data_8RSS
# 
_entry.id   8RSS 
# 
_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   8RSS         pdb_00008rss 10.2210/pdb8rss/pdb 
WWPDB D_1292135963 ?            ?                   
# 
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 2025-04-02 ? 
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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Structure summary'   
# 
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 
3 2 'Structure model' struct_keywords 
# 
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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_DOI'    
5 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
6 2 'Structure model' '_citation.title'                   
7 2 'Structure model' '_struct_keywords.text'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RSS 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              valentin.gordeliy@ibs.fr 
_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 
'Kovalev, K.'    2 0000-0002-2229-181X 
'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            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                eadu5303 
_citation.page_last                 eadu5303 
_citation.title                     'Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adu5303 
_citation.pdbx_database_id_PubMed   40238873 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bukhdruker, S.'       1  0000-0002-0157-532X 
primary 'Gushchin, I.'         2  0000-0002-5348-6070 
primary 'Shevchenko, V.'       3  0000-0001-8478-3839 
primary 'Kovalev, K.'          4  0000-0002-2229-181X 
primary 'Polovinkin, V.'       5  0000-0002-3630-5565 
primary 'Tsybrov, F.'          6  0000-0001-7422-0899 
primary 'Astashkin, R.'        7  0000-0001-9065-8225 
primary 'Alekseev, A.'         8  0000-0001-8990-1662 
primary 'Mikhaylov, A.'        9  0000-0002-4697-0577 
primary 'Bukhalovich, S.'      10 0000-0002-0770-6597 
primary 'Bratanov, D.'         11 ?                   
primary 'Ryzhykau, Y.'         12 0000-0003-3719-1464 
primary 'Kuklina, D.'          13 0000-0002-9614-5137 
primary 'Caramello, N.'        14 0000-0003-0025-0213 
primary 'Rokitskaya, T.'       15 0000-0002-7719-1875 
primary 'Antonenko, Y.'        16 0000-0002-0244-855X 
primary 'Rulev, M.'            17 0000-0001-6103-320X 
primary 'Stoev, C.'            18 0009-0000-6708-8922 
primary 'Zabelskii, D.'        19 0000-0001-6906-975X 
primary 'Round, E.'            20 ?                   
primary 'Rogachev, A.'         21 0000-0003-2872-7976 
primary 'Borshchevskiy, V.'    22 0000-0003-4398-9712 
primary 'Ghai, R.'             23 0000-0002-0591-6152 
primary 'Bourenkov, G.'        24 0000-0002-2617-5920 
primary 'Zeghouf, M.'          25 0000-0003-3686-2510 
primary 'Cherfils, J.'         26 0000-0002-8966-3067 
primary 'Engelhard, M.'        27 ?                   
primary 'Chizhov, I.'          28 0000-0001-7744-9365 
primary 'Rodriguez-Valera, F.' 29 0000-0002-9809-2059 
primary 'Bamberg, E.'          30 0000-0002-5411-6207 
primary 'Gordeliy, V.'         31 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 'Microbial rhodopsin' 24277.076 1   ? ? ? ? 
2 non-polymer syn 'OLEIC ACID'          282.461   3   ? ? ? ? 
3 non-polymer syn EICOSANE              282.547   11  ? ? ? ? 
4 non-polymer man RETINAL               284.436   1   ? ? ? ? 
5 water       nat water                 18.015    147 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MEELTYRLFMVATVGMLAGTVFLLASSREVKPEHRRGVYISALVCGIAWYHYQKMGASWESGSYDTGLRYVDWVLTVPLM
FVEVLAVTRKGAAYNEAVRNWGIAATVMIGAGYYGETSAAGSNEYWTGFVIAMATYVWLMRNLQAEGEGLKGDQAVAFEN
IKNLILVGWIIYPLGYIAPVVGDFDAIREVLYTIADIINKVGLGVLVLQMARVQSGEKVS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEELTYRLFMVATVGMLAGTVFLLASSREVKPEHRRGVYISALVCGIAWYHYQKMGASWESGSYDTGLRYVDWVLTVPLM
FVEVLAVTRKGAAYNEAVRNWGIAATVMIGAGYYGETSAAGSNEYWTGFVIAMATYVWLMRNLQAEGEGLKGDQAVAFEN
IKNLILVGWIIYPLGYIAPVVGDFDAIREVLYTIADIINKVGLGVLVLQMARVQSGEKVS
;
_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 'OLEIC ACID' OLA 
3 EICOSANE     LFA 
4 RETINAL      RET 
5 water        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   GLU n 
1 4   LEU n 
1 5   THR n 
1 6   TYR n 
1 7   ARG n 
1 8   LEU n 
1 9   PHE n 
1 10  MET n 
1 11  VAL n 
1 12  ALA n 
1 13  THR n 
1 14  VAL n 
1 15  GLY n 
1 16  MET n 
1 17  LEU n 
1 18  ALA n 
1 19  GLY n 
1 20  THR n 
1 21  VAL n 
1 22  PHE n 
1 23  LEU n 
1 24  LEU n 
1 25  ALA n 
1 26  SER n 
1 27  SER n 
1 28  ARG n 
1 29  GLU n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  GLU n 
1 34  HIS n 
1 35  ARG n 
1 36  ARG n 
1 37  GLY n 
1 38  VAL n 
1 39  TYR n 
1 40  ILE n 
1 41  SER n 
1 42  ALA n 
1 43  LEU n 
1 44  VAL n 
1 45  CYS n 
1 46  GLY n 
1 47  ILE n 
1 48  ALA n 
1 49  TRP n 
1 50  TYR n 
1 51  HIS n 
1 52  TYR n 
1 53  GLN n 
1 54  LYS n 
1 55  MET n 
1 56  GLY n 
1 57  ALA n 
1 58  SER n 
1 59  TRP n 
1 60  GLU n 
1 61  SER n 
1 62  GLY n 
1 63  SER n 
1 64  TYR n 
1 65  ASP n 
1 66  THR n 
1 67  GLY n 
1 68  LEU n 
1 69  ARG n 
1 70  TYR n 
1 71  VAL n 
1 72  ASP n 
1 73  TRP n 
1 74  VAL n 
1 75  LEU n 
1 76  THR n 
1 77  VAL n 
1 78  PRO n 
1 79  LEU n 
1 80  MET n 
1 81  PHE n 
1 82  VAL n 
1 83  GLU n 
1 84  VAL n 
1 85  LEU n 
1 86  ALA n 
1 87  VAL n 
1 88  THR n 
1 89  ARG n 
1 90  LYS n 
1 91  GLY n 
1 92  ALA n 
1 93  ALA n 
1 94  TYR n 
1 95  ASN n 
1 96  GLU n 
1 97  ALA n 
1 98  VAL n 
1 99  ARG n 
1 100 ASN n 
1 101 TRP n 
1 102 GLY n 
1 103 ILE n 
1 104 ALA n 
1 105 ALA n 
1 106 THR n 
1 107 VAL n 
1 108 MET n 
1 109 ILE n 
1 110 GLY n 
1 111 ALA n 
1 112 GLY n 
1 113 TYR n 
1 114 TYR n 
1 115 GLY n 
1 116 GLU n 
1 117 THR n 
1 118 SER n 
1 119 ALA n 
1 120 ALA n 
1 121 GLY n 
1 122 SER n 
1 123 ASN n 
1 124 GLU n 
1 125 TYR n 
1 126 TRP n 
1 127 THR n 
1 128 GLY n 
1 129 PHE n 
1 130 VAL n 
1 131 ILE n 
1 132 ALA n 
1 133 MET n 
1 134 ALA n 
1 135 THR n 
1 136 TYR n 
1 137 VAL n 
1 138 TRP n 
1 139 LEU n 
1 140 MET n 
1 141 ARG n 
1 142 ASN n 
1 143 LEU n 
1 144 GLN n 
1 145 ALA n 
1 146 GLU n 
1 147 GLY n 
1 148 GLU n 
1 149 GLY n 
1 150 LEU n 
1 151 LYS n 
1 152 GLY n 
1 153 ASP n 
1 154 GLN n 
1 155 ALA n 
1 156 VAL n 
1 157 ALA n 
1 158 PHE n 
1 159 GLU n 
1 160 ASN n 
1 161 ILE n 
1 162 LYS n 
1 163 ASN n 
1 164 LEU n 
1 165 ILE n 
1 166 LEU n 
1 167 VAL n 
1 168 GLY n 
1 169 TRP n 
1 170 ILE n 
1 171 ILE n 
1 172 TYR n 
1 173 PRO n 
1 174 LEU n 
1 175 GLY n 
1 176 TYR n 
1 177 ILE n 
1 178 ALA n 
1 179 PRO n 
1 180 VAL n 
1 181 VAL n 
1 182 GLY n 
1 183 ASP n 
1 184 PHE n 
1 185 ASP n 
1 186 ALA n 
1 187 ILE n 
1 188 ARG n 
1 189 GLU n 
1 190 VAL n 
1 191 LEU n 
1 192 TYR n 
1 193 THR n 
1 194 ILE n 
1 195 ALA n 
1 196 ASP n 
1 197 ILE n 
1 198 ILE n 
1 199 ASN n 
1 200 LYS n 
1 201 VAL n 
1 202 GLY n 
1 203 LEU n 
1 204 GLY n 
1 205 VAL n 
1 206 LEU n 
1 207 VAL n 
1 208 LEU n 
1 209 GLN n 
1 210 MET n 
1 211 ALA n 
1 212 ARG n 
1 213 VAL n 
1 214 GLN n 
1 215 SER n 
1 216 GLY n 
1 217 GLU n 
1 218 LYS n 
1 219 VAL n 
1 220 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 220 ? ? ? ? ? ? ? ? ? 'marine Actinobacteria clade' 62676 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 220 ? ? ? ? ? ? ? ? ? 'marine Actinobacteria clade' 62676 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                'C3 H7 N O2 S'   121.158 
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 
OLA non-polymer         . 'OLEIC ACID'    ?                'C18 H34 O2'     282.461 
PHE 'L-peptide linking' y PHENYLALANINE   ?                'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                'C5 H9 N O2'     115.130 
RET non-polymer         . RETINAL         ?                'C20 H28 O'      284.436 
SER 'L-peptide linking' y SERINE          ?                'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  MET 10  10  10  MET MET A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  CYS 45  45  45  CYS CYS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  MET 55  55  55  MET MET A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  TRP 73  73  73  TRP TRP A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 MET 108 108 108 MET MET A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 MET 133 133 133 MET MET A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 MET 140 140 140 MET MET A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 TRP 169 169 169 TRP TRP A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ASN 199 199 199 ASN ASN A . n 
A 1 200 LYS 200 200 200 LYS LYR A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 GLN 209 209 209 GLN GLN A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 VAL 219 219 ?   ?   ?   A . n 
A 1 220 SER 220 220 ?   ?   ?   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 OLA 1   501 501 OLA OLA A . 
C 2 OLA 1   502 502 OLA OLA A . 
D 2 OLA 1   503 503 OLA OLA A . 
E 3 LFA 1   504 504 LFA LFA A . 
F 3 LFA 1   505 505 LFA LFA A . 
G 3 LFA 1   506 506 LFA LFA A . 
H 3 LFA 1   507 507 LFA LFA A . 
I 3 LFA 1   508 508 LFA LFA A . 
J 3 LFA 1   509 509 LFA LFA A . 
K 3 LFA 1   510 510 LFA LFA A . 
L 3 LFA 1   511 511 LFA LFA A . 
M 3 LFA 1   512 512 LFA LFA A . 
N 3 LFA 1   513 513 LFA LFA A . 
O 3 LFA 1   514 514 LFA LFA A . 
P 4 RET 1   515 200 RET LYR A . 
Q 5 HOH 1   601 684 HOH HOH A . 
Q 5 HOH 2   602 607 HOH HOH A . 
Q 5 HOH 3   603 620 HOH HOH A . 
Q 5 HOH 4   604 709 HOH HOH A . 
Q 5 HOH 5   605 732 HOH HOH A . 
Q 5 HOH 6   606 629 HOH HOH A . 
Q 5 HOH 7   607 671 HOH HOH A . 
Q 5 HOH 8   608 659 HOH HOH A . 
Q 5 HOH 9   609 679 HOH HOH A . 
Q 5 HOH 10  610 713 HOH HOH A . 
Q 5 HOH 11  611 685 HOH HOH A . 
Q 5 HOH 12  612 652 HOH HOH A . 
Q 5 HOH 13  613 664 HOH HOH A . 
Q 5 HOH 14  614 705 HOH HOH A . 
Q 5 HOH 15  615 675 HOH HOH A . 
Q 5 HOH 16  616 623 HOH HOH A . 
Q 5 HOH 17  617 646 HOH HOH A . 
Q 5 HOH 18  618 660 HOH HOH A . 
Q 5 HOH 19  619 653 HOH HOH A . 
Q 5 HOH 20  620 691 HOH HOH A . 
Q 5 HOH 21  621 674 HOH HOH A . 
Q 5 HOH 22  622 724 HOH HOH A . 
Q 5 HOH 23  623 682 HOH HOH A . 
Q 5 HOH 24  624 708 HOH HOH A . 
Q 5 HOH 25  625 643 HOH HOH A . 
Q 5 HOH 26  626 693 HOH HOH A . 
Q 5 HOH 27  627 630 HOH HOH A . 
Q 5 HOH 28  628 633 HOH HOH A . 
Q 5 HOH 29  629 669 HOH HOH A . 
Q 5 HOH 30  630 632 HOH HOH A . 
Q 5 HOH 31  631 655 HOH HOH A . 
Q 5 HOH 32  632 612 HOH HOH A . 
Q 5 HOH 33  633 601 HOH HOH A . 
Q 5 HOH 34  634 651 HOH HOH A . 
Q 5 HOH 35  635 644 HOH HOH A . 
Q 5 HOH 36  636 680 HOH HOH A . 
Q 5 HOH 37  637 606 HOH HOH A . 
Q 5 HOH 38  638 608 HOH HOH A . 
Q 5 HOH 39  639 624 HOH HOH A . 
Q 5 HOH 40  640 706 HOH HOH A . 
Q 5 HOH 41  641 662 HOH HOH A . 
Q 5 HOH 42  642 603 HOH HOH A . 
Q 5 HOH 43  643 656 HOH HOH A . 
Q 5 HOH 44  644 609 HOH HOH A . 
Q 5 HOH 45  645 645 HOH HOH A . 
Q 5 HOH 46  646 628 HOH HOH A . 
Q 5 HOH 47  647 642 HOH HOH A . 
Q 5 HOH 48  648 611 HOH HOH A . 
Q 5 HOH 49  649 673 HOH HOH A . 
Q 5 HOH 50  650 637 HOH HOH A . 
Q 5 HOH 51  651 737 HOH HOH A . 
Q 5 HOH 52  652 613 HOH HOH A . 
Q 5 HOH 53  653 602 HOH HOH A . 
Q 5 HOH 54  654 654 HOH HOH A . 
Q 5 HOH 55  655 619 HOH HOH A . 
Q 5 HOH 56  656 604 HOH HOH A . 
Q 5 HOH 57  657 635 HOH HOH A . 
Q 5 HOH 58  658 742 HOH HOH A . 
Q 5 HOH 59  659 614 HOH HOH A . 
Q 5 HOH 60  660 700 HOH HOH A . 
Q 5 HOH 61  661 688 HOH HOH A . 
Q 5 HOH 62  662 640 HOH HOH A . 
Q 5 HOH 63  663 665 HOH HOH A . 
Q 5 HOH 64  664 658 HOH HOH A . 
Q 5 HOH 65  665 728 HOH HOH A . 
Q 5 HOH 66  666 677 HOH HOH A . 
Q 5 HOH 67  667 701 HOH HOH A . 
Q 5 HOH 68  668 605 HOH HOH A . 
Q 5 HOH 69  669 725 HOH HOH A . 
Q 5 HOH 70  670 636 HOH HOH A . 
Q 5 HOH 71  671 648 HOH HOH A . 
Q 5 HOH 72  672 621 HOH HOH A . 
Q 5 HOH 73  673 639 HOH HOH A . 
Q 5 HOH 74  674 686 HOH HOH A . 
Q 5 HOH 75  675 670 HOH HOH A . 
Q 5 HOH 76  676 741 HOH HOH A . 
Q 5 HOH 77  677 610 HOH HOH A . 
Q 5 HOH 78  678 617 HOH HOH A . 
Q 5 HOH 79  679 726 HOH HOH A . 
Q 5 HOH 80  680 716 HOH HOH A . 
Q 5 HOH 81  681 666 HOH HOH A . 
Q 5 HOH 82  682 649 HOH HOH A . 
Q 5 HOH 83  683 618 HOH HOH A . 
Q 5 HOH 84  684 703 HOH HOH A . 
Q 5 HOH 85  685 638 HOH HOH A . 
Q 5 HOH 86  686 641 HOH HOH A . 
Q 5 HOH 87  687 626 HOH HOH A . 
Q 5 HOH 88  688 687 HOH HOH A . 
Q 5 HOH 89  689 744 HOH HOH A . 
Q 5 HOH 90  690 667 HOH HOH A . 
Q 5 HOH 91  691 631 HOH HOH A . 
Q 5 HOH 92  692 622 HOH HOH A . 
Q 5 HOH 93  693 727 HOH HOH A . 
Q 5 HOH 94  694 634 HOH HOH A . 
Q 5 HOH 95  695 739 HOH HOH A . 
Q 5 HOH 96  696 695 HOH HOH A . 
Q 5 HOH 97  697 710 HOH HOH A . 
Q 5 HOH 98  698 712 HOH HOH A . 
Q 5 HOH 99  699 717 HOH HOH A . 
Q 5 HOH 100 700 711 HOH HOH A . 
Q 5 HOH 101 701 733 HOH HOH A . 
Q 5 HOH 102 702 723 HOH HOH A . 
Q 5 HOH 103 703 722 HOH HOH A . 
Q 5 HOH 104 704 678 HOH HOH A . 
Q 5 HOH 105 705 689 HOH HOH A . 
Q 5 HOH 106 706 702 HOH HOH A . 
Q 5 HOH 107 707 731 HOH HOH A . 
Q 5 HOH 108 708 694 HOH HOH A . 
Q 5 HOH 109 709 668 HOH HOH A . 
Q 5 HOH 110 710 740 HOH HOH A . 
Q 5 HOH 111 711 718 HOH HOH A . 
Q 5 HOH 112 712 661 HOH HOH A . 
Q 5 HOH 113 713 743 HOH HOH A . 
Q 5 HOH 114 714 696 HOH HOH A . 
Q 5 HOH 115 715 738 HOH HOH A . 
Q 5 HOH 116 716 698 HOH HOH A . 
Q 5 HOH 117 717 720 HOH HOH A . 
Q 5 HOH 118 718 746 HOH HOH A . 
Q 5 HOH 119 719 690 HOH HOH A . 
Q 5 HOH 120 720 681 HOH HOH A . 
Q 5 HOH 121 721 714 HOH HOH A . 
Q 5 HOH 122 722 735 HOH HOH A . 
Q 5 HOH 123 723 699 HOH HOH A . 
Q 5 HOH 124 724 704 HOH HOH A . 
Q 5 HOH 125 725 736 HOH HOH A . 
Q 5 HOH 126 726 672 HOH HOH A . 
Q 5 HOH 127 727 747 HOH HOH A . 
Q 5 HOH 128 728 657 HOH HOH A . 
Q 5 HOH 129 729 707 HOH HOH A . 
Q 5 HOH 130 730 734 HOH HOH A . 
Q 5 HOH 131 731 615 HOH HOH A . 
Q 5 HOH 132 732 715 HOH HOH A . 
Q 5 HOH 133 733 616 HOH HOH A . 
Q 5 HOH 134 734 721 HOH HOH A . 
Q 5 HOH 135 735 683 HOH HOH A . 
Q 5 HOH 136 736 650 HOH HOH A . 
Q 5 HOH 137 737 729 HOH HOH A . 
Q 5 HOH 138 738 663 HOH HOH A . 
Q 5 HOH 139 739 697 HOH HOH A . 
Q 5 HOH 140 740 676 HOH HOH A . 
Q 5 HOH 141 741 647 HOH HOH A . 
Q 5 HOH 142 742 692 HOH HOH A . 
Q 5 HOH 143 743 745 HOH HOH A . 
Q 5 HOH 144 744 625 HOH HOH A . 
Q 5 HOH 145 745 627 HOH HOH A . 
Q 5 HOH 146 746 719 HOH HOH A . 
Q 5 HOH 147 747 730 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 2   ? CG  ? A GLU 2   CG  
2   1 Y 1 A GLU 2   ? CD  ? A GLU 2   CD  
3   1 Y 1 A GLU 2   ? OE1 ? A GLU 2   OE1 
4   1 Y 1 A GLU 2   ? OE2 ? A GLU 2   OE2 
5   1 Y 1 A GLU 3   ? CD  ? A GLU 3   CD  
6   1 Y 1 A GLU 3   ? OE1 ? A GLU 3   OE1 
7   1 Y 1 A GLU 3   ? OE2 ? A GLU 3   OE2 
8   1 Y 1 A ARG 7   ? NH1 ? A ARG 7   NH1 
9   1 Y 1 A ARG 7   ? NH2 ? A ARG 7   NH2 
10  1 Y 1 A MET 10  ? CE  ? A MET 10  CE  
11  1 Y 1 A ARG 36  ? NH1 ? A ARG 36  NH1 
12  1 Y 1 A ARG 36  ? NH2 ? A ARG 36  NH2 
13  1 Y 1 A GLU 148 ? CG  ? A GLU 148 CG  
14  1 Y 1 A GLU 148 ? CD  ? A GLU 148 CD  
15  1 Y 1 A GLU 148 ? OE1 ? A GLU 148 OE1 
16  1 Y 1 A GLU 148 ? OE2 ? A GLU 148 OE2 
17  1 Y 1 A LYS 218 ? CG  ? A LYS 218 CG  
18  1 Y 1 A LYS 218 ? CD  ? A LYS 218 CD  
19  1 Y 1 A LYS 218 ? CE  ? A LYS 218 CE  
20  1 Y 1 A LYS 218 ? NZ  ? A LYS 218 NZ  
21  1 N 1 A OLA 502 ? O1  ? C OLA 1   O1  
22  1 N 1 A OLA 502 ? O2  ? C OLA 1   O2  
23  1 N 1 A OLA 502 ? C17 ? C OLA 1   C17 
24  1 N 1 A OLA 502 ? C18 ? C OLA 1   C18 
25  1 N 1 A LFA 504 ? C1  ? E LFA 1   C1  
26  1 N 1 A LFA 504 ? C2  ? E LFA 1   C2  
27  1 N 1 A LFA 504 ? C3  ? E LFA 1   C3  
28  1 N 1 A LFA 504 ? C4  ? E LFA 1   C4  
29  1 N 1 A LFA 504 ? C5  ? E LFA 1   C5  
30  1 N 1 A LFA 504 ? C6  ? E LFA 1   C6  
31  1 N 1 A LFA 504 ? C7  ? E LFA 1   C7  
32  1 N 1 A LFA 504 ? C8  ? E LFA 1   C8  
33  1 N 1 A LFA 504 ? C9  ? E LFA 1   C9  
34  1 N 1 A LFA 504 ? C18 ? E LFA 1   C18 
35  1 N 1 A LFA 504 ? C19 ? E LFA 1   C19 
36  1 N 1 A LFA 504 ? C20 ? E LFA 1   C20 
37  1 N 1 A LFA 505 ? C1  ? F LFA 1   C1  
38  1 N 1 A LFA 505 ? C2  ? F LFA 1   C2  
39  1 N 1 A LFA 505 ? C3  ? F LFA 1   C3  
40  1 N 1 A LFA 505 ? C4  ? F LFA 1   C4  
41  1 N 1 A LFA 505 ? C5  ? F LFA 1   C5  
42  1 N 1 A LFA 505 ? C15 ? F LFA 1   C15 
43  1 N 1 A LFA 505 ? C16 ? F LFA 1   C16 
44  1 N 1 A LFA 505 ? C17 ? F LFA 1   C17 
45  1 N 1 A LFA 505 ? C18 ? F LFA 1   C18 
46  1 N 1 A LFA 505 ? C19 ? F LFA 1   C19 
47  1 N 1 A LFA 505 ? C20 ? F LFA 1   C20 
48  1 N 1 A LFA 506 ? C12 ? G LFA 1   C12 
49  1 N 1 A LFA 506 ? C13 ? G LFA 1   C13 
50  1 N 1 A LFA 506 ? C14 ? G LFA 1   C14 
51  1 N 1 A LFA 506 ? C15 ? G LFA 1   C15 
52  1 N 1 A LFA 506 ? C16 ? G LFA 1   C16 
53  1 N 1 A LFA 506 ? C17 ? G LFA 1   C17 
54  1 N 1 A LFA 506 ? C18 ? G LFA 1   C18 
55  1 N 1 A LFA 506 ? C19 ? G LFA 1   C19 
56  1 N 1 A LFA 506 ? C20 ? G LFA 1   C20 
57  1 N 1 A LFA 507 ? C9  ? H LFA 1   C9  
58  1 N 1 A LFA 507 ? C10 ? H LFA 1   C10 
59  1 N 1 A LFA 507 ? C11 ? H LFA 1   C11 
60  1 N 1 A LFA 507 ? C12 ? H LFA 1   C12 
61  1 N 1 A LFA 507 ? C13 ? H LFA 1   C13 
62  1 N 1 A LFA 507 ? C14 ? H LFA 1   C14 
63  1 N 1 A LFA 507 ? C15 ? H LFA 1   C15 
64  1 N 1 A LFA 507 ? C16 ? H LFA 1   C16 
65  1 N 1 A LFA 507 ? C17 ? H LFA 1   C17 
66  1 N 1 A LFA 507 ? C18 ? H LFA 1   C18 
67  1 N 1 A LFA 507 ? C19 ? H LFA 1   C19 
68  1 N 1 A LFA 507 ? C20 ? H LFA 1   C20 
69  1 N 1 A LFA 508 ? C7  ? I LFA 1   C7  
70  1 N 1 A LFA 508 ? C8  ? I LFA 1   C8  
71  1 N 1 A LFA 508 ? C9  ? I LFA 1   C9  
72  1 N 1 A LFA 508 ? C10 ? I LFA 1   C10 
73  1 N 1 A LFA 508 ? C11 ? I LFA 1   C11 
74  1 N 1 A LFA 508 ? C12 ? I LFA 1   C12 
75  1 N 1 A LFA 508 ? C13 ? I LFA 1   C13 
76  1 N 1 A LFA 508 ? C14 ? I LFA 1   C14 
77  1 N 1 A LFA 508 ? C15 ? I LFA 1   C15 
78  1 N 1 A LFA 508 ? C16 ? I LFA 1   C16 
79  1 N 1 A LFA 508 ? C17 ? I LFA 1   C17 
80  1 N 1 A LFA 508 ? C18 ? I LFA 1   C18 
81  1 N 1 A LFA 508 ? C19 ? I LFA 1   C19 
82  1 N 1 A LFA 508 ? C20 ? I LFA 1   C20 
83  1 N 1 A LFA 509 ? C1  ? J LFA 1   C1  
84  1 N 1 A LFA 509 ? C2  ? J LFA 1   C2  
85  1 N 1 A LFA 509 ? C3  ? J LFA 1   C3  
86  1 N 1 A LFA 509 ? C4  ? J LFA 1   C4  
87  1 N 1 A LFA 509 ? C5  ? J LFA 1   C5  
88  1 N 1 A LFA 509 ? C6  ? J LFA 1   C6  
89  1 N 1 A LFA 509 ? C7  ? J LFA 1   C7  
90  1 N 1 A LFA 509 ? C8  ? J LFA 1   C8  
91  1 N 1 A LFA 509 ? C9  ? J LFA 1   C9  
92  1 N 1 A LFA 509 ? C13 ? J LFA 1   C13 
93  1 N 1 A LFA 509 ? C14 ? J LFA 1   C14 
94  1 N 1 A LFA 509 ? C15 ? J LFA 1   C15 
95  1 N 1 A LFA 509 ? C16 ? J LFA 1   C16 
96  1 N 1 A LFA 509 ? C17 ? J LFA 1   C17 
97  1 N 1 A LFA 509 ? C18 ? J LFA 1   C18 
98  1 N 1 A LFA 509 ? C19 ? J LFA 1   C19 
99  1 N 1 A LFA 509 ? C20 ? J LFA 1   C20 
100 1 N 1 A LFA 510 ? C1  ? K LFA 1   C1  
101 1 N 1 A LFA 510 ? C2  ? K LFA 1   C2  
102 1 N 1 A LFA 510 ? C10 ? K LFA 1   C10 
103 1 N 1 A LFA 510 ? C11 ? K LFA 1   C11 
104 1 N 1 A LFA 510 ? C12 ? K LFA 1   C12 
105 1 N 1 A LFA 510 ? C13 ? K LFA 1   C13 
106 1 N 1 A LFA 510 ? C14 ? K LFA 1   C14 
107 1 N 1 A LFA 510 ? C15 ? K LFA 1   C15 
108 1 N 1 A LFA 510 ? C16 ? K LFA 1   C16 
109 1 N 1 A LFA 510 ? C17 ? K LFA 1   C17 
110 1 N 1 A LFA 510 ? C18 ? K LFA 1   C18 
111 1 N 1 A LFA 510 ? C19 ? K LFA 1   C19 
112 1 N 1 A LFA 510 ? C20 ? K LFA 1   C20 
113 1 N 1 A LFA 511 ? C1  ? L LFA 1   C1  
114 1 N 1 A LFA 511 ? C2  ? L LFA 1   C2  
115 1 N 1 A LFA 511 ? C3  ? L LFA 1   C3  
116 1 N 1 A LFA 511 ? C4  ? L LFA 1   C4  
117 1 N 1 A LFA 511 ? C5  ? L LFA 1   C5  
118 1 N 1 A LFA 511 ? C15 ? L LFA 1   C15 
119 1 N 1 A LFA 511 ? C16 ? L LFA 1   C16 
120 1 N 1 A LFA 511 ? C17 ? L LFA 1   C17 
121 1 N 1 A LFA 511 ? C18 ? L LFA 1   C18 
122 1 N 1 A LFA 511 ? C19 ? L LFA 1   C19 
123 1 N 1 A LFA 511 ? C20 ? L LFA 1   C20 
124 1 N 1 A LFA 512 ? C1  ? M LFA 1   C1  
125 1 N 1 A LFA 512 ? C2  ? M LFA 1   C2  
126 1 N 1 A LFA 512 ? C3  ? M LFA 1   C3  
127 1 N 1 A LFA 512 ? C4  ? M LFA 1   C4  
128 1 N 1 A LFA 512 ? C5  ? M LFA 1   C5  
129 1 N 1 A LFA 512 ? C6  ? M LFA 1   C6  
130 1 N 1 A LFA 512 ? C7  ? M LFA 1   C7  
131 1 N 1 A LFA 513 ? C1  ? N LFA 1   C1  
132 1 N 1 A LFA 513 ? C2  ? N LFA 1   C2  
133 1 N 1 A LFA 513 ? C3  ? N LFA 1   C3  
134 1 N 1 A LFA 513 ? C4  ? N LFA 1   C4  
135 1 N 1 A LFA 513 ? C5  ? N LFA 1   C5  
136 1 N 1 A LFA 513 ? C6  ? N LFA 1   C6  
137 1 N 1 A LFA 513 ? C7  ? N LFA 1   C7  
138 1 N 1 A LFA 513 ? C8  ? N LFA 1   C8  
139 1 N 1 A LFA 513 ? C9  ? N LFA 1   C9  
140 1 N 1 A LFA 513 ? C10 ? N LFA 1   C10 
141 1 N 1 A LFA 513 ? C11 ? N LFA 1   C11 
142 1 N 1 A LFA 513 ? C12 ? N LFA 1   C12 
143 1 N 1 A LFA 513 ? C13 ? N LFA 1   C13 
144 1 N 1 A LFA 513 ? C14 ? N LFA 1   C14 
145 1 N 1 A LFA 513 ? C15 ? N LFA 1   C15 
146 1 N 1 A LFA 513 ? C16 ? N LFA 1   C16 
147 1 N 1 A LFA 514 ? C1  ? O LFA 1   C1  
148 1 N 1 A LFA 514 ? C2  ? O LFA 1   C2  
149 1 N 1 A LFA 514 ? C3  ? O LFA 1   C3  
150 1 N 1 A LFA 514 ? C4  ? O LFA 1   C4  
151 1 N 1 A LFA 514 ? C5  ? O LFA 1   C5  
152 1 N 1 A LFA 514 ? C6  ? O LFA 1   C6  
153 1 N 1 A LFA 514 ? C7  ? O LFA 1   C7  
154 1 N 1 A LFA 514 ? C8  ? O LFA 1   C8  
155 1 N 1 A LFA 514 ? C9  ? O LFA 1   C9  
156 1 N 1 A LFA 514 ? C10 ? O LFA 1   C10 
157 1 N 1 A LFA 514 ? C11 ? O LFA 1   C11 
158 1 N 1 A LFA 514 ? C12 ? O LFA 1   C12 
159 1 N 1 A LFA 514 ? C13 ? O LFA 1   C13 
160 1 N 1 A LFA 514 ? C14 ? O LFA 1   C14 
161 1 N 1 A LFA 514 ? C15 ? O LFA 1   C15 
162 1 N 1 A LFA 514 ? C16 ? O LFA 1   C16 
163 1 N 1 A LFA 514 ? C17 ? O LFA 1   C17 
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? 20220110    1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? 2.3.94      2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? 2.8.4       3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.220 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RSS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.608 
_cell.length_a_esd                 ? 
_cell.length_b                     40.174 
_cell.length_b_esd                 ? 
_cell.length_c                     60.307 
_cell.length_c_esd                 ? 
_cell.volume                       120268.276 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8RSS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            'P 2y' 
_symmetry.space_group_name_H-M             'P 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RSS 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.80 
_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              8.4 
_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    '2.6 M Ammonium Phosphate buffer' 
_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 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         2022-01-20 
_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                          14.12 
_reflns.entry_id                                       8RSS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.41 
_reflns.d_resolution_low                               40.17 
_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                                     27492 
_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                           88.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.0 
_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                                0.047 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
4.50 40.17 ? 19.7 ? ? ? ? 1374 ? ? ? ? ? ? ? ? ? ? ? 2.4 ? ? ? ? 0.019 ? 1 1 0.999 ? ? 92.4 ? ? ? ? ? ? ? ? ? ? ? 
1.41 1.55  ? 1.3  ? ? ? ? 1375 ? ? ? ? ? ? ? ? ? ? ? 1.7 ? ? ? ? 0.344 ? 2 1 0.709 ? ? 46.5 ? ? ? ? ? ? ? ? ? ? ? 
# 
_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                               20.08 
_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                                 8RSS 
_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                             40.17 
_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                     27486 
_refine.ls_number_reflns_R_free                  1347 
_refine.ls_number_reflns_R_work                  26139 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    60.17 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1612 
_refine.ls_R_factor_R_free                       0.1979 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1594 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.4139 
_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                            0.1103 
_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                        40.17 
_refine_hist.number_atoms_solvent             147 
_refine_hist.number_atoms_total               1980 
_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        1696 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         137 
_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' ? 0.0028  ? 2116 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5791  ? 2852 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0558  ? 301  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0040  ? 352  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.5717 ? 812  ? 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 1.46  . . 2   150  3.39  . . . . 0.1934 . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 1.47 1.52  . . 35  639  14.89 . . . . 0.1643 . . . . . . . . . . . 0.2362 
'X-RAY DIFFRACTION' 1.52 1.59  . . 88  1483 34.45 . . . . 0.1833 . . . . . . . . . . . 0.2432 
'X-RAY DIFFRACTION' 1.59 1.68  . . 123 2195 50.93 . . . . 0.1702 . . . . . . . . . . . 0.2342 
'X-RAY DIFFRACTION' 1.68 1.78  . . 125 2566 59.64 . . . . 0.1718 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 1.78 1.92  . . 150 2932 67.54 . . . . 0.1695 . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 1.92 2.11  . . 171 3493 80.28 . . . . 0.1576 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.11 2.42  . . 220 4241 96.98 . . . . 0.1457 . . . . . . . . . . . 0.1834 
'X-RAY DIFFRACTION' 2.42 3.05  . . 212 4218 96.56 . . . . 0.1530 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 3.05 40.17 . . 221 4222 94.43 . . . . 0.1642 . . . . . . . . . . . 0.1962 
# 
_struct.entry_id                     8RSS 
_struct.title                        'Crystal structure of marine actinobacteria clade rhodopsin (MAR) in the O* state' 
_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        8RSS 
_struct_keywords.text            'Mac, MacR, MAR, proteorhodopsin, PR, xanthorodopsin, XR, MEMBRANE PROTEIN, xanthorhodopsin' 
_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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8RSS 
_struct_ref.pdbx_db_accession          8RSS 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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              8RSS 
_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                 220 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8RSS 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  220 
_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       220 
# 
_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)' 5030  ? 
1 MORE         19    ? 
1 'SSA (A^2)'  10000 ? 
# 
_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 
# 
_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 MET A 1   ? SER A 27  ? MET A 1   SER A 27  1 ? 27 
HELX_P HELX_P2  AA2 ARG A 28  ? VAL A 30  ? ARG A 28  VAL A 30  5 ? 3  
HELX_P HELX_P3  AA3 LYS A 31  ? HIS A 34  ? LYS A 31  HIS A 34  5 ? 4  
HELX_P HELX_P4  AA4 ARG A 35  ? GLY A 62  ? ARG A 35  GLY A 62  1 ? 28 
HELX_P HELX_P5  AA5 THR A 66  ? ARG A 89  ? THR A 66  ARG A 89  1 ? 24 
HELX_P HELX_P6  AA6 LYS A 90  ? THR A 117 ? LYS A 90  THR A 117 1 ? 28 
HELX_P HELX_P7  AA7 SER A 122 ? GLU A 146 ? SER A 122 GLU A 146 1 ? 25 
HELX_P HELX_P8  AA8 LYS A 151 ? TRP A 169 ? LYS A 151 TRP A 169 1 ? 19 
HELX_P HELX_P9  AA9 ILE A 170 ? GLY A 182 ? ILE A 170 GLY A 182 1 ? 13 
HELX_P HELX_P10 AB1 PHE A 184 ? SER A 215 ? PHE A 184 SER A 215 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            200 
_struct_conn.ptnr1_label_atom_id           NZ 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           P 
_struct_conn.ptnr2_label_comp_id           RET 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             200 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            RET 
_struct_conn.ptnr2_auth_seq_id             515 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.448 
_struct_conn.pdbx_value_order              sing 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      RET 
_pdbx_modification_feature.label_asym_id                      P 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     LYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      200 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       RET 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        515 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      LYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       200 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C15 
_pdbx_modification_feature.modified_residue_id_linking_atom   NZ 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        RET 
_pdbx_modification_feature.type                               Retinoylation 
_pdbx_modification_feature.category                           Lipid/lipid-like 
# 
_pdbx_entry_details.entry_id                   8RSS 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLU 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     148 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    B 
_pdbx_validate_torsion.phi             -55.33 
_pdbx_validate_torsion.psi             103.24 
# 
_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     692 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   Q 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z   
2 -x,y,-z 
# 
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 VAL 219 ? A VAL 219 
2 1 Y 1 A SER 220 ? A SER 220 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LFA C1   C N N 205 
LFA C2   C N N 206 
LFA C3   C N N 207 
LFA C4   C N N 208 
LFA C5   C N N 209 
LFA C6   C N N 210 
LFA C7   C N N 211 
LFA C8   C N N 212 
LFA C9   C N N 213 
LFA C10  C N N 214 
LFA C11  C N N 215 
LFA C12  C N N 216 
LFA C13  C N N 217 
LFA C14  C N N 218 
LFA C15  C N N 219 
LFA C16  C N N 220 
LFA C17  C N N 221 
LFA C18  C N N 222 
LFA C19  C N N 223 
LFA C20  C N N 224 
LFA H11  H N N 225 
LFA H12  H N N 226 
LFA H13  H N N 227 
LFA H21  H N N 228 
LFA H22  H N N 229 
LFA H31  H N N 230 
LFA H32  H N N 231 
LFA H41  H N N 232 
LFA H42  H N N 233 
LFA H51  H N N 234 
LFA H52  H N N 235 
LFA H61  H N N 236 
LFA H62  H N N 237 
LFA H71  H N N 238 
LFA H72  H N N 239 
LFA H81  H N N 240 
LFA H82  H N N 241 
LFA H91  H N N 242 
LFA H92  H N N 243 
LFA H101 H N N 244 
LFA H102 H N N 245 
LFA H111 H N N 246 
LFA H112 H N N 247 
LFA H121 H N N 248 
LFA H122 H N N 249 
LFA H131 H N N 250 
LFA H132 H N N 251 
LFA H141 H N N 252 
LFA H142 H N N 253 
LFA H151 H N N 254 
LFA H152 H N N 255 
LFA H161 H N N 256 
LFA H162 H N N 257 
LFA H171 H N N 258 
LFA H172 H N N 259 
LFA H181 H N N 260 
LFA H182 H N N 261 
LFA H191 H N N 262 
LFA H192 H N N 263 
LFA H201 H N N 264 
LFA H202 H N N 265 
LFA H203 H N N 266 
LYS N    N N N 267 
LYS CA   C N S 268 
LYS C    C N N 269 
LYS O    O N N 270 
LYS CB   C N N 271 
LYS CG   C N N 272 
LYS CD   C N N 273 
LYS CE   C N N 274 
LYS NZ   N N N 275 
LYS OXT  O N N 276 
LYS H    H N N 277 
LYS H2   H N N 278 
LYS HA   H N N 279 
LYS HB2  H N N 280 
LYS HB3  H N N 281 
LYS HG2  H N N 282 
LYS HG3  H N N 283 
LYS HD2  H N N 284 
LYS HD3  H N N 285 
LYS HE2  H N N 286 
LYS HE3  H N N 287 
LYS HZ1  H N N 288 
LYS HZ2  H N N 289 
LYS HZ3  H N N 290 
LYS HXT  H N N 291 
MET N    N N N 292 
MET CA   C N S 293 
MET C    C N N 294 
MET O    O N N 295 
MET CB   C N N 296 
MET CG   C N N 297 
MET SD   S N N 298 
MET CE   C N N 299 
MET OXT  O N N 300 
MET H    H N N 301 
MET H2   H N N 302 
MET HA   H N N 303 
MET HB2  H N N 304 
MET HB3  H N N 305 
MET HG2  H N N 306 
MET HG3  H N N 307 
MET HE1  H N N 308 
MET HE2  H N N 309 
MET HE3  H N N 310 
MET HXT  H N N 311 
OLA C1   C N N 312 
OLA O1   O N N 313 
OLA O2   O N N 314 
OLA C2   C N N 315 
OLA C3   C N N 316 
OLA C4   C N N 317 
OLA C5   C N N 318 
OLA C6   C N N 319 
OLA C7   C N N 320 
OLA C8   C N N 321 
OLA C9   C N N 322 
OLA C10  C N N 323 
OLA C11  C N N 324 
OLA C12  C N N 325 
OLA C13  C N N 326 
OLA C14  C N N 327 
OLA C15  C N N 328 
OLA C16  C N N 329 
OLA C17  C N N 330 
OLA C18  C N N 331 
OLA HO2  H N N 332 
OLA H21  H N N 333 
OLA H22  H N N 334 
OLA H31  H N N 335 
OLA H32  H N N 336 
OLA H41  H N N 337 
OLA H42  H N N 338 
OLA H51  H N N 339 
OLA H52  H N N 340 
OLA H61  H N N 341 
OLA H62  H N N 342 
OLA H71  H N N 343 
OLA H72  H N N 344 
OLA H81  H N N 345 
OLA H82  H N N 346 
OLA H9   H N N 347 
OLA H10  H N N 348 
OLA H111 H N N 349 
OLA H112 H N N 350 
OLA H121 H N N 351 
OLA H122 H N N 352 
OLA H131 H N N 353 
OLA H132 H N N 354 
OLA H141 H N N 355 
OLA H142 H N N 356 
OLA H151 H N N 357 
OLA H152 H N N 358 
OLA H161 H N N 359 
OLA H162 H N N 360 
OLA H171 H N N 361 
OLA H172 H N N 362 
OLA H181 H N N 363 
OLA H182 H N N 364 
OLA H183 H N N 365 
PHE N    N N N 366 
PHE CA   C N S 367 
PHE C    C N N 368 
PHE O    O N N 369 
PHE CB   C N N 370 
PHE CG   C Y N 371 
PHE CD1  C Y N 372 
PHE CD2  C Y N 373 
PHE CE1  C Y N 374 
PHE CE2  C Y N 375 
PHE CZ   C Y N 376 
PHE OXT  O N N 377 
PHE H    H N N 378 
PHE H2   H N N 379 
PHE HA   H N N 380 
PHE HB2  H N N 381 
PHE HB3  H N N 382 
PHE HD1  H N N 383 
PHE HD2  H N N 384 
PHE HE1  H N N 385 
PHE HE2  H N N 386 
PHE HZ   H N N 387 
PHE HXT  H N N 388 
PRO N    N N N 389 
PRO CA   C N S 390 
PRO C    C N N 391 
PRO O    O N N 392 
PRO CB   C N N 393 
PRO CG   C N N 394 
PRO CD   C N N 395 
PRO OXT  O N N 396 
PRO H    H N N 397 
PRO HA   H N N 398 
PRO HB2  H N N 399 
PRO HB3  H N N 400 
PRO HG2  H N N 401 
PRO HG3  H N N 402 
PRO HD2  H N N 403 
PRO HD3  H N N 404 
PRO HXT  H N N 405 
RET C1   C N N 406 
RET C2   C N N 407 
RET C3   C N N 408 
RET C4   C N N 409 
RET C5   C N N 410 
RET C6   C N N 411 
RET C7   C N N 412 
RET C8   C N N 413 
RET C9   C N N 414 
RET C10  C N N 415 
RET C11  C N N 416 
RET C12  C N N 417 
RET C13  C N N 418 
RET C14  C N N 419 
RET C15  C N N 420 
RET O1   O N N 421 
RET C16  C N N 422 
RET C17  C N N 423 
RET C18  C N N 424 
RET C19  C N N 425 
RET C20  C N N 426 
RET H21  H N N 427 
RET H22  H N N 428 
RET H31  H N N 429 
RET H32  H N N 430 
RET H41  H N N 431 
RET H42  H N N 432 
RET H7   H N N 433 
RET H8   H N N 434 
RET H10  H N N 435 
RET H11  H N N 436 
RET H12  H N N 437 
RET H14  H N N 438 
RET H15  H N N 439 
RET H161 H N N 440 
RET H162 H N N 441 
RET H163 H N N 442 
RET H171 H N N 443 
RET H172 H N N 444 
RET H173 H N N 445 
RET H181 H N N 446 
RET H182 H N N 447 
RET H183 H N N 448 
RET H191 H N N 449 
RET H192 H N N 450 
RET H193 H N N 451 
RET H201 H N N 452 
RET H202 H N N 453 
RET H203 H N N 454 
SER N    N N N 455 
SER CA   C N S 456 
SER C    C N N 457 
SER O    O N N 458 
SER CB   C N N 459 
SER OG   O N N 460 
SER OXT  O N N 461 
SER H    H N N 462 
SER H2   H N N 463 
SER HA   H N N 464 
SER HB2  H N N 465 
SER HB3  H N N 466 
SER HG   H N N 467 
SER HXT  H N N 468 
THR N    N N N 469 
THR CA   C N S 470 
THR C    C N N 471 
THR O    O N N 472 
THR CB   C N R 473 
THR OG1  O N N 474 
THR CG2  C N N 475 
THR OXT  O N N 476 
THR H    H N N 477 
THR H2   H N N 478 
THR HA   H N N 479 
THR HB   H N N 480 
THR HG1  H N N 481 
THR HG21 H N N 482 
THR HG22 H N N 483 
THR HG23 H N N 484 
THR HXT  H N N 485 
TRP N    N N N 486 
TRP CA   C N S 487 
TRP C    C N N 488 
TRP O    O N N 489 
TRP CB   C N N 490 
TRP CG   C Y N 491 
TRP CD1  C Y N 492 
TRP CD2  C Y N 493 
TRP NE1  N Y N 494 
TRP CE2  C Y N 495 
TRP CE3  C Y N 496 
TRP CZ2  C Y N 497 
TRP CZ3  C Y N 498 
TRP CH2  C Y N 499 
TRP OXT  O N N 500 
TRP H    H N N 501 
TRP H2   H N N 502 
TRP HA   H N N 503 
TRP HB2  H N N 504 
TRP HB3  H N N 505 
TRP HD1  H N N 506 
TRP HE1  H N N 507 
TRP HE3  H N N 508 
TRP HZ2  H N N 509 
TRP HZ3  H N N 510 
TRP HH2  H N N 511 
TRP HXT  H N N 512 
TYR N    N N N 513 
TYR CA   C N S 514 
TYR C    C N N 515 
TYR O    O N N 516 
TYR CB   C N N 517 
TYR CG   C Y N 518 
TYR CD1  C Y N 519 
TYR CD2  C Y N 520 
TYR CE1  C Y N 521 
TYR CE2  C Y N 522 
TYR CZ   C Y N 523 
TYR OH   O N N 524 
TYR OXT  O N N 525 
TYR H    H N N 526 
TYR H2   H N N 527 
TYR HA   H N N 528 
TYR HB2  H N N 529 
TYR HB3  H N N 530 
TYR HD1  H N N 531 
TYR HD2  H N N 532 
TYR HE1  H N N 533 
TYR HE2  H N N 534 
TYR HH   H N N 535 
TYR HXT  H N N 536 
VAL N    N N N 537 
VAL CA   C N S 538 
VAL C    C N N 539 
VAL O    O N N 540 
VAL CB   C N N 541 
VAL CG1  C N N 542 
VAL CG2  C N N 543 
VAL OXT  O N N 544 
VAL H    H N N 545 
VAL H2   H N N 546 
VAL HA   H N N 547 
VAL HB   H N N 548 
VAL HG11 H N N 549 
VAL HG12 H N N 550 
VAL HG13 H N N 551 
VAL HG21 H N N 552 
VAL HG22 H N N 553 
VAL HG23 H N N 554 
VAL HXT  H N N 555 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LFA C1  C2   sing N N 194 
LFA C1  H11  sing N N 195 
LFA C1  H12  sing N N 196 
LFA C1  H13  sing N N 197 
LFA C2  C3   sing N N 198 
LFA C2  H21  sing N N 199 
LFA C2  H22  sing N N 200 
LFA C3  C4   sing N N 201 
LFA C3  H31  sing N N 202 
LFA C3  H32  sing N N 203 
LFA C4  C5   sing N N 204 
LFA C4  H41  sing N N 205 
LFA C4  H42  sing N N 206 
LFA C5  C6   sing N N 207 
LFA C5  H51  sing N N 208 
LFA C5  H52  sing N N 209 
LFA C6  C7   sing N N 210 
LFA C6  H61  sing N N 211 
LFA C6  H62  sing N N 212 
LFA C7  C8   sing N N 213 
LFA C7  H71  sing N N 214 
LFA C7  H72  sing N N 215 
LFA C8  C9   sing N N 216 
LFA C8  H81  sing N N 217 
LFA C8  H82  sing N N 218 
LFA C9  C10  sing N N 219 
LFA C9  H91  sing N N 220 
LFA C9  H92  sing N N 221 
LFA C10 C11  sing N N 222 
LFA C10 H101 sing N N 223 
LFA C10 H102 sing N N 224 
LFA C11 C12  sing N N 225 
LFA C11 H111 sing N N 226 
LFA C11 H112 sing N N 227 
LFA C12 C13  sing N N 228 
LFA C12 H121 sing N N 229 
LFA C12 H122 sing N N 230 
LFA C13 C14  sing N N 231 
LFA C13 H131 sing N N 232 
LFA C13 H132 sing N N 233 
LFA C14 C15  sing N N 234 
LFA C14 H141 sing N N 235 
LFA C14 H142 sing N N 236 
LFA C15 C16  sing N N 237 
LFA C15 H151 sing N N 238 
LFA C15 H152 sing N N 239 
LFA C16 C17  sing N N 240 
LFA C16 H161 sing N N 241 
LFA C16 H162 sing N N 242 
LFA C17 C18  sing N N 243 
LFA C17 H171 sing N N 244 
LFA C17 H172 sing N N 245 
LFA C18 C19  sing N N 246 
LFA C18 H181 sing N N 247 
LFA C18 H182 sing N N 248 
LFA C19 C20  sing N N 249 
LFA C19 H191 sing N N 250 
LFA C19 H192 sing N N 251 
LFA C20 H201 sing N N 252 
LFA C20 H202 sing N N 253 
LFA C20 H203 sing N N 254 
LYS N   CA   sing N N 255 
LYS N   H    sing N N 256 
LYS N   H2   sing N N 257 
LYS CA  C    sing N N 258 
LYS CA  CB   sing N N 259 
LYS CA  HA   sing N N 260 
LYS C   O    doub N N 261 
LYS C   OXT  sing N N 262 
LYS CB  CG   sing N N 263 
LYS CB  HB2  sing N N 264 
LYS CB  HB3  sing N N 265 
LYS CG  CD   sing N N 266 
LYS CG  HG2  sing N N 267 
LYS CG  HG3  sing N N 268 
LYS CD  CE   sing N N 269 
LYS CD  HD2  sing N N 270 
LYS CD  HD3  sing N N 271 
LYS CE  NZ   sing N N 272 
LYS CE  HE2  sing N N 273 
LYS CE  HE3  sing N N 274 
LYS NZ  HZ1  sing N N 275 
LYS NZ  HZ2  sing N N 276 
LYS NZ  HZ3  sing N N 277 
LYS OXT HXT  sing N N 278 
MET N   CA   sing N N 279 
MET N   H    sing N N 280 
MET N   H2   sing N N 281 
MET CA  C    sing N N 282 
MET CA  CB   sing N N 283 
MET CA  HA   sing N N 284 
MET C   O    doub N N 285 
MET C   OXT  sing N N 286 
MET CB  CG   sing N N 287 
MET CB  HB2  sing N N 288 
MET CB  HB3  sing N N 289 
MET CG  SD   sing N N 290 
MET CG  HG2  sing N N 291 
MET CG  HG3  sing N N 292 
MET SD  CE   sing N N 293 
MET CE  HE1  sing N N 294 
MET CE  HE2  sing N N 295 
MET CE  HE3  sing N N 296 
MET OXT HXT  sing N N 297 
OLA C1  O1   doub N N 298 
OLA C1  O2   sing N N 299 
OLA C1  C2   sing N N 300 
OLA O2  HO2  sing N N 301 
OLA C2  C3   sing N N 302 
OLA C2  H21  sing N N 303 
OLA C2  H22  sing N N 304 
OLA C3  C4   sing N N 305 
OLA C3  H31  sing N N 306 
OLA C3  H32  sing N N 307 
OLA C4  C5   sing N N 308 
OLA C4  H41  sing N N 309 
OLA C4  H42  sing N N 310 
OLA C5  C6   sing N N 311 
OLA C5  H51  sing N N 312 
OLA C5  H52  sing N N 313 
OLA C6  C7   sing N N 314 
OLA C6  H61  sing N N 315 
OLA C6  H62  sing N N 316 
OLA C7  C8   sing N N 317 
OLA C7  H71  sing N N 318 
OLA C7  H72  sing N N 319 
OLA C8  C9   sing N N 320 
OLA C8  H81  sing N N 321 
OLA C8  H82  sing N N 322 
OLA C9  C10  doub N Z 323 
OLA C9  H9   sing N N 324 
OLA C10 C11  sing N N 325 
OLA C10 H10  sing N N 326 
OLA C11 C12  sing N N 327 
OLA C11 H111 sing N N 328 
OLA C11 H112 sing N N 329 
OLA C12 C13  sing N N 330 
OLA C12 H121 sing N N 331 
OLA C12 H122 sing N N 332 
OLA C13 C14  sing N N 333 
OLA C13 H131 sing N N 334 
OLA C13 H132 sing N N 335 
OLA C14 C15  sing N N 336 
OLA C14 H141 sing N N 337 
OLA C14 H142 sing N N 338 
OLA C15 C16  sing N N 339 
OLA C15 H151 sing N N 340 
OLA C15 H152 sing N N 341 
OLA C16 C17  sing N N 342 
OLA C16 H161 sing N N 343 
OLA C16 H162 sing N N 344 
OLA C17 C18  sing N N 345 
OLA C17 H171 sing N N 346 
OLA C17 H172 sing N N 347 
OLA C18 H181 sing N N 348 
OLA C18 H182 sing N N 349 
OLA C18 H183 sing N N 350 
PHE N   CA   sing N N 351 
PHE N   H    sing N N 352 
PHE N   H2   sing N N 353 
PHE CA  C    sing N N 354 
PHE CA  CB   sing N N 355 
PHE CA  HA   sing N N 356 
PHE C   O    doub N N 357 
PHE C   OXT  sing N N 358 
PHE CB  CG   sing N N 359 
PHE CB  HB2  sing N N 360 
PHE CB  HB3  sing N N 361 
PHE CG  CD1  doub Y N 362 
PHE CG  CD2  sing Y N 363 
PHE CD1 CE1  sing Y N 364 
PHE CD1 HD1  sing N N 365 
PHE CD2 CE2  doub Y N 366 
PHE CD2 HD2  sing N N 367 
PHE CE1 CZ   doub Y N 368 
PHE CE1 HE1  sing N N 369 
PHE CE2 CZ   sing Y N 370 
PHE CE2 HE2  sing N N 371 
PHE CZ  HZ   sing N N 372 
PHE OXT HXT  sing N N 373 
PRO N   CA   sing N N 374 
PRO N   CD   sing N N 375 
PRO N   H    sing N N 376 
PRO CA  C    sing N N 377 
PRO CA  CB   sing N N 378 
PRO CA  HA   sing N N 379 
PRO C   O    doub N N 380 
PRO C   OXT  sing N N 381 
PRO CB  CG   sing N N 382 
PRO CB  HB2  sing N N 383 
PRO CB  HB3  sing N N 384 
PRO CG  CD   sing N N 385 
PRO CG  HG2  sing N N 386 
PRO CG  HG3  sing N N 387 
PRO CD  HD2  sing N N 388 
PRO CD  HD3  sing N N 389 
PRO OXT HXT  sing N N 390 
RET C1  C2   sing N N 391 
RET C1  C6   sing N N 392 
RET C1  C16  sing N N 393 
RET C1  C17  sing N N 394 
RET C2  C3   sing N N 395 
RET C2  H21  sing N N 396 
RET C2  H22  sing N N 397 
RET C3  C4   sing N N 398 
RET C3  H31  sing N N 399 
RET C3  H32  sing N N 400 
RET C4  C5   sing N N 401 
RET C4  H41  sing N N 402 
RET C4  H42  sing N N 403 
RET C5  C6   doub N N 404 
RET C5  C18  sing N N 405 
RET C6  C7   sing N N 406 
RET C7  C8   doub N E 407 
RET C7  H7   sing N N 408 
RET C8  C9   sing N N 409 
RET C8  H8   sing N N 410 
RET C9  C10  doub N E 411 
RET C9  C19  sing N N 412 
RET C10 C11  sing N N 413 
RET C10 H10  sing N N 414 
RET C11 C12  doub N E 415 
RET C11 H11  sing N N 416 
RET C12 C13  sing N N 417 
RET C12 H12  sing N N 418 
RET C13 C14  doub N E 419 
RET C13 C20  sing N N 420 
RET C14 C15  sing N N 421 
RET C14 H14  sing N N 422 
RET C15 O1   doub N N 423 
RET C15 H15  sing N N 424 
RET C16 H161 sing N N 425 
RET C16 H162 sing N N 426 
RET C16 H163 sing N N 427 
RET C17 H171 sing N N 428 
RET C17 H172 sing N N 429 
RET C17 H173 sing N N 430 
RET C18 H181 sing N N 431 
RET C18 H182 sing N N 432 
RET C18 H183 sing N N 433 
RET C19 H191 sing N N 434 
RET C19 H192 sing N N 435 
RET C19 H193 sing N N 436 
RET C20 H201 sing N N 437 
RET C20 H202 sing N N 438 
RET C20 H203 sing N N 439 
SER N   CA   sing N N 440 
SER N   H    sing N N 441 
SER N   H2   sing N N 442 
SER CA  C    sing N N 443 
SER CA  CB   sing N N 444 
SER CA  HA   sing N N 445 
SER C   O    doub N N 446 
SER C   OXT  sing N N 447 
SER CB  OG   sing N N 448 
SER CB  HB2  sing N N 449 
SER CB  HB3  sing N N 450 
SER OG  HG   sing N N 451 
SER OXT HXT  sing N N 452 
THR N   CA   sing N N 453 
THR N   H    sing N N 454 
THR N   H2   sing N N 455 
THR CA  C    sing N N 456 
THR CA  CB   sing N N 457 
THR CA  HA   sing N N 458 
THR C   O    doub N N 459 
THR C   OXT  sing N N 460 
THR CB  OG1  sing N N 461 
THR CB  CG2  sing N N 462 
THR CB  HB   sing N N 463 
THR OG1 HG1  sing N N 464 
THR CG2 HG21 sing N N 465 
THR CG2 HG22 sing N N 466 
THR CG2 HG23 sing N N 467 
THR OXT HXT  sing N N 468 
TRP N   CA   sing N N 469 
TRP N   H    sing N N 470 
TRP N   H2   sing N N 471 
TRP CA  C    sing N N 472 
TRP CA  CB   sing N N 473 
TRP CA  HA   sing N N 474 
TRP C   O    doub N N 475 
TRP C   OXT  sing N N 476 
TRP CB  CG   sing N N 477 
TRP CB  HB2  sing N N 478 
TRP CB  HB3  sing N N 479 
TRP CG  CD1  doub Y N 480 
TRP CG  CD2  sing Y N 481 
TRP CD1 NE1  sing Y N 482 
TRP CD1 HD1  sing N N 483 
TRP CD2 CE2  doub Y N 484 
TRP CD2 CE3  sing Y N 485 
TRP NE1 CE2  sing Y N 486 
TRP NE1 HE1  sing N N 487 
TRP CE2 CZ2  sing Y N 488 
TRP CE3 CZ3  doub Y N 489 
TRP CE3 HE3  sing N N 490 
TRP CZ2 CH2  doub Y N 491 
TRP CZ2 HZ2  sing N N 492 
TRP CZ3 CH2  sing Y N 493 
TRP CZ3 HZ3  sing N N 494 
TRP CH2 HH2  sing N N 495 
TRP OXT HXT  sing N N 496 
TYR N   CA   sing N N 497 
TYR N   H    sing N N 498 
TYR N   H2   sing N N 499 
TYR CA  C    sing N N 500 
TYR CA  CB   sing N N 501 
TYR CA  HA   sing N N 502 
TYR C   O    doub N N 503 
TYR C   OXT  sing N N 504 
TYR CB  CG   sing N N 505 
TYR CB  HB2  sing N N 506 
TYR CB  HB3  sing N N 507 
TYR CG  CD1  doub Y N 508 
TYR CG  CD2  sing Y N 509 
TYR CD1 CE1  sing Y N 510 
TYR CD1 HD1  sing N N 511 
TYR CD2 CE2  doub Y N 512 
TYR CD2 HD2  sing N N 513 
TYR CE1 CZ   doub Y N 514 
TYR CE1 HE1  sing N N 515 
TYR CE2 CZ   sing Y N 516 
TYR CE2 HE2  sing N N 517 
TYR CZ  OH   sing N N 518 
TYR OH  HH   sing N N 519 
TYR OXT HXT  sing N N 520 
VAL N   CA   sing N N 521 
VAL N   H    sing N N 522 
VAL N   H2   sing N N 523 
VAL CA  C    sing N N 524 
VAL CA  CB   sing N N 525 
VAL CA  HA   sing N N 526 
VAL C   O    doub N N 527 
VAL C   OXT  sing N N 528 
VAL CB  CG1  sing N N 529 
VAL CB  CG2  sing N N 530 
VAL CB  HB   sing N N 531 
VAL CG1 HG11 sing N N 532 
VAL CG1 HG12 sing N N 533 
VAL CG1 HG13 sing N N 534 
VAL CG2 HG21 sing N N 535 
VAL CG2 HG22 sing N N 536 
VAL CG2 HG23 sing N N 537 
VAL OXT HXT  sing N N 538 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5JSI 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 2 1' 
_space_group.name_Hall        'P 2y' 
_space_group.IT_number        3 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8RSS 
_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]   0.019760 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003920 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024892 
_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]   0.016905 
_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.
;
? 
