYS A 134 ? 0.60959 0.56171 0.39827 0.06544  -0.03216 -0.08420 134 LYS A CB  
1638 C CG  . LYS A 134 ? 0.74600 0.70922 0.53605 0.06520  -0.02934 -0.07153 134 LYS A CG  
1639 C CD  . LYS A 134 ? 0.79071 0.75750 0.58779 0.05969  -0.04042 -0.07045 134 LYS A CD  
1640 N N   . GLN A 135 ? 0.58953 0.51993 0.41531 0.05481  -0.03411 -0.09689 135 GLN A N   
1641 C CA  . GLN A 135 ? 0.53885 0.45443 0.36351 0.05502  -0.03628 -0.10717 135 GLN A CA  
1642 C C   . GLN A 135 ? 0.66789 0.57641 0.50013 0.04631  -0.04761 -0.11398 135 GLN A C   
1643 O O   . GLN A 135 ? 0.66955 0.56385 0.49686 0.04608  -0.05159 -0.12444 135 GLN A O   
1644 C CB  . GLN A 135 ? 0.54931 0.46248 0.38752 0.05603  -0.02799 -0.10273 135 GLN A CB  
1645 C CG  . GLN A 135 ? 0.62718 0.54580 0.45775 0.06545  -0.01700 -0.09916 135 GLN A CG  
1646 C CD  . GLN A 135 ? 1.07884 0.98867 0.91394 0.07015  -0.01144 -0.10212 135 GLN A CD  
1647 O OE1 . GLN A 135 ? 0.78418 0.68490 0.63103 0.06560  -0.01462 -0.10359 135 GLN A OE1 
1648 N NE2 . GLN A 135 ? 1.03395 0.94664 0.85955 0.07976  -0.00279 -0.10266 135 GLN A NE2 
1649 N N   . ILE A 136 ? 0.64952 0.56757 0.49471 0.03911  -0.05250 -0.10829 136 ILE A N   
1650 C CA  . ILE A 136 ? 0.54734 0.46320 0.40100 0.03058  -0.06339 -0.11392 136 ILE A CA  
1651 C C   . ILE A 136 ? 0.56713 0.49710 0.41968 0.02959  -0.06891 -0.10957 136 ILE A C   
1652 O O   . ILE A 136 ? 0.58441 0.52407 0.43396 0.03379  -0.06329 -0.10044 136 ILE A O   
1653 C CB  . ILE A 136 ? 0.54828 0.46210 0.42477 0.02222  -0.06244 -0.10988 136 ILE A CB  
1654 C CG1 . ILE A 136 ? 0.51749 0.44445 0.40637 0.02155  -0.05618 -0.09695 136 ILE A CG1 
1655 C CG2 . ILE A 136 ? 0.62185 0.52010 0.49873 0.02375  -0.05766 -0.11374 136 ILE A CG2 
1656 C CD1 . ILE A 136 ? 0.62442 0.55053 0.53381 0.01441  -0.05421 -0.09193 136 ILE A CD1 
1657 N N   . ASN A 137 ? 0.55764 0.48877 0.41369 0.02388  -0.08015 -0.11596 137 ASN A N   
1658 C CA  . ASN A 137 ? 0.73060 0.67510 0.58414 0.02448  -0.08640 -0.11243 137 ASN A CA  
1659 C C   . ASN A 137 ? 0.63686 0.59316 0.51032 0.02022  -0.08356 -0.10107 137 ASN A C   
1660 O O   . ASN A 137 ? 0.58082 0.53530 0.47116 0.01522  -0.07871 -0.09737 137 ASN A O   
1661 C CB  . ASN A 137 ? 0.70594 0.65031 0.55674 0.02068  -0.10030 -0.12325 137 ASN A CB  
1662 C CG  . ASN A 137 ? 1.29437 1.23789 1.16846 0.00960  -0.10564 -0.12659 137 ASN A CG  
1663 O OD1 . ASN A 137 ? 0.61405 0.56792 0.50708 0.00469  -0.10484 -0.11897 137 ASN A OD1 
1664 N ND2 . ASN A 137 ? 0.91171 0.84258 0.78429 0.00562  -0.11094 -0.13811 137 ASN A ND2 
1665 N N   . LYS A 138 ? 0.62683 0.59459 0.49673 0.02306  -0.08653 -0.09538 138 LYS A N   
1666 C CA  . LYS A 138 ? 0.61560 0.59374 0.50203 0.02057  -0.08355 -0.08479 138 LYS A CA  
1667 C C   . LYS A 138 ? 0.67002 0.65238 0.57885 0.01159  -0.08912 -0.08684 138 LYS A C   
1668 O O   . LYS A 138 ? 0.49363 0.47944 0.41889 0.00801  -0.08375 -0.08007 138 LYS A O   
1669 C CB  . LYS A 138 ? 0.69056 0.67823 0.56741 0.02607  -0.08659 -0.07889 138 LYS A CB  
1670 C CG  . LYS A 138 ? 0.68689 0.67306 0.54750 0.03381  -0.07728 -0.07140 138 LYS A CG  
1671 N N   A MET A 139 ? 0.56753 0.54950 0.47740 0.00761  -0.09958 -0.09655 139 MET A N   
1672 N N   B MET A 139 ? 0.56991 0.55314 0.47987 0.00786  -0.09997 -0.09602 139 MET A N   
1673 C CA  A MET A 139 ? 0.59765 0.58516 0.53025 -0.00162 -0.10469 -0.09855 139 MET A CA  
1674 C CA  B MET A 139 ? 0.59400 0.58366 0.52700 -0.00112 -0.10498 -0.09746 139 MET A CA  
1675 C C   A MET A 139 ? 0.46481 0.44212 0.40936 -0.00778 -0.09795 -0.09889 139 MET A C   
1676 C C   B MET A 139 ? 0.47154 0.45137 0.41704 -0.00759 -0.09854 -0.09802 139 MET A C   
1677 O O   A MET A 139 ? 0.54674 0.52936 0.51043 -0.01338 -0.09494 -0.09370 139 MET A O   
1678 O O   B MET A 139 ? 0.52858 0.51391 0.49316 -0.01303 -0.09545 -0.09275 139 MET A O   
1679 C CB  A MET A 139 ? 0.64814 0.63824 0.57964 -0.00490 -0.11810 -0.10941 139 MET A CB  
1680 C CB  B MET A 139 ? 0.65400 0.64767 0.58688 -0.00433 -0.11859 -0.10769 139 MET A CB  
1681 C CG  A MET A 139 ? 0.68972 0.69203 0.64611 -0.01347 -0.12445 -0.10990 139 MET A CG  
1682 C CG  B MET A 139 ? 0.60881 0.62018 0.55246 -0.00442 -0.12608 -0.10423 139 MET A CG  
1683 S SD  A MET A 139 ? 1.10772 1.11687 1.06406 -0.01691 -0.14192 -0.12260 139 MET A SD  
1684 S SD  B MET A 139 ? 1.00417 1.02384 0.96533 -0.01393 -0.14038 -0.11514 139 MET A SD  
1685 C CE  A MET A 139 ? 0.72085 0.75228 0.70667 -0.02244 -0.14629 -0.11723 139 MET A CE  
1686 C CE  B MET A 139 ? 0.72131 0.72835 0.69908 -0.02479 -0.13341 -0.11786 139 MET A CE  
1687 N N   A LEU A 140 ? 0.50551 0.46775 0.43823 -0.00618 -0.09532 -0.10479 140 LEU A N   
1688 N N   B LEU A 140 ? 0.51859 0.48341 0.45253 -0.00626 -0.09606 -0.10403 140 LEU A N   
1689 C CA  A LEU A 140 ? 0.53203 0.48302 0.47398 -0.01046 -0.08846 -0.10397 140 LEU A CA  
1690 C CA  B LEU A 140 ? 0.53494 0.48858 0.47822 -0.01071 -0.08929 -0.10338 140 LEU A CA  
1691 C C   A LEU A 140 ? 0.45828 0.41226 0.40486 -0.00738 -0.07764 -0.09271 140 LEU A C   
1692 C C   B LEU A 140 ? 0.47699 0.43361 0.42531 -0.00785 -0.07849 -0.09211 140 LEU A C   
1693 O O   A LEU A 140 ? 0.45691 0.40815 0.41717 -0.01217 -0.07292 -0.08879 140 LEU A O   
1694 O O   B LEU A 140 ? 0.50141 0.45787 0.46521 -0.01317 -0.07448 -0.08769 140 LEU A O   
1695 C CB  A LEU A 140 ? 0.64194 0.57553 0.56895 -0.00766 -0.08805 -0.11278 140 LEU A CB  
1696 C CB  B LEU A 140 ? 0.63673 0.57313 0.56465 -0.00772 -0.08866 -0.11195 140 LEU A CB  
1697 C CG  A LEU A 140 ? 0.66614 0.58552 0.59832 -0.00929 -0.08034 -0.11153 140 LEU A CG  
1698 C CG  B LEU A 140 ? 0.59246 0.51418 0.52851 -0.01208 -0.08351 -0.11285 140 LEU A CG  
1699 C CD1 A LEU A 140 ? 0.63034 0.54881 0.58382 -0.01988 -0.08125 -0.10987 140 LEU A CD1 
1700 C CD1 B LEU A 140 ? 0.58675 0.50756 0.54112 -0.02347 -0.08924 -0.11626 140 LEU A CD1 
1701 C CD2 A LEU A 140 ? 0.69606 0.59781 0.61248 -0.00554 -0.08138 -0.12175 140 LEU A CD2 
1702 C CD2 B LEU A 140 ? 0.69162 0.59626 0.61021 -0.00661 -0.08246 -0.12119 140 LEU A CD2 
1703 N N   . THR A 141 ? 0.48522 0.44468 0.42049 0.00033  -0.07372 -0.08733 141 THR A N   
1704 C CA  . THR A 141 ? 0.41470 0.37759 0.35513 0.00271  -0.06438 -0.07730 141 THR A CA  
1705 C C   . THR A 141 ? 0.38437 0.35827 0.34202 -0.00194 -0.06492 -0.07092 141 THR A C   
1706 O O   . THR A 141 ? 0.39230 0.36572 0.36089 -0.00442 -0.05914 -0.06568 141 THR A O   
1707 C CB  . THR A 141 ? 0.43925 0.40597 0.36494 0.01096  -0.06030 -0.07288 141 THR A CB  
1708 O OG1 . THR A 141 ? 0.45162 0.40953 0.35990 0.01621  -0.05960 -0.07931 141 THR A OG1 
1709 C CG2 . THR A 141 ? 0.37354 0.34292 0.30578 0.01265  -0.05077 -0.06342 141 THR A CG2 
1710 N N   A LEU A 142 ? 0.42626 0.41042 0.38615 -0.00256 -0.07203 -0.07149 142 LEU A N   
1711 N N   B LEU A 142 ? 0.42615 0.41035 0.38584 -0.00245 -0.07200 -0.07142 142 LEU A N   
1712 C CA  A LEU A 142 ? 0.43753 0.43303 0.41350 -0.00553 -0.07210 -0.06547 142 LEU A CA  
1713 C CA  B LEU A 142 ? 0.43946 0.43513 0.41542 -0.00559 -0.07244 -0.06569 142 LEU A CA  
1714 C C   A LEU A 142 ? 0.48407 0.47943 0.47783 -0.01400 -0.07265 -0.06740 142 LEU A C   
1715 C C   B LEU A 142 ? 0.48420 0.47912 0.47767 -0.01401 -0.07258 -0.06755 142 LEU A C   
1716 O O   A LEU A 142 ? 0.44385 0.44389 0.45011 -0.01622 -0.06783 -0.06139 142 LEU A O   
1717 O O   B LEU A 142 ? 0.44618 0.44397 0.45111 -0.01611 -0.06689 -0.06150 142 LEU A O   
1718 C CB  A LEU A 142 ? 0.44126 0.44812 0.41533 -0.00287 -0.07983 -0.06540 142 LEU A CB  
1719 C CB  B LEU A 142 ? 0.44487 0.45180 0.41933 -0.00341 -0.08084 -0.06641 142 LEU A CB  
1720 C CG  A LEU A 142 ? 0.41029 0.41895 0.36994 0.00529  -0.07730 -0.05942 142 LEU A CG  
1721 C CG  B LEU A 142 ? 0.46582 0.48568 0.45530 -0.00418 -0.08147 -0.06027 142 LEU A CG  
1722 C CD1 A LEU A 142 ? 0.49569 0.51287 0.44981 0.00853  -0.08666 -0.06092 142 LEU A CD1 
1723 C CD1 B LEU A 142 ? 0.40084 0.42093 0.38767 0.00072  -0.07351 -0.05101 142 LEU A CD1 
1724 C CD2 A LEU A 142 ? 0.33208 0.34402 0.29982 0.00641  -0.06973 -0.04996 142 LEU A CD2 
1725 C CD2 B LEU A 142 ? 0.62474 0.65522 0.61349 -0.00214 -0.09182 -0.06295 142 LEU A CD2 
1726 N N   A PHE A 143 ? 0.52450 0.51388 0.51929 -0.01896 -0.07810 -0.07572 143 PHE A N   
1727 N N   B PHE A 143 ? 0.52263 0.51314 0.51794 -0.01910 -0.07887 -0.07592 143 PHE A N   
1728 C CA  A PHE A 143 ? 0.57092 0.55952 0.58332 -0.02795 -0.07787 -0.07683 143 PHE A CA  
1729 C CA  B PHE A 143 ? 0.56859 0.55670 0.58046 -0.02797 -0.07815 -0.07728 143 PHE A CA  
1730 C C   A PHE A 143 ? 0.43446 0.41027 0.44722 -0.02911 -0.06903 -0.07356 143 PHE A C   
1731 C C   B PHE A 143 ? 0.43401 0.41060 0.44565 -0.02808 -0.06859 -0.07282 143 PHE A C   
1732 O O   A PHE A 143 ? 0.42695 0.40512 0.45283 -0.03335 -0.06418 -0.06832 143 PHE A O   
1733 O O   B PHE A 143 ? 0.39916 0.37972 0.42205 -0.03036 -0.06297 -0.06619 143 PHE A O   
1734 C CB  A PHE A 143 ? 0.53606 0.52235 0.55155 -0.03409 -0.08718 -0.08685 143 PHE A CB  
1735 C CB  B PHE A 143 ? 0.50295 0.48474 0.51498 -0.03361 -0.08632 -0.08774 143 PHE A CB  
1736 C CG  A PHE A 143 ? 0.62063 0.62354 0.64484 -0.03568 -0.09645 -0.08916 143 PHE A CG  
1737 C CG  B PHE A 143 ? 0.57328 0.54975 0.60167 -0.04351 -0.08472 -0.08884 143 PHE A CG  
1738 C CD1 A PHE A 143 ? 0.59600 0.61308 0.64071 -0.04018 -0.09574 -0.08451 143 PHE A CD1 
1739 C CD1 B PHE A 143 ? 0.62178 0.61168 0.67074 -0.05069 -0.08690 -0.08719 143 PHE A CD1 
1740 C CD2 A PHE A 143 ? 0.74319 0.74810 0.75477 -0.03198 -0.10594 -0.09606 143 PHE A CD2 
1741 C CD2 B PHE A 143 ? 0.50450 0.46257 0.52797 -0.04529 -0.08046 -0.09092 143 PHE A CD2 
1742 C CE1 A PHE A 143 ? 0.56692 0.60066 0.62110 -0.04081 -0.10455 -0.08666 143 PHE A CE1 
1743 C CE1 B PHE A 143 ? 0.57796 0.56316 0.64223 -0.06030 -0.08426 -0.08719 143 PHE A CE1 
1744 C CE2 A PHE A 143 ? 0.51964 0.54057 0.53927 -0.03265 -0.11542 -0.09810 143 PHE A CE2 
1745 C CE2 B PHE A 143 ? 0.56265 0.51427 0.60038 -0.05449 -0.07838 -0.09078 143 PHE A CE2 
1746 C CZ  A PHE A 143 ? 0.57747 0.61322 0.61934 -0.03701 -0.11481 -0.09336 143 PHE A CZ  
1747 C CZ  B PHE A 143 ? 0.62106 0.58628 0.67917 -0.06242 -0.07998 -0.08869 143 PHE A CZ  
1748 N N   . GLY A 144 ? 0.44663 0.40910 0.44465 -0.02476 -0.06681 -0.07654 144 GLY A N   
1749 C CA  . GLY A 144 ? 0.38821 0.33891 0.38603 -0.02444 -0.05903 -0.07318 144 GLY A CA  
1750 C C   . GLY A 144 ? 0.39760 0.35474 0.39766 -0.02050 -0.05173 -0.06373 144 GLY A C   
1751 O O   . GLY A 144 ? 0.39195 0.34694 0.40032 -0.02318 -0.04666 -0.05878 144 GLY A O   
1752 N N   . GLY A 145 ? 0.37080 0.33562 0.36310 -0.01425 -0.05128 -0.06107 145 GLY A N   
1753 C CA  . GLY A 145 ? 0.33542 0.30609 0.33045 -0.01110 -0.04515 -0.05283 145 GLY A CA  
1754 C C   . GLY A 145 ? 0.31707 0.29734 0.32662 -0.01543 -0.04483 -0.04836 145 GLY A C   
1755 O O   . GLY A 145 ? 0.36426 0.34480 0.37881 -0.01545 -0.03935 -0.04291 145 GLY A O   
1756 N N   . SER A 146 ? 0.34073 0.32962 0.35714 -0.01866 -0.05084 -0.05094 146 SER A N   
1757 C CA  . SER A 146 ? 0.35674 0.35621 0.38795 -0.02211 -0.05010 -0.04706 146 SER A CA  
1758 C C   . SER A 146 ? 0.36316 0.35782 0.40464 -0.02866 -0.04643 -0.04636 146 SER A C   
1759 O O   . SER A 146 ? 0.35189 0.35055 0.40084 -0.02941 -0.04122 -0.04088 146 SER A O   
1760 C CB  . SER A 146 ? 0.43818 0.44961 0.47584 -0.02347 -0.05777 -0.05012 146 SER A CB  
