data_9GAX
# 
_entry.id   9GAX 
# 
_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   9GAX         pdb_00009gax 10.2210/pdb9gax/pdb 
WWPDB D_1292140669 ?            ?                   
# 
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 2025-01-22 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.year'                    
5 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GAX 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_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           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              djordje.musil@merckgroup.com 
_pdbx_contact_author.name_first         Djordje 
_pdbx_contact_author.name_last          Musil 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7889-2940 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Musil, D.'  1 ? 
'Freire, F.' 2 ? 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                6149 
_citation.page_last                 6164 
_citation.title                     
'MoA Studies of the TEAD P-Site Binding Ligand MSC-4106 and Its Optimization to TEAD1-Selective Amide M3686.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01949 
_citation.pdbx_database_id_PubMed   39704449 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Heinrich, T.'    1  ? 
primary 'Schwarz, D.'     2  ? 
primary 'Petersson, C.'   3  ? 
primary 'Gunera, J.'      4  ? 
primary 'Garg, S.'        5  ? 
primary 'Schneider, R.'   6  ? 
primary 'Keil, M.'        7  ? 
primary 'Grimmeisen, L.'  8  ? 
primary 'Unzue Lopez, A.' 9  ? 
primary 'Albers, L.'      10 ? 
primary 'Schlesiger, S.'  11 ? 
primary 'Gambardella, A.' 12 ? 
primary 'Bomke, J.'       13 ? 
primary 'Carswell, E.'    14 ? 
primary 'Schilke, H.'     15 ? 
primary 'Diehl, P.'       16 ? 
primary 'Doerfel, B.'     17 ? 
primary 'Musil, D.'       18 ? 
primary 'Trivier, E.'     19 ? 
primary 'Broome, R.'      20 ? 
primary 'Marshall, S.'    21 ? 
primary 'Balsiger, A.'    22 ? 
primary 'Friedrich, E.'   23 ? 
primary 'Lemos, A.R.'     24 ? 
primary 'Santos, S.P.'    25 ? 
primary 'Sousa, P.M.F.'   26 ? 
primary 'Freire, F.'      27 ? 
primary 'Bandeiras, T.M.' 28 ? 
primary 'Bortoluzzi, A.'  29 ? 
primary 'Wienke, D.'      30 ? 
# 
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 'Transcriptional enhancer factor TEF-1' 25460.971 2   ? ? ? ? 
2 non-polymer syn GLYCEROL 92.094    2   ? ? ? ? 
3 non-polymer syn 
'2-methyl-~{N}-[(1~{S})-1-(1-methylpyrazol-3-yl)-2-oxidanyl-ethyl]-4-[4-(trifluoromethyl)phenyl]pyrazolo[3,4-b]indole-7-carboxamide' 
482.458   2   ? ? ? ? 
4 non-polymer syn 'SULFATE ION' 96.063    6   ? ? ? ? 
5 water       nat water 18.015    217 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'NTEF-1,Protein GT-IIC,TEA domain family member 1,TEAD-1,Transcription factor 13,TCF-13' 
# 
_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       
;GPRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFF
LVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFI
HKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFF
LVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFI
HKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL   
3 
'2-methyl-~{N}-[(1~{S})-1-(1-methylpyrazol-3-yl)-2-oxidanyl-ethyl]-4-[4-(trifluoromethyl)phenyl]pyrazolo[3,4-b]indole-7-carboxamide' 
A1IJL 
4 'SULFATE ION' SO4   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   ARG n 
1 4   SER n 
1 5   ILE n 
1 6   GLY n 
1 7   THR n 
1 8   THR n 
1 9   LYS n 
1 10  LEU n 
1 11  ARG n 
1 12  LEU n 
1 13  VAL n 
1 14  GLU n 
1 15  PHE n 
1 16  SER n 
1 17  ALA n 
1 18  PHE n 
1 19  LEU n 
1 20  GLU n 
1 21  GLN n 
1 22  GLN n 
1 23  ARG n 
1 24  ASP n 
1 25  PRO n 
1 26  ASP n 
1 27  SER n 
1 28  TYR n 
1 29  ASN n 
1 30  LYS n 
1 31  HIS n 
1 32  LEU n 
1 33  PHE n 
1 34  VAL n 
1 35  HIS n 
1 36  ILE n 
1 37  GLY n 
1 38  HIS n 
1 39  ALA n 
1 40  ASN n 
1 41  HIS n 
1 42  SER n 
1 43  TYR n 
1 44  SER n 
1 45  ASP n 
1 46  PRO n 
1 47  LEU n 
1 48  LEU n 
1 49  GLU n 
1 50  SER n 
1 51  VAL n 
1 52  ASP n 
1 53  ILE n 
1 54  ARG n 
1 55  GLN n 
1 56  ILE n 
1 57  TYR n 
1 58  ASP n 
1 59  LYS n 
1 60  PHE n 
1 61  PRO n 
1 62  GLU n 
1 63  LYS n 
1 64  LYS n 
1 65  GLY n 
1 66  GLY n 
1 67  LEU n 
1 68  LYS n 
1 69  GLU n 
1 70  LEU n 
1 71  PHE n 
1 72  GLY n 
1 73  LYS n 
1 74  GLY n 
1 75  PRO n 
1 76  GLN n 
1 77  ASN n 
1 78  ALA n 
1 79  PHE n 
1 80  PHE n 
1 81  LEU n 
1 82  VAL n 
1 83  LYS n 
1 84  PHE n 
1 85  TRP n 
1 86  ALA n 
1 87  ASP n 
1 88  LEU n 
1 89  ASN n 
1 90  CYS n 
1 91  ASN n 
1 92  ILE n 
1 93  GLN n 
1 94  ASP n 
1 95  ASP n 
1 96  ALA n 
1 97  GLY n 
1 98  ALA n 
1 99  PHE n 
1 100 TYR n 
1 101 GLY n 
1 102 VAL n 
1 103 THR n 
1 104 SER n 
1 105 GLN n 
1 106 TYR n 
1 107 GLU n 
1 108 SER n 
1 109 SER n 
1 110 GLU n 
1 111 ASN n 
1 112 MET n 
1 113 THR n 
1 114 VAL n 
1 115 THR n 
1 116 CYS n 
1 117 SER n 
1 118 THR n 
1 119 LYS n 
1 120 VAL n 
1 121 CYS n 
1 122 SER n 
1 123 PHE n 
1 124 GLY n 
1 125 LYS n 
1 126 GLN n 
1 127 VAL n 
1 128 VAL n 
1 129 GLU n 
1 130 LYS n 
1 131 VAL n 
1 132 GLU n 
1 133 THR n 
1 134 GLU n 
1 135 TYR n 
1 136 ALA n 
1 137 ARG n 
1 138 PHE n 
1 139 GLU n 
1 140 ASN n 
1 141 GLY n 
1 142 ARG n 
1 143 PHE n 
1 144 VAL n 
1 145 TYR n 
1 146 ARG n 
1 147 ILE n 
1 148 ASN n 
1 149 ARG n 
1 150 SER n 
1 151 PRO n 
1 152 MET n 
1 153 CYS n 
1 154 GLU n 
1 155 TYR n 
1 156 MET n 
1 157 ILE n 
1 158 ASN n 
1 159 PHE n 
1 160 ILE n 
1 161 HIS n 
1 162 LYS n 
1 163 LEU n 
1 164 LYS n 
1 165 HIS n 
1 166 LEU n 
1 167 PRO n 
1 168 GLU n 
1 169 LYS n 
1 170 TYR n 
1 171 MET n 
1 172 MET n 
1 173 ASN n 
1 174 SER n 
1 175 VAL n 
1 176 LEU n 
1 177 GLU n 
1 178 ASN n 
1 179 PHE n 
1 180 THR n 
1 181 ILE n 
1 182 LEU n 
1 183 LEU n 
1 184 VAL n 
1 185 VAL n 
1 186 THR n 
1 187 ASN n 
1 188 ARG n 
1 189 ASP n 
1 190 THR n 
1 191 GLN n 
1 192 GLU n 
1 193 THR n 
1 194 LEU n 
1 195 LEU n 
1 196 CYS n 
1 197 MET n 
1 198 ALA n 
1 199 CYS n 
1 200 VAL n 
1 201 PHE n 
1 202 GLU n 
1 203 VAL n 
1 204 SER n 
1 205 ASN n 
1 206 SER n 
1 207 GLU n 
1 208 HIS n 
1 209 GLY n 
1 210 ALA n 
1 211 GLN n 
1 212 HIS n 
1 213 HIS n 
1 214 ILE n 
1 215 TYR n 
1 216 ARG n 
1 217 LEU n 
1 218 VAL n 
1 219 LYS n 
1 220 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   220 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TEAD1, TCF13, TEF1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IJL non-polymer         . 
'2-methyl-~{N}-[(1~{S})-1-(1-methylpyrazol-3-yl)-2-oxidanyl-ethyl]-4-[4-(trifluoromethyl)phenyl]pyrazolo[3,4-b]indole-7-carboxamide' 
?                               'C24 H21 F3 N6 O2' 482.458 
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ?                               'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'       105.093 
SO4   non-polymer         . 'SULFATE ION' ?                               'O4 S -2'          96.063  
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   GLY 1   207 207 GLY GLY A . n 
A 1 2   PRO 2   208 208 PRO PRO A . n 
A 1 3   ARG 3   209 209 ARG ARG A . n 
A 1 4   SER 4   210 210 SER SER A . n 
A 1 5   ILE 5   211 211 ILE ILE A . n 
A 1 6   GLY 6   212 212 GLY GLY A . n 
A 1 7   THR 7   213 213 THR THR A . n 
A 1 8   THR 8   214 214 THR THR A . n 
A 1 9   LYS 9   215 215 LYS LYS A . n 
A 1 10  LEU 10  216 216 LEU LEU A . n 
A 1 11  ARG 11  217 217 ARG ARG A . n 
A 1 12  LEU 12  218 218 LEU LEU A . n 
A 1 13  VAL 13  219 219 VAL VAL A . n 
A 1 14  GLU 14  220 220 GLU GLU A . n 
A 1 15  PHE 15  221 221 PHE PHE A . n 
A 1 16  SER 16  222 222 SER SER A . n 
A 1 17  ALA 17  223 223 ALA ALA A . n 
A 1 18  PHE 18  224 224 PHE PHE A . n 
A 1 19  LEU 19  225 225 LEU LEU A . n 
A 1 20  GLU 20  226 226 GLU GLU A . n 
A 1 21  GLN 21  227 227 GLN GLN A . n 
A 1 22  GLN 22  228 228 GLN GLN A . n 
A 1 23  ARG 23  229 229 ARG ARG A . n 
A 1 24  ASP 24  230 230 ASP ASP A . n 
A 1 25  PRO 25  231 231 PRO PRO A . n 
A 1 26  ASP 26  232 232 ASP ASP A . n 
A 1 27  SER 27  233 233 SER SER A . n 
A 1 28  TYR 28  234 234 TYR TYR A . n 
A 1 29  ASN 29  235 235 ASN ASN A . n 
A 1 30  LYS 30  236 236 LYS LYS A . n 
A 1 31  HIS 31  237 237 HIS HIS A . n 
A 1 32  LEU 32  238 238 LEU LEU A . n 
A 1 33  PHE 33  239 239 PHE PHE A . n 
A 1 34  VAL 34  240 240 VAL VAL A . n 
A 1 35  HIS 35  241 241 HIS HIS A . n 
A 1 36  ILE 36  242 242 ILE ILE A . n 
A 1 37  GLY 37  243 243 GLY GLY A . n 
A 1 38  HIS 38  244 244 HIS HIS A . n 
A 1 39  ALA 39  245 245 ALA ALA A . n 
A 1 40  ASN 40  246 246 ASN ASN A . n 
A 1 41  HIS 41  247 247 HIS HIS A . n 
A 1 42  SER 42  248 248 SER SER A . n 
A 1 43  TYR 43  249 249 TYR TYR A . n 
A 1 44  SER 44  250 250 SER SER A . n 
A 1 45  ASP 45  251 251 ASP ASP A . n 
A 1 46  PRO 46  252 252 PRO PRO A . n 
A 1 47  LEU 47  253 253 LEU LEU A . n 
A 1 48  LEU 48  254 254 LEU LEU A . n 
A 1 49  GLU 49  255 255 GLU GLU A . n 
A 1 50  SER 50  256 256 SER SER A . n 
A 1 51  VAL 51  257 257 VAL VAL A . n 
A 1 52  ASP 52  258 258 ASP ASP A . n 
A 1 53  ILE 53  259 259 ILE ILE A . n 
A 1 54  ARG 54  260 260 ARG ARG A . n 
A 1 55  GLN 55  261 261 GLN GLN A . n 
A 1 56  ILE 56  262 262 ILE ILE A . n 
A 1 57  TYR 57  263 263 TYR TYR A . n 
A 1 58  ASP 58  264 264 ASP ASP A . n 
A 1 59  LYS 59  265 265 LYS LYS A . n 
A 1 60  PHE 60  266 266 PHE PHE A . n 
A 1 61  PRO 61  267 267 PRO PRO A . n 
A 1 62  GLU 62  268 268 GLU GLU A . n 
A 1 63  LYS 63  269 269 LYS LYS A . n 
A 1 64  LYS 64  270 270 LYS LYS A . n 
A 1 65  GLY 65  271 271 GLY GLY A . n 
A 1 66  GLY 66  272 272 GLY GLY A . n 
A 1 67  LEU 67  273 273 LEU LEU A . n 
A 1 68  LYS 68  274 274 LYS LYS A . n 
A 1 69  GLU 69  275 275 GLU GLU A . n 
A 1 70  LEU 70  276 276 LEU LEU A . n 
A 1 71  PHE 71  277 277 PHE PHE A . n 
A 1 72  GLY 72  278 278 GLY GLY A . n 
A 1 73  LYS 73  279 279 LYS LYS A . n 
A 1 74  GLY 74  280 280 GLY GLY A . n 
A 1 75  PRO 75  281 281 PRO PRO A . n 
A 1 76  GLN 76  282 282 GLN GLN A . n 
A 1 77  ASN 77  283 283 ASN ASN A . n 
A 1 78  ALA 78  284 284 ALA ALA A . n 
A 1 79  PHE 79  285 285 PHE PHE A . n 
A 1 80  PHE 80  286 286 PHE PHE A . n 
A 1 81  LEU 81  287 287 LEU LEU A . n 
A 1 82  VAL 82  288 288 VAL VAL A . n 
A 1 83  LYS 83  289 289 LYS LYS A . n 
A 1 84  PHE 84  290 290 PHE PHE A . n 
A 1 85  TRP 85  291 291 TRP TRP A . n 
A 1 86  ALA 86  292 292 ALA ALA A . n 
A 1 87  ASP 87  293 293 ASP ASP A . n 
A 1 88  LEU 88  294 294 LEU LEU A . n 
A 1 89  ASN 89  295 295 ASN ASN A . n 
A 1 90  CYS 90  296 296 CYS CYS A . n 
A 1 91  ASN 91  297 297 ASN ASN A . n 
A 1 92  ILE 92  298 298 ILE ILE A . n 
A 1 93  GLN 93  299 299 GLN GLN A . n 
A 1 94  ASP 94  300 ?   ?   ?   A . n 
A 1 95  ASP 95  301 ?   ?   ?   A . n 
A 1 96  ALA 96  302 ?   ?   ?   A . n 
A 1 97  GLY 97  303 303 GLY GLY A . n 
A 1 98  ALA 98  304 304 ALA ALA A . n 
A 1 99  PHE 99  305 305 PHE PHE A . n 
A 1 100 TYR 100 306 306 TYR TYR A . n 
A 1 101 GLY 101 307 307 GLY GLY A . n 
A 1 102 VAL 102 308 308 VAL VAL A . n 
A 1 103 THR 103 309 309 THR THR A . n 
A 1 104 SER 104 310 310 SER SER A . n 
A 1 105 GLN 105 311 311 GLN GLN A . n 
A 1 106 TYR 106 312 312 TYR TYR A . n 
A 1 107 GLU 107 313 313 GLU GLU A . n 
A 1 108 SER 108 314 314 SER SER A . n 
A 1 109 SER 109 315 315 SER SER A . n 
A 1 110 GLU 110 316 316 GLU GLU A . n 
A 1 111 ASN 111 317 317 ASN ASN A . n 
A 1 112 MET 112 318 318 MET MET A . n 
A 1 113 THR 113 319 319 THR THR A . n 
A 1 114 VAL 114 320 320 VAL VAL A . n 
A 1 115 THR 115 321 321 THR THR A . n 
A 1 116 CYS 116 322 322 CYS CYS A . n 
A 1 117 SER 117 323 323 SER SER A . n 
A 1 118 THR 118 324 324 THR THR A . n 
A 1 119 LYS 119 325 325 LYS LYS A . n 
A 1 120 VAL 120 326 326 VAL VAL A . n 
A 1 121 CYS 121 327 327 CYS CYS A . n 
A 1 122 SER 122 328 328 SER SER A . n 
A 1 123 PHE 123 329 329 PHE PHE A . n 
A 1 124 GLY 124 330 330 GLY GLY A . n 
A 1 125 LYS 125 331 331 LYS LYS A . n 
A 1 126 GLN 126 332 332 GLN GLN A . n 
A 1 127 VAL 127 333 333 VAL VAL A . n 
A 1 128 VAL 128 334 334 VAL VAL A . n 
A 1 129 GLU 129 335 335 GLU GLU A . n 
A 1 130 LYS 130 336 336 LYS LYS A . n 
A 1 131 VAL 131 337 337 VAL VAL A . n 
A 1 132 GLU 132 338 338 GLU GLU A . n 
A 1 133 THR 133 339 339 THR THR A . n 
A 1 134 GLU 134 340 340 GLU GLU A . n 
A 1 135 TYR 135 341 341 TYR TYR A . n 
A 1 136 ALA 136 342 342 ALA ALA A . n 
A 1 137 ARG 137 343 343 ARG ARG A . n 
A 1 138 PHE 138 344 344 PHE PHE A . n 
A 1 139 GLU 139 345 345 GLU GLU A . n 
A 1 140 ASN 140 346 346 ASN ASN A . n 
A 1 141 GLY 141 347 347 GLY GLY A . n 
A 1 142 ARG 142 348 348 ARG ARG A . n 
A 1 143 PHE 143 349 349 PHE PHE A . n 
A 1 144 VAL 144 350 350 VAL VAL A . n 
A 1 145 TYR 145 351 351 TYR TYR A . n 
A 1 146 ARG 146 352 352 ARG ARG A . n 
A 1 147 ILE 147 353 353 ILE ILE A . n 
A 1 148 ASN 148 354 354 ASN ASN A . n 
A 1 149 ARG 149 355 355 ARG ARG A . n 
A 1 150 SER 150 356 356 SER SER A . n 
A 1 151 PRO 151 357 357 PRO PRO A . n 
A 1 152 MET 152 358 358 MET MET A . n 
A 1 153 CYS 153 359 359 CYS CYS A . n 
A 1 154 GLU 154 360 360 GLU GLU A . n 
A 1 155 TYR 155 361 361 TYR TYR A . n 
A 1 156 MET 156 362 362 MET MET A . n 
A 1 157 ILE 157 363 363 ILE ILE A . n 
A 1 158 ASN 158 364 364 ASN ASN A . n 
A 1 159 PHE 159 365 365 PHE PHE A . n 
A 1 160 ILE 160 366 366 ILE ILE A . n 
A 1 161 HIS 161 367 367 HIS HIS A . n 
A 1 162 LYS 162 368 368 LYS LYS A . n 
A 1 163 LEU 163 369 369 LEU LEU A . n 
A 1 164 LYS 164 370 370 LYS LYS A . n 
A 1 165 HIS 165 371 371 HIS HIS A . n 
A 1 166 LEU 166 372 372 LEU LEU A . n 
A 1 167 PRO 167 373 373 PRO PRO A . n 
A 1 168 GLU 168 374 374 GLU GLU A . n 
A 1 169 LYS 169 375 375 LYS LYS A . n 
A 1 170 TYR 170 376 376 TYR TYR A . n 
A 1 171 MET 171 377 377 MET MET A . n 
A 1 172 MET 172 378 378 MET MET A . n 
A 1 173 ASN 173 379 379 ASN ASN A . n 
A 1 174 SER 174 380 380 SER SER A . n 
A 1 175 VAL 175 381 381 VAL VAL A . n 
A 1 176 LEU 176 382 382 LEU LEU A . n 
A 1 177 GLU 177 383 383 GLU GLU A . n 
A 1 178 ASN 178 384 384 ASN ASN A . n 
A 1 179 PHE 179 385 385 PHE PHE A . n 
A 1 180 THR 180 386 386 THR THR A . n 
A 1 181 ILE 181 387 387 ILE ILE A . n 
A 1 182 LEU 182 388 388 LEU LEU A . n 
A 1 183 LEU 183 389 389 LEU LEU A . n 
A 1 184 VAL 184 390 390 VAL VAL A . n 
A 1 185 VAL 185 391 391 VAL VAL A . n 
A 1 186 THR 186 392 392 THR THR A . n 
A 1 187 ASN 187 393 393 ASN ASN A . n 
A 1 188 ARG 188 394 394 ARG ARG A . n 
A 1 189 ASP 189 395 395 ASP ASP A . n 
A 1 190 THR 190 396 396 THR THR A . n 
A 1 191 GLN 191 397 397 GLN GLN A . n 
A 1 192 GLU 192 398 398 GLU GLU A . n 
A 1 193 THR 193 399 399 THR THR A . n 
A 1 194 LEU 194 400 400 LEU LEU A . n 
A 1 195 LEU 195 401 401 LEU LEU A . n 
A 1 196 CYS 196 402 402 CYS CYS A . n 
A 1 197 MET 197 403 403 MET MET A . n 
A 1 198 ALA 198 404 404 ALA ALA A . n 
A 1 199 CYS 199 405 405 CYS CYS A . n 
A 1 200 VAL 200 406 406 VAL VAL A . n 
A 1 201 PHE 201 407 407 PHE PHE A . n 
A 1 202 GLU 202 408 408 GLU GLU A . n 
A 1 203 VAL 203 409 409 VAL VAL A . n 
A 1 204 SER 204 410 410 SER SER A . n 
A 1 205 ASN 205 411 411 ASN ASN A . n 
A 1 206 SER 206 412 412 SER SER A . n 
A 1 207 GLU 207 413 413 GLU GLU A . n 
A 1 208 HIS 208 414 414 HIS HIS A . n 
A 1 209 GLY 209 415 415 GLY GLY A . n 
A 1 210 ALA 210 416 416 ALA ALA A . n 
A 1 211 GLN 211 417 417 GLN GLN A . n 
A 1 212 HIS 212 418 418 HIS HIS A . n 
A 1 213 HIS 213 419 419 HIS HIS A . n 
A 1 214 ILE 214 420 420 ILE ILE A . n 
A 1 215 TYR 215 421 421 TYR TYR A . n 
A 1 216 ARG 216 422 422 ARG ARG A . n 
A 1 217 LEU 217 423 423 LEU LEU A . n 
A 1 218 VAL 218 424 424 VAL VAL A . n 
A 1 219 LYS 219 425 425 LYS LYS A . n 
A 1 220 ASP 220 426 ?   ?   ?   A . n 
B 1 1   GLY 1   207 207 GLY GLY B . n 
B 1 2   PRO 2   208 208 PRO PRO B . n 
B 1 3   ARG 3   209 209 ARG ARG B . n 
B 1 4   SER 4   210 210 SER SER B . n 
B 1 5   ILE 5   211 211 ILE ILE B . n 
B 1 6   GLY 6   212 212 GLY GLY B . n 
B 1 7   THR 7   213 213 THR THR B . n 
B 1 8   THR 8   214 214 THR THR B . n 
B 1 9   LYS 9   215 215 LYS LYS B . n 
B 1 10  LEU 10  216 216 LEU LEU B . n 
B 1 11  ARG 11  217 217 ARG ARG B . n 
B 1 12  LEU 12  218 218 LEU LEU B . n 
B 1 13  VAL 13  219 219 VAL VAL B . n 
B 1 14  GLU 14  220 220 GLU GLU B . n 
B 1 15  PHE 15  221 221 PHE PHE B . n 
B 1 16  SER 16  222 222 SER SER B . n 
B 1 17  ALA 17  223 223 ALA ALA B . n 
B 1 18  PHE 18  224 224 PHE PHE B . n 
B 1 19  LEU 19  225 225 LEU LEU B . n 
B 1 20  GLU 20  226 226 GLU GLU B . n 
B 1 21  GLN 21  227 227 GLN GLN B . n 
B 1 22  GLN 22  228 228 GLN GLN B . n 
B 1 23  ARG 23  229 229 ARG ARG B . n 
B 1 24  ASP 24  230 230 ASP ASP B . n 
B 1 25  PRO 25  231 231 PRO PRO B . n 
B 1 26  ASP 26  232 232 ASP ASP B . n 
B 1 27  SER 27  233 233 SER SER B . n 
B 1 28  TYR 28  234 234 TYR TYR B . n 
B 1 29  ASN 29  235 235 ASN ASN B . n 
B 1 30  LYS 30  236 236 LYS LYS B . n 
B 1 31  HIS 31  237 237 HIS HIS B . n 
B 1 32  LEU 32  238 238 LEU LEU B . n 
B 1 33  PHE 33  239 239 PHE PHE B . n 
B 1 34  VAL 34  240 240 VAL VAL B . n 
B 1 35  HIS 35  241 241 HIS HIS B . n 
B 1 36  ILE 36  242 242 ILE ILE B . n 
B 1 37  GLY 37  243 243 GLY GLY B . n 
B 1 38  HIS 38  244 244 HIS HIS B . n 
B 1 39  ALA 39  245 245 ALA ALA B . n 
B 1 40  ASN 40  246 246 ASN ASN B . n 
B 1 41  HIS 41  247 247 HIS HIS B . n 
B 1 42  SER 42  248 248 SER SER B . n 
B 1 43  TYR 43  249 249 TYR TYR B . n 
B 1 44  SER 44  250 250 SER SER B . n 
B 1 45  ASP 45  251 251 ASP ASP B . n 
B 1 46  PRO 46  252 252 PRO PRO B . n 
B 1 47  LEU 47  253 253 LEU LEU B . n 
B 1 48  LEU 48  254 254 LEU LEU B . n 
B 1 49  GLU 49  255 255 GLU GLU B . n 
B 1 50  SER 50  256 256 SER SER B . n 
B 1 51  VAL 51  257 257 VAL VAL B . n 
B 1 52  ASP 52  258 258 ASP ASP B . n 
B 1 53  ILE 53  259 259 ILE ILE B . n 
B 1 54  ARG 54  260 260 ARG ARG B . n 
B 1 55  GLN 55  261 261 GLN GLN B . n 
B 1 56  ILE 56  262 262 ILE ILE B . n 
B 1 57  TYR 57  263 263 TYR TYR B . n 
B 1 58  ASP 58  264 264 ASP ASP B . n 
B 1 59  LYS 59  265 265 LYS LYS B . n 
B 1 60  PHE 60  266 266 PHE PHE B . n 
B 1 61  PRO 61  267 267 PRO PRO B . n 
B 1 62  GLU 62  268 268 GLU GLU B . n 
B 1 63  LYS 63  269 269 LYS LYS B . n 
B 1 64  LYS 64  270 270 LYS LYS B . n 
B 1 65  GLY 65  271 271 GLY GLY B . n 
B 1 66  GLY 66  272 272 GLY GLY B . n 
B 1 67  LEU 67  273 273 LEU LEU B . n 
B 1 68  LYS 68  274 274 LYS LYS B . n 
B 1 69  GLU 69  275 275 GLU GLU B . n 
B 1 70  LEU 70  276 276 LEU LEU B . n 
B 1 71  PHE 71  277 277 PHE PHE B . n 
B 1 72  GLY 72  278 278 GLY GLY B . n 
B 1 73  LYS 73  279 279 LYS LYS B . n 
B 1 74  GLY 74  280 280 GLY GLY B . n 
B 1 75  PRO 75  281 281 PRO PRO B . n 
B 1 76  GLN 76  282 282 GLN GLN B . n 
B 1 77  ASN 77  283 283 ASN ASN B . n 
B 1 78  ALA 78  284 284 ALA ALA B . n 
B 1 79  PHE 79  285 285 PHE PHE B . n 
B 1 80  PHE 80  286 286 PHE PHE B . n 
B 1 81  LEU 81  287 287 LEU LEU B . n 
B 1 82  VAL 82  288 288 VAL VAL B . n 
B 1 83  LYS 83  289 289 LYS LYS B . n 
B 1 84  PHE 84  290 290 PHE PHE B . n 
B 1 85  TRP 85  291 291 TRP TRP B . n 
B 1 86  ALA 86  292 292 ALA ALA B . n 
B 1 87  ASP 87  293 293 ASP ASP B . n 
B 1 88  LEU 88  294 294 LEU LEU B . n 
B 1 89  ASN 89  295 295 ASN ASN B . n 
B 1 90  CYS 90  296 296 CYS CYS B . n 
B 1 91  ASN 91  297 297 ASN ASN B . n 
B 1 92  ILE 92  298 298 ILE ILE B . n 
B 1 93  GLN 93  299 299 GLN GLN B . n 
B 1 94  ASP 94  300 300 ASP ASP B . n 
B 1 95  ASP 95  301 301 ASP ASP B . n 
B 1 96  ALA 96  302 302 ALA ALA B . n 
B 1 97  GLY 97  303 303 GLY GLY B . n 
B 1 98  ALA 98  304 304 ALA ALA B . n 
B 1 99  PHE 99  305 305 PHE PHE B . n 
B 1 100 TYR 100 306 306 TYR TYR B . n 
B 1 101 GLY 101 307 307 GLY GLY B . n 
B 1 102 VAL 102 308 308 VAL VAL B . n 
B 1 103 THR 103 309 309 THR THR B . n 
B 1 104 SER 104 310 310 SER SER B . n 
B 1 105 GLN 105 311 311 GLN GLN B . n 
B 1 106 TYR 106 312 312 TYR TYR B . n 
B 1 107 GLU 107 313 313 GLU GLU B . n 
B 1 108 SER 108 314 314 SER SER B . n 
B 1 109 SER 109 315 315 SER SER B . n 
B 1 110 GLU 110 316 316 GLU GLU B . n 
B 1 111 ASN 111 317 317 ASN ASN B . n 
B 1 112 MET 112 318 318 MET MET B . n 
B 1 113 THR 113 319 319 THR THR B . n 
B 1 114 VAL 114 320 320 VAL VAL B . n 
B 1 115 THR 115 321 321 THR THR B . n 
B 1 116 CYS 116 322 322 CYS CYS B . n 
B 1 117 SER 117 323 323 SER SER B . n 
B 1 118 THR 118 324 324 THR THR B . n 
B 1 119 LYS 119 325 325 LYS LYS B . n 
B 1 120 VAL 120 326 326 VAL VAL B . n 
B 1 121 CYS 121 327 327 CYS CYS B . n 
B 1 122 SER 122 328 328 SER SER B . n 
B 1 123 PHE 123 329 329 PHE PHE B . n 
B 1 124 GLY 124 330 330 GLY GLY B . n 
B 1 125 LYS 125 331 331 LYS LYS B . n 
B 1 126 GLN 126 332 332 GLN GLN B . n 
B 1 127 VAL 127 333 333 VAL VAL B . n 
B 1 128 VAL 128 334 334 VAL VAL B . n 
B 1 129 GLU 129 335 335 GLU GLU B . n 
B 1 130 LYS 130 336 336 LYS LYS B . n 
B 1 131 VAL 131 337 337 VAL VAL B . n 
B 1 132 GLU 132 338 338 GLU GLU B . n 
B 1 133 THR 133 339 339 THR THR B . n 
B 1 134 GLU 134 340 340 GLU GLU B . n 
B 1 135 TYR 135 341 341 TYR TYR B . n 
B 1 136 ALA 136 342 342 ALA ALA B . n 
B 1 137 ARG 137 343 343 ARG ARG B . n 
B 1 138 PHE 138 344 344 PHE PHE B . n 
B 1 139 GLU 139 345 345 GLU GLU B . n 
B 1 140 ASN 140 346 346 ASN ASN B . n 
B 1 141 GLY 141 347 347 GLY GLY B . n 
B 1 142 ARG 142 348 348 ARG ARG B . n 
B 1 143 PHE 143 349 349 PHE PHE B . n 
B 1 144 VAL 144 350 350 VAL VAL B . n 
B 1 145 TYR 145 351 351 TYR TYR B . n 
B 1 146 ARG 146 352 352 ARG ARG B . n 
B 1 147 ILE 147 353 353 ILE ILE B . n 
B 1 148 ASN 148 354 354 ASN ASN B . n 
B 1 149 ARG 149 355 355 ARG ARG B . n 
B 1 150 SER 150 356 356 SER SER B . n 
B 1 151 PRO 151 357 357 PRO PRO B . n 
B 1 152 MET 152 358 358 MET MET B . n 
B 1 153 CYS 153 359 359 CYS CYS B . n 
B 1 154 GLU 154 360 360 GLU GLU B . n 
B 1 155 TYR 155 361 361 TYR TYR B . n 
B 1 156 MET 156 362 362 MET MET B . n 
B 1 157 ILE 157 363 363 ILE ILE B . n 
B 1 158 ASN 158 364 364 ASN ASN B . n 
B 1 159 PHE 159 365 365 PHE PHE B . n 
B 1 160 ILE 160 366 366 ILE ILE B . n 
B 1 161 HIS 161 367 367 HIS HIS B . n 
B 1 162 LYS 162 368 368 LYS LYS B . n 
B 1 163 LEU 163 369 369 LEU LEU B . n 
B 1 164 LYS 164 370 370 LYS LYS B . n 
B 1 165 HIS 165 371 371 HIS HIS B . n 
B 1 166 LEU 166 372 372 LEU LEU B . n 
B 1 167 PRO 167 373 373 PRO PRO B . n 
B 1 168 GLU 168 374 374 GLU GLU B . n 
B 1 169 LYS 169 375 375 LYS LYS B . n 
B 1 170 TYR 170 376 376 TYR TYR B . n 
B 1 171 MET 171 377 377 MET MET B . n 
B 1 172 MET 172 378 378 MET MET B . n 
B 1 173 ASN 173 379 379 ASN ASN B . n 
B 1 174 SER 174 380 380 SER SER B . n 
B 1 175 VAL 175 381 381 VAL VAL B . n 
B 1 176 LEU 176 382 382 LEU LEU B . n 
B 1 177 GLU 177 383 383 GLU GLU B . n 
B 1 178 ASN 178 384 384 ASN ASN B . n 
B 1 179 PHE 179 385 385 PHE PHE B . n 
B 1 180 THR 180 386 386 THR THR B . n 
B 1 181 ILE 181 387 387 ILE ILE B . n 
B 1 182 LEU 182 388 388 LEU LEU B . n 
B 1 183 LEU 183 389 389 LEU LEU B . n 
B 1 184 VAL 184 390 390 VAL VAL B . n 
B 1 185 VAL 185 391 391 VAL VAL B . n 
B 1 186 THR 186 392 392 THR THR B . n 
B 1 187 ASN 187 393 393 ASN ASN B . n 
B 1 188 ARG 188 394 394 ARG ARG B . n 
B 1 189 ASP 189 395 395 ASP ASP B . n 
B 1 190 THR 190 396 396 THR THR B . n 
B 1 191 GLN 191 397 397 GLN GLN B . n 
B 1 192 GLU 192 398 398 GLU GLU B . n 
B 1 193 THR 193 399 399 THR THR B . n 
B 1 194 LEU 194 400 400 LEU LEU B . n 
B 1 195 LEU 195 401 401 LEU LEU B . n 
B 1 196 CYS 196 402 402 CYS CYS B . n 
B 1 197 MET 197 403 403 MET MET B . n 
B 1 198 ALA 198 404 404 ALA ALA B . n 
B 1 199 CYS 199 405 405 CYS CYS B . n 
B 1 200 VAL 200 406 406 VAL VAL B . n 
B 1 201 PHE 201 407 407 PHE PHE B . n 
B 1 202 GLU 202 408 408 GLU GLU B . n 
B 1 203 VAL 203 409 409 VAL VAL B . n 
B 1 204 SER 204 410 410 SER SER B . n 
B 1 205 ASN 205 411 411 ASN ASN B . n 
B 1 206 SER 206 412 412 SER SER B . n 
B 1 207 GLU 207 413 413 GLU GLU B . n 
B 1 208 HIS 208 414 414 HIS HIS B . n 
B 1 209 GLY 209 415 415 GLY GLY B . n 
B 1 210 ALA 210 416 416 ALA ALA B . n 
B 1 211 GLN 211 417 417 GLN GLN B . n 
B 1 212 HIS 212 418 418 HIS HIS B . n 
B 1 213 HIS 213 419 419 HIS HIS B . n 
B 1 214 ILE 214 420 420 ILE ILE B . n 
B 1 215 TYR 215 421 421 TYR TYR B . n 
B 1 216 ARG 216 422 422 ARG ARG B . n 
B 1 217 LEU 217 423 423 LEU LEU B . n 
B 1 218 VAL 218 424 424 VAL VAL B . n 
B 1 219 LYS 219 425 425 LYS LYS B . n 
B 1 220 ASP 220 426 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IJL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IJL 
_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 
C 2 GOL   1   501 1   GOL   GOL A . 
D 3 A1IJL 1   502 1   A1IJL INH A . 
E 4 SO4   1   503 2   SO4   SO4 A . 
F 4 SO4   1   504 4   SO4   SO4 A . 
G 4 SO4   1   505 6   SO4   SO4 A . 
H 2 GOL   1   501 2   GOL   GOL B . 
I 3 A1IJL 1   502 2   A1IJL INH B . 
J 4 SO4   1   503 1   SO4   SO4 B . 
K 4 SO4   1   504 3   SO4   SO4 B . 
L 4 SO4   1   505 5   SO4   SO4 B . 
M 5 HOH   1   601 66  HOH   HOH A . 
M 5 HOH   2   602 8   HOH   HOH A . 
M 5 HOH   3   603 49  HOH   HOH A . 
M 5 HOH   4   604 214 HOH   HOH A . 
M 5 HOH   5   605 71  HOH   HOH A . 
M 5 HOH   6   606 203 HOH   HOH A . 
M 5 HOH   7   607 15  HOH   HOH A . 
M 5 HOH   8   608 53  HOH   HOH A . 
M 5 HOH   9   609 9   HOH   HOH A . 
M 5 HOH   10  610 5   HOH   HOH A . 
M 5 HOH   11  611 87  HOH   HOH A . 
M 5 HOH   12  612 17  HOH   HOH A . 
M 5 HOH   13  613 155 HOH   HOH A . 
M 5 HOH   14  614 167 HOH   HOH A . 
M 5 HOH   15  615 106 HOH   HOH A . 
M 5 HOH   16  616 177 HOH   HOH A . 
M 5 HOH   17  617 103 HOH   HOH A . 
M 5 HOH   18  618 190 HOH   HOH A . 
M 5 HOH   19  619 191 HOH   HOH A . 
M 5 HOH   20  620 3   HOH   HOH A . 
M 5 HOH   21  621 159 HOH   HOH A . 
M 5 HOH   22  622 114 HOH   HOH A . 
M 5 HOH   23  623 164 HOH   HOH A . 
M 5 HOH   24  624 152 HOH   HOH A . 
M 5 HOH   25  625 115 HOH   HOH A . 
M 5 HOH   26  626 54  HOH   HOH A . 
M 5 HOH   27  627 86  HOH   HOH A . 
M 5 HOH   28  628 70  HOH   HOH A . 
M 5 HOH   29  629 173 HOH   HOH A . 
M 5 HOH   30  630 157 HOH   HOH A . 
M 5 HOH   31  631 2   HOH   HOH A . 
M 5 HOH   32  632 11  HOH   HOH A . 
M 5 HOH   33  633 4   HOH   HOH A . 
M 5 HOH   34  634 154 HOH   HOH A . 
M 5 HOH   35  635 14  HOH   HOH A . 
M 5 HOH   36  636 52  HOH   HOH A . 
M 5 HOH   37  637 99  HOH   HOH A . 
M 5 HOH   38  638 149 HOH   HOH A . 
M 5 HOH   39  639 59  HOH   HOH A . 
M 5 HOH   40  640 6   HOH   HOH A . 
M 5 HOH   41  641 192 HOH   HOH A . 
M 5 HOH   42  642 146 HOH   HOH A . 
M 5 HOH   43  643 18  HOH   HOH A . 
M 5 HOH   44  644 16  HOH   HOH A . 
M 5 HOH   45  645 89  HOH   HOH A . 
M 5 HOH   46  646 82  HOH   HOH A . 
M 5 HOH   47  647 200 HOH   HOH A . 
M 5 HOH   48  648 79  HOH   HOH A . 
M 5 HOH   49  649 130 HOH   HOH A . 
M 5 HOH   50  650 118 HOH   HOH A . 
M 5 HOH   51  651 13  HOH   HOH A . 
M 5 HOH   52  652 145 HOH   HOH A . 
M 5 HOH   53  653 193 HOH   HOH A . 
M 5 HOH   54  654 7   HOH   HOH A . 
M 5 HOH   55  655 43  HOH   HOH A . 
M 5 HOH   56  656 178 HOH   HOH A . 
M 5 HOH   57  657 183 HOH   HOH A . 
M 5 HOH   58  658 116 HOH   HOH A . 
M 5 HOH   59  659 186 HOH   HOH A . 
M 5 HOH   60  660 65  HOH   HOH A . 
M 5 HOH   61  661 188 HOH   HOH A . 
M 5 HOH   62  662 132 HOH   HOH A . 
M 5 HOH   63  663 121 HOH   HOH A . 
M 5 HOH   64  664 202 HOH   HOH A . 
M 5 HOH   65  665 112 HOH   HOH A . 
M 5 HOH   66  666 163 HOH   HOH A . 
M 5 HOH   67  667 102 HOH   HOH A . 
M 5 HOH   68  668 101 HOH   HOH A . 
M 5 HOH   69  669 162 HOH   HOH A . 
M 5 HOH   70  670 156 HOH   HOH A . 
M 5 HOH   71  671 10  HOH   HOH A . 
M 5 HOH   72  672 111 HOH   HOH A . 
M 5 HOH   73  673 123 HOH   HOH A . 
M 5 HOH   74  674 92  HOH   HOH A . 
M 5 HOH   75  675 215 HOH   HOH A . 
M 5 HOH   76  676 158 HOH   HOH A . 
M 5 HOH   77  677 55  HOH   HOH A . 
M 5 HOH   78  678 153 HOH   HOH A . 
M 5 HOH   79  679 187 HOH   HOH A . 
M 5 HOH   80  680 51  HOH   HOH A . 
M 5 HOH   81  681 1   HOH   HOH A . 
M 5 HOH   82  682 142 HOH   HOH A . 
M 5 HOH   83  683 64  HOH   HOH A . 
M 5 HOH   84  684 198 HOH   HOH A . 
M 5 HOH   85  685 12  HOH   HOH A . 
M 5 HOH   86  686 211 HOH   HOH A . 
M 5 HOH   87  687 91  HOH   HOH A . 
M 5 HOH   88  688 179 HOH   HOH A . 
M 5 HOH   89  689 133 HOH   HOH A . 
M 5 HOH   90  690 141 HOH   HOH A . 
M 5 HOH   91  691 213 HOH   HOH A . 
M 5 HOH   92  692 74  HOH   HOH A . 
M 5 HOH   93  693 77  HOH   HOH A . 
M 5 HOH   94  694 189 HOH   HOH A . 
M 5 HOH   95  695 139 HOH   HOH A . 
M 5 HOH   96  696 108 HOH   HOH A . 
M 5 HOH   97  697 124 HOH   HOH A . 
M 5 HOH   98  698 216 HOH   HOH A . 
M 5 HOH   99  699 184 HOH   HOH A . 
M 5 HOH   100 700 119 HOH   HOH A . 
M 5 HOH   101 701 207 HOH   HOH A . 
M 5 HOH   102 702 127 HOH   HOH A . 
M 5 HOH   103 703 126 HOH   HOH A . 
M 5 HOH   104 704 212 HOH   HOH A . 
M 5 HOH   105 705 172 HOH   HOH A . 
M 5 HOH   106 706 208 HOH   HOH A . 
M 5 HOH   107 707 168 HOH   HOH A . 
M 5 HOH   108 708 176 HOH   HOH A . 
M 5 HOH   109 709 197 HOH   HOH A . 
M 5 HOH   110 710 160 HOH   HOH A . 
M 5 HOH   111 711 199 HOH   HOH A . 
M 5 HOH   112 712 136 HOH   HOH A . 
N 5 HOH   1   601 29  HOH   HOH B . 
N 5 HOH   2   602 57  HOH   HOH B . 
N 5 HOH   3   603 90  HOH   HOH B . 
N 5 HOH   4   604 135 HOH   HOH B . 
N 5 HOH   5   605 204 HOH   HOH B . 
N 5 HOH   6   606 38  HOH   HOH B . 
N 5 HOH   7   607 22  HOH   HOH B . 
N 5 HOH   8   608 210 HOH   HOH B . 
N 5 HOH   9   609 48  HOH   HOH B . 
N 5 HOH   10  610 144 HOH   HOH B . 
N 5 HOH   11  611 209 HOH   HOH B . 
N 5 HOH   12  612 24  HOH   HOH B . 
N 5 HOH   13  613 196 HOH   HOH B . 
N 5 HOH   14  614 27  HOH   HOH B . 
N 5 HOH   15  615 120 HOH   HOH B . 
N 5 HOH   16  616 23  HOH   HOH B . 
N 5 HOH   17  617 28  HOH   HOH B . 
N 5 HOH   18  618 166 HOH   HOH B . 
N 5 HOH   19  619 62  HOH   HOH B . 
N 5 HOH   20  620 32  HOH   HOH B . 
N 5 HOH   21  621 194 HOH   HOH B . 
N 5 HOH   22  622 117 HOH   HOH B . 
N 5 HOH   23  623 35  HOH   HOH B . 
N 5 HOH   24  624 47  HOH   HOH B . 
N 5 HOH   25  625 34  HOH   HOH B . 
N 5 HOH   26  626 25  HOH   HOH B . 
N 5 HOH   27  627 30  HOH   HOH B . 
N 5 HOH   28  628 41  HOH   HOH B . 
N 5 HOH   29  629 110 HOH   HOH B . 
N 5 HOH   30  630 40  HOH   HOH B . 
N 5 HOH   31  631 42  HOH   HOH B . 
N 5 HOH   32  632 50  HOH   HOH B . 
N 5 HOH   33  633 33  HOH   HOH B . 
N 5 HOH   34  634 85  HOH   HOH B . 
N 5 HOH   35  635 69  HOH   HOH B . 
N 5 HOH   36  636 95  HOH   HOH B . 
N 5 HOH   37  637 39  HOH   HOH B . 
N 5 HOH   38  638 201 HOH   HOH B . 
N 5 HOH   39  639 19  HOH   HOH B . 
N 5 HOH   40  640 36  HOH   HOH B . 
N 5 HOH   41  641 147 HOH   HOH B . 
N 5 HOH   42  642 128 HOH   HOH B . 
N 5 HOH   43  643 26  HOH   HOH B . 
N 5 HOH   44  644 107 HOH   HOH B . 
N 5 HOH   45  645 148 HOH   HOH B . 
N 5 HOH   46  646 80  HOH   HOH B . 
N 5 HOH   47  647 98  HOH   HOH B . 
N 5 HOH   48  648 105 HOH   HOH B . 
N 5 HOH   49  649 93  HOH   HOH B . 
N 5 HOH   50  650 122 HOH   HOH B . 
N 5 HOH   51  651 104 HOH   HOH B . 
N 5 HOH   52  652 31  HOH   HOH B . 
N 5 HOH   53  653 21  HOH   HOH B . 
N 5 HOH   54  654 44  HOH   HOH B . 
N 5 HOH   55  655 81  HOH   HOH B . 
N 5 HOH   56  656 45  HOH   HOH B . 
N 5 HOH   57  657 180 HOH   HOH B . 
N 5 HOH   58  658 171 HOH   HOH B . 
N 5 HOH   59  659 100 HOH   HOH B . 
N 5 HOH   60  660 75  HOH   HOH B . 
N 5 HOH   61  661 165 HOH   HOH B . 
N 5 HOH   62  662 72  HOH   HOH B . 
N 5 HOH   63  663 73  HOH   HOH B . 
N 5 HOH   64  664 125 HOH   HOH B . 
N 5 HOH   65  665 20  HOH   HOH B . 
N 5 HOH   66  666 84  HOH   HOH B . 
N 5 HOH   67  667 67  HOH   HOH B . 
N 5 HOH   68  668 113 HOH   HOH B . 
N 5 HOH   69  669 78  HOH   HOH B . 
N 5 HOH   70  670 56  HOH   HOH B . 
N 5 HOH   71  671 63  HOH   HOH B . 
N 5 HOH   72  672 195 HOH   HOH B . 
N 5 HOH   73  673 205 HOH   HOH B . 
N 5 HOH   74  674 134 HOH   HOH B . 
N 5 HOH   75  675 68  HOH   HOH B . 
N 5 HOH   76  676 140 HOH   HOH B . 
N 5 HOH   77  677 143 HOH   HOH B . 
N 5 HOH   78  678 83  HOH   HOH B . 
N 5 HOH   79  679 58  HOH   HOH B . 
N 5 HOH   80  680 76  HOH   HOH B . 
N 5 HOH   81  681 150 HOH   HOH B . 
N 5 HOH   82  682 151 HOH   HOH B . 
N 5 HOH   83  683 60  HOH   HOH B . 
N 5 HOH   84  684 46  HOH   HOH B . 
N 5 HOH   85  685 161 HOH   HOH B . 
N 5 HOH   86  686 175 HOH   HOH B . 
N 5 HOH   87  687 97  HOH   HOH B . 
N 5 HOH   88  688 174 HOH   HOH B . 
N 5 HOH   89  689 129 HOH   HOH B . 
N 5 HOH   90  690 109 HOH   HOH B . 
N 5 HOH   91  691 61  HOH   HOH B . 
N 5 HOH   92  692 96  HOH   HOH B . 
N 5 HOH   93  693 170 HOH   HOH B . 
N 5 HOH   94  694 182 HOH   HOH B . 
N 5 HOH   95  695 88  HOH   HOH B . 
N 5 HOH   96  696 169 HOH   HOH B . 
N 5 HOH   97  697 37  HOH   HOH B . 
N 5 HOH   98  698 94  HOH   HOH B . 
N 5 HOH   99  699 217 HOH   HOH B . 
N 5 HOH   100 700 185 HOH   HOH B . 
N 5 HOH   101 701 206 HOH   HOH B . 
N 5 HOH   102 702 131 HOH   HOH B . 
N 5 HOH   103 703 181 HOH   HOH B . 
N 5 HOH   104 704 138 HOH   HOH B . 
N 5 HOH   105 705 137 HOH   HOH B . 
# 
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 0 A LYS 269 ? CD  ? A LYS 63  CD  
2  1 Y 0 A LYS 269 ? CE  ? A LYS 63  CE  
3  1 Y 0 A LYS 269 ? NZ  ? A LYS 63  NZ  
4  1 Y 0 A LYS 270 ? CG  ? A LYS 64  CG  
5  1 Y 0 A LYS 270 ? CD  ? A LYS 64  CD  
6  1 Y 0 A LYS 270 ? CE  ? A LYS 64  CE  
7  1 Y 0 A LYS 270 ? NZ  ? A LYS 64  NZ  
8  1 Y 0 A LYS 279 ? CD  ? A LYS 73  CD  
9  1 Y 0 A LYS 279 ? CE  ? A LYS 73  CE  
10 1 Y 0 A LYS 279 ? NZ  ? A LYS 73  NZ  
11 1 Y 0 A LYS 331 ? CE  ? A LYS 125 CE  
12 1 Y 0 A LYS 331 ? NZ  ? A LYS 125 NZ  
13 1 Y 0 A HIS 414 ? CG  ? A HIS 208 CG  
14 1 Y 0 A HIS 414 ? ND1 ? A HIS 208 ND1 
15 1 Y 0 A HIS 414 ? CD2 ? A HIS 208 CD2 
16 1 Y 0 A HIS 414 ? CE1 ? A HIS 208 CE1 
17 1 Y 0 A HIS 414 ? NE2 ? A HIS 208 NE2 
18 1 Y 0 B LYS 215 ? CD  ? B LYS 9   CD  
19 1 Y 0 B LYS 215 ? CE  ? B LYS 9   CE  
20 1 Y 0 B LYS 215 ? NZ  ? B LYS 9   NZ  
21 1 Y 0 B LYS 269 ? CG  ? B LYS 63  CG  
22 1 Y 0 B LYS 269 ? CD  ? B LYS 63  CD  
23 1 Y 0 B LYS 269 ? CE  ? B LYS 63  CE  
24 1 Y 0 B LYS 269 ? NZ  ? B LYS 63  NZ  
25 1 Y 0 B ASP 300 ? CG  ? B ASP 94  CG  
26 1 Y 0 B ASP 300 ? OD1 ? B ASP 94  OD1 
27 1 Y 0 B ASP 300 ? OD2 ? B ASP 94  OD2 
28 1 Y 0 B ASP 301 ? CG  ? B ASP 95  CG  
29 1 Y 0 B ASP 301 ? OD1 ? B ASP 95  OD1 
30 1 Y 0 B ASP 301 ? OD2 ? B ASP 95  OD2 
31 1 Y 0 B GLU 413 ? CG  ? B GLU 207 CG  
32 1 Y 0 B GLU 413 ? CD  ? B GLU 207 CD  
33 1 Y 0 B GLU 413 ? OE1 ? B GLU 207 OE1 
34 1 Y 0 B GLU 413 ? OE2 ? B GLU 207 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GAX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     107.995 
_cell.length_a_esd                 ? 
_cell.length_b                     107.995 
_cell.length_b_esd                 ? 
_cell.length_c                     132.202 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9GAX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GAX 
_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             3.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.50 
_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          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '3.5 M Ammonium sulfate, 1% (v/v) MPD, 0.1 M MES pH 6.5' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-26 
_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   0.97625 
_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 ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GAX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.928 
_reflns.d_resolution_low                               83.636 
_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                                     48555 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           92.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_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                                0.173 
_reflns.pdbx_Rpim_I_all                                0.055 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.928 
_reflns_shell.d_res_low                                     2.065 
_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                             2429 
_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                               0.512 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.633 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 9GAX 
_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                            1.93 
_refine.ls_d_res_low                             28.19 
_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                     48534 
_refine.ls_number_reflns_R_free                  2349 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    81.60 
_refine.ls_percent_reflns_R_free                 4.84 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1875 
_refine.ls_R_factor_R_free                       0.2186 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1860 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 22.41 
_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                            0.17 
_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.pdbx_number_atoms_protein        3539 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         112 
_refine_hist.number_atoms_solvent             217 
_refine_hist.number_atoms_total               3868 
_refine_hist.d_res_high                       1.93 
_refine_hist.d_res_low                        28.19 
# 
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' ? 0.008 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.021 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.139 ? 577 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.067 ? 547 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 662 ? f_plane_restr      ? ? 
# 
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' 2.01 2.06 . . 58  1304 40.00  . . . . 0.2544 . . . . . . . . . . . 0.3311 
'X-RAY DIFFRACTION' 2.06 2.11 . . 100 2428 73.00  . . . . 0.2471 . . . . . . . . . . . 0.2716 
'X-RAY DIFFRACTION' 2.11 2.16 . . 154 3070 93.00  . . . . 0.2351 . . . . . . . . . . . 0.2798 
'X-RAY DIFFRACTION' 2.16 2.23 . . 179 3210 99.00  . . . . 0.2318 . . . . . . . . . . . 0.2434 
'X-RAY DIFFRACTION' 2.23 2.30 . . 118 2041 62.00  . . . . 0.2251 . . . . . . . . . . . 0.2381 
'X-RAY DIFFRACTION' 2.30 2.38 . . 149 3287 100.00 . . . . 0.2178 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 2.38 2.48 . . 156 3327 100.00 . . . . 0.2067 . . . . . . . . . . . 0.2511 
'X-RAY DIFFRACTION' 2.48 2.59 . . 193 3299 100.00 . . . . 0.2020 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 2.59 2.73 . . 198 3281 100.00 . . . . 0.1949 . . . . . . . . . . . 0.2207 
'X-RAY DIFFRACTION' 2.73 2.90 . . 168 3313 100.00 . . . . 0.1966 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 2.90 3.12 . . 162 3346 100.00 . . . . 0.1907 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 3.12 3.43 . . 163 3366 100.00 . . . . 0.1678 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 3.44 3.93 . . 162 3203 95.00  . . . . 0.1575 . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 3.93 4.95 . . 162 3430 100.00 . . . . 0.1452 . . . . . . . . . . . 0.1823 
# 
_struct.entry_id                     9GAX 
_struct.title                        
;TEAD1 in complex with a reversible inhibitor N-[(1S)-2-hydroxy-1-(1-methyl-1H-pyrazol-3-yl)ethyl]-2-methyl-8-[4-(trifluoromethyl)phenyl]-2H,8H-pyrazolo[3,4-b]indole-5-carboxamide
;
_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        9GAX 
_struct_keywords.text            
;IRREVERSIBLE COVALENT INHIBITOR, MESOTHELIOMA TUMOR REGRESSION, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSCRIPTION-PROTEIN BINDING COMPLEX
;
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TEAD1_HUMAN 
_struct_ref.pdbx_db_accession          P28347 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFFL
VKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFIH
KLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
;
_struct_ref.pdbx_align_begin           208 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GAX A 1 ? 220 ? P28347 208 ? 426 ? 207 426 
2 1 9GAX B 1 ? 220 ? P28347 208 ? 426 ? 207 426 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GAX PRO A 2 ? UNP P28347 ? ? insertion 208 1 
2 9GAX PRO B 2 ? UNP P28347 ? ? insertion 208 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3820  ? 
1 MORE         -91   ? 
1 'SSA (A^2)'  20510 ? 
# 
_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 
# 
_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 ARG A 54  ? PHE A 60  ? ARG A 260 PHE A 266 5 ? 7  
HELX_P HELX_P2  AA2 GLY A 66  ? GLY A 74  ? GLY A 272 GLY A 280 1 ? 9  
HELX_P HELX_P3  AA3 PRO A 75  ? ASN A 77  ? PRO A 281 ASN A 283 5 ? 3  
HELX_P HELX_P4  AA4 CYS A 153 ? HIS A 165 ? CYS A 359 HIS A 371 1 ? 13 
HELX_P HELX_P5  AA5 GLU A 168 ? GLU A 177 ? GLU A 374 GLU A 383 1 ? 10 
HELX_P HELX_P6  AA6 ARG B 54  ? PHE B 60  ? ARG B 260 PHE B 266 5 ? 7  
HELX_P HELX_P7  AA7 GLY B 66  ? GLY B 74  ? GLY B 272 GLY B 280 1 ? 9  
HELX_P HELX_P8  AA8 PRO B 75  ? ASN B 77  ? PRO B 281 ASN B 283 5 ? 3  
HELX_P HELX_P9  AA9 CYS B 153 ? HIS B 165 ? CYS B 359 HIS B 371 1 ? 13 
HELX_P HELX_P10 AB1 GLU B 168 ? ASN B 178 ? GLU B 374 ASN B 384 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 74 A . ? GLY 280 A PRO 75 A ? PRO 281 A 1 -3.72 
2 GLY 74 B . ? GLY 280 B PRO 75 B ? PRO 281 B 1 -0.41 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 5   ? GLY A 6   ? ILE A 211 GLY A 212 
AA1 2 ARG A 11  ? GLN A 21  ? ARG A 217 GLN A 227 
AA1 3 ASN A 29  ? HIS A 35  ? ASN A 235 HIS A 241 
AA2 1 ILE A 5   ? GLY A 6   ? ILE A 211 GLY A 212 
AA2 2 ARG A 11  ? GLN A 21  ? ARG A 217 GLN A 227 
AA2 3 ALA A 98  ? SER A 108 ? ALA A 304 SER A 314 
AA2 4 ARG A 142 ? PRO A 151 ? ARG A 348 PRO A 357 
AA2 5 ARG A 137 ? GLU A 139 ? ARG A 343 GLU A 345 
AA3 1 SER A 50  ? ASP A 52  ? SER A 256 ASP A 258 
AA3 2 GLN A 211 ? VAL A 218 ? GLN A 417 VAL A 424 
AA3 3 PHE A 79  ? ALA A 86  ? PHE A 285 ALA A 292 
AA3 4 THR A 193 ? VAL A 203 ? THR A 399 VAL A 409 
AA3 5 PHE A 179 ? ASN A 187 ? PHE A 385 ASN A 393 
AA3 6 THR A 113 ? SER A 122 ? THR A 319 SER A 328 
AA3 7 LYS A 125 ? TYR A 135 ? LYS A 331 TYR A 341 
AA4 1 ILE B 5   ? THR B 7   ? ILE B 211 THR B 213 
AA4 2 LEU B 10  ? ASP B 24  ? LEU B 216 ASP B 230 
AA4 3 SER B 27  ? HIS B 35  ? SER B 233 HIS B 241 
AA5 1 ILE B 5   ? THR B 7   ? ILE B 211 THR B 213 
AA5 2 LEU B 10  ? ASP B 24  ? LEU B 216 ASP B 230 
AA5 3 PHE B 99  ? SER B 108 ? PHE B 305 SER B 314 
AA5 4 ARG B 142 ? PRO B 151 ? ARG B 348 PRO B 357 
AA5 5 ARG B 137 ? GLU B 139 ? ARG B 343 GLU B 345 
AA6 1 SER B 50  ? ASP B 52  ? SER B 256 ASP B 258 
AA6 2 GLN B 211 ? VAL B 218 ? GLN B 417 VAL B 424 
AA6 3 PHE B 79  ? ALA B 86  ? PHE B 285 ALA B 292 
AA6 4 THR B 193 ? VAL B 203 ? THR B 399 VAL B 409 
AA6 5 PHE B 179 ? ASN B 187 ? PHE B 385 ASN B 393 
AA6 6 THR B 113 ? SER B 122 ? THR B 319 SER B 328 
AA6 7 LYS B 125 ? TYR B 135 ? LYS B 331 TYR B 341 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 5   ? N ILE A 211 O LEU A 12  ? O LEU A 218 
AA1 2 3 N GLN A 21  ? N GLN A 227 O ASN A 29  ? O ASN A 235 
AA2 1 2 N ILE A 5   ? N ILE A 211 O LEU A 12  ? O LEU A 218 
AA2 2 3 N SER A 16  ? N SER A 222 O THR A 103 ? O THR A 309 
AA2 3 4 N VAL A 102 ? N VAL A 308 O SER A 150 ? O SER A 356 
AA2 4 5 O ARG A 142 ? O ARG A 348 N GLU A 139 ? N GLU A 345 
AA3 1 2 N VAL A 51  ? N VAL A 257 O ARG A 216 ? O ARG A 422 
AA3 2 3 O GLN A 211 ? O GLN A 417 N TRP A 85  ? N TRP A 291 
AA3 3 4 N ALA A 86  ? N ALA A 292 O GLU A 202 ? O GLU A 408 
AA3 4 5 O LEU A 195 ? O LEU A 401 N VAL A 185 ? N VAL A 391 
AA3 5 6 O VAL A 184 ? O VAL A 390 N SER A 117 ? N SER A 323 
AA3 6 7 N CYS A 116 ? N CYS A 322 O GLU A 132 ? O GLU A 338 
AA4 1 2 N ILE B 5   ? N ILE B 211 O LEU B 12  ? O LEU B 218 
AA4 2 3 N GLN B 21  ? N GLN B 227 O ASN B 29  ? O ASN B 235 
AA5 1 2 N ILE B 5   ? N ILE B 211 O LEU B 12  ? O LEU B 218 
AA5 2 3 N GLU B 20  ? N GLU B 226 O PHE B 99  ? O PHE B 305 
AA5 3 4 N SER B 108 ? N SER B 314 O PHE B 143 ? O PHE B 349 
AA5 4 5 O ARG B 142 ? O ARG B 348 N GLU B 139 ? N GLU B 345 
AA6 1 2 N VAL B 51  ? N VAL B 257 O VAL B 218 ? O VAL B 424 
AA6 2 3 O GLN B 211 ? O GLN B 417 N TRP B 85  ? N TRP B 291 
AA6 3 4 N ALA B 86  ? N ALA B 292 O GLU B 202 ? O GLU B 408 
AA6 4 5 O LEU B 194 ? O LEU B 400 N VAL B 185 ? N VAL B 391 
AA6 5 6 O THR B 180 ? O THR B 386 N CYS B 121 ? N CYS B 327 
AA6 6 7 N CYS B 116 ? N CYS B 322 O GLU B 132 ? O GLU B 338 
# 
_pdbx_entry_details.entry_id                   9GAX 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 213 ? ? -109.32 -169.46 
2 1 LYS A 269 ? ? 60.92   -141.84 
3 1 GLN A 397 ? ? 59.45   17.20   
4 1 LYS B 269 ? ? 61.52   -147.97 
5 1 ASP B 301 ? ? 52.64   73.62   
6 1 SER B 412 ? ? 51.28   -124.71 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     628 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   N 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         29.0744 
_pdbx_refine_tls.origin_y         47.8300 
_pdbx_refine_tls.origin_z         8.4282 
_pdbx_refine_tls.T[1][1]          0.1892 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0075 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0122 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2083 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0290 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1931 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6739 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2110 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.3104 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.4955 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2182 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.4704 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0163 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0110 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0231 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0272 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0073 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0297 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0342 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0187 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0000 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 ASP 300 ? A ASP 94  
2 1 Y 1 A ASP 301 ? A ASP 95  
3 1 Y 1 A ALA 302 ? A ALA 96  
4 1 Y 1 A ASP 426 ? A ASP 220 
5 1 Y 1 B ASP 426 ? B ASP 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 
A1IJL C1   C N S 1   
A1IJL C2   C N N 2   
A1IJL C3   C N N 3   
A1IJL N6   N Y N 4   
A1IJL C7   C Y N 5   
A1IJL C8   C Y N 6   
A1IJL C9   C Y N 7   
A1IJL C10  C Y N 8   
A1IJL C11  C Y N 9   
A1IJL C12  C N N 10  
A1IJL C13  C Y N 11  
A1IJL C14  C Y N 12  
A1IJL C15  C Y N 13  
A1IJL C16  C Y N 14  
A1IJL C19  C Y N 15  
A1IJL C20  C N N 16  
A1IJL C21  C Y N 17  
A1IJL C22  C Y N 18  
A1IJL C24  C N N 19  
A1IJL C17  C Y N 20  
A1IJL C18  C Y N 21  
A1IJL C23  C Y N 22  
A1IJL C4   C Y N 23  
A1IJL C5   C Y N 24  
A1IJL C6   C Y N 25  
A1IJL F1   F N N 26  
A1IJL F2   F N N 27  
A1IJL F3   F N N 28  
A1IJL N1   N N N 29  
A1IJL N2   N Y N 30  
A1IJL N3   N Y N 31  
A1IJL N4   N Y N 32  
A1IJL N5   N Y N 33  
A1IJL O1   O N N 34  
A1IJL O2   O N N 35  
A1IJL H1   H N N 36  
A1IJL H2   H N N 37  
A1IJL H3   H N N 38  
A1IJL H4   H N N 39  
A1IJL H5   H N N 40  
A1IJL H6   H N N 41  
A1IJL H7   H N N 42  
A1IJL H8   H N N 43  
A1IJL H9   H N N 44  
A1IJL H10  H N N 45  
A1IJL H11  H N N 46  
A1IJL H12  H N N 47  
A1IJL H13  H N N 48  
A1IJL H14  H N N 49  
A1IJL H15  H N N 50  
A1IJL H16  H N N 51  
A1IJL H17  H N N 52  
A1IJL H18  H N N 53  
A1IJL H19  H N N 54  
A1IJL H20  H N N 55  
A1IJL H21  H N N 56  
ALA   N    N N N 57  
ALA   CA   C N S 58  
ALA   C    C N N 59  
ALA   O    O N N 60  
ALA   CB   C N N 61  
ALA   OXT  O N N 62  
ALA   H    H N N 63  
ALA   H2   H N N 64  
ALA   HA   H N N 65  
ALA   HB1  H N N 66  
ALA   HB2  H N N 67  
ALA   HB3  H N N 68  
ALA   HXT  H N N 69  
ARG   N    N N N 70  
ARG   CA   C N S 71  
ARG   C    C N N 72  
ARG   O    O N N 73  
ARG   CB   C N N 74  
ARG   CG   C N N 75  
ARG   CD   C N N 76  
ARG   NE   N N N 77  
ARG   CZ   C N N 78  
ARG   NH1  N N N 79  
ARG   NH2  N N N 80  
ARG   OXT  O N N 81  
ARG   H    H N N 82  
ARG   H2   H N N 83  
ARG   HA   H N N 84  
ARG   HB2  H N N 85  
ARG   HB3  H N N 86  
ARG   HG2  H N N 87  
ARG   HG3  H N N 88  
ARG   HD2  H N N 89  
ARG   HD3  H N N 90  
ARG   HE   H N N 91  
ARG   HH11 H N N 92  
ARG   HH12 H N N 93  
ARG   HH21 H N N 94  
ARG   HH22 H N N 95  
ARG   HXT  H N N 96  
ASN   N    N N N 97  
ASN   CA   C N S 98  
ASN   C    C N N 99  
ASN   O    O N N 100 
ASN   CB   C N N 101 
ASN   CG   C N N 102 
ASN   OD1  O N N 103 
ASN   ND2  N N N 104 
ASN   OXT  O N N 105 
ASN   H    H N N 106 
ASN   H2   H N N 107 
ASN   HA   H N N 108 
ASN   HB2  H N N 109 
ASN   HB3  H N N 110 
ASN   HD21 H N N 111 
ASN   HD22 H N N 112 
ASN   HXT  H N N 113 
ASP   N    N N N 114 
ASP   CA   C N S 115 
ASP   C    C N N 116 
ASP   O    O N N 117 
ASP   CB   C N N 118 
ASP   CG   C N N 119 
ASP   OD1  O N N 120 
ASP   OD2  O N N 121 
ASP   OXT  O N N 122 
ASP   H    H N N 123 
ASP   H2   H N N 124 
ASP   HA   H N N 125 
ASP   HB2  H N N 126 
ASP   HB3  H N N 127 
ASP   HD2  H N N 128 
ASP   HXT  H N N 129 
CYS   N    N N N 130 
CYS   CA   C N R 131 
CYS   C    C N N 132 
CYS   O    O N N 133 
CYS   CB   C N N 134 
CYS   SG   S N N 135 
CYS   OXT  O N N 136 
CYS   H    H N N 137 
CYS   H2   H N N 138 
CYS   HA   H N N 139 
CYS   HB2  H N N 140 
CYS   HB3  H N N 141 
CYS   HG   H N N 142 
CYS   HXT  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
GOL   C1   C N N 193 
GOL   O1   O N N 194 
GOL   C2   C N N 195 
GOL   O2   O N N 196 
GOL   C3   C N N 197 
GOL   O3   O N N 198 
GOL   H11  H N N 199 
GOL   H12  H N N 200 
GOL   HO1  H N N 201 
GOL   H2   H N N 202 
GOL   HO2  H N N 203 
GOL   H31  H N N 204 
GOL   H32  H N N 205 
GOL   HO3  H N N 206 
HIS   N    N N N 207 
HIS   CA   C N S 208 
HIS   C    C N N 209 
HIS   O    O N N 210 
HIS   CB   C N N 211 
HIS   CG   C Y N 212 
HIS   ND1  N Y N 213 
HIS   CD2  C Y N 214 
HIS   CE1  C Y N 215 
HIS   NE2  N Y N 216 
HIS   OXT  O N N 217 
HIS   H    H N N 218 
HIS   H2   H N N 219 
HIS   HA   H N N 220 
HIS   HB2  H N N 221 
HIS   HB3  H N N 222 
HIS   HD1  H N N 223 
HIS   HD2  H N N 224 
HIS   HE1  H N N 225 
HIS   HE2  H N N 226 
HIS   HXT  H N N 227 
HOH   O    O N N 228 
HOH   H1   H N N 229 
HOH   H2   H N N 230 
ILE   N    N N N 231 
ILE   CA   C N S 232 
ILE   C    C N N 233 
ILE   O    O N N 234 
ILE   CB   C N S 235 
ILE   CG1  C N N 236 
ILE   CG2  C N N 237 
ILE   CD1  C N N 238 
ILE   OXT  O N N 239 
ILE   H    H N N 240 
ILE   H2   H N N 241 
ILE   HA   H N N 242 
ILE   HB   H N N 243 
ILE   HG12 H N N 244 
ILE   HG13 H N N 245 
ILE   HG21 H N N 246 
ILE   HG22 H N N 247 
ILE   HG23 H N N 248 
ILE   HD11 H N N 249 
ILE   HD12 H N N 250 
ILE   HD13 H N N 251 
ILE   HXT  H N N 252 
LEU   N    N N N 253 
LEU   CA   C N S 254 
LEU   C    C N N 255 
LEU   O    O N N 256 
LEU   CB   C N N 257 
LEU   CG   C N N 258 
LEU   CD1  C N N 259 
LEU   CD2  C N N 260 
LEU   OXT  O N N 261 
LEU   H    H N N 262 
LEU   H2   H N N 263 
LEU   HA   H N N 264 
LEU   HB2  H N N 265 
LEU   HB3  H N N 266 
LEU   HG   H N N 267 
LEU   HD11 H N N 268 
LEU   HD12 H N N 269 
LEU   HD13 H N N 270 
LEU   HD21 H N N 271 
LEU   HD22 H N N 272 
LEU   HD23 H N N 273 
LEU   HXT  H N N 274 
LYS   N    N N N 275 
LYS   CA   C N S 276 
LYS   C    C N N 277 
LYS   O    O N N 278 
LYS   CB   C N N 279 
LYS   CG   C N N 280 
LYS   CD   C N N 281 
LYS   CE   C N N 282 
LYS   NZ   N N N 283 
LYS   OXT  O N N 284 
LYS   H    H N N 285 
LYS   H2   H N N 286 
LYS   HA   H N N 287 
LYS   HB2  H N N 288 
LYS   HB3  H N N 289 
LYS   HG2  H N N 290 
LYS   HG3  H N N 291 
LYS   HD2  H N N 292 
LYS   HD3  H N N 293 
LYS   HE2  H N N 294 
LYS   HE3  H N N 295 
LYS   HZ1  H N N 296 
LYS   HZ2  H N N 297 
LYS   HZ3  H N N 298 
LYS   HXT  H N N 299 
MET   N    N N N 300 
MET   CA   C N S 301 
MET   C    C N N 302 
MET   O    O N N 303 
MET   CB   C N N 304 
MET   CG   C N N 305 
MET   SD   S N N 306 
MET   CE   C N N 307 
MET   OXT  O N N 308 
MET   H    H N N 309 
MET   H2   H N N 310 
MET   HA   H N N 311 
MET   HB2  H N N 312 
MET   HB3  H N N 313 
MET   HG2  H N N 314 
MET   HG3  H N N 315 
MET   HE1  H N N 316 
MET   HE2  H N N 317 
MET   HE3  H N N 318 
MET   HXT  H N N 319 
PHE   N    N N N 320 
PHE   CA   C N S 321 
PHE   C    C N N 322 
PHE   O    O N N 323 
PHE   CB   C N N 324 
PHE   CG   C Y N 325 
PHE   CD1  C Y N 326 
PHE   CD2  C Y N 327 
PHE   CE1  C Y N 328 
PHE   CE2  C Y N 329 
PHE   CZ   C Y N 330 
PHE   OXT  O N N 331 
PHE   H    H N N 332 
PHE   H2   H N N 333 
PHE   HA   H N N 334 
PHE   HB2  H N N 335 
PHE   HB3  H N N 336 
PHE   HD1  H N N 337 
PHE   HD2  H N N 338 
PHE   HE1  H N N 339 
PHE   HE2  H N N 340 
PHE   HZ   H N N 341 
PHE   HXT  H N N 342 
PRO   N    N N N 343 
PRO   CA   C N S 344 
PRO   C    C N N 345 
PRO   O    O N N 346 
PRO   CB   C N N 347 
PRO   CG   C N N 348 
PRO   CD   C N N 349 
PRO   OXT  O N N 350 
PRO   H    H N N 351 
PRO   HA   H N N 352 
PRO   HB2  H N N 353 
PRO   HB3  H N N 354 
PRO   HG2  H N N 355 
PRO   HG3  H N N 356 
PRO   HD2  H N N 357 
PRO   HD3  H N N 358 
PRO   HXT  H N N 359 
SER   N    N N N 360 
SER   CA   C N S 361 
SER   C    C N N 362 
SER   O    O N N 363 
SER   CB   C N N 364 
SER   OG   O N N 365 
SER   OXT  O N N 366 
SER   H    H N N 367 
SER   H2   H N N 368 
SER   HA   H N N 369 
SER   HB2  H N N 370 
SER   HB3  H N N 371 
SER   HG   H N N 372 
SER   HXT  H N N 373 
SO4   S    S N N 374 
SO4   O1   O N N 375 
SO4   O2   O N N 376 
SO4   O3   O N N 377 
SO4   O4   O N N 378 
THR   N    N N N 379 
THR   CA   C N S 380 
THR   C    C N N 381 
THR   O    O N N 382 
THR   CB   C N R 383 
THR   OG1  O N N 384 
THR   CG2  C N N 385 
THR   OXT  O N N 386 
THR   H    H N N 387 
THR   H2   H N N 388 
THR   HA   H N N 389 
THR   HB   H N N 390 
THR   HG1  H N N 391 
THR   HG21 H N N 392 
THR   HG22 H N N 393 
THR   HG23 H N N 394 
THR   HXT  H N N 395 
TRP   N    N N N 396 
TRP   CA   C N S 397 
TRP   C    C N N 398 
TRP   O    O N N 399 
TRP   CB   C N N 400 
TRP   CG   C Y N 401 
TRP   CD1  C Y N 402 
TRP   CD2  C Y N 403 
TRP   NE1  N Y N 404 
TRP   CE2  C Y N 405 
TRP   CE3  C Y N 406 
TRP   CZ2  C Y N 407 
TRP   CZ3  C Y N 408 
TRP   CH2  C Y N 409 
TRP   OXT  O N N 410 
TRP   H    H N N 411 
TRP   H2   H N N 412 
TRP   HA   H N N 413 
TRP   HB2  H N N 414 
TRP   HB3  H N N 415 
TRP   HD1  H N N 416 
TRP   HE1  H N N 417 
TRP   HE3  H N N 418 
TRP   HZ2  H N N 419 
TRP   HZ3  H N N 420 
TRP   HH2  H N N 421 
TRP   HXT  H N N 422 
TYR   N    N N N 423 
TYR   CA   C N S 424 
TYR   C    C N N 425 
TYR   O    O N N 426 
TYR   CB   C N N 427 
TYR   CG   C Y N 428 
TYR   CD1  C Y N 429 
TYR   CD2  C Y N 430 
TYR   CE1  C Y N 431 
TYR   CE2  C Y N 432 
TYR   CZ   C Y N 433 
TYR   OH   O N N 434 
TYR   OXT  O N N 435 
TYR   H    H N N 436 
TYR   H2   H N N 437 
TYR   HA   H N N 438 
TYR   HB2  H N N 439 
TYR   HB3  H N N 440 
TYR   HD1  H N N 441 
TYR   HD2  H N N 442 
TYR   HE1  H N N 443 
TYR   HE2  H N N 444 
TYR   HH   H N N 445 
TYR   HXT  H N N 446 
VAL   N    N N N 447 
VAL   CA   C N S 448 
VAL   C    C N N 449 
VAL   O    O N N 450 
VAL   CB   C N N 451 
VAL   CG1  C N N 452 
VAL   CG2  C N N 453 
VAL   OXT  O N N 454 
VAL   H    H N N 455 
VAL   H2   H N N 456 
VAL   HA   H N N 457 
VAL   HB   H N N 458 
VAL   HG11 H N N 459 
VAL   HG12 H N N 460 
VAL   HG13 H N N 461 
VAL   HG21 H N N 462 
VAL   HG22 H N N 463 
VAL   HG23 H N N 464 
VAL   HXT  H N N 465 
# 
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 
A1IJL F2  C24  sing N N 1   
A1IJL F3  C24  sing N N 2   
A1IJL C24 F1   sing N N 3   
A1IJL C24 C23  sing N N 4   
A1IJL C21 C23  doub Y N 5   
A1IJL C21 C18  sing Y N 6   
A1IJL C23 C22  sing Y N 7   
A1IJL C18 C17  doub Y N 8   
A1IJL C22 C19  doub Y N 9   
A1IJL C10 C7   doub Y N 10  
A1IJL C10 C13  sing Y N 11  
A1IJL C7  C5   sing Y N 12  
A1IJL C17 C19  sing Y N 13  
A1IJL C17 N4   sing N N 14  
A1IJL O1  C2   doub N N 15  
A1IJL C13 N4   sing Y N 16  
A1IJL C13 C11  doub Y N 17  
A1IJL N4  C15  sing Y N 18  
A1IJL C5  C2   sing N N 19  
A1IJL C5  C8   doub Y N 20  
A1IJL C2  N1   sing N N 21  
A1IJL C12 N3   sing N N 22  
A1IJL C3  O2   sing N N 23  
A1IJL C3  C1   sing N N 24  
A1IJL N3  N2   sing Y N 25  
A1IJL N3  C9   sing Y N 26  
A1IJL N2  C4   doub Y N 27  
A1IJL C11 C8   sing Y N 28  
A1IJL C11 C14  sing Y N 29  
A1IJL C15 C14  sing Y N 30  
A1IJL C15 N5   doub Y N 31  
A1IJL N1  C1   sing N N 32  
A1IJL C9  C6   doub Y N 33  
A1IJL C4  C1   sing N N 34  
A1IJL C4  C6   sing Y N 35  
A1IJL C14 C16  doub Y N 36  
A1IJL N5  N6   sing Y N 37  
A1IJL N6  C16  sing Y N 38  
A1IJL N6  C20  sing N N 39  
A1IJL C1  H1   sing N N 40  
A1IJL C3  H2   sing N N 41  
A1IJL C3  H3   sing N N 42  
A1IJL C7  H4   sing N N 43  
A1IJL C8  H5   sing N N 44  
A1IJL C9  H6   sing N N 45  
A1IJL C10 H7   sing N N 46  
A1IJL C12 H8   sing N N 47  
A1IJL C12 H9   sing N N 48  
A1IJL C12 H10  sing N N 49  
A1IJL C16 H11  sing N N 50  
A1IJL C19 H12  sing N N 51  
A1IJL C20 H13  sing N N 52  
A1IJL C20 H14  sing N N 53  
A1IJL C20 H15  sing N N 54  
A1IJL C21 H16  sing N N 55  
A1IJL C22 H17  sing N N 56  
A1IJL C18 H18  sing N N 57  
A1IJL C6  H19  sing N N 58  
A1IJL N1  H20  sing N N 59  
A1IJL O2  H21  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
GOL   C1  O1   sing N N 189 
GOL   C1  C2   sing N N 190 
GOL   C1  H11  sing N N 191 
GOL   C1  H12  sing N N 192 
GOL   O1  HO1  sing N N 193 
GOL   C2  O2   sing N N 194 
GOL   C2  C3   sing N N 195 
GOL   C2  H2   sing N N 196 
GOL   O2  HO2  sing N N 197 
GOL   C3  O3   sing N N 198 
GOL   C3  H31  sing N N 199 
GOL   C3  H32  sing N N 200 
GOL   O3  HO3  sing N N 201 
HIS   N   CA   sing N N 202 
HIS   N   H    sing N N 203 
HIS   N   H2   sing N N 204 
HIS   CA  C    sing N N 205 
HIS   CA  CB   sing N N 206 
HIS   CA  HA   sing N N 207 
HIS   C   O    doub N N 208 
HIS   C   OXT  sing N N 209 
HIS   CB  CG   sing N N 210 
HIS   CB  HB2  sing N N 211 
HIS   CB  HB3  sing N N 212 
HIS   CG  ND1  sing Y N 213 
HIS   CG  CD2  doub Y N 214 
HIS   ND1 CE1  doub Y N 215 
HIS   ND1 HD1  sing N N 216 
HIS   CD2 NE2  sing Y N 217 
HIS   CD2 HD2  sing N N 218 
HIS   CE1 NE2  sing Y N 219 
HIS   CE1 HE1  sing N N 220 
HIS   NE2 HE2  sing N N 221 
HIS   OXT HXT  sing N N 222 
HOH   O   H1   sing N N 223 
HOH   O   H2   sing N N 224 
ILE   N   CA   sing N N 225 
ILE   N   H    sing N N 226 
ILE   N   H2   sing N N 227 
ILE   CA  C    sing N N 228 
ILE   CA  CB   sing N N 229 
ILE   CA  HA   sing N N 230 
ILE   C   O    doub N N 231 
ILE   C   OXT  sing N N 232 
ILE   CB  CG1  sing N N 233 
ILE   CB  CG2  sing N N 234 
ILE   CB  HB   sing N N 235 
ILE   CG1 CD1  sing N N 236 
ILE   CG1 HG12 sing N N 237 
ILE   CG1 HG13 sing N N 238 
ILE   CG2 HG21 sing N N 239 
ILE   CG2 HG22 sing N N 240 
ILE   CG2 HG23 sing N N 241 
ILE   CD1 HD11 sing N N 242 
ILE   CD1 HD12 sing N N 243 
ILE   CD1 HD13 sing N N 244 
ILE   OXT HXT  sing N N 245 
LEU   N   CA   sing N N 246 
LEU   N   H    sing N N 247 
LEU   N   H2   sing N N 248 
LEU   CA  C    sing N N 249 