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 
ATOM   1    N N   . MET A 1 1   ? 35.34358  -2.03576  33.50070 1.000 33.11229 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 34.47091  -1.71752  32.37607 1.000 35.01694 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 34.96659  -2.33532  31.07031 1.000 29.73584 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 34.16344  -2.70922  30.21858 1.000 26.97132 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 34.32009  -0.20227  32.21850 1.000 40.71231 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 33.48525  0.45372   33.30202 1.000 42.57210 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 33.48701  2.25009   33.17483 1.000 42.82755 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 35.23106  2.60251   33.37634 1.000 43.32101 ? 1   MET A CE  1 
ATOM   9    N N   . GLU A 1 2   ? 36.29155  -2.44165  30.92156 1.000 27.26288 ? 2   GLU A N   1 
ATOM   10   C CA  . GLU A 1 2   ? 36.86262  -2.94390  29.67345 1.000 26.31407 ? 2   GLU A CA  1 
ATOM   11   C C   . GLU A 1 2   ? 36.51016  -4.40940  29.44575 1.000 24.78408 ? 2   GLU A C   1 
ATOM   12   O O   . GLU A 1 2   ? 36.12856  -4.79804  28.33438 1.000 23.45542 ? 2   GLU A O   1 
ATOM   13   C CB  . GLU A 1 2   ? 38.37899  -2.74678  29.67062 1.000 28.13072 ? 2   GLU A CB  1 
ATOM   14   N N   . GLU A 1 3   ? 36.63844  -5.23758  30.48338 1.000 24.58043 ? 3   GLU A N   1 
ATOM   15   C CA  . GLU A 1 3   ? 36.29705  -6.64832  30.34608 1.000 23.92770 ? 3   GLU A CA  1 
ATOM   16   C C   . GLU A 1 3   ? 34.80007  -6.83196  30.13211 1.000 23.08543 ? 3   GLU A C   1 
ATOM   17   O O   . GLU A 1 3   ? 34.38200  -7.64411  29.29983 1.000 23.99636 ? 3   GLU A O   1 
ATOM   18   C CB  . GLU A 1 3   ? 36.77528  -7.42675  31.57171 1.000 23.77401 ? 3   GLU A CB  1 
ATOM   19   C CG  . GLU A 1 3   ? 36.45013  -8.91292  31.52637 1.000 24.86731 ? 3   GLU A CG  1 
ATOM   20   N N   . LEU A 1 4   ? 33.98002  -6.08163  30.87204 1.000 22.76364 ? 4   LEU A N   1 
ATOM   21   C CA  . LEU A 1 4   ? 32.53568  -6.13440  30.66988 1.000 20.77545 ? 4   LEU A CA  1 
ATOM   22   C C   . LEU A 1 4   ? 32.16704  -5.77548  29.23705 1.000 17.18859 ? 4   LEU A C   1 
ATOM   23   O O   . LEU A 1 4   ? 31.27418  -6.39301  28.64421 1.000 16.00229 ? 4   LEU A O   1 
ATOM   24   C CB  . LEU A 1 4   ? 31.83694  -5.18463  31.64223 1.000 23.39649 ? 4   LEU A CB  1 
ATOM   25   C CG  . LEU A 1 4   ? 30.36735  -4.88457  31.32894 1.000 23.91500 ? 4   LEU A CG  1 
ATOM   26   C CD1 . LEU A 1 4   ? 29.50648  -6.11986  31.53348 1.000 24.46726 ? 4   LEU A CD1 1 
ATOM   27   C CD2 . LEU A 1 4   ? 29.85522  -3.72206  32.16532 1.000 25.67890 ? 4   LEU A CD2 1 
ATOM   28   N N   . THR A 1 5   ? 32.84665  -4.77711  28.66544 1.000 15.23937 ? 5   THR A N   1 
ATOM   29   C CA  . THR A 1 5   ? 32.54466  -4.35735  27.30170 1.000 14.23895 ? 5   THR A CA  1 
ATOM   30   C C   . THR A 1 5   ? 32.88858  -5.45242  26.30021 1.000 12.23303 ? 5   THR A C   1 
ATOM   31   O O   . THR A 1 5   ? 32.10696  -5.73029  25.38374 1.000 12.37727 ? 5   THR A O   1 
ATOM   32   C CB  . THR A 1 5   ? 33.29036  -3.06172  26.98317 1.000 13.88482 ? 5   THR A CB  1 
ATOM   33   O OG1 . THR A 1 5   ? 32.88441  -2.03932  27.90315 1.000 15.56751 ? 5   THR A OG1 1 
ATOM   34   C CG2 . THR A 1 5   ? 32.99152  -2.60742  25.56533 1.000 12.81592 ? 5   THR A CG2 1 
ATOM   35   N N   . TYR A 1 6   ? 34.04076  -6.10094  26.47336 1.000 14.09869 ? 6   TYR A N   1 
ATOM   36   C CA  . TYR A 1 6   ? 34.40846  -7.20806  25.59393 1.000 16.07699 ? 6   TYR A CA  1 
ATOM   37   C C   . TYR A 1 6   ? 33.39591  -8.34444  25.67217 1.000 17.40548 ? 6   TYR A C   1 
ATOM   38   O O   . TYR A 1 6   ? 32.96288  -8.87904  24.64222 1.000 15.72295 ? 6   TYR A O   1 
ATOM   39   C CB  . TYR A 1 6   ? 35.80183  -7.71817  25.95203 1.000 17.85387 ? 6   TYR A CB  1 
ATOM   40   C CG  . TYR A 1 6   ? 36.15344  -9.00826  25.25100 1.000 22.13750 ? 6   TYR A CG  1 
ATOM   41   C CD1 . TYR A 1 6   ? 36.45626  -9.02270  23.89610 1.000 24.79905 ? 6   TYR A CD1 1 
ATOM   42   C CD2 . TYR A 1 6   ? 36.16989  -10.21295 25.93923 1.000 24.29726 ? 6   TYR A CD2 1 
ATOM   43   C CE1 . TYR A 1 6   ? 36.77511  -10.20218 23.24590 1.000 26.69878 ? 6   TYR A CE1 1 
ATOM   44   C CE2 . TYR A 1 6   ? 36.48748  -11.39770 25.29762 1.000 27.30016 ? 6   TYR A CE2 1 
ATOM   45   C CZ  . TYR A 1 6   ? 36.78954  -11.38463 23.95208 1.000 28.61247 ? 6   TYR A CZ  1 
ATOM   46   O OH  . TYR A 1 6   ? 37.10429  -12.55954 23.30894 1.000 33.12376 ? 6   TYR A OH  1 
ATOM   47   N N   A ARG A 1 7   ? 33.00828  -8.73023  26.89107 0.500 17.60824 ? 7   ARG A N   1 
ATOM   48   N N   B ARG A 1 7   ? 33.01086  -8.73229  26.89111 0.500 17.63733 ? 7   ARG A N   1 
ATOM   49   C CA  A ARG A 1 7   ? 32.06237  -9.82987  27.05653 0.500 18.86710 ? 7   ARG A CA  1 
ATOM   50   C CA  B ARG A 1 7   ? 32.06336  -9.83059  27.05535 0.500 18.96166 ? 7   ARG A CA  1 
ATOM   51   C C   A ARG A 1 7   ? 30.72265  -9.51022  26.40761 0.500 17.25440 ? 7   ARG A C   1 
ATOM   52   C C   B ARG A 1 7   ? 30.72526  -9.50970  26.40387 0.500 17.29030 ? 7   ARG A C   1 
ATOM   53   O O   A ARG A 1 7   ? 30.09090  -10.38677 25.80570 0.500 16.44774 ? 7   ARG A O   1 
ATOM   54   O O   B ARG A 1 7   ? 30.09685  -10.38498 25.79672 0.500 16.47199 ? 7   ARG A O   1 
ATOM   55   C CB  A ARG A 1 7   ? 31.87857  -10.14233 28.54141 0.500 21.87843 ? 7   ARG A CB  1 
ATOM   56   C CB  B ARG A 1 7   ? 31.87595  -10.14469 28.53950 0.500 22.10967 ? 7   ARG A CB  1 
ATOM   57   C CG  A ARG A 1 7   ? 33.11435  -10.71821 29.20956 0.500 27.35686 ? 7   ARG A CG  1 
ATOM   58   C CG  B ARG A 1 7   ? 33.08232  -10.79485 29.19203 0.500 27.65420 ? 7   ARG A CG  1 
ATOM   59   C CD  . ARG A 1 7   ? 32.86516  -10.97398 30.68687 1.000 32.37865 ? 7   ARG A CD  1 
ATOM   60   N NE  . ARG A 1 7   ? 33.99425  -11.63951 31.32591 1.000 34.96139 ? 7   ARG A NE  1 
ATOM   61   C CZ  . ARG A 1 7   ? 34.09590  -12.95211 31.48684 1.000 41.80873 ? 7   ARG A CZ  1 
ATOM   62   N N   . LEU A 1 8   ? 30.27299  -8.25827  26.51557 1.000 15.84988 ? 8   LEU A N   1 
ATOM   63   C CA  . LEU A 1 8   ? 29.00795  -7.88197  25.89412 1.000 14.81803 ? 8   LEU A CA  1 
ATOM   64   C C   . LEU A 1 8   ? 29.10225  -7.93592  24.37401 1.000 14.74499 ? 8   LEU A C   1 
ATOM   65   O O   . LEU A 1 8   ? 28.14478  -8.33758  23.70852 1.000 13.71000 ? 8   LEU A O   1 
ATOM   66   C CB  . LEU A 1 8   ? 28.54881  -6.50619  26.38041 1.000 16.24528 ? 8   LEU A CB  1 
ATOM   67   C CG  . LEU A 1 8   ? 28.02130  -6.45895  27.81853 1.000 20.20245 ? 8   LEU A CG  1 
ATOM   68   C CD1 . LEU A 1 8   ? 27.65284  -5.03818  28.21710 1.000 21.40102 ? 8   LEU A CD1 1 
ATOM   69   C CD2 . LEU A 1 8   ? 26.82746  -7.38930  27.98728 1.000 25.45285 ? 8   LEU A CD2 1 
ATOM   70   N N   . PHE A 1 9   ? 30.24739  -7.54478  23.80713 1.000 13.04719 ? 9   PHE A N   1 
ATOM   71   C CA  . PHE A 1 9   ? 30.45610  -7.71259  22.36994 1.000 12.80362 ? 9   PHE A CA  1 
ATOM   72   C C   . PHE A 1 9   ? 30.32929  -9.18064  21.97421 1.000 13.76544 ? 9   PHE A C   1 
ATOM   73   O O   . PHE A 1 9   ? 29.65711  -9.51764  20.99235 1.000 14.09458 ? 9   PHE A O   1 
ATOM   74   C CB  . PHE A 1 9   ? 31.83527  -7.17760  21.96615 1.000 11.39085 ? 9   PHE A CB  1 
ATOM   75   C CG  . PHE A 1 9   ? 31.86619  -5.70060  21.63331 1.000 9.75565  ? 9   PHE A CG  1 
ATOM   76   C CD1 . PHE A 1 9   ? 30.94082  -5.13840  20.76904 1.000 10.41233 ? 9   PHE A CD1 1 
ATOM   77   C CD2 . PHE A 1 9   ? 32.84372  -4.87910  22.17209 1.000 10.02872 ? 9   PHE A CD2 1 
ATOM   78   C CE1 . PHE A 1 9   ? 30.98610  -3.78143  20.45822 1.000 10.86337 ? 9   PHE A CE1 1 
ATOM   79   C CE2 . PHE A 1 9   ? 32.88840  -3.52132  21.86661 1.000 10.94152 ? 9   PHE A CE2 1 
ATOM   80   C CZ  . PHE A 1 9   ? 31.95784  -2.97526  21.01066 1.000 10.78359 ? 9   PHE A CZ  1 
ATOM   81   N N   A MET A 1 10  ? 30.95633  -10.07454 22.74054 0.500 14.27791 ? 10  MET A N   1 
ATOM   82   N N   B MET A 1 10  ? 30.97886  -10.06864 22.73227 0.500 14.07533 ? 10  MET A N   1 
ATOM   83   C CA  A MET A 1 10  ? 30.92875  -11.48981 22.38307 0.500 16.14646 ? 10  MET A CA  1 
ATOM   84   C CA  B MET A 1 10  ? 30.94049  -11.49431 22.41855 0.500 15.42620 ? 10  MET A CA  1 
ATOM   85   C C   A MET A 1 10  ? 29.53571  -12.08521 22.56033 0.500 16.30872 ? 10  MET A C   1 
ATOM   86   C C   B MET A 1 10  ? 29.52343  -12.04194 22.53730 0.500 16.24096 ? 10  MET A C   1 
ATOM   87   O O   A MET A 1 10  ? 29.09158  -12.89244 21.73558 0.500 17.28223 ? 10  MET A O   1 
ATOM   88   O O   B MET A 1 10  ? 29.04995  -12.77130 21.65820 0.500 17.56936 ? 10  MET A O   1 
ATOM   89   C CB  A MET A 1 10  ? 31.97387  -12.26071 23.18967 0.500 19.17842 ? 10  MET A CB  1 
ATOM   90   C CB  B MET A 1 10  ? 31.88838  -12.25849 23.34676 0.500 17.06711 ? 10  MET A CB  1 
ATOM   91   C CG  A MET A 1 10  ? 33.38433  -11.71370 23.03587 0.500 21.71025 ? 10  MET A CG  1 
ATOM   92   C CG  B MET A 1 10  ? 33.33541  -11.78613 23.31508 0.500 18.01468 ? 10  MET A CG  1 
ATOM   93   S SD  A MET A 1 10  ? 33.82838  -11.40713 21.31181 0.500 25.55901 ? 10  MET A SD  1 
ATOM   94   S SD  B MET A 1 10  ? 34.22306  -12.26242 21.82006 0.500 21.73787 ? 10  MET A SD  1 
ATOM   95   N N   . VAL A 1 11  ? 28.83041  -11.69695 23.62488 1.000 15.97967 ? 11  VAL A N   1 
ATOM   96   C CA  . VAL A 1 11  ? 27.46316  -12.17036 23.82079 1.000 16.08840 ? 11  VAL A CA  1 
ATOM   97   C C   . VAL A 1 11  ? 26.54603  -11.61650 22.73743 1.000 14.93186 ? 11  VAL A C   1 
ATOM   98   O O   . VAL A 1 11  ? 25.69823  -12.33468 22.19315 1.000 14.62599 ? 11  VAL A O   1 
ATOM   99   C CB  . VAL A 1 11  ? 26.96490  -11.81414 25.23529 1.000 19.81878 ? 11  VAL A CB  1 
ATOM   100  C CG1 . VAL A 1 11  ? 25.47032  -12.05620 25.34916 1.000 22.14678 ? 11  VAL A CG1 1 
ATOM   101  C CG2 . VAL A 1 11  ? 27.71001  -12.61947 26.28399 1.000 19.52839 ? 11  VAL A CG2 1 
ATOM   102  N N   . ALA A 1 12  ? 26.70618  -10.33406 22.39976 1.000 13.91259 ? 12  ALA A N   1 
ATOM   103  C CA  . ALA A 1 12  ? 25.86345  -9.73517  21.36962 1.000 13.52178 ? 12  ALA A CA  1 
ATOM   104  C C   . ALA A 1 12  ? 26.12279  -10.35427 20.00535 1.000 13.26282 ? 12  ALA A C   1 
ATOM   105  O O   . ALA A 1 12  ? 25.20512  -10.45819 19.18383 1.000 12.31323 ? 12  ALA A O   1 
ATOM   106  C CB  . ALA A 1 12  ? 26.09756  -8.22932  21.30666 1.000 13.01070 ? 12  ALA A CB  1 
ATOM   107  N N   . THR A 1 13  ? 27.36520  -10.75014 19.73985 1.000 13.06690 ? 13  THR A N   1 
ATOM   108  C CA  . THR A 1 13  ? 27.67330  -11.44135 18.49466 1.000 10.95312 ? 13  THR A CA  1 
ATOM   109  C C   . THR A 1 13  ? 26.81695  -12.69401 18.34174 1.000 11.39596 ? 13  THR A C   1 
ATOM   110  O O   . THR A 1 13  ? 26.12753  -12.87477 17.32932 1.000 12.30571 ? 13  THR A O   1 
ATOM   111  C CB  . THR A 1 13  ? 29.15806  -11.79852 18.48446 1.000 11.49975 ? 13  THR A CB  1 
ATOM   112  O OG1 . THR A 1 13  ? 29.94735  -10.59699 18.47106 1.000 12.05163 ? 13  THR A OG1 1 
ATOM   113  C CG2 . THR A 1 13  ? 29.47849  -12.64683 17.29000 1.000 14.24549 ? 13  THR A CG2 1 
ATOM   114  N N   . VAL A 1 14  ? 26.83287  -13.56582 19.35206 1.000 11.29640 ? 14  VAL A N   1 
ATOM   115  C CA  . VAL A 1 14  ? 25.99148  -14.75906 19.31088 1.000 12.23933 ? 14  VAL A CA  1 
ATOM   116  C C   . VAL A 1 14  ? 24.51680  -14.37596 19.31343 1.000 12.70827 ? 14  VAL A C   1 
ATOM   117  O O   . VAL A 1 14  ? 23.68948  -15.04629 18.68197 1.000 12.04475 ? 14  VAL A O   1 
ATOM   118  C CB  . VAL A 1 14  ? 26.35425  -15.71273 20.46678 1.000 13.52995 ? 14  VAL A CB  1 
ATOM   119  C CG1 . VAL A 1 14  ? 25.51640  -16.97983 20.40169 1.000 15.26883 ? 14  VAL A CG1 1 
ATOM   120  C CG2 . VAL A 1 14  ? 27.84022  -16.05034 20.42318 1.000 15.03115 ? 14  VAL A CG2 1 
ATOM   121  N N   . GLY A 1 15  ? 24.16691  -13.28459 19.99994 1.000 11.01773 ? 15  GLY A N   1 
ATOM   122  C CA  . GLY A 1 15  ? 22.78065  -12.84931 20.02174 1.000 11.79113 ? 15  GLY A CA  1 
ATOM   123  C C   . GLY A 1 15  ? 22.26802  -12.45964 18.64930 1.000 12.03810 ? 15  GLY A C   1 
ATOM   124  O O   . GLY A 1 15  ? 21.13396  -12.78821 18.28503 1.000 12.41365 ? 15  GLY A O   1 
ATOM   125  N N   . MET A 1 16  ? 23.09712  -11.75562 17.86680 1.000 13.16925 ? 16  MET A N   1 
ATOM   126  C CA  . MET A 1 16  ? 22.68528  -11.36616 16.52092 1.000 11.20123 ? 16  MET A CA  1 
ATOM   127  C C   . MET A 1 16  ? 22.52025  -12.58210 15.62519 1.000 12.10002 ? 16  MET A C   1 
ATOM   128  O O   . MET A 1 16  ? 21.55714  -12.66309 14.85371 1.000 12.57436 ? 16  MET A O   1 
ATOM   129  C CB  . MET A 1 16  ? 23.69160  -10.39506 15.90783 1.000 11.99332 ? 16  MET A CB  1 
ATOM   130  C CG  . MET A 1 16  ? 23.69621  -9.03015  16.54887 1.000 11.50433 ? 16  MET A CG  1 
ATOM   131  S SD  . MET A 1 16  ? 22.08419  -8.21794  16.48969 1.000 12.77388 ? 16  MET A SD  1 
ATOM   132  C CE  . MET A 1 16  ? 22.51878  -6.63070  17.20043 1.000 12.79660 ? 16  MET A CE  1 
ATOM   133  N N   . LEU A 1 17  ? 23.45530  -13.53148 15.70713 1.000 11.37009 ? 17  LEU A N   1 
ATOM   134  C CA  . LEU A 1 17  ? 23.30625  -14.78246 14.97281 1.000 11.30741 ? 17  LEU A CA  1 
ATOM   135  C C   . LEU A 1 17  ? 22.03298  -15.50604 15.38651 1.000 11.91352 ? 17  LEU A C   1 
ATOM   136  O O   . LEU A 1 17  ? 21.27347  -15.98500 14.53605 1.000 11.47067 ? 17  LEU A O   1 
ATOM   137  C CB  . LEU A 1 17  ? 24.52112  -15.68193 15.20504 1.000 10.30037 ? 17  LEU A CB  1 
ATOM   138  C CG  . LEU A 1 17  ? 24.39896  -17.08491 14.60562 1.000 10.75200 ? 17  LEU A CG  1 
ATOM   139  C CD1 . LEU A 1 17  ? 24.29133  -17.01793 13.08077 1.000 13.76577 ? 17  LEU A CD1 1 
ATOM   140  C CD2 . LEU A 1 17  ? 25.57593  -17.93902 15.02783 1.000 12.54221 ? 17  LEU A CD2 1 
ATOM   141  N N   . ALA A 1 18  ? 21.78163  -15.59223 16.69688 1.000 11.29220 ? 18  ALA A N   1 
ATOM   142  C CA  . ALA A 1 18  ? 20.55962  -16.23519 17.17407 1.000 11.71038 ? 18  ALA A CA  1 
ATOM   143  C C   . ALA A 1 18  ? 19.31375  -15.53251 16.64359 1.000 12.51792 ? 18  ALA A C   1 
ATOM   144  O O   . ALA A 1 18  ? 18.35825  -16.18988 16.21547 1.000 13.42033 ? 18  ALA A O   1 
ATOM   145  C CB  . ALA A 1 18  ? 20.55072  -16.28845 18.70210 1.000 13.11649 ? 18  ALA A CB  1 
ATOM   146  N N   . GLY A 1 19  ? 19.29996  -14.19855 16.66850 1.000 13.19720 ? 19  GLY A N   1 
ATOM   147  C CA  . GLY A 1 19  ? 18.20145  -13.47648 16.04974 1.000 13.15656 ? 19  GLY A CA  1 
ATOM   148  C C   . GLY A 1 19  ? 18.04479  -13.81369 14.57906 1.000 12.77369 ? 19  GLY A C   1 
ATOM   149  O O   . GLY A 1 19  ? 16.93270  -14.05301 14.10400 1.000 12.71497 ? 19  GLY A O   1 
ATOM   150  N N   . THR A 1 20  ? 19.16045  -13.86006 13.84540 1.000 12.17059 ? 20  THR A N   1 
ATOM   151  C CA  . THR A 1 20  ? 19.11740  -14.18035 12.42110 1.000 12.14766 ? 20  THR A CA  1 
ATOM   152  C C   . THR A 1 20  ? 18.44742  -15.52583 12.18444 1.000 12.24776 ? 20  THR A C   1 
ATOM   153  O O   . THR A 1 20  ? 17.45269  -15.62561 11.45807 1.000 13.76156 ? 20  THR A O   1 
ATOM   154  C CB  . THR A 1 20  ? 20.53350  -14.19830 11.83818 1.000 11.84984 ? 20  THR A CB  1 
ATOM   155  O OG1 . THR A 1 20  ? 21.17910  -12.94193 12.06980 1.000 11.99196 ? 20  THR A OG1 1 
ATOM   156  C CG2 . THR A 1 20  ? 20.48361  -14.47278 10.33957 1.000 12.79628 ? 20  THR A CG2 1 
ATOM   157  N N   . VAL A 1 21  ? 18.97712  -16.57505 12.80934 1.000 13.04879 ? 21  VAL A N   1 
ATOM   158  C CA  . VAL A 1 21  ? 18.52073  -17.92054 12.49410 1.000 13.83028 ? 21  VAL A CA  1 
ATOM   159  C C   . VAL A 1 21  ? 17.14638  -18.21776 13.08705 1.000 14.28645 ? 21  VAL A C   1 
ATOM   160  O O   . VAL A 1 21  ? 16.36216  -18.95938 12.48606 1.000 16.64068 ? 21  VAL A O   1 
ATOM   161  C CB  . VAL A 1 21  ? 19.58244  -18.97059 12.86293 1.000 15.30682 ? 21  VAL A CB  1 
ATOM   162  C CG1 . VAL A 1 21  ? 20.83691  -18.74166 12.04502 1.000 16.32788 ? 21  VAL A CG1 1 
ATOM   163  C CG2 . VAL A 1 21  ? 19.90139  -18.90995 14.34468 1.000 15.31482 ? 21  VAL A CG2 1 
ATOM   164  N N   A PHE A 1 22  ? 16.84921  -17.68057 14.27750 0.500 14.74267 ? 22  PHE A N   1 
ATOM   165  N N   B PHE A 1 22  ? 16.80304  -17.64878 14.23822 0.500 14.08233 ? 22  PHE A N   1 
ATOM   166  C CA  A PHE A 1 22  ? 15.50859  -17.81444 14.84313 0.500 15.07445 ? 22  PHE A CA  1 
ATOM   167  C CA  B PHE A 1 22  ? 15.47470  -17.93383 14.76567 0.500 13.74432 ? 22  PHE A CA  1 
ATOM   168  C C   A PHE A 1 22  ? 14.47385  -17.21885 13.90557 0.500 12.83944 ? 22  PHE A C   1 
ATOM   169  C C   B PHE A 1 22  ? 14.37680  -17.10409 14.10049 0.500 12.53625 ? 22  PHE A C   1 
ATOM   170  O O   A PHE A 1 22  ? 13.44978  -17.84409 13.60699 0.500 11.55325 ? 22  PHE A O   1 
ATOM   171  O O   B PHE A 1 22  ? 13.20405  -17.48536 14.17361 0.500 12.54798 ? 22  PHE A O   1 
ATOM   172  C CB  A PHE A 1 22  ? 15.43214  -17.12238 16.20895 0.500 16.20717 ? 22  PHE A CB  1 
ATOM   173  C CB  B PHE A 1 22  ? 15.46054  -17.88123 16.29737 0.500 13.26266 ? 22  PHE A CB  1 
ATOM   174  C CG  A PHE A 1 22  ? 14.03099  -16.71732 16.61464 0.500 15.88062 ? 22  PHE A CG  1 
ATOM   175  C CG  B PHE A 1 22  ? 16.17355  -19.04376 16.94653 0.500 13.55442 ? 22  PHE A CG  1 
ATOM   176  C CD1 A PHE A 1 22  ? 13.17180  -17.63351 17.19876 0.500 15.54339 ? 22  PHE A CD1 1 
ATOM   177  C CD1 B PHE A 1 22  ? 15.52533  -20.25549 17.13328 0.500 13.45320 ? 22  PHE A CD1 1 
ATOM   178  C CD2 A PHE A 1 22  ? 13.58022  -15.41803 16.42095 0.500 16.36983 ? 22  PHE A CD2 1 
ATOM   179  C CD2 B PHE A 1 22  ? 17.49062  -18.92676 17.36401 0.500 12.91307 ? 22  PHE A CD2 1 
ATOM   180  C CE1 A PHE A 1 22  ? 11.88961  -17.26670 17.57201 0.500 16.38987 ? 22  PHE A CE1 1 
ATOM   181  C CE1 B PHE A 1 22  ? 16.17589  -21.32008 17.72454 0.500 13.46025 ? 22  PHE A CE1 1 
ATOM   182  C CE2 A PHE A 1 22  ? 12.29848  -15.04726 16.79025 0.500 16.20652 ? 22  PHE A CE2 1 
ATOM   183  C CE2 B PHE A 1 22  ? 18.14594  -19.99021 17.95569 0.500 12.56146 ? 22  PHE A CE2 1 
ATOM   184  C CZ  A PHE A 1 22  ? 11.45317  -15.97104 17.36700 0.500 17.58479 ? 22  PHE A CZ  1 
ATOM   185  C CZ  B PHE A 1 22  ? 17.48763  -21.18704 18.13647 0.500 12.97952 ? 22  PHE A CZ  1 
ATOM   186  N N   . LEU A 1 23  ? 14.72923  -15.99864 13.43453 1.000 12.85430 ? 23  LEU A N   1 
ATOM   187  C CA  . LEU A 1 23  ? 13.78148  -15.33941 12.54540 1.000 12.81147 ? 23  LEU A CA  1 
ATOM   188  C C   . LEU A 1 23  ? 13.59352  -16.14675 11.26610 1.000 13.02022 ? 23  LEU A C   1 
ATOM   189  O O   . LEU A 1 23  ? 12.46431  -16.33307 10.80168 1.000 12.51400 ? 23  LEU A O   1 
ATOM   190  C CB  . LEU A 1 23  ? 14.25625  -13.91734 12.24426 1.000 12.41005 ? 23  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 23  ? 14.08912  -12.92054 13.39400 1.000 12.95478 ? 23  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 23  ? 14.92975  -11.66190 13.14945 1.000 13.32420 ? 23  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 23  ? 12.61973  -12.56121 13.59011 1.000 14.35178 ? 23  LEU A CD2 1 
ATOM   194  N N   . LEU A 1 24  ? 14.68664  -16.66596 10.70342 1.000 13.71595 ? 24  LEU A N   1 
ATOM   195  C CA  . LEU A 1 24  ? 14.57187  -17.54192 9.54063  1.000 15.52728 ? 24  LEU A CA  1 
ATOM   196  C C   . LEU A 1 24  ? 13.73534  -18.77340 9.86524  1.000 16.69869 ? 24  LEU A C   1 
ATOM   197  O O   . LEU A 1 24  ? 12.83872  -19.14960 9.10103  1.000 17.73368 ? 24  LEU A O   1 
ATOM   198  C CB  . LEU A 1 24  ? 15.96092  -17.94699 9.04421  1.000 16.31415 ? 24  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 24  ? 16.79740  -16.84489 8.39479  1.000 18.01910 ? 24  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 24  ? 18.16818  -17.36811 7.99585  1.000 19.08817 ? 24  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 24  ? 16.07051  -16.26292 7.18942  1.000 19.40456 ? 24  LEU A CD2 1 
ATOM   202  N N   . ALA A 1 25  ? 14.00453  -19.40738 11.01081 1.000 16.63213 ? 25  ALA A N   1 
ATOM   203  C CA  . ALA A 1 25  ? 13.25122  -20.59961 11.38680 1.000 16.73599 ? 25  ALA A CA  1 
ATOM   204  C C   . ALA A 1 25  ? 11.77941  -20.28768 11.62016 1.000 17.30308 ? 25  ALA A C   1 
ATOM   205  O O   . ALA A 1 25  ? 10.91605  -21.12566 11.33759 1.000 17.67028 ? 25  ALA A O   1 
ATOM   206  C CB  . ALA A 1 25  ? 13.85860  -21.23782 12.63509 1.000 16.71554 ? 25  ALA A CB  1 
ATOM   207  N N   A SER A 1 26  ? 11.47475  -19.09180 12.12538 0.500 16.53418 ? 26  SER A N   1 
ATOM   208  N N   B SER A 1 26  ? 11.47005  -19.09576 12.13121 0.500 17.01825 ? 26  SER A N   1 
ATOM   209  C CA  A SER A 1 26  ? 10.10149  -18.70975 12.42569 0.500 17.27515 ? 26  SER A CA  1 
ATOM   210  C CA  B SER A 1 26  ? 10.08756  -18.73981 12.42275 0.500 17.91091 ? 26  SER A CA  1 
ATOM   211  C C   A SER A 1 26  ? 9.30552   -18.30001 11.19428 0.500 17.25049 ? 26  SER A C   1 
ATOM   212  C C   B SER A 1 26  ? 9.29795   -18.32393 11.18826 0.500 17.56408 ? 26  SER A C   1 
ATOM   213  O O   A SER A 1 26  ? 8.08408   -18.14394 11.29551 0.500 17.05704 ? 26  SER A O   1 
ATOM   214  O O   B SER A 1 26  ? 8.07306   -18.18852 11.28078 0.500 17.23752 ? 26  SER A O   1 
ATOM   215  C CB  A SER A 1 26  ? 10.08385  -17.57058 13.44741 0.500 17.32403 ? 26  SER A CB  1 
ATOM   216  C CB  B SER A 1 26  ? 10.02937  -17.62642 13.47274 0.500 18.04458 ? 26  SER A CB  1 
ATOM   217  O OG  A SER A 1 26  ? 10.70884  -17.96529 14.65460 0.500 17.83707 ? 26  SER A OG  1 
ATOM   218  O OG  B SER A 1 26  ? 10.52496  -16.40678 12.95182 0.500 19.25304 ? 26  SER A OG  1 
ATOM   219  N N   . SER A 1 27  ? 9.95671   -18.12623 10.04109 1.000 17.32054 ? 27  SER A N   1 
ATOM   220  C CA  . SER A 1 27  ? 9.24121   -17.66347 8.85168  1.000 20.74952 ? 27  SER A CA  1 
ATOM   221  C C   . SER A 1 27  ? 8.14720   -18.63483 8.41319  1.000 21.47385 ? 27  SER A C   1 
ATOM   222  O O   . SER A 1 27  ? 7.13433   -18.20946 7.84446  1.000 21.98450 ? 27  SER A O   1 
ATOM   223  C CB  . SER A 1 27  ? 10.21984  -17.39583 7.70839  1.000 23.59731 ? 27  SER A CB  1 
ATOM   224  O OG  . SER A 1 27  ? 10.86158  -18.58832 7.29957  1.000 25.65591 ? 27  SER A OG  1 
ATOM   225  N N   A ARG A 1 28  ? 8.32484   -19.93238 8.67292  0.500 20.89185 ? 28  ARG A N   1 
ATOM   226  N N   B ARG A 1 28  ? 8.32345   -19.93306 8.67215  0.500 21.01491 ? 28  ARG A N   1 
ATOM   227  C CA  A ARG A 1 28  ? 7.30006   -20.90780 8.31745  0.500 21.66487 ? 28  ARG A CA  1 
ATOM   228  C CA  B ARG A 1 28  ? 7.30138   -20.91478 8.32324  0.500 21.99559 ? 28  ARG A CA  1 
ATOM   229  C C   A ARG A 1 28  ? 6.01820   -20.72387 9.11876  0.500 22.43418 ? 28  ARG A C   1 
ATOM   230  C C   B ARG A 1 28  ? 6.01955   -20.75056 9.12901  0.500 22.59185 ? 28  ARG A C   1 
ATOM   231  O O   A ARG A 1 28  ? 4.98007   -21.27425 8.73636  0.500 23.16164 ? 28  ARG A O   1 
ATOM   232  O O   B ARG A 1 28  ? 5.00010   -21.34492 8.76231  0.500 23.28170 ? 28  ARG A O   1 
ATOM   233  C CB  A ARG A 1 28  ? 7.82314   -22.32881 8.52624  0.500 23.36367 ? 28  ARG A CB  1 
ATOM   234  C CB  B ARG A 1 28  ? 7.83510   -22.33623 8.51567  0.500 24.14899 ? 28  ARG A CB  1 
ATOM   235  C CG  A ARG A 1 28  ? 8.14281   -22.65928 9.97573  0.500 23.21415 ? 28  ARG A CG  1 
ATOM   236  C CG  B ARG A 1 28  ? 8.41925   -22.58935 9.89653  0.500 25.36524 ? 28  ARG A CG  1 
ATOM   237  C CD  A ARG A 1 28  ? 8.43101   -24.14105 10.16044 0.500 24.24054 ? 28  ARG A CD  1 
ATOM   238  C CD  B ARG A 1 28  ? 8.48076   -24.07296 10.23248 0.500 28.10321 ? 28  ARG A CD  1 
ATOM   239  N NE  A ARG A 1 28  ? 7.28439   -24.96421 9.79542  0.500 23.73355 ? 28  ARG A NE  1 
ATOM   240  N NE  B ARG A 1 28  ? 7.48060   -24.43423 11.23041 0.500 29.18820 ? 28  ARG A NE  1 
ATOM   241  C CZ  A ARG A 1 28  ? 6.23571   -25.17523 10.57903 0.500 25.80178 ? 28  ARG A CZ  1 
ATOM   242  C CZ  B ARG A 1 28  ? 6.30174   -24.97326 10.95205 0.500 29.64970 ? 28  ARG A CZ  1 
ATOM   243  N NH1 A ARG A 1 28  ? 6.14758   -24.62426 11.77932 0.500 27.37523 ? 28  ARG A NH1 1 
ATOM   244  N NH1 B ARG A 1 28  ? 5.95277   -25.26975 9.71068  0.500 29.36819 ? 28  ARG A NH1 1 
ATOM   245  N NH2 A ARG A 1 28  ? 5.24859   -25.95549 10.14641 0.500 26.79082 ? 28  ARG A NH2 1 
ATOM   246  N NH2 B ARG A 1 28  ? 5.45190   -25.22260 11.94451 0.500 30.14656 ? 28  ARG A NH2 1 
ATOM   247  N N   A GLU A 1 29  ? 6.06512   -19.96834 10.21631 0.500 23.82690 ? 29  GLU A N   1 
ATOM   248  N N   B GLU A 1 29  ? 6.04357   -19.97221 10.20937 0.500 23.89926 ? 29  GLU A N   1 
ATOM   249  C CA  A GLU A 1 29  ? 4.90203   -19.80023 11.07592 0.500 25.17543 ? 29  GLU A CA  1 
ATOM   250  C CA  B GLU A 1 29  ? 4.87791   -19.81053 11.06820 0.500 25.30677 ? 29  GLU A CA  1 
ATOM   251  C C   A GLU A 1 29  ? 3.88523   -18.81033 10.52182 0.500 22.91103 ? 29  GLU A C   1 
ATOM   252  C C   B GLU A 1 29  ? 3.90406   -18.75447 10.56397 0.500 22.89505 ? 29  GLU A C   1 
ATOM   253  O O   A GLU A 1 29  ? 2.77001   -18.74043 11.04666 0.500 24.13359 ? 29  GLU A O   1 
ATOM   254  O O   B GLU A 1 29  ? 2.84236   -18.57415 11.17065 0.500 23.90952 ? 29  GLU A O   1 
ATOM   255  C CB  A GLU A 1 29  ? 5.33977   -19.37195 12.48057 0.500 28.51800 ? 29  GLU A CB  1 
ATOM   256  C CB  B GLU A 1 29  ? 5.31617   -19.48605 12.49826 0.500 28.76063 ? 29  GLU A CB  1 
ATOM   257  C CG  A GLU A 1 29  ? 6.42714   -20.24967 13.09634 0.500 31.43935 ? 29  GLU A CG  1 
ATOM   258  C CG  B GLU A 1 29  ? 6.18886   -20.55872 13.13043 0.500 31.94856 ? 29  GLU A CG  1 
ATOM   259  C CD  A GLU A 1 29  ? 5.93109   -21.63212 13.46970 0.500 34.24467 ? 29  GLU A CD  1 
ATOM   260  C CD  B GLU A 1 29  ? 6.71831   -20.14915 14.48700 0.500 35.89877 ? 29  GLU A CD  1 
ATOM   261  O OE1 A GLU A 1 29  ? 4.70817   -21.79774 13.65921 0.500 32.09278 ? 29  GLU A OE1 1 
ATOM   262  O OE1 B GLU A 1 29  ? 6.60782   -18.95430 14.83298 0.500 36.48509 ? 29  GLU A OE1 1 
ATOM   263  O OE2 A GLU A 1 29  ? 6.76641   -22.55476 13.57473 0.500 39.41631 ? 29  GLU A OE2 1 
ATOM   264  O OE2 B GLU A 1 29  ? 7.24578   -21.02104 15.20832 0.500 39.44269 ? 29  GLU A OE2 1 
ATOM   265  N N   . VAL A 1 30  ? 4.23054   -18.05519 9.48029  1.000 21.82865 ? 30  VAL A N   1 
ATOM   266  C CA  . VAL A 1 30  ? 3.33643   -17.06011 8.90515  1.000 21.39453 ? 30  VAL A CA  1 
ATOM   267  C C   . VAL A 1 30  ? 3.07807   -17.41085 7.44593  1.000 21.96815 ? 30  VAL A C   1 
ATOM   268  O O   . VAL A 1 30  ? 3.81513   -18.18216 6.82609  1.000 22.28121 ? 30  VAL A O   1 
ATOM   269  C CB  . VAL A 1 30  ? 3.88312   -15.62347 9.04082  1.000 21.47289 ? 30  VAL A CB  1 
ATOM   270  C CG1 . VAL A 1 30  ? 4.16104   -15.29120 10.50160 1.000 21.56652 ? 30  VAL A CG1 1 
ATOM   271  C CG2 . VAL A 1 30  ? 5.13808   -15.45888 8.20857  1.000 20.28140 ? 30  VAL A CG2 1 
ATOM   272  N N   . LYS A 1 31  ? 2.00661   -16.83686 6.90130  1.000 22.70170 ? 31  LYS A N   1 
ATOM   273  C CA  . LYS A 1 31  ? 1.67459   -17.07250 5.50723  1.000 25.05601 ? 31  LYS A CA  1 
ATOM   274  C C   . LYS A 1 31  ? 2.81720   -16.59428 4.61202  1.000 24.77358 ? 31  LYS A C   1 
ATOM   275  O O   . LYS A 1 31  ? 3.51982   -15.63682 4.94984  1.000 23.82081 ? 31  LYS A O   1 
ATOM   276  C CB  . LYS A 1 31  ? 0.39436   -16.32730 5.13456  1.000 29.07979 ? 31  LYS A CB  1 
ATOM   277  C CG  . LYS A 1 31  ? -0.89006  -17.03154 5.53343  1.000 34.07346 ? 31  LYS A CG  1 
ATOM   278  C CD  . LYS A 1 31  ? -2.09492  -16.14013 5.26128  1.000 38.42301 ? 31  LYS A CD  1 
ATOM   279  C CE  . LYS A 1 31  ? -3.39105  -16.93011 5.24673  1.000 41.92469 ? 31  LYS A CE  1 
ATOM   280  N NZ  . LYS A 1 31  ? -4.24533  -16.63448 6.42789  1.000 47.31144 ? 31  LYS A NZ  1 
ATOM   281  N N   . PRO A 1 32  ? 3.02840   -17.25129 3.46653  1.000 24.45014 ? 32  PRO A N   1 
ATOM   282  C CA  . PRO A 1 32  ? 4.11113   -16.82877 2.56057  1.000 25.37696 ? 32  PRO A CA  1 
ATOM   283  C C   . PRO A 1 32  ? 4.04470   -15.36658 2.15582  1.000 26.14044 ? 32  PRO A C   1 
ATOM   284  O O   . PRO A 1 32  ? 5.09302   -14.73700 1.96008  1.000 27.63040 ? 32  PRO A O   1 
ATOM   285  C CB  . PRO A 1 32  ? 3.93933   -17.75854 1.35146  1.000 25.68726 ? 32  PRO A CB  1 
ATOM   286  C CG  . PRO A 1 32  ? 3.22339   -18.95440 1.88924  1.000 25.51444 ? 32  PRO A CG  1 
ATOM   287  C CD  . PRO A 1 32  ? 2.31602   -18.44171 2.96938  1.000 24.31636 ? 32  PRO A CD  1 
ATOM   288  N N   A GLU A 1 33  ? 2.84610   -14.79713 2.02474  0.500 26.82241 ? 33  GLU A N   1 
ATOM   289  N N   B GLU A 1 33  ? 2.83632   -14.81038 2.03341  0.500 27.18962 ? 33  GLU A N   1 
ATOM   290  C CA  A GLU A 1 33  ? 2.72999   -13.40374 1.61219  0.500 25.74778 ? 33  GLU A CA  1 
ATOM   291  C CA  B GLU A 1 33  ? 2.66495   -13.41508 1.64863  0.500 27.08182 ? 33  GLU A CA  1 
ATOM   292  C C   A GLU A 1 33  ? 3.15404   -12.41936 2.69489  0.500 25.43383 ? 33  GLU A C   1 
ATOM   293  C C   B GLU A 1 33  ? 3.27636   -12.45566 2.65932  0.500 26.18326 ? 33  GLU A C   1 
ATOM   294  O O   A GLU A 1 33  ? 3.20042   -11.21542 2.42185  0.500 25.52676 ? 33  GLU A O   1 
ATOM   295  O O   B GLU A 1 33  ? 3.58249   -11.31237 2.30447  0.500 26.80163 ? 33  GLU A O   1 
ATOM   296  C CB  A GLU A 1 33  ? 1.30333   -13.09365 1.15149  0.500 26.27280 ? 33  GLU A CB  1 
ATOM   297  C CB  B GLU A 1 33  ? 1.17151   -13.10683 1.51500  0.500 28.65117 ? 33  GLU A CB  1 
ATOM   298  C CG  A GLU A 1 33  ? 0.22229   -13.46194 2.15306  0.500 26.47389 ? 33  GLU A CG  1 
ATOM   299  C CG  B GLU A 1 33  ? 0.28339   -14.34490 1.52517  0.500 29.62203 ? 33  GLU A CG  1 
ATOM   300  C CD  A GLU A 1 33  ? -0.28016  -14.88238 1.97616  0.500 27.60616 ? 33  GLU A CD  1 
ATOM   301  C CD  B GLU A 1 33  ? -1.18312  -14.02376 1.76496  0.500 30.02287 ? 33  GLU A CD  1 
ATOM   302  O OE1 A GLU A 1 33  ? 0.47655   -15.72791 1.45260  0.500 26.96167 ? 33  GLU A OE1 1 
ATOM   303  O OE1 B GLU A 1 33  ? -1.49933  -12.86060 2.09136  0.500 31.22771 ? 33  GLU A OE1 1 
ATOM   304  O OE2 A GLU A 1 33  ? -1.43970  -15.15022 2.35362  0.500 27.26749 ? 33  GLU A OE2 1 
ATOM   305  O OE2 B GLU A 1 33  ? -2.02144  -14.94000 1.63065  0.500 30.98019 ? 33  GLU A OE2 1 
ATOM   306  N N   . HIS A 1 34  ? 3.45828   -12.88960 3.90704  1.000 24.52121 ? 34  HIS A N   1 
ATOM   307  C CA  . HIS A 1 34  ? 3.92683   -12.02233 4.98270  1.000 24.09992 ? 34  HIS A CA  1 
ATOM   308  C C   . HIS A 1 34  ? 5.31759   -12.40484 5.48013  1.000 22.71184 ? 34  HIS A C   1 
ATOM   309  O O   . HIS A 1 34  ? 5.72484   -11.97179 6.56355  1.000 23.22247 ? 34  HIS A O   1 
ATOM   310  C CB  . HIS A 1 34  ? 2.92533   -11.99710 6.13910  1.000 23.15925 ? 34  HIS A CB  1 
ATOM   311  C CG  . HIS A 1 34  ? 1.52764   -11.67286 5.71527  1.000 25.57933 ? 34  HIS A CG  1 
ATOM   312  N ND1 . HIS A 1 34  ? 1.19844   -10.49681 5.07736  1.000 27.29515 ? 34  HIS A ND1 1 
ATOM   313  C CD2 . HIS A 1 34  ? 0.37452   -12.37276 5.83252  1.000 25.90711 ? 34  HIS A CD2 1 
ATOM   314  C CE1 . HIS A 1 34  ? -0.09718  -10.48559 4.81954  1.000 26.26505 ? 34  HIS A CE1 1 
ATOM   315  N NE2 . HIS A 1 34  ? -0.62069  -11.61179 5.26928  1.000 26.04860 ? 34  HIS A NE2 1 
ATOM   316  N N   . ARG A 1 35  ? 6.05650   -13.20977 4.71405  1.000 22.03427 ? 35  ARG A N   1 
ATOM   317  C CA  . ARG A 1 35  ? 7.38317   -13.63929 5.13787  1.000 20.17810 ? 35  ARG A CA  1 
ATOM   318  C C   . ARG A 1 35  ? 8.48963   -12.66368 4.77023  1.000 19.74029 ? 35  ARG A C   1 
ATOM   319  O O   . ARG A 1 35  ? 9.58258   -12.75779 5.33997  1.000 18.74487 ? 35  ARG A O   1 
ATOM   320  C CB  . ARG A 1 35  ? 7.71738   -15.01818 4.56507  1.000 20.42401 ? 35  ARG A CB  1 
ATOM   321  C CG  . ARG A 1 35  ? 6.93396   -16.13302 5.21890  1.000 22.31135 ? 35  ARG A CG  1 
ATOM   322  C CD  . ARG A 1 35  ? 7.20511   -17.47083 4.58220  1.000 23.30488 ? 35  ARG A CD  1 
ATOM   323  N NE  . ARG A 1 35  ? 6.24167   -18.46084 5.04542  1.000 24.48553 ? 35  ARG A NE  1 
ATOM   324  C CZ  . ARG A 1 35  ? 6.02257   -19.62519 4.45378  1.000 26.71818 ? 35  ARG A CZ  1 
ATOM   325  N NH1 . ARG A 1 35  ? 6.67591   -19.97656 3.35748  1.000 28.41131 ? 35  ARG A NH1 1 
ATOM   326  N NH2 . ARG A 1 35  ? 5.12264   -20.45528 4.97213  1.000 28.06750 ? 35  ARG A NH2 1 
ATOM   327  N N   . ARG A 1 36  ? 8.23853   -11.73436 3.84425  1.000 19.96528 ? 36  ARG A N   1 
ATOM   328  C CA  . ARG A 1 36  ? 9.30168   -10.83790 3.39732  1.000 21.66745 ? 36  ARG A CA  1 
ATOM   329  C C   . ARG A 1 36  ? 9.89757   -10.05250 4.55762  1.000 19.75385 ? 36  ARG A C   1 
ATOM   330  O O   . ARG A 1 36  ? 11.12313  -9.93364  4.67011  1.000 20.04024 ? 36  ARG A O   1 
ATOM   331  C CB  . ARG A 1 36  ? 8.78330   -9.88386  2.32100  1.000 26.40185 ? 36  ARG A CB  1 
ATOM   332  C CG  . ARG A 1 36  ? 9.84293   -8.90515  1.83959  1.000 30.99273 ? 36  ARG A CG  1 
ATOM   333  C CD  . ARG A 1 36  ? 9.29935   -7.94382  0.79973  1.000 34.84035 ? 36  ARG A CD  1 
ATOM   334  N NE  . ARG A 1 36  ? 10.34847  -7.08472  0.26454  1.000 39.31187 ? 36  ARG A NE  1 
ATOM   335  C CZ  . ARG A 1 36  ? 11.16899  -7.43003  -0.71824 1.000 38.16047 ? 36  ARG A CZ  1 
ATOM   336  N N   . GLY A 1 37  ? 9.04691   -9.51834  5.43530  1.000 17.74207 ? 37  GLY A N   1 
ATOM   337  C CA  . GLY A 1 37  ? 9.54644   -8.72143  6.54263  1.000 17.10556 ? 37  GLY A CA  1 
ATOM   338  C C   . GLY A 1 37  ? 10.35250  -9.52346  7.54211  1.000 16.01520 ? 37  GLY A C   1 
ATOM   339  O O   . GLY A 1 37  ? 11.31907  -9.01830  8.12099  1.000 16.42313 ? 37  GLY A O   1 
ATOM   340  N N   . VAL A 1 38  ? 9.95866   -10.77573 7.77087  1.000 15.19771 ? 38  VAL A N   1 
ATOM   341  C CA  . VAL A 1 38  ? 10.74817  -11.65989 8.62136  1.000 14.83391 ? 38  VAL A CA  1 
ATOM   342  C C   . VAL A 1 38  ? 12.12657  -11.89314 8.01379  1.000 14.53211 ? 38  VAL A C   1 
ATOM   343  O O   . VAL A 1 38  ? 13.14673  -11.86808 8.71636  1.000 12.29172 ? 38  VAL A O   1 
ATOM   344  C CB  . VAL A 1 38  ? 9.99078   -12.97772 8.86397  1.000 14.14232 ? 38  VAL A CB  1 
ATOM   345  C CG1 . VAL A 1 38  ? 10.77946  -13.86626 9.80077  1.000 12.51680 ? 38  VAL A CG1 1 
ATOM   346  C CG2 . VAL A 1 38  ? 8.60709   -12.69760 9.42664  1.000 14.94335 ? 38  VAL A CG2 1 
ATOM   347  N N   . TYR A 1 39  ? 12.18006  -12.12083 6.69803  1.000 14.92030 ? 39  TYR A N   1 
ATOM   348  C CA  . TYR A 1 39  ? 13.46612  -12.32036 6.03692  1.000 15.23075 ? 39  TYR A CA  1 
ATOM   349  C C   . TYR A 1 39  ? 14.32766  -11.06616 6.11328  1.000 14.55753 ? 39  TYR A C   1 
ATOM   350  O O   . TYR A 1 39  ? 15.53345  -11.14841 6.37601  1.000 14.80408 ? 39  TYR A O   1 
ATOM   351  C CB  . TYR A 1 39  ? 13.25817  -12.73369 4.58018  1.000 16.06551 ? 39  TYR A CB  1 
ATOM   352  C CG  . TYR A 1 39  ? 12.63642  -14.10190 4.39393  1.000 19.46202 ? 39  TYR A CG  1 
ATOM   353  C CD1 . TYR A 1 39  ? 12.96981  -15.16136 5.22721  1.000 21.88820 ? 39  TYR A CD1 1 
ATOM   354  C CD2 . TYR A 1 39  ? 11.71853  -14.32924 3.38106  1.000 21.87116 ? 39  TYR A CD2 1 
ATOM   355  C CE1 . TYR A 1 39  ? 12.40216  -16.41281 5.05614  1.000 21.42723 ? 39  TYR A CE1 1 
ATOM   356  C CE2 . TYR A 1 39  ? 11.14476  -15.57329 3.20158  1.000 22.12340 ? 39  TYR A CE2 1 
ATOM   357  C CZ  . TYR A 1 39  ? 11.49048  -16.61104 4.03959  1.000 23.06913 ? 39  TYR A CZ  1 
ATOM   358  O OH  . TYR A 1 39  ? 10.91400  -17.84754 3.85093  1.000 25.62931 ? 39  TYR A OH  1 
ATOM   359  N N   . ILE A 1 40  ? 13.72945  -9.89457  5.88326  1.000 14.34708 ? 40  ILE A N   1 
ATOM   360  C CA  . ILE A 1 40  ? 14.49657  -8.65298  5.95675  1.000 13.32205 ? 40  ILE A CA  1 
ATOM   361  C C   . ILE A 1 40  ? 15.01345  -8.43003  7.37072  1.000 12.87986 ? 40  ILE A C   1 
ATOM   362  O O   . ILE A 1 40  ? 16.15780  -7.99616  7.56931  1.000 13.06715 ? 40  ILE A O   1 
ATOM   363  C CB  . ILE A 1 40  ? 13.67264  -7.46097  5.43142  1.000 14.44637 ? 40  ILE A CB  1 
ATOM   364  C CG1 . ILE A 1 40  ? 13.44321  -7.59703  3.92421  1.000 17.17925 ? 40  ILE A CG1 1 
ATOM   365  C CG2 . ILE A 1 40  ? 14.37594  -6.14342  5.73464  1.000 14.60978 ? 40  ILE A CG2 1 
ATOM   366  C CD1 . ILE A 1 40  ? 12.52655  -6.54697  3.34379  1.000 20.22891 ? 40  ILE A CD1 1 
ATOM   367  N N   . SER A 1 41  ? 14.18582  -8.74167  8.37592  1.000 12.07658 ? 41  SER A N   1 
ATOM   368  C CA  . SER A 1 41  ? 14.63287  -8.65314  9.76303  1.000 12.72536 ? 41  SER A CA  1 
ATOM   369  C C   . SER A 1 41  ? 15.80270  -9.59117  10.02327 1.000 11.36351 ? 41  SER A C   1 
ATOM   370  O O   . SER A 1 41  ? 16.73615  -9.24603  10.76066 1.000 11.00466 ? 41  SER A O   1 
ATOM   371  C CB  . SER A 1 41  ? 13.47766  -8.98529  10.70998 1.000 12.37377 ? 41  SER A CB  1 
ATOM   372  O OG  . SER A 1 41  ? 12.42670  -8.03551  10.61631 1.000 16.68919 ? 41  SER A OG  1 
ATOM   373  N N   . ALA A 1 42  ? 15.76372  -10.78798 9.43473  1.000 8.27923  ? 42  ALA A N   1 
ATOM   374  C CA  . ALA A 1 42  ? 16.88347  -11.71360 9.56946  1.000 8.84398  ? 42  ALA A CA  1 
ATOM   375  C C   . ALA A 1 42  ? 18.13869  -11.16511 8.90122  1.000 10.96692 ? 42  ALA A C   1 
ATOM   376  O O   . ALA A 1 42  ? 19.24291  -11.30903 9.43689  1.000 11.24413 ? 42  ALA A O   1 
ATOM   377  C CB  . ALA A 1 42  ? 16.51345  -13.08155 8.99716  1.000 10.06668 ? 42  ALA A CB  1 
ATOM   378  N N   . LEU A 1 43  ? 17.99115  -10.54123 7.72847  1.000 10.65193 ? 43  LEU A N   1 
ATOM   379  C CA  . LEU A 1 43  ? 19.13702  -9.92493  7.06312  1.000 11.35177 ? 43  LEU A CA  1 
ATOM   380  C C   . LEU A 1 43  ? 19.75027  -8.82528  7.92243  1.000 10.58338 ? 43  LEU A C   1 
ATOM   381  O O   . LEU A 1 43  ? 20.97837  -8.69946  8.00118  1.000 10.74977 ? 43  LEU A O   1 
ATOM   382  C CB  . LEU A 1 43  ? 18.71257  -9.36607  5.70424  1.000 12.60707 ? 43  LEU A CB  1 
ATOM   383  C CG  . LEU A 1 43  ? 19.77142  -8.58246  4.92276  1.000 14.30789 ? 43  LEU A CG  1 
ATOM   384  C CD1 . LEU A 1 43  ? 20.99334  -9.44907  4.66200  1.000 15.07162 ? 43  LEU A CD1 1 
ATOM   385  C CD2 . LEU A 1 43  ? 19.20789  -8.05040  3.61543  1.000 15.52797 ? 43  LEU A CD2 1 
ATOM   386  N N   . VAL A 1 44  ? 18.90789  -8.01248  8.56585  1.000 10.43841 ? 44  VAL A N   1 
ATOM   387  C CA  . VAL A 1 44  ? 19.40010  -6.97560  9.47292  1.000 11.49517 ? 44  VAL A CA  1 
ATOM   388  C C   . VAL A 1 44  ? 20.23627  -7.59255  10.59053 1.000 11.10771 ? 44  VAL A C   1 
ATOM   389  O O   . VAL A 1 44  ? 21.35167  -7.14152  10.88336 1.000 11.04443 ? 44  VAL A O   1 
ATOM   390  C CB  . VAL A 1 44  ? 18.22422  -6.14872  10.02367 1.000 12.15442 ? 44  VAL A CB  1 
ATOM   391  C CG1 . VAL A 1 44  ? 18.67113  -5.29099  11.19058 1.000 12.49624 ? 44  VAL A CG1 1 
ATOM   392  C CG2 . VAL A 1 44  ? 17.62482  -5.28302  8.91884  1.000 13.09074 ? 44  VAL A CG2 1 
ATOM   393  N N   . CYS A 1 45  ? 19.70641  -8.63543  11.23320 1.000 10.71315 ? 45  CYS A N   1 
ATOM   394  C CA  . CYS A 1 45  ? 20.46072  -9.30909  12.28317 1.000 11.86601 ? 45  CYS A CA  1 
ATOM   395  C C   . CYS A 1 45  ? 21.71139  -9.98391  11.73971 1.000 10.70518 ? 45  CYS A C   1 
ATOM   396  O O   . CYS A 1 45  ? 22.72218  -10.06402 12.44711 1.000 10.75929 ? 45  CYS A O   1 
ATOM   397  C CB  . CYS A 1 45  ? 19.57431  -10.31515 13.01702 1.000 11.38539 ? 45  CYS A CB  1 
ATOM   398  S SG  . CYS A 1 45  ? 18.32198  -9.54164  14.05016 1.000 11.97574 ? 45  CYS A SG  1 
ATOM   399  N N   . GLY A 1 46  ? 21.66810  -10.46535 10.49468 1.000 9.66458  ? 46  GLY A N   1 
ATOM   400  C CA  . GLY A 1 46  ? 22.83182  -11.12585 9.92522  1.000 8.50335  ? 46  GLY A CA  1 
ATOM   401  C C   . GLY A 1 46  ? 23.95573  -10.16158 9.60027  1.000 9.58759  ? 46  GLY A C   1 
ATOM   402  O O   . GLY A 1 46  ? 25.13237  -10.46641 9.82211  1.000 10.48615 ? 46  GLY A O   1 
ATOM   403  N N   . ILE A 1 47  ? 23.61410  -8.99687  9.04828  1.000 8.96752  ? 47  ILE A N   1 
ATOM   404  C CA  . ILE A 1 47  ? 24.61345  -7.95587  8.84135  1.000 10.14474 ? 47  ILE A CA  1 
ATOM   405  C C   . ILE A 1 47  ? 25.22333  -7.53942  10.17109 1.000 9.43584  ? 47  ILE A C   1 
ATOM   406  O O   . ILE A 1 47  ? 26.44826  -7.41507  10.29641 1.000 9.64507  ? 47  ILE A O   1 
ATOM   407  C CB  . ILE A 1 47  ? 24.00020  -6.76746  8.07805  1.000 10.09569 ? 47  ILE A CB  1 
ATOM   408  C CG1 . ILE A 1 47  ? 23.59449  -7.20282  6.66814  1.000 10.86878 ? 47  ILE A CG1 1 
ATOM   409  C CG2 . ILE A 1 47  ? 24.98394  -5.60400  8.02266  1.000 9.63423  ? 47  ILE A CG2 1 
ATOM   410  C CD1 . ILE A 1 47  ? 22.68864  -6.22042  5.95576  1.000 13.09801 ? 47  ILE A CD1 1 
ATOM   411  N N   . ALA A 1 48  ? 24.37999  -7.33656  11.19023 1.000 9.96161  ? 48  ALA A N   1 
ATOM   412  C CA  . ALA A 1 48  ? 24.88962  -7.00217  12.51786 1.000 9.97017  ? 48  ALA A CA  1 
ATOM   413  C C   . ALA A 1 48  ? 25.79128  -8.10229  13.06184 1.000 9.99202  ? 48  ALA A C   1 
ATOM   414  O O   . ALA A 1 48  ? 26.83269  -7.81493  13.66512 1.000 10.10285 ? 48  ALA A O   1 
ATOM   415  C CB  . ALA A 1 48  ? 23.73699  -6.72857  13.48122 1.000 9.60194  ? 48  ALA A CB  1 
ATOM   416  N N   . TRP A 1 49  ? 25.40229  -9.36711  12.87084 1.000 9.38141  ? 49  TRP A N   1 
ATOM   417  C CA  . TRP A 1 49  ? 26.25612  -10.47986 13.27598 1.000 12.16684 ? 49  TRP A CA  1 
ATOM   418  C C   . TRP A 1 49  ? 27.65262  -10.34171 12.68018 1.000 11.55219 ? 49  TRP A C   1 
ATOM   419  O O   . TRP A 1 49  ? 28.65874  -10.44015 13.39169 1.000 11.58528 ? 49  TRP A O   1 
ATOM   420  C CB  . TRP A 1 49  ? 25.61405  -11.81093 12.87616 1.000 12.40911 ? 49  TRP A CB  1 
ATOM   421  C CG  . TRP A 1 49  ? 26.47268  -12.99907 13.17424 1.000 14.39891 ? 49  TRP A CG  1 
ATOM   422  C CD1 . TRP A 1 49  ? 27.08784  -13.29564 14.35767 1.000 14.59793 ? 49  TRP A CD1 1 
ATOM   423  C CD2 . TRP A 1 49  ? 26.79664  -14.06225 12.27697 1.000 17.83408 ? 49  TRP A CD2 1 
ATOM   424  N NE1 . TRP A 1 49  ? 27.79012  -14.47107 14.24509 1.000 14.73126 ? 49  TRP A NE1 1 
ATOM   425  C CE2 . TRP A 1 49  ? 27.62477  -14.96405 12.97732 1.000 17.77477 ? 49  TRP A CE2 1 
ATOM   426  C CE3 . TRP A 1 49  ? 26.47248  -14.33854 10.94579 1.000 20.74919 ? 49  TRP A CE3 1 
ATOM   427  C CZ2 . TRP A 1 49  ? 28.12626  -16.12294 12.39288 1.000 21.05524 ? 49  TRP A CZ2 1 
ATOM   428  C CZ3 . TRP A 1 49  ? 26.97347  -15.49061 10.36756 1.000 22.19277 ? 49  TRP A CZ3 1 
ATOM   429  C CH2 . TRP A 1 49  ? 27.79231  -16.36604 11.08841 1.000 23.95873 ? 49  TRP A CH2 1 
ATOM   430  N N   . TYR A 1 50  ? 27.73116  -10.08575 11.37295 1.000 13.47753 ? 50  TYR A N   1 
ATOM   431  C CA  . TYR A 1 50  ? 29.02920  -9.92046  10.72385 1.000 15.47395 ? 50  TYR A CA  1 
ATOM   432  C C   . TYR A 1 50  ? 29.83370  -8.79941  11.37186 1.000 12.49113 ? 50  TYR A C   1 
ATOM   433  O O   . TYR A 1 50  ? 31.00957  -8.97881  11.71325 1.000 11.92242 ? 50  TYR A O   1 
ATOM   434  C CB  . TYR A 1 50  ? 28.83085  -9.64963  9.23085  1.000 19.54105 ? 50  TYR A CB  1 
ATOM   435  C CG  . TYR A 1 50  ? 30.09515  -9.24966  8.50735  1.000 25.83649 ? 50  TYR A CG  1 
ATOM   436  C CD1 . TYR A 1 50  ? 30.97134  -10.20924 8.02139  1.000 30.09178 ? 50  TYR A CD1 1 
ATOM   437  C CD2 . TYR A 1 50  ? 30.40849  -7.91212  8.30447  1.000 28.78615 ? 50  TYR A CD2 1 
ATOM   438  C CE1 . TYR A 1 50  ? 32.12783  -9.84849  7.35784  1.000 34.17432 ? 50  TYR A CE1 1 
ATOM   439  C CE2 . TYR A 1 50  ? 31.56183  -7.54175  7.64362  1.000 33.45758 ? 50  TYR A CE2 1 
ATOM   440  C CZ  . TYR A 1 50  ? 32.41750  -8.51343  7.17166  1.000 39.26696 ? 50  TYR A CZ  1 
ATOM   441  O OH  . TYR A 1 50  ? 33.56820  -8.14784  6.51177  1.000 49.74120 ? 50  TYR A OH  1 
ATOM   442  N N   . HIS A 1 51  ? 29.21397  -7.63212  11.55503 1.000 11.26599 ? 51  HIS A N   1 
ATOM   443  C CA  . HIS A 1 51  ? 29.94763  -6.50738  12.12564 1.000 11.91673 ? 51  HIS A CA  1 
ATOM   444  C C   . HIS A 1 51  ? 30.23589  -6.69832  13.60900 1.000 11.96627 ? 51  HIS A C   1 
ATOM   445  O O   . HIS A 1 51  ? 31.25171  -6.19661  14.10469 1.000 12.85509 ? 51  HIS A O   1 
ATOM   446  C CB  . HIS A 1 51  ? 29.21033  -5.19305  11.86733 1.000 13.27041 ? 51  HIS A CB  1 
ATOM   447  C CG  . HIS A 1 51  ? 29.29990  -4.73057  10.44902 1.000 14.89900 ? 51  HIS A CG  1 
ATOM   448  N ND1 . HIS A 1 51  ? 28.18749  -4.44104  9.68986  1.000 14.55927 ? 51  HIS A ND1 1 
ATOM   449  C CD2 . HIS A 1 51  ? 30.37013  -4.51180  9.64845  1.000 16.93302 ? 51  HIS A CD2 1 
ATOM   450  C CE1 . HIS A 1 51  ? 28.56776  -4.06182  8.48300  1.000 16.00805 ? 51  HIS A CE1 1 
ATOM   451  N NE2 . HIS A 1 51  ? 29.88706  -4.09476  8.43247  1.000 17.20962 ? 51  HIS A NE2 1 
ATOM   452  N N   . TYR A 1 52  ? 29.36703  -7.40711  14.33538 1.000 11.99529 ? 52  TYR A N   1 
ATOM   453  C CA  . TYR A 1 52  ? 29.64097  -7.62596  15.75290 1.000 11.62110 ? 52  TYR A CA  1 
ATOM   454  C C   . TYR A 1 52  ? 30.85176  -8.52261  15.96983 1.000 11.82039 ? 52  TYR A C   1 
ATOM   455  O O   . TYR A 1 52  ? 31.61147  -8.31481  16.92668 1.000 13.03059 ? 52  TYR A O   1 
ATOM   456  C CB  . TYR A 1 52  ? 28.38976  -8.06652  16.52081 1.000 10.81852 ? 52  TYR A CB  1 
ATOM   457  C CG  . TYR A 1 52  ? 27.72064  -6.85491  17.13315 1.000 11.64958 ? 52  TYR A CG  1 
ATOM   458  C CD1 . TYR A 1 52  ? 28.10357  -6.39721  18.38667 1.000 14.62817 ? 52  TYR A CD1 1 
ATOM   459  C CD2 . TYR A 1 52  ? 26.77406  -6.11715  16.42699 1.000 11.92114 ? 52  TYR A CD2 1 
ATOM   460  C CE1 . TYR A 1 52  ? 27.54520  -5.27191  18.94291 1.000 16.06198 ? 52  TYR A CE1 1 
ATOM   461  C CE2 . TYR A 1 52  ? 26.19967  -4.97944  16.98009 1.000 13.64215 ? 52  TYR A CE2 1 
ATOM   462  C CZ  . TYR A 1 52  ? 26.59447  -4.56558  18.24269 1.000 16.13732 ? 52  TYR A CZ  1 
ATOM   463  O OH  . TYR A 1 52  ? 26.04529  -3.44173  18.80934 1.000 16.60426 ? 52  TYR A OH  1 
ATOM   464  N N   A GLN A 1 53  ? 31.05107  -9.51650  15.09895 0.500 12.97234 ? 53  GLN A N   1 
ATOM   465  N N   B GLN A 1 53  ? 31.06255  -9.51314  15.10248 0.500 12.41798 ? 53  GLN A N   1 
ATOM   466  C CA  A GLN A 1 53  ? 32.27683  -10.30629 15.15564 0.500 14.57857 ? 53  GLN A CA  1 
ATOM   467  C CA  B GLN A 1 53  ? 32.28380  -10.30342 15.20762 0.500 13.48207 ? 53  GLN A CA  1 
ATOM   468  C C   A GLN A 1 53  ? 33.49860  -9.41767  14.96741 0.500 14.47771 ? 53  GLN A C   1 
ATOM   469  C C   B GLN A 1 53  ? 33.51285  -9.42311  15.01456 0.500 14.08950 ? 53  GLN A C   1 
ATOM   470  O O   A GLN A 1 53  ? 34.51206  -9.58397  15.65590 0.500 15.69209 ? 53  GLN A O   1 
ATOM   471  O O   B GLN A 1 53  ? 34.51622  -9.57695  15.72075 0.500 14.93922 ? 53  GLN A O   1 
ATOM   472  C CB  A GLN A 1 53  ? 32.24181  -11.41517 14.10036 0.500 15.65211 ? 53  GLN A CB  1 
ATOM   473  C CB  B GLN A 1 53  ? 32.26535  -11.45384 14.20119 0.500 13.74850 ? 53  GLN A CB  1 
ATOM   474  C CG  A GLN A 1 53  ? 31.09247  -12.39089 14.28552 0.500 16.08583 ? 53  GLN A CG  1 
ATOM   475  C CG  B GLN A 1 53  ? 33.44498  -12.40259 14.33019 0.500 13.78034 ? 53  GLN A CG  1 
ATOM   476  C CD  A GLN A 1 53  ? 31.06677  -13.51158 13.26392 0.500 19.30138 ? 53  GLN A CD  1 
ATOM   477  O OE1 A GLN A 1 53  ? 31.18765  -14.68744 13.61357 0.500 17.95183 ? 53  GLN A OE1 1 
ATOM   478  N NE2 A GLN A 1 53  ? 30.88191  -13.15639 11.99805 0.500 19.66806 ? 53  GLN A NE2 1 
ATOM   479  N N   A LYS A 1 54  ? 33.40909  -8.44744  14.05600 0.700 13.74866 ? 54  LYS A N   1 
ATOM   480  N N   B LYS A 1 54  ? 33.43657  -8.46613  14.08683 0.300 14.43625 ? 54  LYS A N   1 
ATOM   481  C CA  A LYS A 1 54  ? 34.52110  -7.52854  13.84347 0.700 15.43362 ? 54  LYS A CA  1 
ATOM   482  C CA  B LYS A 1 54  ? 34.55429  -7.55315  13.87263 0.300 14.70101 ? 54  LYS A CA  1 
ATOM   483  C C   A LYS A 1 54  ? 34.71079  -6.60674  15.04151 0.700 13.76612 ? 54  LYS A C   1 
ATOM   484  C C   B LYS A 1 54  ? 34.72062  -6.59118  15.04336 0.300 13.51865 ? 54  LYS A C   1 
ATOM   485  O O   A LYS A 1 54  ? 35.84487  -6.34516  15.45718 0.700 12.54202 ? 54  LYS A O   1 
ATOM   486  O O   B LYS A 1 54  ? 35.84981  -6.28095  15.44011 0.300 12.76049 ? 54  LYS A O   1 
ATOM   487  C CB  A LYS A 1 54  ? 34.27988  -6.70576  12.57800 0.700 18.89697 ? 54  LYS A CB  1 
ATOM   488  C CB  B LYS A 1 54  ? 34.36296  -6.78191  12.56674 0.300 14.92074 ? 54  LYS A CB  1 
ATOM   489  C CG  A LYS A 1 54  ? 34.08340  -7.52788  11.31661 0.700 22.88400 ? 54  LYS A CG  1 
ATOM   490  C CG  B LYS A 1 54  ? 34.34975  -7.65342  11.32324 0.300 15.21117 ? 54  LYS A CG  1 
ATOM   491  C CD  A LYS A 1 54  ? 35.34250  -8.29601  10.96290 0.700 27.11110 ? 54  LYS A CD  1 
ATOM   492  C CD  B LYS A 1 54  ? 34.16697  -6.81710  10.06814 0.300 17.36931 ? 54  LYS A CD  1 
ATOM   493  C CE  A LYS A 1 54  ? 35.24373  -8.89383  9.57279  0.700 32.82108 ? 54  LYS A CE  1 
ATOM   494  N NZ  A LYS A 1 54  ? 36.53765  -9.48779  9.13605  0.700 40.69637 ? 54  LYS A NZ  1 
ATOM   495  N N   . MET A 1 55  ? 33.61068  -6.10331  15.60685 1.000 13.09927 ? 55  MET A N   1 
ATOM   496  C CA  . MET A 1 55  ? 33.70968  -5.16001  16.71808 1.000 13.03885 ? 55  MET A CA  1 
ATOM   497  C C   . MET A 1 55  ? 34.32933  -5.80253  17.95087 1.000 13.64982 ? 55  MET A C   1 
ATOM   498  O O   . MET A 1 55  ? 35.16065  -5.18081  18.62726 1.000 13.14487 ? 55  MET A O   1 
ATOM   499  C CB  . MET A 1 55  ? 32.34094  -4.56793  17.04816 1.000 13.11027 ? 55  MET A CB  1 
ATOM   500  C CG  . MET A 1 55  ? 31.91078  -3.46528  16.10438 1.000 13.95391 ? 55  MET A CG  1 
ATOM   501  S SD  . MET A 1 55  ? 30.33866  -2.72465  16.57011 1.000 15.39218 ? 55  MET A SD  1 
ATOM   502  C CE  . MET A 1 55  ? 29.20796  -3.65110  15.53496 1.000 14.75041 ? 55  MET A CE  1 
ATOM   503  N N   . GLY A 1 56  ? 33.93628  -7.03994  18.26380 1.000 14.93191 ? 56  GLY A N   1 
ATOM   504  C CA  . GLY A 1 56  ? 34.51911  -7.71362  19.41098 1.000 14.92110 ? 56  GLY A CA  1 
ATOM   505  C C   . GLY A 1 56  ? 36.01896  -7.88818  19.27374 1.000 15.27517 ? 56  GLY A C   1 
ATOM   506  O O   . GLY A 1 56  ? 36.77387  -7.62700  20.21430 1.000 16.36687 ? 56  GLY A O   1 
ATOM   507  N N   . ALA A 1 57  ? 36.47338  -8.31544  18.09082 1.000 16.03806 ? 57  ALA A N   1 
ATOM   508  C CA  . ALA A 1 57  ? 37.90687  -8.43671  17.84343 1.000 15.32262 ? 57  ALA A CA  1 
ATOM   509  C C   . ALA A 1 57  ? 38.59188  -7.07871  17.90809 1.000 14.07496 ? 57  ALA A C   1 
ATOM   510  O O   . ALA A 1 57  ? 39.70860  -6.96089  18.42572 1.000 15.11064 ? 57  ALA A O   1 
ATOM   511  C CB  . ALA A 1 57  ? 38.14839  -9.08292  16.48008 1.000 15.23356 ? 57  ALA A CB  1 
ATOM   512  N N   . SER A 1 58  ? 37.93811  -6.04499  17.37716 1.000 11.94609 ? 58  SER A N   1 
ATOM   513  C CA  . SER A 1 58  ? 38.49145  -4.69581  17.42452 1.000 13.42278 ? 58  SER A CA  1 
ATOM   514  C C   . SER A 1 58  ? 38.65632  -4.22714  18.86513 1.000 14.08329 ? 58  SER A C   1 
ATOM   515  O O   . SER A 1 58  ? 39.71156  -3.70508  19.24810 1.000 14.86106 ? 58  SER A O   1 
ATOM   516  C CB  . SER A 1 58  ? 37.57252  -3.74786  16.65647 1.000 12.93121 ? 58  SER A CB  1 
ATOM   517  O OG  . SER A 1 58  ? 38.14632  -2.46107  16.53692 1.000 12.79516 ? 58  SER A OG  1 
ATOM   518  N N   . TRP A 1 59  ? 37.61370  -4.40520  19.67933 1.000 14.47689 ? 59  TRP A N   1 
ATOM   519  C CA  . TRP A 1 59  ? 37.69662  -4.01513  21.08182 1.000 14.66836 ? 59  TRP A CA  1 
ATOM   520  C C   . TRP A 1 59  ? 38.77676  -4.80389  21.80718 1.000 16.59649 ? 59  TRP A C   1 
ATOM   521  O O   . TRP A 1 59  ? 39.56829  -4.23313  22.56797 1.000 16.04883 ? 59  TRP A O   1 
ATOM   522  C CB  . TRP A 1 59  ? 36.34784  -4.21676  21.76898 1.000 13.65700 ? 59  TRP A CB  1 
ATOM   523  C CG  . TRP A 1 59  ? 36.38512  -3.75806  23.17986 1.000 14.29457 ? 59  TRP A CG  1 
ATOM   524  C CD1 . TRP A 1 59  ? 36.56923  -4.52778  24.29074 1.000 13.99027 ? 59  TRP A CD1 1 
ATOM   525  C CD2 . TRP A 1 59  ? 36.27982  -2.40748  23.63594 1.000 16.10089 ? 59  TRP A CD2 1 
ATOM   526  N NE1 . TRP A 1 59  ? 36.57298  -3.73744  25.41432 1.000 16.21607 ? 59  TRP A NE1 1 
ATOM   527  C CE2 . TRP A 1 59  ? 36.39435  -2.43069  25.03891 1.000 16.14076 ? 59  TRP A CE2 1 
ATOM   528  C CE3 . TRP A 1 59  ? 36.09151  -1.17891  22.99229 1.000 15.63594 ? 59  TRP A CE3 1 
ATOM   529  C CZ2 . TRP A 1 59  ? 36.32235  -1.27082  25.81402 1.000 17.52383 ? 59  TRP A CZ2 1 
ATOM   530  C CZ3 . TRP A 1 59  ? 36.01955  -0.02994  23.76040 1.000 16.79015 ? 59  TRP A CZ3 1 
ATOM   531  C CH2 . TRP A 1 59  ? 36.13479  -0.08465  25.15788 1.000 17.81627 ? 59  TRP A CH2 1 
ATOM   532  N N   . GLU A 1 60  ? 38.82818  -6.11900  21.57499 1.000 17.15121 ? 60  GLU A N   1 
ATOM   533  C CA  . GLU A 1 60  ? 39.81786  -6.96464  22.23728 1.000 20.06042 ? 60  GLU A CA  1 
ATOM   534  C C   . GLU A 1 60  ? 41.24473  -6.52421  21.93286 1.000 19.33550 ? 60  GLU A C   1 
ATOM   535  O O   . GLU A 1 60  ? 42.12648  -6.65772  22.78708 1.000 19.51562 ? 60  GLU A O   1 
ATOM   536  C CB  . GLU A 1 60  ? 39.61525  -8.42578  21.83215 1.000 24.93237 ? 60  GLU A CB  1 
ATOM   537  C CG  . GLU A 1 60  ? 40.50635  -9.40736  22.57619 1.000 31.70195 ? 60  GLU A CG  1 
ATOM   538  C CD  . GLU A 1 60  ? 40.27403  -10.84388 22.15079 1.000 37.21751 ? 60  GLU A CD  1 
ATOM   539  O OE1 . GLU A 1 60  ? 39.88617  -11.06535 20.98278 1.000 38.56783 ? 60  GLU A OE1 1 
ATOM   540  O OE2 . GLU A 1 60  ? 40.47685  -11.75054 22.98605 1.000 42.90739 ? 60  GLU A OE2 1 
ATOM   541  N N   . SER A 1 61  ? 41.49011  -5.98703  20.73523 1.000 19.24507 ? 61  SER A N   1 
ATOM   542  C CA  . SER A 1 61  ? 42.84569  -5.59395  20.36239 1.000 18.42589 ? 61  SER A CA  1 
ATOM   543  C C   . SER A 1 61  ? 43.35974  -4.44754  21.22150 1.000 18.74908 ? 61  SER A C   1 
ATOM   544  O O   . SER A 1 61  ? 44.56958  -4.34056  21.45296 1.000 22.59645 ? 61  SER A O   1 
ATOM   545  C CB  . SER A 1 61  ? 42.87551  -5.17302  18.89403 1.000 17.54775 ? 61  SER A CB  1 
ATOM   546  O OG  . SER A 1 61  ? 42.27365  -3.90240  18.72189 1.000 18.84533 ? 61  SER A OG  1 
ATOM   547  N N   . GLY A 1 62  ? 42.46577  -3.57882  21.69270 1.000 18.43881 ? 62  GLY A N   1 
ATOM   548  C CA  . GLY A 1 62  ? 42.85175  -2.35986  22.36899 1.000 18.16909 ? 62  GLY A CA  1 
ATOM   549  C C   . GLY A 1 62  ? 42.85987  -1.12864  21.48832 1.000 17.89546 ? 62  GLY A C   1 
ATOM   550  O O   . GLY A 1 62  ? 42.96812  -0.01285  22.01207 1.000 19.95428 ? 62  GLY A O   1 
ATOM   551  N N   A SER A 1 63  ? 42.76039  -1.29955  20.17311 0.500 15.74625 ? 63  SER A N   1 
ATOM   552  N N   B SER A 1 63  ? 42.75535  -1.29379  20.17136 0.500 17.40487 ? 63  SER A N   1 
ATOM   553  C CA  A SER A 1 63  ? 42.66524  -0.20386  19.21264 0.500 14.81826 ? 63  SER A CA  1 
ATOM   554  C CA  B SER A 1 63  ? 42.66159  -0.18384  19.22235 0.500 17.11300 ? 63  SER A CA  1 
ATOM   555  C C   A SER A 1 63  ? 41.29977  -0.35122  18.54736 0.500 15.24884 ? 63  SER A C   1 
ATOM   556  C C   B SER A 1 63  ? 41.30920  -0.30164  18.52535 0.500 16.07892 ? 63  SER A C   1 
ATOM   557  O O   A SER A 1 63  ? 41.17662  -0.95423  17.47823 0.500 17.18658 ? 63  SER A O   1 
ATOM   558  O O   B SER A 1 63  ? 41.20509  -0.82126  17.41197 0.500 17.14394 ? 63  SER A O   1 
ATOM   559  C CB  A SER A 1 63  ? 43.80994  -0.28304  18.19595 0.500 14.08604 ? 63  SER A CB  1 
ATOM   560  C CB  B SER A 1 63  ? 43.83146  -0.20776  18.22308 0.500 18.00737 ? 63  SER A CB  1 
ATOM   561  O OG  A SER A 1 63  ? 43.70599  0.73660   17.21744 0.500 13.69648 ? 63  SER A OG  1 
ATOM   562  O OG  B SER A 1 63  ? 45.06171  0.07298   18.86707 0.500 19.67374 ? 63  SER A OG  1 
ATOM   563  N N   . TYR A 1 64  ? 40.26888  0.19310   19.18862 1.000 14.25489 ? 64  TYR A N   1 
ATOM   564  C CA  . TYR A 1 64  ? 38.90095  -0.02809  18.73915 1.000 14.97721 ? 64  TYR A CA  1 
ATOM   565  C C   . TYR A 1 64  ? 38.50483  0.92005   17.60932 1.000 14.05381 ? 64  TYR A C   1 
ATOM   566  O O   . TYR A 1 64  ? 38.87780  2.09769   17.60256 1.000 14.71308 ? 64  TYR A O   1 
ATOM   567  C CB  . TYR A 1 64  ? 37.93428  0.11115   19.91476 1.000 14.26023 ? 64  TYR A CB  1 
ATOM   568  C CG  . TYR A 1 64  ? 36.49264  -0.00905  19.50320 1.000 12.46917 ? 64  TYR A CG  1 
ATOM   569  C CD1 . TYR A 1 64  ? 35.96638  -1.23054  19.09791 1.000 11.51381 ? 64  TYR A CD1 1 
ATOM   570  C CD2 . TYR A 1 64  ? 35.65633  1.09632   19.50768 1.000 11.66524 ? 64  TYR A CD2 1 
ATOM   571  C CE1 . TYR A 1 64  ? 34.64622  -1.34635  18.70894 1.000 11.72897 ? 64  TYR A CE1 1 
ATOM   572  C CE2 . TYR A 1 64  ? 34.33319  0.99230   19.11934 1.000 11.98214 ? 64  TYR A CE2 1 
ATOM   573  C CZ  . TYR A 1 64  ? 33.82921  -0.23119  18.72244 1.000 12.03743 ? 64  TYR A CZ  1 
ATOM   574  O OH  . TYR A 1 64  ? 32.51230  -0.34281  18.33996 1.000 11.75947 ? 64  TYR A OH  1 
ATOM   575  N N   . ASP A 1 65  ? 37.72681  0.39507   16.65924 1.000 14.74475 ? 65  ASP A N   1 
ATOM   576  C CA  . ASP A 1 65  ? 37.30639  1.10813   15.45115 1.000 15.33691 ? 65  ASP A CA  1 
ATOM   577  C C   . ASP A 1 65  ? 35.78821  1.25862   15.49754 1.000 13.48253 ? 65  ASP A C   1 
ATOM   578  O O   . ASP A 1 65  ? 35.05535  0.33161   15.13477 1.000 13.50524 ? 65  ASP A O   1 
ATOM   579  C CB  . ASP A 1 65  ? 37.74736  0.32556   14.21151 1.000 17.25016 ? 65  ASP A CB  1 
ATOM   580  C CG  . ASP A 1 65  ? 37.38698  1.01689   12.90063 1.000 16.47076 ? 65  ASP A CG  1 
ATOM   581  O OD1 . ASP A 1 65  ? 36.90592  2.16964   12.90729 1.000 14.92235 ? 65  ASP A OD1 1 
ATOM   582  O OD2 . ASP A 1 65  ? 37.59546  0.38682   11.84243 1.000 19.33835 ? 65  ASP A OD2 1 
ATOM   583  N N   . THR A 1 66  ? 35.31352  2.42706   15.93938 1.000 12.67224 ? 66  THR A N   1 
ATOM   584  C CA  . THR A 1 66  ? 33.87968  2.69011   15.92348 1.000 10.81648 ? 66  THR A CA  1 
ATOM   585  C C   . THR A 1 66  ? 33.31869  2.76227   14.50751 1.000 12.65611 ? 66  THR A C   1 
ATOM   586  O O   . THR A 1 66  ? 32.09682  2.71199   14.34051 1.000 13.34291 ? 66  THR A O   1 
ATOM   587  C CB  . THR A 1 66  ? 33.54519  3.95597   16.73021 1.000 9.57300  ? 66  THR A CB  1 
ATOM   588  O OG1 . THR A 1 66  ? 32.14998  3.97043   17.06383 1.000 9.93487  ? 66  THR A OG1 1 
ATOM   589  C CG2 . THR A 1 66  ? 33.89419  5.21719   15.94372 1.000 10.43718 ? 66  THR A CG2 1 
ATOM   590  N N   . GLY A 1 67  ? 34.17897  2.85403   13.48920 1.000 13.45302 ? 67  GLY A N   1 
ATOM   591  C CA  . GLY A 1 67  ? 33.70252  2.79092   12.11695 1.000 13.27426 ? 67  GLY A CA  1 
ATOM   592  C C   . GLY A 1 67  ? 32.99133  1.49174   11.78662 1.000 12.05731 ? 67  GLY A C   1 
ATOM   593  O O   . GLY A 1 67  ? 32.11121  1.46648   10.92608 1.000 12.85569 ? 67  GLY A O   1 
ATOM   594  N N   . LEU A 1 68  ? 33.35795  0.39728   12.46118 1.000 11.03577 ? 68  LEU A N   1 