1761 O OG  . SER A 146 ? 0.45717 0.47332 0.48518 -0.01668 -0.06026 -0.04856 146 SER A OG  
1762 N N   . PHE A 147 ? 0.36677 0.35203 0.40804 -0.03335 -0.04894 -0.05181 147 PHE A N   
1763 C CA  . PHE A 147 ? 0.35253 0.33024 0.40202 -0.03962 -0.04465 -0.05020 147 PHE A CA  
1764 C C   . PHE A 147 ? 0.33355 0.30471 0.37814 -0.03585 -0.03666 -0.04356 147 PHE A C   
1765 O O   . PHE A 147 ? 0.31899 0.29281 0.37157 -0.03846 -0.03163 -0.03825 147 PHE A O   
1766 C CB  . PHE A 147 ? 0.43772 0.40154 0.48412 -0.04388 -0.04805 -0.05701 147 PHE A CB  
1767 C CG  . PHE A 147 ? 0.40321 0.35592 0.45600 -0.04980 -0.04291 -0.05428 147 PHE A CG  
1768 C CD1 . PHE A 147 ? 0.51367 0.47148 0.58276 -0.05901 -0.04302 -0.05380 147 PHE A CD1 
1769 C CD2 . PHE A 147 ? 0.39399 0.33206 0.43710 -0.04591 -0.03761 -0.05144 147 PHE A CD2 
1770 C CE1 . PHE A 147 ? 0.61389 0.56072 0.68819 -0.06466 -0.03736 -0.05003 147 PHE A CE1 
1771 C CE2 . PHE A 147 ? 0.49619 0.42294 0.54371 -0.05065 -0.03282 -0.04787 147 PHE A CE2 
1772 C CZ  . PHE A 147 ? 0.47218 0.40260 0.53470 -0.06022 -0.03235 -0.04684 147 PHE A CZ  
1773 N N   . PHE A 148 ? 0.32246 0.28590 0.35384 -0.02933 -0.03539 -0.04384 148 PHE A N   
1774 C CA  . PHE A 148 ? 0.28255 0.24078 0.30999 -0.02554 -0.02901 -0.03813 148 PHE A CA  
1775 C C   . PHE A 148 ? 0.27534 0.24509 0.30608 -0.02283 -0.02614 -0.03243 148 PHE A C   
1776 O O   . PHE A 148 ? 0.29621 0.26474 0.32913 -0.02286 -0.02136 -0.02749 148 PHE A O   
1777 C CB  . PHE A 148 ? 0.35682 0.30519 0.37174 -0.01942 -0.02830 -0.04017 148 PHE A CB  
1778 C CG  . PHE A 148 ? 0.31997 0.25261 0.33188 -0.02166 -0.02900 -0.04445 148 PHE A CG  
1779 C CD1 . PHE A 148 ? 0.36910 0.29190 0.38409 -0.02415 -0.02504 -0.04071 148 PHE A CD1 
1780 C CD2 . PHE A 148 ? 0.37490 0.30178 0.38043 -0.02140 -0.03381 -0.05223 148 PHE A CD2 
1781 C CE1 . PHE A 148 ? 0.41449 0.32086 0.42685 -0.02626 -0.02559 -0.04420 148 PHE A CE1 
1782 C CE2 . PHE A 148 ? 0.38996 0.30047 0.39280 -0.02363 -0.03473 -0.05688 148 PHE A CE2 
1783 C CZ  . PHE A 148 ? 0.38927 0.28915 0.39604 -0.02616 -0.03053 -0.05264 148 PHE A CZ  
1784 N N   . LEU A 149 ? 0.28954 0.26919 0.31932 -0.01993 -0.02901 -0.03299 149 LEU A N   
1785 C CA  . LEU A 149 ? 0.27692 0.26649 0.31119 -0.01802 -0.02688 -0.02833 149 LEU A CA  
1786 C C   . LEU A 149 ? 0.27496 0.26943 0.32067 -0.02272 -0.02441 -0.02591 149 LEU A C   
1787 O O   . LEU A 149 ? 0.27954 0.27488 0.32616 -0.02141 -0.01973 -0.02154 149 LEU A O   
1788 C CB  . LEU A 149 ? 0.26344 0.26206 0.29697 -0.01543 -0.03123 -0.02950 149 LEU A CB  
1789 C CG  . LEU A 149 ? 0.28139 0.28809 0.31917 -0.01287 -0.02900 -0.02493 149 LEU A CG  
1790 C CD1 . LEU A 149 ? 0.28068 0.28360 0.31193 -0.00864 -0.02501 -0.02139 149 LEU A CD1 
1791 C CD2 . LEU A 149 ? 0.36094 0.37672 0.40042 -0.01079 -0.03388 -0.02567 149 LEU A CD2 
1792 N N   . PHE A 150 ? 0.27151 0.26957 0.32604 -0.02830 -0.02743 -0.02896 150 PHE A N   
1793 C CA  A PHE A 150 ? 0.32934 0.33386 0.39657 -0.03334 -0.02428 -0.02650 150 PHE A CA  
1794 C CA  B PHE A 150 ? 0.32881 0.33334 0.39599 -0.03329 -0.02427 -0.02648 150 PHE A CA  
1795 C C   . PHE A 150 ? 0.31863 0.31275 0.38440 -0.03587 -0.01813 -0.02287 150 PHE A C   
1796 O O   . PHE A 150 ? 0.30883 0.30688 0.37876 -0.03629 -0.01272 -0.01824 150 PHE A O   
1797 C CB  A PHE A 150 ? 0.30742 0.31872 0.38637 -0.03969 -0.02921 -0.03088 150 PHE A CB  
1798 C CB  B PHE A 150 ? 0.30835 0.32028 0.38730 -0.03939 -0.02935 -0.03086 150 PHE A CB  
1799 C CG  A PHE A 150 ? 0.32091 0.34405 0.40213 -0.03685 -0.03592 -0.03394 150 PHE A CG  
1800 C CG  B PHE A 150 ? 0.35706 0.38377 0.44148 -0.03660 -0.03428 -0.03227 150 PHE A CG  
1801 C CD1 A PHE A 150 ? 0.31155 0.34023 0.38782 -0.02977 -0.03561 -0.03119 150 PHE A CD1 
1802 C CD1 B PHE A 150 ? 0.38712 0.41365 0.46107 -0.03063 -0.03893 -0.03405 150 PHE A CD1 
1803 C CD2 A PHE A 150 ? 0.38593 0.41397 0.47397 -0.04121 -0.04295 -0.03953 150 PHE A CD2 
1804 C CD2 B PHE A 150 ? 0.34671 0.38755 0.44668 -0.03944 -0.03385 -0.03130 150 PHE A CD2 
1805 C CE1 A PHE A 150 ? 0.37837 0.41654 0.45573 -0.02658 -0.04177 -0.03311 150 PHE A CE1 
1806 C CE1 B PHE A 150 ? 0.39517 0.43382 0.47299 -0.02737 -0.04358 -0.03451 150 PHE A CE1 
1807 C CE2 A PHE A 150 ? 0.42880 0.46781 0.51785 -0.03780 -0.04983 -0.04200 150 PHE A CE2 
1808 C CE2 B PHE A 150 ? 0.29746 0.35171 0.40266 -0.03579 -0.03873 -0.03237 150 PHE A CE2 
1809 C CZ  A PHE A 150 ? 0.40857 0.45227 0.49184 -0.03019 -0.04901 -0.03835 150 PHE A CZ  
1810 C CZ  B PHE A 150 ? 0.32614 0.37850 0.41966 -0.02961 -0.04386 -0.03380 150 PHE A CZ  
1811 N N   . LEU A 151 ? 0.29875 0.27902 0.35770 -0.03693 -0.01874 -0.02480 151 LEU A N   
1812 C CA  . LEU A 151 ? 0.28300 0.25156 0.33890 -0.03824 -0.01320 -0.02061 151 LEU A CA  
1813 C C   . LEU A 151 ? 0.31486 0.28344 0.36290 -0.03168 -0.00905 -0.01556 151 LEU A C   
1814 O O   . LEU A 151 ? 0.28619 0.25373 0.33489 -0.03238 -0.00370 -0.01039 151 LEU A O   
1815 C CB  . LEU A 151 ? 0.31143 0.26405 0.35992 -0.03853 -0.01525 -0.02408 151 LEU A CB  
1816 C CG  . LEU A 151 ? 0.36960 0.30796 0.41326 -0.03851 -0.01005 -0.01930 151 LEU A CG  
1817 C CD1 . LEU A 151 ? 0.34203 0.28165 0.39559 -0.04574 -0.00536 -0.01479 151 LEU A CD1 
1818 C CD2 . LEU A 151 ? 0.39990 0.32131 0.43718 -0.03859 -0.01243 -0.02352 151 LEU A CD2 
1819 N N   . THR A 152 ? 0.30930 0.27911 0.34966 -0.02544 -0.01148 -0.01704 152 THR A N   
1820 C CA  . THR A 152 ? 0.29989 0.27024 0.33391 -0.01973 -0.00875 -0.01326 152 THR A CA  
1821 C C   . THR A 152 ? 0.30431 0.28442 0.34340 -0.01992 -0.00583 -0.01008 152 THR A C   
1822 O O   . THR A 152 ? 0.28105 0.25889 0.31689 -0.01848 -0.00174 -0.00601 152 THR A O   
1823 C CB  . THR A 152 ? 0.30473 0.27796 0.33333 -0.01455 -0.01179 -0.01549 152 THR A CB  
1824 O OG1 . THR A 152 ? 0.29695 0.26105 0.31942 -0.01295 -0.01331 -0.01828 152 THR A OG1 
1825 C CG2 . THR A 152 ? 0.28715 0.26318 0.31204 -0.00980 -0.00975 -0.01215 152 THR A CG2 
1826 N N   . PHE A 153 ? 0.27585 0.26677 0.32235 -0.02114 -0.00801 -0.01204 153 PHE A N   
1827 C CA  . PHE A 153 ? 0.28665 0.28729 0.33828 -0.02022 -0.00529 -0.00981 153 PHE A CA  
1828 C C   . PHE A 153 ? 0.24802 0.25033 0.30654 -0.02490 -0.00021 -0.00698 153 PHE A C   
1829 O O   . PHE A 153 ? 0.29031 0.29586 0.34794 -0.02296 0.00446  -0.00379 153 PHE A O   
1830 C CB  . PHE A 153 ? 0.27869 0.28972 0.33565 -0.01867 -0.00935 -0.01240 153 PHE A CB  
1831 C CG  . PHE A 153 ? 0.29403 0.30413 0.34351 -0.01308 -0.01122 -0.01247 153 PHE A CG  
1832 C CD1 . PHE A 153 ? 0.29756 0.30213 0.34022 -0.01157 -0.01427 -0.01419 153 PHE A CD1 
1833 C CD2 . PHE A 153 ? 0.24956 0.26332 0.29843 -0.00945 -0.00927 -0.01079 153 PHE A CD2 
1834 C CE1 . PHE A 153 ? 0.29399 0.29814 0.33106 -0.00722 -0.01498 -0.01348 153 PHE A CE1 
1835 C CE2 . PHE A 153 ? 0.28432 0.29622 0.32747 -0.00540 -0.01088 -0.01075 153 PHE A CE2 
1836 C CZ  . PHE A 153 ? 0.31316 0.32069 0.35108 -0.00467 -0.01350 -0.01170 153 PHE A CZ  
1837 N N   . TYR A 154 ? 0.26057 0.26003 0.32535 -0.03113 -0.00075 -0.00811 154 TYR A N   
1838 C CA  . TYR A 154 ? 0.29564 0.29533 0.36736 -0.03663 0.00506  -0.00448 154 TYR A CA  
1839 C C   . TYR A 154 ? 0.27967 0.26815 0.34057 -0.03453 0.01053  0.00083  154 TYR A C   
1840 O O   . TYR A 154 ? 0.30847 0.30037 0.36948 -0.03427 0.01672  0.00529  154 TYR A O   
1841 C CB  . TYR A 154 ? 0.32112 0.31756 0.40163 -0.04453 0.00268  -0.00716 154 TYR A CB  
1842 C CG  . TYR A 154 ? 0.33293 0.32876 0.42163 -0.05132 0.00947  -0.00261 154 TYR A CG  
1843 C CD1 . TYR A 154 ? 0.47263 0.48395 0.57470 -0.05412 0.01324  -0.00101 154 TYR A CD1 
1844 C CD2 . TYR A 154 ? 0.43995 0.41971 0.52307 -0.05450 0.01270  0.00063  154 TYR A CD2 
1845 C CE1 . TYR A 154 ? 0.48875 0.50070 0.59913 -0.06072 0.02066  0.00386  154 TYR A CE1 
1846 C CE2 . TYR A 154 ? 0.47638 0.45475 0.56675 -0.06120 0.01985  0.00596  154 TYR A CE2 
1847 C CZ  . TYR A 154 ? 0.50507 0.50022 0.60924 -0.06454 0.02412  0.00765  154 TYR A CZ  
1848 O OH  . TYR A 154 ? 0.50844 0.50376 0.62072 -0.07150 0.03237  0.01353  154 TYR A OH  
1849 N N   . LEU A 155 ? 0.29574 0.27105 0.34662 -0.03230 0.00836  0.00048  155 LEU A N   
1850 C CA  . LEU A 155 ? 0.30325 0.26798 0.34298 -0.02897 0.01229  0.00557  155 LEU A CA  
1851 C C   . LEU A 155 ? 0.28887 0.25999 0.32217 -0.02275 0.01406  0.00758  155 LEU A C   
1852 O O   . LEU A 155 ? 0.31206 0.28074 0.33967 -0.02148 0.01924  0.01257  155 LEU A O   
1853 C CB  . LEU A 155 ? 0.32682 0.27927 0.35788 -0.02560 0.00850  0.00381  155 LEU A CB  
1854 C CG  . LEU A 155 ? 0.33141 0.27264 0.36521 -0.03066 0.00696  0.00164  155 LEU A CG  
1855 C CD1 . LEU A 155 ? 0.34814 0.27989 0.37334 -0.02535 0.00280  -0.00164 155 LEU A CD1 
1856 C CD2 . LEU A 155 ? 0.38332 0.31428 0.41749 -0.03540 0.01283  0.00759  155 LEU A CD2 
1857 N N   . LEU A 156 ? 0.27891 0.25727 0.31207 -0.01878 0.00976  0.00374  156 LEU A N   
1858 C CA  . LEU A 156 ? 0.27040 0.25431 0.29857 -0.01352 0.01065  0.00443  156 LEU A CA  
1859 C C   . LEU A 156 ? 0.29711 0.28951 0.33023 -0.01482 0.01597  0.00642  156 LEU A C   
1860 O O   . LEU A 156 ? 0.30068 0.29243 0.32628 -0.01162 0.01988  0.00930  156 LEU A O   
1861 C CB  . LEU A 156 ? 0.32315 0.31270 0.35291 -0.01066 0.00536  0.00007  156 LEU A CB  
1862 C CG  . LEU A 156 ? 0.53404 0.52913 0.56091 -0.00607 0.00524  -0.00057 156 LEU A CG  
1863 C CD1 . LEU A 156 ? 0.41582 0.40499 0.43200 -0.00218 0.00602  0.00149  156 LEU A CD1 
1864 C CD2 . LEU A 156 ? 0.35965 0.35804 0.38857 -0.00423 0.00023  -0.00402 156 LEU A CD2 
1865 N N   . TYR A 157 ? 0.30085 0.30172 0.34653 -0.01927 0.01628  0.00483  157 TYR A N   
1866 C CA  . TYR A 157 ? 0.29580 0.30766 0.34872 -0.01983 0.02141  0.00612  157 TYR A CA  
1867 C C   . TYR A 157 ? 0.30128 0.30967 0.35174 -0.02242 0.02932  0.01183  157 TYR A C   
1868 O O   . TYR A 157 ? 0.32523 0.33679 0.37014 -0.01876 0.03457  0.01422  157 TYR A O   
1869 C CB  . TYR A 157 ? 0.31655 0.33936 0.38540 -0.02428 0.01935  0.00328  157 TYR A CB  
1870 C CG  . TYR A 157 ? 0.32232 0.35928 0.40047 -0.02317 0.02397  0.00377  157 TYR A CG  
1871 C CD1 . TYR A 157 ? 0.29679 0.33889 0.38210 -0.02739 0.03173  0.00767  157 TYR A CD1 
1872 C CD2 . TYR A 157 ? 0.28349 0.32822 0.36311 -0.01745 0.02110  0.00061  157 TYR A CD2 
1873 C CE1 . TYR A 157 ? 0.29917 0.35587 0.39373 -0.02551 0.03676  0.00795  157 TYR A CE1 
1874 C CE2 . TYR A 157 ? 0.33531 0.39306 0.42366 -0.01512 0.02543  0.00061  157 TYR A CE2 
1875 C CZ  . TYR A 157 ? 0.38334 0.44782 0.47933 -0.01893 0.03337  0.00409  157 TYR A CZ  
1876 O OH  . TYR A 157 ? 0.31382 0.39260 0.41926 -0.01602 0.03845  0.00400  157 TYR A OH  
1877 N N   . VAL A 158 ? 0.27548 0.27644 0.32919 -0.02865 0.03051  0.01414  158 VAL A N   
1878 C CA  . VAL A 158 ? 0.33170 0.32973 0.38525 -0.03243 0.03897  0.02054  158 VAL A CA  
1879 C C   . VAL A 158 ? 0.34024 0.32721 0.37581 -0.02713 0.04217  0.02547  158 VAL A C   
1880 O O   . VAL A 158 ? 0.43420 0.41984 0.46614 -0.02819 0.05018  0.03156  158 VAL A O   
1881 C CB  . VAL A 158 ? 0.34578 0.33797 0.40919 -0.04155 0.03963  0.02181  158 VAL A CB  
1882 C CG1 . VAL A 158 ? 0.46316 0.46922 0.54532 -0.04687 0.03655  0.01696  158 VAL A CG1 
1883 C CG2 . VAL A 158 ? 0.36201 0.33793 0.41677 -0.04095 0.03389  0.02034  158 VAL A CG2 
1884 N N   . LYS A 159 ? 0.35984 0.33941 0.38408 -0.02135 0.03625  0.02334  159 LYS A N   