LEU   CA  CB   sing N N 250 
LEU   CA  HA   sing N N 251 
LEU   C   O    doub N N 252 
LEU   C   OXT  sing N N 253 
LEU   CB  CG   sing N N 254 
LEU   CB  HB2  sing N N 255 
LEU   CB  HB3  sing N N 256 
LEU   CG  CD1  sing N N 257 
LEU   CG  CD2  sing N N 258 
LEU   CG  HG   sing N N 259 
LEU   CD1 HD11 sing N N 260 
LEU   CD1 HD12 sing N N 261 
LEU   CD1 HD13 sing N N 262 
LEU   CD2 HD21 sing N N 263 
LEU   CD2 HD22 sing N N 264 
LEU   CD2 HD23 sing N N 265 
LEU   OXT HXT  sing N N 266 
LYS   N   CA   sing N N 267 
LYS   N   H    sing N N 268 
LYS   N   H2   sing N N 269 
LYS   CA  C    sing N N 270 
LYS   CA  CB   sing N N 271 
LYS   CA  HA   sing N N 272 
LYS   C   O    doub N N 273 
LYS   C   OXT  sing N N 274 
LYS   CB  CG   sing N N 275 
LYS   CB  HB2  sing N N 276 
LYS   CB  HB3  sing N N 277 
LYS   CG  CD   sing N N 278 
LYS   CG  HG2  sing N N 279 
LYS   CG  HG3  sing N N 280 
LYS   CD  CE   sing N N 281 
LYS   CD  HD2  sing N N 282 
LYS   CD  HD3  sing N N 283 
LYS   CE  NZ   sing N N 284 
LYS   CE  HE2  sing N N 285 
LYS   CE  HE3  sing N N 286 
LYS   NZ  HZ1  sing N N 287 
LYS   NZ  HZ2  sing N N 288 
LYS   NZ  HZ3  sing N N 289 
LYS   OXT HXT  sing N N 290 
MET   N   CA   sing N N 291 
MET   N   H    sing N N 292 
MET   N   H2   sing N N 293 
MET   CA  C    sing N N 294 
MET   CA  CB   sing N N 295 
MET   CA  HA   sing N N 296 
MET   C   O    doub N N 297 
MET   C   OXT  sing N N 298 
MET   CB  CG   sing N N 299 
MET   CB  HB2  sing N N 300 
MET   CB  HB3  sing N N 301 
MET   CG  SD   sing N N 302 
MET   CG  HG2  sing N N 303 
MET   CG  HG3  sing N N 304 
MET   SD  CE   sing N N 305 
MET   CE  HE1  sing N N 306 
MET   CE  HE2  sing N N 307 
MET   CE  HE3  sing N N 308 
MET   OXT HXT  sing N N 309 
PHE   N   CA   sing N N 310 
PHE   N   H    sing N N 311 
PHE   N   H2   sing N N 312 
PHE   CA  C    sing N N 313 
PHE   CA  CB   sing N N 314 
PHE   CA  HA   sing N N 315 
PHE   C   O    doub N N 316 
PHE   C   OXT  sing N N 317 
PHE   CB  CG   sing N N 318 
PHE   CB  HB2  sing N N 319 
PHE   CB  HB3  sing N N 320 
PHE   CG  CD1  doub Y N 321 
PHE   CG  CD2  sing Y N 322 
PHE   CD1 CE1  sing Y N 323 
PHE   CD1 HD1  sing N N 324 
PHE   CD2 CE2  doub Y N 325 
PHE   CD2 HD2  sing N N 326 
PHE   CE1 CZ   doub Y N 327 
PHE   CE1 HE1  sing N N 328 
PHE   CE2 CZ   sing Y N 329 
PHE   CE2 HE2  sing N N 330 
PHE   CZ  HZ   sing N N 331 
PHE   OXT HXT  sing N N 332 
PRO   N   CA   sing N N 333 
PRO   N   CD   sing N N 334 
PRO   N   H    sing N N 335 
PRO   CA  C    sing N N 336 
PRO   CA  CB   sing N N 337 
PRO   CA  HA   sing N N 338 
PRO   C   O    doub N N 339 
PRO   C   OXT  sing N N 340 
PRO   CB  CG   sing N N 341 
PRO   CB  HB2  sing N N 342 
PRO   CB  HB3  sing N N 343 
PRO   CG  CD   sing N N 344 
PRO   CG  HG2  sing N N 345 
PRO   CG  HG3  sing N N 346 
PRO   CD  HD2  sing N N 347 
PRO   CD  HD3  sing N N 348 
PRO   OXT HXT  sing N N 349 
SER   N   CA   sing N N 350 
SER   N   H    sing N N 351 
SER   N   H2   sing N N 352 
SER   CA  C    sing N N 353 
SER   CA  CB   sing N N 354 
SER   CA  HA   sing N N 355 
SER   C   O    doub N N 356 
SER   C   OXT  sing N N 357 
SER   CB  OG   sing N N 358 
SER   CB  HB2  sing N N 359 
SER   CB  HB3  sing N N 360 
SER   OG  HG   sing N N 361 
SER   OXT HXT  sing N N 362 
SO4   S   O1   doub N N 363 
SO4   S   O2   doub N N 364 
SO4   S   O3   sing N N 365 
SO4   S   O4   sing N N 366 
THR   N   CA   sing N N 367 
THR   N   H    sing N N 368 
THR   N   H2   sing N N 369 
THR   CA  C    sing N N 370 
THR   CA  CB   sing N N 371 
THR   CA  HA   sing N N 372 
THR   C   O    doub N N 373 
THR   C   OXT  sing N N 374 
THR   CB  OG1  sing N N 375 
THR   CB  CG2  sing N N 376 
THR   CB  HB   sing N N 377 
THR   OG1 HG1  sing N N 378 
THR   CG2 HG21 sing N N 379 
THR   CG2 HG22 sing N N 380 
THR   CG2 HG23 sing N N 381 
THR   OXT HXT  sing N N 382 
TRP   N   CA   sing N N 383 
TRP   N   H    sing N N 384 
TRP   N   H2   sing N N 385 
TRP   CA  C    sing N N 386 
TRP   CA  CB   sing N N 387 
TRP   CA  HA   sing N N 388 
TRP   C   O    doub N N 389 
TRP   C   OXT  sing N N 390 
TRP   CB  CG   sing N N 391 
TRP   CB  HB2  sing N N 392 
TRP   CB  HB3  sing N N 393 
TRP   CG  CD1  doub Y N 394 
TRP   CG  CD2  sing Y N 395 
TRP   CD1 NE1  sing Y N 396 
TRP   CD1 HD1  sing N N 397 
TRP   CD2 CE2  doub Y N 398 
TRP   CD2 CE3  sing Y N 399 
TRP   NE1 CE2  sing Y N 400 
TRP   NE1 HE1  sing N N 401 
TRP   CE2 CZ2  sing Y N 402 
TRP   CE3 CZ3  doub Y N 403 
TRP   CE3 HE3  sing N N 404 
TRP   CZ2 CH2  doub Y N 405 
TRP   CZ2 HZ2  sing N N 406 
TRP   CZ3 CH2  sing Y N 407 
TRP   CZ3 HZ3  sing N N 408 
TRP   CH2 HH2  sing N N 409 
TRP   OXT HXT  sing N N 410 
TYR   N   CA   sing N N 411 
TYR   N   H    sing N N 412 
TYR   N   H2   sing N N 413 
TYR   CA  C    sing N N 414 
TYR   CA  CB   sing N N 415 
TYR   CA  HA   sing N N 416 
TYR   C   O    doub N N 417 
TYR   C   OXT  sing N N 418 
TYR   CB  CG   sing N N 419 
TYR   CB  HB2  sing N N 420 
TYR   CB  HB3  sing N N 421 
TYR   CG  CD1  doub Y N 422 
TYR   CG  CD2  sing Y N 423 
TYR   CD1 CE1  sing Y N 424 
TYR   CD1 HD1  sing N N 425 
TYR   CD2 CE2  doub Y N 426 
TYR   CD2 HD2  sing N N 427 
TYR   CE1 CZ   doub Y N 428 
TYR   CE1 HE1  sing N N 429 
TYR   CE2 CZ   sing Y N 430 
TYR   CE2 HE2  sing N N 431 
TYR   CZ  OH   sing N N 432 
TYR   OH  HH   sing N N 433 
TYR   OXT HXT  sing N N 434 
VAL   N   CA   sing N N 435 
VAL   N   H    sing N N 436 
VAL   N   H2   sing N N 437 
VAL   CA  C    sing N N 438 
VAL   CA  CB   sing N N 439 
VAL   CA  HA   sing N N 440 
VAL   C   O    doub N N 441 
VAL   C   OXT  sing N N 442 
VAL   CB  CG1  sing N N 443 
VAL   CB  CG2  sing N N 444 
VAL   CB  HB   sing N N 445 
VAL   CG1 HG11 sing N N 446 
VAL   CG1 HG12 sing N N 447 
VAL   CG1 HG13 sing N N 448 
VAL   CG2 HG21 sing N N 449 
VAL   CG2 HG22 sing N N 450 
VAL   CG2 HG23 sing N N 451 
VAL   OXT HXT  sing N N 452 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in-house structure' 
# 
_atom_sites.entry_id                    9GAX 
_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]   0.009260 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009260 
_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]   0.007564 
_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 
C 
F 
N 
O 
S 
# 
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   . GLY   A 1 1   ? 21.769 57.497 5.001   1.00 37.88  ? 207 GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 1   ? 20.954 56.939 6.061   1.00 33.01  ? 207 GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 1   ? 21.646 55.806 6.786   1.00 41.18  ? 207 GLY   A C   1 
ATOM   4    O O   . GLY   A 1 1   ? 22.866 55.643 6.666   1.00 36.45  ? 207 GLY   A O   1 
ATOM   5    N N   . PRO   A 1 2   ? 20.874 55.011 7.525   1.00 34.31  ? 208 PRO   A N   1 
ATOM   6    C CA  . PRO   A 1 2   ? 21.481 53.953 8.336   1.00 34.90  ? 208 PRO   A CA  1 
ATOM   7    C C   . PRO   A 1 2   ? 22.196 52.930 7.466   1.00 38.00  ? 208 PRO   A C   1 
ATOM   8    O O   . PRO   A 1 2   ? 21.788 52.639 6.340   1.00 32.69  ? 208 PRO   A O   1 
ATOM   9    C CB  . PRO   A 1 2   ? 20.291 53.345 9.089   1.00 41.28  ? 208 PRO   A CB  1 
ATOM   10   C CG  . PRO   A 1 2   ? 19.095 53.764 8.347   1.00 44.05  ? 208 PRO   A CG  1 
ATOM   11   C CD  . PRO   A 1 2   ? 19.415 55.078 7.700   1.00 43.44  ? 208 PRO   A CD  1 
ATOM   12   N N   . ARG   A 1 3   ? 23.311 52.433 7.988   1.00 34.57  ? 209 ARG   A N   1 
ATOM   13   C CA  . ARG   A 1 3   ? 24.139 51.486 7.257   1.00 34.01  ? 209 ARG   A CA  1 
ATOM   14   C C   . ARG   A 1 3   ? 23.526 50.094 7.245   1.00 31.64  ? 209 ARG   A C   1 
ATOM   15   O O   . ARG   A 1 3   ? 23.602 49.388 6.242   1.00 31.20  ? 209 ARG   A O   1 
ATOM   16   C CB  . ARG   A 1 3   ? 25.524 51.418 7.895   1.00 29.74  ? 209 ARG   A CB  1 
ATOM   17   C CG  . ARG   A 1 3   ? 26.454 50.514 7.167   1.00 35.04  ? 209 ARG   A CG  1 
ATOM   18   C CD  . ARG   A 1 3   ? 27.676 50.282 7.967   1.00 33.00  ? 209 ARG   A CD  1 
ATOM   19   N NE  . ARG   A 1 3   ? 28.471 49.231 7.354   1.00 32.72  ? 209 ARG   A NE  1 
ATOM   20   C CZ  . ARG   A 1 3   ? 28.823 48.120 7.973   1.00 37.66  ? 209 ARG   A CZ  1 
ATOM   21   N NH1 . ARG   A 1 3   ? 28.479 47.895 9.232   1.00 37.49  ? 209 ARG   A NH1 1 
ATOM   22   N NH2 . ARG   A 1 3   ? 29.542 47.217 7.317   1.00 46.63  ? 209 ARG   A NH2 1 
ATOM   23   N N   . SER   A 1 4   ? 22.959 49.666 8.360   1.00 31.37  ? 210 SER   A N   1 
ATOM   24   C CA  . SER   A 1 4   ? 22.569 48.282 8.525   1.00 31.82  ? 210 SER   A CA  1 
ATOM   25   C C   . SER   A 1 4   ? 21.127 48.196 9.021   1.00 33.54  ? 210 SER   A C   1 
ATOM   26   O O   . SER   A 1 4   ? 20.510 49.201 9.387   1.00 32.53  ? 210 SER   A O   1 
ATOM   27   C CB  . SER   A 1 4   ? 23.545 47.571 9.469   1.00 28.69  ? 210 SER   A CB  1 
ATOM   28   O OG  . SER   A 1 4   ? 23.405 48.047 10.798  1.00 42.48  ? 210 SER   A OG  1 
ATOM   29   N N   . ILE   A 1 5   ? 20.585 46.976 9.003   1.00 31.50  ? 211 ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 5   ? 19.210 46.693 9.411   1.00 26.48  ? 211 ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 5   ? 19.248 45.588 10.460  1.00 32.08  ? 211 ILE   A C   1 
ATOM   32   O O   . ILE   A 1 5   ? 19.757 44.491 10.186  1.00 30.51  ? 211 ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 5   ? 18.344 46.248 8.216   1.00 30.32  ? 211 ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 5   ? 18.395 47.261 7.073   1.00 26.35  ? 211 ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 5   ? 16.919 45.933 8.645   1.00 28.09  ? 211 ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 5   ? 17.765 46.739 5.828   1.00 29.10  ? 211 ILE   A CD1 1 
ATOM   37   N N   . GLY   A 1 6   ? 18.690 45.850 11.642  1.00 30.15  ? 212 GLY   A N   1 
ATOM   38   C CA  . GLY   A 1 6   ? 18.454 44.769 12.584  1.00 29.95  ? 212 GLY   A CA  1 
ATOM   39   C C   . GLY   A 1 6   ? 18.543 45.236 14.031  1.00 32.76  ? 212 GLY   A C   1 
ATOM   40   O O   . GLY   A 1 6   ? 18.327 46.394 14.338  1.00 40.75  ? 212 GLY   A O   1 
ATOM   41   N N   . THR   A 1 7   ? 18.858 44.297 14.910  1.00 34.29  ? 213 THR   A N   1 
ATOM   42   C CA  . THR   A 1 7   ? 18.881 44.521 16.350  1.00 39.13  ? 213 THR   A CA  1 
ATOM   43   C C   . THR   A 1 7   ? 20.308 44.520 16.889  1.00 38.88  ? 213 THR   A C   1 
ATOM   44   O O   . THR   A 1 7   ? 21.291 44.482 16.147  1.00 38.58  ? 213 THR   A O   1 
ATOM   45   C CB  . THR   A 1 7   ? 18.062 43.451 17.074  1.00 39.10  ? 213 THR   A CB  1 
ATOM   46   O OG1 . THR   A 1 7   ? 18.813 42.226 17.095  1.00 38.88  ? 213 THR   A OG1 1 
ATOM   47   C CG2 . THR   A 1 7   ? 16.730 43.230 16.400  1.00 41.37  ? 213 THR   A CG2 1 
ATOM   48   N N   . THR   A 1 8   ? 20.419 44.498 18.214  1.00 40.18  ? 214 THR   A N   1 
ATOM   49   C CA  . THR   A 1 8   ? 21.741 44.435 18.815  1.00 42.81  ? 214 THR   A CA  1 
ATOM   50   C C   . THR   A 1 8   ? 22.352 43.042 18.678  1.00 40.35  ? 214 THR   A C   1 
ATOM   51   O O   . THR   A 1 8   ? 23.580 42.912 18.658  1.00 49.74  ? 214 THR   A O   1 
ATOM   52   C CB  . THR   A 1 8   ? 21.665 44.875 20.282  1.00 47.83  ? 214 THR   A CB  1 
ATOM   53   O OG1 . THR   A 1 8   ? 22.965 44.793 20.866  1.00 59.37  ? 214 THR   A OG1 1 
ATOM   54   C CG2 . THR   A 1 8   ? 20.711 43.978 21.062  1.00 49.31  ? 214 THR   A CG2 1 
ATOM   55   N N   . LYS   A 1 9   ? 21.519 41.995 18.560  1.00 31.88  ? 215 LYS   A N   1 
ATOM   56   C CA  . LYS   A 1 9   ? 22.019 40.631 18.428  1.00 33.72  ? 215 LYS   A CA  1 
ATOM   57   C C   . LYS   A 1 9   ? 22.428 40.272 16.994  1.00 39.08  ? 215 LYS   A C   1 
ATOM   58   O O   . LYS   A 1 9   ? 23.310 39.425 16.812  1.00 32.49  ? 215 LYS   A O   1 
ATOM   59   C CB  . LYS   A 1 9   ? 20.964 39.624 18.894  1.00 30.71  ? 215 LYS   A CB  1 
ATOM   60   C CG  . LYS   A 1 9   ? 20.733 39.586 20.392  1.00 49.53  ? 215 LYS   A CG  1 
ATOM   61   C CD  . LYS   A 1 9   ? 19.708 38.512 20.769  1.00 47.59  ? 215 LYS   A CD  1 
ATOM   62   C CE  . LYS   A 1 9   ? 18.960 38.879 22.056  1.00 58.47  ? 215 LYS   A CE  1 
ATOM   63   N NZ  . LYS   A 1 9   ? 18.600 37.673 22.849  1.00 64.73  ? 215 LYS   A NZ  1 
ATOM   64   N N   . LEU   A 1 10  ? 21.793 40.856 15.975  1.00 31.10  ? 216 LEU   A N   1 
ATOM   65   C CA  . LEU   A 1 10  ? 22.109 40.515 14.584  1.00 34.43  ? 216 LEU   A CA  1 
ATOM   66   C C   . LEU   A 1 10  ? 21.730 41.654 13.654  1.00 31.50  ? 216 LEU   A C   1 
ATOM   67   O O   . LEU   A 1 10  ? 20.609 42.160 13.737  1.00 31.68  ? 216 LEU   A O   1 
ATOM   68   C CB  . LEU   A 1 10  ? 21.375 39.244 14.134  1.00 30.40  ? 216 LEU   A CB  1 
ATOM   69   C CG  . LEU   A 1 10  ? 21.889 38.718 12.784  1.00 29.59  ? 216 LEU   A CG  1 
ATOM   70   C CD1 . LEU   A 1 10  ? 23.116 37.816 12.984  1.00 30.27  ? 216 LEU   A CD1 1 
ATOM   71   C CD2 . LEU   A 1 10  ? 20.830 37.967 12.082  1.00 32.92  ? 216 LEU   A CD2 1 
ATOM   72   N N   . ARG   A 1 11  ? 22.630 41.999 12.720  1.00 26.12  ? 217 ARG   A N   1 
ATOM   73   C CA  . ARG   A 1 11  ? 22.387 43.044 11.734  1.00 32.13  ? 217 ARG   A CA  1 
ATOM   74   C C   . ARG   A 1 11  ? 22.733 42.569 10.325  1.00 31.54  ? 217 ARG   A C   1 
ATOM   75   O O   . ARG   A 1 11  ? 23.790 41.971 10.095  1.00 26.91  ? 217 ARG   A O   1 
ATOM   76   C CB  . ARG   A 1 11  ? 23.226 44.285 12.031  1.00 32.83  ? 217 ARG   A CB  1 
ATOM   77   C CG  . ARG   A 1 11  ? 22.833 45.045 13.274  1.00 45.68  ? 217 ARG   A CG  1 
ATOM   78   C CD  . ARG   A 1 11  ? 23.989 45.948 13.672  1.00 53.85  ? 217 ARG   A CD  1 
ATOM   79   N NE  . ARG   A 1 11  ? 24.151 46.065 15.118  1.00 69.35  ? 217 ARG   A NE  1 
ATOM   80   C CZ  . ARG   A 1 11  ? 24.891 45.255 15.869  1.00 80.01  ? 217 ARG   A CZ  1 
ATOM   81   N NH1 . ARG   A 1 11  ? 25.520 44.205 15.352  1.00 68.77  ? 217 ARG   A NH1 1 
ATOM   82   N NH2 . ARG   A 1 11  ? 25.000 45.502 17.174  1.00 76.75  ? 217 ARG   A NH2 1 
ATOM   83   N N   . LEU   A 1 12  ? 21.861 42.884 9.378   1.00 28.46  ? 218 LEU   A N   1 
ATOM   84   C CA  . LEU   A 1 12  ? 22.158 42.742 7.957   1.00 20.73  ? 218 LEU   A CA  1 
ATOM   85   C C   . LEU   A 1 12  ? 22.986 43.956 7.553   1.00 28.81  ? 218 LEU   A C   1 
ATOM   86   O O   . LEU   A 1 12  ? 22.496 45.085 7.618   1.00 26.11  ? 218 LEU   A O   1 
ATOM   87   C CB  . LEU   A 1 12  ? 20.859 42.680 7.155   1.00 24.64  ? 218 LEU   A CB  1 
ATOM   88   C CG  . LEU   A 1 12  ? 21.023 42.659 5.636   1.00 24.67  ? 218 LEU   A CG  1 
ATOM   89   C CD1 . LEU   A 1 12  ? 21.730 41.360 5.176   1.00 25.93  ? 218 LEU   A CD1 1 
ATOM   90   C CD2 . LEU   A 1 12  ? 19.673 42.860 4.918   1.00 28.90  ? 218 LEU   A CD2 1 
ATOM   91   N N   . VAL   A 1 13  ? 24.249 43.760 7.178   1.00 22.59  ? 219 VAL   A N   1 
ATOM   92   C CA  . VAL   A 1 13  ? 25.112 44.901 6.882   1.00 25.94  ? 219 VAL   A CA  1 
ATOM   93   C C   . VAL   A 1 13  ? 25.390 45.049 5.396   1.00 30.62  ? 219 VAL   A C   1 
ATOM   94   O O   . VAL   A 1 13  ? 25.837 46.122 4.965   1.00 33.81  ? 219 VAL   A O   1 
ATOM   95   C CB  . VAL   A 1 13  ? 26.438 44.832 7.658   1.00 28.81  ? 219 VAL   A CB  1 
ATOM   96   C CG1 . VAL   A 1 13  ? 26.170 44.783 9.162   1.00 27.26  ? 219 VAL   A CG1 1 
ATOM   97   C CG2 . VAL   A 1 13  ? 27.241 43.614 7.219   1.00 28.11  ? 219 VAL   A CG2 1 
ATOM   98   N N   . GLU   A 1 14  ? 25.138 44.030 4.605   1.00 27.03  ? 220 GLU   A N   1 
ATOM   99   C CA  . GLU   A 1 14  ? 25.464 44.086 3.197   1.00 29.94  ? 220 GLU   A CA  1 
ATOM   100  C C   . GLU   A 1 14  ? 24.468 43.198 2.470   1.00 28.93  ? 220 GLU   A C   1 
ATOM   101  O O   . GLU   A 1 14  ? 24.080 42.139 2.974   1.00 29.76  ? 220 GLU   A O   1 
ATOM   102  C CB  . GLU   A 1 14  ? 26.900 43.608 2.952   1.00 31.01  ? 220 GLU   A CB  1 
ATOM   103  C CG  . GLU   A 1 14  ? 27.522 44.149 1.685   1.00 50.62  ? 220 GLU   A CG  1 
ATOM   104  C CD  . GLU   A 1 14  ? 28.952 43.665 1.472   1.00 66.40  ? 220 GLU   A CD  1 
ATOM   105  O OE1 . GLU   A 1 14  ? 29.394 42.763 2.218   1.00 67.99  ? 220 GLU   A OE1 1 
ATOM   106  O OE2 . GLU   A 1 14  ? 29.615 44.151 0.524   1.00 67.14  ? 220 GLU   A OE2 1 
ATOM   107  N N   . PHE   A 1 15  ? 24.022 43.655 1.309   1.00 28.37  ? 221 PHE   A N   1 
ATOM   108  C CA  . PHE   A 1 15  ? 23.088 42.850 0.543   1.00 26.64  ? 221 PHE   A CA  1 
ATOM   109  C C   . PHE   A 1 15  ? 23.036 43.417 -0.857  1.00 37.25  ? 221 PHE   A C   1 
ATOM   110  O O   . PHE   A 1 15  ? 23.047 44.643 -1.034  1.00 31.86  ? 221 PHE   A O   1 
ATOM   111  C CB  . PHE   A 1 15  ? 21.672 42.857 1.123   1.00 30.71  ? 221 PHE   A CB  1 
ATOM   112  C CG  . PHE   A 1 15  ? 20.625 42.458 0.115   1.00 33.59  ? 221 PHE   A CG  1 
ATOM   113  C CD1 . PHE   A 1 15  ? 20.572 41.168 -0.383  1.00 31.65  ? 221 PHE   A CD1 1 
ATOM   114  C CD2 . PHE   A 1 15  ? 19.795 43.419 -0.455  1.00 34.23  ? 221 PHE   A CD2 1 
ATOM   115  C CE1 . PHE   A 1 15  ? 19.611 40.796 -1.342  1.00 33.11  ? 221 PHE   A CE1 1 
ATOM   116  C CE2 . PHE   A 1 15  ? 18.845 43.063 -1.423  1.00 32.67  ? 221 PHE   A CE2 1 
ATOM   117  C CZ  . PHE   A 1 15  ? 18.772 41.736 -1.871  1.00 30.67  ? 221 PHE   A CZ  1 
ATOM   118  N N   . SER   A 1 16  ? 22.969 42.519 -1.836  1.00 29.86  ? 222 SER   A N   1 
ATOM   119  C CA  . SER   A 1 16  ? 22.671 42.929 -3.190  1.00 26.75  ? 222 SER   A CA  1 
ATOM   120  C C   . SER   A 1 16  ? 22.219 41.713 -4.001  1.00 29.34  ? 222 SER   A C   1 
ATOM   121  O O   . SER   A 1 16  ? 22.564 40.562 -3.701  1.00 26.27  ? 222 SER   A O   1 
ATOM   122  C CB  . SER   A 1 16  ? 23.878 43.644 -3.816  1.00 31.93  ? 222 SER   A CB  1 
ATOM   123  O OG  . SER   A 1 16  ? 24.822 42.722 -4.310  1.00 36.75  ? 222 SER   A OG  1 
ATOM   124  N N   . ALA   A 1 17  ? 21.393 41.987 -4.991  1.00 21.71  ? 223 ALA   A N   1 
ATOM   125  C CA  . ALA   A 1 17  ? 20.997 41.009 -5.991  1.00 26.29  ? 223 ALA   A CA  1 
ATOM   126  C C   . ALA   A 1 17  ? 21.448 41.607 -7.306  1.00 27.54  ? 223 ALA   A C   1 
ATOM   127  O O   . ALA   A 1 17  ? 21.206 42.793 -7.556  1.00 27.51  ? 223 ALA   A O   1 
ATOM   128  C CB  . ALA   A 1 17  ? 19.485 40.760 -5.979  1.00 21.97  ? 223 ALA   A CB  1 
ATOM   129  N N   . PHE   A 1 18  ? 22.158 40.821 -8.112  1.00 22.71  ? 224 PHE   A N   1 
ATOM   130  C CA  . PHE   A 1 18  ? 22.944 41.421 -9.172  1.00 26.21  ? 224 PHE   A CA  1 
ATOM   131  C C   . PHE   A 1 18  ? 23.011 40.512 -10.392 1.00 26.98  ? 224 PHE   A C   1 
ATOM   132  O O   . PHE   A 1 18  ? 22.650 39.339 -10.351 1.00 26.53  ? 224 PHE   A O   1 
ATOM   133  C CB  . PHE   A 1 18  ? 24.354 41.745 -8.657  1.00 26.21  ? 224 PHE   A CB  1 
ATOM   134  C CG  . PHE   A 1 18  ? 25.090 40.549 -8.130  1.00 25.37  ? 224 PHE   A CG  1 
ATOM   135  C CD1 . PHE   A 1 18  ? 25.794 39.712 -8.982  1.00 32.47  ? 224 PHE   A CD1 1 
ATOM   136  C CD2 . PHE   A 1 18  ? 25.078 40.265 -6.772  1.00 29.74  ? 224 PHE   A CD2 1 
ATOM   137  C CE1 . PHE   A 1 18  ? 26.475 38.602 -8.487  1.00 34.84  ? 224 PHE   A CE1 1 
ATOM   138  C CE2 . PHE   A 1 18  ? 25.752 39.163 -6.270  1.00 29.31  ? 224 PHE   A CE2 1 
ATOM   139  C CZ  . PHE   A 1 18  ? 26.455 38.335 -7.129  1.00 32.67  ? 224 PHE   A CZ  1 
ATOM   140  N N   . LEU   A 1 19  ? 23.512 41.078 -11.479 1.00 28.53  ? 225 LEU   A N   1 
ATOM   141  C CA  . LEU   A 1 19  ? 23.774 40.348 -12.710 1.00 27.22  ? 225 LEU   A CA  1 
ATOM   142  C C   . LEU   A 1 19  ? 25.187 40.685 -13.162 1.00 29.66  ? 225 LEU   A C   1 
ATOM   143  O O   . LEU   A 1 19  ? 25.508 41.861 -13.358 1.00 29.17  ? 225 LEU   A O   1 
ATOM   144  C CB  . LEU   A 1 19  ? 22.769 40.734 -13.791 1.00 22.31  ? 225 LEU   A CB  1 
ATOM   145  C CG  . LEU   A 1 19  ? 23.143 40.369 -15.237 1.00 28.25  ? 225 LEU   A CG  1 
ATOM   146  C CD1 . LEU   A 1 19  ? 23.242 38.855 -15.412 1.00 24.81  ? 225 LEU   A CD1 1 
ATOM   147  C CD2 . LEU   A 1 19  ? 22.154 41.019 -16.230 1.00 27.04  ? 225 LEU   A CD2 1 
ATOM   148  N N   . GLU   A 1 20  ? 26.029 39.667 -13.306 1.00 25.16  ? 226 GLU   A N   1 
ATOM   149  C CA  . GLU   A 1 20  ? 27.357 39.817 -13.895 1.00 32.90  ? 226 GLU   A CA  1 
ATOM   150  C C   . GLU   A 1 20  ? 27.326 39.302 -15.329 1.00 30.71  ? 226 GLU   A C   1 
ATOM   151  O O   . GLU   A 1 20  ? 26.815 38.208 -15.587 1.00 28.18  ? 226 GLU   A O   1 
ATOM   152  C CB  . GLU   A 1 20  ? 28.412 39.041 -13.117 1.00 31.58  ? 226 GLU   A CB  1 
ATOM   153  C CG  . GLU   A 1 20  ? 28.509 39.371 -11.648 1.00 41.16  ? 226 GLU   A CG  1 
ATOM   154  C CD  . GLU   A 1 20  ? 29.454 38.429 -10.914 1.00 46.25  ? 226 GLU   A CD  1 
ATOM   155  O OE1 . GLU   A 1 20  ? 29.286 37.198 -11.036 1.00 49.90  ? 226 GLU   A OE1 1 
ATOM   156  O OE2 . GLU   A 1 20  ? 30.362 38.924 -10.202 1.00 58.36  ? 226 GLU   A OE2 1 
ATOM   157  N N   . GLN   A 1 21  ? 27.869 40.082 -16.250 1.00 32.22  ? 227 GLN   A N   1 
ATOM   158  C CA  . GLN   A 1 21  ? 27.919 39.716 -17.660 1.00 30.82  ? 227 GLN   A CA  1 
ATOM   159  C C   . GLN   A 1 21  ? 29.341 39.860 -18.179 1.00 34.29  ? 227 GLN   A C   1 
ATOM   160  O O   . GLN   A 1 21  ? 30.041 40.822 -17.843 1.00 30.84  ? 227 GLN   A O   1 
ATOM   161  C CB  . GLN   A 1 21  ? 26.983 40.594 -18.477 1.00 33.74  ? 227 GLN   A CB  1 
ATOM   162  C CG  . GLN   A 1 21  ? 25.514 40.344 -18.182 1.00 38.52  ? 227 GLN   A CG  1 
ATOM   163  C CD  . GLN   A 1 21  ? 24.606 41.193 -19.035 1.00 40.70  ? 227 GLN   A CD  1 
ATOM   164  O OE1 . GLN   A 1 21  ? 24.071 40.738 -20.044 1.00 47.65  ? 227 GLN   A OE1 1 
ATOM   165  N NE2 . GLN   A 1 21  ? 24.454 42.450 -18.652 1.00 35.80  ? 227 GLN   A NE2 1 
ATOM   166  N N   . GLN   A 1 22  ? 29.764 38.910 -19.002 1.00 39.44  ? 228 GLN   A N   1 
ATOM   167  C CA  . GLN   A 1 22  ? 31.054 38.972 -19.681 1.00 42.44  ? 228 GLN   A CA  1 
ATOM   168  C C   . GLN   A 1 22  ? 30.802 39.256 -21.148 1.00 46.73  ? 228 GLN   A C   1 
ATOM   169  O O   . GLN   A 1 22  ? 30.376 38.364 -21.881 1.00 43.69  ? 228 GLN   A O   1 
ATOM   170  C CB  . GLN   A 1 22  ? 31.827 37.668 -19.530 1.00 52.15  ? 228 GLN   A CB  1 
ATOM   171  C CG  . GLN   A 1 22  ? 32.774 37.629 -18.371 1.00 52.03  ? 228 GLN   A CG  1 
ATOM   172  C CD  . GLN   A 1 22  ? 34.142 37.185 -18.809 1.00 49.37  ? 228 GLN   A CD  1 
ATOM   173  O OE1 . GLN   A 1 22  ? 34.277 36.224 -19.560 1.00 59.03  ? 228 GLN   A OE1 1 
ATOM   174  N NE2 . GLN   A 1 22  ? 35.168 37.909 -18.380 1.00 56.62  ? 228 GLN   A NE2 1 
ATOM   175  N N   . ARG   A 1 23  ? 31.060 40.494 -21.572 1.00 51.12  ? 229 ARG   A N   1 
ATOM   176  C CA  . ARG   A 1 23  ? 30.944 40.825 -22.986 1.00 68.80  ? 229 ARG   A CA  1 
ATOM   177  C C   . ARG   A 1 23  ? 31.965 40.045 -23.811 1.00 67.97  ? 229 ARG   A C   1 
ATOM   178  O O   . ARG   A 1 23  ? 31.619 39.421 -24.819 1.00 68.37  ? 229 ARG   A O   1 
ATOM   179  C CB  . ARG   A 1 23  ? 31.116 42.333 -23.187 1.00 78.10  ? 229 ARG   A CB  1 
ATOM   180  C CG  . ARG   A 1 23  ? 31.203 42.754 -24.651 1.00 89.16  ? 229 ARG   A CG  1 
ATOM   181  C CD  . ARG   A 1 23  ? 30.718 44.191 -24.859 1.00 100.92 ? 229 ARG   A CD  1 
ATOM   182  N NE  . ARG   A 1 23  ? 29.259 44.311 -24.896 1.00 103.89 ? 229 ARG   A NE  1 
ATOM   183  C CZ  . ARG   A 1 23  ? 28.467 43.860 -25.864 1.00 98.35  ? 229 ARG   A CZ  1 
ATOM   184  N NH1 . ARG   A 1 23  ? 28.955 43.288 -26.955 1.00 96.01  ? 229 ARG   A NH1 1 
ATOM   185  N NH2 . ARG   A 1 23  ? 27.150 43.995 -25.738 1.00 90.46  ? 229 ARG   A NH2 1 
ATOM   186  N N   . ASP   A 1 24  ? 33.228 40.040 -23.374 1.00 57.59  ? 230 ASP   A N   1 
ATOM   187  C CA  . ASP   A 1 24  ? 34.301 39.400 -24.127 1.00 63.99  ? 230 ASP   A CA  1 
ATOM   188  C C   . ASP   A 1 24  ? 35.310 38.808 -23.142 1.00 50.10  ? 230 ASP   A C   1 
ATOM   189  O O   . ASP   A 1 24  ? 35.082 38.891 -21.927 1.00 42.44  ? 230 ASP   A O   1 
ATOM   190  C CB  . ASP   A 1 24  ? 34.896 40.423 -25.098 1.00 52.64  ? 230 ASP   A CB  1 
ATOM   191  C CG  . ASP   A 1 24  ? 35.522 41.584 -24.400 1.00 61.83  ? 230 ASP   A CG  1 
ATOM   192  O OD1 . ASP   A 1 24  ? 36.449 41.370 -23.575 1.00 62.28  ? 230 ASP   A OD1 1 
ATOM   193  O OD2 . ASP   A 1 24  ? 35.040 42.715 -24.651 1.00 73.85  ? 230 ASP   A OD2 1 
ATOM   194  N N   . PRO   A 1 25  ? 36.400 38.170 -23.591 1.00 50.64  ? 231 PRO   A N   1 
ATOM   195  C CA  . PRO   A 1 25  ? 37.232 37.416 -22.632 1.00 48.93  ? 231 PRO   A CA  1 
ATOM   196  C C   . PRO   A 1 25  ? 37.870 38.259 -21.534 1.00 43.74  ? 231 PRO   A C   1 
ATOM   197  O O   . PRO   A 1 25  ? 38.230 37.700 -20.493 1.00 47.11  ? 231 PRO   A O   1 
ATOM   198  C CB  . PRO   A 1 25  ? 38.305 36.770 -23.521 1.00 57.29  ? 231 PRO   A CB  1 
ATOM   199  C CG  . PRO   A 1 25  ? 37.709 36.717 -24.873 1.00 58.80  ? 231 PRO   A CG  1 
ATOM   200  C CD  . PRO   A 1 25  ? 36.835 37.928 -24.982 1.00 57.54  ? 231 PRO   A CD  1 
ATOM   201  N N   . ASP   A 1 26  ? 38.049 39.568 -21.731 1.00 35.19  ? 232 ASP   A N   1 
ATOM   202  C CA  . ASP   A 1 26  ? 38.744 40.391 -20.743 1.00 34.76  ? 232 ASP   A CA  1 
ATOM   203  C C   . ASP   A 1 26  ? 37.883 41.485 -20.139 1.00 31.78  ? 232 ASP   A C   1 
ATOM   204  O O   . ASP   A 1 26  ? 38.424 42.390 -19.495 1.00 34.80  ? 232 ASP   A O   1 
ATOM   205  C CB  . ASP   A 1 26  ? 40.004 41.017 -21.348 1.00 32.07  ? 232 ASP   A CB  1 
ATOM   206  C CG  . ASP   A 1 26  ? 40.928 39.990 -21.915 1.00 33.48  ? 232 ASP   A CG  1 
ATOM   207  O OD1 . ASP   A 1 26  ? 41.311 39.084 -21.165 1.00 38.16  ? 232 ASP   A OD1 1 
ATOM   208  O OD2 . ASP   A 1 26  ? 41.283 40.095 -23.092 1.00 34.45  ? 232 ASP   A OD2 1 
ATOM   209  N N   . SER   A 1 27  ? 36.570 41.436 -20.326 1.00 38.32  ? 233 SER   A N   1 
ATOM   210  C CA  . SER   A 1 27  ? 35.673 42.487 -19.869 1.00 33.58  ? 233 SER   A CA  1 
ATOM   211  C C   . SER   A 1 27  ? 34.541 41.875 -19.063 1.00 36.17  ? 233 SER   A C   1 
ATOM   212  O O   . SER   A 1 27  ? 34.103 40.754 -19.323 1.00 42.96  ? 233 SER   A O   1 
ATOM   213  C CB  . SER   A 1 27  ? 35.065 43.276 -21.033 1.00 40.66  ? 233 SER   A CB  1 
ATOM   214  O OG  . SER   A 1 27  ? 36.056 43.648 -21.961 1.00 54.05  ? 233 SER   A OG  1 
ATOM   215  N N   . TYR   A 1 28  ? 34.029 42.662 -18.129 1.00 30.37  ? 234 TYR   A N   1 
ATOM   216  C CA  . TYR   A 1 28  ? 33.097 42.198 -17.119 1.00 35.76  ? 234 TYR   A CA  1 
ATOM   217  C C   . TYR   A 1 28  ? 32.248 43.407 -16.739 1.00 36.48  ? 234 TYR   A C   1 
ATOM   218  O O   . TYR   A 1 28  ? 32.783 44.500 -16.570 1.00 30.23  ? 234 TYR   A O   1 
ATOM   219  C CB  . TYR   A 1 28  ? 33.905 41.620 -15.940 1.00 41.36  ? 234 TYR   A CB  1 
ATOM   220  C CG  . TYR   A 1 28  ? 33.222 41.446 -14.604 1.00 37.45  ? 234 TYR   A CG  1 
ATOM   221  C CD1 . TYR   A 1 28  ? 33.204 42.477 -13.670 1.00 43.67  ? 234 TYR   A CD1 1 
ATOM   222  C CD2 . TYR   A 1 28  ? 32.680 40.224 -14.241 1.00 52.79  ? 234 TYR   A CD2 1 
ATOM   223  C CE1 . TYR   A 1 28  ? 32.611 42.314 -12.441 1.00 41.15  ? 234 TYR   A CE1 1 
ATOM   224  C CE2 . TYR   A 1 28  ? 32.087 40.044 -13.009 1.00 51.53  ? 234 TYR   A CE2 1 
ATOM   225  C CZ  . TYR   A 1 28  ? 32.053 41.096 -12.115 1.00 50.09  ? 234 TYR   A CZ  1 
ATOM   226  O OH  . TYR   A 1 28  ? 31.458 40.914 -10.894 1.00 56.72  ? 234 TYR   A OH  1 
ATOM   227  N N   . ASN   A 1 29  ? 30.934 43.235 -16.701 1.00 34.65  ? 235 ASN   A N   1 
ATOM   228  C CA  . ASN   A 1 29  ? 29.991 44.222 -16.185 1.00 32.49  ? 235 ASN   A CA  1 
ATOM   229  C C   . ASN   A 1 29  ? 29.220 43.605 -15.020 1.00 33.79  ? 235 ASN   A C   1 
ATOM   230  O O   . ASN   A 1 29  ? 28.886 42.416 -15.046 1.00 31.66  ? 235 ASN   A O   1 
ATOM   231  C CB  . ASN   A 1 29  ? 29.027 44.702 -17.293 1.00 37.46  ? 235 ASN   A CB  1 
ATOM   232  C CG  . ASN   A 1 29  ? 27.992 45.719 -16.788 1.00 55.76  ? 235 ASN   A CG  1 
ATOM   233  O OD1 . ASN   A 1 29  ? 26.964 45.348 -16.212 1.00 49.96  ? 235 ASN   A OD1 1 
ATOM   234  N ND2 . ASN   A 1 29  ? 28.296 47.008 -16.942 1.00 52.68  ? 235 ASN   A ND2 1 
ATOM   235  N N   . LYS   A 1 30  ? 28.977 44.400 -13.982 1.00 30.23  ? 236 LYS   A N   1 
ATOM   236  C CA  . LYS   A 1 30  ? 28.156 43.975 -12.853 1.00 28.11  ? 236 LYS   A CA  1 
ATOM   237  C C   . LYS   A 1 30  ? 27.094 45.037 -12.653 1.00 31.84  ? 236 LYS   A C   1 
ATOM   238  O O   . LYS   A 1 30  ? 27.406 46.232 -12.613 1.00 30.63  ? 236 LYS   A O   1 
ATOM   239  C CB  . LYS   A 1 30  ? 28.970 43.769 -11.574 1.00 25.24  ? 236 LYS   A CB  1 
ATOM   240  C CG  . LYS   A 1 30  ? 28.151 43.265 -10.382 1.00 33.31  ? 236 LYS   A CG  1 
ATOM   241  C CD  . LYS   A 1 30  ? 29.025 42.814 -9.207  1.00 36.65  ? 236 LYS   A CD  1 
ATOM   242  C CE  . LYS   A 1 30  ? 28.153 42.376 -8.035  1.00 44.85  ? 236 LYS   A CE  1 
ATOM   243  N NZ  . LYS   A 1 30  ? 28.897 41.740 -6.893  1.00 46.40  ? 236 LYS   A NZ  1 
ATOM   244  N N   . HIS   A 1 31  ? 25.844 44.605 -12.577 1.00 27.79  ? 237 HIS   A N   1 
ATOM   245  C CA  . HIS   A 1 31  ? 24.709 45.490 -12.390 1.00 26.17  ? 237 HIS   A CA  1 
ATOM   246  C C   . HIS   A 1 31  ? 23.953 45.038 -11.153 1.00 27.37  ? 237 HIS   A C   1 
ATOM   247  O O   . HIS   A 1 31  ? 23.699 43.842 -10.984 1.00 26.51  ? 237 HIS   A O   1 
ATOM   248  C CB  . HIS   A 1 31  ? 23.765 45.479 -13.596 1.00 28.95  ? 237 HIS   A CB  1 
ATOM   249  C CG  . HIS   A 1 31  ? 22.497 46.235 -13.356 1.00 32.70  ? 237 HIS   A CG  1 
ATOM   250  N ND1 . HIS   A 1 31  ? 22.413 47.602 -13.512 1.00 32.02  ? 237 HIS   A ND1 1 
ATOM   251  C CD2 . HIS   A 1 31  ? 21.285 45.830 -12.900 1.00 29.17  ? 237 HIS   A CD2 1 
ATOM   252  C CE1 . HIS   A 1 31  ? 21.191 48.003 -13.205 1.00 34.54  ? 237 HIS   A CE1 1 
ATOM   253  N NE2 . HIS   A 1 31  ? 20.486 46.948 -12.830 1.00 35.04  ? 237 HIS   A NE2 1 
ATOM   254  N N   . LEU   A 1 32  ? 23.579 45.992 -10.305 1.00 23.66  ? 238 LEU   A N   1 
ATOM   255  C CA  . LEU   A 1 32  ? 22.886 45.695 -9.059  1.00 25.03  ? 238 LEU   A CA  1 
ATOM   256  C C   . LEU   A 1 32  ? 21.417 46.054 -9.247  1.00 25.81  ? 238 LEU   A C   1 
ATOM   257  O O   . LEU   A 1 32  ? 21.099 47.207 -9.545  1.00 26.40  ? 238 LEU   A O   1 
ATOM   258  C CB  . LEU   A 1 32  ? 23.473 46.496 -7.896  1.00 23.61  ? 238 LEU   A CB  1 
ATOM   259  C CG  . LEU   A 1 32  ? 24.955 46.339 -7.535  1.00 31.03  ? 238 LEU   A CG  1 
ATOM   260  C CD1 . LEU   A 1 32  ? 25.251 47.200 -6.332  1.00 28.53  ? 238 LEU   A CD1 1 
ATOM   261  C CD2 . LEU   A 1 32  ? 25.351 44.916 -7.268  1.00 30.48  ? 238 LEU   A CD2 1 
ATOM   262  N N   . PHE   A 1 33  ? 20.534 45.067 -9.093  1.00 24.84  ? 239 PHE   A N   1 
ATOM   263  C CA  . PHE   A 1 33  ? 19.097 45.327 -9.152  1.00 22.21  ? 239 PHE   A CA  1 
ATOM   264  C C   . PHE   A 1 33  ? 18.612 45.959 -7.851  1.00 26.43  ? 239 PHE   A C   1 
ATOM   265  O O   . PHE   A 1 33  ? 17.864 46.943 -7.867  1.00 23.20  ? 239 PHE   A O   1 
ATOM   266  C CB  . PHE   A 1 33  ? 18.333 44.018 -9.408  1.00 21.43  ? 239 PHE   A CB  1 
ATOM   267  C CG  . PHE   A 1 33  ? 18.679 43.347 -10.720 1.00 26.58  ? 239 PHE   A CG  1 
ATOM   268  C CD1 . PHE   A 1 33  ? 18.245 43.863 -11.915 1.00 23.65  ? 239 PHE   A CD1 1 
ATOM   269  C CD2 . PHE   A 1 33  ? 19.435 42.185 -10.732 1.00 24.70  ? 239 PHE   A CD2 1 
ATOM   270  C CE1 . PHE   A 1 33  ? 18.563 43.244 -13.115 1.00 24.34  ? 239 PHE   A CE1 1 
ATOM   271  C CE2 . PHE   A 1 33  ? 19.752 41.550 -11.921 1.00 25.24  ? 239 PHE   A CE2 1 
ATOM   272  C CZ  . PHE   A 1 33  ? 19.317 42.093 -13.116 1.00 24.38  ? 239 PHE   A CZ  1 
ATOM   273  N N   . VAL   A 1 34  ? 18.988 45.369 -6.714  1.00 23.48  ? 240 VAL   A N   1 
ATOM   274  C CA  . VAL   A 1 34  ? 18.620 45.893 -5.401  1.00 23.91  ? 240 VAL   A CA  1 
ATOM   275  C C   . VAL   A 1 34  ? 19.819 45.749 -4.478  1.00 26.50  ? 240 VAL   A C   1 
ATOM   276  O O   . VAL   A 1 34  ? 20.652 44.854 -4.650  1.00 22.79  ? 240 VAL   A O   1 
ATOM   277  C CB  . VAL   A 1 34  ? 17.383 45.184 -4.768  1.00 26.79  ? 240 VAL   A CB  1 
ATOM   278  C CG1 . VAL   A 1 34  ? 16.076 45.606 -5.469  1.00 27.85  ? 240 VAL   A CG1 1 
ATOM   279  C CG2 . VAL   A 1 34  ? 17.532 43.685 -4.812  1.00 26.93  ? 240 VAL   A CG2 1 
ATOM   280  N N   . HIS   A 1 35  ? 19.884 46.621 -3.474  1.00 22.65  ? 241 HIS   A N   1 
ATOM   281  C CA  . HIS   A 1 35  ? 20.940 46.560 -2.473  1.00 25.99  ? 241 HIS   A CA  1 
ATOM   282  C C   . HIS   A 1 35  ? 20.544 47.447 -1.297  1.00 25.60  ? 241 HIS   A C   1 
ATOM   283  O O   . HIS   A 1 35  ? 19.583 48.217 -1.374  1.00 24.60  ? 241 HIS   A O   1 
ATOM   284  C CB  . HIS   A 1 35  ? 22.291 46.987 -3.061  1.00 22.35  ? 241 HIS   A CB  1 
ATOM   285  C CG  . HIS   A 1 35  ? 22.296 48.369 -3.623  1.00 25.65  ? 241 HIS   A CG  1 
ATOM   286  N ND1 . HIS   A 1 35  ? 22.197 49.495 -2.832  1.00 21.93  ? 241 HIS   A ND1 1 
ATOM   287  C CD2 . HIS   A 1 35  ? 22.405 48.812 -4.900  1.00 23.53  ? 241 HIS   A CD2 1 
ATOM   288  C CE1 . HIS   A 1 35  ? 22.255 50.571 -3.596  1.00 23.54  ? 241 HIS   A CE1 1 
ATOM   289  N NE2 . HIS   A 1 35  ? 22.377 50.184 -4.857  1.00 24.19  ? 241 HIS   A NE2 1 
ATOM   290  N N   . ILE   A 1 36  ? 21.295 47.333 -0.202  1.00 22.47  ? 242 ILE   A N   1 
ATOM   291  C CA  . ILE   A 1 36  ? 21.018 48.188 0.947   1.00 24.56  ? 242 ILE   A CA  1 
ATOM   292  C C   . ILE   A 1 36  ? 22.130 49.216 1.113   1.00 27.44  ? 242 ILE   A C   1 
ATOM   293  O O   . ILE   A 1 36  ? 22.428 49.632 2.228   1.00 26.86  ? 242 ILE   A O   1 
ATOM   294  C CB  . ILE   A 1 36  ? 20.803 47.370 2.242   1.00 24.17  ? 242 ILE   A CB  1 
ATOM   295  C CG1 . ILE   A 1 36  ? 22.047 46.540 2.615   1.00 22.76  ? 242 ILE   A CG1 1 
ATOM   296  C CG2 . ILE   A 1 36  ? 19.536 46.500 2.139   1.00 25.17  ? 242 ILE   A CG2 1 
ATOM   297  C CD1 . ILE   A 1 36  ? 22.060 46.114 4.110   1.00 26.35  ? 242 ILE   A CD1 1 
ATOM   298  N N   . GLY   A 1 37  ? 22.708 49.676 0.007   1.00 24.47  ? 243 GLY   A N   1 
ATOM   299  C CA  . GLY   A 1 37  ? 23.767 50.654 0.091   1.00 25.11  ? 243 GLY   A CA  1 
ATOM   300  C C   . GLY   A 1 37  ? 23.330 52.102 0.166   1.00 30.88  ? 243 GLY   A C   1 
ATOM   301  O O   . GLY   A 1 37  ? 24.150 52.961 0.465   1.00 30.46  ? 243 GLY   A O   1 
ATOM   302  N N   . HIS   A 1 38  ? 22.057 52.407 -0.096  1.00 28.18  ? 244 HIS   A N   1 
ATOM   303  C CA  . HIS   A 1 38  ? 21.576 53.789 -0.189  1.00 29.50  ? 244 HIS   A CA  1 
ATOM   304  C C   . HIS   A 1 38  ? 20.231 53.870 0.530   1.00 32.29  ? 244 HIS   A C   1 
ATOM   305  O O   . HIS   A 1 38  ? 19.167 53.900 -0.099  1.00 26.99  ? 244 HIS   A O   1 
ATOM   306  C CB  . HIS   A 1 38  ? 21.455 54.215 -1.645  1.00 33.97  ? 244 HIS   A CB  1 
ATOM   307  C CG  . HIS   A 1 38  ? 21.248 55.681 -1.840  1.00 42.68  ? 244 HIS   A CG  1 
ATOM   308  N ND1 . HIS   A 1 38  ? 20.242 56.386 -1.213  1.00 45.29  ? 244 HIS   A ND1 1 
ATOM   309  C CD2 . HIS   A 1 38  ? 21.896 56.570 -2.627  1.00 47.72  ? 244 HIS   A CD2 1 
ATOM   310  C CE1 . HIS   A 1 38  ? 20.285 57.649 -1.599  1.00 45.88  ? 244 HIS   A CE1 1 
ATOM   311  N NE2 . HIS   A 1 38  ? 21.280 57.786 -2.458  1.00 51.44  ? 244 HIS   A NE2 1 
ATOM   312  N N   . ALA   A 1 39  ? 20.269 53.888 1.863   1.00 26.23  ? 245 ALA   A N   1 
ATOM   313  C CA  . ALA   A 1 39  ? 19.035 54.073 2.623   1.00 34.46  ? 245 ALA   A CA  1 
ATOM   314  C C   . ALA   A 1 39  ? 18.571 55.519 2.469   1.00 34.26  ? 245 ALA   A C   1 
ATOM   315  O O   . ALA   A 1 39  ? 19.301 56.440 2.846   1.00 36.20  ? 245 ALA   A O   1 
ATOM   316  C CB  . ALA   A 1 39  ? 19.260 53.717 4.094   1.00 29.67  ? 245 ALA   A CB  1 
ATOM   317  N N   . ASN   A 1 40  ? 17.371 55.741 1.912   1.00 29.12  ? 246 ASN   A N   1 
ATOM   318  C CA  . ASN   A 1 40  ? 16.961 57.115 1.613   1.00 33.81  ? 246 ASN   A CA  1 
ATOM   319  C C   . ASN   A 1 40  ? 16.225 57.743 2.804   1.00 36.88  ? 246 ASN   A C   1 
ATOM   320  O O   . ASN   A 1 40  ? 15.078 58.166 2.726   1.00 45.34  ? 246 ASN   A O   1 
ATOM   321  C CB  . ASN   A 1 40  ? 16.141 57.196 0.324   1.00 30.49  ? 246 ASN   A CB  1 
ATOM   322  C CG  . ASN   A 1 40  ? 14.943 56.273 0.293   1.00 35.67  ? 246 ASN   A CG  1 
ATOM   323  O OD1 . ASN   A 1 40  ? 14.476 55.769 1.311   1.00 39.11  ? 246 ASN   A OD1 1 
ATOM   324  N ND2 . ASN   A 1 40  ? 14.414 56.068 -0.908  1.00 44.14  ? 246 ASN   A ND2 1 
ATOM   325  N N   . HIS   A 1 41  ? 16.935 57.786 3.925   1.00 32.27  ? 247 HIS   A N   1 
ATOM   326  C CA  . HIS   A 1 41  ? 16.506 58.469 5.141   1.00 41.19  ? 247 HIS   A CA  1 
ATOM   327  C C   . HIS   A 1 41  ? 17.276 59.778 5.279   1.00 45.38  ? 247 HIS   A C   1 
ATOM   328  O O   . HIS   A 1 41  ? 18.421 59.888 4.842   1.00 42.36  ? 247 HIS   A O   1 
ATOM   329  C CB  . HIS   A 1 41  ? 16.759 57.608 6.384   1.00 39.11  ? 247 HIS   A CB  1 
ATOM   330  C CG  . HIS   A 1 41  ? 15.994 56.319 6.414   1.00 38.85  ? 247 HIS   A CG  1 
ATOM   331  N ND1 . HIS   A 1 41  ? 14.919 56.111 7.251   1.00 40.39  ? 247 HIS   A ND1 1 
ATOM   332  C CD2 . HIS   A 1 41  ? 16.165 55.162 5.730   1.00 37.69  ? 247 HIS   A CD2 1 
ATOM   333  C CE1 . HIS   A 1 41  ? 14.449 54.889 7.073   1.00 36.50  ? 247 HIS   A CE1 1 
ATOM   334  N NE2 . HIS   A 1 41  ? 15.194 54.287 6.163   1.00 36.79  ? 247 HIS   A NE2 1 
ATOM   335  N N   . SER   A 1 42  ? 16.656 60.770 5.918   1.00 43.63  ? 248 SER   A N   1 
ATOM   336  C CA  . SER   A 1 42  ? 17.300 62.073 6.017   1.00 49.36  ? 248 SER   A CA  1 
ATOM   337  C C   . SER   A 1 42  ? 18.417 62.120 7.061   1.00 48.78  ? 248 SER   A C   1 
ATOM   338  O O   . SER   A 1 42  ? 19.260 63.013 6.986   1.00 58.58  ? 248 SER   A O   1 
ATOM   339  C CB  . SER   A 1 42  ? 16.255 63.158 6.305   1.00 53.37  ? 248 SER   A CB  1 
ATOM   340  O OG  . SER   A 1 42  ? 15.555 62.894 7.515   1.00 62.04  ? 248 SER   A OG  1 
ATOM   341  N N   . TYR   A 1 43  ? 18.460 61.183 8.009   1.00 42.10  ? 249 TYR   A N   1 
ATOM   342  C CA  . TYR   A 1 43  ? 19.491 61.131 9.038   1.00 41.82  ? 249 TYR   A CA  1 
ATOM   343  C C   . TYR   A 1 43  ? 20.304 59.843 8.932   1.00 50.98  ? 249 TYR   A C   1 
ATOM   344  O O   . TYR   A 1 43  ? 19.794 58.800 8.507   1.00 45.20  ? 249 TYR   A O   1 
ATOM   345  C CB  . TYR   A 1 43  ? 18.875 61.215 10.452  1.00 50.20  ? 249 TYR   A CB  1 
ATOM   346  C CG  . TYR   A 1 43  ? 18.031 62.453 10.703  1.00 50.63  ? 249 TYR   A CG  1 
ATOM   347  C CD1 . TYR   A 1 43  ? 18.623 63.675 11.024  1.00 54.84  ? 249 TYR   A CD1 1 
ATOM   348  C CD2 . TYR   A 1 43  ? 16.640 62.398 10.612  1.00 50.26  ? 249 TYR   A CD2 1 
ATOM   349  C CE1 . TYR   A 1 43  ? 17.854 64.807 11.256  1.00 53.80  ? 249 TYR   A CE1 1 
ATOM   350  C CE2 . TYR   A 1 43  ? 15.862 63.519 10.833  1.00 48.29  ? 249 TYR   A CE2 1 
ATOM   351  C CZ  . TYR   A 1 43  ? 16.472 64.724 11.154  1.00 54.08  ? 249 TYR   A CZ  1 
ATOM   352  O OH  . TYR   A 1 43  ? 15.686 65.839 11.363  1.00 58.82  ? 249 TYR   A OH  1 
ATOM   353  N N   . SER   A 1 44  ? 21.577 59.915 9.350   1.00 42.30  ? 250 SER   A N   1 
ATOM   354  C CA  . SER   A 1 44  ? 22.415 58.717 9.399   1.00 50.53  ? 250 SER   A CA  1 
ATOM   355  C C   . SER   A 1 44  ? 21.939 57.742 10.472  1.00 52.54  ? 250 SER   A C   1 
ATOM   356  O O   . SER   A 1 44  ? 22.083 56.524 10.313  1.00 48.75  ? 250 SER   A O   1 
ATOM   357  C CB  . SER   A 1 44  ? 23.884 59.094 9.650   1.00 47.52  ? 250 SER   A CB  1 
ATOM   358  O OG  . SER   A 1 44  ? 24.389 59.967 8.647   1.00 50.12  ? 250 SER   A OG  1 
ATOM   359  N N   . ASP   A 1 45  ? 21.381 58.253 11.570  1.00 48.51  ? 251 ASP   A N   1 
ATOM   360  C CA  . ASP   A 1 45  ? 20.907 57.437 12.689  1.00 50.93  ? 251 ASP   A CA  1 
ATOM   361  C C   . ASP   A 1 45  ? 19.509 57.913 13.065  1.00 52.57  ? 251 ASP   A C   1 
ATOM   362  O O   . ASP   A 1 45  ? 19.315 58.568 14.096  1.00 41.35  ? 251 ASP   A O   1 
ATOM   363  C CB  . ASP   A 1 45  ? 21.851 57.533 13.891  1.00 65.06  ? 251 ASP   A CB  1 
ATOM   364  C CG  . ASP   A 1 45  ? 23.256 57.019 13.594  1.00 68.25  ? 251 ASP   A CG  1 
ATOM   365  O OD1 . ASP   A 1 45  ? 23.388 55.958 12.937  1.00 69.90  ? 251 ASP   A OD1 1 
ATOM   366  O OD2 . ASP   A 1 45  ? 24.230 57.678 14.031  1.00 71.97  ? 251 ASP   A OD2 1 
ATOM   367  N N   . PRO   A 1 46  ? 18.512 57.612 12.242  1.00 47.04  ? 252 PRO   A N   1 
ATOM   368  C CA  . PRO   A 1 46  ? 17.174 58.147 12.481  1.00 37.37  ? 252 PRO   A CA  1 
ATOM   369  C C   . PRO   A 1 46  ? 16.463 57.389 13.592  1.00 38.65  ? 252 PRO   A C   1 
ATOM   370  O O   . PRO   A 1 46  ? 16.898 56.334 14.059  1.00 33.48  ? 252 PRO   A O   1 
ATOM   371  C CB  . PRO   A 1 46  ? 16.479 57.952 11.130  1.00 37.09  ? 252 PRO   A CB  1 
ATOM   372  C CG  . PRO   A 1 46  ? 17.092 56.674 10.599  1.00 40.56  ? 252 PRO   A CG  1 
ATOM   373  C CD  . PRO   A 1 46  ? 18.542 56.701 11.078  1.00 46.54  ? 252 PRO   A CD  1 
ATOM   374  N N   . LEU   A 1 47  ? 15.369 57.984 14.051  1.00 32.19  ? 253 LEU   A N   1 
ATOM   375  C CA  . LEU   A 1 47  ? 14.370 57.259 14.813  1.00 32.70  ? 253 LEU   A CA  1 
ATOM   376  C C   . LEU   A 1 47  ? 13.442 56.638 13.777  1.00 36.17  ? 253 LEU   A C   1 
ATOM   377  O O   . LEU   A 1 47  ? 12.862 57.363 12.966  1.00 38.13  ? 253 LEU   A O   1 
ATOM   378  C CB  . LEU   A 1 47  ? 13.608 58.206 15.737  1.00 33.45  ? 253 LEU   A CB  1 
ATOM   379  C CG  . LEU   A 1 47  ? 14.364 58.885 16.883  1.00 35.04  ? 253 LEU   A CG  1 
ATOM   380  C CD1 . LEU   A 1 47  ? 13.443 59.889 17.587  1.00 32.67  ? 253 LEU   A CD1 1 
ATOM   381  C CD2 . LEU   A 1 47  ? 14.912 57.872 17.877  1.00 37.15  ? 253 LEU   A CD2 1 
ATOM   382  N N   . LEU   A 1 48  ? 13.342 55.315 13.750  1.00 32.60  ? 254 LEU   A N   1 
ATOM   383  C CA  . LEU   A 1 48  ? 12.590 54.698 12.662  1.00 35.68  ? 254 LEU   A CA  1 
ATOM   384  C C   . LEU   A 1 48  ? 11.093 54.912 12.821  1.00 34.78  ? 254 LEU   A C   1 
ATOM   385  O O   . LEU   A 1 48  ? 10.536 54.806 13.917  1.00 31.55  ? 254 LEU   A O   1 
ATOM   386  C CB  . LEU   A 1 48  ? 12.884 53.201 12.533  1.00 35.66  ? 254 LEU   A CB  1 
ATOM   387  C CG  . LEU   A 1 48  ? 14.336 52.880 12.186  1.00 32.93  ? 254 LEU   A CG  1 
ATOM   388  C CD1 . LEU   A 1 48  ? 14.585 51.401 12.330  1.00 32.65  ? 254 LEU   A CD1 1 
ATOM   389  C CD2 . LEU   A 1 48  ? 14.666 53.400 10.797  1.00 30.89  ? 254 LEU   A CD2 1 
ATOM   390  N N   . GLU   A 1 49  ? 10.452 55.226 11.707  1.00 28.77  ? 255 GLU   A N   1 
ATOM   391  C CA  . GLU   A 1 49  ? 9.004  55.276 11.662  1.00 33.02  ? 255 GLU   A CA  1 
ATOM   392  C C   . GLU   A 1 49  ? 8.464  53.853 11.778  1.00 32.53  ? 255 GLU   A C   1 
ATOM   393  O O   . GLU   A 1 49  ? 9.167  52.875 11.508  1.00 30.55  ? 255 GLU   A O   1 
ATOM   394  C CB  . GLU   A 1 49  ? 8.583  55.985 10.375  1.00 34.72  ? 255 GLU   A CB  1 
ATOM   395  C CG  . GLU   A 1 49  ? 7.245  55.664 9.823   1.00 46.28  ? 255 GLU   A CG  1 
ATOM   396  C CD  . GLU   A 1 49  ? 6.907  56.552 8.635   1.00 53.40  ? 255 GLU   A CD  1 
ATOM   397  O OE1 . GLU   A 1 49  ? 7.798  57.310 8.187   1.00 50.18  ? 255 GLU   A OE1 1 
ATOM   398  O OE2 . GLU   A 1 49  ? 5.765  56.460 8.131   1.00 44.35  ? 255 GLU   A OE2 1 
ATOM   399  N N   . SER   A 1 50  ? 7.239  53.719 12.263  1.00 30.24  ? 256 SER   A N   1 
ATOM   400  C CA  . SER   A 1 50  ? 6.682  52.387 12.436  1.00 34.16  ? 256 SER   A CA  1 
ATOM   401  C C   . SER   A 1 50  ? 5.543  52.149 11.451  1.00 37.38  ? 256 SER   A C   1 
ATOM   402  O O   . SER   A 1 50  ? 4.982  53.084 10.875  1.00 33.47  ? 256 SER   A O   1 
ATOM   403  C CB  . SER   A 1 50  ? 6.209  52.173 13.875  1.00 32.23  ? 256 SER   A CB  1 
ATOM   404  O OG  . SER   A 1 50  ? 5.112  53.011 14.144  1.00 41.68  ? 256 SER   A OG  1 
ATOM   405  N N   . VAL   A 1 51  ? 5.234  50.871 11.241  1.00 33.94  ? 257 VAL   A N   1 
ATOM   406  C CA  . VAL   A 1 51  ? 4.143  50.443 10.375  1.00 36.29  ? 257 VAL   A CA  1 
ATOM   407  C C   . VAL   A 1 51  ? 3.360  49.380 11.129  1.00 31.31  ? 257 VAL   A C   1 
ATOM   408  O O   . VAL   A 1 51  ? 3.948  48.458 11.701  1.00 34.21  ? 257 VAL   A O   1 
ATOM   409  C CB  . VAL   A 1 51  ? 4.657  49.898 9.023   1.00 35.39  ? 257 VAL   A CB  1 
ATOM   410  C CG1 . VAL   A 1 51  ? 3.610  49.050 8.341   1.00 34.47  ? 257 VAL   A CG1 1 
ATOM   411  C CG2 . VAL   A 1 51  ? 5.091  51.039 8.108   1.00 35.43  ? 257 VAL   A CG2 1 
ATOM   412  N N   . ASP   A 1 52  ? 2.042  49.511 11.144  1.00 33.07  ? 258 ASP   A N   1 
ATOM   413  C CA  . ASP   A 1 52  ? 1.188  48.528 11.802  1.00 38.18  ? 258 ASP   A CA  1 
ATOM   414  C C   . ASP   A 1 52  ? 1.231  47.216 11.007  1.00 35.55  ? 258 ASP   A C   1 
ATOM   415  O O   . ASP   A 1 52  ? 0.839  47.180 9.832   1.00 37.64  ? 258 ASP   A O   1 
ATOM   416  C CB  . ASP   A 1 52  ? -0.235 49.089 11.865  1.00 39.70  ? 258 ASP   A CB  1 
ATOM   417  C CG  . ASP   A 1 52  ? -1.257 48.094 12.382  1.00 49.32  ? 258 ASP   A CG  1 
ATOM   418  O OD1 . ASP   A 1 52  ? -0.894 47.036 12.938  1.00 48.28  ? 258 ASP   A OD1 1 
ATOM   419  O OD2 . ASP   A 1 52  ? -2.458 48.355 12.162  1.00 56.46  ? 258 ASP   A OD2 1 
ATOM   420  N N   . ILE   A 1 53  ? 1.685  46.134 11.643  1.00 28.96  ? 259 ILE   A N   1 
ATOM   421  C CA  . ILE   A 1 53  ? 1.893  44.887 10.915  1.00 37.07  ? 259 ILE   A CA  1 
ATOM   422  C C   . ILE   A 1 53  ? 0.579  44.294 10.423  1.00 38.23  ? 259 ILE   A C   1 
ATOM   423  O O   . ILE   A 1 53  ? 0.559  43.535 9.448   1.00 36.66  ? 259 ILE   A O   1 
ATOM   424  C CB  . ILE   A 1 53  ? 2.677  43.896 11.798  1.00 34.34  ? 259 ILE   A CB  1 
ATOM   425  C CG1 . ILE   A 1 53  ? 3.271  42.754 10.962  1.00 33.60  ? 259 ILE   A CG1 1 
ATOM   426  C CG2 . ILE   A 1 53  ? 1.832  43.383 12.958  1.00 37.44  ? 259 ILE   A CG2 1 
ATOM   427  C CD1 . ILE   A 1 53  ? 4.312  41.945 11.707  1.00 32.71  ? 259 ILE   A CD1 1 
ATOM   428  N N   . ARG   A 1 54  ? -0.539 44.651 11.042  1.00 37.86  ? 260 ARG   A N   1 
ATOM   429  C CA  . ARG   A 1 54  ? -1.806 44.092 10.589  1.00 46.15  ? 260 ARG   A CA  1 
ATOM   430  C C   . ARG   A 1 54  ? -2.138 44.514 9.167   1.00 44.05  ? 260 ARG   A C   1 
ATOM   431  O O   . ARG   A 1 54  ? -2.867 43.798 8.478   1.00 50.85  ? 260 ARG   A O   1 
ATOM   432  C CB  . ARG   A 1 54  ? -2.912 44.474 11.579  1.00 45.55  ? 260 ARG   A CB  1 
ATOM   433  C CG  . ARG   A 1 54  ? -2.829 43.630 12.849  1.00 44.47  ? 260 ARG   A CG  1 
ATOM   434  C CD  . ARG   A 1 54  ? -3.558 44.212 14.044  1.00 54.92  ? 260 ARG   A CD  1 
ATOM   435  N NE  . ARG   A 1 54  ? -3.684 45.660 13.959  1.00 68.48  ? 260 ARG   A NE  1 
ATOM   436  C CZ  . ARG   A 1 54  ? -3.719 46.465 15.012  1.00 76.06  ? 260 ARG   A CZ  1 
ATOM   437  N NH1 . ARG   A 1 54  ? -3.615 45.994 16.244  1.00 71.52  ? 260 ARG   A NH1 1 
ATOM   438  N NH2 . ARG   A 1 54  ? -3.847 47.776 14.825  1.00 81.54  ? 260 ARG   A NH2 1 
ATOM   439  N N   . GLN   A 1 55  ? -1.570 45.607 8.670   1.00 37.90  ? 261 GLN   A N   1 
ATOM   440  C CA  . GLN   A 1 55  ? -1.925 46.004 7.321   1.00 44.52  ? 261 GLN   A CA  1 
ATOM   441  C C   . GLN   A 1 55  ? -1.032 45.393 6.239   1.00 43.70  ? 261 GLN   A C   1 
ATOM   442  O O   . GLN   A 1 55  ? -1.201 45.744 5.069   1.00 48.46  ? 261 GLN   A O   1 
ATOM   443  C CB  . GLN   A 1 55  ? -1.943 47.524 7.180   1.00 53.72  ? 261 GLN   A CB  1 
ATOM   444  C CG  . GLN   A 1 55  ? -0.640 48.249 7.323   1.00 56.25  ? 261 GLN   A CG  1 
ATOM   445  C CD  . GLN   A 1 55  ? -0.862 49.739 7.520   1.00 65.19  ? 261 GLN   A CD  1 
ATOM   446  O OE1 . GLN   A 1 55  ? -0.090 50.572 7.038   1.00 85.65  ? 261 GLN   A OE1 1 
ATOM   447  N NE2 . GLN   A 1 55  ? -1.906 50.079 8.265   1.00 70.48  ? 261 GLN   A NE2 1 
ATOM   448  N N   . ILE   A 1 56  ? -0.113 44.484 6.577   1.00 39.48  ? 262 ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 56  ? 0.661  43.777 5.560   1.00 38.83  ? 262 ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 56  ? 0.510  42.268 5.658   1.00 41.31  ? 262 ILE   A C   1 
ATOM   451  O O   . ILE   A 1 56  ? 1.129  41.551 4.866   1.00 41.46  ? 262 ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 56  ? 2.164  44.140 5.598   1.00 43.30  ? 262 ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 56  ? 2.818  43.638 6.882   1.00 34.87  ? 262 ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 56  ? 2.369  45.635 5.481   1.00 44.17  ? 262 ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 56  ? 4.348  43.672 6.823   1.00 40.08  ? 262 ILE   A CD1 1 
ATOM   456  N N   . TYR   A 1 57  ? -0.260 41.762 6.630   1.00 39.66  ? 263 TYR   A N   1 
ATOM   457  C CA  . TYR   A 1 57  ? -0.475 40.319 6.771   1.00 42.67  ? 263 TYR   A CA  1 
ATOM   458  C C   . TYR   A 1 57  ? -0.906 39.648 5.472   1.00 42.07  ? 263 TYR   A C   1 
ATOM   459  O O   . TYR   A 1 57  ? -0.516 38.506 5.203   1.00 43.17  ? 263 TYR   A O   1 
ATOM   460  C CB  . TYR   A 1 57  ? -1.523 40.032 7.852   1.00 44.45  ? 263 TYR   A CB  1 
ATOM   461  C CG  . TYR   A 1 57  ? -1.023 40.107 9.264   1.00 43.50  ? 263 TYR   A CG  1 
ATOM   462  C CD1 . TYR   A 1 57  ? 0.309  39.844 9.563   1.00 42.26  ? 263 TYR   A CD1 1 
ATOM   463  C CD2 . TYR   A 1 57  ? -1.887 40.419 10.310  1.00 42.97  ? 263 TYR   A CD2 1 
ATOM   464  C CE1 . TYR   A 1 57  ? 0.773  39.898 10.865  1.00 40.51  ? 263 TYR   A CE1 1 
ATOM   465  C CE2 . TYR   A 1 57  ? -1.439 40.476 11.613  1.00 43.92  ? 263 TYR   A CE2 1 
ATOM   466  C CZ  . TYR   A 1 57  ? -0.110 40.220 11.887  1.00 45.84  ? 263 TYR   A CZ  1 
ATOM   467  O OH  . TYR   A 1 57  ? 0.335  40.277 13.179  1.00 53.90  ? 263 TYR   A OH  1 
ATOM   468  N N   . ASP   A 1 58  ? -1.725 40.315 4.662   1.00 41.62  ? 264 ASP   A N   1 
ATOM   469  C CA  . ASP   A 1 58  ? -2.184 39.639 3.460   1.00 43.17  ? 264 ASP   A CA  1 
ATOM   470  C C   . ASP   A 1 58  ? -1.184 39.718 2.312   1.00 40.26  ? 264 ASP   A C   1 
ATOM   471  O O   . ASP   A 1 58  ? -1.453 39.149 1.252   1.00 40.19  ? 264 ASP   A O   1 
ATOM   472  C CB  . ASP   A 1 58  ? -3.547 40.174 3.006   1.00 47.78  ? 264 ASP   A CB  1 
ATOM   473  C CG  . ASP   A 1 58  ? -3.537 41.648 2.699   1.00 53.12  ? 264 ASP   A CG  1 
ATOM   474  O OD1 . ASP   A 1 58  ? -2.506 42.315 2.927   1.00 57.22  ? 264 ASP   A OD1 1 
ATOM   475  O OD2 . ASP   A 1 58  ? -4.571 42.144 2.203   1.00 59.96  ? 264 ASP   A OD2 1 
ATOM   476  N N   . LYS   A 1 59  ? -0.036 40.373 2.497   1.00 37.63  ? 265 LYS   A N   1 
ATOM   477  C CA  . LYS   A 1 59  ? 1.023  40.402 1.491   1.00 36.00  ? 265 LYS   A CA  1 
ATOM   478  C C   . LYS   A 1 59  ? 2.094  39.342 1.737   1.00 34.32  ? 265 LYS   A C   1 
ATOM   479  O O   . LYS   A 1 59  ? 3.026  39.216 0.933   1.00 35.08  ? 265 LYS   A O   1 
ATOM   480  C CB  . LYS   A 1 59  ? 1.663  41.800 1.433   1.00 36.96  ? 265 LYS   A CB  1 
ATOM   481  C CG  . LYS   A 1 59  ? 0.643  42.909 1.183   1.00 43.45  ? 265 LYS   A CG  1 
ATOM   482  C CD  . LYS   A 1 59  ? 1.243  44.315 1.147   1.00 44.26  ? 265 LYS   A CD  1 
ATOM   483  C CE  . LYS   A 1 59  ? 2.361  44.450 0.147   1.00 45.74  ? 265 LYS   A CE  1 
ATOM   484  N NZ  . LYS   A 1 59  ? 1.993  43.967 -1.223  1.00 49.24  ? 265 LYS   A NZ  1 
ATOM   485  N N   . PHE   A 1 60  ? 1.968  38.565 2.800   1.00 36.28  ? 266 PHE   A N   1 
ATOM   486  C CA  . PHE   A 1 60  ? 2.969  37.584 3.193   1.00 33.45  ? 266 PHE   A CA  1 
ATOM   487  C C   . PHE   A 1 60  ? 2.272  36.291 3.599   1.00 39.38  ? 266 PHE   A C   1 
ATOM   488  O O   . PHE   A 1 60  ? 1.047  36.290 3.787   1.00 38.58  ? 266 PHE   A O   1 
ATOM   489  C CB  . PHE   A 1 60  ? 3.841  38.171 4.317   1.00 33.08  ? 266 PHE   A CB  1 
ATOM   490  C CG  . PHE   A 1 60  ? 4.694  39.335 3.855   1.00 29.84  ? 266 PHE   A CG  1 
ATOM   491  C CD1 . PHE   A 1 60  ? 5.900  39.112 3.209   1.00 34.26  ? 266 PHE   A CD1 1 
ATOM   492  C CD2 . PHE   A 1 60  ? 4.249  40.642 4.000   1.00 32.53  ? 266 PHE   A CD2 1 
ATOM   493  C CE1 . PHE   A 1 60  ? 6.675  40.176 2.767   1.00 33.81  ? 266 PHE   A CE1 1 
ATOM   494  C CE2 . PHE   A 1 60  ? 4.999  41.708 3.542   1.00 35.13  ? 266 PHE   A CE2 1 
ATOM   495  C CZ  . PHE   A 1 60  ? 6.223  41.475 2.915   1.00 30.51  ? 266 PHE   A CZ  1 
ATOM   496  N N   . PRO   A 1 61  ? 2.990  35.173 3.724   1.00 40.72  ? 267 PRO   A N   1 
ATOM   497  C CA  . PRO   A 1 61  ? 2.327  33.911 4.078   1.00 37.74  ? 267 PRO   A CA  1 
ATOM   498  C C   . PRO   A 1 61  ? 1.604  33.996 5.415   1.00 47.87  ? 267 PRO   A C   1 
ATOM   499  O O   . PRO   A 1 61  ? 2.054  34.660 6.352   1.00 47.30  ? 267 PRO   A O   1 
ATOM   500  C CB  . PRO   A 1 61  ? 3.486  32.908 4.140   1.00 41.97  ? 267 PRO   A CB  1 
ATOM   501  C CG  . PRO   A 1 61  ? 4.558  33.520 3.320   1.00 34.96  ? 267 PRO   A CG  1 
ATOM   502  C CD  . PRO   A 1 61  ? 4.440  34.987 3.542   1.00 34.11  ? 267 PRO   A CD  1 
ATOM   503  N N   . GLU   A 1 62  ? 0.474  33.290 5.500   1.00 49.84  ? 268 GLU   A N   1 
ATOM   504  C CA  . GLU   A 1 62  ? -0.403 33.330 6.667   1.00 48.52  ? 268 GLU   A CA  1 
ATOM   505  C C   . GLU   A 1 62  ? -0.580 31.928 7.252   1.00 53.03  ? 268 GLU   A C   1 
ATOM   506  O O   . GLU   A 1 62  ? 0.021  30.954 6.792   1.00 53.76  ? 268 GLU   A O   1 
ATOM   507  C CB  . GLU   A 1 62  ? -1.740 33.975 6.289   1.00 50.01  ? 268 GLU   A CB  1 
ATOM   508  C CG  . GLU   A 1 62  ? -1.575 35.453 5.961   1.00 51.24  ? 268 GLU   A CG  1 
ATOM   509  C CD  . GLU   A 1 62  ? -2.866 36.155 5.598   1.00 54.00  ? 268 GLU   A CD  1 
ATOM   510  O OE1 . GLU   A 1 62  ? -3.180 36.208 4.391   1.00 57.08  ? 268 GLU   A OE1 1 
ATOM   511  O OE2 . GLU   A 1 62  ? -3.539 36.694 6.506   1.00 51.29  ? 268 GLU   A OE2 1 
ATOM   512  N N   . LYS   A 1 63  ? -1.396 31.847 8.297   1.00 55.99  ? 269 LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 63  ? -1.693 30.597 9.028   1.00 65.05  ? 269 LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 63  ? -0.384 30.050 9.617   1.00 66.52  ? 269 LYS   A C   1 
ATOM   515  O O   . LYS   A 1 63  ? 0.442  30.839 10.103  1.00 57.56  ? 269 LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 63  ? -2.457 29.642 8.133   1.00 62.18  ? 269 LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 63  ? -3.570 30.301 7.338   1.00 63.61  ? 269 LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 63  ? -4.872 30.286 8.129   0.00 68.62  ? 269 LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 63  ? -5.221 28.888 8.614   0.00 72.72  ? 269 LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 63  ? -5.834 28.915 9.973   0.00 76.98  ? 269 LYS   A NZ  1 
ATOM   521  N N   . LYS   A 1 64  ? -0.181 28.729 9.621   1.00 70.44  ? 270 LYS   A N   1 
ATOM   522  C CA  . LYS   A 1 64  ? 0.963  28.134 10.312  1.00 70.24  ? 270 LYS   A CA  1 
ATOM   523  C C   . LYS   A 1 64  ? 2.273  28.569 9.669   1.00 67.32  ? 270 LYS   A C   1 
ATOM   524  O O   . LYS   A 1 64  ? 2.435  28.490 8.448   1.00 68.21  ? 270 LYS   A O   1 
ATOM   525  C CB  . LYS   A 1 64  ? 0.869  26.606 10.293  1.00 74.84  ? 270 LYS   A CB  1 
ATOM   526  C CG  . LYS   A 1 64  ? -0.477 26.031 10.693  0.00 79.97  ? 270 LYS   A CG  1 
ATOM   527  C CD  . LYS   A 1 64  ? -0.631 24.621 10.141  0.00 88.05  ? 270 LYS   A CD  1 
ATOM   528  C CE  . LYS   A 1 64  ? -1.956 23.997 10.542  0.00 95.87  ? 270 LYS   A CE  1 
ATOM   529  N NZ  . LYS   A 1 64  ? -2.114 22.632 9.968   0.00 99.95  ? 270 LYS   A NZ  1 
ATOM   530  N N   . GLY   A 1 65  ? 3.215  29.016 10.499  1.00 72.80  ? 271 GLY   A N   1 
ATOM   531  C CA  . GLY   A 1 65  ? 4.485  29.512 10.007  1.00 69.98  ? 271 GLY   A CA  1 
ATOM   532  C C   . GLY   A 1 65  ? 4.438  30.880 9.367   1.00 61.43  ? 271 GLY   A C   1 
ATOM   533  O O   . GLY   A 1 65  ? 5.478  31.365 8.905   1.00 63.20  ? 271 GLY   A O   1 
ATOM   534  N N   . GLY   A 1 66  ? 3.274  31.525 9.342   1.00 56.95  ? 272 GLY   A N   1 
ATOM   535  C CA  . GLY   A 1 66  ? 3.118  32.812 8.704   1.00 54.86  ? 272 GLY   A CA  1 
ATOM   536  C C   . GLY   A 1 66  ? 3.611  33.968 9.555   1.00 48.68  ? 272 GLY   A C   1 
ATOM   537  O O   . GLY   A 1 66  ? 4.102  33.815 10.674  1.00 46.91  ? 272 GLY   A O   1 
ATOM   538  N N   . LEU   A 1 67  ? 3.461  35.165 8.997   1.00 40.69  ? 273 LEU   A N   1 
ATOM   539  C CA  . LEU   A 1 67  ? 4.083  36.330 9.609   1.00 40.56  ? 273 LEU   A CA  1 
ATOM   540  C C   . LEU   A 1 67  ? 3.453  36.661 10.954  1.00 42.27  ? 273 LEU   A C   1 
ATOM   541  O O   . LEU   A 1 67  ? 4.165  37.018 11.902  1.00 41.56  ? 273 LEU   A O   1 
ATOM   542  C CB  . LEU   A 1 67  ? 4.004  37.517 8.654   1.00 40.82  ? 273 LEU   A CB  1 
ATOM   543  C CG  . LEU   A 1 67  ? 4.673  38.821 9.075   1.00 38.35  ? 273 LEU   A CG  1 
ATOM   544  C CD1 . LEU   A 1 67  ? 6.153  38.625 9.409   1.00 34.82  ? 273 LEU   A CD1 1 
ATOM   545  C CD2 . LEU   A 1 67  ? 4.482  39.853 7.978   1.00 35.35  ? 273 LEU   A CD2 1 
ATOM   546  N N   . LYS   A 1 68  ? 2.122  36.557 11.056  1.00 43.76  ? 274 LYS   A N   1 
ATOM   547  C CA  . LYS   A 1 68  ? 1.448  36.832 12.327  1.00 42.51  ? 274 LYS   A CA  1 
ATOM   548  C C   . LYS   A 1 68  ? 1.945  35.899 13.420  1.00 39.01  ? 274 LYS   A C   1 
ATOM   549  O O   . LYS   A 1 68  ? 2.250  36.331 14.537  1.00 41.18  ? 274 LYS   A O   1 
ATOM   550  C CB  . LYS   A 1 68  ? -0.065 36.700 12.160  1.00 41.13  ? 274 LYS   A CB  1 
ATOM   551  C CG  . LYS   A 1 68  ? -0.852 36.968 13.433  1.00 45.43  ? 274 LYS   A CG  1 
ATOM   552  C CD  . LYS   A 1 68  ? -2.349 36.941 13.169  1.00 46.53  ? 274 LYS   A CD  1 
ATOM   553  C CE  . LYS   A 1 68  ? -3.146 36.911 14.473  1.00 49.43  ? 274 LYS   A CE  1 
ATOM   554  N NZ  . LYS   A 1 68  ? -4.586 36.639 14.198  1.00 60.42  ? 274 LYS   A NZ  1 
ATOM   555  N N   . GLU   A 1 69  ? 2.060  34.615 13.107  1.00 41.52  ? 275 GLU   A N   1 
ATOM   556  C CA  . GLU   A 1 69  ? 2.580  33.665 14.079  1.00 43.57  ? 275 GLU   A CA  1 
ATOM   557  C C   . GLU   A 1 69  ? 4.006  34.027 14.494  1.00 42.90  ? 275 GLU   A C   1 
ATOM   558  O O   . GLU   A 1 69  ? 4.336  34.039 15.686  1.00 45.30  ? 275 GLU   A O   1 
ATOM   559  C CB  . GLU   A 1 69  ? 2.507  32.258 13.485  1.00 48.44  ? 275 GLU   A CB  1 
ATOM   560  C CG  . GLU   A 1 69  ? 2.853  31.129 14.447  1.00 58.84  ? 275 GLU   A CG  1 
ATOM   561  C CD  . GLU   A 1 69  ? 2.515  29.765 13.867  1.00 64.61  ? 275 GLU   A CD  1 
ATOM   562  O OE1 . GLU   A 1 69  ? 3.294  29.267 13.027  1.00 63.38  ? 275 GLU   A OE1 1 
ATOM   563  O OE2 . GLU   A 1 69  ? 1.460  29.198 14.234  1.00 82.78  ? 275 GLU   A OE2 1 
ATOM   564  N N   . LEU   A 1 70  ? 4.867  34.341 13.518  1.00 40.56  ? 276 LEU   A N   1 
ATOM   565  C CA  . LEU   A 1 70  ? 6.245  34.709 13.832  1.00 37.45  ? 276 LEU   A CA  1 
ATOM   566  C C   . LEU   A 1 70  ? 6.291  35.929 14.735  1.00 33.48  ? 276 LEU   A C   1 
ATOM   567  O O   . LEU   A 1 70  ? 7.005  35.941 15.745  1.00 40.09  ? 276 LEU   A O   1 
ATOM   568  C CB  . LEU   A 1 70  ? 7.017  34.984 12.544  1.00 38.69  ? 276 LEU   A CB  1 
ATOM   569  C CG  . LEU   A 1 70  ? 7.476  33.761 11.761  1.00 51.58  ? 276 LEU   A CG  1 
ATOM   570  C CD1 . LEU   A 1 70  ? 7.858  34.164 10.337  1.00 45.69  ? 276 LEU   A CD1 1 
ATOM   571  C CD2 . LEU   A 1 70  ? 8.650  33.109 12.474  1.00 47.40  ? 276 LEU   A CD2 1 
ATOM   572  N N   . PHE   A 1 71  ? 5.531  36.972 14.380  1.00 37.62  ? 277 PHE   A N   1 
ATOM   573  C CA  . PHE   A 1 71  ? 5.559  38.217 15.142  1.00 36.11  ? 277 PHE   A CA  1 
ATOM   574  C C   . PHE   A 1 71  ? 5.073  38.002 16.569  1.00 38.59  ? 277 PHE   A C   1 
ATOM   575  O O   . PHE   A 1 71  ? 5.629  38.581 17.509  1.00 37.94  ? 277 PHE   A O   1 
ATOM   576  C CB  . PHE   A 1 71  ? 4.715  39.287 14.445  1.00 40.46  ? 277 PHE   A CB  1 