ATOM   595  C CA  . LEU A 1 68  ? 32.62870  -0.85651  12.28991 1.000 10.68241 ? 68  LEU A CA  1 
ATOM   596  C C   . LEU A 1 68  ? 31.18077  -0.71761  12.73950 1.000 10.19437 ? 68  LEU A C   1 
ATOM   597  O O   . LEU A 1 68  ? 30.26493  -1.22670  12.08307 1.000 12.18023 ? 68  LEU A O   1 
ATOM   598  C CB  . LEU A 1 68  ? 33.31179  -1.96225  13.08797 1.000 10.94171 ? 68  LEU A CB  1 
ATOM   599  C CG  . LEU A 1 68  ? 34.73210  -2.27058  12.63732 1.000 13.35049 ? 68  LEU A CG  1 
ATOM   600  C CD1 . LEU A 1 68  ? 35.43088  -3.11352  13.68246 1.000 13.99495 ? 68  LEU A CD1 1 
ATOM   601  C CD2 . LEU A 1 68  ? 34.70519  -2.98265  11.29288 1.000 14.98301 ? 68  LEU A CD2 1 
ATOM   602  N N   . ARG A 1 69  ? 30.95887  -0.04664  13.87100 1.000 10.17891 ? 69  ARG A N   1 
ATOM   603  C CA  . ARG A 1 69  ? 29.60493  0.17411   14.36311 1.000 10.91078 ? 69  ARG A CA  1 
ATOM   604  C C   . ARG A 1 69  ? 28.82145  1.07235   13.41492 1.000 10.76549 ? 69  ARG A C   1 
ATOM   605  O O   . ARG A 1 69  ? 27.66820  0.77936   13.06917 1.000 11.39590 ? 69  ARG A O   1 
ATOM   606  C CB  . ARG A 1 69  ? 29.66898  0.80292   15.75867 1.000 11.89140 ? 69  ARG A CB  1 
ATOM   607  C CG  . ARG A 1 69  ? 28.31651  1.02609   16.40592 1.000 11.98618 ? 69  ARG A CG  1 
ATOM   608  C CD  . ARG A 1 69  ? 28.02372  -0.04085  17.45710 1.000 11.84348 ? 69  ARG A CD  1 
ATOM   609  N NE  . ARG A 1 69  ? 28.93101  0.06532   18.59318 1.000 9.83941  ? 69  ARG A NE  1 
ATOM   610  C CZ  . ARG A 1 69  ? 28.90563  -0.72367  19.65943 1.000 11.25314 ? 69  ARG A CZ  1 
ATOM   611  N NH1 . ARG A 1 69  ? 28.03451  -1.71457  19.77032 1.000 12.14402 ? 69  ARG A NH1 1 
ATOM   612  N NH2 . ARG A 1 69  ? 29.77078  -0.50776  20.64504 1.000 10.75148 ? 69  ARG A NH2 1 
ATOM   613  N N   . TYR A 1 70  ? 29.44156  2.16785   12.97362 1.000 10.62773 ? 70  TYR A N   1 
ATOM   614  C CA  . TYR A 1 70  ? 28.72817  3.15439   12.17136 1.000 9.97540  ? 70  TYR A CA  1 
ATOM   615  C C   . TYR A 1 70  ? 28.41793  2.63661   10.77187 1.000 10.28887 ? 70  TYR A C   1 
ATOM   616  O O   . TYR A 1 70  ? 27.36749  2.96649   10.20769 1.000 11.65059 ? 70  TYR A O   1 
ATOM   617  C CB  . TYR A 1 70  ? 29.51053  4.46598   12.15190 1.000 10.28352 ? 70  TYR A CB  1 
ATOM   618  C CG  . TYR A 1 70  ? 29.18911  5.32740   13.35260 1.000 10.54406 ? 70  TYR A CG  1 
ATOM   619  C CD1 . TYR A 1 70  ? 29.79407  5.10307   14.58871 1.000 11.36856 ? 70  TYR A CD1 1 
ATOM   620  C CD2 . TYR A 1 70  ? 28.25487  6.34911   13.25553 1.000 10.60932 ? 70  TYR A CD2 1 
ATOM   621  C CE1 . TYR A 1 70  ? 29.48331  5.90025   15.69211 1.000 11.31485 ? 70  TYR A CE1 1 
ATOM   622  C CE2 . TYR A 1 70  ? 27.94115  7.14161   14.34218 1.000 10.93142 ? 70  TYR A CE2 1 
ATOM   623  C CZ  . TYR A 1 70  ? 28.55149  6.91536   15.55338 1.000 11.64577 ? 70  TYR A CZ  1 
ATOM   624  O OH  . TYR A 1 70  ? 28.21596  7.72012   16.61549 1.000 12.12405 ? 70  TYR A OH  1 
ATOM   625  N N   A VAL A 1 71  ? 29.29374  1.80320   10.20403 0.500 11.13297 ? 71  VAL A N   1 
ATOM   626  N N   B VAL A 1 71  ? 29.32319  1.84615   10.19017 0.500 9.86348  ? 71  VAL A N   1 
ATOM   627  C CA  A VAL A 1 71  ? 28.98736  1.21530   8.90186  0.500 11.87405 ? 71  VAL A CA  1 
ATOM   628  C CA  B VAL A 1 71  ? 29.01736  1.19016   8.92179  0.500 9.37434  ? 71  VAL A CA  1 
ATOM   629  C C   A VAL A 1 71  ? 27.88693  0.16519   9.02131  0.500 12.05396 ? 71  VAL A C   1 
ATOM   630  C C   B VAL A 1 71  ? 27.82215  0.26302   9.08274  0.500 9.86147  ? 71  VAL A C   1 
ATOM   631  O O   A VAL A 1 71  ? 27.10081  -0.02985  8.08563  0.500 13.85571 ? 71  VAL A O   1 
ATOM   632  O O   B VAL A 1 71  ? 26.90320  0.25981   8.25354  0.500 10.31063 ? 71  VAL A O   1 
ATOM   633  C CB  A VAL A 1 71  ? 30.25616  0.67747   8.21069  0.500 13.26851 ? 71  VAL A CB  1 
ATOM   634  C CB  B VAL A 1 71  ? 30.25588  0.45478   8.37530  0.500 9.50972  ? 71  VAL A CB  1 
ATOM   635  C CG1 A VAL A 1 71  ? 30.74794  -0.59377  8.88979  0.500 14.10764 ? 71  VAL A CG1 1 
ATOM   636  C CG1 B VAL A 1 71  ? 29.85023  -0.58169  7.34057  0.500 9.18606  ? 71  VAL A CG1 1 
ATOM   637  C CG2 A VAL A 1 71  ? 29.99268  0.43539   6.73369  0.500 13.55429 ? 71  VAL A CG2 1 
ATOM   638  C CG2 B VAL A 1 71  ? 31.22445  1.44307   7.76793  0.500 9.28415  ? 71  VAL A CG2 1 
ATOM   639  N N   . ASP A 1 72  ? 27.80539  -0.52525  10.16223 1.000 10.25209 ? 72  ASP A N   1 
ATOM   640  C CA  . ASP A 1 72  ? 26.67724  -1.41944  10.39978 1.000 10.47225 ? 72  ASP A CA  1 
ATOM   641  C C   . ASP A 1 72  ? 25.37777  -0.63548  10.48615 1.000 11.05452 ? 72  ASP A C   1 
ATOM   642  O O   . ASP A 1 72  ? 24.36643  -1.02802  9.89488  1.000 11.71637 ? 72  ASP A O   1 
ATOM   643  C CB  . ASP A 1 72  ? 26.88312  -2.21320  11.68638 1.000 11.32119 ? 72  ASP A CB  1 
ATOM   644  C CG  . ASP A 1 72  ? 25.86179  -3.31796  11.84630 1.000 13.41821 ? 72  ASP A CG  1 
ATOM   645  O OD1 . ASP A 1 72  ? 25.91571  -4.28799  11.06315 1.000 15.25663 ? 72  ASP A OD1 1 
ATOM   646  O OD2 . ASP A 1 72  ? 25.00078  -3.21991  12.74118 1.000 15.57868 ? 72  ASP A OD2 1 
ATOM   647  N N   . TRP A 1 73  ? 25.39577  0.48664   11.20579 1.000 9.64500  ? 73  TRP A N   1 
ATOM   648  C CA  . TRP A 1 73  ? 24.20214  1.31258   11.33318 1.000 9.32984  ? 73  TRP A CA  1 
ATOM   649  C C   . TRP A 1 73  ? 23.76800  1.87631   9.98896  1.000 10.01195 ? 73  TRP A C   1 
ATOM   650  O O   . TRP A 1 73  ? 22.57343  1.88542   9.66886  1.000 10.87901 ? 73  TRP A O   1 
ATOM   651  C CB  . TRP A 1 73  ? 24.47562  2.46204   12.29302 1.000 9.48953  ? 73  TRP A CB  1 
ATOM   652  C CG  . TRP A 1 73  ? 24.63916  2.05854   13.71273 1.000 9.42651  ? 73  TRP A CG  1 
ATOM   653  C CD1 . TRP A 1 73  ? 24.46617  0.81228   14.24755 1.000 9.86200  ? 73  TRP A CD1 1 
ATOM   654  C CD2 . TRP A 1 73  ? 25.00367  2.91607   14.79321 1.000 9.58708  ? 73  TRP A CD2 1 
ATOM   655  N NE1 . TRP A 1 73  ? 24.69623  0.84760   15.60443 1.000 9.49800  ? 73  TRP A NE1 1 
ATOM   656  C CE2 . TRP A 1 73  ? 25.03188  2.12849   15.96166 1.000 9.82496  ? 73  TRP A CE2 1 
ATOM   657  C CE3 . TRP A 1 73  ? 25.31482  4.27830   14.88700 1.000 10.22043 ? 73  TRP A CE3 1 
ATOM   658  C CZ2 . TRP A 1 73  ? 25.35523  2.65935   17.21143 1.000 10.01518 ? 73  TRP A CZ2 1 
ATOM   659  C CZ3 . TRP A 1 73  ? 25.63568  4.80256   16.12972 1.000 11.95297 ? 73  TRP A CZ3 1 
ATOM   660  C CH2 . TRP A 1 73  ? 25.65665  3.99331   17.27356 1.000 10.96378 ? 73  TRP A CH2 1 
ATOM   661  N N   . VAL A 1 74  ? 24.71873  2.36888   9.19121  1.000 10.12414 ? 74  VAL A N   1 
ATOM   662  C CA  . VAL A 1 74  ? 24.32788  3.03343   7.94969  1.000 11.90525 ? 74  VAL A CA  1 
ATOM   663  C C   . VAL A 1 74  ? 23.68018  2.05216   6.97913  1.000 12.18083 ? 74  VAL A C   1 
ATOM   664  O O   . VAL A 1 74  ? 22.83013  2.44257   6.16671  1.000 13.30707 ? 74  VAL A O   1 
ATOM   665  C CB  . VAL A 1 74  ? 25.49805  3.82372   7.33117  1.000 13.58349 ? 74  VAL A CB  1 
ATOM   666  C CG1 . VAL A 1 74  ? 26.40836  2.90742   6.53029  1.000 12.97985 ? 74  VAL A CG1 1 
ATOM   667  C CG2 . VAL A 1 74  ? 24.96773  4.97102   6.46995  1.000 14.98269 ? 74  VAL A CG2 1 
ATOM   668  N N   . LEU A 1 75  ? 24.03605  0.76849   7.06321  1.000 12.15282 ? 75  LEU A N   1 
ATOM   669  C CA  . LEU A 1 75  ? 23.41528  -0.24649  6.22178  1.000 13.56613 ? 75  LEU A CA  1 
ATOM   670  C C   . LEU A 1 75  ? 22.10266  -0.76419  6.80028  1.000 14.56060 ? 75  LEU A C   1 
ATOM   671  O O   . LEU A 1 75  ? 21.13632  -0.96852  6.05547  1.000 18.03899 ? 75  LEU A O   1 
ATOM   672  C CB  . LEU A 1 75  ? 24.38360  -1.41346  6.01013  1.000 13.60830 ? 75  LEU A CB  1 
ATOM   673  C CG  . LEU A 1 75  ? 25.70126  -1.08178  5.31261  1.000 16.37681 ? 75  LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 75  ? 26.64952  -2.27581  5.34412  1.000 16.08222 ? 75  LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 75  ? 25.44807  -0.62827  3.87747  1.000 18.92649 ? 75  LEU A CD2 1 
ATOM   676  N N   . THR A 1 76  ? 22.03667  -0.97084  8.11826  1.000 11.90745 ? 76  THR A N   1 
ATOM   677  C CA  . THR A 1 76  ? 20.88161  -1.65666  8.68877  1.000 10.68378 ? 76  THR A CA  1 
ATOM   678  C C   . THR A 1 76  ? 19.71540  -0.72244  8.98162  1.000 11.37726 ? 76  THR A C   1 
ATOM   679  O O   . THR A 1 76  ? 18.56137  -1.14809  8.87655  1.000 11.65952 ? 76  THR A O   1 
ATOM   680  C CB  . THR A 1 76  ? 21.27000  -2.40725  9.96407  1.000 10.23959 ? 76  THR A CB  1 
ATOM   681  O OG1 . THR A 1 76  ? 21.86722  -1.49531  10.89210 1.000 11.66474 ? 76  THR A OG1 1 
ATOM   682  C CG2 . THR A 1 76  ? 22.24154  -3.54917  9.65584  1.000 11.62402 ? 76  THR A CG2 1 
ATOM   683  N N   . VAL A 1 77  ? 19.97827  0.52633   9.37669  1.000 10.68594 ? 77  VAL A N   1 
ATOM   684  C CA  . VAL A 1 77  ? 18.87813  1.44039   9.69764  1.000 11.21767 ? 77  VAL A CA  1 
ATOM   685  C C   . VAL A 1 77  ? 17.91515  1.63051   8.53300  1.000 10.66759 ? 77  VAL A C   1 
ATOM   686  O O   . VAL A 1 77  ? 16.69990  1.46880   8.73318  1.000 11.28703 ? 77  VAL A O   1 
ATOM   687  C CB  . VAL A 1 77  ? 19.41468  2.75333   10.29982 1.000 12.00331 ? 77  VAL A CB  1 
ATOM   688  C CG1 . VAL A 1 77  ? 18.28527  3.76562   10.44106 1.000 12.59743 ? 77  VAL A CG1 1 
ATOM   689  C CG2 . VAL A 1 77  ? 20.05119  2.49713   11.65399 1.000 11.86970 ? 77  VAL A CG2 1 
ATOM   690  N N   . PRO A 1 78  ? 18.36029  1.96542   7.31599  1.000 12.96477 ? 78  PRO A N   1 
ATOM   691  C CA  . PRO A 1 78  ? 17.39713  2.07462   6.20869  1.000 14.06609 ? 78  PRO A CA  1 
ATOM   692  C C   . PRO A 1 78  ? 16.66657  0.77636   5.93383  1.000 14.19311 ? 78  PRO A C   1 
ATOM   693  O O   . PRO A 1 78  ? 15.49072  0.80258   5.54486  1.000 13.26374 ? 78  PRO A O   1 
ATOM   694  C CB  . PRO A 1 78  ? 18.27103  2.49724   5.01883  1.000 15.52474 ? 78  PRO A CB  1 
ATOM   695  C CG  . PRO A 1 78  ? 19.49447  3.08102   5.62458  1.000 18.19465 ? 78  PRO A CG  1 
ATOM   696  C CD  . PRO A 1 78  ? 19.72685  2.31324   6.88250  1.000 15.21221 ? 78  PRO A CD  1 
ATOM   697  N N   A LEU A 1 79  ? 17.33028  -0.36943  6.11135  0.500 14.37683 ? 79  LEU A N   1 
ATOM   698  N N   B LEU A 1 79  ? 17.33057  -0.36146  6.14121  0.500 14.89444 ? 79  LEU A N   1 
ATOM   699  C CA  A LEU A 1 79  ? 16.64574  -1.64490  5.92660  0.500 14.28962 ? 79  LEU A CA  1 
ATOM   700  C CA  B LEU A 1 79  ? 16.68306  -1.65157  5.94011  0.500 15.37713 ? 79  LEU A CA  1 
ATOM   701  C C   A LEU A 1 79  ? 15.53275  -1.82173  6.94841  0.500 14.80626 ? 79  LEU A C   1 
ATOM   702  C C   B LEU A 1 79  ? 15.57346  -1.87497  6.96081  0.500 15.47068 ? 79  LEU A C   1 
ATOM   703  O O   A LEU A 1 79  ? 14.45716  -2.33340  6.62056  0.500 14.81574 ? 79  LEU A O   1 
ATOM   704  O O   B LEU A 1 79  ? 14.53976  -2.47323  6.64231  0.500 15.57584 ? 79  LEU A O   1 
ATOM   705  C CB  A LEU A 1 79  ? 17.64049  -2.80329  6.00630  0.500 14.28079 ? 79  LEU A CB  1 
ATOM   706  C CB  B LEU A 1 79  ? 17.73307  -2.75642  6.02565  0.500 16.21554 ? 79  LEU A CB  1 
ATOM   707  C CG  A LEU A 1 79  ? 18.57605  -2.99171  4.81312  0.500 12.87586 ? 79  LEU A CG  1 
ATOM   708  C CG  B LEU A 1 79  ? 17.45148  -4.07156  5.31122  0.500 15.58119 ? 79  LEU A CG  1 
ATOM   709  C CD1 A LEU A 1 79  ? 19.60721  -4.05981  5.12666  0.500 13.88164 ? 79  LEU A CD1 1 
ATOM   710  C CD1 B LEU A 1 79  ? 17.01671  -3.82314  3.87683  0.500 15.02031 ? 79  LEU A CD1 1 
ATOM   711  C CD2 A LEU A 1 79  ? 17.78719  -3.35537  3.56573  0.500 13.29054 ? 79  LEU A CD2 1 
ATOM   712  C CD2 B LEU A 1 79  ? 18.70266  -4.92449  5.35021  0.500 15.82251 ? 79  LEU A CD2 1 
ATOM   713  N N   . MET A 1 80  ? 15.76869  -1.39751  8.19293  1.000 14.17136 ? 80  MET A N   1 
ATOM   714  C CA  . MET A 1 80  ? 14.72764  -1.50777  9.20762  1.000 14.64931 ? 80  MET A CA  1 
ATOM   715  C C   . MET A 1 80  ? 13.50463  -0.67683  8.84081  1.000 12.34924 ? 80  MET A C   1 
ATOM   716  O O   . MET A 1 80  ? 12.37552  -1.07004  9.14990  1.000 14.69218 ? 80  MET A O   1 
ATOM   717  C CB  . MET A 1 80  ? 15.28378  -1.11421  10.57645 1.000 14.08885 ? 80  MET A CB  1 
ATOM   718  C CG  . MET A 1 80  ? 16.34191  -2.08565  11.08482 1.000 14.88764 ? 80  MET A CG  1 
ATOM   719  S SD  . MET A 1 80  ? 17.34398  -1.47363  12.45557 1.000 16.28538 ? 80  MET A SD  1 
ATOM   720  C CE  . MET A 1 80  ? 16.24397  -1.75225  13.83459 1.000 17.39564 ? 80  MET A CE  1 
ATOM   721  N N   . PHE A 1 81  ? 13.70485  0.44856   8.14434  1.000 12.14957 ? 81  PHE A N   1 
ATOM   722  C CA  . PHE A 1 81  ? 12.58035  1.27450   7.71106  1.000 14.02338 ? 81  PHE A CA  1 
ATOM   723  C C   . PHE A 1 81  ? 11.79611  0.62097   6.57654  1.000 16.96360 ? 81  PHE A C   1 
ATOM   724  O O   . PHE A 1 81  ? 10.59815  0.89164   6.41692  1.000 15.50894 ? 81  PHE A O   1 
ATOM   725  C CB  . PHE A 1 81  ? 13.08966  2.64714   7.27043  1.000 14.53548 ? 81  PHE A CB  1 
ATOM   726  C CG  . PHE A 1 81  ? 13.57606  3.51151   8.40370  1.000 14.59851 ? 81  PHE A CG  1 
ATOM   727  C CD1 . PHE A 1 81  ? 13.09818  3.32783   9.68891  1.000 14.11574 ? 81  PHE A CD1 1 
ATOM   728  C CD2 . PHE A 1 81  ? 14.49672  4.52110   8.17604  1.000 15.35068 ? 81  PHE A CD2 1 
ATOM   729  C CE1 . PHE A 1 81  ? 13.54071  4.12989   10.73113 1.000 15.27170 ? 81  PHE A CE1 1 
ATOM   730  C CE2 . PHE A 1 81  ? 14.94057  5.32680   9.21308  1.000 17.12776 ? 81  PHE A CE2 1 
ATOM   731  C CZ  . PHE A 1 81  ? 14.46064  5.13103   10.49113 1.000 16.24231 ? 81  PHE A CZ  1 
ATOM   732  N N   A VAL A 1 82  ? 12.45876  -0.21020  5.76655  0.700 19.04151 ? 82  VAL A N   1 
ATOM   733  N N   B VAL A 1 82  ? 12.44715  -0.25270  5.80439  0.300 18.95723 ? 82  VAL A N   1 
ATOM   734  C CA  A VAL A 1 82  ? 11.79266  -0.86447  4.64077  0.700 20.36461 ? 82  VAL A CA  1 
ATOM   735  C CA  B VAL A 1 82  ? 11.78003  -0.94763  4.70489  0.300 20.61945 ? 82  VAL A CA  1 
ATOM   736  C C   A VAL A 1 82  ? 10.52771  -1.57133  5.10679  0.700 21.75002 ? 82  VAL A C   1 
ATOM   737  C C   B VAL A 1 82  ? 10.56518  -1.71826  5.21259  0.300 22.42571 ? 82  VAL A C   1 
ATOM   738  O O   A VAL A 1 82  ? 9.44229   -1.38470  4.54218  0.700 21.02917 ? 82  VAL A O   1 
ATOM   739  O O   B VAL A 1 82  ? 9.47414   -1.64605  4.63388  0.300 22.85169 ? 82  VAL A O   1 
ATOM   740  C CB  A VAL A 1 82  ? 12.76097  -1.82749  3.92856  0.700 20.05662 ? 82  VAL A CB  1 
ATOM   741  C CB  B VAL A 1 82  ? 12.78152  -1.86018  3.97176  0.300 20.24619 ? 82  VAL A CB  1 
ATOM   742  C CG1 A VAL A 1 82  ? 11.99702  -2.85118  3.10784  0.700 20.74685 ? 82  VAL A CG1 1 
ATOM   743  C CG1 B VAL A 1 82  ? 12.07394  -2.76044  2.97631  0.300 20.46668 ? 82  VAL A CG1 1 
ATOM   744  C CG2 A VAL A 1 82  ? 13.73005  -1.05215  3.05109  0.700 20.76470 ? 82  VAL A CG2 1 
ATOM   745  C CG2 B VAL A 1 82  ? 13.85142  -1.02486  3.28211  0.300 20.45007 ? 82  VAL A CG2 1 
ATOM   746  N N   A GLU A 1 83  ? 10.64132  -2.37379  6.16513  0.700 23.42692 ? 83  GLU A N   1 
ATOM   747  N N   B GLU A 1 83  ? 10.73190  -2.45774  6.31180  0.300 23.31642 ? 83  GLU A N   1 
ATOM   748  C CA  A GLU A 1 83  ? 9.47774   -3.13442  6.59735  0.700 27.39580 ? 83  GLU A CA  1 
ATOM   749  C CA  B GLU A 1 83  ? 9.63007   -3.26401  6.83108  0.300 26.67488 ? 83  GLU A CA  1 
ATOM   750  C C   A GLU A 1 83  ? 8.52754   -2.32170  7.46239  0.700 23.15113 ? 83  GLU A C   1 
ATOM   751  C C   B GLU A 1 83  ? 8.58870   -2.40179  7.53629  0.300 22.73291 ? 83  GLU A C   1 
ATOM   752  O O   A GLU A 1 83  ? 7.32015   -2.58627  7.45104  0.700 23.14810 ? 83  GLU A O   1 
ATOM   753  O O   B GLU A 1 83  ? 7.38674   -2.68153  7.45901  0.300 23.28694 ? 83  GLU A O   1 
ATOM   754  C CB  A GLU A 1 83  ? 9.87913   -4.41630  7.31744  0.700 33.36733 ? 83  GLU A CB  1 
ATOM   755  C CB  B GLU A 1 83  ? 10.16787  -4.33899  7.77569  0.300 32.42410 ? 83  GLU A CB  1 
ATOM   756  C CG  A GLU A 1 83  ? 8.83964   -5.48031  7.14027  0.700 38.87091 ? 83  GLU A CG  1 
ATOM   757  C CD  A GLU A 1 83  ? 8.59067   -5.77858  5.67276  0.700 38.10346 ? 83  GLU A CD  1 
ATOM   758  O OE1 A GLU A 1 83  ? 9.57703   -5.88131  4.91084  0.700 37.46634 ? 83  GLU A OE1 1 
ATOM   759  O OE2 A GLU A 1 83  ? 7.41452   -5.91296  5.28139  0.700 36.81200 ? 83  GLU A OE2 1 
ATOM   760  N N   . VAL A 1 84  ? 9.03291   -1.35051  8.22500  1.000 19.22075 ? 84  VAL A N   1 
ATOM   761  C CA  . VAL A 1 84  ? 8.12448   -0.49911  8.98857  1.000 18.92389 ? 84  VAL A CA  1 
ATOM   762  C C   . VAL A 1 84  ? 7.17962   0.24600   8.05109  1.000 18.05856 ? 84  VAL A C   1 
ATOM   763  O O   . VAL A 1 84  ? 5.96025   0.27073   8.25823  1.000 19.59261 ? 84  VAL A O   1 
ATOM   764  C CB  . VAL A 1 84  ? 8.91381   0.45361   9.90479  1.000 18.71928 ? 84  VAL A CB  1 
ATOM   765  C CG1 . VAL A 1 84  ? 7.98288   1.46821   10.54834 1.000 19.88804 ? 84  VAL A CG1 1 
ATOM   766  C CG2 . VAL A 1 84  ? 9.66541   -0.33347  10.97092 1.000 18.42865 ? 84  VAL A CG2 1 
ATOM   767  N N   . LEU A 1 85  ? 7.72473   0.83391   6.98378  1.000 15.29792 ? 85  LEU A N   1 
ATOM   768  C CA  . LEU A 1 85  ? 6.90670   1.61317   6.05826  1.000 13.83747 ? 85  LEU A CA  1 
ATOM   769  C C   . LEU A 1 85  ? 5.99917   0.74491   5.19025  1.000 15.03860 ? 85  LEU A C   1 
ATOM   770  O O   . LEU A 1 85  ? 4.96128   1.23064   4.72572  1.000 16.63890 ? 85  LEU A O   1 
ATOM   771  C CB  . LEU A 1 85  ? 7.79797   2.52130   5.20493  1.000 13.39748 ? 85  LEU A CB  1 
ATOM   772  C CG  . LEU A 1 85  ? 8.42493   3.69580   5.96213  1.000 14.59201 ? 85  LEU A CG  1 
ATOM   773  C CD1 . LEU A 1 85  ? 9.58693   4.31102   5.19413  1.000 14.81126 ? 85  LEU A CD1 1 
ATOM   774  C CD2 . LEU A 1 85  ? 7.36246   4.74511   6.25792  1.000 15.61604 ? 85  LEU A CD2 1 
ATOM   775  N N   . ALA A 1 86  ? 6.35449   -0.52578  4.97339  1.000 13.60134 ? 86  ALA A N   1 
ATOM   776  C CA  . ALA A 1 86  ? 5.49560   -1.42608  4.20897  1.000 14.98762 ? 86  ALA A CA  1 
ATOM   777  C C   . ALA A 1 86  ? 4.15027   -1.66961  4.88366  1.000 16.66674 ? 86  ALA A C   1 
ATOM   778  O O   . ALA A 1 86  ? 3.17760   -2.00570  4.19667  1.000 17.98035 ? 86  ALA A O   1 
ATOM   779  C CB  . ALA A 1 86  ? 6.20543   -2.75954  3.97365  1.000 15.27869 ? 86  ALA A CB  1 
ATOM   780  N N   . VAL A 1 87  ? 4.07147   -1.50418  6.20659  1.000 17.32292 ? 87  VAL A N   1 
ATOM   781  C CA  . VAL A 1 87  ? 2.81107   -1.72017  6.91011  1.000 17.44907 ? 87  VAL A CA  1 
ATOM   782  C C   . VAL A 1 87  ? 1.77541   -0.69456  6.47368  1.000 17.58572 ? 87  VAL A C   1 
ATOM   783  O O   . VAL A 1 87  ? 0.58556   -1.00754  6.33629  1.000 18.37065 ? 87  VAL A O   1 
ATOM   784  C CB  . VAL A 1 87  ? 3.03931   -1.69238  8.43448  1.000 19.68353 ? 87  VAL A CB  1 
ATOM   785  C CG1 . VAL A 1 87  ? 1.71460   -1.80588  9.18333  1.000 19.65584 ? 87  VAL A CG1 1 
ATOM   786  C CG2 . VAL A 1 87  ? 3.98926   -2.80507  8.85211  1.000 19.40125 ? 87  VAL A CG2 1 
ATOM   787  N N   . THR A 1 88  ? 2.21555   0.53763   6.21794  1.000 17.62335 ? 88  THR A N   1 
ATOM   788  C CA  . THR A 1 88  ? 1.30951   1.65800   6.02770  1.000 18.47214 ? 88  THR A CA  1 
ATOM   789  C C   . THR A 1 88  ? 1.26712   2.21162   4.60897  1.000 19.76711 ? 88  THR A C   1 
ATOM   790  O O   . THR A 1 88  ? 0.33867   2.96263   4.28961  1.000 20.28602 ? 88  THR A O   1 
ATOM   791  C CB  . THR A 1 88  ? 1.66958   2.79137   7.00017  1.000 19.00226 ? 88  THR A CB  1 
ATOM   792  O OG1 . THR A 1 88  ? 3.06443   3.09904   6.88131  1.000 19.89499 ? 88  THR A OG1 1 
ATOM   793  C CG2 . THR A 1 88  ? 1.38579   2.36435   8.43029  1.000 20.61511 ? 88  THR A CG2 1 
ATOM   794  N N   . ARG A 1 89  ? 2.22806   1.86980   3.75344  1.000 19.19060 ? 89  ARG A N   1 
ATOM   795  C CA  . ARG A 1 89  ? 2.30805   2.47768   2.43490  1.000 19.96509 ? 89  ARG A CA  1 
ATOM   796  C C   . ARG A 1 89  ? 2.71244   1.44590   1.39459  1.000 20.39408 ? 89  ARG A C   1 
ATOM   797  O O   . ARG A 1 89  ? 3.40072   0.46723   1.69499  1.000 20.92507 ? 89  ARG A O   1 
ATOM   798  C CB  . ARG A 1 89  ? 3.34281   3.60756   2.40372  1.000 22.89218 ? 89  ARG A CB  1 
ATOM   799  C CG  . ARG A 1 89  ? 3.03134   4.79196   3.29930  1.000 26.29689 ? 89  ARG A CG  1 
ATOM   800  C CD  . ARG A 1 89  ? 4.31711   5.49372   3.70818  1.000 28.09592 ? 89  ARG A CD  1 
ATOM   801  N NE  . ARG A 1 89  ? 4.06672   6.68850   4.50305  1.000 29.26040 ? 89  ARG A NE  1 
ATOM   802  C CZ  . ARG A 1 89  ? 4.23872   7.92758   4.06446  1.000 31.59098 ? 89  ARG A CZ  1 
ATOM   803  N NH1 . ARG A 1 89  ? 4.67730   8.17242   2.84020  1.000 31.61828 ? 89  ARG A NH1 1 
ATOM   804  N NH2 . ARG A 1 89  ? 3.97104   8.94652   4.87709  1.000 33.04961 ? 89  ARG A NH2 1 
ATOM   805  N N   . LYS A 1 90  ? 2.27967   1.68478   0.15907  1.000 20.76057 ? 90  LYS A N   1 
ATOM   806  C CA  . LYS A 1 90  ? 2.79947   0.97337   -0.99856 1.000 19.94814 ? 90  LYS A CA  1 
ATOM   807  C C   . LYS A 1 90  ? 2.93588   1.96834   -2.14080 1.000 20.55980 ? 90  LYS A C   1 
ATOM   808  O O   . LYS A 1 90  ? 2.54491   3.13262   -2.02477 1.000 21.88584 ? 90  LYS A O   1 
ATOM   809  C CB  . LYS A 1 90  ? 1.91334   -0.21354  -1.39331 1.000 20.93856 ? 90  LYS A CB  1 
ATOM   810  C CG  . LYS A 1 90  ? 0.56826   0.19114   -1.95223 1.000 20.41248 ? 90  LYS A CG  1 
ATOM   811  C CD  . LYS A 1 90  ? -0.33614  -1.01378  -2.20615 1.000 20.03339 ? 90  LYS A CD  1 
ATOM   812  C CE  . LYS A 1 90  ? 0.31516   -2.02362  -3.13539 1.000 21.27489 ? 90  LYS A CE  1 
ATOM   813  N NZ  . LYS A 1 90  ? -0.63078  -3.10802  -3.51829 1.000 22.92653 ? 90  LYS A NZ  1 
ATOM   814  N N   . GLY A 1 91  ? 3.50900   1.50316   -3.24715 1.000 19.17365 ? 91  GLY A N   1 
ATOM   815  C CA  . GLY A 1 91  ? 3.57876   2.33280   -4.44038 1.000 18.23341 ? 91  GLY A CA  1 
ATOM   816  C C   . GLY A 1 91  ? 4.39354   3.59079   -4.22033 1.000 18.05665 ? 91  GLY A C   1 
ATOM   817  O O   . GLY A 1 91  ? 5.41751   3.58900   -3.52618 1.000 16.63729 ? 91  GLY A O   1 
ATOM   818  N N   . ALA A 1 92  ? 3.91486   4.69315   -4.80384 1.000 19.91021 ? 92  ALA A N   1 
ATOM   819  C CA  . ALA A 1 92  ? 4.67044   5.94235   -4.78357 1.000 21.68367 ? 92  ALA A CA  1 
ATOM   820  C C   . ALA A 1 92  ? 4.88255   6.45389   -3.36338 1.000 22.20427 ? 92  ALA A C   1 
ATOM   821  O O   . ALA A 1 92  ? 5.97060   6.93721   -3.03090 1.000 22.79130 ? 92  ALA A O   1 
ATOM   822  C CB  . ALA A 1 92  ? 3.97112   6.99551   -5.64254 1.000 23.19216 ? 92  ALA A CB  1 
ATOM   823  N N   . ALA A 1 93  ? 3.85806   6.35583   -2.50987 1.000 21.46584 ? 93  ALA A N   1 
ATOM   824  C CA  . ALA A 1 93  ? 3.99706   6.83653   -1.13685 1.000 20.52806 ? 93  ALA A CA  1 
ATOM   825  C C   . ALA A 1 93  ? 5.07906   6.06696   -0.39174 1.000 18.46939 ? 93  ALA A C   1 
ATOM   826  O O   . ALA A 1 93  ? 5.83543   6.64346   0.39998  1.000 17.84018 ? 93  ALA A O   1 
ATOM   827  C CB  . ALA A 1 93  ? 2.66037   6.73485   -0.40123 1.000 21.13280 ? 93  ALA A CB  1 
ATOM   828  N N   . TYR A 1 94  ? 5.17854   4.76371   -0.64737 1.000 16.06782 ? 94  TYR A N   1 
ATOM   829  C CA  . TYR A 1 94  ? 6.18848   3.94775   0.01278  1.000 14.86521 ? 94  TYR A CA  1 
ATOM   830  C C   . TYR A 1 94  ? 7.58922   4.30400   -0.47221 1.000 15.52968 ? 94  TYR A C   1 
ATOM   831  O O   . TYR A 1 94  ? 8.51222   4.47358   0.33438  1.000 15.62426 ? 94  TYR A O   1 
ATOM   832  C CB  . TYR A 1 94  ? 5.88680   2.47517   -0.24644 1.000 14.98113 ? 94  TYR A CB  1 
ATOM   833  C CG  . TYR A 1 94  ? 6.94567   1.53751   0.25500  1.000 16.04429 ? 94  TYR A CG  1 
ATOM   834  C CD1 . TYR A 1 94  ? 6.96379   1.12924   1.57935  1.000 16.30976 ? 94  TYR A CD1 1 
ATOM   835  C CD2 . TYR A 1 94  ? 7.92485   1.04555   -0.59913 1.000 17.60231 ? 94  TYR A CD2 1 
ATOM   836  C CE1 . TYR A 1 94  ? 7.93239   0.26528   2.04368  1.000 18.64077 ? 94  TYR A CE1 1 
ATOM   837  C CE2 . TYR A 1 94  ? 8.89505   0.18223   -0.14750 1.000 18.34544 ? 94  TYR A CE2 1 
ATOM   838  C CZ  . TYR A 1 94  ? 8.89406   -0.20460  1.17586  1.000 19.14812 ? 94  TYR A CZ  1 
ATOM   839  O OH  . TYR A 1 94  ? 9.85581   -1.06299  1.63471  1.000 21.39096 ? 94  TYR A OH  1 
ATOM   840  N N   . ASN A 1 95  ? 7.76741   4.41094   -1.79325 1.000 17.80482 ? 95  ASN A N   1 
ATOM   841  C CA  . ASN A 1 95  ? 9.08374   4.71268   -2.34855 1.000 20.32712 ? 95  ASN A CA  1 
ATOM   842  C C   . ASN A 1 95  ? 9.60015   6.05256   -1.84470 1.000 20.99194 ? 95  ASN A C   1 
ATOM   843  O O   . ASN A 1 95  ? 10.78920  6.19221   -1.53373 1.000 22.59608 ? 95  ASN A O   1 
ATOM   844  C CB  . ASN A 1 95  ? 9.02476   4.71292   -3.87701 1.000 22.13241 ? 95  ASN A CB  1 
ATOM   845  C CG  . ASN A 1 95  ? 8.58880   3.37646   -4.44758 1.000 24.01985 ? 95  ASN A CG  1 
ATOM   846  O OD1 . ASN A 1 95  ? 8.82515   2.32538   -3.85178 1.000 25.29403 ? 95  ASN A OD1 1 
ATOM   847  N ND2 . ASN A 1 95  ? 7.94987   3.41127   -5.61192 1.000 24.52408 ? 95  ASN A ND2 1 
ATOM   848  N N   . GLU A 1 96  ? 8.72057   7.05040   -1.75441 1.000 21.22549 ? 96  GLU A N   1 
ATOM   849  C CA  . GLU A 1 96  ? 9.14475   8.36460   -1.28417 1.000 23.21225 ? 96  GLU A CA  1 
ATOM   850  C C   . GLU A 1 96  ? 9.57949   8.31279   0.17640  1.000 19.44785 ? 96  GLU A C   1 
ATOM   851  O O   . GLU A 1 96  ? 10.62990  8.85600   0.54077  1.000 19.35347 ? 96  GLU A O   1 
ATOM   852  C CB  . GLU A 1 96  ? 8.02075   9.38372   -1.48482 1.000 27.58263 ? 96  GLU A CB  1 
ATOM   853  C CG  . GLU A 1 96  ? 8.35872   10.78055  -0.98440 1.000 31.03750 ? 96  GLU A CG  1 
ATOM   854  C CD  . GLU A 1 96  ? 7.19403   11.75082  -1.10520 1.000 35.57506 ? 96  GLU A CD  1 
ATOM   855  O OE1 . GLU A 1 96  ? 6.09386   11.31947  -1.51028 1.000 40.06531 ? 96  GLU A OE1 1 
ATOM   856  O OE2 . GLU A 1 96  ? 7.37899   12.94681  -0.79322 1.000 37.48898 ? 96  GLU A OE2 1 
ATOM   857  N N   . ALA A 1 97  ? 8.78630   7.65474   1.02861  1.000 16.25968 ? 97  ALA A N   1 
ATOM   858  C CA  . ALA A 1 97  ? 9.12390   7.59392   2.44896  1.000 14.99129 ? 97  ALA A CA  1 
ATOM   859  C C   . ALA A 1 97  ? 10.39766  6.79341   2.68696  1.000 14.13250 ? 97  ALA A C   1 
ATOM   860  O O   . ALA A 1 97  ? 11.25995  7.21611   3.46195  1.000 14.23866 ? 97  ALA A O   1 
ATOM   861  C CB  . ALA A 1 97  ? 7.96156   7.01617   3.25618  1.000 13.88735 ? 97  ALA A CB  1 
ATOM   862  N N   . VAL A 1 98  ? 10.53381  5.63597   2.03298  1.000 13.14452 ? 98  VAL A N   1 
ATOM   863  C CA  . VAL A 1 98  ? 11.73781  4.82366   2.20231  1.000 13.53094 ? 98  VAL A CA  1 
ATOM   864  C C   . VAL A 1 98  ? 12.97793  5.61054   1.80320  1.000 16.70286 ? 98  VAL A C   1 
ATOM   865  O O   . VAL A 1 98  ? 13.99280  5.60458   2.51184  1.000 18.33285 ? 98  VAL A O   1 
ATOM   866  C CB  . VAL A 1 98  ? 11.61482  3.50108   1.42445  1.000 15.40177 ? 98  VAL A CB  1 
ATOM   867  C CG1 . VAL A 1 98  ? 12.95321  2.77933   1.38712  1.000 18.42099 ? 98  VAL A CG1 1 
ATOM   868  C CG2 . VAL A 1 98  ? 10.56104  2.61942   2.06097  1.000 18.23078 ? 98  VAL A CG2 1 
ATOM   869  N N   . ARG A 1 99  ? 12.91028  6.31722   0.67615  1.000 16.42157 ? 99  ARG A N   1 
ATOM   870  C CA  . ARG A 1 99  ? 14.04894  7.11438   0.23344  1.000 18.52244 ? 99  ARG A CA  1 
ATOM   871  C C   . ARG A 1 99  ? 14.33253  8.25980   1.19865  1.000 16.36043 ? 99  ARG A C   1 
ATOM   872  O O   . ARG A 1 99  ? 15.48219  8.47761   1.59597  1.000 15.92015 ? 99  ARG A O   1 
ATOM   873  C CB  . ARG A 1 99  ? 13.78575  7.65252   -1.17117 1.000 20.21568 ? 99  ARG A CB  1 
ATOM   874  C CG  . ARG A 1 99  ? 14.86492  8.58521   -1.68678 1.000 24.16406 ? 99  ARG A CG  1 
ATOM   875  C CD  . ARG A 1 99  ? 14.32649  9.45399   -2.80762 1.000 28.56846 ? 99  ARG A CD  1 
ATOM   876  N NE  . ARG A 1 99  ? 13.41557  10.47089  -2.29739 1.000 32.07623 ? 99  ARG A NE  1 
ATOM   877  C CZ  . ARG A 1 99  ? 12.54537  11.13969  -3.04108 1.000 37.07685 ? 99  ARG A CZ  1 
ATOM   878  N NH1 . ARG A 1 99  ? 12.42293  10.90785  -4.33759 1.000 39.70096 ? 99  ARG A NH1 1 
ATOM   879  N NH2 . ARG A 1 99  ? 11.77322  12.05923  -2.46772 1.000 36.42255 ? 99  ARG A NH2 1 
ATOM   880  N N   . ASN A 1 100 ? 13.29461  9.01194   1.57717  1.000 13.88168 ? 100 ASN A N   1 
ATOM   881  C CA  . ASN A 1 100 ? 13.49223  10.17527  2.43801  1.000 14.54597 ? 100 ASN A CA  1 
ATOM   882  C C   . ASN A 1 100 ? 13.97310  9.77758   3.82906  1.000 13.18260 ? 100 ASN A C   1 
ATOM   883  O O   . ASN A 1 100 ? 14.87675  10.41506  4.38338  1.000 14.52522 ? 100 ASN A O   1 
ATOM   884  C CB  . ASN A 1 100 ? 12.20964  10.99724  2.52128  1.000 15.38054 ? 100 ASN A CB  1 
ATOM   885  C CG  . ASN A 1 100 ? 11.87734  11.68340  1.21084  1.000 18.44229 ? 100 ASN A CG  1 
ATOM   886  O OD1 . ASN A 1 100 ? 12.71448  11.76115  0.31153  1.000 19.40207 ? 100 ASN A OD1 1 
ATOM   887  N ND2 . ASN A 1 100 ? 10.65839  12.19748  1.10113  1.000 19.90314 ? 100 ASN A ND2 1 
ATOM   888  N N   . TRP A 1 101 ? 13.38232  8.73621   4.41530  1.000 12.77148 ? 101 TRP A N   1 
ATOM   889  C CA  . TRP A 1 101 ? 13.84744  8.29135   5.72415  1.000 11.49054 ? 101 TRP A CA  1 
ATOM   890  C C   . TRP A 1 101 ? 15.26241  7.73464   5.64403  1.000 11.22004 ? 101 TRP A C   1 
ATOM   891  O O   . TRP A 1 101 ? 16.06249  7.92569   6.56747  1.000 13.62717 ? 101 TRP A O   1 
ATOM   892  C CB  . TRP A 1 101 ? 12.91540  7.23224   6.30004  1.000 11.52525 ? 101 TRP A CB  1 
ATOM   893  C CG  . TRP A 1 101 ? 11.53764  7.69307   6.66058  1.000 13.34827 ? 101 TRP A CG  1 
ATOM   894  C CD1 . TRP A 1 101 ? 10.84459  8.74805   6.13234  1.000 14.22235 ? 101 TRP A CD1 1 
ATOM   895  C CD2 . TRP A 1 101 ? 10.67476  7.09051   7.62914  1.000 14.11914 ? 101 TRP A CD2 1 
ATOM   896  N NE1 . TRP A 1 101 ? 9.60089   8.83437   6.71405  1.000 15.22837 ? 101 TRP A NE1 1 
ATOM   897  C CE2 . TRP A 1 101 ? 9.47541   7.83033   7.64048  1.000 14.18473 ? 101 TRP A CE2 1 
ATOM   898  C CE3 . TRP A 1 101 ? 10.80318  5.99637   8.49256  1.000 14.58958 ? 101 TRP A CE3 1 
ATOM   899  C CZ2 . TRP A 1 101 ? 8.40965   7.50689   8.47672  1.000 15.49576 ? 101 TRP A CZ2 1 
ATOM   900  C CZ3 . TRP A 1 101 ? 9.74484   5.67704   9.31939  1.000 16.06048 ? 101 TRP A CZ3 1 
ATOM   901  C CH2 . TRP A 1 101 ? 8.56474   6.43165   9.30830  1.000 16.34132 ? 101 TRP A CH2 1 
ATOM   902  N N   . GLY A 1 102 ? 15.58432  7.03003   4.55569  1.000 11.10485 ? 102 GLY A N   1 
ATOM   903  C CA  . GLY A 1 102 ? 16.92915  6.49825   4.40176  1.000 11.27764 ? 102 GLY A CA  1 
ATOM   904  C C   . GLY A 1 102 ? 17.96973  7.58976   4.24107  1.000 11.67430 ? 102 GLY A C   1 
ATOM   905  O O   . GLY A 1 102 ? 19.08015  7.48960   4.77404  1.000 12.95604 ? 102 GLY A O   1 
ATOM   906  N N   . ILE A 1 103 ? 17.62812  8.64718   3.50516  1.000 12.73697 ? 103 ILE A N   1 
ATOM   907  C CA  . ILE A 1 103 ? 18.51816  9.80002   3.41071  1.000 14.66644 ? 103 ILE A CA  1 
ATOM   908  C C   . ILE A 1 103 ? 18.72483  10.41953  4.78735  1.000 12.91304 ? 103 ILE A C   1 
ATOM   909  O O   . ILE A 1 103 ? 19.85910  10.68906  5.20204  1.000 13.52154 ? 103 ILE A O   1 
ATOM   910  C CB  . ILE A 1 103 ? 17.98018  10.81387  2.38510  1.000 17.11778 ? 103 ILE A CB  1 
ATOM   911  C CG1 . ILE A 1 103 ? 18.03273  10.21349  0.98057  1.000 19.19277 ? 103 ILE A CG1 1 
ATOM   912  C CG2 . ILE A 1 103 ? 18.77730  12.10918  2.43640  1.000 18.52229 ? 103 ILE A CG2 1 
ATOM   913  C CD1 . ILE A 1 103 ? 17.25345  10.99330  -0.04704 1.000 21.57904 ? 103 ILE A CD1 1 
ATOM   914  N N   . ALA A 1 104 ? 17.63183  10.62403  5.53014  1.000 11.36408 ? 104 ALA A N   1 
ATOM   915  C CA  . ALA A 1 104 ? 17.74756  11.20349  6.86533  1.000 10.84705 ? 104 ALA A CA  1 
ATOM   916  C C   . ALA A 1 104 ? 18.61070  10.32990  7.77035  1.000 10.75920 ? 104 ALA A C   1 
ATOM   917  O O   . ALA A 1 104 ? 19.50031  10.83031  8.46730  1.000 11.00136 ? 104 ALA A O   1 
ATOM   918  C CB  . ALA A 1 104 ? 16.36165  11.45055  7.46996  1.000 10.34124 ? 104 ALA A CB  1 
ATOM   919  N N   . ALA A 1 105 ? 18.38599  9.01356   7.74686  1.000 9.93119  ? 105 ALA A N   1 
ATOM   920  C CA  . ALA A 1 105 ? 19.18176  8.11464   8.57833  1.000 10.73519 ? 105 ALA A CA  1 
ATOM   921  C C   . ALA A 1 105 ? 20.66607  8.21597   8.24095  1.000 10.95857 ? 105 ALA A C   1 
ATOM   922  O O   . ALA A 1 105 ? 21.52008  8.22631   9.13895  1.000 10.50509 ? 105 ALA A O   1 
ATOM   923  C CB  . ALA A 1 105 ? 18.68757  6.67645   8.40905  1.000 11.50535 ? 105 ALA A CB  1 
ATOM   924  N N   . THR A 1 106 ? 20.99155  8.30196   6.94925  1.000 10.26470 ? 106 THR A N   1 
ATOM   925  C CA  . THR A 1 106 ? 22.38678  8.40006   6.54114  1.000 10.91391 ? 106 THR A CA  1 
ATOM   926  C C   . THR A 1 106 ? 23.01226  9.69479   7.04309  1.000 9.81557  ? 106 THR A C   1 
ATOM   927  O O   . THR A 1 106 ? 24.15967  9.69907   7.50651  1.000 11.19147 ? 106 THR A O   1 
ATOM   928  C CB  . THR A 1 106 ? 22.48790  8.28623   5.01945  1.000 13.04065 ? 106 THR A CB  1 
ATOM   929  O OG1 . THR A 1 106 ? 21.79424  7.10735   4.58549  1.000 14.31506 ? 106 THR A OG1 1 
ATOM   930  C CG2 . THR A 1 106 ? 23.94680  8.20494   4.58292  1.000 13.47429 ? 106 THR A CG2 1 
ATOM   931  N N   . VAL A 1 107 ? 22.26412  10.80028  6.97921  1.000 9.59967  ? 107 VAL A N   1 
ATOM   932  C CA  . VAL A 1 107 ? 22.75072  12.06476  7.52472  1.000 10.57073 ? 107 VAL A CA  1 
ATOM   933  C C   . VAL A 1 107 ? 22.94737  11.95267  9.03160  1.000 11.68970 ? 107 VAL A C   1 
ATOM   934  O O   . VAL A 1 107 ? 23.95138  12.42042  9.58038  1.000 11.05676 ? 107 VAL A O   1 
ATOM   935  C CB  . VAL A 1 107 ? 21.78956  13.21023  7.15871  1.000 12.16968 ? 107 VAL A CB  1 
ATOM   936  C CG1 . VAL A 1 107 ? 22.16822  14.47518  7.90908  1.000 13.42550 ? 107 VAL A CG1 1 
ATOM   937  C CG2 . VAL A 1 107 ? 21.78917  13.45159  5.65349  1.000 14.05286 ? 107 VAL A CG2 1 
ATOM   938  N N   . MET A 1 108 ? 21.98831  11.33284  9.72012  1.000 11.24273 ? 108 MET A N   1 
ATOM   939  C CA  . MET A 1 108 ? 22.06537  11.18715  11.17038 1.000 10.09805 ? 108 MET A CA  1 
ATOM   940  C C   . MET A 1 108 ? 23.29598  10.38609  11.57181 1.000 10.07874 ? 108 MET A C   1 
ATOM   941  O O   . MET A 1 108 ? 24.06785  10.79672  12.44754 1.000 11.23039 ? 108 MET A O   1 
ATOM   942  C CB  . MET A 1 108 ? 20.79581  10.48950  11.66061 1.000 9.26576  ? 108 MET A CB  1 
ATOM   943  C CG  . MET A 1 108 ? 20.77915  10.14590  13.13905 1.000 9.80105  ? 108 MET A CG  1 
ATOM   944  S SD  . MET A 1 108 ? 19.28444  9.24644   13.58458 1.000 11.55501 ? 108 MET A SD  1 
ATOM   945  C CE  . MET A 1 108 ? 19.58807  7.69099   12.74923 1.000 10.73866 ? 108 MET A CE  1 
ATOM   946  N N   . ILE A 1 109 ? 23.49300  9.23559   10.93046 1.000 8.85645  ? 109 ILE A N   1 
ATOM   947  C CA  . ILE A 1 109 ? 24.61092  8.36115   11.26213 1.000 9.39501  ? 109 ILE A CA  1 
ATOM   948  C C   . ILE A 1 109 ? 25.93706  8.98930   10.84204 1.000 11.83786 ? 109 ILE A C   1 
ATOM   949  O O   . ILE A 1 109 ? 26.92651  8.93530   11.58407 1.000 11.80068 ? 109 ILE A O   1 
ATOM   950  C CB  . ILE A 1 109 ? 24.37569  6.97272   10.63922 1.000 10.75842 ? 109 ILE A CB  1 
ATOM   951  C CG1 . ILE A 1 109 ? 23.15492  6.31520   11.29184 1.000 12.23672 ? 109 ILE A CG1 1 
ATOM   952  C CG2 . ILE A 1 109 ? 25.60760  6.09822   10.77845 1.000 10.74029 ? 109 ILE A CG2 1 
ATOM   953  C CD1 . ILE A 1 109 ? 22.51274  5.21832   10.46408 1.000 16.72971 ? 109 ILE A CD1 1 
ATOM   954  N N   . GLY A 1 110 ? 25.97727  9.60941   9.65827  1.000 10.70128 ? 110 GLY A N   1 
ATOM   955  C CA  . GLY A 1 110 ? 27.19485  10.28043  9.22664  1.000 11.60752 ? 110 GLY A CA  1 
ATOM   956  C C   . GLY A 1 110 ? 27.57863  11.43984  10.12744 1.000 10.59129 ? 110 GLY A C   1 
ATOM   957  O O   . GLY A 1 110 ? 28.75690  11.63386  10.43806 1.000 11.03306 ? 110 GLY A O   1 
ATOM   958  N N   . ALA A 1 111 ? 26.58964  12.23215  10.55125 1.000 10.18296 ? 111 ALA A N   1 
ATOM   959  C CA  . ALA A 1 111 ? 26.85512  13.30810  11.50002 1.000 12.09589 ? 111 ALA A CA  1 
ATOM   960  C C   . ALA A 1 111 ? 27.35399  12.75532  12.83041 1.000 12.24497 ? 111 ALA A C   1 
ATOM   961  O O   . ALA A 1 111 ? 28.28853  13.30027  13.42652 1.000 10.73175 ? 111 ALA A O   1 
ATOM   962  C CB  . ALA A 1 111 ? 25.59900  14.15727  11.69438 1.000 12.41559 ? 111 ALA A CB  1 
ATOM   963  N N   . GLY A 1 112 ? 26.74809  11.66774  13.30732 1.000 11.89932 ? 112 GLY A N   1 
ATOM   964  C CA  . GLY A 1 112 ? 27.24014  11.03372  14.51982 1.000 11.63793 ? 112 GLY A CA  1 
ATOM   965  C C   . GLY A 1 112 ? 28.67194  10.54929  14.38817 1.000 10.41307 ? 112 GLY A C   1 
ATOM   966  O O   . GLY A 1 112 ? 29.48154  10.71935  15.30482 1.000 11.70523 ? 112 GLY A O   1 
ATOM   967  N N   . TYR A 1 113 ? 29.00609  9.94057   13.24483 1.000 11.50991 ? 113 TYR A N   1 
ATOM   968  C CA  . TYR A 1 113 ? 30.37289  9.47969   13.02566 1.000 12.35361 ? 113 TYR A CA  1 
ATOM   969  C C   . TYR A 1 113 ? 31.35013  10.64594  13.03384 1.000 12.02679 ? 113 TYR A C   1 
ATOM   970  O O   . TYR A 1 113 ? 32.42322  10.56497  13.64292 1.000 13.47848 ? 113 TYR A O   1 
ATOM   971  C CB  . TYR A 1 113 ? 30.48039  8.72274   11.70157 1.000 12.84950 ? 113 TYR A CB  1 
ATOM   972  C CG  . TYR A 1 113 ? 31.86541  8.15395   11.47424 1.000 15.04593 ? 113 TYR A CG  1 
ATOM   973  C CD1 . TYR A 1 113 ? 32.30149  7.04888   12.19207 1.000 14.88830 ? 113 TYR A CD1 1 
ATOM   974  C CD2 . TYR A 1 113 ? 32.74149  8.72882   10.55740 1.000 17.35063 ? 113 TYR A CD2 1 
ATOM   975  C CE1 . TYR A 1 113 ? 33.56627  6.52505   12.00219 1.000 16.70386 ? 113 TYR A CE1 1 
ATOM   976  C CE2 . TYR A 1 113 ? 34.01655  8.20904   10.35944 1.000 18.32691 ? 113 TYR A CE2 1 
ATOM   977  C CZ  . TYR A 1 113 ? 34.42420  7.10699   11.08721 1.000 18.18344 ? 113 TYR A CZ  1 
ATOM   978  O OH  . TYR A 1 113 ? 35.68353  6.57686   10.90546 1.000 21.21303 ? 113 TYR A OH  1 
ATOM   979  N N   . TYR A 1 114 ? 30.99590  11.73412  12.34704 1.000 12.93542 ? 114 TYR A N   1 
ATOM   980  C CA  . TYR A 1 114 ? 31.82672  12.93173  12.33209 1.000 13.64855 ? 114 TYR A CA  1 
ATOM   981  C C   . TYR A 1 114 ? 32.10741  13.42337  13.74540 1.000 13.87028 ? 114 TYR A C   1 
ATOM   982  O O   . TYR A 1 114 ? 33.24734  13.75653  14.08645 1.000 15.34769 ? 114 TYR A O   1 
ATOM   983  C CB  . TYR A 1 114 ? 31.12521  14.02087  11.51893 1.000 15.53423 ? 114 TYR A CB  1 
ATOM   984  C CG  . TYR A 1 114 ? 31.73778  15.39524  11.66408 1.000 16.70779 ? 114 TYR A CG  1 
ATOM   985  C CD1 . TYR A 1 114 ? 32.84230  15.76640  10.90759 1.000 17.63555 ? 114 TYR A CD1 1 
ATOM   986  C CD2 . TYR A 1 114 ? 31.21076  16.32741  12.55341 1.000 18.05843 ? 114 TYR A CD2 1 
ATOM   987  C CE1 . TYR A 1 114 ? 33.40647  17.02227  11.03305 1.000 18.43926 ? 114 TYR A CE1 1 
ATOM   988  C CE2 . TYR A 1 114 ? 31.77123  17.58842  12.68608 1.000 19.35417 ? 114 TYR A CE2 1 
ATOM   989  C CZ  . TYR A 1 114 ? 32.86895  17.92840  11.92212 1.000 20.96895 ? 114 TYR A CZ  1 
ATOM   990  O OH  . TYR A 1 114 ? 33.43798  19.17704  12.04086 1.000 23.26069 ? 114 TYR A OH  1 
ATOM   991  N N   . GLY A 1 115 ? 31.07260  13.46769  14.58595 1.000 13.54454 ? 115 GLY A N   1 
ATOM   992  C CA  . GLY A 1 115 ? 31.25507  13.97579  15.93484 1.000 13.43857 ? 115 GLY A CA  1 
ATOM   993  C C   . GLY A 1 115 ? 31.96940  12.99498  16.84603 1.000 11.77186 ? 115 GLY A C   1 
ATOM   994  O O   . GLY A 1 115 ? 32.82065  13.38820  17.64951 1.000 13.53721 ? 115 GLY A O   1 
ATOM   995  N N   . GLU A 1 116 ? 31.63649  11.70708  16.73515 1.000 12.10027 ? 116 GLU A N   1 
ATOM   996  C CA  . GLU A 1 116 ? 32.22500  10.70787  17.62125 1.000 13.09272 ? 116 GLU A CA  1 
ATOM   997  C C   . GLU A 1 116 ? 33.71928  10.54135  17.38142 1.000 14.63584 ? 116 GLU A C   1 
ATOM   998  O O   . GLU A 1 116 ? 34.46361  10.23485  18.32071 1.000 15.39608 ? 116 GLU A O   1 
ATOM   999  C CB  . GLU A 1 116 ? 31.50315  9.37045   17.45919 1.000 14.15726 ? 116 GLU A CB  1 
ATOM   1000 C CG  . GLU A 1 116 ? 32.03348  8.26449   18.35669 1.000 13.55909 ? 116 GLU A CG  1 
ATOM   1001 C CD  . GLU A 1 116 ? 31.00939  7.18332   18.62193 1.000 14.36510 ? 116 GLU A CD  1 
ATOM   1002 O OE1 . GLU A 1 116 ? 29.80606  7.51154   18.72323 1.000 14.80599 ? 116 GLU A OE1 1 
ATOM   1003 O OE2 . GLU A 1 116 ? 31.40878  6.00428   18.73101 1.000 13.62821 ? 116 GLU A OE2 1 
ATOM   1004 N N   . THR A 1 117 ? 34.17811  10.72989  16.14495 1.000 15.98345 ? 117 THR A N   1 
ATOM   1005 C CA  . THR A 1 117 ? 35.60034  10.64808  15.83852 1.000 17.38924 ? 117 THR A CA  1 
ATOM   1006 C C   . THR A 1 117 ? 36.32927  11.96690  16.06990 1.000 18.80792 ? 117 THR A C   1 
ATOM   1007 O O   . THR A 1 117 ? 37.53735  12.04711  15.81983 1.000 20.43562 ? 117 THR A O   1 
ATOM   1008 C CB  . THR A 1 117 ? 35.83009  10.13833  14.40674 1.000 18.61968 ? 117 THR A CB  1 
ATOM   1009 O OG1 . THR A 1 117 ? 35.12651  10.96520  13.47021 1.000 20.48451 ? 117 THR A OG1 1 
ATOM   1010 C CG2 . THR A 1 117 ? 35.35928  8.69807   14.26555 1.000 18.49296 ? 117 THR A CG2 1 
ATOM   1011 N N   . SER A 1 118 ? 35.62579  12.99585  16.53344 1.000 19.80705 ? 118 SER A N   1 
ATOM   1012 C CA  . SER A 1 118 ? 36.23971  14.24126  16.96118 1.000 19.96419 ? 118 SER A CA  1 
ATOM   1013 C C   . SER A 1 118 ? 36.63292  14.13847  18.43158 1.000 20.68006 ? 118 SER A C   1 
ATOM   1014 O O   . SER A 1 118 ? 36.30539  13.17085  19.12032 1.000 23.01741 ? 118 SER A O   1 
ATOM   1015 C CB  . SER A 1 118 ? 35.26704  15.40364  16.75557 1.000 21.23254 ? 118 SER A CB  1 
ATOM   1016 O OG  . SER A 1 118 ? 34.87024  15.50231  15.39703 1.000 23.59669 ? 118 SER A OG  1 
ATOM   1017 N N   . ALA A 1 119 ? 37.35217  15.14857  18.91550 1.000 21.39940 ? 119 ALA A N   1 
ATOM   1018 C CA  . ALA A 1 119 ? 37.70350  15.17659  20.32898 1.000 22.41497 ? 119 ALA A CA  1 
ATOM   1019 C C   . ALA A 1 119 ? 36.43408  15.28420  21.16183 1.000 22.31687 ? 119 ALA A C   1 
ATOM   1020 O O   . ALA A 1 119 ? 35.54712  16.08498  20.85708 1.000 19.87507 ? 119 ALA A O   1 
ATOM   1021 C CB  . ALA A 1 119 ? 38.62730  16.35675  20.61929 1.000 22.52976 ? 119 ALA A CB  1 
ATOM   1022 N N   . ALA A 1 120 ? 36.33709  14.45542  22.19930 1.000 23.92903 ? 120 ALA A N   1 
ATOM   1023 C CA  . ALA A 1 120 ? 35.13796  14.43628  23.02623 1.000 22.78871 ? 120 ALA A CA  1 
ATOM   1024 C C   . ALA A 1 120 ? 34.91984  15.80303  23.65907 1.000 21.05617 ? 120 ALA A C   1 
ATOM   1025 O O   . ALA A 1 120 ? 35.84158  16.38916  24.23154 1.000 22.44273 ? 120 ALA A O   1 
ATOM   1026 C CB  . ALA A 1 120 ? 35.27215  13.37217  24.11369 1.000 23.94620 ? 120 ALA A CB  1 
ATOM   1027 N N   . GLY A 1 121 ? 33.69905  16.31849  23.53630 1.000 19.41265 ? 121 GLY A N   1 
ATOM   1028 C CA  . GLY A 1 121 ? 33.36479  17.61646  24.08055 1.000 20.28278 ? 121 GLY A CA  1 
ATOM   1029 C C   . GLY A 1 121 ? 33.74930  18.80710  23.22671 1.000 19.82116 ? 121 GLY A C   1 
ATOM   1030 O O   . GLY A 1 121 ? 33.47954  19.94479  23.63111 1.000 19.62540 ? 121 GLY A O   1 
ATOM   1031 N N   . SER A 1 122 ? 34.35725  18.59066  22.06186 1.000 18.67656 ? 122 SER A N   1 
ATOM   1032 C CA  . SER A 1 122 ? 34.75974  19.68049  21.18628 1.000 19.62871 ? 122 SER A CA  1 
ATOM   1033 C C   . SER A 1 122 ? 33.55183  20.23970  20.43627 1.000 18.19462 ? 122 SER A C   1 
ATOM   1034 O O   . SER A 1 122 ? 32.45776  19.66917  20.44762 1.000 17.64516 ? 122 SER A O   1 
ATOM   1035 C CB  . SER A 1 122 ? 35.78709  19.18548  20.17175 1.000 19.54866 ? 122 SER A CB  1 
ATOM   1036 O OG  . SER A 1 122 ? 35.19903  18.21192  19.32183 1.000 18.88636 ? 122 SER A OG  1 
ATOM   1037 N N   . ASN A 1 123 ? 33.76339  21.37575  19.76366 1.000 17.96657 ? 123 ASN A N   1 
ATOM   1038 C CA  . ASN A 1 123 ? 32.69289  21.93806  18.94530 1.000 18.05337 ? 123 ASN A CA  1 
ATOM   1039 C C   . ASN A 1 123 ? 32.29043  20.97521  17.83612 1.000 17.57790 ? 123 ASN A C   1 
ATOM   1040 O O   . ASN A 1 123 ? 31.10735  20.86985  17.49690 1.000 17.44113 ? 123 ASN A O   1 
ATOM   1041 C CB  . ASN A 1 123 ? 33.09738  23.29394  18.36647 1.000 19.02730 ? 123 ASN A CB  1 
ATOM   1042 C CG  . ASN A 1 123 ? 31.94557  23.98541  17.65304 1.000 20.96899 ? 123 ASN A CG  1 
ATOM   1043 O OD1 . ASN A 1 123 ? 30.94934  24.35455  18.27582 1.000 22.20194 ? 123 ASN A OD1 1 
ATOM   1044 N ND2 . ASN A 1 123 ? 32.07891  24.16788  16.34391 1.000 22.08073 ? 123 ASN A ND2 1 
ATOM   1045 N N   . GLU A 1 124 ? 33.26082  20.25491  17.26721 1.000 17.67980 ? 124 GLU A N   1 
ATOM   1046 C CA  . GLU A 1 124 ? 32.93960  19.26346  16.24502 1.000 16.79863 ? 124 GLU A CA  1 
ATOM   1047 C C   . GLU A 1 124 ? 32.10339  18.13235  16.82830 1.000 15.09226 ? 124 GLU A C   1 
ATOM   1048 O O   . GLU A 1 124 ? 31.13140  17.68160  16.20824 1.000 15.08561 ? 124 GLU A O   1 
ATOM   1049 C CB  . GLU A 1 124 ? 34.22434  18.70914  15.62309 1.000 21.34030 ? 124 GLU A CB  1 
ATOM   1050 C CG  . GLU A 1 124 ? 35.01433  19.70152  14.77704 1.000 24.17489 ? 124 GLU A CG  1 
ATOM   1051 C CD  . GLU A 1 124 ? 35.79760  20.70179  15.60457 1.000 29.16243 ? 124 GLU A CD  1 
ATOM   1052 O OE1 . GLU A 1 124 ? 35.97949  20.46721  16.81911 1.000 29.11853 ? 124 GLU A OE1 1 
ATOM   1053 O OE2 . GLU A 1 124 ? 36.23445  21.72565  15.03662 1.000 32.70997 ? 124 GLU A OE2 1 
ATOM   1054 N N   . TYR A 1 125 ? 32.47404  17.66126  18.02350 1.000 13.82748 ? 125 TYR A N   1 
ATOM   1055 C CA  . TYR A 1 125 ? 31.69669  16.63467  18.71310 1.000 12.66543 ? 125 TYR A CA  1 
ATOM   1056 C C   . TYR A 1 125 ? 30.25456  17.08347  18.92772 1.000 12.99777 ? 125 TYR A C   1 
ATOM   1057 O O   . TYR A 1 125 ? 29.31379  16.31554  18.68803 1.000 12.65199 ? 125 TYR A O   1 
ATOM   1058 C CB  . TYR A 1 125 ? 32.38019  16.30878  20.04398 1.000 14.47955 ? 125 TYR A CB  1 
ATOM   1059 C CG  . TYR A 1 125 ? 31.59402  15.43436  20.99800 1.000 13.93295 ? 125 TYR A CG  1 
ATOM   1060 C CD1 . TYR A 1 125 ? 31.72812  14.04897  20.98293 1.000 12.77627 ? 125 TYR A CD1 1 
ATOM   1061 C CD2 . TYR A 1 125 ? 30.75243  15.99942  21.94679 1.000 13.39469 ? 125 TYR A CD2 1 
ATOM   1062 C CE1 . TYR A 1 125 ? 31.01555  13.24961  21.87406 1.000 13.32575 ? 125 TYR A CE1 1 
ATOM   1063 C CE2 . TYR A 1 125 ? 30.04389  15.21990  22.83382 1.000 13.31509 ? 125 TYR A CE2 1 
ATOM   1064 C CZ  . TYR A 1 125 ? 30.17488  13.84734  22.79589 1.000 14.24239 ? 125 TYR A CZ  1 
ATOM   1065 O OH  . TYR A 1 125 ? 29.45720  13.08674  23.68525 1.000 14.78735 ? 125 TYR A OH  1 
ATOM   1066 N N   . TRP A 1 126 ? 30.05836  18.32997  19.36910 1.000 14.00642 ? 126 TRP A N   1 
ATOM   1067 C CA  . TRP A 1 126 ? 28.70309  18.81678  19.59985 1.000 15.07697 ? 126 TRP A CA  1 
ATOM   1068 C C   . TRP A 1 126 ? 27.97288  19.10286  18.29564 1.000 14.19102 ? 126 TRP A C   1 
ATOM   1069 O O   . TRP A 1 126 ? 26.75116  18.93827  18.22767 1.000 13.34474 ? 126 TRP A O   1 
ATOM   1070 C CB  . TRP A 1 126 ? 28.71918  20.03865  20.51954 1.000 14.98550 ? 126 TRP A CB  1 
ATOM   1071 C CG  . TRP A 1 126 ? 29.04846  19.66783  21.92819 1.000 16.46902 ? 126 TRP A CG  1 
ATOM   1072 C CD1 . TRP A 1 126 ? 30.15742  20.02920  22.63860 1.000 17.29421 ? 126 TRP A CD1 1 
ATOM   1073 C CD2 . TRP A 1 126 ? 28.27845  18.82008  22.78828 1.000 18.11214 ? 126 TRP A CD2 1 
ATOM   1074 N NE1 . TRP A 1 126 ? 30.11406  19.47344  23.89697 1.000 18.96337 ? 126 TRP A NE1 1 
ATOM   1075 C CE2 . TRP A 1 126 ? 28.97065  18.72741  24.01307 1.000 18.51351 ? 126 TRP A CE2 1 
ATOM   1076 C CE3 . TRP A 1 126 ? 27.06397  18.14132  22.64578 1.000 19.00578 ? 126 TRP A CE3 1 
ATOM   1077 C CZ2 . TRP A 1 126 ? 28.48928  17.97846  25.08728 1.000 20.32357 ? 126 TRP A CZ2 1 
ATOM   1078 C CZ3 . TRP A 1 126 ? 26.58802  17.39955  23.71106 1.000 20.12941 ? 126 TRP A CZ3 1 
ATOM   1079 C CH2 . TRP A 1 126 ? 27.29886  17.32346  24.91655 1.000 20.36254 ? 126 TRP A CH2 1 
ATOM   1080 N N   . THR A 1 127 ? 28.69953  19.51935  17.25522 1.000 13.68584 ? 127 THR A N   1 
ATOM   1081 C CA  . THR A 1 127 ? 28.08074  19.73044  15.94964 1.000 13.80991 ? 127 THR A CA  1 
ATOM   1082 C C   . THR A 1 127 ? 27.48639  18.43661  15.41586 1.000 12.07995 ? 127 THR A C   1 
ATOM   1083 O O   . THR A 1 127 ? 26.33754  18.40698  14.95581 1.000 13.44452 ? 127 THR A O   1 
ATOM   1084 C CB  . THR A 1 127 ? 29.11687  20.27682  14.97069 1.000 15.48884 ? 127 THR A CB  1 
ATOM   1085 O OG1 . THR A 1 127 ? 29.50338  21.59486  15.37304 1.000 16.56023 ? 127 THR A OG1 1 
ATOM   1086 C CG2 . THR A 1 127 ? 28.54995  20.32193  13.55621 1.000 16.00997 ? 127 THR A CG2 1 
ATOM   1087 N N   . GLY A 1 128 ? 28.26436  17.35371  15.46068 1.000 10.38455 ? 128 GLY A N   1 
ATOM   1088 C CA  . GLY A 1 128 ? 27.73983  16.06662  15.04488 1.000 11.81362 ? 128 GLY A CA  1 
ATOM   1089 C C   . GLY A 1 128 ? 26.52502  15.66075  15.85307 1.000 12.86108 ? 128 GLY A C   1 
ATOM   1090 O O   . GLY A 1 128 ? 25.52640  15.19421  15.29825 1.000 13.78401 ? 128 GLY A O   1 
ATOM   1091 N N   . PHE A 1 129 ? 26.58085  15.86859  17.17324 1.000 11.93474 ? 129 PHE A N   1 
ATOM   1092 C CA  . PHE A 1 129 ? 25.46681  15.48996  18.03874 1.000 11.44646 ? 129 PHE A CA  1 
ATOM   1093 C C   . PHE A 1 129 ? 24.20033  16.25215  17.68023 1.000 9.91416  ? 129 PHE A C   1 
ATOM   1094 O O   . PHE A 1 129 ? 23.12072  15.66488  17.56678 1.000 9.80502  ? 129 PHE A O   1 
ATOM   1095 C CB  . PHE A 1 129 ? 25.82482  15.75979  19.49870 1.000 12.17196 ? 129 PHE A CB  1 
ATOM   1096 C CG  . PHE A 1 129 ? 24.71160  15.44693  20.46056 1.000 13.91012 ? 129 PHE A CG  1 
ATOM   1097 C CD1 . PHE A 1 129 ? 24.41397  14.13239  20.78383 1.000 14.98266 ? 129 PHE A CD1 1 
ATOM   1098 C CD2 . PHE A 1 129 ? 23.96579  16.46241  21.04539 1.000 14.69361 ? 129 PHE A CD2 1 
ATOM   1099 C CE1 . PHE A 1 129 ? 23.39807  13.83258  21.67101 1.000 15.20627 ? 129 PHE A CE1 1 
ATOM   1100 C CE2 . PHE A 1 129 ? 22.94417  16.16884  21.93882 1.000 14.69065 ? 129 PHE A CE2 1 
ATOM   1101 C CZ  . PHE A 1 129 ? 22.66422  14.85118  22.25360 1.000 14.84461 ? 129 PHE A CZ  1 
ATOM   1102 N N   . VAL A 1 130 ? 24.31193  17.57197  17.52659 1.000 10.64218 ? 130 VAL A N   1 
ATOM   1103 C CA  . VAL A 1 130 ? 23.13346  18.39969  17.30036 1.000 10.29214 ? 130 VAL A CA  1 
ATOM   1104 C C   . VAL A 1 130 ? 22.49956  18.09517  15.94759 1.000 11.35911 ? 130 VAL A C   1 
ATOM   1105 O O   . VAL A 1 130 ? 21.27352  17.98368  15.83630 1.000 10.17100 ? 130 VAL A O   1 
ATOM   1106 C CB  . VAL A 1 130 ? 23.48977  19.88671  17.46912 1.000 10.63905 ? 130 VAL A CB  1 
ATOM   1107 C CG1 . VAL A 1 130 ? 22.35044  20.76149  16.99172 1.000 10.36834 ? 130 VAL A CG1 1 
ATOM   1108 C CG2 . VAL A 1 130 ? 23.81317  20.17997  18.92773 1.000 12.66853 ? 130 VAL A CG2 1 
ATOM   1109 N N   . ILE A 1 131 ? 23.31425  17.96633  14.89704 1.000 12.61700 ? 131 ILE A N   1 
ATOM   1110 C CA  . ILE A 1 131 ? 22.77053  17.62854  13.58121 1.000 11.73890 ? 131 ILE A CA  1 
ATOM   1111 C C   . ILE A 1 131 ? 22.09893  16.25974  13.61824 1.000 10.86549 ? 131 ILE A C   1 
ATOM   1112 O O   . ILE A 1 131 ? 20.96839  16.08678  13.14216 1.000 12.00221 ? 131 ILE A O   1 
ATOM   1113 C CB  . ILE A 1 131 ? 23.86785  17.70694  12.50515 1.000 12.16151 ? 131 ILE A CB  1 
ATOM   1114 C CG1 . ILE A 1 131 ? 24.35282  19.14595  12.33559 1.000 12.05083 ? 131 ILE A CG1 1 
ATOM   1115 C CG2 . ILE A 1 131 ? 23.36957  17.14521  11.17979 1.000 13.11652 ? 131 ILE A CG2 1 
ATOM   1116 C CD1 . ILE A 1 131 ? 25.54250  19.26295  11.41597 1.000 12.89168 ? 131 ILE A CD1 1 
ATOM   1117 N N   . ALA A 1 132 ? 22.78910  15.26507  14.18698 1.000 10.66854 ? 132 ALA A N   1 
ATOM   1118 C CA  . ALA A 1 132 ? 22.20375  13.93394  14.32213 1.000 11.94743 ? 132 ALA A CA  1 
ATOM   1119 C C   . ALA A 1 132 ? 20.91463  13.96651  15.13790 1.000 11.58758 ? 132 ALA A C   1 
ATOM   1120 O O   . ALA A 1 132 ? 19.93080  13.30766  14.77875 1.000 9.73834  ? 132 ALA A O   1 
ATOM   1121 C CB  . ALA A 1 132 ? 23.21947  12.97281  14.93897 1.000 12.10209 ? 132 ALA A CB  1 
ATOM   1122 N N   A MET A 1 133 ? 20.90186  14.71984  16.24270 0.500 11.16530 ? 133 MET A N   1 
ATOM   1123 N N   B MET A 1 133 ? 20.89381  14.73931  16.22870 0.500 13.12476 ? 133 MET A N   1 
ATOM   1124 C CA  A MET A 1 133 ? 19.70349  14.79492  17.07671 0.500 11.10590 ? 133 MET A CA  1 
ATOM   1125 C CA  B MET A 1 133 ? 19.70530  14.78689  17.07792 0.500 14.46442 ? 133 MET A CA  1 
ATOM   1126 C C   A MET A 1 133 ? 18.51728  15.34326  16.29476 0.500 10.98486 ? 133 MET A C   1 
ATOM   1127 C C   B MET A 1 133 ? 18.50904  15.38105  16.34288 0.500 12.27059 ? 133 MET A C   1 
ATOM   1128 O O   A MET A 1 133 ? 17.40719  14.80442  16.37136 0.500 10.57636 ? 133 MET A O   1 
ATOM   1129 O O   B MET A 1 133 ? 17.38011  14.90414  16.50126 0.500 11.12508 ? 133 MET A O   1 
ATOM   1130 C CB  A MET A 1 133 ? 19.96245  15.66069  18.31224 0.500 10.32005 ? 133 MET A CB  1 
ATOM   1131 C CB  B MET A 1 133 ? 19.99340  15.57563  18.35682 0.500 16.74767 ? 133 MET A CB  1 
ATOM   1132 C CG  A MET A 1 133 ? 20.56386  14.92993  19.49663 0.500 9.56558  ? 133 MET A CG  1 
ATOM   1133 C CG  B MET A 1 133 ? 18.84831  15.57064  19.36212 0.500 19.44262 ? 133 MET A CG  1 
ATOM   1134 S SD  A MET A 1 133 ? 19.54653  13.57981  20.12802 0.500 10.20867 ? 133 MET A SD  1 
ATOM   1135 S SD  B MET A 1 133 ? 18.52745  13.92701  20.02272 0.500 23.24708 ? 133 MET A SD  1 
ATOM   1136 C CE  A MET A 1 133 ? 17.94812  14.37550  20.31070 0.500 13.87108 ? 133 MET A CE  1 
ATOM   1137 C CE  B MET A 1 133 ? 20.20269  13.42154  20.34699 0.500 22.05515 ? 133 MET A CE  1 
ATOM   1138 N N   . ALA A 1 134 ? 18.72991  16.42801  15.54497 1.000 11.66346 ? 134 ALA A N   1 
ATOM   1139 C CA  . ALA A 1 134 ? 17.62770  17.02886  14.80051 1.000 11.94676 ? 134 ALA A CA  1 
ATOM   1140 C C   . ALA A 1 134 ? 17.09106  16.07303  13.74564 1.000 10.17882 ? 134 ALA A C   1 
ATOM   1141 O O   . ALA A 1 134 ? 15.87164  15.95258  13.56648 1.000 10.31052 ? 134 ALA A O   1 
ATOM   1142 C CB  . ALA A 1 134 ? 18.07864  18.33247  14.15608 1.000 12.25459 ? 134 ALA A CB  1 
ATOM   1143 N N   A THR A 1 135 ? 17.98728  15.37961  13.04342 0.500 9.97964  ? 135 THR A N   1 
ATOM   1144 N N   B THR A 1 135 ? 17.98310  15.37704  13.03359 0.500 11.19821 ? 135 THR A N   1 
ATOM   1145 C CA  A THR A 1 135 ? 17.54668  14.40046  12.05931 0.500 9.83034  ? 135 THR A CA  1 
ATOM   1146 C CA  B THR A 1 135 ? 17.52372  14.39919  12.05101 0.500 12.15865 ? 135 THR A CA  1 
ATOM   1147 C C   A THR A 1 135 ? 16.80800  13.25116  12.73328 0.500 11.26387 ? 135 THR A C   1 
ATOM   1148 C C   B THR A 1 135 ? 16.80542  13.23939  12.72948 0.500 12.24977 ? 135 THR A C   1 
ATOM   1149 O O   A THR A 1 135 ? 15.78729  12.77201  12.22653 0.500 12.22044 ? 135 THR A O   1 
ATOM   1150 O O   B THR A 1 135 ? 15.79826  12.73799  12.21752 0.500 12.76975 ? 135 THR A O   1 
ATOM   1151 C CB  A THR A 1 135 ? 18.75546  13.89018  11.27921 0.500 9.83298  ? 135 THR A CB  1 
ATOM   1152 C CB  B THR A 1 135 ? 18.69797  13.90037  11.20611 0.500 13.71358 ? 135 THR A CB  1 
ATOM   1153 O OG1 A THR A 1 135 ? 19.60168  14.99592  10.92486 0.500 9.65658  ? 135 THR A OG1 1 
ATOM   1154 O OG1 B THR A 1 135 ? 19.74623  13.43251  12.06344 0.500 14.75933 ? 135 THR A OG1 1 
ATOM   1155 C CG2 A THR A 1 135 ? 18.30092  13.18151  10.02818 0.500 11.05120 ? 135 THR A CG2 1 
ATOM   1156 C CG2 B THR A 1 135 ? 19.23932  15.01539  10.32605 0.500 15.15919 ? 135 THR A CG2 1 
ATOM   1157 N N   . TYR A 1 136 ? 17.30540  12.81278  13.89005 1.000 11.55991 ? 136 TYR A N   1 
ATOM   1158 C CA  . TYR A 1 136 ? 16.64363  11.76774  14.66081 1.000 12.56702 ? 136 TYR A CA  1 
ATOM   1159 C C   . TYR A 1 136 ? 15.22654  12.18001  15.05709 1.000 11.78456 ? 136 TYR A C   1 
ATOM   1160 O O   . TYR A 1 136 ? 14.27151  11.41653  14.87365 1.000 12.26956 ? 136 TYR A O   1 
ATOM   1161 C CB  . TYR A 1 136 ? 17.51532  11.48490  15.88330 1.000 12.13747 ? 136 TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 136 ? 16.89284  10.71826  17.01801 1.000 16.65676 ? 136 TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 136 ? 16.78719  9.33929   16.97412 1.000 20.21348 ? 136 TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 136 ? 16.46619  11.37310  18.16523 1.000 20.41308 ? 136 TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 136 ? 16.24220  8.63473   18.02762 1.000 21.11613 ? 136 TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 136 ? 15.91772  10.67901  19.21939 1.000 22.43723 ? 136 TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 136 ? 15.81036  9.30823   19.14542 1.000 21.10933 ? 136 TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 136 ? 15.27210  8.60494   20.19411 1.000 24.69418 ? 136 TYR A OH  1 
ATOM   1169 N N   . VAL A 1 137 ? 15.06515  13.39707  15.58169 1.000 11.99021 ? 137 VAL A N   1 
ATOM   1170 C CA  . VAL A 1 137 ? 13.73406  13.86247  15.97275 1.000 12.01718 ? 137 VAL A CA  1 
ATOM   1171 C C   . VAL A 1 137 ? 12.81369  13.94489  14.76196 1.000 11.95040 ? 137 VAL A C   1 
ATOM   1172 O O   . VAL A 1 137 ? 11.63365  13.57955  14.83233 1.000 12.12542 ? 137 VAL A O   1 
ATOM   1173 C CB  . VAL A 1 137 ? 13.82770  15.19920  16.73198 1.000 12.55928 ? 137 VAL A CB  1 
ATOM   1174 C CG1 . VAL A 1 137 ? 12.43968  15.77857  16.95746 1.000 15.02082 ? 137 VAL A CG1 1 
ATOM   1175 C CG2 . VAL A 1 137 ? 14.54755  14.99653  18.05862 1.000 14.13107 ? 137 VAL A CG2 1 
ATOM   1176 N N   . TRP A 1 138 ? 13.34143  14.41162  13.62896 1.000 11.22822 ? 138 TRP A N   1 
ATOM   1177 C CA  . TRP A 1 138 ? 12.56015  14.42865  12.39629 1.000 11.01734 ? 138 TRP A CA  1 
ATOM   1178 C C   . TRP A 1 138 ? 12.08192  13.02743  12.02621 1.000 9.73318  ? 138 TRP A C   1 
ATOM   1179 O O   . TRP A 1 138 ? 10.91652  12.83692  11.65323 1.000 10.24306 ? 138 TRP A O   1 
ATOM   1180 C CB  . TRP A 1 138 ? 13.41174  15.02321  11.27700 1.000 12.21334 ? 138 TRP A CB  1 
ATOM   1181 C CG  . TRP A 1 138 ? 12.69950  15.21679  9.97847  1.000 12.94166 ? 138 TRP A CG  1 
ATOM   1182 C CD1 . TRP A 1 138 ? 11.95710  16.30123  9.60051  1.000 13.63179 ? 138 TRP A CD1 1 
ATOM   1183 C CD2 . TRP A 1 138 ? 12.68483  14.31339  8.86868  1.000 13.30639 ? 138 TRP A CD2 1 
ATOM   1184 N NE1 . TRP A 1 138 ? 11.47684  16.12320  8.32621  1.000 14.49314 ? 138 TRP A NE1 1 
ATOM   1185 C CE2 . TRP A 1 138 ? 11.90624  14.90887  7.85642  1.000 14.75808 ? 138 TRP A CE2 1 
ATOM   1186 C CE3 . TRP A 1 138 ? 13.24836  13.05335  8.63591  1.000 14.96529 ? 138 TRP A CE3 1 
ATOM   1187 C CZ2 . TRP A 1 138 ? 11.67993  14.29015  6.62816  1.000 15.35763 ? 138 TRP A CZ2 1 
ATOM   1188 C CZ3 . TRP A 1 138 ? 13.02259  12.44179  7.41827  1.000 16.60441 ? 138 TRP A CZ3 1 