1885 C CA  . LYS A 159 ? 0.33203 0.30246 0.33950 -0.01573 0.03811  0.02771  159 LYS A CA  
1886 C C   . LYS A 159 ? 0.32068 0.29802 0.31994 -0.00864 0.03749  0.02560  159 LYS A C   
1887 O O   . LYS A 159 ? 0.34542 0.32009 0.33244 -0.00479 0.04179  0.02962  159 LYS A O   
1888 C CB  . LYS A 159 ? 0.38677 0.34468 0.38687 -0.01330 0.03220  0.02717  159 LYS A CB  
1889 C CG  . LYS A 159 ? 0.44963 0.39833 0.43271 -0.00689 0.03298  0.03195  159 LYS A CG  
1890 C CD  . LYS A 159 ? 0.62461 0.55795 0.60285 -0.00717 0.03195  0.03553  159 LYS A CD  
1891 C CE  . LYS A 159 ? 0.59747 0.52174 0.55893 -0.00065 0.03305  0.04149  159 LYS A CE  
1892 N NZ  . LYS A 159 ? 0.66246 0.57759 0.61934 -0.00401 0.04128  0.05006  159 LYS A NZ  
1893 N N   . TYR A 160 ? 0.29734 0.28248 0.30206 -0.00665 0.03206  0.01932  160 TYR A N   
1894 C CA  . TYR A 160 ? 0.33006 0.31795 0.32605 0.00002  0.02952  0.01637  160 TYR A CA  
1895 C C   . TYR A 160 ? 0.38399 0.38314 0.38548 0.00166  0.03175  0.01315  160 TYR A C   
1896 O O   . TYR A 160 ? 0.33384 0.33366 0.32640 0.00721  0.03091  0.01090  160 TYR A O   
1897 C CB  . TYR A 160 ? 0.31301 0.29783 0.30756 0.00246  0.02114  0.01219  160 TYR A CB  
1898 C CG  . TYR A 160 ? 0.31423 0.28840 0.30125 0.00341  0.01895  0.01506  160 TYR A CG  
1899 C CD1 . TYR A 160 ? 0.32688 0.29546 0.30015 0.00820  0.01948  0.01823  160 TYR A CD1 
1900 C CD2 . TYR A 160 ? 0.30705 0.27657 0.30008 0.00020  0.01625  0.01446  160 TYR A CD2 
1901 C CE1 . TYR A 160 ? 0.33645 0.29552 0.30312 0.01011  0.01731  0.02125  160 TYR A CE1 
1902 C CE2 . TYR A 160 ? 0.32277 0.28210 0.30905 0.00215  0.01452  0.01691  160 TYR A CE2 
1903 C CZ  . TYR A 160 ? 0.34888 0.30334 0.32259 0.00726  0.01497  0.02050  160 TYR A CZ  
1904 O OH  . TYR A 160 ? 0.34916 0.29378 0.31626 0.01028  0.01299  0.02332  160 TYR A OH  
1905 N N   . THR A 161 ? 0.32338 0.33128 0.33925 -0.00251 0.03407  0.01240  161 THR A N   
1906 C CA  . THR A 161 ? 0.32883 0.34763 0.35031 0.00039  0.03610  0.00932  161 THR A CA  
1907 C C   . THR A 161 ? 0.36156 0.38579 0.38123 0.00127  0.04574  0.01293  161 THR A C   
1908 O O   . THR A 161 ? 0.33971 0.36034 0.35644 -0.00199 0.05161  0.01868  161 THR A O   
1909 C CB  . THR A 161 ? 0.27046 0.29847 0.30897 -0.00299 0.03323  0.00637  161 THR A CB  
1910 O OG1 . THR A 161 ? 0.33263 0.36486 0.38254 -0.00987 0.03730  0.00953  161 THR A OG1 
1911 C CG2 . THR A 161 ? 0.25373 0.27720 0.29278 -0.00310 0.02455  0.00293  161 THR A CG2 
1912 N N   . LYS A 162 ? 0.29907 0.33168 0.32039 0.00605  0.04780  0.00965  162 LYS A N   
1913 C CA  . LYS A 162 ? 0.31242 0.35400 0.33553 0.00754  0.05757  0.01197  162 LYS A CA  
1914 C C   . LYS A 162 ? 0.33327 0.38892 0.37421 0.00777  0.05772  0.00844  162 LYS A C   
1915 O O   . LYS A 162 ? 0.31916 0.37530 0.36582 0.00884  0.04997  0.00393  162 LYS A O   
1916 C CB  . LYS A 162 ? 0.36915 0.40685 0.37389 0.01541  0.06055  0.01085  162 LYS A CB  
1917 C CG  . LYS A 162 ? 0.41809 0.44440 0.40522 0.01563  0.06237  0.01597  162 LYS A CG  
1918 C CD  . LYS A 162 ? 0.67980 0.70278 0.64739 0.02392  0.06421  0.01397  162 LYS A CD  
1919 C CE  . LYS A 162 ? 0.60928 0.62468 0.55979 0.02474  0.06979  0.02107  162 LYS A CE  
1920 N NZ  . LYS A 162 ? 0.80820 0.82108 0.73804 0.03340  0.07140  0.01857  162 LYS A NZ  
1921 N N   . GLU A 163 ? 0.31706 0.38472 0.36725 0.00694  0.06677  0.01099  163 GLU A N   
1922 C CA  . GLU A 163 ? 0.31111 0.39437 0.38106 0.00695  0.06694  0.00825  163 GLU A CA  
1923 C C   . GLU A 163 ? 0.33337 0.42082 0.39929 0.01672  0.06764  0.00324  163 GLU A C   
1924 O O   . GLU A 163 ? 0.32170 0.41832 0.38863 0.02077  0.07664  0.00390  163 GLU A O   
1925 C CB  . GLU A 163 ? 0.38764 0.48387 0.47309 0.00081  0.07609  0.01315  163 GLU A CB  
1926 C CG  . GLU A 163 ? 0.34717 0.43917 0.44031 -0.00971 0.07432  0.01701  163 GLU A CG  
1927 C CD  . GLU A 163 ? 0.31688 0.40978 0.42155 -0.01308 0.06326  0.01262  163 GLU A CD  
1928 O OE1 . GLU A 163 ? 0.35512 0.46067 0.47296 -0.01037 0.06004  0.00863  163 GLU A OE1 
1929 O OE2 . GLU A 163 ? 0.36088 0.44163 0.46067 -0.01785 0.05784  0.01325  163 GLU A OE2 
1930 N N   . ASN A 164 ? 0.29008 0.37057 0.35182 0.02062  0.05847  -0.00183 164 ASN A N   
1931 C CA  . ASN A 164 ? 0.33516 0.41766 0.39451 0.02964  0.05809  -0.00710 164 ASN A CA  
1932 C C   . ASN A 164 ? 0.28232 0.35932 0.34450 0.03096  0.04753  -0.01110 164 ASN A C   
1933 O O   . ASN A 164 ? 0.27040 0.34142 0.33327 0.02555  0.04097  -0.01000 164 ASN A O   
1934 C CB  . ASN A 164 ? 0.35178 0.42558 0.39072 0.03601  0.06194  -0.00882 164 ASN A CB  
1935 C CG  . ASN A 164 ? 0.33800 0.39578 0.36058 0.03462  0.05522  -0.00927 164 ASN A CG  
1936 O OD1 . ASN A 164 ? 0.31542 0.36654 0.33932 0.03332  0.04623  -0.01171 164 ASN A OD1 
1937 N ND2 . ASN A 164 ? 0.35518 0.40733 0.36237 0.03506  0.05971  -0.00647 164 ASN A ND2 
1938 N N   . TRP A 165 ? 0.28679 0.36527 0.35003 0.03866  0.04645  -0.01559 165 TRP A N   
1939 C CA  . TRP A 165 ? 0.25492 0.33001 0.32357 0.04009  0.03758  -0.01819 165 TRP A CA  
1940 C C   . TRP A 165 ? 0.32387 0.38249 0.37912 0.03885  0.03037  -0.01967 165 TRP A C   
1941 O O   . TRP A 165 ? 0.31461 0.36987 0.37389 0.03625  0.02336  -0.01935 165 TRP A O   
1942 C CB  . TRP A 165 ? 0.34937 0.43061 0.42482 0.04882  0.03861  -0.02182 165 TRP A CB  
1943 C CG  . TRP A 165 ? 0.41508 0.51529 0.51047 0.04809  0.04183  -0.01979 165 TRP A CG  
1944 C CD1 . TRP A 165 ? 0.39710 0.51180 0.50061 0.05007  0.05132  -0.01880 165 TRP A CD1 
1945 C CD2 . TRP A 165 ? 0.28526 0.39321 0.39557 0.04470  0.03541  -0.01846 165 TRP A CD2 
1946 N NE1 . TRP A 165 ? 0.36252 0.49447 0.48730 0.04755  0.05084  -0.01706 165 TRP A NE1 
1947 C CE2 . TRP A 165 ? 0.34604 0.47380 0.47455 0.04448  0.04058  -0.01714 165 TRP A CE2 
1948 C CE3 . TRP A 165 ? 0.31905 0.41956 0.42869 0.04199  0.02586  -0.01828 165 TRP A CE3 
1949 C CZ2 . TRP A 165 ? 0.28571 0.42604 0.43190 0.04166  0.03525  -0.01632 165 TRP A CZ2 
1950 C CZ3 . TRP A 165 ? 0.35203 0.46397 0.47691 0.03985  0.02110  -0.01724 165 TRP A CZ3 
1951 C CH2 . TRP A 165 ? 0.32961 0.46120 0.47260 0.03957  0.02517  -0.01655 165 TRP A CH2 
1952 N N   A MET A 166 ? 0.29317 0.34222 0.33269 0.04061  0.03185  -0.02119 166 MET A N   
1953 N N   B MET A 166 ? 0.29449 0.34366 0.33402 0.04081  0.03197  -0.02127 166 MET A N   
1954 C CA  A MET A 166 ? 0.30728 0.34302 0.33666 0.03851  0.02486  -0.02239 166 MET A CA  
1955 C CA  B MET A 166 ? 0.30977 0.34553 0.33845 0.03869  0.02530  -0.02242 166 MET A CA  
1956 C C   A MET A 166 ? 0.28772 0.32282 0.31965 0.03088  0.02219  -0.01813 166 MET A C   
1957 C C   B MET A 166 ? 0.28803 0.32324 0.31992 0.03104  0.02233  -0.01819 166 MET A C   
1958 O O   A MET A 166 ? 0.33964 0.36902 0.37218 0.02840  0.01573  -0.01831 166 MET A O   
1959 O O   B MET A 166 ? 0.34155 0.37116 0.37434 0.02870  0.01582  -0.01846 166 MET A O   
1960 C CB  A MET A 166 ? 0.33214 0.35947 0.34474 0.04169  0.02620  -0.02506 166 MET A CB  
1961 C CB  B MET A 166 ? 0.34720 0.37559 0.35913 0.04157  0.02752  -0.02450 166 MET A CB  
1962 C CG  A MET A 166 ? 0.59641 0.62426 0.60429 0.04968  0.03026  -0.02977 166 MET A CG  
1963 C CG  B MET A 166 ? 0.53382 0.55519 0.53788 0.04864  0.02597  -0.03096 166 MET A CG  
1964 S SD  A MET A 166 ? 0.84025 0.87506 0.83917 0.05298  0.04135  -0.02814 166 MET A SD  
1965 S SD  B MET A 166 ? 0.48054 0.49640 0.46403 0.05289  0.02974  -0.03371 166 MET A SD  
1966 C CE  A MET A 166 ? 0.37088 0.42369 0.39015 0.05341  0.04861  -0.02516 166 MET A CE  
1967 C CE  B MET A 166 ? 0.33286 0.34582 0.31151 0.04553  0.02694  -0.02813 166 MET A CE  
1968 N N   . ASN A 167 ? 0.27445 0.31505 0.30820 0.02714  0.02752  -0.01415 167 ASN A N   
1969 C CA  . ASN A 167 ? 0.24364 0.28273 0.28070 0.02017  0.02502  -0.01059 167 ASN A CA  
1970 C C   . ASN A 167 ? 0.31342 0.35859 0.36448 0.01738  0.02086  -0.01065 167 ASN A C   
1971 O O   . ASN A 167 ? 0.31262 0.35280 0.36351 0.01410  0.01532  -0.01032 167 ASN A O   
1972 C CB  . ASN A 167 ? 0.23690 0.27973 0.27424 0.01656  0.03209  -0.00611 167 ASN A CB  
1973 C CG  . ASN A 167 ? 0.25159 0.28507 0.27244 0.01761  0.03393  -0.00434 167 ASN A CG  
1974 O OD1 . ASN A 167 ? 0.30053 0.32737 0.31755 0.01379  0.03171  -0.00163 167 ASN A OD1 
1975 N ND2 . ASN A 167 ? 0.30487 0.33756 0.31537 0.02338  0.03758  -0.00611 167 ASN A ND2 
1976 N N   . TYR A 168 ? 0.25139 0.30800 0.31443 0.01917  0.02330  -0.01118 168 TYR A N   
1977 C CA  . TYR A 168 ? 0.27999 0.34343 0.35596 0.01687  0.01845  -0.01128 168 TYR A CA  
1978 C C   . TYR A 168 ? 0.24861 0.30444 0.32059 0.01958  0.01105  -0.01327 168 TYR A C   
1979 O O   . TYR A 168 ? 0.27574 0.33019 0.35001 0.01623  0.00578  -0.01265 168 TYR A O   
1980 C CB  . TYR A 168 ? 0.32517 0.40389 0.41583 0.01942  0.02172  -0.01173 168 TYR A CB  
1981 C CG  . TYR A 168 ? 0.27390 0.36231 0.37099 0.01640  0.03030  -0.00920 168 TYR A CG  
1982 C CD1 . TYR A 168 ? 0.29574 0.38070 0.39087 0.00894  0.03269  -0.00585 168 TYR A CD1 
1983 C CD2 . TYR A 168 ? 0.31824 0.41847 0.42287 0.02137  0.03668  -0.00984 168 TYR A CD2 
1984 C CE1 . TYR A 168 ? 0.26823 0.36119 0.36925 0.00561  0.04150  -0.00249 168 TYR A CE1 
1985 C CE2 . TYR A 168 ? 0.28541 0.39537 0.39625 0.01842  0.04585  -0.00681 168 TYR A CE2 
1986 C CZ  . TYR A 168 ? 0.26810 0.37406 0.37703 0.01019  0.04828  -0.00284 168 TYR A CZ  
1987 O OH  . TYR A 168 ? 0.28590 0.40046 0.40074 0.00689  0.05806  0.00104  168 TYR A OH  
1988 N N   . ILE A 169 ? 0.23880 0.28880 0.30414 0.02555  0.01082  -0.01569 169 ILE A N   
1989 C CA  . ILE A 169 ? 0.24696 0.28847 0.30875 0.02758  0.00458  -0.01687 169 ILE A CA  
1990 C C   . ILE A 169 ? 0.24714 0.28003 0.30171 0.02262  0.00110  -0.01560 169 ILE A C   
1991 O O   . ILE A 169 ? 0.26214 0.29387 0.31876 0.02063  -0.00340 -0.01446 169 ILE A O   
1992 C CB  . ILE A 169 ? 0.24825 0.28257 0.30350 0.03394  0.00518  -0.02014 169 ILE A CB  
1993 C CG1 . ILE A 169 ? 0.23705 0.27971 0.30043 0.04047  0.00800  -0.02170 169 ILE A CG1 
1994 C CG2 . ILE A 169 ? 0.28882 0.31161 0.33938 0.03408  -0.00086 -0.02058 169 ILE A CG2 
1995 C CD1 . ILE A 169 ? 0.33553 0.37009 0.39074 0.04700  0.00978  -0.02587 169 ILE A CD1 
1996 N N   . VAL A 170 ? 0.27816 0.30560 0.32389 0.02112  0.00325  -0.01567 170 VAL A N   
1997 C CA  . VAL A 170 ? 0.29776 0.31790 0.33735 0.01749  0.00008  -0.01469 170 VAL A CA  
1998 C C   . VAL A 170 ? 0.26215 0.28558 0.30635 0.01258  -0.00073 -0.01230 170 VAL A C   
1999 O O   . VAL A 170 ? 0.29436 0.31465 0.33804 0.01073  -0.00462 -0.01182 170 VAL A O   
2000 C CB  . VAL A 170 ? 0.34966 0.36439 0.37901 0.01795  0.00198  -0.01531 170 VAL A CB  
2001 C CG1 . VAL A 170 ? 0.36120 0.37031 0.38624 0.01485  -0.00144 -0.01424 170 VAL A CG1 
2002 C CG2 . VAL A 170 ? 0.30785 0.31814 0.33180 0.02275  0.00157  -0.01902 170 VAL A CG2 
2003 N N   . PHE A 171 ? 0.24439 0.27420 0.29357 0.01034  0.00311  -0.01096 171 PHE A N   
2004 C CA  . PHE A 171 ? 0.29100 0.32193 0.34404 0.00512  0.00206  -0.00946 171 PHE A CA  
2005 C C   . PHE A 171 ? 0.24479 0.28040 0.30521 0.00456  -0.00268 -0.01040 171 PHE A C   
2006 O O   . PHE A 171 ? 0.26948 0.30124 0.32762 0.00235  -0.00638 -0.01047 171 PHE A O   
2007 C CB  . PHE A 171 ? 0.23944 0.27559 0.29742 0.00188  0.00751  -0.00755 171 PHE A CB  
2008 C CG  . PHE A 171 ? 0.25298 0.28833 0.31515 -0.00409 0.00618  -0.00659 171 PHE A CG  