ATOM   577  C CG  . PHE   A 1 71  ? 4.835  40.665 15.061  1.00 39.85  ? 277 PHE   A CG  1 
ATOM   578  C CD1 . PHE   A 1 71  ? 5.944  41.470 14.806  1.00 38.40  ? 277 PHE   A CD1 1 
ATOM   579  C CD2 . PHE   A 1 71  ? 3.830  41.161 15.888  1.00 38.69  ? 277 PHE   A CD2 1 
ATOM   580  C CE1 . PHE   A 1 71  ? 6.049  42.749 15.372  1.00 39.63  ? 277 PHE   A CE1 1 
ATOM   581  C CE2 . PHE   A 1 71  ? 3.926  42.433 16.456  1.00 42.31  ? 277 PHE   A CE2 1 
ATOM   582  C CZ  . PHE   A 1 71  ? 5.032  43.227 16.200  1.00 40.87  ? 277 PHE   A CZ  1 
ATOM   583  N N   . GLY   A 1 72  ? 4.042  37.167 16.747  1.00 42.86  ? 278 GLY   A N   1 
ATOM   584  C CA  . GLY   A 1 72  ? 3.563  36.855 18.087  1.00 41.75  ? 278 GLY   A CA  1 
ATOM   585  C C   . GLY   A 1 72  ? 4.595  36.168 18.960  1.00 44.23  ? 278 GLY   A C   1 
ATOM   586  O O   . GLY   A 1 72  ? 4.643  36.403 20.171  1.00 48.70  ? 278 GLY   A O   1 
ATOM   587  N N   . LYS   A 1 73  ? 5.435  35.313 18.371  1.00 46.50  ? 279 LYS   A N   1 
ATOM   588  C CA  . LYS   A 1 73  ? 6.490  34.679 19.157  1.00 43.51  ? 279 LYS   A CA  1 
ATOM   589  C C   . LYS   A 1 73  ? 7.603  35.663 19.508  1.00 43.12  ? 279 LYS   A C   1 
ATOM   590  O O   . LYS   A 1 73  ? 8.315  35.466 20.503  1.00 44.95  ? 279 LYS   A O   1 
ATOM   591  C CB  . LYS   A 1 73  ? 7.063  33.485 18.403  1.00 42.34  ? 279 LYS   A CB  1 
ATOM   592  C CG  . LYS   A 1 73  ? 6.146  32.279 18.366  1.00 56.65  ? 279 LYS   A CG  1 
ATOM   593  C CD  . LYS   A 1 73  ? 6.880  31.036 17.893  0.00 53.99  ? 279 LYS   A CD  1 
ATOM   594  C CE  . LYS   A 1 73  ? 5.950  29.835 17.847  0.00 59.03  ? 279 LYS   A CE  1 
ATOM   595  N NZ  . LYS   A 1 73  ? 6.666  28.593 17.450  0.00 62.06  ? 279 LYS   A NZ  1 
ATOM   596  N N   . GLY   A 1 74  ? 7.782  36.708 18.699  1.00 42.31  ? 280 GLY   A N   1 
ATOM   597  C CA  . GLY   A 1 74  ? 8.765  37.735 18.956  1.00 41.27  ? 280 GLY   A CA  1 
ATOM   598  C C   . GLY   A 1 74  ? 10.201 37.266 18.783  1.00 46.02  ? 280 GLY   A C   1 
ATOM   599  O O   . GLY   A 1 74  ? 10.468 36.184 18.249  1.00 43.15  ? 280 GLY   A O   1 
ATOM   600  N N   . PRO   A 1 75  ? 11.165 38.089 19.224  1.00 42.04  ? 281 PRO   A N   1 
ATOM   601  C CA  . PRO   A 1 75  ? 11.007 39.440 19.795  1.00 41.94  ? 281 PRO   A CA  1 
ATOM   602  C C   . PRO   A 1 75  ? 10.544 40.461 18.774  1.00 47.73  ? 281 PRO   A C   1 
ATOM   603  O O   . PRO   A 1 75  ? 10.997 40.466 17.636  1.00 39.41  ? 281 PRO   A O   1 
ATOM   604  C CB  . PRO   A 1 75  ? 12.413 39.767 20.310  1.00 42.27  ? 281 PRO   A CB  1 
ATOM   605  C CG  . PRO   A 1 75  ? 13.332 38.960 19.439  1.00 37.84  ? 281 PRO   A CG  1 
ATOM   606  C CD  . PRO   A 1 75  ? 12.579 37.677 19.166  1.00 39.91  ? 281 PRO   A CD  1 
ATOM   607  N N   . GLN   A 1 76  ? 9.643  41.363 19.167  1.00 40.76  ? 282 GLN   A N   1 
ATOM   608  C CA  . GLN   A 1 76  ? 9.031  42.258 18.198  1.00 42.63  ? 282 GLN   A CA  1 
ATOM   609  C C   . GLN   A 1 76  ? 10.005 43.305 17.680  1.00 39.96  ? 282 GLN   A C   1 
ATOM   610  O O   . GLN   A 1 76  ? 9.785  43.847 16.590  1.00 40.83  ? 282 GLN   A O   1 
ATOM   611  C CB  . GLN   A 1 76  ? 7.785  42.892 18.818  1.00 45.24  ? 282 GLN   A CB  1 
ATOM   612  C CG  . GLN   A 1 76  ? 6.783  41.825 19.264  1.00 53.33  ? 282 GLN   A CG  1 
ATOM   613  C CD  . GLN   A 1 76  ? 5.467  42.394 19.759  1.00 66.49  ? 282 GLN   A CD  1 
ATOM   614  O OE1 . GLN   A 1 76  ? 5.284  43.613 19.840  1.00 62.01  ? 282 GLN   A OE1 1 
ATOM   615  N NE2 . GLN   A 1 76  ? 4.525  41.506 20.051  1.00 63.57  ? 282 GLN   A NE2 1 
ATOM   616  N N   . ASN   A 1 77  ? 11.096 43.571 18.407  1.00 35.00  ? 283 ASN   A N   1 
ATOM   617  C CA  . ASN   A 1 77  ? 12.093 44.520 17.922  1.00 36.98  ? 283 ASN   A CA  1 
ATOM   618  C C   . ASN   A 1 77  ? 12.955 43.961 16.777  1.00 37.38  ? 283 ASN   A C   1 
ATOM   619  O O   . ASN   A 1 77  ? 13.781 44.698 16.233  1.00 32.17  ? 283 ASN   A O   1 
ATOM   620  C CB  . ASN   A 1 77  ? 12.977 44.989 19.086  1.00 38.74  ? 283 ASN   A CB  1 
ATOM   621  C CG  . ASN   A 1 77  ? 13.926 43.908 19.596  1.00 46.20  ? 283 ASN   A CG  1 
ATOM   622  O OD1 . ASN   A 1 77  ? 13.831 42.734 19.232  1.00 44.43  ? 283 ASN   A OD1 1 
ATOM   623  N ND2 . ASN   A 1 77  ? 14.844 44.308 20.466  1.00 53.40  ? 283 ASN   A ND2 1 
ATOM   624  N N   . ALA   A 1 78  ? 12.772 42.704 16.392  1.00 34.05  ? 284 ALA   A N   1 
ATOM   625  C CA  . ALA   A 1 78  ? 13.500 42.110 15.274  1.00 31.80  ? 284 ALA   A CA  1 
ATOM   626  C C   . ALA   A 1 78  ? 12.763 42.226 13.943  1.00 28.50  ? 284 ALA   A C   1 
ATOM   627  O O   . ALA   A 1 78  ? 13.277 41.741 12.926  1.00 31.34  ? 284 ALA   A O   1 
ATOM   628  C CB  . ALA   A 1 78  ? 13.780 40.634 15.565  1.00 28.17  ? 284 ALA   A CB  1 
ATOM   629  N N   . PHE   A 1 79  ? 11.582 42.844 13.912  1.00 27.84  ? 285 PHE   A N   1 
ATOM   630  C CA  . PHE   A 1 79  ? 10.724 42.820 12.736  1.00 29.60  ? 285 PHE   A CA  1 
ATOM   631  C C   . PHE   A 1 79  ? 10.717 44.161 12.029  1.00 27.27  ? 285 PHE   A C   1 
ATOM   632  O O   . PHE   A 1 79  ? 10.404 45.200 12.626  1.00 26.54  ? 285 PHE   A O   1 
ATOM   633  C CB  . PHE   A 1 79  ? 9.296  42.389 13.093  1.00 27.44  ? 285 PHE   A CB  1 
ATOM   634  C CG  . PHE   A 1 79  ? 9.177  40.932 13.387  1.00 31.22  ? 285 PHE   A CG  1 
ATOM   635  C CD1 . PHE   A 1 79  ? 9.679  40.404 14.556  1.00 33.56  ? 285 PHE   A CD1 1 
ATOM   636  C CD2 . PHE   A 1 79  ? 8.596  40.075 12.465  1.00 29.27  ? 285 PHE   A CD2 1 
ATOM   637  C CE1 . PHE   A 1 79  ? 9.600  39.049 14.804  1.00 27.62  ? 285 PHE   A CE1 1 
ATOM   638  C CE2 . PHE   A 1 79  ? 8.508  38.716 12.712  1.00 33.06  ? 285 PHE   A CE2 1 
ATOM   639  C CZ  . PHE   A 1 79  ? 9.004  38.204 13.880  1.00 31.82  ? 285 PHE   A CZ  1 
ATOM   640  N N   . PHE   A 1 80  ? 11.018 44.126 10.737  1.00 25.63  ? 286 PHE   A N   1 
ATOM   641  C CA  . PHE   A 1 80  ? 11.088 45.325 9.932   1.00 25.39  ? 286 PHE   A CA  1 
ATOM   642  C C   . PHE   A 1 80  ? 10.336 45.121 8.630   1.00 28.12  ? 286 PHE   A C   1 
ATOM   643  O O   . PHE   A 1 80  ? 10.296 44.023 8.068   1.00 24.79  ? 286 PHE   A O   1 
ATOM   644  C CB  . PHE   A 1 80  ? 12.557 45.681 9.625   1.00 26.12  ? 286 PHE   A CB  1 
ATOM   645  C CG  . PHE   A 1 80  ? 13.382 45.899 10.845  1.00 28.32  ? 286 PHE   A CG  1 
ATOM   646  C CD1 . PHE   A 1 80  ? 14.001 44.833 11.481  1.00 27.29  ? 286 PHE   A CD1 1 
ATOM   647  C CD2 . PHE   A 1 80  ? 13.557 47.180 11.360  1.00 28.49  ? 286 PHE   A CD2 1 
ATOM   648  C CE1 . PHE   A 1 80  ? 14.771 45.037 12.622  1.00 26.78  ? 286 PHE   A CE1 1 
ATOM   649  C CE2 . PHE   A 1 80  ? 14.332 47.388 12.495  1.00 29.92  ? 286 PHE   A CE2 1 
ATOM   650  C CZ  . PHE   A 1 80  ? 14.935 46.319 13.125  1.00 31.36  ? 286 PHE   A CZ  1 
ATOM   651  N N   . LEU   A 1 81  ? 9.800  46.210 8.125   1.00 23.00  ? 287 LEU   A N   1 
ATOM   652  C CA  . LEU   A 1 81  ? 9.343  46.291 6.758   1.00 23.32  ? 287 LEU   A CA  1 
ATOM   653  C C   . LEU   A 1 81  ? 10.380 47.102 5.999   1.00 25.08  ? 287 LEU   A C   1 
ATOM   654  O O   . LEU   A 1 81  ? 10.752 48.196 6.433   1.00 25.47  ? 287 LEU   A O   1 
ATOM   655  C CB  . LEU   A 1 81  ? 7.967  46.960 6.685   1.00 26.64  ? 287 LEU   A CB  1 
ATOM   656  C CG  . LEU   A 1 81  ? 7.405  47.373 5.325   1.00 30.82  ? 287 LEU   A CG  1 
ATOM   657  C CD1 . LEU   A 1 81  ? 6.937  46.162 4.547   1.00 31.42  ? 287 LEU   A CD1 1 
ATOM   658  C CD2 . LEU   A 1 81  ? 6.245  48.317 5.521   1.00 36.85  ? 287 LEU   A CD2 1 
ATOM   659  N N   . VAL   A 1 82  ? 10.861 46.576 4.877   1.00 21.36  ? 288 VAL   A N   1 
ATOM   660  C CA  . VAL   A 1 82  ? 11.862 47.276 4.088   1.00 23.53  ? 288 VAL   A CA  1 
ATOM   661  C C   . VAL   A 1 82  ? 11.332 47.421 2.677   1.00 26.12  ? 288 VAL   A C   1 
ATOM   662  O O   . VAL   A 1 82  ? 11.018 46.426 2.012   1.00 26.57  ? 288 VAL   A O   1 
ATOM   663  C CB  . VAL   A 1 82  ? 13.228 46.567 4.099   1.00 23.31  ? 288 VAL   A CB  1 
ATOM   664  C CG1 . VAL   A 1 82  ? 14.251 47.408 3.347   1.00 24.08  ? 288 VAL   A CG1 1 
ATOM   665  C CG2 . VAL   A 1 82  ? 13.690 46.318 5.536   1.00 25.58  ? 288 VAL   A CG2 1 
ATOM   666  N N   . LYS   A 1 83  ? 11.238 48.655 2.222   1.00 22.97  ? 289 LYS   A N   1 
ATOM   667  C CA  . LYS   A 1 83  ? 10.835 48.952 0.863   1.00 24.18  ? 289 LYS   A CA  1 
ATOM   668  C C   . LYS   A 1 83  ? 12.086 49.106 0.011   1.00 27.14  ? 289 LYS   A C   1 
ATOM   669  O O   . LYS   A 1 83  ? 12.982 49.879 0.359   1.00 25.83  ? 289 LYS   A O   1 
ATOM   670  C CB  . LYS   A 1 83  ? 10.015 50.238 0.812   1.00 25.11  ? 289 LYS   A CB  1 
ATOM   671  C CG  . LYS   A 1 83  ? 9.668  50.635 -0.602  1.00 28.89  ? 289 LYS   A CG  1 
ATOM   672  C CD  . LYS   A 1 83  ? 8.486  51.568 -0.672  1.00 38.49  ? 289 LYS   A CD  1 
ATOM   673  C CE  . LYS   A 1 83  ? 8.168  51.933 -2.130  1.00 35.35  ? 289 LYS   A CE  1 
ATOM   674  N NZ  . LYS   A 1 83  ? 6.795  52.512 -2.249  1.00 43.79  ? 289 LYS   A NZ  1 
ATOM   675  N N   . PHE   A 1 84  ? 12.149 48.371 -1.093  1.00 24.70  ? 290 PHE   A N   1 
ATOM   676  C CA  . PHE   A 1 84  ? 13.270 48.438 -2.021  1.00 25.07  ? 290 PHE   A CA  1 
ATOM   677  C C   . PHE   A 1 84  ? 12.839 49.077 -3.332  1.00 26.24  ? 290 PHE   A C   1 
ATOM   678  O O   . PHE   A 1 84  ? 11.780 48.755 -3.876  1.00 25.88  ? 290 PHE   A O   1 
ATOM   679  C CB  . PHE   A 1 84  ? 13.835 47.044 -2.309  1.00 21.22  ? 290 PHE   A CB  1 
ATOM   680  C CG  . PHE   A 1 84  ? 14.565 46.428 -1.165  1.00 24.66  ? 290 PHE   A CG  1 
ATOM   681  C CD1 . PHE   A 1 84  ? 13.897 45.672 -0.225  1.00 19.69  ? 290 PHE   A CD1 1 
ATOM   682  C CD2 . PHE   A 1 84  ? 15.935 46.564 -1.053  1.00 23.35  ? 290 PHE   A CD2 1 
ATOM   683  C CE1 . PHE   A 1 84  ? 14.563 45.080 0.821   1.00 23.49  ? 290 PHE   A CE1 1 
ATOM   684  C CE2 . PHE   A 1 84  ? 16.628 45.964 0.013   1.00 24.47  ? 290 PHE   A CE2 1 
ATOM   685  C CZ  . PHE   A 1 84  ? 15.942 45.230 0.947   1.00 22.58  ? 290 PHE   A CZ  1 
ATOM   686  N N   . TRP   A 1 85  ? 13.681 49.948 -3.857  1.00 23.45  ? 291 TRP   A N   1 
ATOM   687  C CA  . TRP   A 1 85  ? 13.532 50.478 -5.200  1.00 28.97  ? 291 TRP   A CA  1 
ATOM   688  C C   . TRP   A 1 85  ? 14.533 49.749 -6.082  1.00 26.09  ? 291 TRP   A C   1 
ATOM   689  O O   . TRP   A 1 85  ? 15.743 49.851 -5.857  1.00 25.23  ? 291 TRP   A O   1 
ATOM   690  C CB  . TRP   A 1 85  ? 13.799 51.981 -5.228  1.00 28.12  ? 291 TRP   A CB  1 
ATOM   691  C CG  . TRP   A 1 85  ? 12.662 52.788 -4.739  1.00 30.72  ? 291 TRP   A CG  1 
ATOM   692  C CD1 . TRP   A 1 85  ? 11.672 53.373 -5.487  1.00 34.07  ? 291 TRP   A CD1 1 
ATOM   693  C CD2 . TRP   A 1 85  ? 12.361 53.082 -3.369  1.00 30.95  ? 291 TRP   A CD2 1 
ATOM   694  N NE1 . TRP   A 1 85  ? 10.789 54.028 -4.663  1.00 32.60  ? 291 TRP   A NE1 1 
ATOM   695  C CE2 . TRP   A 1 85  ? 11.191 53.872 -3.359  1.00 33.42  ? 291 TRP   A CE2 1 
ATOM   696  C CE3 . TRP   A 1 85  ? 12.976 52.768 -2.151  1.00 26.89  ? 291 TRP   A CE3 1 
ATOM   697  C CZ2 . TRP   A 1 85  ? 10.621 54.349 -2.177  1.00 32.36  ? 291 TRP   A CZ2 1 
ATOM   698  C CZ3 . TRP   A 1 85  ? 12.401 53.242 -0.968  1.00 31.93  ? 291 TRP   A CZ3 1 
ATOM   699  C CH2 . TRP   A 1 85  ? 11.236 54.026 -0.997  1.00 29.28  ? 291 TRP   A CH2 1 
ATOM   700  N N   . ALA   A 1 86  ? 14.030 49.003 -7.061  1.00 24.58  ? 292 ALA   A N   1 
ATOM   701  C CA  . ALA   A 1 86  ? 14.866 48.166 -7.910  1.00 26.89  ? 292 ALA   A CA  1 
ATOM   702  C C   . ALA   A 1 86  ? 15.319 48.920 -9.149  1.00 32.62  ? 292 ALA   A C   1 
ATOM   703  O O   . ALA   A 1 86  ? 14.546 49.658 -9.767  1.00 29.69  ? 292 ALA   A O   1 
ATOM   704  C CB  . ALA   A 1 86  ? 14.120 46.902 -8.332  1.00 28.49  ? 292 ALA   A CB  1 
ATOM   705  N N   . ASP   A 1 87  ? 16.584 48.731 -9.505  1.00 26.63  ? 293 ASP   A N   1 
ATOM   706  C CA  . ASP   A 1 87  ? 17.166 49.347 -10.688 1.00 29.46  ? 293 ASP   A CA  1 
ATOM   707  C C   . ASP   A 1 87  ? 17.143 48.308 -11.797 1.00 32.46  ? 293 ASP   A C   1 
ATOM   708  O O   . ASP   A 1 87  ? 17.912 47.347 -11.763 1.00 26.99  ? 293 ASP   A O   1 
ATOM   709  C CB  . ASP   A 1 87  ? 18.592 49.818 -10.417 1.00 28.18  ? 293 ASP   A CB  1 
ATOM   710  C CG  . ASP   A 1 87  ? 19.222 50.541 -11.614 1.00 31.31  ? 293 ASP   A CG  1 
ATOM   711  O OD1 . ASP   A 1 87  ? 18.755 50.379 -12.756 1.00 31.48  ? 293 ASP   A OD1 1 
ATOM   712  O OD2 . ASP   A 1 87  ? 20.210 51.275 -11.403 1.00 34.44  ? 293 ASP   A OD2 1 
ATOM   713  N N   . LEU   A 1 88  ? 16.282 48.514 -12.787 1.00 31.08  ? 294 LEU   A N   1 
ATOM   714  C CA  . LEU   A 1 88  ? 16.159 47.600 -13.913 1.00 36.68  ? 294 LEU   A CA  1 
ATOM   715  C C   . LEU   A 1 88  ? 16.786 48.143 -15.194 1.00 37.02  ? 294 LEU   A C   1 
ATOM   716  O O   . LEU   A 1 88  ? 16.592 47.551 -16.259 1.00 40.84  ? 294 LEU   A O   1 
ATOM   717  C CB  . LEU   A 1 88  ? 14.685 47.272 -14.147 1.00 31.28  ? 294 LEU   A CB  1 
ATOM   718  C CG  . LEU   A 1 88  ? 13.912 46.691 -12.971 1.00 35.11  ? 294 LEU   A CG  1 
ATOM   719  C CD1 . LEU   A 1 88  ? 12.467 46.548 -13.366 1.00 41.54  ? 294 LEU   A CD1 1 
ATOM   720  C CD2 . LEU   A 1 88  ? 14.465 45.350 -12.576 1.00 38.59  ? 294 LEU   A CD2 1 
ATOM   721  N N   . ASN   A 1 89  ? 17.544 49.241 -15.117 1.00 39.38  ? 295 ASN   A N   1 
ATOM   722  C CA  . ASN   A 1 89  ? 18.225 49.823 -16.281 1.00 42.13  ? 295 ASN   A CA  1 
ATOM   723  C C   . ASN   A 1 89  ? 19.512 49.051 -16.528 1.00 33.91  ? 295 ASN   A C   1 
ATOM   724  O O   . ASN   A 1 89  ? 20.608 49.435 -16.119 1.00 41.14  ? 295 ASN   A O   1 
ATOM   725  C CB  . ASN   A 1 89  ? 18.522 51.295 -16.062 1.00 39.34  ? 295 ASN   A CB  1 
ATOM   726  C CG  . ASN   A 1 89  ? 17.270 52.111 -15.883 1.00 62.22  ? 295 ASN   A CG  1 
ATOM   727  O OD1 . ASN   A 1 89  ? 16.249 51.839 -16.523 1.00 68.32  ? 295 ASN   A OD1 1 
ATOM   728  N ND2 . ASN   A 1 89  ? 17.322 53.104 -14.986 1.00 55.21  ? 295 ASN   A ND2 1 
ATOM   729  N N   . CYS   A 1 90  ? 19.374 47.941 -17.224 1.00 37.73  ? 296 CYS   A N   1 
ATOM   730  C CA  A CYS   A 1 90  ? 20.503 47.062 -17.490 0.55 40.30  ? 296 CYS   A CA  1 
ATOM   731  C CA  B CYS   A 1 90  ? 20.525 47.110 -17.521 0.45 40.32  ? 296 CYS   A CA  1 
ATOM   732  C C   . CYS   A 1 90  ? 20.287 46.391 -18.838 1.00 44.32  ? 296 CYS   A C   1 
ATOM   733  O O   . CYS   A 1 90  ? 19.193 45.890 -19.106 1.00 47.49  ? 296 CYS   A O   1 
ATOM   734  C CB  A CYS   A 1 90  ? 20.637 46.019 -16.376 0.55 40.86  ? 296 CYS   A CB  1 
ATOM   735  C CB  B CYS   A 1 90  ? 20.803 46.128 -16.376 0.45 40.85  ? 296 CYS   A CB  1 
ATOM   736  S SG  A CYS   A 1 90  ? 21.848 44.715 -16.652 0.55 36.46  ? 296 CYS   A SG  1 
ATOM   737  S SG  B CYS   A 1 90  ? 19.811 44.627 -16.361 0.45 41.40  ? 296 CYS   A SG  1 
ATOM   738  N N   . ASN   A 1 91  ? 21.312 46.388 -19.677 1.00 50.23  ? 297 ASN   A N   1 
ATOM   739  C CA  . ASN   A 1 91  ? 21.255 45.695 -20.956 1.00 46.54  ? 297 ASN   A CA  1 
ATOM   740  C C   . ASN   A 1 91  ? 21.597 44.230 -20.744 1.00 47.66  ? 297 ASN   A C   1 
ATOM   741  O O   . ASN   A 1 91  ? 22.745 43.893 -20.438 1.00 48.43  ? 297 ASN   A O   1 
ATOM   742  C CB  . ASN   A 1 91  ? 22.208 46.334 -21.960 1.00 53.80  ? 297 ASN   A CB  1 
ATOM   743  C CG  . ASN   A 1 91  ? 22.139 45.665 -23.306 1.00 61.10  ? 297 ASN   A CG  1 
ATOM   744  O OD1 . ASN   A 1 91  ? 21.103 45.106 -23.676 1.00 62.21  ? 297 ASN   A OD1 1 
ATOM   745  N ND2 . ASN   A 1 91  ? 23.250 45.688 -24.041 1.00 72.89  ? 297 ASN   A ND2 1 
ATOM   746  N N   . ILE   A 1 92  ? 20.615 43.353 -20.927 1.00 41.36  ? 298 ILE   A N   1 
ATOM   747  C CA  . ILE   A 1 92  ? 20.840 41.922 -20.775 1.00 48.16  ? 298 ILE   A CA  1 
ATOM   748  C C   . ILE   A 1 92  ? 21.264 41.405 -22.149 1.00 56.54  ? 298 ILE   A C   1 
ATOM   749  O O   . ILE   A 1 92  ? 20.437 41.223 -23.044 1.00 54.49  ? 298 ILE   A O   1 
ATOM   750  C CB  . ILE   A 1 92  ? 19.606 41.203 -20.231 1.00 49.26  ? 298 ILE   A CB  1 
ATOM   751  C CG1 . ILE   A 1 92  ? 19.260 41.757 -18.851 1.00 42.75  ? 298 ILE   A CG1 1 
ATOM   752  C CG2 . ILE   A 1 92  ? 19.893 39.718 -20.059 1.00 55.02  ? 298 ILE   A CG2 1 
ATOM   753  C CD1 . ILE   A 1 92  ? 17.945 41.277 -18.295 1.00 49.98  ? 298 ILE   A CD1 1 
ATOM   754  N N   . GLN   A 1 93  ? 22.572 41.200 -22.318 1.00 56.37  ? 299 GLN   A N   1 
ATOM   755  C CA  . GLN   A 1 93  ? 23.193 40.804 -23.587 1.00 64.97  ? 299 GLN   A CA  1 
ATOM   756  C C   . GLN   A 1 93  ? 22.907 39.357 -23.971 1.00 61.51  ? 299 GLN   A C   1 
ATOM   757  O O   . GLN   A 1 93  ? 22.735 38.499 -23.112 1.00 55.40  ? 299 GLN   A O   1 
ATOM   758  C CB  . GLN   A 1 93  ? 24.712 41.032 -23.518 1.00 62.90  ? 299 GLN   A CB  1 
ATOM   759  C CG  . GLN   A 1 93  ? 25.113 42.446 -23.067 1.00 71.80  ? 299 GLN   A CG  1 
ATOM   760  C CD  . GLN   A 1 93  ? 26.534 42.539 -22.510 1.00 63.87  ? 299 GLN   A CD  1 
ATOM   761  O OE1 . GLN   A 1 93  ? 27.420 41.779 -22.896 1.00 73.64  ? 299 GLN   A OE1 1 
ATOM   762  N NE2 . GLN   A 1 93  ? 26.750 43.485 -21.599 1.00 68.08  ? 299 GLN   A NE2 1 
ATOM   763  N N   . GLY   A 1 97  ? 27.617 35.242 -21.549 1.00 42.40  ? 303 GLY   A N   1 
ATOM   764  C CA  . GLY   A 1 97  ? 27.985 34.620 -20.291 1.00 47.00  ? 303 GLY   A CA  1 
ATOM   765  C C   . GLY   A 1 97  ? 27.443 35.466 -19.143 1.00 52.01  ? 303 GLY   A C   1 
ATOM   766  O O   . GLY   A 1 97  ? 27.913 36.593 -18.960 1.00 45.79  ? 303 GLY   A O   1 
ATOM   767  N N   . ALA   A 1 98  ? 26.452 34.945 -18.401 1.00 35.39  ? 304 ALA   A N   1 
ATOM   768  C CA  . ALA   A 1 98  ? 25.715 35.726 -17.407 1.00 32.25  ? 304 ALA   A CA  1 
ATOM   769  C C   . ALA   A 1 98  ? 25.548 34.941 -16.120 1.00 33.70  ? 304 ALA   A C   1 
ATOM   770  O O   . ALA   A 1 98  ? 25.250 33.746 -16.140 1.00 36.40  ? 304 ALA   A O   1 
ATOM   771  C CB  . ALA   A 1 98  ? 24.333 36.156 -17.907 1.00 30.47  ? 304 ALA   A CB  1 
ATOM   772  N N   . PHE   A 1 99  ? 25.745 35.617 -14.993 1.00 30.54  ? 305 PHE   A N   1 
ATOM   773  C CA  . PHE   A 1 99  ? 25.527 35.022 -13.682 1.00 28.59  ? 305 PHE   A CA  1 
ATOM   774  C C   . PHE   A 1 99  ? 24.619 35.955 -12.894 1.00 31.91  ? 305 PHE   A C   1 
ATOM   775  O O   . PHE   A 1 99  ? 24.969 37.118 -12.664 1.00 26.16  ? 305 PHE   A O   1 
ATOM   776  C CB  . PHE   A 1 99  ? 26.849 34.790 -12.935 1.00 29.31  ? 305 PHE   A CB  1 
ATOM   777  C CG  . PHE   A 1 99  ? 26.667 34.204 -11.564 1.00 31.81  ? 305 PHE   A CG  1 
ATOM   778  C CD1 . PHE   A 1 99  ? 26.366 32.859 -11.408 1.00 27.67  ? 305 PHE   A CD1 1 
ATOM   779  C CD2 . PHE   A 1 99  ? 26.724 35.009 -10.426 1.00 28.72  ? 305 PHE   A CD2 1 
ATOM   780  C CE1 . PHE   A 1 99  ? 26.168 32.307 -10.143 1.00 29.45  ? 305 PHE   A CE1 1 
ATOM   781  C CE2 . PHE   A 1 99  ? 26.523 34.461 -9.158  1.00 30.50  ? 305 PHE   A CE2 1 
ATOM   782  C CZ  . PHE   A 1 99  ? 26.244 33.108 -9.013  1.00 28.33  ? 305 PHE   A CZ  1 
ATOM   783  N N   . TYR   A 1 100 ? 23.449 35.457 -12.513 1.00 23.47  ? 306 TYR   A N   1 
ATOM   784  C CA  . TYR   A 1 100 ? 22.519 36.174 -11.657 1.00 27.09  ? 306 TYR   A CA  1 
ATOM   785  C C   . TYR   A 1 100 ? 22.785 35.678 -10.252 1.00 27.09  ? 306 TYR   A C   1 
ATOM   786  O O   . TYR   A 1 100 ? 22.762 34.472 -10.020 1.00 28.85  ? 306 TYR   A O   1 
ATOM   787  C CB  . TYR   A 1 100 ? 21.065 35.896 -12.058 1.00 23.48  ? 306 TYR   A CB  1 
ATOM   788  C CG  . TYR   A 1 100 ? 20.683 36.435 -13.401 1.00 24.58  ? 306 TYR   A CG  1 
ATOM   789  C CD1 . TYR   A 1 100 ? 21.011 35.747 -14.563 1.00 27.18  ? 306 TYR   A CD1 1 
ATOM   790  C CD2 . TYR   A 1 100 ? 19.978 37.624 -13.524 1.00 27.62  ? 306 TYR   A CD2 1 
ATOM   791  C CE1 . TYR   A 1 100 ? 20.653 36.239 -15.802 1.00 30.82  ? 306 TYR   A CE1 1 
ATOM   792  C CE2 . TYR   A 1 100 ? 19.620 38.119 -14.751 1.00 27.44  ? 306 TYR   A CE2 1 
ATOM   793  C CZ  . TYR   A 1 100 ? 19.949 37.414 -15.894 1.00 31.64  ? 306 TYR   A CZ  1 
ATOM   794  O OH  . TYR   A 1 100 ? 19.594 37.909 -17.125 1.00 33.99  ? 306 TYR   A OH  1 
ATOM   795  N N   . GLY   A 1 101 ? 23.069 36.593 -9.320  1.00 26.44  ? 307 GLY   A N   1 
ATOM   796  C CA  . GLY   A 1 101 ? 23.481 36.191 -7.991  1.00 26.08  ? 307 GLY   A CA  1 
ATOM   797  C C   . GLY   A 1 101 ? 22.899 37.066 -6.892  1.00 27.93  ? 307 GLY   A C   1 
ATOM   798  O O   . GLY   A 1 101 ? 22.366 38.148 -7.141  1.00 25.68  ? 307 GLY   A O   1 
ATOM   799  N N   . VAL   A 1 102 ? 23.010 36.558 -5.661  1.00 25.35  ? 308 VAL   A N   1 
ATOM   800  C CA  . VAL   A 1 102 ? 22.581 37.259 -4.453  1.00 28.52  ? 308 VAL   A CA  1 
ATOM   801  C C   . VAL   A 1 102 ? 23.712 37.181 -3.427  1.00 30.88  ? 308 VAL   A C   1 
ATOM   802  O O   . VAL   A 1 102 ? 24.288 36.110 -3.205  1.00 32.84  ? 308 VAL   A O   1 
ATOM   803  C CB  . VAL   A 1 102 ? 21.284 36.658 -3.867  1.00 26.81  ? 308 VAL   A CB  1 
ATOM   804  C CG1 . VAL   A 1 102 ? 20.846 37.448 -2.665  1.00 33.82  ? 308 VAL   A CG1 1 
ATOM   805  C CG2 . VAL   A 1 102 ? 20.169 36.672 -4.910  1.00 27.37  ? 308 VAL   A CG2 1 
ATOM   806  N N   . THR   A 1 103 ? 24.026 38.304 -2.796  1.00 28.05  ? 309 THR   A N   1 
ATOM   807  C CA  . THR   A 1 103 ? 25.042 38.312 -1.751  1.00 34.26  ? 309 THR   A CA  1 
ATOM   808  C C   . THR   A 1 103 ? 24.473 38.964 -0.499  1.00 30.54  ? 309 THR   A C   1 
ATOM   809  O O   . THR   A 1 103 ? 23.746 39.954 -0.585  1.00 28.29  ? 309 THR   A O   1 
ATOM   810  C CB  . THR   A 1 103 ? 26.292 39.036 -2.238  1.00 30.52  ? 309 THR   A CB  1 
ATOM   811  O OG1 . THR   A 1 103 ? 26.966 38.193 -3.177  1.00 33.36  ? 309 THR   A OG1 1 
ATOM   812  C CG2 . THR   A 1 103 ? 27.245 39.348 -1.098  1.00 31.92  ? 309 THR   A CG2 1 
ATOM   813  N N   . SER   A 1 104 ? 24.773 38.393 0.664   1.00 30.26  ? 310 SER   A N   1 
ATOM   814  C CA  . SER   A 1 104 ? 24.355 39.057 1.887   1.00 26.48  ? 310 SER   A CA  1 
ATOM   815  C C   . SER   A 1 104 ? 25.354 38.780 3.000   1.00 32.29  ? 310 SER   A C   1 
ATOM   816  O O   . SER   A 1 104 ? 26.066 37.767 2.991   1.00 29.51  ? 310 SER   A O   1 
ATOM   817  C CB  . SER   A 1 104 ? 22.929 38.654 2.298   1.00 29.58  ? 310 SER   A CB  1 
ATOM   818  O OG  . SER   A 1 104 ? 22.764 37.265 2.310   1.00 37.33  ? 310 SER   A OG  1 
ATOM   819  N N   . GLN   A 1 105 ? 25.419 39.716 3.951   1.00 28.62  ? 311 GLN   A N   1 
ATOM   820  C CA  . GLN   A 1 105 ? 26.298 39.557 5.097   1.00 26.12  ? 311 GLN   A CA  1 
ATOM   821  C C   . GLN   A 1 105 ? 25.589 40.055 6.349   1.00 27.63  ? 311 GLN   A C   1 
ATOM   822  O O   . GLN   A 1 105 ? 24.987 41.133 6.350   1.00 28.64  ? 311 GLN   A O   1 
ATOM   823  C CB  . GLN   A 1 105 ? 27.629 40.294 4.894   1.00 26.37  ? 311 GLN   A CB  1 
ATOM   824  C CG  . GLN   A 1 105 ? 28.486 40.305 6.150   1.00 30.27  ? 311 GLN   A CG  1 
ATOM   825  C CD  . GLN   A 1 105 ? 29.908 40.700 5.873   1.00 34.33  ? 311 GLN   A CD  1 
ATOM   826  O OE1 . GLN   A 1 105 ? 30.498 40.264 4.889   1.00 38.52  ? 311 GLN   A OE1 1 
ATOM   827  N NE2 . GLN   A 1 105 ? 30.474 41.525 6.741   1.00 34.48  ? 311 GLN   A NE2 1 
ATOM   828  N N   . TYR   A 1 106 ? 25.624 39.233 7.385   1.00 23.99  ? 312 TYR   A N   1 
ATOM   829  C CA  . TYR   A 1 106 ? 25.107 39.559 8.699   1.00 24.05  ? 312 TYR   A CA  1 
ATOM   830  C C   . TYR   A 1 106 ? 26.272 39.605 9.678   1.00 26.18  ? 312 TYR   A C   1 
ATOM   831  O O   . TYR   A 1 106 ? 27.317 38.989 9.448   1.00 25.80  ? 312 TYR   A O   1 
ATOM   832  C CB  . TYR   A 1 106 ? 24.084 38.515 9.158   1.00 23.89  ? 312 TYR   A CB  1 
ATOM   833  C CG  . TYR   A 1 106 ? 22.937 38.312 8.190   1.00 26.27  ? 312 TYR   A CG  1 
ATOM   834  C CD1 . TYR   A 1 106 ? 23.054 37.435 7.114   1.00 31.88  ? 312 TYR   A CD1 1 
ATOM   835  C CD2 . TYR   A 1 106 ? 21.735 38.970 8.365   1.00 27.93  ? 312 TYR   A CD2 1 
ATOM   836  C CE1 . TYR   A 1 106 ? 21.997 37.228 6.222   1.00 32.35  ? 312 TYR   A CE1 1 
ATOM   837  C CE2 . TYR   A 1 106 ? 20.667 38.772 7.483   1.00 34.42  ? 312 TYR   A CE2 1 
ATOM   838  C CZ  . TYR   A 1 106 ? 20.806 37.900 6.416   1.00 40.34  ? 312 TYR   A CZ  1 
ATOM   839  O OH  . TYR   A 1 106 ? 19.754 37.716 5.538   1.00 41.67  ? 312 TYR   A OH  1 
ATOM   840  N N   . GLU   A 1 107 ? 26.069 40.314 10.790  1.00 24.32  ? 313 GLU   A N   1 
ATOM   841  C CA  . GLU   A 1 107 ? 27.085 40.450 11.831  1.00 29.97  ? 313 GLU   A CA  1 
ATOM   842  C C   . GLU   A 1 107 ? 26.447 40.369 13.198  1.00 31.53  ? 313 GLU   A C   1 
ATOM   843  O O   . GLU   A 1 107 ? 25.310 40.811 13.403  1.00 28.75  ? 313 GLU   A O   1 
ATOM   844  C CB  . GLU   A 1 107 ? 27.859 41.759 11.752  1.00 28.15  ? 313 GLU   A CB  1 
ATOM   845  C CG  . GLU   A 1 107 ? 28.791 41.786 10.575  1.00 41.62  ? 313 GLU   A CG  1 
ATOM   846  C CD  . GLU   A 1 107 ? 29.389 43.144 10.318  1.00 41.72  ? 313 GLU   A CD  1 
ATOM   847  O OE1 . GLU   A 1 107 ? 29.272 44.025 11.197  1.00 46.92  ? 313 GLU   A OE1 1 
ATOM   848  O OE2 . GLU   A 1 107 ? 30.014 43.300 9.246   1.00 45.03  ? 313 GLU   A OE2 1 
ATOM   849  N N   A SER   A 1 108 ? 27.205 39.811 14.135  0.53 28.90  ? 314 SER   A N   1 
ATOM   850  N N   B SER   A 1 108 ? 27.205 39.817 14.144  0.47 29.52  ? 314 SER   A N   1 
ATOM   851  C CA  A SER   A 1 108 ? 26.749 39.656 15.502  0.53 32.93  ? 314 SER   A CA  1 
ATOM   852  C CA  B SER   A 1 108 ? 26.722 39.613 15.499  0.47 33.12  ? 314 SER   A CA  1 
ATOM   853  C C   A SER   A 1 108 ? 27.929 39.736 16.457  0.53 34.92  ? 314 SER   A C   1 
ATOM   854  C C   B SER   A 1 108 ? 27.893 39.611 16.476  0.47 34.89  ? 314 SER   A C   1 
ATOM   855  O O   A SER   A 1 108 ? 29.093 39.558 16.076  0.53 30.94  ? 314 SER   A O   1 
ATOM   856  O O   B SER   A 1 108 ? 29.030 39.280 16.120  0.47 31.13  ? 314 SER   A O   1 
ATOM   857  C CB  A SER   A 1 108 ? 26.017 38.332 15.706  0.53 33.13  ? 314 SER   A CB  1 
ATOM   858  C CB  B SER   A 1 108 ? 25.923 38.309 15.604  0.47 33.13  ? 314 SER   A CB  1 
ATOM   859  O OG  A SER   A 1 108 ? 25.608 38.214 17.055  0.53 34.41  ? 314 SER   A OG  1 
ATOM   860  O OG  B SER   A 1 108 ? 26.762 37.181 15.774  0.47 32.49  ? 314 SER   A OG  1 
ATOM   861  N N   . SER   A 1 109 ? 27.598 40.019 17.712  1.00 33.52  ? 315 SER   A N   1 
ATOM   862  C CA  . SER   A 1 109 ? 28.550 39.948 18.804  1.00 41.57  ? 315 SER   A CA  1 
ATOM   863  C C   . SER   A 1 109 ? 28.651 38.547 19.374  1.00 36.99  ? 315 SER   A C   1 
ATOM   864  O O   . SER   A 1 109 ? 29.615 38.245 20.075  1.00 42.93  ? 315 SER   A O   1 
ATOM   865  C CB  . SER   A 1 109 ? 28.127 40.911 19.916  1.00 44.31  ? 315 SER   A CB  1 
ATOM   866  O OG  . SER   A 1 109 ? 26.762 40.669 20.256  1.00 61.51  ? 315 SER   A OG  1 
ATOM   867  N N   . GLU   A 1 110 ? 27.677 37.691 19.100  1.00 37.78  ? 316 GLU   A N   1 
ATOM   868  C CA  . GLU   A 1 110 ? 27.659 36.345 19.635  1.00 41.18  ? 316 GLU   A CA  1 
ATOM   869  C C   . GLU   A 1 110 ? 28.007 35.327 18.557  1.00 40.74  ? 316 GLU   A C   1 
ATOM   870  O O   . GLU   A 1 110 ? 27.713 35.521 17.370  1.00 38.98  ? 316 GLU   A O   1 
ATOM   871  C CB  . GLU   A 1 110 ? 26.294 36.028 20.241  1.00 44.54  ? 316 GLU   A CB  1 
ATOM   872  C CG  . GLU   A 1 110 ? 25.914 36.983 21.346  1.00 61.65  ? 316 GLU   A CG  1 
ATOM   873  C CD  . GLU   A 1 110 ? 25.064 36.324 22.402  1.00 81.48  ? 316 GLU   A CD  1 
ATOM   874  O OE1 . GLU   A 1 110 ? 25.396 36.476 23.600  1.00 92.04  ? 316 GLU   A OE1 1 
ATOM   875  O OE2 . GLU   A 1 110 ? 24.069 35.657 22.037  1.00 85.34  ? 316 GLU   A OE2 1 
ATOM   876  N N   . ASN   A 1 111 ? 28.665 34.252 18.987  1.00 37.95  ? 317 ASN   A N   1 
ATOM   877  C CA  . ASN   A 1 111 ? 29.027 33.146 18.108  1.00 35.75  ? 317 ASN   A CA  1 
ATOM   878  C C   . ASN   A 1 111 ? 27.826 32.212 18.011  1.00 39.08  ? 317 ASN   A C   1 
ATOM   879  O O   . ASN   A 1 111 ? 27.455 31.569 18.992  1.00 39.37  ? 317 ASN   A O   1 
ATOM   880  C CB  . ASN   A 1 111 ? 30.265 32.434 18.653  1.00 34.41  ? 317 ASN   A CB  1 
ATOM   881  C CG  . ASN   A 1 111 ? 30.782 31.345 17.717  1.00 49.10  ? 317 ASN   A CG  1 
ATOM   882  O OD1 . ASN   A 1 111 ? 30.141 31.003 16.733  1.00 40.37  ? 317 ASN   A OD1 1 
ATOM   883  N ND2 . ASN   A 1 111 ? 31.953 30.802 18.028  1.00 57.91  ? 317 ASN   A ND2 1 
ATOM   884  N N   . MET   A 1 112 ? 27.215 32.150 16.832  1.00 29.62  ? 318 MET   A N   1 
ATOM   885  C CA  . MET   A 1 112 ? 25.948 31.466 16.601  1.00 31.92  ? 318 MET   A CA  1 
ATOM   886  C C   . MET   A 1 112 ? 26.042 30.743 15.276  1.00 34.04  ? 318 MET   A C   1 
ATOM   887  O O   . MET   A 1 112 ? 26.852 31.094 14.423  1.00 33.00  ? 318 MET   A O   1 
ATOM   888  C CB  . MET   A 1 112 ? 24.790 32.455 16.484  1.00 34.73  ? 318 MET   A CB  1 
ATOM   889  C CG  . MET   A 1 112 ? 24.591 33.345 17.649  1.00 35.38  ? 318 MET   A CG  1 
ATOM   890  S SD  . MET   A 1 112 ? 23.053 34.223 17.443  1.00 40.10  ? 318 MET   A SD  1 
ATOM   891  C CE  . MET   A 1 112 ? 23.721 35.576 16.505  1.00 30.13  ? 318 MET   A CE  1 
ATOM   892  N N   . THR   A 1 113 ? 25.196 29.743 15.101  1.00 31.09  ? 319 THR   A N   1 
ATOM   893  C CA  . THR   A 1 113 ? 24.901 29.206 13.788  1.00 32.33  ? 319 THR   A CA  1 
ATOM   894  C C   . THR   A 1 113 ? 23.519 29.732 13.414  1.00 28.81  ? 319 THR   A C   1 
ATOM   895  O O   . THR   A 1 113 ? 22.589 29.628 14.216  1.00 31.30  ? 319 THR   A O   1 
ATOM   896  C CB  . THR   A 1 113 ? 24.928 27.677 13.808  1.00 33.46  ? 319 THR   A CB  1 
ATOM   897  O OG1 . THR   A 1 113 ? 26.264 27.245 14.066  1.00 37.75  ? 319 THR   A OG1 1 
ATOM   898  C CG2 . THR   A 1 113 ? 24.540 27.132 12.447  1.00 39.07  ? 319 THR   A CG2 1 
ATOM   899  N N   . VAL   A 1 114 ? 23.396 30.353 12.243  1.00 27.74  ? 320 VAL   A N   1 
ATOM   900  C CA  . VAL   A 1 114 ? 22.131 30.968 11.854  1.00 32.34  ? 320 VAL   A CA  1 
ATOM   901  C C   . VAL   A 1 114 ? 21.563 30.271 10.626  1.00 32.24  ? 320 VAL   A C   1 
ATOM   902  O O   . VAL   A 1 114 ? 22.291 29.701 9.808   1.00 31.97  ? 320 VAL   A O   1 
ATOM   903  C CB  . VAL   A 1 114 ? 22.258 32.493 11.591  1.00 31.86  ? 320 VAL   A CB  1 
ATOM   904  C CG1 . VAL   A 1 114 ? 22.778 33.207 12.813  1.00 25.59  ? 320 VAL   A CG1 1 
ATOM   905  C CG2 . VAL   A 1 114 ? 23.158 32.755 10.392  1.00 26.68  ? 320 VAL   A CG2 1 
ATOM   906  N N   . THR   A 1 115 ? 20.240 30.323 10.497  1.00 25.58  ? 321 THR   A N   1 
ATOM   907  C CA  . THR   A 1 115 ? 19.568 29.873 9.289   1.00 32.12  ? 321 THR   A CA  1 
ATOM   908  C C   . THR   A 1 115 ? 18.857 31.067 8.688   1.00 33.20  ? 321 THR   A C   1 
ATOM   909  O O   . THR   A 1 115 ? 18.151 31.790 9.399   1.00 33.23  ? 321 THR   A O   1 
ATOM   910  C CB  . THR   A 1 115 ? 18.552 28.758 9.565   1.00 37.04  ? 321 THR   A CB  1 
ATOM   911  O OG1 . THR   A 1 115 ? 17.588 29.224 10.512  1.00 48.17  ? 321 THR   A OG1 1 
ATOM   912  C CG2 . THR   A 1 115 ? 19.251 27.547 10.137  1.00 38.14  ? 321 THR   A CG2 1 
ATOM   913  N N   . CYS   A 1 116 ? 19.047 31.281 7.393   1.00 29.48  ? 322 CYS   A N   1 
ATOM   914  C CA  A CYS   A 1 116 ? 18.404 32.375 6.680   0.45 31.61  ? 322 CYS   A CA  1 
ATOM   915  C CA  B CYS   A 1 116 ? 18.415 32.376 6.674   0.55 31.63  ? 322 CYS   A CA  1 
ATOM   916  C C   . CYS   A 1 116 ? 17.382 31.802 5.710   1.00 32.04  ? 322 CYS   A C   1 
ATOM   917  O O   . CYS   A 1 116 ? 17.742 31.101 4.760   1.00 32.03  ? 322 CYS   A O   1 
ATOM   918  C CB  A CYS   A 1 116 ? 19.416 33.240 5.932   0.45 32.65  ? 322 CYS   A CB  1 
ATOM   919  C CB  B CYS   A 1 116 ? 19.465 33.201 5.933   0.55 32.63  ? 322 CYS   A CB  1 
ATOM   920  S SG  A CYS   A 1 116 ? 18.627 34.561 4.977   0.45 41.04  ? 322 CYS   A SG  1 
ATOM   921  S SG  B CYS   A 1 116 ? 20.894 33.652 6.967   0.55 34.56  ? 322 CYS   A SG  1 
ATOM   922  N N   . SER   A 1 117 ? 16.114 32.111 5.948   1.00 29.18  ? 323 SER   A N   1 
ATOM   923  C CA  . SER   A 1 117 ? 15.018 31.661 5.108   1.00 31.94  ? 323 SER   A CA  1 
ATOM   924  C C   . SER   A 1 117 ? 14.548 32.806 4.213   1.00 29.68  ? 323 SER   A C   1 
ATOM   925  O O   . SER   A 1 117 ? 14.220 33.888 4.703   1.00 31.11  ? 323 SER   A O   1 
ATOM   926  C CB  . SER   A 1 117 ? 13.872 31.140 5.981   1.00 27.36  ? 323 SER   A CB  1 
ATOM   927  O OG  . SER   A 1 117 ? 12.691 30.994 5.214   1.00 38.81  ? 323 SER   A OG  1 
ATOM   928  N N   . THR   A 1 118 ? 14.531 32.572 2.905   1.00 26.91  ? 324 THR   A N   1 
ATOM   929  C CA  . THR   A 1 118 ? 14.052 33.530 1.916   1.00 28.60  ? 324 THR   A CA  1 
ATOM   930  C C   . THR   A 1 118 ? 12.806 32.938 1.283   1.00 33.17  ? 324 THR   A C   1 
ATOM   931  O O   . THR   A 1 118 ? 12.888 31.884 0.642   1.00 33.63  ? 324 THR   A O   1 
ATOM   932  C CB  . THR   A 1 118 ? 15.097 33.779 0.822   1.00 32.74  ? 324 THR   A CB  1 
ATOM   933  O OG1 . THR   A 1 118 ? 16.337 34.177 1.412   1.00 34.94  ? 324 THR   A OG1 1 
ATOM   934  C CG2 . THR   A 1 118 ? 14.600 34.852 -0.191  1.00 26.90  ? 324 THR   A CG2 1 
ATOM   935  N N   . LYS   A 1 119 ? 11.668 33.608 1.445   1.00 25.37  ? 325 LYS   A N   1 
ATOM   936  C CA  . LYS   A 1 119 ? 10.414 33.180 0.831   1.00 28.69  ? 325 LYS   A CA  1 
ATOM   937  C C   . LYS   A 1 119 ? 9.978  34.234 -0.174  1.00 29.32  ? 325 LYS   A C   1 
ATOM   938  O O   . LYS   A 1 119 ? 9.696  35.374 0.203   1.00 30.89  ? 325 LYS   A O   1 
ATOM   939  C CB  . LYS   A 1 119 ? 9.340  32.961 1.893   1.00 28.29  ? 325 LYS   A CB  1 
ATOM   940  C CG  . LYS   A 1 119 ? 9.520  31.664 2.649   1.00 31.26  ? 325 LYS   A CG  1 
ATOM   941  C CD  . LYS   A 1 119 ? 8.578  31.563 3.823   1.00 43.53  ? 325 LYS   A CD  1 
ATOM   942  C CE  . LYS   A 1 119 ? 8.819  30.267 4.580   1.00 40.42  ? 325 LYS   A CE  1 
ATOM   943  N NZ  . LYS   A 1 119 ? 8.032  30.200 5.834   1.00 53.98  ? 325 LYS   A NZ  1 
ATOM   944  N N   . VAL   A 1 120 ? 9.926  33.855 -1.441  1.00 28.95  ? 326 VAL   A N   1 
ATOM   945  C CA  . VAL   A 1 120 ? 9.463  34.731 -2.501  1.00 30.43  ? 326 VAL   A CA  1 
ATOM   946  C C   . VAL   A 1 120 ? 7.960  34.518 -2.653  1.00 30.27  ? 326 VAL   A C   1 
ATOM   947  O O   . VAL   A 1 120 ? 7.498  33.379 -2.754  1.00 29.17  ? 326 VAL   A O   1 
ATOM   948  C CB  . VAL   A 1 120 ? 10.203 34.437 -3.812  1.00 31.07  ? 326 VAL   A CB  1 
ATOM   949  C CG1 . VAL   A 1 120 ? 9.629  35.259 -4.919  1.00 31.03  ? 326 VAL   A CG1 1 
ATOM   950  C CG2 . VAL   A 1 120 ? 11.718 34.651 -3.663  1.00 32.64  ? 326 VAL   A CG2 1 
ATOM   951  N N   . CYS   A 1 121 ? 7.194  35.604 -2.641  1.00 27.66  ? 327 CYS   A N   1 
ATOM   952  C CA  . CYS   A 1 121 ? 5.744  35.518 -2.563  1.00 28.27  ? 327 CYS   A CA  1 
ATOM   953  C C   . CYS   A 1 121 ? 5.061  36.274 -3.682  1.00 35.40  ? 327 CYS   A C   1 
ATOM   954  O O   . CYS   A 1 121 ? 5.491  37.356 -4.088  1.00 32.91  ? 327 CYS   A O   1 
ATOM   955  C CB  . CYS   A 1 121 ? 5.206  36.007 -1.224  1.00 30.77  ? 327 CYS   A CB  1 
ATOM   956  S SG  . CYS   A 1 121 ? 5.958  35.202 0.156   1.00 37.52  ? 327 CYS   A SG  1 
ATOM   957  N N   . SER   A 1 122 ? 3.981  35.679 -4.171  1.00 32.46  ? 328 SER   A N   1 
ATOM   958  C CA  . SER   A 1 122 ? 3.161  36.259 -5.222  1.00 36.91  ? 328 SER   A CA  1 
ATOM   959  C C   . SER   A 1 122 ? 1.737  36.326 -4.696  1.00 39.31  ? 328 SER   A C   1 
ATOM   960  O O   . SER   A 1 122 ? 1.180  35.302 -4.292  1.00 39.99  ? 328 SER   A O   1 
ATOM   961  C CB  . SER   A 1 122 ? 3.234  35.418 -6.495  1.00 39.03  ? 328 SER   A CB  1 
ATOM   962  O OG  . SER   A 1 122 ? 2.587  36.074 -7.555  1.00 39.78  ? 328 SER   A OG  1 
ATOM   963  N N   . PHE   A 1 123 ? 1.166  37.531 -4.665  1.00 38.35  ? 329 PHE   A N   1 
ATOM   964  C CA  . PHE   A 1 123 ? -0.166 37.739 -4.095  1.00 36.07  ? 329 PHE   A CA  1 
ATOM   965  C C   . PHE   A 1 123 ? -0.249 37.197 -2.676  1.00 41.00  ? 329 PHE   A C   1 
ATOM   966  O O   . PHE   A 1 123 ? -1.256 36.618 -2.270  1.00 41.26  ? 329 PHE   A O   1 
ATOM   967  C CB  . PHE   A 1 123 ? -1.252 37.120 -4.989  1.00 37.72  ? 329 PHE   A CB  1 
ATOM   968  C CG  . PHE   A 1 123 ? -1.456 37.881 -6.259  1.00 35.17  ? 329 PHE   A CG  1 
ATOM   969  C CD1 . PHE   A 1 123 ? -0.710 37.591 -7.379  1.00 37.98  ? 329 PHE   A CD1 1 
ATOM   970  C CD2 . PHE   A 1 123 ? -2.312 38.969 -6.292  1.00 39.31  ? 329 PHE   A CD2 1 
ATOM   971  C CE1 . PHE   A 1 123 ? -0.862 38.322 -8.536  1.00 41.25  ? 329 PHE   A CE1 1 
ATOM   972  C CE2 . PHE   A 1 123 ? -2.460 39.706 -7.445  1.00 41.15  ? 329 PHE   A CE2 1 
ATOM   973  C CZ  . PHE   A 1 123 ? -1.728 39.385 -8.566  1.00 38.43  ? 329 PHE   A CZ  1 
ATOM   974  N N   . GLY   A 1 124 ? 0.831  37.373 -1.911  1.00 37.39  ? 330 GLY   A N   1 
ATOM   975  C CA  . GLY   A 1 124 ? 0.853  36.945 -0.525  1.00 37.66  ? 330 GLY   A CA  1 
ATOM   976  C C   . GLY   A 1 124 ? 1.126  35.474 -0.287  1.00 40.36  ? 330 GLY   A C   1 
ATOM   977  O O   . GLY   A 1 124 ? 1.233  35.062 0.874   1.00 42.23  ? 330 GLY   A O   1 
ATOM   978  N N   . LYS   A 1 125 ? 1.263  34.667 -1.333  1.00 37.76  ? 331 LYS   A N   1 
ATOM   979  C CA  . LYS   A 1 125 ? 1.498  33.236 -1.176  1.00 41.85  ? 331 LYS   A CA  1 
ATOM   980  C C   . LYS   A 1 125 ? 2.914  32.876 -1.609  1.00 35.78  ? 331 LYS   A C   1 
ATOM   981  O O   . LYS   A 1 125 ? 3.398  33.356 -2.635  1.00 34.55  ? 331 LYS   A O   1 
ATOM   982  C CB  . LYS   A 1 125 ? 0.493  32.425 -1.996  1.00 39.98  ? 331 LYS   A CB  1 
ATOM   983  C CG  . LYS   A 1 125 ? -0.941 32.933 -1.899  1.00 52.69  ? 331 LYS   A CG  1 
ATOM   984  C CD  . LYS   A 1 125 ? -1.889 31.856 -1.371  1.00 53.10  ? 331 LYS   A CD  1 
ATOM   985  C CE  . LYS   A 1 125 ? -3.316 32.380 -1.311  0.00 52.18  ? 331 LYS   A CE  1 
ATOM   986  N NZ  . LYS   A 1 125 ? -3.429 33.606 -0.471  0.00 51.46  ? 331 LYS   A NZ  1 
ATOM   987  N N   . GLN   A 1 126 ? 3.551  32.002 -0.837  1.00 35.92  ? 332 GLN   A N   1 
ATOM   988  C CA  . GLN   A 1 126 ? 4.898  31.546 -1.150  1.00 36.83  ? 332 GLN   A CA  1 
ATOM   989  C C   . GLN   A 1 126 ? 4.915  30.782 -2.462  1.00 35.74  ? 332 GLN   A C   1 
ATOM   990  O O   . GLN   A 1 126 ? 4.177  29.814 -2.630  1.00 36.14  ? 332 GLN   A O   1 
ATOM   991  C CB  . GLN   A 1 126 ? 5.404  30.647 -0.033  1.00 41.20  ? 332 GLN   A CB  1 
ATOM   992  C CG  . GLN   A 1 126 ? 6.808  30.128 -0.230  1.00 42.69  ? 332 GLN   A CG  1 
ATOM   993  C CD  . GLN   A 1 126 ? 7.079  28.950 0.656   1.00 46.79  ? 332 GLN   A CD  1 
ATOM   994  O OE1 . GLN   A 1 126 ? 6.856  29.008 1.872   1.00 51.69  ? 332 GLN   A OE1 1 
ATOM   995  N NE2 . GLN   A 1 126 ? 7.576  27.876 0.069   1.00 46.84  ? 332 GLN   A NE2 1 
ATOM   996  N N   . VAL   A 1 127 ? 5.774  31.194 -3.387  1.00 30.57  ? 333 VAL   A N   1 
ATOM   997  C CA  . VAL   A 1 127 ? 5.949  30.477 -4.636  1.00 32.21  ? 333 VAL   A CA  1 
ATOM   998  C C   . VAL   A 1 127 ? 7.273  29.713 -4.672  1.00 34.82  ? 333 VAL   A C   1 
ATOM   999  O O   . VAL   A 1 127 ? 7.317  28.593 -5.180  1.00 41.90  ? 333 VAL   A O   1 
ATOM   1000 C CB  . VAL   A 1 127 ? 5.794  31.414 -5.856  1.00 29.37  ? 333 VAL   A CB  1 
ATOM   1001 C CG1 . VAL   A 1 127 ? 4.363  31.908 -5.954  1.00 34.09  ? 333 VAL   A CG1 1 
ATOM   1002 C CG2 . VAL   A 1 127 ? 6.726  32.582 -5.789  1.00 34.53  ? 333 VAL   A CG2 1 
ATOM   1003 N N   . VAL   A 1 128 ? 8.360  30.274 -4.124  1.00 30.70  ? 334 VAL   A N   1 
ATOM   1004 C CA  . VAL   A 1 128 ? 9.625  29.554 -3.982  1.00 31.93  ? 334 VAL   A CA  1 
ATOM   1005 C C   . VAL   A 1 128 ? 10.265 29.947 -2.659  1.00 32.41  ? 334 VAL   A C   1 
ATOM   1006 O O   . VAL   A 1 128 ? 9.980  31.003 -2.093  1.00 32.72  ? 334 VAL   A O   1 
ATOM   1007 C CB  . VAL   A 1 128 ? 10.621 29.779 -5.164  1.00 36.09  ? 334 VAL   A CB  1 
ATOM   1008 C CG1 . VAL   A 1 128 ? 10.137 29.059 -6.431  1.00 42.94  ? 334 VAL   A CG1 1 
ATOM   1009 C CG2 . VAL   A 1 128 ? 10.818 31.252 -5.476  1.00 34.47  ? 334 VAL   A CG2 1 
ATOM   1010 N N   . GLU   A 1 129 ? 11.124 29.069 -2.151  1.00 32.66  ? 335 GLU   A N   1 
ATOM   1011 C CA  . GLU   A 1 129 ? 11.716 29.280 -0.840  1.00 30.95  ? 335 GLU   A CA  1 
ATOM   1012 C C   . GLU   A 1 129 ? 13.132 28.720 -0.836  1.00 34.09  ? 335 GLU   A C   1 
ATOM   1013 O O   . GLU   A 1 129 ? 13.414 27.707 -1.482  1.00 36.95  ? 335 GLU   A O   1 
ATOM   1014 C CB  . GLU   A 1 129 ? 10.929 28.588 0.288   1.00 34.57  ? 335 GLU   A CB  1 
ATOM   1015 C CG  . GLU   A 1 129 ? 11.641 28.793 1.630   1.00 45.34  ? 335 GLU   A CG  1 
ATOM   1016 C CD  . GLU   A 1 129 ? 11.112 27.986 2.791   1.00 59.25  ? 335 GLU   A CD  1 
ATOM   1017 O OE1 . GLU   A 1 129 ? 10.286 27.068 2.572   1.00 60.33  ? 335 GLU   A OE1 1 
ATOM   1018 O OE2 . GLU   A 1 129 ? 11.525 28.304 3.935   1.00 52.40  ? 335 GLU   A OE2 1 
ATOM   1019 N N   . LYS   A 1 130 ? 14.018 29.371 -0.092  1.00 32.39  ? 336 LYS   A N   1 
ATOM   1020 C CA  . LYS   A 1 130 ? 15.344 28.822 0.151   1.00 32.86  ? 336 LYS   A CA  1 
ATOM   1021 C C   . LYS   A 1 130 ? 15.722 29.000 1.607   1.00 37.80  ? 336 LYS   A C   1 
ATOM   1022 O O   . LYS   A 1 130 ? 15.398 30.019 2.222   1.00 36.02  ? 336 LYS   A O   1 
ATOM   1023 C CB  . LYS   A 1 130 ? 16.420 29.475 -0.717  1.00 34.92  ? 336 LYS   A CB  1 
ATOM   1024 C CG  . LYS   A 1 130 ? 17.583 28.525 -0.906  1.00 43.38  ? 336 LYS   A CG  1 
ATOM   1025 C CD  . LYS   A 1 130 ? 18.853 29.178 -1.378  1.00 48.56  ? 336 LYS   A CD  1 
ATOM   1026 C CE  . LYS   A 1 130 ? 19.850 28.094 -1.818  1.00 48.34  ? 336 LYS   A CE  1 
ATOM   1027 N NZ  . LYS   A 1 130 ? 21.248 28.608 -1.991  1.00 59.70  ? 336 LYS   A NZ  1 
ATOM   1028 N N   . VAL   A 1 131 ? 16.418 28.005 2.148   1.00 32.31  ? 337 VAL   A N   1 
ATOM   1029 C CA  . VAL   A 1 131 ? 16.942 28.038 3.507   1.00 35.22  ? 337 VAL   A CA  1 
ATOM   1030 C C   . VAL   A 1 131 ? 18.440 27.781 3.410   1.00 35.52  ? 337 VAL   A C   1 
ATOM   1031 O O   . VAL   A 1 131 ? 18.870 26.785 2.818   1.00 33.68  ? 337 VAL   A O   1 
ATOM   1032 C CB  . VAL   A 1 131 ? 16.255 27.009 4.422   1.00 33.75  ? 337 VAL   A CB  1 
ATOM   1033 C CG1 . VAL   A 1 131 ? 16.901 27.003 5.806   1.00 40.16  ? 337 VAL   A CG1 1 
ATOM   1034 C CG2 . VAL   A 1 131 ? 14.748 27.291 4.529   1.00 37.00  ? 337 VAL   A CG2 1 
ATOM   1035 N N   . GLU   A 1 132 ? 19.224 28.718 3.920   1.00 29.16  ? 338 GLU   A N   1 
ATOM   1036 C CA  . GLU   A 1 132 ? 20.677 28.681 3.897   1.00 32.22  ? 338 GLU   A CA  1 
ATOM   1037 C C   . GLU   A 1 132 ? 21.162 28.689 5.334   1.00 37.45  ? 338 GLU   A C   1 
ATOM   1038 O O   . GLU   A 1 132 ? 20.572 29.364 6.179   1.00 34.56  ? 338 GLU   A O   1 
ATOM   1039 C CB  . GLU   A 1 132 ? 21.211 29.880 3.101   1.00 34.85  ? 338 GLU   A CB  1 
ATOM   1040 C CG  . GLU   A 1 132 ? 20.940 29.750 1.608   1.00 47.09  ? 338 GLU   A CG  1 
ATOM   1041 C CD  . GLU   A 1 132 ? 20.937 31.061 0.835   1.00 57.73  ? 338 GLU   A CD  1 
ATOM   1042 O OE1 . GLU   A 1 132 ? 21.653 31.172 -0.187  1.00 56.82  ? 338 GLU   A OE1 1 
ATOM   1043 O OE2 . GLU   A 1 132 ? 20.175 31.979 1.236   1.00 52.73  ? 338 GLU   A OE2 1 
ATOM   1044 N N   . THR   A 1 133 ? 22.203 27.913 5.621   1.00 32.38  ? 339 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 133 ? 22.788 27.837 6.954   1.00 32.84  ? 339 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 133 ? 24.181 28.442 6.927   1.00 33.37  ? 339 THR   A C   1 
ATOM   1047 O O   . THR   A 1 133 ? 24.950 28.194 5.996   1.00 30.90  ? 339 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 133 ? 22.864 26.389 7.437   1.00 34.15  ? 339 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 133 ? 21.557 25.806 7.371   1.00 42.73  ? 339 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 133 ? 23.362 26.321 8.867   1.00 31.76  ? 339 THR   A CG2 1 
ATOM   1051 N N   . GLU   A 1 134 ? 24.505 29.259 7.929   1.00 30.99  ? 340 GLU   A N   1 
ATOM   1052 C CA  . GLU   A 1 134 ? 25.798 29.922 7.915   1.00 27.31  ? 340 GLU   A CA  1 
ATOM   1053 C C   . GLU   A 1 134 ? 26.392 29.881 9.311   1.00 31.16  ? 340 GLU   A C   1 
ATOM   1054 O O   . GLU   A 1 134 ? 25.697 30.110 10.307  1.00 28.60  ? 340 GLU   A O   1 
ATOM   1055 C CB  . GLU   A 1 134 ? 25.696 31.369 7.428   1.00 30.97  ? 340 GLU   A CB  1 
ATOM   1056 C CG  . GLU   A 1 134 ? 25.822 31.563 5.909   1.00 42.67  ? 340 GLU   A CG  1 
ATOM   1057 C CD  . GLU   A 1 134 ? 26.938 30.761 5.224   1.00 49.44  ? 340 GLU   A CD  1 
ATOM   1058 O OE1 . GLU   A 1 134 ? 28.044 30.582 5.798   1.00 46.68  ? 340 GLU   A OE1 1 
ATOM   1059 O OE2 . GLU   A 1 134 ? 26.704 30.334 4.070   1.00 49.98  ? 340 GLU   A OE2 1 
ATOM   1060 N N   . TYR   A 1 135 ? 27.674 29.564 9.366   1.00 27.03  ? 341 TYR   A N   1 
ATOM   1061 C CA  . TYR   A 1 135 ? 28.421 29.460 10.605  1.00 28.54  ? 341 TYR   A CA  1 
ATOM   1062 C C   . TYR   A 1 135 ? 29.229 30.730 10.794  1.00 30.93  ? 341 TYR   A C   1 
ATOM   1063 O O   . TYR   A 1 135 ? 29.782 31.278 9.834   1.00 30.39  ? 341 TYR   A O   1 
ATOM   1064 C CB  . TYR   A 1 135 ? 29.345 28.234 10.594  1.00 32.45  ? 341 TYR   A CB  1 
ATOM   1065 C CG  . TYR   A 1 135 ? 28.560 26.948 10.430  1.00 35.48  ? 341 TYR   A CG  1 
ATOM   1066 C CD1 . TYR   A 1 135 ? 28.096 26.564 9.187   1.00 38.68  ? 341 TYR   A CD1 1 
ATOM   1067 C CD2 . TYR   A 1 135 ? 28.229 26.170 11.517  1.00 41.53  ? 341 TYR   A CD2 1 
ATOM   1068 C CE1 . TYR   A 1 135 ? 27.354 25.430 9.024   1.00 41.31  ? 341 TYR   A CE1 1 
ATOM   1069 C CE2 . TYR   A 1 135 ? 27.485 25.017 11.359  1.00 45.54  ? 341 TYR   A CE2 1 
ATOM   1070 C CZ  . TYR   A 1 135 ? 27.053 24.659 10.104  1.00 44.83  ? 341 TYR   A CZ  1 
ATOM   1071 O OH  . TYR   A 1 135 ? 26.302 23.514 9.915   1.00 70.79  ? 341 TYR   A OH  1 
ATOM   1072 N N   . ALA   A 1 136 ? 29.282 31.185 12.038  1.00 29.01  ? 342 ALA   A N   1 
ATOM   1073 C CA  . ALA   A 1 136 ? 30.003 32.400 12.389  1.00 31.98  ? 342 ALA   A CA  1 
ATOM   1074 C C   . ALA   A 1 136 ? 31.481 32.291 12.049  1.00 31.50  ? 342 ALA   A C   1 
ATOM   1075 O O   . ALA   A 1 136 ? 32.119 31.259 12.268  1.00 37.02  ? 342 ALA   A O   1 
ATOM   1076 C CB  . ALA   A 1 136 ? 29.829 32.690 13.886  1.00 29.19  ? 342 ALA   A CB  1 
ATOM   1077 N N   . ARG   A 1 137 ? 32.023 33.376 11.516  1.00 34.09  ? 343 ARG   A N   1 
ATOM   1078 C CA  . ARG   A 1 137 ? 33.445 33.527 11.264  1.00 36.07  ? 343 ARG   A CA  1 
ATOM   1079 C C   . ARG   A 1 137 ? 33.938 34.732 12.057  1.00 34.35  ? 343 ARG   A C   1 
ATOM   1080 O O   . ARG   A 1 137 ? 33.382 35.828 11.928  1.00 30.11  ? 343 ARG   A O   1 
ATOM   1081 C CB  . ARG   A 1 137 ? 33.697 33.730 9.769   1.00 36.32  ? 343 ARG   A CB  1 
ATOM   1082 C CG  . ARG   A 1 137 ? 35.132 34.083 9.438   1.00 49.03  ? 343 ARG   A CG  1 
ATOM   1083 C CD  . ARG   A 1 137 ? 35.395 34.084 7.940   1.00 56.42  ? 343 ARG   A CD  1 
ATOM   1084 N NE  . ARG   A 1 137 ? 36.825 34.062 7.648   1.00 65.93  ? 343 ARG   A NE  1 
ATOM   1085 C CZ  . ARG   A 1 137 ? 37.341 34.063 6.426   1.00 71.03  ? 343 ARG   A CZ  1 
ATOM   1086 N NH1 . ARG   A 1 137 ? 36.568 34.072 5.350   1.00 76.42  ? 343 ARG   A NH1 1 
ATOM   1087 N NH2 . ARG   A 1 137 ? 38.664 34.042 6.279   1.00 81.99  ? 343 ARG   A NH2 1 
ATOM   1088 N N   . PHE   A 1 138 ? 34.964 34.545 12.880  1.00 30.66  ? 344 PHE   A N   1 
ATOM   1089 C CA  . PHE   A 1 138 ? 35.483 35.666 13.660  1.00 31.36  ? 344 PHE   A CA  1 
ATOM   1090 C C   . PHE   A 1 138 ? 36.311 36.574 12.768  1.00 29.43  ? 344 PHE   A C   1 
ATOM   1091 O O   . PHE   A 1 138 ? 37.267 36.124 12.135  1.00 38.48  ? 344 PHE   A O   1 
ATOM   1092 C CB  . PHE   A 1 138 ? 36.328 35.190 14.835  1.00 40.89  ? 344 PHE   A CB  1 
ATOM   1093 C CG  . PHE   A 1 138 ? 36.792 36.311 15.722  1.00 38.34  ? 344 PHE   A CG  1 
ATOM   1094 C CD1 . PHE   A 1 138 ? 35.902 36.952 16.568  1.00 38.88  ? 344 PHE   A CD1 1 
ATOM   1095 C CD2 . PHE   A 1 138 ? 38.100 36.768 15.659  1.00 39.48  ? 344 PHE   A CD2 1 
ATOM   1096 C CE1 . PHE   A 1 138 ? 36.316 37.992 17.375  1.00 36.79  ? 344 PHE   A CE1 1 
ATOM   1097 C CE2 . PHE   A 1 138 ? 38.520 37.809 16.468  1.00 37.08  ? 344 PHE   A CE2 1 
ATOM   1098 C CZ  . PHE   A 1 138 ? 37.629 38.413 17.326  1.00 40.61  ? 344 PHE   A CZ  1 
ATOM   1099 N N   . GLU   A 1 139 ? 35.952 37.855 12.720  1.00 32.41  ? 345 GLU   A N   1 
ATOM   1100 C CA  . GLU   A 1 139 ? 36.615 38.818 11.846  1.00 36.30  ? 345 GLU   A CA  1 
ATOM   1101 C C   . GLU   A 1 139 ? 36.710 40.160 12.557  1.00 36.62  ? 345 GLU   A C   1 
ATOM   1102 O O   . GLU   A 1 139 ? 35.682 40.798 12.813  1.00 38.14  ? 345 GLU   A O   1 
ATOM   1103 C CB  . GLU   A 1 139 ? 35.867 39.002 10.530  1.00 41.10  ? 345 GLU   A CB  1 
ATOM   1104 C CG  . GLU   A 1 139 ? 36.305 38.104 9.408   1.00 55.54  ? 345 GLU   A CG  1 
ATOM   1105 C CD  . GLU   A 1 139 ? 35.392 38.230 8.202   1.00 58.78  ? 345 GLU   A CD  1 
ATOM   1106 O OE1 . GLU   A 1 139 ? 34.996 37.166 7.660   1.00 67.02  ? 345 GLU   A OE1 1 
ATOM   1107 O OE2 . GLU   A 1 139 ? 35.036 39.368 7.817   1.00 59.65  ? 345 GLU   A OE2 1 
ATOM   1108 N N   . ASN   A 1 140 ? 37.938 40.595 12.843  1.00 35.85  ? 346 ASN   A N   1 
ATOM   1109 C CA  . ASN   A 1 140 ? 38.210 41.943 13.354  1.00 37.71  ? 346 ASN   A CA  1 
ATOM   1110 C C   . ASN   A 1 140 ? 37.305 42.320 14.519  1.00 32.60  ? 346 ASN   A C   1 
ATOM   1111 O O   . ASN   A 1 140 ? 36.791 43.436 14.599  1.00 37.50  ? 346 ASN   A O   1 
ATOM   1112 C CB  . ASN   A 1 140 ? 38.117 42.977 12.235  1.00 35.40  ? 346 ASN   A CB  1 
ATOM   1113 C CG  . ASN   A 1 140 ? 39.164 42.757 11.191  1.00 41.49  ? 346 ASN   A CG  1 
ATOM   1114 O OD1 . ASN   A 1 140 ? 40.341 42.571 11.511  1.00 45.96  ? 346 ASN   A OD1 1 
ATOM   1115 N ND2 . ASN   A 1 140 ? 38.763 42.766 9.937   1.00 54.10  ? 346 ASN   A ND2 1 
ATOM   1116 N N   . GLY   A 1 141 ? 37.096 41.376 15.423  1.00 30.28  ? 347 GLY   A N   1 
ATOM   1117 C CA  . GLY   A 1 141 ? 36.444 41.648 16.675  1.00 30.48  ? 347 GLY   A CA  1 
ATOM   1118 C C   . GLY   A 1 141 ? 34.989 41.241 16.766  1.00 31.26  ? 347 GLY   A C   1 
ATOM   1119 O O   . GLY   A 1 141 ? 34.413 41.341 17.855  1.00 31.46  ? 347 GLY   A O   1 
ATOM   1120 N N   . ARG   A 1 142 ? 34.372 40.787 15.676  1.00 33.62  ? 348 ARG   A N   1 
ATOM   1121 C CA  . ARG   A 1 142 ? 32.960 40.410 15.710  1.00 33.30  ? 348 ARG   A CA  1 
ATOM   1122 C C   . ARG   A 1 142 ? 32.758 39.183 14.823  1.00 31.21  ? 348 ARG   A C   1 
ATOM   1123 O O   . ARG   A 1 142 ? 33.666 38.754 14.103  1.00 32.48  ? 348 ARG   A O   1 
ATOM   1124 C CB  . ARG   A 1 142 ? 32.077 41.603 15.275  1.00 33.38  ? 348 ARG   A CB  1 
ATOM   1125 C CG  . ARG   A 1 142 ? 31.849 41.680 13.778  1.00 36.94  ? 348 ARG   A CG  1 
ATOM   1126 C CD  . ARG   A 1 142 ? 32.822 42.595 13.089  1.00 44.08  ? 348 ARG   A CD  1 
ATOM   1127 N NE  . ARG   A 1 142 ? 32.352 43.029 11.780  1.00 43.63  ? 348 ARG   A NE  1 
ATOM   1128 C CZ  . ARG   A 1 142 ? 33.148 43.123 10.725  1.00 53.69  ? 348 ARG   A CZ  1 
ATOM   1129 N NH1 . ARG   A 1 142 ? 34.405 42.708 10.775  1.00 54.94  ? 348 ARG   A NH1 1 
ATOM   1130 N NH2 . ARG   A 1 142 ? 32.656 43.584 9.575   1.00 58.05  ? 348 ARG   A NH2 1 
ATOM   1131 N N   . PHE   A 1 143 ? 31.564 38.604 14.887  1.00 28.82  ? 349 PHE   A N   1 
ATOM   1132 C CA  . PHE   A 1 143 ? 31.242 37.414 14.112  1.00 32.30  ? 349 PHE   A CA  1 
ATOM   1133 C C   . PHE   A 1 143 ? 30.476 37.810 12.859  1.00 32.90  ? 349 PHE   A C   1 
ATOM   1134 O O   . PHE   A 1 143 ? 29.541 38.616 12.916  1.00 27.48  ? 349 PHE   A O   1 
ATOM   1135 C CB  . PHE   A 1 143 ? 30.466 36.410 14.966  1.00 28.53  ? 349 PHE   A CB  1 
ATOM   1136 C CG  . PHE   A 1 143 ? 31.285 35.910 16.126  1.00 32.64  ? 349 PHE   A CG  1 
ATOM   1137 C CD1 . PHE   A 1 143 ? 32.260 34.948 15.925  1.00 31.60  ? 349 PHE   A CD1 1 
ATOM   1138 C CD2 . PHE   A 1 143 ? 31.172 36.497 17.371  1.00 32.20  ? 349 PHE   A CD2 1 
ATOM   1139 C CE1 . PHE   A 1 143 ? 33.068 34.535 16.963  1.00 33.07  ? 349 PHE   A CE1 1 
ATOM   1140 C CE2 . PHE   A 1 143 ? 31.972 36.079 18.425  1.00 34.46  ? 349 PHE   A CE2 1 
ATOM   1141 C CZ  . PHE   A 1 143 ? 32.917 35.095 18.212  1.00 36.22  ? 349 PHE   A CZ  1 
ATOM   1142 N N   . VAL   A 1 144 ? 30.895 37.254 11.735  1.00 26.60  ? 350 VAL   A N   1 
ATOM   1143 C CA  . VAL   A 1 144 ? 30.366 37.580 10.418  1.00 32.24  ? 350 VAL   A CA  1 
ATOM   1144 C C   . VAL   A 1 144 ? 29.743 36.330 9.796   1.00 25.34  ? 350 VAL   A C   1 
ATOM   1145 O O   . VAL   A 1 144 ? 30.301 35.234 9.891   1.00 27.43  ? 350 VAL   A O   1 
ATOM   1146 C CB  . VAL   A 1 144 ? 31.486 38.153 9.534   1.00 33.39  ? 350 VAL   A CB  1 
ATOM   1147 C CG1 . VAL   A 1 144 ? 30.996 38.361 8.122   1.00 36.99  ? 350 VAL   A CG1 1 
ATOM   1148 C CG2 . VAL   A 1 144 ? 32.011 39.477 10.144  1.00 34.43  ? 350 VAL   A CG2 1 
ATOM   1149 N N   . TYR   A 1 145 ? 28.572 36.493 9.187   1.00 27.20  ? 351 TYR   A N   1 
ATOM   1150 C CA  . TYR   A 1 145 ? 27.852 35.420 8.498   1.00 26.19  ? 351 TYR   A CA  1 
ATOM   1151 C C   . TYR   A 1 145 ? 27.717 35.872 7.062   1.00 26.28  ? 351 TYR   A C   1 
ATOM   1152 O O   . TYR   A 1 145 ? 26.911 36.762 6.777   1.00 28.36  ? 351 TYR   A O   1 
ATOM   1153 C CB  . TYR   A 1 145 ? 26.471 35.172 9.112   1.00 25.56  ? 351 TYR   A CB  1 
ATOM   1154 C CG  . TYR   A 1 145 ? 26.552 34.957 10.582  1.00 27.93  ? 351 TYR   A CG  1 
ATOM   1155 C CD1 . TYR   A 1 145 ? 26.583 36.039 11.459  1.00 27.01  ? 351 TYR   A CD1 1 
ATOM   1156 C CD2 . TYR   A 1 145 ? 26.646 33.684 11.104  1.00 25.12  ? 351 TYR   A CD2 1 
ATOM   1157 C CE1 . TYR   A 1 145 ? 26.710 35.850 12.822  1.00 30.43  ? 351 TYR   A CE1 1 
ATOM   1158 C CE2 . TYR   A 1 145 ? 26.741 33.486 12.454  1.00 25.06  ? 351 TYR   A CE2 1 
ATOM   1159 C CZ  . TYR   A 1 145 ? 26.778 34.567 13.312  1.00 31.53  ? 351 TYR   A CZ  1 
ATOM   1160 O OH  . TYR   A 1 145 ? 26.895 34.353 14.665  1.00 31.08  ? 351 TYR   A OH  1 
ATOM   1161 N N   . ARG   A 1 146 ? 28.486 35.267 6.160   1.00 27.36  ? 352 ARG   A N   1 
ATOM   1162 C CA  A ARG   A 1 146 ? 28.498 35.705 4.774   0.54 32.81  ? 352 ARG   A CA  1 
ATOM   1163 C CA  B ARG   A 1 146 ? 28.560 35.681 4.762   0.46 32.80  ? 352 ARG   A CA  1 
ATOM   1164 C C   . ARG   A 1 146 ? 27.933 34.626 3.861   1.00 34.33  ? 352 ARG   A C   1 
ATOM   1165 O O   . ARG   A 1 146 ? 28.369 33.474 3.879   1.00 39.17  ? 352 ARG   A O   1 
ATOM   1166 C CB  A ARG   A 1 146 ? 29.895 36.116 4.312   0.54 31.43  ? 352 ARG   A CB  1 
ATOM   1167 C CB  B ARG   A 1 146 ? 30.012 35.897 4.351   0.46 31.61  ? 352 ARG   A CB  1 
ATOM   1168 C CG  A ARG   A 1 146 ? 29.883 36.654 2.880   0.54 33.69  ? 352 ARG   A CG  1 
ATOM   1169 C CG  B ARG   A 1 146 ? 30.397 37.333 4.177   0.46 33.57  ? 352 ARG   A CG  1 
ATOM   1170 C CD  A ARG   A 1 146 ? 31.183 37.340 2.482   0.54 35.22  ? 352 ARG   A CD  1 
ATOM   1171 C CD  B ARG   A 1 146 ? 31.738 37.461 3.467   0.46 36.15  ? 352 ARG   A CD  1 
ATOM   1172 N NE  A ARG   A 1 146 ? 31.076 37.950 1.162   0.54 38.44  ? 352 ARG   A NE  1 
ATOM   1173 N NE  B ARG   A 1 146 ? 32.509 38.580 3.994   0.46 38.75  ? 352 ARG   A NE  1 
ATOM   1174 C CZ  A ARG   A 1 146 ? 30.619 39.174 0.934   0.54 40.51  ? 352 ARG   A CZ  1 
ATOM   1175 C CZ  B ARG   A 1 146 ? 33.330 38.496 5.032   0.46 36.84  ? 352 ARG   A CZ  1 
ATOM   1176 N NH1 A ARG   A 1 146 ? 30.202 39.952 1.918   0.54 39.97  ? 352 ARG   A NH1 1 
ATOM   1177 N NH1 B ARG   A 1 146 ? 33.544 37.349 5.652   0.46 34.19  ? 352 ARG   A NH1 1 
ATOM   1178 N NH2 A ARG   A 1 146 ? 30.576 39.628 -0.316  0.54 42.72  ? 352 ARG   A NH2 1 
ATOM   1179 N NH2 B ARG   A 1 146 ? 33.956 39.589 5.451   0.46 38.19  ? 352 ARG   A NH2 1 
ATOM   1180 N N   . ILE   A 1 147 ? 26.940 35.020 3.073   1.00 31.62  ? 353 ILE   A N   1 
ATOM   1181 C CA  . ILE   A 1 147 ? 26.388 34.190 2.012   1.00 37.53  ? 353 ILE   A CA  1 
ATOM   1182 C C   . ILE   A 1 147 ? 26.850 34.865 0.731   1.00 32.52  ? 353 ILE   A C   1 
ATOM   1183 O O   . ILE   A 1 147 ? 26.235 35.834 0.281   1.00 37.80  ? 353 ILE   A O   1 
ATOM   1184 C CB  . ILE   A 1 147 ? 24.850 34.093 2.098   1.00 39.12  ? 353 ILE   A CB  1 
ATOM   1185 C CG1 . ILE   A 1 147 ? 24.421 33.633 3.491   1.00 35.79  ? 353 ILE   A CG1 1 
ATOM   1186 C CG2 . ILE   A 1 147 ? 24.304 33.126 1.044   1.00 40.04  ? 353 ILE   A CG2 1 
ATOM   1187 C CD1 . ILE   A 1 147 ? 22.946 33.590 3.690   1.00 40.15  ? 353 ILE   A CD1 1 
ATOM   1188 N N   . ASN   A 1 148 ? 27.979 34.424 0.176   1.00 37.31  ? 354 ASN   A N   1 
ATOM   1189 C CA  . ASN   A 1 148 ? 28.617 35.133 -0.930  1.00 44.69  ? 354 ASN   A CA  1 
ATOM   1190 C C   . ASN   A 1 148 ? 28.162 34.542 -2.262  1.00 39.19  ? 354 ASN   A C   1 
ATOM   1191 O O   . ASN   A 1 148 ? 28.205 33.326 -2.444  1.00 38.92  ? 354 ASN   A O   1 
ATOM   1192 C CB  . ASN   A 1 148 ? 30.148 35.058 -0.812  1.00 43.11  ? 354 ASN   A CB  1 
ATOM   1193 C CG  . ASN   A 1 148 ? 30.859 36.048 -1.732  1.00 45.93  ? 354 ASN   A CG  1 
ATOM   1194 O OD1 . ASN   A 1 148 ? 30.468 37.210 -1.833  1.00 60.03  ? 354 ASN   A OD1 1 
ATOM   1195 N ND2 . ASN   A 1 148 ? 31.895 35.589 -2.412  1.00 44.13  ? 354 ASN   A ND2 1 
ATOM   1196 N N   . ARG   A 1 149 ? 27.686 35.401 -3.166  1.00 39.17  ? 355 ARG   A N   1 
ATOM   1197 C CA  . ARG   A 1 149 ? 27.484 35.044 -4.572  1.00 36.73  ? 355 ARG   A CA  1 
ATOM   1198 C C   . ARG   A 1 149 ? 26.652 33.761 -4.720  1.00 36.06  ? 355 ARG   A C   1 
ATOM   1199 O O   . ARG   A 1 149 ? 27.071 32.782 -5.332  1.00 44.08  ? 355 ARG   A O   1 
ATOM   1200 C CB  . ARG   A 1 149 ? 28.840 34.895 -5.267  1.00 38.11  ? 355 ARG   A CB  1 
ATOM   1201 C CG  . ARG   A 1 149 ? 28.817 35.163 -6.743  1.00 46.00  ? 355 ARG   A CG  1 
ATOM   1202 C CD  . ARG   A 1 149 ? 30.195 35.462 -7.331  1.00 39.95  ? 355 ARG   A CD  1 
ATOM   1203 N NE  . ARG   A 1 149 ? 30.108 35.314 -8.779  1.00 41.51  ? 355 ARG   A NE  1 
ATOM   1204 C CZ  . ARG   A 1 149 ? 30.136 34.136 -9.397  1.00 48.67  ? 355 ARG   A CZ  1 
ATOM   1205 N NH1 . ARG   A 1 149 ? 30.223 33.001 -8.719  1.00 48.23  ? 355 ARG   A NH1 1 
ATOM   1206 N NH2 . ARG   A 1 149 ? 30.033 34.092 -10.720 1.00 46.33  ? 355 ARG   A NH2 1 
ATOM   1207 N N   . SER   A 1 150 ? 25.496 33.750 -4.115  1.00 35.11  ? 356 SER   A N   1 
ATOM   1208 C CA  . SER   A 1 150 ? 24.620 32.598 -4.238  1.00 34.86  ? 356 SER   A CA  1 
ATOM   1209 C C   . SER   A 1 150 ? 23.814 32.722 -5.532  1.00 31.48  ? 356 SER   A C   1 
ATOM   1210 O O   . SER   A 1 150 ? 23.328 33.811 -5.849  1.00 29.98  ? 356 SER   A O   1 
ATOM   1211 C CB  . SER   A 1 150 ? 23.725 32.519 -3.004  1.00 35.91  ? 356 SER   A CB  1 
ATOM   1212 O OG  . SER   A 1 150 ? 22.648 31.629 -3.163  1.00 49.08  ? 356 SER   A OG  1 
ATOM   1213 N N   . PRO   A 1 151 ? 23.720 31.670 -6.343  1.00 31.78  ? 357 PRO   A N   1 
ATOM   1214 C CA  . PRO   A 1 151 ? 22.961 31.789 -7.596  1.00 28.49  ? 357 PRO   A CA  1 
ATOM   1215 C C   . PRO   A 1 151 ? 21.510 32.169 -7.326  1.00 27.28  ? 357 PRO   A C   1 
ATOM   1216 O O   . PRO   A 1 151 ? 20.883 31.663 -6.399  1.00 28.23  ? 357 PRO   A O   1 
ATOM   1217 C CB  . PRO   A 1 151 ? 23.081 30.396 -8.226  1.00 31.63  ? 357 PRO   A CB  1 
ATOM   1218 C CG  . PRO   A 1 151 ? 23.540 29.513 -7.155  1.00 38.37  ? 357 PRO   A CG  1 
ATOM   1219 C CD  . PRO   A 1 151 ? 24.322 30.340 -6.185  1.00 34.45  ? 357 PRO   A CD  1 
ATOM   1220 N N   . MET   A 1 152 ? 21.014 33.126 -8.100  1.00 28.63  ? 358 MET   A N   1 
ATOM   1221 C CA  . MET   A 1 152 ? 19.600 33.490 -8.077  1.00 28.13  ? 358 MET   A CA  1 
ATOM   1222 C C   . MET   A 1 152 ? 18.768 32.321 -8.599  1.00 26.57  ? 358 MET   A C   1 
ATOM   1223 O O   . MET   A 1 152 ? 19.156 31.667 -9.565  1.00 25.84  ? 358 MET   A O   1 