ATOM   1189 C CH2 . TRP A 1 138 ? 12.24373  13.05917  6.42982  1.000 17.16313 ? 138 TRP A CH2 1 
ATOM   1190 N N   . LEU A 1 139 ? 12.97012  12.03299  12.11998 1.000 10.33765 ? 139 LEU A N   1 
ATOM   1191 C CA  . LEU A 1 139 ? 12.57528  10.65440  11.83336 1.000 9.44802  ? 139 LEU A CA  1 
ATOM   1192 C C   . LEU A 1 139 ? 11.50793  10.16293  12.80643 1.000 9.83404  ? 139 LEU A C   1 
ATOM   1193 O O   . LEU A 1 139 ? 10.52342  9.53454   12.39435 1.000 10.35428 ? 139 LEU A O   1 
ATOM   1194 C CB  . LEU A 1 139 ? 13.80252  9.73951   11.87401 1.000 9.87394  ? 139 LEU A CB  1 
ATOM   1195 C CG  . LEU A 1 139 ? 14.72918  9.76878   10.65648 1.000 13.12431 ? 139 LEU A CG  1 
ATOM   1196 C CD1 . LEU A 1 139 ? 16.03872  9.06039   10.97852 1.000 14.29281 ? 139 LEU A CD1 1 
ATOM   1197 C CD2 . LEU A 1 139 ? 14.05405  9.11993   9.45715  1.000 14.70513 ? 139 LEU A CD2 1 
ATOM   1198 N N   A MET A 1 140 ? 11.69156  10.42794  14.10339 0.500 10.61844 ? 140 MET A N   1 
ATOM   1199 N N   B MET A 1 140 ? 11.68155  10.43819  14.10243 0.500 11.11789 ? 140 MET A N   1 
ATOM   1200 C CA  A MET A 1 140 ? 10.72677  9.96140   15.09505 0.500 11.91822 ? 140 MET A CA  1 
ATOM   1201 C CA  B MET A 1 140 ? 10.72327  9.94541   15.08856 0.500 12.84530 ? 140 MET A CA  1 
ATOM   1202 C C   A MET A 1 140 ? 9.36677   10.61618  14.89736 0.500 12.16405 ? 140 MET A C   1 
ATOM   1203 C C   B MET A 1 140 ? 9.36539   10.62444  14.93764 0.500 12.63447 ? 140 MET A C   1 
ATOM   1204 O O   A MET A 1 140 ? 8.32693   9.95889   15.02890 0.500 12.36220 ? 140 MET A O   1 
ATOM   1205 O O   B MET A 1 140 ? 8.32363   9.98901   15.13890 0.500 12.73470 ? 140 MET A O   1 
ATOM   1206 C CB  A MET A 1 140 ? 11.25177  10.22010  16.50693 0.500 10.42750 ? 140 MET A CB  1 
ATOM   1207 C CB  B MET A 1 140 ? 11.27637  10.11311  16.50576 0.500 12.20823 ? 140 MET A CB  1 
ATOM   1208 C CG  A MET A 1 140 ? 12.45804  9.37325   16.89166 0.500 10.07888 ? 140 MET A CG  1 
ATOM   1209 C CG  B MET A 1 140 ? 12.67210  9.51312   16.74090 0.500 11.71397 ? 140 MET A CG  1 
ATOM   1210 S SD  A MET A 1 140 ? 12.16588  7.60960   16.65660 0.500 10.99463 ? 140 MET A SD  1 
ATOM   1211 S SD  B MET A 1 140 ? 12.78982  7.70851   16.70651 0.500 13.35183 ? 140 MET A SD  1 
ATOM   1212 C CE  A MET A 1 140 ? 13.06980  7.30361   15.14020 0.500 13.14248 ? 140 MET A CE  1 
ATOM   1213 C CE  B MET A 1 140 ? 13.09511  7.38557   14.96924 0.500 14.68210 ? 140 MET A CE  1 
ATOM   1214 N N   . ARG A 1 141 ? 9.35411   11.91185  14.57945 1.000 12.51056 ? 141 ARG A N   1 
ATOM   1215 C CA  . ARG A 1 141 ? 8.09029   12.59720  14.33296 1.000 15.54646 ? 141 ARG A CA  1 
ATOM   1216 C C   . ARG A 1 141 ? 7.38910   12.02728  13.10505 1.000 14.98485 ? 141 ARG A C   1 
ATOM   1217 O O   . ARG A 1 141 ? 6.16687   11.83580  13.11333 1.000 15.44187 ? 141 ARG A O   1 
ATOM   1218 C CB  . ARG A 1 141 ? 8.33173   14.10063  14.17693 1.000 20.23947 ? 141 ARG A CB  1 
ATOM   1219 C CG  . ARG A 1 141 ? 8.79474   14.80638  15.44927 1.000 26.38624 ? 141 ARG A CG  1 
ATOM   1220 C CD  . ARG A 1 141 ? 7.65969   14.99891  16.44326 1.000 31.95416 ? 141 ARG A CD  1 
ATOM   1221 N NE  . ARG A 1 141 ? 6.47136   15.55453  15.80482 1.000 38.46741 ? 141 ARG A NE  1 
ATOM   1222 C CZ  . ARG A 1 141 ? 5.41704   16.02632  16.45591 1.000 46.32077 ? 141 ARG A CZ  1 
ATOM   1223 N NH1 . ARG A 1 141 ? 5.38046   16.06462  17.77776 1.000 53.08187 ? 141 ARG A NH1 1 
ATOM   1224 N NH2 . ARG A 1 141 ? 4.37392   16.47328  15.76265 1.000 46.47206 ? 141 ARG A NH2 1 
ATOM   1225 N N   . ASN A 1 142 ? 8.14764   11.74114  12.04151 1.000 14.07028 ? 142 ASN A N   1 
ATOM   1226 C CA  . ASN A 1 142 ? 7.56074   11.06153  10.89193 1.000 16.34275 ? 142 ASN A CA  1 
ATOM   1227 C C   . ASN A 1 142 ? 7.01230   9.69910   11.28636 1.000 15.44924 ? 142 ASN A C   1 
ATOM   1228 O O   . ASN A 1 142 ? 5.91550   9.31687   10.86222 1.000 15.03042 ? 142 ASN A O   1 
ATOM   1229 C CB  . ASN A 1 142 ? 8.58282   10.91294  9.76321  1.000 18.82647 ? 142 ASN A CB  1 
ATOM   1230 C CG  . ASN A 1 142 ? 8.60958   12.11329  8.83926  1.000 24.91077 ? 142 ASN A CG  1 
ATOM   1231 O OD1 . ASN A 1 142 ? 7.69952   12.31610  8.03477  1.000 31.16084 ? 142 ASN A OD1 1 
ATOM   1232 N ND2 . ASN A 1 142 ? 9.65475   12.91228  8.94577  1.000 24.06231 ? 142 ASN A ND2 1 
ATOM   1233 N N   . LEU A 1 143 ? 7.76246   8.95196   12.09872 1.000 14.68236 ? 143 LEU A N   1 
ATOM   1234 C CA  . LEU A 1 143 ? 7.31030   7.62851   12.50916 1.000 12.66413 ? 143 LEU A CA  1 
ATOM   1235 C C   . LEU A 1 143 ? 6.03106   7.71248   13.33218 1.000 14.39781 ? 143 LEU A C   1 
ATOM   1236 O O   . LEU A 1 143 ? 5.10700   6.91526   13.13715 1.000 14.66709 ? 143 LEU A O   1 
ATOM   1237 C CB  . LEU A 1 143 ? 8.41323   6.92658   13.29748 1.000 12.43584 ? 143 LEU A CB  1 
ATOM   1238 C CG  . LEU A 1 143 ? 8.01609   5.57478   13.87677 1.000 10.97185 ? 143 LEU A CG  1 
ATOM   1239 C CD1 . LEU A 1 143 ? 7.74151   4.57296   12.75971 1.000 11.97776 ? 143 LEU A CD1 1 
ATOM   1240 C CD2 . LEU A 1 143 ? 9.09831   5.05630   14.80884 1.000 11.66876 ? 143 LEU A CD2 1 
ATOM   1241 N N   . GLN A 1 144 ? 5.95685   8.67668   14.25420 1.000 16.62484 ? 144 GLN A N   1 
ATOM   1242 C CA  . GLN A 1 144 ? 4.74156   8.84624   15.04532 1.000 19.51841 ? 144 GLN A CA  1 
ATOM   1243 C C   . GLN A 1 144 ? 3.52779   9.10610   14.16551 1.000 19.26692 ? 144 GLN A C   1 
ATOM   1244 O O   . GLN A 1 144 ? 2.41847   8.67820   14.50012 1.000 19.92367 ? 144 GLN A O   1 
ATOM   1245 C CB  . GLN A 1 144 ? 4.91656   9.98007   16.05557 1.000 21.91499 ? 144 GLN A CB  1 
ATOM   1246 C CG  . GLN A 1 144 ? 5.83893   9.63908   17.20726 1.000 26.63574 ? 144 GLN A CG  1 
ATOM   1247 C CD  . GLN A 1 144 ? 6.09374   10.82106  18.12004 1.000 32.70005 ? 144 GLN A CD  1 
ATOM   1248 O OE1 . GLN A 1 144 ? 6.46752   11.90334  17.66568 1.000 32.67573 ? 144 GLN A OE1 1 
ATOM   1249 N NE2 . GLN A 1 144 ? 5.88914   10.62093  19.41647 1.000 33.55184 ? 144 GLN A NE2 1 
ATOM   1250 N N   . ALA A 1 145 ? 3.71710   9.78374   13.03341 1.000 17.34650 ? 145 ALA A N   1 
ATOM   1251 C CA  . ALA A 1 145 ? 2.60147   10.10942  12.15391 1.000 18.04496 ? 145 ALA A CA  1 
ATOM   1252 C C   . ALA A 1 145 ? 2.11830   8.92076   11.33184 1.000 19.35900 ? 145 ALA A C   1 
ATOM   1253 O O   . ALA A 1 145 ? 0.99603   8.96111   10.81779 1.000 21.29156 ? 145 ALA A O   1 
ATOM   1254 C CB  . ALA A 1 145 ? 2.98334   11.26470  11.22517 1.000 19.99515 ? 145 ALA A CB  1 
ATOM   1255 N N   . GLU A 1 146 ? 2.92220   7.86875   11.20295 1.000 17.86803 ? 146 GLU A N   1 
ATOM   1256 C CA  . GLU A 1 146 ? 2.52864   6.72711   10.38981 1.000 20.48018 ? 146 GLU A CA  1 
ATOM   1257 C C   . GLU A 1 146 ? 1.47176   5.89126   11.09693 1.000 25.81109 ? 146 GLU A C   1 
ATOM   1258 O O   . GLU A 1 146 ? 1.46048   5.77468   12.32482 1.000 25.19275 ? 146 GLU A O   1 
ATOM   1259 C CB  . GLU A 1 146 ? 3.74022   5.84197   10.10239 1.000 19.00335 ? 146 GLU A CB  1 
ATOM   1260 C CG  . GLU A 1 146 ? 4.73453   6.44619   9.13248  1.000 22.39843 ? 146 GLU A CG  1 
ATOM   1261 C CD  . GLU A 1 146 ? 4.13650   6.67078   7.75725  1.000 24.29951 ? 146 GLU A CD  1 
ATOM   1262 O OE1 . GLU A 1 146 ? 3.40378   5.78273   7.26850  1.000 26.50094 ? 146 GLU A OE1 1 
ATOM   1263 O OE2 . GLU A 1 146 ? 4.39528   7.74057   7.16875  1.000 25.69639 ? 146 GLU A OE2 1 
ATOM   1264 N N   A GLY A 1 147 ? 0.53089   5.37045   10.31017 0.500 29.16236 ? 147 GLY A N   1 
ATOM   1265 N N   B GLY A 1 147 ? 0.62957   5.23578   10.30305 0.500 29.57623 ? 147 GLY A N   1 
ATOM   1266 C CA  A GLY A 1 147 ? -0.48061  4.45835   10.81640 0.500 35.15809 ? 147 GLY A CA  1 
ATOM   1267 C CA  B GLY A 1 147 ? -0.39204  4.37404   10.84987 0.500 35.12448 ? 147 GLY A CA  1 
ATOM   1268 C C   A GLY A 1 147 ? -1.49520  5.05919   11.76462 0.500 42.52711 ? 147 GLY A C   1 
ATOM   1269 C C   B GLY A 1 147 ? -1.56763  5.09615   11.45256 0.500 41.29262 ? 147 GLY A C   1 
ATOM   1270 O O   A GLY A 1 147 ? -2.00332  4.35250   12.64127 0.500 40.22687 ? 147 GLY A O   1 
ATOM   1271 O O   B GLY A 1 147 ? -2.51964  4.43578   11.88817 0.500 37.03523 ? 147 GLY A O   1 
ATOM   1272 N N   A GLU A 1 148 ? -1.82292  6.34377   11.60371 0.700 51.64571 ? 148 GLU A N   1 
ATOM   1273 N N   B GLU A 1 148 ? -1.52683  6.42635   11.51780 0.300 51.15950 ? 148 GLU A N   1 
ATOM   1274 C CA  A GLU A 1 148 ? -2.72061  6.99774   12.55220 0.700 61.97694 ? 148 GLU A CA  1 
ATOM   1275 C CA  B GLU A 1 148 ? -2.70261  7.20864   11.86183 0.300 61.97650 ? 148 GLU A CA  1 
ATOM   1276 C C   A GLU A 1 148 ? -4.14548  6.46069   12.46292 0.700 55.04364 ? 148 GLU A C   1 
ATOM   1277 C C   B GLU A 1 148 ? -3.81820  6.83784   10.89625 0.300 55.34118 ? 148 GLU A C   1 
ATOM   1278 O O   A GLU A 1 148 ? -4.85065  6.41456   13.47757 0.700 54.26949 ? 148 GLU A O   1 
ATOM   1279 O O   B GLU A 1 148 ? -3.80674  7.25099   9.73171  0.300 54.97530 ? 148 GLU A O   1 
ATOM   1280 C CB  A GLU A 1 148 ? -2.69936  8.51277   12.34672 0.700 60.71574 ? 148 GLU A CB  1 
ATOM   1281 C CB  B GLU A 1 148 ? -2.39164  8.70444   11.78530 0.300 60.87632 ? 148 GLU A CB  1 
ATOM   1282 N N   A GLY A 1 149 ? -4.58671  6.05184   11.27287 0.500 48.95136 ? 149 GLY A N   1 
ATOM   1283 N N   B GLY A 1 149 ? -4.76512  6.03174   11.36737 0.500 49.74698 ? 149 GLY A N   1 
ATOM   1284 C CA  A GLY A 1 149 ? -5.93920  5.56072   11.09493 0.500 44.32236 ? 149 GLY A CA  1 
ATOM   1285 C CA  B GLY A 1 149 ? -5.82773  5.52212   10.52593 0.500 45.77922 ? 149 GLY A CA  1 
ATOM   1286 C C   A GLY A 1 149 ? -6.14076  4.07850   11.31482 0.500 37.17917 ? 149 GLY A C   1 
ATOM   1287 C C   B GLY A 1 149 ? -6.06785  4.03880   10.72411 0.500 39.24849 ? 149 GLY A C   1 
ATOM   1288 O O   A GLY A 1 149 ? -7.28203  3.60811   11.27288 0.500 35.02020 ? 149 GLY A O   1 
ATOM   1289 O O   B GLY A 1 149 ? -7.04954  3.48867   10.21625 0.500 38.42178 ? 149 GLY A O   1 
ATOM   1290 N N   A LEU A 1 150 ? -5.06322  3.33082   11.54706 0.500 33.92390 ? 150 LEU A N   1 
ATOM   1291 N N   B LEU A 1 150 ? -5.18098  3.38201   11.46621 0.500 35.06563 ? 150 LEU A N   1 
ATOM   1292 C CA  A LEU A 1 150 ? -5.16753  1.89348   11.75980 0.500 31.58776 ? 150 LEU A CA  1 
ATOM   1293 C CA  B LEU A 1 150 ? -5.27595  1.94920   11.69971 0.500 32.13652 ? 150 LEU A CA  1 
ATOM   1294 C C   A LEU A 1 150 ? -6.00062  1.59071   12.99939 0.500 28.29944 ? 150 LEU A C   1 
ATOM   1295 C C   B LEU A 1 150 ? -6.10025  1.65255   12.94594 0.500 28.58783 ? 150 LEU A C   1 
ATOM   1296 O O   A LEU A 1 150 ? -5.96994  2.32336   13.99166 0.500 27.21788 ? 150 LEU A O   1 
ATOM   1297 O O   B LEU A 1 150 ? -6.15328  2.44745   13.88818 0.500 27.83556 ? 150 LEU A O   1 
ATOM   1298 C CB  A LEU A 1 150 ? -3.77326  1.29126   11.94353 0.500 30.16392 ? 150 LEU A CB  1 
ATOM   1299 C CB  B LEU A 1 150 ? -3.88324  1.33450   11.85553 0.500 30.98132 ? 150 LEU A CB  1 
ATOM   1300 C CG  A LEU A 1 150 ? -3.04112  0.72293   10.72844 0.500 30.00220 ? 150 LEU A CG  1 
ATOM   1301 C CG  B LEU A 1 150 ? -3.10096  1.04530   10.57443 0.500 31.13093 ? 150 LEU A CG  1 
ATOM   1302 C CD1 A LEU A 1 150 ? -1.59259  0.41877   11.08094 0.500 30.75712 ? 150 LEU A CD1 1 
ATOM   1303 C CD1 B LEU A 1 150 ? -1.66153  0.67650   10.89690 0.500 32.24312 ? 150 LEU A CD1 1 
ATOM   1304 C CD2 A LEU A 1 150 ? -3.74277  -0.52859  10.23647 0.500 29.52017 ? 150 LEU A CD2 1 
ATOM   1305 C CD2 B LEU A 1 150 ? -3.77697  -0.06612  9.79168  0.500 30.61854 ? 150 LEU A CD2 1 
ATOM   1306 N N   . LYS A 1 151 ? -6.74059  0.48527   12.93883 1.000 26.57980 ? 151 LYS A N   1 
ATOM   1307 C CA  . LYS A 1 151 ? -7.53987  0.00477   14.05619 1.000 24.75830 ? 151 LYS A CA  1 
ATOM   1308 C C   . LYS A 1 151 ? -7.26588  -1.48160  14.25061 1.000 23.14320 ? 151 LYS A C   1 
ATOM   1309 O O   . LYS A 1 151 ? -6.60419  -2.12708  13.43263 1.000 24.54268 ? 151 LYS A O   1 
ATOM   1310 C CB  . LYS A 1 151 ? -9.03986  0.22830   13.81507 1.000 26.04464 ? 151 LYS A CB  1 
ATOM   1311 C CG  . LYS A 1 151 ? -9.47056  1.68447   13.76770 1.000 28.55005 ? 151 LYS A CG  1 
ATOM   1312 C CD  . LYS A 1 151 ? -9.21787  2.38150   15.09489 1.000 31.35899 ? 151 LYS A CD  1 
ATOM   1313 C CE  . LYS A 1 151 ? -10.03156 3.66155   15.20342 1.000 35.85103 ? 151 LYS A CE  1 
ATOM   1314 N NZ  . LYS A 1 151 ? -9.68353  4.64017   14.13706 1.000 35.22666 ? 151 LYS A NZ  1 
ATOM   1315 N N   . GLY A 1 152 ? -7.77874  -2.02465  15.35386 1.000 19.98021 ? 152 GLY A N   1 
ATOM   1316 C CA  . GLY A 1 152 ? -7.71025  -3.45931  15.57039 1.000 18.51603 ? 152 GLY A CA  1 
ATOM   1317 C C   . GLY A 1 152 ? -6.30643  -3.99889  15.82556 1.000 16.31286 ? 152 GLY A C   1 
ATOM   1318 O O   . GLY A 1 152 ? -5.36466  -3.27112  16.15991 1.000 15.20180 ? 152 GLY A O   1 
ATOM   1319 N N   . ASP A 1 153 ? -6.18336  -5.31965  15.64676 1.000 17.18525 ? 153 ASP A N   1 
ATOM   1320 C CA  . ASP A 1 153 ? -4.94137  -6.01903  15.97122 1.000 18.70257 ? 153 ASP A CA  1 
ATOM   1321 C C   . ASP A 1 153 ? -3.75671  -5.46688  15.18792 1.000 17.18126 ? 153 ASP A C   1 
ATOM   1322 O O   . ASP A 1 153 ? -2.63849  -5.38841  15.71428 1.000 16.83698 ? 153 ASP A O   1 
ATOM   1323 C CB  . ASP A 1 153 ? -5.09457  -7.51355  15.68471 1.000 21.87291 ? 153 ASP A CB  1 
ATOM   1324 C CG  . ASP A 1 153 ? -5.75570  -8.27080  16.81886 1.000 27.10215 ? 153 ASP A CG  1 
ATOM   1325 O OD1 . ASP A 1 153 ? -6.02365  -7.66822  17.87878 1.000 28.33199 ? 153 ASP A OD1 1 
ATOM   1326 O OD2 . ASP A 1 153 ? -6.00743  -9.48206  16.64499 1.000 31.21067 ? 153 ASP A OD2 1 
ATOM   1327 N N   A GLN A 1 154 ? -3.97178  -5.09921  13.92175 0.500 17.44295 ? 154 GLN A N   1 
ATOM   1328 N N   B GLN A 1 154 ? -3.97809  -5.09427  13.92479 0.500 17.03181 ? 154 GLN A N   1 
ATOM   1329 C CA  A GLN A 1 154 ? -2.87721  -4.55047  13.12713 0.500 18.85933 ? 154 GLN A CA  1 
ATOM   1330 C CA  B GLN A 1 154 ? -2.89486  -4.54712  13.11517 0.500 18.06984 ? 154 GLN A CA  1 
ATOM   1331 C C   A GLN A 1 154 ? -2.39773  -3.22091  13.69358 0.500 17.03971 ? 154 GLN A C   1 
ATOM   1332 C C   B GLN A 1 154 ? -2.40476  -3.21994  13.67922 0.500 16.66792 ? 154 GLN A C   1 
ATOM   1333 O O   A GLN A 1 154 ? -1.19415  -2.93581  13.69138 0.500 15.59821 ? 154 GLN A O   1 
ATOM   1334 O O   B GLN A 1 154 ? -1.20109  -2.93581  13.66139 0.500 15.29013 ? 154 GLN A O   1 
ATOM   1335 C CB  A GLN A 1 154 ? -3.29727  -4.39904  11.66427 0.500 23.00999 ? 154 GLN A CB  1 
ATOM   1336 C CB  B GLN A 1 154 ? -3.36136  -4.38107  11.66869 0.500 21.19093 ? 154 GLN A CB  1 
ATOM   1337 C CG  A GLN A 1 154 ? -3.55472  -5.71527  10.94947 0.500 26.39525 ? 154 GLN A CG  1 
ATOM   1338 C CG  B GLN A 1 154 ? -2.25131  -4.05458  10.68425 0.500 23.52658 ? 154 GLN A CG  1 
ATOM   1339 C CD  A GLN A 1 154 ? -3.65970  -5.55105  9.44560  0.500 28.19615 ? 154 GLN A CD  1 
ATOM   1340 C CD  B GLN A 1 154 ? -2.77893  -3.77008  9.28984  0.500 26.77065 ? 154 GLN A CD  1 
ATOM   1341 O OE1 A GLN A 1 154 ? -2.79856  -4.93844  8.81425  0.500 31.78407 ? 154 GLN A OE1 1 
ATOM   1342 O OE1 B GLN A 1 154 ? -2.01786  -3.71538  8.32421  0.500 27.23442 ? 154 GLN A OE1 1 
ATOM   1343 N NE2 A GLN A 1 154 ? -4.72064  -6.09689  8.86398  0.500 29.70660 ? 154 GLN A NE2 1 
ATOM   1344 N NE2 B GLN A 1 154 ? -4.08853  -3.58222  9.18018  0.500 27.53724 ? 154 GLN A NE2 1 
ATOM   1345 N N   . ALA A 1 155 ? -3.32453  -2.39624  14.19043 1.000 16.46041 ? 155 ALA A N   1 
ATOM   1346 C CA  . ALA A 1 155 ? -2.93065  -1.13582  14.81061 1.000 14.61436 ? 155 ALA A CA  1 
ATOM   1347 C C   . ALA A 1 155 ? -2.11073  -1.37670  16.06929 1.000 14.64582 ? 155 ALA A C   1 
ATOM   1348 O O   . ALA A 1 155 ? -1.11201  -0.68767  16.30700 1.000 15.69068 ? 155 ALA A O   1 
ATOM   1349 C CB  . ALA A 1 155 ? -4.16772  -0.30731  15.15287 1.000 15.72571 ? 155 ALA A CB  1 
ATOM   1350 N N   . VAL A 1 156 ? -2.52850  -2.33950  16.89610 1.000 13.86239 ? 156 VAL A N   1 
ATOM   1351 C CA  . VAL A 1 156 ? -1.77897  -2.64560  18.11062 1.000 13.91957 ? 156 VAL A CA  1 
ATOM   1352 C C   . VAL A 1 156 ? -0.39183  -3.16819  17.76638 1.000 12.32915 ? 156 VAL A C   1 
ATOM   1353 O O   . VAL A 1 156 ? 0.60806   -2.75849  18.36814 1.000 11.36380 ? 156 VAL A O   1 
ATOM   1354 C CB  . VAL A 1 156 ? -2.56374  -3.62204  19.00709 1.000 15.37417 ? 156 VAL A CB  1 
ATOM   1355 C CG1 . VAL A 1 156 ? -1.72125  -4.02741  20.21283 1.000 16.18508 ? 156 VAL A CG1 1 
ATOM   1356 C CG2 . VAL A 1 156 ? -3.86972  -2.99043  19.45498 1.000 16.06735 ? 156 VAL A CG2 1 
ATOM   1357 N N   . ALA A 1 157 ? -0.30404  -4.07309  16.78637 1.000 12.71275 ? 157 ALA A N   1 
ATOM   1358 C CA  . ALA A 1 157 ? 0.99694   -4.62104  16.40920 1.000 12.95192 ? 157 ALA A CA  1 
ATOM   1359 C C   . ALA A 1 157 ? 1.91306   -3.54277  15.83886 1.000 12.69266 ? 157 ALA A C   1 
ATOM   1360 O O   . ALA A 1 157 ? 3.12497   -3.55379  16.08460 1.000 12.58577 ? 157 ALA A O   1 
ATOM   1361 C CB  . ALA A 1 157 ? 0.81690   -5.76835  15.41420 1.000 13.94135 ? 157 ALA A CB  1 
ATOM   1362 N N   . PHE A 1 158 ? 1.35010   -2.59278  15.08665 1.000 12.59779 ? 158 PHE A N   1 
ATOM   1363 C CA  . PHE A 1 158 ? 2.16292   -1.51083  14.53839 1.000 12.17794 ? 158 PHE A CA  1 
ATOM   1364 C C   . PHE A 1 158 ? 2.57328   -0.52101  15.62404 1.000 12.89468 ? 158 PHE A C   1 
ATOM   1365 O O   . PHE A 1 158 ? 3.70925   -0.02509  15.62353 1.000 12.95868 ? 158 PHE A O   1 
ATOM   1366 C CB  . PHE A 1 158 ? 1.41724   -0.81061  13.40094 1.000 12.55221 ? 158 PHE A CB  1 
ATOM   1367 C CG  . PHE A 1 158 ? 2.28047   0.11995   12.60072 1.000 12.77195 ? 158 PHE A CG  1 
ATOM   1368 C CD1 . PHE A 1 158 ? 3.38201   -0.35913  11.90949 1.000 13.11699 ? 158 PHE A CD1 1 
ATOM   1369 C CD2 . PHE A 1 158 ? 1.99656   1.47101   12.54137 1.000 15.29966 ? 158 PHE A CD2 1 
ATOM   1370 C CE1 . PHE A 1 158 ? 4.18183   0.49822   11.17397 1.000 15.17597 ? 158 PHE A CE1 1 
ATOM   1371 C CE2 . PHE A 1 158 ? 2.79353   2.33059   11.80944 1.000 15.37207 ? 158 PHE A CE2 1 
ATOM   1372 C CZ  . PHE A 1 158 ? 3.88611   1.84411   11.12624 1.000 16.13583 ? 158 PHE A CZ  1 
ATOM   1373 N N   A GLU A 1 159 ? 1.66851   -0.21703  16.55958 0.500 12.22439 ? 159 GLU A N   1 
ATOM   1374 N N   B GLU A 1 159 ? 1.65593   -0.21619  16.54781 0.500 12.92265 ? 159 GLU A N   1 
ATOM   1375 C CA  A GLU A 1 159 ? 2.04425   0.64864   17.67405 0.500 12.41750 ? 159 GLU A CA  1 
ATOM   1376 C CA  B GLU A 1 159 ? 1.99585   0.61764   17.69683 0.500 13.97729 ? 159 GLU A CA  1 
ATOM   1377 C C   A GLU A 1 159 ? 3.16300   0.03677   18.50845 0.500 11.12104 ? 159 GLU A C   1 
ATOM   1378 C C   B GLU A 1 159 ? 3.16942   0.03148   18.47093 0.500 11.81760 ? 159 GLU A C   1 
ATOM   1379 O O   A GLU A 1 159 ? 4.01957   0.76447   19.02153 0.500 11.76724 ? 159 GLU A O   1 
ATOM   1380 O O   B GLU A 1 159 ? 4.06590   0.76470   18.90328 0.500 12.34518 ? 159 GLU A O   1 
ATOM   1381 C CB  A GLU A 1 159 ? 0.83180   0.97979   18.54363 0.500 12.84798 ? 159 GLU A CB  1 
ATOM   1382 C CB  B GLU A 1 159 ? 0.77271   0.76659   18.60377 0.500 16.13918 ? 159 GLU A CB  1 
ATOM   1383 C CG  A GLU A 1 159 ? -0.11050  1.99992   17.92787 0.500 13.02415 ? 159 GLU A CG  1 
ATOM   1384 C CG  B GLU A 1 159 ? 1.03642   1.48742   19.91938 0.500 17.33458 ? 159 GLU A CG  1 
ATOM   1385 C CD  A GLU A 1 159 ? 0.58768   3.29253   17.54033 0.500 13.46586 ? 159 GLU A CD  1 
ATOM   1386 C CD  B GLU A 1 159 ? 0.81492   2.98477   19.82760 0.500 19.12839 ? 159 GLU A CD  1 
ATOM   1387 O OE1 A GLU A 1 159 ? 1.36870   3.82227   18.35938 0.500 13.96121 ? 159 GLU A OE1 1 
ATOM   1388 O OE1 B GLU A 1 159 ? 0.37560   3.46129   18.75848 0.500 19.65252 ? 159 GLU A OE1 1 
ATOM   1389 O OE2 A GLU A 1 159 ? 0.36242   3.77408   16.40874 0.500 13.10853 ? 159 GLU A OE2 1 
ATOM   1390 O OE2 B GLU A 1 159 ? 1.07236   3.68391   20.83138 0.500 18.98979 ? 159 GLU A OE2 1 
ATOM   1391 N N   . ASN A 1 160 ? 3.18664   -1.29266  18.64715 1.000 11.11060 ? 160 ASN A N   1 
ATOM   1392 C CA  . ASN A 1 160 ? 4.30118   -1.93087  19.34647 1.000 11.67946 ? 160 ASN A CA  1 
ATOM   1393 C C   . ASN A 1 160 ? 5.61214   -1.72927  18.59690 1.000 12.47573 ? 160 ASN A C   1 
ATOM   1394 O O   . ASN A 1 160 ? 6.65276   -1.45992  19.21180 1.000 11.55195 ? 160 ASN A O   1 
ATOM   1395 C CB  . ASN A 1 160 ? 4.02235   -3.41696  19.55362 1.000 12.59106 ? 160 ASN A CB  1 
ATOM   1396 C CG  . ASN A 1 160 ? 2.88367   -3.66164  20.51500 1.000 13.23229 ? 160 ASN A CG  1 
ATOM   1397 O OD1 . ASN A 1 160 ? 2.52484   -2.78818  21.30731 1.000 15.40215 ? 160 ASN A OD1 1 
ATOM   1398 N ND2 . ASN A 1 160 ? 2.30577   -4.85339  20.45316 1.000 13.06467 ? 160 ASN A ND2 1 
ATOM   1399 N N   . ILE A 1 161 ? 5.58217   -1.86450  17.26668 1.000 12.11983 ? 161 ILE A N   1 
ATOM   1400 C CA  . ILE A 1 161 ? 6.76065   -1.57141  16.45311 1.000 12.40534 ? 161 ILE A CA  1 
ATOM   1401 C C   . ILE A 1 161 ? 7.19479   -0.12404  16.64705 1.000 11.85187 ? 161 ILE A C   1 
ATOM   1402 O O   . ILE A 1 161 ? 8.37197   0.16226   16.89850 1.000 11.42817 ? 161 ILE A O   1 
ATOM   1403 C CB  . ILE A 1 161 ? 6.48141   -1.88898  14.97346 1.000 12.79358 ? 161 ILE A CB  1 
ATOM   1404 C CG1 . ILE A 1 161 ? 6.43058   -3.40191  14.74819 1.000 14.47829 ? 161 ILE A CG1 1 
ATOM   1405 C CG2 . ILE A 1 161 ? 7.51459   -1.22948  14.07672 1.000 12.65273 ? 161 ILE A CG2 1 
ATOM   1406 C CD1 . ILE A 1 161 ? 6.02775   -3.79471  13.34929 1.000 14.82687 ? 161 ILE A CD1 1 
ATOM   1407 N N   . LYS A 1 162 ? 6.24574   0.80946   16.53521 1.000 10.07723 ? 162 LYS A N   1 
ATOM   1408 C CA  . LYS A 1 162 ? 6.56924   2.22461   16.68649 1.000 10.65032 ? 162 LYS A CA  1 
ATOM   1409 C C   . LYS A 1 162 ? 7.18096   2.50860   18.05247 1.000 11.75573 ? 162 LYS A C   1 
ATOM   1410 O O   . LYS A 1 162 ? 8.20547   3.19398   18.15478 1.000 11.04136 ? 162 LYS A O   1 
ATOM   1411 C CB  . LYS A 1 162 ? 5.32240   3.07770   16.45299 1.000 13.11263 ? 162 LYS A CB  1 
ATOM   1412 C CG  . LYS A 1 162 ? 4.90206   3.12666   14.99814 1.000 15.74030 ? 162 LYS A CG  1 
ATOM   1413 C CD  . LYS A 1 162 ? 3.50500   3.69689   14.83101 1.000 17.98623 ? 162 LYS A CD  1 
ATOM   1414 C CE  . LYS A 1 162 ? 3.35576   5.05373   15.47306 1.000 15.67432 ? 162 LYS A CE  1 
ATOM   1415 N NZ  . LYS A 1 162 ? 2.05858   5.66579   15.07398 1.000 14.00413 ? 162 LYS A NZ  1 
ATOM   1416 N N   . ASN A 1 163 ? 6.57385   1.97331   19.11594 1.000 11.57594 ? 163 ASN A N   1 
ATOM   1417 C CA  . ASN A 1 163 ? 7.05594   2.26636   20.46200 1.000 12.80405 ? 163 ASN A CA  1 
ATOM   1418 C C   . ASN A 1 163 ? 8.42891   1.65856   20.72850 1.000 11.75492 ? 163 ASN A C   1 
ATOM   1419 O O   . ASN A 1 163 ? 9.22387   2.23909   21.47802 1.000 13.27948 ? 163 ASN A O   1 
ATOM   1420 C CB  . ASN A 1 163 ? 6.04283   1.80873   21.51138 1.000 13.39591 ? 163 ASN A CB  1 
ATOM   1421 C CG  . ASN A 1 163 ? 4.79637   2.67759   21.53791 1.000 16.18710 ? 163 ASN A CG  1 
ATOM   1422 O OD1 . ASN A 1 163 ? 4.84013   3.86146   21.19316 1.000 19.26857 ? 163 ASN A OD1 1 
ATOM   1423 N ND2 . ASN A 1 163 ? 3.67985   2.09554   21.94959 1.000 16.91712 ? 163 ASN A ND2 1 
ATOM   1424 N N   . LEU A 1 164 ? 8.73236   0.49705   20.14399 1.000 10.50719 ? 164 LEU A N   1 
ATOM   1425 C CA  . LEU A 1 164 ? 10.07823  -0.04630  20.29531 1.000 10.86119 ? 164 LEU A CA  1 
ATOM   1426 C C   . LEU A 1 164 ? 11.11940  0.91079   19.73027 1.000 9.47887  ? 164 LEU A C   1 
ATOM   1427 O O   . LEU A 1 164 ? 12.16351  1.14792   20.35043 1.000 12.14468 ? 164 LEU A O   1 
ATOM   1428 C CB  . LEU A 1 164 ? 10.18506  -1.40695  19.61285 1.000 11.77340 ? 164 LEU A CB  1 
ATOM   1429 C CG  . LEU A 1 164 ? 11.61203  -1.95695  19.58785 1.000 13.37392 ? 164 LEU A CG  1 
ATOM   1430 C CD1 . LEU A 1 164 ? 12.10825  -2.19367  21.00571 1.000 14.43147 ? 164 LEU A CD1 1 
ATOM   1431 C CD2 . LEU A 1 164 ? 11.67527  -3.22896  18.79122 1.000 14.37131 ? 164 LEU A CD2 1 
ATOM   1432 N N   . ILE A 1 165 ? 10.84811  1.47668   18.55486 1.000 8.67155  ? 165 ILE A N   1 
ATOM   1433 C CA  . ILE A 1 165 ? 11.77969  2.42385   17.95454 1.000 9.58152  ? 165 ILE A CA  1 
ATOM   1434 C C   . ILE A 1 165 ? 11.80220  3.72676   18.74566 1.000 9.39979  ? 165 ILE A C   1 
ATOM   1435 O O   . ILE A 1 165 ? 12.87303  4.26022   19.06257 1.000 9.00529  ? 165 ILE A O   1 
ATOM   1436 C CB  . ILE A 1 165 ? 11.42854  2.64484   16.47278 1.000 8.99798  ? 165 ILE A CB  1 
ATOM   1437 C CG1 . ILE A 1 165 ? 11.62851  1.34505   15.69396 1.000 10.66614 ? 165 ILE A CG1 1 
ATOM   1438 C CG2 . ILE A 1 165 ? 12.23439  3.80077   15.88459 1.000 9.35623  ? 165 ILE A CG2 1 
ATOM   1439 C CD1 . ILE A 1 165 ? 11.02883  1.36866   14.31180 1.000 11.92975 ? 165 ILE A CD1 1 
ATOM   1440 N N   . LEU A 1 166 ? 10.61994  4.24562   19.09473 1.000 11.47350 ? 166 LEU A N   1 
ATOM   1441 C CA  . LEU A 1 166 ? 10.54236  5.53831   19.77166 1.000 12.08760 ? 166 LEU A CA  1 
ATOM   1442 C C   . LEU A 1 166 ? 11.24469  5.50722   21.12183 1.000 13.55236 ? 166 LEU A C   1 
ATOM   1443 O O   . LEU A 1 166 ? 11.86825  6.49634   21.52411 1.000 14.59748 ? 166 LEU A O   1 
ATOM   1444 C CB  . LEU A 1 166 ? 9.08295   5.96006   19.93939 1.000 12.42396 ? 166 LEU A CB  1 
ATOM   1445 C CG  . LEU A 1 166 ? 8.32537   6.34389   18.66798 1.000 13.33155 ? 166 LEU A CG  1 
ATOM   1446 C CD1 . LEU A 1 166 ? 6.82996   6.38785   18.95879 1.000 14.68985 ? 166 LEU A CD1 1 
ATOM   1447 C CD2 . LEU A 1 166 ? 8.81145   7.68356   18.10703 1.000 13.30556 ? 166 LEU A CD2 1 
ATOM   1448 N N   . VAL A 1 167 ? 11.16015  4.38495   21.83171 1.000 12.09033 ? 167 VAL A N   1 
ATOM   1449 C CA  . VAL A 1 167 ? 11.82085  4.24736   23.12804 1.000 11.04984 ? 167 VAL A CA  1 
ATOM   1450 C C   . VAL A 1 167 ? 13.24366  3.72649   22.97685 1.000 9.93085  ? 167 VAL A C   1 
ATOM   1451 O O   . VAL A 1 167 ? 14.18834  4.28482   23.54645 1.000 11.40663 ? 167 VAL A O   1 
ATOM   1452 C CB  . VAL A 1 167 ? 10.98958  3.34050   24.06086 1.000 12.73885 ? 167 VAL A CB  1 
ATOM   1453 C CG1 . VAL A 1 167 ? 11.70290  3.16118   25.38792 1.000 13.74088 ? 167 VAL A CG1 1 
ATOM   1454 C CG2 . VAL A 1 167 ? 9.59949   3.90963   24.26603 1.000 13.92064 ? 167 VAL A CG2 1 
ATOM   1455 N N   . GLY A 1 168 ? 13.41041  2.65317   22.20088 1.000 9.56647  ? 168 GLY A N   1 
ATOM   1456 C CA  . GLY A 1 168 ? 14.68875  1.96167   22.14711 1.000 10.57326 ? 168 GLY A CA  1 
ATOM   1457 C C   . GLY A 1 168 ? 15.80198  2.75298   21.48928 1.000 11.27694 ? 168 GLY A C   1 
ATOM   1458 O O   . GLY A 1 168 ? 16.97270  2.59176   21.84610 1.000 11.70824 ? 168 GLY A O   1 
ATOM   1459 N N   . TRP A 1 169 ? 15.46855  3.61803   20.53138 1.000 9.74502  ? 169 TRP A N   1 
ATOM   1460 C CA  . TRP A 1 169 ? 16.52137  4.36843   19.86029 1.000 11.60568 ? 169 TRP A CA  1 
ATOM   1461 C C   . TRP A 1 169 ? 17.05845  5.51818   20.70204 1.000 11.22429 ? 169 TRP A C   1 
ATOM   1462 O O   . TRP A 1 169 ? 18.07184  6.11671   20.32514 1.000 10.65465 ? 169 TRP A O   1 
ATOM   1463 C CB  . TRP A 1 169 ? 16.06328  4.85413   18.48190 1.000 12.32517 ? 169 TRP A CB  1 
ATOM   1464 C CG  . TRP A 1 169 ? 15.85124  3.73878   17.48510 1.000 12.02652 ? 169 TRP A CG  1 
ATOM   1465 C CD1 . TRP A 1 169 ? 15.56666  2.42686   17.75909 1.000 13.08744 ? 169 TRP A CD1 1 
ATOM   1466 C CD2 . TRP A 1 169 ? 15.90646  3.84400   16.05854 1.000 12.13612 ? 169 TRP A CD2 1 
ATOM   1467 N NE1 . TRP A 1 169 ? 15.44104  1.71329   16.58894 1.000 12.12942 ? 169 TRP A NE1 1 
ATOM   1468 C CE2 . TRP A 1 169 ? 15.64573  2.56056   15.53187 1.000 12.55222 ? 169 TRP A CE2 1 
ATOM   1469 C CE3 . TRP A 1 169 ? 16.15702  4.89713   15.17410 1.000 14.13360 ? 169 TRP A CE3 1 
ATOM   1470 C CZ2 . TRP A 1 169 ? 15.62279  2.30666   14.16123 1.000 12.87636 ? 169 TRP A CZ2 1 
ATOM   1471 C CZ3 . TRP A 1 169 ? 16.13467  4.64025   13.81244 1.000 13.29482 ? 169 TRP A CZ3 1 
ATOM   1472 C CH2 . TRP A 1 169 ? 15.87014  3.35655   13.32160 1.000 12.68853 ? 169 TRP A CH2 1 
ATOM   1473 N N   . ILE A 1 170 ? 16.41616  5.82423   21.83375 1.000 10.25920 ? 170 ILE A N   1 
ATOM   1474 C CA  . ILE A 1 170 ? 16.92223  6.85103   22.74089 1.000 11.07436 ? 170 ILE A CA  1 
ATOM   1475 C C   . ILE A 1 170 ? 18.25871  6.43093   23.33219 1.000 9.13288  ? 170 ILE A C   1 
ATOM   1476 O O   . ILE A 1 170 ? 19.07037  7.27870   23.72774 1.000 10.06436 ? 170 ILE A O   1 
ATOM   1477 C CB  . ILE A 1 170 ? 15.86994  7.16051   23.82773 1.000 11.78485 ? 170 ILE A CB  1 
ATOM   1478 C CG1 . ILE A 1 170 ? 14.56175  7.64877   23.18940 1.000 12.56101 ? 170 ILE A CG1 1 
ATOM   1479 C CG2 . ILE A 1 170 ? 16.39260  8.18551   24.84181 1.000 13.99271 ? 170 ILE A CG2 1 
ATOM   1480 C CD1 . ILE A 1 170 ? 13.46517  7.95760   24.18906 1.000 16.60179 ? 170 ILE A CD1 1 
ATOM   1481 N N   . ILE A 1 171 ? 18.51589  5.12304   23.40012 1.000 8.55596  ? 171 ILE A N   1 
ATOM   1482 C CA  . ILE A 1 171 ? 19.76117  4.64896   23.99379 1.000 9.05840  ? 171 ILE A CA  1 
ATOM   1483 C C   . ILE A 1 171 ? 20.96712  5.17698   23.23066 1.000 10.06478 ? 171 ILE A C   1 
ATOM   1484 O O   . ILE A 1 171 ? 22.01610  5.45087   23.82663 1.000 10.51154 ? 171 ILE A O   1 
ATOM   1485 C CB  . ILE A 1 171 ? 19.76916  3.11183   24.08966 1.000 9.79970  ? 171 ILE A CB  1 
ATOM   1486 C CG1 . ILE A 1 171 ? 18.54841  2.61104   24.86003 1.000 11.56602 ? 171 ILE A CG1 1 
ATOM   1487 C CG2 . ILE A 1 171 ? 21.04002  2.62922   24.76720 1.000 9.69720  ? 171 ILE A CG2 1 
ATOM   1488 C CD1 . ILE A 1 171 ? 18.30094  1.11665   24.69730 1.000 12.46962 ? 171 ILE A CD1 1 
ATOM   1489 N N   . TYR A 1 172 ? 20.84568  5.33710   21.91014 1.000 9.73248  ? 172 TYR A N   1 
ATOM   1490 C CA  . TYR A 1 172 ? 21.99849  5.77180   21.12275 1.000 11.01941 ? 172 TYR A CA  1 
ATOM   1491 C C   . TYR A 1 172 ? 22.50435  7.15750   21.49721 1.000 9.70033  ? 172 TYR A C   1 
ATOM   1492 O O   . TYR A 1 172 ? 23.70924  7.28932   21.77055 1.000 9.58554  ? 172 TYR A O   1 
ATOM   1493 C CB  . TYR A 1 172 ? 21.73785  5.61337   19.62252 1.000 11.38308 ? 172 TYR A CB  1 
ATOM   1494 C CG  . TYR A 1 172 ? 21.41347  4.20189   19.22234 1.000 9.87205  ? 172 TYR A CG  1 
ATOM   1495 C CD1 . TYR A 1 172 ? 22.41989  3.26276   19.03872 1.000 8.71738  ? 172 TYR A CD1 1 
ATOM   1496 C CD2 . TYR A 1 172 ? 20.10141  3.80220   19.03806 1.000 9.81106  ? 172 TYR A CD2 1 
ATOM   1497 C CE1 . TYR A 1 172 ? 22.12614  1.96179   18.67889 1.000 9.81035  ? 172 TYR A CE1 1 
ATOM   1498 C CE2 . TYR A 1 172 ? 19.79508  2.50082   18.67758 1.000 9.74948  ? 172 TYR A CE2 1 
ATOM   1499 C CZ  . TYR A 1 172 ? 20.81034  1.58655   18.49471 1.000 9.28615  ? 172 TYR A CZ  1 
ATOM   1500 O OH  . TYR A 1 172 ? 20.50368  0.29331   18.13759 1.000 9.41942  ? 172 TYR A OH  1 
ATOM   1501 N N   . PRO A 1 173 ? 21.68810  8.21936   21.50500 1.000 9.20091  ? 173 PRO A N   1 
ATOM   1502 C CA  . PRO A 1 173 ? 22.21615  9.51921   21.95527 1.000 9.69908  ? 173 PRO A CA  1 
ATOM   1503 C C   . PRO A 1 173 ? 22.74254  9.49316   23.38022 1.000 10.38257 ? 173 PRO A C   1 
ATOM   1504 O O   . PRO A 1 173 ? 23.71988  10.19434  23.68075 1.000 10.79386 ? 173 PRO A O   1 
ATOM   1505 C CB  . PRO A 1 173 ? 21.02615  10.47600  21.78391 1.000 10.04296 ? 173 PRO A CB  1 
ATOM   1506 C CG  . PRO A 1 173 ? 19.81895  9.60231   21.66336 1.000 9.83516  ? 173 PRO A CG  1 
ATOM   1507 C CD  . PRO A 1 173 ? 20.30262  8.33918   21.01449 1.000 8.97081  ? 173 PRO A CD  1 
ATOM   1508 N N   . LEU A 1 174 ? 22.13907  8.68758   24.26155 1.000 12.55127 ? 174 LEU A N   1 
ATOM   1509 C CA  . LEU A 1 174 ? 22.68665  8.52563   25.60533 1.000 12.12588 ? 174 LEU A CA  1 
ATOM   1510 C C   . LEU A 1 174 ? 24.09044  7.93538   25.55733 1.000 13.03761 ? 174 LEU A C   1 
ATOM   1511 O O   . LEU A 1 174 ? 24.99957  8.41432   26.24330 1.000 15.21286 ? 174 LEU A O   1 
ATOM   1512 C CB  . LEU A 1 174 ? 21.76354  7.65839   26.46154 1.000 12.84984 ? 174 LEU A CB  1 
ATOM   1513 C CG  . LEU A 1 174 ? 20.39585  8.25452   26.80503 1.000 14.86209 ? 174 LEU A CG  1 
ATOM   1514 C CD1 . LEU A 1 174 ? 19.51484  7.23499   27.51787 1.000 17.13843 ? 174 LEU A CD1 1 
ATOM   1515 C CD2 . LEU A 1 174 ? 20.54462  9.51346   27.64469 1.000 18.03175 ? 174 LEU A CD2 1 
ATOM   1516 N N   . GLY A 1 175 ? 24.28746  6.89149   24.74851 1.000 12.25349 ? 175 GLY A N   1 
ATOM   1517 C CA  . GLY A 1 175 ? 25.61693  6.31712   24.61647 1.000 10.82437 ? 175 GLY A CA  1 
ATOM   1518 C C   . GLY A 1 175 ? 26.62422  7.29885   24.04587 1.000 9.66875  ? 175 GLY A C   1 
ATOM   1519 O O   . GLY A 1 175 ? 27.77390  7.35651   24.48765 1.000 11.19548 ? 175 GLY A O   1 
ATOM   1520 N N   . TYR A 1 176 ? 26.19826  8.10244   23.07205 1.000 10.16252 ? 176 TYR A N   1 
ATOM   1521 C CA  . TYR A 1 176 ? 27.09652  9.07674   22.46407 1.000 11.76940 ? 176 TYR A CA  1 
ATOM   1522 C C   . TYR A 1 176 ? 27.58847  10.09225  23.48816 1.000 12.41798 ? 176 TYR A C   1 
ATOM   1523 O O   . TYR A 1 176 ? 28.75431  10.50307  23.45473 1.000 12.92060 ? 176 TYR A O   1 
ATOM   1524 C CB  . TYR A 1 176 ? 26.35884  9.78518   21.33007 1.000 11.29881 ? 176 TYR A CB  1 
ATOM   1525 C CG  . TYR A 1 176 ? 27.17123  10.79552  20.55474 1.000 11.18333 ? 176 TYR A CG  1 
ATOM   1526 C CD1 . TYR A 1 176 ? 27.34644  12.09303  21.02752 1.000 11.62870 ? 176 TYR A CD1 1 
ATOM   1527 C CD2 . TYR A 1 176 ? 27.72705  10.46477  19.32798 1.000 11.11783 ? 176 TYR A CD2 1 
ATOM   1528 C CE1 . TYR A 1 176 ? 28.06806  13.02712  20.30709 1.000 12.14080 ? 176 TYR A CE1 1 
ATOM   1529 C CE2 . TYR A 1 176 ? 28.44758  11.38991  18.59764 1.000 11.39100 ? 176 TYR A CE2 1 
ATOM   1530 C CZ  . TYR A 1 176 ? 28.61859  12.66775  19.09358 1.000 12.29912 ? 176 TYR A CZ  1 
ATOM   1531 O OH  . TYR A 1 176 ? 29.33009  13.59109  18.37118 1.000 13.65620 ? 176 TYR A OH  1 
ATOM   1532 N N   A ILE A 1 177 ? 26.72617  10.52122  24.41718 0.500 12.96871 ? 177 ILE A N   1 
ATOM   1533 N N   B ILE A 1 177 ? 26.69818  10.49503  24.39799 0.500 13.06163 ? 177 ILE A N   1 
ATOM   1534 C CA  A ILE A 1 177 ? 27.13962  11.54344  25.38106 0.500 14.78778 ? 177 ILE A CA  1 
ATOM   1535 C CA  B ILE A 1 177 ? 26.97188  11.51095  25.40508 0.500 14.46978 ? 177 ILE A CA  1 
ATOM   1536 C C   A ILE A 1 177 ? 27.67002  10.96528  26.68690 0.500 15.74625 ? 177 ILE A C   1 
ATOM   1537 C C   B ILE A 1 177 ? 27.78592  10.94347  26.55989 0.500 15.49890 ? 177 ILE A C   1 
ATOM   1538 O O   A ILE A 1 177 ? 28.11271  11.73099  27.55544 0.500 16.42866 ? 177 ILE A O   1 
ATOM   1539 O O   B ILE A 1 177 ? 28.58042  11.66736  27.17341 0.500 15.51019 ? 177 ILE A O   1 
ATOM   1540 C CB  A ILE A 1 177 ? 26.06009  12.60915  25.65815 0.500 15.22088 ? 177 ILE A CB  1 
ATOM   1541 C CB  B ILE A 1 177 ? 25.63087  12.10332  25.87850 0.500 14.76388 ? 177 ILE A CB  1 
ATOM   1542 C CG1 A ILE A 1 177 ? 24.88961  11.99766  26.42539 0.500 14.67106 ? 177 ILE A CG1 1 
ATOM   1543 C CG1 B ILE A 1 177 ? 24.97575  12.90580  24.75350 0.500 12.27183 ? 177 ILE A CG1 1 
ATOM   1544 C CG2 A ILE A 1 177 ? 25.60182  13.25368  24.36223 0.500 15.60734 ? 177 ILE A CG2 1 
ATOM   1545 C CG2 B ILE A 1 177 ? 25.80247  12.97020  27.11436 0.500 15.75379 ? 177 ILE A CG2 1 
ATOM   1546 C CD1 A ILE A 1 177 ? 24.03737  13.03003  27.10546 0.500 15.68465 ? 177 ILE A CD1 1 
ATOM   1547 C CD1 B ILE A 1 177 ? 25.81994  14.05432  24.27364 0.500 11.65994 ? 177 ILE A CD1 1 
ATOM   1548 N N   . ALA A 1 178 ? 27.62488  9.64850   26.86254 1.000 15.82867 ? 178 ALA A N   1 
ATOM   1549 C CA  . ALA A 1 178 ? 28.24716  9.02801   28.03409 1.000 15.61261 ? 178 ALA A CA  1 
ATOM   1550 C C   . ALA A 1 178 ? 29.70346  9.42700   28.26451 1.000 16.67589 ? 178 ALA A C   1 
ATOM   1551 O O   . ALA A 1 178 ? 30.06130  9.69738   29.41945 1.000 17.71532 ? 178 ALA A O   1 
ATOM   1552 C CB  . ALA A 1 178 ? 28.10085  7.49950   27.98846 1.000 16.72565 ? 178 ALA A CB  1 
ATOM   1553 N N   . PRO A 1 179 ? 30.55975  9.51463   27.23696 1.000 15.67612 ? 179 PRO A N   1 
ATOM   1554 C CA  . PRO A 1 179 ? 31.96026  9.89107   27.49086 1.000 16.84232 ? 179 PRO A CA  1 
ATOM   1555 C C   . PRO A 1 179 ? 32.15481  11.28665  28.06757 1.000 18.17412 ? 179 PRO A C   1 
ATOM   1556 O O   . PRO A 1 179 ? 33.19388  11.53498  28.69230 1.000 19.52979 ? 179 PRO A O   1 
ATOM   1557 C CB  . PRO A 1 179 ? 32.62086  9.74194   26.11324 1.000 18.34503 ? 179 PRO A CB  1 
ATOM   1558 C CG  . PRO A 1 179 ? 31.79531  8.70465   25.43075 1.000 19.66374 ? 179 PRO A CG  1 
ATOM   1559 C CD  . PRO A 1 179 ? 30.39033  9.00720   25.86009 1.000 17.19552 ? 179 PRO A CD  1 
ATOM   1560 N N   . VAL A 1 180 ? 31.20331  12.20835  27.88484 1.000 18.88747 ? 180 VAL A N   1 
ATOM   1561 C CA  . VAL A 1 180 ? 31.33686  13.53714  28.48393 1.000 21.01728 ? 180 VAL A CA  1 
ATOM   1562 C C   . VAL A 1 180 ? 30.65817  13.64292  29.84284 1.000 23.72971 ? 180 VAL A C   1 
ATOM   1563 O O   . VAL A 1 180 ? 30.87594  14.63331  30.55630 1.000 24.80360 ? 180 VAL A O   1 
ATOM   1564 C CB  . VAL A 1 180 ? 30.92564  14.68000  27.53083 1.000 21.35874 ? 180 VAL A CB  1 
ATOM   1565 C CG1 . VAL A 1 180 ? 31.61669  14.52190  26.18338 1.000 22.66376 ? 180 VAL A CG1 1 
ATOM   1566 C CG2 . VAL A 1 180 ? 29.41779  14.73025  27.36283 1.000 20.67256 ? 180 VAL A CG2 1 
ATOM   1567 N N   . VAL A 1 181 ? 29.84836  12.65566  30.22667 1.000 28.15691 ? 181 VAL A N   1 
ATOM   1568 C CA  . VAL A 1 181 ? 29.23034  12.66950  31.54757 1.000 33.00606 ? 181 VAL A CA  1 
ATOM   1569 C C   . VAL A 1 181 ? 30.18639  12.12466  32.60501 1.000 31.83981 ? 181 VAL A C   1 
ATOM   1570 O O   . VAL A 1 181 ? 30.16268  12.56976  33.75816 1.000 32.80582 ? 181 VAL A O   1 
ATOM   1571 C CB  . VAL A 1 181 ? 27.88634  11.91921  31.51323 1.000 38.60299 ? 181 VAL A CB  1 
ATOM   1572 C CG1 . VAL A 1 181 ? 27.32721  11.72885  32.91817 1.000 41.88769 ? 181 VAL A CG1 1 
ATOM   1573 C CG2 . VAL A 1 181 ? 26.89294  12.66837  30.64248 1.000 39.33149 ? 181 VAL A CG2 1 
ATOM   1574 N N   . GLY A 1 182 ? 31.04495  11.18142  32.23854 1.000 31.73906 ? 182 GLY A N   1 
ATOM   1575 C CA  . GLY A 1 182 ? 32.03063  10.67086  33.16112 1.000 32.36441 ? 182 GLY A CA  1 
ATOM   1576 C C   . GLY A 1 182 ? 33.16733  10.00159  32.42340 1.000 32.10692 ? 182 GLY A C   1 
ATOM   1577 O O   . GLY A 1 182 ? 33.28296  10.10080  31.19992 1.000 31.80871 ? 182 GLY A O   1 
ATOM   1578 N N   . ASP A 1 183 ? 34.01008  9.30819   33.19298 1.000 32.78793 ? 183 ASP A N   1 
ATOM   1579 C CA  . ASP A 1 183 ? 35.10247  8.51030   32.64058 1.000 34.40514 ? 183 ASP A CA  1 
ATOM   1580 C C   . ASP A 1 183 ? 34.52406  7.26309   31.98228 1.000 31.09252 ? 183 ASP A C   1 
ATOM   1581 O O   . ASP A 1 183 ? 34.82451  6.13640   32.39262 1.000 32.08417 ? 183 ASP A O   1 
ATOM   1582 C CB  . ASP A 1 183 ? 36.07092  8.11603   33.75962 1.000 38.61054 ? 183 ASP A CB  1 
ATOM   1583 C CG  . ASP A 1 183 ? 37.35628  7.50715   33.24063 1.000 44.22784 ? 183 ASP A CG  1 
ATOM   1584 O OD1 . ASP A 1 183 ? 37.58418  7.54066   32.01290 1.000 42.73785 ? 183 ASP A OD1 1 
ATOM   1585 O OD2 . ASP A 1 183 ? 38.13743  6.98965   34.06149 1.000 43.55237 ? 183 ASP A OD2 1 
ATOM   1586 N N   . PHE A 1 184 ? 33.70113  7.45075   30.95268 1.000 27.80486 ? 184 PHE A N   1 
ATOM   1587 C CA  . PHE A 1 184 ? 32.74612  6.43677   30.52019 1.000 28.17400 ? 184 PHE A CA  1 
ATOM   1588 C C   . PHE A 1 184 ? 32.90336  6.07041   29.05057 1.000 24.62066 ? 184 PHE A C   1 
ATOM   1589 O O   . PHE A 1 184 ? 31.90901  5.76525   28.39234 1.000 25.74942 ? 184 PHE A O   1 
ATOM   1590 C CB  . PHE A 1 184 ? 31.30527  6.89738   30.76171 1.000 30.84131 ? 184 PHE A CB  1 
ATOM   1591 C CG  . PHE A 1 184 ? 30.94651  7.10769   32.21092 1.000 35.49969 ? 184 PHE A CG  1 
ATOM   1592 C CD1 . PHE A 1 184 ? 31.69424  6.54023   33.23003 1.000 35.30684 ? 184 PHE A CD1 1 
ATOM   1593 C CD2 . PHE A 1 184 ? 29.83531  7.86860   32.54804 1.000 38.02403 ? 184 PHE A CD2 1 
ATOM   1594 C CE1 . PHE A 1 184 ? 31.35433  6.74326   34.55689 1.000 35.74269 ? 184 PHE A CE1 1 
ATOM   1595 C CE2 . PHE A 1 184 ? 29.48704  8.07255   33.87230 1.000 37.31410 ? 184 PHE A CE2 1 
ATOM   1596 C CZ  . PHE A 1 184 ? 30.24859  7.50869   34.87829 1.000 37.68334 ? 184 PHE A CZ  1 
ATOM   1597 N N   . ASP A 1 185 ? 34.12727  6.09101   28.51306 1.000 21.54498 ? 185 ASP A N   1 
ATOM   1598 C CA  . ASP A 1 185 ? 34.30478  5.72319   27.10819 1.000 19.88268 ? 185 ASP A CA  1 
ATOM   1599 C C   . ASP A 1 185 ? 33.73580  4.33567   26.82944 1.000 16.86499 ? 185 ASP A C   1 
ATOM   1600 O O   . ASP A 1 185 ? 32.98624  4.14047   25.86558 1.000 17.78538 ? 185 ASP A O   1 
ATOM   1601 C CB  . ASP A 1 185 ? 35.78142  5.79138   26.70724 1.000 21.14489 ? 185 ASP A CB  1 
ATOM   1602 C CG  . ASP A 1 185 ? 36.19710  7.16946   26.21584 1.000 25.06286 ? 185 ASP A CG  1 
ATOM   1603 O OD1 . ASP A 1 185 ? 35.50953  8.16156   26.53950 1.000 23.65977 ? 185 ASP A OD1 1 
ATOM   1604 O OD2 . ASP A 1 185 ? 37.21474  7.26051   25.49508 1.000 25.63773 ? 185 ASP A OD2 1 
ATOM   1605 N N   . ALA A 1 186 ? 34.06601  3.35969   27.68079 1.000 14.74985 ? 186 ALA A N   1 
ATOM   1606 C CA  . ALA A 1 186 ? 33.55835  2.00537   27.48060 1.000 13.51212 ? 186 ALA A CA  1 
ATOM   1607 C C   . ALA A 1 186 ? 32.04463  1.92981   27.65051 1.000 13.31901 ? 186 ALA A C   1 
ATOM   1608 O O   . ALA A 1 186 ? 31.39508  1.08878   27.01827 1.000 14.79966 ? 186 ALA A O   1 
ATOM   1609 C CB  . ALA A 1 186 ? 34.24818  1.03063   28.43408 1.000 14.22612 ? 186 ALA A CB  1 
ATOM   1610 N N   . ILE A 1 187 ? 31.46897  2.79001   28.49568 1.000 12.91860 ? 187 ILE A N   1 
ATOM   1611 C CA  . ILE A 1 187 ? 30.02256  2.78474   28.70636 1.000 12.90130 ? 187 ILE A CA  1 
ATOM   1612 C C   . ILE A 1 187 ? 29.27950  3.14452   27.42590 1.000 12.15860 ? 187 ILE A C   1 
ATOM   1613 O O   . ILE A 1 187 ? 28.18919  2.61834   27.16008 1.000 12.60702 ? 187 ILE A O   1 
ATOM   1614 C CB  . ILE A 1 187 ? 29.64554  3.69677   29.89023 1.000 14.77772 ? 187 ILE A CB  1 
ATOM   1615 C CG1 . ILE A 1 187 ? 30.32426  3.20055   31.16553 1.000 17.67589 ? 187 ILE A CG1 1 
ATOM   1616 C CG2 . ILE A 1 187 ? 28.13927  3.74779   30.07739 1.000 15.22799 ? 187 ILE A CG2 1 
ATOM   1617 C CD1 . ILE A 1 187 ? 30.01200  1.74943   31.49013 1.000 18.55552 ? 187 ILE A CD1 1 
ATOM   1618 N N   . ARG A 1 188 ? 29.84637  4.04105   26.61355 1.000 12.03968 ? 188 ARG A N   1 
ATOM   1619 C CA  . ARG A 1 188 ? 29.28760  4.29188   25.28815 1.000 9.90230  ? 188 ARG A CA  1 
ATOM   1620 C C   . ARG A 1 188 ? 29.14735  2.99254   24.50397 1.000 9.17364  ? 188 ARG A C   1 
ATOM   1621 O O   . ARG A 1 188 ? 28.09331  2.71104   23.91971 1.000 10.15230 ? 188 ARG A O   1 
ATOM   1622 C CB  . ARG A 1 188 ? 30.17311  5.27789   24.52480 1.000 10.74345 ? 188 ARG A CB  1 
ATOM   1623 C CG  . ARG A 1 188 ? 29.83222  5.39333   23.04519 1.000 10.14970 ? 188 ARG A CG  1 
ATOM   1624 C CD  . ARG A 1 188 ? 30.68712  6.44478   22.35783 1.000 11.21218 ? 188 ARG A CD  1 
ATOM   1625 N NE  . ARG A 1 188 ? 32.10838  6.14859   22.47760 1.000 12.58509 ? 188 ARG A NE  1 
ATOM   1626 C CZ  . ARG A 1 188 ? 33.07075  7.04828   22.33816 1.000 13.35881 ? 188 ARG A CZ  1 
ATOM   1627 N NH1 . ARG A 1 188 ? 32.79771  8.31484   22.06580 1.000 12.91958 ? 188 ARG A NH1 1 
ATOM   1628 N NH2 . ARG A 1 188 ? 34.33657  6.67125   22.49294 1.000 14.56711 ? 188 ARG A NH2 1 
ATOM   1629 N N   . GLU A 1 189 ? 30.20212  2.17342   24.49804 1.000 8.11482  ? 189 GLU A N   1 
ATOM   1630 C CA  . GLU A 1 189 ? 30.15669  0.92851   23.73558 1.000 8.22386  ? 189 GLU A CA  1 
ATOM   1631 C C   . GLU A 1 189 ? 29.17398  -0.06398  24.34058 1.000 9.59317  ? 189 GLU A C   1 
ATOM   1632 O O   . GLU A 1 189 ? 28.51354  -0.81040  23.60992 1.000 10.95648 ? 189 GLU A O   1 
ATOM   1633 C CB  . GLU A 1 189 ? 31.55619  0.31636   23.62548 1.000 9.91215  ? 189 GLU A CB  1 
ATOM   1634 C CG  . GLU A 1 189 ? 32.66031  1.30334   23.24943 1.000 9.36601  ? 189 GLU A CG  1 
ATOM   1635 C CD  . GLU A 1 189 ? 32.32487  2.17278   22.03821 1.000 11.46591 ? 189 GLU A CD  1 
ATOM   1636 O OE1 . GLU A 1 189 ? 31.51448  1.76029   21.17586 1.000 13.40473 ? 189 GLU A OE1 1 
ATOM   1637 O OE2 . GLU A 1 189 ? 32.88498  3.28334   21.94997 1.000 13.64315 ? 189 GLU A OE2 1 
ATOM   1638 N N   . VAL A 1 190 ? 29.07571  -0.08983  25.67306 1.000 9.12631  ? 190 VAL A N   1 
ATOM   1639 C CA  . VAL A 1 190 ? 28.11175  -0.95099  26.34790 1.000 11.02227 ? 190 VAL A CA  1 
ATOM   1640 C C   . VAL A 1 190 ? 26.69711  -0.57782  25.92822 1.000 11.47949 ? 190 VAL A C   1 
ATOM   1641 O O   . VAL A 1 190 ? 25.89441  -1.43455  25.53292 1.000 11.29258 ? 190 VAL A O   1 
ATOM   1642 C CB  . VAL A 1 190 ? 28.30114  -0.85555  27.87456 1.000 11.67024 ? 190 VAL A CB  1 
ATOM   1643 C CG1 . VAL A 1 190 ? 27.10021  -1.44243  28.61501 1.000 12.48509 ? 190 VAL A CG1 1 
ATOM   1644 C CG2 . VAL A 1 190 ? 29.59284  -1.54386  28.29727 1.000 12.05021 ? 190 VAL A CG2 1 
ATOM   1645 N N   . LEU A 1 191 ? 26.37640  0.71608   25.99796 1.000 9.95453  ? 191 LEU A N   1 
ATOM   1646 C CA  . LEU A 1 191 ? 25.03366  1.17012   25.65785 1.000 9.16546  ? 191 LEU A CA  1 
ATOM   1647 C C   . LEU A 1 191 ? 24.70723  0.91561   24.18957 1.000 9.40265  ? 191 LEU A C   1 
ATOM   1648 O O   . LEU A 1 191 ? 23.59373  0.48346   23.87135 1.000 10.05897 ? 191 LEU A O   1 
ATOM   1649 C CB  . LEU A 1 191 ? 24.87049  2.64609   26.01868 1.000 10.40683 ? 191 LEU A CB  1 
ATOM   1650 C CG  . LEU A 1 191 ? 24.83663  2.96938   27.51200 1.000 12.40565 ? 191 LEU A CG  1 
ATOM   1651 C CD1 . LEU A 1 191 ? 24.86895  4.47307   27.71275 1.000 12.52422 ? 191 LEU A CD1 1 
ATOM   1652 C CD2 . LEU A 1 191 ? 23.59740  2.36518   28.16700 1.000 13.73177 ? 191 LEU A CD2 1 
ATOM   1653 N N   . TYR A 1 192 ? 25.66023  1.17361   23.28128 1.000 9.64189  ? 192 TYR A N   1 
ATOM   1654 C CA  . TYR A 1 192 ? 25.41676  0.91014   21.86132 1.000 9.35096  ? 192 TYR A CA  1 
ATOM   1655 C C   . TYR A 1 192 ? 25.12823  -0.56472  21.61762 1.000 8.24005  ? 192 TYR A C   1 
ATOM   1656 O O   . TYR A 1 192 ? 24.26780  -0.91141  20.79820 1.000 9.42605  ? 192 TYR A O   1 
ATOM   1657 C CB  . TYR A 1 192 ? 26.62641  1.30402   21.01176 1.000 9.41670  ? 192 TYR A CB  1 
ATOM   1658 C CG  . TYR A 1 192 ? 26.86916  2.78018   20.79121 1.000 8.92349  ? 192 TYR A CG  1 
ATOM   1659 C CD1 . TYR A 1 192 ? 25.93870  3.73740   21.17702 1.000 8.77279  ? 192 TYR A CD1 1 
ATOM   1660 C CD2 . TYR A 1 192 ? 28.04662  3.21250   20.19376 1.000 7.99517  ? 192 TYR A CD2 1 
ATOM   1661 C CE1 . TYR A 1 192 ? 26.17856  5.08351   20.97121 1.000 9.44114  ? 192 TYR A CE1 1 
ATOM   1662 C CE2 . TYR A 1 192 ? 28.29399  4.54361   19.98698 1.000 7.95780  ? 192 TYR A CE2 1 
ATOM   1663 C CZ  . TYR A 1 192 ? 27.35581  5.47837   20.37154 1.000 9.33877  ? 192 TYR A CZ  1 
ATOM   1664 O OH  . TYR A 1 192 ? 27.60889  6.81081   20.16247 1.000 10.68995 ? 192 TYR A OH  1 
ATOM   1665 N N   . THR A 1 193 ? 25.86331  -1.44626  22.29873 1.000 9.33647  ? 193 THR A N   1 
ATOM   1666 C CA  . THR A 1 193 ? 25.67468  -2.88181  22.11696 1.000 10.04582 ? 193 THR A CA  1 
ATOM   1667 C C   . THR A 1 193 ? 24.31684  -3.33154  22.64478 1.000 9.66399  ? 193 THR A C   1 
ATOM   1668 O O   . THR A 1 193 ? 23.59119  -4.07215  21.96912 1.000 9.78571  ? 193 THR A O   1 
ATOM   1669 C CB  . THR A 1 193 ? 26.80724  -3.62960  22.81442 1.000 11.02172 ? 193 THR A CB  1 
ATOM   1670 O OG1 . THR A 1 193 ? 28.03045  -3.38335  22.11038 1.000 12.80539 ? 193 THR A OG1 1 
ATOM   1671 C CG2 . THR A 1 193 ? 26.51722  -5.12298  22.85366 1.000 11.70936 ? 193 THR A CG2 1 
ATOM   1672 N N   . ILE A 1 194 ? 23.96093  -2.89797  23.85939 1.000 10.49737 ? 194 ILE A N   1 
ATOM   1673 C CA  . ILE A 1 194 ? 22.64767  -3.21586  24.41613 1.000 11.81022 ? 194 ILE A CA  1 
ATOM   1674 C C   . ILE A 1 194 ? 21.54562  -2.72163  23.48753 1.000 11.18934 ? 194 ILE A C   1 
ATOM   1675 O O   . ILE A 1 194 ? 20.58646  -3.44675  23.18961 1.000 12.22023 ? 194 ILE A O   1 
ATOM   1676 C CB  . ILE A 1 194 ? 22.50595  -2.63219  25.83499 1.000 12.43857 ? 194 ILE A CB  1 
ATOM   1677 C CG1 . ILE A 1 194 ? 23.47014  -3.32141  26.80097 1.000 14.25376 ? 194 ILE A CG1 1 
ATOM   1678 C CG2 . ILE A 1 194 ? 21.06927  -2.76167  26.33156 1.000 14.36779 ? 194 ILE A CG2 1 
ATOM   1679 C CD1 . ILE A 1 194 ? 23.59772  -2.61651  28.13299 1.000 17.27754 ? 194 ILE A CD1 1 
ATOM   1680 N N   . ALA A 1 195 ? 21.68139  -1.48411  22.99698 1.000 10.51276 ? 195 ALA A N   1 
ATOM   1681 C CA  . ALA A 1 195 ? 20.66323  -0.91521  22.11980 1.000 9.84011  ? 195 ALA A CA  1 
ATOM   1682 C C   . ALA A 1 195 ? 20.53151  -1.71122  20.82785 1.000 10.14812 ? 195 ALA A C   1 
ATOM   1683 O O   . ALA A 1 195 ? 19.41365  -1.97274  20.36412 1.000 9.34690  ? 195 ALA A O   1 
ATOM   1684 C CB  . ALA A 1 195 ? 20.98021  0.55028   21.82484 1.000 9.57961  ? 195 ALA A CB  1 
ATOM   1685 N N   . ASP A 1 196 ? 21.65851  -2.11918  20.23664 1.000 9.46627  ? 196 ASP A N   1 
ATOM   1686 C CA  . ASP A 1 196 ? 21.58477  -2.86435  18.98349 1.000 9.67656  ? 196 ASP A CA  1 
ATOM   1687 C C   . ASP A 1 196 ? 20.86397  -4.19044  19.17133 1.000 9.86844  ? 196 ASP A C   1 
ATOM   1688 O O   . ASP A 1 196 ? 20.05526  -4.58607  18.32581 1.000 10.07214 ? 196 ASP A O   1 
ATOM   1689 C CB  . ASP A 1 196 ? 22.97740  -3.09291  18.39761 1.000 11.05742 ? 196 ASP A CB  1 
ATOM   1690 C CG  . ASP A 1 196 ? 23.51179  -1.87505  17.66784 1.000 13.21073 ? 196 ASP A CG  1 
ATOM   1691 O OD1 . ASP A 1 196 ? 22.74933  -0.90350  17.47238 1.000 12.58762 ? 196 ASP A OD1 1 
ATOM   1692 O OD2 . ASP A 1 196 ? 24.69810  -1.89181  17.28353 1.000 14.29949 ? 196 ASP A OD2 1 
ATOM   1693 N N   . ILE A 1 197 ? 21.15052  -4.89761  20.26793 1.000 9.64864  ? 197 ILE A N   1 
ATOM   1694 C CA  . ILE A 1 197 ? 20.45690  -6.15479  20.53859 1.000 10.12448 ? 197 ILE A CA  1 
ATOM   1695 C C   . ILE A 1 197 ? 18.96216  -5.91131  20.70168 1.000 11.21963 ? 197 ILE A C   1 
ATOM   1696 O O   . ILE A 1 197 ? 18.13425  -6.56695  20.05715 1.000 12.01010 ? 197 ILE A O   1 
ATOM   1697 C CB  . ILE A 1 197 ? 21.06225  -6.85946  21.76500 1.000 11.30982 ? 197 ILE A CB  1 
ATOM   1698 C CG1 . ILE A 1 197 ? 22.43909  -7.42603  21.41606 1.000 12.07198 ? 197 ILE A CG1 1 
ATOM   1699 C CG2 . ILE A 1 197 ? 20.12517  -7.96172  22.26096 1.000 12.26316 ? 197 ILE A CG2 1 
ATOM   1700 C CD1 . ILE A 1 197 ? 22.40252  -8.50082  20.34127 1.000 14.20518 ? 197 ILE A CD1 1 
ATOM   1701 N N   . ILE A 1 198 ? 18.59790  -4.95580  21.56236 1.000 11.64072 ? 198 ILE A N   1 
ATOM   1702 C CA  . ILE A 1 198 ? 17.18849  -4.65430  21.80474 1.000 12.33809 ? 198 ILE A CA  1 
ATOM   1703 C C   . ILE A 1 198 ? 16.49813  -4.25276  20.50975 1.000 12.64549 ? 198 ILE A C   1 
ATOM   1704 O O   . ILE A 1 198 ? 15.40508  -4.73315  20.19178 1.000 11.80830 ? 198 ILE A O   1 
ATOM   1705 C CB  . ILE A 1 198 ? 17.04616  -3.56310  22.88262 1.000 13.16819 ? 198 ILE A CB  1 
ATOM   1706 C CG1 . ILE A 1 198 ? 17.50693  -4.08753  24.24331 1.000 14.06687 ? 198 ILE A CG1 1 
ATOM   1707 C CG2 . ILE A 1 198 ? 15.60707  -3.07045  22.96021 1.000 15.14308 ? 198 ILE A CG2 1 
ATOM   1708 C CD1 . ILE A 1 198 ? 17.50289  -3.03454  25.33832 1.000 15.39334 ? 198 ILE A CD1 1 
ATOM   1709 N N   . ASN A 1 199 ? 17.12759  -3.37257  19.74129 1.000 11.90749 ? 199 ASN A N   1 
ATOM   1710 C CA  . ASN A 1 199 ? 16.45554  -2.77514  18.59441 1.000 11.06864 ? 199 ASN A CA  1 
ATOM   1711 C C   . ASN A 1 199 ? 16.41129  -3.67918  17.37088 1.000 12.95321 ? 199 ASN A C   1 
ATOM   1712 O O   . ASN A 1 199 ? 15.42477  -3.68168  16.63936 1.000 14.82113 ? 199 ASN A O   1 
ATOM   1713 C CB  . ASN A 1 199 ? 17.07406  -1.41723  18.26948 1.000 9.53800  ? 199 ASN A CB  1 
ATOM   1714 C CG  . ASN A 1 199 ? 16.70243  -0.36753  19.30011 1.000 11.46166 ? 199 ASN A CG  1 
ATOM   1715 O OD1 . ASN A 1 199 ? 15.52374  -0.19341  19.61652 1.000 12.95627 ? 199 ASN A OD1 1 
ATOM   1716 N ND2 . ASN A 1 199 ? 17.70234  0.30716   19.85909 1.000 12.16130 ? 199 ASN A ND2 1 
ATOM   1717 N N   . LYS A 1 200 ? 17.46299  -4.46134  17.16265 1.000 11.81296 ? 200 LYS A N   1 
ATOM   1718 C CA  . LYS A 1 200 ? 17.51289  -5.34765  16.02499 1.000 11.71402 ? 200 LYS A CA  1 
ATOM   1719 C C   . LYS A 1 200 ? 16.74882  -6.65100  16.20783 1.000 11.76800 ? 200 LYS A C   1 
ATOM   1720 O O   . LYS A 1 200 ? 15.90540  -7.06347  15.40500 1.000 12.18324 ? 200 LYS A O   1 
ATOM   1721 C CB  . LYS A 1 200 ? 18.92905  -5.65856  15.53051 1.000 11.61407 ? 200 LYS A CB  1 
ATOM   1722 C CG  . LYS A 1 200 ? 19.52213  -4.40658  14.93759 1.000 12.20910 ? 200 LYS A CG  1 
ATOM   1723 C CD  . LYS A 1 200 ? 20.87290  -4.63533  14.29966 1.000 14.15154 ? 200 LYS A CD  1 
ATOM   1724 C CE  . LYS A 1 200 ? 21.21825  -3.46524  13.38140 1.000 13.26426 ? 200 LYS A CE  1 
ATOM   1725 N NZ  . LYS A 1 200 ? 21.64687  -2.28311  14.09959 1.000 11.66500 ? 200 LYS A NZ  1 
ATOM   1726 N N   . VAL A 1 201 ? 17.06570  -7.33728  17.30082 1.000 12.72183 ? 201 VAL A N   1 
ATOM   1727 C CA  . VAL A 1 201 ? 16.34249  -8.55322  17.63974 1.000 13.76617 ? 201 VAL A CA  1 
ATOM   1728 C C   . VAL A 1 201 ? 14.89381  -8.21764  17.97682 1.000 11.77220 ? 201 VAL A C   1 
ATOM   1729 O O   . VAL A 1 201 ? 13.97333  -8.88604  17.51431 1.000 12.75861 ? 201 VAL A O   1 
ATOM   1730 C CB  . VAL A 1 201 ? 17.01968  -9.34388  18.77131 1.000 14.83300 ? 201 VAL A CB  1 
ATOM   1731 C CG1 . VAL A 1 201 ? 16.23353  -10.61776 19.05120 1.000 15.85981 ? 201 VAL A CG1 1 
ATOM   1732 C CG2 . VAL A 1 201 ? 18.45748  -9.67274  18.40283 1.000 16.37415 ? 201 VAL A CG2 1 
ATOM   1733 N N   . GLY A 1 202 ? 14.70501  -7.16462  18.77395 1.000 11.77037 ? 202 GLY A N   1 
ATOM   1734 C CA  . GLY A 1 202 ? 13.35865  -6.76664  19.15927 1.000 13.75322 ? 202 GLY A CA  1 
ATOM   1735 C C   . GLY A 1 202 ? 12.48041  -6.39244  17.97952 1.000 12.46492 ? 202 GLY A C   1 
ATOM   1736 O O   . GLY A 1 202 ? 11.32212  -6.80870  17.89999 1.000 12.87169 ? 202 GLY A O   1 
ATOM   1737 N N   . LEU A 1 203 ? 13.00313  -5.57473  17.05793 1.000 11.09361 ? 203 LEU A N   1 
ATOM   1738 C CA  . LEU A 1 203 ? 12.18913  -5.21070  15.90055 1.000 10.61271 ? 203 LEU A CA  1 
ATOM   1739 C C   . LEU A 1 203 ? 11.85651  -6.43508  15.06283 1.000 10.85568 ? 203 LEU A C   1 
ATOM   1740 O O   . LEU A 1 203 ? 10.71897  -6.58752  14.60446 1.000 12.41479 ? 203 LEU A O   1 
ATOM   1741 C CB  . LEU A 1 203 ? 12.85961  -4.13157  15.04857 1.000 11.00215 ? 203 LEU A CB  1 
ATOM   1742 C CG  . LEU A 1 203 ? 12.04039  -3.65738  13.83976 1.000 12.64428 ? 203 LEU A CG  1 
ATOM   1743 C CD1 . LEU A 1 203 ? 10.64404  -3.15914  14.24504 1.000 12.49183 ? 203 LEU A CD1 1 
ATOM   1744 C CD2 . LEU A 1 203 ? 12.78525  -2.58862  13.04781 1.000 14.53602 ? 203 LEU A CD2 1 
ATOM   1745 N N   . GLY A 1 204 ? 12.83601  -7.32042  14.85726 1.000 11.69007 ? 204 GLY A N   1 
ATOM   1746 C CA  . GLY A 1 204 ? 12.56358  -8.55627  14.14157 1.000 12.44580 ? 204 GLY A CA  1 
ATOM   1747 C C   . GLY A 1 204 ? 11.44365  -9.36242  14.77200 1.000 11.83780 ? 204 GLY A C   1 
ATOM   1748 O O   . GLY A 1 204 ? 10.55539  -9.85922  14.07503 1.000 13.24953 ? 204 GLY A O   1 
ATOM   1749 N N   . VAL A 1 205 ? 11.46385  -9.49233  16.10146 1.000 11.25630 ? 205 VAL A N   1 
ATOM   1750 C CA  . VAL A 1 205 ? 10.39573  -10.20165 16.80503 1.000 12.18556 ? 205 VAL A CA  1 
ATOM   1751 C C   . VAL A 1 205 ? 9.05090   -9.52755  16.56526 1.000 11.32511 ? 205 VAL A C   1 
ATOM   1752 O O   . VAL A 1 205 ? 8.04217   -10.19494 16.30257 1.000 11.80128 ? 205 VAL A O   1 
ATOM   1753 C CB  . VAL A 1 205 ? 10.72446  -10.31009 18.30624 1.000 13.98665 ? 205 VAL A CB  1 
ATOM   1754 C CG1 . VAL A 1 205 ? 9.50109   -10.76714 19.08794 1.000 16.72484 ? 205 VAL A CG1 1 
ATOM   1755 C CG2 . VAL A 1 205 ? 11.89345  -11.25782 18.52790 1.000 12.79938 ? 205 VAL A CG2 1 
ATOM   1756 N N   . LEU A 1 206 ? 9.01180   -8.19513  16.65108 1.000 11.85405 ? 206 LEU A N   1 
ATOM   1757 C CA  . LEU A 1 206 ? 7.75079   -7.48443  16.47191 1.000 13.24672 ? 206 LEU A CA  1 
ATOM   1758 C C   . LEU A 1 206 ? 7.29126   -7.49396  15.01962 1.000 12.52089 ? 206 LEU A C   1 
ATOM   1759 O O   . LEU A 1 206 ? 6.08353   -7.48444  14.75685 1.000 13.73248 ? 206 LEU A O   1 
ATOM   1760 C CB  . LEU A 1 206 ? 7.87250   -6.05810  16.99827 1.000 13.30776 ? 206 LEU A CB  1 
ATOM   1761 C CG  . LEU A 1 206 ? 8.04027   -5.95767  18.51394 1.000 12.88464 ? 206 LEU A CG  1 
ATOM   1762 C CD1 . LEU A 1 206 ? 8.16625   -4.50754  18.92129 1.000 13.90151 ? 206 LEU A CD1 1 
ATOM   1763 C CD2 . LEU A 1 206 ? 6.86184   -6.60564  19.21458 1.000 14.81993 ? 206 LEU A CD2 1 
ATOM   1764 N N   . VAL A 1 207 ? 8.22890   -7.49996  14.06862 1.000 12.38177 ? 207 VAL A N   1 
ATOM   1765 C CA  . VAL A 1 207 ? 7.85377   -7.67656  12.66823 1.000 12.58572 ? 207 VAL A CA  1 
ATOM   1766 C C   . VAL A 1 207 ? 7.27910   -9.06831  12.44822 1.000 13.50414 ? 207 VAL A C   1 
ATOM   1767 O O   . VAL A 1 207 ? 6.27746   -9.23923  11.74042 1.000 14.40120 ? 207 VAL A O   1 
ATOM   1768 C CB  . VAL A 1 207 ? 9.03976   -7.37062  11.73403 1.000 12.58710 ? 207 VAL A CB  1 
ATOM   1769 C CG1 . VAL A 1 207 ? 8.74478   -7.85152  10.30969 1.000 11.68034 ? 207 VAL A CG1 1 
ATOM   1770 C CG2 . VAL A 1 207 ? 9.33744   -5.87989  11.73968 1.000 12.12348 ? 207 VAL A CG2 1 
ATOM   1771 N N   . LEU A 1 208 ? 7.88839   -10.08178 13.06670 1.000 14.09418 ? 208 LEU A N   1 
ATOM   1772 C CA  . LEU A 1 208 ? 7.29999   -11.41630 13.04813 1.000 13.69819 ? 208 LEU A CA  1 
ATOM   1773 C C   . LEU A 1 208 ? 5.89812   -11.40734 13.65057 1.000 14.64403 ? 208 LEU A C   1 
ATOM   1774 O O   . LEU A 1 208 ? 4.97278   -12.00145 13.09048 1.000 14.27684 ? 208 LEU A O   1 
ATOM   1775 C CB  . LEU A 1 208 ? 8.21437   -12.40257 13.77598 1.000 13.12394 ? 208 LEU A CB  1 
ATOM   1776 C CG  . LEU A 1 208 ? 7.63761   -13.79528 14.02019 1.000 14.15267 ? 208 LEU A CG  1 
ATOM   1777 C CD1 . LEU A 1 208 ? 7.39390   -14.53726 12.71071 1.000 15.22296 ? 208 LEU A CD1 1 
ATOM   1778 C CD2 . LEU A 1 208 ? 8.57390   -14.58074 14.91941 1.000 15.39158 ? 208 LEU A CD2 1 
ATOM   1779 N N   A GLN A 1 209 ? 5.71360   -10.71304 14.77972 0.500 14.14673 ? 209 GLN A N   1 
ATOM   1780 N N   B GLN A 1 209 ? 5.72751   -10.74461 14.79716 0.500 14.60861 ? 209 GLN A N   1 
ATOM   1781 C CA  A GLN A 1 209 ? 4.37817   -10.60237 15.36350 0.500 15.01618 ? 209 GLN A CA  1 
ATOM   1782 C CA  B GLN A 1 209 ? 4.40865   -10.67373 15.41884 0.500 16.03928 ? 209 GLN A CA  1 
ATOM   1783 C C   A GLN A 1 209 ? 3.42071   -9.85525  14.44209 0.500 15.29379 ? 209 GLN A C   1 