2009 C CD1 . PHE A 171 ? 0.29313 0.31867 0.34723 -0.00631 0.00629  -0.00512 171 PHE A CD1 
2010 C CD2 . PHE A 171 ? 0.28242 0.32640 0.35656 -0.00710 0.00408  -0.00767 171 PHE A CD2 
2011 C CE1 . PHE A 171 ? 0.28556 0.30828 0.34290 -0.01148 0.00491  -0.00493 171 PHE A CE1 
2012 C CE2 . PHE A 171 ? 0.32592 0.36786 0.40345 -0.01289 0.00200  -0.00792 171 PHE A CE2 
2013 C CZ  . PHE A 171 ? 0.29779 0.32825 0.36661 -0.01511 0.00272  -0.00665 171 PHE A CZ  
2014 N N   . TYR A 172 ? 0.25178 0.29614 0.32066 0.00724  -0.00267 -0.01118 172 TYR A N   
2015 C CA  . TYR A 172 ? 0.22960 0.28011 0.30593 0.00693  -0.00765 -0.01182 172 TYR A CA  
2016 C C   . TYR A 172 ? 0.22541 0.26957 0.29550 0.01027  -0.01248 -0.01184 172 TYR A C   
2017 O O   . TYR A 172 ? 0.25500 0.29987 0.32532 0.00920  -0.01710 -0.01185 172 TYR A O   
2018 C CB  . TYR A 172 ? 0.28073 0.34452 0.36992 0.00885  -0.00637 -0.01237 172 TYR A CB  
2019 C CG  . TYR A 172 ? 0.23154 0.30308 0.32966 0.00314  -0.00248 -0.01180 172 TYR A CG  
2020 C CD1 . TYR A 172 ? 0.24476 0.31868 0.34821 -0.00277 -0.00609 -0.01244 172 TYR A CD1 
2021 C CD2 . TYR A 172 ? 0.25722 0.33269 0.35764 0.00347  0.00504  -0.01063 172 TYR A CD2 
2022 C CE1 . TYR A 172 ? 0.24749 0.32694 0.35991 -0.00905 -0.00259 -0.01180 172 TYR A CE1 
2023 C CE2 . TYR A 172 ? 0.29976 0.38156 0.40857 -0.00252 0.00951  -0.00909 172 TYR A CE2 
2024 C CZ  . TYR A 172 ? 0.28018 0.36355 0.39567 -0.00924 0.00560  -0.00960 172 TYR A CZ  
2025 O OH  . TYR A 172 ? 0.32662 0.41506 0.45152 -0.01615 0.00997  -0.00801 172 TYR A OH  
2026 N N   A PHE A 173 ? 0.24224 0.27982 0.30640 0.01413  -0.01147 -0.01185 173 PHE A N   
2027 N N   B PHE A 173 ? 0.24319 0.28066 0.30722 0.01405  -0.01142 -0.01185 173 PHE A N   
2028 C CA  A PHE A 173 ? 0.25205 0.28199 0.31021 0.01592  -0.01512 -0.01102 173 PHE A CA  
2029 C CA  B PHE A 173 ? 0.25375 0.28374 0.31196 0.01593  -0.01508 -0.01104 173 PHE A CA  
2030 C C   A PHE A 173 ? 0.29694 0.32188 0.34915 0.01181  -0.01646 -0.01025 173 PHE A C   
2031 C C   B PHE A 173 ? 0.29591 0.32049 0.34788 0.01196  -0.01641 -0.01024 173 PHE A C   
2032 O O   A PHE A 173 ? 0.24830 0.27289 0.29894 0.01151  -0.01985 -0.00939 173 PHE A O   
2033 O O   B PHE A 173 ? 0.27379 0.29698 0.32349 0.01197  -0.01970 -0.00918 173 PHE A O   
2034 C CB  A PHE A 173 ? 0.29456 0.31698 0.34792 0.01920  -0.01361 -0.01176 173 PHE A CB  
2035 C CB  B PHE A 173 ? 0.29356 0.31620 0.34720 0.01939  -0.01369 -0.01175 173 PHE A CB  
2036 C CG  A PHE A 173 ? 0.27746 0.29190 0.32688 0.02098  -0.01670 -0.01040 173 PHE A CG  
2037 C CG  B PHE A 173 ? 0.32345 0.33701 0.37128 0.01934  -0.01633 -0.01042 173 PHE A CG  
2038 C CD1 A PHE A 173 ? 0.33826 0.35374 0.38827 0.02160  -0.02016 -0.00811 173 PHE A CD1 
2039 C CD1 B PHE A 173 ? 0.30456 0.31618 0.35311 0.02234  -0.01922 -0.00862 173 PHE A CD1 
2040 C CD2 A PHE A 173 ? 0.34707 0.35260 0.39186 0.02184  -0.01613 -0.01138 173 PHE A CD2 
2041 C CD2 B PHE A 173 ? 0.31476 0.32227 0.35698 0.01638  -0.01574 -0.01052 173 PHE A CD2 
2042 C CE1 A PHE A 173 ? 0.44467 0.45196 0.49034 0.02307  -0.02200 -0.00573 173 PHE A CE1 
2043 C CE1 B PHE A 173 ? 0.46546 0.46855 0.50901 0.02173  -0.02063 -0.00648 173 PHE A CE1 
2044 C CE2 A PHE A 173 ? 0.45649 0.45398 0.49880 0.02245  -0.01832 -0.00962 173 PHE A CE2 
2045 C CE2 B PHE A 173 ? 0.42901 0.42978 0.46799 0.01565  -0.01746 -0.00898 173 PHE A CE2 
2046 C CZ  A PHE A 173 ? 0.44911 0.44724 0.49171 0.02309  -0.02075 -0.00626 173 PHE A CZ  
2047 C CZ  B PHE A 173 ? 0.39852 0.39674 0.43806 0.01798  -0.01946 -0.00673 173 PHE A CZ  
2048 N N   . MET A 174 ? 0.23861 0.26025 0.28717 0.00918  -0.01369 -0.01057 174 MET A N   
2049 C CA  A MET A 174 ? 0.26305 0.28021 0.30658 0.00620  -0.01448 -0.01011 174 MET A CA  
2050 C CA  B MET A 174 ? 0.26350 0.28066 0.30704 0.00634  -0.01469 -0.01008 174 MET A CA  
2051 C C   . MET A 174 ? 0.28545 0.30620 0.33164 0.00362  -0.01662 -0.01063 174 MET A C   
2052 O O   . MET A 174 ? 0.27578 0.29407 0.31795 0.00327  -0.01907 -0.01058 174 MET A O   
2053 C CB  A MET A 174 ? 0.26835 0.28217 0.30831 0.00474  -0.01137 -0.01013 174 MET A CB  
2054 C CB  B MET A 174 ? 0.27502 0.28807 0.31430 0.00508  -0.01192 -0.01009 174 MET A CB  
2055 C CG  A MET A 174 ? 0.63512 0.64318 0.66934 0.00604  -0.01153 -0.01013 174 MET A CG  
2056 C CG  B MET A 174 ? 0.13165 0.14032 0.16640 0.00341  -0.01285 -0.00968 174 MET A CG  
2057 S SD  A MET A 174 ? 0.44353 0.44755 0.47212 0.00491  -0.00991 -0.00964 174 MET A SD  
2058 S SD  B MET A 174 ? 0.20904 0.21399 0.23959 0.00287  -0.01007 -0.00924 174 MET A SD  
2059 C CE  A MET A 174 ? 0.22331 0.22762 0.25370 0.00174  -0.00936 -0.00895 174 MET A CE  
2060 C CE  B MET A 174 ? 0.17483 0.17548 0.20141 0.00243  -0.01150 -0.00900 174 MET A CE  
2061 N N   . PHE A 175 ? 0.23964 0.26646 0.29275 0.00160  -0.01558 -0.01141 175 PHE A N   
2062 C CA  . PHE A 175 ? 0.25836 0.28832 0.31504 -0.00182 -0.01827 -0.01285 175 PHE A CA  
2063 C C   . PHE A 175 ? 0.28585 0.31915 0.34254 0.00042  -0.02353 -0.01349 175 PHE A C   
2064 O O   . PHE A 175 ? 0.27910 0.30989 0.33116 -0.00074 -0.02667 -0.01475 175 PHE A O   
2065 C CB  . PHE A 175 ? 0.25735 0.29486 0.32418 -0.00484 -0.01597 -0.01325 175 PHE A CB  
2066 C CG  . PHE A 175 ? 0.30190 0.34178 0.37397 -0.01000 -0.01857 -0.01531 175 PHE A CG  
2067 C CD1 . PHE A 175 ? 0.29165 0.32390 0.35674 -0.01186 -0.02134 -0.01697 175 PHE A CD1 
2068 C CD2 . PHE A 175 ? 0.34968 0.39963 0.43447 -0.01321 -0.01794 -0.01595 175 PHE A CD2 
2069 C CE1 . PHE A 175 ? 0.30395 0.33703 0.37358 -0.01680 -0.02424 -0.01988 175 PHE A CE1 
2070 C CE2 . PHE A 175 ? 0.61160 0.66370 0.70275 -0.01898 -0.02089 -0.01844 175 PHE A CE2 
2071 C CZ  . PHE A 175 ? 0.43103 0.47371 0.51390 -0.02079 -0.02438 -0.02071 175 PHE A CZ  
2072 N N   . LEU A 176 ? 0.24997 0.28839 0.31078 0.00434  -0.02456 -0.01263 176 LEU A N   
2073 C CA  . LEU A 176 ? 0.27822 0.31958 0.33820 0.00742  -0.02988 -0.01238 176 LEU A CA  
2074 C C   . LEU A 176 ? 0.27104 0.30366 0.31946 0.00892  -0.03083 -0.01067 176 LEU A C   
2075 O O   . LEU A 176 ? 0.28358 0.31621 0.32698 0.00924  -0.03470 -0.01111 176 LEU A O   
2076 C CB  . LEU A 176 ? 0.26864 0.31526 0.33461 0.01248  -0.03028 -0.01120 176 LEU A CB  
2077 C CG  . LEU A 176 ? 0.32636 0.37429 0.39000 0.01729  -0.03570 -0.00967 176 LEU A CG  
2078 C CD1 . LEU A 176 ? 0.30540 0.36093 0.37140 0.01567  -0.04165 -0.01179 176 LEU A CD1 
2079 C CD2 . LEU A 176 ? 0.31488 0.36694 0.38528 0.02319  -0.03547 -0.00858 176 LEU A CD2 
2080 N N   . VAL A 177 ? 0.22744 0.25311 0.27161 0.00983  -0.02731 -0.00884 177 VAL A N   
2081 C CA  . VAL A 177 ? 0.23939 0.25811 0.27483 0.01075  -0.02721 -0.00663 177 VAL A CA  
2082 C C   . VAL A 177 ? 0.21978 0.23654 0.24972 0.00810  -0.02725 -0.00807 177 VAL A C   
2083 O O   . VAL A 177 ? 0.23492 0.25015 0.25794 0.00934  -0.02894 -0.00719 177 VAL A O   
2084 C CB  . VAL A 177 ? 0.23718 0.25004 0.27167 0.01101  -0.02377 -0.00528 177 VAL A CB  
2085 C CG1 . VAL A 177 ? 0.31375 0.32121 0.34168 0.01031  -0.02268 -0.00321 177 VAL A CG1 
2086 C CG2 . VAL A 177 ? 0.24772 0.25981 0.28539 0.01470  -0.02427 -0.00406 177 VAL A CG2 
2087 N N   . TRP A 178 ? 0.22750 0.24358 0.25953 0.00495  -0.02510 -0.01018 178 TRP A N   
2088 C CA  . TRP A 178 ? 0.27257 0.28559 0.29958 0.00309  -0.02528 -0.01213 178 TRP A CA  
2089 C C   . TRP A 178 ? 0.25692 0.27308 0.28276 0.00267  -0.02988 -0.01474 178 TRP A C   
2090 O O   . TRP A 178 ? 0.26170 0.27501 0.27940 0.00366  -0.03114 -0.01575 178 TRP A O   
2091 C CB  . TRP A 178 ? 0.23750 0.24768 0.26666 0.00035  -0.02238 -0.01330 178 TRP A CB  
2092 C CG  . TRP A 178 ? 0.23966 0.24618 0.26685 0.00143  -0.01907 -0.01136 178 TRP A CG  
2093 C CD1 . TRP A 178 ? 0.27145 0.27834 0.29977 0.00311  -0.01814 -0.00943 178 TRP A CD1 
2094 C CD2 . TRP A 178 ? 0.26731 0.26927 0.29135 0.00111  -0.01704 -0.01161 178 TRP A CD2 
2095 N NE1 . TRP A 178 ? 0.25567 0.25947 0.28223 0.00326  -0.01612 -0.00884 178 TRP A NE1 
2096 C CE2 . TRP A 178 ? 0.30546 0.30685 0.32956 0.00246  -0.01541 -0.00986 178 TRP A CE2 
2097 C CE3 . TRP A 178 ? 0.27820 0.27600 0.29958 0.00012  -0.01678 -0.01339 178 TRP A CE3 
2098 C CZ2 . TRP A 178 ? 0.29060 0.28927 0.31277 0.00315  -0.01395 -0.00961 178 TRP A CZ2 
2099 C CZ3 . TRP A 178 ? 0.25585 0.24959 0.27471 0.00140  -0.01471 -0.01275 178 TRP A CZ3 
2100 C CH2 . TRP A 178 ? 0.23601 0.23119 0.25556 0.00306  -0.01352 -0.01076 178 TRP A CH2 
2101 N N   A PHE A 179 ? 0.26922 0.29196 0.30317 0.00139  -0.03253 -0.01619 179 PHE A N   
2102 N N   B PHE A 179 ? 0.26985 0.29273 0.30389 0.00155  -0.03252 -0.01605 179 PHE A N   
2103 C CA  A PHE A 179 ? 0.28721 0.31421 0.32107 0.00086  -0.03826 -0.01928 179 PHE A CA  
2104 C CA  B PHE A 179 ? 0.27453 0.30256 0.30982 0.00091  -0.03829 -0.01909 179 PHE A CA  
2105 C C   A PHE A 179 ? 0.27118 0.29784 0.29572 0.00548  -0.04144 -0.01760 179 PHE A C   
2106 C C   B PHE A 179 ? 0.26106 0.28926 0.28751 0.00547  -0.04200 -0.01766 179 PHE A C   
2107 O O   A PHE A 179 ? 0.22849 0.25401 0.24534 0.00588  -0.04505 -0.02024 179 PHE A O   
2108 O O   B PHE A 179 ? 0.29987 0.32943 0.32146 0.00567  -0.04696 -0.02063 179 PHE A O   
2109 C CB  A PHE A 179 ? 0.28213 0.31896 0.32881 -0.00081 -0.04066 -0.02049 179 PHE A CB  
2110 C CB  B PHE A 179 ? 0.25903 0.29676 0.30751 -0.00025 -0.03966 -0.01955 179 PHE A CB  
2111 C CG  A PHE A 179 ? 0.36091 0.40389 0.40962 -0.00187 -0.04778 -0.02436 179 PHE A CG  
2112 C CG  B PHE A 179 ? 0.28554 0.33134 0.33911 -0.00154 -0.04641 -0.02311 179 PHE A CG  
2113 C CD1 A PHE A 179 ? 0.39906 0.44110 0.45082 -0.00742 -0.04961 -0.02899 179 PHE A CD1 
2114 C CD1 B PHE A 179 ? 0.36736 0.41859 0.41890 0.00317  -0.05197 -0.02239 179 PHE A CD1 
2115 C CD2 A PHE A 179 ? 0.39321 0.44202 0.44015 0.00281  -0.05318 -0.02349 179 PHE A CD2 
2116 C CD2 B PHE A 179 ? 0.35149 0.39945 0.41251 -0.00756 -0.04754 -0.02703 179 PHE A CD2 
2117 C CE1 A PHE A 179 ? 0.48770 0.53553 0.54165 -0.00887 -0.05722 -0.03357 179 PHE A CE1 
2118 C CE1 B PHE A 179 ? 0.43029 0.49025 0.48687 0.00224  -0.05936 -0.02614 179 PHE A CE1 
2119 C CE2 A PHE A 179 ? 0.42038 0.47566 0.46862 0.00221  -0.06091 -0.02752 179 PHE A CE2 
2120 C CE2 B PHE A 179 ? 0.51635 0.57262 0.58365 -0.00953 -0.05462 -0.03108 179 PHE A CE2 
2121 C CZ  A PHE A 179 ? 0.36989 0.42508 0.42194 -0.00390 -0.06318 -0.03301 179 PHE A CZ  
2122 C CZ  B PHE A 179 ? 0.34724 0.41026 0.41236 -0.00444 -0.06091 -0.03091 179 PHE A CZ  
2123 N N   . LEU A 180 ? 0.23772 0.26394 0.26150 0.00912  -0.03980 -0.01310 180 LEU A N   
2124 C CA  . LEU A 180 ? 0.27521 0.29990 0.28974 0.01359  -0.04206 -0.01003 180 LEU A CA  
2125 C C   . LEU A 180 ? 0.25099 0.26920 0.25317 0.01400  -0.03964 -0.00941 180 LEU A C   
2126 O O   . LEU A 180 ? 0.28215 0.29957 0.27428 0.01733  -0.04188 -0.00774 180 LEU A O   
2127 C CB  . LEU A 180 ? 0.26712 0.29035 0.28432 0.01678  -0.04012 -0.00519 180 LEU A CB  
2128 C CG  . LEU A 180 ? 0.28735 0.31860 0.31472 0.01890  -0.04385 -0.00582 180 LEU A CG  
2129 C CD1 . LEU A 180 ? 0.31949 0.34766 0.35092 0.02178  -0.04085 -0.00245 180 LEU A CD1 
2130 C CD2 . LEU A 180 ? 0.34306 0.37974 0.36695 0.02272  -0.05104 -0.00579 180 LEU A CD2 
2131 N N   . TYR A 181 ? 0.24766 0.26175 0.24997 0.01132  -0.03502 -0.01055 181 TYR A N   
2132 C CA  . TYR A 181 ? 0.30892 0.31871 0.30061 0.01221  -0.03285 -0.01112 181 TYR A CA  