ATOM   1224 C CB  . MET   A 1 152 ? 19.384 34.705 -8.977  1.00 27.80  ? 358 MET   A CB  1 
ATOM   1225 C CG  . MET   A 1 152 ? 18.515 35.790 -8.435  1.00 37.47  ? 358 MET   A CG  1 
ATOM   1226 S SD  . MET   A 1 152 ? 18.193 37.065 -9.638  1.00 31.04  ? 358 MET   A SD  1 
ATOM   1227 C CE  . MET   A 1 152 ? 19.464 38.271 -9.179  1.00 25.49  ? 358 MET   A CE  1 
ATOM   1228 N N   . CYS   A 1 153 ? 17.606 32.076 -7.996  1.00 29.24  ? 359 CYS   A N   1 
ATOM   1229 C CA  . CYS   A 1 153 ? 16.782 30.971 -8.487  1.00 32.35  ? 359 CYS   A CA  1 
ATOM   1230 C C   . CYS   A 1 153 ? 16.193 31.319 -9.847  1.00 31.96  ? 359 CYS   A C   1 
ATOM   1231 O O   . CYS   A 1 153 ? 16.009 32.494 -10.190 1.00 27.87  ? 359 CYS   A O   1 
ATOM   1232 C CB  . CYS   A 1 153 ? 15.664 30.625 -7.502  1.00 31.98  ? 359 CYS   A CB  1 
ATOM   1233 S SG  . CYS   A 1 153 ? 14.473 31.965 -7.237  1.00 36.91  ? 359 CYS   A SG  1 
ATOM   1234 N N   . GLU   A 1 154 ? 15.921 30.276 -10.639 1.00 28.77  ? 360 GLU   A N   1 
ATOM   1235 C CA  . GLU   A 1 154 ? 15.394 30.475 -11.989 1.00 31.59  ? 360 GLU   A CA  1 
ATOM   1236 C C   . GLU   A 1 154 ? 14.088 31.265 -11.972 1.00 27.75  ? 360 GLU   A C   1 
ATOM   1237 O O   . GLU   A 1 154 ? 13.827 32.065 -12.879 1.00 28.47  ? 360 GLU   A O   1 
ATOM   1238 C CB  . GLU   A 1 154 ? 15.183 29.118 -12.676 1.00 41.01  ? 360 GLU   A CB  1 
ATOM   1239 C CG  . GLU   A 1 154 ? 16.487 28.401 -13.031 1.00 55.44  ? 360 GLU   A CG  1 
ATOM   1240 C CD  . GLU   A 1 154 ? 17.248 29.077 -14.160 1.00 62.67  ? 360 GLU   A CD  1 
ATOM   1241 O OE1 . GLU   A 1 154 ? 16.609 29.796 -14.970 1.00 65.00  ? 360 GLU   A OE1 1 
ATOM   1242 O OE2 . GLU   A 1 154 ? 18.495 28.923 -14.207 1.00 60.72  ? 360 GLU   A OE2 1 
ATOM   1243 N N   . TYR   A 1 155 ? 13.253 31.059 -10.948 1.00 29.31  ? 361 TYR   A N   1 
ATOM   1244 C CA  . TYR   A 1 155 ? 11.996 31.805 -10.882 1.00 26.84  ? 361 TYR   A CA  1 
ATOM   1245 C C   . TYR   A 1 155 ? 12.263 33.313 -10.936 1.00 27.33  ? 361 TYR   A C   1 
ATOM   1246 O O   . TYR   A 1 155 ? 11.644 34.040 -11.717 1.00 25.18  ? 361 TYR   A O   1 
ATOM   1247 C CB  . TYR   A 1 155 ? 11.221 31.432 -9.609  1.00 31.34  ? 361 TYR   A CB  1 
ATOM   1248 C CG  . TYR   A 1 155 ? 9.907  32.179 -9.471  1.00 31.68  ? 361 TYR   A CG  1 
ATOM   1249 C CD1 . TYR   A 1 155 ? 9.871  33.477 -8.964  1.00 33.91  ? 361 TYR   A CD1 1 
ATOM   1250 C CD2 . TYR   A 1 155 ? 8.698  31.582 -9.824  1.00 31.98  ? 361 TYR   A CD2 1 
ATOM   1251 C CE1 . TYR   A 1 155 ? 8.688  34.177 -8.860  1.00 30.51  ? 361 TYR   A CE1 1 
ATOM   1252 C CE2 . TYR   A 1 155 ? 7.497  32.272 -9.705  1.00 33.55  ? 361 TYR   A CE2 1 
ATOM   1253 C CZ  . TYR   A 1 155 ? 7.501  33.569 -9.220  1.00 34.91  ? 361 TYR   A CZ  1 
ATOM   1254 O OH  . TYR   A 1 155 ? 6.332  34.278 -9.099  1.00 39.47  ? 361 TYR   A OH  1 
ATOM   1255 N N   . MET   A 1 156 ? 13.191 33.803 -10.100 1.00 27.31  ? 362 MET   A N   1 
ATOM   1256 C CA  . MET   A 1 156 ? 13.529 35.232 -10.086 1.00 26.67  ? 362 MET   A CA  1 
ATOM   1257 C C   . MET   A 1 156 ? 14.220 35.714 -11.347 1.00 24.78  ? 362 MET   A C   1 
ATOM   1258 O O   . MET   A 1 156 ? 13.952 36.832 -11.786 1.00 26.89  ? 362 MET   A O   1 
ATOM   1259 C CB  . MET   A 1 156 ? 14.344 35.577 -8.837  1.00 20.03  ? 362 MET   A CB  1 
ATOM   1260 C CG  . MET   A 1 156 ? 13.631 35.609 -7.500  1.00 21.68  ? 362 MET   A CG  1 
ATOM   1261 S SD  . MET   A 1 156 ? 12.047 36.502 -7.706  1.00 34.10  ? 362 MET   A SD  1 
ATOM   1262 C CE  . MET   A 1 156 ? 12.679 38.193 -7.792  1.00 33.64  ? 362 MET   A CE  1 
ATOM   1263 N N   . ILE   A 1 157 ? 15.099 34.904 -11.954 1.00 25.43  ? 363 ILE   A N   1 
ATOM   1264 C CA  . ILE   A 1 157 ? 15.719 35.316 -13.214 1.00 24.48  ? 363 ILE   A CA  1 
ATOM   1265 C C   . ILE   A 1 157 ? 14.644 35.535 -14.266 1.00 27.22  ? 363 ILE   A C   1 
ATOM   1266 O O   . ILE   A 1 157 ? 14.610 36.561 -14.955 1.00 28.89  ? 363 ILE   A O   1 
ATOM   1267 C CB  . ILE   A 1 157 ? 16.746 34.269 -13.692 1.00 27.48  ? 363 ILE   A CB  1 
ATOM   1268 C CG1 . ILE   A 1 157 ? 17.863 34.066 -12.673 1.00 28.65  ? 363 ILE   A CG1 1 
ATOM   1269 C CG2 . ILE   A 1 157 ? 17.301 34.679 -15.059 1.00 25.45  ? 363 ILE   A CG2 1 
ATOM   1270 C CD1 . ILE   A 1 157 ? 18.836 32.925 -13.025 1.00 30.76  ? 363 ILE   A CD1 1 
ATOM   1271 N N   . ASN   A 1 158 ? 13.738 34.567 -14.385 1.00 26.34  ? 364 ASN   A N   1 
ATOM   1272 C CA  . ASN   A 1 158 ? 12.636 34.661 -15.338 1.00 27.70  ? 364 ASN   A CA  1 
ATOM   1273 C C   . ASN   A 1 158 ? 11.718 35.840 -15.026 1.00 27.38  ? 364 ASN   A C   1 
ATOM   1274 O O   . ASN   A 1 158 ? 11.304 36.570 -15.933 1.00 29.23  ? 364 ASN   A O   1 
ATOM   1275 C CB  . ASN   A 1 158 ? 11.875 33.335 -15.318 1.00 26.93  ? 364 ASN   A CB  1 
ATOM   1276 C CG  . ASN   A 1 158 ? 10.752 33.289 -16.352 1.00 37.02  ? 364 ASN   A CG  1 
ATOM   1277 O OD1 . ASN   A 1 158 ? 9.581  33.390 -16.004 1.00 47.68  ? 364 ASN   A OD1 1 
ATOM   1278 N ND2 . ASN   A 1 158 ? 11.109 33.197 -17.610 1.00 41.06  ? 364 ASN   A ND2 1 
ATOM   1279 N N   . PHE   A 1 159 ? 11.408 36.055 -13.747 1.00 24.43  ? 365 PHE   A N   1 
ATOM   1280 C CA  . PHE   A 1 159 ? 10.573 37.202 -13.364 1.00 27.33  ? 365 PHE   A CA  1 
ATOM   1281 C C   . PHE   A 1 159 ? 11.219 38.526 -13.749 1.00 28.96  ? 365 PHE   A C   1 
ATOM   1282 O O   . PHE   A 1 159 ? 10.551 39.429 -14.283 1.00 29.73  ? 365 PHE   A O   1 
ATOM   1283 C CB  . PHE   A 1 159 ? 10.299 37.138 -11.855 1.00 28.68  ? 365 PHE   A CB  1 
ATOM   1284 C CG  . PHE   A 1 159 ? 9.508  38.301 -11.318 1.00 31.23  ? 365 PHE   A CG  1 
ATOM   1285 C CD1 . PHE   A 1 159 ? 8.171  38.463 -11.643 1.00 32.97  ? 365 PHE   A CD1 1 
ATOM   1286 C CD2 . PHE   A 1 159 ? 10.089 39.206 -10.455 1.00 36.07  ? 365 PHE   A CD2 1 
ATOM   1287 C CE1 . PHE   A 1 159 ? 7.437  39.526 -11.139 1.00 35.33  ? 365 PHE   A CE1 1 
ATOM   1288 C CE2 . PHE   A 1 159 ? 9.357  40.275 -9.946  1.00 35.37  ? 365 PHE   A CE2 1 
ATOM   1289 C CZ  . PHE   A 1 159 ? 8.026  40.431 -10.294 1.00 31.79  ? 365 PHE   A CZ  1 
ATOM   1290 N N   . ILE   A 1 160 ? 12.524 38.665 -13.486 1.00 28.47  ? 366 ILE   A N   1 
ATOM   1291 C CA  . ILE   A 1 160 ? 13.254 39.870 -13.881 1.00 27.02  ? 366 ILE   A CA  1 
ATOM   1292 C C   . ILE   A 1 160 ? 13.184 40.082 -15.397 1.00 23.99  ? 366 ILE   A C   1 
ATOM   1293 O O   . ILE   A 1 160 ? 12.982 41.206 -15.879 1.00 25.52  ? 366 ILE   A O   1 
ATOM   1294 C CB  . ILE   A 1 160 ? 14.718 39.780 -13.384 1.00 24.01  ? 366 ILE   A CB  1 
ATOM   1295 C CG1 . ILE   A 1 160 ? 14.770 39.915 -11.852 1.00 24.17  ? 366 ILE   A CG1 1 
ATOM   1296 C CG2 . ILE   A 1 160 ? 15.565 40.848 -14.053 1.00 23.71  ? 366 ILE   A CG2 1 
ATOM   1297 C CD1 . ILE   A 1 160 ? 16.157 39.583 -11.256 1.00 24.47  ? 366 ILE   A CD1 1 
ATOM   1298 N N   . HIS   A 1 161 ? 13.346 39.017 -16.178 1.00 27.70  ? 367 HIS   A N   1 
ATOM   1299 C CA  . HIS   A 1 161 ? 13.274 39.177 -17.635 1.00 28.57  ? 367 HIS   A CA  1 
ATOM   1300 C C   . HIS   A 1 161 ? 11.895 39.661 -18.082 1.00 31.50  ? 367 HIS   A C   1 
ATOM   1301 O O   . HIS   A 1 161 ? 11.779 40.561 -18.917 1.00 33.76  ? 367 HIS   A O   1 
ATOM   1302 C CB  . HIS   A 1 161 ? 13.611 37.865 -18.341 1.00 28.38  ? 367 HIS   A CB  1 
ATOM   1303 C CG  . HIS   A 1 161 ? 15.061 37.507 -18.308 1.00 36.95  ? 367 HIS   A CG  1 
ATOM   1304 N ND1 . HIS   A 1 161 ? 15.558 36.381 -18.925 1.00 50.74  ? 367 HIS   A ND1 1 
ATOM   1305 C CD2 . HIS   A 1 161 ? 16.120 38.112 -17.720 1.00 42.11  ? 367 HIS   A CD2 1 
ATOM   1306 C CE1 . HIS   A 1 161 ? 16.862 36.313 -18.729 1.00 49.17  ? 367 HIS   A CE1 1 
ATOM   1307 N NE2 . HIS   A 1 161 ? 17.227 37.346 -17.994 1.00 40.76  ? 367 HIS   A NE2 1 
ATOM   1308 N N   . LYS   A 1 162 ? 10.840 39.064 -17.547 1.00 26.01  ? 368 LYS   A N   1 
ATOM   1309 C CA  . LYS   A 1 162 ? 9.501  39.450 -17.976 1.00 31.31  ? 368 LYS   A CA  1 
ATOM   1310 C C   . LYS   A 1 162 ? 9.130  40.835 -17.471 1.00 31.51  ? 368 LYS   A C   1 
ATOM   1311 O O   . LYS   A 1 162 ? 8.466  41.596 -18.177 1.00 31.85  ? 368 LYS   A O   1 
ATOM   1312 C CB  . LYS   A 1 162 ? 8.505  38.397 -17.519 1.00 33.13  ? 368 LYS   A CB  1 
ATOM   1313 C CG  . LYS   A 1 162 ? 8.789  37.071 -18.203 1.00 38.76  ? 368 LYS   A CG  1 
ATOM   1314 C CD  . LYS   A 1 162 ? 7.746  36.049 -17.898 1.00 43.07  ? 368 LYS   A CD  1 
ATOM   1315 C CE  . LYS   A 1 162 ? 8.018  34.769 -18.671 1.00 49.94  ? 368 LYS   A CE  1 
ATOM   1316 N NZ  . LYS   A 1 162 ? 7.278  33.639 -18.051 1.00 51.65  ? 368 LYS   A NZ  1 
ATOM   1317 N N   . LEU   A 1 163 ? 9.578  41.194 -16.266 1.00 29.63  ? 369 LEU   A N   1 
ATOM   1318 C CA  . LEU   A 1 163 ? 9.361  42.546 -15.760 1.00 30.49  ? 369 LEU   A CA  1 
ATOM   1319 C C   . LEU   A 1 163 ? 10.032 43.591 -16.650 1.00 34.37  ? 369 LEU   A C   1 
ATOM   1320 O O   . LEU   A 1 163 ? 9.424  44.614 -16.995 1.00 35.77  ? 369 LEU   A O   1 
ATOM   1321 C CB  . LEU   A 1 163 ? 9.888  42.636 -14.326 1.00 28.65  ? 369 LEU   A CB  1 
ATOM   1322 C CG  . LEU   A 1 163 ? 9.436  43.762 -13.420 1.00 38.75  ? 369 LEU   A CG  1 
ATOM   1323 C CD1 . LEU   A 1 163 ? 7.918  43.791 -13.283 1.00 27.05  ? 369 LEU   A CD1 1 
ATOM   1324 C CD2 . LEU   A 1 163 ? 10.104 43.547 -12.063 1.00 30.26  ? 369 LEU   A CD2 1 
ATOM   1325 N N   . LYS   A 1 164 ? 11.294 43.348 -17.031 1.00 30.71  ? 370 LYS   A N   1 
ATOM   1326 C CA  . LYS   A 1 164 ? 12.040 44.289 -17.863 1.00 41.63  ? 370 LYS   A CA  1 
ATOM   1327 C C   . LYS   A 1 164 ? 11.440 44.439 -19.245 1.00 33.96  ? 370 LYS   A C   1 
ATOM   1328 O O   . LYS   A 1 164 ? 11.634 45.469 -19.889 1.00 37.74  ? 370 LYS   A O   1 
ATOM   1329 C CB  . LYS   A 1 164 ? 13.498 43.848 -18.027 1.00 29.98  ? 370 LYS   A CB  1 
ATOM   1330 C CG  . LYS   A 1 164 ? 14.379 44.157 -16.842 1.00 43.83  ? 370 LYS   A CG  1 
ATOM   1331 C CD  . LYS   A 1 164 ? 15.822 43.738 -17.117 1.00 46.36  ? 370 LYS   A CD  1 
ATOM   1332 C CE  . LYS   A 1 164 ? 16.366 44.370 -18.393 1.00 41.79  ? 370 LYS   A CE  1 
ATOM   1333 N NZ  . LYS   A 1 164 ? 16.197 45.849 -18.395 1.00 46.00  ? 370 LYS   A NZ  1 
ATOM   1334 N N   . HIS   A 1 165 ? 10.764 43.408 -19.734 1.00 33.86  ? 371 HIS   A N   1 
ATOM   1335 C CA  . HIS   A 1 165 ? 10.157 43.440 -21.054 1.00 36.43  ? 371 HIS   A CA  1 
ATOM   1336 C C   . HIS   A 1 165 ? 8.945  44.373 -21.137 1.00 36.69  ? 371 HIS   A C   1 
ATOM   1337 O O   . HIS   A 1 165 ? 8.503  44.687 -22.245 1.00 41.25  ? 371 HIS   A O   1 
ATOM   1338 C CB  . HIS   A 1 165 ? 9.789  42.002 -21.419 1.00 42.49  ? 371 HIS   A CB  1 
ATOM   1339 C CG  . HIS   A 1 165 ? 9.441  41.794 -22.859 1.00 55.86  ? 371 HIS   A CG  1 
ATOM   1340 N ND1 . HIS   A 1 165 ? 10.316 42.071 -23.887 1.00 53.41  ? 371 HIS   A ND1 1 
ATOM   1341 C CD2 . HIS   A 1 165 ? 8.326  41.284 -23.439 1.00 52.92  ? 371 HIS   A CD2 1 
ATOM   1342 C CE1 . HIS   A 1 165 ? 9.741  41.777 -25.040 1.00 59.96  ? 371 HIS   A CE1 1 
ATOM   1343 N NE2 . HIS   A 1 165 ? 8.535  41.292 -24.795 1.00 54.38  ? 371 HIS   A NE2 1 
ATOM   1344 N N   . LEU   A 1 166 ? 8.385  44.808 -20.009 1.00 34.30  ? 372 LEU   A N   1 
ATOM   1345 C CA  . LEU   A 1 166 ? 7.264  45.747 -20.046 1.00 31.88  ? 372 LEU   A CA  1 
ATOM   1346 C C   . LEU   A 1 166 ? 7.733  47.105 -20.565 1.00 36.18  ? 372 LEU   A C   1 
ATOM   1347 O O   . LEU   A 1 166 ? 8.865  47.513 -20.303 1.00 37.88  ? 372 LEU   A O   1 
ATOM   1348 C CB  . LEU   A 1 166 ? 6.653  45.882 -18.650 1.00 28.70  ? 372 LEU   A CB  1 
ATOM   1349 C CG  . LEU   A 1 166 ? 5.965  44.619 -18.127 1.00 30.26  ? 372 LEU   A CG  1 
ATOM   1350 C CD1 . LEU   A 1 166 ? 5.442  44.797 -16.709 1.00 30.29  ? 372 LEU   A CD1 1 
ATOM   1351 C CD2 . LEU   A 1 166 ? 4.785  44.270 -19.047 1.00 28.74  ? 372 LEU   A CD2 1 
ATOM   1352 N N   . PRO   A 1 167 ? 6.902  47.821 -21.331 1.00 38.54  ? 373 PRO   A N   1 
ATOM   1353 C CA  . PRO   A 1 167 ? 7.374  49.074 -21.938 1.00 33.97  ? 373 PRO   A CA  1 
ATOM   1354 C C   . PRO   A 1 167 ? 7.320  50.277 -21.024 1.00 40.21  ? 373 PRO   A C   1 
ATOM   1355 O O   . PRO   A 1 167 ? 7.928  51.299 -21.358 1.00 42.26  ? 373 PRO   A O   1 
ATOM   1356 C CB  . PRO   A 1 167 ? 6.418  49.273 -23.130 1.00 34.71  ? 373 PRO   A CB  1 
ATOM   1357 C CG  . PRO   A 1 167 ? 5.162  48.623 -22.689 1.00 38.43  ? 373 PRO   A CG  1 
ATOM   1358 C CD  . PRO   A 1 167 ? 5.571  47.435 -21.827 1.00 37.52  ? 373 PRO   A CD  1 
ATOM   1359 N N   . GLU   A 1 168 ? 6.599  50.219 -19.910 1.00 36.84  ? 374 GLU   A N   1 
ATOM   1360 C CA  . GLU   A 1 168 ? 6.429  51.380 -19.057 1.00 36.27  ? 374 GLU   A CA  1 
ATOM   1361 C C   . GLU   A 1 168 ? 6.697  51.023 -17.604 1.00 39.63  ? 374 GLU   A C   1 
ATOM   1362 O O   . GLU   A 1 168 ? 6.361  49.933 -17.132 1.00 33.10  ? 374 GLU   A O   1 
ATOM   1363 C CB  . GLU   A 1 168 ? 5.018  51.980 -19.181 1.00 38.45  ? 374 GLU   A CB  1 
ATOM   1364 C CG  . GLU   A 1 168 ? 4.632  52.380 -20.603 1.00 44.26  ? 374 GLU   A CG  1 
ATOM   1365 C CD  . GLU   A 1 168 ? 5.423  53.568 -21.106 1.00 56.46  ? 374 GLU   A CD  1 
ATOM   1366 O OE1 . GLU   A 1 168 ? 5.878  54.380 -20.272 1.00 59.16  ? 374 GLU   A OE1 1 
ATOM   1367 O OE2 . GLU   A 1 168 ? 5.617  53.676 -22.335 1.00 64.64  ? 374 GLU   A OE2 1 
ATOM   1368 N N   . LYS   A 1 169 ? 7.285  51.987 -16.898 1.00 37.94  ? 375 LYS   A N   1 
ATOM   1369 C CA  . LYS   A 1 169 ? 7.563  51.841 -15.475 1.00 38.32  ? 375 LYS   A CA  1 
ATOM   1370 C C   . LYS   A 1 169 ? 6.308  51.565 -14.669 1.00 34.86  ? 375 LYS   A C   1 
ATOM   1371 O O   . LYS   A 1 169 ? 6.333  50.768 -13.720 1.00 31.57  ? 375 LYS   A O   1 
ATOM   1372 C CB  . LYS   A 1 169 ? 8.253  53.105 -14.967 1.00 34.69  ? 375 LYS   A CB  1 
ATOM   1373 C CG  . LYS   A 1 169 ? 8.663  53.054 -13.535 1.00 44.71  ? 375 LYS   A CG  1 
ATOM   1374 C CD  . LYS   A 1 169 ? 9.771  54.071 -13.268 1.00 60.71  ? 375 LYS   A CD  1 
ATOM   1375 C CE  . LYS   A 1 169 ? 9.118  55.462 -13.053 1.00 72.79  ? 375 LYS   A CE  1 
ATOM   1376 N NZ  . LYS   A 1 169 ? 8.029  55.551 -12.023 1.00 82.46  ? 375 LYS   A NZ  1 
ATOM   1377 N N   . TYR   A 1 170 ? 5.194  52.226 -15.008 1.00 32.76  ? 376 TYR   A N   1 
ATOM   1378 C CA  A TYR   A 1 170 ? 3.992  52.047 -14.204 0.50 35.45  ? 376 TYR   A CA  1 
ATOM   1379 C CA  B TYR   A 1 170 ? 3.992  52.047 -14.204 0.50 35.45  ? 376 TYR   A CA  1 
ATOM   1380 C C   . TYR   A 1 170 ? 3.456  50.621 -14.301 1.00 32.27  ? 376 TYR   A C   1 
ATOM   1381 O O   . TYR   A 1 170 ? 2.894  50.109 -13.326 1.00 31.37  ? 376 TYR   A O   1 
ATOM   1382 C CB  A TYR   A 1 170 ? 2.930  53.090 -14.589 0.50 34.43  ? 376 TYR   A CB  1 
ATOM   1383 C CB  B TYR   A 1 170 ? 2.930  53.090 -14.589 0.50 34.43  ? 376 TYR   A CB  1 
ATOM   1384 C CG  A TYR   A 1 170 ? 2.166  52.832 -15.878 0.50 40.76  ? 376 TYR   A CG  1 
ATOM   1385 C CG  B TYR   A 1 170 ? 2.166  52.832 -15.877 0.50 40.76  ? 376 TYR   A CG  1 
ATOM   1386 C CD1 A TYR   A 1 170 ? 1.038  52.018 -15.892 0.50 42.86  ? 376 TYR   A CD1 1 
ATOM   1387 C CD1 B TYR   A 1 170 ? 1.037  52.019 -15.891 0.50 42.86  ? 376 TYR   A CD1 1 
ATOM   1388 C CD2 A TYR   A 1 170 ? 2.538  53.449 -17.064 0.50 43.50  ? 376 TYR   A CD2 1 
ATOM   1389 C CD2 B TYR   A 1 170 ? 2.538  53.449 -17.064 0.50 43.50  ? 376 TYR   A CD2 1 
ATOM   1390 C CE1 A TYR   A 1 170 ? 0.329  51.794 -17.067 0.50 45.24  ? 376 TYR   A CE1 1 
ATOM   1391 C CE1 B TYR   A 1 170 ? 0.329  51.795 -17.066 0.50 45.24  ? 376 TYR   A CE1 1 
ATOM   1392 C CE2 A TYR   A 1 170 ? 1.832  53.234 -18.245 0.50 42.33  ? 376 TYR   A CE2 1 
ATOM   1393 C CE2 B TYR   A 1 170 ? 1.831  53.234 -18.245 0.50 42.33  ? 376 TYR   A CE2 1 
ATOM   1394 C CZ  A TYR   A 1 170 ? 0.732  52.406 -18.236 0.50 45.88  ? 376 TYR   A CZ  1 
ATOM   1395 C CZ  B TYR   A 1 170 ? 0.731  52.407 -18.235 0.50 45.88  ? 376 TYR   A CZ  1 
ATOM   1396 O OH  A TYR   A 1 170 ? 0.023  52.185 -19.398 0.50 53.46  ? 376 TYR   A OH  1 
ATOM   1397 O OH  B TYR   A 1 170 ? 0.022  52.186 -19.396 0.50 53.46  ? 376 TYR   A OH  1 
ATOM   1398 N N   . MET   A 1 171 ? 3.633  49.954 -15.446 1.00 32.11  ? 377 MET   A N   1 
ATOM   1399 C CA  . MET   A 1 171 ? 3.190  48.562 -15.530 1.00 35.73  ? 377 MET   A CA  1 
ATOM   1400 C C   . MET   A 1 171 ? 4.055  47.666 -14.644 1.00 28.98  ? 377 MET   A C   1 
ATOM   1401 O O   . MET   A 1 171 ? 3.560  46.725 -14.019 1.00 31.65  ? 377 MET   A O   1 
ATOM   1402 C CB  . MET   A 1 171 ? 3.216  48.051 -16.976 1.00 33.19  ? 377 MET   A CB  1 
ATOM   1403 C CG  . MET   A 1 171 ? 2.502  48.955 -17.999 1.00 34.26  ? 377 MET   A CG  1 
ATOM   1404 S SD  . MET   A 1 171 ? 2.852  48.483 -19.714 1.00 34.06  ? 377 MET   A SD  1 
ATOM   1405 C CE  . MET   A 1 171 ? 1.924  49.747 -20.596 1.00 32.23  ? 377 MET   A CE  1 
ATOM   1406 N N   . MET   A 1 172 ? 5.357  47.935 -14.614 1.00 31.59  ? 378 MET   A N   1 
ATOM   1407 C CA  . MET   A 1 172 ? 6.286  47.231 -13.733 1.00 28.71  ? 378 MET   A CA  1 
ATOM   1408 C C   . MET   A 1 172 ? 5.856  47.406 -12.282 1.00 25.39  ? 378 MET   A C   1 
ATOM   1409 O O   . MET   A 1 172 ? 5.754  46.440 -11.514 1.00 29.08  ? 378 MET   A O   1 
ATOM   1410 C CB  . MET   A 1 172 ? 7.654  47.853 -13.981 1.00 33.44  ? 378 MET   A CB  1 
ATOM   1411 C CG  . MET   A 1 172 ? 8.282  47.477 -15.313 1.00 36.55  ? 378 MET   A CG  1 
ATOM   1412 S SD  . MET   A 1 172 ? 10.004 48.006 -15.468 1.00 37.67  ? 378 MET   A SD  1 
ATOM   1413 C CE  . MET   A 1 172 ? 10.278 48.018 -17.251 1.00 30.58  ? 378 MET   A CE  1 
ATOM   1414 N N   . ASN   A 1 173 ? 5.537  48.643 -11.907 1.00 27.06  ? 379 ASN   A N   1 
ATOM   1415 C CA  . ASN   A 1 173 ? 5.107  48.898 -10.541 1.00 30.04  ? 379 ASN   A CA  1 
ATOM   1416 C C   . ASN   A 1 173 ? 3.812  48.175 -10.213 1.00 34.40  ? 379 ASN   A C   1 
ATOM   1417 O O   . ASN   A 1 173 ? 3.641  47.714 -9.080  1.00 31.78  ? 379 ASN   A O   1 
ATOM   1418 C CB  . ASN   A 1 173 ? 4.991  50.404 -10.303 1.00 28.07  ? 379 ASN   A CB  1 
ATOM   1419 C CG  . ASN   A 1 173 ? 6.334  51.025 -10.017 1.00 33.40  ? 379 ASN   A CG  1 
ATOM   1420 O OD1 . ASN   A 1 173 ? 7.253  50.326 -9.588  1.00 30.45  ? 379 ASN   A OD1 1 
ATOM   1421 N ND2 . ASN   A 1 173 ? 6.476  52.317 -10.277 1.00 29.37  ? 379 ASN   A ND2 1 
ATOM   1422 N N   . SER   A 1 174 ? 2.904  48.024 -11.191 1.00 30.42  ? 380 SER   A N   1 
ATOM   1423 C CA  . SER   A 1 174 ? 1.670  47.276 -10.933 1.00 31.71  ? 380 SER   A CA  1 
ATOM   1424 C C   . SER   A 1 174 ? 1.953  45.812 -10.650 1.00 31.53  ? 380 SER   A C   1 
ATOM   1425 O O   . SER   A 1 174 ? 1.303  45.205 -9.789  1.00 34.54  ? 380 SER   A O   1 
ATOM   1426 C CB  . SER   A 1 174 ? 0.711  47.389 -12.119 1.00 34.16  ? 380 SER   A CB  1 
ATOM   1427 O OG  . SER   A 1 174 ? 0.100  48.658 -12.121 1.00 41.28  ? 380 SER   A OG  1 
ATOM   1428 N N   . VAL   A 1 175 ? 2.903  45.222 -11.380 1.00 29.41  ? 381 VAL   A N   1 
ATOM   1429 C CA  . VAL   A 1 175 ? 3.282  43.833 -11.119 1.00 31.97  ? 381 VAL   A CA  1 
ATOM   1430 C C   . VAL   A 1 175 ? 3.938  43.705 -9.737  1.00 35.11  ? 381 VAL   A C   1 
ATOM   1431 O O   . VAL   A 1 175 ? 3.650  42.773 -8.974  1.00 33.88  ? 381 VAL   A O   1 
ATOM   1432 C CB  . VAL   A 1 175 ? 4.215  43.332 -12.244 1.00 29.99  ? 381 VAL   A CB  1 
ATOM   1433 C CG1 . VAL   A 1 175 ? 4.847  41.990 -11.888 1.00 29.28  ? 381 VAL   A CG1 1 
ATOM   1434 C CG2 . VAL   A 1 175 ? 3.500  43.289 -13.611 1.00 26.91  ? 381 VAL   A CG2 1 
ATOM   1435 N N   . LEU   A 1 176 ? 4.828  44.644 -9.391  1.00 30.12  ? 382 LEU   A N   1 
ATOM   1436 C CA  . LEU   A 1 176 ? 5.553  44.567 -8.125  1.00 29.49  ? 382 LEU   A CA  1 
ATOM   1437 C C   . LEU   A 1 176 ? 4.670  44.812 -6.921  1.00 32.03  ? 382 LEU   A C   1 
ATOM   1438 O O   . LEU   A 1 176 ? 5.050  44.435 -5.817  1.00 32.78  ? 382 LEU   A O   1 
ATOM   1439 C CB  . LEU   A 1 176 ? 6.710  45.560 -8.101  1.00 26.67  ? 382 LEU   A CB  1 
ATOM   1440 C CG  . LEU   A 1 176 ? 7.790  45.230 -9.103  1.00 25.92  ? 382 LEU   A CG  1 
ATOM   1441 C CD1 . LEU   A 1 176 ? 8.808  46.357 -9.181  1.00 31.61  ? 382 LEU   A CD1 1 
ATOM   1442 C CD2 . LEU   A 1 176 ? 8.435  43.897 -8.698  1.00 28.07  ? 382 LEU   A CD2 1 
ATOM   1443 N N   . GLU   A 1 177 ? 3.495  45.410 -7.111  1.00 32.43  ? 383 GLU   A N   1 
ATOM   1444 C CA  . GLU   A 1 177 ? 2.566  45.598 -6.004  1.00 35.64  ? 383 GLU   A CA  1 
ATOM   1445 C C   . GLU   A 1 177 ? 2.197  44.269 -5.366  1.00 36.59  ? 383 GLU   A C   1 
ATOM   1446 O O   . GLU   A 1 177 ? 1.820  44.223 -4.190  1.00 33.61  ? 383 GLU   A O   1 
ATOM   1447 C CB  . GLU   A 1 177 ? 1.304  46.275 -6.527  1.00 38.53  ? 383 GLU   A CB  1 
ATOM   1448 C CG  . GLU   A 1 177 ? 1.257  47.771 -6.414  1.00 44.58  ? 383 GLU   A CG  1 
ATOM   1449 C CD  . GLU   A 1 177 ? 0.068  48.310 -7.203  1.00 57.24  ? 383 GLU   A CD  1 
ATOM   1450 O OE1 . GLU   A 1 177 ? -0.950 47.590 -7.273  1.00 53.87  ? 383 GLU   A OE1 1 
ATOM   1451 O OE2 . GLU   A 1 177 ? 0.189  49.376 -7.853  1.00 59.40  ? 383 GLU   A OE2 1 
ATOM   1452 N N   . ASN   A 1 178 ? 2.266  43.179 -6.132  1.00 33.58  ? 384 ASN   A N   1 
ATOM   1453 C CA  . ASN   A 1 178 ? 1.885  41.857 -5.640  1.00 35.77  ? 384 ASN   A CA  1 
ATOM   1454 C C   . ASN   A 1 178 ? 3.080  40.941 -5.413  1.00 36.86  ? 384 ASN   A C   1 
ATOM   1455 O O   . ASN   A 1 178 ? 2.903  39.744 -5.144  1.00 32.61  ? 384 ASN   A O   1 
ATOM   1456 C CB  . ASN   A 1 178 ? 0.896  41.219 -6.616  1.00 39.24  ? 384 ASN   A CB  1 
ATOM   1457 C CG  . ASN   A 1 178 ? -0.304 42.114 -6.855  1.00 45.16  ? 384 ASN   A CG  1 
ATOM   1458 O OD1 . ASN   A 1 178 ? -1.027 42.435 -5.913  1.00 37.03  ? 384 ASN   A OD1 1 
ATOM   1459 N ND2 . ASN   A 1 178 ? -0.498 42.550 -8.093  1.00 42.12  ? 384 ASN   A ND2 1 
ATOM   1460 N N   . PHE   A 1 179 ? 4.286  41.475 -5.494  1.00 29.67  ? 385 PHE   A N   1 
ATOM   1461 C CA  . PHE   A 1 179 ? 5.507  40.706 -5.319  1.00 30.22  ? 385 PHE   A CA  1 
ATOM   1462 C C   . PHE   A 1 179 ? 6.158  41.109 -3.997  1.00 27.13  ? 385 PHE   A C   1 
ATOM   1463 O O   . PHE   A 1 179 ? 6.466  42.290 -3.790  1.00 30.74  ? 385 PHE   A O   1 
ATOM   1464 C CB  . PHE   A 1 179 ? 6.440  40.969 -6.496  1.00 27.86  ? 385 PHE   A CB  1 
ATOM   1465 C CG  . PHE   A 1 179 ? 7.772  40.323 -6.356  1.00 32.64  ? 385 PHE   A CG  1 
ATOM   1466 C CD1 . PHE   A 1 179 ? 7.943  38.988 -6.676  1.00 33.30  ? 385 PHE   A CD1 1 
ATOM   1467 C CD2 . PHE   A 1 179 ? 8.853  41.046 -5.878  1.00 24.94  ? 385 PHE   A CD2 1 
ATOM   1468 C CE1 . PHE   A 1 179 ? 9.179  38.386 -6.540  1.00 30.61  ? 385 PHE   A CE1 1 
ATOM   1469 C CE2 . PHE   A 1 179 ? 10.085 40.455 -5.724  1.00 29.21  ? 385 PHE   A CE2 1 
ATOM   1470 C CZ  . PHE   A 1 179 ? 10.260 39.131 -6.052  1.00 27.53  ? 385 PHE   A CZ  1 
ATOM   1471 N N   . THR   A 1 180 ? 6.378  40.143 -3.108  1.00 28.27  ? 386 THR   A N   1 
ATOM   1472 C CA  . THR   A 1 180 ? 7.056  40.433 -1.843  1.00 29.78  ? 386 THR   A CA  1 
ATOM   1473 C C   . THR   A 1 180 ? 8.056  39.329 -1.516  1.00 27.68  ? 386 THR   A C   1 
ATOM   1474 O O   . THR   A 1 180 ? 7.996  38.228 -2.065  1.00 27.28  ? 386 THR   A O   1 
ATOM   1475 C CB  . THR   A 1 180 ? 6.078  40.559 -0.673  1.00 28.35  ? 386 THR   A CB  1 
ATOM   1476 O OG1 . THR   A 1 180 ? 5.392  39.312 -0.501  1.00 28.74  ? 386 THR   A OG1 1 
ATOM   1477 C CG2 . THR   A 1 180 ? 5.073  41.715 -0.886  1.00 27.71  ? 386 THR   A CG2 1 
ATOM   1478 N N   . ILE   A 1 181 ? 8.968  39.622 -0.589  1.00 26.84  ? 387 ILE   A N   1 
ATOM   1479 C CA  . ILE   A 1 181 ? 9.952  38.647 -0.126  1.00 22.28  ? 387 ILE   A CA  1 
ATOM   1480 C C   . ILE   A 1 181 ? 9.992  38.717 1.387   1.00 23.16  ? 387 ILE   A C   1 
ATOM   1481 O O   . ILE   A 1 181 ? 10.044 39.807 1.958   1.00 28.12  ? 387 ILE   A O   1 
ATOM   1482 C CB  . ILE   A 1 181 ? 11.349 38.900 -0.730  1.00 21.81  ? 387 ILE   A CB  1 
ATOM   1483 C CG1 . ILE   A 1 181 ? 11.309 38.706 -2.257  1.00 24.02  ? 387 ILE   A CG1 1 
ATOM   1484 C CG2 . ILE   A 1 181 ? 12.381 37.961 -0.087  1.00 21.22  ? 387 ILE   A CG2 1 
ATOM   1485 C CD1 . ILE   A 1 181 ? 12.674 38.913 -2.979  1.00 21.89  ? 387 ILE   A CD1 1 
ATOM   1486 N N   . LEU   A 1 182 ? 9.957  37.566 2.037   1.00 26.14  ? 388 LEU   A N   1 
ATOM   1487 C CA  . LEU   A 1 182 ? 10.039 37.495 3.485   1.00 23.28  ? 388 LEU   A CA  1 
ATOM   1488 C C   . LEU   A 1 182 ? 11.365 36.852 3.855   1.00 33.40  ? 388 LEU   A C   1 
ATOM   1489 O O   . LEU   A 1 182 ? 11.625 35.701 3.487   1.00 29.29  ? 388 LEU   A O   1 
ATOM   1490 C CB  . LEU   A 1 182 ? 8.877  36.703 4.078   1.00 22.75  ? 388 LEU   A CB  1 
ATOM   1491 C CG  . LEU   A 1 182 ? 8.853  36.657 5.610   1.00 26.19  ? 388 LEU   A CG  1 
ATOM   1492 C CD1 . LEU   A 1 182 ? 8.678  38.064 6.234   1.00 27.61  ? 388 LEU   A CD1 1 
ATOM   1493 C CD2 . LEU   A 1 182 ? 7.748  35.720 6.073   1.00 26.67  ? 388 LEU   A CD2 1 
ATOM   1494 N N   . LEU   A 1 183 ? 12.210 37.601 4.552   1.00 25.70  ? 389 LEU   A N   1 
ATOM   1495 C CA  A LEU   A 1 183 ? 13.500 37.102 4.995   0.43 26.73  ? 389 LEU   A CA  1 
ATOM   1496 C CA  B LEU   A 1 183 ? 13.506 37.113 5.002   0.57 26.72  ? 389 LEU   A CA  1 
ATOM   1497 C C   . LEU   A 1 183 ? 13.429 36.880 6.499   1.00 29.04  ? 389 LEU   A C   1 
ATOM   1498 O O   . LEU   A 1 183 ? 13.049 37.787 7.248   1.00 30.22  ? 389 LEU   A O   1 
ATOM   1499 C CB  A LEU   A 1 183 ? 14.615 38.083 4.622   0.43 29.16  ? 389 LEU   A CB  1 
ATOM   1500 C CB  B LEU   A 1 183 ? 14.623 38.113 4.694   0.57 29.81  ? 389 LEU   A CB  1 
ATOM   1501 C CG  A LEU   A 1 183 ? 16.048 37.820 5.088   0.43 26.82  ? 389 LEU   A CG  1 
ATOM   1502 C CG  B LEU   A 1 183 ? 14.869 38.579 3.261   0.57 26.38  ? 389 LEU   A CG  1 
ATOM   1503 C CD1 A LEU   A 1 183 ? 16.895 37.560 3.852   0.43 35.82  ? 389 LEU   A CD1 1 
ATOM   1504 C CD1 B LEU   A 1 183 ? 15.864 39.730 3.252   0.57 30.23  ? 389 LEU   A CD1 1 
ATOM   1505 C CD2 A LEU   A 1 183 ? 16.616 38.982 5.856   0.43 30.15  ? 389 LEU   A CD2 1 
ATOM   1506 C CD2 B LEU   A 1 183 ? 15.356 37.446 2.373   0.57 28.40  ? 389 LEU   A CD2 1 
ATOM   1507 N N   . VAL   A 1 184 ? 13.766 35.673 6.938   1.00 22.26  ? 390 VAL   A N   1 
ATOM   1508 C CA  . VAL   A 1 184 ? 13.776 35.367 8.364   1.00 24.85  ? 390 VAL   A CA  1 
ATOM   1509 C C   . VAL   A 1 184 ? 15.111 34.743 8.727   1.00 32.32  ? 390 VAL   A C   1 
ATOM   1510 O O   . VAL   A 1 184 ? 15.504 33.729 8.146   1.00 32.27  ? 390 VAL   A O   1 
ATOM   1511 C CB  . VAL   A 1 184 ? 12.630 34.428 8.775   1.00 29.18  ? 390 VAL   A CB  1 
ATOM   1512 C CG1 . VAL   A 1 184 ? 12.730 34.138 10.244  1.00 27.26  ? 390 VAL   A CG1 1 
ATOM   1513 C CG2 . VAL   A 1 184 ? 11.286 35.056 8.444   1.00 30.46  ? 390 VAL   A CG2 1 
ATOM   1514 N N   . VAL   A 1 185 ? 15.790 35.317 9.711   1.00 28.21  ? 391 VAL   A N   1 
ATOM   1515 C CA  . VAL   A 1 185 ? 17.048 34.771 10.197  1.00 25.53  ? 391 VAL   A CA  1 
ATOM   1516 C C   . VAL   A 1 185 ? 16.837 34.258 11.612  1.00 29.82  ? 391 VAL   A C   1 
ATOM   1517 O O   . VAL   A 1 185 ? 16.308 34.968 12.479  1.00 28.89  ? 391 VAL   A O   1 
ATOM   1518 C CB  . VAL   A 1 185 ? 18.183 35.800 10.133  1.00 29.34  ? 391 VAL   A CB  1 
ATOM   1519 C CG1 . VAL   A 1 185 ? 19.490 35.121 10.488  1.00 26.10  ? 391 VAL   A CG1 1 
ATOM   1520 C CG2 . VAL   A 1 185 ? 18.258 36.399 8.726   1.00 26.21  ? 391 VAL   A CG2 1 
ATOM   1521 N N   . THR   A 1 186 ? 17.253 33.025 11.838  1.00 29.53  ? 392 THR   A N   1 
ATOM   1522 C CA  . THR   A 1 186 ? 16.971 32.301 13.066  1.00 29.53  ? 392 THR   A CA  1 
ATOM   1523 C C   . THR   A 1 186 ? 18.270 31.790 13.661  1.00 32.53  ? 392 THR   A C   1 
ATOM   1524 O O   . THR   A 1 186 ? 19.156 31.351 12.928  1.00 34.93  ? 392 THR   A O   1 
ATOM   1525 C CB  . THR   A 1 186 ? 16.029 31.114 12.778  1.00 31.82  ? 392 THR   A CB  1 
ATOM   1526 O OG1 . THR   A 1 186 ? 14.826 31.595 12.160  1.00 36.36  ? 392 THR   A OG1 1 
ATOM   1527 C CG2 . THR   A 1 186 ? 15.712 30.360 14.043  1.00 33.42  ? 392 THR   A CG2 1 
ATOM   1528 N N   . ASN   A 1 187 ? 18.379 31.840 14.985  1.00 29.61  ? 393 ASN   A N   1 
ATOM   1529 C CA  . ASN   A 1 187 ? 19.469 31.165 15.678  1.00 34.35  ? 393 ASN   A CA  1 
ATOM   1530 C C   . ASN   A 1 187 ? 19.176 29.671 15.613  1.00 37.52  ? 393 ASN   A C   1 
ATOM   1531 O O   . ASN   A 1 187 ? 18.178 29.211 16.164  1.00 34.63  ? 393 ASN   A O   1 
ATOM   1532 C CB  . ASN   A 1 187 ? 19.548 31.675 17.117  1.00 39.91  ? 393 ASN   A CB  1 
ATOM   1533 C CG  . ASN   A 1 187 ? 20.661 31.021 17.936  1.00 42.88  ? 393 ASN   A CG  1 
ATOM   1534 O OD1 . ASN   A 1 187 ? 21.027 29.866 17.722  1.00 45.75  ? 393 ASN   A OD1 1 
ATOM   1535 N ND2 . ASN   A 1 187 ? 21.187 31.772 18.901  1.00 43.58  ? 393 ASN   A ND2 1 
ATOM   1536 N N   . ARG   A 1 188 ? 20.007 28.904 14.910  1.00 34.01  ? 394 ARG   A N   1 
ATOM   1537 C CA  . ARG   A 1 188 ? 19.627 27.513 14.665  1.00 41.78  ? 394 ARG   A CA  1 
ATOM   1538 C C   . ARG   A 1 188 ? 19.565 26.687 15.945  1.00 42.51  ? 394 ARG   A C   1 
ATOM   1539 O O   . ARG   A 1 188 ? 18.804 25.720 16.012  1.00 56.29  ? 394 ARG   A O   1 
ATOM   1540 C CB  . ARG   A 1 188 ? 20.576 26.861 13.668  1.00 38.53  ? 394 ARG   A CB  1 
ATOM   1541 C CG  . ARG   A 1 188 ? 20.090 25.503 13.177  1.00 44.13  ? 394 ARG   A CG  1 
ATOM   1542 C CD  . ARG   A 1 188 ? 21.106 24.925 12.260  1.00 40.84  ? 394 ARG   A CD  1 
ATOM   1543 N NE  . ARG   A 1 188 ? 22.274 24.389 12.953  1.00 38.93  ? 394 ARG   A NE  1 
ATOM   1544 C CZ  . ARG   A 1 188 ? 23.201 23.665 12.340  1.00 35.48  ? 394 ARG   A CZ  1 
ATOM   1545 N NH1 . ARG   A 1 188 ? 23.075 23.331 11.071  1.00 38.59  ? 394 ARG   A NH1 1 
ATOM   1546 N NH2 . ARG   A 1 188 ? 24.293 23.299 13.007  1.00 37.97  ? 394 ARG   A NH2 1 
ATOM   1547 N N   . ASP   A 1 189 ? 20.313 27.062 16.969  1.00 45.53  ? 395 ASP   A N   1 
ATOM   1548 C CA  . ASP   A 1 189 ? 20.391 26.233 18.164  1.00 55.26  ? 395 ASP   A CA  1 
ATOM   1549 C C   . ASP   A 1 189 ? 19.308 26.550 19.190  1.00 56.25  ? 395 ASP   A C   1 
ATOM   1550 O O   . ASP   A 1 189 ? 18.851 25.632 19.878  1.00 65.70  ? 395 ASP   A O   1 
ATOM   1551 C CB  . ASP   A 1 189 ? 21.787 26.361 18.779  1.00 57.52  ? 395 ASP   A CB  1 
ATOM   1552 C CG  . ASP   A 1 189 ? 22.887 25.906 17.803  1.00 77.18  ? 395 ASP   A CG  1 
ATOM   1553 O OD1 . ASP   A 1 189 ? 22.591 25.054 16.929  1.00 72.83  ? 395 ASP   A OD1 1 
ATOM   1554 O OD2 . ASP   A 1 189 ? 24.030 26.412 17.874  1.00 69.82  ? 395 ASP   A OD2 1 
ATOM   1555 N N   . THR   A 1 190 ? 18.853 27.807 19.286  1.00 54.64  ? 396 THR   A N   1 
ATOM   1556 C CA  . THR   A 1 190 ? 17.777 28.185 20.202  1.00 40.73  ? 396 THR   A CA  1 
ATOM   1557 C C   . THR   A 1 190 ? 16.435 28.401 19.508  1.00 47.10  ? 396 THR   A C   1 
ATOM   1558 O O   . THR   A 1 190 ? 15.429 28.601 20.192  1.00 44.11  ? 396 THR   A O   1 
ATOM   1559 C CB  . THR   A 1 190 ? 18.137 29.466 20.947  1.00 49.77  ? 396 THR   A CB  1 
ATOM   1560 O OG1 . THR   A 1 190 ? 18.172 30.544 20.013  1.00 50.35  ? 396 THR   A OG1 1 
ATOM   1561 C CG2 . THR   A 1 190 ? 19.508 29.347 21.567  1.00 56.35  ? 396 THR   A CG2 1 
ATOM   1562 N N   . GLN   A 1 191 ? 16.404 28.391 18.178  1.00 41.82  ? 397 GLN   A N   1 
ATOM   1563 C CA  . GLN   A 1 191 ? 15.231 28.682 17.355  1.00 38.97  ? 397 GLN   A CA  1 
ATOM   1564 C C   . GLN   A 1 191 ? 14.662 30.075 17.587  1.00 38.56  ? 397 GLN   A C   1 
ATOM   1565 O O   . GLN   A 1 191 ? 13.535 30.355 17.180  1.00 39.33  ? 397 GLN   A O   1 
ATOM   1566 C CB  . GLN   A 1 191 ? 14.131 27.631 17.540  1.00 39.48  ? 397 GLN   A CB  1 
ATOM   1567 C CG  . GLN   A 1 191 ? 14.516 26.328 16.898  1.00 46.74  ? 397 GLN   A CG  1 
ATOM   1568 C CD  . GLN   A 1 191 ? 14.568 26.436 15.386  1.00 58.92  ? 397 GLN   A CD  1 
ATOM   1569 O OE1 . GLN   A 1 191 ? 13.636 26.930 14.750  1.00 58.26  ? 397 GLN   A OE1 1 
ATOM   1570 N NE2 . GLN   A 1 191 ? 15.696 26.034 14.806  1.00 63.50  ? 397 GLN   A NE2 1 
ATOM   1571 N N   . GLU   A 1 192 ? 15.412 30.989 18.191  1.00 35.29  ? 398 GLU   A N   1 
ATOM   1572 C CA  . GLU   A 1 192 ? 14.903 32.344 18.332  1.00 39.94  ? 398 GLU   A CA  1 
ATOM   1573 C C   . GLU   A 1 192 ? 15.018 33.105 17.013  1.00 42.21  ? 398 GLU   A C   1 
ATOM   1574 O O   . GLU   A 1 192 ? 16.012 32.993 16.292  1.00 34.02  ? 398 GLU   A O   1 
ATOM   1575 C CB  . GLU   A 1 192 ? 15.636 33.111 19.430  1.00 44.60  ? 398 GLU   A CB  1 
ATOM   1576 C CG  . GLU   A 1 192 ? 17.019 33.595 19.044  1.00 57.22  ? 398 GLU   A CG  1 
ATOM   1577 C CD  . GLU   A 1 192 ? 17.685 34.446 20.115  1.00 68.37  ? 398 GLU   A CD  1 
ATOM   1578 O OE1 . GLU   A 1 192 ? 18.792 34.057 20.569  1.00 67.94  ? 398 GLU   A OE1 1 
ATOM   1579 O OE2 . GLU   A 1 192 ? 17.075 35.456 20.543  1.00 61.61  ? 398 GLU   A OE2 1 
ATOM   1580 N N   . THR   A 1 193 ? 13.986 33.875 16.695  1.00 36.51  ? 399 THR   A N   1 
ATOM   1581 C CA  . THR   A 1 193 ? 14.035 34.747 15.532  1.00 33.12  ? 399 THR   A CA  1 
ATOM   1582 C C   . THR   A 1 193 ? 15.009 35.882 15.805  1.00 35.38  ? 399 THR   A C   1 
ATOM   1583 O O   . THR   A 1 193 ? 14.863 36.619 16.786  1.00 33.93  ? 399 THR   A O   1 
ATOM   1584 C CB  . THR   A 1 193 ? 12.636 35.267 15.217  1.00 34.91  ? 399 THR   A CB  1 
ATOM   1585 O OG1 . THR   A 1 193 ? 11.800 34.149 14.874  1.00 35.58  ? 399 THR   A OG1 1 
ATOM   1586 C CG2 . THR   A 1 193 ? 12.662 36.264 14.066  1.00 30.26  ? 399 THR   A CG2 1 
ATOM   1587 N N   . LEU   A 1 194 ? 16.035 35.985 14.967  1.00 30.80  ? 400 LEU   A N   1 
ATOM   1588 C CA  . LEU   A 1 194 ? 17.035 37.027 15.118  1.00 27.82  ? 400 LEU   A CA  1 
ATOM   1589 C C   . LEU   A 1 194 ? 16.670 38.263 14.318  1.00 29.54  ? 400 LEU   A C   1 
ATOM   1590 O O   . LEU   A 1 194 ? 16.892 39.385 14.778  1.00 28.30  ? 400 LEU   A O   1 
ATOM   1591 C CB  . LEU   A 1 194 ? 18.404 36.510 14.674  1.00 25.07  ? 400 LEU   A CB  1 
ATOM   1592 C CG  . LEU   A 1 194 ? 19.009 35.400 15.538  1.00 31.06  ? 400 LEU   A CG  1 
ATOM   1593 C CD1 . LEU   A 1 194 ? 20.276 34.846 14.886  1.00 26.29  ? 400 LEU   A CD1 1 
ATOM   1594 C CD2 . LEU   A 1 194 ? 19.297 35.910 16.951  1.00 32.13  ? 400 LEU   A CD2 1 
ATOM   1595 N N   . LEU   A 1 195 ? 16.100 38.069 13.129  1.00 28.42  ? 401 LEU   A N   1 
ATOM   1596 C CA  . LEU   A 1 195 ? 15.771 39.169 12.246  1.00 28.97  ? 401 LEU   A CA  1 
ATOM   1597 C C   . LEU   A 1 195 ? 14.680 38.699 11.292  1.00 29.36  ? 401 LEU   A C   1 
ATOM   1598 O O   . LEU   A 1 195 ? 14.739 37.587 10.771  1.00 28.46  ? 401 LEU   A O   1 
ATOM   1599 C CB  . LEU   A 1 195 ? 17.019 39.633 11.481  1.00 25.76  ? 401 LEU   A CB  1 
ATOM   1600 C CG  . LEU   A 1 195 ? 16.886 40.768 10.473  1.00 34.06  ? 401 LEU   A CG  1 
ATOM   1601 C CD1 . LEU   A 1 195 ? 16.307 42.029 11.154  1.00 31.12  ? 401 LEU   A CD1 1 
ATOM   1602 C CD2 . LEU   A 1 195 ? 18.231 41.082 9.820   1.00 32.07  ? 401 LEU   A CD2 1 
ATOM   1603 N N   . CYS   A 1 196 ? 13.688 39.547 11.068  1.00 24.11  ? 402 CYS   A N   1 
ATOM   1604 C CA  . CYS   A 1 196 ? 12.669 39.287 10.067  1.00 23.69  ? 402 CYS   A CA  1 
ATOM   1605 C C   . CYS   A 1 196 ? 12.472 40.556 9.262   1.00 28.58  ? 402 CYS   A C   1 
ATOM   1606 O O   . CYS   A 1 196 ? 12.224 41.617 9.834   1.00 31.43  ? 402 CYS   A O   1 
ATOM   1607 C CB  . CYS   A 1 196 ? 11.352 38.841 10.706  1.00 23.32  ? 402 CYS   A CB  1 
ATOM   1608 S SG  . CYS   A 1 196 ? 10.027 38.689 9.504   1.00 31.41  ? 402 CYS   A SG  1 
ATOM   1609 N N   . MET   A 1 197 ? 12.615 40.457 7.943   1.00 25.39  ? 403 MET   A N   1 
ATOM   1610 C CA  . MET   A 1 197 ? 12.438 41.596 7.059   1.00 25.97  ? 403 MET   A CA  1 
ATOM   1611 C C   . MET   A 1 197 ? 11.355 41.237 6.053   1.00 23.47  ? 403 MET   A C   1 
ATOM   1612 O O   . MET   A 1 197 ? 11.528 40.324 5.235   1.00 28.76  ? 403 MET   A O   1 
ATOM   1613 C CB  . MET   A 1 197 ? 13.735 41.967 6.332   1.00 24.18  ? 403 MET   A CB  1 
ATOM   1614 C CG  . MET   A 1 197 ? 14.772 42.594 7.240   1.00 33.71  ? 403 MET   A CG  1 
ATOM   1615 S SD  . MET   A 1 197 ? 16.399 42.707 6.441   1.00 42.58  ? 403 MET   A SD  1 
ATOM   1616 C CE  . MET   A 1 197 ? 15.908 43.335 4.835   1.00 37.12  ? 403 MET   A CE  1 
ATOM   1617 N N   . ALA   A 1 198 ? 10.255 41.962 6.117   1.00 23.58  ? 404 ALA   A N   1 
ATOM   1618 C CA  . ALA   A 1 198 ? 9.186  41.895 5.138   1.00 23.11  ? 404 ALA   A CA  1 
ATOM   1619 C C   . ALA   A 1 198 ? 9.518  42.903 4.055   1.00 27.25  ? 404 ALA   A C   1 
ATOM   1620 O O   . ALA   A 1 198 ? 9.549  44.113 4.316   1.00 27.07  ? 404 ALA   A O   1 
ATOM   1621 C CB  . ALA   A 1 198 ? 7.854  42.210 5.815   1.00 21.46  ? 404 ALA   A CB  1 
ATOM   1622 N N   . CYS   A 1 199 ? 9.798  42.423 2.850   1.00 22.62  ? 405 CYS   A N   1 
ATOM   1623 C CA  . CYS   A 1 199 ? 10.308 43.271 1.782   1.00 25.54  ? 405 CYS   A CA  1 
ATOM   1624 C C   . CYS   A 1 199 ? 9.229  43.550 0.752   1.00 29.14  ? 405 CYS   A C   1 
ATOM   1625 O O   . CYS   A 1 199 ? 8.580  42.610 0.267   1.00 25.76  ? 405 CYS   A O   1 
ATOM   1626 C CB  . CYS   A 1 199 ? 11.516 42.620 1.102   1.00 22.98  ? 405 CYS   A CB  1 
ATOM   1627 S SG  . CYS   A 1 199 ? 12.788 42.114 2.301   1.00 27.99  ? 405 CYS   A SG  1 
ATOM   1628 N N   . VAL   A 1 200 ? 9.069  44.836 0.390   1.00 24.69  ? 406 VAL   A N   1 
ATOM   1629 C CA  . VAL   A 1 200 ? 8.200  45.244 -0.705  1.00 22.97  ? 406 VAL   A CA  1 
ATOM   1630 C C   . VAL   A 1 200 ? 9.030  46.044 -1.709  1.00 23.47  ? 406 VAL   A C   1 
ATOM   1631 O O   . VAL   A 1 200 ? 10.142 46.489 -1.419  1.00 24.96  ? 406 VAL   A O   1 
ATOM   1632 C CB  . VAL   A 1 200 ? 6.963  46.044 -0.205  1.00 27.78  ? 406 VAL   A CB  1 
ATOM   1633 C CG1 . VAL   A 1 200 ? 6.129  45.186 0.721   1.00 31.09  ? 406 VAL   A CG1 1 
ATOM   1634 C CG2 . VAL   A 1 200 ? 7.369  47.319 0.519   1.00 22.42  ? 406 VAL   A CG2 1 
ATOM   1635 N N   . PHE   A 1 201 ? 8.481  46.213 -2.916  1.00 24.77  ? 407 PHE   A N   1 
ATOM   1636 C CA  . PHE   A 1 201 ? 9.276  46.602 -4.069  1.00 26.21  ? 407 PHE   A CA  1 
ATOM   1637 C C   . PHE   A 1 201 ? 8.558  47.574 -4.992  1.00 28.33  ? 407 PHE   A C   1 
ATOM   1638 O O   . PHE   A 1 201 ? 7.354  47.478 -5.242  1.00 26.12  ? 407 PHE   A O   1 
ATOM   1639 C CB  . PHE   A 1 201 ? 9.698  45.376 -4.892  1.00 21.09  ? 407 PHE   A CB  1 
ATOM   1640 C CG  . PHE   A 1 201 ? 10.546 44.407 -4.115  1.00 24.35  ? 407 PHE   A CG  1 
ATOM   1641 C CD1 . PHE   A 1 201 ? 9.959  43.440 -3.325  1.00 24.45  ? 407 PHE   A CD1 1 
ATOM   1642 C CD2 . PHE   A 1 201 ? 11.935 44.494 -4.158  1.00 20.26  ? 407 PHE   A CD2 1 
ATOM   1643 C CE1 . PHE   A 1 201 ? 10.734 42.563 -2.580  1.00 23.97  ? 407 PHE   A CE1 1 
ATOM   1644 C CE2 . PHE   A 1 201 ? 12.723 43.617 -3.432  1.00 21.94  ? 407 PHE   A CE2 1 
ATOM   1645 C CZ  . PHE   A 1 201 ? 12.129 42.654 -2.638  1.00 27.29  ? 407 PHE   A CZ  1 
ATOM   1646 N N   . GLU   A 1 202 ? 9.366  48.449 -5.569  1.00 28.20  ? 408 GLU   A N   1 
ATOM   1647 C CA  . GLU   A 1 202 ? 8.975  49.412 -6.579  1.00 28.33  ? 408 GLU   A CA  1 
ATOM   1648 C C   . GLU   A 1 202 ? 10.162 49.553 -7.516  1.00 32.26  ? 408 GLU   A C   1 
ATOM   1649 O O   . GLU   A 1 202 ? 11.287 49.195 -7.162  1.00 33.47  ? 408 GLU   A O   1 
ATOM   1650 C CB  . GLU   A 1 202 ? 8.626  50.746 -5.906  1.00 29.91  ? 408 GLU   A CB  1 
ATOM   1651 C CG  . GLU   A 1 202 ? 8.105  51.856 -6.756  1.00 45.92  ? 408 GLU   A CG  1 
ATOM   1652 C CD  . GLU   A 1 202 ? 7.446  52.948 -5.910  1.00 54.06  ? 408 GLU   A CD  1 
ATOM   1653 O OE1 . GLU   A 1 202 ? 6.676  52.613 -4.985  1.00 48.14  ? 408 GLU   A OE1 1 
ATOM   1654 O OE2 . GLU   A 1 202 ? 7.695  54.141 -6.187  1.00 65.73  ? 408 GLU   A OE2 1 
ATOM   1655 N N   . VAL   A 1 203 ? 9.917  50.086 -8.704  1.00 27.24  ? 409 VAL   A N   1 
ATOM   1656 C CA  . VAL   A 1 203 ? 10.988 50.375 -9.644  1.00 29.80  ? 409 VAL   A CA  1 
ATOM   1657 C C   . VAL   A 1 203 ? 11.605 51.729 -9.316  1.00 32.22  ? 409 VAL   A C   1 
ATOM   1658 O O   . VAL   A 1 203 ? 10.902 52.705 -9.032  1.00 34.04  ? 409 VAL   A O   1 
ATOM   1659 C CB  . VAL   A 1 203 ? 10.456 50.332 -11.092 1.00 34.14  ? 409 VAL   A CB  1 
ATOM   1660 C CG1 . VAL   A 1 203 ? 11.485 50.876 -12.042 1.00 36.99  ? 409 VAL   A CG1 1 
ATOM   1661 C CG2 . VAL   A 1 203 ? 10.111 48.896 -11.486 1.00 27.39  ? 409 VAL   A CG2 1 
ATOM   1662 N N   . SER   A 1 204 ? 12.931 51.794 -9.359  1.00 28.60  ? 410 SER   A N   1 
ATOM   1663 C CA  . SER   A 1 204 ? 13.620 53.048 -9.104  1.00 36.97  ? 410 SER   A CA  1 
ATOM   1664 C C   . SER   A 1 204 ? 13.220 54.098 -10.128 1.00 42.07  ? 410 SER   A C   1 
ATOM   1665 O O   . SER   A 1 204 ? 13.090 53.821 -11.317 1.00 40.84  ? 410 SER   A O   1 
ATOM   1666 C CB  . SER   A 1 204 ? 15.129 52.841 -9.138  1.00 40.43  ? 410 SER   A CB  1 
ATOM   1667 O OG  . SER   A 1 204 ? 15.579 52.694 -10.481 1.00 56.53  ? 410 SER   A OG  1 
ATOM   1668 N N   . ASN   A 1 205 ? 13.008 55.306 -9.643  1.00 61.39  ? 411 ASN   A N   1 
ATOM   1669 C CA  . ASN   A 1 205 ? 12.686 56.465 -10.455 1.00 70.89  ? 411 ASN   A CA  1 
ATOM   1670 C C   . ASN   A 1 205 ? 13.779 57.520 -10.436 1.00 76.87  ? 411 ASN   A C   1 
ATOM   1671 O O   . ASN   A 1 205 ? 14.076 58.102 -11.478 1.00 78.78  ? 411 ASN   A O   1 
ATOM   1672 C CB  . ASN   A 1 205 ? 11.345 57.058 -9.988  1.00 73.31  ? 411 ASN   A CB  1 
ATOM   1673 C CG  . ASN   A 1 205 ? 11.129 56.911 -8.472  1.00 81.02  ? 411 ASN   A CG  1 
ATOM   1674 O OD1 . ASN   A 1 205 ? 12.070 57.002 -7.672  1.00 81.38  ? 411 ASN   A OD1 1 
ATOM   1675 N ND2 . ASN   A 1 205 ? 9.883  56.646 -8.079  1.00 80.33  ? 411 ASN   A ND2 1 
ATOM   1676 N N   . SER   A 1 206 ? 14.413 57.747 -9.285  1.00 89.92  ? 412 SER   A N   1 
ATOM   1677 C CA  . SER   A 1 206 ? 15.509 58.705 -9.211  1.00 97.42  ? 412 SER   A CA  1 
ATOM   1678 C C   . SER   A 1 206 ? 16.751 58.125 -9.869  1.00 88.16  ? 412 SER   A C   1 
ATOM   1679 O O   . SER   A 1 206 ? 17.078 56.948 -9.691  1.00 81.03  ? 412 SER   A O   1 
ATOM   1680 C CB  . SER   A 1 206 ? 15.829 59.071 -7.758  1.00 86.25  ? 412 SER   A CB  1 
ATOM   1681 O OG  . SER   A 1 206 ? 16.813 58.197 -7.219  1.00 72.72  ? 412 SER   A OG  1 
ATOM   1682 N N   . GLU   A 1 207 ? 17.464 58.959 -10.616 1.00 81.11  ? 413 GLU   A N   1 
ATOM   1683 C CA  . GLU   A 1 207 ? 18.665 58.466 -11.267 1.00 74.35  ? 413 GLU   A CA  1 
ATOM   1684 C C   . GLU   A 1 207 ? 19.822 58.310 -10.314 1.00 70.20  ? 413 GLU   A C   1 
ATOM   1685 O O   . GLU   A 1 207 ? 20.961 58.240 -10.769 1.00 71.63  ? 413 GLU   A O   1 
ATOM   1686 C CB  . GLU   A 1 207 ? 19.035 59.365 -12.445 1.00 80.69  ? 413 GLU   A CB  1 
ATOM   1687 C CG  . GLU   A 1 207 ? 17.986 59.341 -13.556 1.00 87.06  ? 413 GLU   A CG  1 
ATOM   1688 C CD  . GLU   A 1 207 ? 17.160 58.046 -13.578 1.00 85.24  ? 413 GLU   A CD  1 
ATOM   1689 O OE1 . GLU   A 1 207 ? 15.914 58.115 -13.746 1.00 82.77  ? 413 GLU   A OE1 1 
ATOM   1690 O OE2 . GLU   A 1 207 ? 17.748 56.958 -13.393 1.00 83.11  ? 413 GLU   A OE2 1 
ATOM   1691 N N   . HIS   A 1 208 ? 19.558 58.248 -9.010  1.00 79.40  ? 414 HIS   A N   1 
ATOM   1692 C CA  . HIS   A 1 208 ? 20.517 57.687 -8.072  1.00 80.99  ? 414 HIS   A CA  1 
ATOM   1693 C C   . HIS   A 1 208 ? 20.341 56.176 -7.934  1.00 71.01  ? 414 HIS   A C   1 
ATOM   1694 O O   . HIS   A 1 208 ? 21.080 55.547 -7.169  1.00 76.05  ? 414 HIS   A O   1 
ATOM   1695 C CB  . HIS   A 1 208 ? 20.402 58.364 -6.699  1.00 71.76  ? 414 HIS   A CB  1 
ATOM   1696 C CG  . HIS   A 1 208 ? 21.700 58.440 -5.957  0.00 68.67  ? 414 HIS   A CG  1 
ATOM   1697 N ND1 . HIS   A 1 208 ? 22.319 59.636 -5.666  0.00 70.20  ? 414 HIS   A ND1 1 
ATOM   1698 C CD2 . HIS   A 1 208 ? 22.521 57.470 -5.491  0.00 66.21  ? 414 HIS   A CD2 1 
ATOM   1699 C CE1 . HIS   A 1 208 ? 23.449 59.401 -5.024  0.00 68.88  ? 414 HIS   A CE1 1 
ATOM   1700 N NE2 . HIS   A 1 208 ? 23.595 58.094 -4.905  0.00 66.09  ? 414 HIS   A NE2 1 
ATOM   1701 N N   . GLY   A 1 209 ? 19.383 55.585 -8.656  1.00 59.75  ? 415 GLY   A N   1 
ATOM   1702 C CA  . GLY   A 1 209 ? 19.277 54.139 -8.774  1.00 48.43  ? 415 GLY   A CA  1 
ATOM   1703 C C   . GLY   A 1 209 ? 18.570 53.440 -7.631  1.00 39.09  ? 415 GLY   A C   1 
ATOM   1704 O O   . GLY   A 1 209 ? 17.588 53.946 -7.089  1.00 28.54  ? 415 GLY   A O   1 
ATOM   1705 N N   . ALA   A 1 210 ? 19.084 52.279 -7.251  1.00 30.27  ? 416 ALA   A N   1 
ATOM   1706 C CA  . ALA   A 1 210 ? 18.458 51.462 -6.229  1.00 28.27  ? 416 ALA   A CA  1 
ATOM   1707 C C   . ALA   A 1 210 ? 18.616 52.107 -4.858  1.00 27.89  ? 416 ALA   A C   1 
ATOM   1708 O O   . ALA   A 1 210 ? 19.646 52.706 -4.555  1.00 28.60  ? 416 ALA   A O   1 
ATOM   1709 C CB  . ALA   A 1 210 ? 19.079 50.061 -6.240  1.00 23.04  ? 416 ALA   A CB  1 
ATOM   1710 N N   . GLN   A 1 211 ? 17.581 51.979 -4.028  1.00 26.47  ? 417 GLN   A N   1 
ATOM   1711 C CA  . GLN   A 1 211 ? 17.535 52.590 -2.702  1.00 25.31  ? 417 GLN   A CA  1 
ATOM   1712 C C   . GLN   A 1 211 ? 16.651 51.714 -1.828  1.00 24.97  ? 417 GLN   A C   1 
ATOM   1713 O O   . GLN   A 1 211 ? 15.951 50.821 -2.320  1.00 27.98  ? 417 GLN   A O   1 
ATOM   1714 C CB  . GLN   A 1 211 ? 16.982 54.034 -2.789  1.00 26.37  ? 417 GLN   A CB  1 
ATOM   1715 C CG  . GLN   A 1 211 ? 17.912 55.018 -3.525  1.00 40.41  ? 417 GLN   A CG  1 
ATOM   1716 C CD  . GLN   A 1 211 ? 17.399 56.458 -3.590  1.00 44.89  ? 417 GLN   A CD  1 
ATOM   1717 O OE1 . GLN   A 1 211 ? 16.516 56.845 -2.841  1.00 38.77  ? 417 GLN   A OE1 1 
ATOM   1718 N NE2 . GLN   A 1 211 ? 17.985 57.259 -4.481  1.00 49.05  ? 417 GLN   A NE2 1 
ATOM   1719 N N   . HIS   A 1 212 ? 16.646 51.982 -0.527  1.00 23.22  ? 418 HIS   A N   1 
ATOM   1720 C CA  . HIS   A 1 212 ? 15.733 51.262 0.347   1.00 22.79  ? 418 HIS   A CA  1 
ATOM   1721 C C   . HIS   A 1 212 ? 15.317 52.158 1.502   1.00 25.29  ? 418 HIS   A C   1 
ATOM   1722 O O   . HIS   A 1 212 ? 15.968 53.158 1.796   1.00 24.54  ? 418 HIS   A O   1 
ATOM   1723 C CB  . HIS   A 1 212 ? 16.343 49.945 0.866   1.00 23.19  ? 418 HIS   A CB  1 
ATOM   1724 C CG  . HIS   A 1 212 ? 17.408 50.132 1.900   1.00 27.50  ? 418 HIS   A CG  1 
ATOM   1725 N ND1 . HIS   A 1 212 ? 18.646 50.666 1.604   1.00 22.55  ? 418 HIS   A ND1 1 
ATOM   1726 C CD2 . HIS   A 1 212 ? 17.420 49.864 3.227   1.00 22.94  ? 418 HIS   A CD2 1 
ATOM   1727 C CE1 . HIS   A 1 212 ? 19.372 50.720 2.705   1.00 26.58  ? 418 HIS   A CE1 1 
ATOM   1728 N NE2 . HIS   A 1 212 ? 18.655 50.234 3.703   1.00 22.81  ? 418 HIS   A NE2 1 
ATOM   1729 N N   . HIS   A 1 213 ? 14.209 51.787 2.145   1.00 23.24  ? 419 HIS   A N   1 
ATOM   1730 C CA  . HIS   A 1 213 ? 13.661 52.545 3.261   1.00 24.20  ? 419 HIS   A CA  1 
ATOM   1731 C C   . HIS   A 1 213 ? 13.198 51.563 4.325   1.00 23.56  ? 419 HIS   A C   1 
ATOM   1732 O O   . HIS   A 1 213 ? 12.533 50.582 4.010   1.00 26.98  ? 419 HIS   A O   1 
ATOM   1733 C CB  . HIS   A 1 213 ? 12.507 53.453 2.796   1.00 23.44  ? 419 HIS   A CB  1 
ATOM   1734 C CG  . HIS   A 1 213 ? 12.189 54.538 3.772   1.00 34.37  ? 419 HIS   A CG  1 
ATOM   1735 N ND1 . HIS   A 1 213 ? 12.590 55.844 3.581   1.00 41.32  ? 419 HIS   A ND1 1 
ATOM   1736 C CD2 . HIS   A 1 213 ? 11.592 54.501 4.985   1.00 34.34  ? 419 HIS   A CD2 1 
ATOM   1737 C CE1 . HIS   A 1 213 ? 12.219 56.573 4.620   1.00 39.71  ? 419 HIS   A CE1 1 
ATOM   1738 N NE2 . HIS   A 1 213 ? 11.609 55.784 5.484   1.00 38.14  ? 419 HIS   A NE2 1 
ATOM   1739 N N   . ILE   A 1 214 ? 13.550 51.815 5.582   1.00 22.55  ? 420 ILE   A N   1 
ATOM   1740 C CA  . ILE   A 1 214 ? 13.320 50.891 6.683   1.00 23.34  ? 420 ILE   A CA  1 
ATOM   1741 C C   . ILE   A 1 214 ? 12.206 51.413 7.582   1.00 28.84  ? 420 ILE   A C   1 
ATOM   1742 O O   . ILE   A 1 214 ? 12.165 52.604 7.902   1.00 28.07  ? 420 ILE   A O   1 
ATOM   1743 C CB  . ILE   A 1 214 ? 14.612 50.705 7.504   1.00 27.80  ? 420 ILE   A CB  1 
ATOM   1744 C CG1 . ILE   A 1 214 ? 15.763 50.275 6.592   1.00 24.59  ? 420 ILE   A CG1 1 
ATOM   1745 C CG2 . ILE   A 1 214 ? 14.388 49.724 8.649   1.00 27.68  ? 420 ILE   A CG2 1 
ATOM   1746 C CD1 . ILE   A 1 214 ? 17.154 50.640 7.165   1.00 32.68  ? 420 ILE   A CD1 1 
ATOM   1747 N N   . TYR   A 1 215 ? 11.336 50.510 8.019   1.00 24.99  ? 421 TYR   A N   1 
ATOM   1748 C CA  . TYR   A 1 215 ? 10.267 50.776 8.971   1.00 27.42  ? 421 TYR   A CA  1 
ATOM   1749 C C   . TYR   A 1 215 ? 10.282 49.680 10.011  1.00 30.85  ? 421 TYR   A C   1 
ATOM   1750 O O   . TYR   A 1 215 ? 10.538 48.518 9.685   1.00 29.71  ? 421 TYR   A O   1 
ATOM   1751 C CB  . TYR   A 1 215 ? 8.882  50.766 8.316   1.00 27.49  ? 421 TYR   A CB  1 
ATOM   1752 C CG  . TYR   A 1 215 ? 8.712  51.750 7.195   1.00 29.35  ? 421 TYR   A CG  1 
ATOM   1753 C CD1 . TYR   A 1 215 ? 9.023  51.388 5.893   1.00 29.08  ? 421 TYR   A CD1 1 
ATOM   1754 C CD2 . TYR   A 1 215 ? 8.224  53.030 7.427   1.00 33.14  ? 421 TYR   A CD2 1 
ATOM   1755 C CE1 . TYR   A 1 215 ? 8.873  52.275 4.860   1.00 33.52  ? 421 TYR   A CE1 1 
ATOM   1756 C CE2 . TYR   A 1 215 ? 8.065  53.931 6.397   1.00 31.55  ? 421 TYR   A CE2 1 
ATOM   1757 C CZ  . TYR   A 1 215 ? 8.382  53.541 5.117   1.00 33.61  ? 421 TYR   A CZ  1 
ATOM   1758 O OH  . TYR   A 1 215 ? 8.231  54.417 4.084   1.00 38.70  ? 421 TYR   A OH  1 
ATOM   1759 N N   . ARG   A 1 216 ? 9.983  50.040 11.258  1.00 26.38  ? 422 ARG   A N   1 
ATOM   1760 C CA  A ARG   A 1 216 ? 9.743  49.061 12.310  0.48 30.40  ? 422 ARG   A CA  1 
ATOM   1761 C CA  B ARG   A 1 216 ? 9.760  49.030 12.274  0.52 31.41  ? 422 ARG   A CA  1 
ATOM   1762 C C   . ARG   A 1 216 ? 8.316  48.548 12.195  1.00 30.86  ? 422 ARG   A C   1 
ATOM   1763 O O   . ARG   A 1 216 ? 7.394  49.324 11.942  1.00 31.13  ? 422 ARG   A O   1 
ATOM   1764 C CB  A ARG   A 1 216 ? 9.920  49.694 13.694  0.48 32.25  ? 422 ARG   A CB  1 
ATOM   1765 C CB  B ARG   A 1 216 ? 10.072 49.587 13.667  0.52 32.34  ? 422 ARG   A CB  1 
ATOM   1766 C CG  A ARG   A 1 216 ? 11.331 50.007 14.127  0.48 35.00  ? 422 ARG   A CG  1 
ATOM   1767 C CG  B ARG   A 1 216 ? 11.559 49.834 13.895  0.52 34.54  ? 422 ARG   A CG  1 
ATOM   1768 C CD  A ARG   A 1 216 ? 11.308 50.715 15.484  0.48 34.05  ? 422 ARG   A CD  1 
ATOM   1769 C CD  B ARG   A 1 216 ? 11.901 50.016 15.367  0.52 36.25  ? 422 ARG   A CD  1 
ATOM   1770 N NE  A ARG   A 1 216 ? 10.550 51.962 15.434  0.48 34.54  ? 422 ARG   A NE  1 
ATOM   1771 N NE  B ARG   A 1 216 ? 12.354 48.765 15.966  0.52 38.55  ? 422 ARG   A NE  1 
ATOM   1772 C CZ  A ARG   A 1 216 ? 9.386  52.161 16.040  0.48 34.87  ? 422 ARG   A CZ  1 
ATOM   1773 C CZ  B ARG   A 1 216 ? 13.626 48.432 16.133  0.52 31.52  ? 422 ARG   A CZ  1 
ATOM   1774 N NH1 A ARG   A 1 216 ? 8.813  51.213 16.761  0.48 29.69  ? 422 ARG   A NH1 1 
ATOM   1775 N NH1 B ARG   A 1 216 ? 14.607 49.233 15.751  0.52 31.26  ? 422 ARG   A NH1 1 
ATOM   1776 N NH2 A ARG   A 1 216 ? 8.783  53.342 15.919  0.48 36.10  ? 422 ARG   A NH2 1 
ATOM   1777 N NH2 B ARG   A 1 216 ? 13.922 47.266 16.699  0.52 37.53  ? 422 ARG   A NH2 1 
ATOM   1778 N N   . LEU   A 1 217 ? 8.125  47.253 12.388  1.00 30.94  ? 423 LEU   A N   1 
ATOM   1779 C CA  . LEU   A 1 217 ? 6.792  46.661 12.373  1.00 30.28  ? 423 LEU   A CA  1 
ATOM   1780 C C   . LEU   A 1 217 ? 6.298  46.581 13.813  1.00 32.96  ? 423 LEU   A C   1 
ATOM   1781 O O   . LEU   A 1 217 ? 6.998  46.033 14.665  1.00 31.19  ? 423 LEU   A O   1 
ATOM   1782 C CB  . LEU   A 1 217 ? 6.818  45.276 11.736  1.00 27.63  ? 423 LEU   A CB  1 
ATOM   1783 C CG  . LEU   A 1 217 ? 6.885  45.240 10.203  1.00 28.86  ? 423 LEU   A CG  1 
ATOM   1784 C CD1 . LEU   A 1 217 ? 7.103  43.807 9.738   1.00 23.62  ? 423 LEU   A CD1 1 
ATOM   1785 C CD2 . LEU   A 1 217 ? 5.604  45.810 9.607   1.00 30.76  ? 423 LEU   A CD2 1 
ATOM   1786 N N   . VAL   A 1 218 ? 5.121  47.161 14.086  1.00 27.50  ? 424 VAL   A N   1 
ATOM   1787 C CA  . VAL   A 1 218 ? 4.521  47.179 15.419  1.00 35.56  ? 424 VAL   A CA  1 
ATOM   1788 C C   . VAL   A 1 218 ? 3.097  46.615 15.360  1.00 42.37  ? 424 VAL   A C   1 
ATOM   1789 O O   . VAL   A 1 218 ? 2.455  46.576 14.307  1.00 36.83  ? 424 VAL   A O   1 
ATOM   1790 C CB  . VAL   A 1 218 ? 4.502  48.595 16.035  1.00 35.39  ? 424 VAL   A CB  1 
ATOM   1791 C CG1 . VAL   A 1 218 ? 5.914  49.164 16.152  1.00 32.95  ? 424 VAL   A CG1 1 
ATOM   1792 C CG2 . VAL   A 1 218 ? 3.625  49.520 15.211  1.00 35.10  ? 424 VAL   A CG2 1 
ATOM   1793 N N   . LYS   A 1 219 ? 2.600  46.181 16.519  1.00 37.08  ? 425 LYS   A N   1 
ATOM   1794 C CA  . LYS   A 1 219 ? 1.298  45.497 16.568  1.00 45.16  ? 425 LYS   A CA  1 
ATOM   1795 C C   . LYS   A 1 219 ? 0.162  46.498 16.707  1.00 52.05  ? 425 LYS   A C   1 
ATOM   1796 O O   . LYS   A 1 219 ? 0.359  47.599 17.221  1.00 54.75  ? 425 LYS   A O   1 
ATOM   1797 C CB  . LYS   A 1 219 ? 1.242  44.505 17.728  1.00 52.97  ? 425 LYS   A CB  1 
ATOM   1798 C CG  . LYS   A 1 219 ? 1.436  45.158 19.099  1.00 66.24  ? 425 LYS   A CG  1 
ATOM   1799 C CD  . LYS   A 1 219 ? 1.847  44.155 20.176  1.00 66.98  ? 425 LYS   A CD  1 
ATOM   1800 C CE  . LYS   A 1 219 ? 1.931  44.827 21.543  1.00 74.12  ? 425 LYS   A CE  1 
ATOM   1801 N NZ  . LYS   A 1 219 ? 2.873  45.983 21.571  1.00 71.40  ? 425 LYS   A NZ  1 
ATOM   1802 N N   . GLY   B 1 1   ? 24.322 54.058 19.880  1.00 50.33  ? 207 GLY   B N   1 
ATOM   1803 C CA  . GLY   B 1 1   ? 24.178 54.120 18.435  1.00 47.82  ? 207 GLY   B CA  1 
ATOM   1804 C C   . GLY   B 1 1   ? 24.849 52.973 17.698  1.00 45.03  ? 207 GLY   B C   1 
ATOM   1805 O O   . GLY   B 1 1   ? 24.913 51.852 18.208  1.00 48.22  ? 207 GLY   B O   1 
ATOM   1806 N N   . PRO   B 1 2   ? 25.358 53.247 16.502  1.00 40.74  ? 208 PRO   B N   1 
ATOM   1807 C CA  . PRO   B 1 2   ? 25.892 52.176 15.654  1.00 37.86  ? 208 PRO   B CA  1 
ATOM   1808 C C   . PRO   B 1 2   ? 27.276 51.723 16.101  1.00 38.08  ? 208 PRO   B C   1 
ATOM   1809 O O   . PRO   B 1 2   ? 27.944 52.360 16.915  1.00 35.48  ? 208 PRO   B O   1 
ATOM   1810 C CB  . PRO   B 1 2   ? 25.951 52.832 14.274  1.00 42.38  ? 208 PRO   B CB  1 
ATOM   1811 C CG  . PRO   B 1 2   ? 26.217 54.282 14.594  1.00 44.55  ? 208 PRO   B CG  1 
ATOM   1812 C CD  . PRO   B 1 2   ? 25.382 54.555 15.822  1.00 44.31  ? 208 PRO   B CD  1 
ATOM   1813 N N   . ARG   B 1 3   ? 27.695 50.587 15.534  1.00 29.87  ? 209 ARG   B N   1 
ATOM   1814 C CA  . ARG   B 1 3   ? 29.033 50.064 15.766  1.00 33.75  ? 209 ARG   B CA  1 
ATOM   1815 C C   . ARG   B 1 3   ? 30.069 50.807 14.920  1.00 34.72  ? 209 ARG   B C   1 
ATOM   1816 O O   . ARG   B 1 3   ? 31.150 51.140 15.415  1.00 28.92  ? 209 ARG   B O   1 
ATOM   1817 C CB  . ARG   B 1 3   ? 29.055 48.555 15.471  1.00 33.39  ? 209 ARG   B CB  1 
ATOM   1818 C CG  . ARG   B 1 3   ? 30.356 47.854 15.815  1.00 32.62  ? 209 ARG   B CG  1 
ATOM   1819 C CD  . ARG   B 1 3   ? 30.520 46.499 15.097  1.00 34.38  ? 209 ARG   B CD  1 
ATOM   1820 N NE  . ARG   B 1 3   ? 30.312 46.638 13.663  1.00 38.56  ? 209 ARG   B NE  1 
ATOM   1821 C CZ  . ARG   B 1 3   ? 31.224 47.092 12.811  1.00 46.67  ? 209 ARG   B CZ  1 
ATOM   1822 N NH1 . ARG   B 1 3   ? 32.452 47.398 13.207  1.00 37.11  ? 209 ARG   B NH1 1 
ATOM   1823 N NH2 . ARG   B 1 3   ? 30.900 47.235 11.526  1.00 42.87  ? 209 ARG   B NH2 1 
ATOM   1824 N N   . SER   B 1 4   ? 29.758 51.096 13.652  1.00 26.63  ? 210 SER   B N   1 
ATOM   1825 C CA  . SER   B 1 4   ? 30.700 51.819 12.806  1.00 26.56  ? 210 SER   B CA  1 
ATOM   1826 C C   . SER   B 1 4   ? 30.739 53.303 13.175  1.00 26.96  ? 210 SER   B C   1 
ATOM   1827 O O   . SER   B 1 4   ? 29.839 53.838 13.827  1.00 26.11  ? 210 SER   B O   1 
ATOM   1828 C CB  . SER   B 1 4   ? 30.329 51.664 11.328  1.00 27.93  ? 210 SER   B CB  1 
ATOM   1829 O OG  . SER   B 1 4   ? 29.070 52.253 11.093  1.00 37.09  ? 210 SER   B OG  1 
ATOM   1830 N N   . ILE   B 1 5   ? 31.786 53.975 12.716  1.00 26.41  ? 211 ILE   B N   1 
ATOM   1831 C CA  . ILE   B 1 5   ? 32.091 55.349 13.098  1.00 23.28  ? 211 ILE   B CA  1 
ATOM   1832 C C   . ILE   B 1 5   ? 31.977 56.262 11.876  1.00 27.95  ? 211 ILE   B C   1 
ATOM   1833 O O   . ILE   B 1 5   ? 32.773 56.169 10.933  1.00 26.55  ? 211 ILE   B O   1 
ATOM   1834 C CB  . ILE   B 1 5   ? 33.488 55.436 13.735  1.00 26.86  ? 211 ILE   B CB  1 
ATOM   1835 C CG1 . ILE   B 1 5   ? 33.599 54.408 14.866  1.00 30.23  ? 211 ILE   B CG1 1 
ATOM   1836 C CG2 . ILE   B 1 5   ? 33.787 56.861 14.191  1.00 25.49  ? 211 ILE   B CG2 1 
ATOM   1837 C CD1 . ILE   B 1 5   ? 34.973 54.025 15.247  1.00 28.78  ? 211 ILE   B CD1 1 
ATOM   1838 N N   . GLY   B 1 6   ? 31.019 57.179 11.891  1.00 24.62  ? 212 GLY   B N   1 
ATOM   1839 C CA  . GLY   B 1 6   ? 30.984 58.203 10.874  1.00 25.51  ? 212 GLY   B CA  1 
ATOM   1840 C C   . GLY   B 1 6   ? 29.566 58.509 10.457  1.00 29.59  ? 212 GLY   B C   1 
ATOM   1841 O O   . GLY   B 1 6   ? 28.625 58.295 11.209  1.00 28.57  ? 212 GLY   B O   1 
ATOM   1842 N N   . THR   B 1 7   ? 29.438 59.006 9.236   1.00 31.56  ? 213 THR   B N   1 
ATOM   1843 C CA  . THR   B 1 7   ? 28.174 59.388 8.635   1.00 35.25  ? 213 THR   B CA  1 
ATOM   1844 C C   . THR   B 1 7   ? 28.059 58.727 7.260   1.00 32.00  ? 213 THR   B C   1 
ATOM   1845 O O   . THR   B 1 7   ? 28.988 58.064 6.787   1.00 29.15  ? 213 THR   B O   1 
ATOM   1846 C CB  . THR   B 1 7   ? 28.072 60.914 8.502   1.00 36.20  ? 213 THR   B CB  1 
ATOM   1847 O OG1 . THR   B 1 7   ? 29.044 61.372 7.552   1.00 33.16  ? 213 THR   B OG1 1 
ATOM   1848 C CG2 . THR   B 1 7   ? 28.338 61.586 9.844   1.00 39.75  ? 213 THR   B CG2 1 
ATOM   1849 N N   . THR   B 1 8   ? 26.910 58.940 6.607   1.00 31.87  ? 214 THR   B N   1 
ATOM   1850 C CA  . THR   B 1 8   ? 26.699 58.450 5.240   1.00 33.55  ? 214 THR   B CA  1 
ATOM   1851 C C   . THR   B 1 8   ? 27.853 58.828 4.328   1.00 33.64  ? 214 THR   B C   1 
ATOM   1852 O O   . THR   B 1 8   ? 28.321 58.016 3.520   1.00 30.73  ? 214 THR   B O   1 
ATOM   1853 C CB  . THR   B 1 8   ? 25.397 59.028 4.691   1.00 38.20  ? 214 THR   B CB  1 
ATOM   1854 O OG1 . THR   B 1 8   ? 24.344 58.733 5.604   1.00 44.38  ? 214 THR   B OG1 1 
ATOM   1855 C CG2 . THR   B 1 8   ? 25.052 58.420 3.331   1.00 38.27  ? 214 THR   B CG2 1 
ATOM   1856 N N   . LYS   B 1 9   ? 28.341 60.054 4.465   1.00 31.57  ? 215 LYS   B N   1 
ATOM   1857 C CA  . LYS   B 1 9   ? 29.417 60.521 3.608   1.00 30.56  ? 215 LYS   B CA  1 
ATOM   1858 C C   . LYS   B 1 9   ? 30.676 59.675 3.773   1.00 35.34  ? 215 LYS   B C   1 
ATOM   1859 O O   . LYS   B 1 9   ? 31.416 59.469 2.808   1.00 33.29  ? 215 LYS   B O   1 
ATOM   1860 C CB  . LYS   B 1 9   ? 29.700 61.989 3.914   1.00 34.25  ? 215 LYS   B CB  1 
ATOM   1861 C CG  . LYS   B 1 9   ? 30.748 62.618 3.025   1.00 48.21  ? 215 LYS   B CG  1 
ATOM   1862 C CD  . LYS   B 1 9   ? 30.239 63.887 2.360   0.00 42.74  ? 215 LYS   B CD  1 
ATOM   1863 C CE  . LYS   B 1 9   ? 31.205 64.368 1.287   0.00 43.29  ? 215 LYS   B CE  1 
ATOM   1864 N NZ  . LYS   B 1 9   ? 31.352 63.384 0.177   0.00 42.71  ? 215 LYS   B NZ  1 
ATOM   1865 N N   . LEU   B 1 10  ? 30.956 59.201 4.992   1.00 27.27  ? 216 LEU   B N   1 
ATOM   1866 C CA  . LEU   B 1 10  ? 32.107 58.322 5.215   1.00 28.74  ? 216 LEU   B CA  1 
ATOM   1867 C C   . LEU   B 1 10  ? 32.061 57.673 6.587   1.00 27.17  ? 216 LEU   B C   1 
ATOM   1868 O O   . LEU   B 1 10  ? 31.966 58.362 7.601   1.00 28.37  ? 216 LEU   B O   1 
ATOM   1869 C CB  . LEU   B 1 10  ? 33.432 59.063 5.053   1.00 21.92  ? 216 LEU   B CB  1 
ATOM   1870 C CG  . LEU   B 1 10  ? 34.550 58.012 4.909   1.00 31.46  ? 216 LEU   B CG  1 