ATOM   1784 C C   B GLN A 1 209 ? 3.39003   -10.06030 14.46704 0.500 14.66342 ? 209 GLN A C   1 
ATOM   1785 O O   A GLN A 1 209 ? 2.22339   -10.16128 14.41098 0.500 16.01840 ? 209 GLN A O   1 
ATOM   1786 O O   B GLN A 1 209 ? 2.28161   -10.58414 14.30259 0.500 14.25437 ? 209 GLN A O   1 
ATOM   1787 C CB  A GLN A 1 209 ? 4.43761   -9.92418  16.73490 0.500 15.82468 ? 209 GLN A CB  1 
ATOM   1788 C CB  B GLN A 1 209 ? 4.48538   -9.87842  16.72214 0.500 19.17140 ? 209 GLN A CB  1 
ATOM   1789 C CG  A GLN A 1 209 ? 5.13756   -10.73861 17.81719 0.500 17.31506 ? 209 GLN A CG  1 
ATOM   1790 C CG  B GLN A 1 209 ? 5.23131   -10.58752 17.84187 0.500 22.46445 ? 209 GLN A CG  1 
ATOM   1791 C CD  A GLN A 1 209 ? 5.06007   -10.08752 19.19377 0.500 20.65677 ? 209 GLN A CD  1 
ATOM   1792 C CD  B GLN A 1 209 ? 4.38732   -11.64096 18.53247 0.500 25.50319 ? 209 GLN A CD  1 
ATOM   1793 O OE1 A GLN A 1 209 ? 4.28653   -9.15303  19.41321 0.500 20.48139 ? 209 GLN A OE1 1 
ATOM   1794 O OE1 B GLN A 1 209 ? 4.02071   -12.65309 17.93538 0.500 25.83771 ? 209 GLN A OE1 1 
ATOM   1795 N NE2 A GLN A 1 209 ? 5.86644   -10.58219 20.12716 0.500 20.48194 ? 209 GLN A NE2 1 
ATOM   1796 N NE2 B GLN A 1 209 ? 4.06790   -11.40199 19.79895 0.500 27.56930 ? 209 GLN A NE2 1 
ATOM   1797 N N   A MET A 1 210 ? 3.92328   -8.86975  13.69409 0.500 15.93362 ? 210 MET A N   1 
ATOM   1798 N N   B MET A 1 210 ? 3.76149   -8.95432  13.81520 0.500 15.07505 ? 210 MET A N   1 
ATOM   1799 C CA  A MET A 1 210 ? 3.08279   -8.17686  12.72245 0.500 16.88655 ? 210 MET A CA  1 
ATOM   1800 C CA  B MET A 1 210 ? 2.87240   -8.32761  12.84280 0.500 15.70782 ? 210 MET A CA  1 
ATOM   1801 C C   A MET A 1 210 ? 2.63554   -9.12671  11.61768 0.500 16.83825 ? 210 MET A C   1 
ATOM   1802 C C   B MET A 1 210 ? 2.53174   -9.28395  11.70653 0.500 16.30002 ? 210 MET A C   1 
ATOM   1803 O O   A MET A 1 210 ? 1.50063   -9.04491  11.13298 0.500 17.19130 ? 210 MET A O   1 
ATOM   1804 O O   B MET A 1 210 ? 1.37626   -9.34940  11.26887 0.500 16.71112 ? 210 MET A O   1 
ATOM   1805 C CB  A MET A 1 210 ? 3.84957   -6.99298  12.13145 0.500 17.95897 ? 210 MET A CB  1 
ATOM   1806 C CB  B MET A 1 210 ? 3.50170   -7.04222  12.30225 0.500 15.03792 ? 210 MET A CB  1 
ATOM   1807 C CG  A MET A 1 210 ? 3.00360   -6.06293  11.27882 0.500 19.94878 ? 210 MET A CG  1 
ATOM   1808 C CG  B MET A 1 210 ? 2.77959   -6.45976  11.09367 0.500 16.18258 ? 210 MET A CG  1 
ATOM   1809 S SD  A MET A 1 210 ? 2.21502   -4.77952  12.26240 0.500 20.68706 ? 210 MET A SD  1 
ATOM   1810 S SD  B MET A 1 210 ? 1.13294   -5.82363  11.46584 0.500 15.75229 ? 210 MET A SD  1 
ATOM   1811 C CE  A MET A 1 210 ? 0.65549   -4.60271  11.40136 0.500 20.97394 ? 210 MET A CE  1 
ATOM   1812 C CE  B MET A 1 210 ? 1.53137   -4.19499  12.08832 0.500 16.71211 ? 210 MET A CE  1 
ATOM   1813 N N   . ALA A 1 211 ? 3.52051   -10.04229 11.21869 1.000 16.11456 ? 211 ALA A N   1 
ATOM   1814 C CA  . ALA A 1 211 ? 3.22813   -11.00418 10.16305 1.000 18.38938 ? 211 ALA A CA  1 
ATOM   1815 C C   . ALA A 1 211 ? 2.23539   -12.06152 10.62682 1.000 18.73378 ? 211 ALA A C   1 
ATOM   1816 O O   . ALA A 1 211 ? 1.40936   -12.52325 9.83039  1.000 20.73688 ? 211 ALA A O   1 
ATOM   1817 C CB  . ALA A 1 211 ? 4.52209   -11.65331 9.67588  1.000 20.10548 ? 211 ALA A CB  1 
ATOM   1818 N N   A ARG A 1 212 ? 2.29945   -12.45909 11.90096 0.500 19.62657 ? 212 ARG A N   1 
ATOM   1819 N N   B ARG A 1 212 ? 2.29787   -12.46147 11.90044 0.500 19.66246 ? 212 ARG A N   1 
ATOM   1820 C CA  A ARG A 1 212 ? 1.30006   -13.37773 12.43936 0.500 20.46953 ? 212 ARG A CA  1 
ATOM   1821 C CA  B ARG A 1 212 ? 1.28427   -13.37145 12.42566 0.500 20.68967 ? 212 ARG A CA  1 
ATOM   1822 C C   A ARG A 1 212 ? -0.08855  -12.75278 12.40088 0.500 20.80266 ? 212 ARG A C   1 
ATOM   1823 C C   B ARG A 1 212 ? -0.09292  -12.72075 12.40165 0.500 20.91499 ? 212 ARG A C   1 
ATOM   1824 O O   A ARG A 1 212 ? -1.06348  -13.40079 12.00374 0.500 20.71152 ? 212 ARG A O   1 
ATOM   1825 O O   B ARG A 1 212 ? -1.08348  -13.35844 12.02602 0.500 20.74184 ? 212 ARG A O   1 
ATOM   1826 C CB  A ARG A 1 212 ? 1.65876   -13.76992 13.87243 0.500 22.00089 ? 212 ARG A CB  1 
ATOM   1827 C CB  B ARG A 1 212 ? 1.64031   -13.80817 13.84679 0.500 22.81326 ? 212 ARG A CB  1 
ATOM   1828 C CG  A ARG A 1 212 ? 2.94125   -14.56771 14.02316 0.500 23.57814 ? 212 ARG A CG  1 
ATOM   1829 C CG  B ARG A 1 212 ? 3.07029   -14.28916 14.02288 0.500 25.60521 ? 212 ARG A CG  1 
ATOM   1830 C CD  A ARG A 1 212 ? 3.15902   -14.93501 15.48244 0.500 25.13299 ? 212 ARG A CD  1 
ATOM   1831 C CD  B ARG A 1 212 ? 3.29172   -14.81854 15.42858 0.500 28.41130 ? 212 ARG A CD  1 
ATOM   1832 N NE  A ARG A 1 212 ? 4.37486   -15.71204 15.68698 0.500 28.58130 ? 212 ARG A NE  1 
ATOM   1833 N NE  B ARG A 1 212 ? 3.00536   -16.24441 15.51709 0.500 32.40988 ? 212 ARG A NE  1 
ATOM   1834 C CZ  A ARG A 1 212 ? 4.44184   -17.03301 15.59414 0.500 32.07438 ? 212 ARG A CZ  1 
ATOM   1835 C CZ  B ARG A 1 212 ? 3.92986   -17.18517 15.65205 0.500 34.42204 ? 212 ARG A CZ  1 
ATOM   1836 N NH1 A ARG A 1 212 ? 3.38109   -17.75791 15.27840 0.500 31.30669 ? 212 ARG A NH1 1 
ATOM   1837 N NH1 B ARG A 1 212 ? 5.21323   -16.88215 15.76499 0.500 34.73755 ? 212 ARG A NH1 1 
ATOM   1838 N NH2 A ARG A 1 212 ? 5.60177   -17.64189 15.82503 0.500 36.11809 ? 212 ARG A NH2 1 
ATOM   1839 N NH2 B ARG A 1 212 ? 3.55725   -18.46147 15.68075 0.500 36.13368 ? 212 ARG A NH2 1 
ATOM   1840 N N   A VAL A 1 213 ? -0.19565  -11.48872 12.81927 0.500 20.98887 ? 213 VAL A N   1 
ATOM   1841 N N   B VAL A 1 213 ? -0.17267  -11.44681 12.79676 0.500 21.13984 ? 213 VAL A N   1 
ATOM   1842 C CA  A VAL A 1 213 ? -1.48095  -10.79280 12.79125 0.500 21.55680 ? 213 VAL A CA  1 
ATOM   1843 C CA  B VAL A 1 213 ? -1.43930  -10.72088 12.73431 0.500 21.89058 ? 213 VAL A CA  1 
ATOM   1844 C C   A VAL A 1 213 ? -2.00631  -10.70038 11.36386 0.500 22.29752 ? 213 VAL A C   1 
ATOM   1845 C C   B VAL A 1 213 ? -1.89800  -10.56432 11.28927 0.500 22.71887 ? 213 VAL A C   1 
ATOM   1846 O O   A VAL A 1 213 ? -3.17740  -10.99414 11.09163 0.500 23.05768 ? 213 VAL A O   1 
ATOM   1847 O O   B VAL A 1 213 ? -3.07784  -10.76401 10.96933 0.500 22.95456 ? 213 VAL A O   1 
ATOM   1848 C CB  A VAL A 1 213 ? -1.35385  -9.40478  13.44490 0.500 21.74805 ? 213 VAL A CB  1 
ATOM   1849 C CB  B VAL A 1 213 ? -1.31767  -9.36535  13.45670 0.500 21.91671 ? 213 VAL A CB  1 
ATOM   1850 C CG1 A VAL A 1 213 ? -2.61190  -8.58535  13.20486 0.500 22.65628 ? 213 VAL A CG1 1 
ATOM   1851 C CG1 B VAL A 1 213 ? -2.56156  -8.52404  13.22898 0.500 22.65287 ? 213 VAL A CG1 1 
ATOM   1852 C CG2 A VAL A 1 213 ? -1.07039  -9.54175  14.93550 0.500 22.52336 ? 213 VAL A CG2 1 
ATOM   1853 C CG2 B VAL A 1 213 ? -1.06954  -9.57556  14.94632 0.500 22.69666 ? 213 VAL A CG2 1 
ATOM   1854 N N   A GLN A 1 214 ? -1.14481  -10.28468 10.43106 0.500 22.85606 ? 214 GLN A N   1 
ATOM   1855 N N   B GLN A 1 214 ? -0.97554  -10.19824 10.39475 0.500 23.65447 ? 214 GLN A N   1 
ATOM   1856 C CA  A GLN A 1 214 ? -1.54822  -10.20090 9.03165  0.500 24.72355 ? 214 GLN A CA  1 
ATOM   1857 C CA  B GLN A 1 214 ? -1.30807  -10.09673 8.97821  0.500 25.58130 ? 214 GLN A CA  1 
ATOM   1858 C C   A GLN A 1 214 ? -1.92453  -11.56807 8.47731  0.500 25.55954 ? 214 GLN A C   1 
ATOM   1859 C C   B GLN A 1 214 ? -1.73878  -11.43507 8.39079  0.500 26.17354 ? 214 GLN A C   1 
ATOM   1860 O O   A GLN A 1 214 ? -2.79949  -11.66728 7.60859  0.500 25.40751 ? 214 GLN A O   1 
ATOM   1861 O O   B GLN A 1 214 ? -2.47302  -11.45407 7.39709  0.500 25.96542 ? 214 GLN A O   1 
ATOM   1862 C CB  A GLN A 1 214 ? -0.43302  -9.56066  8.20446  0.500 26.40270 ? 214 GLN A CB  1 
ATOM   1863 C CB  B GLN A 1 214 ? -0.12648  -9.51494  8.19489  0.500 27.65149 ? 214 GLN A CB  1 
ATOM   1864 C CG  A GLN A 1 214 ? -0.16370  -8.10199  8.55524  0.500 27.59372 ? 214 GLN A CG  1 
ATOM   1865 C CG  B GLN A 1 214 ? 0.06226   -8.00658  8.37096  0.500 28.23304 ? 214 GLN A CG  1 
ATOM   1866 C CD  A GLN A 1 214 ? 1.20937   -7.63610  8.10844  0.500 29.12524 ? 214 GLN A CD  1 
ATOM   1867 C CD  B GLN A 1 214 ? 1.38186   -7.50490  7.80430  0.500 29.25298 ? 214 GLN A CD  1 
ATOM   1868 O OE1 A GLN A 1 214 ? 2.13270   -8.43774  7.96613  0.500 30.88624 ? 214 GLN A OE1 1 
ATOM   1869 O OE1 B GLN A 1 214 ? 2.43550   -8.10449  8.02605  0.500 29.95820 ? 214 GLN A OE1 1 
ATOM   1870 N NE2 A GLN A 1 214 ? 1.35077   -6.33410  7.88409  0.500 30.12918 ? 214 GLN A NE2 1 
ATOM   1871 N NE2 B GLN A 1 214 ? 1.32976   -6.39759  7.07181  0.500 29.87253 ? 214 GLN A NE2 1 
ATOM   1872 N N   A SER A 1 215 ? -1.28847  -12.63124 8.97273  0.500 26.89267 ? 215 SER A N   1 
ATOM   1873 N N   B SER A 1 215 ? -1.31726  -12.54880 8.98931  0.500 27.40488 ? 215 SER A N   1 
ATOM   1874 C CA  A SER A 1 215 ? -1.67750  -13.98906 8.61326  0.500 26.98755 ? 215 SER A CA  1 
ATOM   1875 C CA  B SER A 1 215 ? -1.71112  -13.88013 8.54568  0.500 27.55433 ? 215 SER A CA  1 
ATOM   1876 C C   A SER A 1 215 ? -2.99253  -14.41304 9.25031  0.500 28.41258 ? 215 SER A C   1 
ATOM   1877 C C   B SER A 1 215 ? -3.00281  -14.36350 9.19225  0.500 28.57319 ? 215 SER A C   1 
ATOM   1878 O O   A SER A 1 215 ? -3.41727  -15.55413 9.03848  0.500 28.80089 ? 215 SER A O   1 
ATOM   1879 O O   B SER A 1 215 ? -3.41953  -15.49627 8.93508  0.500 28.69673 ? 215 SER A O   1 
ATOM   1880 C CB  A SER A 1 215 ? -0.57676  -14.97935 8.99919  0.500 26.05844 ? 215 SER A CB  1 
ATOM   1881 C CB  B SER A 1 215 ? -0.59144  -14.88990 8.82355  0.500 26.86983 ? 215 SER A CB  1 
ATOM   1882 O OG  A SER A 1 215 ? 0.63278   -14.69021 8.32089  0.500 25.56369 ? 215 SER A OG  1 
ATOM   1883 O OG  B SER A 1 215 ? 0.62027   -14.49226 8.20526  0.500 26.47866 ? 215 SER A OG  1 
ATOM   1884 N N   . GLY A 1 216 ? -3.64216  -13.53914 10.01780 1.000 29.76152 ? 216 GLY A N   1 
ATOM   1885 C CA  . GLY A 1 216 ? -4.88031  -13.90426 10.67217 1.000 33.76646 ? 216 GLY A CA  1 
ATOM   1886 C C   . GLY A 1 216 ? -4.71957  -14.66399 11.96830 1.000 40.14109 ? 216 GLY A C   1 
ATOM   1887 O O   . GLY A 1 216 ? -5.72336  -15.11600 12.53094 1.000 38.14805 ? 216 GLY A O   1 
ATOM   1888 N N   A GLU A 1 217 ? -3.49437  -14.82821 12.45794 0.500 45.24753 ? 217 GLU A N   1 
ATOM   1889 N N   B GLU A 1 217 ? -3.49452  -14.81848 12.46222 0.500 45.23720 ? 217 GLU A N   1 
ATOM   1890 C CA  A GLU A 1 217 ? -3.28373  -15.53254 13.71260 0.500 49.47427 ? 217 GLU A CA  1 
ATOM   1891 C CA  B GLU A 1 217 ? -3.26894  -15.53043 13.71083 0.500 49.46133 ? 217 GLU A CA  1 
ATOM   1892 C C   A GLU A 1 217 ? -3.71799  -14.66576 14.88734 0.500 46.68670 ? 217 GLU A C   1 
ATOM   1893 C C   B GLU A 1 217 ? -3.68805  -14.66732 14.89684 0.500 46.67731 ? 217 GLU A C   1 
ATOM   1894 O O   A GLU A 1 217 ? -3.64005  -13.43483 14.84619 0.500 45.95997 ? 217 GLU A O   1 
ATOM   1895 O O   B GLU A 1 217 ? -3.57774  -13.43845 14.87082 0.500 45.95089 ? 217 GLU A O   1 
ATOM   1896 C CB  A GLU A 1 217 ? -1.81140  -15.90693 13.87272 0.500 53.47155 ? 217 GLU A CB  1 
ATOM   1897 C CB  B GLU A 1 217 ? -1.79170  -15.90775 13.83527 0.500 53.46587 ? 217 GLU A CB  1 
ATOM   1898 C CG  A GLU A 1 217 ? -1.29996  -16.86842 12.81763 0.500 52.68578 ? 217 GLU A CG  1 
ATOM   1899 C CG  B GLU A 1 217 ? -1.44860  -16.75700 15.04818 0.500 52.68361 ? 217 GLU A CG  1 
ATOM   1900 C CD  A GLU A 1 217 ? 0.20319   -17.04912 12.87538 0.500 59.10588 ? 217 GLU A CD  1 
ATOM   1901 C CD  B GLU A 1 217 ? 0.01840   -17.13949 15.09496 0.500 58.98901 ? 217 GLU A CD  1 
ATOM   1902 O OE1 A GLU A 1 217 ? 0.74749   -17.20734 13.98871 0.500 61.15365 ? 217 GLU A OE1 1 
ATOM   1903 O OE1 B GLU A 1 217 ? 0.66607   -17.16018 14.02669 0.500 60.97361 ? 217 GLU A OE1 1 
ATOM   1904 O OE2 A GLU A 1 217 ? 0.84099   -17.01978 11.80376 0.500 61.61951 ? 217 GLU A OE2 1 
ATOM   1905 O OE2 B GLU A 1 217 ? 0.52590   -17.41567 16.20197 0.500 61.62532 ? 217 GLU A OE2 1 
ATOM   1906 N N   . LYS A 1 218 ? -4.18152  -15.32548 15.94265 1.000 46.74043 ? 218 LYS A N   1 
ATOM   1907 C CA  . LYS A 1 218 ? -4.62634  -14.63290 17.14577 1.000 49.52015 ? 218 LYS A CA  1 
ATOM   1908 C C   . LYS A 1 218 ? -3.44132  -14.24254 18.02266 1.000 52.21572 ? 218 LYS A C   1 
ATOM   1909 O O   . LYS A 1 218 ? -3.50089  -13.25857 18.76080 1.000 54.27614 ? 218 LYS A O   1 
ATOM   1910 C CB  . LYS A 1 218 ? -5.60054  -15.50790 17.93743 1.000 51.45002 ? 218 LYS A CB  1 
HETATM 1911 C C1  . OLA B 2 .   ? 16.21902  -15.14481 2.51407  1.000 42.79470 ? 501 OLA A C1  1 
HETATM 1912 O O1  . OLA B 2 .   ? 15.61842  -16.22625 2.32763  1.000 43.08437 ? 501 OLA A O1  1 
HETATM 1913 O O2  . OLA B 2 .   ? 16.45036  -14.40313 1.53602  1.000 43.00627 ? 501 OLA A O2  1 
HETATM 1914 C C2  . OLA B 2 .   ? 16.67149  -14.73786 3.89499  1.000 39.51976 ? 501 OLA A C2  1 
HETATM 1915 C C3  . OLA B 2 .   ? 17.27070  -13.33798 3.83358  1.000 35.20542 ? 501 OLA A C3  1 
HETATM 1916 C C4  . OLA B 2 .   ? 18.74866  -13.34713 4.20203  1.000 33.56583 ? 501 OLA A C4  1 
HETATM 1917 C C5  . OLA B 2 .   ? 19.00127  -14.22581 5.41979  1.000 33.19480 ? 501 OLA A C5  1 
HETATM 1918 C C6  . OLA B 2 .   ? 20.02944  -13.58417 6.33922  1.000 32.63048 ? 501 OLA A C6  1 
HETATM 1919 C C7  . OLA B 2 .   ? 21.40023  -14.21779 6.15420  1.000 32.33197 ? 501 OLA A C7  1 
HETATM 1920 C C8  . OLA B 2 .   ? 22.47676  -13.14420 6.18671  1.000 32.56644 ? 501 OLA A C8  1 
HETATM 1921 C C9  . OLA B 2 .   ? 23.60225  -13.59931 7.08130  1.000 32.46029 ? 501 OLA A C9  1 
HETATM 1922 C C10 . OLA B 2 .   ? 24.72676  -12.68727 7.31744  1.000 32.23476 ? 501 OLA A C10 1 
HETATM 1923 C C11 . OLA B 2 .   ? 25.45212  -12.07484 6.14472  1.000 32.20250 ? 501 OLA A C11 1 
HETATM 1924 C C12 . OLA B 2 .   ? 25.69478  -10.60485 6.44976  1.000 32.46419 ? 501 OLA A C12 1 
HETATM 1925 C C13 . OLA B 2 .   ? 27.02921  -10.12465 5.89588  1.000 33.85949 ? 501 OLA A C13 1 
HETATM 1926 C C14 . OLA B 2 .   ? 26.99055  -8.62088  5.65403  1.000 34.44696 ? 501 OLA A C14 1 
HETATM 1927 C C15 . OLA B 2 .   ? 28.38036  -8.07452  5.35219  1.000 34.64657 ? 501 OLA A C15 1 
HETATM 1928 C C16 . OLA B 2 .   ? 28.37314  -6.55072  5.31946  1.000 34.94100 ? 501 OLA A C16 1 
HETATM 1929 C C17 . OLA B 2 .   ? 29.52922  -6.02639  4.47674  1.000 36.08082 ? 501 OLA A C17 1 
HETATM 1930 C C18 . OLA B 2 .   ? 29.98235  -4.65049  4.95184  1.000 35.94264 ? 501 OLA A C18 1 
HETATM 1931 C C1  . OLA C 2 .   ? 3.19368   -6.98018  23.19253 1.000 33.21416 ? 502 OLA A C1  1 
HETATM 1932 C C2  . OLA C 2 .   ? 4.69170   -6.70464  23.26990 1.000 32.29205 ? 502 OLA A C2  1 
HETATM 1933 C C3  . OLA C 2 .   ? 5.04241   -5.44236  22.49036 1.000 30.55811 ? 502 OLA A C3  1 
HETATM 1934 C C4  . OLA C 2 .   ? 6.40040   -4.88378  22.89547 1.000 29.11163 ? 502 OLA A C4  1 
HETATM 1935 C C5  . OLA C 2 .   ? 6.43806   -3.36387  22.77703 1.000 28.41249 ? 502 OLA A C5  1 
HETATM 1936 C C6  . OLA C 2 .   ? 7.83059   -2.84223  23.11189 1.000 27.59375 ? 502 OLA A C6  1 
HETATM 1937 C C7  . OLA C 2 .   ? 7.75554   -1.37514  23.46115 1.000 26.93679 ? 502 OLA A C7  1 
HETATM 1938 C C8  . OLA C 2 .   ? 8.95671   -0.64500  23.89319 1.000 27.23859 ? 502 OLA A C8  1 
HETATM 1939 C C9  . OLA C 2 .   ? 10.13942  -1.39995  24.45021 1.000 27.98482 ? 502 OLA A C9  1 
HETATM 1940 C C10 . OLA C 2 .   ? 11.10123  -0.42242  25.11088 1.000 29.11510 ? 502 OLA A C10 1 
HETATM 1941 C C11 . OLA C 2 .   ? 12.43801  -1.08435  25.42664 1.000 31.01203 ? 502 OLA A C11 1 
HETATM 1942 C C12 . OLA C 2 .   ? 13.24640  -0.24779  26.41321 1.000 33.24560 ? 502 OLA A C12 1 
HETATM 1943 C C13 . OLA C 2 .   ? 14.59079  -0.89639  26.71680 1.000 34.01670 ? 502 OLA A C13 1 
HETATM 1944 C C14 . OLA C 2 .   ? 15.35416  -0.14405  27.80082 1.000 34.11765 ? 502 OLA A C14 1 
HETATM 1945 C C15 . OLA C 2 .   ? 16.70518  -0.80654  28.04747 1.000 33.46107 ? 502 OLA A C15 1 
HETATM 1946 C C16 . OLA C 2 .   ? 17.63802  0.06571   28.87954 1.000 33.28393 ? 502 OLA A C16 1 
HETATM 1947 C C1  . OLA D 2 .   ? 35.84197  3.90762   8.20743  1.000 44.56192 ? 503 OLA A C1  1 
HETATM 1948 O O1  . OLA D 2 .   ? 37.01728  4.26803   8.43583  1.000 44.82169 ? 503 OLA A O1  1 
HETATM 1949 O O2  . OLA D 2 .   ? 35.59808  2.68863   8.08056  1.000 45.04148 ? 503 OLA A O2  1 
HETATM 1950 C C2  . OLA D 2 .   ? 34.73098  4.92181   8.07240  1.000 41.62990 ? 503 OLA A C2  1 
HETATM 1951 C C3  . OLA D 2 .   ? 33.40190  4.18510   7.96212  1.000 37.96477 ? 503 OLA A C3  1 
HETATM 1952 C C4  . OLA D 2 .   ? 32.31310  4.86170   8.78716  1.000 36.09731 ? 503 OLA A C4  1 
HETATM 1953 C C5  . OLA D 2 .   ? 31.49642  5.82811   7.93842  1.000 35.13814 ? 503 OLA A C5  1 
HETATM 1954 C C6  . OLA D 2 .   ? 30.03749  5.39479   7.87756  1.000 34.37746 ? 503 OLA A C6  1 
HETATM 1955 C C7  . OLA D 2 .   ? 29.10143  6.57783   8.10119  1.000 33.22402 ? 503 OLA A C7  1 
HETATM 1956 C C8  . OLA D 2 .   ? 29.10270  7.51040   6.89684  1.000 32.52836 ? 503 OLA A C8  1 
HETATM 1957 C C9  . OLA D 2 .   ? 27.68279  7.84666   6.52288  1.000 31.59526 ? 503 OLA A C9  1 
HETATM 1958 C C10 . OLA D 2 .   ? 27.42319  8.67825   5.34305  1.000 31.70928 ? 503 OLA A C10 1 
HETATM 1959 C C11 . OLA D 2 .   ? 27.77487  10.14482  5.40742  1.000 32.20921 ? 503 OLA A C11 1 
HETATM 1960 C C12 . OLA D 2 .   ? 26.90683  10.92868  4.42765  1.000 32.87552 ? 503 OLA A C12 1 
HETATM 1961 C C13 . OLA D 2 .   ? 26.63402  12.36566  4.87667  1.000 33.69267 ? 503 OLA A C13 1 
HETATM 1962 C C14 . OLA D 2 .   ? 27.02608  12.63218  6.32663  1.000 34.30437 ? 503 OLA A C14 1 
HETATM 1963 C C15 . OLA D 2 .   ? 26.58565  14.02183  6.77627  1.000 34.57715 ? 503 OLA A C15 1 
HETATM 1964 C C16 . OLA D 2 .   ? 27.55896  14.58823  7.80647  1.000 34.09136 ? 503 OLA A C16 1 
HETATM 1965 C C17 . OLA D 2 .   ? 27.00476  15.84914  8.45977  1.000 33.56254 ? 503 OLA A C17 1 
HETATM 1966 C C18 . OLA D 2 .   ? 28.08789  16.57679  9.24922  1.000 32.27663 ? 503 OLA A C18 1 
HETATM 1967 C C10 . LFA E 3 .   ? 22.16168  18.79513  8.05411  1.000 35.28056 ? 504 LFA A C10 1 
HETATM 1968 C C11 . LFA E 3 .   ? 20.69080  19.13323  8.03722  1.000 33.84789 ? 504 LFA A C11 1 
HETATM 1969 C C12 . LFA E 3 .   ? 19.91719  18.60547  9.22042  1.000 33.34564 ? 504 LFA A C12 1 
HETATM 1970 C C13 . LFA E 3 .   ? 18.42992  18.82227  9.12089  1.000 33.38328 ? 504 LFA A C13 1 
HETATM 1971 C C14 . LFA E 3 .   ? 17.62255  18.15257  10.20323 1.000 32.42895 ? 504 LFA A C14 1 
HETATM 1972 C C15 . LFA E 3 .   ? 16.19248  17.90313  9.80659  1.000 31.97772 ? 504 LFA A C15 1 
HETATM 1973 C C16 . LFA E 3 .   ? 16.05451  17.05562  8.56651  1.000 30.59345 ? 504 LFA A C16 1 
HETATM 1974 C C17 . LFA E 3 .   ? 14.70606  17.14372  7.89969  1.000 29.98657 ? 504 LFA A C17 1 
HETATM 1975 C C6  . LFA F 3 .   ? 31.91859  23.94367  24.02747 1.000 38.67724 ? 505 LFA A C6  1 
HETATM 1976 C C7  . LFA F 3 .   ? 30.71520  23.44101  23.26432 1.000 39.54015 ? 505 LFA A C7  1 
HETATM 1977 C C8  . LFA F 3 .   ? 29.40708  24.06203  23.69242 1.000 38.21792 ? 505 LFA A C8  1 
HETATM 1978 C C9  . LFA F 3 .   ? 28.95428  23.68261  25.08317 1.000 37.77657 ? 505 LFA A C9  1 
HETATM 1979 C C10 . LFA F 3 .   ? 28.18426  22.38551  25.16222 1.000 36.64416 ? 505 LFA A C10 1 
HETATM 1980 C C11 . LFA F 3 .   ? 26.84431  22.42183  24.46382 1.000 36.16501 ? 505 LFA A C11 1 
HETATM 1981 C C12 . LFA F 3 .   ? 26.04377  21.14366  24.56595 1.000 36.66044 ? 505 LFA A C12 1 
HETATM 1982 C C13 . LFA F 3 .   ? 24.72143  21.18358  23.83575 1.000 35.32826 ? 505 LFA A C13 1 
HETATM 1983 C C14 . LFA F 3 .   ? 23.91896  19.90832  23.92010 1.000 35.28255 ? 505 LFA A C14 1 
HETATM 1984 C C1  . LFA G 3 .   ? 17.04845  -5.46777  28.77665 1.000 40.27252 ? 506 LFA A C1  1 
HETATM 1985 C C2  . LFA G 3 .   ? 15.70368  -5.99350  28.33211 1.000 39.53382 ? 506 LFA A C2  1 
HETATM 1986 C C3  . LFA G 3 .   ? 15.00415  -5.11829  27.32192 1.000 39.82784 ? 506 LFA A C3  1 
HETATM 1987 C C4  . LFA G 3 .   ? 13.81143  -5.78039  26.67686 1.000 38.90147 ? 506 LFA A C4  1 
HETATM 1988 C C5  . LFA G 3 .   ? 13.20657  -5.00730  25.53092 1.000 37.87894 ? 506 LFA A C5  1 
HETATM 1989 C C6  . LFA G 3 .   ? 12.32880  -5.84201  24.63079 1.000 37.73296 ? 506 LFA A C6  1 
HETATM 1990 C C7  . LFA G 3 .   ? 11.75661  -5.10382  23.44652 1.000 36.24991 ? 506 LFA A C7  1 
HETATM 1991 C C8  . LFA G 3 .   ? 11.12218  -6.00200  22.41318 1.000 34.56086 ? 506 LFA A C8  1 
HETATM 1992 C C9  . LFA G 3 .   ? 10.02170  -6.88564  22.94749 1.000 35.02602 ? 506 LFA A C9  1 
HETATM 1993 C C10 . LFA G 3 .   ? 9.49638   -7.89271  21.95262 1.000 34.32514 ? 506 LFA A C10 1 
HETATM 1994 C C11 . LFA G 3 .   ? 8.40049   -8.78064  22.48875 1.000 34.68800 ? 506 LFA A C11 1 
HETATM 1995 C C1  . LFA H 3 .   ? 20.62984  12.94473  26.20646 1.000 35.78773 ? 507 LFA A C1  1 
HETATM 1996 C C2  . LFA H 3 .   ? 19.81246  13.14793  24.95578 1.000 36.15318 ? 507 LFA A C2  1 
HETATM 1997 C C3  . LFA H 3 .   ? 18.53564  12.35059  24.94123 1.000 36.81079 ? 507 LFA A C3  1 
HETATM 1998 C C4  . LFA H 3 .   ? 17.64174  12.65959  23.76754 1.000 37.41706 ? 507 LFA A C4  1 
HETATM 1999 C C5  . LFA H 3 .   ? 16.29768  11.97751  23.81341 1.000 36.41637 ? 507 LFA A C5  1 
HETATM 2000 C C6  . LFA H 3 .   ? 15.34785  12.41724  22.72620 1.000 36.57070 ? 507 LFA A C6  1 
HETATM 2001 C C7  . LFA H 3 .   ? 13.98226  11.77918  22.79626 1.000 36.76691 ? 507 LFA A C7  1 
HETATM 2002 C C8  . LFA H 3 .   ? 13.02381  12.25087  21.72978 1.000 37.30944 ? 507 LFA A C8  1 
HETATM 2003 C C1  . LFA I 3 .   ? 16.27040  -14.60101 19.91714 1.000 35.37833 ? 508 LFA A C1  1 
HETATM 2004 C C2  . LFA I 3 .   ? 17.70652  -14.32216 20.29142 1.000 34.06420 ? 508 LFA A C2  1 
HETATM 2005 C C3  . LFA I 3 .   ? 17.85615  -13.29988 21.38817 1.000 33.98733 ? 508 LFA A C3  1 
HETATM 2006 C C4  . LFA I 3 .   ? 19.28395  -13.00042 21.77211 1.000 32.94374 ? 508 LFA A C4  1 
HETATM 2007 C C5  . LFA I 3 .   ? 19.42958  -11.97619 22.87106 1.000 33.84789 ? 508 LFA A C5  1 
HETATM 2008 C C6  . LFA I 3 .   ? 20.85622  -11.71395 23.28971 1.000 34.53042 ? 508 LFA A C6  1 
HETATM 2009 C C10 . LFA J 3 .   ? 16.75547  -9.15878  23.16443 1.000 31.69721 ? 509 LFA A C10 1 
HETATM 2010 C C11 . LFA J 3 .   ? 15.46575  -8.38791  23.04614 1.000 31.15012 ? 509 LFA A C11 1 
HETATM 2011 C C12 . LFA J 3 .   ? 14.44163  -9.03143  22.14485 1.000 33.24224 ? 509 LFA A C12 1 
HETATM 2012 C C3  . LFA K 3 .   ? 20.42867  19.31052  21.46440 1.000 39.25675 ? 510 LFA A C3  1 
HETATM 2013 C C4  . LFA K 3 .   ? 19.34500  18.27688  21.65052 1.000 38.52877 ? 510 LFA A C4  1 
HETATM 2014 C C5  . LFA K 3 .   ? 18.67234  18.31667  23.00137 1.000 37.21236 ? 510 LFA A C5  1 
HETATM 2015 C C6  . LFA K 3 .   ? 17.55779  17.31268  23.17158 1.000 36.77022 ? 510 LFA A C6  1 
HETATM 2016 C C7  . LFA K 3 .   ? 16.42039  17.47669  22.19188 1.000 38.24078 ? 510 LFA A C7  1 
HETATM 2017 C C8  . LFA K 3 .   ? 15.29630  16.48832  22.37727 1.000 37.45697 ? 510 LFA A C8  1 
HETATM 2018 C C9  . LFA K 3 .   ? 14.15608  16.65762  21.40485 1.000 38.70139 ? 510 LFA A C9  1 
HETATM 2019 C C6  . LFA L 3 .   ? 23.12146  4.50453   31.74598 1.000 34.38650 ? 511 LFA A C6  1 
HETATM 2020 C C7  . LFA L 3 .   ? 24.25490  5.49173   31.61219 1.000 34.57166 ? 511 LFA A C7  1 
HETATM 2021 C C8  . LFA L 3 .   ? 23.88247  6.77190   30.90476 1.000 33.89146 ? 511 LFA A C8  1 
HETATM 2022 C C9  . LFA L 3 .   ? 25.00806  7.77373   30.79794 1.000 36.29459 ? 511 LFA A C9  1 
HETATM 2023 C C10 . LFA L 3 .   ? 24.63917  9.04808   30.07665 1.000 37.02508 ? 511 LFA A C10 1 
HETATM 2024 C C11 . LFA L 3 .   ? 23.48146  9.79575   30.69151 1.000 37.94835 ? 511 LFA A C11 1 
HETATM 2025 C C12 . LFA L 3 .   ? 23.16788  11.11201  30.02389 1.000 37.66792 ? 511 LFA A C12 1 
HETATM 2026 C C13 . LFA L 3 .   ? 21.98191  11.83731  30.61018 1.000 37.92332 ? 511 LFA A C13 1 
HETATM 2027 C C14 . LFA L 3 .   ? 21.68909  13.16984  29.96718 1.000 39.21094 ? 511 LFA A C14 1 
HETATM 2028 C C8  . LFA M 3 .   ? 28.54356  3.97385   2.88792  1.000 40.46962 ? 512 LFA A C8  1 
HETATM 2029 C C9  . LFA M 3 .   ? 27.37375  4.84596   2.50224  1.000 41.54506 ? 512 LFA A C9  1 
HETATM 2030 C C10 . LFA M 3 .   ? 26.02698  4.22857   2.78555  1.000 42.99572 ? 512 LFA A C10 1 
HETATM 2031 C C11 . LFA M 3 .   ? 24.84857  5.06672   2.35287  1.000 43.88102 ? 512 LFA A C11 1 
HETATM 2032 C C12 . LFA M 3 .   ? 23.50875  4.43387   2.64072  1.000 44.25497 ? 512 LFA A C12 1 
HETATM 2033 C C13 . LFA M 3 .   ? 23.36319  3.03471   2.09503  1.000 44.33298 ? 512 LFA A C13 1 
HETATM 2034 C C14 . LFA M 3 .   ? 22.04903  2.36552   2.42004  1.000 44.94486 ? 512 LFA A C14 1 
HETATM 2035 C C15 . LFA M 3 .   ? 21.99691  0.90752   2.03248  1.000 46.84592 ? 512 LFA A C15 1 
HETATM 2036 C C16 . LFA M 3 .   ? 20.70829  0.19950   2.37978  1.000 45.90583 ? 512 LFA A C16 1 
HETATM 2037 C C17 . LFA M 3 .   ? 19.52031  0.59040   1.53236  1.000 44.35975 ? 512 LFA A C17 1 
HETATM 2038 C C18 . LFA M 3 .   ? 18.28286  -0.23340  1.80023  1.000 41.86528 ? 512 LFA A C18 1 
HETATM 2039 C C19 . LFA M 3 .   ? 17.10552  0.03052   0.89656  1.000 39.49704 ? 512 LFA A C19 1 
HETATM 2040 C C20 . LFA M 3 .   ? 16.59678  1.45024   0.95562  1.000 39.09160 ? 512 LFA A C20 1 
HETATM 2041 C C17 . LFA N 3 .   ? 20.48890  6.67815   0.78943  1.000 38.61094 ? 513 LFA A C17 1 
HETATM 2042 C C18 . LFA N 3 .   ? 20.24178  5.23854   1.16517  1.000 38.98349 ? 513 LFA A C18 1 
HETATM 2043 C C19 . LFA N 3 .   ? 18.83307  4.93574   1.60653  1.000 39.79097 ? 513 LFA A C19 1 
HETATM 2044 C C20 . LFA N 3 .   ? 17.78889  5.21429   0.55159  1.000 40.21670 ? 513 LFA A C20 1 
HETATM 2045 C C18 . LFA O 3 .   ? 14.59575  14.12437  3.07475  1.000 36.00793 ? 514 LFA A C18 1 
HETATM 2046 C C19 . LFA O 3 .   ? 15.83498  14.40021  3.88595  1.000 35.99326 ? 514 LFA A C19 1 
HETATM 2047 C C20 . LFA O 3 .   ? 15.54667  14.77601  5.31891  1.000 34.90310 ? 514 LFA A C20 1 
HETATM 2048 C C1  . RET P 4 .   ? 24.05751  9.08658   16.96063 1.000 8.65279  ? 515 RET A C1  1 
HETATM 2049 C C2  . RET P 4 .   ? 24.82772  10.37350  17.25907 1.000 9.21369  ? 515 RET A C2  1 
HETATM 2050 C C3  . RET P 4 .   ? 24.31748  11.07454  18.49317 1.000 9.74575  ? 515 RET A C3  1 
HETATM 2051 C C4  . RET P 4 .   ? 22.87786  11.47412  18.29901 1.000 9.84335  ? 515 RET A C4  1 
HETATM 2052 C C5  . RET P 4 .   ? 22.03764  10.41838  17.66900 1.000 10.06793 ? 515 RET A C5  1 
HETATM 2053 C C6  . RET P 4 .   ? 22.55156  9.31436   17.05972 1.000 9.30671  ? 515 RET A C6  1 
HETATM 2054 C C7  . RET P 4 .   ? 21.67709  8.29931   16.44963 1.000 9.80157  ? 515 RET A C7  1 
HETATM 2055 C C8  . RET P 4 .   ? 21.81336  6.96133   16.50172 1.000 9.51342  ? 515 RET A C8  1 
HETATM 2056 C C9  . RET P 4 .   ? 20.84748  5.98891   16.01874 1.000 9.22589  ? 515 RET A C9  1 
HETATM 2057 C C10 . RET P 4 .   ? 21.28333  4.72534   15.85695 1.000 9.34906  ? 515 RET A C10 1 
HETATM 2058 C C11 . RET P 4 .   ? 20.49088  3.60672   15.41958 1.000 10.89982 ? 515 RET A C11 1 
HETATM 2059 C C12 . RET P 4 .   ? 21.02463  2.39024   15.22148 1.000 10.92036 ? 515 RET A C12 1 
HETATM 2060 C C13 . RET P 4 .   ? 20.38215  1.12499   14.92755 1.000 10.41314 ? 515 RET A C13 1 
HETATM 2061 C C14 . RET P 4 .   ? 21.14432  0.04949   14.64651 1.000 11.96473 ? 515 RET A C14 1 
HETATM 2062 C C15 . RET P 4 .   ? 20.61662  -1.27419  14.23560 1.000 12.51593 ? 515 RET A C15 1 
HETATM 2063 C C16 . RET P 4 .   ? 24.58781  8.05610   17.95725 1.000 10.41036 ? 515 RET A C16 1 
HETATM 2064 C C17 . RET P 4 .   ? 24.45411  8.64741   15.54979 1.000 9.67787  ? 515 RET A C17 1 
HETATM 2065 C C18 . RET P 4 .   ? 20.58490  10.72608  17.78996 1.000 11.21223 ? 515 RET A C18 1 
HETATM 2066 C C19 . RET P 4 .   ? 19.41582  6.33666   16.18029 1.000 10.08464 ? 515 RET A C19 1 
HETATM 2067 C C20 . RET P 4 .   ? 18.89480  1.12971   14.86712 1.000 11.59611 ? 515 RET A C20 1 
HETATM 2068 O O   A HOH Q 5 .   ? 12.82434  -3.66647  6.98738  0.700 30.58325 ? 601 HOH A O   1 
HETATM 2069 O O   A HOH Q 5 .   ? 13.56622  7.19147   19.73618 0.500 15.87873 ? 602 HOH A O   1 
HETATM 2070 O O   B HOH Q 5 .   ? 12.86547  8.62769   20.49967 0.500 13.64539 ? 602 HOH A O   1 
HETATM 2071 O O   . HOH Q 5 .   ? 31.24615  25.78149  20.02785 1.000 21.51753 ? 603 HOH A O   1 
HETATM 2072 O O   . HOH Q 5 .   ? 36.26256  1.16436   9.67943  1.000 35.66358 ? 604 HOH A O   1 
HETATM 2073 O O   . HOH Q 5 .   ? 14.09845  -16.24643 0.56200  1.000 44.56497 ? 605 HOH A O   1 
HETATM 2074 O O   . HOH Q 5 .   ? 23.97381  -2.84080  14.83366 1.000 24.97184 ? 606 HOH A O   1 
HETATM 2075 O O   A HOH Q 5 .   ? 31.63666  -16.94149 12.97074 0.500 27.40582 ? 607 HOH A O   1 
HETATM 2076 O O   B HOH Q 5 .   ? 31.87412  -17.83687 13.09615 0.500 32.17263 ? 607 HOH A O   1 
HETATM 2077 O O   . HOH Q 5 .   ? -6.82314  4.69402   14.50762 1.000 32.83800 ? 608 HOH A O   1 
HETATM 2078 O O   . HOH Q 5 .   ? -0.56049  -4.37493  6.49463  1.000 33.71180 ? 609 HOH A O   1 
HETATM 2079 O O   . HOH Q 5 .   ? -4.77731  -14.24020 6.66051  1.000 50.20722 ? 610 HOH A O   1 
HETATM 2080 O O   . HOH Q 5 .   ? 40.50249  3.71921   18.59493 1.000 41.24991 ? 611 HOH A O   1 
HETATM 2081 O O   . HOH Q 5 .   ? 3.35439   5.10692   19.19305 1.000 30.75110 ? 612 HOH A O   1 
HETATM 2082 O O   . HOH Q 5 .   ? 36.89585  5.06821   12.50691 1.000 34.17608 ? 613 HOH A O   1 
HETATM 2083 O O   . HOH Q 5 .   ? 8.62588   -18.61892 16.30398 1.000 47.66694 ? 614 HOH A O   1 
HETATM 2084 O O   . HOH Q 5 .   ? 9.30073   -22.61880 13.32239 1.000 36.73675 ? 615 HOH A O   1 
HETATM 2085 O O   . HOH Q 5 .   ? -0.82447  2.07270   14.88910 1.000 21.10036 ? 616 HOH A O   1 
HETATM 2086 O O   . HOH Q 5 .   ? -1.20048  4.38128   5.78615  1.000 27.04242 ? 617 HOH A O   1 
HETATM 2087 O O   . HOH Q 5 .   ? 37.05669  6.47522   29.72312 1.000 25.27874 ? 618 HOH A O   1 
HETATM 2088 O O   A HOH Q 5 .   ? 13.52640  -5.77038  11.21967 0.700 23.55573 ? 619 HOH A O   1 
HETATM 2089 O O   B HOH Q 5 .   ? 14.47539  -5.29933  11.47370 0.300 25.30242 ? 619 HOH A O   1 
HETATM 2090 O O   . HOH Q 5 .   ? 36.80989  16.72110  14.18081 1.000 36.45830 ? 620 HOH A O   1 
HETATM 2091 O O   . HOH Q 5 .   ? 34.95178  -4.60022  33.58907 1.000 48.37198 ? 621 HOH A O   1 
HETATM 2092 O O   . HOH Q 5 .   ? 9.22840   -18.72086 2.05659  1.000 45.80428 ? 622 HOH A O   1 
HETATM 2093 O O   . HOH Q 5 .   ? -1.83638  -0.03670  6.48918  1.000 31.69106 ? 623 HOH A O   1 
HETATM 2094 O O   . HOH Q 5 .   ? 2.77073   -8.39463  5.10764  1.000 37.43829 ? 624 HOH A O   1 
HETATM 2095 O O   . HOH Q 5 .   ? 10.85703  -21.01633 8.30410  1.000 26.21337 ? 625 HOH A O   1 
HETATM 2096 O O   . HOH Q 5 .   ? 35.79479  19.54431  10.92385 1.000 46.59691 ? 626 HOH A O   1 
HETATM 2097 O O   . HOH Q 5 .   ? 34.97138  3.88838   23.44537 1.000 23.95195 ? 627 HOH A O   1 
HETATM 2098 O O   . HOH Q 5 .   ? 5.09123   10.03118  8.28516  1.000 23.94390 ? 628 HOH A O   1 
HETATM 2099 O O   . HOH Q 5 .   ? 6.63156   -12.60683 1.68893  1.000 30.62707 ? 629 HOH A O   1 
HETATM 2100 O O   . HOH Q 5 .   ? 36.03008  10.37263  25.19060 1.000 23.63738 ? 630 HOH A O   1 
HETATM 2101 O O   . HOH Q 5 .   ? 36.05575  3.62393   29.41361 1.000 30.68415 ? 631 HOH A O   1 
HETATM 2102 O O   . HOH Q 5 .   ? 33.54393  4.74522   19.83758 1.000 15.78561 ? 632 HOH A O   1 
HETATM 2103 O O   . HOH Q 5 .   ? 31.15744  1.94920   18.49876 1.000 11.01923 ? 633 HOH A O   1 
HETATM 2104 O O   . HOH Q 5 .   ? 40.61149  1.60028   21.43687 1.000 31.44337 ? 634 HOH A O   1 
HETATM 2105 O O   . HOH Q 5 .   ? -4.26661  -6.67255  19.63244 1.000 27.86756 ? 635 HOH A O   1 
HETATM 2106 O O   . HOH Q 5 .   ? 4.84026   -23.11784 6.73480  1.000 37.27634 ? 636 HOH A O   1 
HETATM 2107 O O   . HOH Q 5 .   ? 39.79747  -2.75045  14.42075 1.000 15.27770 ? 637 HOH A O   1 
HETATM 2108 O O   A HOH Q 5 .   ? 26.34863  -1.88488  15.13957 0.500 18.80066 ? 638 HOH A O   1 
HETATM 2109 O O   . HOH Q 5 .   ? 34.64097  11.66720  20.65133 1.000 19.97285 ? 639 HOH A O   1 
HETATM 2110 O O   . HOH Q 5 .   ? 9.82762   14.10196  -1.03701 1.000 38.17671 ? 640 HOH A O   1 
HETATM 2111 O O   . HOH Q 5 .   ? 6.48889   -9.40725  7.10772  1.000 27.09774 ? 641 HOH A O   1 
HETATM 2112 O O   . HOH Q 5 .   ? 4.16372   -6.07140  16.37460 1.000 14.17536 ? 642 HOH A O   1 
HETATM 2113 O O   . HOH Q 5 .   ? 41.42257  -9.09755  18.37403 1.000 32.64235 ? 643 HOH A O   1 
HETATM 2114 O O   . HOH Q 5 .   ? 15.80337  -7.20726  12.67058 1.000 17.01790 ? 644 HOH A O   1 
HETATM 2115 O O   . HOH Q 5 .   ? 35.12081  9.37295   28.98262 1.000 26.60903 ? 645 HOH A O   1 
HETATM 2116 O O   . HOH Q 5 .   ? 7.33767   10.36615  6.12306  1.000 23.80778 ? 646 HOH A O   1 
HETATM 2117 O O   . HOH Q 5 .   ? 3.28812   -0.52939  22.69067 1.000 26.29268 ? 647 HOH A O   1 
HETATM 2118 O O   . HOH Q 5 .   ? 37.81552  -6.52091  13.52248 1.000 15.42558 ? 648 HOH A O   1 
HETATM 2119 O O   A HOH Q 5 .   ? 32.68048  -10.39099 18.76932 0.500 29.25300 ? 649 HOH A O   1 
HETATM 2120 O O   B HOH Q 5 .   ? 32.59404  -12.44509 18.82024 0.500 29.23576 ? 649 HOH A O   1 
HETATM 2121 O O   . HOH Q 5 .   ? 34.86126  -11.32589 17.83086 1.000 23.64688 ? 650 HOH A O   1 
HETATM 2122 O O   A HOH Q 5 .   ? 0.29690   6.14164   7.65982  0.700 42.77412 ? 651 HOH A O   1 
HETATM 2123 O O   B HOH Q 5 .   ? -0.61389  7.72222   8.89477  0.300 42.84028 ? 651 HOH A O   1 
HETATM 2124 O O   . HOH Q 5 .   ? 2.91102   -6.94265  18.45788 1.000 14.92740 ? 652 HOH A O   1 
HETATM 2125 O O   . HOH Q 5 .   ? 37.14888  4.20988   17.09973 1.000 13.27229 ? 653 HOH A O   1 
HETATM 2126 O O   A HOH Q 5 .   ? 0.45356   -2.76318  23.17515 0.500 23.66338 ? 654 HOH A O   1 
HETATM 2127 O O   B HOH Q 5 .   ? 0.29232   -1.61071  21.30904 0.500 23.60130 ? 654 HOH A O   1 
HETATM 2128 O O   A HOH Q 5 .   ? -6.49911  -4.73999  12.44490 0.500 18.68233 ? 655 HOH A O   1 
HETATM 2129 O O   B HOH Q 5 .   ? -6.26733  -6.47997  12.67046 0.500 20.86521 ? 655 HOH A O   1 
HETATM 2130 O O   . HOH Q 5 .   ? 30.43596  9.62331   21.30553 1.000 13.05224 ? 656 HOH A O   1 
HETATM 2131 O O   . HOH Q 5 .   ? 4.23603   13.23111  14.60071 1.000 24.39947 ? 657 HOH A O   1 
HETATM 2132 O O   . HOH Q 5 .   ? 7.60339   -15.83307 1.29294  1.000 47.69456 ? 658 HOH A O   1 
HETATM 2133 O O   . HOH Q 5 .   ? 28.55488  23.99450  16.51103 1.000 16.77503 ? 659 HOH A O   1 
HETATM 2134 O O   B HOH Q 5 .   ? 6.43640   -5.24690  6.76488  0.300 33.24422 ? 660 HOH A O   1 
HETATM 2135 O O   A HOH Q 5 .   ? -3.78809  3.32796   15.48223 0.700 31.41492 ? 661 HOH A O   1 
HETATM 2136 O O   B HOH Q 5 .   ? -2.48772  4.00851   14.36678 0.300 31.40201 ? 661 HOH A O   1 
HETATM 2137 O O   . HOH Q 5 .   ? 36.43115  8.23913   18.75337 1.000 23.50982 ? 662 HOH A O   1 
HETATM 2138 O O   . HOH Q 5 .   ? 7.48495   -0.16088  -4.14256 1.000 35.06855 ? 663 HOH A O   1 
HETATM 2139 O O   . HOH Q 5 .   ? 0.93953   5.30494   -2.91142 1.000 29.62484 ? 664 HOH A O   1 
HETATM 2140 O O   . HOH Q 5 .   ? 9.96866   -21.00220 16.03048 1.000 46.36444 ? 665 HOH A O   1 
HETATM 2141 O O   . HOH Q 5 .   ? 35.63932  13.80488  12.54766 1.000 35.14693 ? 666 HOH A O   1 
HETATM 2142 O O   . HOH Q 5 .   ? 2.22041   -21.63410 9.44420  1.000 41.19337 ? 667 HOH A O   1 
HETATM 2143 O O   . HOH Q 5 .   ? 29.96154  -3.87672  24.18127 1.000 15.05465 ? 668 HOH A O   1 
HETATM 2144 O O   . HOH Q 5 .   ? 10.73721  8.58438   -4.60489 1.000 49.95353 ? 669 HOH A O   1 
HETATM 2145 O O   . HOH Q 5 .   ? 38.89845  -2.17959  12.01029 1.000 22.01763 ? 670 HOH A O   1 
HETATM 2146 O O   . HOH Q 5 .   ? 35.16088  9.94031   22.47083 1.000 26.74549 ? 671 HOH A O   1 
HETATM 2147 O O   . HOH Q 5 .   ? 32.87694  -10.95998 10.72087 1.000 22.26110 ? 672 HOH A O   1 
HETATM 2148 O O   . HOH Q 5 .   ? 36.26502  22.81460  20.08201 1.000 26.29694 ? 673 HOH A O   1 
HETATM 2149 O O   . HOH Q 5 .   ? 37.14959  7.51746   22.60363 1.000 44.39646 ? 674 HOH A O   1 
HETATM 2150 O O   . HOH Q 5 .   ? 5.05473   -0.90233  -2.69069 1.000 36.99916 ? 675 HOH A O   1 
HETATM 2151 O O   . HOH Q 5 .   ? 7.65984   7.96515   -5.17646 1.000 42.89689 ? 676 HOH A O   1 
HETATM 2152 O O   . HOH Q 5 .   ? 14.14452  -0.96731  17.15842 1.000 15.10604 ? 677 HOH A O   1 
HETATM 2153 O O   . HOH Q 5 .   ? 21.66638  5.03797   6.85770  1.000 18.99188 ? 678 HOH A O   1 
HETATM 2154 O O   . HOH Q 5 .   ? 6.16738   -8.44845  4.48810  1.000 49.65434 ? 679 HOH A O   1 
HETATM 2155 O O   . HOH Q 5 .   ? 34.49061  0.05832   8.76702  1.000 50.33409 ? 680 HOH A O   1 
HETATM 2156 O O   . HOH Q 5 .   ? 8.16204   14.53264  6.16456  1.000 35.11450 ? 681 HOH A O   1 
HETATM 2157 O O   . HOH Q 5 .   ? 3.61038   -2.42092  1.16178  1.000 29.79269 ? 682 HOH A O   1 
HETATM 2158 O O   . HOH Q 5 .   ? 15.07605  3.76106   4.53666  1.000 18.22240 ? 683 HOH A O   1 
HETATM 2159 O O   . HOH Q 5 .   ? 35.78396  -10.63502 6.51382  1.000 45.00166 ? 684 HOH A O   1 
HETATM 2160 O O   . HOH Q 5 .   ? -8.46483  -7.16735  15.22963 1.000 24.24805 ? 685 HOH A O   1 
HETATM 2161 O O   . HOH Q 5 .   ? 39.68165  -1.47145  23.66280 1.000 26.32076 ? 686 HOH A O   1 
HETATM 2162 O O   . HOH Q 5 .   ? 3.70309   -5.41360  5.56761  1.000 48.78769 ? 687 HOH A O   1 
HETATM 2163 O O   . HOH Q 5 .   ? -7.17364  -0.83224  10.28891 1.000 38.28726 ? 688 HOH A O   1 
HETATM 2164 O O   . HOH Q 5 .   ? 34.46591  12.85664  31.10617 1.000 42.84723 ? 689 HOH A O   1 
HETATM 2165 O O   . HOH Q 5 .   ? 0.24631   -5.78699  22.43835 1.000 26.58282 ? 690 HOH A O   1 
HETATM 2166 O O   . HOH Q 5 .   ? -1.92359  -7.18259  18.02751 1.000 22.87357 ? 691 HOH A O   1 
HETATM 2167 O O   . HOH Q 5 .   ? -0.00000  3.67677   0.00000  0.500 19.95882 ? 692 HOH A O   1 
HETATM 2168 O O   . HOH Q 5 .   ? 5.89486   -25.70068 6.70917  1.000 48.40688 ? 693 HOH A O   1 
HETATM 2169 O O   . HOH Q 5 .   ? 5.29494   -8.04553  9.06230  1.000 25.51085 ? 694 HOH A O   1 
HETATM 2170 O O   . HOH Q 5 .   ? 5.08556   -8.68383  2.00510  1.000 47.14152 ? 695 HOH A O   1 
HETATM 2171 O O   . HOH Q 5 .   ? -7.16546  -9.17408  20.26553 1.000 36.05408 ? 696 HOH A O   1 
HETATM 2172 O O   . HOH Q 5 .   ? -5.38794  -10.23223 9.03910  1.000 42.77265 ? 697 HOH A O   1 
HETATM 2173 O O   . HOH Q 5 .   ? 37.61259  8.87640   10.31223 1.000 49.18528 ? 698 HOH A O   1 
HETATM 2174 O O   . HOH Q 5 .   ? 1.81090   -21.43800 12.14003 1.000 44.41342 ? 699 HOH A O   1 
HETATM 2175 O O   . HOH Q 5 .   ? -6.45681  -12.08932 18.19502 1.000 40.65134 ? 700 HOH A O   1 
HETATM 2176 O O   . HOH Q 5 .   ? 38.06692  -4.34519  33.06280 1.000 42.91015 ? 701 HOH A O   1 
HETATM 2177 O O   . HOH Q 5 .   ? 0.20084   -6.77057  4.21390  1.000 48.96430 ? 702 HOH A O   1 
HETATM 2178 O O   . HOH Q 5 .   ? 39.64833  9.76273   15.66485 1.000 42.95613 ? 703 HOH A O   1 
HETATM 2179 O O   . HOH Q 5 .   ? -5.76307  -10.84325 12.84816 1.000 37.76535 ? 704 HOH A O   1 
HETATM 2180 O O   . HOH Q 5 .   ? 9.99965   17.77340  6.09555  1.000 46.74405 ? 705 HOH A O   1 
HETATM 2181 O O   . HOH Q 5 .   ? -2.95369  -10.19988 18.27998 1.000 35.73627 ? 706 HOH A O   1 
HETATM 2182 O O   . HOH Q 5 .   ? 4.14826   -27.46185 7.60835  1.000 46.23321 ? 707 HOH A O   1 
HETATM 2183 O O   A HOH Q 5 .   ? 12.33941  -4.14300  10.00246 0.700 35.76880 ? 708 HOH A O   1 
HETATM 2184 O O   B HOH Q 5 .   ? 12.74631  -4.71415  9.97386  0.300 38.23263 ? 708 HOH A O   1 
HETATM 2185 O O   . HOH Q 5 .   ? 3.81153   8.20046   19.51189 1.000 37.58942 ? 709 HOH A O   1 
HETATM 2186 O O   . HOH Q 5 .   ? 14.55701  9.35929   -6.14089 1.000 47.58008 ? 710 HOH A O   1 
HETATM 2187 O O   . HOH Q 5 .   ? -9.04503  7.57584   15.29037 1.000 47.62887 ? 711 HOH A O   1 
HETATM 2188 O O   . HOH Q 5 .   ? -12.59648 5.92830   14.71428 1.000 28.98044 ? 712 HOH A O   1 
HETATM 2189 O O   . HOH Q 5 .   ? 1.23003   7.69252   3.27054  1.000 47.75632 ? 713 HOH A O   1 
HETATM 2190 O O   . HOH Q 5 .   ? 9.35685   12.47193  19.08778 1.000 41.19029 ? 714 HOH A O   1 
HETATM 2191 O O   . HOH Q 5 .   ? 0.79487   -19.82887 8.64911  1.000 42.83715 ? 715 HOH A O   1 
HETATM 2192 O O   . HOH Q 5 .   ? 33.57493  8.69869   36.42463 1.000 35.77004 ? 716 HOH A O   1 
HETATM 2193 O O   . HOH Q 5 .   ? -2.51578  -10.63672 20.60292 1.000 41.87260 ? 717 HOH A O   1 
HETATM 2194 O O   . HOH Q 5 .   ? 46.29381  0.40989   22.00260 1.000 53.79700 ? 718 HOH A O   1 
HETATM 2195 O O   . HOH Q 5 .   ? 3.55738   -5.04995  2.83191  1.000 36.16369 ? 719 HOH A O   1 
HETATM 2196 O O   . HOH Q 5 .   ? 9.03321   11.52067  3.99841  1.000 42.27935 ? 720 HOH A O   1 
HETATM 2197 O O   A HOH Q 5 .   ? -5.28646  3.43091   8.15639  0.500 37.35425 ? 721 HOH A O   1 
HETATM 2198 O O   A HOH Q 5 .   ? 6.840     1.750     -8.387   0.500 42.84512 ? 722 HOH A O   1 
HETATM 2199 O O   . HOH Q 5 .   ? 38.19383  17.35439  16.43845 1.000 38.56303 ? 723 HOH A O   1 
HETATM 2200 O O   A HOH Q 5 .   ? 32.02145  19.89001  26.73919 0.500 34.03999 ? 724 HOH A O   1 
HETATM 2201 O O   B HOH Q 5 .   ? 31.23999  19.47514  27.85137 0.500 36.02640 ? 724 HOH A O   1 
HETATM 2202 O O   . HOH Q 5 .   ? 48.080    0.548     20.526   1.000 42.84332 ? 725 HOH A O   1 
HETATM 2203 O O   . HOH Q 5 .   ? 36.95841  -11.74773 19.14919 1.000 34.82642 ? 726 HOH A O   1 
HETATM 2204 O O   . HOH Q 5 .   ? -3.96599  -11.85008 22.00034 1.000 59.94531 ? 727 HOH A O   1 
HETATM 2205 O O   . HOH Q 5 .   ? 37.54937  2.45313   27.49299 1.000 35.41384 ? 728 HOH A O   1 
HETATM 2206 O O   . HOH Q 5 .   ? 5.90143   -10.43555 -0.37563 1.000 45.36945 ? 729 HOH A O   1 
HETATM 2207 O O   . HOH Q 5 .   ? 34.28172  0.27689   5.58546  1.000 52.14028 ? 730 HOH A O   1 
HETATM 2208 O O   . HOH Q 5 .   ? 35.99714  5.57422   19.34703 1.000 17.62866 ? 731 HOH A O   1 
HETATM 2209 O O   . HOH Q 5 .   ? 9.21788   14.22240  3.92278  1.000 44.88901 ? 732 HOH A O   1 
HETATM 2210 O O   . HOH Q 5 .   ? 40.314    -5.531    14.415   1.000 19.35047 ? 733 HOH A O   1 
HETATM 2211 O O   . HOH Q 5 .   ? 5.47526   -2.17734  -0.28573 1.000 44.75658 ? 734 HOH A O   1 
HETATM 2212 O O   . HOH Q 5 .   ? 37.52178  4.75060   21.25816 1.000 39.36851 ? 735 HOH A O   1 
HETATM 2213 O O   . HOH Q 5 .   ? 38.52997  8.43845   17.17898 1.000 29.44734 ? 736 HOH A O   1 
HETATM 2214 O O   . HOH Q 5 .   ? 9.10699   -13.94363 0.57191  1.000 45.31517 ? 737 HOH A O   1 
HETATM 2215 O O   . HOH Q 5 .   ? 0.47613   -8.02880  18.62762 1.000 29.85430 ? 738 HOH A O   1 
HETATM 2216 O O   . HOH Q 5 .   ? -1.576    9.523     7.168    1.000 34.76836 ? 739 HOH A O   1 
HETATM 2217 O O   . HOH Q 5 .   ? 39.47708  0.79571   24.00267 1.000 38.60523 ? 740 HOH A O   1 
HETATM 2218 O O   . HOH Q 5 .   ? 37.22496  3.22526   24.25992 1.000 34.11023 ? 741 HOH A O   1 
HETATM 2219 O O   . HOH Q 5 .   ? -8.88802  -5.51660  11.94876 1.000 36.63553 ? 742 HOH A O   1 
HETATM 2220 O O   . HOH Q 5 .   ? 11.67298  -17.31082 -0.47759 1.000 49.19179 ? 743 HOH A O   1 
HETATM 2221 O O   . HOH Q 5 .   ? 38.74809  -8.99442  12.94686 1.000 24.15165 ? 744 HOH A O   1 
HETATM 2222 O O   . HOH Q 5 .   ? 37.93678  -5.11327  11.56598 1.000 23.70173 ? 745 HOH A O   1 
HETATM 2223 O O   . HOH Q 5 .   ? 33.39310  18.10078  27.86063 1.000 45.61459 ? 746 HOH A O   1 
HETATM 2224 O O   . HOH Q 5 .   ? 48.598    -2.690    23.657   1.000 44.61939 ? 747 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 
1    N N   . MET A 1   ? 0.44110 0.41691 0.40010 -0.08606 -0.03266 0.01678  1   MET A N   
2    C CA  . MET A 1   ? 0.47130 0.42449 0.43469 -0.10350 -0.01292 0.01826  1   MET A CA  
3    C C   . MET A 1   ? 0.40385 0.34533 0.38064 -0.11694 -0.00939 0.01443  1   MET A C   
4    O O   . MET A 1   ? 0.37083 0.28761 0.36635 -0.11462 0.00373  0.01784  1   MET A O   
5    C CB  . MET A 1   ? 0.51854 0.53055 0.49780 -0.07009 -0.02411 0.04362  1   MET A CB  
6    C CG  . MET A 1   ? 0.54002 0.54209 0.53544 -0.03734 -0.04779 0.07059  1   MET A CG  
7    S SD  . MET A 1   ? 0.54193 0.54273 0.54259 -0.00073 -0.05757 0.09589  1   MET A SD  
8    C CE  . MET A 1   ? 0.54295 0.56030 0.54276 0.00909  -0.06217 0.09437  1   MET A CE  
9    N N   . GLU A 2   ? 0.35508 0.34554 0.33525 -0.11358 -0.03691 -0.00599 2   GLU A N   
10   C CA  . GLU A 2   ? 0.32717 0.33976 0.33289 -0.09045 -0.04691 0.01468  2   GLU A CA  
11   C C   . GLU A 2   ? 0.30110 0.32589 0.31470 -0.07029 -0.03963 0.01568  2   GLU A C   
12   O O   . GLU A 2   ? 0.27927 0.29533 0.31661 -0.08515 -0.02113 0.01176  2   GLU A O   
13   C CB  . GLU A 2   ? 0.35215 0.38553 0.33116 -0.08113 -0.06002 0.02421  2   GLU A CB  
14   N N   . GLU A 3   ? 0.30286 0.33134 0.29975 -0.05255 -0.05305 0.02469  3   GLU A N   
15   C CA  . GLU A 3   ? 0.31103 0.33316 0.26495 -0.04124 -0.06675 0.04252  3   GLU A CA  
16   C C   . GLU A 3   ? 0.32742 0.29792 0.25180 -0.05164 -0.07285 0.04065  3   GLU A C   
17   O O   . GLU A 3   ? 0.36389 0.27546 0.27241 -0.03284 -0.04186 0.06678  3   GLU A O   
18   C CB  . GLU A 3   ? 0.29824 0.33843 0.26664 -0.03064 -0.09140 0.07396  3   GLU A CB  
19   C CG  . GLU A 3   ? 0.29989 0.34653 0.29843 -0.00166 -0.09739 0.11237  3   GLU A CG  
20   N N   . LEU A 4   ? 0.31562 0.32512 0.22418 -0.06605 -0.08102 0.00097  4   LEU A N   
21   C CA  . LEU A 4   ? 0.28697 0.29504 0.20736 -0.07535 -0.06554 -0.02614 4   LEU A CA  
22   C C   . LEU A 4   ? 0.25394 0.23324 0.16592 -0.07423 -0.05418 -0.03671 4   LEU A C   
23   O O   . LEU A 4   ? 0.25401 0.20457 0.14943 -0.09381 -0.04999 -0.03404 4   LEU A O   
24   C CB  . LEU A 4   ? 0.30128 0.35349 0.23419 -0.03781 -0.03786 -0.02747 4   LEU A CB  
25   C CG  . LEU A 4   ? 0.30733 0.35257 0.24875 -0.00486 -0.03069 -0.02465 4   LEU A CG  
26   C CD1 . LEU A 4   ? 0.32040 0.36234 0.24691 0.00448  0.00025  -0.01644 4   LEU A CD1 
27   C CD2 . LEU A 4   ? 0.33252 0.38392 0.25924 0.02476  -0.00470 -0.02598 4   LEU A CD2 
28   N N   . THR A 5   ? 0.22844 0.20866 0.14193 -0.05049 -0.01878 -0.02147 5   THR A N   
29   C CA  . THR A 5   ? 0.19084 0.19631 0.15386 -0.01833 -0.00305 -0.01313 5   THR A CA  
30   C C   . THR A 5   ? 0.16301 0.16114 0.14064 -0.01461 -0.02712 0.01366  5   THR A C   
31   O O   . THR A 5   ? 0.15733 0.19650 0.11645 -0.02132 -0.04264 0.01534  5   THR A O   
32   C CB  . THR A 5   ? 0.19475 0.17852 0.15429 -0.02377 0.03576  -0.04679 5   THR A CB  
33   O OG1 . THR A 5   ? 0.21335 0.21058 0.16756 -0.03040 0.05329  -0.03958 5   THR A OG1 
34   C CG2 . THR A 5   ? 0.17398 0.16243 0.15054 -0.02095 0.05367  -0.05459 5   THR A CG2 
35   N N   . TYR A 6   ? 0.14907 0.18464 0.20198 0.00089  -0.03469 0.03374  6   TYR A N   
36   C CA  . TYR A 6   ? 0.18961 0.18093 0.24031 -0.00628 -0.03386 0.02976  6   TYR A CA  
37   C C   . TYR A 6   ? 0.22632 0.21101 0.22400 -0.01839 -0.04313 0.02710  6   TYR A C   
38   O O   . TYR A 6   ? 0.21589 0.18716 0.19435 -0.00953 -0.05903 0.02424  6   TYR A O   
39   C CB  . TYR A 6   ? 0.17621 0.21835 0.28380 0.01514  -0.07138 0.01656  6   TYR A CB  
40   C CG  . TYR A 6   ? 0.22635 0.26342 0.35136 0.00467  -0.06351 -0.00186 6   TYR A CG  
41   C CD1 . TYR A 6   ? 0.25784 0.29893 0.38548 -0.01251 -0.03503 -0.01398 6   TYR A CD1 
42   C CD2 . TYR A 6   ? 0.26245 0.28894 0.37179 0.01658  -0.05510 -0.00341 6   TYR A CD2 
43   C CE1 . TYR A 6   ? 0.28204 0.32378 0.40861 -0.02427 -0.01684 -0.02883 6   TYR A CE1 
44   C CE2 . TYR A 6   ? 0.30614 0.33226 0.39889 0.02092  -0.02122 -0.01987 6   TYR A CE2 
45   C CZ  . TYR A 6   ? 0.31527 0.34139 0.43048 0.00730  -0.01449 -0.03269 6   TYR A CZ  
46   O OH  . TYR A 6   ? 0.38749 0.38775 0.48331 0.03036  0.01115  -0.03410 6   TYR A OH  
47   N N   A ARG A 7   ? 0.23916 0.19632 0.23355 -0.03462 -0.04828 0.05475  7   ARG A N   
48   N N   B ARG A 7   ? 0.23916 0.19710 0.23388 -0.03418 -0.04943 0.05436  7   ARG A N   
49   C CA  A ARG A 7   ? 0.24599 0.22410 0.24678 -0.04130 -0.02164 0.04950  7   ARG A CA  
50   C CA  B ARG A 7   ? 0.24687 0.22634 0.24724 -0.03890 -0.02271 0.04933  7   ARG A CA  
51   C C   A ARG A 7   ? 0.22965 0.19480 0.23114 -0.04321 -0.00765 0.02976  7   ARG A C   
52   C C   B ARG A 7   ? 0.23008 0.19523 0.23164 -0.04164 -0.00804 0.02984  7   ARG A C   
53   O O   A ARG A 7   ? 0.21872 0.17682 0.22940 -0.02384 -0.02232 0.01681  7   ARG A O   
54   O O   B ARG A 7   ? 0.21876 0.17671 0.23040 -0.02155 -0.02199 0.01722  7   ARG A O   
55   C CB  A ARG A 7   ? 0.27648 0.27162 0.28318 -0.03768 -0.02602 0.08123  7   ARG A CB  
56   C CB  B ARG A 7   ? 0.27866 0.27779 0.28361 -0.03300 -0.02702 0.08118  7   ARG A CB  
57   C CG  A ARG A 7   ? 0.34829 0.34211 0.34903 -0.03872 -0.01835 0.08982  7   ARG A CG  
58   C CG  B ARG A 7   ? 0.35119 0.34973 0.34982 -0.03358 -0.01915 0.08971  7   ARG A CG  
59   C CD  . ARG A 7   ? 0.39078 0.43445 0.40502 -0.03213 -0.00014 0.08143  7   ARG A CD  
60   N NE  . ARG A 7   ? 0.41174 0.45752 0.45911 -0.02734 -0.00802 0.05972  7   ARG A NE  
61   C CZ  . ARG A 7   ? 0.50037 0.54857 0.53960 -0.02436 0.04508  0.04026  7   ARG A CZ  
62   N N   . LEU A 8   ? 0.20817 0.17666 0.21739 -0.05632 -0.00071 0.01003  8   LEU A N   
63   C CA  . LEU A 8   ? 0.21916 0.15689 0.18696 -0.03952 -0.00405 -0.00381 8   LEU A CA  
64   C C   . LEU A 8   ? 0.20830 0.17884 0.17311 -0.01746 0.00634  -0.00289 8   LEU A C   
65   O O   . LEU A 8   ? 0.18329 0.20148 0.13615 -0.04039 -0.01493 -0.01902 8   LEU A O   
66   C CB  . LEU A 8   ? 0.25434 0.17157 0.19134 -0.08215 0.03125  -0.01276 8   LEU A CB  
67   C CG  . LEU A 8   ? 0.30197 0.24906 0.21657 -0.08452 0.03502  -0.00996 8   LEU A CG  
68   C CD1 . LEU A 8   ? 0.31846 0.30971 0.18497 -0.05167 0.03243  0.02614  8   LEU A CD1 
69   C CD2 . LEU A 8   ? 0.34009 0.35751 0.26949 -0.08412 0.07524  -0.02191 8   LEU A CD2 
70   N N   . PHE A 9   ? 0.16846 0.15043 0.17684 -0.02380 -0.00669 0.00220  9   PHE A N   
71   C CA  . PHE A 9   ? 0.15380 0.14127 0.19141 -0.01662 -0.00335 -0.00169 9   PHE A CA  
72   C C   . PHE A 9   ? 0.16947 0.14300 0.21055 -0.01739 -0.01065 -0.00535 9   PHE A C   
73   O O   . PHE A 9   ? 0.17743 0.17311 0.18499 -0.01029 -0.00543 0.01095  9   PHE A O   
74   C CB  . PHE A 9   ? 0.12895 0.13058 0.17327 -0.02955 0.03209  0.00039  9   PHE A CB  
75   C CG  . PHE A 9   ? 0.09948 0.12066 0.15053 -0.01455 0.02070  -0.01802 9   PHE A CG  
76   C CD1 . PHE A 9   ? 0.11933 0.12958 0.14671 0.00460  0.03255  -0.00677 9   PHE A CD1 
77   C CD2 . PHE A 9   ? 0.11888 0.11697 0.14520 -0.03113 0.01023  -0.03052 9   PHE A CD2 
78   C CE1 . PHE A 9   ? 0.12625 0.13729 0.14922 -0.03804 0.04706  -0.02831 9   PHE A CE1 
79   C CE2 . PHE A 9   ? 0.12227 0.14959 0.14387 0.00300  0.01179  -0.03957 9   PHE A CE2 
80   C CZ  . PHE A 9   ? 0.09823 0.16857 0.14293 -0.00465 0.04760  -0.03282 9   PHE A CZ  
81   N N   A MET A 10  ? 0.19844 0.12027 0.22379 -0.00501 -0.01843 0.00701  10  MET A N   
82   N N   B MET A 10  ? 0.19439 0.11709 0.22332 -0.00365 -0.01894 0.00486  10  MET A N   
83   C CA  A MET A 10  ? 0.24761 0.13619 0.22969 -0.00027 -0.01060 0.01732  10  MET A CA  
84   C CA  B MET A 10  ? 0.23197 0.12245 0.23171 -0.00152 -0.02028 0.01522  10  MET A CA  
85   C C   A MET A 10  ? 0.26166 0.13738 0.22062 -0.03344 -0.01211 0.01576  10  MET A C   
86   C C   B MET A 10  ? 0.25846 0.13639 0.22223 -0.03034 -0.01302 0.01184  10  MET A C   
87   O O   A MET A 10  ? 0.29396 0.13506 0.22763 -0.02698 0.00044  0.01653  10  MET A O   
88   O O   B MET A 10  ? 0.29634 0.13941 0.23180 -0.02273 0.00147  0.00729  10  MET A O   
89   C CB  A MET A 10  ? 0.27354 0.20920 0.24594 0.02893  0.02744  0.01485  10  MET A CB  
90   C CB  B MET A 10  ? 0.23539 0.16432 0.24876 0.01353  -0.01065 0.01933  10  MET A CB  
91   C CG  A MET A 10  ? 0.28787 0.25733 0.27969 0.05740  0.06472  0.00211  10  MET A CG  
92   C CG  B MET A 10  ? 0.23237 0.18605 0.26606 0.01555  -0.00752 0.01451  10  MET A CG  
93   S SD  A MET A 10  ? 0.33353 0.29680 0.34079 0.06820  0.09756  -0.01057 10  MET A SD  
94   S SD  B MET A 10  ? 0.26202 0.23974 0.32418 0.01392  0.01139  0.00605  10  MET A SD  
95   N N   . VAL A 11  ? 0.24570 0.16034 0.20112 -0.05453 -0.02207 0.01484  11  VAL A N   
96   C CA  . VAL A 11  ? 0.20538 0.22924 0.17667 -0.07063 -0.01068 0.03524  11  VAL A CA  
97   C C   . VAL A 11  ? 0.18463 0.22508 0.15764 -0.07758 0.00612  0.02886  11  VAL A C   
98   O O   . VAL A 11  ? 0.19837 0.20838 0.14897 -0.08728 -0.00703 0.04419  11  VAL A O   
99   C CB  . VAL A 11  ? 0.23296 0.29637 0.22369 -0.07134 -0.00177 0.05302  11  VAL A CB  
100  C CG1 . VAL A 11  ? 0.26029 0.32485 0.25633 -0.05129 0.02214  0.05636  11  VAL A CG1 
101  C CG2 . VAL A 11  ? 0.24202 0.29001 0.20996 -0.08156 0.01092  0.07999  11  VAL A CG2 
102  N N   . ALA A 12  ? 0.18006 0.17788 0.17067 -0.03510 0.00792  -0.00928 12  ALA A N   
103  C CA  . ALA A 12  ? 0.19174 0.13561 0.18642 -0.01713 0.00502  -0.02755 12  ALA A CA  
104  C C   . ALA A 12  ? 0.17117 0.11732 0.21543 -0.02010 0.02798  -0.02371 12  ALA A C   
105  O O   . ALA A 12  ? 0.13985 0.13266 0.19534 -0.00183 -0.01268 -0.02256 12  ALA A O   
106  C CB  . ALA A 12  ? 0.20678 0.11126 0.17630 0.00209  -0.00388 -0.01122 12  ALA A CB  
107  N N   . THR A 13  ? 0.16876 0.09587 0.23185 -0.01352 0.03108  0.00252  13  THR A N   
108  C CA  . THR A 13  ? 0.13152 0.08402 0.20062 0.00760  0.01694  -0.01795 13  THR A CA  
109  C C   . THR A 13  ? 0.16330 0.08074 0.18896 0.00791  0.02163  -0.00662 13  THR A C   
110  O O   . THR A 13  ? 0.19049 0.10846 0.16861 -0.00983 0.00475  0.00724  13  THR A O   
111  C CB  . THR A 13  ? 0.12383 0.11118 0.20193 0.00094  0.00882  -0.01892 13  THR A CB  
112  O OG1 . THR A 13  ? 0.12806 0.10963 0.22022 -0.01363 0.02150  -0.00506 13  THR A OG1 
113  C CG2 . THR A 13  ? 0.16227 0.17590 0.20310 -0.01262 0.01714  -0.06507 13  THR A CG2 
114  N N   . VAL A 14  ? 0.16503 0.08131 0.18287 -0.05315 -0.01580 0.01295  14  VAL A N   
115  C CA  . VAL A 14  ? 0.17435 0.10188 0.18880 -0.03171 -0.00838 0.04599  14  VAL A CA  
116  C C   . VAL A 14  ? 0.18079 0.14632 0.15575 -0.00988 -0.00558 0.03099  14  VAL A C   
117  O O   . VAL A 14  ? 0.16560 0.15326 0.13879 -0.02331 -0.00745 -0.01385 14  VAL A O   
118  C CB  . VAL A 14  ? 0.14862 0.14748 0.21798 -0.04137 -0.01287 0.07506  14  VAL A CB  
119  C CG1 . VAL A 14  ? 0.16310 0.17118 0.24587 -0.04912 0.01297  0.09572  14  VAL A CG1 
120  C CG2 . VAL A 14  ? 0.15495 0.19636 0.21981 -0.02675 -0.01466 0.04951  14  VAL A CG2 
121  N N   . GLY A 15  ? 0.16556 0.12074 0.13232 0.00980  0.00283  0.00986  15  GLY A N   
122  C CA  . GLY A 15  ? 0.16944 0.12521 0.15336 -0.00723 0.04542  0.01605  15  GLY A CA  
123  C C   . GLY A 15  ? 0.16128 0.11618 0.17993 -0.02666 0.03115  0.00292  15  GLY A C   
124  O O   . GLY A 15  ? 0.15417 0.13853 0.17896 -0.03123 0.04986  -0.00572 15  GLY A O   
125  N N   . MET A 16  ? 0.18586 0.14986 0.16465 -0.01502 0.04310  0.02106  16  MET A N   
126  C CA  . MET A 16  ? 0.17036 0.11508 0.14015 -0.02078 -0.00476 0.00007  16  MET A CA  
127  C C   . MET A 16  ? 0.17608 0.11651 0.16716 -0.00640 0.01582  -0.01133 16  MET A C   
128  O O   . MET A 16  ? 0.16098 0.13199 0.18479 0.01017  -0.01196 -0.01598 16  MET A O   
129  C CB  . MET A 16  ? 0.18820 0.15285 0.11464 -0.03284 -0.00643 -0.00152 16  MET A CB  
130  C CG  . MET A 16  ? 0.15816 0.14553 0.13343 0.01723  -0.02094 0.01699  16  MET A CG  
131  S SD  . MET A 16  ? 0.16949 0.16966 0.14619 -0.02781 0.02235  -0.00481 16  MET A SD  
132  C CE  . MET A 16  ? 0.16440 0.11795 0.20387 -0.02164 0.04915  -0.00275 16  MET A CE  
133  N N   . LEU A 17  ? 0.15852 0.10276 0.17073 0.02537  0.04526  -0.02638 17  LEU A N   
134  C CA  . LEU A 17  ? 0.19287 0.07327 0.16348 0.02532  0.04529  -0.02489 17  LEU A CA  
135  C C   . LEU A 17  ? 0.18962 0.10182 0.16122 0.01697  0.01785  -0.03090 17  LEU A C   
136  O O   . LEU A 17  ? 0.19759 0.09987 0.13838 0.02154  0.00024  -0.03587 17  LEU A O   
137  C CB  . LEU A 17  ? 0.16620 0.07527 0.14990 0.04516  0.03925  -0.00706 17  LEU A CB  
138  C CG  . LEU A 17  ? 0.17902 0.06884 0.16066 0.04190  0.02314  -0.01544 17  LEU A CG  
139  C CD1 . LEU A 17  ? 0.21237 0.11405 0.19661 0.02144  0.06053  -0.03843 17  LEU A CD1 
140  C CD2 . LEU A 17  ? 0.20460 0.09721 0.17474 0.02942  0.03796  -0.05245 17  LEU A CD2 
141  N N   . ALA A 18  ? 0.17973 0.08165 0.16768 -0.00165 -0.00407 -0.00388 18  ALA A N   
142  C CA  . ALA A 18  ? 0.16554 0.08165 0.19775 0.01860  0.00045  -0.02553 18  ALA A CA  
143  C C   . ALA A 18  ? 0.14926 0.11373 0.21263 -0.01867 -0.00644 -0.02144 18  ALA A C   
144  O O   . ALA A 18  ? 0.15103 0.13112 0.22776 -0.01543 -0.01837 0.00476  18  ALA A O   
145  C CB  . ALA A 18  ? 0.19223 0.10133 0.20480 -0.00749 0.02523  -0.03420 18  ALA A CB  
146  N N   . GLY A 19  ? 0.12458 0.14279 0.23406 -0.00671 -0.00502 -0.00175 19  GLY A N   
147  C CA  . GLY A 19  ? 0.13253 0.13273 0.23464 0.01033  -0.02222 -0.02872 19  GLY A CA  
148  C C   . GLY A 19  ? 0.14904 0.11083 0.22548 0.00628  -0.02754 -0.03241 19  GLY A C   
149  O O   . GLY A 19  ? 0.14884 0.12754 0.20673 0.00145  -0.02459 -0.02925 19  GLY A O   
150  N N   . THR A 20  ? 0.14715 0.10295 0.21233 -0.00510 -0.04280 -0.01397 20  THR A N   
151  C CA  . THR A 20  ? 0.15473 0.10072 0.20610 -0.01801 -0.01697 -0.01344 20  THR A CA  
152  C C   . THR A 20  ? 0.15102 0.10025 0.21408 0.00201  -0.01959 0.01485  20  THR A C   
153  O O   . THR A 20  ? 0.18584 0.11113 0.22590 0.01438  -0.01697 0.01609  20  THR A O   
154  C CB  . THR A 20  ? 0.15192 0.13825 0.16007 -0.04797 -0.00903 -0.02860 20  THR A CB  
155  O OG1 . THR A 20  ? 0.15818 0.15416 0.14330 -0.05205 0.03537  0.00073  20  THR A OG1 
156  C CG2 . THR A 20  ? 0.14570 0.17489 0.16561 -0.02826 -0.01651 -0.02277 20  THR A CG2 
157  N N   . VAL A 21  ? 0.17534 0.08507 0.23538 0.00997  -0.01995 0.02327  21  VAL A N   
158  C CA  . VAL A 21  ? 0.20764 0.07871 0.23914 -0.00015 -0.04616 0.00233  21  VAL A CA  
159  C C   . VAL A 21  ? 0.18128 0.11849 0.24306 -0.01956 -0.03681 0.01361  21  VAL A C   
160  O O   . VAL A 21  ? 0.18005 0.16461 0.28761 -0.01231 -0.05294 0.01211  21  VAL A O   
161  C CB  . VAL A 21  ? 0.24223 0.09203 0.24733 -0.00046 -0.06404 -0.03337 21  VAL A CB  
162  C CG1 . VAL A 21  ? 0.22544 0.12288 0.27207 0.02114  -0.05857 -0.05413 21  VAL A CG1 
163  C CG2 . VAL A 21  ? 0.24848 0.09496 0.23846 -0.00861 -0.05525 -0.04954 21  VAL A CG2 
164  N N   A PHE A 22  ? 0.18140 0.15423 0.22452 -0.03536 -0.01959 0.02410  22  PHE A N   