2133 C C   . TYR A 181 ? 0.31640 0.32665 0.30162 0.01228  -0.03753 -0.01646 181 TYR A C   
2134 O O   . TYR A 181 ? 0.32874 0.33698 0.30178 0.01522  -0.03780 -0.01666 181 TYR A O   
2135 C CB  . TYR A 181 ? 0.26915 0.27545 0.26367 0.01009  -0.02775 -0.01173 181 TYR A CB  
2136 C CG  . TYR A 181 ? 0.27701 0.28224 0.27491 0.01027  -0.02333 -0.00714 181 TYR A CG  
2137 C CD1 . TYR A 181 ? 0.24557 0.25182 0.25211 0.00907  -0.02323 -0.00590 181 TYR A CD1 
2138 C CD2 . TYR A 181 ? 0.24312 0.24668 0.23593 0.01153  -0.01918 -0.00445 181 TYR A CD2 
2139 C CE1 . TYR A 181 ? 0.30005 0.30446 0.30940 0.00887  -0.02007 -0.00275 181 TYR A CE1 
2140 C CE2 . TYR A 181 ? 0.26237 0.26544 0.26008 0.01067  -0.01569 -0.00066 181 TYR A CE2 
2141 C CZ  . TYR A 181 ? 0.25889 0.26180 0.26455 0.00920  -0.01670 -0.00028 181 TYR A CZ  
2142 O OH  . TYR A 181 ? 0.27503 0.27667 0.28559 0.00799  -0.01433 0.00222  181 TYR A OH  
2143 N N   . GLY A 182 ? 0.27237 0.28497 0.26536 0.00884  -0.04102 -0.02105 182 GLY A N   
2144 C CA  . GLY A 182 ? 0.29128 0.30461 0.27986 0.00816  -0.04696 -0.02687 182 GLY A CA  
2145 C C   . GLY A 182 ? 0.29627 0.31486 0.27924 0.01185  -0.05309 -0.02615 182 GLY A C   
2146 O O   . GLY A 182 ? 0.34870 0.36595 0.32005 0.01394  -0.05707 -0.02958 182 GLY A O   
2147 N N   . PHE A 183 ? 0.28963 0.31383 0.27983 0.01344  -0.05421 -0.02185 183 PHE A N   
2148 C CA  . PHE A 183 ? 0.29708 0.32596 0.28176 0.01811  -0.06028 -0.02015 183 PHE A CA  
2149 C C   . PHE A 183 ? 0.33828 0.36130 0.30535 0.02301  -0.05811 -0.01613 183 PHE A C   
2150 O O   . PHE A 183 ? 0.32113 0.34501 0.27615 0.02647  -0.06336 -0.01763 183 PHE A O   
2151 C CB  . PHE A 183 ? 0.29192 0.32598 0.28767 0.01985  -0.06036 -0.01561 183 PHE A CB  
2152 C CG  . PHE A 183 ? 0.33235 0.37206 0.32501 0.02531  -0.06739 -0.01364 183 PHE A CG  
2153 C CD1 . PHE A 183 ? 0.38520 0.43384 0.38172 0.02502  -0.07609 -0.01888 183 PHE A CD1 
2154 C CD2 . PHE A 183 ? 0.32524 0.36105 0.31153 0.03076  -0.06566 -0.00640 183 PHE A CD2 
2155 C CE1 . PHE A 183 ? 0.40587 0.46068 0.39965 0.03091  -0.08344 -0.01697 183 PHE A CE1 
2156 C CE2 . PHE A 183 ? 0.37748 0.41756 0.36012 0.03675  -0.07234 -0.00388 183 PHE A CE2 
2157 C CZ  . PHE A 183 ? 0.38738 0.43756 0.37347 0.03734  -0.08153 -0.00911 183 PHE A CZ  
2158 N N   . ALA A 184 ? 0.29259 0.31013 0.25819 0.02327  -0.05033 -0.01090 184 ALA A N   
2159 C CA  . ALA A 184 ? 0.32949 0.34191 0.28045 0.02686  -0.04616 -0.00625 184 ALA A CA  
2160 C C   . ALA A 184 ? 0.28084 0.29095 0.21843 0.02787  -0.04651 -0.01119 184 ALA A C   
2161 O O   . ALA A 184 ? 0.32757 0.33583 0.24963 0.03233  -0.04617 -0.00865 184 ALA A O   
2162 C CB  . ALA A 184 ? 0.32568 0.33403 0.28180 0.02490  -0.03770 -0.00162 184 ALA A CB  
2163 N N   . PHE A 185 ? 0.31666 0.32577 0.25909 0.02415  -0.04660 -0.01801 185 PHE A N   
2164 C CA  . PHE A 185 ? 0.33681 0.34205 0.26681 0.02543  -0.04677 -0.02383 185 PHE A CA  
2165 C C   . PHE A 185 ? 0.37151 0.37848 0.28801 0.02913  -0.05458 -0.02710 185 PHE A C   
2166 O O   . PHE A 185 ? 0.39386 0.39722 0.29385 0.03283  -0.05364 -0.02944 185 PHE A O   
2167 C CB  . PHE A 185 ? 0.35999 0.36269 0.29928 0.02056  -0.04727 -0.03075 185 PHE A CB  
2168 C CG  . PHE A 185 ? 0.35250 0.34949 0.28007 0.02183  -0.04831 -0.03809 185 PHE A CG  
2169 C CD1 . PHE A 185 ? 0.42928 0.42094 0.35160 0.02373  -0.04092 -0.03818 185 PHE A CD1 
2170 C CD2 . PHE A 185 ? 0.39800 0.39506 0.32065 0.02126  -0.05688 -0.04553 185 PHE A CD2 
2171 C CE1 . PHE A 185 ? 0.40767 0.39306 0.31838 0.02596  -0.04154 -0.04555 185 PHE A CE1 
2172 C CE2 . PHE A 185 ? 0.39535 0.38545 0.30608 0.02270  -0.05813 -0.05333 185 PHE A CE2 
2173 C CZ  . PHE A 185 ? 0.42467 0.40838 0.32891 0.02542  -0.05008 -0.05327 185 PHE A CZ  
2174 N N   . MET A 186 ? 0.36489 0.37801 0.28773 0.02882  -0.06245 -0.02746 186 MET A N   
2175 C CA  . MET A 186 ? 0.44388 0.46026 0.35530 0.03246  -0.07170 -0.03093 186 MET A CA  
2176 C C   . MET A 186 ? 0.47476 0.48964 0.36778 0.03969  -0.07052 -0.02402 186 MET A C   
2177 O O   . MET A 186 ? 0.44712 0.46363 0.32614 0.04389  -0.07793 -0.02690 186 MET A O   
2178 C CB  . MET A 186 ? 0.38527 0.41087 0.31169 0.03052  -0.08014 -0.03221 186 MET A CB  
2179 C CG  . MET A 186 ? 0.47567 0.50375 0.42143 0.02287  -0.08085 -0.03796 186 MET A CG  
2180 S SD  . MET A 186 ? 0.66380 0.70514 0.62516 0.02046  -0.09257 -0.04253 186 MET A SD  
2181 C CE  . MET A 186 ? 0.55011 0.59752 0.51463 0.02678  -0.09223 -0.03259 186 MET A CE  
2182 N N   . PHE A 187 ? 0.36890 0.29269 0.32883 0.04113  -0.08097 -0.00115 187 PHE A N   
2183 C CA  . PHE A 187 ? 0.36995 0.29256 0.31341 0.04256  -0.06967 -0.00111 187 PHE A CA  
2184 C C   . PHE A 187 ? 0.37181 0.29391 0.30594 0.04700  -0.06349 -0.01235 187 PHE A C   
2185 O O   . PHE A 187 ? 0.38433 0.30858 0.32665 0.04808  -0.06507 -0.01971 187 PHE A O   
2186 C CB  . PHE A 187 ? 0.40495 0.33333 0.35196 0.03862  -0.05686 0.00597  187 PHE A CB  
2187 C CG  . PHE A 187 ? 0.37400 0.30167 0.32479 0.03557  -0.05989 0.01819  187 PHE A CG  
2188 C CD1 . PHE A 187 ? 0.46171 0.38656 0.40125 0.03580  -0.05536 0.02493  187 PHE A CD1 
2189 C CD2 . PHE A 187 ? 0.38087 0.31119 0.34689 0.03294  -0.06682 0.02363  187 PHE A CD2 
2190 C CE1 . PHE A 187 ? 0.38870 0.31300 0.33229 0.03336  -0.05754 0.03690  187 PHE A CE1 
2191 C CE2 . PHE A 187 ? 0.41281 0.34255 0.38246 0.03088  -0.06897 0.03562  187 PHE A CE2 
2192 C CZ  . PHE A 187 ? 0.37344 0.30000 0.33206 0.03103  -0.06430 0.04232  187 PHE A CZ  
2193 N N   . PRO A 188 ? 0.42323 0.34294 0.34042 0.05011  -0.05591 -0.01328 188 PRO A N   
2194 C CA  . PRO A 188 ? 0.45344 0.37332 0.36145 0.05512  -0.04828 -0.02288 188 PRO A CA  
2195 C C   . PRO A 188 ? 0.44848 0.37651 0.36686 0.05300  -0.03578 -0.02454 188 PRO A C   
2196 O O   . PRO A 188 ? 0.37017 0.30312 0.29913 0.04774  -0.03140 -0.01831 188 PRO A O   
2197 C CB  . PRO A 188 ? 0.45923 0.37613 0.34775 0.05845  -0.04189 -0.02032 188 PRO A CB  
2198 C CG  . PRO A 188 ? 0.54121 0.45456 0.42800 0.05576  -0.05052 -0.01114 188 PRO A CG  
2199 C CD  . PRO A 188 ? 0.42211 0.33932 0.32806 0.04971  -0.05373 -0.00487 188 PRO A CD  
2200 N N   A PHE A 189 ? 0.39171 0.32090 0.30744 0.05735  -0.03072 -0.03328 189 PHE A N   
2201 N N   B PHE A 189 ? 0.39180 0.32088 0.30578 0.05756  -0.02956 -0.03286 189 PHE A N   
2202 C CA  A PHE A 189 ? 0.37673 0.31386 0.30394 0.05576  -0.02041 -0.03591 189 PHE A CA  
2203 C CA  B PHE A 189 ? 0.37583 0.31256 0.30171 0.05628  -0.02026 -0.03627 189 PHE A CA  
2204 C C   A PHE A 189 ? 0.34283 0.28576 0.27606 0.05028  -0.00958 -0.02857 189 PHE A C   
2205 C C   B PHE A 189 ? 0.33734 0.28042 0.27015 0.05082  -0.00893 -0.02942 189 PHE A C   
2206 O O   A PHE A 189 ? 0.32098 0.26896 0.26901 0.04521  -0.00999 -0.02668 189 PHE A O   
2207 O O   B PHE A 189 ? 0.33407 0.28287 0.28211 0.04627  -0.00822 -0.02888 189 PHE A O   
2208 C CB  A PHE A 189 ? 0.37131 0.30858 0.28909 0.06227  -0.01181 -0.04315 189 PHE A CB  
2209 C CB  B PHE A 189 ? 0.37429 0.31067 0.29043 0.06308  -0.01264 -0.04390 189 PHE A CB  
2210 C CG  A PHE A 189 ? 0.35008 0.29595 0.27972 0.06090  -0.00017 -0.04493 189 PHE A CG  
2211 C CG  B PHE A 189 ? 0.34752 0.29161 0.27690 0.06258  -0.00453 -0.04788 189 PHE A CG  
2212 C CD1 A PHE A 189 ? 0.30842 0.25885 0.25446 0.05909  -0.00411 -0.04902 189 PHE A CD1 
2213 C CD1 B PHE A 189 ? 0.34119 0.28729 0.28446 0.06187  -0.01202 -0.05266 189 PHE A CD1 
2214 C CD2 A PHE A 189 ? 0.34459 0.29434 0.26993 0.06158  0.01452  -0.04215 189 PHE A CD2 
2215 C CD2 B PHE A 189 ? 0.41113 0.36085 0.34019 0.06289  0.01057  -0.04627 189 PHE A CD2 
2216 C CE1 A PHE A 189 ? 0.37918 0.33801 0.33700 0.05762  0.00585  -0.05043 189 PHE A CE1 
2217 C CE1 B PHE A 189 ? 0.37626 0.33022 0.33248 0.06133  -0.00480 -0.05574 189 PHE A CE1 
2218 C CE2 A PHE A 189 ? 0.36256 0.32038 0.30048 0.06013  0.02477  -0.04357 189 PHE A CE2 
2219 C CE2 B PHE A 189 ? 0.35470 0.31197 0.29737 0.06219  0.01759  -0.04941 189 PHE A CE2 
2220 C CZ  A PHE A 189 ? 0.35082 0.31321 0.30487 0.05799  0.02016  -0.04779 189 PHE A CZ  
2221 C CZ  B PHE A 189 ? 0.40517 0.36467 0.36114 0.06137  0.00973  -0.05416 189 PHE A CZ  
2222 N N   . SER A 190 ? 0.36437 0.30652 0.28613 0.05143  0.00025  -0.02442 190 SER A N   
2223 C CA  . SER A 190 ? 0.36112 0.30840 0.28941 0.04671  0.01219  -0.01879 190 SER A CA  
2224 C C   . SER A 190 ? 0.34796 0.29517 0.28467 0.04061  0.00737  -0.01170 190 SER A C   
2225 O O   . SER A 190 ? 0.34580 0.29780 0.29494 0.03586  0.01109  -0.01085 190 SER A O   
2226 C CB  . SER A 190 ? 0.38520 0.33147 0.30037 0.04941  0.02344  -0.01466 190 SER A CB  
2227 O OG  . SER A 190 ? 0.42492 0.37525 0.34791 0.04454  0.03445  -0.00924 190 SER A OG  
2228 N N   . ILE A 191 ? 0.35759 0.29940 0.28783 0.04093  -0.00146 -0.00658 191 ILE A N   
2229 C CA  . ILE A 191 ? 0.32920 0.27074 0.26675 0.03611  -0.00550 0.00144  191 ILE A CA  
2230 C C   . ILE A 191 ? 0.32360 0.26829 0.27590 0.03359  -0.01403 -0.00105 191 ILE A C   
2231 O O   . ILE A 191 ? 0.32927 0.27740 0.29103 0.02926  -0.01152 0.00265  191 ILE A O   
2232 C CB  . ILE A 191 ? 0.36512 0.30063 0.29331 0.03755  -0.01348 0.00804  191 ILE A CB  
2233 C CG1 . ILE A 191 ? 0.42217 0.35614 0.33717 0.03927  -0.00313 0.01259  191 ILE A CG1 
2234 C CG2 . ILE A 191 ? 0.38894 0.32422 0.32634 0.03350  -0.01956 0.01663  191 ILE A CG2 
2235 C CD1 . ILE A 191 ? 0.50002 0.42843 0.40331 0.04186  -0.01137 0.01745  191 ILE A CD1 
2236 N N   A LYS A 192 ? 0.31100 0.25413 0.26502 0.03651  -0.02468 -0.00680 192 LYS A N   
2237 N N   B LYS A 192 ? 0.31828 0.26189 0.27255 0.03658  -0.02378 -0.00752 192 LYS A N   
2238 C CA  A LYS A 192 ? 0.30910 0.25623 0.27795 0.03491  -0.03204 -0.00976 192 LYS A CA  
2239 C CA  B LYS A 192 ? 0.31110 0.25805 0.28008 0.03485  -0.03263 -0.00942 192 LYS A CA  
2240 C C   A LYS A 192 ? 0.27102 0.22572 0.24940 0.03190  -0.02277 -0.01265 192 LYS A C   
2241 C C   B LYS A 192 ? 0.29281 0.24752 0.27270 0.03206  -0.02511 -0.01300 192 LYS A C   
2242 O O   A LYS A 192 ? 0.24856 0.20736 0.23722 0.02795  -0.02371 -0.00924 192 LYS A O   
2243 O O   B LYS A 192 ? 0.28652 0.24554 0.27844 0.02890  -0.02901 -0.01091 192 LYS A O   
2244 C CB  A LYS A 192 ? 0.30867 0.25280 0.27660 0.03943  -0.04115 -0.01761 192 LYS A CB  
2245 C CB  B LYS A 192 ? 0.30968 0.25300 0.27804 0.03914  -0.04350 -0.01617 192 LYS A CB  
2246 C CG  A LYS A 192 ? 0.29196 0.24056 0.27593 0.03850  -0.04844 -0.02099 192 LYS A CG  
2247 C CG  B LYS A 192 ? 0.29749 0.24543 0.28180 0.03840  -0.05031 -0.02010 192 LYS A CG  
2248 C CD  A LYS A 192 ? 0.33148 0.27519 0.31545 0.04289  -0.05944 -0.02745 192 LYS A CD  
2249 C CD  B LYS A 192 ? 0.33066 0.27370 0.31412 0.04304  -0.06039 -0.02726 192 LYS A CD  
2250 C CE  A LYS A 192 ? 0.38735 0.32832 0.35935 0.04813  -0.05316 -0.03624 192 LYS A CE  
2251 C CE  B LYS A 192 ? 0.38506 0.32647 0.35745 0.04787  -0.05263 -0.03596 192 LYS A CE  
2252 N NZ  A LYS A 192 ? 0.46546 0.40095 0.43737 0.05282  -0.06332 -0.04387 192 LYS A NZ  
2253 N NZ  B LYS A 192 ? 0.49403 0.42742 0.45891 0.05337  -0.06180 -0.04286 192 LYS A NZ  
2254 N N   A ASN A 193 ? 0.28702 0.24373 0.26191 0.03395  -0.01370 -0.01866 193 ASN A N   
2255 N N   B ASN A 193 ? 0.29677 0.25378 0.27321 0.03344  -0.01475 -0.01819 193 ASN A N   
2256 C CA  A ASN A 193 ? 0.33243 0.29669 0.31841 0.03112  -0.00649 -0.02202 193 ASN A CA  