ATOM   1871 C CD1 . LEU   B 1 10  ? 34.744 57.605 3.449   1.00 30.38  ? 216 LEU   B CD1 1 
ATOM   1872 C CD2 . LEU   B 1 10  ? 35.846 58.454 5.507   1.00 32.86  ? 216 LEU   B CD2 1 
ATOM   1873 N N   . ARG   B 1 11  ? 32.114 56.350 6.625   1.00 27.66  ? 217 ARG   B N   1 
ATOM   1874 C CA  . ARG   B 1 11  ? 32.046 55.586 7.859   1.00 29.88  ? 217 ARG   B CA  1 
ATOM   1875 C C   . ARG   B 1 11  ? 33.245 54.662 7.905   1.00 27.63  ? 217 ARG   B C   1 
ATOM   1876 O O   . ARG   B 1 11  ? 33.533 53.985 6.912   1.00 26.62  ? 217 ARG   B O   1 
ATOM   1877 C CB  . ARG   B 1 11  ? 30.783 54.720 7.921   1.00 27.19  ? 217 ARG   B CB  1 
ATOM   1878 C CG  . ARG   B 1 11  ? 29.559 55.398 8.378   1.00 37.32  ? 217 ARG   B CG  1 
ATOM   1879 C CD  . ARG   B 1 11  ? 28.406 54.422 8.310   1.00 33.87  ? 217 ARG   B CD  1 
ATOM   1880 N NE  . ARG   B 1 11  ? 27.165 55.048 8.732   1.00 36.51  ? 217 ARG   B NE  1 
ATOM   1881 C CZ  . ARG   B 1 11  ? 26.151 55.332 7.926   1.00 36.37  ? 217 ARG   B CZ  1 
ATOM   1882 N NH1 . ARG   B 1 11  ? 26.202 55.067 6.632   1.00 35.32  ? 217 ARG   B NH1 1 
ATOM   1883 N NH2 . ARG   B 1 11  ? 25.054 55.890 8.437   1.00 42.14  ? 217 ARG   B NH2 1 
ATOM   1884 N N   . LEU   B 1 12  ? 33.904 54.596 9.062   1.00 26.07  ? 218 LEU   B N   1 
ATOM   1885 C CA  . LEU   B 1 12  ? 34.871 53.543 9.334   1.00 27.03  ? 218 LEU   B CA  1 
ATOM   1886 C C   . LEU   B 1 12  ? 34.082 52.337 9.821   1.00 21.84  ? 218 LEU   B C   1 
ATOM   1887 O O   . LEU   B 1 12  ? 33.446 52.407 10.871  1.00 25.97  ? 218 LEU   B O   1 
ATOM   1888 C CB  . LEU   B 1 12  ? 35.884 53.989 10.398  1.00 23.54  ? 218 LEU   B CB  1 
ATOM   1889 C CG  . LEU   B 1 12  ? 36.904 52.956 10.888  1.00 24.62  ? 218 LEU   B CG  1 
ATOM   1890 C CD1 . LEU   B 1 12  ? 37.889 52.595 9.755   1.00 22.23  ? 218 LEU   B CD1 1 
ATOM   1891 C CD2 . LEU   B 1 12  ? 37.672 53.402 12.149  1.00 25.37  ? 218 LEU   B CD2 1 
ATOM   1892 N N   . VAL   B 1 13  ? 34.098 51.238 9.070   1.00 22.03  ? 219 VAL   B N   1 
ATOM   1893 C CA  . VAL   B 1 13  ? 33.254 50.090 9.395   1.00 24.80  ? 219 VAL   B CA  1 
ATOM   1894 C C   . VAL   B 1 13  ? 34.052 48.902 9.889   1.00 25.98  ? 219 VAL   B C   1 
ATOM   1895 O O   . VAL   B 1 13  ? 33.464 47.959 10.447  1.00 29.21  ? 219 VAL   B O   1 
ATOM   1896 C CB  . VAL   B 1 13  ? 32.368 49.671 8.199   1.00 24.42  ? 219 VAL   B CB  1 
ATOM   1897 C CG1 . VAL   B 1 13  ? 31.470 50.832 7.762   1.00 28.40  ? 219 VAL   B CG1 1 
ATOM   1898 C CG2 . VAL   B 1 13  ? 33.204 49.139 7.035   1.00 22.76  ? 219 VAL   B CG2 1 
ATOM   1899 N N   . GLU   B 1 14  ? 35.358 48.913 9.721   1.00 22.98  ? 220 GLU   B N   1 
ATOM   1900 C CA  . GLU   B 1 14  ? 36.146 47.770 10.130  1.00 28.38  ? 220 GLU   B CA  1 
ATOM   1901 C C   . GLU   B 1 14  ? 37.496 48.326 10.513  1.00 31.95  ? 220 GLU   B C   1 
ATOM   1902 O O   . GLU   B 1 14  ? 38.024 49.205 9.825   1.00 28.12  ? 220 GLU   B O   1 
ATOM   1903 C CB  . GLU   B 1 14  ? 36.269 46.740 9.007   1.00 32.80  ? 220 GLU   B CB  1 
ATOM   1904 C CG  . GLU   B 1 14  ? 36.524 45.318 9.520   1.00 51.93  ? 220 GLU   B CG  1 
ATOM   1905 C CD  . GLU   B 1 14  ? 36.468 44.267 8.421   1.00 69.32  ? 220 GLU   B CD  1 
ATOM   1906 O OE1 . GLU   B 1 14  ? 36.434 44.640 7.226   1.00 67.27  ? 220 GLU   B OE1 1 
ATOM   1907 O OE2 . GLU   B 1 14  ? 36.474 43.067 8.747   1.00 69.64  ? 220 GLU   B OE2 1 
ATOM   1908 N N   . PHE   B 1 15  ? 38.005 47.874 11.645  1.00 29.30  ? 221 PHE   B N   1 
ATOM   1909 C CA  . PHE   B 1 15  ? 39.304 48.322 12.098  1.00 25.83  ? 221 PHE   B CA  1 
ATOM   1910 C C   . PHE   B 1 15  ? 39.846 47.300 13.074  1.00 31.89  ? 221 PHE   B C   1 
ATOM   1911 O O   . PHE   B 1 15  ? 39.094 46.768 13.903  1.00 27.77  ? 221 PHE   B O   1 
ATOM   1912 C CB  . PHE   B 1 15  ? 39.262 49.692 12.778  1.00 28.88  ? 221 PHE   B CB  1 
ATOM   1913 C CG  . PHE   B 1 15  ? 40.554 50.030 13.433  1.00 29.95  ? 221 PHE   B CG  1 
ATOM   1914 C CD1 . PHE   B 1 15  ? 41.651 50.398 12.670  1.00 33.17  ? 221 PHE   B CD1 1 
ATOM   1915 C CD2 . PHE   B 1 15  ? 40.723 49.831 14.793  1.00 31.81  ? 221 PHE   B CD2 1 
ATOM   1916 C CE1 . PHE   B 1 15  ? 42.877 50.656 13.264  1.00 33.95  ? 221 PHE   B CE1 1 
ATOM   1917 C CE2 . PHE   B 1 15  ? 41.951 50.079 15.396  1.00 31.88  ? 221 PHE   B CE2 1 
ATOM   1918 C CZ  . PHE   B 1 15  ? 43.032 50.493 14.623  1.00 31.07  ? 221 PHE   B CZ  1 
ATOM   1919 N N   . SER   B 1 16  ? 41.141 47.018 12.959  1.00 25.65  ? 222 SER   B N   1 
ATOM   1920 C CA  . SER   B 1 16  ? 41.814 46.247 13.987  1.00 28.70  ? 222 SER   B CA  1 
ATOM   1921 C C   . SER   B 1 16  ? 43.311 46.459 13.873  1.00 25.01  ? 222 SER   B C   1 
ATOM   1922 O O   . SER   B 1 16  ? 43.846 46.686 12.788  1.00 24.80  ? 222 SER   B O   1 
ATOM   1923 C CB  . SER   B 1 16  ? 41.453 44.754 13.923  1.00 27.71  ? 222 SER   B CB  1 
ATOM   1924 O OG  . SER   B 1 16  ? 42.190 44.069 12.946  1.00 36.87  ? 222 SER   B OG  1 
ATOM   1925 N N   . ALA   B 1 17  ? 43.972 46.415 15.019  1.00 21.64  ? 223 ALA   B N   1 
ATOM   1926 C CA  . ALA   B 1 17  ? 45.421 46.395 15.102  1.00 23.02  ? 223 ALA   B CA  1 
ATOM   1927 C C   . ALA   B 1 17  ? 45.779 45.087 15.768  1.00 25.13  ? 223 ALA   B C   1 
ATOM   1928 O O   . ALA   B 1 17  ? 45.197 44.742 16.801  1.00 27.82  ? 223 ALA   B O   1 
ATOM   1929 C CB  . ALA   B 1 17  ? 45.959 47.580 15.905  1.00 21.56  ? 223 ALA   B CB  1 
ATOM   1930 N N   . PHE   B 1 18  ? 46.705 44.343 15.173  1.00 22.76  ? 224 PHE   B N   1 
ATOM   1931 C CA  . PHE   B 1 18  ? 46.824 42.942 15.538  1.00 23.42  ? 224 PHE   B CA  1 
ATOM   1932 C C   . PHE   B 1 18  ? 48.269 42.457 15.439  1.00 26.59  ? 224 PHE   B C   1 
ATOM   1933 O O   . PHE   B 1 18  ? 49.135 43.108 14.862  1.00 24.24  ? 224 PHE   B O   1 
ATOM   1934 C CB  . PHE   B 1 18  ? 45.904 42.091 14.650  1.00 20.69  ? 224 PHE   B CB  1 
ATOM   1935 C CG  . PHE   B 1 18  ? 46.177 42.249 13.174  1.00 22.70  ? 224 PHE   B CG  1 
ATOM   1936 C CD1 . PHE   B 1 18  ? 47.181 41.525 12.559  1.00 23.39  ? 224 PHE   B CD1 1 
ATOM   1937 C CD2 . PHE   B 1 18  ? 45.431 43.127 12.414  1.00 21.89  ? 224 PHE   B CD2 1 
ATOM   1938 C CE1 . PHE   B 1 18  ? 47.445 41.685 11.190  1.00 30.12  ? 224 PHE   B CE1 1 
ATOM   1939 C CE2 . PHE   B 1 18  ? 45.686 43.299 11.043  1.00 25.42  ? 224 PHE   B CE2 1 
ATOM   1940 C CZ  . PHE   B 1 18  ? 46.695 42.568 10.437  1.00 31.87  ? 224 PHE   B CZ  1 
ATOM   1941 N N   . LEU   B 1 19  ? 48.498 41.274 16.000  1.00 25.23  ? 225 LEU   B N   1 
ATOM   1942 C CA  . LEU   B 1 19  ? 49.763 40.552 15.912  1.00 22.57  ? 225 LEU   B CA  1 
ATOM   1943 C C   . LEU   B 1 19  ? 49.471 39.146 15.401  1.00 27.35  ? 225 LEU   B C   1 
ATOM   1944 O O   . LEU   B 1 19  ? 48.664 38.430 16.002  1.00 26.20  ? 225 LEU   B O   1 
ATOM   1945 C CB  . LEU   B 1 19  ? 50.430 40.481 17.289  1.00 23.61  ? 225 LEU   B CB  1 
ATOM   1946 C CG  . LEU   B 1 19  ? 51.625 39.532 17.418  1.00 28.05  ? 225 LEU   B CG  1 
ATOM   1947 C CD1 . LEU   B 1 19  ? 52.692 39.889 16.380  1.00 32.29  ? 225 LEU   B CD1 1 
ATOM   1948 C CD2 . LEU   B 1 19  ? 52.194 39.609 18.831  1.00 28.99  ? 225 LEU   B CD2 1 
ATOM   1949 N N   . GLU   B 1 20  ? 50.096 38.761 14.289  1.00 26.56  ? 226 GLU   B N   1 
ATOM   1950 C CA  . GLU   B 1 20  ? 50.034 37.394 13.776  1.00 29.60  ? 226 GLU   B CA  1 
ATOM   1951 C C   . GLU   B 1 20  ? 51.353 36.696 14.058  1.00 32.61  ? 226 GLU   B C   1 
ATOM   1952 O O   . GLU   B 1 20  ? 52.420 37.266 13.833  1.00 28.54  ? 226 GLU   B O   1 
ATOM   1953 C CB  . GLU   B 1 20  ? 49.767 37.327 12.255  1.00 29.42  ? 226 GLU   B CB  1 
ATOM   1954 C CG  . GLU   B 1 20  ? 48.447 37.927 11.818  1.00 38.24  ? 226 GLU   B CG  1 
ATOM   1955 C CD  . GLU   B 1 20  ? 48.302 38.077 10.291  1.00 53.85  ? 226 GLU   B CD  1 
ATOM   1956 O OE1 . GLU   B 1 20  ? 49.290 38.398 9.596   1.00 55.11  ? 226 GLU   B OE1 1 
ATOM   1957 O OE2 . GLU   B 1 20  ? 47.164 37.921 9.793   1.00 53.37  ? 226 GLU   B OE2 1 
ATOM   1958 N N   . GLN   B 1 21  ? 51.275 35.458 14.537  1.00 29.28  ? 227 GLN   B N   1 
ATOM   1959 C CA  . GLN   B 1 21  ? 52.452 34.677 14.889  1.00 31.15  ? 227 GLN   B CA  1 
ATOM   1960 C C   . GLN   B 1 21  ? 52.318 33.282 14.290  1.00 40.26  ? 227 GLN   B C   1 
ATOM   1961 O O   . GLN   B 1 21  ? 51.301 32.611 14.487  1.00 37.17  ? 227 GLN   B O   1 
ATOM   1962 C CB  . GLN   B 1 21  ? 52.615 34.597 16.415  1.00 39.90  ? 227 GLN   B CB  1 
ATOM   1963 C CG  . GLN   B 1 21  ? 53.004 35.936 17.058  1.00 39.17  ? 227 GLN   B CG  1 
ATOM   1964 C CD  . GLN   B 1 21  ? 53.108 35.877 18.580  1.00 47.45  ? 227 GLN   B CD  1 
ATOM   1965 O OE1 . GLN   B 1 21  ? 54.188 36.041 19.138  1.00 51.09  ? 227 GLN   B OE1 1 
ATOM   1966 N NE2 . GLN   B 1 21  ? 51.986 35.665 19.251  1.00 39.06  ? 227 GLN   B NE2 1 
ATOM   1967 N N   . GLN   B 1 22  ? 53.330 32.848 13.556  1.00 42.20  ? 228 GLN   B N   1 
ATOM   1968 C CA  . GLN   B 1 22  ? 53.365 31.481 13.054  1.00 42.77  ? 228 GLN   B CA  1 
ATOM   1969 C C   . GLN   B 1 22  ? 54.127 30.640 14.063  1.00 51.04  ? 228 GLN   B C   1 
ATOM   1970 O O   . GLN   B 1 22  ? 55.355 30.720 14.149  1.00 47.73  ? 228 GLN   B O   1 
ATOM   1971 C CB  . GLN   B 1 22  ? 54.026 31.399 11.690  1.00 48.79  ? 228 GLN   B CB  1 
ATOM   1972 C CG  . GLN   B 1 22  ? 54.048 29.996 11.151  1.00 47.59  ? 228 GLN   B CG  1 
ATOM   1973 C CD  . GLN   B 1 22  ? 52.977 29.784 10.126  1.00 44.29  ? 228 GLN   B CD  1 
ATOM   1974 O OE1 . GLN   B 1 22  ? 52.262 30.725 9.768   1.00 46.54  ? 228 GLN   B OE1 1 
ATOM   1975 N NE2 . GLN   B 1 22  ? 52.839 28.550 9.649   1.00 40.22  ? 228 GLN   B NE2 1 
ATOM   1976 N N   . ARG   B 1 23  ? 53.422 29.838 14.786  1.00 75.52  ? 229 ARG   B N   1 
ATOM   1977 C CA  . ARG   B 1 23  ? 54.023 29.023 15.801  1.00 75.99  ? 229 ARG   B CA  1 
ATOM   1978 C C   . ARG   B 1 23  ? 54.624 27.732 15.266  1.00 70.56  ? 229 ARG   B C   1 
ATOM   1979 O O   . ARG   B 1 23  ? 55.738 27.401 15.615  1.00 74.26  ? 229 ARG   B O   1 
ATOM   1980 C CB  . ARG   B 1 23  ? 52.889 28.702 16.760  1.00 81.41  ? 229 ARG   B CB  1 
ATOM   1981 C CG  . ARG   B 1 23  ? 51.511 28.666 16.103  1.00 75.68  ? 229 ARG   B CG  1 
ATOM   1982 C CD  . ARG   B 1 23  ? 50.406 28.275 17.054  1.00 75.95  ? 229 ARG   B CD  1 
ATOM   1983 N NE  . ARG   B 1 23  ? 50.223 26.835 17.104  1.00 89.59  ? 229 ARG   B NE  1 
ATOM   1984 C CZ  . ARG   B 1 23  ? 50.156 26.131 18.226  1.00 98.33  ? 229 ARG   B CZ  1 
ATOM   1985 N NH1 . ARG   B 1 23  ? 50.254 26.736 19.402  1.00 101.75 ? 229 ARG   B NH1 1 
ATOM   1986 N NH2 . ARG   B 1 23  ? 49.992 24.820 18.171  1.00 101.22 ? 229 ARG   B NH2 1 
ATOM   1987 N N   . ASP   B 1 24  ? 53.911 27.029 14.413  1.00 66.00  ? 230 ASP   B N   1 
ATOM   1988 C CA  . ASP   B 1 24  ? 54.304 25.731 13.870  1.00 61.33  ? 230 ASP   B CA  1 
ATOM   1989 C C   . ASP   B 1 24  ? 54.116 25.777 12.357  1.00 53.61  ? 230 ASP   B C   1 
ATOM   1990 O O   . ASP   B 1 24  ? 53.574 26.768 11.846  1.00 51.10  ? 230 ASP   B O   1 
ATOM   1991 C CB  . ASP   B 1 24  ? 53.466 24.612 14.502  1.00 63.47  ? 230 ASP   B CB  1 
ATOM   1992 C CG  . ASP   B 1 24  ? 53.523 24.616 16.022  1.00 80.77  ? 230 ASP   B CG  1 
ATOM   1993 O OD1 . ASP   B 1 24  ? 54.637 24.751 16.576  1.00 85.16  ? 230 ASP   B OD1 1 
ATOM   1994 O OD2 . ASP   B 1 24  ? 52.457 24.453 16.663  1.00 79.02  ? 230 ASP   B OD2 1 
ATOM   1995 N N   . PRO   B 1 25  ? 54.533 24.757 11.596  1.00 53.54  ? 231 PRO   B N   1 
ATOM   1996 C CA  . PRO   B 1 25  ? 54.429 24.877 10.128  1.00 48.93  ? 231 PRO   B CA  1 
ATOM   1997 C C   . PRO   B 1 25  ? 52.997 24.930 9.586   1.00 44.22  ? 231 PRO   B C   1 
ATOM   1998 O O   . PRO   B 1 25  ? 52.801 25.476 8.495   1.00 44.28  ? 231 PRO   B O   1 
ATOM   1999 C CB  . PRO   B 1 25  ? 55.181 23.645 9.598   1.00 54.76  ? 231 PRO   B CB  1 
ATOM   2000 C CG  . PRO   B 1 25  ? 55.730 22.928 10.765  1.00 55.40  ? 231 PRO   B CG  1 
ATOM   2001 C CD  . PRO   B 1 25  ? 55.244 23.534 12.025  1.00 54.49  ? 231 PRO   B CD  1 
ATOM   2002 N N   . ASP   B 1 26  ? 51.991 24.397 10.280  1.00 36.20  ? 232 ASP   B N   1 
ATOM   2003 C CA  . ASP   B 1 26  ? 50.632 24.421 9.740   1.00 34.41  ? 232 ASP   B CA  1 
ATOM   2004 C C   . ASP   B 1 26  ? 49.654 25.208 10.596  1.00 35.29  ? 232 ASP   B C   1 
ATOM   2005 O O   . ASP   B 1 26  ? 48.439 25.034 10.459  1.00 31.09  ? 232 ASP   B O   1 
ATOM   2006 C CB  . ASP   B 1 26  ? 50.091 23.010 9.531   1.00 32.54  ? 232 ASP   B CB  1 
ATOM   2007 C CG  . ASP   B 1 26  ? 50.947 22.218 8.582   1.00 40.23  ? 232 ASP   B CG  1 
ATOM   2008 O OD1 . ASP   B 1 26  ? 51.138 22.695 7.442   1.00 36.92  ? 232 ASP   B OD1 1 
ATOM   2009 O OD2 . ASP   B 1 26  ? 51.399 21.128 8.971   1.00 38.51  ? 232 ASP   B OD2 1 
ATOM   2010 N N   . SER   B 1 27  ? 50.134 26.060 11.480  1.00 35.37  ? 233 SER   B N   1 
ATOM   2011 C CA  . SER   B 1 27  ? 49.197 26.753 12.341  1.00 40.47  ? 233 SER   B CA  1 
ATOM   2012 C C   . SER   B 1 27  ? 49.693 28.163 12.593  1.00 43.10  ? 233 SER   B C   1 
ATOM   2013 O O   . SER   B 1 27  ? 50.895 28.426 12.564  1.00 37.84  ? 233 SER   B O   1 
ATOM   2014 C CB  . SER   B 1 27  ? 48.991 26.005 13.663  1.00 44.79  ? 233 SER   B CB  1 
ATOM   2015 O OG  . SER   B 1 27  ? 50.181 25.993 14.424  1.00 58.85  ? 233 SER   B OG  1 
ATOM   2016 N N   . TYR   B 1 28  ? 48.751 29.077 12.817  1.00 33.35  ? 234 TYR   B N   1 
ATOM   2017 C CA  . TYR   B 1 28  ? 49.119 30.422 13.216  1.00 41.08  ? 234 TYR   B CA  1 
ATOM   2018 C C   . TYR   B 1 28  ? 48.124 30.954 14.238  1.00 40.48  ? 234 TYR   B C   1 
ATOM   2019 O O   . TYR   B 1 28  ? 47.006 30.451 14.370  1.00 34.44  ? 234 TYR   B O   1 
ATOM   2020 C CB  . TYR   B 1 28  ? 49.239 31.351 12.009  1.00 45.54  ? 234 TYR   B CB  1 
ATOM   2021 C CG  . TYR   B 1 28  ? 47.933 31.811 11.407  1.00 33.30  ? 234 TYR   B CG  1 
ATOM   2022 C CD1 . TYR   B 1 28  ? 47.324 31.081 10.410  1.00 37.43  ? 234 TYR   B CD1 1 
ATOM   2023 C CD2 . TYR   B 1 28  ? 47.316 32.977 11.836  1.00 39.62  ? 234 TYR   B CD2 1 
ATOM   2024 C CE1 . TYR   B 1 28  ? 46.128 31.498 9.849   1.00 38.95  ? 234 TYR   B CE1 1 
ATOM   2025 C CE2 . TYR   B 1 28  ? 46.118 33.408 11.286  1.00 37.83  ? 234 TYR   B CE2 1 
ATOM   2026 C CZ  . TYR   B 1 28  ? 45.527 32.662 10.294  1.00 42.17  ? 234 TYR   B CZ  1 
ATOM   2027 O OH  . TYR   B 1 28  ? 44.335 33.071 9.724   1.00 50.11  ? 234 TYR   B OH  1 
ATOM   2028 N N   . ASN   B 1 29  ? 48.582 31.968 14.976  1.00 30.11  ? 235 ASN   B N   1 
ATOM   2029 C CA  . ASN   B 1 29  ? 47.828 32.721 15.966  1.00 37.81  ? 235 ASN   B CA  1 
ATOM   2030 C C   . ASN   B 1 29  ? 47.606 34.134 15.456  1.00 32.42  ? 235 ASN   B C   1 
ATOM   2031 O O   . ASN   B 1 29  ? 48.465 34.705 14.788  1.00 31.87  ? 235 ASN   B O   1 
ATOM   2032 C CB  . ASN   B 1 29  ? 48.579 32.820 17.300  1.00 41.74  ? 235 ASN   B CB  1 
ATOM   2033 C CG  . ASN   B 1 29  ? 48.490 31.564 18.125  1.00 62.59  ? 235 ASN   B CG  1 
ATOM   2034 O OD1 . ASN   B 1 29  ? 47.452 30.900 18.155  1.00 67.00  ? 235 ASN   B OD1 1 
ATOM   2035 N ND2 . ASN   B 1 29  ? 49.577 31.237 18.826  1.00 71.81  ? 235 ASN   B ND2 1 
ATOM   2036 N N   . LYS   B 1 30  ? 46.457 34.710 15.792  1.00 30.45  ? 236 LYS   B N   1 
ATOM   2037 C CA  . LYS   B 1 30  ? 46.199 36.118 15.534  1.00 26.44  ? 236 LYS   B CA  1 
ATOM   2038 C C   . LYS   B 1 30  ? 45.598 36.690 16.799  1.00 31.64  ? 236 LYS   B C   1 
ATOM   2039 O O   . LYS   B 1 30  ? 44.643 36.127 17.346  1.00 29.30  ? 236 LYS   B O   1 
ATOM   2040 C CB  . LYS   B 1 30  ? 45.266 36.345 14.351  1.00 28.49  ? 236 LYS   B CB  1 
ATOM   2041 C CG  . LYS   B 1 30  ? 45.058 37.818 14.019  1.00 32.19  ? 236 LYS   B CG  1 
ATOM   2042 C CD  . LYS   B 1 30  ? 44.342 38.006 12.682  1.00 34.19  ? 236 LYS   B CD  1 
ATOM   2043 C CE  . LYS   B 1 30  ? 44.123 39.466 12.408  1.00 38.15  ? 236 LYS   B CE  1 
ATOM   2044 N NZ  . LYS   B 1 30  ? 43.617 39.722 11.036  1.00 41.23  ? 236 LYS   B NZ  1 
ATOM   2045 N N   . HIS   B 1 31  ? 46.194 37.762 17.295  1.00 26.05  ? 237 HIS   B N   1 
ATOM   2046 C CA  . HIS   B 1 31  ? 45.707 38.453 18.476  1.00 24.78  ? 237 HIS   B CA  1 
ATOM   2047 C C   . HIS   B 1 31  ? 45.361 39.884 18.105  1.00 23.77  ? 237 HIS   B C   1 
ATOM   2048 O O   . HIS   B 1 31  ? 46.161 40.569 17.470  1.00 25.36  ? 237 HIS   B O   1 
ATOM   2049 C CB  . HIS   B 1 31  ? 46.744 38.468 19.593  1.00 25.38  ? 237 HIS   B CB  1 
ATOM   2050 C CG  . HIS   B 1 31  ? 46.343 39.320 20.757  1.00 32.00  ? 237 HIS   B CG  1 
ATOM   2051 N ND1 . HIS   B 1 31  ? 45.517 38.865 21.757  1.00 34.33  ? 237 HIS   B ND1 1 
ATOM   2052 C CD2 . HIS   B 1 31  ? 46.626 40.612 21.060  1.00 29.29  ? 237 HIS   B CD2 1 
ATOM   2053 C CE1 . HIS   B 1 31  ? 45.319 39.830 22.636  1.00 33.94  ? 237 HIS   B CE1 1 
ATOM   2054 N NE2 . HIS   B 1 31  ? 45.995 40.895 22.247  1.00 31.55  ? 237 HIS   B NE2 1 
ATOM   2055 N N   . LEU   B 1 32  ? 44.202 40.347 18.542  1.00 23.92  ? 238 LEU   B N   1 
ATOM   2056 C CA  . LEU   B 1 32  ? 43.741 41.705 18.259  1.00 24.75  ? 238 LEU   B CA  1 
ATOM   2057 C C   . LEU   B 1 32  ? 43.974 42.585 19.494  1.00 26.25  ? 238 LEU   B C   1 
ATOM   2058 O O   . LEU   B 1 32  ? 43.419 42.311 20.559  1.00 26.58  ? 238 LEU   B O   1 
ATOM   2059 C CB  . LEU   B 1 32  ? 42.258 41.703 17.894  1.00 24.02  ? 238 LEU   B CB  1 
ATOM   2060 C CG  . LEU   B 1 32  ? 41.771 41.354 16.481  1.00 30.29  ? 238 LEU   B CG  1 
ATOM   2061 C CD1 . LEU   B 1 32  ? 42.566 40.276 15.841  1.00 29.61  ? 238 LEU   B CD1 1 
ATOM   2062 C CD2 . LEU   B 1 32  ? 40.270 41.040 16.481  1.00 31.93  ? 238 LEU   B CD2 1 
ATOM   2063 N N   . PHE   B 1 33  ? 44.779 43.639 19.347  1.00 23.82  ? 239 PHE   B N   1 
ATOM   2064 C CA  . PHE   B 1 33  ? 44.986 44.594 20.438  1.00 23.45  ? 239 PHE   B CA  1 
ATOM   2065 C C   . PHE   B 1 33  ? 43.796 45.536 20.583  1.00 23.24  ? 239 PHE   B C   1 
ATOM   2066 O O   . PHE   B 1 33  ? 43.291 45.748 21.697  1.00 23.71  ? 239 PHE   B O   1 
ATOM   2067 C CB  . PHE   B 1 33  ? 46.269 45.418 20.214  1.00 21.80  ? 239 PHE   B CB  1 
ATOM   2068 C CG  . PHE   B 1 33  ? 47.530 44.594 20.165  1.00 26.19  ? 239 PHE   B CG  1 
ATOM   2069 C CD1 . PHE   B 1 33  ? 48.087 44.067 21.325  1.00 23.97  ? 239 PHE   B CD1 1 
ATOM   2070 C CD2 . PHE   B 1 33  ? 48.171 44.371 18.958  1.00 24.70  ? 239 PHE   B CD2 1 
ATOM   2071 C CE1 . PHE   B 1 33  ? 49.248 43.312 21.269  1.00 26.50  ? 239 PHE   B CE1 1 
ATOM   2072 C CE2 . PHE   B 1 33  ? 49.340 43.613 18.889  1.00 29.13  ? 239 PHE   B CE2 1 
ATOM   2073 C CZ  . PHE   B 1 33  ? 49.881 43.086 20.045  1.00 24.58  ? 239 PHE   B CZ  1 
ATOM   2074 N N   . VAL   B 1 34  ? 43.357 46.138 19.475  1.00 23.68  ? 240 VAL   B N   1 
ATOM   2075 C CA  . VAL   B 1 34  ? 42.183 47.004 19.445  1.00 22.90  ? 240 VAL   B CA  1 
ATOM   2076 C C   . VAL   B 1 34  ? 41.382 46.694 18.187  1.00 24.27  ? 240 VAL   B C   1 
ATOM   2077 O O   . VAL   B 1 34  ? 41.929 46.236 17.185  1.00 26.82  ? 240 VAL   B O   1 
ATOM   2078 C CB  . VAL   B 1 34  ? 42.562 48.506 19.467  1.00 25.09  ? 240 VAL   B CB  1 
ATOM   2079 C CG1 . VAL   B 1 34  ? 43.055 48.911 20.863  1.00 30.04  ? 240 VAL   B CG1 1 
ATOM   2080 C CG2 . VAL   B 1 34  ? 43.610 48.822 18.432  1.00 28.36  ? 240 VAL   B CG2 1 
ATOM   2081 N N   . HIS   B 1 35  ? 40.082 46.991 18.225  1.00 20.26  ? 241 HIS   B N   1 
ATOM   2082 C CA  . HIS   B 1 35  ? 39.216 46.786 17.059  1.00 24.97  ? 241 HIS   B CA  1 
ATOM   2083 C C   . HIS   B 1 35  ? 37.886 47.495 17.310  1.00 24.92  ? 241 HIS   B C   1 
ATOM   2084 O O   . HIS   B 1 35  ? 37.599 47.914 18.432  1.00 25.92  ? 241 HIS   B O   1 
ATOM   2085 C CB  . HIS   B 1 35  ? 38.996 45.295 16.777  1.00 17.81  ? 241 HIS   B CB  1 
ATOM   2086 C CG  . HIS   B 1 35  ? 38.374 44.548 17.917  1.00 22.85  ? 241 HIS   B CG  1 
ATOM   2087 N ND1 . HIS   B 1 35  ? 37.060 44.727 18.298  1.00 21.50  ? 241 HIS   B ND1 1 
ATOM   2088 C CD2 . HIS   B 1 35  ? 38.876 43.590 18.733  1.00 23.89  ? 241 HIS   B CD2 1 
ATOM   2089 C CE1 . HIS   B 1 35  ? 36.785 43.920 19.310  1.00 25.52  ? 241 HIS   B CE1 1 
ATOM   2090 N NE2 . HIS   B 1 35  ? 37.876 43.224 19.600  1.00 25.46  ? 241 HIS   B NE2 1 
ATOM   2091 N N   . ILE   B 1 36  ? 37.062 47.610 16.264  1.00 22.67  ? 242 ILE   B N   1 
ATOM   2092 C CA  . ILE   B 1 36  ? 35.740 48.216 16.440  1.00 20.05  ? 242 ILE   B CA  1 
ATOM   2093 C C   . ILE   B 1 36  ? 34.637 47.183 16.246  1.00 20.63  ? 242 ILE   B C   1 
ATOM   2094 O O   . ILE   B 1 36  ? 33.533 47.513 15.808  1.00 23.45  ? 242 ILE   B O   1 
ATOM   2095 C CB  . ILE   B 1 36  ? 35.532 49.446 15.530  1.00 26.27  ? 242 ILE   B CB  1 
ATOM   2096 C CG1 . ILE   B 1 36  ? 35.639 49.086 14.045  1.00 24.08  ? 242 ILE   B CG1 1 
ATOM   2097 C CG2 . ILE   B 1 36  ? 36.520 50.579 15.887  1.00 21.94  ? 242 ILE   B CG2 1 
ATOM   2098 C CD1 . ILE   B 1 36  ? 35.120 50.197 13.130  1.00 25.13  ? 242 ILE   B CD1 1 
ATOM   2099 N N   . GLY   B 1 37  ? 34.893 45.944 16.664  1.00 25.40  ? 243 GLY   B N   1 
ATOM   2100 C CA  . GLY   B 1 37  ? 33.904 44.894 16.575  1.00 27.23  ? 243 GLY   B CA  1 
ATOM   2101 C C   . GLY   B 1 37  ? 32.937 44.766 17.744  1.00 32.21  ? 243 GLY   B C   1 
ATOM   2102 O O   . GLY   B 1 37  ? 31.924 44.079 17.609  1.00 29.75  ? 243 GLY   B O   1 
ATOM   2103 N N   . HIS   B 1 38  ? 33.213 45.394 18.889  1.00 26.48  ? 244 HIS   B N   1 
ATOM   2104 C CA  . HIS   B 1 38  ? 32.407 45.217 20.102  1.00 26.93  ? 244 HIS   B CA  1 
ATOM   2105 C C   . HIS   B 1 38  ? 32.084 46.581 20.714  1.00 27.16  ? 244 HIS   B C   1 
ATOM   2106 O O   . HIS   B 1 38  ? 32.798 47.054 21.601  1.00 28.03  ? 244 HIS   B O   1 
ATOM   2107 C CB  . HIS   B 1 38  ? 33.150 44.330 21.098  1.00 29.33  ? 244 HIS   B CB  1 
ATOM   2108 C CG  . HIS   B 1 38  ? 32.314 43.844 22.244  1.00 34.48  ? 244 HIS   B CG  1 
ATOM   2109 N ND1 . HIS   B 1 38  ? 31.556 44.689 23.025  1.00 43.59  ? 244 HIS   B ND1 1 
ATOM   2110 C CD2 . HIS   B 1 38  ? 32.222 42.623 22.820  1.00 36.61  ? 244 HIS   B CD2 1 
ATOM   2111 C CE1 . HIS   B 1 38  ? 30.978 43.996 23.990  1.00 38.87  ? 244 HIS   B CE1 1 
ATOM   2112 N NE2 . HIS   B 1 38  ? 31.369 42.741 23.889  1.00 47.02  ? 244 HIS   B NE2 1 
ATOM   2113 N N   . ALA   B 1 39  ? 30.992 47.195 20.271  1.00 32.51  ? 245 ALA   B N   1 
ATOM   2114 C CA  . ALA   B 1 39  ? 30.582 48.473 20.837  1.00 28.72  ? 245 ALA   B CA  1 
ATOM   2115 C C   . ALA   B 1 39  ? 30.243 48.336 22.322  1.00 29.26  ? 245 ALA   B C   1 
ATOM   2116 O O   . ALA   B 1 39  ? 29.504 47.440 22.725  1.00 34.70  ? 245 ALA   B O   1 
ATOM   2117 C CB  . ALA   B 1 39  ? 29.386 49.029 20.066  1.00 28.64  ? 245 ALA   B CB  1 
ATOM   2118 N N   . ASN   B 1 40  ? 30.848 49.205 23.133  1.00 30.68  ? 246 ASN   B N   1 
ATOM   2119 C CA  . ASN   B 1 40  ? 30.567 49.347 24.562  1.00 36.37  ? 246 ASN   B CA  1 
ATOM   2120 C C   . ASN   B 1 40  ? 29.301 50.163 24.800  1.00 43.45  ? 246 ASN   B C   1 
ATOM   2121 O O   . ASN   B 1 40  ? 28.638 50.000 25.826  1.00 37.98  ? 246 ASN   B O   1 
ATOM   2122 C CB  . ASN   B 1 40  ? 31.782 50.025 25.230  1.00 38.61  ? 246 ASN   B CB  1 
ATOM   2123 C CG  . ASN   B 1 40  ? 31.630 50.218 26.717  1.00 48.53  ? 246 ASN   B CG  1 
ATOM   2124 O OD1 . ASN   B 1 40  ? 31.330 51.319 27.183  1.00 51.01  ? 246 ASN   B OD1 1 
ATOM   2125 N ND2 . ASN   B 1 40  ? 31.885 49.166 27.479  1.00 47.00  ? 246 ASN   B ND2 1 
ATOM   2126 N N   . HIS   B 1 41  ? 28.964 51.053 23.876  1.00 38.87  ? 247 HIS   B N   1 
ATOM   2127 C CA  . HIS   B 1 41  ? 27.751 51.831 24.005  1.00 40.72  ? 247 HIS   B CA  1 
ATOM   2128 C C   . HIS   B 1 41  ? 26.583 51.001 23.479  1.00 44.11  ? 247 HIS   B C   1 
ATOM   2129 O O   . HIS   B 1 41  ? 26.769 50.018 22.753  1.00 44.64  ? 247 HIS   B O   1 
ATOM   2130 C CB  . HIS   B 1 41  ? 27.877 53.135 23.221  1.00 40.53  ? 247 HIS   B CB  1 
ATOM   2131 C CG  . HIS   B 1 41  ? 28.277 52.932 21.791  1.00 35.65  ? 247 HIS   B CG  1 
ATOM   2132 N ND1 . HIS   B 1 41  ? 29.582 52.716 21.398  1.00 29.19  ? 247 HIS   B ND1 1 
ATOM   2133 C CD2 . HIS   B 1 41  ? 27.533 52.921 20.657  1.00 43.18  ? 247 HIS   B CD2 1 
ATOM   2134 C CE1 . HIS   B 1 41  ? 29.622 52.568 20.086  1.00 29.40  ? 247 HIS   B CE1 1 
ATOM   2135 N NE2 . HIS   B 1 41  ? 28.393 52.692 19.611  1.00 41.97  ? 247 HIS   B NE2 1 
ATOM   2136 N N   . SER   B 1 42  ? 25.369 51.410 23.834  1.00 46.00  ? 248 SER   B N   1 
ATOM   2137 C CA  . SER   B 1 42  ? 24.185 50.638 23.473  1.00 55.15  ? 248 SER   B CA  1 
ATOM   2138 C C   . SER   B 1 42  ? 23.771 50.870 22.022  1.00 51.90  ? 248 SER   B C   1 
ATOM   2139 O O   . SER   B 1 42  ? 23.726 52.006 21.548  1.00 52.85  ? 248 SER   B O   1 
ATOM   2140 C CB  . SER   B 1 42  ? 23.024 50.997 24.398  1.00 59.60  ? 248 SER   B CB  1 
ATOM   2141 O OG  . SER   B 1 42  ? 21.857 50.276 24.038  1.00 68.28  ? 248 SER   B OG  1 
ATOM   2142 N N   . TYR   B 1 43  ? 23.432 49.783 21.324  1.00 58.06  ? 249 TYR   B N   1 
ATOM   2143 C CA  . TYR   B 1 43  ? 22.800 49.901 20.014  1.00 56.90  ? 249 TYR   B CA  1 
ATOM   2144 C C   . TYR   B 1 43  ? 21.320 50.276 20.121  1.00 62.12  ? 249 TYR   B C   1 
ATOM   2145 O O   . TYR   B 1 43  ? 20.725 50.664 19.112  1.00 63.64  ? 249 TYR   B O   1 
ATOM   2146 C CB  . TYR   B 1 43  ? 22.988 48.589 19.231  1.00 65.70  ? 249 TYR   B CB  1 
ATOM   2147 C CG  . TYR   B 1 43  ? 22.551 48.593 17.763  1.00 67.41  ? 249 TYR   B CG  1 
ATOM   2148 C CD1 . TYR   B 1 43  ? 21.251 48.248 17.383  1.00 69.16  ? 249 TYR   B CD1 1 
ATOM   2149 C CD2 . TYR   B 1 43  ? 23.455 48.945 16.754  1.00 60.00  ? 249 TYR   B CD2 1 
ATOM   2150 C CE1 . TYR   B 1 43  ? 20.862 48.250 16.029  1.00 64.58  ? 249 TYR   B CE1 1 
ATOM   2151 C CE2 . TYR   B 1 43  ? 23.078 48.961 15.408  1.00 61.54  ? 249 TYR   B CE2 1 
ATOM   2152 C CZ  . TYR   B 1 43  ? 21.779 48.609 15.047  1.00 74.08  ? 249 TYR   B CZ  1 
ATOM   2153 O OH  . TYR   B 1 43  ? 21.407 48.620 13.705  1.00 64.35  ? 249 TYR   B OH  1 
ATOM   2154 N N   . SER   B 1 44  ? 20.739 50.233 21.332  1.00 67.36  ? 250 SER   B N   1 
ATOM   2155 C CA  . SER   B 1 44  ? 19.312 50.519 21.521  1.00 66.44  ? 250 SER   B CA  1 
ATOM   2156 C C   . SER   B 1 44  ? 19.002 52.010 21.418  1.00 63.19  ? 250 SER   B C   1 
ATOM   2157 O O   . SER   B 1 44  ? 18.016 52.394 20.783  1.00 70.33  ? 250 SER   B O   1 
ATOM   2158 C CB  . SER   B 1 44  ? 18.830 49.982 22.870  1.00 62.80  ? 250 SER   B CB  1 
ATOM   2159 O OG  . SER   B 1 44  ? 18.648 48.583 22.817  1.00 74.98  ? 250 SER   B OG  1 
ATOM   2160 N N   . ASP   B 1 45  ? 19.785 52.866 22.071  1.00 58.23  ? 251 ASP   B N   1 
ATOM   2161 C CA  . ASP   B 1 45  ? 19.635 54.297 21.797  1.00 60.51  ? 251 ASP   B CA  1 
ATOM   2162 C C   . ASP   B 1 45  ? 20.109 54.540 20.373  1.00 51.47  ? 251 ASP   B C   1 
ATOM   2163 O O   . ASP   B 1 45  ? 21.245 54.179 20.044  1.00 53.62  ? 251 ASP   B O   1 
ATOM   2164 C CB  . ASP   B 1 45  ? 20.437 55.200 22.752  1.00 59.35  ? 251 ASP   B CB  1 
ATOM   2165 C CG  . ASP   B 1 45  ? 20.504 54.684 24.188  1.00 68.95  ? 251 ASP   B CG  1 
ATOM   2166 O OD1 . ASP   B 1 45  ? 19.466 54.241 24.728  1.00 73.70  ? 251 ASP   B OD1 1 
ATOM   2167 O OD2 . ASP   B 1 45  ? 21.591 54.778 24.805  1.00 66.65  ? 251 ASP   B OD2 1 
ATOM   2168 N N   . PRO   B 1 46  ? 19.299 55.124 19.495  1.00 58.75  ? 252 PRO   B N   1 
ATOM   2169 C CA  . PRO   B 1 46  ? 19.836 55.494 18.177  1.00 57.46  ? 252 PRO   B CA  1 
ATOM   2170 C C   . PRO   B 1 46  ? 20.807 56.658 18.248  1.00 54.07  ? 252 PRO   B C   1 
ATOM   2171 O O   . PRO   B 1 46  ? 21.627 56.811 17.332  1.00 50.70  ? 252 PRO   B O   1 
ATOM   2172 C CB  . PRO   B 1 46  ? 18.584 55.860 17.362  1.00 58.04  ? 252 PRO   B CB  1 
ATOM   2173 C CG  . PRO   B 1 46  ? 17.441 55.208 18.076  1.00 62.98  ? 252 PRO   B CG  1 
ATOM   2174 C CD  . PRO   B 1 46  ? 17.815 55.184 19.533  1.00 64.35  ? 252 PRO   B CD  1 
ATOM   2175 N N   . LEU   B 1 47  ? 20.752 57.463 19.318  1.00 49.51  ? 253 LEU   B N   1 
ATOM   2176 C CA  . LEU   B 1 47  ? 21.558 58.670 19.450  1.00 46.28  ? 253 LEU   B CA  1 
ATOM   2177 C C   . LEU   B 1 47  ? 22.849 58.410 20.214  1.00 45.97  ? 253 LEU   B C   1 
ATOM   2178 O O   . LEU   B 1 47  ? 22.842 57.779 21.278  1.00 46.53  ? 253 LEU   B O   1 
ATOM   2179 C CB  . LEU   B 1 47  ? 20.795 59.756 20.197  1.00 42.14  ? 253 LEU   B CB  1 
ATOM   2180 C CG  . LEU   B 1 47  ? 19.921 60.652 19.337  1.00 53.98  ? 253 LEU   B CG  1 
ATOM   2181 C CD1 . LEU   B 1 47  ? 18.563 60.005 19.277  1.00 47.16  ? 253 LEU   B CD1 1 
ATOM   2182 C CD2 . LEU   B 1 47  ? 19.881 62.100 19.863  1.00 48.05  ? 253 LEU   B CD2 1 
ATOM   2183 N N   . LEU   B 1 48  ? 23.940 58.982 19.713  1.00 38.63  ? 254 LEU   B N   1 
ATOM   2184 C CA  . LEU   B 1 48  ? 25.225 58.910 20.395  1.00 36.19  ? 254 LEU   B CA  1 
ATOM   2185 C C   . LEU   B 1 48  ? 25.299 59.923 21.531  1.00 37.81  ? 254 LEU   B C   1 
ATOM   2186 O O   . LEU   B 1 48  ? 24.755 61.023 21.436  1.00 37.70  ? 254 LEU   B O   1 
ATOM   2187 C CB  . LEU   B 1 48  ? 26.359 59.179 19.404  1.00 38.93  ? 254 LEU   B CB  1 
ATOM   2188 C CG  . LEU   B 1 48  ? 26.564 58.071 18.359  1.00 38.98  ? 254 LEU   B CG  1 
ATOM   2189 C CD1 . LEU   B 1 48  ? 27.489 58.537 17.240  1.00 39.98  ? 254 LEU   B CD1 1 
ATOM   2190 C CD2 . LEU   B 1 48  ? 27.089 56.796 19.020  1.00 33.51  ? 254 LEU   B CD2 1 
ATOM   2191 N N   . GLU   B 1 49  ? 25.984 59.541 22.604  1.00 30.27  ? 255 GLU   B N   1 
ATOM   2192 C CA  . GLU   B 1 49  ? 26.394 60.486 23.628  1.00 31.27  ? 255 GLU   B CA  1 
ATOM   2193 C C   . GLU   B 1 49  ? 27.355 61.504 23.026  1.00 35.74  ? 255 GLU   B C   1 
ATOM   2194 O O   . GLU   B 1 49  ? 28.046 61.239 22.039  1.00 35.64  ? 255 GLU   B O   1 
ATOM   2195 C CB  . GLU   B 1 49  ? 27.092 59.751 24.763  1.00 36.92  ? 255 GLU   B CB  1 
ATOM   2196 C CG  . GLU   B 1 49  ? 26.215 58.778 25.522  1.00 43.57  ? 255 GLU   B CG  1 
ATOM   2197 C CD  . GLU   B 1 49  ? 27.038 57.761 26.296  1.00 47.80  ? 255 GLU   B CD  1 
ATOM   2198 O OE1 . GLU   B 1 49  ? 27.481 58.096 27.408  1.00 49.73  ? 255 GLU   B OE1 1 
ATOM   2199 O OE2 . GLU   B 1 49  ? 27.271 56.641 25.774  1.00 49.24  ? 255 GLU   B OE2 1 
ATOM   2200 N N   . SER   B 1 50  ? 27.413 62.674 23.632  1.00 35.32  ? 256 SER   B N   1 
ATOM   2201 C CA  . SER   B 1 50  ? 28.279 63.729 23.146  1.00 36.50  ? 256 SER   B CA  1 
ATOM   2202 C C   . SER   B 1 50  ? 29.332 64.058 24.189  1.00 39.46  ? 256 SER   B C   1 
ATOM   2203 O O   . SER   B 1 50  ? 29.183 63.761 25.376  1.00 39.52  ? 256 SER   B O   1 
ATOM   2204 C CB  . SER   B 1 50  ? 27.471 64.967 22.785  1.00 36.10  ? 256 SER   B CB  1 
ATOM   2205 O OG  . SER   B 1 50  ? 26.879 65.475 23.955  1.00 44.26  ? 256 SER   B OG  1 
ATOM   2206 N N   . VAL   B 1 51  ? 30.422 64.635 23.703  1.00 32.64  ? 257 VAL   B N   1 
ATOM   2207 C CA  . VAL   B 1 51  ? 31.563 65.048 24.502  1.00 33.19  ? 257 VAL   B CA  1 
ATOM   2208 C C   . VAL   B 1 51  ? 31.963 66.426 24.007  1.00 35.33  ? 257 VAL   B C   1 
ATOM   2209 O O   . VAL   B 1 51  ? 32.059 66.652 22.795  1.00 30.18  ? 257 VAL   B O   1 
ATOM   2210 C CB  . VAL   B 1 51  ? 32.745 64.064 24.394  1.00 37.01  ? 257 VAL   B CB  1 
ATOM   2211 C CG1 . VAL   B 1 51  ? 34.040 64.735 24.797  1.00 36.50  ? 257 VAL   B CG1 1 
ATOM   2212 C CG2 . VAL   B 1 51  ? 32.495 62.853 25.266  1.00 38.15  ? 257 VAL   B CG2 1 
ATOM   2213 N N   . ASP   B 1 52  ? 32.133 67.358 24.941  1.00 35.98  ? 258 ASP   B N   1 
ATOM   2214 C CA  . ASP   B 1 52  ? 32.527 68.724 24.622  1.00 35.54  ? 258 ASP   B CA  1 
ATOM   2215 C C   . ASP   B 1 52  ? 33.969 68.720 24.142  1.00 29.25  ? 258 ASP   B C   1 
ATOM   2216 O O   . ASP   B 1 52  ? 34.864 68.291 24.872  1.00 33.99  ? 258 ASP   B O   1 
ATOM   2217 C CB  . ASP   B 1 52  ? 32.354 69.592 25.872  1.00 36.89  ? 258 ASP   B CB  1 
ATOM   2218 C CG  . ASP   B 1 52  ? 32.934 70.993 25.724  1.00 42.94  ? 258 ASP   B CG  1 
ATOM   2219 O OD1 . ASP   B 1 52  ? 33.138 71.477 24.599  1.00 39.09  ? 258 ASP   B OD1 1 
ATOM   2220 O OD2 . ASP   B 1 52  ? 33.214 71.613 26.771  1.00 54.78  ? 258 ASP   B OD2 1 
ATOM   2221 N N   . ILE   B 1 53  ? 34.196 69.186 22.908  1.00 33.29  ? 259 ILE   B N   1 
ATOM   2222 C CA  . ILE   B 1 53  ? 35.518 69.059 22.298  1.00 33.29  ? 259 ILE   B CA  1 
ATOM   2223 C C   . ILE   B 1 53  ? 36.556 69.899 23.021  1.00 36.74  ? 259 ILE   B C   1 
ATOM   2224 O O   . ILE   B 1 53  ? 37.751 69.581 22.985  1.00 34.34  ? 259 ILE   B O   1 
ATOM   2225 C CB  . ILE   B 1 53  ? 35.465 69.420 20.803  1.00 32.83  ? 259 ILE   B CB  1 
ATOM   2226 C CG1 . ILE   B 1 53  ? 36.680 68.821 20.076  1.00 30.36  ? 259 ILE   B CG1 1 
ATOM   2227 C CG2 . ILE   B 1 53  ? 35.380 70.943 20.610  1.00 32.12  ? 259 ILE   B CG2 1 
ATOM   2228 C CD1 . ILE   B 1 53  ? 36.698 69.109 18.606  1.00 32.54  ? 259 ILE   B CD1 1 
ATOM   2229 N N   . ARG   B 1 54  ? 36.131 70.976 23.687  1.00 34.93  ? 260 ARG   B N   1 
ATOM   2230 C CA  . ARG   B 1 54  ? 37.082 71.848 24.370  1.00 41.79  ? 260 ARG   B CA  1 
ATOM   2231 C C   . ARG   B 1 54  ? 37.840 71.118 25.473  1.00 39.95  ? 260 ARG   B C   1 
ATOM   2232 O O   . ARG   B 1 54  ? 38.978 71.482 25.777  1.00 41.09  ? 260 ARG   B O   1 
ATOM   2233 C CB  . ARG   B 1 54  ? 36.354 73.097 24.909  1.00 35.34  ? 260 ARG   B CB  1 
ATOM   2234 C CG  . ARG   B 1 54  ? 35.749 73.946 23.775  1.00 43.52  ? 260 ARG   B CG  1 
ATOM   2235 C CD  . ARG   B 1 54  ? 34.735 74.994 24.254  1.00 56.30  ? 260 ARG   B CD  1 
ATOM   2236 N NE  . ARG   B 1 54  ? 33.590 74.390 24.928  1.00 46.33  ? 260 ARG   B NE  1 
ATOM   2237 C CZ  . ARG   B 1 54  ? 32.566 75.072 25.425  1.00 61.13  ? 260 ARG   B CZ  1 
ATOM   2238 N NH1 . ARG   B 1 54  ? 32.505 76.396 25.341  1.00 51.54  ? 260 ARG   B NH1 1 
ATOM   2239 N NH2 . ARG   B 1 54  ? 31.576 74.412 26.019  1.00 55.43  ? 260 ARG   B NH2 1 
ATOM   2240 N N   . GLN   B 1 55  ? 37.274 70.056 26.038  1.00 38.63  ? 261 GLN   B N   1 
ATOM   2241 C CA  . GLN   B 1 55  ? 37.974 69.335 27.091  1.00 45.10  ? 261 GLN   B CA  1 
ATOM   2242 C C   . GLN   B 1 55  ? 38.908 68.231 26.591  1.00 44.42  ? 261 GLN   B C   1 
ATOM   2243 O O   . GLN   B 1 55  ? 39.472 67.512 27.419  1.00 44.42  ? 261 GLN   B O   1 
ATOM   2244 C CB  . GLN   B 1 55  ? 36.980 68.763 28.106  1.00 53.46  ? 261 GLN   B CB  1 
ATOM   2245 C CG  . GLN   B 1 55  ? 36.140 67.593 27.663  1.00 50.72  ? 261 GLN   B CG  1 
ATOM   2246 C CD  . GLN   B 1 55  ? 35.005 67.313 28.651  1.00 70.13  ? 261 GLN   B CD  1 
ATOM   2247 O OE1 . GLN   B 1 55  ? 34.533 66.182 28.762  1.00 76.37  ? 261 GLN   B OE1 1 
ATOM   2248 N NE2 . GLN   B 1 55  ? 34.593 68.337 29.395  1.00 65.84  ? 261 GLN   B NE2 1 
ATOM   2249 N N   . ILE   B 1 56  ? 39.121 68.092 25.281  1.00 35.20  ? 262 ILE   B N   1 
ATOM   2250 C CA  . ILE   B 1 56  ? 40.129 67.168 24.765  1.00 39.00  ? 262 ILE   B CA  1 
ATOM   2251 C C   . ILE   B 1 56  ? 41.176 67.853 23.900  1.00 37.64  ? 262 ILE   B C   1 
ATOM   2252 O O   . ILE   B 1 56  ? 42.068 67.177 23.385  1.00 34.05  ? 262 ILE   B O   1 
ATOM   2253 C CB  . ILE   B 1 56  ? 39.482 65.987 24.005  1.00 38.58  ? 262 ILE   B CB  1 
ATOM   2254 C CG1 . ILE   B 1 56  ? 38.880 66.444 22.682  1.00 32.77  ? 262 ILE   B CG1 1 
ATOM   2255 C CG2 . ILE   B 1 56  ? 38.451 65.272 24.842  1.00 41.41  ? 262 ILE   B CG2 1 
ATOM   2256 C CD1 . ILE   B 1 56  ? 38.864 65.340 21.640  1.00 33.84  ? 262 ILE   B CD1 1 
ATOM   2257 N N   . TYR   B 1 57  ? 41.108 69.180 23.738  1.00 35.34  ? 263 TYR   B N   1 
ATOM   2258 C CA  . TYR   B 1 57  ? 42.085 69.900 22.925  1.00 38.55  ? 263 TYR   B CA  1 
ATOM   2259 C C   . TYR   B 1 57  ? 43.523 69.639 23.356  1.00 35.88  ? 263 TYR   B C   1 
ATOM   2260 O O   . TYR   B 1 57  ? 44.420 69.582 22.511  1.00 37.95  ? 263 TYR   B O   1 
ATOM   2261 C CB  . TYR   B 1 57  ? 41.798 71.409 22.952  1.00 40.70  ? 263 TYR   B CB  1 
ATOM   2262 C CG  . TYR   B 1 57  ? 40.669 71.864 22.038  1.00 37.35  ? 263 TYR   B CG  1 
ATOM   2263 C CD1 . TYR   B 1 57  ? 40.370 71.162 20.877  1.00 40.58  ? 263 TYR   B CD1 1 
ATOM   2264 C CD2 . TYR   B 1 57  ? 39.921 72.997 22.328  1.00 41.96  ? 263 TYR   B CD2 1 
ATOM   2265 C CE1 . TYR   B 1 57  ? 39.352 71.568 20.035  1.00 41.32  ? 263 TYR   B CE1 1 
ATOM   2266 C CE2 . TYR   B 1 57  ? 38.891 73.414 21.493  1.00 37.00  ? 263 TYR   B CE2 1 
ATOM   2267 C CZ  . TYR   B 1 57  ? 38.624 72.703 20.346  1.00 39.47  ? 263 TYR   B CZ  1 
ATOM   2268 O OH  . TYR   B 1 57  ? 37.621 73.100 19.504  1.00 48.07  ? 263 TYR   B OH  1 
ATOM   2269 N N   . ASP   B 1 58  ? 43.782 69.508 24.660  1.00 39.42  ? 264 ASP   B N   1 
ATOM   2270 C CA  . ASP   B 1 58  ? 45.176 69.352 25.066  1.00 34.46  ? 264 ASP   B CA  1 
ATOM   2271 C C   . ASP   B 1 58  ? 45.700 67.926 24.893  1.00 43.69  ? 264 ASP   B C   1 
ATOM   2272 O O   . ASP   B 1 58  ? 46.904 67.700 25.082  1.00 40.52  ? 264 ASP   B O   1 
ATOM   2273 C CB  . ASP   B 1 58  ? 45.393 69.823 26.516  1.00 42.66  ? 264 ASP   B CB  1 
ATOM   2274 C CG  . ASP   B 1 58  ? 44.639 69.002 27.533  1.00 52.50  ? 264 ASP   B CG  1 
ATOM   2275 O OD1 . ASP   B 1 58  ? 44.886 69.141 28.752  1.00 70.80  ? 264 ASP   B OD1 1 
ATOM   2276 O OD2 . ASP   B 1 58  ? 43.792 68.188 27.102  1.00 66.30  ? 264 ASP   B OD2 1 
ATOM   2277 N N   . LYS   B 1 59  ? 44.848 66.970 24.511  1.00 35.04  ? 265 LYS   B N   1 
ATOM   2278 C CA  . LYS   B 1 59  ? 45.298 65.608 24.244  1.00 35.24  ? 265 LYS   B CA  1 
ATOM   2279 C C   . LYS   B 1 59  ? 45.636 65.371 22.772  1.00 35.82  ? 265 LYS   B C   1 
ATOM   2280 O O   . LYS   B 1 59  ? 46.040 64.258 22.409  1.00 32.56  ? 265 LYS   B O   1 
ATOM   2281 C CB  . LYS   B 1 59  ? 44.236 64.605 24.709  1.00 38.75  ? 265 LYS   B CB  1 
ATOM   2282 C CG  . LYS   B 1 59  ? 43.834 64.767 26.164  1.00 44.73  ? 265 LYS   B CG  1 
ATOM   2283 C CD  . LYS   B 1 59  ? 42.788 63.764 26.601  1.00 42.36  ? 265 LYS   B CD  1 
ATOM   2284 C CE  . LYS   B 1 59  ? 42.553 63.853 28.092  1.00 57.24  ? 265 LYS   B CE  1 
ATOM   2285 N NZ  . LYS   B 1 59  ? 41.828 65.118 28.428  1.00 66.38  ? 265 LYS   B NZ  1 
ATOM   2286 N N   . PHE   B 1 60  ? 45.507 66.382 21.925  1.00 29.24  ? 266 PHE   B N   1 
ATOM   2287 C CA  . PHE   B 1 60  ? 45.705 66.240 20.491  1.00 32.13  ? 266 PHE   B CA  1 
ATOM   2288 C C   . PHE   B 1 60  ? 46.485 67.439 19.980  1.00 36.94  ? 266 PHE   B C   1 
ATOM   2289 O O   . PHE   B 1 60  ? 46.625 68.439 20.692  1.00 35.07  ? 266 PHE   B O   1 
ATOM   2290 C CB  . PHE   B 1 60  ? 44.346 66.087 19.788  1.00 31.07  ? 266 PHE   B CB  1 
ATOM   2291 C CG  . PHE   B 1 60  ? 43.667 64.800 20.130  1.00 28.35  ? 266 PHE   B CG  1 
ATOM   2292 C CD1 . PHE   B 1 60  ? 44.007 63.638 19.472  1.00 28.96  ? 266 PHE   B CD1 1 
ATOM   2293 C CD2 . PHE   B 1 60  ? 42.782 64.728 21.184  1.00 29.68  ? 266 PHE   B CD2 1 
ATOM   2294 C CE1 . PHE   B 1 60  ? 43.415 62.450 19.812  1.00 22.32  ? 266 PHE   B CE1 1 
ATOM   2295 C CE2 . PHE   B 1 60  ? 42.205 63.540 21.545  1.00 31.56  ? 266 PHE   B CE2 1 
ATOM   2296 C CZ  . PHE   B 1 60  ? 42.518 62.390 20.850  1.00 29.79  ? 266 PHE   B CZ  1 
ATOM   2297 N N   . PRO   B 1 61  ? 47.048 67.356 18.769  1.00 38.13  ? 267 PRO   B N   1 
ATOM   2298 C CA  . PRO   B 1 61  ? 47.838 68.486 18.248  1.00 37.20  ? 267 PRO   B CA  1 
ATOM   2299 C C   . PRO   B 1 61  ? 47.042 69.786 18.187  1.00 40.11  ? 267 PRO   B C   1 
ATOM   2300 O O   . PRO   B 1 61  ? 45.836 69.795 17.939  1.00 40.06  ? 267 PRO   B O   1 
ATOM   2301 C CB  . PRO   B 1 61  ? 48.248 68.019 16.845  1.00 42.47  ? 267 PRO   B CB  1 
ATOM   2302 C CG  . PRO   B 1 61  ? 48.168 66.514 16.910  1.00 41.27  ? 267 PRO   B CG  1 
ATOM   2303 C CD  . PRO   B 1 61  ? 47.029 66.217 17.826  1.00 36.33  ? 267 PRO   B CD  1 
ATOM   2304 N N   . GLU   B 1 62  ? 47.741 70.901 18.416  1.00 39.67  ? 268 GLU   B N   1 
ATOM   2305 C CA  . GLU   B 1 62  ? 47.100 72.206 18.532  1.00 45.60  ? 268 GLU   B CA  1 
ATOM   2306 C C   . GLU   B 1 62  ? 47.725 73.196 17.552  1.00 48.72  ? 268 GLU   B C   1 
ATOM   2307 O O   . GLU   B 1 62  ? 48.659 72.875 16.810  1.00 52.21  ? 268 GLU   B O   1 
ATOM   2308 C CB  . GLU   B 1 62  ? 47.172 72.723 19.975  1.00 48.59  ? 268 GLU   B CB  1 
ATOM   2309 C CG  . GLU   B 1 62  ? 46.332 71.899 20.931  1.00 46.80  ? 268 GLU   B CG  1 
ATOM   2310 C CD  . GLU   B 1 62  ? 46.341 72.429 22.352  1.00 53.57  ? 268 GLU   B CD  1 
ATOM   2311 O OE1 . GLU   B 1 62  ? 47.219 72.021 23.139  1.00 52.76  ? 268 GLU   B OE1 1 
ATOM   2312 O OE2 . GLU   B 1 62  ? 45.449 73.241 22.685  1.00 56.61  ? 268 GLU   B OE2 1 
ATOM   2313 N N   . LYS   B 1 63  ? 47.176 74.405 17.537  1.00 51.59  ? 269 LYS   B N   1 
ATOM   2314 C CA  . LYS   B 1 63  ? 47.597 75.472 16.620  1.00 55.74  ? 269 LYS   B CA  1 
ATOM   2315 C C   . LYS   B 1 63  ? 47.355 75.006 15.176  1.00 56.31  ? 269 LYS   B C   1 
ATOM   2316 O O   . LYS   B 1 63  ? 46.397 74.268 14.905  1.00 47.15  ? 269 LYS   B O   1 
ATOM   2317 C CB  . LYS   B 1 63  ? 49.024 75.898 16.932  1.00 63.66  ? 269 LYS   B CB  1 
ATOM   2318 C CG  . LYS   B 1 63  ? 49.240 76.316 18.379  0.00 57.77  ? 269 LYS   B CG  1 
ATOM   2319 C CD  . LYS   B 1 63  ? 50.597 75.876 18.899  0.00 59.38  ? 269 LYS   B CD  1 
ATOM   2320 C CE  . LYS   B 1 63  ? 50.513 75.451 20.356  0.00 60.52  ? 269 LYS   B CE  1 
ATOM   2321 N NZ  . LYS   B 1 63  ? 51.366 74.265 20.639  0.00 62.32  ? 269 LYS   B NZ  1 
ATOM   2322 N N   . LYS   B 1 64  ? 48.194 75.449 14.238  1.00 55.44  ? 270 LYS   B N   1 
ATOM   2323 C CA  . LYS   B 1 64  ? 47.926 75.231 12.818  1.00 51.30  ? 270 LYS   B CA  1 
ATOM   2324 C C   . LYS   B 1 64  ? 47.782 73.747 12.525  1.00 55.49  ? 270 LYS   B C   1 
ATOM   2325 O O   . LYS   B 1 64  ? 48.584 72.933 12.984  1.00 56.80  ? 270 LYS   B O   1 
ATOM   2326 C CB  . LYS   B 1 64  ? 49.048 75.838 11.968  1.00 64.88  ? 270 LYS   B CB  1 
ATOM   2327 C CG  . LYS   B 1 64  ? 48.925 75.600 10.465  1.00 64.70  ? 270 LYS   B CG  1 
ATOM   2328 C CD  . LYS   B 1 64  ? 49.518 76.751 9.649   1.00 77.99  ? 270 LYS   B CD  1 
ATOM   2329 C CE  . LYS   B 1 64  ? 49.687 76.359 8.178   1.00 74.98  ? 270 LYS   B CE  1 
ATOM   2330 N NZ  . LYS   B 1 64  ? 49.557 77.509 7.232   1.00 80.13  ? 270 LYS   B NZ  1 
ATOM   2331 N N   . GLY   B 1 65  ? 46.732 73.394 11.786  1.00 56.61  ? 271 GLY   B N   1 
ATOM   2332 C CA  . GLY   B 1 65  ? 46.463 72.005 11.475  1.00 57.85  ? 271 GLY   B CA  1 
ATOM   2333 C C   . GLY   B 1 65  ? 45.969 71.159 12.628  1.00 49.05  ? 271 GLY   B C   1 
ATOM   2334 O O   . GLY   B 1 65  ? 45.720 69.963 12.429  1.00 54.86  ? 271 GLY   B O   1 
ATOM   2335 N N   . GLY   B 1 66  ? 45.807 71.731 13.821  1.00 43.33  ? 272 GLY   B N   1 
ATOM   2336 C CA  . GLY   B 1 66  ? 45.371 70.974 14.978  1.00 45.15  ? 272 GLY   B CA  1 
ATOM   2337 C C   . GLY   B 1 66  ? 43.865 70.772 15.033  1.00 46.14  ? 272 GLY   B C   1 
ATOM   2338 O O   . GLY   B 1 66  ? 43.109 71.179 14.152  1.00 39.76  ? 272 GLY   B O   1 
ATOM   2339 N N   . LEU   B 1 67  ? 43.421 70.141 16.121  1.00 40.61  ? 273 LEU   B N   1 
ATOM   2340 C CA  . LEU   B 1 67  ? 42.038 69.682 16.192  1.00 35.31  ? 273 LEU   B CA  1 
ATOM   2341 C C   . LEU   B 1 67  ? 41.054 70.845 16.223  1.00 34.40  ? 273 LEU   B C   1 
ATOM   2342 O O   . LEU   B 1 67  ? 39.993 70.783 15.591  1.00 36.16  ? 273 LEU   B O   1 
ATOM   2343 C CB  . LEU   B 1 67  ? 41.858 68.779 17.407  1.00 29.29  ? 273 LEU   B CB  1 
ATOM   2344 C CG  . LEU   B 1 67  ? 40.506 68.118 17.590  1.00 29.37  ? 273 LEU   B CG  1 
ATOM   2345 C CD1 . LEU   B 1 67  ? 40.096 67.316 16.343  1.00 26.51  ? 273 LEU   B CD1 1 
ATOM   2346 C CD2 . LEU   B 1 67  ? 40.567 67.245 18.807  1.00 29.04  ? 273 LEU   B CD2 1 
ATOM   2347 N N   . LYS   B 1 68  ? 41.382 71.914 16.948  1.00 36.27  ? 274 LYS   B N   1 
ATOM   2348 C CA  . LYS   B 1 68  ? 40.456 73.038 17.046  1.00 34.32  ? 274 LYS   B CA  1 
ATOM   2349 C C   . LYS   B 1 68  ? 40.237 73.682 15.684  1.00 38.09  ? 274 LYS   B C   1 
ATOM   2350 O O   . LYS   B 1 68  ? 39.100 73.981 15.301  1.00 35.54  ? 274 LYS   B O   1 
ATOM   2351 C CB  . LYS   B 1 68  ? 40.985 74.052 18.058  1.00 39.03  ? 274 LYS   B CB  1 
ATOM   2352 C CG  . LYS   B 1 68  ? 40.129 75.275 18.253  1.00 40.60  ? 274 LYS   B CG  1 
ATOM   2353 C CD  . LYS   B 1 68  ? 40.732 76.128 19.350  1.00 45.28  ? 274 LYS   B CD  1 
ATOM   2354 C CE  . LYS   B 1 68  ? 40.131 77.528 19.379  1.00 52.17  ? 274 LYS   B CE  1 
ATOM   2355 N NZ  . LYS   B 1 68  ? 40.882 78.428 20.300  1.00 58.56  ? 274 LYS   B NZ  1 
ATOM   2356 N N   . GLU   B 1 69  ? 41.307 73.855 14.918  1.00 36.34  ? 275 GLU   B N   1 
ATOM   2357 C CA  . GLU   B 1 69  ? 41.171 74.417 13.578  1.00 43.19  ? 275 GLU   B CA  1 
ATOM   2358 C C   . GLU   B 1 69  ? 40.411 73.479 12.633  1.00 41.13  ? 275 GLU   B C   1 
ATOM   2359 O O   . GLU   B 1 69  ? 39.602 73.938 11.821  1.00 37.90  ? 275 GLU   B O   1 
ATOM   2360 C CB  . GLU   B 1 69  ? 42.555 74.754 13.019  1.00 45.70  ? 275 GLU   B CB  1 
ATOM   2361 C CG  . GLU   B 1 69  ? 42.509 75.740 11.858  1.00 57.85  ? 275 GLU   B CG  1 
ATOM   2362 C CD  . GLU   B 1 69  ? 43.704 75.649 10.929  1.00 67.73  ? 275 GLU   B CD  1 
ATOM   2363 O OE1 . GLU   B 1 69  ? 44.800 75.261 11.391  1.00 64.07  ? 275 GLU   B OE1 1 
ATOM   2364 O OE2 . GLU   B 1 69  ? 43.559 76.008 9.741   1.00 80.71  ? 275 GLU   B OE2 1 
ATOM   2365 N N   . LEU   B 1 70  ? 40.662 72.166 12.708  1.00 37.84  ? 276 LEU   B N   1 
ATOM   2366 C CA  . LEU   B 1 70  ? 39.894 71.223 11.893  1.00 36.09  ? 276 LEU   B CA  1 
ATOM   2367 C C   . LEU   B 1 70  ? 38.412 71.298 12.221  1.00 33.89  ? 276 LEU   B C   1 
ATOM   2368 O O   . LEU   B 1 70  ? 37.567 71.384 11.320  1.00 32.29  ? 276 LEU   B O   1 
ATOM   2369 C CB  . LEU   B 1 70  ? 40.404 69.798 12.111  1.00 33.92  ? 276 LEU   B CB  1 
ATOM   2370 C CG  . LEU   B 1 70  ? 41.696 69.427 11.396  1.00 39.46  ? 276 LEU   B CG  1 
ATOM   2371 C CD1 . LEU   B 1 70  ? 42.271 68.153 11.991  1.00 40.36  ? 276 LEU   B CD1 1 
ATOM   2372 C CD2 . LEU   B 1 70  ? 41.429 69.267 9.931   1.00 35.41  ? 276 LEU   B CD2 1 
ATOM   2373 N N   . PHE   B 1 71  ? 38.076 71.238 13.515  1.00 27.91  ? 277 PHE   B N   1 
ATOM   2374 C CA  . PHE   B 1 71  ? 36.678 71.286 13.943  1.00 34.81  ? 277 PHE   B CA  1 
ATOM   2375 C C   . PHE   B 1 71  ? 36.011 72.588 13.537  1.00 33.80  ? 277 PHE   B C   1 
ATOM   2376 O O   . PHE   B 1 71  ? 34.837 72.593 13.149  1.00 35.03  ? 277 PHE   B O   1 
ATOM   2377 C CB  . PHE   B 1 71  ? 36.575 71.103 15.461  1.00 30.31  ? 277 PHE   B CB  1 
ATOM   2378 C CG  . PHE   B 1 71  ? 35.163 70.951 15.964  1.00 33.87  ? 277 PHE   B CG  1 
ATOM   2379 C CD1 . PHE   B 1 71  ? 34.473 69.749 15.810  1.00 29.88  ? 277 PHE   B CD1 1 
ATOM   2380 C CD2 . PHE   B 1 71  ? 34.526 72.006 16.605  1.00 35.42  ? 277 PHE   B CD2 1 
ATOM   2381 C CE1 . PHE   B 1 71  ? 33.193 69.608 16.282  1.00 37.80  ? 277 PHE   B CE1 1 
ATOM   2382 C CE2 . PHE   B 1 71  ? 33.237 71.882 17.081  1.00 35.34  ? 277 PHE   B CE2 1 
ATOM   2383 C CZ  . PHE   B 1 71  ? 32.560 70.685 16.925  1.00 40.09  ? 277 PHE   B CZ  1 
ATOM   2384 N N   . GLY   B 1 72  ? 36.737 73.703 13.627  1.00 35.97  ? 278 GLY   B N   1 
ATOM   2385 C CA  . GLY   B 1 72  ? 36.180 74.971 13.195  1.00 33.18  ? 278 GLY   B CA  1 
ATOM   2386 C C   . GLY   B 1 72  ? 35.843 75.004 11.719  1.00 40.39  ? 278 GLY   B C   1 
ATOM   2387 O O   . GLY   B 1 72  ? 34.863 75.636 11.321  1.00 46.25  ? 278 GLY   B O   1 
ATOM   2388 N N   . LYS   B 1 73  ? 36.641 74.330 10.883  1.00 39.45  ? 279 LYS   B N   1 
ATOM   2389 C CA  . LYS   B 1 73  ? 36.303 74.280 9.462   1.00 36.50  ? 279 LYS   B CA  1 
ATOM   2390 C C   . LYS   B 1 73  ? 35.136 73.341 9.180   1.00 36.61  ? 279 LYS   B C   1 
ATOM   2391 O O   . LYS   B 1 73  ? 34.376 73.574 8.235   1.00 48.48  ? 279 LYS   B O   1 
ATOM   2392 C CB  . LYS   B 1 73  ? 37.521 73.890 8.628   1.00 44.00  ? 279 LYS   B CB  1 
ATOM   2393 C CG  . LYS   B 1 73  ? 38.691 74.834 8.812   1.00 52.34  ? 279 LYS   B CG  1 
ATOM   2394 C CD  . LYS   B 1 73  ? 39.694 74.708 7.675   1.00 66.85  ? 279 LYS   B CD  1 
ATOM   2395 C CE  . LYS   B 1 73  ? 41.117 74.850 8.161   1.00 64.49  ? 279 LYS   B CE  1 
ATOM   2396 N NZ  . LYS   B 1 73  ? 42.030 75.273 7.059   1.00 71.55  ? 279 LYS   B NZ  1 
ATOM   2397 N N   . GLY   B 1 74  ? 34.964 72.294 9.979   1.00 37.92  ? 280 GLY   B N   1 
ATOM   2398 C CA  . GLY   B 1 74  ? 33.829 71.418 9.831   1.00 35.54  ? 280 GLY   B CA  1 
ATOM   2399 C C   . GLY   B 1 74  ? 33.974 70.436 8.682   1.00 36.45  ? 280 GLY   B C   1 
ATOM   2400 O O   . GLY   B 1 74  ? 35.039 70.322 8.064   1.00 36.10  ? 280 GLY   B O   1 
ATOM   2401 N N   . PRO   B 1 75  ? 32.893 69.693 8.375   1.00 36.42  ? 281 PRO   B N   1 
ATOM   2402 C CA  . PRO   B 1 75  ? 31.567 69.709 9.032   1.00 33.60  ? 281 PRO   B CA  1 
ATOM   2403 C C   . PRO   B 1 75  ? 31.609 69.107 10.418  1.00 36.60  ? 281 PRO   B C   1 
ATOM   2404 O O   . PRO   B 1 75  ? 32.208 68.055 10.637  1.00 36.31  ? 281 PRO   B O   1 
ATOM   2405 C CB  . PRO   B 1 75  ? 30.698 68.862 8.092   1.00 34.50  ? 281 PRO   B CB  1 
ATOM   2406 C CG  . PRO   B 1 75  ? 31.674 67.923 7.426   1.00 31.42  ? 281 PRO   B CG  1 
ATOM   2407 C CD  . PRO   B 1 75  ? 32.936 68.734 7.253   1.00 31.20  ? 281 PRO   B CD  1 
ATOM   2408 N N   . GLN   B 1 76  ? 30.952 69.740 11.383  1.00 32.07  ? 282 GLN   B N   1 
ATOM   2409 C CA  . GLN   B 1 76  ? 31.083 69.288 12.754  1.00 34.24  ? 282 GLN   B CA  1 
ATOM   2410 C C   . GLN   B 1 76  ? 30.454 67.923 12.965  1.00 35.15  ? 282 GLN   B C   1 
ATOM   2411 O O   . GLN   B 1 76  ? 30.797 67.241 13.935  1.00 36.01  ? 282 GLN   B O   1 
ATOM   2412 C CB  . GLN   B 1 76  ? 30.473 70.330 13.684  1.00 38.65  ? 282 GLN   B CB  1 
ATOM   2413 C CG  . GLN   B 1 76  ? 31.173 71.665 13.534  1.00 43.32  ? 282 GLN   B CG  1 
ATOM   2414 C CD  . GLN   B 1 76  ? 30.710 72.716 14.530  1.00 50.22  ? 282 GLN   B CD  1 
ATOM   2415 O OE1 . GLN   B 1 76  ? 29.696 72.550 15.224  1.00 51.82  ? 282 GLN   B OE1 1 
ATOM   2416 N NE2 . GLN   B 1 76  ? 31.440 73.828 14.579  1.00 58.41  ? 282 GLN   B NE2 1 
ATOM   2417 N N   . ASN   B 1 77  ? 29.581 67.481 12.064  1.00 32.31  ? 283 ASN   B N   1 
ATOM   2418 C CA  . ASN   B 1 77  ? 28.980 66.168 12.251  1.00 33.81  ? 283 ASN   B CA  1 
ATOM   2419 C C   . ASN   B 1 77  ? 29.926 65.026 11.893  1.00 33.84  ? 283 ASN   B C   1 
ATOM   2420 O O   . ASN   B 1 77  ? 29.573 63.862 12.102  1.00 30.65  ? 283 ASN   B O   1 
ATOM   2421 C CB  . ASN   B 1 77  ? 27.674 66.059 11.459  1.00 37.11  ? 283 ASN   B CB  1 
ATOM   2422 C CG  . ASN   B 1 77  ? 27.892 65.983 9.954   1.00 44.26  ? 283 ASN   B CG  1 
ATOM   2423 O OD1 . ASN   B 1 77  ? 28.975 66.275 9.437   1.00 44.44  ? 283 ASN   B OD1 1 
ATOM   2424 N ND2 . ASN   B 1 77  ? 26.867 65.540 9.248   1.00 52.73  ? 283 ASN   B ND2 1 
ATOM   2425 N N   . ALA   B 1 78  ? 31.115 65.330 11.400  1.00 27.86  ? 284 ALA   B N   1 
ATOM   2426 C CA  . ALA   B 1 78  ? 32.109 64.325 11.044  1.00 30.49  ? 284 ALA   B CA  1 
ATOM   2427 C C   . ALA   B 1 78  ? 33.111 64.038 12.159  1.00 29.85  ? 284 ALA   B C   1 
ATOM   2428 O O   . ALA   B 1 78  ? 34.039 63.252 11.935  1.00 27.22  ? 284 ALA   B O   1 
ATOM   2429 C CB  . ALA   B 1 78  ? 32.879 64.777 9.795   1.00 29.37  ? 284 ALA   B CB  1 
ATOM   2430 N N   . PHE   B 1 79  ? 32.958 64.646 13.340  1.00 25.17  ? 285 PHE   B N   1 
ATOM   2431 C CA  . PHE   B 1 79  ? 33.962 64.585 14.405  1.00 27.37  ? 285 PHE   B CA  1 
ATOM   2432 C C   . PHE   B 1 79  ? 33.511 63.687 15.554  1.00 27.14  ? 285 PHE   B C   1 
ATOM   2433 O O   . PHE   B 1 79  ? 32.433 63.878 16.128  1.00 26.20  ? 285 PHE   B O   1 
ATOM   2434 C CB  . PHE   B 1 79  ? 34.311 65.998 14.910  1.00 25.94  ? 285 PHE   B CB  1 
ATOM   2435 C CG  . PHE   B 1 79  ? 35.181 66.786 13.940  1.00 27.87  ? 285 PHE   B CG  1 
ATOM   2436 C CD1 . PHE   B 1 79  ? 34.659 67.290 12.755  1.00 25.74  ? 285 PHE   B CD1 1 
ATOM   2437 C CD2 . PHE   B 1 79  ? 36.538 66.967 14.198  1.00 27.26  ? 285 PHE   B CD2 1 
ATOM   2438 C CE1 . PHE   B 1 79  ? 35.472 67.954 11.842  1.00 29.39  ? 285 PHE   B CE1 1 
ATOM   2439 C CE2 . PHE   B 1 79  ? 37.355 67.644 13.307  1.00 26.85  ? 285 PHE   B CE2 1 
ATOM   2440 C CZ  . PHE   B 1 79  ? 36.821 68.135 12.111  1.00 26.98  ? 285 PHE   B CZ  1 
ATOM   2441 N N   . PHE   B 1 80  ? 34.356 62.723 15.908  1.00 22.97  ? 286 PHE   B N   1 
ATOM   2442 C CA  . PHE   B 1 80  ? 34.024 61.759 16.937  1.00 23.28  ? 286 PHE   B CA  1 
ATOM   2443 C C   . PHE   B 1 80  ? 35.210 61.569 17.861  1.00 25.43  ? 286 PHE   B C   1 
ATOM   2444 O O   . PHE   B 1 80  ? 36.366 61.681 17.452  1.00 25.91  ? 286 PHE   B O   1 
ATOM   2445 C CB  . PHE   B 1 80  ? 33.626 60.402 16.320  1.00 21.57  ? 286 PHE   B CB  1 
ATOM   2446 C CG  . PHE   B 1 80  ? 32.454 60.484 15.394  1.00 22.36  ? 286 PHE   B CG  1 
ATOM   2447 C CD1 . PHE   B 1 80  ? 32.631 60.825 14.063  1.00 22.69  ? 286 PHE   B CD1 1 
ATOM   2448 C CD2 . PHE   B 1 80  ? 31.183 60.170 15.839  1.00 23.04  ? 286 PHE   B CD2 1 
ATOM   2449 C CE1 . PHE   B 1 80  ? 31.548 60.910 13.213  1.00 26.71  ? 286 PHE   B CE1 1 
ATOM   2450 C CE2 . PHE   B 1 80  ? 30.104 60.243 14.996  1.00 30.05  ? 286 PHE   B CE2 1 
ATOM   2451 C CZ  . PHE   B 1 80  ? 30.281 60.616 13.686  1.00 26.35  ? 286 PHE   B CZ  1 
ATOM   2452 N N   . LEU   B 1 81  ? 34.902 61.261 19.112  1.00 24.51  ? 287 LEU   B N   1 
ATOM   2453 C CA  . LEU   B 1 81  ? 35.862 60.765 20.077  1.00 22.16  ? 287 LEU   B CA  1 
ATOM   2454 C C   . LEU   B 1 81  ? 35.561 59.291 20.264  1.00 24.66  ? 287 LEU   B C   1 
ATOM   2455 O O   . LEU   B 1 81  ? 34.411 58.924 20.516  1.00 23.86  ? 287 LEU   B O   1 
ATOM   2456 C CB  . LEU   B 1 81  ? 35.726 61.505 21.411  1.00 24.89  ? 287 LEU   B CB  1 
ATOM   2457 C CG  . LEU   B 1 81  ? 36.488 60.990 22.630  1.00 28.90  ? 287 LEU   B CG  1 
ATOM   2458 C CD1 . LEU   B 1 81  ? 37.951 61.326 22.468  1.00 25.36  ? 287 LEU   B CD1 1 
ATOM   2459 C CD2 . LEU   B 1 81  ? 35.919 61.654 23.881  1.00 38.99  ? 287 LEU   B CD2 1 
ATOM   2460 N N   . VAL   B 1 82  ? 36.575 58.444 20.126  1.00 20.28  ? 288 VAL   B N   1 
ATOM   2461 C CA  . VAL   B 1 82  ? 36.391 57.009 20.259  1.00 25.21  ? 288 VAL   B CA  1 
ATOM   2462 C C   . VAL   B 1 82  ? 37.342 56.523 21.328  1.00 24.63  ? 288 VAL   B C   1 
ATOM   2463 O O   . VAL   B 1 82  ? 38.564 56.708 21.224  1.00 23.37  ? 288 VAL   B O   1 
ATOM   2464 C CB  . VAL   B 1 82  ? 36.614 56.268 18.925  1.00 27.10  ? 288 VAL   B CB  1 
ATOM   2465 C CG1 . VAL   B 1 82  ? 36.288 54.793 19.080  1.00 26.03  ? 288 VAL   B CG1 1 
ATOM   2466 C CG2 . VAL   B 1 82  ? 35.733 56.873 17.851  1.00 24.66  ? 288 VAL   B CG2 1 
ATOM   2467 N N   . LYS   B 1 83  ? 36.789 55.913 22.356  1.00 23.43  ? 289 LYS   B N   1 
ATOM   2468 C CA  . LYS   B 1 83  ? 37.593 55.313 23.393  1.00 23.22  ? 289 LYS   B CA  1 
ATOM   2469 C C   . LYS   B 1 83  ? 37.738 53.845 23.058  1.00 26.49  ? 289 LYS   B C   1 
ATOM   2470 O O   . LYS   B 1 83  ? 36.737 53.171 22.788  1.00 22.09  ? 289 LYS   B O   1 
ATOM   2471 C CB  . LYS   B 1 83  ? 36.950 55.476 24.776  1.00 24.90  ? 289 LYS   B CB  1 
ATOM   2472 C CG  . LYS   B 1 83  ? 37.775 54.853 25.879  1.00 30.38  ? 289 LYS   B CG  1 
ATOM   2473 C CD  . LYS   B 1 83  ? 37.289 55.341 27.259  1.00 38.63  ? 289 LYS   B CD  1 
ATOM   2474 C CE  . LYS   B 1 83  ? 38.168 54.785 28.371  1.00 43.88  ? 289 LYS   B CE  1 
ATOM   2475 N NZ  . LYS   B 1 83  ? 37.946 55.519 29.656  1.00 46.56  ? 289 LYS   B NZ  1 
ATOM   2476 N N   . PHE   B 1 84  ? 38.977 53.363 23.089  1.00 21.92  ? 290 PHE   B N   1 
ATOM   2477 C CA  . PHE   B 1 84  ? 39.319 51.971 22.822  1.00 23.22  ? 290 PHE   B CA  1 
ATOM   2478 C C   . PHE   B 1 84  ? 39.846 51.340 24.099  1.00 26.61  ? 290 PHE   B C   1 
ATOM   2479 O O   . PHE   B 1 84  ? 40.681 51.934 24.789  1.00 24.84  ? 290 PHE   B O   1 
ATOM   2480 C CB  . PHE   B 1 84  ? 40.410 51.854 21.749  1.00 20.34  ? 290 PHE   B CB  1 
ATOM   2481 C CG  . PHE   B 1 84  ? 39.954 52.243 20.350  1.00 24.43  ? 290 PHE   B CG  1 
ATOM   2482 C CD1 . PHE   B 1 84  ? 40.038 53.557 19.925  1.00 22.70  ? 290 PHE   B CD1 1 
ATOM   2483 C CD2 . PHE   B 1 84  ? 39.444 51.294 19.473  1.00 23.53  ? 290 PHE   B CD2 1 
ATOM   2484 C CE1 . PHE   B 1 84  ? 39.626 53.931 18.644  1.00 23.81  ? 290 PHE   B CE1 1 
ATOM   2485 C CE2 . PHE   B 1 84  ? 39.026 51.657 18.186  1.00 21.40  ? 290 PHE   B CE2 1 
ATOM   2486 C CZ  . PHE   B 1 84  ? 39.122 52.973 17.774  1.00 24.37  ? 290 PHE   B CZ  1 
ATOM   2487 N N   . TRP   B 1 85  ? 39.384 50.130 24.391  1.00 22.83  ? 291 TRP   B N   1 
ATOM   2488 C CA  . TRP   B 1 85  ? 39.975 49.291 25.426  1.00 26.94  ? 291 TRP   B CA  1 
ATOM   2489 C C   . TRP   B 1 85  ? 40.888 48.310 24.717  1.00 24.34  ? 291 TRP   B C   1 
ATOM   2490 O O   . TRP   B 1 85  ? 40.427 47.572 23.845  1.00 26.64  ? 291 TRP   B O   1 
ATOM   2491 C CB  . TRP   B 1 85  ? 38.896 48.544 26.207  1.00 24.97  ? 291 TRP   B CB  1 
ATOM   2492 C CG  . TRP   B 1 85  ? 38.232 49.423 27.207  1.00 30.35  ? 291 TRP   B CG  1 
ATOM   2493 C CD1 . TRP   B 1 85  ? 38.547 49.566 28.539  1.00 30.25  ? 291 TRP   B CD1 1 
ATOM   2494 C CD2 . TRP   B 1 85  ? 37.168 50.340 26.946  1.00 24.57  ? 291 TRP   B CD2 1 
ATOM   2495 N NE1 . TRP   B 1 85  ? 37.716 50.497 29.121  1.00 29.41  ? 291 TRP   B NE1 1 
ATOM   2496 C CE2 . TRP   B 1 85  ? 36.864 50.990 28.169  1.00 30.19  ? 291 TRP   B CE2 1 
ATOM   2497 C CE3 . TRP   B 1 85  ? 36.441 50.681 25.801  1.00 27.30  ? 291 TRP   B CE3 1 
ATOM   2498 C CZ2 . TRP   B 1 85  ? 35.858 51.943 28.274  1.00 35.00  ? 291 TRP   B CZ2 1 
ATOM   2499 C CZ3 . TRP   B 1 85  ? 35.438 51.637 25.907  1.00 32.28  ? 291 TRP   B CZ3 1 
ATOM   2500 C CH2 . TRP   B 1 85  ? 35.153 52.253 27.137  1.00 33.49  ? 291 TRP   B CH2 1 
ATOM   2501 N N   . ALA   B 1 86  ? 42.171 48.325 25.067  1.00 23.92  ? 292 ALA   B N   1 
ATOM   2502 C CA  . ALA   B 1 86  ? 43.190 47.520 24.407  1.00 22.93  ? 292 ALA   B CA  1 
ATOM   2503 C C   . ALA   B 1 86  ? 43.385 46.200 25.130  1.00 24.30  ? 292 ALA   B C   1 
ATOM   2504 O O   . ALA   B 1 86  ? 43.469 46.154 26.357  1.00 27.36  ? 292 ALA   B O   1 
ATOM   2505 C CB  . ALA   B 1 86  ? 44.525 48.267 24.365  1.00 23.69  ? 292 ALA   B CB  1 
ATOM   2506 N N   . ASP   B 1 87  ? 43.456 45.124 24.370  1.00 26.32  ? 293 ASP   B N   1 
ATOM   2507 C CA  . ASP   B 1 87  ? 43.679 43.799 24.928  1.00 25.56  ? 293 ASP   B CA  1 
ATOM   2508 C C   . ASP   B 1 87  ? 45.168 43.500 24.776  1.00 28.53  ? 293 ASP   B C   1 
ATOM   2509 O O   . ASP   B 1 87  ? 45.652 43.272 23.666  1.00 27.19  ? 293 ASP   B O   1 
ATOM   2510 C CB  . ASP   B 1 87  ? 42.806 42.762 24.222  1.00 26.80  ? 293 ASP   B CB  1 
ATOM   2511 C CG  . ASP   B 1 87  ? 42.921 41.361 24.827  1.00 32.66  ? 293 ASP   B CG  1 
ATOM   2512 O OD1 . ASP   B 1 87  ? 43.906 41.069 25.522  1.00 31.74  ? 293 ASP   B OD1 1 
ATOM   2513 O OD2 . ASP   B 1 87  ? 42.008 40.543 24.605  1.00 32.54  ? 293 ASP   B OD2 1 
ATOM   2514 N N   . LEU   B 1 88  ? 45.893 43.496 25.889  1.00 27.34  ? 294 LEU   B N   1 
ATOM   2515 C CA  . LEU   B 1 88  ? 47.327 43.251 25.861  1.00 32.43  ? 294 LEU   B CA  1 
ATOM   2516 C C   . LEU   B 1 88  ? 47.693 41.842 26.322  1.00 35.45  ? 294 LEU   B C   1 
ATOM   2517 O O   . LEU   B 1 88  ? 48.875 41.561 26.520  1.00 37.70  ? 294 LEU   B O   1 