165  N N   B PHE A 22  ? 0.17637 0.12785 0.23085 -0.04198 -0.01364 0.03339  22  PHE A N   
166  C CA  A PHE A 22  ? 0.18405 0.18589 0.20282 -0.03260 -0.01231 -0.00451 22  PHE A CA  
167  C CA  B PHE A 22  ? 0.16949 0.14137 0.21136 -0.02556 0.00142  0.00828  22  PHE A CA  
168  C C   A PHE A 22  ? 0.16529 0.15262 0.16993 -0.01072 -0.00048 -0.02279 22  PHE A C   
169  C C   B PHE A 22  ? 0.14876 0.14114 0.18643 -0.00280 -0.00631 -0.01726 22  PHE A C   
170  O O   A PHE A 22  ? 0.16070 0.13727 0.14100 0.00276  -0.00396 -0.04439 22  PHE A O   
171  O O   B PHE A 22  ? 0.13822 0.16445 0.17410 0.00508  -0.01725 -0.04719 22  PHE A O   
172  C CB  A PHE A 22  ? 0.19951 0.19448 0.22181 -0.04939 -0.00455 -0.01175 22  PHE A CB  
173  C CB  B PHE A 22  ? 0.18598 0.10910 0.20884 -0.01131 0.02776  0.00896  22  PHE A CB  
174  C CG  A PHE A 22  ? 0.21941 0.16258 0.22140 -0.03857 -0.00428 -0.00732 22  PHE A CG  
175  C CG  B PHE A 22  ? 0.17928 0.13481 0.20092 0.00601  0.04408  -0.00419 22  PHE A CG  
176  C CD1 A PHE A 22  ? 0.21094 0.15606 0.22357 -0.04368 0.00841  -0.00697 22  PHE A CD1 
177  C CD1 B PHE A 22  ? 0.20317 0.11964 0.18835 0.03051  0.03979  -0.02066 22  PHE A CD1 
178  C CD2 A PHE A 22  ? 0.23000 0.16221 0.22977 -0.03656 0.01096  0.00119  22  PHE A CD2 
179  C CD2 B PHE A 22  ? 0.16802 0.13639 0.18623 0.04966  0.02216  0.00636  22  PHE A CD2 
180  C CE1 A PHE A 22  ? 0.23706 0.14403 0.24165 -0.02756 0.01567  0.01075  22  PHE A CE1 
181  C CE1 B PHE A 22  ? 0.21312 0.10363 0.19468 0.04267  0.05882  -0.02156 22  PHE A CE1 
182  C CE2 A PHE A 22  ? 0.24241 0.12989 0.24347 -0.03888 0.00239  0.00810  22  PHE A CE2 
183  C CE2 B PHE A 22  ? 0.17299 0.12575 0.17854 0.06085  0.03470  -0.00719 22  PHE A CE2 
184  C CZ  A PHE A 22  ? 0.25682 0.15722 0.25411 -0.02156 0.02106  0.01142  22  PHE A CZ  
185  C CZ  B PHE A 22  ? 0.19897 0.10742 0.18676 0.06437  0.04388  -0.01999 22  PHE A CZ  
186  N N   . LEU A 23  ? 0.17600 0.14904 0.16337 -0.00216 -0.00232 -0.00663 23  LEU A N   
187  C CA  . LEU A 23  ? 0.17718 0.13731 0.17228 -0.01675 -0.00478 -0.00901 23  LEU A CA  
188  C C   . LEU A 23  ? 0.19624 0.13755 0.16092 -0.00370 -0.00762 -0.00371 23  LEU A C   
189  O O   . LEU A 23  ? 0.17347 0.16136 0.14064 0.00937  -0.03338 -0.02109 23  LEU A O   
190  C CB  . LEU A 23  ? 0.15724 0.13149 0.18280 -0.04446 -0.02094 -0.02478 23  LEU A CB  
191  C CG  . LEU A 23  ? 0.12899 0.15520 0.20803 -0.03408 -0.00307 -0.03394 23  LEU A CG  
192  C CD1 . LEU A 23  ? 0.13115 0.16194 0.21318 -0.01139 -0.01040 -0.01848 23  LEU A CD1 
193  C CD2 . LEU A 23  ? 0.14338 0.19429 0.20762 -0.04834 -0.00303 -0.05281 23  LEU A CD2 
194  N N   . LEU A 24  ? 0.18343 0.13409 0.20363 -0.01417 -0.00639 -0.02075 24  LEU A N   
195  C CA  . LEU A 24  ? 0.20682 0.14345 0.23970 -0.01078 -0.00133 -0.02507 24  LEU A CA  
196  C C   . LEU A 24  ? 0.19579 0.17710 0.26159 0.00056  -0.01699 -0.02136 24  LEU A C   
197  O O   . LEU A 24  ? 0.21400 0.19283 0.26697 -0.00898 -0.01936 -0.02743 24  LEU A O   
198  C CB  . LEU A 24  ? 0.20881 0.15083 0.26023 -0.04162 0.01566  -0.00892 24  LEU A CB  
199  C CG  . LEU A 24  ? 0.24573 0.16567 0.27324 -0.04145 0.01638  -0.01833 24  LEU A CG  
200  C CD1 . LEU A 24  ? 0.27598 0.17884 0.27044 -0.04158 0.03504  -0.03643 24  LEU A CD1 
201  C CD2 . LEU A 24  ? 0.26494 0.19439 0.27795 -0.03771 0.03554  -0.00433 24  LEU A CD2 
202  N N   . ALA A 25  ? 0.18920 0.16439 0.27836 0.01098  0.00094  -0.01445 25  ALA A N   
203  C CA  . ALA A 25  ? 0.18206 0.16353 0.29030 0.00361  0.00561  -0.02534 25  ALA A CA  
204  C C   . ALA A 25  ? 0.16114 0.20646 0.28984 0.00981  0.00846  -0.03533 25  ALA A C   
205  O O   . ALA A 25  ? 0.18646 0.19691 0.28802 0.00021  0.05358  -0.04539 25  ALA A O   
206  C CB  . ALA A 25  ? 0.20909 0.13542 0.29060 -0.02955 0.01268  0.00167  25  ALA A CB  
207  N N   A SER A 26  ? 0.14790 0.19189 0.28844 0.00872  -0.00970 -0.03653 26  SER A N   
208  N N   B SER A 26  ? 0.15246 0.20192 0.29224 0.01329  -0.00195 -0.04352 26  SER A N   
209  C CA  A SER A 26  ? 0.17121 0.19441 0.29076 0.00461  -0.01124 -0.04037 26  SER A CA  
210  C CA  B SER A 26  ? 0.16673 0.21367 0.30013 0.01842  -0.00144 -0.04910 26  SER A CA  
211  C C   A SER A 26  ? 0.16929 0.17825 0.30790 0.01028  -0.02505 -0.03933 26  SER A C   
212  C C   B SER A 26  ? 0.17119 0.18544 0.31073 0.01631  -0.02173 -0.04646 26  SER A C   
213  O O   A SER A 26  ? 0.17307 0.16202 0.31299 0.00049  -0.01430 -0.04393 26  SER A O   
214  O O   B SER A 26  ? 0.17638 0.16487 0.31370 0.00930  -0.01909 -0.05102 26  SER A O   
215  C CB  A SER A 26  ? 0.19293 0.18094 0.28437 -0.03100 -0.00994 -0.04793 26  SER A CB  
216  C CB  B SER A 26  ? 0.17492 0.20711 0.30358 0.00330  -0.00621 -0.05654 26  SER A CB  
217  O OG  A SER A 26  ? 0.19497 0.21428 0.26848 -0.03790 -0.00495 -0.04826 26  SER A OG  
218  O OG  B SER A 26  ? 0.19815 0.23466 0.29872 0.01451  0.00430  -0.06231 26  SER A OG  
219  N N   . SER A 27  ? 0.15077 0.19256 0.31477 -0.00446 -0.04249 -0.04563 27  SER A N   
220  C CA  . SER A 27  ? 0.20944 0.24669 0.33225 -0.00786 -0.00880 -0.02626 27  SER A CA  
221  C C   . SER A 27  ? 0.23134 0.24791 0.33666 -0.02667 -0.00044 -0.03033 27  SER A C   
222  O O   . SER A 27  ? 0.26784 0.24952 0.31796 -0.00818 0.00931  -0.04063 27  SER A O   
223  C CB  . SER A 27  ? 0.23120 0.31391 0.35148 -0.00579 0.00239  -0.02680 27  SER A CB  
224  O OG  . SER A 27  ? 0.24830 0.35353 0.37298 -0.01454 0.00576  -0.03788 27  SER A OG  
225  N N   A ARG A 28  ? 0.21902 0.22679 0.34798 -0.04872 -0.01373 -0.04312 28  ARG A N   
226  N N   B ARG A 28  ? 0.22228 0.22716 0.34903 -0.04892 -0.01736 -0.04262 28  ARG A N   
227  C CA  A ARG A 28  ? 0.23237 0.21228 0.37851 -0.05138 -0.03223 -0.03685 28  ARG A CA  
228  C CA  B ARG A 28  ? 0.24156 0.21361 0.38057 -0.05138 -0.03822 -0.03574 28  ARG A CA  
229  C C   A ARG A 28  ? 0.24814 0.23514 0.36911 -0.05380 -0.02554 -0.04131 28  ARG A C   
230  C C   B ARG A 28  ? 0.24938 0.23860 0.37040 -0.05381 -0.02811 -0.04194 28  ARG A C   
231  O O   A ARG A 28  ? 0.25448 0.27300 0.35256 -0.05411 -0.01170 -0.04772 28  ARG A O   
232  O O   B ARG A 28  ? 0.25235 0.27917 0.35308 -0.05411 -0.01159 -0.05003 28  ARG A O   
233  C CB  A ARG A 28  ? 0.25996 0.21954 0.40822 -0.03903 -0.02993 -0.03921 28  ARG A CB  
234  C CB  B ARG A 28  ? 0.28480 0.21955 0.41320 -0.03590 -0.04071 -0.03300 28  ARG A CB  
235  C CG  A ARG A 28  ? 0.25049 0.20882 0.42273 -0.03209 -0.04961 -0.03114 28  ARG A CG  
236  C CG  B ARG A 28  ? 0.29665 0.23569 0.43142 -0.01786 -0.06283 -0.01124 28  ARG A CG  
237  C CD  A ARG A 28  ? 0.26985 0.21571 0.43547 -0.03133 -0.04172 -0.01976 28  ARG A CD  
238  C CD  B ARG A 28  ? 0.33072 0.28754 0.44953 -0.00301 -0.03984 0.01836  28  ARG A CD  
239  N NE  A ARG A 28  ? 0.27028 0.18808 0.44340 -0.03194 -0.05023 -0.00145 28  ARG A NE  
240  N NE  B ARG A 28  ? 0.33959 0.30651 0.46292 0.02012  -0.04291 0.04372  28  ARG A NE  
241  C CZ  A ARG A 28  ? 0.29801 0.23411 0.44823 -0.02514 -0.04613 0.03277  28  ARG A CZ  
242  C CZ  B ARG A 28  ? 0.34164 0.31974 0.46517 0.04036  -0.03543 0.05856  28  ARG A CZ  
243  N NH1 A ARG A 28  ? 0.31879 0.26726 0.45409 -0.02524 -0.02511 0.05952  28  ARG A NH1 
244  N NH1 B ARG A 28  ? 0.35505 0.29891 0.46189 0.05881  -0.03042 0.06243  28  ARG A NH1 
245  N NH2 A ARG A 28  ? 0.28906 0.26079 0.46808 -0.03533 -0.04891 0.02967  28  ARG A NH2 
246  N NH2 B ARG A 28  ? 0.32896 0.34838 0.46809 0.04451  -0.02931 0.05522  28  ARG A NH2 
247  N N   A GLU A 29  ? 0.28523 0.23213 0.38795 -0.04715 -0.02892 -0.02935 29  GLU A N   
248  N N   B GLU A 29  ? 0.28451 0.23324 0.39032 -0.05135 -0.03046 -0.02972 29  GLU A N   
249  C CA  A GLU A 29  ? 0.29411 0.25912 0.40332 0.01133  -0.03802 -0.00303 29  GLU A CA  
250  C CA  B GLU A 29  ? 0.29652 0.25637 0.40866 0.00464  -0.03929 -0.00278 29  GLU A CA  
251  C C   A GLU A 29  ? 0.25109 0.26900 0.35043 0.00049  -0.05915 -0.00666 29  GLU A C   
252  C C   B GLU A 29  ? 0.25066 0.26596 0.35328 -0.00739 -0.06015 -0.00754 29  GLU A C   
253  O O   A GLU A 29  ? 0.25118 0.31991 0.34588 -0.01720 -0.04119 -0.00305 29  GLU A O   
254  O O   B GLU A 29  ? 0.24811 0.31069 0.34965 -0.03086 -0.04430 -0.00587 29  GLU A O   
255  C CB  A GLU A 29  ? 0.33733 0.30034 0.44589 0.05488  -0.02868 0.02112  29  GLU A CB  
256  C CB  B GLU A 29  ? 0.34555 0.28858 0.45864 0.04654  -0.03325 0.02450  29  GLU A CB  
257  C CG  A GLU A 29  ? 0.36850 0.34300 0.48305 0.05507  -0.02732 0.02223  29  GLU A CG  
258  C CG  B GLU A 29  ? 0.38571 0.32481 0.50337 0.04203  -0.03582 0.03085  29  GLU A CG  
259  C CD  A GLU A 29  ? 0.39974 0.38430 0.51710 0.04013  0.00202  0.01817  29  GLU A CD  
260  C CD  B GLU A 29  ? 0.42480 0.39374 0.54544 0.01971  -0.00898 0.02673  29  GLU A CD  
261  O OE1 A GLU A 29  ? 0.36402 0.37117 0.48419 0.06071  -0.00100 0.02435  29  GLU A OE1 
262  O OE1 B GLU A 29  ? 0.42118 0.43317 0.53191 0.01918  0.00048  0.00656  29  GLU A OE1 
263  O OE2 A GLU A 29  ? 0.46158 0.45258 0.58347 0.01376  0.03378  0.01116  29  GLU A OE2 
264  O OE2 B GLU A 29  ? 0.46201 0.45272 0.58391 -0.00195 0.01115  0.03038  29  GLU A OE2 
265  N N   . VAL A 30  ? 0.24344 0.25343 0.33252 -0.01274 -0.06591 -0.03348 30  VAL A N   
266  C CA  . VAL A 30  ? 0.23709 0.27030 0.30550 -0.00155 -0.07642 -0.03684 30  VAL A CA  
267  C C   . VAL A 30  ? 0.22820 0.28867 0.31782 -0.01190 -0.09053 -0.04053 30  VAL A C   
268  O O   . VAL A 30  ? 0.24182 0.29534 0.30942 -0.03301 -0.08174 -0.05499 30  VAL A O   
269  C CB  . VAL A 30  ? 0.26197 0.25229 0.30161 0.01386  -0.03661 -0.06178 30  VAL A CB  
270  C CG1 . VAL A 30  ? 0.27248 0.26770 0.27926 0.04701  -0.00273 -0.06280 30  VAL A CG1 
271  C CG2 . VAL A 30  ? 0.25156 0.21007 0.30898 -0.02088 -0.02962 -0.09651 30  VAL A CG2 
272  N N   . LYS A 31  ? 0.24918 0.29062 0.32276 0.00704  -0.09366 -0.01882 31  LYS A N   
273  C CA  . LYS A 31  ? 0.27432 0.35430 0.32339 -0.00045 -0.09924 -0.05342 31  LYS A CA  
274  C C   . LYS A 31  ? 0.26378 0.38608 0.29142 -0.02391 -0.09286 -0.10296 31  LYS A C   
275  O O   . LYS A 31  ? 0.22858 0.37574 0.30076 -0.03610 -0.09323 -0.11164 31  LYS A O   
276  C CB  . LYS A 31  ? 0.33141 0.41841 0.35508 -0.01183 -0.10991 -0.03599 31  LYS A CB  
277  C CG  . LYS A 31  ? 0.41659 0.49187 0.38618 -0.02652 -0.08556 -0.02212 31  LYS A CG  
278  C CD  . LYS A 31  ? 0.48192 0.56155 0.41643 -0.05201 -0.04451 -0.02716 31  LYS A CD  
279  C CE  . LYS A 31  ? 0.51485 0.61208 0.46602 -0.06294 -0.03268 -0.05335 31  LYS A CE  
280  N NZ  . LYS A 31  ? 0.57566 0.68993 0.53203 -0.06216 0.00399  -0.07334 31  LYS A NZ  
281  N N   . PRO A 32  ? 0.27287 0.41438 0.24175 -0.05380 -0.06890 -0.11673 32  PRO A N   
282  C CA  . PRO A 32  ? 0.29401 0.43071 0.23949 -0.03931 -0.04272 -0.10318 32  PRO A CA  
283  C C   . PRO A 32  ? 0.30103 0.43874 0.25345 -0.01042 -0.03907 -0.07406 32  PRO A C   
284  O O   . PRO A 32  ? 0.32711 0.45372 0.26900 -0.00798 0.00222  -0.07721 32  PRO A O   
285  C CB  . PRO A 32  ? 0.32039 0.41701 0.23860 -0.05339 -0.03502 -0.08256 32  PRO A CB  
286  C CG  . PRO A 32  ? 0.33119 0.39294 0.24530 -0.06072 -0.01979 -0.08330 32  PRO A CG  
287  C CD  . PRO A 32  ? 0.30301 0.38064 0.24026 -0.05907 -0.03646 -0.10472 32  PRO A CD  
288  N N   A GLU A 33  ? 0.31778 0.44607 0.25528 0.00174  -0.04112 -0.05878 33  GLU A N   
289  N N   B GLU A 33  ? 0.31893 0.45116 0.26300 0.00210  -0.04135 -0.05635 33  GLU A N   
290  C CA  A GLU A 33  ? 0.29377 0.43159 0.25294 -0.00552 -0.06826 -0.02665 33  GLU A CA  
291  C CA  B GLU A 33  ? 0.32183 0.43753 0.26963 -0.00585 -0.07132 -0.02128 33  GLU A CA  
292  C C   A GLU A 33  ? 0.27882 0.42604 0.26151 0.01682  -0.05846 -0.00276 33  GLU A C   
293  C C   B GLU A 33  ? 0.30238 0.42698 0.26548 0.01710  -0.05443 -0.00903 33  GLU A C   
294  O O   A GLU A 33  ? 0.28302 0.42027 0.26661 0.01967  -0.03246 0.01420  33  GLU A O   
295  O O   B GLU A 33  ? 0.33177 0.42018 0.26639 0.01894  -0.01412 -0.00726 33  GLU A O   
296  C CB  A GLU A 33  ? 0.29534 0.45769 0.24522 -0.02752 -0.07852 -0.02314 33  GLU A CB  
297  C CB  B GLU A 33  ? 0.34867 0.46337 0.27658 -0.03041 -0.08698 -0.00509 33  GLU A CB  
298  C CG  A GLU A 33  ? 0.29413 0.46564 0.24612 -0.02584 -0.09502 -0.01337 33  GLU A CG  
299  C CG  B GLU A 33  ? 0.35945 0.48628 0.27977 -0.03648 -0.07845 0.00391  33  GLU A CG  
300  C CD  A GLU A 33  ? 0.31273 0.49472 0.24146 -0.01184 -0.07227 -0.01348 33  GLU A CD  
301  C CD  B GLU A 33  ? 0.36518 0.48443 0.29111 -0.02287 -0.09005 0.01253  33  GLU A CD  
302  O OE1 A GLU A 33  ? 0.29265 0.50009 0.23168 0.03101  -0.09283 -0.01623 33  GLU A OE1 
303  O OE1 B GLU A 33  ? 0.39026 0.50740 0.28885 -0.00756 -0.07489 0.02122  33  GLU A OE1 
304  O OE2 A GLU A 33  ? 0.32523 0.46114 0.24967 -0.03813 -0.08675 -0.00837 33  GLU A OE2 
305  O OE2 B GLU A 33  ? 0.37687 0.50147 0.29877 -0.01717 -0.07885 0.01650  33  GLU A OE2 
306  N N   . HIS A 34  ? 0.26673 0.41236 0.25260 0.04231  -0.08920 -0.00140 34  HIS A N   
307  C CA  . HIS A 34  ? 0.26568 0.40297 0.24704 0.04526  -0.07172 -0.02032 34  HIS A CA  
308  C C   . HIS A 34  ? 0.25620 0.35922 0.24753 0.05361  -0.08366 -0.03089 34  HIS A C   
309  O O   . HIS A 34  ? 0.27343 0.36322 0.24570 0.06000  -0.07232 -0.05302 34  HIS A O   
310  C CB  . HIS A 34  ? 0.25255 0.38778 0.23962 0.05927  -0.08891 -0.02778 34  HIS A CB  
311  C CG  . HIS A 34  ? 0.30661 0.41272 0.25257 0.06770  -0.03301 -0.00749 34  HIS A CG  
312  N ND1 . HIS A 34  ? 0.34092 0.43016 0.26601 0.06880  0.02225  -0.00684 34  HIS A ND1 
313  C CD2 . HIS A 34  ? 0.31028 0.42817 0.24590 0.06303  0.00430  -0.01887 34  HIS A CD2 
314  C CE1 . HIS A 34  ? 0.31440 0.43437 0.24919 0.05961  0.00192  -0.02011 34  HIS A CE1 
315  N NE2 . HIS A 34  ? 0.31916 0.43427 0.23630 0.05909  0.00773  -0.03309 34  HIS A NE2 
316  N N   . ARG A 35  ? 0.24330 0.35117 0.24273 -0.00568 -0.07441 -0.03464 35  ARG A N   
317  C CA  . ARG A 35  ? 0.22813 0.29928 0.23927 -0.03327 -0.09051 -0.02351 35  ARG A CA  
318  C C   . ARG A 35  ? 0.24336 0.28260 0.22409 -0.03055 -0.07315 0.01196  35  ARG A C   
319  O O   . ARG A 35  ? 0.21316 0.28290 0.21616 -0.05897 -0.08593 0.01322  35  ARG A O   
320  C CB  . ARG A 35  ? 0.20513 0.30425 0.26664 -0.06014 -0.08472 -0.04569 35  ARG A CB  
321  C CG  . ARG A 35  ? 0.22691 0.33268 0.28814 -0.05132 -0.07870 -0.06129 35  ARG A CG  
322  C CD  . ARG A 35  ? 0.25323 0.34022 0.29203 -0.03402 -0.05792 -0.06350 35  ARG A CD  
323  N NE  . ARG A 35  ? 0.28935 0.34549 0.29549 -0.01062 -0.01267 -0.04827 35  ARG A NE  
324  C CZ  . ARG A 35  ? 0.33482 0.36941 0.31094 -0.02735 0.04071  -0.06709 35  ARG A CZ  
325  N NH1 . ARG A 35  ? 0.36685 0.40733 0.30532 -0.02088 0.04164  -0.06292 35  ARG A NH1 
326  N NH2 . ARG A 35  ? 0.35342 0.38079 0.33223 -0.05068 0.05640  -0.08975 35  ARG A NH2 
327  N N   . ARG A 36  ? 0.27862 0.25982 0.22015 -0.01632 -0.07166 0.04281  36  ARG A N   
328  C CA  . ARG A 36  ? 0.29864 0.28705 0.23758 -0.03245 -0.06082 0.03806  36  ARG A CA  
329  C C   . ARG A 36  ? 0.24169 0.28731 0.22156 -0.04572 -0.05916 0.03498  36  ARG A C   
330  O O   . ARG A 36  ? 0.24221 0.29262 0.22661 -0.06652 -0.04317 0.02705  36  ARG A O   
331  C CB  . ARG A 36  ? 0.37122 0.35548 0.27645 -0.01941 -0.04618 0.04610  36  ARG A CB  
332  C CG  . ARG A 36  ? 0.42180 0.44182 0.31397 -0.02131 -0.04683 0.04729  36  ARG A CG  
333  C CD  . ARG A 36  ? 0.46707 0.50191 0.35479 -0.02655 -0.04842 0.05102  36  ARG A CD  
334  N NE  . ARG A 36  ? 0.52463 0.58408 0.38496 -0.01156 0.01030  0.04734  36  ARG A NE  
335  C CZ  . ARG A 36  ? 0.50286 0.58219 0.36488 -0.00536 0.01809  0.03210  36  ARG A CZ  
336  N N   . GLY A 37  ? 0.20158 0.27838 0.19415 -0.02334 -0.06608 0.01016  37  GLY A N   
337  C CA  . GLY A 37  ? 0.20412 0.27294 0.17287 0.00182  -0.04515 0.01437  37  GLY A CA  
338  C C   . GLY A 37  ? 0.20670 0.25372 0.14808 0.01976  -0.03237 0.02614  37  GLY A C   
339  O O   . GLY A 37  ? 0.19476 0.26209 0.16715 0.01358  -0.03296 0.05579  37  GLY A O   
340  N N   . VAL A 38  ? 0.20562 0.24338 0.12844 0.00443  -0.00397 -0.00279 38  VAL A N   
341  C CA  . VAL A 38  ? 0.19767 0.25566 0.11029 0.00896  0.01343  -0.01000 38  VAL A CA  
342  C C   . VAL A 38  ? 0.18930 0.23765 0.12520 0.01524  -0.00839 -0.03941 38  VAL A C   
343  O O   . VAL A 38  ? 0.15655 0.21590 0.09458 0.03175  -0.00694 -0.05344 38  VAL A O   
344  C CB  . VAL A 38  ? 0.17389 0.27125 0.09221 -0.04096 -0.00456 0.03076  38  VAL A CB  
345  C CG1 . VAL A 38  ? 0.17120 0.21888 0.08551 -0.03384 -0.03229 0.05074  38  VAL A CG1 
346  C CG2 . VAL A 38  ? 0.15530 0.30280 0.10968 -0.04058 0.00662  0.04218  38  VAL A CG2 
347  N N   . TYR A 39  ? 0.21228 0.20783 0.14679 0.01350  -0.01445 -0.02541 39  TYR A N   
348  C CA  . TYR A 39  ? 0.22850 0.17437 0.17583 -0.00622 -0.01864 -0.02822 39  TYR A CA  
349  C C   . TYR A 39  ? 0.21623 0.17018 0.16672 -0.00119 -0.04568 0.00229  39  TYR A C   
350  O O   . TYR A 39  ? 0.18568 0.19835 0.17846 0.01275  -0.02646 0.00372  39  TYR A O   
351  C CB  . TYR A 39  ? 0.24824 0.18982 0.17236 -0.05666 -0.03969 -0.03713 39  TYR A CB  
352  C CG  . TYR A 39  ? 0.30721 0.22835 0.20391 -0.07765 -0.03423 -0.05460 39  TYR A CG  
353  C CD1 . TYR A 39  ? 0.34762 0.27017 0.21386 -0.07660 -0.02510 -0.06175 39  TYR A CD1 
354  C CD2 . TYR A 39  ? 0.32601 0.26934 0.23566 -0.08177 -0.02274 -0.05705 39  TYR A CD2 
355  C CE1 . TYR A 39  ? 0.36069 0.25228 0.20116 -0.07975 -0.02747 -0.06765 39  TYR A CE1 
356  C CE2 . TYR A 39  ? 0.35198 0.26034 0.22827 -0.08477 -0.01492 -0.07143 39  TYR A CE2 
357  C CZ  . TYR A 39  ? 0.37268 0.28479 0.21905 -0.08444 -0.00680 -0.07003 39  TYR A CZ  
358  O OH  . TYR A 39  ? 0.41603 0.32994 0.22782 -0.08766 0.01333  -0.06777 39  TYR A OH  
359  N N   . ILE A 40  ? 0.23780 0.13043 0.17689 -0.01113 -0.03846 -0.00547 40  ILE A N   
360  C CA  . ILE A 40  ? 0.22914 0.11394 0.16310 0.01017  -0.05367 0.00853  40  ILE A CA  
361  C C   . ILE A 40  ? 0.18401 0.13856 0.16680 0.02825  -0.05697 0.00799  40  ILE A C   
362  O O   . ILE A 40  ? 0.17642 0.14913 0.17093 -0.00189 -0.05311 -0.00099 40  ILE A O   
363  C CB  . ILE A 40  ? 0.22979 0.16322 0.15589 0.02658  -0.08492 0.04209  40  ILE A CB  
364  C CG1 . ILE A 40  ? 0.26934 0.22926 0.15413 0.01196  -0.08223 0.04400  40  ILE A CG1 
365  C CG2 . ILE A 40  ? 0.22163 0.17077 0.16271 0.04024  -0.06289 0.06648  40  ILE A CG2 
366  C CD1 . ILE A 40  ? 0.28315 0.31524 0.17022 -0.01901 -0.07896 0.03271  40  ILE A CD1 
367  N N   . SER A 41  ? 0.15933 0.14489 0.15464 0.02758  -0.02710 -0.00051 41  SER A N   
368  C CA  . SER A 41  ? 0.15259 0.18790 0.14302 0.05873  0.02996  0.01908  41  SER A CA  
369  C C   . SER A 41  ? 0.14788 0.14025 0.14363 0.03264  0.03302  0.01601  41  SER A C   
370  O O   . SER A 41  ? 0.15606 0.11752 0.14455 0.01490  -0.01172 0.01282  41  SER A O   
371  C CB  . SER A 41  ? 0.12888 0.20223 0.13904 0.07224  0.05162  0.01713  41  SER A CB  
372  O OG  . SER A 41  ? 0.20556 0.27197 0.15658 0.04700  0.08379  0.03536  41  SER A OG  
373  N N   . ALA A 42  ? 0.15013 0.07751 0.08694 0.03787  0.05728  0.01623  42  ALA A N   
374  C CA  . ALA A 42  ? 0.19417 0.06959 0.07227 0.01822  0.04193  -0.00532 42  ALA A CA  
375  C C   . ALA A 42  ? 0.20795 0.11724 0.09150 0.00514  0.01701  0.01064  42  ALA A C   
376  O O   . ALA A 42  ? 0.17967 0.13995 0.10760 0.01811  -0.01305 0.00698  42  ALA A O   
377  C CB  . ALA A 42  ? 0.21585 0.09498 0.07166 -0.00711 0.04688  0.00101  42  ALA A CB  
378  N N   . LEU A 43  ? 0.21420 0.10078 0.08974 -0.02032 -0.00355 0.00434  43  LEU A N   
379  C CA  . LEU A 43  ? 0.19868 0.15492 0.07772 -0.01038 0.02153  -0.01176 43  LEU A CA  
380  C C   . LEU A 43  ? 0.17857 0.12757 0.09598 -0.02247 0.00080  -0.00151 43  LEU A C   
381  O O   . LEU A 43  ? 0.16339 0.15281 0.09225 0.01511  -0.02153 -0.01787 43  LEU A O   
382  C CB  . LEU A 43  ? 0.19668 0.21653 0.06580 0.00191  0.04017  -0.00617 43  LEU A CB  
383  C CG  . LEU A 43  ? 0.18859 0.26258 0.09246 0.00897  0.05686  0.00035  43  LEU A CG  
384  C CD1 . LEU A 43  ? 0.19220 0.25393 0.12652 0.00560  0.08943  -0.00791 43  LEU A CD1 
385  C CD2 . LEU A 43  ? 0.22020 0.27053 0.09926 -0.00577 0.06778  0.01311  43  LEU A CD2 
386  N N   . VAL A 44  ? 0.19659 0.11338 0.08664 -0.03259 -0.00023 -0.01248 44  VAL A N   
387  C CA  . VAL A 44  ? 0.18951 0.14271 0.10455 -0.00750 -0.01305 -0.00877 44  VAL A CA  
388  C C   . VAL A 44  ? 0.16761 0.15037 0.10406 -0.01964 -0.00637 -0.02975 44  VAL A C   
389  O O   . VAL A 44  ? 0.17313 0.12514 0.12136 -0.03324 0.01550  -0.00405 44  VAL A O   
390  C CB  . VAL A 44  ? 0.18869 0.18124 0.09188 -0.01568 -0.02778 0.01285  44  VAL A CB  
391  C CG1 . VAL A 44  ? 0.20646 0.18320 0.08514 -0.00255 -0.03571 0.00866  44  VAL A CG1 
392  C CG2 . VAL A 44  ? 0.21403 0.18108 0.10228 -0.02566 -0.01755 0.03371  44  VAL A CG2 
393  N N   . CYS A 45  ? 0.15525 0.14271 0.10908 0.00131  0.03440  -0.01459 45  CYS A N   
394  C CA  . CYS A 45  ? 0.16052 0.15916 0.13118 0.00121  0.03734  -0.01101 45  CYS A CA  
395  C C   . CYS A 45  ? 0.14974 0.12283 0.13418 -0.00109 0.03206  -0.01512 45  CYS A C   
396  O O   . CYS A 45  ? 0.13746 0.12531 0.14603 -0.01603 -0.00048 -0.01750 45  CYS A O   
397  C CB  . CYS A 45  ? 0.15936 0.15005 0.12318 0.00238  0.00971  0.00898  45  CYS A CB  
398  S SG  . CYS A 45  ? 0.16026 0.15644 0.13833 -0.00866 0.00286  0.00877  45  CYS A SG  
399  N N   . GLY A 46  ? 0.14983 0.09825 0.11914 0.00937  0.05208  0.00913  46  GLY A N   
400  C CA  . GLY A 46  ? 0.14743 0.08106 0.09460 -0.02487 0.05373  0.01123  46  GLY A CA  
401  C C   . GLY A 46  ? 0.16241 0.11687 0.08501 -0.01627 0.04059  -0.00720 46  GLY A C   
402  O O   . GLY A 46  ? 0.17187 0.15264 0.07392 -0.00742 -0.00103 0.00043  46  GLY A O   
403  N N   . ILE A 47  ? 0.14470 0.13971 0.05631 -0.03865 0.02871  0.00089  47  ILE A N   
404  C CA  . ILE A 47  ? 0.14470 0.17260 0.06816 0.01129  0.02204  -0.00584 47  ILE A CA  
405  C C   . ILE A 47  ? 0.12948 0.14532 0.08372 -0.00264 0.02545  0.01389  47  ILE A C   
406  O O   . ILE A 47  ? 0.12836 0.14372 0.09439 -0.01863 0.02647  -0.00371 47  ILE A O   
407  C CB  . ILE A 47  ? 0.17095 0.15373 0.05891 -0.01204 -0.00853 0.00890  47  ILE A CB  
408  C CG1 . ILE A 47  ? 0.17633 0.16038 0.07625 0.00353  0.00598  0.02677  47  ILE A CG1 
409  C CG2 . ILE A 47  ? 0.16282 0.14981 0.05343 -0.03555 0.00819  -0.02153 47  ILE A CG2 
410  C CD1 . ILE A 47  ? 0.20282 0.20224 0.09261 -0.02442 0.00972  0.02472  47  ILE A CD1 
411  N N   . ALA A 48  ? 0.14983 0.14502 0.08364 0.01459  0.00895  0.03632  48  ALA A N   
412  C CA  . ALA A 48  ? 0.12426 0.15088 0.10368 -0.04061 0.03770  0.02199  48  ALA A CA  
413  C C   . ALA A 48  ? 0.12321 0.13293 0.12351 0.00570  0.03880  0.02694  48  ALA A C   
414  O O   . ALA A 48  ? 0.09403 0.16024 0.12959 0.00849  0.00335  0.02340  48  ALA A O   
415  C CB  . ALA A 48  ? 0.12408 0.14923 0.09153 -0.02216 0.05239  0.02953  48  ALA A CB  
416  N N   . TRP A 49  ? 0.12908 0.08592 0.14145 0.00357  0.05181  0.00963  49  TRP A N   
417  C CA  . TRP A 49  ? 0.17885 0.10622 0.17722 0.01324  0.05548  0.01309  49  TRP A CA  
418  C C   . TRP A 49  ? 0.16500 0.10004 0.17390 0.02568  0.05367  0.02101  49  TRP A C   
419  O O   . TRP A 49  ? 0.15781 0.12963 0.15275 0.02464  0.06991  -0.00480 49  TRP A O   
420  C CB  . TRP A 49  ? 0.16627 0.08489 0.22033 0.04682  0.04369  0.01853  49  TRP A CB  
421  C CG  . TRP A 49  ? 0.16000 0.12951 0.25759 0.03188  -0.00052 -0.02631 49  TRP A CG  
422  C CD1 . TRP A 49  ? 0.16870 0.10694 0.27902 0.02220  0.02205  -0.04329 49  TRP A CD1 
423  C CD2 . TRP A 49  ? 0.21515 0.19994 0.26252 0.06470  0.01249  -0.03328 49  TRP A CD2 
424  N NE1 . TRP A 49  ? 0.18083 0.10809 0.27081 0.01134  -0.00499 -0.07450 49  TRP A NE1 
425  C CE2 . TRP A 49  ? 0.20680 0.20012 0.26844 0.05009  -0.00422 -0.05602 49  TRP A CE2 
426  C CE3 . TRP A 49  ? 0.23507 0.28583 0.26747 0.10255  0.00782  -0.00664 49  TRP A CE3 
427  C CZ2 . TRP A 49  ? 0.26615 0.24810 0.28576 0.04194  -0.00766 -0.06528 49  TRP A CZ2 
428  C CZ3 . TRP A 49  ? 0.26326 0.29376 0.28620 0.08954  0.00179  -0.03579 49  TRP A CZ3 
429  C CH2 . TRP A 49  ? 0.29728 0.30498 0.30807 0.05736  0.00530  -0.05285 49  TRP A CH2 
430  N N   . TYR A 50  ? 0.17877 0.14467 0.18864 -0.03532 0.05097  -0.00039 50  TYR A N   
431  C CA  . TYR A 50  ? 0.19062 0.18767 0.20966 -0.01802 0.04389  0.01892  50  TYR A CA  
432  C C   . TYR A 50  ? 0.16221 0.15929 0.15310 -0.01005 0.04118  0.01155  50  TYR A C   
433  O O   . TYR A 50  ? 0.15141 0.15433 0.14726 0.01689  0.03761  0.01835  50  TYR A O   
434  C CB  . TYR A 50  ? 0.25146 0.22980 0.26121 0.00056  0.02418  0.01318  50  TYR A CB  
435  C CG  . TYR A 50  ? 0.33626 0.32612 0.31929 0.02389  0.02164  0.01025  50  TYR A CG  
436  C CD1 . TYR A 50  ? 0.39634 0.37740 0.36962 0.04059  0.04117  0.03481  50  TYR A CD1 
437  C CD2 . TYR A 50  ? 0.35791 0.37561 0.36023 0.01240  0.02652  0.00643  50  TYR A CD2 
438  C CE1 . TYR A 50  ? 0.44124 0.43285 0.42438 0.03616  0.06978  0.03326  50  TYR A CE1 
439  C CE2 . TYR A 50  ? 0.41763 0.43141 0.42220 -0.00183 0.06160  0.00524  50  TYR A CE2 
440  C CZ  . TYR A 50  ? 0.49716 0.50495 0.48985 0.00958  0.11748  0.02364  50  TYR A CZ  
441  O OH  . TYR A 50  ? 0.62361 0.66743 0.59889 0.00162  0.23094  0.03181  50  TYR A OH  
442  N N   . HIS A 51  ? 0.16504 0.10864 0.15438 -0.01511 0.07105  0.02935  51  HIS A N   
443  C CA  . HIS A 51  ? 0.17225 0.10301 0.17752 0.00884  0.06107  0.00562  51  HIS A CA  
444  C C   . HIS A 51  ? 0.15625 0.12249 0.17592 -0.00576 0.02038  0.01177  51  HIS A C   
445  O O   . HIS A 51  ? 0.15204 0.15808 0.17832 -0.04228 0.00757  0.00665  51  HIS A O   
446  C CB  . HIS A 51  ? 0.19205 0.13832 0.17385 0.02153  0.05842  0.01822  51  HIS A CB  
447  C CG  . HIS A 51  ? 0.21014 0.18337 0.17258 0.03331  0.07743  0.02667  51  HIS A CG  
448  N ND1 . HIS A 51  ? 0.19904 0.18624 0.16791 -0.00070 0.06535  0.01056  51  HIS A ND1 
449  C CD2 . HIS A 51  ? 0.23164 0.24912 0.16262 0.04776  0.07372  0.03650  51  HIS A CD2 
450  C CE1 . HIS A 51  ? 0.21309 0.23030 0.16484 0.02010  0.09921  0.04227  51  HIS A CE1 
451  N NE2 . HIS A 51  ? 0.23726 0.25843 0.15820 0.03922  0.08578  0.05340  51  HIS A NE2 
452  N N   . TYR A 52  ? 0.16508 0.11664 0.17405 0.01608  0.02361  0.01696  52  TYR A N   
453  C CA  . TYR A 52  ? 0.15272 0.12735 0.16149 0.01872  -0.00316 0.02530  52  TYR A CA  
454  C C   . TYR A 52  ? 0.13810 0.13644 0.17458 0.00719  -0.00726 0.01933  52  TYR A C   
455  O O   . TYR A 52  ? 0.15404 0.15290 0.18817 0.03506  0.01222  0.01042  52  TYR A O   
456  C CB  . TYR A 52  ? 0.10189 0.15070 0.15847 0.00711  -0.00922 0.02571  52  TYR A CB  
457  C CG  . TYR A 52  ? 0.08360 0.16680 0.19223 0.00813  0.00155  0.03710  52  TYR A CG  
458  C CD1 . TYR A 52  ? 0.08708 0.25487 0.21385 0.03007  0.00040  0.03575  52  TYR A CD1 
459  C CD2 . TYR A 52  ? 0.07475 0.16940 0.20879 0.02072  0.00136  0.00829  52  TYR A CD2 
460  C CE1 . TYR A 52  ? 0.10377 0.28161 0.22489 0.02340  0.00750  0.01273  52  TYR A CE1 
461  C CE2 . TYR A 52  ? 0.10085 0.20542 0.21208 0.03352  0.02255  -0.00423 52  TYR A CE2 
462  C CZ  . TYR A 52  ? 0.13263 0.25771 0.22281 0.03539  0.02243  -0.00480 52  TYR A CZ  
463  O OH  . TYR A 52  ? 0.15518 0.26128 0.21442 0.02107  0.03339  -0.03473 52  TYR A OH  
464  N N   A GLN A 53  ? 0.16213 0.13852 0.19224 0.02875  0.01231  0.03344  53  GLN A N   
465  N N   B GLN A 53  ? 0.15646 0.13965 0.17572 0.03239  0.01530  0.03931  53  GLN A N   
466  C CA  A GLN A 53  ? 0.17278 0.16552 0.21562 0.01767  0.02803  0.01305  53  GLN A CA  
467  C CA  B GLN A 53  ? 0.16678 0.16190 0.18358 0.03531  0.02686  0.03075  53  GLN A CA  
468  C C   A GLN A 53  ? 0.15560 0.16989 0.22459 -0.00639 0.02698  0.00377  53  GLN A C   
469  C C   B GLN A 53  ? 0.15632 0.17953 0.19949 0.01452  0.01039  0.01973  53  GLN A C   
470  O O   A GLN A 53  ? 0.16532 0.20020 0.23071 0.01564  0.04195  0.02004  53  GLN A O   
471  O O   B GLN A 53  ? 0.15636 0.19644 0.21482 0.02838  0.02046  0.02527  53  GLN A O   
472  C CB  A GLN A 53  ? 0.17890 0.18567 0.23014 0.02319  0.00806  0.00744  53  GLN A CB  
473  C CB  B GLN A 53  ? 0.17908 0.16097 0.18232 0.05185  0.02745  0.04187  53  GLN A CB  
474  C CG  A GLN A 53  ? 0.19485 0.17836 0.23798 0.03355  0.00724  -0.00628 53  GLN A CG  
475  C CG  B GLN A 53  ? 0.19261 0.15487 0.17612 0.07730  0.04350  0.02535  53  GLN A CG  
476  C CD  A GLN A 53  ? 0.24325 0.24125 0.24886 0.04762  0.05777  0.01470  53  GLN A CD  
477  O OE1 A GLN A 53  ? 0.22889 0.18483 0.26837 0.04189  0.03190  0.00285  53  GLN A OE1 
478  N NE2 A GLN A 53  ? 0.25455 0.25429 0.23845 0.03455  0.04798  0.03862  53  GLN A NE2 
479  N N   A LYS A 54  ? 0.14776 0.13505 0.23958 -0.03261 0.06201  -0.01615 54  LYS A N   
480  N N   B LYS A 54  ? 0.16080 0.17717 0.21055 -0.00683 0.03780  0.00114  54  LYS A N   
481  C CA  A LYS A 54  ? 0.15971 0.16866 0.25803 -0.03208 0.05440  -0.03899 54  LYS A CA  
482  C CA  B LYS A 54  ? 0.15764 0.19072 0.21021 -0.01576 0.05464  -0.01907 54  LYS A CA  
483  C C   A LYS A 54  ? 0.15842 0.16989 0.19474 -0.01538 0.04817  -0.03654 54  LYS A C   
484  C C   B LYS A 54  ? 0.15004 0.17483 0.18878 -0.00486 0.03982  -0.02530 54  LYS A C   
485  O O   A LYS A 54  ? 0.14385 0.16336 0.16933 -0.00015 0.04925  -0.02605 54  LYS A O   
486  O O   B LYS A 54  ? 0.14169 0.16261 0.18053 -0.00549 0.03975  -0.02170 54  LYS A O   
487  C CB  A LYS A 54  ? 0.20147 0.19664 0.31989 -0.03021 0.07039  -0.01612 54  LYS A CB  
488  C CB  B LYS A 54  ? 0.15513 0.20135 0.21044 -0.03027 0.08156  -0.00975 54  LYS A CB  
489  C CG  A LYS A 54  ? 0.25806 0.24482 0.36661 0.00472  0.08430  0.00033  54  LYS A CG  
490  C CG  B LYS A 54  ? 0.16067 0.20099 0.21629 -0.02448 0.08532  -0.00039 54  LYS A CG  
491  C CD  A LYS A 54  ? 0.30275 0.32735 0.40000 0.03293  0.08698  -0.01615 54  LYS A CD  
492  C CD  B LYS A 54  ? 0.19585 0.24132 0.22278 -0.00402 0.09125  0.00357  54  LYS A CD  
493  C CE  A LYS A 54  ? 0.37955 0.41253 0.45497 0.04723  0.09016  -0.02348 54  LYS A CE  
494  N NZ  A LYS A 54  ? 0.48806 0.54442 0.51379 0.02953  0.14440  -0.03409 54  LYS A NZ  
495  N N   . MET A 55  ? 0.14891 0.16448 0.18433 -0.00557 0.04421  -0.02335 55  MET A N   
496  C CA  . MET A 55  ? 0.14996 0.15534 0.19013 0.02515  0.04221  -0.02438 55  MET A CA  
497  C C   . MET A 55  ? 0.14099 0.16949 0.20815 0.01299  0.03324  0.01434  55  MET A C   
498  O O   . MET A 55  ? 0.14946 0.15750 0.19249 0.01417  0.02519  0.00791  55  MET A O   
499  C CB  . MET A 55  ? 0.14473 0.15634 0.19706 0.00912  0.06131  -0.03402 55  MET A CB  
500  C CG  . MET A 55  ? 0.15574 0.17382 0.20063 0.00997  0.03952  -0.01756 55  MET A CG  
501  S SD  . MET A 55  ? 0.17604 0.18698 0.22182 0.02146  0.02261  0.00507  55  MET A SD  
502  C CE  . MET A 55  ? 0.14930 0.16683 0.24431 -0.00422 0.02283  -0.04024 55  MET A CE  
503  N N   . GLY A 56  ? 0.14823 0.19559 0.22353 0.00883  0.03559  0.04927  56  GLY A N   
504  C CA  . GLY A 56  ? 0.15453 0.18914 0.22327 0.02716  0.00951  0.04349  56  GLY A CA  
505  C C   . GLY A 56  ? 0.16001 0.20585 0.21453 0.04296  -0.00396 0.01734  56  GLY A C   
506  O O   . GLY A 56  ? 0.18751 0.21003 0.22433 0.04251  -0.00029 0.04407  56  GLY A O   
507  N N   . ALA A 57  ? 0.16014 0.22528 0.22395 0.04018  0.01843  -0.04159 57  ALA A N   
508  C CA  . ALA A 57  ? 0.16495 0.22259 0.19465 0.03665  0.02011  -0.04747 57  ALA A CA  
509  C C   . ALA A 57  ? 0.16257 0.20824 0.16398 0.00944  0.03080  -0.04521 57  ALA A C   
510  O O   . ALA A 57  ? 0.19795 0.21760 0.15858 -0.01352 0.01658  -0.02207 57  ALA A O   
511  C CB  . ALA A 57  ? 0.16901 0.20825 0.20154 0.02175  0.03824  -0.05058 57  ALA A CB  
512  N N   . SER A 58  ? 0.14415 0.17550 0.13425 0.02545  -0.01058 -0.02398 58  SER A N   
513  C CA  . SER A 58  ? 0.16575 0.18981 0.15444 0.04170  -0.01846 -0.02045 58  SER A CA  
514  C C   . SER A 58  ? 0.16588 0.20105 0.16817 0.03234  -0.00885 -0.00513 58  SER A C   
515  O O   . SER A 58  ? 0.13058 0.24473 0.18934 0.01842  0.00085  -0.01439 58  SER A O   
516  C CB  . SER A 58  ? 0.17342 0.16212 0.15578 0.06517  0.00308  -0.00593 58  SER A CB  
517  O OG  . SER A 58  ? 0.16638 0.15298 0.16679 0.02488  0.00561  -0.04094 58  SER A OG  
518  N N   . TRP A 59  ? 0.17153 0.21098 0.16754 0.03894  -0.00987 0.03281  59  TRP A N   
519  C CA  . TRP A 59  ? 0.15509 0.22703 0.17521 0.03441  0.00930  0.02715  59  TRP A CA  
520  C C   . TRP A 59  ? 0.15156 0.28038 0.19865 0.03567  0.02634  0.03764  59  TRP A C   
521  O O   . TRP A 59  ? 0.17017 0.26351 0.17610 0.02566  0.00015  0.01888  59  TRP A O   
522  C CB  . TRP A 59  ? 0.14443 0.19956 0.17491 0.04974  -0.01732 0.01681  59  TRP A CB  
523  C CG  . TRP A 59  ? 0.14337 0.19578 0.20397 -0.00130 0.00100  -0.01161 59  TRP A CG  
524  C CD1 . TRP A 59  ? 0.15303 0.17008 0.20846 -0.02724 0.00012  -0.02416 59  TRP A CD1 
525  C CD2 . TRP A 59  ? 0.15696 0.21431 0.24049 -0.00705 0.01540  -0.02485 59  TRP A CD2 
526  N NE1 . TRP A 59  ? 0.18959 0.19497 0.23157 -0.02129 0.01952  -0.00836 59  TRP A NE1 
527  C CE2 . TRP A 59  ? 0.17363 0.19777 0.24187 -0.01332 -0.00207 -0.01208 59  TRP A CE2 
528  C CE3 . TRP A 59  ? 0.14615 0.18147 0.26647 -0.03858 -0.00268 -0.02693 59  TRP A CE3 
529  C CZ2 . TRP A 59  ? 0.19000 0.21459 0.26124 -0.01846 0.00244  -0.00237 59  TRP A CZ2 
530  C CZ3 . TRP A 59  ? 0.15103 0.21401 0.27291 -0.01198 -0.01276 -0.02480 59  TRP A CZ3 
531  C CH2 . TRP A 59  ? 0.17762 0.22649 0.27282 -0.00913 -0.00778 -0.02284 59  TRP A CH2 
532  N N   . GLU A 60  ? 0.12288 0.27460 0.25419 0.04046  0.00260  0.07704  60  GLU A N   
533  C CA  . GLU A 60  ? 0.14577 0.30949 0.30695 0.02327  -0.00756 0.09366  60  GLU A CA  
534  C C   . GLU A 60  ? 0.15359 0.30315 0.27792 0.00940  -0.00746 0.08766  60  GLU A C   
535  O O   . GLU A 60  ? 0.15240 0.32402 0.26508 0.00268  -0.00140 0.08630  60  GLU A O   
536  C CB  . GLU A 60  ? 0.20680 0.36187 0.37865 0.04818  0.00546  0.09792  60  GLU A CB  
537  C CG  . GLU A 60  ? 0.31637 0.42867 0.45949 0.01840  0.02683  0.07424  60  GLU A CG  
538  C CD  . GLU A 60  ? 0.40149 0.47571 0.53690 0.00796  0.02842  0.05399  60  GLU A CD  
539  O OE1 . GLU A 60  ? 0.41810 0.50683 0.54047 0.01099  0.04021  0.06401  60  GLU A OE1 
540  O OE2 . GLU A 60  ? 0.46814 0.56581 0.59634 -0.01265 0.04060  0.02253  60  GLU A OE2 
541  N N   . SER A 61  ? 0.15966 0.29698 0.27458 -0.00692 -0.00359 0.09539  61  SER A N   
542  C CA  . SER A 61  ? 0.13143 0.30777 0.26091 0.01747  -0.02118 0.11547  61  SER A CA  
543  C C   . SER A 61  ? 0.13850 0.33537 0.23851 -0.00630 -0.04067 0.13754  61  SER A C   
544  O O   . SER A 61  ? 0.15210 0.43553 0.27094 -0.03284 -0.03496 0.17902  61  SER A O   
545  C CB  . SER A 61  ? 0.12157 0.26085 0.28431 0.05126  -0.02400 0.08540  61  SER A CB  
546  O OG  . SER A 61  ? 0.13780 0.26494 0.31330 0.01113  0.00527  0.04958  61  SER A OG  
547  N N   . GLY A 62  ? 0.16499 0.32262 0.21297 -0.02897 -0.04716 0.11978  62  GLY A N   
548  C CA  . GLY A 62  ? 0.19514 0.28955 0.20565 -0.02946 -0.05965 0.07425  62  GLY A CA  
549  C C   . GLY A 62  ? 0.19687 0.29157 0.19150 -0.03523 -0.03137 0.03604  62  GLY A C   
550  O O   . GLY A 62  ? 0.24401 0.30355 0.21061 -0.04128 -0.00869 0.02571  62  GLY A O   
551  N N   A SER A 63  ? 0.13541 0.29045 0.17243 -0.00336 -0.05895 0.03617  63  SER A N   
552  N N   B SER A 63  ? 0.16477 0.31695 0.17959 -0.00694 -0.05685 0.03226  63  SER A N   
553  C CA  A SER A 63  ? 0.11856 0.25137 0.19311 -0.00967 -0.03452 0.03147  63  SER A CA  
554  C CA  B SER A 63  ? 0.15315 0.31386 0.18321 -0.01981 -0.03706 0.01949  63  SER A CA  
555  C C   A SER A 63  ? 0.13768 0.25559 0.18611 -0.04154 -0.02718 -0.01353 63  SER A C   
556  C C   B SER A 63  ? 0.14041 0.27636 0.19416 -0.03776 -0.04746 -0.01600 63  SER A C   
557  O O   A SER A 63  ? 0.16538 0.27916 0.20848 -0.03074 -0.01109 -0.02746 63  SER A O   
558  O O   B SER A 63  ? 0.13406 0.28543 0.23190 -0.01149 -0.06532 -0.02491 63  SER A O   
559  C CB  A SER A 63  ? 0.10278 0.21407 0.21835 0.03148  -0.01869 0.08040  63  SER A CB  
560  C CB  B SER A 63  ? 0.16937 0.33752 0.17731 -0.01110 -0.02022 0.04826  63  SER A CB  
561  O OG  A SER A 63  ? 0.10900 0.17920 0.23220 0.03601  0.00915  0.10183  63  SER A OG  
562  O OG  B SER A 63  ? 0.21329 0.34708 0.18715 -0.01348 0.00418  0.06658  63  SER A OG  
563  N N   . TYR A 64  ? 0.13181 0.23338 0.17643 -0.02632 -0.04963 -0.00818 64  TYR A N   
564  C CA  . TYR A 64  ? 0.14510 0.23615 0.18782 -0.01839 -0.02161 0.01927  64  TYR A CA  
565  C C   . TYR A 64  ? 0.15364 0.19073 0.18961 -0.05010 -0.00960 0.03561  64  TYR A C   
566  O O   . TYR A 64  ? 0.18035 0.17400 0.20467 -0.05478 -0.00084 0.02873  64  TYR A O   
567  C CB  . TYR A 64  ? 0.13625 0.22618 0.17939 -0.02170 -0.03747 0.00172  64  TYR A CB  
568  C CG  . TYR A 64  ? 0.12146 0.19951 0.15280 -0.02523 -0.06257 -0.01318 64  TYR A CG  
569  C CD1 . TYR A 64  ? 0.12808 0.15480 0.15458 -0.04282 -0.00808 -0.01838 64  TYR A CD1 
570  C CD2 . TYR A 64  ? 0.12634 0.17285 0.14404 -0.02564 -0.05320 0.00919  64  TYR A CD2 
571  C CE1 . TYR A 64  ? 0.14750 0.15603 0.14211 -0.04309 0.01233  -0.00983 64  TYR A CE1 
572  C CE2 . TYR A 64  ? 0.13907 0.18564 0.13056 -0.02955 -0.06825 0.01846  64  TYR A CE2 
573  C CZ  . TYR A 64  ? 0.15261 0.17796 0.12680 -0.04727 -0.02444 0.00479  64  TYR A CZ  
574  O OH  . TYR A 64  ? 0.17812 0.15964 0.10905 -0.04476 -0.00365 0.01596  64  TYR A OH  
575  N N   . ASP A 65  ? 0.14477 0.22324 0.19222 -0.04979 0.00450  0.03936  65  ASP A N   
576  C CA  . ASP A 65  ? 0.14533 0.24631 0.19110 -0.03410 0.01146  0.02050  65  ASP A CA  
577  C C   . ASP A 65  ? 0.14777 0.18267 0.18183 -0.02245 0.01570  0.03011  65  ASP A C   
578  O O   . ASP A 65  ? 0.14626 0.18132 0.18556 0.01578  0.01880  0.02431  65  ASP A O   
579  C CB  . ASP A 65  ? 0.17599 0.29359 0.18585 -0.00662 0.05917  0.03529  65  ASP A CB  
580  C CG  . ASP A 65  ? 0.17834 0.26088 0.18659 0.01893  0.06305  0.04204  65  ASP A CG  
581  O OD1 . ASP A 65  ? 0.16594 0.23153 0.16951 0.03306  0.06844  0.04768  65  ASP A OD1 
582  O OD2 . ASP A 65  ? 0.21094 0.33234 0.19149 0.04647  0.06697  0.06050  65  ASP A OD2 
583  N N   . THR A 66  ? 0.14895 0.16306 0.16948 0.01036  0.00175  0.02696  66  THR A N   
584  C CA  . THR A 66  ? 0.15650 0.11069 0.14379 0.01485  -0.00515 0.02739  66  THR A CA  
585  C C   . THR A 66  ? 0.19216 0.13154 0.15717 0.00594  0.00225  0.00868  66  THR A C   
586  O O   . THR A 66  ? 0.15655 0.17346 0.17696 0.00872  -0.02591 0.01600  66  THR A O   
587  C CB  . THR A 66  ? 0.13241 0.11481 0.11652 0.00358  -0.00946 0.02168  66  THR A CB  
588  O OG1 . THR A 66  ? 0.13957 0.14352 0.09439 -0.00377 -0.00693 -0.00059 66  THR A OG1 
589  C CG2 . THR A 66  ? 0.13357 0.12959 0.13340 -0.02682 0.01632  0.01054  66  THR A CG2 
590  N N   . GLY A 67  ? 0.21742 0.15618 0.13755 -0.00022 0.02727  0.00004  67  GLY A N   
591  C CA  . GLY A 67  ? 0.21501 0.16554 0.12381 -0.01499 0.04686  -0.02116 67  GLY A CA  
592  C C   . GLY A 67  ? 0.18887 0.17842 0.09084 -0.01678 0.03874  -0.00542 67  GLY A C   
593  O O   . GLY A 67  ? 0.19537 0.20487 0.08822 0.00213  0.02688  0.00528  67  GLY A O   
594  N N   . LEU A 68  ? 0.14932 0.17103 0.09896 0.00933  0.03040  -0.01003 68  LEU A N   
595  C CA  . LEU A 68  ? 0.14602 0.15894 0.10093 0.01292  0.01849  -0.00882 68  LEU A CA  
596  C C   . LEU A 68  ? 0.14919 0.15097 0.08718 -0.00983 0.02342  -0.01290 68  LEU A C   
597  O O   . LEU A 68  ? 0.19594 0.17554 0.09132 -0.00740 0.04502  -0.04314 68  LEU A O   
598  C CB  . LEU A 68  ? 0.13923 0.15383 0.12268 0.01694  -0.00999 0.01147  68  LEU A CB  
599  C CG  . LEU A 68  ? 0.15815 0.18929 0.15981 0.03387  0.00336  0.01182  68  LEU A CG  
600  C CD1 . LEU A 68  ? 0.13717 0.22569 0.16888 0.04598  -0.02712 0.01800  68  LEU A CD1 
601  C CD2 . LEU A 68  ? 0.18919 0.18476 0.19533 0.02695  0.03785  0.00056  68  LEU A CD2 
602  N N   . ARG A 69  ? 0.15857 0.13561 0.09258 -0.01387 0.04489  -0.01251 69  ARG A N   
603  C CA  . ARG A 69  ? 0.15689 0.15072 0.10696 -0.02041 0.03453  0.00252  69  ARG A CA  
604  C C   . ARG A 69  ? 0.18264 0.10130 0.12510 -0.04512 0.03264  0.00067  69  ARG A C   
605  O O   . ARG A 69  ? 0.16290 0.13009 0.14001 -0.03807 0.00026  0.00590  69  ARG A O   
606  C CB  . ARG A 69  ? 0.15966 0.18124 0.11092 -0.02835 0.04667  0.01733  69  ARG A CB  
607  C CG  . ARG A 69  ? 0.14867 0.19425 0.11250 -0.01518 0.03583  0.05064  69  ARG A CG  
608  C CD  . ARG A 69  ? 0.15309 0.18446 0.11245 -0.00066 0.02942  0.05055  69  ARG A CD  
609  N NE  . ARG A 69  ? 0.13999 0.14975 0.08411 0.01263  0.00865  0.05774  69  ARG A NE  
610  C CZ  . ARG A 69  ? 0.17667 0.14306 0.10784 0.03838  0.03030  0.04287  69  ARG A CZ  
611  N NH1 . ARG A 69  ? 0.22219 0.10770 0.13153 0.01008  0.04960  0.04638  69  ARG A NH1 
612  N NH2 . ARG A 69  ? 0.18039 0.15971 0.06841 0.03010  -0.00226 0.01566  69  ARG A NH2 
613  N N   . TYR A 70  ? 0.19750 0.08986 0.11645 0.00081  0.04084  0.00798  70  TYR A N   
614  C CA  . TYR A 70  ? 0.18557 0.06513 0.12832 -0.00397 0.02466  -0.01827 70  TYR A CA  
615  C C   . TYR A 70  ? 0.16769 0.07745 0.14579 -0.01484 -0.00517 -0.03369 70  TYR A C   
616  O O   . TYR A 70  ? 0.16535 0.15163 0.12569 0.01318  -0.05579 -0.01351 70  TYR A O   
617  C CB  . TYR A 70  ? 0.17227 0.10053 0.11793 -0.00934 0.04245  -0.02463 70  TYR A CB  
618  C CG  . TYR A 70  ? 0.16447 0.09995 0.13621 0.00963  0.03724  -0.01692 70  TYR A CG  
619  C CD1 . TYR A 70  ? 0.17811 0.11749 0.13636 -0.00971 0.04470  0.00008  70  TYR A CD1 
620  C CD2 . TYR A 70  ? 0.12701 0.13571 0.14039 0.04249  0.02862  0.00963  70  TYR A CD2 
621  C CE1 . TYR A 70  ? 0.15160 0.13496 0.14335 -0.01820 0.03888  0.01350  70  TYR A CE1 
622  C CE2 . TYR A 70  ? 0.13244 0.14678 0.13612 0.01759  0.01999  0.03879  70  TYR A CE2 
623  C CZ  . TYR A 70  ? 0.14939 0.15711 0.13598 0.01081  0.02533  0.02245  70  TYR A CZ  
624  O OH  . TYR A 70  ? 0.15970 0.18571 0.11525 0.02123  0.01679  0.01185  70  TYR A OH  
625  N N   A VAL A 71  ? 0.17261 0.09917 0.15122 -0.01723 0.02487  -0.03123 71  VAL A N   
626  N N   B VAL A 71  ? 0.14138 0.09234 0.14105 -0.01969 0.02614  -0.03605 71  VAL A N   
627  C CA  A VAL A 71  ? 0.17753 0.11165 0.16198 -0.00282 0.02936  -0.01446 71  VAL A CA  
628  C CA  B VAL A 71  ? 0.11638 0.09500 0.14481 -0.00477 0.01598  -0.02273 71  VAL A CA  
629  C C   A VAL A 71  ? 0.17486 0.11996 0.16318 -0.01211 0.03637  0.00627  71  VAL A C   
630  C C   B VAL A 71  ? 0.11960 0.10054 0.15456 -0.00045 0.01614  -0.01907 71  VAL A C   
631  O O   A VAL A 71  ? 0.19243 0.16532 0.16870 -0.00533 0.04489  0.03824  71  VAL A O   
632  O O   B VAL A 71  ? 0.10084 0.13484 0.15607 0.01953  0.00130  -0.01372 71  VAL A O   
633  C CB  A VAL A 71  ? 0.18159 0.15749 0.16506 0.04050  0.04562  -0.01988 71  VAL A CB  
634  C CB  B VAL A 71  ? 0.09181 0.14337 0.12614 0.01743  0.02885  -0.01075 71  VAL A CB  
635  C CG1 A VAL A 71  ? 0.18453 0.17911 0.17239 0.08608  0.05092  -0.02467 71  VAL A CG1 
636  C CG1 B VAL A 71  ? 0.08296 0.13303 0.13305 0.01124  0.02229  0.00372  71  VAL A CG1 
637  C CG2 A VAL A 71  ? 0.17935 0.17128 0.16437 0.01935  0.03606  -0.00404 71  VAL A CG2 
638  C CG2 B VAL A 71  ? 0.07640 0.18055 0.09581 0.02230  0.03010  -0.00566 71  VAL A CG2 
639  N N   . ASP A 72  ? 0.15380 0.08232 0.15342 -0.02542 0.05347  -0.00997 72  ASP A N   
640  C CA  . ASP A 72  ? 0.15825 0.09474 0.14490 0.00930  0.02798  -0.00362 72  ASP A CA  
641  C C   . ASP A 72  ? 0.16570 0.11679 0.13753 0.03362  0.02436  0.00224  72  ASP A C   
642  O O   . ASP A 72  ? 0.16460 0.15679 0.12379 0.03846  0.00669  0.01073  72  ASP A O   
643  C CB  . ASP A 72  ? 0.17333 0.09846 0.15837 -0.00794 -0.00104 -0.03936 72  ASP A CB  
644  C CG  . ASP A 72  ? 0.19383 0.12076 0.19523 0.00543  -0.03888 -0.03250 72  ASP A CG  
645  O OD1 . ASP A 72  ? 0.21277 0.13647 0.23045 -0.01349 -0.05430 -0.03805 72  ASP A OD1 
646  O OD2 . ASP A 72  ? 0.20189 0.18129 0.20874 -0.00008 -0.05158 -0.02479 72  ASP A OD2 
647  N N   . TRP A 73  ? 0.15035 0.09928 0.11684 0.02634  0.02801  0.03636  73  TRP A N   
648  C CA  . TRP A 73  ? 0.15527 0.08569 0.11353 -0.00208 0.00688  0.02478  73  TRP A CA  
649  C C   . TRP A 73  ? 0.17982 0.10332 0.09727 -0.00159 -0.00047 0.00914  73  TRP A C   
650  O O   . TRP A 73  ? 0.17515 0.13933 0.09887 0.01784  -0.00673 0.01759  73  TRP A O   
651  C CB  . TRP A 73  ? 0.16055 0.09665 0.10336 -0.01292 0.00707  -0.00794 73  TRP A CB  
652  C CG  . TRP A 73  ? 0.13210 0.11784 0.10822 -0.02537 0.00885  -0.00805 73  TRP A CG  
653  C CD1 . TRP A 73  ? 0.11519 0.14896 0.11057 0.00072  -0.01264 0.00301  73  TRP A CD1 
654  C CD2 . TRP A 73  ? 0.12873 0.13144 0.10410 -0.00938 0.00262  -0.02791 73  TRP A CD2 
655  N NE1 . TRP A 73  ? 0.13396 0.11494 0.11199 -0.00542 0.01956  -0.03581 73  TRP A NE1 
656  C CE2 . TRP A 73  ? 0.13388 0.12518 0.11424 -0.00687 -0.00123 -0.00841 73  TRP A CE2 
657  C CE3 . TRP A 73  ? 0.15492 0.13341 0.10000 -0.00040 -0.00408 -0.05040 73  TRP A CE3 
658  C CZ2 . TRP A 73  ? 0.15569 0.12240 0.10245 -0.00894 0.02147  -0.02187 73  TRP A CZ2 
659  C CZ3 . TRP A 73  ? 0.14943 0.19462 0.11011 -0.01970 -0.02009 -0.03091 73  TRP A CZ3 
660  C CH2 . TRP A 73  ? 0.15033 0.16495 0.10130 -0.01144 0.02546  -0.01891 73  TRP A CH2 
661  N N   . VAL A 74  ? 0.16717 0.11686 0.10064 -0.00254 -0.02014 0.00557  74  VAL A N   
662  C CA  . VAL A 74  ? 0.18569 0.13712 0.12953 -0.00983 0.01650  0.04328  74  VAL A CA  
663  C C   . VAL A 74  ? 0.17146 0.13546 0.15590 0.00404  0.02155  0.04590  74  VAL A C   
664  O O   . VAL A 74  ? 0.17184 0.16482 0.16895 0.00324  0.02832  0.03601  74  VAL A O   
665  C CB  . VAL A 74  ? 0.20422 0.18245 0.12944 -0.01143 0.04304  0.07779  74  VAL A CB  
666  C CG1 . VAL A 74  ? 0.17380 0.19183 0.12755 -0.03140 0.03668  0.07166  74  VAL A CG1 
667  C CG2 . VAL A 74  ? 0.21232 0.21682 0.14013 -0.02362 0.04172  0.08170  74  VAL A CG2 
668  N N   . LEU A 75  ? 0.17260 0.13659 0.15257 -0.02008 0.02942  0.01733  75  LEU A N   
669  C CA  . LEU A 75  ? 0.18702 0.17086 0.15757 -0.02325 0.00282  -0.01320 75  LEU A CA  
670  C C   . LEU A 75  ? 0.18387 0.20315 0.16622 -0.01463 -0.00015 -0.01427 75  LEU A C   
671  O O   . LEU A 75  ? 0.22583 0.28442 0.17515 -0.05464 -0.01381 -0.02620 75  LEU A O   
672  C CB  . LEU A 75  ? 0.19605 0.17006 0.15094 -0.02971 -0.01655 -0.03490 75  LEU A CB  
673  C CG  . LEU A 75  ? 0.21532 0.24033 0.16660 -0.00278 -0.02715 -0.02434 75  LEU A CG  
674  C CD1 . LEU A 75  ? 0.23017 0.23868 0.14221 -0.01611 -0.01078 -0.06151 75  LEU A CD1 
675  C CD2 . LEU A 75  ? 0.24942 0.26759 0.20211 0.01674  -0.01749 0.01216  75  LEU A CD2 
676  N N   . THR A 76  ? 0.16148 0.13725 0.15371 -0.00097 0.03737  -0.01054 76  THR A N   
677  C CA  . THR A 76  ? 0.14765 0.12398 0.13431 -0.00237 0.02434  -0.00072 76  THR A CA  
678  C C   . THR A 76  ? 0.18410 0.12495 0.12324 0.00697  0.02713  -0.00466 76  THR A C   
679  O O   . THR A 76  ? 0.17582 0.13778 0.12941 0.01692  0.02973  0.01589  76  THR A O   
680  C CB  . THR A 76  ? 0.15295 0.13490 0.10121 0.01860  0.03175  -0.00235 76  THR A CB  
681  O OG1 . THR A 76  ? 0.17837 0.16618 0.09867 0.00604  0.00567  0.00005  76  THR A OG1 
682  C CG2 . THR A 76  ? 0.18440 0.15641 0.10085 0.04826  0.03743  -0.00162 76  THR A CG2 
683  N N   . VAL A 77  ? 0.18741 0.09152 0.12708 0.03957  0.04013  0.03678  77  VAL A N   
684  C CA  . VAL A 77  ? 0.19316 0.10983 0.12323 0.03144  -0.01141 0.00784  77  VAL A CA  
685  C C   . VAL A 77  ? 0.17930 0.11383 0.11218 0.03459  0.00303  0.02343  77  VAL A C   
686  O O   . VAL A 77  ? 0.18905 0.13951 0.10029 0.03561  0.01315  0.00427  77  VAL A O   
687  C CB  . VAL A 77  ? 0.20956 0.11618 0.13032 0.02092  -0.00484 -0.00724 77  VAL A CB  
688  C CG1 . VAL A 77  ? 0.21247 0.14259 0.12359 0.00785  0.01052  -0.02822 77  VAL A CG1 
689  C CG2 . VAL A 77  ? 0.21746 0.13070 0.10283 0.01315  -0.02630 -0.01561 77  VAL A CG2 
690  N N   . PRO A 78  ? 0.17214 0.18332 0.13714 0.00208  -0.00455 0.00323  78  PRO A N   
691  C CA  . PRO A 78  ? 0.19941 0.20373 0.13131 -0.00016 -0.01343 0.00709  78  PRO A CA  
692  C C   . PRO A 78  ? 0.20205 0.20665 0.13057 0.03512  -0.00130 0.01347  78  PRO A C   
693  O O   . PRO A 78  ? 0.17624 0.18757 0.14016 -0.00958 -0.00814 -0.00606 78  PRO A O   
694  C CB  . PRO A 78  ? 0.21347 0.22322 0.15318 -0.05406 -0.02910 0.00952  78  PRO A CB  
695  C CG  . PRO A 78  ? 0.24922 0.24020 0.20189 -0.04593 0.00138  0.02251  78  PRO A CG  
696  C CD  . PRO A 78  ? 0.20574 0.19959 0.17266 -0.01572 -0.00125 0.02297  78  PRO A CD  
697  N N   A LEU A 79  ? 0.21921 0.18548 0.14157 0.05994  0.02322  0.00751  79  LEU A N   
698  N N   B LEU A 79  ? 0.22582 0.19082 0.14928 0.06043  0.02172  0.00870  79  LEU A N   
699  C CA  A LEU A 79  ? 0.21596 0.17208 0.15490 0.06806  -0.00332 0.00894  79  LEU A CA  
700  C CA  B LEU A 79  ? 0.23002 0.18612 0.16812 0.06254  -0.00428 0.01456  79  LEU A CA  
701  C C   A LEU A 79  ? 0.21766 0.17699 0.16792 0.04933  -0.04420 0.00364  79  LEU A C   
702  C C   B LEU A 79  ? 0.21509 0.20107 0.17165 0.04414  -0.04836 0.00163  79  LEU A C   
703  O O   A LEU A 79  ? 0.21255 0.17706 0.17332 0.06406  -0.07321 -0.00391 79  LEU A O   
704  O O   B LEU A 79  ? 0.19226 0.22707 0.17247 0.04669  -0.07326 -0.01363 79  LEU A O   
705  C CB  A LEU A 79  ? 0.21159 0.17788 0.15314 0.06654  0.00479  -0.00428 79  LEU A CB  
706  C CB  B LEU A 79  ? 0.24524 0.19161 0.17927 0.04810  0.01032  0.00541  79  LEU A CB  
707  C CG  A LEU A 79  ? 0.17533 0.16488 0.14902 0.06459  -0.01567 0.00286  79  LEU A CG  
708  C CG  B LEU A 79  ? 0.22908 0.18219 0.18074 0.03391  -0.01496 0.01139  79  LEU A CG  
709  C CD1 A LEU A 79  ? 0.18864 0.18842 0.15038 0.07765  0.00403  0.01475  79  LEU A CD1 
710  C CD1 B LEU A 79  ? 0.21834 0.18112 0.17124 0.01861  -0.03029 -0.00289 79  LEU A CD1 
711  C CD2 A LEU A 79  ? 0.16482 0.17937 0.16079 0.05408  -0.01459 -0.01136 79  LEU A CD2 
712  C CD2 B LEU A 79  ? 0.22511 0.19272 0.18336 0.02640  -0.02048 0.00788  79  LEU A CD2 
713  N N   . MET A 80  ? 0.19712 0.16116 0.18017 0.03555  -0.06481 0.01054  80  MET A N   
714  C CA  . MET A 80  ? 0.19291 0.17403 0.18966 -0.01204 -0.05807 0.02469  80  MET A CA  
715  C C   . MET A 80  ? 0.15949 0.12741 0.18232 -0.03395 -0.06948 0.04690  80  MET A C   
716  O O   . MET A 80  ? 0.18008 0.18829 0.18986 -0.06057 -0.02586 0.04028  80  MET A O   
717  C CB  . MET A 80  ? 0.17274 0.19977 0.16280 -0.02748 -0.06180 0.04361  80  MET A CB  
718  C CG  . MET A 80  ? 0.18994 0.20838 0.16735 -0.02571 -0.01856 0.02628  80  MET A CG  
719  S SD  . MET A 80  ? 0.21332 0.23399 0.17146 -0.00612 0.01328  0.03682  80  MET A SD  
720  C CE  . MET A 80  ? 0.24451 0.22221 0.19424 -0.05851 0.05813  0.04404  80  MET A CE  
721  N N   . PHE A 81  ? 0.15045 0.11691 0.19427 -0.00338 -0.07185 0.03580  81  PHE A N   
722  C CA  . PHE A 81  ? 0.16001 0.16098 0.21183 0.03487  -0.07291 0.00772  81  PHE A CA  
723  C C   . PHE A 81  ? 0.21486 0.19472 0.23496 0.07481  -0.05813 -0.00595 81  PHE A C   
724  O O   . PHE A 81  ? 0.18069 0.20202 0.20657 0.03866  -0.07574 -0.00939 81  PHE A O   
725  C CB  . PHE A 81  ? 0.16653 0.17196 0.21379 0.04343  -0.06703 0.00156  81  PHE A CB  
726  C CG  . PHE A 81  ? 0.17267 0.17727 0.20474 0.01961  -0.06814 -0.00660 81  PHE A CG  
727  C CD1 . PHE A 81  ? 0.19564 0.15933 0.18136 -0.00686 -0.06826 -0.00058 81  PHE A CD1 
728  C CD2 . PHE A 81  ? 0.17950 0.19867 0.20508 0.01200  -0.06477 -0.01355 81  PHE A CD2 
729  C CE1 . PHE A 81  ? 0.21321 0.16565 0.20139 -0.03725 -0.06185 -0.01203 81  PHE A CE1 
730  C CE2 . PHE A 81  ? 0.21334 0.23096 0.20648 0.01453  -0.04637 -0.00342 81  PHE A CE2 
731  C CZ  . PHE A 81  ? 0.21570 0.19512 0.20631 -0.00571 -0.06287 -0.00261 81  PHE A CZ  
732  N N   A VAL A 82  ? 0.25403 0.22440 0.24506 0.07692  -0.06414 -0.02138 82  VAL A N   
733  N N   B VAL A 82  ? 0.24314 0.22969 0.24746 0.06468  -0.06183 -0.01521 82  VAL A N   
734  C CA  A VAL A 82  ? 0.27740 0.23667 0.25970 0.08136  -0.04410 -0.02238 82  VAL A CA  
735  C CA  B VAL A 82  ? 0.26642 0.25731 0.25971 0.04594  -0.03040 -0.01614 82  VAL A CA  
736  C C   A VAL A 82  ? 0.31596 0.23680 0.27364 0.04673  -0.04093 -0.00579 82  VAL A C   
737  C C   B VAL A 82  ? 0.30042 0.27308 0.27858 0.02430  -0.01974 -0.01068 82  VAL A C   
738  O O   A VAL A 82  ? 0.30566 0.21521 0.27814 -0.02063 -0.07865 -0.00251 82  VAL A O   
739  O O   B VAL A 82  ? 0.31198 0.26359 0.29269 -0.00389 -0.04228 -0.01277 82  VAL A O   
740  C CB  A VAL A 82  ? 0.26362 0.25064 0.24780 0.09089  -0.03599 -0.03743 82  VAL A CB  
741  C CB  B VAL A 82  ? 0.26029 0.26043 0.24855 0.04111  -0.01701 -0.01627 82  VAL A CB  
742  C CG1 A VAL A 82  ? 0.27804 0.24555 0.26469 0.14414  -0.01934 -0.05456 82  VAL A CG1 
743  C CG1 B VAL A 82  ? 0.26553 0.25795 0.25416 0.05924  -0.01219 -0.02357 82  VAL A CG1 
744  C CG2 A VAL A 82  ? 0.25805 0.29120 0.23972 0.04499  -0.03914 -0.02116 82  VAL A CG2 
745  C CG2 B VAL A 82  ? 0.26063 0.27375 0.24263 0.02325  -0.01278 0.00089  82  VAL A CG2 
746  N N   A GLU A 83  ? 0.33561 0.25920 0.29531 0.07323  -0.01998 0.00200  83  GLU A N   
747  N N   B GLU A 83  ? 0.30727 0.28303 0.29562 0.04106  -0.01780 0.00139  83  GLU A N   
748  C CA  A GLU A 83  ? 0.36616 0.33564 0.33912 0.06969  0.00531  0.00515  83  GLU A CA  
749  C CA  B GLU A 83  ? 0.34575 0.33495 0.33282 0.04376  0.00875  0.00396  83  GLU A CA  
750  C C   A GLU A 83  ? 0.32447 0.27418 0.28099 0.04817  -0.02643 -0.02630 83  GLU A C   
751  C C   B GLU A 83  ? 0.30675 0.26906 0.28794 0.03269  -0.03489 -0.01154 83  GLU A C   
752  O O   A GLU A 83  ? 0.33024 0.28802 0.26126 0.02072  -0.04543 -0.06303 83  GLU A O   
753  O O   B GLU A 83  ? 0.31591 0.28787 0.28102 0.02122  -0.03949 -0.03142 83  GLU A O   
754  C CB  A GLU A 83  ? 0.42952 0.41949 0.41880 0.06744  0.01977  0.04057  83  GLU A CB  
755  C CB  B GLU A 83  ? 0.41754 0.41101 0.40342 0.04722  0.06293  0.01914  83  GLU A CB  
756  C CG  A GLU A 83  ? 0.49668 0.49251 0.48773 0.05016  0.03506  0.05675  83  GLU A CG  
757  C CD  A GLU A 83  ? 0.50502 0.44984 0.49290 0.03030  0.00749  0.06824  83  GLU A CD  
758  O OE1 A GLU A 83  ? 0.48862 0.45989 0.47504 0.03432  0.00536  0.07629  83  GLU A OE1 
759  O OE2 A GLU A 83  ? 0.50813 0.39298 0.49758 0.01404  -0.01002 0.07412  83  GLU A OE2 
760  N N   . VAL A 84  ? 0.27456 0.20929 0.24646 0.02197  -0.06188 -0.01893 84  VAL A N   
761  C CA  . VAL A 84  ? 0.25544 0.22303 0.24055 0.02659  -0.02997 -0.00698 84  VAL A CA  
762  C C   . VAL A 84  ? 0.22700 0.23489 0.22426 0.03111  -0.02692 -0.00883 84  VAL A C   
763  O O   . VAL A 84  ? 0.22491 0.27627 0.24325 0.03360  0.00064  0.02944  84  VAL A O   
764  C CB  . VAL A 84  ? 0.26467 0.19488 0.25169 0.01834  -0.04957 -0.01232 84  VAL A CB  
765  C CG1 . VAL A 84  ? 0.27051 0.20751 0.27763 0.03817  -0.02413 -0.03843 84  VAL A CG1 
766  C CG2 . VAL A 84  ? 0.25459 0.20940 0.23621 0.00604  -0.07358 0.00499  84  VAL A CG2 
767  N N   . LEU A 85  ? 0.21276 0.19294 0.17556 0.03016  -0.01363 -0.03536 85  LEU A N   
768  C CA  . LEU A 85  ? 0.19360 0.16962 0.16254 0.01078  0.00640  -0.05647 85  LEU A CA  
769  C C   . LEU A 85  ? 0.21178 0.22573 0.13389 -0.00695 0.00385  -0.03404 85  LEU A C   
770  O O   . LEU A 85  ? 0.23022 0.24092 0.16106 -0.01104 -0.00238 -0.02600 85  LEU A O   
771  C CB  . LEU A 85  ? 0.19762 0.15808 0.15334 0.01826  0.00220  -0.05376 85  LEU A CB  
772  C CG  . LEU A 85  ? 0.17605 0.20022 0.17816 0.01074  0.00157  -0.03413 85  LEU A CG  
773  C CD1 . LEU A 85  ? 0.18853 0.18158 0.19265 -0.00083 0.01486  -0.01826 85  LEU A CD1 
774  C CD2 . LEU A 85  ? 0.19201 0.21867 0.18266 0.02722  -0.02724 -0.02552 85  LEU A CD2 
775  N N   . ALA A 86  ? 0.18618 0.20417 0.12644 -0.02289 -0.00258 -0.03783 86  ALA A N   
776  C CA  . ALA A 86  ? 0.19519 0.22575 0.14852 -0.00111 0.01317  0.01175  86  ALA A CA  
777  C C   . ALA A 86  ? 0.21273 0.25246 0.16807 -0.01534 0.00389  0.00662  86  ALA A C   
778  O O   . ALA A 86  ? 0.22903 0.29571 0.15843 -0.02021 0.00390  -0.01284 86  ALA A O   
779  C CB  . ALA A 86  ? 0.19675 0.23629 0.14748 0.01547  0.00716  0.06124  86  ALA A CB  
780  N N   . VAL A 87  ? 0.22382 0.24811 0.18626 0.00647  0.04783  0.00322  87  VAL A N   
781  C CA  . VAL A 87  ? 0.19855 0.26944 0.19499 0.00690  0.03635  0.01407  87  VAL A CA  
782  C C   . VAL A 87  ? 0.17645 0.29092 0.20081 -0.01520 0.03762  -0.01121 87  VAL A C   
783  O O   . VAL A 87  ? 0.15889 0.30560 0.23351 -0.03339 0.02810  -0.01642 87  VAL A O   
784  C CB  . VAL A 87  ? 0.24410 0.30717 0.19661 0.03984  0.05864  0.03623  87  VAL A CB  
785  C CG1 . VAL A 87  ? 0.25848 0.31328 0.17508 0.08622  0.03064  0.03805  87  VAL A CG1 
786  C CG2 . VAL A 87  ? 0.25441 0.27649 0.20626 0.02735  0.08693  0.06245  87  VAL A CG2 
787  N N   . THR A 88  ? 0.18841 0.29582 0.18537 0.01500  0.04613  0.00135  88  THR A N   
788  C CA  . THR A 88  ? 0.21888 0.29274 0.19023 0.03525  0.02902  0.01296  88  THR A CA  
789  C C   . THR A 88  ? 0.22366 0.32150 0.20589 0.02624  0.01009  -0.01650 88  THR A C   
790  O O   . THR A 88  ? 0.21346 0.36420 0.19312 0.02839  -0.02240 0.01545  88  THR A O   
791  C CB  . THR A 88  ? 0.24669 0.29036 0.18495 0.01665  0.03849  0.02303  88  THR A CB  
792  O OG1 . THR A 88  ? 0.25930 0.31014 0.18649 0.00950  0.04767  0.02437  88  THR A OG1 
793  C CG2 . THR A 88  ? 0.28628 0.29482 0.20218 0.01260  0.04137  0.01244  88  THR A CG2 
794  N N   . ARG A 89  ? 0.20935 0.28657 0.23324 0.00737  0.00294  -0.04715 89  ARG A N   
795  C CA  . ARG A 89  ? 0.21978 0.30228 0.23652 -0.00397 -0.01402 -0.03806 89  ARG A CA  
796  C C   . ARG A 89  ? 0.21785 0.33842 0.21862 -0.03392 -0.05727 -0.03873 89  ARG A C   
797  O O   . ARG A 89  ? 0.20701 0.35471 0.23334 -0.04867 -0.05676 -0.05853 89  ARG A O   
798  C CB  . ARG A 89  ? 0.28259 0.33414 0.25307 -0.02045 0.03182  -0.02729 89  ARG A CB  