2257 C CA  B ASN A 193 ? 0.32232 0.28697 0.31043 0.03038  -0.00830 -0.02133 193 ASN A CA  
2258 C C   A ASN A 193 ? 0.30591 0.27231 0.29460 0.02590  0.00155  -0.01657 193 ASN A C   
2259 C C   B ASN A 193 ? 0.30887 0.27536 0.29808 0.02559  0.00127  -0.01623 193 ASN A C   
2260 O O   A ASN A 193 ? 0.30662 0.27858 0.30664 0.02197  0.00214  -0.01736 193 ASN A O   
2261 O O   B ASN A 193 ? 0.30028 0.27233 0.30039 0.02156  0.00288  -0.01699 193 ASN A O   
2262 C CB  A ASN A 193 ? 0.30434 0.27042 0.28728 0.03496  0.00133  -0.02864 193 ASN A CB  
2263 C CB  B ASN A 193 ? 0.32613 0.29347 0.31404 0.03399  -0.00235 -0.02899 193 ASN A CB  
2264 C CG  A ASN A 193 ? 0.27927 0.24684 0.26847 0.03832  -0.00607 -0.03561 193 ASN A CG  
2265 C CG  B ASN A 193 ? 0.31008 0.27532 0.29861 0.03875  -0.01205 -0.03498 193 ASN A CG  
2266 O OD1 A ASN A 193 ? 0.24141 0.21539 0.24477 0.03576  -0.00810 -0.03758 193 ASN A OD1 
2267 O OD1 B ASN A 193 ? 0.32690 0.29710 0.32814 0.03815  -0.01629 -0.03855 193 ASN A OD1 
2268 N ND2 A ASN A 193 ? 0.30926 0.27058 0.28797 0.04408  -0.01093 -0.03925 193 ASN A ND2 
2269 N ND2 B ASN A 193 ? 0.27070 0.22838 0.24549 0.04358  -0.01577 -0.03617 193 ASN A ND2 
2270 N N   . GLN A 194 ? 0.28907 0.25087 0.26731 0.02595  0.00747  -0.01108 194 GLN A N   
2271 C CA  . GLN A 194 ? 0.29577 0.25762 0.27561 0.02137  0.01455  -0.00521 194 GLN A CA  
2272 C C   . GLN A 194 ? 0.31109 0.27316 0.29747 0.01847  0.00637  -0.00082 194 GLN A C   
2273 O O   . GLN A 194 ? 0.29748 0.26265 0.29092 0.01447  0.00962  -0.00030 194 GLN A O   
2274 C CB  . GLN A 194 ? 0.31079 0.26717 0.27829 0.02277  0.02067  0.00102  194 GLN A CB  
2275 C CG  . GLN A 194 ? 0.31069 0.26782 0.27241 0.02505  0.03213  -0.00116 194 GLN A CG  
2276 C CD  . GLN A 194 ? 0.40467 0.35688 0.35416 0.02680  0.03694  0.00606  194 GLN A CD  
2277 O OE1 . GLN A 194 ? 0.42131 0.37172 0.37135 0.02363  0.04204  0.01270  194 GLN A OE1 
2278 N NE2 . GLN A 194 ? 0.41300 0.36281 0.35085 0.03219  0.03515  0.00482  194 GLN A NE2 
2279 N N   A MET A 195 ? 0.27022 0.22897 0.25441 0.02055  -0.00418 0.00282  195 MET A N   
2280 N N   B MET A 195 ? 0.27495 0.23398 0.25952 0.02083  -0.00476 0.00196  195 MET A N   
2281 C CA  A MET A 195 ? 0.29357 0.25325 0.28484 0.01842  -0.01110 0.00832  195 MET A CA  
2282 C CA  B MET A 195 ? 0.28111 0.24081 0.27274 0.01929  -0.01353 0.00718  195 MET A CA  
2283 C C   A MET A 195 ? 0.25368 0.22041 0.25737 0.01657  -0.01441 0.00347  195 MET A C   
2284 C C   B MET A 195 ? 0.27885 0.24547 0.28317 0.01781  -0.01790 0.00240  195 MET A C   
2285 O O   A MET A 195 ? 0.20912 0.17864 0.21774 0.01346  -0.01249 0.00586  195 MET A O   
2286 O O   B MET A 195 ? 0.21417 0.18374 0.22469 0.01521  -0.01896 0.00586  195 MET A O   
2287 C CB  A MET A 195 ? 0.31629 0.27187 0.30581 0.02104  -0.02266 0.01333  195 MET A CB  
2288 C CB  B MET A 195 ? 0.25354 0.20878 0.24242 0.02242  -0.02505 0.01059  195 MET A CB  
2289 C CG  A MET A 195 ? 0.25400 0.20323 0.23148 0.02241  -0.01983 0.01950  195 MET A CG  
2290 C CG  B MET A 195 ? 0.36171 0.31125 0.34244 0.02266  -0.02482 0.02006  195 MET A CG  
2291 S SD  A MET A 195 ? 0.27404 0.21818 0.24947 0.02546  -0.03459 0.02390  195 MET A SD  
2292 S SD  B MET A 195 ? 0.29947 0.24532 0.28316 0.02490  -0.04111 0.02556  195 MET A SD  
2293 C CE  A MET A 195 ? 0.30687 0.24588 0.27099 0.02545  -0.02899 0.03382  195 MET A CE  
2294 C CE  B MET A 195 ? 0.40040 0.34101 0.37464 0.02459  -0.03721 0.03705  195 MET A CE  
2295 N N   A TYR A 196 ? 0.25955 0.22925 0.26800 0.01873  -0.01923 -0.00349 196 TYR A N   
2296 N N   B TYR A 196 ? 0.23192 0.20121 0.24005 0.02000  -0.02113 -0.00509 196 TYR A N   
2297 C CA  A TYR A 196 ? 0.22307 0.20039 0.24421 0.01720  -0.02256 -0.00777 196 TYR A CA  
2298 C CA  B TYR A 196 ? 0.23122 0.20799 0.25232 0.01866  -0.02491 -0.00924 196 TYR A CA  
2299 C C   A TYR A 196 ? 0.26747 0.24941 0.29194 0.01316  -0.01284 -0.01045 196 TYR A C   
2300 C C   B TYR A 196 ? 0.30247 0.28425 0.32759 0.01438  -0.01602 -0.01078 196 TYR A C   
2301 O O   A TYR A 196 ? 0.29344 0.28123 0.32681 0.01056  -0.01521 -0.01102 196 TYR A O   
2302 O O   B TYR A 196 ? 0.25709 0.24295 0.28892 0.01174  -0.01856 -0.00860 196 TYR A O   
2303 C CB  A TYR A 196 ? 0.24810 0.22729 0.27324 0.02057  -0.02697 -0.01509 196 TYR A CB  
2304 C CB  B TYR A 196 ? 0.23872 0.21723 0.26310 0.02201  -0.02782 -0.01707 196 TYR A CB  
2305 C CG  A TYR A 196 ? 0.25289 0.22805 0.27836 0.02412  -0.03878 -0.01396 196 TYR A CG  
2306 C CG  B TYR A 196 ? 0.33027 0.30468 0.35498 0.02573  -0.03957 -0.01686 196 TYR A CG  
2307 C CD1 A TYR A 196 ? 0.26469 0.24018 0.29653 0.02339  -0.04780 -0.00735 196 TYR A CD1 
2308 C CD1 B TYR A 196 ? 0.23506 0.20666 0.26115 0.02535  -0.04796 -0.00935 196 TYR A CD1 
2309 C CD2 A TYR A 196 ? 0.29782 0.26854 0.31744 0.02848  -0.04099 -0.01943 196 TYR A CD2 
2310 C CD2 B TYR A 196 ? 0.30519 0.27814 0.32936 0.02983  -0.04226 -0.02402 196 TYR A CD2 
2311 C CE1 A TYR A 196 ? 0.25510 0.22696 0.28977 0.02622  -0.05921 -0.00597 196 TYR A CE1 
2312 C CE1 B TYR A 196 ? 0.29133 0.25888 0.31957 0.02835  -0.05943 -0.00903 196 TYR A CE1 
2313 C CE2 A TYR A 196 ? 0.28668 0.25276 0.30721 0.03140  -0.05270 -0.01910 196 TYR A CE2 
2314 C CE2 B TYR A 196 ? 0.32813 0.29608 0.35277 0.03313  -0.05361 -0.02463 196 TYR A CE2 
2315 C CZ  A TYR A 196 ? 0.29631 0.26302 0.32534 0.02995  -0.06204 -0.01218 196 TYR A CZ  
2316 C CZ  B TYR A 196 ? 0.27340 0.23871 0.30076 0.03206  -0.06257 -0.01712 196 TYR A CZ  
2317 O OH  A TYR A 196 ? 0.31647 0.27846 0.34866 0.03248  -0.07428 -0.01131 196 TYR A OH  
2318 O OH  B TYR A 196 ? 0.25835 0.21841 0.28802 0.03487  -0.07461 -0.01743 196 TYR A OH  
2319 N N   A ASN A 197 ? 0.22871 0.20835 0.24670 0.01271  -0.00225 -0.01212 197 ASN A N   
2320 N N   B ASN A 197 ? 0.26667 0.24802 0.28762 0.01383  -0.00561 -0.01430 197 ASN A N   
2321 C CA  A ASN A 197 ? 0.22888 0.21210 0.25128 0.00848  0.00673  -0.01445 197 ASN A CA  
2322 C CA  B ASN A 197 ? 0.23501 0.22078 0.26136 0.00947  0.00259  -0.01662 197 ASN A CA  
2323 C C   A ASN A 197 ? 0.24023 0.22166 0.26175 0.00497  0.00775  -0.00935 197 ASN A C   
2324 C C   B ASN A 197 ? 0.20006 0.18420 0.22533 0.00586  0.00371  -0.01139 197 ASN A C   
2325 O O   A ASN A 197 ? 0.22860 0.21447 0.25700 0.00136  0.00852  -0.01173 197 ASN A O   
2326 O O   B ASN A 197 ? 0.28557 0.27468 0.31822 0.00256  0.00284  -0.01318 197 ASN A O   
2327 C CB  A ASN A 197 ? 0.24851 0.22926 0.26500 0.00907  0.01823  -0.01570 197 ASN A CB  
2328 C CB  B ASN A 197 ? 0.25582 0.23997 0.27735 0.00980  0.01424  -0.01878 197 ASN A CB  
2329 C CG  A ASN A 197 ? 0.22723 0.21156 0.24645 0.01236  0.01983  -0.02183 197 ASN A CG  
2330 C CG  B ASN A 197 ? 0.26506 0.25119 0.28710 0.01416  0.01454  -0.02421 197 ASN A CG  
2331 O OD1 A ASN A 197 ? 0.23058 0.21953 0.25753 0.01358  0.01291  -0.02594 197 ASN A OD1 
2332 O OD1 B ASN A 197 ? 0.28866 0.27888 0.31808 0.01571  0.00728  -0.02802 197 ASN A OD1 
2333 N ND2 A ASN A 197 ? 0.24086 0.22330 0.25410 0.01420  0.02958  -0.02198 197 ASN A ND2 
2334 N ND2 B ASN A 197 ? 0.32127 0.30452 0.33537 0.01659  0.02347  -0.02422 197 ASN A ND2 
2335 N N   A ILE A 198 ? 0.26419 0.23904 0.27700 0.00624  0.00757  -0.00222 198 ILE A N   
2336 N N   B ILE A 198 ? 0.25503 0.23218 0.27080 0.00682  0.00521  -0.00470 198 ILE A N   
2337 C CA  A ILE A 198 ? 0.26307 0.23543 0.27415 0.00384  0.00927  0.00330  198 ILE A CA  
2338 C CA  B ILE A 198 ? 0.26175 0.23625 0.27531 0.00407  0.00815  0.00057  198 ILE A CA  
2339 C C   A ILE A 198 ? 0.26316 0.23873 0.27950 0.00458  -0.00108 0.00644  198 ILE A C   
2340 C C   B ILE A 198 ? 0.27835 0.25590 0.29702 0.00434  -0.00142 0.00376  198 ILE A C   
2341 O O   A ILE A 198 ? 0.26927 0.24583 0.28686 0.00254  -0.00033 0.00826  198 ILE A O   
2342 O O   B ILE A 198 ? 0.25945 0.23955 0.28116 0.00169  -0.00053 0.00340  198 ILE A O   
2343 C CB  A ILE A 198 ? 0.32403 0.28856 0.32478 0.00498  0.01475  0.01066  198 ILE A CB  
2344 C CB  B ILE A 198 ? 0.25154 0.21816 0.25446 0.00535  0.01324  0.00774  198 ILE A CB  
2345 C CG1 A ILE A 198 ? 0.27696 0.23950 0.27330 0.00488  0.02502  0.00810  198 ILE A CG1 
2346 C CG1 B ILE A 198 ? 0.32767 0.29225 0.32676 0.00431  0.02507  0.00541  198 ILE A CG1 
2347 C CG2 A ILE A 198 ? 0.28710 0.24841 0.28593 0.00274  0.01878  0.01589  198 ILE A CG2 
2348 C CG2 B ILE A 198 ? 0.28232 0.24583 0.28334 0.00393  0.01385  0.01467  198 ILE A CG2 
2349 C CD1 A ILE A 198 ? 0.26002 0.22546 0.26244 0.00073  0.03381  0.00230  198 ILE A CD1 
2350 C CD1 B ILE A 198 ? 0.46054 0.41836 0.44965 0.00581  0.03084  0.01247  198 ILE A CD1 
2351 N N   . LEU A 199 ? 0.25792 0.23507 0.27755 0.00775  -0.01077 0.00717  199 LEU A N   
2352 C CA  . LEU A 199 ? 0.27888 0.25995 0.30554 0.00871  -0.02036 0.01107  199 LEU A CA  
2353 C C   . LEU A 199 ? 0.24439 0.23381 0.28010 0.00651  -0.02189 0.00555  199 LEU A C   
2354 O O   . LEU A 199 ? 0.29442 0.28704 0.33299 0.00600  -0.02484 0.00903  199 LEU A O   
2355 C CB  . LEU A 199 ? 0.26509 0.24531 0.29479 0.01239  -0.03063 0.01319  199 LEU A CB  
2356 C CG  . LEU A 199 ? 0.27662 0.24952 0.29949 0.01458  -0.03308 0.02126  199 LEU A CG  
2357 C CD1 . LEU A 199 ? 0.28057 0.25173 0.30604 0.01779  -0.04320 0.02004  199 LEU A CD1 
2358 C CD2 . LEU A 199 ? 0.29026 0.26303 0.31513 0.01472  -0.03552 0.03142  199 LEU A CD2 
2359 N N   A ASP A 200 ? 0.25688 0.25025 0.29700 0.00542  -0.01954 -0.00264 200 ASP A N   
2360 N N   B ASP A 200 ? 0.25719 0.25062 0.29741 0.00544  -0.01967 -0.00264 200 ASP A N   
2361 C CA  A ASP A 200 ? 0.28524 0.28725 0.33488 0.00297  -0.02113 -0.00775 200 ASP A CA  
2362 C CA  B ASP A 200 ? 0.28507 0.28715 0.33479 0.00297  -0.02120 -0.00776 200 ASP A CA  
2363 C C   A ASP A 200 ? 0.26784 0.26980 0.31461 -0.00079 -0.01585 -0.00745 200 ASP A C   
2364 C C   B ASP A 200 ? 0.26924 0.27130 0.31614 -0.00087 -0.01571 -0.00769 200 ASP A C   
2365 O O   A ASP A 200 ? 0.26849 0.27664 0.32048 -0.00199 -0.02013 -0.00799 200 ASP A O   
2366 O O   B ASP A 200 ? 0.27187 0.28041 0.32441 -0.00230 -0.01971 -0.00886 200 ASP A O   
2367 C CB  A ASP A 200 ? 0.28446 0.29018 0.33936 0.00230  -0.01764 -0.01565 200 ASP A CB  
2368 C CB  B ASP A 200 ? 0.28362 0.28952 0.33882 0.00242  -0.01800 -0.01567 200 ASP A CB  
2369 C CG  A ASP A 200 ? 0.25158 0.25817 0.31037 0.00645  -0.02379 -0.01746 200 ASP A CG  
2370 C CG  B ASP A 200 ? 0.28573 0.29559 0.34870 0.00593  -0.02605 -0.01781 200 ASP A CG  
2371 O OD1 A ASP A 200 ? 0.28104 0.28733 0.34215 0.00914  -0.03279 -0.01339 200 ASP A OD1 
2372 O OD1 B ASP A 200 ? 0.23985 0.24927 0.30478 0.00856  -0.03466 -0.01333 200 ASP A OD1 
2373 O OD2 A ASP A 200 ? 0.31007 0.31754 0.37021 0.00729  -0.01953 -0.02295 200 ASP A OD2 
2374 O OD2 B ASP A 200 ? 0.30064 0.31390 0.36861 0.00626  -0.02346 -0.02381 200 ASP A OD2 
2375 N N   . ILE A 201 ? 0.25839 0.25311 0.29650 -0.00242 -0.00666 -0.00650 201 ILE A N   
2376 C CA  . ILE A 201 ? 0.28099 0.27358 0.31539 -0.00578 -0.00135 -0.00654 201 ILE A CA  
2377 C C   . ILE A 201 ? 0.33034 0.32284 0.36196 -0.00387 -0.00667 -0.00001 201 ILE A C   
2378 O O   . ILE A 201 ? 0.31569 0.31140 0.34805 -0.00560 -0.00780 -0.00174 201 ILE A O   
2379 C CB  . ILE A 201 ? 0.29929 0.28300 0.32521 -0.00703 0.00942  -0.00499 201 ILE A CB  
2380 C CG1 . ILE A 201 ? 0.28744 0.27199 0.31667 -0.00861 0.01586  -0.01066 201 ILE A CG1 