ATOM   2518 C CB  . LEU   B 1 88  ? 48.050 44.285 26.721  1.00 30.25  ? 294 LEU   B CB  1 
ATOM   2519 C CG  . LEU   B 1 88  ? 47.810 45.754 26.388  1.00 36.43  ? 294 LEU   B CG  1 
ATOM   2520 C CD1 . LEU   B 1 88  ? 48.479 46.650 27.419  1.00 35.26  ? 294 LEU   B CD1 1 
ATOM   2521 C CD2 . LEU   B 1 88  ? 48.367 46.057 25.006  1.00 34.50  ? 294 LEU   B CD2 1 
ATOM   2522 N N   . ASN   B 1 89  ? 46.709 40.960 26.505  1.00 35.86  ? 295 ASN   B N   1 
ATOM   2523 C CA  . ASN   B 1 89  ? 46.933 39.587 26.971  1.00 34.69  ? 295 ASN   B CA  1 
ATOM   2524 C C   . ASN   B 1 89  ? 47.339 38.730 25.784  1.00 38.85  ? 295 ASN   B C   1 
ATOM   2525 O O   . ASN   B 1 89  ? 46.536 38.021 25.180  1.00 44.82  ? 295 ASN   B O   1 
ATOM   2526 C CB  . ASN   B 1 89  ? 45.681 39.024 27.612  1.00 41.18  ? 295 ASN   B CB  1 
ATOM   2527 C CG  . ASN   B 1 89  ? 45.224 39.841 28.777  1.00 48.65  ? 295 ASN   B CG  1 
ATOM   2528 O OD1 . ASN   B 1 89  ? 46.034 40.277 29.596  1.00 62.39  ? 295 ASN   B OD1 1 
ATOM   2529 N ND2 . ASN   B 1 89  ? 43.916 40.073 28.860  1.00 55.80  ? 295 ASN   B ND2 1 
ATOM   2530 N N   . CYS   B 1 90  ? 48.610 38.798 25.440  1.00 39.85  ? 296 CYS   B N   1 
ATOM   2531 C CA  A CYS   B 1 90  ? 49.106 38.047 24.304  0.55 40.19  ? 296 CYS   B CA  1 
ATOM   2532 C CA  B CYS   B 1 90  ? 49.116 38.081 24.283  0.45 40.20  ? 296 CYS   B CA  1 
ATOM   2533 C C   . CYS   B 1 90  ? 50.541 37.636 24.586  1.00 41.73  ? 296 CYS   B C   1 
ATOM   2534 O O   . CYS   B 1 90  ? 51.333 38.421 25.112  1.00 42.25  ? 296 CYS   B O   1 
ATOM   2535 C CB  A CYS   B 1 90  ? 48.984 38.865 23.013  0.55 39.93  ? 296 CYS   B CB  1 
ATOM   2536 C CB  B CYS   B 1 90  ? 49.052 38.981 23.041  0.45 39.85  ? 296 CYS   B CB  1 
ATOM   2537 S SG  A CYS   B 1 90  ? 50.090 40.277 22.903  0.55 39.90  ? 296 CYS   B SG  1 
ATOM   2538 S SG  B CYS   B 1 90  ? 49.961 38.432 21.593  0.45 40.28  ? 296 CYS   B SG  1 
ATOM   2539 N N   . ASN   B 1 91  ? 50.855 36.384 24.282  1.00 46.74  ? 297 ASN   B N   1 
ATOM   2540 C CA  . ASN   B 1 91  ? 52.203 35.870 24.482  1.00 48.12  ? 297 ASN   B CA  1 
ATOM   2541 C C   . ASN   B 1 91  ? 53.020 36.208 23.246  1.00 50.70  ? 297 ASN   B C   1 
ATOM   2542 O O   . ASN   B 1 91  ? 52.803 35.638 22.174  1.00 58.07  ? 297 ASN   B O   1 
ATOM   2543 C CB  . ASN   B 1 91  ? 52.196 34.366 24.746  1.00 49.96  ? 297 ASN   B CB  1 
ATOM   2544 C CG  . ASN   B 1 91  ? 53.601 33.786 24.811  1.00 59.92  ? 297 ASN   B CG  1 
ATOM   2545 O OD1 . ASN   B 1 91  ? 54.553 34.479 25.173  1.00 59.86  ? 297 ASN   B OD1 1 
ATOM   2546 N ND2 . ASN   B 1 91  ? 53.737 32.513 24.448  1.00 71.14  ? 297 ASN   B ND2 1 
ATOM   2547 N N   . ILE   B 1 92  ? 53.956 37.140 23.392  1.00 50.01  ? 298 ILE   B N   1 
ATOM   2548 C CA  . ILE   B 1 92  ? 54.830 37.537 22.298  1.00 53.06  ? 298 ILE   B CA  1 
ATOM   2549 C C   . ILE   B 1 92  ? 56.005 36.559 22.281  1.00 64.47  ? 298 ILE   B C   1 
ATOM   2550 O O   . ILE   B 1 92  ? 56.941 36.675 23.076  1.00 65.08  ? 298 ILE   B O   1 
ATOM   2551 C CB  . ILE   B 1 92  ? 55.280 38.988 22.447  1.00 49.73  ? 298 ILE   B CB  1 
ATOM   2552 C CG1 . ILE   B 1 92  ? 54.125 39.921 22.050  1.00 47.50  ? 298 ILE   B CG1 1 
ATOM   2553 C CG2 . ILE   B 1 92  ? 56.527 39.239 21.621  1.00 60.07  ? 298 ILE   B CG2 1 
ATOM   2554 C CD1 . ILE   B 1 92  ? 54.297 41.351 22.497  1.00 53.19  ? 298 ILE   B CD1 1 
ATOM   2555 N N   . GLN   B 1 93  ? 55.954 35.595 21.355  1.00 59.07  ? 299 GLN   B N   1 
ATOM   2556 C CA  . GLN   B 1 93  ? 56.872 34.466 21.284  1.00 67.04  ? 299 GLN   B CA  1 
ATOM   2557 C C   . GLN   B 1 93  ? 58.213 34.862 20.661  1.00 71.55  ? 299 GLN   B C   1 
ATOM   2558 O O   . GLN   B 1 93  ? 58.339 35.872 19.962  1.00 68.42  ? 299 GLN   B O   1 
ATOM   2559 C CB  . GLN   B 1 93  ? 56.250 33.316 20.477  1.00 71.04  ? 299 GLN   B CB  1 
ATOM   2560 C CG  . GLN   B 1 93  ? 54.851 32.847 20.941  1.00 72.56  ? 299 GLN   B CG  1 
ATOM   2561 C CD  . GLN   B 1 93  ? 54.062 32.101 19.848  1.00 78.62  ? 299 GLN   B CD  1 
ATOM   2562 O OE1 . GLN   B 1 93  ? 54.643 31.485 18.949  1.00 84.12  ? 299 GLN   B OE1 1 
ATOM   2563 N NE2 . GLN   B 1 93  ? 52.733 32.146 19.940  1.00 71.11  ? 299 GLN   B NE2 1 
ATOM   2564 N N   . ASP   B 1 94  ? 59.223 34.033 20.919  1.00 75.14  ? 300 ASP   B N   1 
ATOM   2565 C CA  . ASP   B 1 94  ? 60.551 34.206 20.344  1.00 77.48  ? 300 ASP   B CA  1 
ATOM   2566 C C   . ASP   B 1 94  ? 60.647 33.429 19.036  1.00 78.82  ? 300 ASP   B C   1 
ATOM   2567 O O   . ASP   B 1 94  ? 60.276 32.251 18.980  1.00 78.26  ? 300 ASP   B O   1 
ATOM   2568 C CB  . ASP   B 1 94  ? 61.631 33.733 21.321  1.00 70.28  ? 300 ASP   B CB  1 
ATOM   2569 C CG  . ASP   B 1 94  ? 61.572 34.457 22.650  0.00 73.23  ? 300 ASP   B CG  1 
ATOM   2570 O OD1 . ASP   B 1 94  ? 60.996 35.564 22.702  0.00 72.85  ? 300 ASP   B OD1 1 
ATOM   2571 O OD2 . ASP   B 1 94  ? 62.100 33.916 23.645  0.00 73.90  ? 300 ASP   B OD2 1 
ATOM   2572 N N   . ASP   B 1 95  ? 61.144 34.091 17.990  1.00 81.66  ? 301 ASP   B N   1 
ATOM   2573 C CA  . ASP   B 1 95  ? 61.298 33.501 16.658  1.00 84.09  ? 301 ASP   B CA  1 
ATOM   2574 C C   . ASP   B 1 95  ? 59.982 32.879 16.172  1.00 83.48  ? 301 ASP   B C   1 
ATOM   2575 O O   . ASP   B 1 95  ? 59.810 31.660 16.133  1.00 79.85  ? 301 ASP   B O   1 
ATOM   2576 C CB  . ASP   B 1 95  ? 62.435 32.470 16.656  1.00 77.01  ? 301 ASP   B CB  1 
ATOM   2577 C CG  . ASP   B 1 95  ? 63.790 33.095 16.922  0.00 81.26  ? 301 ASP   B CG  1 
ATOM   2578 O OD1 . ASP   B 1 95  ? 63.830 34.233 17.436  0.00 81.44  ? 301 ASP   B OD1 1 
ATOM   2579 O OD2 . ASP   B 1 95  ? 64.815 32.449 16.620  0.00 82.56  ? 301 ASP   B OD2 1 
ATOM   2580 N N   . ALA   B 1 96  ? 59.038 33.762 15.798  1.00 75.97  ? 302 ALA   B N   1 
ATOM   2581 C CA  . ALA   B 1 96  ? 57.728 33.301 15.350  1.00 74.18  ? 302 ALA   B CA  1 
ATOM   2582 C C   . ALA   B 1 96  ? 57.236 34.023 14.096  1.00 70.53  ? 302 ALA   B C   1 
ATOM   2583 O O   . ALA   B 1 96  ? 56.020 34.053 13.846  1.00 58.57  ? 302 ALA   B O   1 
ATOM   2584 C CB  . ALA   B 1 96  ? 56.682 33.451 16.469  1.00 65.46  ? 302 ALA   B CB  1 
ATOM   2585 N N   . GLY   B 1 97  ? 58.137 34.608 13.305  1.00 53.71  ? 303 GLY   B N   1 
ATOM   2586 C CA  . GLY   B 1 97  ? 57.745 35.331 12.107  1.00 51.62  ? 303 GLY   B CA  1 
ATOM   2587 C C   . GLY   B 1 97  ? 56.632 36.336 12.335  1.00 46.19  ? 303 GLY   B C   1 
ATOM   2588 O O   . GLY   B 1 97  ? 55.807 36.554 11.441  1.00 54.80  ? 303 GLY   B O   1 
ATOM   2589 N N   . ALA   B 1 98  ? 56.614 36.951 13.523  1.00 35.89  ? 304 ALA   B N   1 
ATOM   2590 C CA  . ALA   B 1 98  ? 55.539 37.852 13.928  1.00 38.42  ? 304 ALA   B CA  1 
ATOM   2591 C C   . ALA   B 1 98  ? 55.312 38.976 12.923  1.00 34.90  ? 304 ALA   B C   1 
ATOM   2592 O O   . ALA   B 1 98  ? 56.251 39.578 12.409  1.00 32.34  ? 304 ALA   B O   1 
ATOM   2593 C CB  . ALA   B 1 98  ? 55.855 38.446 15.299  1.00 29.96  ? 304 ALA   B CB  1 
ATOM   2594 N N   . PHE   B 1 99  ? 54.045 39.254 12.638  1.00 27.46  ? 305 PHE   B N   1 
ATOM   2595 C CA  . PHE   B 1 99  ? 53.663 40.394 11.828  1.00 27.23  ? 305 PHE   B CA  1 
ATOM   2596 C C   . PHE   B 1 99  ? 52.693 41.246 12.637  1.00 27.71  ? 305 PHE   B C   1 
ATOM   2597 O O   . PHE   B 1 99  ? 51.638 40.768 13.067  1.00 25.14  ? 305 PHE   B O   1 
ATOM   2598 C CB  . PHE   B 1 99  ? 53.037 39.952 10.507  1.00 26.91  ? 305 PHE   B CB  1 
ATOM   2599 C CG  . PHE   B 1 99  ? 52.567 41.090 9.663   1.00 32.92  ? 305 PHE   B CG  1 
ATOM   2600 C CD1 . PHE   B 1 99  ? 53.470 41.873 8.965   1.00 31.93  ? 305 PHE   B CD1 1 
ATOM   2601 C CD2 . PHE   B 1 99  ? 51.224 41.405 9.598   1.00 27.37  ? 305 PHE   B CD2 1 
ATOM   2602 C CE1 . PHE   B 1 99  ? 53.047 42.933 8.190   1.00 29.86  ? 305 PHE   B CE1 1 
ATOM   2603 C CE2 . PHE   B 1 99  ? 50.795 42.469 8.825   1.00 34.94  ? 305 PHE   B CE2 1 
ATOM   2604 C CZ  . PHE   B 1 99  ? 51.712 43.231 8.120   1.00 27.66  ? 305 PHE   B CZ  1 
ATOM   2605 N N   . TYR   B 1 100 ? 53.070 42.491 12.866  1.00 23.06  ? 306 TYR   B N   1 
ATOM   2606 C CA  . TYR   B 1 100 ? 52.236 43.473 13.535  1.00 24.83  ? 306 TYR   B CA  1 
ATOM   2607 C C   . TYR   B 1 100 ? 51.566 44.274 12.433  1.00 27.77  ? 306 TYR   B C   1 
ATOM   2608 O O   . TYR   B 1 100 ? 52.259 44.907 11.634  1.00 26.80  ? 306 TYR   B O   1 
ATOM   2609 C CB  . TYR   B 1 100 ? 53.079 44.397 14.421  1.00 21.87  ? 306 TYR   B CB  1 
ATOM   2610 C CG  . TYR   B 1 100 ? 53.678 43.732 15.634  1.00 25.73  ? 306 TYR   B CG  1 
ATOM   2611 C CD1 . TYR   B 1 100 ? 54.849 42.992 15.523  1.00 27.02  ? 306 TYR   B CD1 1 
ATOM   2612 C CD2 . TYR   B 1 100 ? 53.097 43.861 16.898  1.00 28.47  ? 306 TYR   B CD2 1 
ATOM   2613 C CE1 . TYR   B 1 100 ? 55.411 42.379 16.627  1.00 26.16  ? 306 TYR   B CE1 1 
ATOM   2614 C CE2 . TYR   B 1 100 ? 53.652 43.242 18.003  1.00 32.85  ? 306 TYR   B CE2 1 
ATOM   2615 C CZ  . TYR   B 1 100 ? 54.814 42.508 17.855  1.00 34.36  ? 306 TYR   B CZ  1 
ATOM   2616 O OH  . TYR   B 1 100 ? 55.374 41.892 18.938  1.00 41.47  ? 306 TYR   B OH  1 
ATOM   2617 N N   . GLY   B 1 101 ? 50.226 44.258 12.381  1.00 23.65  ? 307 GLY   B N   1 
ATOM   2618 C CA  . GLY   B 1 101 ? 49.529 44.903 11.288  1.00 23.44  ? 307 GLY   B CA  1 
ATOM   2619 C C   . GLY   B 1 101 ? 48.331 45.718 11.737  1.00 27.68  ? 307 GLY   B C   1 
ATOM   2620 O O   . GLY   B 1 101 ? 47.877 45.627 12.875  1.00 24.08  ? 307 GLY   B O   1 
ATOM   2621 N N   . VAL   B 1 102 ? 47.841 46.535 10.813  1.00 21.69  ? 308 VAL   B N   1 
ATOM   2622 C CA  A VAL   B 1 102 ? 46.637 47.335 10.991  0.50 27.58  ? 308 VAL   B CA  1 
ATOM   2623 C CA  B VAL   B 1 102 ? 46.612 47.286 11.012  0.50 26.19  ? 308 VAL   B CA  1 
ATOM   2624 C C   . VAL   B 1 102 ? 45.758 47.156 9.762   1.00 27.61  ? 308 VAL   B C   1 
ATOM   2625 O O   . VAL   B 1 102 ? 46.253 47.223 8.629   1.00 29.39  ? 308 VAL   B O   1 
ATOM   2626 C CB  A VAL   B 1 102 ? 46.971 48.831 11.193  0.50 26.79  ? 308 VAL   B CB  1 
ATOM   2627 C CB  B VAL   B 1 102 ? 46.857 48.776 11.354  0.50 26.73  ? 308 VAL   B CB  1 
ATOM   2628 C CG1 A VAL   B 1 102 ? 45.721 49.600 11.541  0.50 25.19  ? 308 VAL   B CG1 1 
ATOM   2629 C CG1 B VAL   B 1 102 ? 47.292 48.922 12.815  0.50 26.41  ? 308 VAL   B CG1 1 
ATOM   2630 C CG2 A VAL   B 1 102 ? 48.045 49.010 12.266  0.50 26.17  ? 308 VAL   B CG2 1 
ATOM   2631 C CG2 B VAL   B 1 102 ? 47.870 49.392 10.422  0.50 27.20  ? 308 VAL   B CG2 1 
ATOM   2632 N N   . THR   B 1 103 ? 44.468 46.957 9.973   1.00 23.95  ? 309 THR   B N   1 
ATOM   2633 C CA  . THR   B 1 103 ? 43.530 46.822 8.863   1.00 24.53  ? 309 THR   B CA  1 
ATOM   2634 C C   . THR   B 1 103 ? 42.386 47.788 9.086   1.00 30.76  ? 309 THR   B C   1 
ATOM   2635 O O   . THR   B 1 103 ? 41.924 47.943 10.221  1.00 26.02  ? 309 THR   B O   1 
ATOM   2636 C CB  . THR   B 1 103 ? 43.008 45.387 8.777   1.00 28.79  ? 309 THR   B CB  1 
ATOM   2637 O OG1 . THR   B 1 103 ? 44.057 44.557 8.276   1.00 33.06  ? 309 THR   B OG1 1 
ATOM   2638 C CG2 . THR   B 1 103 ? 41.811 45.285 7.820   1.00 32.31  ? 309 THR   B CG2 1 
ATOM   2639 N N   . SER   B 1 104 ? 41.955 48.465 8.022   1.00 25.61  ? 310 SER   B N   1 
ATOM   2640 C CA  . SER   B 1 104 ? 40.797 49.334 8.149   1.00 30.28  ? 310 SER   B CA  1 
ATOM   2641 C C   . SER   B 1 104 ? 39.978 49.333 6.864   1.00 31.48  ? 310 SER   B C   1 
ATOM   2642 O O   . SER   B 1 104 ? 40.483 49.051 5.772   1.00 28.56  ? 310 SER   B O   1 
ATOM   2643 C CB  . SER   B 1 104 ? 41.206 50.758 8.574   1.00 28.24  ? 310 SER   B CB  1 
ATOM   2644 O OG  . SER   B 1 104 ? 42.237 51.299 7.785   1.00 38.10  ? 310 SER   B OG  1 
ATOM   2645 N N   . GLN   B 1 105 ? 38.689 49.608 7.013   1.00 28.68  ? 311 GLN   B N   1 
ATOM   2646 C CA  . GLN   B 1 105 ? 37.805 49.710 5.864   1.00 30.17  ? 311 GLN   B CA  1 
ATOM   2647 C C   . GLN   B 1 105 ? 36.842 50.851 6.096   1.00 27.99  ? 311 GLN   B C   1 
ATOM   2648 O O   . GLN   B 1 105 ? 36.303 50.996 7.194   1.00 27.48  ? 311 GLN   B O   1 
ATOM   2649 C CB  . GLN   B 1 105 ? 37.030 48.416 5.615   1.00 27.58  ? 311 GLN   B CB  1 
ATOM   2650 C CG  . GLN   B 1 105 ? 35.911 48.583 4.589   1.00 32.79  ? 311 GLN   B CG  1 
ATOM   2651 C CD  . GLN   B 1 105 ? 35.388 47.250 4.087   1.00 43.79  ? 311 GLN   B CD  1 
ATOM   2652 O OE1 . GLN   B 1 105 ? 36.165 46.328 3.845   1.00 44.15  ? 311 GLN   B OE1 1 
ATOM   2653 N NE2 . GLN   B 1 105 ? 34.073 47.150 3.907   1.00 39.76  ? 311 GLN   B NE2 1 
ATOM   2654 N N   . TYR   B 1 106 ? 36.665 51.669 5.072   1.00 23.24  ? 312 TYR   B N   1 
ATOM   2655 C CA  . TYR   B 1 106 ? 35.720 52.767 5.084   1.00 23.20  ? 312 TYR   B CA  1 
ATOM   2656 C C   . TYR   B 1 106 ? 34.678 52.530 4.001   1.00 30.11  ? 312 TYR   B C   1 
ATOM   2657 O O   . TYR   B 1 106 ? 34.930 51.846 3.006   1.00 26.03  ? 312 TYR   B O   1 
ATOM   2658 C CB  . TYR   B 1 106 ? 36.418 54.100 4.812   1.00 24.77  ? 312 TYR   B CB  1 
ATOM   2659 C CG  . TYR   B 1 106 ? 37.512 54.437 5.789   1.00 29.24  ? 312 TYR   B CG  1 
ATOM   2660 C CD1 . TYR   B 1 106 ? 38.798 53.961 5.595   1.00 29.11  ? 312 TYR   B CD1 1 
ATOM   2661 C CD2 . TYR   B 1 106 ? 37.270 55.274 6.872   1.00 29.91  ? 312 TYR   B CD2 1 
ATOM   2662 C CE1 . TYR   B 1 106 ? 39.819 54.282 6.470   1.00 35.61  ? 312 TYR   B CE1 1 
ATOM   2663 C CE2 . TYR   B 1 106 ? 38.274 55.603 7.748   1.00 32.33  ? 312 TYR   B CE2 1 
ATOM   2664 C CZ  . TYR   B 1 106 ? 39.548 55.110 7.543   1.00 32.75  ? 312 TYR   B CZ  1 
ATOM   2665 O OH  . TYR   B 1 106 ? 40.550 55.443 8.430   1.00 40.74  ? 312 TYR   B OH  1 
ATOM   2666 N N   . GLU   B 1 107 ? 33.527 53.164 4.166   1.00 24.39  ? 313 GLU   B N   1 
ATOM   2667 C CA  . GLU   B 1 107 ? 32.467 53.112 3.175   1.00 28.98  ? 313 GLU   B CA  1 
ATOM   2668 C C   . GLU   B 1 107 ? 31.933 54.514 2.982   1.00 26.96  ? 313 GLU   B C   1 
ATOM   2669 O O   . GLU   B 1 107 ? 31.940 55.332 3.903   1.00 27.93  ? 313 GLU   B O   1 
ATOM   2670 C CB  . GLU   B 1 107 ? 31.330 52.187 3.608   1.00 24.22  ? 313 GLU   B CB  1 
ATOM   2671 C CG  . GLU   B 1 107 ? 31.764 50.763 3.661   1.00 35.35  ? 313 GLU   B CG  1 
ATOM   2672 C CD  . GLU   B 1 107 ? 30.675 49.852 4.193   1.00 33.21  ? 313 GLU   B CD  1 
ATOM   2673 O OE1 . GLU   B 1 107 ? 29.592 50.367 4.566   1.00 35.96  ? 313 GLU   B OE1 1 
ATOM   2674 O OE2 . GLU   B 1 107 ? 30.916 48.628 4.207   1.00 46.94  ? 313 GLU   B OE2 1 
ATOM   2675 N N   . SER   B 1 108 ? 31.490 54.786 1.764   1.00 27.11  ? 314 SER   B N   1 
ATOM   2676 C CA  . SER   B 1 108 ? 30.968 56.089 1.406   1.00 28.79  ? 314 SER   B CA  1 
ATOM   2677 C C   . SER   B 1 108 ? 29.860 55.912 0.375   1.00 28.14  ? 314 SER   B C   1 
ATOM   2678 O O   . SER   B 1 108 ? 29.816 54.919 -0.353  1.00 26.65  ? 314 SER   B O   1 
ATOM   2679 C CB  . SER   B 1 108 ? 32.066 56.983 0.838   1.00 31.47  ? 314 SER   B CB  1 
ATOM   2680 O OG  . SER   B 1 108 ? 31.549 58.260 0.542   1.00 38.84  ? 314 SER   B OG  1 
ATOM   2681 N N   . SER   B 1 109 ? 28.973 56.898 0.321   1.00 28.95  ? 315 SER   B N   1 
ATOM   2682 C CA  . SER   B 1 109 ? 27.972 56.968 -0.731  1.00 28.28  ? 315 SER   B CA  1 
ATOM   2683 C C   . SER   B 1 109 ? 28.525 57.619 -1.988  1.00 34.12  ? 315 SER   B C   1 
ATOM   2684 O O   . SER   B 1 109 ? 27.916 57.506 -3.047  1.00 30.77  ? 315 SER   B O   1 
ATOM   2685 C CB  . SER   B 1 109 ? 26.761 57.765 -0.257  1.00 34.56  ? 315 SER   B CB  1 
ATOM   2686 O OG  . SER   B 1 109 ? 27.191 59.003 0.286   1.00 37.10  ? 315 SER   B OG  1 
ATOM   2687 N N   . GLU   B 1 110 ? 29.668 58.289 -1.904  1.00 31.21  ? 316 GLU   B N   1 
ATOM   2688 C CA  . GLU   B 1 110 ? 30.230 58.982 -3.045  1.00 36.07  ? 316 GLU   B CA  1 
ATOM   2689 C C   . GLU   B 1 110 ? 31.559 58.363 -3.459  1.00 36.88  ? 316 GLU   B C   1 
ATOM   2690 O O   . GLU   B 1 110 ? 32.269 57.760 -2.647  1.00 30.76  ? 316 GLU   B O   1 
ATOM   2691 C CB  . GLU   B 1 110 ? 30.394 60.474 -2.746  1.00 43.69  ? 316 GLU   B CB  1 
ATOM   2692 C CG  . GLU   B 1 110 ? 29.095 61.093 -2.243  1.00 51.14  ? 316 GLU   B CG  1 
ATOM   2693 C CD  . GLU   B 1 110 ? 28.771 62.397 -2.928  1.00 64.36  ? 316 GLU   B CD  1 
ATOM   2694 O OE1 . GLU   B 1 110 ? 28.814 63.446 -2.248  1.00 79.21  ? 316 GLU   B OE1 1 
ATOM   2695 O OE2 . GLU   B 1 110 ? 28.470 62.375 -4.141  1.00 81.07  ? 316 GLU   B OE2 1 
ATOM   2696 N N   . ASN   B 1 111 ? 31.856 58.490 -4.755  1.00 31.90  ? 317 ASN   B N   1 
ATOM   2697 C CA  . ASN   B 1 111 ? 33.059 57.943 -5.365  1.00 33.78  ? 317 ASN   B CA  1 
ATOM   2698 C C   . ASN   B 1 111 ? 34.125 59.029 -5.285  1.00 39.62  ? 317 ASN   B C   1 
ATOM   2699 O O   . ASN   B 1 111 ? 34.000 60.073 -5.936  1.00 39.74  ? 317 ASN   B O   1 
ATOM   2700 C CB  . ASN   B 1 111 ? 32.789 57.547 -6.818  1.00 32.67  ? 317 ASN   B CB  1 
ATOM   2701 C CG  . ASN   B 1 111 ? 33.939 56.768 -7.438  1.00 41.73  ? 317 ASN   B CG  1 
ATOM   2702 O OD1 . ASN   B 1 111 ? 34.995 56.598 -6.838  1.00 43.09  ? 317 ASN   B OD1 1 
ATOM   2703 N ND2 . ASN   B 1 111 ? 33.736 56.304 -8.672  1.00 43.00  ? 317 ASN   B ND2 1 
ATOM   2704 N N   . MET   B 1 112 ? 35.190 58.767 -4.538  1.00 30.51  ? 318 MET   B N   1 
ATOM   2705 C CA  . MET   B 1 112 ? 36.060 59.816 -4.053  1.00 34.35  ? 318 MET   B CA  1 
ATOM   2706 C C   . MET   B 1 112 ? 37.466 59.232 -4.061  1.00 30.47  ? 318 MET   B C   1 
ATOM   2707 O O   . MET   B 1 112 ? 37.645 58.016 -4.009  1.00 36.14  ? 318 MET   B O   1 
ATOM   2708 C CB  . MET   B 1 112 ? 35.642 60.108 -2.620  1.00 37.49  ? 318 MET   B CB  1 
ATOM   2709 C CG  . MET   B 1 112 ? 34.419 60.959 -2.431  1.00 39.53  ? 318 MET   B CG  1 
ATOM   2710 S SD  . MET   B 1 112 ? 34.508 61.828 -0.888  1.00 37.02  ? 318 MET   B SD  1 
ATOM   2711 C CE  . MET   B 1 112 ? 34.033 60.423 0.114   1.00 33.84  ? 318 MET   B CE  1 
ATOM   2712 N N   . THR   B 1 113 ? 38.473 60.083 -4.133  1.00 32.09  ? 319 THR   B N   1 
ATOM   2713 C CA  . THR   B 1 113 ? 39.813 59.690 -3.738  1.00 31.33  ? 319 THR   B CA  1 
ATOM   2714 C C   . THR   B 1 113 ? 40.034 60.294 -2.353  1.00 30.99  ? 319 THR   B C   1 
ATOM   2715 O O   . THR   B 1 113 ? 39.783 61.485 -2.151  1.00 31.82  ? 319 THR   B O   1 
ATOM   2716 C CB  . THR   B 1 113 ? 40.851 60.196 -4.738  1.00 38.35  ? 319 THR   B CB  1 
ATOM   2717 O OG1 . THR   B 1 113 ? 40.677 59.508 -5.980  1.00 44.24  ? 319 THR   B OG1 1 
ATOM   2718 C CG2 . THR   B 1 113 ? 42.257 59.949 -4.229  1.00 36.73  ? 319 THR   B CG2 1 
ATOM   2719 N N   . VAL   B 1 114 ? 40.429 59.474 -1.392  1.00 27.79  ? 320 VAL   B N   1 
ATOM   2720 C CA  . VAL   B 1 114 ? 40.522 59.965 -0.019  1.00 26.88  ? 320 VAL   B CA  1 
ATOM   2721 C C   . VAL   B 1 114 ? 41.955 59.874 0.480   1.00 30.14  ? 320 VAL   B C   1 
ATOM   2722 O O   . VAL   B 1 114 ? 42.738 59.011 0.069   1.00 31.34  ? 320 VAL   B O   1 
ATOM   2723 C CB  . VAL   B 1 114 ? 39.576 59.228 0.959   1.00 31.42  ? 320 VAL   B CB  1 
ATOM   2724 C CG1 . VAL   B 1 114 ? 38.128 59.291 0.479   1.00 32.19  ? 320 VAL   B CG1 1 
ATOM   2725 C CG2 . VAL   B 1 114 ? 40.025 57.783 1.170   1.00 29.53  ? 320 VAL   B CG2 1 
ATOM   2726 N N   . THR   B 1 115 ? 42.272 60.760 1.421   1.00 32.22  ? 321 THR   B N   1 
ATOM   2727 C CA  . THR   B 1 115 ? 43.566 60.811 2.087   1.00 32.94  ? 321 THR   B CA  1 
ATOM   2728 C C   . THR   B 1 115 ? 43.325 60.478 3.553   1.00 31.48  ? 321 THR   B C   1 
ATOM   2729 O O   . THR   B 1 115 ? 42.519 61.144 4.211   1.00 29.36  ? 321 THR   B O   1 
ATOM   2730 C CB  . THR   B 1 115 ? 44.174 62.214 1.964   1.00 34.09  ? 321 THR   B CB  1 
ATOM   2731 O OG1 . THR   B 1 115 ? 44.488 62.480 0.595   1.00 45.99  ? 321 THR   B OG1 1 
ATOM   2732 C CG2 . THR   B 1 115 ? 45.450 62.270 2.712   1.00 39.68  ? 321 THR   B CG2 1 
ATOM   2733 N N   . CYS   B 1 116 ? 44.004 59.454 4.059   1.00 28.84  ? 322 CYS   B N   1 
ATOM   2734 C CA  A CYS   B 1 116 ? 43.851 58.999 5.438   0.47 30.06  ? 322 CYS   B CA  1 
ATOM   2735 C CA  B CYS   B 1 116 ? 43.852 59.007 5.442   0.53 31.21  ? 322 CYS   B CA  1 
ATOM   2736 C C   . CYS   B 1 116 ? 45.101 59.389 6.222   1.00 36.76  ? 322 CYS   B C   1 
ATOM   2737 O O   . CYS   B 1 116 ? 46.186 58.850 5.975   1.00 31.76  ? 322 CYS   B O   1 
ATOM   2738 C CB  A CYS   B 1 116 ? 43.627 57.490 5.483   0.47 33.33  ? 322 CYS   B CB  1 
ATOM   2739 C CB  B CYS   B 1 116 ? 43.615 57.502 5.516   0.53 33.34  ? 322 CYS   B CB  1 
ATOM   2740 S SG  A CYS   B 1 116 ? 43.270 56.822 7.124   0.47 50.09  ? 322 CYS   B SG  1 
ATOM   2741 S SG  B CYS   B 1 116 ? 42.177 56.939 4.603   0.53 35.46  ? 322 CYS   B SG  1 
ATOM   2742 N N   . SER   B 1 117 ? 44.947 60.301 7.174   1.00 29.83  ? 323 SER   B N   1 
ATOM   2743 C CA  . SER   B 1 117 ? 46.062 60.767 7.989   1.00 29.90  ? 323 SER   B CA  1 
ATOM   2744 C C   . SER   B 1 117 ? 45.958 60.159 9.386   1.00 35.75  ? 323 SER   B C   1 
ATOM   2745 O O   . SER   B 1 117 ? 44.929 60.315 10.050  1.00 33.44  ? 323 SER   B O   1 
ATOM   2746 C CB  . SER   B 1 117 ? 46.059 62.296 8.046   1.00 30.26  ? 323 SER   B CB  1 
ATOM   2747 O OG  . SER   B 1 117 ? 46.906 62.779 9.074   1.00 34.11  ? 323 SER   B OG  1 
ATOM   2748 N N   . THR   B 1 118 ? 47.012 59.455 9.824   1.00 26.36  ? 324 THR   B N   1 
ATOM   2749 C CA  . THR   B 1 118 ? 47.111 58.932 11.183  1.00 29.57  ? 324 THR   B CA  1 
ATOM   2750 C C   . THR   B 1 118 ? 48.220 59.679 11.920  1.00 30.37  ? 324 THR   B C   1 
ATOM   2751 O O   . THR   B 1 118 ? 49.379 59.629 11.506  1.00 33.76  ? 324 THR   B O   1 
ATOM   2752 C CB  . THR   B 1 118 ? 47.408 57.433 11.196  1.00 29.81  ? 324 THR   B CB  1 
ATOM   2753 O OG1 . THR   B 1 118 ? 46.400 56.733 10.476  1.00 33.12  ? 324 THR   B OG1 1 
ATOM   2754 C CG2 . THR   B 1 118 ? 47.406 56.917 12.623  1.00 31.86  ? 324 THR   B CG2 1 
ATOM   2755 N N   . LYS   B 1 119 ? 47.871 60.358 13.011  1.00 24.59  ? 325 LYS   B N   1 
ATOM   2756 C CA  . LYS   B 1 119 ? 48.852 61.043 13.843  1.00 29.37  ? 325 LYS   B CA  1 
ATOM   2757 C C   . LYS   B 1 119 ? 48.869 60.382 15.206  1.00 30.29  ? 325 LYS   B C   1 
ATOM   2758 O O   . LYS   B 1 119 ? 47.849 60.374 15.904  1.00 27.76  ? 325 LYS   B O   1 
ATOM   2759 C CB  . LYS   B 1 119 ? 48.530 62.530 13.968  1.00 27.95  ? 325 LYS   B CB  1 
ATOM   2760 C CG  . LYS   B 1 119 ? 48.891 63.318 12.736  1.00 35.26  ? 325 LYS   B CG  1 
ATOM   2761 C CD  . LYS   B 1 119 ? 48.400 64.749 12.808  1.00 38.11  ? 325 LYS   B CD  1 
ATOM   2762 C CE  . LYS   B 1 119 ? 48.727 65.470 11.518  1.00 45.03  ? 325 LYS   B CE  1 
ATOM   2763 N NZ  . LYS   B 1 119 ? 48.110 66.808 11.464  1.00 57.60  ? 325 LYS   B NZ  1 
ATOM   2764 N N   . VAL   B 1 120 ? 50.013 59.805 15.566  1.00 22.23  ? 326 VAL   B N   1 
ATOM   2765 C CA  . VAL   B 1 120 ? 50.198 59.182 16.868  1.00 23.67  ? 326 VAL   B CA  1 
ATOM   2766 C C   . VAL   B 1 120 ? 50.767 60.245 17.797  1.00 27.97  ? 326 VAL   B C   1 
ATOM   2767 O O   . VAL   B 1 120 ? 51.743 60.925 17.451  1.00 32.74  ? 326 VAL   B O   1 
ATOM   2768 C CB  . VAL   B 1 120 ? 51.134 57.967 16.766  1.00 28.69  ? 326 VAL   B CB  1 
ATOM   2769 C CG1 . VAL   B 1 120 ? 51.432 57.388 18.145  1.00 31.75  ? 326 VAL   B CG1 1 
ATOM   2770 C CG2 . VAL   B 1 120 ? 50.531 56.886 15.860  1.00 24.60  ? 326 VAL   B CG2 1 
ATOM   2771 N N   . CYS   B 1 121 ? 50.139 60.433 18.949  1.00 26.50  ? 327 CYS   B N   1 
ATOM   2772 C CA  . CYS   B 1 121 ? 50.506 61.545 19.807  1.00 27.28  ? 327 CYS   B CA  1 
ATOM   2773 C C   . CYS   B 1 121 ? 50.856 61.077 21.211  1.00 28.83  ? 327 CYS   B C   1 
ATOM   2774 O O   . CYS   B 1 121 ? 50.287 60.120 21.727  1.00 27.38  ? 327 CYS   B O   1 
ATOM   2775 C CB  . CYS   B 1 121 ? 49.395 62.595 19.887  1.00 28.55  ? 327 CYS   B CB  1 
ATOM   2776 S SG  . CYS   B 1 121 ? 48.806 63.150 18.296  1.00 36.71  ? 327 CYS   B SG  1 
ATOM   2777 N N   . SER   B 1 122 ? 51.783 61.811 21.829  1.00 29.31  ? 328 SER   B N   1 
ATOM   2778 C CA  . SER   B 1 122 ? 52.241 61.578 23.194  1.00 35.18  ? 328 SER   B CA  1 
ATOM   2779 C C   . SER   B 1 122 ? 52.141 62.900 23.935  1.00 30.57  ? 328 SER   B C   1 
ATOM   2780 O O   . SER   B 1 122 ? 52.776 63.879 23.529  1.00 31.81  ? 328 SER   B O   1 
ATOM   2781 C CB  . SER   B 1 122 ? 53.687 61.083 23.216  1.00 32.84  ? 328 SER   B CB  1 
ATOM   2782 O OG  . SER   B 1 122 ? 54.081 60.780 24.536  1.00 33.23  ? 328 SER   B OG  1 
ATOM   2783 N N   . PHE   B 1 123 ? 51.358 62.921 25.013  1.00 29.33  ? 329 PHE   B N   1 
ATOM   2784 C CA  . PHE   B 1 123 ? 51.074 64.150 25.751  1.00 37.33  ? 329 PHE   B CA  1 
ATOM   2785 C C   . PHE   B 1 123 ? 50.587 65.250 24.818  1.00 33.88  ? 329 PHE   B C   1 
ATOM   2786 O O   . PHE   B 1 123 ? 50.969 66.411 24.940  1.00 35.89  ? 329 PHE   B O   1 
ATOM   2787 C CB  . PHE   B 1 123 ? 52.293 64.609 26.563  1.00 34.29  ? 329 PHE   B CB  1 
ATOM   2788 C CG  . PHE   B 1 123 ? 52.550 63.759 27.771  1.00 31.22  ? 329 PHE   B CG  1 
ATOM   2789 C CD1 . PHE   B 1 123 ? 53.341 62.629 27.687  1.00 34.19  ? 329 PHE   B CD1 1 
ATOM   2790 C CD2 . PHE   B 1 123 ? 51.946 64.056 28.972  1.00 35.29  ? 329 PHE   B CD2 1 
ATOM   2791 C CE1 . PHE   B 1 123 ? 53.547 61.835 28.795  1.00 30.96  ? 329 PHE   B CE1 1 
ATOM   2792 C CE2 . PHE   B 1 123 ? 52.144 63.258 30.075  1.00 36.21  ? 329 PHE   B CE2 1 
ATOM   2793 C CZ  . PHE   B 1 123 ? 52.959 62.156 29.985  1.00 33.18  ? 329 PHE   B CZ  1 
ATOM   2794 N N   . GLY   B 1 124 ? 49.729 64.875 23.868  1.00 33.16  ? 330 GLY   B N   1 
ATOM   2795 C CA  . GLY   B 1 124 ? 49.127 65.822 22.960  1.00 35.63  ? 330 GLY   B CA  1 
ATOM   2796 C C   . GLY   B 1 124 ? 50.010 66.293 21.828  1.00 38.83  ? 330 GLY   B C   1 
ATOM   2797 O O   . GLY   B 1 124 ? 49.561 67.119 21.029  1.00 42.93  ? 330 GLY   B O   1 
ATOM   2798 N N   . LYS   B 1 125 ? 51.216 65.781 21.729  1.00 31.90  ? 331 LYS   B N   1 
ATOM   2799 C CA  . LYS   B 1 125 ? 52.114 66.155 20.666  1.00 31.98  ? 331 LYS   B CA  1 
ATOM   2800 C C   . LYS   B 1 125 ? 52.374 65.031 19.690  1.00 37.20  ? 331 LYS   B C   1 
ATOM   2801 O O   . LYS   B 1 125 ? 52.663 63.926 20.082  1.00 31.87  ? 331 LYS   B O   1 
ATOM   2802 C CB  . LYS   B 1 125 ? 53.447 66.646 21.219  1.00 35.01  ? 331 LYS   B CB  1 
ATOM   2803 C CG  . LYS   B 1 125 ? 53.321 67.709 22.287  1.00 50.19  ? 331 LYS   B CG  1 
ATOM   2804 C CD  . LYS   B 1 125 ? 54.338 68.807 22.092  1.00 61.40  ? 331 LYS   B CD  1 
ATOM   2805 C CE  . LYS   B 1 125 ? 54.367 69.729 23.296  1.00 69.21  ? 331 LYS   B CE  1 
ATOM   2806 N NZ  . LYS   B 1 125 ? 55.700 70.370 23.451  1.00 87.76  ? 331 LYS   B NZ  1 
ATOM   2807 N N   . GLN   B 1 126 ? 52.370 65.359 18.414  1.00 35.41  ? 332 GLN   B N   1 
ATOM   2808 C CA  . GLN   B 1 126 ? 52.631 64.379 17.394  1.00 35.56  ? 332 GLN   B CA  1 
ATOM   2809 C C   . GLN   B 1 126 ? 54.014 63.830 17.465  1.00 34.90  ? 332 GLN   B C   1 
ATOM   2810 O O   . GLN   B 1 126 ? 54.977 64.570 17.479  1.00 35.14  ? 332 GLN   B O   1 
ATOM   2811 C CB  . GLN   B 1 126 ? 52.411 64.981 16.007  1.00 37.99  ? 332 GLN   B CB  1 
ATOM   2812 C CG  . GLN   B 1 126 ? 52.437 63.989 14.862  1.00 36.18  ? 332 GLN   B CG  1 
ATOM   2813 C CD  . GLN   B 1 126 ? 52.683 64.659 13.529  1.00 45.15  ? 332 GLN   B CD  1 
ATOM   2814 O OE1 . GLN   B 1 126 ? 51.851 65.390 13.033  1.00 48.57  ? 332 GLN   B OE1 1 
ATOM   2815 N NE2 . GLN   B 1 126 ? 53.830 64.407 12.946  1.00 46.83  ? 332 GLN   B NE2 1 
ATOM   2816 N N   . VAL   B 1 127 ? 54.105 62.519 17.507  1.00 31.76  ? 333 VAL   B N   1 
ATOM   2817 C CA  . VAL   B 1 127 ? 55.409 61.873 17.489  1.00 33.81  ? 333 VAL   B CA  1 
ATOM   2818 C C   . VAL   B 1 127 ? 55.692 61.182 16.157  1.00 38.05  ? 333 VAL   B C   1 
ATOM   2819 O O   . VAL   B 1 127 ? 56.815 61.259 15.657  1.00 33.73  ? 333 VAL   B O   1 
ATOM   2820 C CB  . VAL   B 1 127 ? 55.590 60.899 18.675  1.00 36.35  ? 333 VAL   B CB  1 
ATOM   2821 C CG1 . VAL   B 1 127 ? 55.686 61.682 19.993  1.00 37.19  ? 333 VAL   B CG1 1 
ATOM   2822 C CG2 . VAL   B 1 127 ? 54.464 59.921 18.758  1.00 40.40  ? 333 VAL   B CG2 1 
ATOM   2823 N N   . VAL   B 1 128 ? 54.704 60.497 15.561  1.00 32.50  ? 334 VAL   B N   1 
ATOM   2824 C CA  . VAL   B 1 128 ? 54.845 59.956 14.211  1.00 34.38  ? 334 VAL   B CA  1 
ATOM   2825 C C   . VAL   B 1 128 ? 53.526 60.130 13.469  1.00 38.36  ? 334 VAL   B C   1 
ATOM   2826 O O   . VAL   B 1 128 ? 52.456 60.276 14.069  1.00 33.17  ? 334 VAL   B O   1 
ATOM   2827 C CB  . VAL   B 1 128 ? 55.280 58.466 14.173  1.00 40.65  ? 334 VAL   B CB  1 
ATOM   2828 C CG1 . VAL   B 1 128 ? 56.742 58.304 14.589  1.00 40.17  ? 334 VAL   B CG1 1 
ATOM   2829 C CG2 . VAL   B 1 128 ? 54.384 57.603 15.032  1.00 36.36  ? 334 VAL   B CG2 1 
ATOM   2830 N N   . GLU   B 1 129 ? 53.617 60.114 12.141  1.00 37.07  ? 335 GLU   B N   1 
ATOM   2831 C CA  . GLU   B 1 129 ? 52.459 60.353 11.293  1.00 38.41  ? 335 GLU   B CA  1 
ATOM   2832 C C   . GLU   B 1 129 ? 52.558 59.540 10.008  1.00 38.61  ? 335 GLU   B C   1 
ATOM   2833 O O   . GLU   B 1 129 ? 53.651 59.235 9.517   1.00 37.45  ? 335 GLU   B O   1 
ATOM   2834 C CB  . GLU   B 1 129 ? 52.293 61.844 10.965  1.00 39.83  ? 335 GLU   B CB  1 
ATOM   2835 C CG  . GLU   B 1 129 ? 51.034 62.119 10.147  1.00 49.47  ? 335 GLU   B CG  1 
ATOM   2836 C CD  . GLU   B 1 129 ? 51.089 63.415 9.376   1.00 52.27  ? 335 GLU   B CD  1 
ATOM   2837 O OE1 . GLU   B 1 129 ? 52.173 64.037 9.340   1.00 59.89  ? 335 GLU   B OE1 1 
ATOM   2838 O OE2 . GLU   B 1 129 ? 50.024 63.845 8.877   1.00 56.45  ? 335 GLU   B OE2 1 
ATOM   2839 N N   . LYS   B 1 130 ? 51.398 59.171 9.482   1.00 32.46  ? 336 LYS   B N   1 
ATOM   2840 C CA  . LYS   B 1 130 ? 51.325 58.455 8.221   1.00 36.87  ? 336 LYS   B CA  1 
ATOM   2841 C C   . LYS   B 1 130 ? 50.164 59.010 7.424   1.00 36.89  ? 336 LYS   B C   1 
ATOM   2842 O O   . LYS   B 1 130 ? 49.082 59.241 7.971   1.00 34.13  ? 336 LYS   B O   1 
ATOM   2843 C CB  . LYS   B 1 130 ? 51.145 56.951 8.444   1.00 37.22  ? 336 LYS   B CB  1 
ATOM   2844 C CG  . LYS   B 1 130 ? 51.776 56.067 7.371   1.00 44.19  ? 336 LYS   B CG  1 
ATOM   2845 C CD  . LYS   B 1 130 ? 50.964 54.815 7.119   1.00 49.37  ? 336 LYS   B CD  1 
ATOM   2846 C CE  . LYS   B 1 130 ? 51.356 54.165 5.794   1.00 59.17  ? 336 LYS   B CE  1 
ATOM   2847 N NZ  . LYS   B 1 130 ? 50.870 52.754 5.755   1.00 67.44  ? 336 LYS   B NZ  1 
ATOM   2848 N N   . VAL   B 1 131 ? 50.385 59.204 6.131   1.00 32.50  ? 337 VAL   B N   1 
ATOM   2849 C CA  . VAL   B 1 131 ? 49.347 59.647 5.213   1.00 31.29  ? 337 VAL   B CA  1 
ATOM   2850 C C   . VAL   B 1 131 ? 49.225 58.580 4.132   1.00 36.06  ? 337 VAL   B C   1 
ATOM   2851 O O   . VAL   B 1 131 ? 50.225 58.209 3.514   1.00 38.59  ? 337 VAL   B O   1 
ATOM   2852 C CB  . VAL   B 1 131 ? 49.676 61.017 4.609   1.00 38.07  ? 337 VAL   B CB  1 
ATOM   2853 C CG1 . VAL   B 1 131 ? 48.656 61.393 3.578   1.00 39.42  ? 337 VAL   B CG1 1 
ATOM   2854 C CG2 . VAL   B 1 131 ? 49.734 62.050 5.694   1.00 38.21  ? 337 VAL   B CG2 1 
ATOM   2855 N N   . GLU   B 1 132 ? 48.022 58.043 3.954   1.00 31.17  ? 338 GLU   B N   1 
ATOM   2856 C CA  . GLU   B 1 132 ? 47.736 57.045 2.934   1.00 36.61  ? 338 GLU   B CA  1 
ATOM   2857 C C   . GLU   B 1 132 ? 46.667 57.583 1.991   1.00 33.88  ? 338 GLU   B C   1 
ATOM   2858 O O   . GLU   B 1 132 ? 45.791 58.351 2.390   1.00 35.16  ? 338 GLU   B O   1 
ATOM   2859 C CB  . GLU   B 1 132 ? 47.266 55.708 3.552   1.00 37.21  ? 338 GLU   B CB  1 
ATOM   2860 C CG  . GLU   B 1 132 ? 48.352 54.881 4.215   1.00 52.12  ? 338 GLU   B CG  1 
ATOM   2861 C CD  . GLU   B 1 132 ? 47.880 54.098 5.438   1.00 60.47  ? 338 GLU   B CD  1 
ATOM   2862 O OE1 . GLU   B 1 132 ? 47.046 54.615 6.218   1.00 64.51  ? 338 GLU   B OE1 1 
ATOM   2863 O OE2 . GLU   B 1 132 ? 48.359 52.951 5.620   1.00 67.56  ? 338 GLU   B OE2 1 
ATOM   2864 N N   . THR   B 1 133 ? 46.747 57.189 0.730   1.00 33.45  ? 339 THR   B N   1 
ATOM   2865 C CA  . THR   B 1 133 ? 45.762 57.560 -0.277  1.00 31.24  ? 339 THR   B CA  1 
ATOM   2866 C C   . THR   B 1 133 ? 45.037 56.298 -0.701  1.00 32.75  ? 339 THR   B C   1 
ATOM   2867 O O   . THR   B 1 133 ? 45.682 55.288 -0.989  1.00 33.56  ? 339 THR   B O   1 
ATOM   2868 C CB  . THR   B 1 133 ? 46.442 58.213 -1.471  1.00 41.95  ? 339 THR   B CB  1 
ATOM   2869 O OG1 . THR   B 1 133 ? 47.188 59.328 -0.997  1.00 38.48  ? 339 THR   B OG1 1 
ATOM   2870 C CG2 . THR   B 1 133 ? 45.419 58.698 -2.491  1.00 29.84  ? 339 THR   B CG2 1 
ATOM   2871 N N   . GLU   B 1 134 ? 43.707 56.337 -0.709  1.00 30.59  ? 340 GLU   B N   1 
ATOM   2872 C CA  . GLU   B 1 134 ? 42.930 55.176 -1.117  1.00 30.63  ? 340 GLU   B CA  1 
ATOM   2873 C C   . GLU   B 1 134 ? 41.880 55.568 -2.145  1.00 30.79  ? 340 GLU   B C   1 
ATOM   2874 O O   . GLU   B 1 134 ? 41.362 56.684 -2.139  1.00 30.09  ? 340 GLU   B O   1 
ATOM   2875 C CB  . GLU   B 1 134 ? 42.274 54.487 0.084   1.00 35.10  ? 340 GLU   B CB  1 
ATOM   2876 C CG  . GLU   B 1 134 ? 43.208 53.531 0.822   1.00 46.31  ? 340 GLU   B CG  1 
ATOM   2877 C CD  . GLU   B 1 134 ? 43.811 52.442 -0.075  1.00 46.09  ? 340 GLU   B CD  1 
ATOM   2878 O OE1 . GLU   B 1 134 ? 43.181 52.034 -1.093  1.00 46.55  ? 340 GLU   B OE1 1 
ATOM   2879 O OE2 . GLU   B 1 134 ? 44.927 51.990 0.246   1.00 59.42  ? 340 GLU   B OE2 1 
ATOM   2880 N N   . TYR   B 1 135 ? 41.565 54.613 -3.019  1.00 30.38  ? 341 TYR   B N   1 
ATOM   2881 C CA  . TYR   B 1 135 ? 40.641 54.808 -4.123  1.00 26.95  ? 341 TYR   B CA  1 
ATOM   2882 C C   . TYR   B 1 135 ? 39.445 53.881 -3.944  1.00 30.76  ? 341 TYR   B C   1 
ATOM   2883 O O   . TYR   B 1 135 ? 39.594 52.740 -3.505  1.00 29.69  ? 341 TYR   B O   1 
ATOM   2884 C CB  . TYR   B 1 135 ? 41.346 54.543 -5.476  1.00 29.09  ? 341 TYR   B CB  1 
ATOM   2885 C CG  . TYR   B 1 135 ? 42.594 55.397 -5.667  1.00 32.70  ? 341 TYR   B CG  1 
ATOM   2886 C CD1 . TYR   B 1 135 ? 43.798 55.042 -5.093  1.00 33.82  ? 341 TYR   B CD1 1 
ATOM   2887 C CD2 . TYR   B 1 135 ? 42.535 56.590 -6.361  1.00 34.74  ? 341 TYR   B CD2 1 
ATOM   2888 C CE1 . TYR   B 1 135 ? 44.927 55.836 -5.247  1.00 33.36  ? 341 TYR   B CE1 1 
ATOM   2889 C CE2 . TYR   B 1 135 ? 43.645 57.391 -6.509  1.00 38.92  ? 341 TYR   B CE2 1 
ATOM   2890 C CZ  . TYR   B 1 135 ? 44.836 57.004 -5.953  1.00 34.26  ? 341 TYR   B CZ  1 
ATOM   2891 O OH  . TYR   B 1 135 ? 45.946 57.806 -6.108  1.00 54.82  ? 341 TYR   B OH  1 
ATOM   2892 N N   . ALA   B 1 136 ? 38.262 54.378 -4.294  1.00 27.29  ? 342 ALA   B N   1 
ATOM   2893 C CA  . ALA   B 1 136 ? 37.022 53.656 -4.033  1.00 32.74  ? 342 ALA   B CA  1 
ATOM   2894 C C   . ALA   B 1 136 ? 36.837 52.462 -4.962  1.00 39.73  ? 342 ALA   B C   1 
ATOM   2895 O O   . ALA   B 1 136 ? 37.152 52.517 -6.154  1.00 39.32  ? 342 ALA   B O   1 
ATOM   2896 C CB  . ALA   B 1 136 ? 35.834 54.607 -4.176  1.00 34.65  ? 342 ALA   B CB  1 
ATOM   2897 N N   . ARG   B 1 137 ? 36.234 51.425 -4.420  1.00 34.00  ? 343 ARG   B N   1 
ATOM   2898 C CA  . ARG   B 1 137 ? 35.834 50.282 -5.192  1.00 39.21  ? 343 ARG   B CA  1 
ATOM   2899 C C   . ARG   B 1 137 ? 34.309 50.146 -4.961  1.00 34.25  ? 343 ARG   B C   1 
ATOM   2900 O O   . ARG   B 1 137 ? 33.875 50.068 -3.832  1.00 31.63  ? 343 ARG   B O   1 
ATOM   2901 C CB  . ARG   B 1 137 ? 36.502 49.029 -4.708  1.00 37.71  ? 343 ARG   B CB  1 
ATOM   2902 C CG  . ARG   B 1 137 ? 36.149 47.808 -5.519  1.00 48.42  ? 343 ARG   B CG  1 
ATOM   2903 C CD  . ARG   B 1 137 ? 36.945 46.612 -5.058  1.00 58.64  ? 343 ARG   B CD  1 
ATOM   2904 N NE  . ARG   B 1 137 ? 36.326 45.377 -5.512  1.00 69.24  ? 343 ARG   B NE  1 
ATOM   2905 C CZ  . ARG   B 1 137 ? 36.919 44.190 -5.505  1.00 78.31  ? 343 ARG   B CZ  1 
ATOM   2906 N NH1 . ARG   B 1 137 ? 38.162 44.059 -5.064  1.00 85.67  ? 343 ARG   B NH1 1 
ATOM   2907 N NH2 . ARG   B 1 137 ? 36.262 43.128 -5.942  1.00 84.58  ? 343 ARG   B NH2 1 
ATOM   2908 N N   . PHE   B 1 138 ? 33.512 50.107 -6.025  1.00 35.63  ? 344 PHE   B N   1 
ATOM   2909 C CA  . PHE   B 1 138 ? 32.060 49.987 -5.874  1.00 34.83  ? 344 PHE   B CA  1 
ATOM   2910 C C   . PHE   B 1 138 ? 31.706 48.557 -5.483  1.00 29.24  ? 344 PHE   B C   1 
ATOM   2911 O O   . PHE   B 1 138 ? 32.085 47.613 -6.173  1.00 39.66  ? 344 PHE   B O   1 
ATOM   2912 C CB  . PHE   B 1 138 ? 31.334 50.406 -7.152  1.00 41.46  ? 344 PHE   B CB  1 
ATOM   2913 C CG  . PHE   B 1 138 ? 29.826 50.408 -7.017  1.00 33.37  ? 344 PHE   B CG  1 
ATOM   2914 C CD1 . PHE   B 1 138 ? 29.185 51.409 -6.303  1.00 31.62  ? 344 PHE   B CD1 1 
ATOM   2915 C CD2 . PHE   B 1 138 ? 29.056 49.398 -7.590  1.00 33.66  ? 344 PHE   B CD2 1 
ATOM   2916 C CE1 . PHE   B 1 138 ? 27.809 51.418 -6.167  1.00 36.47  ? 344 PHE   B CE1 1 
ATOM   2917 C CE2 . PHE   B 1 138 ? 27.669 49.390 -7.445  1.00 26.67  ? 344 PHE   B CE2 1 
ATOM   2918 C CZ  . PHE   B 1 138 ? 27.045 50.401 -6.739  1.00 30.03  ? 344 PHE   B CZ  1 
ATOM   2919 N N   . GLU   B 1 139 ? 31.010 48.388 -4.358  1.00 30.02  ? 345 GLU   B N   1 
ATOM   2920 C CA  . GLU   B 1 139 ? 30.657 47.065 -3.850  1.00 32.35  ? 345 GLU   B CA  1 
ATOM   2921 C C   . GLU   B 1 139 ? 29.276 47.121 -3.222  1.00 35.88  ? 345 GLU   B C   1 
ATOM   2922 O O   . GLU   B 1 139 ? 29.085 47.826 -2.228  1.00 29.86  ? 345 GLU   B O   1 
ATOM   2923 C CB  . GLU   B 1 139 ? 31.645 46.565 -2.789  1.00 32.50  ? 345 GLU   B CB  1 
ATOM   2924 C CG  . GLU   B 1 139 ? 32.961 46.073 -3.321  1.00 45.66  ? 345 GLU   B CG  1 
ATOM   2925 C CD  . GLU   B 1 139 ? 33.913 45.686 -2.201  1.00 50.98  ? 345 GLU   B CD  1 
ATOM   2926 O OE1 . GLU   B 1 139 ? 33.439 45.494 -1.057  1.00 46.34  ? 345 GLU   B OE1 1 
ATOM   2927 O OE2 . GLU   B 1 139 ? 35.135 45.604 -2.454  1.00 63.35  ? 345 GLU   B OE2 1 
ATOM   2928 N N   . ASN   B 1 140 ? 28.332 46.364 -3.780  1.00 38.71  ? 346 ASN   B N   1 
ATOM   2929 C CA  . ASN   B 1 140 ? 27.010 46.160 -3.178  1.00 36.85  ? 346 ASN   B CA  1 
ATOM   2930 C C   . ASN   B 1 140 ? 26.343 47.476 -2.782  1.00 27.85  ? 346 ASN   B C   1 
ATOM   2931 O O   . ASN   B 1 140 ? 25.761 47.610 -1.708  1.00 33.00  ? 346 ASN   B O   1 
ATOM   2932 C CB  . ASN   B 1 140 ? 27.091 45.208 -1.989  1.00 38.21  ? 346 ASN   B CB  1 
ATOM   2933 C CG  . ASN   B 1 140 ? 27.594 43.820 -2.391  1.00 45.08  ? 346 ASN   B CG  1 
ATOM   2934 O OD1 . ASN   B 1 140 ? 27.107 43.227 -3.353  1.00 49.47  ? 346 ASN   B OD1 1 
ATOM   2935 N ND2 . ASN   B 1 140 ? 28.561 43.298 -1.649  1.00 50.07  ? 346 ASN   B ND2 1 
ATOM   2936 N N   . GLY   B 1 141 ? 26.450 48.467 -3.650  1.00 27.03  ? 347 GLY   B N   1 
ATOM   2937 C CA  . GLY   B 1 141 ? 25.682 49.677 -3.509  1.00 27.79  ? 347 GLY   B CA  1 
ATOM   2938 C C   . GLY   B 1 141 ? 26.407 50.838 -2.868  1.00 30.28  ? 347 GLY   B C   1 
ATOM   2939 O O   . GLY   B 1 141 ? 25.816 51.910 -2.754  1.00 30.19  ? 347 GLY   B O   1 
ATOM   2940 N N   . ARG   B 1 142 ? 27.655 50.660 -2.442  1.00 26.56  ? 348 ARG   B N   1 
ATOM   2941 C CA  A ARG   B 1 142 ? 28.436 51.696 -1.769  0.50 32.73  ? 348 ARG   B CA  1 
ATOM   2942 C CA  B ARG   B 1 142 ? 28.410 51.763 -1.870  0.50 32.70  ? 348 ARG   B CA  1 
ATOM   2943 C C   . ARG   B 1 142 ? 29.869 51.654 -2.285  1.00 25.60  ? 348 ARG   B C   1 
ATOM   2944 O O   . ARG   B 1 142 ? 30.311 50.664 -2.865  1.00 29.64  ? 348 ARG   B O   1 
ATOM   2945 C CB  A ARG   B 1 142 ? 28.448 51.533 -0.226  0.50 29.82  ? 348 ARG   B CB  1 
ATOM   2946 C CB  B ARG   B 1 142 ? 28.271 51.803 -0.345  0.50 29.67  ? 348 ARG   B CB  1 
ATOM   2947 C CG  A ARG   B 1 142 ? 27.550 50.436 0.361   0.50 30.78  ? 348 ARG   B CG  1 
ATOM   2948 C CG  B ARG   B 1 142 ? 29.130 50.796 0.371   0.50 28.80  ? 348 ARG   B CG  1 
ATOM   2949 C CD  A ARG   B 1 142 ? 27.901 50.111 1.826   0.50 33.10  ? 348 ARG   B CD  1 
ATOM   2950 C CD  B ARG   B 1 142 ? 28.391 49.500 0.596   0.50 32.78  ? 348 ARG   B CD  1 
ATOM   2951 N NE  A ARG   B 1 142 ? 26.762 50.144 2.747   0.50 34.82  ? 348 ARG   B NE  1 
ATOM   2952 N NE  B ARG   B 1 142 ? 29.079 48.663 1.572   0.50 38.08  ? 348 ARG   B NE  1 
ATOM   2953 C CZ  A ARG   B 1 142 ? 26.019 49.092 3.072   0.50 34.82  ? 348 ARG   B CZ  1 
ATOM   2954 C CZ  B ARG   B 1 142 ? 29.618 47.480 1.312   0.50 33.19  ? 348 ARG   B CZ  1 
ATOM   2955 N NH1 A ARG   B 1 142 ? 26.225 47.903 2.533   0.50 31.84  ? 348 ARG   B NH1 1 
ATOM   2956 N NH1 B ARG   B 1 142 ? 29.555 46.942 0.108   0.50 34.19  ? 348 ARG   B NH1 1 
ATOM   2957 N NH2 A ARG   B 1 142 ? 25.038 49.238 3.959   0.50 35.15  ? 348 ARG   B NH2 1 
ATOM   2958 N NH2 B ARG   B 1 142 ? 30.238 46.825 2.287   0.50 36.59  ? 348 ARG   B NH2 1 
ATOM   2959 N N   . PHE   B 1 143 ? 30.605 52.719 -2.028  1.00 26.69  ? 349 PHE   B N   1 
ATOM   2960 C CA  . PHE   B 1 143 ? 32.016 52.782 -2.350  1.00 26.08  ? 349 PHE   B CA  1 
ATOM   2961 C C   . PHE   B 1 143 ? 32.819 52.385 -1.117  1.00 27.09  ? 349 PHE   B C   1 
ATOM   2962 O O   . PHE   B 1 143 ? 32.571 52.888 -0.014  1.00 26.63  ? 349 PHE   B O   1 
ATOM   2963 C CB  . PHE   B 1 143 ? 32.356 54.183 -2.862  1.00 26.34  ? 349 PHE   B CB  1 
ATOM   2964 C CG  . PHE   B 1 143 ? 31.620 54.514 -4.137  1.00 26.65  ? 349 PHE   B CG  1 
ATOM   2965 C CD1 . PHE   B 1 143 ? 32.054 54.015 -5.352  1.00 30.79  ? 349 PHE   B CD1 1 
ATOM   2966 C CD2 . PHE   B 1 143 ? 30.431 55.221 -4.100  1.00 24.78  ? 349 PHE   B CD2 1 
ATOM   2967 C CE1 . PHE   B 1 143 ? 31.345 54.273 -6.524  1.00 35.81  ? 349 PHE   B CE1 1 
ATOM   2968 C CE2 . PHE   B 1 143 ? 29.719 55.481 -5.260  1.00 31.89  ? 349 PHE   B CE2 1 
ATOM   2969 C CZ  . PHE   B 1 143 ? 30.179 55.005 -6.472  1.00 35.94  ? 349 PHE   B CZ  1 
ATOM   2970 N N   . VAL   B 1 144 ? 33.750 51.458 -1.307  1.00 23.76  ? 350 VAL   B N   1 
ATOM   2971 C CA  . VAL   B 1 144 ? 34.509 50.850 -0.226  1.00 27.44  ? 350 VAL   B CA  1 
ATOM   2972 C C   . VAL   B 1 144 ? 35.980 51.217 -0.405  1.00 29.52  ? 350 VAL   B C   1 
ATOM   2973 O O   . VAL   B 1 144 ? 36.490 51.240 -1.531  1.00 27.82  ? 350 VAL   B O   1 
ATOM   2974 C CB  . VAL   B 1 144 ? 34.294 49.325 -0.209  1.00 32.44  ? 350 VAL   B CB  1 
ATOM   2975 C CG1 . VAL   B 1 144 ? 35.183 48.662 0.812   1.00 30.54  ? 350 VAL   B CG1 1 
ATOM   2976 C CG2 . VAL   B 1 144 ? 32.829 49.000 0.067   1.00 29.61  ? 350 VAL   B CG2 1 
ATOM   2977 N N   . TYR   B 1 145 ? 36.647 51.545 0.703   1.00 23.88  ? 351 TYR   B N   1 
ATOM   2978 C CA  . TYR   B 1 145 ? 38.063 51.906 0.738   1.00 23.03  ? 351 TYR   B CA  1 
ATOM   2979 C C   . TYR   B 1 145 ? 38.741 50.966 1.723   1.00 29.67  ? 351 TYR   B C   1 
ATOM   2980 O O   . TYR   B 1 145 ? 38.414 50.980 2.912   1.00 31.68  ? 351 TYR   B O   1 
ATOM   2981 C CB  . TYR   B 1 145 ? 38.254 53.358 1.187   1.00 26.54  ? 351 TYR   B CB  1 
ATOM   2982 C CG  . TYR   B 1 145 ? 37.480 54.366 0.392   1.00 25.95  ? 351 TYR   B CG  1 
ATOM   2983 C CD1 . TYR   B 1 145 ? 36.131 54.575 0.643   1.00 23.35  ? 351 TYR   B CD1 1 
ATOM   2984 C CD2 . TYR   B 1 145 ? 38.093 55.128 -0.605  1.00 29.02  ? 351 TYR   B CD2 1 
ATOM   2985 C CE1 . TYR   B 1 145 ? 35.399 55.485 -0.086  1.00 26.14  ? 351 TYR   B CE1 1 
ATOM   2986 C CE2 . TYR   B 1 145 ? 37.367 56.070 -1.334  1.00 26.65  ? 351 TYR   B CE2 1 
ATOM   2987 C CZ  . TYR   B 1 145 ? 36.016 56.235 -1.063  1.00 32.93  ? 351 TYR   B CZ  1 
ATOM   2988 O OH  . TYR   B 1 145 ? 35.271 57.135 -1.787  1.00 33.30  ? 351 TYR   B OH  1 
ATOM   2989 N N   . ARG   B 1 146 ? 39.653 50.132 1.243   1.00 28.43  ? 352 ARG   B N   1 
ATOM   2990 C CA  . ARG   B 1 146 ? 40.296 49.125 2.082   1.00 31.69  ? 352 ARG   B CA  1 
ATOM   2991 C C   . ARG   B 1 146 ? 41.776 49.407 2.224   1.00 34.79  ? 352 ARG   B C   1 
ATOM   2992 O O   . ARG   B 1 146 ? 42.471 49.600 1.226   1.00 35.52  ? 352 ARG   B O   1 
ATOM   2993 C CB  . ARG   B 1 146 ? 40.150 47.718 1.517   1.00 30.13  ? 352 ARG   B CB  1 
ATOM   2994 C CG  . ARG   B 1 146 ? 38.856 47.091 1.793   1.00 44.34  ? 352 ARG   B CG  1 
ATOM   2995 C CD  . ARG   B 1 146 ? 38.874 45.672 1.329   1.00 45.77  ? 352 ARG   B CD  1 
ATOM   2996 N NE  . ARG   B 1 146 ? 37.553 45.096 1.500   1.00 48.42  ? 352 ARG   B NE  1 
ATOM   2997 C CZ  . ARG   B 1 146 ? 36.649 45.049 0.535   1.00 46.96  ? 352 ARG   B CZ  1 
ATOM   2998 N NH1 . ARG   B 1 146 ? 36.920 45.485 -0.685  1.00 46.59  ? 352 ARG   B NH1 1 
ATOM   2999 N NH2 . ARG   B 1 146 ? 35.443 44.566 0.804   1.00 50.58  ? 352 ARG   B NH2 1 
ATOM   3000 N N   . ILE   B 1 147 ? 42.248 49.394 3.456   1.00 28.23  ? 353 ILE   B N   1 
ATOM   3001 C CA  . ILE   B 1 147 ? 43.670 49.401 3.769   1.00 33.32  ? 353 ILE   B CA  1 
ATOM   3002 C C   . ILE   B 1 147 ? 43.904 48.084 4.487   1.00 35.53  ? 353 ILE   B C   1 
ATOM   3003 O O   . ILE   B 1 147 ? 43.676 47.960 5.692   1.00 32.17  ? 353 ILE   B O   1 
ATOM   3004 C CB  . ILE   B 1 147 ? 44.076 50.604 4.623   1.00 40.05  ? 353 ILE   B CB  1 
ATOM   3005 C CG1 . ILE   B 1 147 ? 43.444 51.873 4.057   1.00 36.80  ? 353 ILE   B CG1 1 
ATOM   3006 C CG2 . ILE   B 1 147 ? 45.596 50.732 4.721   1.00 49.81  ? 353 ILE   B CG2 1 
ATOM   3007 C CD1 . ILE   B 1 147 ? 44.084 53.155 4.542   1.00 42.31  ? 353 ILE   B CD1 1 
ATOM   3008 N N   . ASN   B 1 148 ? 44.295 47.062 3.742   1.00 35.25  ? 354 ASN   B N   1 
ATOM   3009 C CA  . ASN   B 1 148 ? 44.373 45.714 4.285   1.00 38.96  ? 354 ASN   B CA  1 
ATOM   3010 C C   . ASN   B 1 148 ? 45.793 45.422 4.754   1.00 38.09  ? 354 ASN   B C   1 
ATOM   3011 O O   . ASN   B 1 148 ? 46.753 45.640 4.014   1.00 42.39  ? 354 ASN   B O   1 
ATOM   3012 C CB  . ASN   B 1 148 ? 43.940 44.676 3.243   1.00 40.53  ? 354 ASN   B CB  1 
ATOM   3013 C CG  . ASN   B 1 148 ? 43.586 43.333 3.872   1.00 55.24  ? 354 ASN   B CG  1 
ATOM   3014 O OD1 . ASN   B 1 148 ? 43.046 43.271 4.977   1.00 60.43  ? 354 ASN   B OD1 1 
ATOM   3015 N ND2 . ASN   B 1 148 ? 43.936 42.254 3.193   1.00 52.84  ? 354 ASN   B ND2 1 
ATOM   3016 N N   . ARG   B 1 149 ? 45.920 44.941 5.986   1.00 35.53  ? 355 ARG   B N   1 
ATOM   3017 C CA  . ARG   B 1 149 ? 47.160 44.348 6.481   1.00 36.32  ? 355 ARG   B CA  1 
ATOM   3018 C C   . ARG   B 1 149 ? 48.372 45.274 6.303   1.00 31.53  ? 355 ARG   B C   1 
ATOM   3019 O O   . ARG   B 1 149 ? 49.429 44.873 5.823   1.00 36.89  ? 355 ARG   B O   1 
ATOM   3020 C CB  . ARG   B 1 149 ? 47.400 43.001 5.803   1.00 33.38  ? 355 ARG   B CB  1 
ATOM   3021 C CG  . ARG   B 1 149 ? 48.214 42.061 6.643   1.00 43.15  ? 355 ARG   B CG  1 
ATOM   3022 C CD  . ARG   B 1 149 ? 47.949 40.580 6.361   1.00 40.35  ? 355 ARG   B CD  1 
ATOM   3023 N NE  . ARG   B 1 149 ? 49.029 39.771 6.918   1.00 45.91  ? 355 ARG   B NE  1 
ATOM   3024 C CZ  . ARG   B 1 149 ? 50.273 39.748 6.452   1.00 42.80  ? 355 ARG   B CZ  1 
ATOM   3025 N NH1 . ARG   B 1 149 ? 50.599 40.320 5.299   1.00 41.78  ? 355 ARG   B NH1 1 
ATOM   3026 N NH2 . ARG   B 1 149 ? 51.212 39.113 7.145   1.00 46.55  ? 355 ARG   B NH2 1 
ATOM   3027 N N   . SER   B 1 150 ? 48.225 46.507 6.714   1.00 29.22  ? 356 SER   B N   1 
ATOM   3028 C CA  . SER   B 1 150 ? 49.346 47.439 6.647   1.00 33.05  ? 356 SER   B CA  1 
ATOM   3029 C C   . SER   B 1 150 ? 50.279 47.219 7.845   1.00 31.16  ? 356 SER   B C   1 
ATOM   3030 O O   . SER   B 1 150 ? 49.803 47.090 8.974   1.00 30.87  ? 356 SER   B O   1 
ATOM   3031 C CB  . SER   B 1 150 ? 48.797 48.865 6.617   1.00 32.06  ? 356 SER   B CB  1 
ATOM   3032 O OG  . SER   B 1 150 ? 49.821 49.816 6.792   1.00 49.95  ? 356 SER   B OG  1 
ATOM   3033 N N   . PRO   B 1 151 ? 51.601 47.162 7.648   1.00 30.52  ? 357 PRO   B N   1 
ATOM   3034 C CA  . PRO   B 1 151 ? 52.507 46.938 8.793   1.00 32.76  ? 357 PRO   B CA  1 
ATOM   3035 C C   . PRO   B 1 151 ? 52.438 48.082 9.798   1.00 30.84  ? 357 PRO   B C   1 
ATOM   3036 O O   . PRO   B 1 151 ? 52.312 49.245 9.415   1.00 29.41  ? 357 PRO   B O   1 
ATOM   3037 C CB  . PRO   B 1 151 ? 53.900 46.869 8.146   1.00 34.09  ? 357 PRO   B CB  1 
ATOM   3038 C CG  . PRO   B 1 151 ? 53.735 47.464 6.777   1.00 32.41  ? 357 PRO   B CG  1 
ATOM   3039 C CD  . PRO   B 1 151 ? 52.320 47.231 6.363   1.00 31.12  ? 357 PRO   B CD  1 
ATOM   3040 N N   . MET   B 1 152 ? 52.525 47.750 11.092  1.00 24.87  ? 358 MET   B N   1 
ATOM   3041 C CA  . MET   B 1 152 ? 52.645 48.798 12.115  1.00 28.67  ? 358 MET   B CA  1 
ATOM   3042 C C   . MET   B 1 152 ? 54.008 49.463 12.028  1.00 30.22  ? 358 MET   B C   1 
ATOM   3043 O O   . MET   B 1 152 ? 55.013 48.796 11.802  1.00 28.92  ? 358 MET   B O   1 
ATOM   3044 C CB  . MET   B 1 152 ? 52.517 48.237 13.522  1.00 26.40  ? 358 MET   B CB  1 
ATOM   3045 C CG  . MET   B 1 152 ? 51.156 47.998 14.045  1.00 29.00  ? 358 MET   B CG  1 
ATOM   3046 S SD  . MET   B 1 152 ? 51.349 47.511 15.809  1.00 29.02  ? 358 MET   B SD  1 
ATOM   3047 C CE  . MET   B 1 152 ? 49.840 46.605 16.067  1.00 21.42  ? 358 MET   B CE  1 
ATOM   3048 N N   . CYS   B 1 153 ? 54.054 50.772 12.253  1.00 27.48  ? 359 CYS   B N   1 
ATOM   3049 C CA  . CYS   B 1 153 ? 55.357 51.431 12.303  1.00 31.90  ? 359 CYS   B CA  1 
ATOM   3050 C C   . CYS   B 1 153 ? 56.159 50.922 13.501  1.00 29.74  ? 359 CYS   B C   1 
ATOM   3051 O O   . CYS   B 1 153 ? 55.610 50.416 14.485  1.00 29.64  ? 359 CYS   B O   1 
ATOM   3052 C CB  . CYS   B 1 153 ? 55.196 52.947 12.374  1.00 32.48  ? 359 CYS   B CB  1 
ATOM   3053 S SG  . CYS   B 1 153 ? 54.299 53.565 13.856  1.00 40.01  ? 359 CYS   B SG  1 
ATOM   3054 N N   . GLU   B 1 154 ? 57.480 51.058 13.409  1.00 30.30  ? 360 GLU   B N   1 
ATOM   3055 C CA  . GLU   B 1 154 ? 58.342 50.581 14.488  1.00 34.71  ? 360 GLU   B CA  1 
ATOM   3056 C C   . GLU   B 1 154 ? 58.031 51.269 15.812  1.00 34.06  ? 360 GLU   B C   1 
ATOM   3057 O O   . GLU   B 1 154 ? 58.102 50.634 16.867  1.00 31.98  ? 360 GLU   B O   1 
ATOM   3058 C CB  . GLU   B 1 154 ? 59.811 50.782 14.131  1.00 36.81  ? 360 GLU   B CB  1 
ATOM   3059 C CG  . GLU   B 1 154 ? 60.747 49.977 15.035  1.00 44.54  ? 360 GLU   B CG  1 
ATOM   3060 C CD  . GLU   B 1 154 ? 60.477 48.489 14.999  1.00 39.28  ? 360 GLU   B CD  1 
ATOM   3061 O OE1 . GLU   B 1 154 ? 60.326 47.933 13.891  1.00 39.61  ? 360 GLU   B OE1 1 
ATOM   3062 O OE2 . GLU   B 1 154 ? 60.423 47.872 16.083  1.00 38.42  ? 360 GLU   B OE2 1 
ATOM   3063 N N   . TYR   B 1 155 ? 57.664 52.560 15.779  1.00 32.92  ? 361 TYR   B N   1 
ATOM   3064 C CA  . TYR   B 1 155 ? 57.311 53.249 17.022  1.00 34.96  ? 361 TYR   B CA  1 
ATOM   3065 C C   . TYR   B 1 155 ? 56.201 52.510 17.761  1.00 32.53  ? 361 TYR   B C   1 
ATOM   3066 O O   . TYR   B 1 155 ? 56.285 52.299 18.977  1.00 29.48  ? 361 TYR   B O   1 
ATOM   3067 C CB  . TYR   B 1 155 ? 56.899 54.706 16.747  1.00 36.68  ? 361 TYR   B CB  1 
ATOM   3068 C CG  . TYR   B 1 155 ? 56.554 55.489 18.017  1.00 36.64  ? 361 TYR   B CG  1 
ATOM   3069 C CD1 . TYR   B 1 155 ? 55.273 55.439 18.583  1.00 32.93  ? 361 TYR   B CD1 1 
ATOM   3070 C CD2 . TYR   B 1 155 ? 57.525 56.248 18.676  1.00 41.13  ? 361 TYR   B CD2 1 
ATOM   3071 C CE1 . TYR   B 1 155 ? 54.973 56.130 19.764  1.00 39.41  ? 361 TYR   B CE1 1 
ATOM   3072 C CE2 . TYR   B 1 155 ? 57.231 56.943 19.847  1.00 36.36  ? 361 TYR   B CE2 1 
ATOM   3073 C CZ  . TYR   B 1 155 ? 55.958 56.888 20.384  1.00 39.20  ? 361 TYR   B CZ  1 
ATOM   3074 O OH  . TYR   B 1 155 ? 55.676 57.577 21.549  1.00 39.08  ? 361 TYR   B OH  1 
ATOM   3075 N N   . MET   B 1 156 ? 55.161 52.064 17.040  1.00 29.09  ? 362 MET   B N   1 
ATOM   3076 C CA  . MET   B 1 156 ? 54.067 51.406 17.745  1.00 25.59  ? 362 MET   B CA  1 
ATOM   3077 C C   . MET   B 1 156 ? 54.423 49.990 18.187  1.00 30.29  ? 362 MET   B C   1 
ATOM   3078 O O   . MET   B 1 156 ? 53.977 49.552 19.255  1.00 26.81  ? 362 MET   B O   1 
ATOM   3079 C CB  . MET   B 1 156 ? 52.794 51.401 16.897  1.00 28.04  ? 362 MET   B CB  1 
ATOM   3080 C CG  . MET   B 1 156 ? 52.205 52.811 16.787  1.00 31.16  ? 362 MET   B CG  1 
ATOM   3081 S SD  . MET   B 1 156 ? 51.594 53.373 18.390  1.00 35.02  ? 362 MET   B SD  1 
ATOM   3082 C CE  . MET   B 1 156 ? 50.703 51.944 19.011  1.00 28.41  ? 362 MET   B CE  1 
ATOM   3083 N N   . ILE   B 1 157 ? 55.218 49.259 17.406  1.00 28.54  ? 363 ILE   B N   1 
ATOM   3084 C CA  . ILE   B 1 157 ? 55.638 47.931 17.849  1.00 28.86  ? 363 ILE   B CA  1 
ATOM   3085 C C   . ILE   B 1 157 ? 56.442 48.047 19.137  1.00 29.90  ? 363 ILE   B C   1 
ATOM   3086 O O   . ILE   B 1 157 ? 56.225 47.306 20.103  1.00 31.87  ? 363 ILE   B O   1 
ATOM   3087 C CB  . ILE   B 1 157 ? 56.445 47.225 16.741  1.00 31.17  ? 363 ILE   B CB  1 
ATOM   3088 C CG1 . ILE   B 1 157 ? 55.601 47.103 15.465  1.00 27.27  ? 363 ILE   B CG1 1 
ATOM   3089 C CG2 . ILE   B 1 157 ? 56.917 45.849 17.237  1.00 33.26  ? 363 ILE   B CG2 1 
ATOM   3090 C CD1 . ILE   B 1 157 ? 56.336 46.553 14.230  1.00 29.31  ? 363 ILE   B CD1 1 
ATOM   3091 N N   . ASN   B 1 158 ? 57.363 49.001 19.174  1.00 34.26  ? 364 ASN   B N   1 
ATOM   3092 C CA  . ASN   B 1 158 ? 58.183 49.218 20.358  1.00 30.29  ? 364 ASN   B CA  1 
ATOM   3093 C C   . ASN   B 1 158 ? 57.329 49.676 21.540  1.00 30.52  ? 364 ASN   B C   1 
ATOM   3094 O O   . ASN   B 1 158 ? 57.507 49.205 22.673  1.00 30.39  ? 364 ASN   B O   1 
ATOM   3095 C CB  . ASN   B 1 158 ? 59.277 50.232 19.998  1.00 33.45  ? 364 ASN   B CB  1 
ATOM   3096 C CG  . ASN   B 1 158 ? 60.027 50.740 21.208  1.00 45.46  ? 364 ASN   B CG  1 
ATOM   3097 O OD1 . ASN   B 1 158 ? 59.755 51.837 21.718  1.00 50.64  ? 364 ASN   B OD1 1 
ATOM   3098 N ND2 . ASN   B 1 158 ? 60.955 49.917 21.711  1.00 47.86  ? 364 ASN   B ND2 1 
ATOM   3099 N N   . PHE   B 1 159 ? 56.355 50.547 21.282  1.00 26.15  ? 365 PHE   B N   1 
ATOM   3100 C CA  . PHE   B 1 159 ? 55.473 51.016 22.348  1.00 31.75  ? 365 PHE   B CA  1 
ATOM   3101 C C   . PHE   B 1 159 ? 54.693 49.870 22.970  1.00 29.67  ? 365 PHE   B C   1 
ATOM   3102 O O   . PHE   B 1 159 ? 54.551 49.796 24.200  1.00 28.18  ? 365 PHE   B O   1 
ATOM   3103 C CB  . PHE   B 1 159 ? 54.526 52.081 21.786  1.00 30.57  ? 365 PHE   B CB  1 
ATOM   3104 C CG  . PHE   B 1 159 ? 53.547 52.614 22.779  1.00 34.89  ? 365 PHE   B CG  1 
ATOM   3105 C CD1 . PHE   B 1 159 ? 53.968 53.430 23.820  1.00 33.67  ? 365 PHE   B CD1 1 
ATOM   3106 C CD2 . PHE   B 1 159 ? 52.201 52.303 22.677  1.00 36.24  ? 365 PHE   B CD2 1 
ATOM   3107 C CE1 . PHE   B 1 159 ? 53.059 53.933 24.740  1.00 35.00  ? 365 PHE   B CE1 1 
ATOM   3108 C CE2 . PHE   B 1 159 ? 51.282 52.804 23.588  1.00 33.66  ? 365 PHE   B CE2 1 
ATOM   3109 C CZ  . PHE   B 1 159 ? 51.716 53.617 24.633  1.00 28.36  ? 365 PHE   B CZ  1 
ATOM   3110 N N   . ILE   B 1 160 ? 54.161 48.971 22.131  1.00 29.46  ? 366 ILE   B N   1 
ATOM   3111 C CA  . ILE   B 1 160 ? 53.430 47.805 22.622  1.00 24.71  ? 366 ILE   B CA  1 
ATOM   3112 C C   . ILE   B 1 160 ? 54.332 46.918 23.481  1.00 31.56  ? 366 ILE   B C   1 
ATOM   3113 O O   . ILE   B 1 160 ? 53.903 46.382 24.514  1.00 30.59  ? 366 ILE   B O   1 
ATOM   3114 C CB  . ILE   B 1 160 ? 52.840 47.008 21.437  1.00 26.57  ? 366 ILE   B CB  1 
ATOM   3115 C CG1 . ILE   B 1 160 ? 51.700 47.778 20.738  1.00 24.91  ? 366 ILE   B CG1 1 
ATOM   3116 C CG2 . ILE   B 1 160 ? 52.383 45.628 21.902  1.00 26.38  ? 366 ILE   B CG2 1 
ATOM   3117 C CD1 . ILE   B 1 160 ? 51.244 47.135 19.416  1.00 23.89  ? 366 ILE   B CD1 1 
ATOM   3118 N N   . HIS   B 1 161 ? 55.579 46.705 23.050  1.00 27.27  ? 367 HIS   B N   1 
ATOM   3119 C CA  . HIS   B 1 161 ? 56.505 45.919 23.870  1.00 31.89  ? 367 HIS   B CA  1 
ATOM   3120 C C   . HIS   B 1 161 ? 56.771 46.605 25.205  1.00 31.44  ? 367 HIS   B C   1 
ATOM   3121 O O   . HIS   B 1 161 ? 56.772 45.951 26.246  1.00 33.17  ? 367 HIS   B O   1 
ATOM   3122 C CB  . HIS   B 1 161 ? 57.844 45.690 23.150  1.00 32.21  ? 367 HIS   B CB  1 
ATOM   3123 C CG  . HIS   B 1 161 ? 57.759 44.739 21.994  1.00 49.27  ? 367 HIS   B CG  1 
ATOM   3124 N ND1 . HIS   B 1 161 ? 58.770 44.606 21.065  1.00 55.67  ? 367 HIS   B ND1 1 
ATOM   3125 C CD2 . HIS   B 1 161 ? 56.748 43.947 21.563  1.00 50.54  ? 367 HIS   B CD2 1 
ATOM   3126 C CE1 . HIS   B 1 161 ? 58.411 43.724 20.150  1.00 48.99  ? 367 HIS   B CE1 1 
ATOM   3127 N NE2 . HIS   B 1 161 ? 57.184 43.317 20.424  1.00 52.21  ? 367 HIS   B NE2 1 
ATOM   3128 N N   . LYS   B 1 162 ? 57.010 47.924 25.186  1.00 32.98  ? 368 LYS   B N   1 
ATOM   3129 C CA  A LYS   B 1 162 ? 57.231 48.696 26.415  0.53 33.22  ? 368 LYS   B CA  1 
ATOM   3130 C CA  B LYS   B 1 162 ? 57.259 48.625 26.439  0.47 33.21  ? 368 LYS   B CA  1 
ATOM   3131 C C   . LYS   B 1 162 ? 56.040 48.569 27.346  1.00 33.32  ? 368 LYS   B C   1 
ATOM   3132 O O   . LYS   B 1 162 ? 56.175 48.373 28.561  1.00 32.18  ? 368 LYS   B O   1 
ATOM   3133 C CB  A LYS   B 1 162 ? 57.422 50.178 26.075  0.53 33.92  ? 368 LYS   B CB  1 
ATOM   3134 C CB  B LYS   B 1 162 ? 57.668 50.068 26.159  0.47 34.35  ? 368 LYS   B CB  1 
ATOM   3135 C CG  A LYS   B 1 162 ? 58.787 50.628 25.584  0.53 35.26  ? 368 LYS   B CG  1 
ATOM   3136 C CG  B LYS   B 1 162 ? 59.091 50.190 25.637  0.47 33.84  ? 368 LYS   B CG  1 
ATOM   3137 C CD  A LYS   B 1 162 ? 58.666 52.089 25.125  0.53 38.55  ? 368 LYS   B CD  1 
ATOM   3138 C CD  B LYS   B 1 162 ? 59.359 51.595 25.162  0.47 42.82  ? 368 LYS   B CD  1 
ATOM   3139 C CE  A LYS   B 1 162 ? 60.010 52.794 25.013  0.53 45.50  ? 368 LYS   B CE  1 
ATOM   3140 C CE  B LYS   B 1 162 ? 60.804 51.776 24.730  0.47 44.29  ? 368 LYS   B CE  1 
ATOM   3141 N NZ  A LYS   B 1 162 ? 60.916 52.070 24.080  0.53 43.94  ? 368 LYS   B NZ  1 
ATOM   3142 N NZ  B LYS   B 1 162 ? 60.948 53.018 23.918  0.47 45.31  ? 368 LYS   B NZ  1 
ATOM   3143 N N   . LEU   B 1 163 ? 54.849 48.710 26.778  1.00 30.15  ? 369 LEU   B N   1 
ATOM   3144 C CA  . LEU   B 1 163 ? 53.640 48.674 27.572  1.00 28.16  ? 369 LEU   B CA  1 
ATOM   3145 C C   . LEU   B 1 163 ? 53.471 47.318 28.247  1.00 32.05  ? 369 LEU   B C   1 
ATOM   3146 O O   . LEU   B 1 163 ? 53.134 47.243 29.435  1.00 32.30  ? 369 LEU   B O   1 
ATOM   3147 C CB  . LEU   B 1 163 ? 52.471 49.032 26.645  1.00 28.41  ? 369 LEU   B CB  1 
ATOM   3148 C CG  . LEU   B 1 163 ? 51.160 49.561 27.156  1.00 37.57  ? 369 LEU   B CG  1 
ATOM   3149 C CD1 . LEU   B 1 163 ? 51.415 50.867 27.910  1.00 31.24  ? 369 LEU   B CD1 1 
ATOM   3150 C CD2 . LEU   B 1 163 ? 50.246 49.801 25.936  1.00 35.36  ? 369 LEU   B CD2 1 
ATOM   3151 N N   . LYS   B 1 164 ? 53.743 46.231 27.520  1.00 32.00  ? 370 LYS   B N   1 
ATOM   3152 C CA  . LYS   B 1 164 ? 53.568 44.887 28.068  1.00 34.06  ? 370 LYS   B CA  1 
ATOM   3153 C C   . LYS   B 1 164 ? 54.622 44.536 29.115  1.00 34.42  ? 370 LYS   B C   1 
ATOM   3154 O O   . LYS   B 1 164 ? 54.370 43.670 29.955  1.00 40.63  ? 370 LYS   B O   1 
ATOM   3155 C CB  . LYS   B 1 164 ? 53.592 43.856 26.933  1.00 33.29  ? 370 LYS   B CB  1 
ATOM   3156 C CG  . LYS   B 1 164 ? 52.269 43.767 26.156  1.00 36.86  ? 370 LYS   B CG  1 
ATOM   3157 C CD  . LYS   B 1 164 ? 52.227 42.562 25.198  1.00 46.28  ? 370 LYS   B CD  1 
ATOM   3158 C CE  . LYS   B 1 164 ? 52.282 41.215 25.904  1.00 42.00  ? 370 LYS   B CE  1 
ATOM   3159 N NZ  . LYS   B 1 164 ? 51.830 41.284 27.311  1.00 55.59  ? 370 LYS   B NZ  1 
ATOM   3160 N N   . HIS   B 1 165 ? 55.790 45.178 29.088  1.00 34.82  ? 371 HIS   B N   1 
ATOM   3161 C CA  A HIS   B 1 165 ? 56.813 44.906 30.087  0.53 38.75  ? 371 HIS   B CA  1 
ATOM   3162 C CA  B HIS   B 1 165 ? 56.831 44.927 30.082  0.47 38.75  ? 371 HIS   B CA  1 
ATOM   3163 C C   . HIS   B 1 165 ? 56.604 45.674 31.391  1.00 36.51  ? 371 HIS   B C   1 
ATOM   3164 O O   . HIS   B 1 165 ? 57.397 45.512 32.317  1.00 42.88  ? 371 HIS   B O   1 
ATOM   3165 C CB  A HIS   B 1 165 ? 58.192 45.205 29.500  0.53 39.70  ? 371 HIS   B CB  1 