799  C CG  . ARG A 89  ? 0.34363 0.37401 0.28152 -0.04441 0.03957  -0.03179 89  ARG A CG  
800  C CD  . ARG A 89  ? 0.36857 0.40064 0.29830 -0.04238 0.03853  -0.02298 89  ARG A CD  
801  N NE  . ARG A 89  ? 0.39327 0.41289 0.30560 -0.02387 0.02561  -0.02610 89  ARG A NE  
802  C CZ  . ARG A 89  ? 0.41735 0.45045 0.33251 0.04323  0.00388  -0.02756 89  ARG A CZ  
803  N NH1 . ARG A 89  ? 0.40912 0.46502 0.32721 0.04567  0.01166  -0.02872 89  ARG A NH1 
804  N NH2 . ARG A 89  ? 0.43688 0.46859 0.35027 0.08043  -0.03086 -0.03529 89  ARG A NH2 
805  N N   . LYS A 90  ? 0.20889 0.36209 0.21782 -0.05194 -0.07408 -0.03989 90  LYS A N   
806  C CA  . LYS A 90  ? 0.21799 0.34368 0.19627 -0.05254 -0.08394 -0.01770 90  LYS A CA  
807  C C   . LYS A 90  ? 0.23354 0.34799 0.19965 -0.04736 -0.06360 -0.00432 90  LYS A C   
808  O O   . LYS A 90  ? 0.26384 0.34580 0.22192 -0.04187 -0.02143 -0.00795 90  LYS A O   
809  C CB  . LYS A 90  ? 0.24764 0.34553 0.20240 -0.05637 -0.05311 -0.00956 90  LYS A CB  
810  C CG  . LYS A 90  ? 0.21650 0.32998 0.22910 -0.04702 -0.07163 -0.03084 90  LYS A CG  
811  C CD  . LYS A 90  ? 0.20859 0.30608 0.24650 -0.04414 -0.07492 -0.06538 90  LYS A CD  
812  C CE  . LYS A 90  ? 0.23537 0.29908 0.27390 -0.02470 -0.06966 -0.06164 90  LYS A CE  
813  N NZ  . LYS A 90  ? 0.27463 0.29129 0.30518 -0.00156 -0.05604 -0.03784 90  LYS A NZ  
814  N N   . GLY A 91  ? 0.22643 0.32502 0.17706 -0.03917 -0.05744 0.01191  91  GLY A N   
815  C CA  . GLY A 91  ? 0.21125 0.30575 0.17578 -0.02667 -0.05523 0.04115  91  GLY A CA  
816  C C   . GLY A 91  ? 0.23577 0.29951 0.15078 0.00613  -0.05116 0.05843  91  GLY A C   
817  O O   . GLY A 91  ? 0.23548 0.26290 0.13376 0.03244  -0.03174 0.06710  91  GLY A O   
818  N N   . ALA A 92  ? 0.28206 0.30624 0.16820 0.01852  -0.05345 0.03873  92  ALA A N   
819  C CA  . ALA A 92  ? 0.33485 0.29931 0.18972 0.03640  -0.08190 0.02321  92  ALA A CA  
820  C C   . ALA A 92  ? 0.36779 0.27450 0.20137 0.04048  -0.08791 -0.00681 92  ALA A C   
821  O O   . ALA A 92  ? 0.40387 0.24852 0.21357 0.00186  -0.12215 -0.02340 92  ALA A O   
822  C CB  . ALA A 92  ? 0.35237 0.32221 0.20662 0.06547  -0.07756 0.03421  92  ALA A CB  
823  N N   . ALA A 93  ? 0.32693 0.29508 0.19359 0.09287  -0.08929 -0.01356 93  ALA A N   
824  C CA  . ALA A 93  ? 0.29012 0.30238 0.18748 0.11839  -0.08105 0.00266  93  ALA A CA  
825  C C   . ALA A 93  ? 0.25161 0.28098 0.16916 0.10702  -0.05067 0.01886  93  ALA A C   
826  O O   . ALA A 93  ? 0.25870 0.26350 0.15564 0.10822  -0.05923 0.02566  93  ALA A O   
827  C CB  . ALA A 93  ? 0.29856 0.29360 0.21078 0.14160  -0.07925 -0.02165 93  ALA A CB  
828  N N   . TYR A 94  ? 0.20393 0.24639 0.16018 0.06442  -0.03602 0.02484  94  TYR A N   
829  C CA  . TYR A 94  ? 0.19593 0.20919 0.15969 0.00423  -0.02827 -0.00322 94  TYR A CA  
830  C C   . TYR A 94  ? 0.21693 0.21606 0.15707 -0.01997 -0.01813 -0.04156 94  TYR A C   
831  O O   . TYR A 94  ? 0.20827 0.23432 0.15106 -0.03406 0.00657  -0.05328 94  TYR A O   
832  C CB  . TYR A 94  ? 0.18857 0.20738 0.17327 -0.02037 -0.03162 0.00522  94  TYR A CB  
833  C CG  . TYR A 94  ? 0.22410 0.19947 0.18605 -0.02338 -0.04193 0.00342  94  TYR A CG  
834  C CD1 . TYR A 94  ? 0.23593 0.18975 0.19401 0.00697  -0.05120 0.00634  94  TYR A CD1 
835  C CD2 . TYR A 94  ? 0.24686 0.22148 0.20047 -0.02777 -0.04979 -0.00831 94  TYR A CD2 
836  C CE1 . TYR A 94  ? 0.26298 0.24079 0.20449 0.02752  -0.03722 -0.01166 94  TYR A CE1 
837  C CE2 . TYR A 94  ? 0.25797 0.23288 0.20619 0.01676  -0.05640 -0.00422 94  TYR A CE2 
838  C CZ  . TYR A 94  ? 0.26130 0.25755 0.20869 0.05251  -0.05614 -0.01101 94  TYR A CZ  
839  O OH  . TYR A 94  ? 0.28593 0.29516 0.23168 0.08317  -0.04120 -0.01975 94  TYR A OH  
840  N N   . ASN A 95  ? 0.26828 0.22568 0.18254 -0.02436 -0.01238 -0.04727 95  ASN A N   
841  C CA  . ASN A 95  ? 0.31266 0.25839 0.20129 -0.02628 -0.00121 -0.04578 95  ASN A CA  
842  C C   . ASN A 95  ? 0.32931 0.25125 0.21704 -0.04885 -0.01580 -0.03290 95  ASN A C   
843  O O   . ASN A 95  ? 0.34864 0.27098 0.23893 -0.05996 0.00285  -0.02965 95  ASN A O   
844  C CB  . ASN A 95  ? 0.34808 0.30066 0.19220 -0.00822 0.02671  -0.04167 95  ASN A CB  
845  C CG  . ASN A 95  ? 0.37889 0.33222 0.20154 -0.00428 0.02086  -0.03864 95  ASN A CG  
846  O OD1 . ASN A 95  ? 0.41954 0.33405 0.20747 -0.01793 0.04857  -0.06087 95  ASN A OD1 
847  N ND2 . ASN A 95  ? 0.38397 0.36143 0.18640 -0.00554 0.01097  -0.04139 95  ASN A ND2 
848  N N   . GLU A 96  ? 0.34519 0.24526 0.21602 -0.00527 -0.04294 -0.00911 96  GLU A N   
849  C CA  . GLU A 96  ? 0.37664 0.25992 0.24540 0.01941  -0.05937 0.00042  96  GLU A CA  
850  C C   . GLU A 96  ? 0.30842 0.22754 0.20297 0.03317  -0.07693 0.00935  96  GLU A C   
851  O O   . GLU A 96  ? 0.30518 0.23645 0.19371 0.02093  -0.04448 -0.00024 96  GLU A O   
852  C CB  . GLU A 96  ? 0.44960 0.29952 0.29889 0.03165  -0.06855 0.00843  96  GLU A CB  
853  C CG  . GLU A 96  ? 0.48202 0.35627 0.34100 0.02915  -0.06940 0.00658  96  GLU A CG  
854  C CD  . GLU A 96  ? 0.53414 0.42771 0.38984 0.05545  -0.06374 0.01265  96  GLU A CD  
855  O OE1 . GLU A 96  ? 0.59014 0.50306 0.42911 0.08082  -0.04638 0.03281  96  GLU A OE1 
856  O OE2 . GLU A 96  ? 0.56341 0.46571 0.39529 0.08463  -0.05756 0.00671  96  GLU A OE2 
857  N N   . ALA A 97  ? 0.26412 0.18660 0.16708 0.04122  -0.09227 0.01790  97  ALA A N   
858  C CA  . ALA A 97  ? 0.21681 0.19913 0.15366 0.00113  -0.07211 0.00901  97  ALA A CA  
859  C C   . ALA A 97  ? 0.19821 0.18840 0.15036 -0.01529 -0.06474 0.01436  97  ALA A C   
860  O O   . ALA A 97  ? 0.18137 0.21183 0.14780 -0.00689 -0.04226 0.01174  97  ALA A O   
861  C CB  . ALA A 97  ? 0.19616 0.18714 0.14436 0.01059  -0.07238 0.01100  97  ALA A CB  
862  N N   . VAL A 98  ? 0.20255 0.14663 0.15026 -0.00013 -0.05035 0.00732  98  VAL A N   
863  C CA  . VAL A 98  ? 0.22774 0.13197 0.15441 0.00024  -0.03945 -0.02902 98  VAL A CA  
864  C C   . VAL A 98  ? 0.27393 0.18685 0.17385 -0.01940 -0.02704 -0.05473 98  VAL A C   
865  O O   . VAL A 98  ? 0.29694 0.19490 0.20472 -0.04446 -0.02518 -0.04201 98  VAL A O   
866  C CB  . VAL A 98  ? 0.23649 0.15606 0.19265 0.02080  -0.03545 -0.03034 98  VAL A CB  
867  C CG1 . VAL A 98  ? 0.27953 0.22452 0.19587 0.01185  -0.04362 -0.05687 98  VAL A CG1 
868  C CG2 . VAL A 98  ? 0.27625 0.20350 0.21294 0.01101  -0.00097 -0.01290 98  VAL A CG2 
869  N N   . ARG A 99  ? 0.27397 0.19432 0.15566 -0.06022 -0.05114 -0.06470 99  ARG A N   
870  C CA  . ARG A 99  ? 0.30427 0.24843 0.15107 -0.06133 -0.04234 -0.03343 99  ARG A CA  
871  C C   . ARG A 99  ? 0.30890 0.21270 0.10002 -0.03027 -0.01164 -0.01589 99  ARG A C   
872  O O   . ARG A 99  ? 0.32133 0.19916 0.08440 -0.00227 0.02247  -0.01315 99  ARG A O   
873  C CB  . ARG A 99  ? 0.31634 0.27509 0.17668 -0.06286 -0.08220 0.01075  99  ARG A CB  
874  C CG  . ARG A 99  ? 0.36795 0.31357 0.23660 -0.04874 -0.07802 0.03608  99  ARG A CG  
875  C CD  . ARG A 99  ? 0.43057 0.35111 0.30379 -0.04468 -0.03758 0.04857  99  ARG A CD  
876  N NE  . ARG A 99  ? 0.48470 0.39240 0.34164 -0.03897 -0.01999 0.04316  99  ARG A NE  
877  C CZ  . ARG A 99  ? 0.57834 0.46262 0.36779 -0.00953 0.02449  0.03478  99  ARG A CZ  
878  N NH1 . ARG A 99  ? 0.61709 0.49457 0.39679 0.00331  0.01363  0.01655  99  ARG A NH1 
879  N NH2 . ARG A 99  ? 0.57948 0.45597 0.34844 -0.00662 0.03238  0.03915  99  ARG A NH2 
880  N N   . ASN A 100 ? 0.27994 0.14936 0.09815 -0.01775 -0.03230 0.01046  100 ASN A N   
881  C CA  . ASN A 100 ? 0.27040 0.15620 0.12609 -0.02024 -0.05473 0.01531  100 ASN A CA  
882  C C   . ASN A 100 ? 0.23560 0.13648 0.12879 -0.05242 -0.05306 -0.00191 100 ASN A C   
883  O O   . ASN A 100 ? 0.25988 0.15161 0.14041 -0.03355 -0.04553 0.01047  100 ASN A O   
884  C CB  . ASN A 100 ? 0.26800 0.17759 0.13880 0.03229  -0.08085 0.03746  100 ASN A CB  
885  C CG  . ASN A 100 ? 0.30615 0.24171 0.15286 0.03694  -0.08513 0.05637  100 ASN A CG  
886  O OD1 . ASN A 100 ? 0.32523 0.25069 0.16127 0.01218  -0.07410 0.04163  100 ASN A OD1 
887  N ND2 . ASN A 100 ? 0.30822 0.26559 0.18242 0.04333  -0.10751 0.05525  100 ASN A ND2 
888  N N   . TRP A 101 ? 0.18508 0.16803 0.13215 -0.02250 -0.01938 0.00438  101 TRP A N   
889  C CA  . TRP A 101 ? 0.17274 0.13472 0.12912 -0.00045 -0.03604 0.00499  101 TRP A CA  
890  C C   . TRP A 101 ? 0.18877 0.10979 0.12774 -0.02218 -0.01684 -0.02275 101 TRP A C   
891  O O   . TRP A 101 ? 0.20700 0.15073 0.16004 -0.04569 0.00900  -0.03199 101 TRP A O   
892  C CB  . TRP A 101 ? 0.13609 0.16740 0.13442 -0.00478 -0.06717 0.00393  101 TRP A CB  
893  C CG  . TRP A 101 ? 0.15810 0.19396 0.15512 0.01046  -0.05220 -0.00051 101 TRP A CG  
894  C CD1 . TRP A 101 ? 0.15556 0.21347 0.17135 0.01571  -0.05133 0.00577  101 TRP A CD1 
895  C CD2 . TRP A 101 ? 0.17043 0.20986 0.15617 0.04048  -0.04675 -0.01158 101 TRP A CD2 
896  N NE1 . TRP A 101 ? 0.17780 0.22574 0.17507 0.00002  -0.06147 -0.00693 101 TRP A NE1 
897  C CE2 . TRP A 101 ? 0.17385 0.20592 0.15919 0.02314  -0.05218 -0.00494 101 TRP A CE2 
898  C CE3 . TRP A 101 ? 0.19241 0.20704 0.15489 0.05555  -0.03068 -0.01815 101 TRP A CE3 
899  C CZ2 . TRP A 101 ? 0.20623 0.22066 0.16188 0.00525  -0.02539 -0.01216 101 TRP A CZ2 
900  C CZ3 . TRP A 101 ? 0.21893 0.22963 0.16166 0.03894  -0.01080 -0.02204 101 TRP A CZ3 
901  C CH2 . TRP A 101 ? 0.22702 0.22541 0.16847 0.03052  -0.01590 -0.00993 101 TRP A CH2 
902  N N   . GLY A 102 ? 0.20152 0.11664 0.10377 -0.00146 0.01754  -0.00541 102 GLY A N   
903  C CA  . GLY A 102 ? 0.18328 0.14913 0.09609 -0.01101 -0.00598 -0.00301 102 GLY A CA  
904  C C   . GLY A 102 ? 0.16974 0.17768 0.09615 -0.01808 -0.02104 -0.01338 102 GLY A C   
905  O O   . GLY A 102 ? 0.18094 0.21473 0.09660 -0.00297 -0.01395 -0.02098 102 GLY A O   
906  N N   . ILE A 103 ? 0.18432 0.18020 0.11942 -0.02956 -0.02038 0.00358  103 ILE A N   
907  C CA  . ILE A 103 ? 0.22867 0.19706 0.13152 -0.02478 0.00844  0.01950  103 ILE A CA  
908  C C   . ILE A 103 ? 0.20755 0.17210 0.11099 -0.01664 -0.01737 0.02880  103 ILE A C   
909  O O   . ILE A 103 ? 0.21065 0.18367 0.11944 -0.01857 -0.00557 0.05484  103 ILE A O   
910  C CB  . ILE A 103 ? 0.27305 0.23089 0.14646 -0.02794 0.01367  0.04266  103 ILE A CB  
911  C CG1 . ILE A 103 ? 0.28812 0.29563 0.14549 -0.00487 0.01884  0.05021  103 ILE A CG1 
912  C CG2 . ILE A 103 ? 0.29613 0.23429 0.17335 -0.05834 0.03803  0.05582  103 ILE A CG2 
913  C CD1 . ILE A 103 ? 0.31816 0.35749 0.14426 -0.01850 0.00163  0.04536  103 ILE A CD1 
914  N N   . ALA A 104 ? 0.20978 0.14902 0.07298 -0.01102 -0.01274 0.01907  104 ALA A N   
915  C CA  . ALA A 104 ? 0.19893 0.14025 0.07296 0.00853  0.02565  0.00690  104 ALA A CA  
916  C C   . ALA A 104 ? 0.19391 0.14264 0.07225 0.00591  -0.00220 0.01073  104 ALA A C   
917  O O   . ALA A 104 ? 0.19261 0.13173 0.09366 -0.01213 -0.01020 0.03105  104 ALA A O   
918  C CB  . ALA A 104 ? 0.20076 0.13274 0.05942 0.00361  0.02655  -0.01576 104 ALA A CB  
919  N N   . ALA A 105 ? 0.18105 0.12156 0.07474 0.01926  0.01240  0.01552  105 ALA A N   
920  C CA  . ALA A 105 ? 0.19946 0.12041 0.08802 0.02060  0.00812  -0.00770 105 ALA A CA  
921  C C   . ALA A 105 ? 0.20285 0.15185 0.06168 -0.01596 -0.00024 -0.01068 105 ALA A C   
922  O O   . ALA A 105 ? 0.19504 0.13551 0.06860 -0.00639 0.02919  -0.02532 105 ALA A O   
923  C CB  . ALA A 105 ? 0.19961 0.13286 0.10468 -0.00617 0.01006  -0.00043 105 ALA A CB  
924  N N   . THR A 106 ? 0.18652 0.14192 0.06157 -0.01854 -0.00395 -0.01885 106 THR A N   
925  C CA  . THR A 106 ? 0.18290 0.15160 0.08018 0.00460  -0.01611 -0.00881 106 THR A CA  
926  C C   . THR A 106 ? 0.14521 0.15047 0.07726 0.00856  -0.01719 0.01946  106 THR A C   
927  O O   . THR A 106 ? 0.15383 0.17451 0.09688 -0.00756 -0.01336 0.00313  106 THR A O   
928  C CB  . THR A 106 ? 0.21529 0.18788 0.09231 -0.01998 0.01042  0.02080  106 THR A CB  
929  O OG1 . THR A 106 ? 0.23925 0.19819 0.10647 -0.02003 0.03487  0.02839  106 THR A OG1 
930  C CG2 . THR A 106 ? 0.21714 0.19349 0.10134 -0.01318 0.02382  0.04080  106 THR A CG2 
931  N N   . VAL A 107 ? 0.14699 0.14485 0.07290 -0.00857 -0.00782 0.00698  107 VAL A N   
932  C CA  . VAL A 107 ? 0.19273 0.13054 0.07837 0.00905  -0.02084 0.02119  107 VAL A CA  
933  C C   . VAL A 107 ? 0.18961 0.15510 0.09945 0.01987  0.00665  0.03178  107 VAL A C   
934  O O   . VAL A 107 ? 0.15550 0.15552 0.10908 0.00232  -0.01173 0.03145  107 VAL A O   
935  C CB  . VAL A 107 ? 0.23067 0.13325 0.09848 -0.01815 -0.02782 0.04208  107 VAL A CB  
936  C CG1 . VAL A 107 ? 0.28404 0.11781 0.10826 0.00087  -0.00990 0.02290  107 VAL A CG1 
937  C CG2 . VAL A 107 ? 0.23918 0.17959 0.11518 -0.00082 -0.01256 0.07935  107 VAL A CG2 
938  N N   . MET A 108 ? 0.18251 0.14413 0.10053 0.01385  0.02721  0.04565  108 MET A N   
939  C CA  . MET A 108 ? 0.16931 0.11370 0.10066 -0.00937 0.01918  0.02969  108 MET A CA  
940  C C   . MET A 108 ? 0.16697 0.10227 0.11371 0.00401  0.02511  0.03409  108 MET A C   
941  O O   . MET A 108 ? 0.17688 0.12831 0.12151 0.00646  0.01755  0.00987  108 MET A O   
942  C CB  . MET A 108 ? 0.14451 0.11187 0.09567 -0.00656 0.00762  0.02401  108 MET A CB  
943  C CG  . MET A 108 ? 0.14969 0.11302 0.10968 -0.00257 -0.00125 0.02803  108 MET A CG  
944  S SD  . MET A 108 ? 0.16181 0.15258 0.12464 0.01455  -0.00490 0.02324  108 MET A SD  
945  C CE  . MET A 108 ? 0.19710 0.13140 0.07952 -0.00936 0.01359  0.02769  108 MET A CE  
946  N N   . ILE A 109 ? 0.13251 0.07896 0.12504 0.01014  0.02248  0.01739  109 ILE A N   
947  C CA  . ILE A 109 ? 0.12365 0.08489 0.14843 0.02853  0.01935  -0.00465 109 ILE A CA  
948  C C   . ILE A 109 ? 0.14201 0.15728 0.15050 -0.00262 0.00454  -0.02632 109 ILE A C   
949  O O   . ILE A 109 ? 0.16115 0.15756 0.12966 -0.01738 -0.01442 -0.02537 109 ILE A O   
950  C CB  . ILE A 109 ? 0.15319 0.07245 0.18313 0.01576  0.03736  -0.01606 109 ILE A CB  
951  C CG1 . ILE A 109 ? 0.19357 0.09518 0.17619 0.00079  -0.00128 -0.00856 109 ILE A CG1 
952  C CG2 . ILE A 109 ? 0.12715 0.07406 0.20687 0.01185  0.03857  -0.02901 109 ILE A CG2 
953  C CD1 . ILE A 109 ? 0.25318 0.19019 0.19228 0.02984  0.00667  0.01415  109 ILE A CD1 
954  N N   . GLY A 110 ? 0.12786 0.13944 0.13931 0.01417  0.01317  -0.04480 110 GLY A N   
955  C CA  . GLY A 110 ? 0.15852 0.14053 0.14199 -0.01165 0.02789  -0.06018 110 GLY A CA  
956  C C   . GLY A 110 ? 0.15081 0.12464 0.12697 -0.02316 0.01323  -0.03324 110 GLY A C   
957  O O   . GLY A 110 ? 0.16270 0.13943 0.11707 -0.01814 0.02681  -0.01273 110 GLY A O   
958  N N   . ALA A 111 ? 0.15334 0.09808 0.13549 -0.01908 0.02547  -0.04693 111 ALA A N   
959  C CA  . ALA A 111 ? 0.16622 0.13335 0.16002 0.01643  0.01919  -0.03156 111 ALA A CA  
960  C C   . ALA A 111 ? 0.17682 0.15904 0.12939 0.00133  0.01203  -0.01178 111 ALA A C   
961  O O   . ALA A 111 ? 0.15586 0.11679 0.13511 -0.02635 -0.01346 -0.02794 111 ALA A O   
962  C CB  . ALA A 111 ? 0.15117 0.13572 0.18485 0.01091  0.00593  -0.05119 111 ALA A CB  
963  N N   . GLY A 112 ? 0.18990 0.14737 0.11486 0.01084  0.03045  0.02872  112 GLY A N   
964  C CA  . GLY A 112 ? 0.19525 0.13728 0.10966 -0.01005 0.05669  0.04516  112 GLY A CA  
965  C C   . GLY A 112 ? 0.16210 0.11309 0.12046 -0.01126 0.03906  0.02887  112 GLY A C   
966  O O   . GLY A 112 ? 0.16701 0.14843 0.12931 0.01084  0.03128  0.07622  112 GLY A O   
967  N N   . TYR A 113 ? 0.12533 0.14750 0.16449 -0.00020 0.05509  0.02801  113 TYR A N   
968  C CA  . TYR A 113 ? 0.12616 0.13827 0.20496 -0.00710 0.03007  -0.01725 113 TYR A CA  
969  C C   . TYR A 113 ? 0.11937 0.13900 0.19859 -0.03437 0.01971  -0.00831 113 TYR A C   
970  O O   . TYR A 113 ? 0.15740 0.16120 0.19352 -0.03198 0.01779  -0.01288 113 TYR A O   
971  C CB  . TYR A 113 ? 0.11391 0.14856 0.22575 -0.01333 0.01709  -0.02914 113 TYR A CB  
972  C CG  . TYR A 113 ? 0.11636 0.20117 0.25415 -0.02350 0.01503  -0.03590 113 TYR A CG  
973  C CD1 . TYR A 113 ? 0.11260 0.20425 0.24883 0.02969  -0.02230 -0.02525 113 TYR A CD1 
974  C CD2 . TYR A 113 ? 0.14720 0.24041 0.27164 -0.01265 0.01628  -0.03082 113 TYR A CD2 
975  C CE1 . TYR A 113 ? 0.14021 0.24303 0.25143 0.05270  -0.00973 -0.03394 113 TYR A CE1 
976  C CE2 . TYR A 113 ? 0.18757 0.22859 0.28017 0.06289  0.01846  -0.01800 113 TYR A CE2 
977  C CZ  . TYR A 113 ? 0.17066 0.23858 0.28164 0.10591  0.00509  -0.03666 113 TYR A CZ  
978  O OH  . TYR A 113 ? 0.22876 0.26714 0.31010 0.08045  0.02636  -0.07213 113 TYR A OH  
979  N N   . TYR A 114 ? 0.15410 0.12889 0.20849 -0.05388 0.01493  -0.00834 114 TYR A N   
980  C CA  . TYR A 114 ? 0.17083 0.14839 0.19937 -0.06165 -0.00697 0.02558  114 TYR A CA  
981  C C   . TYR A 114 ? 0.18958 0.14855 0.18888 -0.04932 -0.02380 0.01832  114 TYR A C   
982  O O   . TYR A 114 ? 0.21570 0.17804 0.18941 -0.03066 -0.03167 0.00952  114 TYR A O   
983  C CB  . TYR A 114 ? 0.19978 0.16679 0.22367 -0.05111 0.00659  0.05281  114 TYR A CB  
984  C CG  . TYR A 114 ? 0.21546 0.17530 0.24406 -0.05817 0.00783  0.04230  114 TYR A CG  
985  C CD1 . TYR A 114 ? 0.26248 0.16487 0.24272 -0.07485 0.03502  0.05644  114 TYR A CD1 
986  C CD2 . TYR A 114 ? 0.24639 0.17916 0.26058 -0.05548 0.01653  0.04719  114 TYR A CD2 
987  C CE1 . TYR A 114 ? 0.29142 0.15646 0.25273 -0.09761 0.04538  0.03759  114 TYR A CE1 
988  C CE2 . TYR A 114 ? 0.28886 0.17330 0.27321 -0.07168 0.04599  0.04876  114 TYR A CE2 
989  C CZ  . TYR A 114 ? 0.33443 0.17799 0.28431 -0.10420 0.07190  0.02335  114 TYR A CZ  
990  O OH  . TYR A 114 ? 0.37009 0.19669 0.31703 -0.11947 0.09497  -0.00380 114 TYR A OH  
991  N N   . GLY A 115 ? 0.20210 0.13379 0.17874 -0.02644 -0.02806 0.02153  115 GLY A N   
992  C CA  . GLY A 115 ? 0.19116 0.11292 0.20653 -0.00997 0.00396  -0.00741 115 GLY A CA  
993  C C   . GLY A 115 ? 0.15266 0.08766 0.20695 -0.01561 -0.00182 0.01465  115 GLY A C   
994  O O   . GLY A 115 ? 0.17761 0.11806 0.21868 -0.02464 0.03477  0.01171  115 GLY A O   
995  N N   . GLU A 116 ? 0.14540 0.09946 0.21490 0.00395  0.01977  0.04958  116 GLU A N   
996  C CA  . GLU A 116 ? 0.13515 0.12409 0.23822 -0.03223 -0.00493 0.05109  116 GLU A CA  
997  C C   . GLU A 116 ? 0.15222 0.13880 0.26507 -0.03651 -0.00370 0.00563  116 GLU A C   
998  O O   . GLU A 116 ? 0.15696 0.14910 0.27892 -0.00992 -0.00678 -0.00307 116 GLU A O   
999  C CB  . GLU A 116 ? 0.16139 0.13910 0.23742 -0.04823 -0.03306 0.05573  116 GLU A CB  
1000 C CG  . GLU A 116 ? 0.15860 0.12240 0.23419 -0.03207 -0.01881 0.05885  116 GLU A CG  
1001 C CD  . GLU A 116 ? 0.16861 0.13831 0.23889 -0.01172 -0.01985 0.01939  116 GLU A CD  
1002 O OE1 . GLU A 116 ? 0.17640 0.13707 0.24909 0.00240  -0.01487 0.02151  116 GLU A OE1 
1003 O OE2 . GLU A 116 ? 0.12613 0.15343 0.23825 0.01612  -0.04473 -0.01348 116 GLU A OE2 
1004 N N   . THR A 117 ? 0.15455 0.15197 0.30077 -0.05992 -0.00748 0.01379  117 THR A N   
1005 C CA  . THR A 117 ? 0.14736 0.19226 0.32110 -0.04108 0.01203  -0.01201 117 THR A CA  
1006 C C   . THR A 117 ? 0.18040 0.19438 0.33984 -0.05608 0.02710  -0.05295 117 THR A C   
1007 O O   . THR A 117 ? 0.19061 0.23134 0.35451 -0.07531 0.06941  -0.04935 117 THR A O   
1008 C CB  . THR A 117 ? 0.15184 0.23807 0.31755 -0.02508 -0.01160 -0.01388 117 THR A CB  
1009 O OG1 . THR A 117 ? 0.15139 0.28194 0.34499 -0.03478 0.01947  -0.04109 117 THR A OG1 
1010 C CG2 . THR A 117 ? 0.15608 0.24289 0.30367 -0.01610 -0.00241 -0.01787 117 THR A CG2 
1011 N N   . SER A 118 ? 0.22501 0.19058 0.33699 -0.07151 -0.00642 -0.06733 118 SER A N   
1012 C CA  . SER A 118 ? 0.24139 0.17675 0.34041 -0.07718 -0.05615 -0.05027 118 SER A CA  
1013 C C   . SER A 118 ? 0.23575 0.21069 0.33931 -0.04836 -0.07114 -0.07183 118 SER A C   
1014 O O   . SER A 118 ? 0.26915 0.25558 0.34983 -0.04139 -0.06029 -0.04809 118 SER A O   
1015 C CB  . SER A 118 ? 0.26093 0.19321 0.35260 -0.09252 -0.07951 -0.03227 118 SER A CB  
1016 O OG  . SER A 118 ? 0.28479 0.23210 0.37968 -0.09559 -0.07304 0.00938  118 SER A OG  
1017 N N   . ALA A 119 ? 0.22886 0.24471 0.33950 -0.03728 -0.08531 -0.07158 119 ALA A N   
1018 C CA  . ALA A 119 ? 0.24073 0.26560 0.34534 -0.03009 -0.10119 -0.07529 119 ALA A CA  
1019 C C   . ALA A 119 ? 0.24463 0.24670 0.35661 0.00266  -0.10318 -0.05046 119 ALA A C   
1020 O O   . ALA A 119 ? 0.18795 0.20849 0.35872 0.01826  -0.11520 -0.06115 119 ALA A O   
1021 C CB  . ALA A 119 ? 0.24817 0.26851 0.33934 -0.06451 -0.09097 -0.07821 119 ALA A CB  
1022 N N   . ALA A 120 ? 0.29169 0.27467 0.34283 0.02818  -0.11239 -0.01975 120 ALA A N   
1023 C CA  . ALA A 120 ? 0.31723 0.23739 0.31125 0.03298  -0.09038 -0.01412 120 ALA A CA  
1024 C C   . ALA A 120 ? 0.29308 0.22312 0.28384 0.01519  -0.08964 -0.03470 120 ALA A C   
1025 O O   . ALA A 120 ? 0.28821 0.28037 0.28415 0.02299  -0.08676 -0.06047 120 ALA A O   
1026 C CB  . ALA A 120 ? 0.35873 0.22602 0.32510 0.00906  -0.06944 -0.01162 120 ALA A CB  
1027 N N   . GLY A 121 ? 0.26859 0.19540 0.27360 -0.02781 -0.07292 -0.00977 121 GLY A N   
1028 C CA  . GLY A 121 ? 0.28055 0.20686 0.28324 -0.04689 -0.08891 -0.00664 121 GLY A CA  
1029 C C   . GLY A 121 ? 0.26903 0.20596 0.27812 -0.05507 -0.09508 0.00375  121 GLY A C   
1030 O O   . GLY A 121 ? 0.27395 0.21667 0.25506 -0.02518 -0.14035 0.02600  121 GLY A O   
1031 N N   . SER A 122 ? 0.22424 0.19390 0.29149 -0.04658 -0.06732 -0.00154 122 SER A N   
1032 C CA  . SER A 122 ? 0.24303 0.19996 0.30281 -0.02173 -0.03805 -0.00062 122 SER A CA  
1033 C C   . SER A 122 ? 0.25262 0.14978 0.28891 -0.05434 -0.03253 0.01946  122 SER A C   
1034 O O   . SER A 122 ? 0.23125 0.16479 0.27440 -0.03633 -0.06048 0.01560  122 SER A O   
1035 C CB  . SER A 122 ? 0.20411 0.23702 0.30163 -0.02547 -0.05911 -0.02221 122 SER A CB  
1036 O OG  . SER A 122 ? 0.18772 0.25148 0.27840 -0.04411 -0.06778 -0.04214 122 SER A OG  
1037 N N   . ASN A 123 ? 0.25695 0.12860 0.29709 -0.08512 -0.02428 0.03265  123 ASN A N   
1038 C CA  . ASN A 123 ? 0.24771 0.13224 0.30599 -0.08431 -0.02719 0.03179  123 ASN A CA  
1039 C C   . ASN A 123 ? 0.21121 0.14401 0.31266 -0.07761 -0.02336 0.00465  123 ASN A C   
1040 O O   . ASN A 123 ? 0.18703 0.14485 0.33080 -0.03639 -0.00307 0.02431  123 ASN A O   
1041 C CB  . ASN A 123 ? 0.26015 0.13896 0.32384 -0.05770 -0.03867 0.03478  123 ASN A CB  
1042 C CG  . ASN A 123 ? 0.28011 0.16765 0.34896 0.00545  -0.02878 0.01850  123 ASN A CG  
1043 O OD1 . ASN A 123 ? 0.26652 0.18045 0.39660 0.03403  -0.03205 -0.01084 123 ASN A OD1 
1044 N ND2 . ASN A 123 ? 0.30567 0.19419 0.33911 0.02977  -0.04785 0.03298  123 ASN A ND2 
1045 N N   . GLU A 124 ? 0.18177 0.18213 0.30784 -0.06022 -0.01860 0.00529  124 GLU A N   
1046 C CA  . GLU A 124 ? 0.16640 0.15997 0.31190 -0.05001 -0.03568 0.00877  124 GLU A CA  
1047 C C   . GLU A 124 ? 0.15107 0.14001 0.28236 -0.01532 -0.00561 0.01157  124 GLU A C   
1048 O O   . GLU A 124 ? 0.16339 0.12571 0.28409 -0.01718 0.01309  0.03531  124 GLU A O   
1049 C CB  . GLU A 124 ? 0.22060 0.25159 0.33864 -0.05820 -0.03533 0.01513  124 GLU A CB  
1050 C CG  . GLU A 124 ? 0.25083 0.29759 0.37012 -0.05354 -0.05006 0.02655  124 GLU A CG  
1051 C CD  . GLU A 124 ? 0.34212 0.34801 0.41791 -0.06320 -0.02621 0.03072  124 GLU A CD  
1052 O OE1 . GLU A 124 ? 0.31806 0.38888 0.39943 -0.06976 -0.02519 0.04101  124 GLU A OE1 
1053 O OE2 . GLU A 124 ? 0.42522 0.33959 0.47802 -0.04910 -0.01535 0.00233  124 GLU A OE2 
1054 N N   . TYR A 125 ? 0.12687 0.14169 0.25682 -0.01853 -0.01571 -0.01230 125 TYR A N   
1055 C CA  . TYR A 125 ? 0.10353 0.16430 0.21340 -0.00653 -0.03477 0.01405  125 TYR A CA  
1056 C C   . TYR A 125 ? 0.12247 0.15764 0.21375 -0.00322 -0.01857 -0.00290 125 TYR A C   
1057 O O   . TYR A 125 ? 0.13234 0.16147 0.18691 -0.01221 -0.00857 -0.00279 125 TYR A O   
1058 C CB  . TYR A 125 ? 0.14776 0.19368 0.20872 -0.01689 -0.03702 0.01117  125 TYR A CB  
1059 C CG  . TYR A 125 ? 0.16844 0.15989 0.20106 -0.00733 -0.04752 0.03689  125 TYR A CG  
1060 C CD1 . TYR A 125 ? 0.17111 0.13285 0.18148 -0.02736 -0.06158 0.06116  125 TYR A CD1 
1061 C CD2 . TYR A 125 ? 0.18224 0.11878 0.20791 -0.00231 -0.06174 0.01942  125 TYR A CD2 
1062 C CE1 . TYR A 125 ? 0.18204 0.14308 0.18119 -0.02345 -0.05881 0.03727  125 TYR A CE1 
1063 C CE2 . TYR A 125 ? 0.19323 0.12005 0.19263 -0.02490 -0.03944 0.01210  125 TYR A CE2 
1064 C CZ  . TYR A 125 ? 0.20478 0.15527 0.18109 -0.04283 -0.02413 0.01885  125 TYR A CZ  
1065 O OH  . TYR A 125 ? 0.20082 0.18299 0.17804 -0.04720 -0.00804 -0.00328 125 TYR A OH  
1066 N N   . TRP A 126 ? 0.14164 0.15032 0.24022 -0.00374 0.01461  -0.02719 126 TRP A N   
1067 C CA  . TRP A 126 ? 0.19050 0.14246 0.23990 0.01626  0.02097  -0.05284 126 TRP A CA  
1068 C C   . TRP A 126 ? 0.16922 0.14495 0.22502 0.03646  0.00980  -0.03699 126 TRP A C   
1069 O O   . TRP A 126 ? 0.14720 0.13905 0.22078 0.02202  -0.00653 -0.05519 126 TRP A O   
1070 C CB  . TRP A 126 ? 0.19767 0.12933 0.24238 -0.03955 0.00112  -0.07031 126 TRP A CB  
1071 C CG  . TRP A 126 ? 0.21278 0.16693 0.24604 -0.06604 -0.02281 -0.05287 126 TRP A CG  
1072 C CD1 . TRP A 126 ? 0.22003 0.19602 0.24105 -0.06033 -0.05228 -0.03802 126 TRP A CD1 
1073 C CD2 . TRP A 126 ? 0.25530 0.19382 0.23906 -0.04100 0.00780  -0.03044 126 TRP A CD2 
1074 N NE1 . TRP A 126 ? 0.25844 0.22234 0.23973 -0.03959 -0.01806 -0.01614 126 TRP A NE1 
1075 C CE2 . TRP A 126 ? 0.26257 0.20323 0.23762 -0.02721 -0.00059 -0.00636 126 TRP A CE2 
1076 C CE3 . TRP A 126 ? 0.27219 0.21227 0.23767 -0.07288 0.01502  -0.04184 126 TRP A CE3 
1077 C CZ2 . TRP A 126 ? 0.28624 0.24492 0.24105 -0.03404 0.01917  -0.01823 126 TRP A CZ2 
1078 C CZ3 . TRP A 126 ? 0.28547 0.24479 0.23456 -0.07206 0.01974  -0.04267 126 TRP A CZ3 
1079 C CH2 . TRP A 126 ? 0.28995 0.24226 0.24148 -0.06161 0.00837  -0.03989 126 TRP A CH2 
1080 N N   . THR A 127 ? 0.17218 0.12535 0.22247 0.01802  -0.00385 -0.01375 127 THR A N   
1081 C CA  . THR A 127 ? 0.20394 0.10513 0.21565 -0.03369 0.03962  -0.02648 127 THR A CA  
1082 C C   . THR A 127 ? 0.19241 0.08806 0.17851 -0.01603 0.03237  -0.00546 127 THR A C   
1083 O O   . THR A 127 ? 0.20879 0.11173 0.19030 -0.00504 0.05472  0.02662  127 THR A O   
1084 C CB  . THR A 127 ? 0.20551 0.10992 0.27308 -0.04697 0.05307  -0.00975 127 THR A CB  
1085 O OG1 . THR A 127 ? 0.20819 0.10423 0.31680 -0.02763 0.06374  0.01030  127 THR A OG1 
1086 C CG2 . THR A 127 ? 0.21368 0.12625 0.26838 -0.07335 0.06178  -0.00196 127 THR A CG2 
1087 N N   . GLY A 128 ? 0.15286 0.07248 0.16923 0.01193  0.01544  -0.01785 128 GLY A N   
1088 C CA  . GLY A 128 ? 0.16262 0.10221 0.18403 0.02912  0.00451  -0.02365 128 GLY A CA  
1089 C C   . GLY A 128 ? 0.15910 0.12919 0.20037 0.01344  0.01373  -0.02681 128 GLY A C   
1090 O O   . GLY A 128 ? 0.14322 0.16035 0.22016 0.00460  0.01597  -0.02639 128 GLY A O   
1091 N N   . PHE A 129 ? 0.16267 0.11462 0.17617 0.02229  -0.00628 -0.05417 129 PHE A N   
1092 C CA  . PHE A 129 ? 0.17068 0.11385 0.15038 0.01806  0.00099  -0.03100 129 PHE A CA  
1093 C C   . PHE A 129 ? 0.15799 0.09791 0.12079 -0.01300 -0.01858 -0.01464 129 PHE A C   
1094 O O   . PHE A 129 ? 0.15575 0.12255 0.09424 -0.01424 -0.01450 -0.00592 129 PHE A O   
1095 C CB  . PHE A 129 ? 0.16820 0.14597 0.14831 0.03336  -0.03881 -0.00392 129 PHE A CB  
1096 C CG  . PHE A 129 ? 0.18999 0.16640 0.17213 0.02340  -0.03457 -0.01803 129 PHE A CG  
1097 C CD1 . PHE A 129 ? 0.21005 0.16416 0.19506 0.02676  -0.01889 -0.02553 129 PHE A CD1 
1098 C CD2 . PHE A 129 ? 0.18117 0.20170 0.17541 0.00249  -0.03525 -0.03669 129 PHE A CD2 
1099 C CE1 . PHE A 129 ? 0.20054 0.15731 0.21992 0.00313  -0.00221 -0.03492 129 PHE A CE1 
1100 C CE2 . PHE A 129 ? 0.18123 0.17687 0.20009 0.00752  -0.02822 -0.04261 129 PHE A CE2 
1101 C CZ  . PHE A 129 ? 0.19511 0.14874 0.22017 0.00819  0.00420  -0.03414 129 PHE A CZ  
1102 N N   . VAL A 130 ? 0.15187 0.10722 0.14526 -0.00992 -0.01791 -0.01606 130 VAL A N   
1103 C CA  . VAL A 130 ? 0.16085 0.08803 0.14217 0.01731  0.00250  0.00601  130 VAL A CA  
1104 C C   . VAL A 130 ? 0.16247 0.11710 0.15202 -0.01647 0.01912  0.00576  130 VAL A C   
1105 O O   . VAL A 130 ? 0.12100 0.13213 0.13333 -0.02754 -0.01629 0.01610  130 VAL A O   
1106 C CB  . VAL A 130 ? 0.14360 0.12059 0.14005 0.02103  -0.03462 0.00031  130 VAL A CB  
1107 C CG1 . VAL A 130 ? 0.11850 0.12196 0.15349 0.02920  -0.03357 0.02119  130 VAL A CG1 
1108 C CG2 . VAL A 130 ? 0.17121 0.16942 0.14071 0.03429  -0.04066 -0.00073 130 VAL A CG2 
1109 N N   . ILE A 131 ? 0.18664 0.11897 0.17378 -0.00573 0.02792  0.01229  131 ILE A N   
1110 C CA  . ILE A 131 ? 0.18912 0.08892 0.16798 -0.02980 0.04923  0.03690  131 ILE A CA  
1111 C C   . ILE A 131 ? 0.17288 0.06613 0.17384 -0.02734 0.02745  0.02787  131 ILE A C   
1112 O O   . ILE A 131 ? 0.16120 0.10589 0.18894 -0.01604 0.00168  0.03254  131 ILE A O   
1113 C CB  . ILE A 131 ? 0.17127 0.11885 0.17197 -0.05076 0.05043  0.03986  131 ILE A CB  
1114 C CG1 . ILE A 131 ? 0.16184 0.14041 0.15562 -0.04996 0.04505  0.05549  131 ILE A CG1 
1115 C CG2 . ILE A 131 ? 0.20056 0.12347 0.17433 -0.03253 0.08481  0.02838  131 ILE A CG2 
1116 C CD1 . ILE A 131 ? 0.16579 0.15021 0.17382 -0.05030 0.04041  0.06549  131 ILE A CD1 
1117 N N   . ALA A 132 ? 0.17203 0.06969 0.16364 -0.01511 0.03765  0.03535  132 ALA A N   
1118 C CA  . ALA A 132 ? 0.18121 0.09797 0.17477 0.01283  0.03001  0.06758  132 ALA A CA  
1119 C C   . ALA A 132 ? 0.15030 0.13677 0.15321 -0.01338 0.01469  0.04440  132 ALA A C   
1120 O O   . ALA A 132 ? 0.11886 0.14135 0.10980 -0.02049 0.00964  0.03109  132 ALA A O   
1121 C CB  . ALA A 132 ? 0.14489 0.12667 0.18827 0.04017  0.02251  0.04238  132 ALA A CB  
1122 N N   A MET A 133 ? 0.13532 0.14208 0.14683 -0.02234 0.00344  0.01446  133 MET A N   
1123 N N   B MET A 133 ? 0.16912 0.16038 0.16918 -0.02803 0.00139  0.01342  133 MET A N   
1124 C CA  A MET A 133 ? 0.14614 0.13128 0.14456 -0.01500 0.00111  -0.00074 133 MET A CA  
1125 C CA  B MET A 133 ? 0.20704 0.17104 0.17151 -0.03032 0.01179  -0.00805 133 MET A CA  
1126 C C   A MET A 133 ? 0.16533 0.10396 0.14809 0.00257  0.00981  -0.00777 133 MET A C   
1127 C C   B MET A 133 ? 0.18920 0.11102 0.16600 -0.01555 0.00274  -0.01977 133 MET A C   
1128 O O   A MET A 133 ? 0.15481 0.10589 0.14115 0.01098  0.01361  0.00035  133 MET A O   
1129 O O   B MET A 133 ? 0.16207 0.10011 0.16052 -0.02005 -0.01104 -0.02975 133 MET A O   
1130 C CB  A MET A 133 ? 0.13040 0.11306 0.14866 0.00499  -0.03576 0.01032  133 MET A CB  
1131 C CB  B MET A 133 ? 0.24854 0.19872 0.18908 -0.01668 0.00097  0.00430  133 MET A CB  
1132 C CG  A MET A 133 ? 0.11786 0.09915 0.14643 0.01406  -0.03646 0.02457  133 MET A CG  
1133 C CG  B MET A 133 ? 0.29647 0.22439 0.21787 0.01078  -0.00220 0.03255  133 MET A CG  
1134 S SD  A MET A 133 ? 0.13290 0.10112 0.15386 0.02269  -0.03036 0.05121  133 MET A SD  
1135 S SD  B MET A 133 ? 0.34726 0.28347 0.25256 0.04799  0.02992  0.05010  133 MET A SD  
1136 C CE  A MET A 133 ? 0.15487 0.18768 0.18448 0.07195  -0.00979 0.06842  133 MET A CE  
1137 C CE  B MET A 133 ? 0.31111 0.29003 0.23686 0.04848  0.04091  0.07996  133 MET A CE  
1138 N N   . ALA A 134 ? 0.17427 0.11501 0.15388 0.02837  0.00749  0.00492  134 ALA A N   
1139 C CA  . ALA A 134 ? 0.16550 0.12259 0.16584 0.02308  0.00984  0.03035  134 ALA A CA  
1140 C C   . ALA A 134 ? 0.11751 0.12448 0.14476 0.00124  -0.01763 0.00068  134 ALA A C   
1141 O O   . ALA A 134 ? 0.10387 0.14278 0.14510 -0.00742 0.02092  0.00254  134 ALA A O   
1142 C CB  . ALA A 134 ? 0.15749 0.13311 0.17501 0.02948  0.00489  0.03879  134 ALA A CB  
1143 N N   A THR A 135 ? 0.12908 0.10626 0.14384 0.00855  -0.01961 -0.00147 135 THR A N   
1144 N N   B THR A 135 ? 0.15409 0.12230 0.14909 0.01159  -0.00873 -0.00159 135 THR A N   
1145 C CA  A THR A 135 ? 0.12242 0.09832 0.15276 0.01957  -0.01744 0.00541  135 THR A CA  
1146 C CA  B THR A 135 ? 0.17181 0.13119 0.15898 0.03669  0.01446  0.00930  135 THR A CA  
1147 C C   A THR A 135 ? 0.12962 0.13229 0.16606 0.01756  -0.00243 -0.00700 135 THR A C   
1148 C C   B THR A 135 ? 0.15165 0.14199 0.17180 0.02041  0.00457  -0.00623 135 THR A C   
1149 O O   A THR A 135 ? 0.14170 0.15086 0.17177 0.01601  -0.00023 -0.00713 135 THR A O   
1150 O O   B THR A 135 ? 0.15333 0.14884 0.18302 0.01853  -0.00709 -0.00347 135 THR A O   
1151 C CB  A THR A 135 ? 0.10592 0.11669 0.15100 -0.00857 -0.01568 0.00283  135 THR A CB  
1152 C CB  B THR A 135 ? 0.20491 0.15552 0.16062 0.05003  0.04908  0.02879  135 THR A CB  
1153 O OG1 A THR A 135 ? 0.11993 0.09634 0.15063 0.02334  -0.02818 0.00202  135 THR A OG1 
1154 O OG1 B THR A 135 ? 0.22663 0.16955 0.16460 0.07192  0.06478  0.02919  135 THR A OG1 
1155 C CG2 A THR A 135 ? 0.09834 0.16580 0.15575 -0.04029 -0.00416 -0.00731 135 THR A CG2 
1156 C CG2 B THR A 135 ? 0.23238 0.18057 0.16303 0.04586  0.07098  0.03629  135 THR A CG2 
1157 N N   . TYR A 136 ? 0.15158 0.09961 0.18803 0.00395  0.00270  -0.00119 136 TYR A N   
1158 C CA  . TYR A 136 ? 0.17974 0.10908 0.18867 -0.00832 0.00532  0.02166  136 TYR A CA  
1159 C C   . TYR A 136 ? 0.16779 0.11076 0.16920 -0.02888 -0.01452 -0.00745 136 TYR A C   
1160 O O   . TYR A 136 ? 0.17591 0.14077 0.14951 -0.04481 -0.02815 -0.00920 136 TYR A O   
1161 C CB  . TYR A 136 ? 0.19591 0.07759 0.18767 -0.05379 -0.00031 -0.00388 136 TYR A CB  
1162 C CG  . TYR A 136 ? 0.28345 0.13161 0.21782 -0.06286 0.03763  0.00912  136 TYR A CG  
1163 C CD1 . TYR A 136 ? 0.32975 0.19940 0.23887 -0.05580 0.05328  -0.01458 136 TYR A CD1 
1164 C CD2 . TYR A 136 ? 0.32074 0.22421 0.23065 -0.05396 0.07141  0.02478  136 TYR A CD2 
1165 C CE1 . TYR A 136 ? 0.32592 0.23465 0.24175 -0.06522 0.05808  -0.01353 136 TYR A CE1 
1166 C CE2 . TYR A 136 ? 0.33227 0.28220 0.23804 -0.04224 0.08326  0.03233  136 TYR A CE2 
1167 C CZ  . TYR A 136 ? 0.28956 0.26748 0.24501 -0.06349 0.03425  0.01647  136 TYR A CZ  
1168 O OH  . TYR A 136 ? 0.26955 0.39885 0.26986 -0.03436 0.03242  0.02817  136 TYR A OH  
1169 N N   . VAL A 137 ? 0.17038 0.12429 0.16090 0.00971  -0.00537 -0.01580 137 VAL A N   
1170 C CA  . VAL A 137 ? 0.16030 0.14861 0.14769 0.00443  -0.02575 -0.04061 137 VAL A CA  
1171 C C   . VAL A 137 ? 0.15589 0.14201 0.15616 -0.00370 -0.01406 -0.03664 137 VAL A C   
1172 O O   . VAL A 137 ? 0.14133 0.15686 0.16252 -0.01078 -0.03363 -0.04064 137 VAL A O   
1173 C CB  . VAL A 137 ? 0.16518 0.16879 0.14322 0.02520  -0.02487 -0.04342 137 VAL A CB  
1174 C CG1 . VAL A 137 ? 0.18117 0.21959 0.16996 0.02925  0.00366  -0.04989 137 VAL A CG1 
1175 C CG2 . VAL A 137 ? 0.17953 0.20110 0.15628 -0.01230 -0.03424 -0.04900 137 VAL A CG2 
1176 N N   . TRP A 138 ? 0.14658 0.14876 0.13128 -0.03344 -0.01817 -0.00867 138 TRP A N   
1177 C CA  . TRP A 138 ? 0.15579 0.14425 0.11857 -0.04936 -0.01394 0.00194  138 TRP A CA  
1178 C C   . TRP A 138 ? 0.13402 0.14267 0.09313 -0.02745 -0.01557 0.01980  138 TRP A C   
1179 O O   . TRP A 138 ? 0.13435 0.15697 0.09786 -0.02477 -0.02566 -0.00057 138 TRP A O   
1180 C CB  . TRP A 138 ? 0.17583 0.14219 0.14604 -0.04913 -0.03388 0.01705  138 TRP A CB  
1181 C CG  . TRP A 138 ? 0.15504 0.17250 0.16418 -0.03097 -0.05932 0.02245  138 TRP A CG  
1182 C CD1 . TRP A 138 ? 0.15447 0.18630 0.17717 -0.00892 -0.06614 0.04408  138 TRP A CD1 
1183 C CD2 . TRP A 138 ? 0.17004 0.16183 0.17372 -0.00536 -0.06134 0.01300  138 TRP A CD2 
1184 N NE1 . TRP A 138 ? 0.18455 0.18427 0.18186 0.00635  -0.06174 0.05829  138 TRP A NE1 
1185 C CE2 . TRP A 138 ? 0.19213 0.17437 0.19424 -0.00662 -0.05529 0.02348  138 TRP A CE2 
1186 C CE3 . TRP A 138 ? 0.21902 0.15577 0.19382 0.00887  -0.03503 -0.00597 138 TRP A CE3 
1187 C CZ2 . TRP A 138 ? 0.19699 0.19039 0.19614 -0.01191 -0.06597 -0.00305 138 TRP A CZ2 
1188 C CZ3 . TRP A 138 ? 0.22338 0.19203 0.21548 0.01269  -0.05667 -0.00946 138 TRP A CZ3 
1189 C CH2 . TRP A 138 ? 0.20744 0.22371 0.22097 0.03046  -0.05493 -0.01061 138 TRP A CH2 
1190 N N   . LEU A 139 ? 0.16157 0.13535 0.09587 -0.00553 0.02819  0.02307  139 LEU A N   
1191 C CA  . LEU A 139 ? 0.12644 0.11429 0.11824 0.02849  0.01810  0.02230  139 LEU A CA  
1192 C C   . LEU A 139 ? 0.13762 0.12283 0.11320 -0.00175 0.00520  -0.00567 139 LEU A C   
1193 O O   . LEU A 139 ? 0.14296 0.16148 0.08898 -0.01173 0.02141  -0.00827 139 LEU A O   
1194 C CB  . LEU A 139 ? 0.09084 0.14751 0.13681 0.04530  0.03578  0.00696  139 LEU A CB  
1195 C CG  . LEU A 139 ? 0.12129 0.23204 0.14533 0.02569  0.03928  0.00085  139 LEU A CG  
1196 C CD1 . LEU A 139 ? 0.13054 0.25229 0.16024 0.06122  0.03473  0.00939  139 LEU A CD1 
1197 C CD2 . LEU A 139 ? 0.15323 0.27545 0.13005 0.02070  0.05838  -0.00040 139 LEU A CD2 
1198 N N   A MET A 140 ? 0.14672 0.12648 0.13025 -0.00865 0.02068  -0.02588 140 MET A N   
1199 N N   B MET A 140 ? 0.15580 0.13213 0.13450 -0.01018 0.01140  -0.02773 140 MET A N   
1200 C CA  A MET A 140 ? 0.13101 0.17362 0.14822 -0.01377 0.01405  0.00191  140 MET A CA  
1201 C CA  B MET A 140 ? 0.15726 0.18661 0.14419 -0.01264 0.00590  -0.00597 140 MET A CA  
1202 C C   A MET A 140 ? 0.12774 0.17088 0.16357 -0.01089 0.02272  -0.02521 140 MET A C   
1203 C C   B MET A 140 ? 0.13145 0.17789 0.17071 -0.01341 0.01732  -0.02734 140 MET A C   
1204 O O   A MET A 140 ? 0.12071 0.19681 0.15218 -0.00822 0.02672  -0.04037 140 MET A O   
1205 O O   B MET A 140 ? 0.11131 0.20517 0.16738 -0.01237 0.02559  -0.04108 140 MET A O   
1206 C CB  A MET A 140 ? 0.08603 0.16002 0.15014 -0.01045 -0.01530 0.03375  140 MET A CB  
1207 C CB  B MET A 140 ? 0.15214 0.18920 0.12251 -0.00084 -0.01097 0.01750  140 MET A CB  
1208 C CG  A MET A 140 ? 0.08426 0.15213 0.14656 -0.00640 -0.00352 0.05901  140 MET A CG  
1209 C CG  B MET A 140 ? 0.15330 0.18376 0.10802 0.00685  -0.00861 0.03530  140 MET A CG  
1210 S SD  A MET A 140 ? 0.08251 0.16696 0.16828 -0.01407 0.00584  0.06356  140 MET A SD  
1211 S SD  B MET A 140 ? 0.18560 0.21377 0.10794 -0.01867 0.03858  0.03404  140 MET A SD  
1212 C CE  A MET A 140 ? 0.10777 0.20113 0.19045 -0.01589 0.00376  0.06239  140 MET A CE  
1213 C CE  B MET A 140 ? 0.22586 0.22064 0.11136 -0.01087 0.03936  0.04063  140 MET A CE  
1214 N N   . ARG A 141 ? 0.12930 0.14934 0.19670 0.00027  -0.00341 -0.00996 141 ARG A N   
1215 C CA  . ARG A 141 ? 0.16598 0.16288 0.26183 0.03761  -0.02710 -0.01961 141 ARG A CA  
1216 C C   . ARG A 141 ? 0.14497 0.15019 0.27420 0.00684  -0.04129 -0.02104 141 ARG A C   
1217 O O   . ARG A 141 ? 0.11424 0.19556 0.27692 0.02314  -0.01775 -0.04722 141 ARG A O   
1218 C CB  . ARG A 141 ? 0.22621 0.20967 0.33313 0.04716  -0.02531 -0.04831 141 ARG A CB  
1219 C CG  . ARG A 141 ? 0.27627 0.33775 0.38854 0.05327  -0.01036 -0.06559 141 ARG A CG  
1220 C CD  . ARG A 141 ? 0.34230 0.42167 0.45014 0.05000  -0.00580 -0.06190 141 ARG A CD  
1221 N NE  . ARG A 141 ? 0.44598 0.47811 0.53750 0.04162  0.02084  -0.05855 141 ARG A NE  
1222 C CZ  . ARG A 141 ? 0.55511 0.58213 0.62274 0.05852  0.07245  -0.04843 141 ARG A CZ  
1223 N NH1 . ARG A 141 ? 0.64475 0.68243 0.68969 0.05369  0.11296  -0.04666 141 ARG A NH1 
1224 N NH2 . ARG A 141 ? 0.53249 0.61240 0.62084 0.08692  0.07297  -0.03739 141 ARG A NH2 
1225 N N   . ASN A 142 ? 0.15102 0.10818 0.27540 -0.00399 -0.03111 0.02471  142 ASN A N   
1226 C CA  . ASN A 142 ? 0.20003 0.13769 0.28324 -0.04412 0.00391  0.02030  142 ASN A CA  
1227 C C   . ASN A 142 ? 0.18512 0.13471 0.26717 -0.02218 0.02055  0.00305  142 ASN A C   
1228 O O   . ASN A 142 ? 0.15728 0.14254 0.27128 -0.04394 -0.01027 -0.01229 142 ASN A O   
1229 C CB  . ASN A 142 ? 0.23648 0.18469 0.29416 -0.04501 -0.02214 0.08996  142 ASN A CB  
1230 C CG  . ASN A 142 ? 0.31919 0.28992 0.33738 -0.03073 -0.02862 0.08812  142 ASN A CG  
1231 O OD1 . ASN A 142 ? 0.39471 0.37222 0.41704 -0.01065 -0.02783 0.08250  142 ASN A OD1 
1232 N ND2 . ASN A 142 ? 0.31525 0.29314 0.30587 -0.04473 -0.02222 0.09731  142 ASN A ND2 
1233 N N   . LEU A 143 ? 0.18786 0.12978 0.24023 -0.02373 0.02276  0.00981  143 LEU A N   
1234 C CA  . LEU A 143 ? 0.16467 0.10197 0.21453 -0.01560 -0.00393 0.01465  143 LEU A CA  
1235 C C   . LEU A 143 ? 0.16282 0.14023 0.24401 -0.04628 -0.00994 -0.01320 143 LEU A C   
1236 O O   . LEU A 143 ? 0.15678 0.15724 0.24326 -0.02553 0.00088  -0.01036 143 LEU A O   
1237 C CB  . LEU A 143 ? 0.17512 0.12725 0.17013 0.00993  -0.01571 0.04057  143 LEU A CB  
1238 C CG  . LEU A 143 ? 0.17590 0.09868 0.14230 0.00636  -0.00890 0.03730  143 LEU A CG  
1239 C CD1 . LEU A 143 ? 0.19966 0.11937 0.13606 0.00923  0.04468  0.00588  143 LEU A CD1 
1240 C CD2 . LEU A 143 ? 0.17235 0.12971 0.14130 0.02249  -0.02509 0.04481  143 LEU A CD2 
1241 N N   . GLN A 144 ? 0.17769 0.18200 0.27198 -0.03346 -0.00657 -0.04861 144 GLN A N   
1242 C CA  . GLN A 144 ? 0.20126 0.23457 0.30578 0.00549  0.00281  -0.06090 144 GLN A CA  
1243 C C   . GLN A 144 ? 0.18243 0.23048 0.31914 0.00740  0.03308  -0.06703 144 GLN A C   
1244 O O   . GLN A 144 ? 0.17695 0.24898 0.33108 0.01737  0.07885  -0.04612 144 GLN A O   
1245 C CB  . GLN A 144 ? 0.25702 0.26736 0.30829 0.01288  -0.00233 -0.06290 144 GLN A CB  
1246 C CG  . GLN A 144 ? 0.32988 0.33286 0.34930 0.01761  0.00728  -0.05211 144 GLN A CG  
1247 C CD  . GLN A 144 ? 0.39363 0.44195 0.40687 0.03164  0.04871  -0.04882 144 GLN A CD  
1248 O OE1 . GLN A 144 ? 0.41180 0.42189 0.40784 0.00897  0.02858  -0.07077 144 GLN A OE1 
1249 N NE2 . GLN A 144 ? 0.39562 0.45819 0.42101 0.06564  0.04600  -0.02939 144 GLN A NE2 
1250 N N   . ALA A 145 ? 0.15844 0.19515 0.30549 0.00583  0.02129  -0.04528 145 ALA A N   
1251 C CA  . ALA A 145 ? 0.17177 0.20755 0.30631 -0.00768 -0.01063 -0.03032 145 ALA A CA  
1252 C C   . ALA A 145 ? 0.16854 0.23745 0.32956 0.03857  -0.03613 -0.02280 145 ALA A C   
1253 O O   . ALA A 145 ? 0.17822 0.27934 0.35142 0.05426  -0.03744 -0.06191 145 ALA A O   
1254 C CB  . ALA A 145 ? 0.22805 0.19825 0.33343 0.02133  0.00116  -0.01483 145 ALA A CB  
1255 N N   . GLU A 146 ? 0.12792 0.18841 0.36257 0.02541  -0.03722 -0.00084 146 GLU A N   
1256 C CA  . GLU A 146 ? 0.17885 0.20224 0.39707 0.01007  -0.02644 0.01797  146 GLU A CA  
1257 C C   . GLU A 146 ? 0.24200 0.24283 0.49588 0.01280  -0.02650 0.00465  146 GLU A C   
1258 O O   . GLU A 146 ? 0.24099 0.24660 0.46962 -0.02411 -0.01965 0.01101  146 GLU A O   
1259 C CB  . GLU A 146 ? 0.17226 0.19432 0.35547 0.00924  -0.01988 0.01965  146 GLU A CB  
1260 C CG  . GLU A 146 ? 0.21374 0.27502 0.36228 -0.01491 0.00284  -0.02567 146 GLU A CG  
1261 C CD  . GLU A 146 ? 0.22024 0.31803 0.38500 -0.04483 0.00653  -0.04246 146 GLU A CD  
1262 O OE1 . GLU A 146 ? 0.22549 0.36620 0.41522 -0.05957 0.03503  -0.03060 146 GLU A OE1 
1263 O OE2 . GLU A 146 ? 0.22420 0.35139 0.40076 0.00340  0.00420  -0.07796 146 GLU A OE2 
1264 N N   A GLY A 147 ? 0.27481 0.27438 0.55885 0.01751  -0.04378 -0.01117 147 GLY A N   
1265 N N   B GLY A 147 ? 0.27902 0.28585 0.55889 0.00645  -0.03420 -0.01768 147 GLY A N   
1266 C CA  A GLY A 147 ? 0.33145 0.35881 0.64559 -0.00622 -0.02956 -0.02043 147 GLY A CA  
1267 C CA  B GLY A 147 ? 0.32484 0.37168 0.63805 -0.01795 -0.02278 -0.03271 147 GLY A CA  
1268 C C   A GLY A 147 ? 0.40121 0.47666 0.73797 -0.01839 0.01818  -0.00946 147 GLY A C   
1269 C C   B GLY A 147 ? 0.37356 0.47207 0.72329 -0.01898 0.00934  -0.01930 147 GLY A C   
1270 O O   A GLY A 147 ? 0.37155 0.42773 0.72916 -0.03671 -0.01414 -0.02702 147 GLY A O   
1271 O O   B GLY A 147 ? 0.30111 0.40282 0.70324 -0.01519 -0.04157 -0.03193 147 GLY A O   
1272 N N   A GLU A 148 ? 0.50232 0.60749 0.85249 0.00684  0.06074  0.02767  148 GLU A N   
1273 N N   B GLU A 148 ? 0.49292 0.60622 0.84469 0.00306  0.05275  0.01852  148 GLU A N   
1274 C CA  A GLU A 148 ? 0.63855 0.76266 0.95363 0.01546  0.13679  0.04458  148 GLU A CA  
1275 C CA  B GLU A 148 ? 0.63855 0.76264 0.95363 0.01851  0.11801  0.04221  148 GLU A CA  
1276 C C   A GLU A 148 ? 0.55048 0.65835 0.88258 0.00707  0.08763  0.04975  148 GLU A C   
1277 C C   B GLU A 148 ? 0.56340 0.65836 0.88095 0.02649  0.05780  0.04950  148 GLU A C   
1278 O O   A GLU A 148 ? 0.51927 0.66817 0.87456 -0.01772 0.07222  0.04199  148 GLU A O   
1279 O O   B GLU A 148 ? 0.53878 0.68239 0.86765 0.02585  0.03104  0.04104  148 GLU A O   
1280 C CB  A GLU A 148 ? 0.61997 0.75192 0.93503 0.01828  0.14608  0.04496  148 GLU A CB  
1281 C CB  B GLU A 148 ? 0.61824 0.75715 0.93764 0.01928  0.12777  0.04624  148 GLU A CB  
1282 N N   A GLY A 149 ? 0.46480 0.57522 0.81990 0.02344  0.01422  0.06486  149 GLY A N   
1283 N N   B GLY A 149 ? 0.48136 0.57880 0.83000 0.03308  -0.01429 0.06253  149 GLY A N   
1284 C CA  A GLY A 149 ? 0.42511 0.51605 0.74289 0.03471  0.02277  0.08465  149 GLY A CA  
1285 C CA  B GLY A 149 ? 0.44773 0.52566 0.76601 0.04267  -0.00032 0.07266  149 GLY A CA  
1286 C C   A GLY A 149 ? 0.32815 0.40783 0.67667 0.03950  -0.02972 0.09874  149 GLY A C   
1287 C C   B GLY A 149 ? 0.35235 0.42899 0.70992 0.05678  -0.05391 0.07106  149 GLY A C   
1288 O O   A GLY A 149 ? 0.30135 0.38113 0.64813 0.02925  -0.04125 0.10625  149 GLY A O   
1289 O O   B GLY A 149 ? 0.33855 0.42456 0.69674 0.06406  -0.05647 0.05660  149 GLY A O   
1290 N N   A LEU A 150 ? 0.27507 0.37771 0.63618 0.05393  -0.02708 0.10686  150 LEU A N   
1291 N N   B LEU A 150 ? 0.28959 0.38555 0.65719 0.06605  -0.04992 0.09150  150 LEU A N   
1292 C CA  A LEU A 150 ? 0.25214 0.35935 0.58870 0.04619  -0.01625 0.09924  150 LEU A CA  
1293 C CA  B LEU A 150 ? 0.26147 0.36250 0.59707 0.05640  -0.03490 0.09602  150 LEU A CA  
1294 C C   A LEU A 150 ? 0.22755 0.29648 0.55122 0.03445  -0.02799 0.09547  150 LEU A C   
1295 C C   B LEU A 150 ? 0.23428 0.29985 0.55208 0.04644  -0.04920 0.10046  150 LEU A C   
1296 O O   A LEU A 150 ? 0.21882 0.28267 0.53267 0.01857  0.01627  0.10394  150 LEU A O   
1297 O O   B LEU A 150 ? 0.23270 0.29417 0.53075 0.03827  -0.01786 0.11443  150 LEU A O   
1298 C CB  A LEU A 150 ? 0.21975 0.34888 0.57746 0.04228  -0.03222 0.09038  150 LEU A CB  
1299 C CB  B LEU A 150 ? 0.23979 0.35392 0.58344 0.04066  -0.03323 0.08246  150 LEU A CB  
1300 C CG  A LEU A 150 ? 0.22634 0.35109 0.56252 0.02459  -0.02589 0.07280  150 LEU A CG  
1301 C CG  B LEU A 150 ? 0.25986 0.35566 0.56732 0.01160  -0.00344 0.05383  150 LEU A CG  
1302 C CD1 A LEU A 150 ? 0.24511 0.37275 0.55077 0.01683  -0.02079 0.07450  150 LEU A CD1 
1303 C CD1 B LEU A 150 ? 0.28508 0.37645 0.56356 -0.00295 0.02138  0.05799  150 LEU A CD1 
1304 C CD2 A LEU A 150 ? 0.22897 0.34306 0.54960 0.01942  -0.01424 0.06085  150 LEU A CD2 
1305 C CD2 B LEU A 150 ? 0.27064 0.34305 0.54967 0.00824  0.00862  0.02864  150 LEU A CD2 
1306 N N   . LYS A 151 ? 0.18797 0.29774 0.52420 0.02433  -0.06607 0.08305  151 LYS A N   
1307 C CA  . LYS A 151 ? 0.15373 0.30179 0.48518 -0.01283 -0.06330 0.09185  151 LYS A CA  
1308 C C   . LYS A 151 ? 0.14107 0.29938 0.43890 -0.01486 -0.04627 0.08136  151 LYS A C   
1309 O O   . LYS A 151 ? 0.18400 0.30029 0.44821 -0.05228 -0.00784 0.07012  151 LYS A O   
1310 C CB  . LYS A 151 ? 0.15253 0.32131 0.51573 -0.00733 -0.05570 0.11275  151 LYS A CB  
1311 C CG  . LYS A 151 ? 0.18311 0.33337 0.56829 0.00360  -0.01944 0.14102  151 LYS A CG  
1312 C CD  . LYS A 151 ? 0.23032 0.33946 0.62172 0.05272  0.01624  0.16488  151 LYS A CD  
1313 C CE  . LYS A 151 ? 0.30338 0.40238 0.65641 0.06296  0.07079  0.17895  151 LYS A CE  
1314 N NZ  . LYS A 151 ? 0.30665 0.38934 0.64246 0.07583  0.07262  0.18320  151 LYS A NZ  
1315 N N   . GLY A 152 ? 0.12645 0.26444 0.36827 -0.02225 -0.02762 0.08507  152 GLY A N   
1316 C CA  . GLY A 152 ? 0.13319 0.23702 0.33332 -0.01003 -0.03093 0.07785  152 GLY A CA  
1317 C C   . GLY A 152 ? 0.11418 0.19948 0.30615 -0.01300 -0.02348 0.06167  152 GLY A C   
1318 O O   . GLY A 152 ? 0.07869 0.22756 0.27135 0.00253  -0.03109 0.03453  152 GLY A O   
1319 N N   . ASP A 153 ? 0.15070 0.18656 0.31570 -0.02368 -0.00667 0.01191  153 ASP A N   
1320 C CA  . ASP A 153 ? 0.19701 0.19092 0.32268 -0.00616 0.00365  -0.00696 153 ASP A CA  
1321 C C   . ASP A 153 ? 0.17862 0.18535 0.28884 0.00434  -0.01204 -0.01480 153 ASP A C   
1322 O O   . ASP A 153 ? 0.15690 0.21208 0.27075 -0.02045 -0.02223 -0.00793 153 ASP A O   
1323 C CB  . ASP A 153 ? 0.24839 0.22109 0.36159 -0.01098 0.01675  -0.00529 153 ASP A CB  
1324 C CG  . ASP A 153 ? 0.30047 0.31626 0.41302 -0.04097 -0.00005 -0.00183 153 ASP A CG  
1325 O OD1 . ASP A 153 ? 0.32581 0.32818 0.42250 -0.08931 -0.00210 -0.00914 153 ASP A OD1 
1326 O OD2 . ASP A 153 ? 0.33135 0.40094 0.45357 -0.01953 -0.00739 0.02238  153 ASP A OD2 
1327 N N   A GLN A 154 ? 0.19158 0.19058 0.28059 -0.00398 -0.00444 -0.03299 154 GLN A N   
1328 N N   B GLN A 154 ? 0.18671 0.18653 0.27389 -0.00414 -0.00365 -0.03370 154 GLN A N   
1329 C CA  A GLN A 154 ? 0.22036 0.22324 0.27297 -0.01160 -0.01365 -0.02506 154 GLN A CA  
1330 C CA  B GLN A 154 ? 0.21006 0.21667 0.25984 -0.01184 -0.01337 -0.02607 154 GLN A CA  
1331 C C   A GLN A 154 ? 0.18461 0.23179 0.23103 -0.01726 -0.01129 -0.00914 154 GLN A C   
1332 C C   B GLN A 154 ? 0.18025 0.22871 0.22434 -0.01631 -0.01227 -0.01215 154 GLN A C   
1333 O O   A GLN A 154 ? 0.14672 0.23617 0.20977 -0.04638 0.00077  -0.00603 154 GLN A O   
1334 O O   B GLN A 154 ? 0.14313 0.23530 0.20252 -0.04329 -0.00074 -0.01336 154 GLN A O   
1335 C CB  A GLN A 154 ? 0.28166 0.28947 0.30315 -0.02556 -0.00906 -0.01512 154 GLN A CB  
1336 C CB  B GLN A 154 ? 0.25423 0.27589 0.27504 -0.02895 -0.01624 -0.01639 154 GLN A CB  
1337 C CG  A GLN A 154 ? 0.30942 0.36884 0.32465 -0.01928 0.00180  -0.00862 154 GLN A CG  
1338 C CG  B GLN A 154 ? 0.28010 0.32784 0.28596 -0.02674 -0.02367 -0.01299 154 GLN A CG  
1339 C CD  A GLN A 154 ? 0.31113 0.39054 0.36965 -0.01598 -0.03563 -0.00718 154 GLN A CD  
1340 C CD  B GLN A 154 ? 0.31189 0.37671 0.32857 -0.03231 0.01144  -0.01290 154 GLN A CD  
1341 O OE1 A GLN A 154 ? 0.34956 0.44440 0.41369 -0.01541 -0.01474 -0.01480 154 GLN A OE1 
1342 O OE1 B GLN A 154 ? 0.32557 0.38126 0.32796 -0.03966 0.03709  -0.01447 154 GLN A OE1 
1343 N NE2 A GLN A 154 ? 0.32451 0.42310 0.38111 -0.00986 -0.00979 -0.00788 154 GLN A NE2 
1344 N NE2 B GLN A 154 ? 0.31610 0.38934 0.34085 -0.03429 -0.00765 -0.01617 154 GLN A NE2 
1345 N N   . ALA A 155 ? 0.19520 0.20141 0.22882 0.00867  -0.00095 -0.02003 155 ALA A N   
1346 C CA  . ALA A 155 ? 0.18658 0.14526 0.22343 0.03150  -0.01212 -0.02044 155 ALA A CA  
1347 C C   . ALA A 155 ? 0.16032 0.16073 0.23542 0.02311  -0.02381 -0.00836 155 ALA A C   
1348 O O   . ALA A 155 ? 0.14984 0.18363 0.26270 -0.00217 -0.02282 0.00781  155 ALA A O   
1349 C CB  . ALA A 155 ? 0.20576 0.16170 0.23004 0.05411  0.01349  -0.03652 155 ALA A CB  
1350 N N   . VAL A 156 ? 0.14500 0.17777 0.20394 -0.00579 -0.01966 -0.00136 156 VAL A N   
1351 C CA  . VAL A 156 ? 0.10581 0.24274 0.18033 -0.01526 -0.02102 0.00993  156 VAL A CA  
1352 C C   . VAL A 156 ? 0.08632 0.23402 0.14811 0.00026  0.01052  0.04692  156 VAL A C   
1353 O O   . VAL A 156 ? 0.09347 0.21714 0.12116 -0.01394 0.00711  0.06067  156 VAL A O   
1354 C CB  . VAL A 156 ? 0.11469 0.29141 0.17805 -0.02611 -0.04023 0.02071  156 VAL A CB  
1355 C CG1 . VAL A 156 ? 0.14796 0.26361 0.20339 -0.02892 -0.03507 -0.00009 156 VAL A CG1 
1356 C CG2 . VAL A 156 ? 0.10170 0.31930 0.18948 -0.04112 -0.03813 0.01129  156 VAL A CG2 
1357 N N   . ALA A 157 ? 0.08795 0.22730 0.16777 -0.01482 0.01160  0.01030  157 ALA A N   
1358 C CA  . ALA A 157 ? 0.10886 0.19996 0.18329 0.01122  0.01428  -0.02198 157 ALA A CA  
1359 C C   . ALA A 157 ? 0.11261 0.20081 0.16884 -0.00536 -0.01658 -0.02658 157 ALA A C   
1360 O O   . ALA A 157 ? 0.11461 0.19176 0.17184 -0.02642 0.00628  -0.00959 157 ALA A O   
1361 C CB  . ALA A 157 ? 0.11656 0.21323 0.19992 0.02463  0.02073  -0.05717 157 ALA A CB  
1362 N N   . PHE A 158 ? 0.12134 0.18039 0.17693 -0.01348 -0.00611 -0.00666 158 PHE A N   
1363 C CA  . PHE A 158 ? 0.13311 0.17484 0.15477 -0.00724 -0.03424 0.00432  158 PHE A CA  
1364 C C   . PHE A 158 ? 0.13552 0.19904 0.15538 -0.00456 -0.02721 -0.00317 158 PHE A C   
1365 O O   . PHE A 158 ? 0.12128 0.19606 0.17503 -0.02087 -0.02354 -0.04369 158 PHE A O   
1366 C CB  . PHE A 158 ? 0.13943 0.19115 0.14634 -0.01415 -0.02096 0.03224  158 PHE A CB  
1367 C CG  . PHE A 158 ? 0.13404 0.20770 0.14354 -0.01586 -0.00034 0.04048  158 PHE A CG  
1368 C CD1 . PHE A 158 ? 0.14934 0.21033 0.13872 0.01281  0.00966  0.05587  158 PHE A CD1 
1369 C CD2 . PHE A 158 ? 0.16824 0.27571 0.13737 -0.02575 0.01232  0.02492  158 PHE A CD2 
1370 C CE1 . PHE A 158 ? 0.18097 0.24228 0.15337 0.04171  0.02465  0.06116  158 PHE A CE1 
1371 C CE2 . PHE A 158 ? 0.15756 0.28952 0.13699 -0.01217 0.02111  0.01248  158 PHE A CE2 
1372 C CZ  . PHE A 158 ? 0.19302 0.27206 0.14801 0.00928  0.03464  0.02075  158 PHE A CZ  
1373 N N   A GLU A 159 ? 0.12745 0.20746 0.12956 0.00658  -0.03572 0.00487  159 GLU A N   
1374 N N   B GLU A 159 ? 0.13757 0.20958 0.14385 0.01226  -0.04652 0.00367  159 GLU A N   
1375 C CA  A GLU A 159 ? 0.13383 0.21019 0.12778 0.00658  -0.00150 0.01248  159 GLU A CA  
1376 C CA  B GLU A 159 ? 0.15709 0.22116 0.15282 0.01746  -0.01294 0.01139  159 GLU A CA  
1377 C C   A GLU A 159 ? 0.11818 0.18196 0.12242 0.00443  0.00036  0.02576  159 GLU A C   
1378 C C   B GLU A 159 ? 0.13476 0.18352 0.13073 0.00767  -0.00758 0.02737  159 GLU A C   
1379 O O   A GLU A 159 ? 0.13544 0.19030 0.12135 -0.00370 -0.00301 0.02024  159 GLU A O   
1380 O O   B GLU A 159 ? 0.15638 0.19049 0.12220 -0.00556 -0.00815 0.02442  159 GLU A O   
1381 C CB  A GLU A 159 ? 0.13797 0.21708 0.13311 -0.00236 0.01252  0.01014  159 GLU A CB  
1382 C CB  B GLU A 159 ? 0.17586 0.25801 0.17934 0.01883  0.00240  0.00786  159 GLU A CB  
1383 C CG  A GLU A 159 ? 0.13554 0.21091 0.14840 -0.00749 0.04721  0.01089  159 GLU A CG  
1384 C CG  B GLU A 159 ? 0.17752 0.28114 0.19998 0.01034  0.02202  0.00938  159 GLU A CG  
1385 C CD  A GLU A 159 ? 0.13949 0.20457 0.16759 -0.02910 0.05075  -0.00767 159 GLU A CD  
1386 C CD  B GLU A 159 ? 0.18622 0.32682 0.21376 0.00045  0.03082  0.01375  159 GLU A CD  
1387 O OE1 A GLU A 159 ? 0.11340 0.23525 0.18181 -0.06702 0.02157  -0.01269 159 GLU A OE1 
1388 O OE1 B GLU A 159 ? 0.19538 0.33179 0.21954 -0.01796 0.06123  0.05103  159 GLU A OE1 
1389 O OE2 A GLU A 159 ? 0.15846 0.17820 0.16140 -0.00186 0.09530  -0.00333 159 GLU A OE2 
1390 O OE2 B GLU A 159 ? 0.16865 0.33174 0.22114 0.00027  -0.01614 -0.01824 159 GLU A OE2 
1391 N N   . ASN A 160 ? 0.12321 0.16341 0.13553 0.00005  0.00755  0.04112  160 ASN A N   
1392 C CA  . ASN A 160 ? 0.16207 0.12956 0.15213 0.00612  0.03738  0.02684  160 ASN A CA  
1393 C C   . ASN A 160 ? 0.16621 0.17577 0.13205 0.02851  0.04218  0.04913  160 ASN A C   
1394 O O   . ASN A 160 ? 0.14317 0.18833 0.10743 0.00892  0.03755  0.05305  160 ASN A O   
1395 C CB  . ASN A 160 ? 0.17649 0.13407 0.16784 -0.01259 0.06763  0.04648  160 ASN A CB  
1396 C CG  . ASN A 160 ? 0.18576 0.15092 0.16609 -0.01586 0.08278  0.03301  160 ASN A CG  
1397 O OD1 . ASN A 160 ? 0.21401 0.19785 0.17336 -0.03082 0.10765  -0.00254 160 ASN A OD1 
1398 N ND2 . ASN A 160 ? 0.20636 0.14238 0.14766 -0.04184 0.06113  0.02729  160 ASN A ND2 
1399 N N   . ILE A 161 ? 0.16562 0.15812 0.13676 0.02950  0.04906  0.03573  161 ILE A N   
1400 C CA  . ILE A 161 ? 0.18568 0.16059 0.12507 0.00835  0.07190  -0.00877 161 ILE A CA  
1401 C C   . ILE A 161 ? 0.16457 0.17976 0.10598 0.01953  0.03319  0.01527  161 ILE A C   
1402 O O   . ILE A 161 ? 0.14714 0.18461 0.10246 0.00562  -0.01350 -0.02697 161 ILE A O   
1403 C CB  . ILE A 161 ? 0.17942 0.18163 0.12505 0.01750  0.05264  -0.01490 161 ILE A CB  
1404 C CG1 . ILE A 161 ? 0.20148 0.19995 0.14868 0.04665  0.06868  -0.05467 161 ILE A CG1 
1405 C CG2 . ILE A 161 ? 0.17479 0.18817 0.11778 -0.00629 0.06694  -0.00689 161 ILE A CG2 
1406 C CD1 . ILE A 161 ? 0.19914 0.21590 0.14832 0.04579  0.04627  -0.06415 161 ILE A CD1 
1407 N N   . LYS A 162 ? 0.14208 0.12586 0.11495 0.02526  0.01160  0.01105  162 LYS A N   
1408 C CA  . LYS A 162 ? 0.12164 0.15189 0.13113 0.03227  -0.04392 0.03945  162 LYS A CA  
1409 C C   . LYS A 162 ? 0.13023 0.17634 0.14009 0.00480  -0.01783 0.02071  162 LYS A C   
1410 O O   . LYS A 162 ? 0.11959 0.16267 0.13727 -0.00365 0.00408  0.00968  162 LYS A O   
1411 C CB  . LYS A 162 ? 0.16982 0.18762 0.14078 0.04684  -0.03647 0.06946  162 LYS A CB  
1412 C CG  . LYS A 162 ? 0.20619 0.23635 0.15553 0.07011  -0.03965 0.07053  162 LYS A CG  
1413 C CD  . LYS A 162 ? 0.24432 0.25960 0.17948 0.08199  -0.00269 0.05040  162 LYS A CD  
1414 C CE  . LYS A 162 ? 0.21967 0.19479 0.18109 0.10009  -0.00103 0.06131  162 LYS A CE  
1415 N NZ  . LYS A 162 ? 0.18163 0.18686 0.16360 0.06635  -0.00445 0.03415  162 LYS A NZ  
1416 N N   . ASN A 163 ? 0.11754 0.14540 0.17689 0.01374  0.01198  0.03932  163 ASN A N   
1417 C CA  . ASN A 163 ? 0.12339 0.18300 0.18010 0.01452  0.02339  0.04519  163 ASN A CA  
1418 C C   . ASN A 163 ? 0.12234 0.16452 0.15977 0.01510  0.02566  0.05148  163 ASN A C   
1419 O O   . ASN A 163 ? 0.14630 0.20086 0.15740 0.03300  0.03623  0.05768  163 ASN A O   
1420 C CB  . ASN A 163 ? 0.12605 0.18273 0.20020 0.01077  0.02846  0.00870  163 ASN A CB  
1421 C CG  . ASN A 163 ? 0.15880 0.23132 0.22492 0.02835  0.03780  -0.01519 163 ASN A CG  
1422 O OD1 . ASN A 163 ? 0.20895 0.26258 0.26058 0.05268  0.05688  -0.01290 163 ASN A OD1 
1423 N ND2 . ASN A 163 ? 0.15095 0.27473 0.21709 0.01040  -0.00108 -0.02519 163 ASN A ND2 
1424 N N   . LEU A 164 ? 0.11024 0.14777 0.14121 -0.00371 0.03768  0.03809  164 LEU A N   
1425 C CA  . LEU A 164 ? 0.12949 0.16227 0.12091 0.02542  0.01363  0.02567  164 LEU A CA  
1426 C C   . LEU A 164 ? 0.12394 0.13003 0.10619 0.01872  0.00660  0.05387  164 LEU A C   
1427 O O   . LEU A 164 ? 0.18756 0.16327 0.11062 0.01485  0.04114  0.03096  164 LEU A O   
1428 C CB  . LEU A 164 ? 0.14478 0.17396 0.12860 0.05849  0.01503  0.01330  164 LEU A CB  
1429 C CG  . LEU A 164 ? 0.18555 0.19353 0.12907 0.05808  0.02228  0.00263  164 LEU A CG  
1430 C CD1 . LEU A 164 ? 0.19235 0.23758 0.11840 0.06156  -0.02151 0.02921  164 LEU A CD1 
1431 C CD2 . LEU A 164 ? 0.20610 0.20692 0.13302 0.07452  0.03221  -0.00889 164 LEU A CD2 
1432 N N   . ILE A 165 ? 0.11334 0.13574 0.08040 0.00278  0.01399  0.02134  165 ILE A N   
1433 C CA  . ILE A 165 ? 0.14621 0.13613 0.08172 -0.00813 0.02623  -0.00954 165 ILE A CA  