2381 C CG2 . ILE A 201 ? 0.32733 0.30713 0.34886 -0.01007 0.01453  -0.00490 201 ILE A CG2 
2382 C CD1 . ILE A 201 ? 0.33193 0.30824 0.35330 -0.00883 0.02645  -0.00758 201 ILE A CD1 
2383 N N   . VAL A 202 ? 0.27921 0.26801 0.30747 -0.00008 -0.00993 0.00790  202 VAL A N   
2384 C CA  . VAL A 202 ? 0.30166 0.29018 0.32803 0.00257  -0.01423 0.01623  202 VAL A CA  
2385 C C   . VAL A 202 ? 0.26777 0.26577 0.30370 0.00420  -0.02421 0.01640  202 VAL A C   
2386 O O   . VAL A 202 ? 0.32164 0.32319 0.35729 0.00459  -0.02595 0.01840  202 VAL A O   
2387 C CB  . VAL A 202 ? 0.34696 0.32902 0.36893 0.00580  -0.01481 0.02534  202 VAL A CB  
2388 C CG1 . VAL A 202 ? 0.38523 0.36716 0.40631 0.00877  -0.01799 0.03524  202 VAL A CG1 
2389 C CG2 . VAL A 202 ? 0.35779 0.33145 0.37086 0.00441  -0.00478 0.02576  202 VAL A CG2 
2390 N N   . SER A 203 ? 0.22059 0.22278 0.26488 0.00553  -0.03074 0.01436  203 SER A N   
2391 C CA  . SER A 203 ? 0.21565 0.22684 0.27068 0.00749  -0.04036 0.01568  203 SER A CA  
2392 C C   . SER A 203 ? 0.27288 0.29276 0.33318 0.00477  -0.04092 0.00886  203 SER A C   
2393 O O   . SER A 203 ? 0.27313 0.30029 0.33839 0.00618  -0.04666 0.01191  203 SER A O   
2394 C CB  . SER A 203 ? 0.26723 0.27920 0.32991 0.00980  -0.04701 0.01499  203 SER A CB  
2395 O OG  . SER A 203 ? 0.26425 0.27865 0.33014 0.00785  -0.04459 0.00553  203 SER A OG  
2396 N N   A LYS A 204 ? 0.27704 0.29696 0.33714 0.00102  -0.03533 0.00027  204 LYS A N   
2397 N N   B LYS A 204 ? 0.28011 0.29991 0.33995 0.00097  -0.03517 0.00031  204 LYS A N   
2398 C CA  A LYS A 204 ? 0.27883 0.30721 0.34495 -0.00212 -0.03642 -0.00608 204 LYS A CA  
2399 C CA  B LYS A 204 ? 0.28101 0.30972 0.34810 -0.00203 -0.03670 -0.00642 204 LYS A CA  
2400 C C   A LYS A 204 ? 0.22109 0.24586 0.27840 -0.00540 -0.03030 -0.00812 204 LYS A C   
2401 C C   B LYS A 204 ? 0.26139 0.28811 0.32167 -0.00601 -0.03080 -0.01008 204 LYS A C   
2402 O O   A LYS A 204 ? 0.25913 0.28777 0.31471 -0.00511 -0.03346 -0.00660 204 LYS A O   
2403 O O   B LYS A 204 ? 0.23618 0.26955 0.29852 -0.00717 -0.03450 -0.01168 204 LYS A O   
2404 C CB  A LYS A 204 ? 0.26309 0.29543 0.33767 -0.00414 -0.03516 -0.01382 204 LYS A CB  
2405 C CB  B LYS A 204 ? 0.29235 0.32410 0.36753 -0.00333 -0.03562 -0.01342 204 LYS A CB  
2406 C CG  A LYS A 204 ? 0.26740 0.30490 0.35236 -0.00063 -0.04259 -0.01310 204 LYS A CG  
2407 C CG  B LYS A 204 ? 0.24169 0.27501 0.32381 0.00078  -0.04200 -0.01149 204 LYS A CG  
2408 C CD  A LYS A 204 ? 0.23767 0.27650 0.32829 -0.00144 -0.03929 -0.01995 204 LYS A CD  
2409 C CD  B LYS A 204 ? 0.23733 0.27198 0.32498 0.00044  -0.03925 -0.01832 204 LYS A CD  
2410 C CE  A LYS A 204 ? 0.28379 0.32464 0.38224 0.00280  -0.04577 -0.01947 204 LYS A CE  
2411 C CE  B LYS A 204 ? 0.28143 0.32300 0.38143 0.00349  -0.04747 -0.01892 204 LYS A CE  
2412 N NZ  A LYS A 204 ? 0.25784 0.28910 0.34877 0.00639  -0.04636 -0.01608 204 LYS A NZ  
2413 N NZ  B LYS A 204 ? 0.23478 0.27014 0.33318 0.00798  -0.05172 -0.01597 204 LYS A NZ  
2414 N N   A ASN A 205 ? 0.24896 0.26596 0.30032 -0.00818 -0.02141 -0.01143 205 ASN A N   
2415 N N   B ASN A 205 ? 0.25630 0.27399 0.30869 -0.00818 -0.02181 -0.01178 205 ASN A N   
2416 C CA  A ASN A 205 ? 0.29104 0.30543 0.33788 -0.01256 -0.01575 -0.01646 205 ASN A CA  
2417 C CA  B ASN A 205 ? 0.29013 0.30460 0.33708 -0.01232 -0.01599 -0.01614 205 ASN A CA  
2418 C C   A ASN A 205 ? 0.29937 0.30705 0.33442 -0.01119 -0.01333 -0.01159 205 ASN A C   
2419 C C   B ASN A 205 ? 0.29048 0.30036 0.32701 -0.01043 -0.01565 -0.01083 205 ASN A C   
2420 O O   A ASN A 205 ? 0.27558 0.28278 0.30670 -0.01380 -0.01205 -0.01566 205 ASN A O   
2421 O O   B ASN A 205 ? 0.25002 0.26292 0.28456 -0.01193 -0.01760 -0.01380 205 ASN A O   
2422 C CB  A ASN A 205 ? 0.27318 0.28270 0.32076 -0.01592 -0.00705 -0.02139 205 ASN A CB  
2423 C CB  B ASN A 205 ? 0.28581 0.29235 0.32956 -0.01502 -0.00603 -0.01909 205 ASN A CB  
2424 C CG  A ASN A 205 ? 0.31526 0.33159 0.37398 -0.01599 -0.00900 -0.02528 205 ASN A CG  
2425 C CG  B ASN A 205 ? 0.25638 0.26778 0.31005 -0.01648 -0.00512 -0.02432 205 ASN A CG  
2426 O OD1 A ASN A 205 ? 0.38420 0.39729 0.44211 -0.01364 -0.00633 -0.02370 205 ASN A OD1 
2427 O OD1 B ASN A 205 ? 0.31647 0.33733 0.38018 -0.01669 -0.01139 -0.02738 205 ASN A OD1 
2428 N ND2 A ASN A 205 ? 0.33955 0.36556 0.40845 -0.01831 -0.01385 -0.03022 205 ASN A ND2 
2429 N ND2 B ASN A 205 ? 0.17985 0.18524 0.23100 -0.01698 0.00304  -0.02475 205 ASN A ND2 
2430 N N   . ILE A 206 ? 0.28533 0.28787 0.31479 -0.00691 -0.01307 -0.00285 206 ILE A N   
2431 C CA  . ILE A 206 ? 0.28553 0.28292 0.30484 -0.00454 -0.01107 0.00307  206 ILE A CA  
2432 C C   . ILE A 206 ? 0.31512 0.32119 0.33663 -0.00186 -0.01920 0.00549  206 ILE A C   
2433 O O   . ILE A 206 ? 0.31207 0.31683 0.32566 -0.00138 -0.01795 0.00531  206 ILE A O   
2434 C CB  . ILE A 206 ? 0.37372 0.36352 0.38781 -0.00082 -0.00805 0.01280  206 ILE A CB  
2435 C CG1 . ILE A 206 ? 0.43786 0.41792 0.44601 -0.00344 0.00216  0.01089  206 ILE A CG1 
2436 C CG2 . ILE A 206 ? 0.34914 0.33735 0.35676 0.00374  -0.00908 0.02207  206 ILE A CG2 
2437 C CD1 . ILE A 206 ? 0.48943 0.46246 0.49278 -0.00022 0.00526  0.02038  206 ILE A CD1 
2438 N N   A TYR A 207 ? 0.34173 0.35699 0.37407 0.00002  -0.02752 0.00723  207 TYR A N   
2439 N N   B TYR A 207 ? 0.33738 0.35224 0.36934 0.00043  -0.02753 0.00813  207 TYR A N   
2440 C CA  A TYR A 207 ? 0.33489 0.36021 0.37147 0.00254  -0.03541 0.00968  207 TYR A CA  
2441 C CA  B TYR A 207 ? 0.33387 0.35859 0.36984 0.00312  -0.03533 0.01094  207 TYR A CA  
2442 C C   A TYR A 207 ? 0.31870 0.34883 0.35387 -0.00122 -0.03598 0.00098  207 TYR A C   
2443 C C   B TYR A 207 ? 0.30973 0.34010 0.34550 -0.00068 -0.03643 0.00200  207 TYR A C   
2444 O O   A TYR A 207 ? 0.33786 0.36953 0.36572 0.00056  -0.03716 0.00249  207 TYR A O   
2445 O O   B TYR A 207 ? 0.34021 0.37599 0.37284 0.00138  -0.04025 0.00374  207 TYR A O   
2446 C CB  A TYR A 207 ? 0.37469 0.40889 0.42542 0.00441  -0.04373 0.01170  207 TYR A CB  
2447 C CB  B TYR A 207 ? 0.41792 0.45104 0.46757 0.00562  -0.04382 0.01439  207 TYR A CB  
2448 C CG  A TYR A 207 ? 0.35159 0.39567 0.40753 0.00848  -0.05158 0.01803  207 TYR A CG  
2449 C CG  B TYR A 207 ? 0.49295 0.53417 0.54683 0.01060  -0.05107 0.02301  207 TYR A CG  
2450 C CD1 A TYR A 207 ? 0.50933 0.55180 0.56306 0.01377  -0.05298 0.02942  207 TYR A CD1 
2451 C CD1 B TYR A 207 ? 0.49858 0.54816 0.55164 0.01083  -0.05422 0.02127  207 TYR A CD1 
2452 C CD2 A TYR A 207 ? 0.34059 0.39609 0.40421 0.00727  -0.05727 0.01357  207 TYR A CD2 
2453 C CD2 B TYR A 207 ? 0.48405 0.52499 0.54344 0.01517  -0.05507 0.03326  207 TYR A CD2 
2454 C CE1 A TYR A 207 ? 0.50316 0.55522 0.56243 0.01806  -0.05952 0.03642  207 TYR A CE1 
2455 C CE1 B TYR A 207 ? 0.42842 0.48622 0.48536 0.01598  -0.06021 0.03000  207 TYR A CE1 
2456 C CE2 A TYR A 207 ? 0.34875 0.41406 0.41734 0.01148  -0.06414 0.02030  207 TYR A CE2 
2457 C CE2 B TYR A 207 ? 0.34629 0.39526 0.41142 0.01999  -0.06127 0.04228  207 TYR A CE2 
2458 C CZ  A TYR A 207 ? 0.33709 0.40062 0.40342 0.01702  -0.06500 0.03181  207 TYR A CZ  
2459 C CZ  B TYR A 207 ? 0.40231 0.45994 0.46595 0.02062  -0.06340 0.04083  207 TYR A CZ  
2460 O OH  A TYR A 207 ? 0.43355 0.50736 0.50545 0.02172  -0.07118 0.03961  207 TYR A OH  
2461 O OH  B TYR A 207 ? 0.30614 0.37254 0.37532 0.02596  -0.06893 0.05051  207 TYR A OH  
2462 N N   A SER A 208 ? 0.30462 0.33728 0.34673 -0.00624 -0.03531 -0.00801 208 SER A N   
2463 N N   B SER A 208 ? 0.33781 0.36723 0.37697 -0.00608 -0.03322 -0.00723 208 SER A N   
2464 C CA  A SER A 208 ? 0.34356 0.38138 0.38655 -0.01054 -0.03694 -0.01641 208 SER A CA  
2465 C CA  B SER A 208 ? 0.33410 0.36867 0.37446 -0.01045 -0.03483 -0.01585 208 SER A CA  
2466 C C   A SER A 208 ? 0.40325 0.43230 0.43197 -0.01189 -0.03152 -0.01897 208 SER A C   
2467 C C   B SER A 208 ? 0.39261 0.41779 0.41948 -0.01256 -0.02858 -0.01940 208 SER A C   
2468 O O   A SER A 208 ? 0.31080 0.34382 0.33456 -0.01169 -0.03532 -0.02109 208 SER A O   
2469 O O   B SER A 208 ? 0.34025 0.36883 0.36317 -0.01387 -0.03175 -0.02377 208 SER A O   
2470 C CB  A SER A 208 ? 0.37751 0.41744 0.43057 -0.01587 -0.03504 -0.02460 208 SER A CB  
2471 C CB  B SER A 208 ? 0.37970 0.41849 0.43203 -0.01519 -0.03454 -0.02340 208 SER A CB  
2472 O OG  A SER A 208 ? 0.27371 0.32241 0.34000 -0.01449 -0.04033 -0.02356 208 SER A OG  
2473 O OG  B SER A 208 ? 0.55291 0.58266 0.60136 -0.01957 -0.02593 -0.02876 208 SER A OG  
2474 N N   A ILE A 209 ? 0.31791 0.33479 0.33951 -0.01299 -0.02258 -0.01882 209 ILE A N   
2475 N N   B ILE A 209 ? 0.30258 0.31571 0.32205 -0.01278 -0.01987 -0.01772 209 ILE A N   
2476 C CA  A ILE A 209 ? 0.30716 0.31405 0.31543 -0.01406 -0.01653 -0.02132 209 ILE A CA  
2477 C CA  B ILE A 209 ? 0.35587 0.35869 0.36198 -0.01360 -0.01348 -0.01964 209 ILE A CA  
2478 C C   A ILE A 209 ? 0.32493 0.33128 0.32238 -0.00799 -0.01844 -0.01403 209 ILE A C   
2479 C C   B ILE A 209 ? 0.32245 0.32617 0.31863 -0.00799 -0.01649 -0.01346 209 ILE A C   
2480 O O   A ILE A 209 ? 0.29403 0.29870 0.28187 -0.00803 -0.01875 -0.01786 209 ILE A O   
2481 O O   B ILE A 209 ? 0.31725 0.31771 0.30330 -0.00837 -0.01563 -0.01761 209 ILE A O   
2482 C CB  A ILE A 209 ? 0.43682 0.43131 0.44118 -0.01565 -0.00619 -0.02070 209 ILE A CB  
2483 C CB  B ILE A 209 ? 0.25912 0.24966 0.26014 -0.01356 -0.00357 -0.01627 209 ILE A CB  
2484 C CG1 A ILE A 209 ? 0.35004 0.34569 0.36484 -0.02158 -0.00359 -0.02836 209 ILE A CG1 
2485 C CG1 B ILE A 209 ? 0.39897 0.38859 0.40885 -0.01864 0.00058  -0.02216 209 ILE A CG1 
2486 C CG2 A ILE A 209 ? 0.35867 0.34167 0.34903 -0.01555 0.00055  -0.02165 209 ILE A CG2 
2487 C CG2 B ILE A 209 ? 0.37172 0.35111 0.35912 -0.01339 0.00324  -0.01706 209 ILE A CG2 
2488 C CD1 A ILE A 209 ? 0.52234 0.50982 0.53698 -0.02175 0.00503  -0.02538 209 ILE A CD1 
2489 C CD1 B ILE A 209 ? 0.30523 0.28482 0.31128 -0.01785 0.00964  -0.01744 209 ILE A CD1 
2490 N N   . PHE A 210 ? 0.30623 0.31431 0.30547 -0.00246 -0.02010 -0.00333 210 PHE A N   
2491 C CA  . PHE A 210 ? 0.35905 0.36836 0.35047 0.00400  -0.02198 0.00531  210 PHE A CA  
2492 C C   . PHE A 210 ? 0.34156 0.36166 0.33302 0.00479  -0.02968 0.00207  210 PHE A C   
2493 O O   . PHE A 210 ? 0.31480 0.33252 0.29362 0.00713  -0.02857 0.00140  210 PHE A O   
2494 C CB  . PHE A 210 ? 0.29818 0.31054 0.29727 0.00883  -0.02487 0.01701  210 PHE A CB  
2495 C CG  . PHE A 210 ? 0.29474 0.31238 0.29143 0.01584  -0.02870 0.02750  210 PHE A CG  
2496 C CD1 . PHE A 210 ? 0.34314 0.35321 0.32638 0.02024  -0.02262 0.03355  210 PHE A CD1 
2497 C CD2 . PHE A 210 ? 0.35628 0.38658 0.36477 0.01849  -0.03783 0.03198  210 PHE A CD2 
2498 C CE1 . PHE A 210 ? 0.40292 0.41854 0.38423 0.02739  -0.02545 0.04409  210 PHE A CE1 
2499 C CE2 . PHE A 210 ? 0.32107 0.35707 0.32854 0.02535  -0.04094 0.04271  210 PHE A CE2 
2500 C CZ  . PHE A 210 ? 0.35428 0.38306 0.34800 0.02992  -0.03457 0.04897  210 PHE A CZ  
2501 N N   . ILE A 211 ? 0.29904 0.33119 0.30430 0.00322  -0.03752 0.00011  211 ILE A N   
2502 C CA  . ILE A 211 ? 0.25016 0.29412 0.25732 0.00351  -0.04538 -0.00289 211 ILE A CA  
2503 C C   . ILE A 211 ? 0.24944 0.28961 0.24726 -0.00133 -0.04387 -0.01420 211 ILE A C   
2504 O O   . ILE A 211 ? 0.27630 0.32028 0.26528 0.00078  -0.04745 -0.01550 211 ILE A O   