ATOM   3166 C CB  B HIS   B 1 165 ? 58.219 45.295 29.535  0.47 39.68  ? 371 HIS   B CB  1 
ATOM   3167 C CG  A HIS   B 1 165 ? 58.674 44.142 28.563  0.53 42.57  ? 371 HIS   B CG  1 
ATOM   3168 C CG  B HIS   B 1 165 ? 59.350 44.739 30.352  0.47 43.64  ? 371 HIS   B CG  1 
ATOM   3169 N ND1 A HIS   B 1 165 ? 59.140 44.417 27.297  0.53 38.76  ? 371 HIS   B ND1 1 
ATOM   3170 N ND1 B HIS   B 1 165 ? 60.027 45.486 31.294  0.47 47.65  ? 371 HIS   B ND1 1 
ATOM   3171 C CD2 A HIS   B 1 165 ? 58.723 42.795 28.699  0.53 40.56  ? 371 HIS   B CD2 1 
ATOM   3172 C CD2 B HIS   B 1 165 ? 59.896 43.500 30.395  0.47 42.81  ? 371 HIS   B CD2 1 
ATOM   3173 C CE1 A HIS   B 1 165 ? 59.477 43.288 26.700  0.53 44.34  ? 371 HIS   B CE1 1 
ATOM   3174 C CE1 B HIS   B 1 165 ? 60.955 44.737 31.864  0.47 43.02  ? 371 HIS   B CE1 1 
ATOM   3175 N NE2 A HIS   B 1 165 ? 59.232 42.289 27.530  0.53 46.76  ? 371 HIS   B NE2 1 
ATOM   3176 N NE2 B HIS   B 1 165 ? 60.894 43.527 31.339  0.47 40.91  ? 371 HIS   B NE2 1 
ATOM   3177 N N   . LEU   B 1 166 ? 55.550 46.478 31.496  1.00 37.51  ? 372 LEU   B N   1 
ATOM   3178 C CA  . LEU   B 1 166 ? 55.265 47.168 32.748  1.00 34.81  ? 372 LEU   B CA  1 
ATOM   3179 C C   . LEU   B 1 166 ? 54.781 46.166 33.796  1.00 39.57  ? 372 LEU   B C   1 
ATOM   3180 O O   . LEU   B 1 166 ? 54.044 45.229 33.469  1.00 43.45  ? 372 LEU   B O   1 
ATOM   3181 C CB  . LEU   B 1 166 ? 54.197 48.239 32.538  1.00 31.28  ? 372 LEU   B CB  1 
ATOM   3182 C CG  . LEU   B 1 166 ? 54.583 49.431 31.677  1.00 33.35  ? 372 LEU   B CG  1 
ATOM   3183 C CD1 . LEU   B 1 166 ? 53.430 50.425 31.564  1.00 30.33  ? 372 LEU   B CD1 1 
ATOM   3184 C CD2 . LEU   B 1 166 ? 55.790 50.101 32.258  1.00 33.95  ? 372 LEU   B CD2 1 
ATOM   3185 N N   . PRO   B 1 167 ? 55.139 46.356 35.072  1.00 43.36  ? 373 PRO   B N   1 
ATOM   3186 C CA  . PRO   B 1 167 ? 54.771 45.360 36.087  1.00 41.54  ? 373 PRO   B CA  1 
ATOM   3187 C C   . PRO   B 1 167 ? 53.337 45.411 36.570  1.00 50.41  ? 373 PRO   B C   1 
ATOM   3188 O O   . PRO   B 1 167 ? 52.878 44.408 37.133  1.00 51.93  ? 373 PRO   B O   1 
ATOM   3189 C CB  . PRO   B 1 167 ? 55.742 45.659 37.233  1.00 44.49  ? 373 PRO   B CB  1 
ATOM   3190 C CG  . PRO   B 1 167 ? 56.045 47.080 37.095  1.00 40.74  ? 373 PRO   B CG  1 
ATOM   3191 C CD  . PRO   B 1 167 ? 56.017 47.402 35.623  1.00 39.18  ? 373 PRO   B CD  1 
ATOM   3192 N N   . GLU   B 1 168 ? 52.613 46.518 36.393  1.00 41.19  ? 374 GLU   B N   1 
ATOM   3193 C CA  . GLU   B 1 168 ? 51.266 46.654 36.934  1.00 37.78  ? 374 GLU   B CA  1 
ATOM   3194 C C   . GLU   B 1 168 ? 50.308 47.159 35.877  1.00 34.87  ? 374 GLU   B C   1 
ATOM   3195 O O   . GLU   B 1 168 ? 50.676 47.955 35.017  1.00 37.18  ? 374 GLU   B O   1 
ATOM   3196 C CB  . GLU   B 1 168 ? 51.210 47.618 38.132  1.00 40.50  ? 374 GLU   B CB  1 
ATOM   3197 C CG  . GLU   B 1 168 ? 52.195 47.311 39.238  1.00 47.37  ? 374 GLU   B CG  1 
ATOM   3198 C CD  . GLU   B 1 168 ? 51.831 46.051 39.993  1.00 49.72  ? 374 GLU   B CD  1 
ATOM   3199 O OE1 . GLU   B 1 168 ? 52.721 45.487 40.664  1.00 68.71  ? 374 GLU   B OE1 1 
ATOM   3200 O OE2 . GLU   B 1 168 ? 50.653 45.628 39.922  1.00 63.33  ? 374 GLU   B OE2 1 
ATOM   3201 N N   . LYS   B 1 169 ? 49.057 46.714 35.981  1.00 33.98  ? 375 LYS   B N   1 
ATOM   3202 C CA  . LYS   B 1 169 ? 48.055 47.163 35.030  1.00 39.87  ? 375 LYS   B CA  1 
ATOM   3203 C C   . LYS   B 1 169 ? 47.827 48.659 35.146  1.00 35.97  ? 375 LYS   B C   1 
ATOM   3204 O O   . LYS   B 1 169 ? 47.632 49.342 34.131  1.00 32.89  ? 375 LYS   B O   1 
ATOM   3205 C CB  . LYS   B 1 169 ? 46.730 46.423 35.223  1.00 40.55  ? 375 LYS   B CB  1 
ATOM   3206 C CG  . LYS   B 1 169 ? 45.760 46.720 34.065  1.00 43.78  ? 375 LYS   B CG  1 
ATOM   3207 C CD  . LYS   B 1 169 ? 44.285 46.794 34.482  1.00 52.28  ? 375 LYS   B CD  1 
ATOM   3208 C CE  . LYS   B 1 169 ? 43.553 45.475 34.419  1.00 64.05  ? 375 LYS   B CE  1 
ATOM   3209 N NZ  . LYS   B 1 169 ? 42.072 45.726 34.531  1.00 59.37  ? 375 LYS   B NZ  1 
ATOM   3210 N N   . TYR   B 1 170 ? 47.833 49.198 36.371  1.00 35.23  ? 376 TYR   B N   1 
ATOM   3211 C CA  A TYR   B 1 170 ? 47.557 50.624 36.514  0.50 35.47  ? 376 TYR   B CA  1 
ATOM   3212 C CA  B TYR   B 1 170 ? 47.557 50.624 36.513  0.50 35.47  ? 376 TYR   B CA  1 
ATOM   3213 C C   . TYR   B 1 170 ? 48.633 51.454 35.838  1.00 29.58  ? 376 TYR   B C   1 
ATOM   3214 O O   . TYR   B 1 170 ? 48.352 52.550 35.350  1.00 32.03  ? 376 TYR   B O   1 
ATOM   3215 C CB  A TYR   B 1 170 ? 47.392 51.005 37.994  0.50 33.73  ? 376 TYR   B CB  1 
ATOM   3216 C CB  B TYR   B 1 170 ? 47.392 51.005 37.993  0.50 33.73  ? 376 TYR   B CB  1 
ATOM   3217 C CG  A TYR   B 1 170 ? 48.675 51.157 38.796  0.50 37.20  ? 376 TYR   B CG  1 
ATOM   3218 C CG  B TYR   B 1 170 ? 48.674 51.156 38.796  0.50 37.20  ? 376 TYR   B CG  1 
ATOM   3219 C CD1 A TYR   B 1 170 ? 49.390 52.349 38.791  0.50 36.00  ? 376 TYR   B CD1 1 
ATOM   3220 C CD1 B TYR   B 1 170 ? 49.389 52.349 38.793  0.50 36.00  ? 376 TYR   B CD1 1 
ATOM   3221 C CD2 A TYR   B 1 170 ? 49.131 50.126 39.615  0.50 38.37  ? 376 TYR   B CD2 1 
ATOM   3222 C CD2 B TYR   B 1 170 ? 49.131 50.125 39.614  0.50 38.37  ? 376 TYR   B CD2 1 
ATOM   3223 C CE1 A TYR   B 1 170 ? 50.552 52.494 39.543  0.50 36.42  ? 376 TYR   B CE1 1 
ATOM   3224 C CE1 B TYR   B 1 170 ? 50.551 52.493 39.545  0.50 36.42  ? 376 TYR   B CE1 1 
ATOM   3225 C CE2 A TYR   B 1 170 ? 50.290 50.263 40.371  0.50 37.89  ? 376 TYR   B CE2 1 
ATOM   3226 C CE2 B TYR   B 1 170 ? 50.290 50.261 40.370  0.50 37.89  ? 376 TYR   B CE2 1 
ATOM   3227 C CZ  A TYR   B 1 170 ? 50.993 51.448 40.333  0.50 36.62  ? 376 TYR   B CZ  1 
ATOM   3228 C CZ  B TYR   B 1 170 ? 50.992 51.447 40.334  0.50 36.62  ? 376 TYR   B CZ  1 
ATOM   3229 O OH  A TYR   B 1 170 ? 52.142 51.596 41.077  0.50 36.37  ? 376 TYR   B OH  1 
ATOM   3230 O OH  B TYR   B 1 170 ? 52.141 51.594 41.078  0.50 36.37  ? 376 TYR   B OH  1 
ATOM   3231 N N   . MET   B 1 171 ? 49.862 50.936 35.774  1.00 32.55  ? 377 MET   B N   1 
ATOM   3232 C CA  . MET   B 1 171 ? 50.912 51.660 35.079  1.00 32.53  ? 377 MET   B CA  1 
ATOM   3233 C C   . MET   B 1 171 ? 50.666 51.656 33.579  1.00 27.19  ? 377 MET   B C   1 
ATOM   3234 O O   . MET   B 1 171 ? 50.945 52.655 32.911  1.00 30.21  ? 377 MET   B O   1 
ATOM   3235 C CB  . MET   B 1 171 ? 52.267 51.046 35.412  1.00 26.42  ? 377 MET   B CB  1 
ATOM   3236 C CG  . MET   B 1 171 ? 52.686 51.222 36.888  1.00 33.80  ? 377 MET   B CG  1 
ATOM   3237 S SD  . MET   B 1 171 ? 54.262 50.391 37.185  1.00 42.87  ? 377 MET   B SD  1 
ATOM   3238 C CE  . MET   B 1 171 ? 55.427 51.606 36.655  1.00 34.53  ? 377 MET   B CE  1 
ATOM   3239 N N   . MET   B 1 172 ? 50.129 50.551 33.049  1.00 27.14  ? 378 MET   B N   1 
ATOM   3240 C CA  . MET   B 1 172 ? 49.725 50.520 31.644  1.00 30.87  ? 378 MET   B CA  1 
ATOM   3241 C C   . MET   B 1 172 ? 48.618 51.529 31.365  1.00 26.87  ? 378 MET   B C   1 
ATOM   3242 O O   . MET   B 1 172 ? 48.667 52.254 30.368  1.00 26.97  ? 378 MET   B O   1 
ATOM   3243 C CB  . MET   B 1 172 ? 49.285 49.117 31.227  1.00 29.56  ? 378 MET   B CB  1 
ATOM   3244 C CG  . MET   B 1 172 ? 50.393 48.057 31.217  1.00 31.82  ? 378 MET   B CG  1 
ATOM   3245 S SD  . MET   B 1 172 ? 49.735 46.365 31.192  1.00 38.22  ? 378 MET   B SD  1 
ATOM   3246 C CE  . MET   B 1 172 ? 51.193 45.410 31.663  1.00 35.88  ? 378 MET   B CE  1 
ATOM   3247 N N   . ASN   B 1 173 ? 47.608 51.585 32.238  1.00 23.98  ? 379 ASN   B N   1 
ATOM   3248 C CA  . ASN   B 1 173 ? 46.564 52.598 32.092  1.00 27.66  ? 379 ASN   B CA  1 
ATOM   3249 C C   . ASN   B 1 173 ? 47.120 54.015 32.169  1.00 28.82  ? 379 ASN   B C   1 
ATOM   3250 O O   . ASN   B 1 173 ? 46.700 54.888 31.395  1.00 29.24  ? 379 ASN   B O   1 
ATOM   3251 C CB  . ASN   B 1 173 ? 45.469 52.370 33.128  1.00 26.46  ? 379 ASN   B CB  1 
ATOM   3252 C CG  . ASN   B 1 173 ? 44.431 51.382 32.644  1.00 34.21  ? 379 ASN   B CG  1 
ATOM   3253 O OD1 . ASN   B 1 173 ? 44.207 51.273 31.444  1.00 33.92  ? 379 ASN   B OD1 1 
ATOM   3254 N ND2 . ASN   B 1 173 ? 43.822 50.636 33.555  1.00 33.71  ? 379 ASN   B ND2 1 
ATOM   3255 N N   . SER   B 1 174 ? 48.072 54.266 33.086  1.00 25.03  ? 380 SER   B N   1 
ATOM   3256 C CA  . SER   B 1 174 ? 48.736 55.570 33.152  1.00 25.75  ? 380 SER   B CA  1 
ATOM   3257 C C   . SER   B 1 174 ? 49.360 55.949 31.816  1.00 26.95  ? 380 SER   B C   1 
ATOM   3258 O O   . SER   B 1 174 ? 49.151 57.058 31.300  1.00 27.18  ? 380 SER   B O   1 
ATOM   3259 C CB  . SER   B 1 174 ? 49.822 55.553 34.243  1.00 26.77  ? 380 SER   B CB  1 
ATOM   3260 O OG  . SER   B 1 174 ? 49.218 55.591 35.534  1.00 30.91  ? 380 SER   B OG  1 
ATOM   3261 N N   . VAL   B 1 175 ? 50.173 55.053 31.263  1.00 21.94  ? 381 VAL   B N   1 
ATOM   3262 C CA  . VAL   B 1 175 ? 50.859 55.342 30.020  1.00 22.21  ? 381 VAL   B CA  1 
ATOM   3263 C C   . VAL   B 1 175 ? 49.854 55.524 28.884  1.00 26.57  ? 381 VAL   B C   1 
ATOM   3264 O O   . VAL   B 1 175 ? 49.965 56.462 28.095  1.00 25.96  ? 381 VAL   B O   1 
ATOM   3265 C CB  . VAL   B 1 175 ? 51.882 54.232 29.723  1.00 26.94  ? 381 VAL   B CB  1 
ATOM   3266 C CG1 . VAL   B 1 175 ? 52.424 54.373 28.312  1.00 27.92  ? 381 VAL   B CG1 1 
ATOM   3267 C CG2 . VAL   B 1 175 ? 53.026 54.313 30.756  1.00 31.49  ? 381 VAL   B CG2 1 
ATOM   3268 N N   . LEU   B 1 176 ? 48.834 54.663 28.810  1.00 26.28  ? 382 LEU   B N   1 
ATOM   3269 C CA  . LEU   B 1 176 ? 47.860 54.800 27.721  1.00 28.60  ? 382 LEU   B CA  1 
ATOM   3270 C C   . LEU   B 1 176 ? 47.049 56.081 27.839  1.00 30.18  ? 382 LEU   B C   1 
ATOM   3271 O O   . LEU   B 1 176 ? 46.573 56.598 26.824  1.00 27.58  ? 382 LEU   B O   1 
ATOM   3272 C CB  . LEU   B 1 176 ? 46.928 53.589 27.683  1.00 26.56  ? 382 LEU   B CB  1 
ATOM   3273 C CG  . LEU   B 1 176 ? 47.506 52.310 27.068  1.00 23.94  ? 382 LEU   B CG  1 
ATOM   3274 C CD1 . LEU   B 1 176 ? 46.477 51.171 27.144  1.00 27.75  ? 382 LEU   B CD1 1 
ATOM   3275 C CD2 . LEU   B 1 176 ? 47.891 52.577 25.616  1.00 26.58  ? 382 LEU   B CD2 1 
ATOM   3276 N N   . GLU   B 1 177 ? 46.923 56.630 29.050  1.00 27.26  ? 383 GLU   B N   1 
ATOM   3277 C CA  . GLU   B 1 177 ? 46.147 57.852 29.241  1.00 31.24  ? 383 GLU   B CA  1 
ATOM   3278 C C   . GLU   B 1 177 ? 46.764 59.038 28.513  1.00 32.11  ? 383 GLU   B C   1 
ATOM   3279 O O   . GLU   B 1 177 ? 46.042 59.948 28.099  1.00 30.63  ? 383 GLU   B O   1 
ATOM   3280 C CB  . GLU   B 1 177 ? 45.983 58.111 30.747  1.00 29.28  ? 383 GLU   B CB  1 
ATOM   3281 C CG  . GLU   B 1 177 ? 45.123 59.278 31.133  1.00 40.26  ? 383 GLU   B CG  1 
ATOM   3282 C CD  . GLU   B 1 177 ? 45.072 59.451 32.655  1.00 50.29  ? 383 GLU   B CD  1 
ATOM   3283 O OE1 . GLU   B 1 177 ? 46.029 60.012 33.219  1.00 50.38  ? 383 GLU   B OE1 1 
ATOM   3284 O OE2 . GLU   B 1 177 ? 44.082 59.019 33.284  1.00 57.56  ? 383 GLU   B OE2 1 
ATOM   3285 N N   . ASN   B 1 178 ? 48.059 59.025 28.283  1.00 25.25  ? 384 ASN   B N   1 
ATOM   3286 C CA  . ASN   B 1 178 ? 48.730 60.106 27.572  1.00 29.01  ? 384 ASN   B CA  1 
ATOM   3287 C C   . ASN   B 1 178 ? 49.061 59.758 26.109  1.00 30.22  ? 384 ASN   B C   1 
ATOM   3288 O O   . ASN   B 1 178 ? 49.738 60.501 25.438  1.00 29.95  ? 384 ASN   B O   1 
ATOM   3289 C CB  . ASN   B 1 178 ? 49.966 60.524 28.344  1.00 26.40  ? 384 ASN   B CB  1 
ATOM   3290 C CG  . ASN   B 1 178 ? 49.665 60.828 29.789  1.00 29.38  ? 384 ASN   B CG  1 
ATOM   3291 O OD1 . ASN   B 1 178 ? 50.122 60.131 30.675  1.00 33.59  ? 384 ASN   B OD1 1 
ATOM   3292 N ND2 . ASN   B 1 178 ? 48.889 61.866 30.026  1.00 30.34  ? 384 ASN   B ND2 1 
ATOM   3293 N N   . PHE   B 1 179 ? 48.586 58.626 25.652  1.00 25.54  ? 385 PHE   B N   1 
ATOM   3294 C CA  . PHE   B 1 179 ? 48.761 58.163 24.280  1.00 25.53  ? 385 PHE   B CA  1 
ATOM   3295 C C   . PHE   B 1 179 ? 47.448 58.356 23.526  1.00 25.43  ? 385 PHE   B C   1 
ATOM   3296 O O   . PHE   B 1 179 ? 46.401 57.849 23.956  1.00 29.38  ? 385 PHE   B O   1 
ATOM   3297 C CB  . PHE   B 1 179 ? 49.165 56.689 24.303  1.00 24.25  ? 385 PHE   B CB  1 
ATOM   3298 C CG  . PHE   B 1 179 ? 49.229 56.053 22.947  1.00 29.54  ? 385 PHE   B CG  1 
ATOM   3299 C CD1 . PHE   B 1 179 ? 50.352 56.199 22.158  1.00 30.68  ? 385 PHE   B CD1 1 
ATOM   3300 C CD2 . PHE   B 1 179 ? 48.161 55.313 22.466  1.00 29.51  ? 385 PHE   B CD2 1 
ATOM   3301 C CE1 . PHE   B 1 179 ? 50.413 55.620 20.912  1.00 29.49  ? 385 PHE   B CE1 1 
ATOM   3302 C CE2 . PHE   B 1 179 ? 48.206 54.747 21.209  1.00 28.03  ? 385 PHE   B CE2 1 
ATOM   3303 C CZ  . PHE   B 1 179 ? 49.330 54.904 20.431  1.00 30.55  ? 385 PHE   B CZ  1 
ATOM   3304 N N   . THR   B 1 180 ? 47.489 59.082 22.410  1.00 22.74  ? 386 THR   B N   1 
ATOM   3305 C CA  . THR   B 1 180 ? 46.282 59.280 21.621  1.00 21.99  ? 386 THR   B CA  1 
ATOM   3306 C C   . THR   B 1 180 ? 46.608 59.174 20.133  1.00 24.42  ? 386 THR   B C   1 
ATOM   3307 O O   . THR   B 1 180 ? 47.757 59.323 19.705  1.00 26.67  ? 386 THR   B O   1 
ATOM   3308 C CB  . THR   B 1 180 ? 45.608 60.643 21.887  1.00 23.21  ? 386 THR   B CB  1 
ATOM   3309 O OG1 . THR   B 1 180 ? 46.529 61.685 21.551  1.00 26.49  ? 386 THR   B OG1 1 
ATOM   3310 C CG2 . THR   B 1 180 ? 45.111 60.791 23.335  1.00 26.40  ? 386 THR   B CG2 1 
ATOM   3311 N N   . ILE   B 1 181 ? 45.575 58.925 19.333  1.00 23.24  ? 387 ILE   B N   1 
ATOM   3312 C CA  . ILE   B 1 181 ? 45.734 58.848 17.883  1.00 19.09  ? 387 ILE   B CA  1 
ATOM   3313 C C   . ILE   B 1 181 ? 44.669 59.722 17.251  1.00 22.28  ? 387 ILE   B C   1 
ATOM   3314 O O   . ILE   B 1 181 ? 43.499 59.645 17.625  1.00 24.69  ? 387 ILE   B O   1 
ATOM   3315 C CB  . ILE   B 1 181 ? 45.632 57.404 17.356  1.00 19.65  ? 387 ILE   B CB  1 
ATOM   3316 C CG1 . ILE   B 1 181 ? 46.793 56.585 17.905  1.00 22.18  ? 387 ILE   B CG1 1 
ATOM   3317 C CG2 . ILE   B 1 181 ? 45.619 57.417 15.798  1.00 20.74  ? 387 ILE   B CG2 1 
ATOM   3318 C CD1 . ILE   B 1 181 ? 46.845 55.112 17.495  1.00 24.20  ? 387 ILE   B CD1 1 
ATOM   3319 N N   . LEU   B 1 182 ? 45.067 60.563 16.310  1.00 24.37  ? 388 LEU   B N   1 
ATOM   3320 C CA  . LEU   B 1 182 ? 44.118 61.388 15.588  1.00 25.70  ? 388 LEU   B CA  1 
ATOM   3321 C C   . LEU   B 1 182 ? 44.057 60.877 14.155  1.00 25.86  ? 388 LEU   B C   1 
ATOM   3322 O O   . LEU   B 1 182 ? 45.068 60.892 13.444  1.00 29.34  ? 388 LEU   B O   1 
ATOM   3323 C CB  . LEU   B 1 182 ? 44.514 62.860 15.631  1.00 26.07  ? 388 LEU   B CB  1 
ATOM   3324 C CG  . LEU   B 1 182 ? 43.481 63.785 14.989  1.00 29.19  ? 388 LEU   B CG  1 
ATOM   3325 C CD1 . LEU   B 1 182 ? 42.162 63.781 15.792  1.00 28.23  ? 388 LEU   B CD1 1 
ATOM   3326 C CD2 . LEU   B 1 182 ? 44.042 65.196 14.830  1.00 30.15  ? 388 LEU   B CD2 1 
ATOM   3327 N N   A LEU   B 1 183 ? 42.876 60.432 13.741  0.54 26.80  ? 389 LEU   B N   1 
ATOM   3328 N N   B LEU   B 1 183 ? 42.889 60.378 13.757  0.46 27.18  ? 389 LEU   B N   1 
ATOM   3329 C CA  A LEU   B 1 183 ? 42.621 59.927 12.399  0.54 28.81  ? 389 LEU   B CA  1 
ATOM   3330 C CA  B LEU   B 1 183 ? 42.632 59.936 12.394  0.46 28.19  ? 389 LEU   B CA  1 
ATOM   3331 C C   A LEU   B 1 183 ? 41.778 60.946 11.644  0.54 29.36  ? 389 LEU   B C   1 
ATOM   3332 C C   B LEU   B 1 183 ? 41.823 61.009 11.681  0.46 28.89  ? 389 LEU   B C   1 
ATOM   3333 O O   A LEU   B 1 183 ? 40.701 61.323 12.110  0.54 30.62  ? 389 LEU   B O   1 
ATOM   3334 O O   B LEU   B 1 183 ? 40.817 61.487 12.211  0.46 30.39  ? 389 LEU   B O   1 
ATOM   3335 C CB  A LEU   B 1 183 ? 41.916 58.574 12.472  0.54 30.42  ? 389 LEU   B CB  1 
ATOM   3336 C CB  B LEU   B 1 183 ? 41.867 58.611 12.375  0.46 30.43  ? 389 LEU   B CB  1 
ATOM   3337 C CG  A LEU   B 1 183 ? 41.376 57.965 11.185  0.54 32.62  ? 389 LEU   B CG  1 
ATOM   3338 C CG  B LEU   B 1 183 ? 42.449 57.399 13.106  0.46 33.33  ? 389 LEU   B CG  1 
ATOM   3339 C CD1 A LEU   B 1 183 ? 42.463 57.920 10.147  0.54 31.29  ? 389 LEU   B CD1 1 
ATOM   3340 C CD1 B LEU   B 1 183 ? 41.345 56.430 13.468  0.46 31.88  ? 389 LEU   B CD1 1 
ATOM   3341 C CD2 A LEU   B 1 183 ? 40.859 56.563 11.463  0.54 32.81  ? 389 LEU   B CD2 1 
ATOM   3342 C CD2 B LEU   B 1 183 ? 43.528 56.695 12.302  0.46 33.92  ? 389 LEU   B CD2 1 
ATOM   3343 N N   . VAL   B 1 184 ? 42.268 61.401 10.492  1.00 26.74  ? 390 VAL   B N   1 
ATOM   3344 C CA  . VAL   B 1 184 ? 41.554 62.379 9.679   1.00 29.88  ? 390 VAL   B CA  1 
ATOM   3345 C C   . VAL   B 1 184 ? 41.487 61.853 8.255   1.00 30.47  ? 390 VAL   B C   1 
ATOM   3346 O O   . VAL   B 1 184 ? 42.524 61.541 7.650   1.00 26.83  ? 390 VAL   B O   1 
ATOM   3347 C CB  . VAL   B 1 184 ? 42.205 63.773 9.709   1.00 27.36  ? 390 VAL   B CB  1 
ATOM   3348 C CG1 . VAL   B 1 184 ? 41.399 64.725 8.861   1.00 29.87  ? 390 VAL   B CG1 1 
ATOM   3349 C CG2 . VAL   B 1 184 ? 42.299 64.301 11.154  1.00 28.05  ? 390 VAL   B CG2 1 
ATOM   3350 N N   . VAL   B 1 185 ? 40.274 61.716 7.732   1.00 28.33  ? 391 VAL   B N   1 
ATOM   3351 C CA  . VAL   B 1 185 ? 40.065 61.299 6.354   1.00 27.07  ? 391 VAL   B CA  1 
ATOM   3352 C C   . VAL   B 1 185 ? 39.520 62.491 5.596   1.00 30.89  ? 391 VAL   B C   1 
ATOM   3353 O O   . VAL   B 1 185 ? 38.513 63.093 6.001   1.00 28.40  ? 391 VAL   B O   1 
ATOM   3354 C CB  . VAL   B 1 185 ? 39.115 60.099 6.239   1.00 31.26  ? 391 VAL   B CB  1 
ATOM   3355 C CG1 . VAL   B 1 185 ? 39.115 59.609 4.793   1.00 29.29  ? 391 VAL   B CG1 1 
ATOM   3356 C CG2 . VAL   B 1 185 ? 39.534 58.990 7.199   1.00 27.71  ? 391 VAL   B CG2 1 
ATOM   3357 N N   . THR   B 1 186 ? 40.180 62.824 4.497   1.00 29.58  ? 392 THR   B N   1 
ATOM   3358 C CA  A THR   B 1 186 ? 39.901 64.006 3.701   0.60 30.31  ? 392 THR   B CA  1 
ATOM   3359 C CA  B THR   B 1 186 ? 39.797 63.985 3.718   0.40 30.48  ? 392 THR   B CA  1 
ATOM   3360 C C   . THR   B 1 186 ? 39.616 63.600 2.261   1.00 31.54  ? 392 THR   B C   1 
ATOM   3361 O O   . THR   B 1 186 ? 40.237 62.668 1.751   1.00 27.16  ? 392 THR   B O   1 
ATOM   3362 C CB  A THR   B 1 186 ? 41.111 64.945 3.756   0.60 29.83  ? 392 THR   B CB  1 
ATOM   3363 C CB  B THR   B 1 186 ? 40.827 65.108 3.809   0.40 30.47  ? 392 THR   B CB  1 
ATOM   3364 O OG1 A THR   B 1 186 ? 41.420 65.224 5.127   0.60 28.63  ? 392 THR   B OG1 1 
ATOM   3365 O OG1 B THR   B 1 186 ? 42.046 64.674 3.208   0.40 32.88  ? 392 THR   B OG1 1 
ATOM   3366 C CG2 A THR   B 1 186 ? 40.850 66.237 3.018   0.60 34.21  ? 392 THR   B CG2 1 
ATOM   3367 C CG2 B THR   B 1 186 ? 41.076 65.487 5.257   0.40 30.82  ? 392 THR   B CG2 1 
ATOM   3368 N N   . ASN   B 1 187 ? 38.718 64.327 1.605   1.00 28.80  ? 393 ASN   B N   1 
ATOM   3369 C CA  . ASN   B 1 187 ? 38.503 64.160 0.171   1.00 31.02  ? 393 ASN   B CA  1 
ATOM   3370 C C   . ASN   B 1 187 ? 39.701 64.806 -0.516  1.00 35.18  ? 393 ASN   B C   1 
ATOM   3371 O O   . ASN   B 1 187 ? 39.889 66.020 -0.426  1.00 37.75  ? 393 ASN   B O   1 
ATOM   3372 C CB  . ASN   B 1 187 ? 37.186 64.823 -0.237  1.00 33.33  ? 393 ASN   B CB  1 
ATOM   3373 C CG  . ASN   B 1 187 ? 36.882 64.704 -1.741  1.00 40.09  ? 393 ASN   B CG  1 
ATOM   3374 O OD1 . ASN   B 1 187 ? 37.776 64.663 -2.578  1.00 36.34  ? 393 ASN   B OD1 1 
ATOM   3375 N ND2 . ASN   B 1 187 ? 35.602 64.650 -2.071  1.00 36.29  ? 393 ASN   B ND2 1 
ATOM   3376 N N   . ARG   B 1 188 ? 40.543 64.001 -1.161  1.00 34.28  ? 394 ARG   B N   1 
ATOM   3377 C CA  . ARG   B 1 188 ? 41.797 64.538 -1.681  1.00 38.73  ? 394 ARG   B CA  1 
ATOM   3378 C C   . ARG   B 1 188 ? 41.574 65.628 -2.726  1.00 42.10  ? 394 ARG   B C   1 
ATOM   3379 O O   . ARG   B 1 188 ? 42.382 66.552 -2.824  1.00 47.21  ? 394 ARG   B O   1 
ATOM   3380 C CB  . ARG   B 1 188 ? 42.648 63.413 -2.258  1.00 36.20  ? 394 ARG   B CB  1 
ATOM   3381 C CG  . ARG   B 1 188 ? 44.019 63.847 -2.749  1.00 43.76  ? 394 ARG   B CG  1 
ATOM   3382 C CD  . ARG   B 1 188 ? 44.637 62.733 -3.555  1.00 47.47  ? 394 ARG   B CD  1 
ATOM   3383 N NE  . ARG   B 1 188 ? 46.075 62.881 -3.726  1.00 60.27  ? 394 ARG   B NE  1 
ATOM   3384 C CZ  . ARG   B 1 188 ? 46.793 62.183 -4.597  1.00 78.55  ? 394 ARG   B CZ  1 
ATOM   3385 N NH1 . ARG   B 1 188 ? 46.244 61.246 -5.359  1.00 69.17  ? 394 ARG   B NH1 1 
ATOM   3386 N NH2 . ARG   B 1 188 ? 48.097 62.427 -4.706  1.00 83.44  ? 394 ARG   B NH2 1 
ATOM   3387 N N   . ASP   B 1 189 ? 40.480 65.561 -3.490  1.00 38.35  ? 395 ASP   B N   1 
ATOM   3388 C CA  . ASP   B 1 189 ? 40.277 66.535 -4.562  1.00 44.86  ? 395 ASP   B CA  1 
ATOM   3389 C C   . ASP   B 1 189 ? 39.723 67.868 -4.054  1.00 48.68  ? 395 ASP   B C   1 
ATOM   3390 O O   . ASP   B 1 189 ? 40.095 68.918 -4.580  1.00 47.44  ? 395 ASP   B O   1 
ATOM   3391 C CB  . ASP   B 1 189 ? 39.366 65.948 -5.643  1.00 43.71  ? 395 ASP   B CB  1 
ATOM   3392 C CG  . ASP   B 1 189 ? 39.975 64.710 -6.305  1.00 60.78  ? 395 ASP   B CG  1 
ATOM   3393 O OD1 . ASP   B 1 189 ? 41.194 64.730 -6.596  1.00 58.21  ? 395 ASP   B OD1 1 
ATOM   3394 O OD2 . ASP   B 1 189 ? 39.243 63.716 -6.528  1.00 61.70  ? 395 ASP   B OD2 1 
ATOM   3395 N N   . THR   B 1 190 ? 38.852 67.864 -3.037  1.00 44.56  ? 396 THR   B N   1 
ATOM   3396 C CA  . THR   B 1 190 ? 38.257 69.095 -2.514  1.00 41.45  ? 396 THR   B CA  1 
ATOM   3397 C C   . THR   B 1 190 ? 38.846 69.558 -1.183  1.00 45.68  ? 396 THR   B C   1 
ATOM   3398 O O   . THR   B 1 190 ? 38.500 70.649 -0.724  1.00 46.46  ? 396 THR   B O   1 
ATOM   3399 C CB  . THR   B 1 190 ? 36.751 68.921 -2.312  1.00 44.23  ? 396 THR   B CB  1 
ATOM   3400 O OG1 . THR   B 1 190 ? 36.526 68.019 -1.219  1.00 48.22  ? 396 THR   B OG1 1 
ATOM   3401 C CG2 . THR   B 1 190 ? 36.114 68.355 -3.547  1.00 43.08  ? 396 THR   B CG2 1 
ATOM   3402 N N   . GLN   B 1 191 ? 39.679 68.747 -0.537  1.00 41.39  ? 397 GLN   B N   1 
ATOM   3403 C CA  . GLN   B 1 191 ? 40.266 68.999 0.781   1.00 44.12  ? 397 GLN   B CA  1 
ATOM   3404 C C   . GLN   B 1 191 ? 39.229 69.078 1.905   1.00 38.48  ? 397 GLN   B C   1 
ATOM   3405 O O   . GLN   B 1 191 ? 39.555 69.513 3.014   1.00 42.41  ? 397 GLN   B O   1 
ATOM   3406 C CB  . GLN   B 1 191 ? 41.140 70.258 0.771   1.00 44.86  ? 397 GLN   B CB  1 
ATOM   3407 C CG  . GLN   B 1 191 ? 42.397 70.051 -0.049  1.00 44.08  ? 397 GLN   B CG  1 
ATOM   3408 C CD  . GLN   B 1 191 ? 43.312 69.026 0.580   1.00 55.99  ? 397 GLN   B CD  1 
ATOM   3409 O OE1 . GLN   B 1 191 ? 43.640 69.110 1.763   1.00 66.91  ? 397 GLN   B OE1 1 
ATOM   3410 N NE2 . GLN   B 1 191 ? 43.689 68.014 -0.199  1.00 48.42  ? 397 GLN   B NE2 1 
ATOM   3411 N N   . GLU   B 1 192 ? 37.996 68.645 1.659   1.00 35.88  ? 398 GLU   B N   1 
ATOM   3412 C CA  . GLU   B 1 192 ? 36.979 68.607 2.698   1.00 41.76  ? 398 GLU   B CA  1 
ATOM   3413 C C   . GLU   B 1 192 ? 37.249 67.477 3.686   1.00 36.51  ? 398 GLU   B C   1 
ATOM   3414 O O   . GLU   B 1 192 ? 37.606 66.357 3.301   1.00 33.08  ? 398 GLU   B O   1 
ATOM   3415 C CB  . GLU   B 1 192 ? 35.612 68.407 2.064   1.00 37.70  ? 398 GLU   B CB  1 
ATOM   3416 C CG  . GLU   B 1 192 ? 35.094 69.639 1.351   1.00 57.40  ? 398 GLU   B CG  1 
ATOM   3417 C CD  . GLU   B 1 192 ? 33.646 69.500 0.942   1.00 75.38  ? 398 GLU   B CD  1 
ATOM   3418 O OE1 . GLU   B 1 192 ? 33.029 68.464 1.283   1.00 78.50  ? 398 GLU   B OE1 1 
ATOM   3419 O OE2 . GLU   B 1 192 ? 33.130 70.418 0.267   1.00 82.40  ? 398 GLU   B OE2 1 
ATOM   3420 N N   . THR   B 1 193 ? 37.052 67.766 4.969   1.00 33.65  ? 399 THR   B N   1 
ATOM   3421 C CA  . THR   B 1 193 ? 37.172 66.730 5.984   1.00 32.07  ? 399 THR   B CA  1 
ATOM   3422 C C   . THR   B 1 193 ? 35.958 65.825 5.904   1.00 29.16  ? 399 THR   B C   1 
ATOM   3423 O O   . THR   B 1 193 ? 34.822 66.295 5.978   1.00 34.01  ? 399 THR   B O   1 
ATOM   3424 C CB  . THR   B 1 193 ? 37.302 67.349 7.381   1.00 31.69  ? 399 THR   B CB  1 
ATOM   3425 O OG1 . THR   B 1 193 ? 38.498 68.131 7.438   1.00 35.76  ? 399 THR   B OG1 1 
ATOM   3426 C CG2 . THR   B 1 193 ? 37.373 66.281 8.446   1.00 29.55  ? 399 THR   B CG2 1 
ATOM   3427 N N   . LEU   B 1 194 ? 36.192 64.528 5.751   1.00 29.07  ? 400 LEU   B N   1 
ATOM   3428 C CA  . LEU   B 1 194 ? 35.112 63.554 5.672   1.00 26.34  ? 400 LEU   B CA  1 
ATOM   3429 C C   . LEU   B 1 194 ? 34.825 62.919 7.016   1.00 30.56  ? 400 LEU   B C   1 
ATOM   3430 O O   . LEU   B 1 194 ? 33.663 62.672 7.353   1.00 27.73  ? 400 LEU   B O   1 
ATOM   3431 C CB  . LEU   B 1 194 ? 35.479 62.457 4.665   1.00 27.81  ? 400 LEU   B CB  1 
ATOM   3432 C CG  . LEU   B 1 194 ? 35.633 62.909 3.211   1.00 29.23  ? 400 LEU   B CG  1 
ATOM   3433 C CD1 . LEU   B 1 194 ? 36.214 61.799 2.339   1.00 27.15  ? 400 LEU   B CD1 1 
ATOM   3434 C CD2 . LEU   B 1 194 ? 34.294 63.383 2.651   1.00 32.61  ? 400 LEU   B CD2 1 
ATOM   3435 N N   . LEU   B 1 195 ? 35.876 62.651 7.788   1.00 24.38  ? 401 LEU   B N   1 
ATOM   3436 C CA  . LEU   B 1 195 ? 35.765 61.963 9.061   1.00 26.43  ? 401 LEU   B CA  1 
ATOM   3437 C C   . LEU   B 1 195 ? 36.971 62.330 9.912   1.00 26.10  ? 401 LEU   B C   1 
ATOM   3438 O O   . LEU   B 1 195 ? 38.104 62.322 9.423   1.00 25.32  ? 401 LEU   B O   1 
ATOM   3439 C CB  . LEU   B 1 195 ? 35.699 60.446 8.847   1.00 24.98  ? 401 LEU   B CB  1 
ATOM   3440 C CG  . LEU   B 1 195 ? 35.658 59.538 10.073  1.00 28.79  ? 401 LEU   B CG  1 
ATOM   3441 C CD1 . LEU   B 1 195 ? 34.482 59.875 10.991  1.00 27.79  ? 401 LEU   B CD1 1 
ATOM   3442 C CD2 . LEU   B 1 195 ? 35.599 58.087 9.629   1.00 28.46  ? 401 LEU   B CD2 1 
ATOM   3443 N N   . CYS   B 1 196 ? 36.732 62.636 11.184  1.00 24.71  ? 402 CYS   B N   1 
ATOM   3444 C CA  . CYS   B 1 196 ? 37.822 62.865 12.123  1.00 28.23  ? 402 CYS   B CA  1 
ATOM   3445 C C   . CYS   B 1 196 ? 37.523 62.093 13.401  1.00 29.07  ? 402 CYS   B C   1 
ATOM   3446 O O   . CYS   B 1 196 ? 36.441 62.234 13.985  1.00 26.14  ? 402 CYS   B O   1 
ATOM   3447 C CB  . CYS   B 1 196 ? 38.032 64.362 12.387  1.00 26.60  ? 402 CYS   B CB  1 
ATOM   3448 S SG  . CYS   B 1 196 ? 39.219 64.679 13.743  1.00 28.92  ? 402 CYS   B SG  1 
ATOM   3449 N N   . MET   B 1 197 ? 38.441 61.215 13.789  1.00 25.41  ? 403 MET   B N   1 
ATOM   3450 C CA  . MET   B 1 197 ? 38.276 60.389 14.976  1.00 27.82  ? 403 MET   B CA  1 
ATOM   3451 C C   . MET   B 1 197 ? 39.440 60.661 15.905  1.00 27.71  ? 403 MET   B C   1 
ATOM   3452 O O   . MET   B 1 197 ? 40.601 60.376 15.568  1.00 25.54  ? 403 MET   B O   1 
ATOM   3453 C CB  . MET   B 1 197 ? 38.221 58.900 14.629  1.00 25.96  ? 403 MET   B CB  1 
ATOM   3454 C CG  . MET   B 1 197 ? 37.014 58.523 13.766  1.00 40.51  ? 403 MET   B CG  1 
ATOM   3455 S SD  . MET   B 1 197 ? 37.147 56.773 13.316  1.00 42.10  ? 403 MET   B SD  1 
ATOM   3456 C CE  . MET   B 1 197 ? 37.916 56.153 14.857  1.00 29.06  ? 403 MET   B CE  1 
ATOM   3457 N N   . ALA   B 1 198 ? 39.117 61.211 17.062  1.00 26.77  ? 404 ALA   B N   1 
ATOM   3458 C CA  . ALA   B 1 198 ? 40.061 61.423 18.141  1.00 22.92  ? 404 ALA   B CA  1 
ATOM   3459 C C   . ALA   B 1 198 ? 40.007 60.187 19.020  1.00 28.17  ? 404 ALA   B C   1 
ATOM   3460 O O   . ALA   B 1 198 ? 38.958 59.892 19.590  1.00 27.09  ? 404 ALA   B O   1 
ATOM   3461 C CB  . ALA   B 1 198 ? 39.675 62.683 18.918  1.00 21.25  ? 404 ALA   B CB  1 
ATOM   3462 N N   . CYS   B 1 199 ? 41.114 59.452 19.108  1.00 22.30  ? 405 CYS   B N   1 
ATOM   3463 C CA  . CYS   B 1 199 ? 41.136 58.151 19.758  1.00 23.20  ? 405 CYS   B CA  1 
ATOM   3464 C C   . CYS   B 1 199 ? 41.865 58.217 21.095  1.00 25.17  ? 405 CYS   B C   1 
ATOM   3465 O O   . CYS   B 1 199 ? 42.999 58.688 21.162  1.00 24.84  ? 405 CYS   B O   1 
ATOM   3466 C CB  . CYS   B 1 199 ? 41.796 57.109 18.851  1.00 20.02  ? 405 CYS   B CB  1 
ATOM   3467 S SG  . CYS   B 1 199 ? 41.095 57.078 17.148  1.00 29.03  ? 405 CYS   B SG  1 
ATOM   3468 N N   . VAL   B 1 200 ? 41.218 57.721 22.147  1.00 23.61  ? 406 VAL   B N   1 
ATOM   3469 C CA  . VAL   B 1 200 ? 41.827 57.610 23.464  1.00 23.03  ? 406 VAL   B CA  1 
ATOM   3470 C C   . VAL   B 1 200 ? 41.792 56.138 23.879  1.00 24.74  ? 406 VAL   B C   1 
ATOM   3471 O O   . VAL   B 1 200 ? 41.057 55.324 23.308  1.00 22.13  ? 406 VAL   B O   1 
ATOM   3472 C CB  . VAL   B 1 200 ? 41.115 58.520 24.506  1.00 26.11  ? 406 VAL   B CB  1 
ATOM   3473 C CG1 . VAL   B 1 200 ? 41.191 59.976 24.090  1.00 25.73  ? 406 VAL   B CG1 1 
ATOM   3474 C CG2 . VAL   B 1 200 ? 39.657 58.137 24.639  1.00 24.82  ? 406 VAL   B CG2 1 
ATOM   3475 N N   . PHE   B 1 201 ? 42.610 55.789 24.874  1.00 24.14  ? 407 PHE   B N   1 
ATOM   3476 C CA  . PHE   B 1 201 ? 42.885 54.381 25.142  1.00 25.98  ? 407 PHE   B CA  1 
ATOM   3477 C C   . PHE   B 1 201 ? 42.966 54.076 26.627  1.00 25.53  ? 407 PHE   B C   1 
ATOM   3478 O O   . PHE   B 1 201 ? 43.437 54.888 27.431  1.00 26.55  ? 407 PHE   B O   1 
ATOM   3479 C CB  . PHE   B 1 201 ? 44.205 53.927 24.496  1.00 25.52  ? 407 PHE   B CB  1 
ATOM   3480 C CG  . PHE   B 1 201 ? 44.219 54.081 22.999  1.00 24.23  ? 407 PHE   B CG  1 
ATOM   3481 C CD1 . PHE   B 1 201 ? 44.596 55.271 22.424  1.00 19.41  ? 407 PHE   B CD1 1 
ATOM   3482 C CD2 . PHE   B 1 201 ? 43.812 53.032 22.184  1.00 20.38  ? 407 PHE   B CD2 1 
ATOM   3483 C CE1 . PHE   B 1 201 ? 44.558 55.431 21.026  1.00 19.94  ? 407 PHE   B CE1 1 
ATOM   3484 C CE2 . PHE   B 1 201 ? 43.802 53.169 20.781  1.00 20.75  ? 407 PHE   B CE2 1 
ATOM   3485 C CZ  . PHE   B 1 201 ? 44.160 54.357 20.211  1.00 22.55  ? 407 PHE   B CZ  1 
ATOM   3486 N N   . GLU   B 1 202 ? 42.614 52.834 26.942  1.00 25.08  ? 408 GLU   B N   1 
ATOM   3487 C CA  . GLU   B 1 202 ? 42.670 52.268 28.279  1.00 26.85  ? 408 GLU   B CA  1 
ATOM   3488 C C   . GLU   B 1 202 ? 42.900 50.775 28.096  1.00 29.78  ? 408 GLU   B C   1 
ATOM   3489 O O   . GLU   B 1 202 ? 42.672 50.240 27.013  1.00 25.80  ? 408 GLU   B O   1 
ATOM   3490 C CB  . GLU   B 1 202 ? 41.360 52.532 29.025  1.00 24.68  ? 408 GLU   B CB  1 
ATOM   3491 C CG  . GLU   B 1 202 ? 41.384 52.375 30.518  1.00 46.08  ? 408 GLU   B CG  1 
ATOM   3492 C CD  . GLU   B 1 202 ? 40.047 52.761 31.117  1.00 51.40  ? 408 GLU   B CD  1 
ATOM   3493 O OE1 . GLU   B 1 202 ? 39.718 53.967 31.088  1.00 56.99  ? 408 GLU   B OE1 1 
ATOM   3494 O OE2 . GLU   B 1 202 ? 39.344 51.870 31.638  1.00 59.84  ? 408 GLU   B OE2 1 
ATOM   3495 N N   . VAL   B 1 203 ? 43.352 50.095 29.144  1.00 26.89  ? 409 VAL   B N   1 
ATOM   3496 C CA  . VAL   B 1 203 ? 43.544 48.648 29.072  1.00 31.81  ? 409 VAL   B CA  1 
ATOM   3497 C C   . VAL   B 1 203 ? 42.220 47.944 29.334  1.00 31.66  ? 409 VAL   B C   1 
ATOM   3498 O O   . VAL   B 1 203 ? 41.462 48.344 30.218  1.00 31.04  ? 409 VAL   B O   1 
ATOM   3499 C CB  . VAL   B 1 203 ? 44.618 48.201 30.076  1.00 35.13  ? 409 VAL   B CB  1 
ATOM   3500 C CG1 . VAL   B 1 203 ? 44.692 46.686 30.136  1.00 35.84  ? 409 VAL   B CG1 1 
ATOM   3501 C CG2 . VAL   B 1 203 ? 45.945 48.793 29.714  1.00 31.04  ? 409 VAL   B CG2 1 
ATOM   3502 N N   . SER   B 1 204 ? 41.934 46.880 28.574  1.00 26.20  ? 410 SER   B N   1 
ATOM   3503 C CA  . SER   B 1 204 ? 40.692 46.130 28.775  1.00 30.62  ? 410 SER   B CA  1 
ATOM   3504 C C   . SER   B 1 204 ? 40.662 45.457 30.148  1.00 36.25  ? 410 SER   B C   1 
ATOM   3505 O O   . SER   B 1 204 ? 41.694 45.119 30.723  1.00 38.12  ? 410 SER   B O   1 
ATOM   3506 C CB  . SER   B 1 204 ? 40.527 45.062 27.696  1.00 36.34  ? 410 SER   B CB  1 
ATOM   3507 O OG  . SER   B 1 204 ? 41.613 44.157 27.757  1.00 40.81  ? 410 SER   B OG  1 
ATOM   3508 N N   . ASN   B 1 205 ? 39.456 45.278 30.637  1.00 36.40  ? 411 ASN   B N   1 
ATOM   3509 C CA  . ASN   B 1 205 ? 39.267 44.713 31.958  1.00 55.89  ? 411 ASN   B CA  1 
ATOM   3510 C C   . ASN   B 1 205 ? 38.885 43.257 31.990  1.00 65.32  ? 411 ASN   B C   1 
ATOM   3511 O O   . ASN   B 1 205 ? 37.978 42.855 31.279  1.00 63.42  ? 411 ASN   B O   1 
ATOM   3512 C CB  . ASN   B 1 205 ? 38.208 45.514 32.698  1.00 56.21  ? 411 ASN   B CB  1 
ATOM   3513 C CG  . ASN   B 1 205 ? 38.590 46.960 32.870  1.00 60.25  ? 411 ASN   B CG  1 
ATOM   3514 O OD1 . ASN   B 1 205 ? 39.654 47.267 33.389  1.00 57.72  ? 411 ASN   B OD1 1 
ATOM   3515 N ND2 . ASN   B 1 205 ? 37.724 47.856 32.431  1.00 58.53  ? 411 ASN   B ND2 1 
ATOM   3516 N N   . SER   B 1 206 ? 39.596 42.479 32.790  1.00 72.02  ? 412 SER   B N   1 
ATOM   3517 C CA  . SER   B 1 206 ? 39.382 41.048 32.985  1.00 78.04  ? 412 SER   B CA  1 
ATOM   3518 C C   . SER   B 1 206 ? 39.322 40.312 31.650  1.00 83.88  ? 412 SER   B C   1 
ATOM   3519 O O   . SER   B 1 206 ? 40.253 40.411 30.841  1.00 73.00  ? 412 SER   B O   1 
ATOM   3520 C CB  . SER   B 1 206 ? 38.111 40.812 33.808  1.00 84.45  ? 412 SER   B CB  1 
ATOM   3521 O OG  . SER   B 1 206 ? 38.200 39.608 34.555  1.00 94.39  ? 412 SER   B OG  1 
ATOM   3522 N N   . GLU   B 1 207 ? 38.236 39.573 31.409  1.00 80.08  ? 413 GLU   B N   1 
ATOM   3523 C CA  . GLU   B 1 207 ? 38.052 38.831 30.169  1.00 76.59  ? 413 GLU   B CA  1 
ATOM   3524 C C   . GLU   B 1 207 ? 37.020 39.477 29.253  1.00 70.31  ? 413 GLU   B C   1 
ATOM   3525 O O   . GLU   B 1 207 ? 36.437 38.793 28.404  1.00 66.10  ? 413 GLU   B O   1 
ATOM   3526 C CB  . GLU   B 1 207 ? 37.666 37.380 30.461  1.00 74.13  ? 413 GLU   B CB  1 
ATOM   3527 C CG  . GLU   B 1 207 ? 38.803 36.548 31.030  0.00 76.77  ? 413 GLU   B CG  1 
ATOM   3528 C CD  . GLU   B 1 207 ? 39.990 36.470 30.089  0.00 76.11  ? 413 GLU   B CD  1 
ATOM   3529 O OE1 . GLU   B 1 207 ? 39.780 36.222 28.883  0.00 74.26  ? 413 GLU   B OE1 1 
ATOM   3530 O OE2 . GLU   B 1 207 ? 41.133 36.659 30.555  0.00 76.40  ? 413 GLU   B OE2 1 
ATOM   3531 N N   . HIS   B 1 208 ? 36.788 40.784 29.396  1.00 62.98  ? 414 HIS   B N   1 
ATOM   3532 C CA  . HIS   B 1 208 ? 35.861 41.463 28.498  1.00 66.08  ? 414 HIS   B CA  1 
ATOM   3533 C C   . HIS   B 1 208 ? 36.482 41.751 27.138  1.00 55.79  ? 414 HIS   B C   1 
ATOM   3534 O O   . HIS   B 1 208 ? 35.749 41.945 26.164  1.00 59.33  ? 414 HIS   B O   1 
ATOM   3535 C CB  . HIS   B 1 208 ? 35.348 42.740 29.166  1.00 53.63  ? 414 HIS   B CB  1 
ATOM   3536 C CG  . HIS   B 1 208 ? 34.569 42.465 30.415  1.00 68.33  ? 414 HIS   B CG  1 
ATOM   3537 N ND1 . HIS   B 1 208 ? 35.081 42.684 31.678  1.00 75.73  ? 414 HIS   B ND1 1 
ATOM   3538 C CD2 . HIS   B 1 208 ? 33.325 41.960 30.596  1.00 65.51  ? 414 HIS   B CD2 1 
ATOM   3539 C CE1 . HIS   B 1 208 ? 34.184 42.331 32.582  1.00 71.13  ? 414 HIS   B CE1 1 
ATOM   3540 N NE2 . HIS   B 1 208 ? 33.109 41.890 31.952  1.00 71.43  ? 414 HIS   B NE2 1 
ATOM   3541 N N   . GLY   B 1 209 ? 37.802 41.747 27.045  1.00 45.27  ? 415 GLY   B N   1 
ATOM   3542 C CA  . GLY   B 1 209 ? 38.463 41.913 25.779  1.00 45.91  ? 415 GLY   B CA  1 
ATOM   3543 C C   . GLY   B 1 209 ? 38.368 43.334 25.252  1.00 34.00  ? 415 GLY   B C   1 
ATOM   3544 O O   . GLY   B 1 209 ? 37.887 44.260 25.908  1.00 30.47  ? 415 GLY   B O   1 
ATOM   3545 N N   . ALA   B 1 210 ? 38.846 43.487 24.025  1.00 30.69  ? 416 ALA   B N   1 
ATOM   3546 C CA  . ALA   B 1 210 ? 38.880 44.798 23.406  1.00 25.39  ? 416 ALA   B CA  1 
ATOM   3547 C C   . ALA   B 1 210 ? 37.461 45.255 23.097  1.00 26.85  ? 416 ALA   B C   1 
ATOM   3548 O O   . ALA   B 1 210 ? 36.598 44.447 22.733  1.00 25.96  ? 416 ALA   B O   1 
ATOM   3549 C CB  . ALA   B 1 210 ? 39.728 44.762 22.135  1.00 21.19  ? 416 ALA   B CB  1 
ATOM   3550 N N   . GLN   B 1 211 ? 37.224 46.558 23.262  1.00 21.67  ? 417 GLN   B N   1 
ATOM   3551 C CA  . GLN   B 1 211 ? 35.925 47.162 23.021  1.00 23.53  ? 417 GLN   B CA  1 
ATOM   3552 C C   . GLN   B 1 211 ? 36.149 48.604 22.604  1.00 28.23  ? 417 GLN   B C   1 
ATOM   3553 O O   . GLN   B 1 211 ? 37.261 49.120 22.685  1.00 26.04  ? 417 GLN   B O   1 
ATOM   3554 C CB  . GLN   B 1 211 ? 35.032 47.089 24.272  1.00 29.20  ? 417 GLN   B CB  1 
ATOM   3555 C CG  . GLN   B 1 211 ? 34.586 45.681 24.634  1.00 33.41  ? 417 GLN   B CG  1 
ATOM   3556 C CD  . GLN   B 1 211 ? 33.677 45.624 25.858  1.00 37.71  ? 417 GLN   B CD  1 
ATOM   3557 O OE1 . GLN   B 1 211 ? 33.046 46.608 26.226  1.00 40.47  ? 417 GLN   B OE1 1 
ATOM   3558 N NE2 . GLN   B 1 211 ? 33.632 44.469 26.499  1.00 45.32  ? 417 GLN   B NE2 1 
ATOM   3559 N N   . HIS   B 1 212 ? 35.083 49.271 22.163  1.00 24.87  ? 418 HIS   B N   1 
ATOM   3560 C CA  . HIS   B 1 212 ? 35.188 50.691 21.855  1.00 24.63  ? 418 HIS   B CA  1 
ATOM   3561 C C   . HIS   B 1 212 ? 33.887 51.388 22.220  1.00 27.25  ? 418 HIS   B C   1 
ATOM   3562 O O   . HIS   B 1 212 ? 32.819 50.765 22.308  1.00 26.15  ? 418 HIS   B O   1 
ATOM   3563 C CB  . HIS   B 1 212 ? 35.568 50.943 20.372  1.00 19.48  ? 418 HIS   B CB  1 
ATOM   3564 C CG  . HIS   B 1 212 ? 34.464 50.678 19.405  1.00 23.93  ? 418 HIS   B CG  1 
ATOM   3565 N ND1 . HIS   B 1 212 ? 33.957 49.410 19.183  1.00 23.53  ? 418 HIS   B ND1 1 
ATOM   3566 C CD2 . HIS   B 1 212 ? 33.794 51.504 18.569  1.00 22.18  ? 418 HIS   B CD2 1 
ATOM   3567 C CE1 . HIS   B 1 212 ? 32.992 49.482 18.284  1.00 24.06  ? 418 HIS   B CE1 1 
ATOM   3568 N NE2 . HIS   B 1 212 ? 32.875 50.740 17.896  1.00 25.72  ? 418 HIS   B NE2 1 
ATOM   3569 N N   . HIS   B 1 213 ? 33.995 52.696 22.450  1.00 23.64  ? 419 HIS   B N   1 
ATOM   3570 C CA  . HIS   B 1 213 ? 32.840 53.519 22.806  1.00 24.39  ? 419 HIS   B CA  1 
ATOM   3571 C C   . HIS   B 1 213 ? 32.908 54.791 21.987  1.00 23.41  ? 419 HIS   B C   1 
ATOM   3572 O O   . HIS   B 1 213 ? 33.927 55.489 22.014  1.00 25.58  ? 419 HIS   B O   1 
ATOM   3573 C CB  . HIS   B 1 213 ? 32.823 53.847 24.314  1.00 27.37  ? 419 HIS   B CB  1 
ATOM   3574 C CG  . HIS   B 1 213 ? 31.499 54.337 24.826  1.00 35.05  ? 419 HIS   B CG  1 
ATOM   3575 N ND1 . HIS   B 1 213 ? 30.776 53.670 25.794  1.00 39.25  ? 419 HIS   B ND1 1 
ATOM   3576 C CD2 . HIS   B 1 213 ? 30.755 55.416 24.482  1.00 29.93  ? 419 HIS   B CD2 1 
ATOM   3577 C CE1 . HIS   B 1 213 ? 29.659 54.330 26.041  1.00 38.35  ? 419 HIS   B CE1 1 
ATOM   3578 N NE2 . HIS   B 1 213 ? 29.626 55.399 25.268  1.00 35.50  ? 419 HIS   B NE2 1 
ATOM   3579 N N   . ILE   B 1 214 ? 31.822 55.109 21.278  1.00 24.36  ? 420 ILE   B N   1 
ATOM   3580 C CA  . ILE   B 1 214 ? 31.787 56.248 20.365  1.00 24.65  ? 420 ILE   B CA  1 
ATOM   3581 C C   . ILE   B 1 214 ? 31.035 57.404 20.997  1.00 26.77  ? 420 ILE   B C   1 
ATOM   3582 O O   . ILE   B 1 214 ? 29.950 57.221 21.558  1.00 27.37  ? 420 ILE   B O   1 
ATOM   3583 C CB  . ILE   B 1 214 ? 31.131 55.887 19.018  1.00 26.43  ? 420 ILE   B CB  1 
ATOM   3584 C CG1 . ILE   B 1 214 ? 31.819 54.685 18.377  1.00 29.71  ? 420 ILE   B CG1 1 
ATOM   3585 C CG2 . ILE   B 1 214 ? 31.135 57.106 18.077  1.00 23.57  ? 420 ILE   B CG2 1 
ATOM   3586 C CD1 . ILE   B 1 214 ? 31.057 54.137 17.175  1.00 29.43  ? 420 ILE   B CD1 1 
ATOM   3587 N N   . TYR   B 1 215 ? 31.586 58.602 20.839  1.00 24.22  ? 421 TYR   B N   1 
ATOM   3588 C CA  . TYR   B 1 215 ? 30.991 59.855 21.277  1.00 25.57  ? 421 TYR   B CA  1 
ATOM   3589 C C   . TYR   B 1 215 ? 31.028 60.831 20.118  1.00 30.47  ? 421 TYR   B C   1 
ATOM   3590 O O   . TYR   B 1 215 ? 32.032 60.911 19.404  1.00 27.66  ? 421 TYR   B O   1 
ATOM   3591 C CB  . TYR   B 1 215 ? 31.768 60.469 22.447  1.00 28.54  ? 421 TYR   B CB  1 
ATOM   3592 C CG  . TYR   B 1 215 ? 31.868 59.597 23.668  1.00 29.29  ? 421 TYR   B CG  1 
ATOM   3593 C CD1 . TYR   B 1 215 ? 30.899 59.650 24.653  1.00 31.91  ? 421 TYR   B CD1 1 
ATOM   3594 C CD2 . TYR   B 1 215 ? 32.955 58.734 23.851  1.00 27.93  ? 421 TYR   B CD2 1 
ATOM   3595 C CE1 . TYR   B 1 215 ? 30.988 58.882 25.785  1.00 30.25  ? 421 TYR   B CE1 1 
ATOM   3596 C CE2 . TYR   B 1 215 ? 33.056 57.949 24.985  1.00 27.25  ? 421 TYR   B CE2 1 
ATOM   3597 C CZ  . TYR   B 1 215 ? 32.050 58.035 25.950  1.00 33.94  ? 421 TYR   B CZ  1 
ATOM   3598 O OH  . TYR   B 1 215 ? 32.096 57.284 27.091  1.00 34.56  ? 421 TYR   B OH  1 
ATOM   3599 N N   . ARG   B 1 216 ? 29.954 61.595 19.932  1.00 29.02  ? 422 ARG   B N   1 
ATOM   3600 C CA  . ARG   B 1 216 ? 30.029 62.698 18.989  1.00 29.53  ? 422 ARG   B CA  1 
ATOM   3601 C C   . ARG   B 1 216 ? 30.727 63.862 19.681  1.00 29.89  ? 422 ARG   B C   1 
ATOM   3602 O O   . ARG   B 1 216 ? 30.509 64.099 20.872  1.00 31.28  ? 422 ARG   B O   1 
ATOM   3603 C CB  . ARG   B 1 216 ? 28.628 63.093 18.498  1.00 34.53  ? 422 ARG   B CB  1 
ATOM   3604 C CG  . ARG   B 1 216 ? 28.621 63.865 17.188  1.00 49.58  ? 422 ARG   B CG  1 
ATOM   3605 C CD  . ARG   B 1 216 ? 27.196 63.986 16.610  1.00 66.20  ? 422 ARG   B CD  1 
ATOM   3606 N NE  . ARG   B 1 216 ? 26.732 62.782 15.919  1.00 62.95  ? 422 ARG   B NE  1 
ATOM   3607 C CZ  . ARG   B 1 216 ? 26.895 62.526 14.622  1.00 60.17  ? 422 ARG   B CZ  1 
ATOM   3608 N NH1 . ARG   B 1 216 ? 27.511 63.374 13.816  1.00 57.62  ? 422 ARG   B NH1 1 
ATOM   3609 N NH2 . ARG   B 1 216 ? 26.420 61.392 14.119  1.00 58.08  ? 422 ARG   B NH2 1 
ATOM   3610 N N   . LEU   B 1 217 ? 31.602 64.559 18.954  1.00 27.38  ? 423 LEU   B N   1 
ATOM   3611 C CA  . LEU   B 1 217 ? 32.284 65.734 19.490  1.00 29.06  ? 423 LEU   B CA  1 
ATOM   3612 C C   . LEU   B 1 217 ? 31.457 66.970 19.165  1.00 32.45  ? 423 LEU   B C   1 
ATOM   3613 O O   . LEU   B 1 217 ? 31.119 67.185 18.000  1.00 30.24  ? 423 LEU   B O   1 
ATOM   3614 C CB  . LEU   B 1 217 ? 33.685 65.880 18.898  1.00 23.27  ? 423 LEU   B CB  1 
ATOM   3615 C CG  . LEU   B 1 217 ? 34.743 64.938 19.478  1.00 28.12  ? 423 LEU   B CG  1 
ATOM   3616 C CD1 . LEU   B 1 217 ? 36.023 65.014 18.661  1.00 25.99  ? 423 LEU   B CD1 1 
ATOM   3617 C CD2 . LEU   B 1 217 ? 35.015 65.250 20.968  1.00 30.39  ? 423 LEU   B CD2 1 
ATOM   3618 N N   . VAL   B 1 218 ? 31.116 67.764 20.195  1.00 34.32  ? 424 VAL   B N   1 
ATOM   3619 C CA  . VAL   B 1 218 ? 30.256 68.937 20.047  1.00 32.63  ? 424 VAL   B CA  1 
ATOM   3620 C C   . VAL   B 1 218 ? 30.915 70.141 20.712  1.00 37.82  ? 424 VAL   B C   1 
ATOM   3621 O O   . VAL   B 1 218 ? 31.891 70.016 21.455  1.00 32.94  ? 424 VAL   B O   1 
ATOM   3622 C CB  . VAL   B 1 218 ? 28.842 68.724 20.638  1.00 36.51  ? 424 VAL   B CB  1 
ATOM   3623 C CG1 . VAL   B 1 218 ? 28.129 67.593 19.944  1.00 33.97  ? 424 VAL   B CG1 1 
ATOM   3624 C CG2 . VAL   B 1 218 ? 28.905 68.480 22.152  1.00 31.74  ? 424 VAL   B CG2 1 
ATOM   3625 N N   . LYS   B 1 219 ? 30.331 71.317 20.451  1.00 39.54  ? 425 LYS   B N   1 
ATOM   3626 C CA  . LYS   B 1 219 ? 30.801 72.618 20.963  1.00 39.21  ? 425 LYS   B CA  1 
ATOM   3627 C C   . LYS   B 1 219 ? 32.192 73.064 20.607  1.00 47.05  ? 425 LYS   B C   1 
ATOM   3628 O O   . LYS   B 1 219 ? 32.679 74.019 21.219  1.00 52.69  ? 425 LYS   B O   1 
ATOM   3629 C CB  . LYS   B 1 219 ? 30.707 72.687 22.482  1.00 42.07  ? 425 LYS   B CB  1 
ATOM   3630 C CG  . LYS   B 1 219 ? 29.353 72.488 23.023  1.00 48.84  ? 425 LYS   B CG  1 
ATOM   3631 C CD  . LYS   B 1 219 ? 28.467 73.412 22.224  1.00 55.20  ? 425 LYS   B CD  1 
ATOM   3632 C CE  . LYS   B 1 219 ? 27.737 74.345 23.147  1.00 66.45  ? 425 LYS   B CE  1 
ATOM   3633 N NZ  . LYS   B 1 219 ? 28.776 75.323 23.616  1.00 52.09  ? 425 LYS   B NZ  1 
HETATM 3634 C C1  . GOL   C 2 .   ? 31.657 35.432 -14.354 1.00 59.90  ? 501 GOL   A C1  1 
HETATM 3635 O O1  . GOL   C 2 .   ? 32.062 36.597 -13.682 1.00 66.66  ? 501 GOL   A O1  1 
HETATM 3636 C C2  . GOL   C 2 .   ? 31.006 35.883 -15.681 1.00 65.22  ? 501 GOL   A C2  1 
HETATM 3637 O O2  . GOL   C 2 .   ? 29.951 36.739 -15.465 1.00 66.54  ? 501 GOL   A O2  1 
HETATM 3638 C C3  . GOL   C 2 .   ? 30.527 34.597 -16.355 1.00 65.94  ? 501 GOL   A C3  1 
HETATM 3639 O O3  . GOL   C 2 .   ? 29.628 34.008 -15.463 1.00 69.33  ? 501 GOL   A O3  1 
HETATM 3640 C C1  . A1IJL D 3 .   ? 17.570 32.603 -3.269  1.00 33.30  ? 502 A1IJL A C1  1 
HETATM 3641 C C2  . A1IJL D 3 .   ? 17.074 34.528 -4.716  1.00 36.02  ? 502 A1IJL A C2  1 
HETATM 3642 C C3  . A1IJL D 3 .   ? 18.727 32.041 -4.094  1.00 37.47  ? 502 A1IJL A C3  1 
HETATM 3643 N N6  . A1IJL D 3 .   ? 15.740 40.977 -1.529  1.00 33.23  ? 502 A1IJL A N6  1 
HETATM 3644 C C7  . A1IJL D 3 .   ? 16.470 36.558 -6.024  1.00 34.76  ? 502 A1IJL A C7  1 
HETATM 3645 C C8  . A1IJL D 3 .   ? 16.646 36.775 -3.629  1.00 30.88  ? 502 A1IJL A C8  1 
HETATM 3646 C C9  . A1IJL D 3 .   ? 14.217 31.050 -3.479  1.00 39.45  ? 502 A1IJL A C9  1 
HETATM 3647 C C10 . A1IJL D 3 .   ? 16.110 37.880 -6.169  1.00 33.77  ? 502 A1IJL A C10 1 
HETATM 3648 C C11 . A1IJL D 3 .   ? 16.290 38.119 -3.748  1.00 35.97  ? 502 A1IJL A C11 1 
HETATM 3649 C C12 . A1IJL D 3 .   ? 14.741 28.861 -4.626  1.00 41.01  ? 502 A1IJL A C12 1 
HETATM 3650 C C13 . A1IJL D 3 .   ? 16.021 38.663 -5.024  1.00 35.65  ? 502 A1IJL A C13 1 
HETATM 3651 C C14 . A1IJL D 3 .   ? 16.111 39.189 -2.812  1.00 30.40  ? 502 A1IJL A C14 1 
HETATM 3652 C C15 . A1IJL D 3 .   ? 15.740 40.306 -3.539  1.00 30.65  ? 502 A1IJL A C15 1 
HETATM 3653 C C16 . A1IJL D 3 .   ? 16.108 39.665 -1.488  1.00 30.83  ? 502 A1IJL A C16 1 
HETATM 3654 C C19 . A1IJL D 3 .   ? 14.017 41.452 -5.795  1.00 30.52  ? 502 A1IJL A C19 1 
HETATM 3655 C C20 . A1IJL D 3 .   ? 15.620 41.892 -0.396  1.00 30.46  ? 502 A1IJL A C20 1 
HETATM 3656 C C21 . A1IJL D 3 .   ? 15.349 41.702 -8.198  1.00 31.72  ? 502 A1IJL A C21 1 
HETATM 3657 C C22 . A1IJL D 3 .   ? 13.461 42.199 -6.816  1.00 33.09  ? 502 A1IJL A C22 1 
HETATM 3658 C C24 . A1IJL D 3 .   ? 13.490 43.103 -9.126  1.00 43.23  ? 502 A1IJL A C24 1 
HETATM 3659 C C17 . A1IJL D 3 .   ? 15.263 40.877 -5.951  1.00 29.94  ? 502 A1IJL A C17 1 
HETATM 3660 C C18 . A1IJL D 3 .   ? 15.906 40.949 -7.173  1.00 30.91  ? 502 A1IJL A C18 1 
HETATM 3661 C C23 . A1IJL D 3 .   ? 14.126 42.328 -8.019  1.00 30.94  ? 502 A1IJL A C23 1 
HETATM 3662 C C4  . A1IJL D 3 .   ? 16.307 31.818 -3.459  1.00 39.46  ? 502 A1IJL A C4  1 
HETATM 3663 C C5  . A1IJL D 3 .   ? 16.750 35.993 -4.777  1.00 33.40  ? 502 A1IJL A C5  1 
HETATM 3664 C C6  . A1IJL D 3 .   ? 14.978 32.111 -3.091  1.00 32.33  ? 502 A1IJL A C6  1 
HETATM 3665 F F1  . A1IJL D 3 .   ? 12.696 44.077 -8.699  1.00 36.57  ? 502 A1IJL A F1  1 
HETATM 3666 F F2  . A1IJL D 3 .   ? 14.378 43.653 -9.945  1.00 42.33  ? 502 A1IJL A F2  1 
HETATM 3667 F F3  . A1IJL D 3 .   ? 12.703 42.346 -9.890  1.00 39.66  ? 502 A1IJL A F3  1 
HETATM 3668 N N1  . A1IJL D 3 .   ? 17.403 34.036 -3.520  1.00 32.88  ? 502 A1IJL A N1  1 
HETATM 3669 N N2  . A1IJL D 3 .   ? 16.364 30.620 -4.042  1.00 35.31  ? 502 A1IJL A N2  1 
HETATM 3670 N N3  . A1IJL D 3 .   ? 15.069 30.164 -4.053  1.00 45.33  ? 502 A1IJL A N3  1 
HETATM 3671 N N4  . A1IJL D 3 .   ? 15.719 40.033 -4.886  1.00 28.44  ? 502 A1IJL A N4  1 
HETATM 3672 N N5  . A1IJL D 3 .   ? 15.501 41.417 -2.809  1.00 29.00  ? 502 A1IJL A N5  1 
HETATM 3673 O O1  . A1IJL D 3 .   ? 16.892 33.804 -5.699  1.00 31.98  ? 502 A1IJL A O1  1 
HETATM 3674 O O2  . A1IJL D 3 .   ? 19.918 32.767 -3.811  1.00 45.68  ? 502 A1IJL A O2  1 
HETATM 3675 S S   . SO4   E 4 .   ? 22.384 62.274 11.976  1.00 78.16  ? 503 SO4   A S   1 
HETATM 3676 O O1  . SO4   E 4 .   ? 21.882 60.983 12.464  1.00 52.90  ? 503 SO4   A O1  1 
HETATM 3677 O O2  . SO4   E 4 .   ? 22.113 62.429 10.542  1.00 57.90  ? 503 SO4   A O2  1 
HETATM 3678 O O3  . SO4   E 4 .   ? 21.721 63.357 12.709  1.00 69.84  ? 503 SO4   A O3  1 
HETATM 3679 O O4  . SO4   E 4 .   ? 23.832 62.345 12.185  1.00 77.91  ? 503 SO4   A O4  1 
HETATM 3680 S S   . SO4   F 4 .   ? 12.858 60.407 5.836   1.00 64.10  ? 504 SO4   A S   1 
HETATM 3681 O O1  . SO4   F 4 .   ? 13.217 59.630 4.651   1.00 64.14  ? 504 SO4   A O1  1 
HETATM 3682 O O2  . SO4   F 4 .   ? 11.736 59.780 6.531   1.00 62.14  ? 504 SO4   A O2  1 
HETATM 3683 O O3  . SO4   F 4 .   ? 13.998 60.471 6.749   1.00 59.59  ? 504 SO4   A O3  1 
HETATM 3684 O O4  . SO4   F 4 .   ? 12.490 61.767 5.437   1.00 70.36  ? 504 SO4   A O4  1 
HETATM 3685 S S   . SO4   G 4 .   ? 8.543  40.831 22.710  1.00 103.26 ? 505 SO4   A S   1 
HETATM 3686 O O1  . SO4   G 4 .   ? 9.992  40.829 22.914  1.00 90.72  ? 505 SO4   A O1  1 
HETATM 3687 O O2  . SO4   G 4 .   ? 8.155  39.698 21.872  1.00 73.89  ? 505 SO4   A O2  1 
HETATM 3688 O O3  . SO4   G 4 .   ? 7.883  40.716 24.010  1.00 111.49 ? 505 SO4   A O3  1 
HETATM 3689 O O4  . SO4   G 4 .   ? 8.148  42.083 22.064  1.00 81.82  ? 505 SO4   A O4  1 
HETATM 3690 C C1  . GOL   H 2 .   ? 50.321 34.582 9.461   1.00 63.18  ? 501 GOL   B C1  1 
HETATM 3691 O O1  . GOL   H 2 .   ? 49.528 35.044 8.379   1.00 65.55  ? 501 GOL   B O1  1 
HETATM 3692 C C2  . GOL   H 2 .   ? 51.816 34.569 9.036   1.00 58.07  ? 501 GOL   B C2  1 
HETATM 3693 O O2  . GOL   H 2 .   ? 52.518 33.582 9.713   1.00 68.09  ? 501 GOL   B O2  1 
HETATM 3694 C C3  . GOL   H 2 .   ? 52.381 35.993 9.369   1.00 56.73  ? 501 GOL   B C3  1 
HETATM 3695 O O3  . GOL   H 2 .   ? 53.729 35.801 9.754   1.00 61.40  ? 501 GOL   B O3  1 
HETATM 3696 C C1  . A1IJL I 3 .   ? 50.536 53.345 10.626  1.00 36.74  ? 502 A1IJL B C1  1 
HETATM 3697 C C2  . A1IJL I 3 .   ? 50.265 52.141 12.765  1.00 35.18  ? 502 A1IJL B C2  1 
HETATM 3698 C C3  . A1IJL I 3 .   ? 51.309 52.246 9.904   1.00 36.64  ? 502 A1IJL B C3  1 
HETATM 3699 N N6  . A1IJL I 3 .   ? 43.922 53.055 16.282  1.00 33.74  ? 502 A1IJL B N6  1 
HETATM 3700 C C7  . A1IJL I 3 .   ? 49.807 51.052 14.946  1.00 28.99  ? 502 A1IJL B C7  1 
HETATM 3701 C C8  . A1IJL I 3 .   ? 48.072 52.420 13.959  1.00 29.88  ? 502 A1IJL B C8  1 
HETATM 3702 C C9  . A1IJL I 3 .   ? 52.322 56.293 11.971  1.00 38.29  ? 502 A1IJL B C9  1 
HETATM 3703 C C10 . A1IJL I 3 .   ? 49.029 50.791 16.049  1.00 30.88  ? 502 A1IJL B C10 1 
HETATM 3704 C C11 . A1IJL I 3 .   ? 47.266 52.169 15.065  1.00 30.84  ? 502 A1IJL B C11 1 
HETATM 3705 C C12 . A1IJL I 3 .   ? 54.541 56.128 10.777  1.00 40.34  ? 502 A1IJL B C12 1 
HETATM 3706 C C13 . A1IJL I 3 .   ? 47.754 51.346 16.100  1.00 28.22  ? 502 A1IJL B C13 1 
HETATM 3707 C C14 . A1IJL I 3 .   ? 45.940 52.570 15.460  1.00 27.77  ? 502 A1IJL B C14 1 
HETATM 3708 C C15 . A1IJL I 3 .   ? 45.700 51.994 16.686  1.00 30.03  ? 502 A1IJL B C15 1 
HETATM 3709 C C16 . A1IJL I 3 .   ? 44.744 53.270 15.215  1.00 30.19  ? 502 A1IJL B C16 1 
HETATM 3710 C C19 . A1IJL I 3 .   ? 46.624 51.380 19.465  1.00 27.18  ? 502 A1IJL B C19 1 
HETATM 3711 C C20 . A1IJL I 3 .   ? 42.568 53.561 16.498  1.00 29.12  ? 502 A1IJL B C20 1 
HETATM 3712 C C21 . A1IJL I 3 .   ? 47.941 48.985 19.805  1.00 30.68  ? 502 A1IJL B C21 1 
HETATM 3713 C C22 . A1IJL I 3 .   ? 46.889 50.919 20.741  1.00 28.97  ? 502 A1IJL B C22 1 
HETATM 3714 C C24 . A1IJL I 3 .   ? 47.860 49.239 22.290  1.00 35.64  ? 502 A1IJL B C24 1 
HETATM 3715 C C17 . A1IJL I 3 .   ? 46.948 50.609 18.363  1.00 26.13  ? 502 A1IJL B C17 1 
HETATM 3716 C C18 . A1IJL I 3 .   ? 47.667 49.444 18.526  1.00 27.53  ? 502 A1IJL B C18 1 
HETATM 3717 C C23 . A1IJL I 3 .   ? 47.535 49.710 20.912  1.00 28.75  ? 502 A1IJL B C23 1 
HETATM 3718 C C4  . A1IJL I 3 .   ? 51.423 54.472 11.058  1.00 33.34  ? 502 A1IJL B C4  1 
HETATM 3719 C C5  . A1IJL I 3 .   ? 49.336 51.844 13.898  1.00 29.68  ? 502 A1IJL B C5  1 
HETATM 3720 C C6  . A1IJL I 3 .   ? 51.190 55.535 11.950  1.00 33.93  ? 502 A1IJL B C6  1 
HETATM 3721 F F1  . A1IJL I 3 .   ? 47.114 49.805 23.218  1.00 34.72  ? 502 A1IJL B F1  1 
HETATM 3722 F F2  . A1IJL I 3 .   ? 47.733 47.927 22.457  1.00 35.45  ? 502 A1IJL B F2  1 
HETATM 3723 F F3  . A1IJL I 3 .   ? 49.112 49.532 22.627  1.00 38.05  ? 502 A1IJL B F3  1 
HETATM 3724 N N1  . A1IJL I 3 .   ? 49.739 52.788 11.721  1.00 34.86  ? 502 A1IJL B N1  1 
HETATM 3725 N N2  . A1IJL I 3 .   ? 52.649 54.576 10.543  1.00 40.20  ? 502 A1IJL B N2  1 
HETATM 3726 N N3  . A1IJL I 3 .   ? 53.188 55.698 11.117  1.00 41.32  ? 502 A1IJL B N3  1 
HETATM 3727 N N4  . A1IJL I 3 .   ? 46.756 51.215 17.081  1.00 29.60  ? 502 A1IJL B N4  1 
HETATM 3728 N N5  . A1IJL I 3 .   ? 44.499 52.251 17.232  1.00 27.05  ? 502 A1IJL B N5  1 
HETATM 3729 O O1  . A1IJL I 3 .   ? 51.475 51.943 12.901  1.00 32.71  ? 502 A1IJL B O1  1 
HETATM 3730 O O2  . A1IJL I 3 .   ? 50.413 51.269 9.403   1.00 39.25  ? 502 A1IJL B O2  1 
HETATM 3731 S S   . SO4   J 4 .   ? 26.508 49.546 12.096  1.00 42.85  ? 503 SO4   B S   1 
HETATM 3732 O O1  . SO4   J 4 .   ? 26.705 48.294 11.395  1.00 44.20  ? 503 SO4   B O1  1 
HETATM 3733 O O2  . SO4   J 4 .   ? 25.307 50.240 11.658  1.00 47.77  ? 503 SO4   B O2  1 
HETATM 3734 O O3  . SO4   J 4 .   ? 26.372 49.269 13.520  1.00 52.12  ? 503 SO4   B O3  1 
HETATM 3735 O O4  . SO4   J 4 .   ? 27.632 50.419 11.854  1.00 46.95  ? 503 SO4   B O4  1 
HETATM 3736 S S   . SO4   K 4 .   ? 23.627 60.638 16.444  1.00 108.51 ? 504 SO4   B S   1 
HETATM 3737 O O1  . SO4   K 4 .   ? 23.779 60.742 14.987  1.00 86.07  ? 504 SO4   B O1  1 
HETATM 3738 O O2  . SO4   K 4 .   ? 22.269 61.033 16.816  1.00 98.46  ? 504 SO4   B O2  1 
HETATM 3739 O O3  . SO4   K 4 .   ? 23.861 59.248 16.857  1.00 85.52  ? 504 SO4   B O3  1 
HETATM 3740 O O4  . SO4   K 4 .   ? 24.572 61.544 17.109  1.00 86.86  ? 504 SO4   B O4  1 
HETATM 3741 S S   . SO4   L 4 .   ? 22.239 47.110 24.085  1.00 101.05 ? 505 SO4   B S   1 
HETATM 3742 O O1  . SO4   L 4 .   ? 23.561 46.710 23.596  1.00 78.41  ? 505 SO4   B O1  1 
HETATM 3743 O O2  . SO4   L 4 .   ? 21.634 48.068 23.157  1.00 83.08  ? 505 SO4   B O2  1 
HETATM 3744 O O3  . SO4   L 4 .   ? 21.372 45.935 24.176  1.00 97.16  ? 505 SO4   B O3  1 
HETATM 3745 O O4  . SO4   L 4 .   ? 22.383 47.728 25.405  1.00 88.67  ? 505 SO4   B O4  1 
HETATM 3746 O O   . HOH   M 5 .   ? 17.903 39.948 17.221  1.00 41.60  ? 601 HOH   A O   1 
HETATM 3747 O O   . HOH   M 5 .   ? 17.833 32.157 2.012   1.00 32.42  ? 602 HOH   A O   1 
HETATM 3748 O O   . HOH   M 5 .   ? 13.547 56.933 -5.659  1.00 57.58  ? 603 HOH   A O   1 
HETATM 3749 O O   . HOH   M 5 .   ? 20.442 25.176 5.207   1.00 46.32  ? 604 HOH   A O   1 
HETATM 3750 O O   . HOH   M 5 .   ? 4.103  33.181 -9.531  1.00 41.78  ? 605 HOH   A O   1 
HETATM 3751 O O   . HOH   M 5 .   ? 29.248 32.291 7.230   1.00 39.86  ? 606 HOH   A O   1 
HETATM 3752 O O   . HOH   M 5 .   ? 6.079  44.789 -3.419  1.00 27.16  ? 607 HOH   A O   1 
HETATM 3753 O O   . HOH   M 5 .   ? 25.615 43.184 -15.912 1.00 30.16  ? 608 HOH   A O   1 
HETATM 3754 O O   . HOH   M 5 .   ? 20.182 36.705 3.215   1.00 37.70  ? 609 HOH   A O   1 
HETATM 3755 O O   . HOH   M 5 .   ? 9.364  34.897 16.005  1.00 34.14  ? 610 HOH   A O   1 
HETATM 3756 O O   . HOH   M 5 .   ? -1.400 45.804 -9.114  1.00 49.59  ? 611 HOH   A O   1 
HETATM 3757 O O   . HOH   M 5 .   ? 21.912 53.638 -5.600  1.00 39.38  ? 612 HOH   A O   1 
HETATM 3758 O O   . HOH   M 5 .   ? 1.150  37.300 6.808   1.00 41.74  ? 613 HOH   A O   1 
HETATM 3759 O O   . HOH   M 5 .   ? 4.938  46.018 18.883  1.00 57.77  ? 614 HOH   A O   1 
HETATM 3760 O O   . HOH   M 5 .   ? 12.257 59.109 11.090  1.00 43.20  ? 615 HOH   A O   1 
HETATM 3761 O O   . HOH   M 5 .   ? 4.026  54.668 8.980   1.00 45.55  ? 616 HOH   A O   1 
HETATM 3762 O O   . HOH   M 5 .   ? 12.026 34.115 18.763  1.00 43.69  ? 617 HOH   A O   1 
HETATM 3763 O O   . HOH   M 5 .   ? 17.179 54.068 -12.071 1.00 58.59  ? 618 HOH   A O   1 
HETATM 3764 O O   . HOH   M 5 .   ? 12.443 32.183 13.220  1.00 42.20  ? 619 HOH   A O   1 
HETATM 3765 O O   . HOH   M 5 .   ? 11.758 54.896 9.179   1.00 31.01  ? 620 HOH   A O   1 
HETATM 3766 O O   . HOH   M 5 .   ? 17.994 28.927 -5.290  1.00 47.65  ? 621 HOH   A O   1 
HETATM 3767 O O   . HOH   M 5 .   ? 23.775 29.038 17.474  1.00 46.03  ? 622 HOH   A O   1 
HETATM 3768 O O   . HOH   M 5 .   ? 31.679 29.130 13.835  1.00 45.38  ? 623 HOH   A O   1 
HETATM 3769 O O   . HOH   M 5 .   ? 0.382  33.481 10.554  1.00 49.91  ? 624 HOH   A O   1 
HETATM 3770 O O   . HOH   M 5 .   ? 4.078  38.091 -8.524  1.00 46.34  ? 625 HOH   A O   1 
HETATM 3771 O O   . HOH   M 5 .   ? 29.121 31.583 -6.605  1.00 45.92  ? 626 HOH   A O   1 
HETATM 3772 O O   . HOH   M 5 .   ? 13.434 41.322 -20.908 1.00 45.35  ? 627 HOH   A O   1 
HETATM 3773 O O   . HOH   M 5 .   ? 8.601  54.080 -9.356  1.00 46.06  ? 628 HOH   A O   1 
HETATM 3774 O O   . HOH   M 5 .   ? 15.392 26.019 -2.264  1.00 48.79  ? 629 HOH   A O   1 
HETATM 3775 O O   . HOH   M 5 .   ? 11.391 46.428 14.962  1.00 46.56  ? 630 HOH   A O   1 
HETATM 3776 O O   . HOH   M 5 .   ? 19.851 50.900 -0.998  1.00 22.49  ? 631 HOH   A O   1 
HETATM 3777 O O   . HOH   M 5 .   ? 3.099  38.977 -2.537  1.00 34.81  ? 632 HOH   A O   1 
HETATM 3778 O O   . HOH   M 5 .   ? 8.493  55.131 17.959  1.00 38.74  ? 633 HOH   A O   1 
HETATM 3779 O O   . HOH   M 5 .   ? -2.803 36.402 9.133   1.00 49.66  ? 634 HOH   A O   1 
HETATM 3780 O O   . HOH   M 5 .   ? 1.719  51.693 -11.418 1.00 37.42  ? 635 HOH   A O   1 
HETATM 3781 O O   . HOH   M 5 .   ? 20.312 50.352 5.948   1.00 31.55  ? 636 HOH   A O   1 
HETATM 3782 O O   . HOH   M 5 .   ? 20.807 36.641 -19.252 1.00 44.94  ? 637 HOH   A O   1 
HETATM 3783 O O   . HOH   M 5 .   ? 27.800 45.908 12.594  1.00 49.50  ? 638 HOH   A O   1 
HETATM 3784 O O   . HOH   M 5 .   ? 26.885 47.321 18.079  1.00 55.25  ? 639 HOH   A O   1 
HETATM 3785 O O   . HOH   M 5 .   ? 15.258 31.083 9.463   1.00 30.88  ? 640 HOH   A O   1 
HETATM 3786 O O   . HOH   M 5 .   ? 23.839 29.469 0.138   1.00 59.21  ? 641 HOH   A O   1 
HETATM 3787 O O   . HOH   M 5 .   ? 10.792 56.927 7.895   1.00 46.57  ? 642 HOH   A O   1 
HETATM 3788 O O   . HOH   M 5 .   ? 0.879  51.810 10.053  1.00 45.37  ? 643 HOH   A O   1 
HETATM 3789 O O   . HOH   M 5 .   ? 3.930  45.792 -2.088  1.00 46.39  ? 644 HOH   A O   1 
HETATM 3790 O O   . HOH   M 5 .   ? 32.024 41.476 19.316  1.00 41.48  ? 645 HOH   A O   1 
HETATM 3791 O O   . HOH   M 5 .   ? 16.108 41.148 19.651  1.00 46.93  ? 646 HOH   A O   1 
HETATM 3792 O O   . HOH   M 5 .   ? 18.461 53.999 14.017  1.00 54.04  ? 647 HOH   A O   1 
HETATM 3793 O O   . HOH   M 5 .   ? 13.996 58.603 8.853   1.00 42.71  ? 648 HOH   A O   1 
HETATM 3794 O O   . HOH   M 5 .   ? 9.160  51.934 -23.814 1.00 53.12  ? 649 HOH   A O   1 
HETATM 3795 O O   . HOH   M 5 .   ? 10.867 55.558 16.621  1.00 38.23  ? 650 HOH   A O   1 
HETATM 3796 O O   . HOH   M 5 .   ? 22.505 35.963 -0.189  1.00 38.74  ? 651 HOH   A O   1 
HETATM 3797 O O   . HOH   M 5 .   ? 16.380 38.259 18.527  1.00 44.39  ? 652 HOH   A O   1 
HETATM 3798 O O   . HOH   M 5 .   ? 15.172 55.434 -6.968  1.00 52.52  ? 653 HOH   A O   1 
HETATM 3799 O O   . HOH   M 5 .   ? 11.207 33.416 5.171   1.00 34.69  ? 654 HOH   A O   1 
HETATM 3800 O O   . HOH   M 5 .   ? 36.142 45.756 13.093  1.00 34.54  ? 655 HOH   A O   1 
HETATM 3801 O O   . HOH   M 5 .   ? 22.524 55.472 3.148   1.00 47.96  ? 656 HOH   A O   1 
HETATM 3802 O O   . HOH   M 5 .   ? 19.290 24.886 0.717   1.00 61.15  ? 657 HOH   A O   1 
HETATM 3803 O O   . HOH   M 5 .   ? 23.729 47.853 -19.148 1.00 56.09  ? 658 HOH   A O   1 
HETATM 3804 O O   . HOH   M 5 .   ? 14.134 33.882 -19.025 1.00 56.12  ? 659 HOH   A O   1 
HETATM 3805 O O   . HOH   M 5 .   ? 22.703 52.960 3.623   1.00 39.53  ? 660 HOH   A O   1 
HETATM 3806 O O   . HOH   M 5 .   ? 14.967 51.056 -13.193 1.00 36.49  ? 661 HOH   A O   1 
HETATM 3807 O O   . HOH   M 5 .   ? 17.229 49.366 14.539  1.00 49.99  ? 662 HOH   A O   1 
HETATM 3808 O O   . HOH   M 5 .   ? 5.069  48.587 -6.636  1.00 43.38  ? 663 HOH   A O   1 
HETATM 3809 O O   . HOH   M 5 .   ? 14.709 53.831 15.863  1.00 43.29  ? 664 HOH   A O   1 
HETATM 3810 O O   . HOH   M 5 .   ? 10.779 43.170 21.330  1.00 54.09  ? 665 HOH   A O   1 
HETATM 3811 O O   . HOH   M 5 .   ? 17.995 44.066 -22.065 1.00 49.77  ? 666 HOH   A O   1 
HETATM 3812 O O   . HOH   M 5 .   ? 8.072  54.552 -18.127 1.00 46.20  ? 667 HOH   A O   1 