1434 C C   . ILE A 165 ? 0.14758 0.13402 0.07555 0.03961  0.03143  -0.00436 165 ILE A C   
1435 O O   . ILE A 165 ? 0.14339 0.14763 0.05114 0.00642  0.03006  -0.02066 165 ILE A O   
1436 C CB  . ILE A 165 ? 0.15861 0.11558 0.06769 -0.02819 0.04296  -0.02435 165 ILE A CB  
1437 C CG1 . ILE A 165 ? 0.17921 0.13347 0.09259 -0.04048 0.04594  -0.04781 165 ILE A CG1 
1438 C CG2 . ILE A 165 ? 0.16118 0.12661 0.06770 -0.03405 0.04456  -0.01687 165 ILE A CG2 
1439 C CD1 . ILE A 165 ? 0.18463 0.16992 0.09872 -0.04332 0.04841  -0.05493 165 ILE A CD1 
1440 N N   . LEU A 166 ? 0.17063 0.14077 0.12453 0.06286  0.03710  -0.00925 166 LEU A N   
1441 C CA  . LEU A 166 ? 0.15457 0.16519 0.13952 0.02008  -0.00478 -0.01967 166 LEU A CA  
1442 C C   . LEU A 166 ? 0.19378 0.18870 0.13245 0.01471  0.00060  -0.04604 166 LEU A C   
1443 O O   . LEU A 166 ? 0.24226 0.18450 0.12788 -0.00654 -0.01502 -0.05975 166 LEU A O   
1444 C CB  . LEU A 166 ? 0.12736 0.16759 0.17711 0.03269  0.00080  0.01751  166 LEU A CB  
1445 C CG  . LEU A 166 ? 0.12136 0.18895 0.19623 0.01291  -0.01148 0.05851  166 LEU A CG  
1446 C CD1 . LEU A 166 ? 0.11731 0.23791 0.20293 0.01856  0.01327  0.02942  166 LEU A CD1 
1447 C CD2 . LEU A 166 ? 0.11089 0.17820 0.21647 -0.00503 -0.00189 0.07013  166 LEU A CD2 
1448 N N   . VAL A 167 ? 0.15394 0.19776 0.10767 0.00877  0.00419  -0.02044 167 VAL A N   
1449 C CA  . VAL A 167 ? 0.15191 0.18292 0.08501 -0.04502 0.01051  -0.02673 167 VAL A CA  
1450 C C   . VAL A 167 ? 0.17053 0.12433 0.08246 -0.02490 0.05022  -0.00682 167 VAL A C   
1451 O O   . VAL A 167 ? 0.20150 0.16411 0.06779 -0.03088 0.02671  -0.01801 167 VAL A O   
1452 C CB  . VAL A 167 ? 0.17152 0.23136 0.08114 -0.03430 0.04436  -0.00575 167 VAL A CB  
1453 C CG1 . VAL A 167 ? 0.19525 0.23443 0.09241 -0.03144 0.05852  0.00475  167 VAL A CG1 
1454 C CG2 . VAL A 167 ? 0.18438 0.24256 0.10199 -0.02262 0.06691  -0.00801 167 VAL A CG2 
1455 N N   . GLY A 168 ? 0.15661 0.10347 0.10341 0.02338  0.02551  0.00351  168 GLY A N   
1456 C CA  . GLY A 168 ? 0.13753 0.11823 0.14598 0.01375  0.01951  -0.02144 168 GLY A CA  
1457 C C   . GLY A 168 ? 0.14058 0.14193 0.14596 -0.01770 0.02556  -0.03548 168 GLY A C   
1458 O O   . GLY A 168 ? 0.12177 0.15502 0.16807 -0.01940 0.01881  -0.01776 168 GLY A O   
1459 N N   . TRP A 169 ? 0.14194 0.11362 0.11471 0.00229  0.01486  0.00346  169 TRP A N   
1460 C CA  . TRP A 169 ? 0.18470 0.13096 0.12531 0.02064  0.02446  -0.00160 169 TRP A CA  
1461 C C   . TRP A 169 ? 0.15673 0.14701 0.12273 0.04138  0.02276  -0.01835 169 TRP A C   
1462 O O   . TRP A 169 ? 0.15003 0.14395 0.11085 0.03357  0.04774  -0.00378 169 TRP A O   
1463 C CB  . TRP A 169 ? 0.16600 0.18077 0.12153 -0.00505 0.03923  0.02283  169 TRP A CB  
1464 C CG  . TRP A 169 ? 0.12932 0.20028 0.12735 -0.00455 0.04711  0.01896  169 TRP A CG  
1465 C CD1 . TRP A 169 ? 0.14265 0.22880 0.12581 0.00865  0.02613  0.01761  169 TRP A CD1 
1466 C CD2 . TRP A 169 ? 0.11908 0.22733 0.11471 -0.00293 0.05506  0.02824  169 TRP A CD2 
1467 N NE1 . TRP A 169 ? 0.10324 0.23741 0.12022 0.00453  0.02763  -0.00313 169 TRP A NE1 
1468 C CE2 . TRP A 169 ? 0.11622 0.25342 0.10728 -0.00210 0.04496  0.01173  169 TRP A CE2 
1469 C CE3 . TRP A 169 ? 0.13701 0.26753 0.13248 -0.01235 0.05545  0.04545  169 TRP A CE3 
1470 C CZ2 . TRP A 169 ? 0.14181 0.24382 0.10361 -0.02813 0.03821  0.01225  169 TRP A CZ2 
1471 C CZ3 . TRP A 169 ? 0.13623 0.25592 0.11300 -0.02635 0.04765  0.03263  169 TRP A CZ3 
1472 C CH2 . TRP A 169 ? 0.13263 0.24856 0.10091 -0.04148 0.03378  0.01655  169 TRP A CH2 
1473 N N   . ILE A 170 ? 0.13548 0.13651 0.11781 0.03139  0.01321  -0.04621 170 ILE A N   
1474 C CA  . ILE A 170 ? 0.14052 0.16955 0.11070 0.03830  0.02094  -0.03030 170 ILE A CA  
1475 C C   . ILE A 170 ? 0.13765 0.12318 0.08617 0.00769  0.04027  -0.01664 170 ILE A C   
1476 O O   . ILE A 170 ? 0.18782 0.10545 0.08913 0.01386  0.05552  -0.00706 170 ILE A O   
1477 C CB  . ILE A 170 ? 0.09113 0.21882 0.13783 0.02285  -0.03954 -0.06801 170 ILE A CB  
1478 C CG1 . ILE A 170 ? 0.10716 0.22894 0.14116 0.06791  -0.00741 -0.06026 170 ILE A CG1 
1479 C CG2 . ILE A 170 ? 0.11492 0.23182 0.18492 0.01043  -0.03181 -0.07124 170 ILE A CG2 
1480 C CD1 . ILE A 170 ? 0.19853 0.26948 0.16278 0.07398  0.01008  -0.06527 170 ILE A CD1 
1481 N N   . ILE A 171 ? 0.10946 0.13208 0.08354 0.03611  0.04693  0.00176  171 ILE A N   
1482 C CA  . ILE A 171 ? 0.14242 0.11728 0.08447 0.03892  0.02120  0.02946  171 ILE A CA  
1483 C C   . ILE A 171 ? 0.15833 0.13401 0.09007 0.00340  0.02556  0.02791  171 ILE A C   
1484 O O   . ILE A 171 ? 0.14604 0.16901 0.08433 -0.01534 0.05068  -0.00664 171 ILE A O   
1485 C CB  . ILE A 171 ? 0.13380 0.12150 0.11705 -0.00794 0.02050  0.03526  171 ILE A CB  
1486 C CG1 . ILE A 171 ? 0.15940 0.13014 0.14991 -0.06126 0.01498  0.00743  171 ILE A CG1 
1487 C CG2 . ILE A 171 ? 0.11995 0.12915 0.11935 0.00787  -0.00337 -0.00042 171 ILE A CG2 
1488 C CD1 . ILE A 171 ? 0.16975 0.13060 0.17344 -0.04791 -0.00527 -0.00613 171 ILE A CD1 
1489 N N   . TYR A 172 ? 0.17253 0.11589 0.08137 -0.01806 0.02297  -0.01516 172 TYR A N   
1490 C CA  . TYR A 172 ? 0.17426 0.13342 0.11101 -0.01512 0.03887  -0.02560 172 TYR A CA  
1491 C C   . TYR A 172 ? 0.13580 0.11695 0.11581 -0.00575 0.02175  -0.00865 172 TYR A C   
1492 O O   . TYR A 172 ? 0.10717 0.11192 0.14512 -0.01821 -0.00001 -0.00447 172 TYR A O   
1493 C CB  . TYR A 172 ? 0.17753 0.14820 0.10678 0.01722  0.04615  -0.02307 172 TYR A CB  
1494 C CG  . TYR A 172 ? 0.16366 0.10970 0.10173 -0.00069 0.03879  -0.03727 172 TYR A CG  
1495 C CD1 . TYR A 172 ? 0.13535 0.08584 0.11003 0.02377  0.03175  -0.04162 172 TYR A CD1 
1496 C CD2 . TYR A 172 ? 0.13823 0.12305 0.11149 -0.01637 0.05130  0.01347  172 TYR A CD2 
1497 C CE1 . TYR A 172 ? 0.14893 0.11437 0.10945 -0.02185 0.01859  -0.01569 172 TYR A CE1 
1498 C CE2 . TYR A 172 ? 0.16692 0.09739 0.10613 0.00904  0.06080  0.03424  172 TYR A CE2 
1499 C CZ  . TYR A 172 ? 0.13643 0.10697 0.10943 -0.01604 0.03977  0.01367  172 TYR A CZ  
1500 O OH  . TYR A 172 ? 0.15104 0.12576 0.08109 -0.02362 -0.02244 0.01878  172 TYR A OH  
1501 N N   . PRO A 173 ? 0.12648 0.11888 0.10424 0.01339  0.00999  0.01556  173 PRO A N   
1502 C CA  . PRO A 173 ? 0.13131 0.12493 0.11228 0.02240  -0.01030 0.00521  173 PRO A CA  
1503 C C   . PRO A 173 ? 0.15202 0.12078 0.12169 -0.00945 -0.00082 -0.00454 173 PRO A C   
1504 O O   . PRO A 173 ? 0.14155 0.14455 0.12402 -0.00936 0.01703  -0.01648 173 PRO A O   
1505 C CB  . PRO A 173 ? 0.11610 0.14915 0.11633 -0.00066 0.00177  0.01881  173 PRO A CB  
1506 C CG  . PRO A 173 ? 0.14225 0.11684 0.11460 -0.00512 0.00326  -0.00476 173 PRO A CG  
1507 C CD  . PRO A 173 ? 0.12430 0.11005 0.10650 0.01444  -0.00208 0.01561  173 PRO A CD  
1508 N N   . LEU A 174 ? 0.15161 0.17020 0.15508 0.02611  0.03688  0.00154  174 LEU A N   
1509 C CA  . LEU A 174 ? 0.15347 0.16504 0.14221 0.01037  0.00397  0.02375  174 LEU A CA  
1510 C C   . LEU A 174 ? 0.16888 0.15065 0.17584 0.00391  0.04441  0.04571  174 LEU A C   
1511 O O   . LEU A 174 ? 0.22154 0.16101 0.19547 0.01382  0.04507  0.02293  174 LEU A O   
1512 C CB  . LEU A 174 ? 0.14237 0.20935 0.13652 0.00398  -0.01076 0.00990  174 LEU A CB  
1513 C CG  . LEU A 174 ? 0.15827 0.24509 0.16133 -0.02295 -0.03950 0.00669  174 LEU A CG  
1514 C CD1 . LEU A 174 ? 0.17005 0.30184 0.17929 -0.00577 -0.02550 0.04840  174 LEU A CD1 
1515 C CD2 . LEU A 174 ? 0.21879 0.28062 0.18572 -0.01114 -0.00657 -0.01862 174 LEU A CD2 
1516 N N   . GLY A 175 ? 0.14803 0.15311 0.16444 -0.00080 0.05460  0.03112  175 GLY A N   
1517 C CA  . GLY A 175 ? 0.09677 0.15360 0.16091 0.02231  0.02862  0.03059  175 GLY A CA  
1518 C C   . GLY A 175 ? 0.08442 0.11860 0.16435 0.02135  0.03129  0.01429  175 GLY A C   
1519 O O   . GLY A 175 ? 0.08879 0.15675 0.17984 0.00892  0.02303  0.01150  175 GLY A O   
1520 N N   . TYR A 176 ? 0.12997 0.10029 0.15587 0.02091  0.02892  0.00630  176 TYR A N   
1521 C CA  . TYR A 176 ? 0.17794 0.10145 0.16779 0.00518  0.00518  -0.00072 176 TYR A CA  
1522 C C   . TYR A 176 ? 0.19297 0.09960 0.17925 -0.01056 -0.01113 -0.01846 176 TYR A C   
1523 O O   . TYR A 176 ? 0.18692 0.12041 0.18359 -0.03185 -0.01009 -0.02360 176 TYR A O   
1524 C CB  . TYR A 176 ? 0.18283 0.08819 0.15829 0.00896  -0.00706 0.00203  176 TYR A CB  
1525 C CG  . TYR A 176 ? 0.16545 0.09182 0.16766 -0.00939 -0.02752 -0.01359 176 TYR A CG  
1526 C CD1 . TYR A 176 ? 0.15189 0.12346 0.16648 0.01216  -0.04255 0.01229  176 TYR A CD1 
1527 C CD2 . TYR A 176 ? 0.15746 0.09092 0.17404 -0.01101 -0.03778 -0.04842 176 TYR A CD2 
1528 C CE1 . TYR A 176 ? 0.15396 0.14711 0.16023 0.00261  -0.04334 0.01996  176 TYR A CE1 
1529 C CE2 . TYR A 176 ? 0.14219 0.12225 0.16837 -0.04910 -0.04338 -0.04347 176 TYR A CE2 
1530 C CZ  . TYR A 176 ? 0.13670 0.14578 0.18483 -0.01426 -0.04064 0.00802  176 TYR A CZ  
1531 O OH  . TYR A 176 ? 0.17403 0.15888 0.18596 -0.01547 -0.01388 0.02816  176 TYR A OH  
1532 N N   A ILE A 177 ? 0.19429 0.11492 0.18354 0.00829  -0.01645 -0.01526 177 ILE A N   
1533 N N   B ILE A 177 ? 0.19407 0.11009 0.19213 0.00934  -0.01240 -0.01822 177 ILE A N   
1534 C CA  A ILE A 177 ? 0.20563 0.16500 0.19124 0.01050  -0.00191 -0.01442 177 ILE A CA  
1535 C CA  B ILE A 177 ? 0.19995 0.14147 0.20836 0.01725  -0.01007 -0.01790 177 ILE A CA  
1536 C C   A ILE A 177 ? 0.21563 0.17004 0.21262 0.00058  0.01434  -0.00636 177 ILE A C   
1537 C C   B ILE A 177 ? 0.20740 0.15334 0.22814 0.02885  0.00030  -0.00984 177 ILE A C   
1538 O O   A ILE A 177 ? 0.22520 0.17149 0.22752 -0.02872 0.04147  -0.01440 177 ILE A O   
1539 O O   B ILE A 177 ? 0.19824 0.13860 0.25247 0.02510  -0.00346 -0.01597 177 ILE A O   
1540 C CB  A ILE A 177 ? 0.19893 0.20269 0.17670 -0.00083 0.00197  -0.03456 177 ILE A CB  
1541 C CB  B ILE A 177 ? 0.19760 0.16161 0.20175 0.00244  -0.00446 -0.03377 177 ILE A CB  
1542 C CG1 A ILE A 177 ? 0.18587 0.19829 0.17327 0.01941  -0.01295 -0.02740 177 ILE A CG1 
1543 C CG1 B ILE A 177 ? 0.18742 0.11455 0.16431 -0.03764 -0.01046 -0.04041 177 ILE A CG1 
1544 C CG2 A ILE A 177 ? 0.21944 0.21131 0.16225 -0.01410 0.00919  -0.03954 177 ILE A CG2 
1545 C CG2 B ILE A 177 ? 0.18931 0.20142 0.20784 0.01163  -0.00662 -0.04109 177 ILE A CG2 
1546 C CD1 A ILE A 177 ? 0.20742 0.18971 0.19881 0.02935  -0.00691 -0.02281 177 ILE A CD1 
1547 C CD1 B ILE A 177 ? 0.17162 0.11291 0.15850 -0.05673 -0.00448 -0.03891 177 ILE A CD1 
1548 N N   . ALA A 178 ? 0.21597 0.16428 0.22117 0.01311  -0.00855 0.01116  178 ALA A N   
1549 C CA  . ALA A 178 ? 0.22258 0.15320 0.21743 0.00142  -0.04158 0.02288  178 ALA A CA  
1550 C C   . ALA A 178 ? 0.21530 0.21374 0.20457 -0.01366 -0.06265 -0.01086 178 ALA A C   
1551 O O   . ALA A 178 ? 0.23452 0.23711 0.20147 -0.01264 -0.07600 -0.01585 178 ALA A O   
1552 C CB  . ALA A 178 ? 0.25476 0.15296 0.22778 -0.00631 -0.01553 0.05992  178 ALA A CB  
1553 N N   . PRO A 179 ? 0.18323 0.18836 0.22404 -0.02576 -0.06878 -0.04016 179 PRO A N   
1554 C CA  . PRO A 179 ? 0.19182 0.20699 0.24112 -0.01725 -0.07892 -0.05697 179 PRO A CA  
1555 C C   . PRO A 179 ? 0.21616 0.22639 0.24798 -0.01952 -0.10538 -0.06832 179 PRO A C   
1556 O O   . PRO A 179 ? 0.23172 0.25062 0.25971 -0.02776 -0.10997 -0.04728 179 PRO A O   
1557 C CB  . PRO A 179 ? 0.21221 0.22817 0.25665 -0.02292 -0.02032 -0.06518 179 PRO A CB  
1558 C CG  . PRO A 179 ? 0.22292 0.25034 0.27387 -0.01704 -0.01016 -0.03903 179 PRO A CG  
1559 C CD  . PRO A 179 ? 0.19217 0.22833 0.23285 -0.01545 -0.05794 -0.00996 179 PRO A CD  
1560 N N   . VAL A 180 ? 0.26291 0.18723 0.26750 0.01711  -0.09220 -0.07963 180 VAL A N   
1561 C CA  . VAL A 180 ? 0.30585 0.18984 0.30287 -0.02568 -0.06715 -0.08902 180 VAL A CA  
1562 C C   . VAL A 180 ? 0.35504 0.20905 0.33753 -0.05017 -0.05891 -0.10691 180 VAL A C   
1563 O O   . VAL A 180 ? 0.37135 0.22563 0.34544 -0.04907 -0.06758 -0.08728 180 VAL A O   
1564 C CB  . VAL A 180 ? 0.29847 0.21504 0.29803 -0.00628 -0.07120 -0.06862 180 VAL A CB  
1565 C CG1 . VAL A 180 ? 0.31458 0.23409 0.31245 -0.01754 -0.06725 -0.03521 180 VAL A CG1 
1566 C CG2 . VAL A 180 ? 0.28400 0.21630 0.28516 0.00174  -0.07527 -0.07522 180 VAL A CG2 
1567 N N   . VAL A 181 ? 0.38554 0.30694 0.37735 -0.04929 -0.03507 -0.10882 181 VAL A N   
1568 C CA  . VAL A 181 ? 0.43709 0.39462 0.42237 -0.02514 -0.00390 -0.09082 181 VAL A CA  
1569 C C   . VAL A 181 ? 0.42042 0.38387 0.40547 0.00554  0.01310  -0.07377 181 VAL A C   
1570 O O   . VAL A 181 ? 0.43068 0.39453 0.42127 0.01676  0.03561  -0.06854 181 VAL A O   
1571 C CB  . VAL A 181 ? 0.51722 0.45914 0.49038 -0.00534 0.01189  -0.09176 181 VAL A CB  
1572 C CG1 . VAL A 181 ? 0.55932 0.50276 0.52946 -0.01048 0.04924  -0.07359 181 VAL A CG1 
1573 C CG2 . VAL A 181 ? 0.52695 0.47331 0.49416 0.02568  -0.01039 -0.10230 181 VAL A CG2 
1574 N N   . GLY A 182 ? 0.42248 0.39735 0.38612 0.00429  -0.00743 -0.05737 182 GLY A N   
1575 C CA  . GLY A 182 ? 0.42568 0.41031 0.39371 -0.03389 -0.02992 -0.07512 182 GLY A CA  
1576 C C   . GLY A 182 ? 0.42016 0.40073 0.39902 -0.06905 -0.04276 -0.07993 182 GLY A C   
1577 O O   . GLY A 182 ? 0.41847 0.39638 0.39374 -0.08844 -0.05097 -0.07865 182 GLY A O   
1578 N N   . ASP A 183 ? 0.43084 0.42928 0.38568 -0.06497 -0.04277 -0.06156 183 ASP A N   
1579 C CA  . ASP A 183 ? 0.43940 0.47262 0.39522 -0.04778 -0.03896 -0.01908 183 ASP A CA  
1580 C C   . ASP A 183 ? 0.40635 0.40455 0.37048 -0.06380 -0.05439 -0.02229 183 ASP A C   
1581 O O   . ASP A 183 ? 0.39795 0.45224 0.36886 -0.05688 -0.05570 -0.05001 183 ASP A O   
1582 C CB  . ASP A 183 ? 0.48102 0.54636 0.43965 -0.01713 -0.04307 0.00166  183 ASP A CB  
1583 C CG  . ASP A 183 ? 0.55771 0.63627 0.48648 -0.01805 0.00894  0.00306  183 ASP A CG  
1584 O OD1 . ASP A 183 ? 0.53330 0.62610 0.46445 -0.02568 -0.01455 -0.01397 183 ASP A OD1 
1585 O OD2 . ASP A 183 ? 0.54739 0.64058 0.46683 -0.01834 -0.01765 0.01384  183 ASP A OD2 
1586 N N   . PHE A 184 ? 0.36495 0.34447 0.34704 -0.08181 -0.06208 -0.01516 184 PHE A N   
1587 C CA  . PHE A 184 ? 0.37271 0.34465 0.35312 -0.07292 -0.00813 -0.02328 184 PHE A CA  
1588 C C   . PHE A 184 ? 0.33545 0.24318 0.35685 -0.00162 -0.00152 0.00581  184 PHE A C   
1589 O O   . PHE A 184 ? 0.33174 0.26894 0.37768 0.05177  0.02172  0.03884  184 PHE A O   
1590 C CB  . PHE A 184 ? 0.40943 0.38898 0.37341 -0.07768 -0.02927 -0.03205 184 PHE A CB  
1591 C CG  . PHE A 184 ? 0.47101 0.47641 0.40141 -0.03392 0.00315  -0.01135 184 PHE A CG  
1592 C CD1 . PHE A 184 ? 0.45813 0.48345 0.39992 -0.03920 -0.00663 -0.01853 184 PHE A CD1 
1593 C CD2 . PHE A 184 ? 0.49840 0.53328 0.41306 -0.00301 0.02596  0.00590  184 PHE A CD2 
1594 C CE1 . PHE A 184 ? 0.47106 0.49632 0.39068 -0.04590 0.01953  -0.02242 184 PHE A CE1 
1595 C CE2 . PHE A 184 ? 0.48706 0.52112 0.40959 -0.01273 0.03227  0.00713  184 PHE A CE2 
1596 C CZ  . PHE A 184 ? 0.50555 0.53086 0.39538 -0.03197 0.06091  -0.00692 184 PHE A CZ  
1597 N N   . ASP A 185 ? 0.29933 0.19354 0.32574 0.01340  0.02039  -0.02819 185 ASP A N   
1598 C CA  . ASP A 185 ? 0.25495 0.20653 0.29397 0.00504  0.03557  -0.00261 185 ASP A CA  
1599 C C   . ASP A 185 ? 0.19833 0.19305 0.24941 -0.01495 0.01084  0.00298  185 ASP A C   
1600 O O   . ASP A 185 ? 0.21033 0.22041 0.24502 -0.00051 0.02629  0.04139  185 ASP A O   
1601 C CB  . ASP A 185 ? 0.26710 0.23276 0.30355 -0.00790 0.05283  0.00863  185 ASP A CB  
1602 C CG  . ASP A 185 ? 0.30107 0.34192 0.30928 -0.03726 0.09569  0.02072  185 ASP A CG  
1603 O OD1 . ASP A 185 ? 0.27493 0.30146 0.32258 -0.04050 0.05200  0.03903  185 ASP A OD1 
1604 O OD2 . ASP A 185 ? 0.30498 0.33601 0.33313 -0.05324 0.07869  0.02339  185 ASP A OD2 
1605 N N   . ALA A 186 ? 0.16278 0.17963 0.21801 -0.00246 0.00105  -0.00108 186 ALA A N   
1606 C CA  . ALA A 186 ? 0.13834 0.17737 0.19769 0.03510  -0.01882 0.01421  186 ALA A CA  
1607 C C   . ALA A 186 ? 0.14796 0.18524 0.17286 0.04615  -0.01172 0.01873  186 ALA A C   
1608 O O   . ALA A 186 ? 0.20598 0.20175 0.15459 0.06545  0.02078  -0.02768 186 ALA A O   
1609 C CB  . ALA A 186 ? 0.15000 0.18281 0.20772 0.01525  -0.03902 0.01964  186 ALA A CB  
1610 N N   . ILE A 187 ? 0.13172 0.19852 0.16061 0.05057  -0.00117 0.01610  187 ILE A N   
1611 C CA  . ILE A 187 ? 0.13671 0.20854 0.14494 0.03442  -0.04667 -0.01814 187 ILE A CA  
1612 C C   . ILE A 187 ? 0.13462 0.21272 0.11463 -0.01129 -0.04407 -0.03805 187 ILE A C   
1613 O O   . ILE A 187 ? 0.14707 0.22749 0.10445 -0.00579 -0.04263 -0.05525 187 ILE A O   
1614 C CB  . ILE A 187 ? 0.18227 0.22606 0.15316 0.01835  -0.05313 -0.03702 187 ILE A CB  
1615 C CG1 . ILE A 187 ? 0.23627 0.25701 0.17832 0.01543  -0.02688 -0.02931 187 ILE A CG1 
1616 C CG2 . ILE A 187 ? 0.20731 0.23092 0.14037 0.05509  -0.02879 -0.04627 187 ILE A CG2 
1617 C CD1 . ILE A 187 ? 0.25638 0.25420 0.19445 -0.00438 -0.00984 -0.01836 187 ILE A CD1 
1618 N N   . ARG A 188 ? 0.17390 0.17745 0.10610 -0.02006 0.00246  -0.04066 188 ARG A N   
1619 C CA  . ARG A 188 ? 0.18554 0.10776 0.08294 -0.03750 0.01218  -0.01281 188 ARG A CA  
1620 C C   . ARG A 188 ? 0.18375 0.09674 0.06807 -0.02328 0.01430  -0.00542 188 ARG A C   
1621 O O   . ARG A 188 ? 0.17399 0.13807 0.07368 -0.02624 -0.00025 0.00591  188 ARG A O   
1622 C CB  . ARG A 188 ? 0.18551 0.12644 0.09625 -0.04172 0.03757  -0.03957 188 ARG A CB  
1623 C CG  . ARG A 188 ? 0.14920 0.14460 0.09184 -0.04222 0.00456  -0.04488 188 ARG A CG  
1624 C CD  . ARG A 188 ? 0.13977 0.19341 0.09283 -0.02015 0.00721  -0.02831 188 ARG A CD  
1625 N NE  . ARG A 188 ? 0.17398 0.19881 0.10538 -0.00763 -0.00418 -0.01829 188 ARG A NE  
1626 C CZ  . ARG A 188 ? 0.17272 0.20982 0.12504 0.00150  -0.01235 -0.01390 188 ARG A CZ  
1627 N NH1 . ARG A 188 ? 0.18553 0.20235 0.10301 0.01625  -0.00478 -0.01049 188 ARG A NH1 
1628 N NH2 . ARG A 188 ? 0.17881 0.20395 0.17073 0.03742  -0.03013 0.01811  188 ARG A NH2 
1629 N N   . GLU A 189 ? 0.14661 0.11800 0.04372 0.00923  0.02347  0.00358  189 GLU A N   
1630 C CA  . GLU A 189 ? 0.12442 0.13646 0.05159 0.02112  0.01561  0.03078  189 GLU A CA  
1631 C C   . GLU A 189 ? 0.12520 0.18541 0.05389 0.01654  0.00286  0.02672  189 GLU A C   
1632 O O   . GLU A 189 ? 0.14390 0.20591 0.06649 -0.02305 0.02922  0.01555  189 GLU A O   
1633 C CB  . GLU A 189 ? 0.12240 0.18342 0.07080 -0.00644 0.04154  0.01267  189 GLU A CB  
1634 C CG  . GLU A 189 ? 0.12700 0.15028 0.07858 0.00178  0.02479  -0.00573 189 GLU A CG  
1635 C CD  . GLU A 189 ? 0.16183 0.15555 0.11827 -0.00068 0.01568  -0.02518 189 GLU A CD  
1636 O OE1 . GLU A 189 ? 0.18701 0.19082 0.13150 0.00126  0.00027  -0.03132 189 GLU A OE1 
1637 O OE2 . GLU A 189 ? 0.19204 0.18096 0.14537 0.01274  -0.00217 0.00669  189 GLU A OE2 
1638 N N   . VAL A 190 ? 0.08910 0.18943 0.06822 0.04562  0.01984  0.03832  190 VAL A N   
1639 C CA  . VAL A 190 ? 0.15463 0.18941 0.07476 0.03290  0.01462  0.04925  190 VAL A CA  
1640 C C   . VAL A 190 ? 0.16061 0.16780 0.10776 0.02632  0.01868  0.03252  190 VAL A C   
1641 O O   . VAL A 190 ? 0.15462 0.14312 0.13133 0.01601  0.00674  0.00966  190 VAL A O   
1642 C CB  . VAL A 190 ? 0.15094 0.22225 0.07023 0.04022  0.00067  0.03536  190 VAL A CB  
1643 C CG1 . VAL A 190 ? 0.18334 0.22704 0.06400 0.04094  0.01095  0.00380  190 VAL A CG1 
1644 C CG2 . VAL A 190 ? 0.14516 0.23254 0.08016 0.04162  0.02141  0.04638  190 VAL A CG2 
1645 N N   . LEU A 191 ? 0.13506 0.15358 0.08959 0.01287  -0.00535 0.05445  191 LEU A N   
1646 C CA  . LEU A 191 ? 0.12575 0.14494 0.07756 0.01031  -0.01062 0.04841  191 LEU A CA  
1647 C C   . LEU A 191 ? 0.12545 0.14676 0.08505 -0.01271 -0.02329 0.02229  191 LEU A C   
1648 O O   . LEU A 191 ? 0.11751 0.16459 0.10009 -0.02567 0.00441  0.01931  191 LEU A O   
1649 C CB  . LEU A 191 ? 0.14447 0.17652 0.07443 -0.02389 0.01347  0.00810  191 LEU A CB  
1650 C CG  . LEU A 191 ? 0.18031 0.18129 0.10975 -0.03858 0.02546  -0.00771 191 LEU A CG  
1651 C CD1 . LEU A 191 ? 0.22895 0.15109 0.09583 -0.06305 0.04061  -0.01003 191 LEU A CD1 
1652 C CD2 . LEU A 191 ? 0.20150 0.19960 0.12065 -0.03223 0.04331  0.00366  191 LEU A CD2 
1653 N N   . TYR A 192 ? 0.13556 0.12853 0.10226 -0.01235 -0.01079 0.01994  192 TYR A N   
1654 C CA  . TYR A 192 ? 0.13950 0.10047 0.11532 -0.01448 -0.01313 0.02826  192 TYR A CA  
1655 C C   . TYR A 192 ? 0.08986 0.08596 0.13726 -0.00011 -0.00251 0.00259  192 TYR A C   
1656 O O   . TYR A 192 ? 0.09333 0.12671 0.13811 -0.00167 -0.00487 -0.02395 192 TYR A O   
1657 C CB  . TYR A 192 ? 0.15908 0.10262 0.09608 -0.03109 -0.00142 0.05037  192 TYR A CB  
1658 C CG  . TYR A 192 ? 0.16001 0.11582 0.06323 -0.00259 -0.03114 0.03030  192 TYR A CG  
1659 C CD1 . TYR A 192 ? 0.15100 0.11117 0.07116 0.01380  -0.03815 0.02838  192 TYR A CD1 
1660 C CD2 . TYR A 192 ? 0.13830 0.12448 0.04100 0.00389  -0.02151 0.00708  192 TYR A CD2 
1661 C CE1 . TYR A 192 ? 0.16597 0.12627 0.06648 -0.00108 -0.04528 0.01663  192 TYR A CE1 
1662 C CE2 . TYR A 192 ? 0.14311 0.11315 0.04610 0.02691  -0.02212 0.00177  192 TYR A CE2 
1663 C CZ  . TYR A 192 ? 0.17383 0.11762 0.06337 -0.00482 -0.04347 -0.00755 192 TYR A CZ  
1664 O OH  . TYR A 192 ? 0.17551 0.13272 0.09794 0.01307  -0.03459 -0.01716 192 TYR A OH  
1665 N N   . THR A 193 ? 0.11501 0.08505 0.15469 0.00703  0.03325  0.00286  193 THR A N   
1666 C CA  . THR A 193 ? 0.13517 0.08413 0.16240 0.05244  0.02436  0.01337  193 THR A CA  
1667 C C   . THR A 193 ? 0.14645 0.09499 0.12574 0.00136  0.01536  -0.03274 193 THR A C   
1668 O O   . THR A 193 ? 0.16319 0.10182 0.10680 0.00629  0.02058  -0.00969 193 THR A O   
1669 C CB  . THR A 193 ? 0.12896 0.09899 0.19083 0.05414  0.03115  -0.00922 193 THR A CB  
1670 O OG1 . THR A 193 ? 0.14308 0.14466 0.19880 0.01826  0.01062  -0.00495 193 THR A OG1 
1671 C CG2 . THR A 193 ? 0.12435 0.10106 0.21949 0.02950  0.01604  -0.00000 193 THR A CG2 
1672 N N   . ILE A 194 ? 0.16695 0.11599 0.11592 0.02121  0.01860  -0.02902 194 ILE A N   
1673 C CA  . ILE A 194 ? 0.18280 0.16233 0.10361 0.00715  0.04261  0.00314  194 ILE A CA  
1674 C C   . ILE A 194 ? 0.16388 0.13272 0.12854 0.00573  0.02914  -0.00056 194 ILE A C   
1675 O O   . ILE A 194 ? 0.19141 0.14283 0.13007 0.01342  0.03140  -0.00124 194 ILE A O   
1676 C CB  . ILE A 194 ? 0.14719 0.21889 0.10652 0.01058  0.06091  -0.00004 194 ILE A CB  
1677 C CG1 . ILE A 194 ? 0.17741 0.25827 0.10589 0.00193  0.04480  -0.01286 194 ILE A CG1 
1678 C CG2 . ILE A 194 ? 0.16831 0.25508 0.12252 -0.01370 0.07641  0.00967  194 ILE A CG2 
1679 C CD1 . ILE A 194 ? 0.21707 0.29773 0.14167 0.00197  0.05631  -0.02687 194 ILE A CD1 
1680 N N   . ALA A 195 ? 0.15086 0.14246 0.10612 0.03873  0.01388  0.00773  195 ALA A N   
1681 C CA  . ALA A 195 ? 0.15656 0.13255 0.08476 0.03610  -0.00906 0.00967  195 ALA A CA  
1682 C C   . ALA A 195 ? 0.14435 0.13375 0.10748 0.02265  -0.01804 0.00066  195 ALA A C   
1683 O O   . ALA A 195 ? 0.12385 0.14256 0.08873 -0.00545 -0.04878 0.00127  195 ALA A O   
1684 C CB  . ALA A 195 ? 0.15880 0.13089 0.07428 0.02106  -0.01771 0.04003  195 ALA A CB  
1685 N N   . ASP A 196 ? 0.15239 0.09420 0.11309 -0.00451 0.02411  0.00283  196 ASP A N   
1686 C CA  . ASP A 196 ? 0.14656 0.08877 0.13233 0.00861  0.03441  -0.02604 196 ASP A CA  
1687 C C   . ASP A 196 ? 0.12018 0.11226 0.14252 0.02023  0.02191  0.01586  196 ASP A C   
1688 O O   . ASP A 196 ? 0.13705 0.10975 0.13589 0.00819  0.00146  0.01422  196 ASP A O   
1689 C CB  . ASP A 196 ? 0.13299 0.13802 0.14912 -0.02258 0.08089  -0.03223 196 ASP A CB  
1690 C CG  . ASP A 196 ? 0.17538 0.16358 0.16299 -0.01055 0.09164  -0.04685 196 ASP A CG  
1691 O OD1 . ASP A 196 ? 0.16497 0.14361 0.16969 0.00371  0.08269  -0.02205 196 ASP A OD1 
1692 O OD2 . ASP A 196 ? 0.19032 0.17323 0.17976 -0.05022 0.08609  -0.05481 196 ASP A OD2 
1693 N N   . ILE A 197 ? 0.12848 0.10930 0.12882 -0.00442 0.03424  0.02413  197 ILE A N   
1694 C CA  . ILE A 197 ? 0.12411 0.12757 0.13301 0.01303  -0.00017 0.01792  197 ILE A CA  
1695 C C   . ILE A 197 ? 0.13524 0.14285 0.14820 -0.01714 -0.00173 0.01464  197 ILE A C   
1696 O O   . ILE A 197 ? 0.13489 0.16298 0.15846 -0.01523 -0.02752 0.01603  197 ILE A O   
1697 C CB  . ILE A 197 ? 0.14532 0.13157 0.15283 -0.00031 0.03841  -0.00863 197 ILE A CB  
1698 C CG1 . ILE A 197 ? 0.15941 0.15442 0.14485 0.00298  0.04191  -0.02262 197 ILE A CG1 
1699 C CG2 . ILE A 197 ? 0.16972 0.13916 0.15706 -0.02298 0.02873  -0.01156 197 ILE A CG2 
1700 C CD1 . ILE A 197 ? 0.20277 0.18964 0.14732 0.01223  0.06957  -0.02021 197 ILE A CD1 
1701 N N   . ILE A 198 ? 0.13380 0.14075 0.16775 -0.00484 0.03576  0.01156  198 ILE A N   
1702 C CA  . ILE A 198 ? 0.12609 0.16325 0.17945 0.00094  0.02216  -0.03391 198 ILE A CA  
1703 C C   . ILE A 198 ? 0.12427 0.15666 0.19954 -0.01946 0.02573  -0.02668 198 ILE A C   
1704 O O   . ILE A 198 ? 0.11367 0.13962 0.19537 -0.01814 -0.00139 -0.03178 198 ILE A O   
1705 C CB  . ILE A 198 ? 0.13670 0.18170 0.18193 0.02715  0.02503  -0.04853 198 ILE A CB  
1706 C CG1 . ILE A 198 ? 0.16548 0.17746 0.19154 0.04993  0.02462  -0.05997 198 ILE A CG1 
1707 C CG2 . ILE A 198 ? 0.14514 0.25141 0.17882 0.02460  0.01180  -0.06599 198 ILE A CG2 
1708 C CD1 . ILE A 198 ? 0.18077 0.19718 0.20693 0.06147  0.06324  -0.06057 198 ILE A CD1 
1709 N N   . ASN A 199 ? 0.10702 0.14899 0.19642 0.00760  0.02065  -0.01518 199 ASN A N   
1710 C CA  . ASN A 199 ? 0.15068 0.08875 0.18113 -0.00535 -0.01525 -0.01795 199 ASN A CA  
1711 C C   . ASN A 199 ? 0.16622 0.13337 0.19257 -0.02212 -0.01267 -0.01038 199 ASN A C   
1712 O O   . ASN A 199 ? 0.16909 0.17595 0.21810 -0.01520 -0.02441 -0.02761 199 ASN A O   
1713 C CB  . ASN A 199 ? 0.14366 0.06819 0.15054 0.00716  -0.02113 0.00184  199 ASN A CB  
1714 C CG  . ASN A 199 ? 0.18018 0.10213 0.15318 0.00878  -0.01491 -0.03777 199 ASN A CG  
1715 O OD1 . ASN A 199 ? 0.18023 0.14388 0.16816 0.01082  -0.01366 -0.04751 199 ASN A OD1 
1716 N ND2 . ASN A 199 ? 0.19271 0.12524 0.14413 -0.02048 -0.00665 -0.03722 199 ASN A ND2 
1717 N N   . LYS A 200 ? 0.16372 0.09860 0.18652 -0.00706 0.00544  0.01270  200 LYS A N   
1718 C CA  . LYS A 200 ? 0.16297 0.11016 0.17195 0.00536  -0.00387 -0.02345 200 LYS A CA  
1719 C C   . LYS A 200 ? 0.18195 0.09394 0.17123 -0.01581 -0.00503 -0.04351 200 LYS A C   
1720 O O   . LYS A 200 ? 0.19137 0.12093 0.15061 -0.00234 -0.00108 -0.00179 200 LYS A O   
1721 C CB  . LYS A 200 ? 0.13134 0.13801 0.17193 0.00270  0.04080  -0.01774 200 LYS A CB  
1722 C CG  . LYS A 200 ? 0.12860 0.16126 0.17403 0.00095  0.06885  0.00875  200 LYS A CG  
1723 C CD  . LYS A 200 ? 0.17950 0.17210 0.18610 -0.01634 0.09893  0.03489  200 LYS A CD  
1724 C CE  . LYS A 200 ? 0.18627 0.15430 0.16341 -0.03311 0.08332  0.03514  200 LYS A CE  
1725 N NZ  . LYS A 200 ? 0.18534 0.12229 0.13559 -0.03971 0.07451  0.01436  200 LYS A NZ  
1726 N N   . VAL A 201 ? 0.18140 0.11390 0.18806 -0.03149 -0.01847 -0.05710 201 VAL A N   
1727 C CA  . VAL A 201 ? 0.17013 0.13895 0.21398 -0.02720 -0.01781 -0.03351 201 VAL A CA  
1728 C C   . VAL A 201 ? 0.16011 0.07335 0.21384 -0.00273 -0.01061 -0.03225 201 VAL A C   
1729 O O   . VAL A 201 ? 0.17736 0.10677 0.20064 -0.01585 -0.02201 -0.04482 201 VAL A O   
1730 C CB  . VAL A 201 ? 0.13933 0.17923 0.24502 -0.05066 -0.04702 0.00089  201 VAL A CB  
1731 C CG1 . VAL A 201 ? 0.16707 0.19513 0.24040 -0.03322 -0.04804 0.03622  201 VAL A CG1 
1732 C CG2 . VAL A 201 ? 0.12953 0.22524 0.26737 -0.05438 -0.04279 -0.00596 201 VAL A CG2 
1733 N N   . GLY A 202 ? 0.13411 0.09204 0.22107 0.02752  -0.01222 -0.02093 202 GLY A N   
1734 C CA  . GLY A 202 ? 0.16190 0.12676 0.23390 -0.00144 -0.00629 -0.01771 202 GLY A CA  
1735 C C   . GLY A 202 ? 0.14730 0.10816 0.21815 -0.01165 -0.00833 -0.02983 202 GLY A C   
1736 O O   . GLY A 202 ? 0.15755 0.11746 0.21406 -0.02328 -0.01503 -0.01891 202 GLY A O   
1737 N N   . LEU A 203 ? 0.12448 0.10147 0.19555 0.02843  -0.01286 -0.03308 203 LEU A N   
1738 C CA  . LEU A 203 ? 0.10665 0.12462 0.17196 0.01608  -0.03331 -0.00774 203 LEU A CA  
1739 C C   . LEU A 203 ? 0.11261 0.12423 0.17562 0.02173  -0.04710 -0.00071 203 LEU A C   
1740 O O   . LEU A 203 ? 0.11973 0.15904 0.19294 -0.00230 -0.06696 -0.00277 203 LEU A O   
1741 C CB  . LEU A 203 ? 0.09256 0.15138 0.17409 0.00895  -0.04601 0.00181  203 LEU A CB  
1742 C CG  . LEU A 203 ? 0.08173 0.19977 0.19892 -0.00715 -0.03569 0.05791  203 LEU A CG  
1743 C CD1 . LEU A 203 ? 0.08200 0.19235 0.20028 -0.01283 -0.04021 0.07111  203 LEU A CD1 
1744 C CD2 . LEU A 203 ? 0.12127 0.23440 0.19664 -0.01385 -0.01880 0.06518  203 LEU A CD2 
1745 N N   . GLY A 204 ? 0.15002 0.10777 0.18638 0.00491  -0.01430 0.02170  204 GLY A N   
1746 C CA  . GLY A 204 ? 0.17019 0.10505 0.19765 0.00622  -0.00980 0.01460  204 GLY A CA  
1747 C C   . GLY A 204 ? 0.14252 0.11109 0.19617 0.02473  -0.03242 0.00745  204 GLY A C   
1748 O O   . GLY A 204 ? 0.14143 0.15412 0.20787 0.00458  -0.04863 -0.01647 204 GLY A O   
1749 N N   . VAL A 205 ? 0.12504 0.11357 0.18908 0.04517  -0.03980 0.03632  205 VAL A N   
1750 C CA  . VAL A 205 ? 0.14792 0.13981 0.17527 0.01795  -0.05093 0.03041  205 VAL A CA  
1751 C C   . VAL A 205 ? 0.13866 0.12073 0.17091 0.02014  -0.03584 -0.00351 205 VAL A C   
1752 O O   . VAL A 205 ? 0.13257 0.15609 0.15974 0.00156  -0.02329 -0.01321 205 VAL A O   
1753 C CB  . VAL A 205 ? 0.17750 0.17515 0.17878 0.01770  -0.03595 0.09519  205 VAL A CB  
1754 C CG1 . VAL A 205 ? 0.21135 0.24208 0.18204 0.02408  -0.03431 0.11243  205 VAL A CG1 
1755 C CG2 . VAL A 205 ? 0.15867 0.15847 0.16917 -0.01728 -0.04345 0.09182  205 VAL A CG2 
1756 N N   . LEU A 206 ? 0.13049 0.12634 0.19356 0.04769  -0.01345 -0.03550 206 LEU A N   
1757 C CA  . LEU A 206 ? 0.15571 0.14604 0.20156 0.03693  -0.03271 -0.07409 206 LEU A CA  
1758 C C   . LEU A 206 ? 0.13486 0.13666 0.20422 0.02327  -0.05684 -0.05835 206 LEU A C   
1759 O O   . LEU A 206 ? 0.12575 0.17340 0.22262 0.01384  -0.05794 -0.05840 206 LEU A O   
1760 C CB  . LEU A 206 ? 0.16135 0.16209 0.18220 0.00948  -0.03273 -0.08347 206 LEU A CB  
1761 C CG  . LEU A 206 ? 0.17933 0.14892 0.16130 -0.00779 -0.02984 -0.06502 206 LEU A CG  
1762 C CD1 . LEU A 206 ? 0.19764 0.18069 0.14987 -0.00230 -0.01304 -0.05185 206 LEU A CD1 
1763 C CD2 . LEU A 206 ? 0.23036 0.17262 0.16011 -0.03650 -0.02092 -0.04123 206 LEU A CD2 
1764 N N   . VAL A 207 ? 0.13733 0.13638 0.19674 0.03403  -0.04436 -0.02762 207 VAL A N   
1765 C CA  . VAL A 207 ? 0.15677 0.13188 0.18955 -0.02348 -0.02990 -0.03860 207 VAL A CA  
1766 C C   . VAL A 207 ? 0.18022 0.12743 0.20545 0.01277  0.01083  -0.00600 207 VAL A C   
1767 O O   . VAL A 207 ? 0.17552 0.16992 0.20174 0.02852  0.00380  0.02747  207 VAL A O   
1768 C CB  . VAL A 207 ? 0.17736 0.14442 0.15647 -0.01197 -0.05390 -0.04713 207 VAL A CB  
1769 C CG1 . VAL A 207 ? 0.13510 0.16737 0.14133 0.01518  -0.07500 -0.04279 207 VAL A CG1 
1770 C CG2 . VAL A 207 ? 0.18664 0.12393 0.15006 -0.01315 -0.06942 0.01412  207 VAL A CG2 
1771 N N   . LEU A 208 ? 0.18700 0.12554 0.22297 -0.00895 0.03258  -0.01968 208 LEU A N   
1772 C CA  . LEU A 208 ? 0.16004 0.13873 0.22170 0.02225  0.01231  -0.02245 208 LEU A CA  
1773 C C   . LEU A 208 ? 0.16094 0.16895 0.22651 -0.00375 0.00272  -0.03169 208 LEU A C   
1774 O O   . LEU A 208 ? 0.14346 0.18118 0.21781 -0.02384 0.01069  -0.03492 208 LEU A O   
1775 C CB  . LEU A 208 ? 0.13702 0.13686 0.22477 0.03255  0.00304  -0.02350 208 LEU A CB  
1776 C CG  . LEU A 208 ? 0.15328 0.15644 0.22802 0.01936  -0.03341 -0.01072 208 LEU A CG  
1777 C CD1 . LEU A 208 ? 0.16209 0.17241 0.24390 -0.00619 -0.02639 0.00923  208 LEU A CD1 
1778 C CD2 . LEU A 208 ? 0.17798 0.17501 0.23181 0.00662  -0.01686 -0.01812 208 LEU A CD2 
1779 N N   A GLN A 209 ? 0.15305 0.16036 0.22410 -0.00493 -0.01068 -0.01821 209 GLN A N   
1780 N N   B GLN A 209 ? 0.15513 0.16539 0.23454 0.00373  -0.01267 -0.02091 209 GLN A N   
1781 C CA  A GLN A 209 ? 0.16446 0.17583 0.23026 -0.02000 -0.00872 -0.02311 209 GLN A CA  
1782 C CA  B GLN A 209 ? 0.17359 0.18282 0.25301 0.00081  -0.01018 -0.03130 209 GLN A CA  
1783 C C   A GLN A 209 ? 0.15067 0.19466 0.23577 -0.03813 -0.01574 -0.04554 209 GLN A C   
1784 C C   B GLN A 209 ? 0.13278 0.17449 0.24987 -0.00984 -0.00822 -0.06822 209 GLN A C   
1785 O O   A GLN A 209 ? 0.14845 0.22789 0.23229 -0.02680 -0.00247 -0.04678 209 GLN A O   
1786 O O   B GLN A 209 ? 0.11228 0.17066 0.25867 0.00940  0.02114  -0.07764 209 GLN A O   
1787 C CB  A GLN A 209 ? 0.17706 0.19091 0.23330 -0.02184 -0.02854 -0.03142 209 GLN A CB  
1788 C CB  B GLN A 209 ? 0.22860 0.22215 0.27767 -0.00676 -0.02253 -0.03423 209 GLN A CB  
1789 C CG  A GLN A 209 ? 0.19192 0.21333 0.25264 -0.00194 -0.02638 -0.01291 209 GLN A CG  
1790 C CG  B GLN A 209 ? 0.27759 0.26895 0.30701 -0.01049 0.00396  -0.02778 209 GLN A CG  
1791 C CD  A GLN A 209 ? 0.21885 0.26855 0.29747 0.03118  0.01265  0.01440  209 GLN A CD  
1792 C CD  B GLN A 209 ? 0.31527 0.30138 0.35236 -0.01641 0.03331  -0.02692 209 GLN A CD  
1793 O OE1 A GLN A 209 ? 0.21944 0.25843 0.30033 0.04610  0.00508  0.01897  209 GLN A OE1 
1794 O OE1 B GLN A 209 ? 0.34813 0.28288 0.35070 -0.03746 0.05991  -0.03803 209 GLN A OE1 
1795 N NE2 A GLN A 209 ? 0.22042 0.28658 0.27122 0.02073  0.02533  0.03361  209 GLN A NE2 
1796 N NE2 B GLN A 209 ? 0.30843 0.34921 0.38987 -0.01319 0.02962  -0.02040 209 GLN A NE2 
1797 N N   A MET A 210 ? 0.16071 0.19440 0.25030 -0.00966 0.00820  -0.03814 210 MET A N   
1798 N N   B MET A 210 ? 0.13261 0.19334 0.24684 0.00720  -0.00579 -0.06959 210 MET A N   
1799 C CA  A MET A 210 ? 0.17351 0.20404 0.26406 0.01597  0.01792  -0.03441 210 MET A CA  
1800 C CA  B MET A 210 ? 0.15369 0.19150 0.25164 0.01516  -0.00554 -0.05617 210 MET A CA  
1801 C C   A MET A 210 ? 0.18495 0.19958 0.25524 0.03960  0.00468  -0.05439 210 MET A C   
1802 C C   B MET A 210 ? 0.16220 0.20603 0.25110 0.02406  -0.02381 -0.05769 210 MET A C   
1803 O O   A MET A 210 ? 0.20207 0.19741 0.25372 0.05404  0.01608  -0.08257 210 MET A O   
1804 O O   B MET A 210 ? 0.16316 0.22270 0.24908 0.01674  -0.03727 -0.08079 210 MET A O   
1805 C CB  A MET A 210 ? 0.17982 0.22507 0.27747 0.00448  0.01907  -0.00631 210 MET A CB  
1806 C CB  B MET A 210 ? 0.15403 0.16393 0.25341 0.00022  -0.01323 -0.04967 210 MET A CB  
1807 C CG  A MET A 210 ? 0.20763 0.25739 0.29294 0.00575  0.02359  0.01275  210 MET A CG  
1808 C CG  B MET A 210 ? 0.18104 0.17996 0.25386 0.00358  -0.00707 -0.05060 210 MET A CG  
1809 S SD  A MET A 210 ? 0.22451 0.26096 0.30054 0.01714  0.01575  0.03346  210 MET A SD  
1810 S SD  B MET A 210 ? 0.17595 0.16806 0.25451 0.02167  0.00234  -0.04425 210 MET A SD  
1811 C CE  A MET A 210 ? 0.21924 0.28554 0.29214 -0.00947 0.02530  0.04317  210 MET A CE  
1812 C CE  B MET A 210 ? 0.20340 0.17652 0.25507 0.04827  0.01891  -0.04468 210 MET A CE  
1813 N N   . ALA A 211 ? 0.16832 0.18544 0.25852 0.03681  -0.02309 -0.05671 211 ALA A N   
1814 C CA  . ALA A 211 ? 0.16867 0.24108 0.28896 0.01371  -0.02610 -0.05764 211 ALA A CA  
1815 C C   . ALA A 211 ? 0.14684 0.26863 0.29633 -0.00796 -0.06368 -0.08737 211 ALA A C   
1816 O O   . ALA A 211 ? 0.17289 0.31751 0.29751 -0.01766 -0.06513 -0.09384 211 ALA A O   
1817 C CB  . ALA A 211 ? 0.19170 0.26989 0.30232 -0.02324 0.00016  -0.04956 211 ALA A CB  
1818 N N   A ARG A 212 ? 0.14447 0.27478 0.32647 0.00178  -0.04882 -0.08450 212 ARG A N   
1819 N N   B ARG A 212 ? 0.14513 0.27549 0.32646 0.00052  -0.04900 -0.08557 212 ARG A N   
1820 C CA  A ARG A 212 ? 0.17140 0.25476 0.35159 -0.01458 -0.05304 -0.08097 212 ARG A CA  
1821 C CA  B ARG A 212 ? 0.17420 0.25988 0.35204 -0.01549 -0.05366 -0.08289 212 ARG A CA  
1822 C C   A ARG A 212 ? 0.18288 0.26384 0.34368 -0.00746 -0.03798 -0.07761 212 ARG A C   
1823 C C   B ARG A 212 ? 0.18564 0.26556 0.34347 -0.00942 -0.03956 -0.07803 212 ARG A C   
1824 O O   A ARG A 212 ? 0.19568 0.25096 0.34031 -0.02083 -0.05260 -0.09076 212 ARG A O   
1825 O O   B ARG A 212 ? 0.19832 0.25096 0.33882 -0.02598 -0.05526 -0.09418 212 ARG A O   
1826 C CB  A ARG A 212 ? 0.20627 0.24363 0.38603 -0.01182 -0.04948 -0.05447 212 ARG A CB  
1827 C CB  B ARG A 212 ? 0.21433 0.26441 0.38806 -0.01026 -0.05048 -0.05811 212 ARG A CB  
1828 C CG  A ARG A 212 ? 0.25468 0.23845 0.40273 -0.02072 -0.01861 -0.05125 212 ARG A CG  
1829 C CG  B ARG A 212 ? 0.27613 0.28832 0.40844 -0.01462 -0.01293 -0.05311 212 ARG A CG  
1830 C CD  A ARG A 212 ? 0.28392 0.26268 0.40834 -0.03429 -0.00852 -0.05459 212 ARG A CD  
1831 C CD  B ARG A 212 ? 0.31946 0.33636 0.42368 -0.01981 0.01284  -0.05014 212 ARG A CD  
1832 N NE  A ARG A 212 ? 0.34486 0.31540 0.42570 -0.02644 0.02631  -0.03924 212 ARG A NE  
1833 N NE  B ARG A 212 ? 0.38076 0.40592 0.44475 -0.01608 0.05242  -0.03760 212 ARG A NE  
1834 C CZ  A ARG A 212 ? 0.39400 0.36409 0.46060 -0.00873 0.04407  -0.01985 212 ARG A CZ  
1835 C CZ  B ARG A 212 ? 0.41410 0.42254 0.47124 -0.00991 0.05669  -0.03307 212 ARG A CZ  
1836 N NH1 A ARG A 212 ? 0.39153 0.36133 0.43665 -0.02620 0.05554  -0.02385 212 ARG A NH1 
1837 N NH1 B ARG A 212 ? 0.41908 0.45152 0.44926 -0.00773 0.08400  -0.03084 212 ARG A NH1 
1838 N NH2 A ARG A 212 ? 0.42906 0.43811 0.50516 0.02162  0.07668  -0.01113 212 ARG A NH2 
1839 N NH2 B ARG A 212 ? 0.42934 0.43815 0.50543 -0.00692 0.04982  -0.04371 212 ARG A NH2 
1840 N N   A VAL A 213 ? 0.19086 0.26511 0.34151 0.01693  -0.01632 -0.07486 213 VAL A N   
1841 N N   B VAL A 213 ? 0.19546 0.26625 0.34151 0.01755  -0.01829 -0.07241 213 VAL A N   
1842 C CA  A VAL A 213 ? 0.19225 0.28483 0.34198 0.02008  -0.03456 -0.07374 213 VAL A CA  
1843 C CA  B VAL A 213 ? 0.19984 0.28878 0.34312 0.02463  -0.02909 -0.06725 213 VAL A CA  
1844 C C   A VAL A 213 ? 0.19010 0.30732 0.34978 -0.00231 -0.06930 -0.09748 213 VAL A C   
1845 C C   B VAL A 213 ? 0.19673 0.31354 0.35295 0.01112  -0.05930 -0.07970 213 VAL A C   
1846 O O   A VAL A 213 ? 0.19482 0.33404 0.34722 -0.00409 -0.07812 -0.10373 213 VAL A O   
1847 O O   B VAL A 213 ? 0.19505 0.32928 0.34784 0.01030  -0.07691 -0.07968 213 VAL A O   
1848 C CB  A VAL A 213 ? 0.21272 0.27466 0.33895 0.02408  -0.02375 -0.06887 213 VAL A CB  
1849 C CB  B VAL A 213 ? 0.21664 0.27527 0.34082 0.02673  -0.01912 -0.06514 213 VAL A CB  
1850 C CG1 A VAL A 213 ? 0.22741 0.29561 0.33781 0.02429  -0.01173 -0.07275 213 VAL A CG1 
1851 C CG1 B VAL A 213 ? 0.22810 0.29158 0.34103 0.02498  -0.00535 -0.07014 213 VAL A CG1 
1852 C CG2 A VAL A 213 ? 0.24119 0.27086 0.34374 0.01469  -0.00763 -0.06076 213 VAL A CG2 
1853 C CG2 B VAL A 213 ? 0.24328 0.27370 0.34540 0.01673  -0.00458 -0.05791 213 VAL A CG2 
1854 N N   A GLN A 214 ? 0.18724 0.31150 0.36969 0.03181  -0.06605 -0.07830 214 GLN A N   
1855 N N   B GLN A 214 ? 0.20293 0.32530 0.37054 0.04400  -0.05420 -0.06068 214 GLN A N   
1856 C CA  A GLN A 214 ? 0.22273 0.33619 0.38046 0.03908  -0.07570 -0.06198 214 GLN A CA  
1857 C CA  B GLN A 214 ? 0.24117 0.34841 0.38240 0.04953  -0.05499 -0.04962 214 GLN A CA  
1858 C C   A GLN A 214 ? 0.22971 0.35801 0.38342 0.03082  -0.08796 -0.05996 214 GLN A C   
1859 C C   B GLN A 214 ? 0.24422 0.36355 0.38670 0.03332  -0.05841 -0.05006 214 GLN A C   
1860 O O   A GLN A 214 ? 0.23663 0.35160 0.37714 0.05055  -0.09742 -0.05027 214 GLN A O   
1861 O O   B GLN A 214 ? 0.24734 0.35150 0.38773 0.04012  -0.05466 -0.04199 214 GLN A O   
1862 C CB  A GLN A 214 ? 0.26831 0.35001 0.38486 0.04667  -0.06831 -0.04613 214 GLN A CB  
1863 C CB  B GLN A 214 ? 0.29618 0.36534 0.38912 0.05967  -0.03329 -0.03704 214 GLN A CB  
1864 C CG  A GLN A 214 ? 0.30528 0.35533 0.38783 0.06401  -0.04496 -0.04352 214 GLN A CG  
1865 C CG  B GLN A 214 ? 0.31833 0.36198 0.39242 0.06062  -0.01751 -0.04249 214 GLN A CG  
1866 C CD  A GLN A 214 ? 0.33802 0.36928 0.39933 0.07243  -0.03693 -0.04807 214 GLN A CD  
1867 C CD  B GLN A 214 ? 0.33457 0.37257 0.40434 0.05882  -0.01006 -0.04753 214 GLN A CD  
1868 O OE1 A GLN A 214 ? 0.38056 0.38660 0.40637 0.07401  -0.00992 -0.03395 214 GLN A OE1 
1869 O OE1 B GLN A 214 ? 0.34907 0.38380 0.40540 0.04516  -0.00078 -0.02699 214 GLN A OE1 
1870 N NE2 A GLN A 214 ? 0.34768 0.39150 0.40559 0.07410  -0.03381 -0.07285 214 GLN A NE2 
1871 N NE2 B GLN A 214 ? 0.34187 0.38078 0.41237 0.06498  0.00208  -0.07458 214 GLN A NE2 
1872 N N   A SER A 215 ? 0.24367 0.37934 0.39880 0.01267  -0.06059 -0.06947 215 SER A N   
1873 N N   B SER A 215 ? 0.25665 0.38514 0.39948 0.01217  -0.05248 -0.06513 215 SER A N   
1874 C CA  A SER A 215 ? 0.24546 0.36297 0.41697 -0.00737 -0.06163 -0.08429 215 SER A CA  
1875 C CA  B SER A 215 ? 0.25314 0.37545 0.41835 -0.01014 -0.05968 -0.08177 215 SER A CA  
1876 C C   A SER A 215 ? 0.25907 0.37895 0.44153 -0.03986 -0.04153 -0.08918 215 SER A C   
1877 C C   B SER A 215 ? 0.26151 0.38266 0.44148 -0.04081 -0.04116 -0.08802 215 SER A C   
1878 O O   A SER A 215 ? 0.26018 0.38572 0.44840 -0.03656 -0.03327 -0.08021 215 SER A O   
1879 O O   B SER A 215 ? 0.26123 0.38316 0.44595 -0.03849 -0.03532 -0.07861 215 SER A O   
1880 C CB  A SER A 215 ? 0.24566 0.33541 0.40903 -0.01324 -0.08012 -0.09933 215 SER A CB  
1881 C CB  B SER A 215 ? 0.25474 0.35509 0.41111 -0.01650 -0.07665 -0.10071 215 SER A CB  
1882 O OG  A SER A 215 ? 0.24591 0.31762 0.40777 -0.00018 -0.08704 -0.10492 215 SER A OG  
1883 O OG  B SER A 215 ? 0.25325 0.34457 0.40825 -0.00018 -0.08700 -0.10532 215 SER A OG  
1884 N N   . GLY A 216 ? 0.26060 0.40186 0.46835 -0.04971 -0.04056 -0.08827 216 GLY A N   
1885 C CA  . GLY A 216 ? 0.30745 0.43523 0.54029 -0.07966 -0.04847 -0.07474 216 GLY A CA  
1886 C C   . GLY A 216 ? 0.40387 0.50308 0.61823 -0.07387 -0.02228 -0.06321 216 GLY A C   
1887 O O   . GLY A 216 ? 0.36871 0.51077 0.56997 -0.08473 -0.03060 -0.05886 216 GLY A O   
1888 N N   A GLU A 217 ? 0.47835 0.56799 0.67285 -0.06325 -0.02104 -0.06052 217 GLU A N   
1889 N N   B GLU A 217 ? 0.47839 0.56798 0.67244 -0.06341 -0.02004 -0.06072 217 GLU A N   
1890 C CA  A GLU A 217 ? 0.53412 0.64067 0.70501 -0.04762 0.00011  -0.05361 217 GLU A CA  
1891 C CA  B GLU A 217 ? 0.53412 0.64063 0.70456 -0.04803 0.00277  -0.05471 217 GLU A CA  
1892 C C   A GLU A 217 ? 0.51002 0.56391 0.69996 -0.04159 -0.01970 -0.04261 217 GLU A C   
1893 C C   B GLU A 217 ? 0.50998 0.56390 0.69964 -0.04187 -0.01884 -0.04288 217 GLU A C   
1894 O O   A GLU A 217 ? 0.47862 0.59000 0.67765 -0.04308 -0.02599 -0.04508 217 GLU A O   
1895 O O   B GLU A 217 ? 0.47864 0.58988 0.67740 -0.04346 -0.02559 -0.04529 217 GLU A O   
1896 C CB  A GLU A 217 ? 0.58839 0.72131 0.72198 -0.04084 0.03305  -0.05324 217 GLU A CB  
1897 C CB  B GLU A 217 ? 0.58841 0.72125 0.72180 -0.04168 0.03928  -0.05713 217 GLU A CB  
1898 C CG  A GLU A 217 ? 0.59477 0.66411 0.74294 -0.04689 -0.02121 -0.04608 217 GLU A CG  
1899 C CG  B GLU A 217 ? 0.59477 0.66403 0.74294 -0.04852 -0.01370 -0.05342 217 GLU A CG  
1900 C CD  A GLU A 217 ? 0.69764 0.71473 0.83339 -0.05988 0.00265  -0.04542 217 GLU A CD  
1901 C CD  B GLU A 217 ? 0.69566 0.71380 0.83185 -0.06131 0.00369  -0.04957 217 GLU A CD  
1902 O OE1 A GLU A 217 ? 0.71738 0.74439 0.86179 -0.07250 0.03179  -0.04087 217 GLU A OE1 
1903 O OE1 B GLU A 217 ? 0.71410 0.74341 0.85921 -0.07052 0.03149  -0.04153 217 GLU A OE1 
1904 O OE2 A GLU A 217 ? 0.72363 0.77491 0.84272 -0.05808 0.05220  -0.05099 217 GLU A OE2 
1905 O OE2 B GLU A 217 ? 0.72381 0.77495 0.84272 -0.06535 0.04937  -0.05555 217 GLU A OE2 
1906 N N   . LYS A 218 ? 0.50470 0.60607 0.66515 -0.03839 -0.02460 -0.03991 218 LYS A N   
1907 C CA  . LYS A 218 ? 0.52585 0.64366 0.71203 -0.03987 0.00720  -0.05036 218 LYS A CA  
1908 C C   . LYS A 218 ? 0.56623 0.68874 0.72900 -0.04140 0.08903  -0.02806 218 LYS A C   
1909 O O   . LYS A 218 ? 0.60032 0.69990 0.76203 -0.03530 0.06706  -0.01579 218 LYS A O   
1910 C CB  . LYS A 218 ? 0.55406 0.67109 0.72971 -0.03814 0.03446  -0.07042 218 LYS A CB  
1911 C C1  . OLA B .   ? 0.61098 0.57195 0.44307 -0.02276 0.11668  0.10682  501 OLA A C1  
1912 O O1  . OLA B .   ? 0.62843 0.57416 0.43442 -0.04684 0.10125  0.08649  501 OLA A O1  
1913 O O2  . OLA B .   ? 0.62615 0.55383 0.45407 -0.03061 0.09574  0.10185  501 OLA A O2  
1914 C C2  . OLA B .   ? 0.57459 0.50151 0.42546 -0.01005 0.11067  0.06351  501 OLA A C2  
1915 C C3  . OLA B .   ? 0.50985 0.44683 0.38097 -0.01998 0.07162  0.04174  501 OLA A C3  
1916 C C4  . OLA B .   ? 0.46637 0.45647 0.35251 -0.02634 0.06060  0.03431  501 OLA A C4  
1917 C C5  . OLA B .   ? 0.45629 0.46702 0.33795 -0.02053 0.07133  0.02475  501 OLA A C5  
1918 C C6  . OLA B .   ? 0.44967 0.46965 0.32049 -0.00798 0.05280  0.00619  501 OLA A C6  
1919 C C7  . OLA B .   ? 0.44930 0.46386 0.31530 0.01558  0.02734  -0.01501 501 OLA A C7  
1920 C C8  . OLA B .   ? 0.44331 0.47100 0.32307 0.01201  0.03201  -0.02675 501 OLA A C8  
1921 C C9  . OLA B .   ? 0.45182 0.45369 0.32783 0.00043  0.02413  -0.03727 501 OLA A C9  
1922 C C10 . OLA B .   ? 0.45328 0.43649 0.33500 -0.00976 0.02991  -0.03741 501 OLA A C10 
1923 C C11 . OLA B .   ? 0.45311 0.42288 0.34756 -0.01725 0.02778  -0.03565 501 OLA A C11 
1924 C C12 . OLA B .   ? 0.45310 0.41753 0.36287 -0.00250 0.02017  -0.00703 501 OLA A C12 
1925 C C13 . OLA B .   ? 0.45821 0.45022 0.37808 0.02009  -0.00278 0.00424  501 OLA A C13 
1926 C C14 . OLA B .   ? 0.44972 0.46645 0.39266 0.00773  -0.01918 0.00512  501 OLA A C14 
1927 C C15 . OLA B .   ? 0.45484 0.46401 0.39756 -0.00759 -0.03256 -0.00333 501 OLA A C15 
1928 C C16 . OLA B .   ? 0.48013 0.46107 0.38640 -0.01977 -0.03669 -0.00625 501 OLA A C16 
1929 C C17 . OLA B .   ? 0.50662 0.48414 0.38014 -0.01779 -0.03190 0.00054  501 OLA A C17 
1930 C C18 . OLA B .   ? 0.50748 0.48241 0.37577 -0.02148 -0.02465 0.01190  501 OLA A C18 
1931 C C1  . OLA C .   ? 0.48463 0.45007 0.32729 -0.02940 0.01575  0.07583  502 OLA A C1  
1932 C C2  . OLA C .   ? 0.46495 0.44019 0.32181 -0.02970 0.02593  0.04757  502 OLA A C2  
1933 C C3  . OLA C .   ? 0.43670 0.42259 0.30178 -0.02804 0.04083  0.01096  502 OLA A C3  
1934 C C4  . OLA C .   ? 0.40858 0.40154 0.29599 -0.04128 0.04485  -0.01730 502 OLA A C4  
1935 C C5  . OLA C .   ? 0.38273 0.40426 0.29255 -0.02133 0.05641  -0.02401 502 OLA A C5  
1936 C C6  . OLA C .   ? 0.36312 0.39394 0.29137 -0.00060 0.06647  -0.02999 502 OLA A C6  
1937 C C7  . OLA C .   ? 0.35246 0.37585 0.29517 0.00440  0.06083  -0.00009 502 OLA A C7  
1938 C C8  . OLA C .   ? 0.36944 0.36861 0.29689 -0.00011 0.04753  0.03701  502 OLA A C8  
1939 C C9  . OLA C .   ? 0.39463 0.36537 0.30329 0.01294  0.03290  0.05277  502 OLA A C9  
1940 C C10 . OLA C .   ? 0.41364 0.37225 0.32035 0.00538  0.02396  0.01762  502 OLA A C10 
1941 C C11 . OLA C .   ? 0.43185 0.40649 0.33998 0.02447  0.02237  -0.02531 502 OLA A C11 
1942 C C12 . OLA C .   ? 0.44014 0.45515 0.36789 0.04312  0.03963  -0.04414 502 OLA A C12 
1943 C C13 . OLA C .   ? 0.44407 0.47599 0.37242 0.02642  0.05784  -0.04763 502 OLA A C13 
1944 C C14 . OLA C .   ? 0.47130 0.46995 0.35506 -0.00143 0.07040  -0.02405 502 OLA A C14 
1945 C C15 . OLA C .   ? 0.50596 0.44205 0.32336 -0.02329 0.11124  0.01417  502 OLA A C15 
1946 C C16 . OLA C .   ? 0.52027 0.44135 0.30302 -0.02298 0.11469  0.03751  502 OLA A C16 
1947 C C1  . OLA D .   ? 0.60548 0.59891 0.48876 -0.04706 0.04605  -0.01373 503 OLA A C1  
1948 O O1  . OLA D .   ? 0.61211 0.59739 0.49352 -0.05687 0.01951  -0.03274 503 OLA A O1  
1949 O O2  . OLA D .   ? 0.62432 0.58978 0.49728 -0.05101 0.05068  0.00106  503 OLA A O2  
1950 C C2  . OLA D .   ? 0.60527 0.52015 0.45632 -0.01405 0.03953  -0.01978 503 OLA A C2  
1951 C C3  . OLA D .   ? 0.56349 0.45765 0.42135 -0.01774 0.04438  -0.02833 503 OLA A C3  
1952 C C4  . OLA D .   ? 0.53477 0.44231 0.39446 -0.03066 0.06525  -0.02096 503 OLA A C4  
1953 C C5  . OLA D .   ? 0.52592 0.43513 0.37404 -0.02179 0.08262  -0.00335 503 OLA A C5  
1954 C C6  . OLA D .   ? 0.51001 0.43277 0.36341 -0.01516 0.08561  0.01304  503 OLA A C6  
1955 C C7  . OLA D .   ? 0.48147 0.41164 0.36925 -0.00906 0.05808  0.01647  503 OLA A C7  
1956 C C8  . OLA D .   ? 0.45462 0.41010 0.37121 0.01454  0.03177  0.01178  503 OLA A C8  
1957 C C9  . OLA D .   ? 0.43311 0.40105 0.36632 0.02120  0.00010  0.01372  503 OLA A C9  
1958 C C10 . OLA D .   ? 0.42724 0.41511 0.36245 0.02802  -0.02744 0.03095  503 OLA A C10 
1959 C C11 . OLA D .   ? 0.42784 0.43880 0.35716 0.02347  -0.02491 0.05336  503 OLA A C11 
1960 C C12 . OLA D .   ? 0.44242 0.45529 0.35141 0.00078  -0.00939 0.07452  503 OLA A C12 
1961 C C13 . OLA D .   ? 0.46250 0.46916 0.34851 -0.00611 0.01252  0.07198  503 OLA A C13 
1962 C C14 . OLA D .   ? 0.48421 0.47252 0.34668 -0.01956 0.02195  0.04259  503 OLA A C14 
1963 C C15 . OLA D .   ? 0.50360 0.46344 0.34674 -0.01844 0.02943  0.02762  503 OLA A C15 
1964 C C16 . OLA D .   ? 0.49614 0.45021 0.34896 -0.01935 0.04239  0.02847  503 OLA A C16 
1965 C C17 . OLA D .   ? 0.48864 0.44101 0.34557 -0.02434 0.07673  0.04261  503 OLA A C17 
1966 C C18 . OLA D .   ? 0.47115 0.42397 0.33125 -0.02130 0.09302  0.05255  503 OLA A C18 
1967 C C10 . LFA E .   ? 0.44688 0.45068 0.44295 0.04207  0.02622  0.02405  504 LFA A C10 
1968 C C11 . LFA E .   ? 0.42337 0.44446 0.41823 0.04316  0.00780  0.02806  504 LFA A C11 
1969 C C12 . LFA E .   ? 0.43313 0.41703 0.41682 0.02772  -0.00914 0.02206  504 LFA A C12 
1970 C C13 . LFA E .   ? 0.44765 0.40087 0.41989 0.02839  -0.01566 0.00577  504 LFA A C13 
1971 C C14 . LFA E .   ? 0.43416 0.38809 0.40990 0.04128  0.00737  0.00995  504 LFA A C14 
1972 C C15 . LFA E .   ? 0.41773 0.40452 0.39276 0.04098  0.05097  0.01612  504 LFA A C15 
1973 C C16 . LFA E .   ? 0.38065 0.40356 0.37820 0.02752  0.05282  0.02813  504 LFA A C16 
1974 C C17 . LFA E .   ? 0.37296 0.39849 0.36791 0.01321  0.05739  0.03006  504 LFA A C17 
1975 C C6  . LFA F .   ? 0.51959 0.45694 0.49303 -0.03277 -0.01796 -0.01370 505 LFA A C6  
1976 C C7  . LFA F .   ? 0.52829 0.49569 0.47836 -0.00082 0.01118  -0.00743 505 LFA A C7  
1977 C C8  . LFA F .   ? 0.49480 0.49607 0.46123 0.00512  0.00143  -0.01057 505 LFA A C8  
1978 C C9  . LFA F .   ? 0.49828 0.48514 0.45192 -0.00076 0.01820  -0.01818 505 LFA A C9  
1979 C C10 . LFA F .   ? 0.47846 0.46561 0.44824 0.01235  -0.00365 -0.02127 505 LFA A C10 
1980 C C11 . LFA F .   ? 0.46218 0.45667 0.45526 0.03875  -0.00530 -0.00119 505 LFA A C11 
1981 C C12 . LFA F .   ? 0.47081 0.45566 0.46647 0.03629  0.00813  0.00991  505 LFA A C12 
1982 C C13 . LFA F .   ? 0.46006 0.41315 0.46910 0.03089  -0.01870 0.00813  505 LFA A C13 
1983 C C14 . LFA F .   ? 0.46468 0.40651 0.46938 0.01594  -0.03078 -0.00204 505 LFA A C14 
1984 C C1  . LFA G .   ? 0.53219 0.51516 0.48282 0.00253  0.02953  -0.03851 506 LFA A C1  
1985 C C2  . LFA G .   ? 0.50891 0.50116 0.49203 0.00356  -0.00245 -0.02829 506 LFA A C2  
1986 C C3  . LFA G .   ? 0.51406 0.49522 0.50400 -0.00345 0.00436  -0.01321 506 LFA A C3  
1987 C C4  . LFA G .   ? 0.48326 0.49189 0.50293 -0.01150 0.01379  0.00351  506 LFA A C4  
1988 C C5  . LFA G .   ? 0.47239 0.46956 0.49727 -0.00367 0.02131  0.02863  506 LFA A C5  
1989 C C6  . LFA G .   ? 0.49349 0.44923 0.49097 0.00263  0.02797  0.04803  506 LFA A C6  
1990 C C7  . LFA G .   ? 0.47377 0.44005 0.46352 -0.00316 0.03143  0.05392  506 LFA A C7  
1991 C C8  . LFA G .   ? 0.43872 0.43495 0.43949 -0.00386 0.00360  0.04880  506 LFA A C8  
1992 C C9  . LFA G .   ? 0.44807 0.44973 0.43303 0.00339  -0.01301 0.03301  506 LFA A C9  
1993 C C10 . LFA G .   ? 0.45429 0.42328 0.42662 0.01472  -0.05234 0.01498  506 LFA A C10 
1994 C C11 . LFA G .   ? 0.46105 0.44190 0.41503 0.02602  -0.03357 0.01014  506 LFA A C11 
1995 C C1  . LFA H .   ? 0.43366 0.49515 0.43096 0.00386  0.03647  0.02944  507 LFA A C1  
1996 C C2  . LFA H .   ? 0.44425 0.50737 0.42203 -0.00548 0.05174  0.00886  507 LFA A C2  
1997 C C3  . LFA H .   ? 0.47358 0.48958 0.43549 -0.00001 0.04226  0.00017  507 LFA A C3  
1998 C C4  . LFA H .   ? 0.49880 0.47327 0.44961 -0.00051 0.03559  0.00312  507 LFA A C4  
1999 C C5  . LFA H .   ? 0.48341 0.44483 0.45542 -0.01510 0.00568  -0.00247 507 LFA A C5  
2000 C C6  . LFA H .   ? 0.46974 0.45861 0.46117 -0.02315 0.01275  -0.00245 507 LFA A C6  
2001 C C7  . LFA H .   ? 0.45070 0.48646 0.45982 -0.00547 0.03023  0.00726  507 LFA A C7  
2002 C C8  . LFA H .   ? 0.43749 0.52725 0.45285 0.00483  0.04599  0.00599  507 LFA A C8  
2003 C C1  . LFA I .   ? 0.50602 0.41064 0.42755 0.00587  0.03837  0.02510  508 LFA A C1  
2004 C C2  . LFA I .   ? 0.46784 0.40651 0.41993 0.03132  0.00501  0.03919  508 LFA A C2  
2005 C C3  . LFA I .   ? 0.45022 0.41851 0.42263 0.04112  -0.00661 0.05161  508 LFA A C3  
2006 C C4  . LFA I .   ? 0.42371 0.39856 0.42944 0.04076  -0.02467 0.03940  508 LFA A C4  
2007 C C5  . LFA I .   ? 0.44212 0.40050 0.44345 0.03626  -0.00311 0.01468  508 LFA A C5  
2008 C C6  . LFA I .   ? 0.45741 0.39907 0.45552 0.03003  -0.00088 -0.00996 508 LFA A C6  
2009 C C10 . LFA J .   ? 0.42268 0.39873 0.38293 -0.01067 0.01304  -0.00770 509 LFA A C10 
2010 C C11 . LFA J .   ? 0.41722 0.38589 0.38045 0.01247  0.01123  -0.00138 509 LFA A C11 
2011 C C12 . LFA J .   ? 0.46791 0.40609 0.38905 0.03601  0.03351  -0.00441 509 LFA A C12 
2012 C C3  . LFA K .   ? 0.48514 0.52131 0.48513 0.03332  -0.02987 -0.00268 510 LFA A C3  
2013 C C4  . LFA K .   ? 0.48812 0.49618 0.47962 0.02873  -0.02883 -0.01131 510 LFA A C4  
2014 C C5  . LFA K .   ? 0.47321 0.47647 0.46422 0.01390  -0.02498 -0.02777 510 LFA A C5  
2015 C C6  . LFA K .   ? 0.47137 0.46347 0.46225 0.00385  -0.02009 -0.03439 510 LFA A C6  
2016 C C7  . LFA K .   ? 0.49708 0.49275 0.46315 0.00422  0.01727  -0.02042 510 LFA A C7  
2017 C C8  . LFA K .   ? 0.47513 0.48517 0.46289 0.00803  -0.00167 -0.00667 510 LFA A C8  
2018 C C9  . LFA K .   ? 0.50836 0.49658 0.46554 0.01011  0.01127  -0.00033 510 LFA A C9  
2019 C C6  . LFA L .   ? 0.42258 0.44953 0.43442 -0.05794 0.08296  -0.04561 511 LFA A C6  
2020 C C7  . LFA L .   ? 0.43865 0.42778 0.44714 -0.02820 0.04209  -0.02930 511 LFA A C7  
2021 C C8  . LFA L .   ? 0.42910 0.43707 0.42155 -0.02659 0.02320  -0.02157 511 LFA A C8  
2022 C C9  . LFA L .   ? 0.45364 0.47832 0.44707 -0.02933 0.03477  -0.00758 511 LFA A C9  
2023 C C10 . LFA L .   ? 0.46506 0.49081 0.45091 -0.02698 0.01833  0.00257  511 LFA A C10 
2024 C C11 . LFA L .   ? 0.48966 0.48623 0.46597 -0.02531 -0.00884 0.00457  511 LFA A C11 
2025 C C12 . LFA L .   ? 0.47900 0.48027 0.47193 -0.02611 -0.01371 -0.00484 511 LFA A C12 
2026 C C13 . LFA L .   ? 0.47490 0.50326 0.46276 -0.01376 0.01832  -0.01296 511 LFA A C13 
2027 C C14 . LFA L .   ? 0.48623 0.53041 0.47319 -0.00759 0.03992  -0.01377 511 LFA A C14 
2028 C C8  . LFA M .   ? 0.51178 0.54736 0.47852 -0.00774 0.01075  0.04814  512 LFA A C8  
2029 C C9  . LFA M .   ? 0.53101 0.55033 0.49718 -0.00858 0.01161  0.03816  512 LFA A C9  
2030 C C10 . LFA M .   ? 0.55319 0.56212 0.51833 -0.00856 0.00525  0.03743  512 LFA A C10 
2031 C C11 . LFA M .   ? 0.57414 0.56466 0.52848 -0.00155 -0.00219 0.03496  512 LFA A C11 
2032 C C12 . LFA M .   ? 0.58315 0.56975 0.52858 -0.00507 0.00153  0.01729  512 LFA A C12 
2033 C C13 . LFA M .   ? 0.57674 0.57364 0.53407 -0.00787 0.01077  0.00193  512 LFA A C13 
2034 C C14 . LFA M .   ? 0.57490 0.57649 0.55630 -0.00193 0.01198  -0.00437 512 LFA A C14 
2035 C C15 . LFA M .   ? 0.59164 0.60686 0.58143 0.00245  0.04628  0.00491  512 LFA A C15 
2036 C C16 . LFA M .   ? 0.57061 0.61765 0.55596 -0.00851 0.03975  0.01143  512 LFA A C16 
2037 C C17 . LFA M .   ? 0.56557 0.58586 0.53403 -0.00512 0.02869  0.02099  512 LFA A C17 
2038 C C18 . LFA M .   ? 0.54194 0.52852 0.52023 0.01629  -0.01252 0.02698  512 LFA A C18 
2039 C C19 . LFA M .   ? 0.50751 0.49757 0.49563 0.04617  -0.02250 0.02527  512 LFA A C19 
2040 C C20 . LFA M .   ? 0.50156 0.50417 0.47957 0.05870  0.00680  0.00594  512 LFA A C20 
2041 C C17 . LFA N .   ? 0.50596 0.49897 0.46211 -0.00161 0.01084  0.00102  513 LFA A C17 
2042 C C18 . LFA N .   ? 0.50394 0.50604 0.47121 0.02145  0.00467  -0.00487 513 LFA A C18 
2043 C C19 . LFA N .   ? 0.50810 0.52825 0.47552 0.04795  0.01101  -0.00504 513 LFA A C19 
2044 C C20 . LFA N .   ? 0.50632 0.54386 0.47787 0.07110  0.01502  -0.00546 513 LFA A C20 
2045 C C18 . LFA O .   ? 0.49331 0.43420 0.44063 0.00189  0.02247  0.01275  514 LFA A C18 
2046 C C19 . LFA O .   ? 0.50646 0.42553 0.43560 0.01151  0.03463  0.02490  514 LFA A C19 
2047 C C20 . LFA O .   ? 0.48802 0.41127 0.42686 0.01054  0.02764  0.03503  514 LFA A C20 
2048 C C1  . RET P .   ? 0.08682 0.13607 0.10588 0.02331  0.01821  -0.03508 515 RET A C1  
2049 C C2  . RET P .   ? 0.09140 0.14362 0.11506 0.01270  0.04907  -0.03399 515 RET A C2  
2050 C C3  . RET P .   ? 0.11323 0.13488 0.12218 0.01626  0.05793  -0.03453 515 RET A C3  
2051 C C4  . RET P .   ? 0.12046 0.12585 0.12769 0.00929  0.05264  -0.02499 515 RET A C4  
2052 C C5  . RET P .   ? 0.10600 0.13378 0.14276 0.01956  0.04118  -0.00656 515 RET A C5  
2053 C C6  . RET P .   ? 0.10085 0.13268 0.12009 0.00435  0.01748  0.02263  515 RET A C6  
2054 C C7  . RET P .   ? 0.14087 0.11988 0.11166 -0.00434 0.00054  0.06921  515 RET A C7  
2055 C C8  . RET P .   ? 0.13851 0.11538 0.10757 -0.02933 -0.01382 0.06219  515 RET A C8  
2056 C C9  . RET P .   ? 0.14400 0.11837 0.08817 -0.03032 -0.02494 0.05332  515 RET A C9  
2057 C C10 . RET P .   ? 0.16809 0.09103 0.09610 -0.00433 -0.02202 0.04760  515 RET A C10 
2058 C C11 . RET P .   ? 0.18577 0.10726 0.12111 0.02339  -0.01460 0.06034  515 RET A C11 
2059 C C12 . RET P .   ? 0.19036 0.11079 0.11377 0.01898  0.00498  0.06121  515 RET A C12 
2060 C C13 . RET P .   ? 0.15867 0.12989 0.10709 0.02975  -0.00302 0.05217  515 RET A C13 
2061 C C14 . RET P .   ? 0.18436 0.16629 0.10395 -0.00298 0.02226  0.07139  515 RET A C14 
2062 C C15 . RET P .   ? 0.17385 0.18858 0.11313 -0.02735 0.04834  0.03955  515 RET A C15 
2063 C C16 . RET P .   ? 0.11031 0.19609 0.08915 0.02541  -0.01423 -0.04716 515 RET A C16 
2064 C C17 . RET P .   ? 0.11159 0.15637 0.09975 0.01917  0.02847  -0.05531 515 RET A C17 
2065 C C18 . RET P .   ? 0.12403 0.13786 0.16412 0.02819  0.03691  -0.01633 515 RET A C18 
2066 C C19 . RET P .   ? 0.13848 0.16149 0.08321 -0.02205 -0.04424 0.04285  515 RET A C19 
2067 C C20 . RET P .   ? 0.16694 0.15445 0.11921 0.05208  -0.00719 0.05661  515 RET A C20 
# 