2505 C CB  . ILE A 211 ? 0.27904 0.33546 0.30443 0.00158  -0.05279 -0.00409 211 ILE A CB  
2506 C CG1 . ILE A 211 ? 0.33594 0.39624 0.37075 0.00689  -0.05585 0.00707  211 ILE A CG1 
2507 C CG2 . ILE A 211 ? 0.28583 0.35457 0.31395 0.00072  -0.06047 -0.00820 211 ILE A CG2 
2508 C CD1 . ILE A 211 ? 0.30384 0.36979 0.33495 0.01415  -0.05943 0.01775  211 ILE A CD1 
2509 N N   . PHE A 212 ? 0.28273 0.31546 0.28275 -0.00782 -0.03883 -0.02256 212 PHE A N   
2510 C CA  . PHE A 212 ? 0.32649 0.35447 0.31925 -0.01301 -0.03766 -0.03352 212 PHE A CA  
2511 C C   . PHE A 212 ? 0.31648 0.33372 0.28975 -0.00932 -0.03283 -0.03258 212 PHE A C   
2512 O O   . PHE A 212 ? 0.33377 0.35167 0.29745 -0.00963 -0.03622 -0.03849 212 PHE A O   
2513 C CB  . PHE A 212 ? 0.35795 0.37876 0.35748 -0.02002 -0.03169 -0.04080 212 PHE A CB  
2514 C CG  . PHE A 212 ? 0.32237 0.33609 0.31513 -0.02548 -0.02988 -0.05148 212 PHE A CG  
2515 C CD1 . PHE A 212 ? 0.33459 0.35680 0.33484 -0.03085 -0.03716 -0.06017 212 PHE A CD1 
2516 C CD2 . PHE A 212 ? 0.38808 0.38666 0.36754 -0.02524 -0.02144 -0.05278 212 PHE A CD2 
2517 C CE1 . PHE A 212 ? 0.34491 0.36017 0.33965 -0.03629 -0.03667 -0.07049 212 PHE A CE1 
2518 C CE2 . PHE A 212 ? 0.45045 0.44141 0.42421 -0.03036 -0.02018 -0.06319 212 PHE A CE2 
2519 C CZ  . PHE A 212 ? 0.39292 0.39199 0.37421 -0.03606 -0.02818 -0.07235 212 PHE A CZ  
2520 N N   . ILE A 213 ? 0.30147 0.30854 0.26838 -0.00554 -0.02486 -0.02509 213 ILE A N   
2521 C CA  . ILE A 213 ? 0.36717 0.36328 0.31582 -0.00131 -0.01898 -0.02329 213 ILE A CA  
2522 C C   . ILE A 213 ? 0.33550 0.33950 0.27596 0.00602  -0.02446 -0.01715 213 ILE A C   
2523 O O   . ILE A 213 ? 0.34271 0.34228 0.26760 0.00826  -0.02381 -0.02102 213 ILE A O   
2524 C CB  . ILE A 213 ? 0.36972 0.35443 0.31556 0.00122  -0.00922 -0.01523 213 ILE A CB  
2525 C CG1 . ILE A 213 ? 0.37377 0.34975 0.32477 -0.00587 -0.00279 -0.02239 213 ILE A CG1 
2526 C CG2 . ILE A 213 ? 0.39244 0.36683 0.32000 0.00731  -0.00281 -0.01082 213 ILE A CG2 
2527 C CD1 . ILE A 213 ? 0.42050 0.38759 0.37166 -0.00400 0.00590  -0.01409 213 ILE A CD1 
2528 N N   . VAL A 214 ? 0.33189 0.34766 0.28275 0.01017  -0.02996 -0.00746 214 VAL A N   
2529 C CA  . VAL A 214 ? 0.35645 0.38185 0.30195 0.01718  -0.03552 -0.00093 214 VAL A CA  
2530 C C   . VAL A 214 ? 0.37094 0.40370 0.31220 0.01444  -0.04277 -0.01115 214 VAL A C   
2531 O O   . VAL A 214 ? 0.34288 0.37533 0.26868 0.01906  -0.04352 -0.01147 214 VAL A O   
2532 C CB  . VAL A 214 ? 0.33256 0.36985 0.29314 0.02143  -0.04077 0.01106  214 VAL A CB  
2533 C CG1 . VAL A 214 ? 0.30334 0.35211 0.25969 0.02859  -0.04660 0.01783  214 VAL A CG1 
2534 C CG2 . VAL A 214 ? 0.32271 0.35184 0.28512 0.02494  -0.03414 0.02207  214 VAL A CG2 
2535 N N   . ILE A 215 ? 0.27084 0.31012 0.22523 0.00705  -0.04811 -0.01968 215 ILE A N   
2536 C CA  . ILE A 215 ? 0.29271 0.33963 0.24477 0.00375  -0.05582 -0.02919 215 ILE A CA  
2537 C C   . ILE A 215 ? 0.29024 0.32413 0.22384 0.00169  -0.05198 -0.03925 215 ILE A C   
2538 O O   . ILE A 215 ? 0.32693 0.36314 0.24691 0.00456  -0.05617 -0.04245 215 ILE A O   
2539 C CB  . ILE A 215 ? 0.37819 0.43347 0.34963 -0.00419 -0.06103 -0.03589 215 ILE A CB  
2540 C CG1 . ILE A 215 ? 0.31379 0.38371 0.30173 -0.00104 -0.06681 -0.02672 215 ILE A CG1 
2541 C CG2 . ILE A 215 ? 0.31340 0.37354 0.28210 -0.00934 -0.06805 -0.04739 215 ILE A CG2 
2542 C CD1 . ILE A 215 ? 0.34383 0.42114 0.35159 -0.00769 -0.07035 -0.03174 215 ILE A CD1 
2543 N N   A LEU A 216 ? 0.33811 0.35797 0.27114 -0.00326 -0.04405 -0.04460 216 LEU A N   
2544 N N   B LEU A 216 ? 0.34057 0.36036 0.27349 -0.00320 -0.04399 -0.04453 216 LEU A N   
2545 C CA  A LEU A 216 ? 0.34906 0.35507 0.26628 -0.00579 -0.04012 -0.05482 216 LEU A CA  
2546 C CA  B LEU A 216 ? 0.35050 0.35647 0.26773 -0.00580 -0.04010 -0.05484 216 LEU A CA  
2547 C C   A LEU A 216 ? 0.37472 0.37369 0.27033 0.00315  -0.03607 -0.04970 216 LEU A C   
2548 C C   B LEU A 216 ? 0.37562 0.37424 0.27116 0.00307  -0.03587 -0.04979 216 LEU A C   
2549 O O   A LEU A 216 ? 0.44581 0.44105 0.32554 0.00404  -0.03857 -0.05744 216 LEU A O   
2550 O O   B LEU A 216 ? 0.44671 0.44089 0.32618 0.00382  -0.03799 -0.05773 216 LEU A O   
2551 C CB  A LEU A 216 ? 0.36058 0.35296 0.28277 -0.01146 -0.03090 -0.05851 216 LEU A CB  
2552 C CB  B LEU A 216 ? 0.36112 0.35358 0.28346 -0.01159 -0.03100 -0.05870 216 LEU A CB  
2553 C CG  A LEU A 216 ? 0.55432 0.53983 0.47793 -0.02045 -0.03158 -0.07299 216 LEU A CG  
2554 C CG  B LEU A 216 ? 0.40214 0.38002 0.31272 -0.01603 -0.02739 -0.07077 216 LEU A CG  
2555 C CD1 A LEU A 216 ? 0.55288 0.52189 0.47569 -0.02334 -0.02005 -0.07450 216 LEU A CD1 
2556 C CD1 B LEU A 216 ? 0.53397 0.51912 0.44920 -0.02281 -0.03751 -0.08281 216 LEU A CD1 
2557 C CD2 A LEU A 216 ? 0.54036 0.52369 0.44721 -0.01973 -0.03724 -0.08185 216 LEU A CD2 
2558 C CD2 B LEU A 216 ? 0.53215 0.49765 0.44965 -0.02089 -0.01745 -0.07217 216 LEU A CD2 
2559 N N   . ASN A 217 ? 0.39853 0.39575 0.29335 0.01013  -0.02998 -0.03642 217 ASN A N   
2560 C CA  . ASN A 217 ? 0.44020 0.43098 0.31578 0.01950  -0.02484 -0.02959 217 ASN A CA  
2561 C C   . ASN A 217 ? 0.40617 0.40942 0.27348 0.02558  -0.03303 -0.02750 217 ASN A C   
2562 O O   . ASN A 217 ? 0.47088 0.46821 0.31768 0.03050  -0.03160 -0.03064 217 ASN A O   
2563 C CB  . ASN A 217 ? 0.43178 0.42048 0.31264 0.02515  -0.01777 -0.01436 217 ASN A CB  
2564 C CG  . ASN A 217 ? 0.65764 0.64192 0.52165 0.03583  -0.01223 -0.00441 217 ASN A CG  
2565 O OD1 . ASN A 217 ? 0.72456 0.69462 0.57167 0.03782  -0.00469 -0.00834 217 ASN A OD1 
2566 N ND2 . ASN A 217 ? 0.58547 0.58178 0.45493 0.04300  -0.01555 0.00902  217 ASN A ND2 
2567 N N   . GLN A 218 ? 0.38109 0.40161 0.26386 0.02534  -0.04174 -0.02279 218 GLN A N   
2568 C CA  . GLN A 218 ? 0.44542 0.47938 0.32187 0.03154  -0.04943 -0.01925 218 GLN A CA  
2569 C C   . GLN A 218 ? 0.49983 0.53498 0.36607 0.02710  -0.05654 -0.03386 218 GLN A C   
2570 O O   . GLN A 218 ? 0.48937 0.52850 0.33937 0.03336  -0.05995 -0.03377 218 GLN A O   
2571 C CB  . GLN A 218 ? 0.43625 0.48849 0.33388 0.03235  -0.05680 -0.00993 218 GLN A CB  
2572 C CG  . GLN A 218 ? 0.40327 0.45618 0.30982 0.03838  -0.05185 0.00593  218 GLN A CG  
2573 C CD  . GLN A 218 ? 0.49467 0.54511 0.38518 0.04941  -0.04677 0.01687  218 GLN A CD  
2574 O OE1 . GLN A 218 ? 0.62114 0.68065 0.50240 0.05533  -0.05121 0.01911  218 GLN A OE1 
2575 N NE2 . GLN A 218 ? 0.73670 0.77528 0.62386 0.05257  -0.03720 0.02425  218 GLN A NE2 
2576 N N   . SER A 219 ? 0.44403 0.47589 0.31948 0.01661  -0.05897 -0.04619 219 SER A N   
2577 C CA  . SER A 219 ? 0.43534 0.47239 0.30787 0.01108  -0.06844 -0.05899 219 SER A CA  
2578 C C   . SER A 219 ? 0.48220 0.50194 0.34038 0.00602  -0.06523 -0.07325 219 SER A C   
2579 O O   . SER A 219 ? 0.55149 0.57368 0.40797 0.00015  -0.07346 -0.08526 219 SER A O   
2580 C CB  . SER A 219 ? 0.40276 0.45237 0.30024 0.00260  -0.07568 -0.06194 219 SER A CB  
2581 O OG  . SER A 219 ? 0.51118 0.57430 0.42443 0.00663  -0.07737 -0.04900 219 SER A OG  
2582 N N   . TYR A 220 ? 0.48623 0.48862 0.33539 0.00787  -0.05377 -0.07208 220 TYR A N   
2583 C CA  . TYR A 220 ? 0.61641 0.60125 0.45635 0.00189  -0.04988 -0.08566 220 TYR A CA  
2584 C C   . TYR A 220 ? 0.78354 0.76537 0.60249 0.00318  -0.05645 -0.09681 220 TYR A C   
2585 O O   . TYR A 220 ? 0.61636 0.59278 0.43601 -0.00529 -0.06129 -0.11107 220 TYR A O   
2586 C CB  . TYR A 220 ? 0.55828 0.52567 0.39014 0.00560  -0.03603 -0.08066 220 TYR A CB  
2587 C CG  . TYR A 220 ? 0.88901 0.83766 0.71300 -0.00049 -0.03133 -0.09416 220 TYR A CG  
2588 C CD1 . TYR A 220 ? 0.83639 0.78129 0.67819 -0.01100 -0.03033 -0.10105 220 TYR A CD1 
2589 C CD2 . TYR A 220 ? 0.82739 0.76187 0.62649 0.00454  -0.02771 -0.09997 220 TYR A CD2 
2590 C CE1 . TYR A 220 ? 1.01850 0.94623 0.85518 -0.01677 -0.02602 -0.11297 220 TYR A CE1 
2591 C CE2 . TYR A 220 ? 1.09399 1.01023 0.88670 -0.00117 -0.02356 -0.11283 220 TYR A CE2 
2592 C CZ  . TYR A 220 ? 1.16542 1.07853 0.97787 -0.01205 -0.02287 -0.11907 220 TYR A CZ  
2593 O OH  . TYR A 220 ? 1.30313 1.19830 1.11141 -0.01783 -0.01872 -0.13118 220 TYR A OH  
2594 N N   . LYS A 221 ? 0.61108 0.59654 0.41141 0.01387  -0.05700 -0.09036 221 LYS A N   
2595 C CA  . LYS A 221 ? 0.61384 0.59681 0.39153 0.01633  -0.06353 -0.10077 221 LYS A CA  
2596 C C   . LYS A 221 ? 0.80728 0.80615 0.59494 0.00957  -0.07833 -0.10847 221 LYS A C   
2597 O O   . LYS A 221 ? 0.74852 0.74188 0.52786 0.00383  -0.08518 -0.12339 221 LYS A O   
2598 C CB  . LYS A 221 ? 0.69617 0.68196 0.45296 0.03036  -0.06046 -0.09011 221 LYS A CB  
2599 C CG  . LYS A 221 ? 0.74561 0.71363 0.48738 0.03788  -0.04606 -0.08438 221 LYS A CG  
2600 N N   . LEU A 222 ? 0.67050 0.68923 0.47655 0.01028  -0.08372 -0.09820 222 LEU A N   
2601 C CA  . LEU A 222 ? 0.78967 0.82493 0.60849 0.00381  -0.09726 -0.10380 222 LEU A CA  
2602 C C   . LEU A 222 ? 0.78791 0.81745 0.62324 -0.00949 -0.09961 -0.11613 222 LEU A C   
2603 O O   . LEU A 222 ? 0.82122 0.85427 0.65688 -0.01612 -0.10995 -0.12779 222 LEU A O   
2604 C CB  . LEU A 222 ? 0.59471 0.65056 0.43320 0.00705  -0.10046 -0.08935 222 LEU A CB  
2605 C CG  . LEU A 222 ? 0.85337 0.93043 0.70130 0.00522  -0.11414 -0.08983 222 LEU A CG  
2606 C CD1 . LEU A 222 ? 0.72901 0.80980 0.55163 0.01274  -0.12022 -0.09200 222 LEU A CD1 
2607 C CD2 . LEU A 222 ? 0.71587 0.81017 0.58557 0.00843  -0.11484 -0.07483 222 LEU A CD2 
2608 N N   . LEU A 223 ? 0.81517 0.83568 0.66412 -0.01331 -0.08998 -0.11342 223 LEU A N   
2609 C CA  . LEU A 223 ? 0.81701 0.83239 0.68361 -0.02524 -0.09045 -0.12310 223 LEU A CA  
2610 C C   . LEU A 223 ? 0.97786 0.97614 0.82983 -0.03016 -0.09104 -0.13858 223 LEU A C   
2611 O O   . LEU A 223 ? 1.35153 1.35196 1.21264 -0.03942 -0.09960 -0.14975 223 LEU A O   
2612 C CB  . LEU A 223 ? 0.71077 0.71960 0.59172 -0.02635 -0.07877 -0.11548 223 LEU A CB  
2613 C CG  . LEU A 223 ? 0.82017 0.82304 0.72025 -0.03722 -0.07612 -0.12261 223 LEU A CG  
2614 C CD1 . LEU A 223 ? 0.64207 0.66257 0.56567 -0.04418 -0.08588 -0.12404 223 LEU A CD1 
2615 C CD2 . LEU A 223 ? 0.70490 0.69968 0.61207 -0.03552 -0.06339 -0.11384 223 LEU A CD2 
2616 N N   . LEU A 224 ? 1.09320 1.07410 0.92339 -0.02412 -0.08205 -0.13931 224 LEU A N   
2617 C CA  . LEU A 224 ? 1.10251 1.06459 0.91856 -0.02835 -0.08138 -0.15415 224 LEU A CA  
2618 C C   . LEU A 224 ? 1.17692 1.14320 0.97664 -0.02817 -0.09450 -0.16485 224 LEU A C   
2619 O O   . LEU A 224 ? 1.18158 1.15596 0.96433 -0.01874 -0.09787 -0.15951 224 LEU A O   
2620 C CB  . LEU A 224 ? 0.91596 0.85889 0.71236 -0.02062 -0.06780 -0.15097 224 LEU A CB  
2621 C CG  . LEU A 224 ? 1.20232 1.12559 1.00435 -0.02747 -0.05854 -0.15802 224 LEU A CG  
2622 C CD1 . LEU A 224 ? 0.87394 0.80320 0.70475 -0.03389 -0.05383 -0.15101 224 LEU A CD1 
2623 C CD2 . LEU A 224 ? 1.25773 1.16231 1.03813 -0.01887 -0.04564 -0.15497 224 LEU A CD2 
2624 N N   . GLU A 225 ? 1.25391 1.21514 1.05942 -0.03859 -0.10220 -0.17960 225 GLU A N   
2625 C CA  . GLU A 225 ? 1.26654 1.23185 1.05854 -0.04012 -0.11641 -0.19120 225 GLU A CA  
2626 C C   . GLU A 225 ? 1.04352 0.99318 0.83681 -0.05078 -0.12063 -0.20878 225 GLU A C   
2627 O O   . GLU A 225 ? 1.09557 1.03458 0.90505 -0.05779 -0.11309 -0.21076 225 GLU A O   
2628 C CB  . GLU A 225 ? 1.12365 1.11453 0.93313 -0.04288 -0.12895 -0.18651 225 GLU A CB  
# 