HETATM 3813 O O   . HOH   M 5 .   ? -1.423 35.657 2.021   1.00 54.73  ? 668 HOH   A O   1 
HETATM 3814 O O   . HOH   M 5 .   ? 18.069 35.123 -0.855  1.00 38.61  ? 669 HOH   A O   1 
HETATM 3815 O O   . HOH   M 5 .   ? 9.166  32.479 7.351   1.00 47.11  ? 670 HOH   A O   1 
HETATM 3816 O O   . HOH   M 5 .   ? 29.512 34.374 21.833  1.00 54.76  ? 671 HOH   A O   1 
HETATM 3817 O O   . HOH   M 5 .   ? 6.912  54.746 -0.288  1.00 49.38  ? 672 HOH   A O   1 
HETATM 3818 O O   . HOH   M 5 .   ? 4.444  29.490 3.548   1.00 50.65  ? 673 HOH   A O   1 
HETATM 3819 O O   . HOH   M 5 .   ? 2.756  39.965 -9.429  1.00 49.91  ? 674 HOH   A O   1 
HETATM 3820 O O   . HOH   M 5 .   ? 16.528 27.645 -9.357  1.00 38.81  ? 675 HOH   A O   1 
HETATM 3821 O O   . HOH   M 5 .   ? 20.593 33.979 -0.947  1.00 45.61  ? 676 HOH   A O   1 
HETATM 3822 O O   . HOH   M 5 .   ? 11.203 26.423 -3.558  1.00 41.20  ? 677 HOH   A O   1 
HETATM 3823 O O   . HOH   M 5 .   ? 0.135  35.825 8.928   1.00 46.73  ? 678 HOH   A O   1 
HETATM 3824 O O   . HOH   M 5 .   ? 40.195 36.710 11.718  1.00 50.30  ? 679 HOH   A O   1 
HETATM 3825 O O   . HOH   M 5 .   ? 24.302 53.569 10.609  1.00 49.50  ? 680 HOH   A O   1 
HETATM 3826 O O   . HOH   M 5 .   ? 17.352 48.498 -3.659  1.00 24.79  ? 681 HOH   A O   1 
HETATM 3827 O O   . HOH   M 5 .   ? 21.499 53.613 12.634  1.00 56.76  ? 682 HOH   A O   1 
HETATM 3828 O O   . HOH   M 5 .   ? 16.610 25.371 0.639   1.00 46.50  ? 683 HOH   A O   1 
HETATM 3829 O O   . HOH   M 5 .   ? 5.736  43.821 -23.209 1.00 49.41  ? 684 HOH   A O   1 
HETATM 3830 O O   . HOH   M 5 .   ? 1.305  41.123 -2.122  1.00 38.88  ? 685 HOH   A O   1 
HETATM 3831 O O   . HOH   M 5 .   ? 14.150 60.588 12.908  1.00 42.07  ? 686 HOH   A O   1 
HETATM 3832 O O   . HOH   M 5 .   ? 28.393 31.308 1.666   1.00 51.85  ? 687 HOH   A O   1 
HETATM 3833 O O   . HOH   M 5 .   ? 26.003 24.477 15.433  1.00 52.70  ? 688 HOH   A O   1 
HETATM 3834 O O   . HOH   M 5 .   ? 29.131 40.230 -4.174  1.00 50.79  ? 689 HOH   A O   1 
HETATM 3835 O O   . HOH   M 5 .   ? 33.459 32.027 20.474  1.00 53.05  ? 690 HOH   A O   1 
HETATM 3836 O O   . HOH   M 5 .   ? 23.840 64.377 14.771  1.00 58.24  ? 691 HOH   A O   1 
HETATM 3837 O O   . HOH   M 5 .   ? 17.934 48.862 12.084  1.00 42.59  ? 692 HOH   A O   1 
HETATM 3838 O O   . HOH   M 5 .   ? 15.756 26.868 11.494  1.00 51.61  ? 693 HOH   A O   1 
HETATM 3839 O O   . HOH   M 5 .   ? 19.704 54.232 -13.193 1.00 58.56  ? 694 HOH   A O   1 
HETATM 3840 O O   . HOH   M 5 .   ? 1.840  30.680 1.520   1.00 50.51  ? 695 HOH   A O   1 
HETATM 3841 O O   . HOH   M 5 .   ? -2.615 53.582 -18.172 1.00 55.57  ? 696 HOH   A O   1 
HETATM 3842 O O   . HOH   M 5 .   ? 10.232 56.743 1.406   1.00 51.10  ? 697 HOH   A O   1 
HETATM 3843 O O   . HOH   M 5 .   ? 5.816  55.245 -16.352 1.00 48.20  ? 698 HOH   A O   1 
HETATM 3844 O O   . HOH   M 5 .   ? 23.883 30.041 20.203  1.00 56.00  ? 699 HOH   A O   1 
HETATM 3845 O O   . HOH   M 5 .   ? -1.135 41.034 -2.744  1.00 53.18  ? 700 HOH   A O   1 
HETATM 3846 O O   . HOH   M 5 .   ? 31.351 31.399 3.932   1.00 55.29  ? 701 HOH   A O   1 
HETATM 3847 O O   . HOH   M 5 .   ? 30.912 32.353 1.035   1.00 55.61  ? 702 HOH   A O   1 
HETATM 3848 O O   . HOH   M 5 .   ? 9.955  53.187 19.746  1.00 47.65  ? 703 HOH   A O   1 
HETATM 3849 O O   . HOH   M 5 .   ? 12.679 54.244 17.817  1.00 48.19  ? 704 HOH   A O   1 
HETATM 3850 O O   . HOH   M 5 .   ? 11.129 30.408 11.387  1.00 49.44  ? 705 HOH   A O   1 
HETATM 3851 O O   . HOH   M 5 .   ? 32.587 33.275 5.649   1.00 56.72  ? 706 HOH   A O   1 
HETATM 3852 O O   . HOH   M 5 .   ? 10.475 31.104 9.011   1.00 46.72  ? 707 HOH   A O   1 
HETATM 3853 O O   . HOH   M 5 .   ? 18.990 36.583 -21.688 1.00 59.65  ? 708 HOH   A O   1 
HETATM 3854 O O   . HOH   M 5 .   ? 27.363 21.956 15.650  1.00 59.71  ? 709 HOH   A O   1 
HETATM 3855 O O   . HOH   M 5 .   ? 28.423 29.004 -6.847  1.00 45.68  ? 710 HOH   A O   1 
HETATM 3856 O O   . HOH   M 5 .   ? 12.595 33.890 21.472  1.00 52.89  ? 711 HOH   A O   1 
HETATM 3857 O O   . HOH   M 5 .   ? 18.763 52.509 12.102  1.00 51.13  ? 712 HOH   A O   1 
HETATM 3858 O O   . HOH   N 5 .   ? 58.058 53.451 21.121  1.00 36.52  ? 601 HOH   B O   1 
HETATM 3859 O O   . HOH   N 5 .   ? 28.815 70.982 16.866  1.00 46.38  ? 602 HOH   B O   1 
HETATM 3860 O O   . HOH   N 5 .   ? 33.287 55.229 27.905  1.00 42.71  ? 603 HOH   B O   1 
HETATM 3861 O O   . HOH   N 5 .   ? 33.504 78.139 23.823  1.00 51.10  ? 604 HOH   B O   1 
HETATM 3862 O O   . HOH   N 5 .   ? 38.202 56.623 -6.087  1.00 48.40  ? 605 HOH   B O   1 
HETATM 3863 O O   . HOH   N 5 .   ? 41.482 49.237 32.631  1.00 41.72  ? 606 HOH   B O   1 
HETATM 3864 O O   . HOH   N 5 .   ? 35.928 70.279 5.639   1.00 33.66  ? 607 HOH   B O   1 
HETATM 3865 O O   . HOH   N 5 .   ? 51.007 67.512 14.258  1.00 54.47  ? 608 HOH   B O   1 
HETATM 3866 O O   . HOH   N 5 .   ? 52.806 49.921 42.964  1.00 41.63  ? 609 HOH   B O   1 
HETATM 3867 O O   . HOH   N 5 .   ? 36.011 41.908 22.594  1.00 44.68  ? 610 HOH   B O   1 
HETATM 3868 O O   . HOH   N 5 .   ? 20.743 54.169 27.198  1.00 53.77  ? 611 HOH   B O   1 
HETATM 3869 O O   . HOH   N 5 .   ? 37.673 62.746 -4.677  1.00 38.64  ? 612 HOH   B O   1 
HETATM 3870 O O   . HOH   N 5 .   ? 25.184 67.466 23.979  1.00 34.20  ? 613 HOH   B O   1 
HETATM 3871 O O   . HOH   N 5 .   ? 40.752 51.058 -1.310  1.00 38.22  ? 614 HOH   B O   1 
HETATM 3872 O O   . HOH   N 5 .   ? 54.163 42.623 33.085  1.00 51.85  ? 615 HOH   B O   1 
HETATM 3873 O O   . HOH   N 5 .   ? 37.540 70.247 8.938   1.00 30.48  ? 616 HOH   B O   1 
HETATM 3874 O O   . HOH   N 5 .   ? 25.015 46.484 0.561   1.00 34.55  ? 617 HOH   B O   1 
HETATM 3875 O O   . HOH   N 5 .   ? 42.690 53.893 8.463   1.00 45.38  ? 618 HOH   B O   1 
HETATM 3876 O O   . HOH   N 5 .   ? 43.885 69.810 19.928  1.00 36.20  ? 619 HOH   B O   1 
HETATM 3877 O O   . HOH   N 5 .   ? 44.419 57.809 25.719  1.00 26.45  ? 620 HOH   B O   1 
HETATM 3878 O O   . HOH   N 5 .   ? 40.415 77.379 22.700  1.00 56.64  ? 621 HOH   B O   1 
HETATM 3879 O O   . HOH   N 5 .   ? 43.666 74.230 20.935  1.00 51.23  ? 622 HOH   B O   1 
HETATM 3880 O O   . HOH   N 5 .   ? 52.296 57.793 27.932  1.00 29.22  ? 623 HOH   B O   1 
HETATM 3881 O O   . HOH   N 5 .   ? 44.000 73.911 16.089  1.00 43.08  ? 624 HOH   B O   1 
HETATM 3882 O O   . HOH   N 5 .   ? 52.518 58.716 25.331  1.00 33.05  ? 625 HOH   B O   1 
HETATM 3883 O O   . HOH   N 5 .   ? 46.991 56.830 7.823   1.00 35.09  ? 626 HOH   B O   1 
HETATM 3884 O O   . HOH   N 5 .   ? 44.268 54.813 30.174  1.00 31.01  ? 627 HOH   B O   1 
HETATM 3885 O O   . HOH   N 5 .   ? 48.742 59.465 32.930  0.55 32.84  ? 628 HOH   B O   1 
HETATM 3886 O O   . HOH   N 5 .   ? 56.383 63.502 13.288  1.00 56.72  ? 629 HOH   B O   1 
HETATM 3887 O O   . HOH   N 5 .   ? 53.789 56.978 23.446  1.00 33.40  ? 630 HOH   B O   1 
HETATM 3888 O O   . HOH   N 5 .   ? 27.418 57.013 22.598  1.00 29.13  ? 631 HOH   B O   1 
HETATM 3889 O O   . HOH   N 5 .   ? 57.618 40.343 18.549  1.00 44.43  ? 632 HOH   B O   1 
HETATM 3890 O O   . HOH   N 5 .   ? 43.540 60.002 26.931  1.00 40.13  ? 633 HOH   B O   1 
HETATM 3891 O O   . HOH   N 5 .   ? 58.633 48.893 29.718  1.00 44.07  ? 634 HOH   B O   1 
HETATM 3892 O O   . HOH   N 5 .   ? 48.466 69.638 22.469  1.00 50.71  ? 635 HOH   B O   1 
HETATM 3893 O O   . HOH   N 5 .   ? 56.683 61.742 24.544  1.00 47.29  ? 636 HOH   B O   1 
HETATM 3894 O O   . HOH   N 5 .   ? 35.327 47.069 19.785  1.00 21.28  ? 637 HOH   B O   1 
HETATM 3895 O O   . HOH   N 5 .   ? 23.641 62.718 19.523  1.00 49.86  ? 638 HOH   B O   1 
HETATM 3896 O O   . HOH   N 5 .   ? 31.669 60.993 8.477   1.00 32.07  ? 639 HOH   B O   1 
HETATM 3897 O O   . HOH   N 5 .   ? 48.386 62.235 23.561  1.00 30.39  ? 640 HOH   B O   1 
HETATM 3898 O O   . HOH   N 5 .   ? 54.378 53.379 8.701   1.00 36.01  ? 641 HOH   B O   1 
HETATM 3899 O O   . HOH   N 5 .   ? 55.492 64.533 23.713  1.00 50.37  ? 642 HOH   B O   1 
HETATM 3900 O O   . HOH   N 5 .   ? 43.492 63.467 5.853   1.00 32.60  ? 643 HOH   B O   1 
HETATM 3901 O O   . HOH   N 5 .   ? 28.251 62.247 27.557  1.00 46.57  ? 644 HOH   B O   1 
HETATM 3902 O O   . HOH   N 5 .   ? 53.516 51.131 7.706   1.00 43.76  ? 645 HOH   B O   1 
HETATM 3903 O O   . HOH   N 5 .   ? 29.070 45.905 18.665  1.00 38.84  ? 646 HOH   B O   1 
HETATM 3904 O O   . HOH   N 5 .   ? 22.857 51.425 10.924  1.00 51.24  ? 647 HOH   B O   1 
HETATM 3905 O O   . HOH   N 5 .   ? 34.712 64.706 -4.748  1.00 49.79  ? 648 HOH   B O   1 
HETATM 3906 O O   . HOH   N 5 .   ? 44.839 50.283 8.211   1.00 38.76  ? 649 HOH   B O   1 
HETATM 3907 O O   . HOH   N 5 .   ? 50.147 69.082 24.480  1.00 50.81  ? 650 HOH   B O   1 
HETATM 3908 O O   . HOH   N 5 .   ? 30.044 59.789 -6.528  1.00 44.62  ? 651 HOH   B O   1 
HETATM 3909 O O   . HOH   N 5 .   ? 44.646 43.656 28.447  1.00 35.49  ? 652 HOH   B O   1 
HETATM 3910 O O   . HOH   N 5 .   ? 45.451 63.049 11.616  1.00 32.09  ? 653 HOH   B O   1 
HETATM 3911 O O   . HOH   N 5 .   ? 57.678 59.424 22.421  1.00 41.86  ? 654 HOH   B O   1 
HETATM 3912 O O   . HOH   N 5 .   ? 56.220 60.500 11.001  1.00 42.27  ? 655 HOH   B O   1 
HETATM 3913 O O   . HOH   N 5 .   ? 49.545 36.269 17.872  1.00 34.36  ? 656 HOH   B O   1 
HETATM 3914 O O   . HOH   N 5 .   ? 41.530 39.467 27.380  1.00 58.51  ? 657 HOH   B O   1 
HETATM 3915 O O   . HOH   N 5 .   ? 26.214 52.973 2.591   1.00 54.48  ? 658 HOH   B O   1 
HETATM 3916 O O   . HOH   N 5 .   ? 31.503 66.671 27.673  1.00 50.84  ? 659 HOH   B O   1 
HETATM 3917 O O   . HOH   N 5 .   ? 25.181 55.626 22.166  1.00 44.37  ? 660 HOH   B O   1 
HETATM 3918 O O   . HOH   N 5 .   ? 40.754 69.253 5.648   1.00 53.76  ? 661 HOH   B O   1 
HETATM 3919 O O   . HOH   N 5 .   ? 32.105 53.122 29.329  1.00 50.14  ? 662 HOH   B O   1 
HETATM 3920 O O   . HOH   N 5 .   ? 29.061 44.996 -6.242  1.00 50.09  ? 663 HOH   B O   1 
HETATM 3921 O O   . HOH   N 5 .   ? 55.331 58.276 7.330   1.00 51.16  ? 664 HOH   B O   1 
HETATM 3922 O O   . HOH   N 5 .   ? 39.552 48.128 21.102  1.00 25.06  ? 665 HOH   B O   1 
HETATM 3923 O O   . HOH   N 5 .   ? 28.015 55.111 3.225   1.00 44.54  ? 666 HOH   B O   1 
HETATM 3924 O O   . HOH   N 5 .   ? 47.211 47.430 38.639  1.00 42.24  ? 667 HOH   B O   1 
HETATM 3925 O O   . HOH   N 5 .   ? 27.915 54.928 11.583  1.00 39.28  ? 668 HOH   B O   1 
HETATM 3926 O O   . HOH   N 5 .   ? 31.527 64.153 5.956   1.00 43.13  ? 669 HOH   B O   1 
HETATM 3927 O O   . HOH   N 5 .   ? 45.443 65.544 11.312  1.00 44.12  ? 670 HOH   B O   1 
HETATM 3928 O O   . HOH   N 5 .   ? 43.534 72.120 18.972  1.00 41.60  ? 671 HOH   B O   1 
HETATM 3929 O O   . HOH   N 5 .   ? 47.928 65.409 7.456   1.00 56.86  ? 672 HOH   B O   1 
HETATM 3930 O O   . HOH   N 5 .   ? 32.464 66.246 4.161   1.00 50.17  ? 673 HOH   B O   1 
HETATM 3931 O O   . HOH   N 5 .   ? 45.152 75.708 19.312  1.00 52.43  ? 674 HOH   B O   1 
HETATM 3932 O O   . HOH   N 5 .   ? 53.217 58.989 5.157   1.00 41.27  ? 675 HOH   B O   1 
HETATM 3933 O O   . HOH   N 5 .   ? 26.185 61.749 0.986   1.00 58.06  ? 676 HOH   B O   1 
HETATM 3934 O O   . HOH   N 5 .   ? 48.077 63.783 27.847  1.00 39.77  ? 677 HOH   B O   1 
HETATM 3935 O O   . HOH   N 5 .   ? 29.277 64.515 6.989   1.00 45.24  ? 678 HOH   B O   1 
HETATM 3936 O O   . HOH   N 5 .   ? 29.072 56.753 14.267  1.00 35.12  ? 679 HOH   B O   1 
HETATM 3937 O O   . HOH   N 5 .   ? 27.983 52.941 5.003   1.00 45.38  ? 680 HOH   B O   1 
HETATM 3938 O O   . HOH   N 5 .   ? 36.473 50.774 31.918  1.00 50.49  ? 681 HOH   B O   1 
HETATM 3939 O O   . HOH   N 5 .   ? 54.753 38.345 26.122  1.00 49.73  ? 682 HOH   B O   1 
HETATM 3940 O O   . HOH   N 5 .   ? 58.121 54.601 13.497  1.00 42.95  ? 683 HOH   B O   1 
HETATM 3941 O O   . HOH   N 5 .   ? 48.366 66.141 27.324  1.00 45.49  ? 684 HOH   B O   1 
HETATM 3942 O O   . HOH   N 5 .   ? 46.807 53.685 10.853  1.00 39.32  ? 685 HOH   B O   1 
HETATM 3943 O O   . HOH   N 5 .   ? 26.911 62.711 5.741   1.00 49.75  ? 686 HOH   B O   1 
HETATM 3944 O O   . HOH   N 5 .   ? 43.983 51.155 36.655  1.00 44.68  ? 687 HOH   B O   1 
HETATM 3945 O O   . HOH   N 5 .   ? 46.959 52.177 8.341   1.00 51.36  ? 688 HOH   B O   1 
HETATM 3946 O O   . HOH   N 5 .   ? 51.988 68.465 17.814  1.00 50.61  ? 689 HOH   B O   1 
HETATM 3947 O O   . HOH   N 5 .   ? 27.616 45.385 21.033  1.00 51.74  ? 690 HOH   B O   1 
HETATM 3948 O O   . HOH   N 5 .   ? 58.296 52.829 10.782  1.00 44.13  ? 691 HOH   B O   1 
HETATM 3949 O O   . HOH   N 5 .   ? 60.707 54.320 19.787  1.00 52.73  ? 692 HOH   B O   1 
HETATM 3950 O O   . HOH   N 5 .   ? 48.005 65.067 30.408  1.00 51.75  ? 693 HOH   B O   1 
HETATM 3951 O O   . HOH   N 5 .   ? 37.678 55.568 -8.556  1.00 51.09  ? 694 HOH   B O   1 
HETATM 3952 O O   . HOH   N 5 .   ? 50.954 70.528 19.609  1.00 53.85  ? 695 HOH   B O   1 
HETATM 3953 O O   . HOH   N 5 .   ? 44.313 78.411 19.200  1.00 52.77  ? 696 HOH   B O   1 
HETATM 3954 O O   . HOH   N 5 .   ? 46.798 62.824 26.008  1.00 36.09  ? 697 HOH   B O   1 
HETATM 3955 O O   . HOH   N 5 .   ? 42.496 76.095 22.672  1.00 49.94  ? 698 HOH   B O   1 
HETATM 3956 O O   . HOH   N 5 .   ? 28.396 66.791 27.373  1.00 57.91  ? 699 HOH   B O   1 
HETATM 3957 O O   . HOH   N 5 .   ? 41.885 53.720 34.514  1.00 52.66  ? 700 HOH   B O   1 
HETATM 3958 O O   . HOH   N 5 .   ? 41.870 52.458 36.777  1.00 58.62  ? 701 HOH   B O   1 
HETATM 3959 O O   . HOH   N 5 .   ? 50.844 48.121 43.481  1.00 47.12  ? 702 HOH   B O   1 
HETATM 3960 O O   . HOH   N 5 .   ? 56.933 30.601 9.793   1.00 53.83  ? 703 HOH   B O   1 
HETATM 3961 O O   . HOH   N 5 .   ? 47.247 65.065 4.933   1.00 48.80  ? 704 HOH   B O   1 
HETATM 3962 O O   . HOH   N 5 .   ? 59.271 60.654 20.518  1.00 49.21  ? 705 HOH   B 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   . GLY   A 1   ? 0.4758 0.4757 0.4879 0.0215  -0.0098 -0.0343 207 GLY   A N   
2    C CA  . GLY   A 1   ? 0.4103 0.4164 0.4275 0.0238  -0.0062 -0.0377 207 GLY   A CA  
3    C C   . GLY   A 1   ? 0.5132 0.5234 0.5281 0.0217  -0.0012 -0.0372 207 GLY   A C   
4    O O   . GLY   A 1   ? 0.4557 0.4635 0.4656 0.0192  -0.0007 -0.0350 207 GLY   A O   
5    N N   . PRO   A 2   ? 0.4228 0.4392 0.4416 0.0226  0.0022  -0.0392 208 PRO   A N   
6    C CA  . PRO   A 2   ? 0.4300 0.4494 0.4465 0.0206  0.0063  -0.0385 208 PRO   A CA  
7    C C   . PRO   A 2   ? 0.4702 0.4894 0.4844 0.0178  0.0067  -0.0356 208 PRO   A C   
8    O O   . PRO   A 2   ? 0.4022 0.4218 0.4180 0.0174  0.0050  -0.0348 208 PRO   A O   
9    C CB  . PRO   A 2   ? 0.5069 0.5331 0.5285 0.0217  0.0093  -0.0409 208 PRO   A CB  
10   C CG  . PRO   A 2   ? 0.5396 0.5671 0.5668 0.0238  0.0069  -0.0425 208 PRO   A CG  
11   C CD  . PRO   A 2   ? 0.5347 0.5556 0.5603 0.0253  0.0022  -0.0423 208 PRO   A CD  
12   N N   . ARG   A 3   ? 0.4282 0.4467 0.4387 0.0160  0.0084  -0.0344 209 ARG   A N   
13   C CA  . ARG   A 3   ? 0.4216 0.4401 0.4304 0.0136  0.0088  -0.0324 209 ARG   A CA  
14   C C   . ARG   A 3   ? 0.3890 0.4118 0.4013 0.0129  0.0108  -0.0323 209 ARG   A C   
15   O O   . ARG   A 3   ? 0.3829 0.4064 0.3960 0.0118  0.0102  -0.0317 209 ARG   A O   
16   C CB  . ARG   A 3   ? 0.3695 0.3862 0.3744 0.0123  0.0096  -0.0315 209 ARG   A CB  
17   C CG  . ARG   A 3   ? 0.4367 0.4539 0.4408 0.0102  0.0098  -0.0303 209 ARG   A CG  
18   C CD  . ARG   A 3   ? 0.4118 0.4283 0.4136 0.0093  0.0106  -0.0299 209 ARG   A CD  
19   N NE  . ARG   A 3   ? 0.4076 0.4255 0.4103 0.0078  0.0109  -0.0295 209 ARG   A NE  
20   C CZ  . ARG   A 3   ? 0.4692 0.4884 0.4733 0.0075  0.0120  -0.0292 209 ARG   A CZ  
21   N NH1 . ARG   A 3   ? 0.4673 0.4864 0.4709 0.0081  0.0130  -0.0288 209 ARG   A NH1 
22   N NH2 . ARG   A 3   ? 0.5818 0.6022 0.5876 0.0065  0.0118  -0.0295 209 ARG   A NH2 
23   N N   . SER   A 4   ? 0.3841 0.4098 0.3980 0.0133  0.0132  -0.0331 210 SER   A N   
24   C CA  . SER   A 4   ? 0.3879 0.4168 0.4044 0.0119  0.0151  -0.0324 210 SER   A CA  
25   C C   . SER   A 4   ? 0.4067 0.4401 0.4274 0.0127  0.0167  -0.0339 210 SER   A C   
26   O O   . SER   A 4   ? 0.3932 0.4277 0.4150 0.0146  0.0166  -0.0359 210 SER   A O   
27   C CB  . SER   A 4   ? 0.3496 0.3775 0.3630 0.0104  0.0165  -0.0309 210 SER   A CB  
28   O OG  . SER   A 4   ? 0.5246 0.5533 0.5360 0.0109  0.0180  -0.0315 210 SER   A OG  
29   N N   . ILE   A 5   ? 0.3789 0.4153 0.4026 0.0111  0.0181  -0.0332 211 ILE   A N   
30   C CA  . ILE   A 5   ? 0.3119 0.3537 0.3404 0.0110  0.0199  -0.0345 211 ILE   A CA  
31   C C   . ILE   A 5   ? 0.3826 0.4261 0.4101 0.0083  0.0227  -0.0327 211 ILE   A C   
32   O O   . ILE   A 5   ? 0.3636 0.4050 0.3907 0.0064  0.0221  -0.0306 211 ILE   A O   
33   C CB  . ILE   A 5   ? 0.3581 0.4019 0.3919 0.0110  0.0185  -0.0351 211 ILE   A CB  
34   C CG1 . ILE   A 5   ? 0.3088 0.3500 0.3425 0.0132  0.0151  -0.0360 211 ILE   A CG1 
35   C CG2 . ILE   A 5   ? 0.3258 0.3760 0.3654 0.0107  0.0205  -0.0366 211 ILE   A CG2 
36   C CD1 . ILE   A 5   ? 0.3419 0.3844 0.3793 0.0128  0.0132  -0.0362 211 ILE   A CD1 
37   N N   . GLY   A 6   ? 0.3571 0.4044 0.3841 0.0079  0.0253  -0.0337 212 GLY   A N   
38   C CA  . GLY   A 6   ? 0.3540 0.4037 0.3802 0.0046  0.0279  -0.0317 212 GLY   A CA  
39   C C   . GLY   A 6   ? 0.3904 0.4421 0.4121 0.0040  0.0304  -0.0322 212 GLY   A C   
40   O O   . GLY   A 6   ? 0.4911 0.5446 0.5126 0.0064  0.0309  -0.0352 212 GLY   A O   
41   N N   . THR   A 7   ? 0.4113 0.4625 0.4292 0.0007  0.0317  -0.0291 213 THR   A N   
42   C CA  . THR   A 7   ? 0.4734 0.5271 0.4861 -0.0010 0.0343  -0.0290 213 THR   A CA  
43   C C   . THR   A 7   ? 0.4748 0.5223 0.4804 -0.0012 0.0325  -0.0266 213 THR   A C   
44   O O   . THR   A 7   ? 0.4728 0.5148 0.4782 0.0002  0.0295  -0.0256 213 THR   A O   
45   C CB  . THR   A 7   ? 0.4715 0.5297 0.4843 -0.0054 0.0372  -0.0268 213 THR   A CB  
46   O OG1 . THR   A 7   ? 0.4715 0.5241 0.4817 -0.0082 0.0352  -0.0220 213 THR   A OG1 
47   C CG2 . THR   A 7   ? 0.4957 0.5598 0.5166 -0.0056 0.0385  -0.0288 213 THR   A CG2 
48   N N   . THR   A 8   ? 0.4925 0.5417 0.4923 -0.0034 0.0344  -0.0257 214 THR   A N   
49   C CA  . THR   A 8   ? 0.5300 0.5736 0.5231 -0.0039 0.0324  -0.0233 214 THR   A CA  
50   C C   . THR   A 8   ? 0.5006 0.5394 0.4931 -0.0064 0.0301  -0.0185 214 THR   A C   
51   O O   . THR   A 8   ? 0.6222 0.6554 0.6121 -0.0057 0.0271  -0.0168 214 THR   A O   
52   C CB  . THR   A 8   ? 0.5947 0.6416 0.5811 -0.0055 0.0348  -0.0239 214 THR   A CB  
53   O OG1 . THR   A 8   ? 0.7449 0.7863 0.7248 -0.0060 0.0323  -0.0214 214 THR   A OG1 
54   C CG2 . THR   A 8   ? 0.6121 0.6642 0.5972 -0.0101 0.0380  -0.0218 214 THR   A CG2 
55   N N   . LYS   A 9   ? 0.3916 0.4323 0.3871 -0.0093 0.0311  -0.0164 215 LYS   A N   
56   C CA  . LYS   A 9   ? 0.4166 0.4521 0.4123 -0.0117 0.0284  -0.0121 215 LYS   A CA  
57   C C   . LYS   A 9   ? 0.4837 0.5156 0.4856 -0.0093 0.0255  -0.0128 215 LYS   A C   
58   O O   . LYS   A 9   ? 0.4021 0.4284 0.4040 -0.0097 0.0223  -0.0104 215 LYS   A O   
59   C CB  . LYS   A 9   ? 0.3773 0.4159 0.3737 -0.0164 0.0305  -0.0094 215 LYS   A CB  
60   C CG  . LYS   A 9   ? 0.6172 0.6585 0.6060 -0.0203 0.0329  -0.0071 215 LYS   A CG  
61   C CD  . LYS   A 9   ? 0.5914 0.6357 0.5811 -0.0257 0.0348  -0.0039 215 LYS   A CD  
62   C CE  . LYS   A 9   ? 0.7287 0.7804 0.7126 -0.0294 0.0394  -0.0041 215 LYS   A CE  
63   N NZ  . LYS   A 9   ? 0.8094 0.8606 0.7893 -0.0361 0.0399  0.0016  215 LYS   A NZ  
64   N N   . LEU   A 10  ? 0.3798 0.4148 0.3870 -0.0069 0.0264  -0.0163 216 LEU   A N   
65   C CA  . LEU   A 10  ? 0.4212 0.4536 0.4336 -0.0051 0.0239  -0.0172 216 LEU   A CA  
66   C C   . LEU   A 10  ? 0.3822 0.4172 0.3974 -0.0019 0.0243  -0.0211 216 LEU   A C   
67   O O   . LEU   A 10  ? 0.3821 0.4222 0.3995 -0.0017 0.0265  -0.0230 216 LEU   A O   
68   C CB  . LEU   A 10  ? 0.3684 0.4010 0.3856 -0.0075 0.0235  -0.0157 216 LEU   A CB  
69   C CG  . LEU   A 10  ? 0.3577 0.3871 0.3796 -0.0058 0.0206  -0.0168 216 LEU   A CG  
70   C CD1 . LEU   A 10  ? 0.3688 0.3921 0.3894 -0.0064 0.0175  -0.0145 216 LEU   A CD1 
71   C CD2 . LEU   A 10  ? 0.3972 0.4287 0.4249 -0.0072 0.0208  -0.0173 216 LEU   A CD2 
72   N N   . ARG   A 11  ? 0.3150 0.3468 0.3306 0.0004  0.0219  -0.0222 217 ARG   A N   
73   C CA  . ARG   A 11  ? 0.3900 0.4231 0.4076 0.0030  0.0215  -0.0251 217 ARG   A CA  
74   C C   . ARG   A 11  ? 0.3821 0.4134 0.4029 0.0036  0.0193  -0.0257 217 ARG   A C   
75   O O   . ARG   A 11  ? 0.3247 0.3529 0.3449 0.0033  0.0177  -0.0249 217 ARG   A O   
76   C CB  . ARG   A 11  ? 0.4010 0.4322 0.4143 0.0049  0.0210  -0.0261 217 ARG   A CB  
77   C CG  . ARG   A 11  ? 0.5640 0.5974 0.5742 0.0050  0.0231  -0.0268 217 ARG   A CG  
78   C CD  . ARG   A 11  ? 0.6702 0.7002 0.6756 0.0062  0.0219  -0.0272 217 ARG   A CD  
79   N NE  . ARG   A 11  ? 0.8678 0.8985 0.8684 0.0052  0.0233  -0.0266 217 ARG   A NE  
80   C CZ  . ARG   A 11  ? 1.0048 1.0334 1.0019 0.0032  0.0228  -0.0238 217 ARG   A CZ  
81   N NH1 . ARG   A 11  ? 0.8628 0.8885 0.8616 0.0023  0.0208  -0.0217 217 ARG   A NH1 
82   N NH2 . ARG   A 11  ? 0.9649 0.9943 0.9568 0.0022  0.0239  -0.0235 217 ARG   A NH2 
83   N N   . LEU   A 12  ? 0.3411 0.3749 0.3655 0.0045  0.0191  -0.0274 218 LEU   A N   
84   C CA  . LEU   A 12  ? 0.2428 0.2756 0.2691 0.0051  0.0171  -0.0286 218 LEU   A CA  
85   C C   . LEU   A 12  ? 0.3471 0.3779 0.3697 0.0067  0.0159  -0.0294 218 LEU   A C   
86   O O   . LEU   A 12  ? 0.3128 0.3444 0.3347 0.0081  0.0160  -0.0303 218 LEU   A O   
87   C CB  . LEU   A 12  ? 0.2897 0.3258 0.3206 0.0053  0.0169  -0.0299 218 LEU   A CB  
88   C CG  . LEU   A 12  ? 0.2899 0.3255 0.3220 0.0059  0.0147  -0.0313 218 LEU   A CG  
89   C CD1 . LEU   A 12  ? 0.3060 0.3400 0.3394 0.0045  0.0138  -0.0312 218 LEU   A CD1 
90   C CD2 . LEU   A 12  ? 0.3410 0.3800 0.3772 0.0064  0.0140  -0.0327 218 LEU   A CD2 
91   N N   . VAL   A 13  ? 0.2697 0.2981 0.2905 0.0065  0.0148  -0.0292 219 VAL   A N   
92   C CA  . VAL   A 13  ? 0.3140 0.3406 0.3310 0.0073  0.0139  -0.0297 219 VAL   A CA  
93   C C   . VAL   A 13  ? 0.3731 0.3999 0.3902 0.0070  0.0124  -0.0307 219 VAL   A C   
94   O O   . VAL   A 13  ? 0.4150 0.4406 0.4290 0.0072  0.0115  -0.0308 219 VAL   A O   
95   C CB  . VAL   A 13  ? 0.3520 0.3764 0.3662 0.0069  0.0139  -0.0289 219 VAL   A CB  
96   C CG1 . VAL   A 13  ? 0.3329 0.3571 0.3456 0.0069  0.0152  -0.0276 219 VAL   A CG1 
97   C CG2 . VAL   A 13  ? 0.3424 0.3667 0.3589 0.0061  0.0132  -0.0291 219 VAL   A CG2 
98   N N   . GLU   A 14  ? 0.3262 0.3545 0.3464 0.0063  0.0121  -0.0316 220 GLU   A N   
99   C CA  . GLU   A 14  ? 0.3629 0.3921 0.3826 0.0057  0.0109  -0.0329 220 GLU   A CA  
100  C C   . GLU   A 14  ? 0.3480 0.3794 0.3717 0.0054  0.0104  -0.0340 220 GLU   A C   
101  O O   . GLU   A 14  ? 0.3572 0.3889 0.3846 0.0051  0.0110  -0.0339 220 GLU   A O   
102  C CB  . GLU   A 14  ? 0.3767 0.4058 0.3957 0.0049  0.0109  -0.0339 220 GLU   A CB  
103  C CG  . GLU   A 14  ? 0.6256 0.6561 0.6418 0.0037  0.0102  -0.0351 220 GLU   A CG  
104  C CD  . GLU   A 14  ? 0.8248 0.8567 0.8413 0.0030  0.0107  -0.0369 220 GLU   A CD  
105  O OE1 . GLU   A 14  ? 0.8441 0.8755 0.8639 0.0037  0.0109  -0.0373 220 GLU   A OE1 
106  O OE2 . GLU   A 14  ? 0.8345 0.8682 0.8483 0.0014  0.0106  -0.0379 220 GLU   A OE2 
107  N N   . PHE   A 15  ? 0.3409 0.3733 0.3637 0.0051  0.0090  -0.0347 221 PHE   A N   
108  C CA  . PHE   A 15  ? 0.3170 0.3516 0.3435 0.0048  0.0082  -0.0360 221 PHE   A CA  
109  C C   . PHE   A 15  ? 0.4522 0.4877 0.4757 0.0041  0.0063  -0.0368 221 PHE   A C   
110  O O   . PHE   A 15  ? 0.3856 0.4196 0.4053 0.0043  0.0053  -0.0355 221 PHE   A O   
111  C CB  . PHE   A 15  ? 0.3669 0.4027 0.3973 0.0056  0.0084  -0.0354 221 PHE   A CB  
112  C CG  . PHE   A 15  ? 0.4015 0.4397 0.4351 0.0053  0.0069  -0.0367 221 PHE   A CG  
113  C CD1 . PHE   A 15  ? 0.3754 0.4148 0.4123 0.0042  0.0067  -0.0382 221 PHE   A CD1 
114  C CD2 . PHE   A 15  ? 0.4095 0.4484 0.4425 0.0062  0.0049  -0.0366 221 PHE   A CD2 
115  C CE1 . PHE   A 15  ? 0.3921 0.4338 0.4319 0.0038  0.0050  -0.0397 221 PHE   A CE1 
116  C CE2 . PHE   A 15  ? 0.3880 0.4292 0.4240 0.0059  0.0030  -0.0379 221 PHE   A CE2 
117  C CZ  . PHE   A 15  ? 0.3611 0.4039 0.4002 0.0046  0.0032  -0.0395 221 PHE   A CZ  
118  N N   . SER   A 16  ? 0.3573 0.3949 0.3824 0.0031  0.0057  -0.0389 222 SER   A N   
119  C CA  . SER   A 16  ? 0.3184 0.3573 0.3406 0.0021  0.0037  -0.0396 222 SER   A CA  
120  C C   . SER   A 16  ? 0.3491 0.3907 0.3749 0.0014  0.0030  -0.0423 222 SER   A C   
121  O O   . SER   A 16  ? 0.3088 0.3509 0.3386 0.0014  0.0041  -0.0441 222 SER   A O   
122  C CB  . SER   A 16  ? 0.3862 0.4249 0.4021 0.0005  0.0037  -0.0395 222 SER   A CB  
123  O OG  . SER   A 16  ? 0.4462 0.4875 0.4626 -0.0007 0.0049  -0.0423 222 SER   A OG  
124  N N   . ALA   A 17  ? 0.2524 0.2954 0.2772 0.0009  0.0007  -0.0427 223 ALA   A N   
125  C CA  . ALA   A 17  ? 0.3088 0.3544 0.3357 -0.0001 -0.0004 -0.0456 223 ALA   A CA  
126  C C   . ALA   A 17  ? 0.3265 0.3734 0.3464 -0.0019 -0.0019 -0.0462 223 ALA   A C   
127  O O   . ALA   A 17  ? 0.3282 0.3735 0.3435 -0.0022 -0.0037 -0.0435 223 ALA   A O   
128  C CB  . ALA   A 17  ? 0.2520 0.2986 0.2841 0.0007  -0.0021 -0.0455 223 ALA   A CB  
129  N N   . PHE   A 18  ? 0.2647 0.3144 0.2836 -0.0034 -0.0012 -0.0496 224 PHE   A N   
130  C CA  . PHE   A 18  ? 0.3110 0.3626 0.3222 -0.0059 -0.0014 -0.0501 224 PHE   A CA  
131  C C   . PHE   A 18  ? 0.3194 0.3754 0.3301 -0.0075 -0.0019 -0.0546 224 PHE   A C   
132  O O   . PHE   A 18  ? 0.3113 0.3685 0.3284 -0.0065 -0.0018 -0.0577 224 PHE   A O   
133  C CB  . PHE   A 18  ? 0.3119 0.3632 0.3208 -0.0064 0.0012  -0.0498 224 PHE   A CB  
134  C CG  . PHE   A 18  ? 0.2987 0.3516 0.3136 -0.0053 0.0035  -0.0532 224 PHE   A CG  
135  C CD1 . PHE   A 18  ? 0.3871 0.4444 0.4025 -0.0065 0.0044  -0.0581 224 PHE   A CD1 
136  C CD2 . PHE   A 18  ? 0.3534 0.4031 0.3735 -0.0031 0.0044  -0.0517 224 PHE   A CD2 
137  C CE1 . PHE   A 18  ? 0.4146 0.4727 0.4365 -0.0051 0.0057  -0.0615 224 PHE   A CE1 
138  C CE2 . PHE   A 18  ? 0.3460 0.3961 0.3716 -0.0021 0.0057  -0.0544 224 PHE   A CE2 
139  C CZ  . PHE   A 18  ? 0.3868 0.4409 0.4137 -0.0029 0.0061  -0.0593 224 PHE   A CZ  
140  N N   . LEU   A 19  ? 0.3410 0.3994 0.3438 -0.0104 -0.0023 -0.0549 225 LEU   A N   
141  C CA  . LEU   A 19  ? 0.3234 0.3869 0.3240 -0.0125 -0.0023 -0.0596 225 LEU   A CA  
142  C C   . LEU   A 19  ? 0.3550 0.4222 0.3497 -0.0152 0.0003  -0.0611 225 LEU   A C   
143  O O   . LEU   A 19  ? 0.3517 0.4176 0.3390 -0.0174 0.0000  -0.0573 225 LEU   A O   
144  C CB  . LEU   A 19  ? 0.2628 0.3268 0.2583 -0.0141 -0.0059 -0.0586 225 LEU   A CB  
145  C CG  . LEU   A 19  ? 0.3381 0.4078 0.3276 -0.0174 -0.0061 -0.0627 225 LEU   A CG  
146  C CD1 . LEU   A 19  ? 0.2909 0.3643 0.2874 -0.0163 -0.0048 -0.0694 225 LEU   A CD1 
147  C CD2 . LEU   A 19  ? 0.3252 0.3942 0.3079 -0.0193 -0.0105 -0.0601 225 LEU   A CD2 
148  N N   . GLU   A 20  ? 0.2952 0.3668 0.2938 -0.0150 0.0028  -0.0667 226 GLU   A N   
149  C CA  . GLU   A 20  ? 0.3929 0.4701 0.3870 -0.0178 0.0056  -0.0697 226 GLU   A CA  
150  C C   . GLU   A 20  ? 0.3643 0.4479 0.3545 -0.0205 0.0054  -0.0747 226 GLU   A C   
151  O O   . GLU   A 20  ? 0.3301 0.4149 0.3257 -0.0189 0.0045  -0.0792 226 GLU   A O   
152  C CB  . GLU   A 20  ? 0.3731 0.4519 0.3749 -0.0156 0.0084  -0.0735 226 GLU   A CB  
153  C CG  . GLU   A 20  ? 0.4950 0.5680 0.5011 -0.0130 0.0086  -0.0692 226 GLU   A CG  
154  C CD  . GLU   A 20  ? 0.5562 0.6304 0.5705 -0.0106 0.0104  -0.0731 226 GLU   A CD  
155  O OE1 . GLU   A 20  ? 0.5999 0.6752 0.6210 -0.0088 0.0098  -0.0778 226 GLU   A OE1 
156  O OE2 . GLU   A 20  ? 0.7098 0.7835 0.7242 -0.0104 0.0119  -0.0716 226 GLU   A OE2 
157  N N   . GLN   A 21  ? 0.3854 0.4730 0.3657 -0.0249 0.0062  -0.0741 227 GLN   A N   
158  C CA  . GLN   A 21  ? 0.3674 0.4618 0.3420 -0.0283 0.0063  -0.0787 227 GLN   A CA  
159  C C   . GLN   A 21  ? 0.4100 0.5124 0.3804 -0.0318 0.0104  -0.0824 227 GLN   A C   
160  O O   . GLN   A 21  ? 0.3680 0.4696 0.3343 -0.0338 0.0118  -0.0784 227 GLN   A O   
161  C CB  . GLN   A 21  ? 0.4084 0.5004 0.3731 -0.0312 0.0026  -0.0737 227 GLN   A CB  
162  C CG  . GLN   A 21  ? 0.4693 0.5555 0.4387 -0.0280 -0.0016 -0.0715 227 GLN   A CG  
163  C CD  . GLN   A 21  ? 0.5008 0.5848 0.4610 -0.0306 -0.0059 -0.0670 227 GLN   A CD  
164  O OE1 . GLN   A 21  ? 0.5887 0.6759 0.5458 -0.0322 -0.0079 -0.0699 227 GLN   A OE1 
165  N NE2 . GLN   A 21  ? 0.4421 0.5204 0.3978 -0.0312 -0.0078 -0.0600 227 GLN   A NE2 
166  N N   . GLN   A 22  ? 0.4721 0.5825 0.4439 -0.0327 0.0123  -0.0904 228 GLN   A N   
167  C CA  . GLN   A 22  ? 0.5082 0.6283 0.4760 -0.0366 0.0165  -0.0952 228 GLN   A CA  
168  C C   . GLN   A 22  ? 0.5647 0.6904 0.5206 -0.0420 0.0160  -0.0962 228 GLN   A C   
169  O O   . GLN   A 22  ? 0.5244 0.6540 0.4816 -0.0416 0.0152  -0.1021 228 GLN   A O   
170  C CB  . GLN   A 22  ? 0.6254 0.7517 0.6042 -0.0334 0.0192  -0.1047 228 GLN   A CB  
171  C CG  . GLN   A 22  ? 0.6215 0.7467 0.6088 -0.0305 0.0213  -0.1047 228 GLN   A CG  
172  C CD  . GLN   A 22  ? 0.5831 0.7194 0.5733 -0.0319 0.0256  -0.1130 228 GLN   A CD  
173  O OE1 . GLN   A 22  ? 0.7021 0.8453 0.6956 -0.0316 0.0265  -0.1215 228 GLN   A OE1 
174  N NE2 . GLN   A 22  ? 0.6744 0.8131 0.6637 -0.0336 0.0283  -0.1110 228 GLN   A NE2 
175  N N   . ARG   A 23  ? 0.6241 0.7499 0.5684 -0.0473 0.0161  -0.0903 229 ARG   A N   
176  C CA  . ARG   A 23  ? 0.8505 0.9819 0.7818 -0.0535 0.0157  -0.0907 229 ARG   A CA  
177  C C   . ARG   A 23  ? 0.8354 0.9801 0.7669 -0.0561 0.0206  -0.1006 229 ARG   A C   
178  O O   . ARG   A 23  ? 0.8398 0.9901 0.7679 -0.0576 0.0202  -0.1060 229 ARG   A O   
179  C CB  . ARG   A 23  ? 0.9735 1.1016 0.8925 -0.0590 0.0146  -0.0818 229 ARG   A CB  
180  C CG  . ARG   A 23  ? 1.1163 1.2508 1.0204 -0.0666 0.0146  -0.0816 229 ARG   A CG  
181  C CD  . ARG   A 23  ? 1.2721 1.3984 1.1641 -0.0709 0.0102  -0.0708 229 ARG   A CD  
182  N NE  . ARG   A 23  ? 1.3130 1.4303 1.2042 -0.0681 0.0037  -0.0663 229 ARG   A NE  
183  C CZ  . ARG   A 23  ? 1.2437 1.3631 1.1300 -0.0692 0.0008  -0.0685 229 ARG   A CZ  
184  N NH1 . ARG   A 23  ? 1.2125 1.3427 1.0928 -0.0735 0.0038  -0.0751 229 ARG   A NH1 
185  N NH2 . ARG   A 23  ? 1.1461 1.2571 1.0338 -0.0660 -0.0052 -0.0643 229 ARG   A NH2 
186  N N   . ASP   A 24  ? 0.7006 0.8509 0.6368 -0.0563 0.0252  -0.1038 230 ASP   A N   
187  C CA  . ASP   A 24  ? 0.7767 0.9408 0.7137 -0.0589 0.0303  -0.1136 230 ASP   A CA  
188  C C   . ASP   A 24  ? 0.5953 0.7621 0.5463 -0.0543 0.0335  -0.1189 230 ASP   A C   
189  O O   . ASP   A 24  ? 0.4988 0.6561 0.4575 -0.0495 0.0315  -0.1143 230 ASP   A O   
190  C CB  . ASP   A 24  ? 0.6357 0.8067 0.5576 -0.0677 0.0328  -0.1108 230 ASP   A CB  
191  C CG  . ASP   A 24  ? 0.7543 0.9213 0.6736 -0.0701 0.0337  -0.1031 230 ASP   A CG  
192  O OD1 . ASP   A 24  ? 0.7558 0.9254 0.6851 -0.0673 0.0368  -0.1062 230 ASP   A OD1 
193  O OD2 . ASP   A 24  ? 0.9126 1.0732 0.8202 -0.0744 0.0307  -0.0939 230 ASP   A OD2 
194  N N   . PRO   A 25  ? 0.5964 0.7758 0.5518 -0.0553 0.0382  -0.1287 231 PRO   A N   
195  C CA  . PRO   A 25  ? 0.5690 0.7501 0.5399 -0.0496 0.0400  -0.1344 231 PRO   A CA  
196  C C   . PRO   A 25  ? 0.5041 0.6805 0.4773 -0.0492 0.0407  -0.1279 231 PRO   A C   
197  O O   . PRO   A 25  ? 0.5437 0.7170 0.5294 -0.0435 0.0403  -0.1300 231 PRO   A O   
198  C CB  . PRO   A 25  ? 0.6688 0.8660 0.6420 -0.0519 0.0451  -0.1463 231 PRO   A CB  
199  C CG  . PRO   A 25  ? 0.6900 0.8923 0.6518 -0.0566 0.0449  -0.1485 231 PRO   A CG  
200  C CD  . PRO   A 25  ? 0.6818 0.8747 0.6297 -0.0608 0.0416  -0.1362 231 PRO   A CD  
201  N N   . ASP   A 26  ? 0.4000 0.5756 0.3615 -0.0552 0.0415  -0.1202 232 ASP   A N   
202  C CA  . ASP   A 26  ? 0.3950 0.5671 0.3587 -0.0553 0.0423  -0.1147 232 ASP   A CA  
203  C C   . ASP   A 26  ? 0.3641 0.5225 0.3210 -0.0556 0.0382  -0.1029 232 ASP   A C   
204  O O   . ASP   A 26  ? 0.4037 0.5591 0.3593 -0.0572 0.0387  -0.0975 232 ASP   A O   
205  C CB  . ASP   A 26  ? 0.3588 0.5429 0.3169 -0.0623 0.0475  -0.1169 232 ASP   A CB  
206  C CG  . ASP   A 26  ? 0.3692 0.5681 0.3350 -0.0619 0.0520  -0.1295 232 ASP   A CG  
207  O OD1 . ASP   A 26  ? 0.4235 0.6227 0.4036 -0.0554 0.0519  -0.1354 232 ASP   A OD1 
208  O OD2 . ASP   A 26  ? 0.3804 0.5905 0.3379 -0.0681 0.0554  -0.1335 232 ASP   A OD2 
209  N N   . SER   A 27  ? 0.4508 0.6012 0.4038 -0.0541 0.0339  -0.0990 233 SER   A N   
210  C CA  . SER   A 27  ? 0.3969 0.5351 0.3437 -0.0543 0.0297  -0.0885 233 SER   A CA  
211  C C   . SER   A 27  ? 0.4302 0.5588 0.3851 -0.0474 0.0257  -0.0871 233 SER   A C   
212  O O   . SER   A 27  ? 0.5137 0.6444 0.4743 -0.0443 0.0252  -0.0930 233 SER   A O   
213  C CB  . SER   A 27  ? 0.4918 0.6296 0.4236 -0.0606 0.0276  -0.0837 233 SER   A CB  
214  O OG  . SER   A 27  ? 0.6605 0.8089 0.5841 -0.0678 0.0316  -0.0860 233 SER   A OG  
215  N N   . TYR   A 28  ? 0.3604 0.4785 0.3151 -0.0455 0.0229  -0.0793 234 TYR   A N   
216  C CA  . TYR   A 28  ? 0.4287 0.5381 0.3919 -0.0392 0.0198  -0.0775 234 TYR   A CA  
217  C C   . TYR   A 28  ? 0.4432 0.5426 0.4003 -0.0397 0.0161  -0.0682 234 TYR   A C   
218  O O   . TYR   A 28  ? 0.3665 0.4642 0.3180 -0.0428 0.0165  -0.0635 234 TYR   A O   
219  C CB  . TYR   A 28  ? 0.4957 0.6053 0.4704 -0.0348 0.0219  -0.0805 234 TYR   A CB  
220  C CG  . TYR   A 28  ? 0.4468 0.5469 0.4291 -0.0293 0.0194  -0.0769 234 TYR   A CG  
221  C CD1 . TYR   A 28  ? 0.5286 0.6217 0.5091 -0.0289 0.0184  -0.0701 234 TYR   A CD1 
222  C CD2 . TYR   A 28  ? 0.6386 0.7371 0.6300 -0.0247 0.0183  -0.0807 234 TYR   A CD2 
223  C CE1 . TYR   A 28  ? 0.4970 0.5825 0.4839 -0.0242 0.0166  -0.0673 234 TYR   A CE1 
224  C CE2 . TYR   A 28  ? 0.6233 0.7138 0.6209 -0.0203 0.0163  -0.0773 234 TYR   A CE2 
225  C CZ  . TYR   A 28  ? 0.6079 0.6923 0.6031 -0.0202 0.0157  -0.0707 234 TYR   A CZ  
226  O OH  . TYR   A 28  ? 0.6923 0.7697 0.6933 -0.0162 0.0141  -0.0677 234 TYR   A OH  
227  N N   . ASN   A 29  ? 0.4217 0.5152 0.3797 -0.0370 0.0123  -0.0660 235 ASN   A N   
228  C CA  . ASN   A 29  ? 0.3984 0.4823 0.3536 -0.0359 0.0083  -0.0583 235 ASN   A CA  
229  C C   . ASN   A 29  ? 0.4132 0.4916 0.3790 -0.0297 0.0070  -0.0583 235 ASN   A C   
230  O O   . ASN   A 29  ? 0.3832 0.4639 0.3558 -0.0271 0.0074  -0.0632 235 ASN   A O   
231  C CB  . ASN   A 29  ? 0.4650 0.5474 0.4110 -0.0389 0.0044  -0.0552 235 ASN   A CB  
232  C CG  . ASN   A 29  ? 0.7006 0.7731 0.6450 -0.0373 -0.0003 -0.0478 235 ASN   A CG  
233  O OD1 . ASN   A 29  ? 0.6262 0.6946 0.5776 -0.0327 -0.0026 -0.0475 235 ASN   A OD1 
234  N ND2 . ASN   A 29  ? 0.6655 0.7344 0.6016 -0.0409 -0.0018 -0.0421 235 ASN   A ND2 
235  N N   . LYS   A 30  ? 0.3700 0.4413 0.3372 -0.0277 0.0057  -0.0530 236 LYS   A N   
236  C CA  . LYS   A 30  ? 0.3420 0.4081 0.3179 -0.0225 0.0045  -0.0522 236 LYS   A CA  
237  C C   . LYS   A 30  ? 0.3926 0.4518 0.3653 -0.0219 0.0006  -0.0462 236 LYS   A C   
238  O O   . LYS   A 30  ? 0.3805 0.4364 0.3472 -0.0240 -0.0004 -0.0418 236 LYS   A O   
239  C CB  . LYS   A 30  ? 0.3038 0.3689 0.2863 -0.0199 0.0071  -0.0528 236 LYS   A CB  
240  C CG  . LYS   A 30  ? 0.4049 0.4652 0.3957 -0.0152 0.0062  -0.0519 236 LYS   A CG  
241  C CD  . LYS   A 30  ? 0.4452 0.5052 0.4423 -0.0130 0.0085  -0.0532 236 LYS   A CD  
242  C CE  . LYS   A 30  ? 0.5484 0.6036 0.5522 -0.0091 0.0076  -0.0517 236 LYS   A CE  
243  N NZ  . LYS   A 30  ? 0.5662 0.6207 0.5762 -0.0069 0.0092  -0.0529 236 LYS   A NZ  
244  N N   . HIS   A 31  ? 0.3406 0.3977 0.3175 -0.0192 -0.0019 -0.0462 237 HIS   A N   
245  C CA  . HIS   A 31  ? 0.3225 0.3737 0.2983 -0.0179 -0.0059 -0.0415 237 HIS   A CA  
246  C C   . HIS   A 31  ? 0.3353 0.3839 0.3207 -0.0133 -0.0056 -0.0417 237 HIS   A C   
247  O O   . HIS   A 31  ? 0.3213 0.3725 0.3132 -0.0116 -0.0044 -0.0453 237 HIS   A O   
248  C CB  . HIS   A 31  ? 0.3587 0.4108 0.3303 -0.0194 -0.0096 -0.0414 237 HIS   A CB  
249  C CG  . HIS   A 31  ? 0.4076 0.4543 0.3805 -0.0172 -0.0142 -0.0375 237 HIS   A CG  
250  N ND1 . HIS   A 31  ? 0.4028 0.4444 0.3694 -0.0186 -0.0175 -0.0325 237 HIS   A ND1 
251  C CD2 . HIS   A 31  ? 0.3607 0.4064 0.3413 -0.0137 -0.0159 -0.0381 237 HIS   A CD2 
252  C CE1 . HIS   A 31  ? 0.4346 0.4724 0.4052 -0.0155 -0.0214 -0.0305 237 HIS   A CE1 
253  N NE2 . HIS   A 31  ? 0.4371 0.4778 0.4163 -0.0126 -0.0202 -0.0340 237 HIS   A NE2 
254  N N   . LEU   A 32  ? 0.2898 0.3333 0.2760 -0.0114 -0.0070 -0.0379 238 LEU   A N   
255  C CA  . LEU   A 32  ? 0.3050 0.3465 0.2994 -0.0075 -0.0064 -0.0378 238 LEU   A CA  
256  C C   . LEU   A 32  ? 0.3149 0.3546 0.3114 -0.0058 -0.0103 -0.0364 238 LEU   A C   
257  O O   . LEU   A 32  ? 0.3249 0.3610 0.3170 -0.0062 -0.0136 -0.0332 238 LEU   A O   
258  C CB  . LEU   A 32  ? 0.2883 0.3261 0.2827 -0.0064 -0.0050 -0.0355 238 LEU   A CB  
259  C CG  . LEU   A 32  ? 0.3823 0.4216 0.3753 -0.0077 -0.0016 -0.0365 238 LEU   A CG  
260  C CD1 . LEU   A 32  ? 0.3518 0.3869 0.3452 -0.0062 -0.0011 -0.0340 238 LEU   A CD1 
261  C CD2 . LEU   A 32  ? 0.3722 0.4152 0.3708 -0.0069 0.0012  -0.0404 238 LEU   A CD2 
262  N N   . PHE   A 33  ? 0.2994 0.3414 0.3028 -0.0041 -0.0102 -0.0387 239 PHE   A N   
263  C CA  . PHE   A 33  ? 0.2651 0.3064 0.2724 -0.0022 -0.0136 -0.0379 239 PHE   A CA  
264  C C   . PHE   A 33  ? 0.3178 0.3565 0.3300 0.0008  -0.0132 -0.0363 239 PHE   A C   
265  O O   . PHE   A 33  ? 0.2776 0.3140 0.2899 0.0022  -0.0165 -0.0344 239 PHE   A O   
266  C CB  . PHE   A 33  ? 0.2517 0.2970 0.2654 -0.0018 -0.0134 -0.0412 239 PHE   A CB  
267  C CG  . PHE   A 33  ? 0.3174 0.3657 0.3269 -0.0045 -0.0141 -0.0438 239 PHE   A CG  
268  C CD1 . PHE   A 33  ? 0.2821 0.3306 0.2859 -0.0062 -0.0181 -0.0429 239 PHE   A CD1 
269  C CD2 . PHE   A 33  ? 0.2920 0.3431 0.3034 -0.0054 -0.0109 -0.0473 239 PHE   A CD2 
270  C CE1 . PHE   A 33  ? 0.2912 0.3431 0.2904 -0.0089 -0.0185 -0.0456 239 PHE   A CE1 
271  C CE2 . PHE   A 33  ? 0.2988 0.3534 0.3068 -0.0077 -0.0114 -0.0506 239 PHE   A CE2 
272  C CZ  . PHE   A 33  ? 0.2899 0.3452 0.2914 -0.0096 -0.0149 -0.0498 239 PHE   A CZ  
273  N N   . VAL   A 34  ? 0.2787 0.3181 0.2952 0.0019  -0.0093 -0.0372 240 VAL   A N   
274  C CA  . VAL   A 34  ? 0.2834 0.3212 0.3040 0.0044  -0.0082 -0.0361 240 VAL   A CA  
275  C C   . VAL   A 34  ? 0.3171 0.3537 0.3361 0.0040  -0.0046 -0.0358 240 VAL   A C   
276  O O   . VAL   A 34  ? 0.2698 0.3079 0.2882 0.0026  -0.0025 -0.0372 240 VAL   A O   
277  C CB  . VAL   A 34  ? 0.3159 0.3568 0.3452 0.0061  -0.0075 -0.0376 240 VAL   A CB  
278  C CG1 . VAL   A 34  ? 0.3280 0.3700 0.3601 0.0072  -0.0116 -0.0378 240 VAL   A CG1 
279  C CG2 . VAL   A 34  ? 0.3157 0.3593 0.3483 0.0048  -0.0053 -0.0397 240 VAL   A CG2 
280  N N   . HIS   A 35  ? 0.2691 0.3032 0.2882 0.0056  -0.0040 -0.0343 241 HIS   A N   
281  C CA  . HIS   A 35  ? 0.3123 0.3451 0.3302 0.0055  -0.0009 -0.0340 241 HIS   A CA  
282  C C   . HIS   A 35  ? 0.3074 0.3383 0.3269 0.0078  -0.0007 -0.0331 241 HIS   A C   
283  O O   . HIS   A 35  ? 0.2943 0.3246 0.3156 0.0094  -0.0030 -0.0329 241 HIS   A O   
284  C CB  . HIS   A 35  ? 0.2690 0.3002 0.2801 0.0033  -0.0009 -0.0332 241 HIS   A CB  
285  C CG  . HIS   A 35  ? 0.3136 0.3414 0.3195 0.0028  -0.0040 -0.0310 241 HIS   A CG  
286  N ND1 . HIS   A 35  ? 0.2679 0.2920 0.2734 0.0044  -0.0050 -0.0295 241 HIS   A ND1 
287  C CD2 . HIS   A 35  ? 0.2888 0.3159 0.2893 0.0005  -0.0067 -0.0299 241 HIS   A CD2 
288  C CE1 . HIS   A 35  ? 0.2910 0.3116 0.2916 0.0032  -0.0084 -0.0274 241 HIS   A CE1 
289  N NE2 . HIS   A 35  ? 0.2999 0.3223 0.2970 0.0007  -0.0095 -0.0273 241 HIS   A NE2 
290  N N   . ILE   A 36  ? 0.2682 0.2984 0.2873 0.0080  0.0021  -0.0328 242 ILE   A N   
291  C CA  . ILE   A 36  ? 0.2948 0.3235 0.3148 0.0099  0.0026  -0.0325 242 ILE   A CA  
292  C C   . ILE   A 36  ? 0.3344 0.3591 0.3489 0.0094  0.0020  -0.0312 242 ILE   A C   
293  O O   . ILE   A 36  ? 0.3277 0.3511 0.3419 0.0104  0.0033  -0.0312 242 ILE   A O   
294  C CB  . ILE   A 36  ? 0.2878 0.3189 0.3115 0.0104  0.0059  -0.0331 242 ILE   A CB  
295  C CG1 . ILE   A 36  ? 0.2709 0.3013 0.2925 0.0088  0.0079  -0.0326 242 ILE   A CG1 
296  C CG2 . ILE   A 36  ? 0.2972 0.3323 0.3270 0.0106  0.0063  -0.0343 242 ILE   A CG2 
297  C CD1 . ILE   A 36  ? 0.3157 0.3468 0.3387 0.0091  0.0105  -0.0323 242 ILE   A CD1 
298  N N   . GLY   A 37  ? 0.2991 0.3218 0.3089 0.0077  -0.0001 -0.0301 243 GLY   A N   
299  C CA  . GLY   A 37  ? 0.3101 0.3291 0.3148 0.0065  -0.0007 -0.0287 243 GLY   A CA  
300  C C   . GLY   A 37  ? 0.3851 0.3997 0.3885 0.0079  -0.0040 -0.0275 243 GLY   A C   
301  O O   . GLY   A 37  ? 0.3822 0.3931 0.3820 0.0071  -0.0045 -0.0264 243 GLY   A O   
302  N N   . HIS   A 38  ? 0.3499 0.3644 0.3567 0.0099  -0.0065 -0.0280 244 HIS   A N   
303  C CA  . HIS   A 38  ? 0.3682 0.3779 0.3746 0.0114  -0.0107 -0.0271 244 HIS   A CA  
304  C C   . HIS   A 38  ? 0.4005 0.4124 0.4141 0.0153  -0.0109 -0.0296 244 HIS   A C   
305  O O   . HIS   A 38  ? 0.3319 0.3449 0.3490 0.0165  -0.0137 -0.0301 244 HIS   A O   
306  C CB  . HIS   A 38  ? 0.4272 0.4342 0.4294 0.0095  -0.0150 -0.0248 244 HIS   A CB  
307  C CG  . HIS   A 38  ? 0.5403 0.5407 0.5407 0.0103  -0.0200 -0.0230 244 HIS   A CG  
308  N ND1 . HIS   A 38  ? 0.5720 0.5707 0.5781 0.0143  -0.0224 -0.0247 244 HIS   A ND1 
309  C CD2 . HIS   A 38  ? 0.6083 0.6031 0.6019 0.0074  -0.0235 -0.0198 244 HIS   A CD2 
310  C CE1 . HIS   A 38  ? 0.5827 0.5744 0.5860 0.0143  -0.0276 -0.0226 244 HIS   A CE1 
311  N NE2 . HIS   A 38  ? 0.6567 0.6456 0.6521 0.0098  -0.0284 -0.0192 244 HIS   A NE2 
312  N N   . ALA   A 39  ? 0.3224 0.3357 0.3386 0.0170  -0.0079 -0.0314 245 ALA   A N   
313  C CA  . ALA   A 39  ? 0.4233 0.4396 0.4464 0.0204  -0.0077 -0.0343 245 ALA   A CA  
314  C C   . ALA   A 39  ? 0.4220 0.4334 0.4463 0.0229  -0.0126 -0.0347 245 ALA   A C   
315  O O   . ALA   A 39  ? 0.4494 0.4558 0.4703 0.0230  -0.0137 -0.0341 245 ALA   A O   
316  C CB  . ALA   A 39  ? 0.3612 0.3806 0.3855 0.0210  -0.0031 -0.0361 245 ALA   A CB  
317  N N   . ASN   A 40  ? 0.3547 0.3674 0.3843 0.0251  -0.0160 -0.0359 246 ASN   A N   
318  C CA  . ASN   A 40  ? 0.4156 0.4225 0.4464 0.0276  -0.0218 -0.0360 246 ASN   A CA  
319  C C   . ASN   A 40  ? 0.4514 0.4604 0.4893 0.0318  -0.0212 -0.0405 246 ASN   A C   
320  O O   . ASN   A 40  ? 0.5556 0.5663 0.6007 0.0352  -0.0242 -0.0432 246 ASN   A O   
321  C CB  . ASN   A 40  ? 0.3733 0.3793 0.4058 0.0279  -0.0270 -0.0347 246 ASN   A CB  
322  C CG  . ASN   A 40  ? 0.4337 0.4476 0.4738 0.0293  -0.0254 -0.0374 246 ASN   A CG  
323  O OD1 . ASN   A 40  ? 0.4734 0.4936 0.5191 0.0308  -0.0210 -0.0407 246 ASN   A OD1 
324  N ND2 . ASN   A 40  ? 0.5410 0.5547 0.5812 0.0286  -0.0293 -0.0359 246 ASN   A ND2 
325  N N   . HIS   A 41  ? 0.3936 0.4030 0.4293 0.0315  -0.0173 -0.0416 247 HIS   A N   
326  C CA  . HIS   A 41  ? 0.5045 0.5154 0.5450 0.0350  -0.0163 -0.0460 247 HIS   A CA  
327  C C   . HIS   A 41  ? 0.5617 0.5640 0.5984 0.0356  -0.0200 -0.0454 247 HIS   A C   
328  O O   . HIS   A 41  ? 0.5279 0.5247 0.5571 0.0323  -0.0207 -0.0414 247 HIS   A O   
329  C CB  . HIS   A 41  ? 0.4762 0.4936 0.5162 0.0340  -0.0094 -0.0478 247 HIS   A CB  
330  C CG  . HIS   A 41  ? 0.4687 0.4945 0.5128 0.0330  -0.0056 -0.0485 247 HIS   A CG  
331  N ND1 . HIS   A 41  ? 0.4833 0.5169 0.5345 0.0351  -0.0027 -0.0528 247 HIS   A ND1 
332  C CD2 . HIS   A 41  ? 0.4541 0.4817 0.4962 0.0300  -0.0042 -0.0456 247 HIS   A CD2 
333  C CE1 . HIS   A 41  ? 0.4314 0.4709 0.4847 0.0331  0.0002  -0.0521 247 HIS   A CE1 
334  N NE2 . HIS   A 41  ? 0.4381 0.4738 0.4861 0.0302  -0.0008 -0.0478 247 HIS   A NE2 
335  N N   . SER   A 42  ? 0.5380 0.5394 0.5803 0.0397  -0.0222 -0.0496 248 SER   A N   
336  C CA  . SER   A 42  ? 0.6145 0.6068 0.6540 0.0405  -0.0265 -0.0492 248 SER   A CA  
337  C C   . SER   A 42  ? 0.6092 0.6007 0.6433 0.0388  -0.0226 -0.0496 248 SER   A C   
338  O O   . SER   A 42  ? 0.7375 0.7210 0.7673 0.0378  -0.0258 -0.0479 248 SER   A O   
339  C CB  . SER   A 42  ? 0.6629 0.6539 0.7111 0.0459  -0.0310 -0.0542 248 SER   A CB  
340  O OG  . SER   A 42  ? 0.7676 0.7675 0.8221 0.0487  -0.0262 -0.0604 248 SER   A OG  
341  N N   . TYR   A 43  ? 0.5221 0.5214 0.5561 0.0381  -0.0161 -0.0515 249 TYR   A N   
342  C CA  . TYR   A 43  ? 0.5204 0.5195 0.5492 0.0364  -0.0126 -0.0518 249 TYR   A CA  
343  C C   . TYR   A 43  ? 0.6372 0.6394 0.6606 0.0322  -0.0082 -0.0480 249 TYR   A C   
344  O O   . TYR   A 43  ? 0.5616 0.5689 0.5868 0.0313  -0.0061 -0.0469 249 TYR   A O   
345  C CB  . TYR   A 43  ? 0.6229 0.6285 0.6560 0.0393  -0.0089 -0.0578 249 TYR   A CB  
346  C CG  . TYR   A 43  ? 0.6267 0.6305 0.6666 0.0441  -0.0128 -0.0630 249 TYR   A CG  
347  C CD1 . TYR   A 43  ? 0.6831 0.6792 0.7214 0.0453  -0.0164 -0.0644 249 TYR   A CD1 
348  C CD2 . TYR   A 43  ? 0.6170 0.6269 0.6658 0.0474  -0.0131 -0.0670 249 TYR   A CD2 
349  C CE1 . TYR   A 43  ? 0.6682 0.6623 0.7136 0.0501  -0.0205 -0.0697 249 TYR   A CE1 
350  C CE2 . TYR   A 43  ? 0.5899 0.5986 0.6462 0.0523  -0.0170 -0.0724 249 TYR   A CE2 
351  C CZ  . TYR   A 43  ? 0.6666 0.6670 0.7211 0.0537  -0.0208 -0.0739 249 TYR   A CZ  
352  O OH  . TYR   A 43  ? 0.7245 0.7232 0.7873 0.0589  -0.0252 -0.0797 249 TYR   A OH  
353  N N   . SER   A 44  ? 0.5304 0.5293 0.5475 0.0298  -0.0071 -0.0462 250 SER   A N   
354  C CA  . SER   A 44  ? 0.6351 0.6370 0.6478 0.0263  -0.0033 -0.0433 250 SER   A CA  
355  C C   . SER   A 44  ? 0.6574 0.6670 0.6719 0.0266  0.0018  -0.0454 250 SER   A C   
356  O O   . SER   A 44  ? 0.6085 0.6217 0.6220 0.0244  0.0046  -0.0433 250 SER   A O   
357  C CB  . SER   A 44  ? 0.6006 0.5977 0.6073 0.0239  -0.0037 -0.0414 250 SER   A CB  
358  O OG  . SER   A 44  ? 0.6366 0.6267 0.6410 0.0227  -0.0082 -0.0388 250 SER   A OG  
359  N N   . ASP   A 45  ? 0.6047 0.6170 0.6216 0.0291  0.0031  -0.0497 251 ASP   A N   
360  C CA  . ASP   A 45  ? 0.6326 0.6524 0.6502 0.0289  0.0080  -0.0519 251 ASP   A CA  
361  C C   . ASP   A 45  ? 0.6492 0.6742 0.6739 0.0323  0.0084  -0.0570 251 ASP   A C   
362  O O   . ASP   A 45  ? 0.5063 0.5331 0.5317 0.0342  0.0095  -0.0613 251 ASP   A O   
363  C CB  . ASP   A 45  ? 0.8136 0.8328 0.8256 0.0277  0.0100  -0.0524 251 ASP   A CB  
364  C CG  . ASP   A 45  ? 0.8573 0.8725 0.8635 0.0245  0.0097  -0.0478 251 ASP   A CG  
365  O OD1 . ASP   A 45  ? 0.8778 0.8943 0.8838 0.0225  0.0106  -0.0446 251 ASP   A OD1 
366  O OD2 . ASP   A 45  ? 0.9072 0.9181 0.9094 0.0241  0.0084  -0.0479 251 ASP   A OD2 
367  N N   . PRO   A 46  ? 0.5764 0.6042 0.6069 0.0333  0.0075  -0.0571 252 PRO   A N   
368  C CA  . PRO   A 46  ? 0.4495 0.4823 0.4881 0.0369  0.0072  -0.0624 252 PRO   A CA  
369  C C   . PRO   A 46  ? 0.4617 0.5047 0.5023 0.0362  0.0130  -0.0654 252 PRO   A C   
370  O O   . PRO   A 46  ? 0.3969 0.4425 0.4328 0.0326  0.0169  -0.0626 252 PRO   A O   
371  C CB  . PRO   A 46  ? 0.4446 0.4768 0.4880 0.0375  0.0039  -0.0606 252 PRO   A CB  
372  C CG  . PRO   A 46  ? 0.4901 0.5223 0.5286 0.0334  0.0059  -0.0553 252 PRO   A CG  
373  C CD  . PRO   A 46  ? 0.5703 0.5975 0.6005 0.0311  0.0068  -0.0528 252 PRO   A CD  
374  N N   . LEU   A 47  ? 0.3755 0.4243 0.4234 0.0395  0.0135  -0.0714 253 LEU   A N   
375  C CA  . LEU   A 47  ? 0.3768 0.4368 0.4288 0.0387  0.0188  -0.0745 253 LEU   A CA  
376  C C   . LEU   A 47  ? 0.4175 0.4807 0.4762 0.0387  0.0177  -0.0733 253 LEU   A C   
377  O O   . LEU   A 47  ? 0.4408 0.5019 0.5059 0.0422  0.0131  -0.0752 253 LEU   A O   
378  C CB  . LEU   A 47  ? 0.3824 0.4483 0.4401 0.0423  0.0199  -0.0824 253 LEU   A CB  
379  C CG  . LEU   A 47  ? 0.4051 0.4691 0.4569 0.0426  0.0211  -0.0851 253 LEU   A CG  
380  C CD1 . LEU   A 47  ? 0.3705 0.4407 0.4299 0.0471  0.0215  -0.0940 253 LEU   A CD1 
381  C CD2 . LEU   A 47  ? 0.4334 0.5014 0.4768 0.0378  0.0267  -0.0824 253 LEU   A CD2 
382  N N   . LEU   A 48  ? 0.3713 0.4388 0.4285 0.0348  0.0212  -0.0699 254 LEU   A N   
383  C CA  . LEU   A 48  ? 0.4078 0.4772 0.4707 0.0345  0.0196  -0.0683 254 LEU   A CA  
384  C C   . LEU   A 48  ? 0.3895 0.4686 0.4632 0.0370  0.0206  -0.0741 254 LEU   A C   
385  O O   . LEU   A 48  ? 0.3449 0.4329 0.4209 0.0365  0.0254  -0.0781 254 LEU   A O   
386  C CB  . LEU   A 48  ? 0.4084 0.4791 0.4673 0.0296  0.0226  -0.0633 254 LEU   A CB  
387  C CG  . LEU   A 48  ? 0.3799 0.4416 0.4297 0.0273  0.0212  -0.0578 254 LEU   A CG  
388  C CD1 . LEU   A 48  ? 0.3767 0.4404 0.4235 0.0229  0.0243  -0.0539 254 LEU   A CD1 
389  C CD2 . LEU   A 48  ? 0.3565 0.4108 0.4064 0.0290  0.0156  -0.0558 254 LEU   A CD2 
390  N N   . GLU   A 49  ? 0.3117 0.3895 0.3921 0.0396  0.0160  -0.0746 255 GLU   A N   
391  C CA  . GLU   A 49  ? 0.3585 0.4458 0.4503 0.0419  0.0163  -0.0797 255 GLU   A CA  
392  C C   . GLU   A 49  ? 0.3491 0.4445 0.4424 0.0375  0.0211  -0.0780 255 GLU   A C   
393  O O   . GLU   A 49  ? 0.3276 0.4192 0.4140 0.0335  0.0222  -0.0723 255 GLU   A O   
394  C CB  . GLU   A 49  ? 0.3799 0.4620 0.4774 0.0457  0.0090  -0.0799 255 GLU   A CB  
395  C CG  . GLU   A 49  ? 0.5200 0.6099 0.6284 0.0470  0.0080  -0.0826 255 GLU   A CG  
396  C CD  . GLU   A 49  ? 0.6107 0.6943 0.7239 0.0512  -0.0002 -0.0829 255 GLU   A CD  
397  O OE1 . GLU   A 49  ? 0.5758 0.6483 0.6825 0.0522  -0.0048 -0.0799 255 GLU   A OE1 
398  O OE2 . GLU   A 49  ? 0.4908 0.5804 0.6139 0.0531  -0.0023 -0.0856 255 GLU   A OE2 
399  N N   . SER   A 50  ? 0.3131 0.4202 0.4156 0.0381  0.0243  -0.0831 256 SER   A N   
400  C CA  . SER   A 50  ? 0.3595 0.4746 0.4637 0.0333  0.0289  -0.0814 256 SER   A CA  
401  C C   . SER   A 50  ? 0.3951 0.5150 0.5100 0.0347  0.0261  -0.0830 256 SER   A C   
402  O O   . SER   A 50  ? 0.3433 0.4628 0.4657 0.0396  0.0213  -0.0867 256 SER   A O   
403  C CB  . SER   A 50  ? 0.3311 0.4573 0.4363 0.0311  0.0359  -0.0853 256 SER   A CB  
404  O OG  . SER   A 50  ? 0.4440 0.5793 0.5602 0.0352  0.0361  -0.0932 256 SER   A OG  
405  N N   . VAL   A 51  ? 0.3501 0.4739 0.4656 0.0301  0.0286  -0.0799 257 VAL   A N   
406  C CA  . VAL   A 51  ? 0.3747 0.5040 0.5001 0.0304  0.0266  -0.0811 257 VAL   A CA  
407  C C   . VAL   A 51  ? 0.3064 0.4474 0.4358 0.0255  0.0330  -0.0820 257 VAL   A C   
408  O O   . VAL   A 51  ? 0.3462 0.4858 0.4677 0.0203  0.0370  -0.0777 257 VAL   A O   
409  C CB  . VAL   A 51  ? 0.3678 0.4877 0.4891 0.0294  0.0217  -0.0755 257 VAL   A CB  
410  C CG1 . VAL   A 51  ? 0.3511 0.4777 0.4810 0.0276  0.0212  -0.0759 257 VAL   A CG1 
411  C CG2 . VAL   A 51  ? 0.3719 0.4823 0.4917 0.0342  0.0147  -0.0753 257 VAL   A CG2 
412  N N   . ASP   A 52  ? 0.3208 0.4732 0.4626 0.0269  0.0338  -0.0876 258 ASP   A N   
413  C CA  . ASP   A 52  ? 0.3798 0.5444 0.5265 0.0218  0.0399  -0.0887 258 ASP   A CA  
414  C C   . ASP   A 52  ? 0.3480 0.5093 0.4932 0.0172  0.0389  -0.0829 258 ASP   A C   
415  O O   . ASP   A 52  ? 0.3734 0.5325 0.5241 0.0192  0.0337  -0.0828 258 ASP   A O   
416  C CB  . ASP   A 52  ? 0.3896 0.5675 0.5514 0.0251  0.0402  -0.0967 258 ASP   A CB  
417  C CG  . ASP   A 52  ? 0.5045 0.6963 0.6733 0.0196  0.0462  -0.0982 258 ASP   A CG  
418  O OD1 . ASP   A 52  ? 0.4938 0.6856 0.6550 0.0129  0.0508  -0.0933 258 ASP   A OD1 
419  O OD2 . ASP   A 52  ? 0.5868 0.7894 0.7691 0.0219  0.0457  -0.1042 258 ASP   A OD2 
420  N N   . ILE   A 53  ? 0.2673 0.4280 0.4050 0.0109  0.0434  -0.0782 259 ILE   A N   
421  C CA  . ILE   A 53  ? 0.3724 0.5281 0.5079 0.0067  0.0419  -0.0726 259 ILE   A CA  
422  C C   . ILE   A 53  ? 0.3799 0.5452 0.5273 0.0050  0.0420  -0.0750 259 ILE   A C   
423  O O   . ILE   A 53  ? 0.3611 0.5222 0.5096 0.0036  0.0387  -0.0721 259 ILE   A O   
424  C CB  . ILE   A 53  ? 0.3424 0.4948 0.4676 0.0006  0.0463  -0.0672 259 ILE   A CB  
425  C CG1 . ILE   A 53  ? 0.3375 0.4807 0.4585 -0.0025 0.0433  -0.0612 259 ILE   A CG1 
426  C CG2 . ILE   A 53  ? 0.3764 0.5413 0.5050 -0.0046 0.0530  -0.0688 259 ILE   A CG2 
427  C CD1 . ILE   A 53  ? 0.3320 0.4687 0.4421 -0.0071 0.0457  -0.0555 259 ILE   A CD1 
428  N N   . ARG   A 54  ? 0.3675 0.5463 0.5247 0.0053  0.0455  -0.0809 260 ARG   A N   
429  C CA  . ARG   A 54  ? 0.4651 0.6540 0.6346 0.0036  0.0456  -0.0834 260 ARG   A CA  
430  C C   . ARG   A 54  ? 0.4375 0.6225 0.6137 0.0087  0.0381  -0.0850 260 ARG   A C   
431  O O   . ARG   A 54  ? 0.5199 0.7087 0.7033 0.0067  0.0364  -0.0849 260 ARG   A O   
432  C CB  . ARG   A 54  ? 0.4488 0.6541 0.6279 0.0031  0.0511  -0.0902 260 ARG   A CB  
433  C CG  . ARG   A 54  ? 0.4352 0.6462 0.6084 -0.0046 0.0588  -0.0876 260 ARG   A CG  
434  C CD  . ARG   A 54  ? 0.5607 0.7866 0.7392 -0.0049 0.0652  -0.0942 260 ARG   A CD  
435  N NE  . ARG   A 54  ? 0.7302 0.9576 0.9141 0.0033  0.0625  -0.1011 260 ARG   A NE  
436  C CZ  . ARG   A 54  ? 0.8241 1.0583 1.0074 0.0049  0.0666  -0.1063 260 ARG   A CZ  
437  N NH1 . ARG   A 54  ? 0.7668 1.0073 0.9435 -0.0012 0.0739  -0.1053 260 ARG   A NH1 
438  N NH2 . ARG   A 54  ? 0.8915 1.1258 1.0807 0.0128  0.0631  -0.1127 260 ARG   A NH2 
439  N N   . GLN   A 55  ? 0.3634 0.5402 0.5365 0.0149  0.0330  -0.0857 261 GLN   A N   
440  C CA  . GLN   A 55  ? 0.4465 0.6197 0.6253 0.0192  0.0256  -0.0868 261 GLN   A CA  
441  C C   . GLN   A 55  ? 0.4434 0.6038 0.6131 0.0178  0.0212  -0.0805 261 GLN   A C   
442  O O   . GLN   A 55  ? 0.5042 0.6604 0.6765 0.0212  0.0147  -0.0807 261 GLN   A O   
443  C CB  . GLN   A 55  ? 0.5628 0.7338 0.7444 0.0265  0.0212  -0.0910 261 GLN   A CB  
444  C CG  . GLN   A 55  ? 0.6030 0.7618 0.7725 0.0288  0.0197  -0.0881 261 GLN   A CG  
445  C CD  . GLN   A 55  ? 0.7143 0.8737 0.8888 0.0354  0.0168  -0.0935 261 GLN   A CD  
446  O OE1 . GLN   A 55  ? 0.9792 1.1276 1.1475 0.0389  0.0118  -0.0917 261 GLN   A OE1 
447  N NE2 . GLN   A 55  ? 0.7733 0.9458 0.9590 0.0369  0.0200  -0.1004 261 GLN   A NE2 
448  N N   . ILE   A 56  ? 0.3953 0.5497 0.5549 0.0130  0.0243  -0.0752 262 ILE   A N   
449  C CA  . ILE   A 56  ? 0.3929 0.5369 0.5454 0.0114  0.0206  -0.0702 262 ILE   A CA  
450  C C   . ILE   A 56  ? 0.4236 0.5695 0.5764 0.0050  0.0235  -0.0672 262 ILE   A C   
451  O O   . ILE   A 56  ? 0.4299 0.5678 0.5775 0.0034  0.0208  -0.0636 262 ILE   A O   
452  C CB  . ILE   A 56  ? 0.4579 0.5898 0.5974 0.0125  0.0197  -0.0662 262 ILE   A CB  
453  C CG1 . ILE   A 56  ? 0.3536 0.4852 0.4860 0.0085  0.0257  -0.0637 262 ILE   A CG1 
454  C CG2 . ILE   A 56  ? 0.4703 0.5990 0.6090 0.0184  0.0163  -0.0687 262 ILE   A CG2 
455  C CD1 . ILE   A 56  ? 0.4277 0.5475 0.5477 0.0086  0.0246  -0.0593 262 ILE   A CD1 
456  N N   . TYR   A 57  ? 0.3974 0.5536 0.5558 0.0011  0.0290  -0.0687 263 TYR   A N   
457  C CA  . TYR   A 57  ? 0.4347 0.5926 0.5938 -0.0055 0.0315  -0.0656 263 TYR   A CA  
458  C C   . TYR   A 57  ? 0.4260 0.5822 0.5903 -0.0060 0.0267  -0.0653 263 TYR   A C   
459  O O   . TYR   A 57  ? 0.4428 0.5937 0.6036 -0.0102 0.0264  -0.0616 263 TYR   A O   
460  C CB  . TYR   A 57  ? 0.4503 0.6217 0.6170 -0.0096 0.0376  -0.0681 263 TYR   A CB  
461  C CG  . TYR   A 57  ? 0.4402 0.6129 0.5996 -0.0124 0.0435  -0.0666 263 TYR   A CG  
462  C CD1 . TYR   A 57  ? 0.4326 0.5938 0.5791 -0.0135 0.0436  -0.0614 263 TYR   A CD1 
463  C CD2 . TYR   A 57  ? 0.4272 0.6131 0.5924 -0.0140 0.0491  -0.0707 263 TYR   A CD2 
464  C CE1 . TYR   A 57  ? 0.4126 0.5748 0.5519 -0.0162 0.0486  -0.0598 263 TYR   A CE1 
465  C CE2 . TYR   A 57  ? 0.4413 0.6287 0.5989 -0.0169 0.0546  -0.0693 263 TYR   A CE2 
466  C CZ  . TYR   A 57  ? 0.4740 0.6492 0.6184 -0.0179 0.0541  -0.0637 263 TYR   A CZ  
467  O OH  . TYR   A 57  ? 0.5784 0.7550 0.7148 -0.0209 0.0590  -0.0623 263 TYR   A OH  
468  N N   . ASP   A 58  ? 0.4159 0.5766 0.5888 -0.0018 0.0226  -0.0695 264 ASP   A N   
469  C CA  . ASP   A 58  ? 0.4342 0.5940 0.6120 -0.0027 0.0180  -0.0695 264 ASP   A CA  
470  C C   . ASP   A 58  ? 0.4044 0.5518 0.5734 -0.0002 0.0123  -0.0668 264 ASP   A C   
471  O O   . ASP   A 58  ? 0.4032 0.5490 0.5747 -0.0009 0.0083  -0.0667 264 ASP   A O   
472  C CB  . ASP   A 58  ? 0.4846 0.6549 0.6760 0.0002  0.0153  -0.0750 264 ASP   A CB  
473  C CG  . ASP   A 58  ? 0.5523 0.7213 0.7445 0.0074  0.0113  -0.0780 264 ASP   A CG  
474  O OD1 . ASP   A 58  ? 0.6104 0.7711 0.7927 0.0098  0.0112  -0.0760 264 ASP   A OD1 
475  O OD2 . ASP   A 58  ? 0.6329 0.8091 0.8361 0.0105  0.0078  -0.0824 264 ASP   A OD2 
476  N N   . LYS   A 59  ? 0.3774 0.5164 0.5361 0.0023  0.0122  -0.0646 265 LYS   A N   
477  C CA  . LYS   A 59  ? 0.3636 0.4913 0.5130 0.0038  0.0078  -0.0619 265 LYS   A CA  
478  C C   . LYS   A 59  ? 0.3475 0.4679 0.4884 -0.0002 0.0101  -0.0577 265 LYS   A C   
479  O O   . LYS   A 59  ? 0.3624 0.4743 0.4959 0.0005  0.0071  -0.0558 265 LYS   A O   
480  C CB  . LYS   A 59  ? 0.3794 0.5019 0.5230 0.0089  0.0056  -0.0621 265 LYS   A CB  
481  C CG  . LYS   A 59  ? 0.4566 0.5852 0.6090 0.0135  0.0024  -0.0664 265 LYS   A CG  
482  C CD  . LYS   A 59  ? 0.4706 0.5933 0.6177 0.0184  -0.0004 -0.0666 265 LYS   A CD  
483  C CE  . LYS   A 59  ? 0.4967 0.6082 0.6331 0.0189  -0.0046 -0.0629 265 LYS   A CE  
484  N NZ  . LYS   A 59  ? 0.5408 0.6512 0.6788 0.0184  -0.0097 -0.0627 265 LYS   A NZ  
485  N N   . PHE   A 60  ? 0.3709 0.4947 0.5129 -0.0046 0.0152  -0.0563 266 PHE   A N   
486  C CA  . PHE   A 60  ? 0.3400 0.4567 0.4744 -0.0084 0.0171  -0.0522 266 PHE   A CA  
487  C C   . PHE   A 60  ? 0.4117 0.5328 0.5518 -0.0142 0.0195  -0.0512 266 PHE   A C   
488  O O   . PHE   A 60  ? 0.3952 0.5261 0.5447 -0.0155 0.0209  -0.0538 266 PHE   A O   
489  C CB  . PHE   A 60  ? 0.3389 0.4527 0.4654 -0.0076 0.0206  -0.0503 266 PHE   A CB  
490  C CG  . PHE   A 60  ? 0.3020 0.4098 0.4221 -0.0025 0.0178  -0.0507 266 PHE   A CG  
491  C CD1 . PHE   A 60  ? 0.3638 0.4621 0.4759 -0.0020 0.0153  -0.0483 266 PHE   A CD1 
492  C CD2 . PHE   A 60  ? 0.3339 0.4456 0.4566 0.0016  0.0173  -0.0537 266 PHE   A CD2 
493  C CE1 . PHE   A 60  ? 0.3618 0.4549 0.4679 0.0019  0.0128  -0.0484 266 PHE   A CE1 
494  C CE2 . PHE   A 60  ? 0.3708 0.4763 0.4878 0.0059  0.0142  -0.0537 266 PHE   A CE2 
495  C CZ  . PHE   A 60  ? 0.3182 0.4144 0.4265 0.0057  0.0121  -0.0508 266 PHE   A CZ  
496  N N   . PRO   A 61  ? 0.4324 0.5467 0.5679 -0.0179 0.0199  -0.0476 267 PRO   A N   
497  C CA  . PRO   A 61  ? 0.3919 0.5093 0.5328 -0.0240 0.0216  -0.0462 267 PRO   A CA  
498  C C   . PRO   A 61  ? 0.5162 0.6425 0.6602 -0.0275 0.0272  -0.0459 267 PRO   A C   
499  O O   . PRO   A 61  ? 0.5107 0.6373 0.6491 -0.0265 0.0303  -0.0450 267 PRO   A O   
500  C CB  . PRO   A 61  ? 0.4514 0.5581 0.5851 -0.0264 0.0206  -0.0421 267 PRO   A CB  
501  C CG  . PRO   A 61  ? 0.3674 0.4667 0.4943 -0.0214 0.0173  -0.0428 267 PRO   A CG  
502  C CD  . PRO   A 61  ? 0.3556 0.4591 0.4813 -0.0169 0.0184  -0.0448 267 PRO   A CD  
503  N N   . GLU   A 62  ? 0.5356 0.6695 0.6885 -0.0319 0.0284  -0.0467 268 GLU   A N   
504  C CA  . GLU   A 62  ? 0.5138 0.6586 0.6711 -0.0359 0.0340  -0.0471 268 GLU   A CA  
505  C C   . GLU   A 62  ? 0.5711 0.7150 0.7288 -0.0441 0.0361  -0.0428 268 GLU   A C   
506  O O   . GLU   A 62  ? 0.5846 0.7187 0.7392 -0.0460 0.0329  -0.0397 268 GLU   A O   
507  C CB  . GLU   A 62  ? 0.5245 0.6818 0.6937 -0.0338 0.0340  -0.0527 268 GLU   A CB  
508  C CG  . GLU   A 62  ? 0.5402 0.6982 0.7087 -0.0261 0.0322  -0.0565 268 GLU   A CG  
509  C CD  . GLU   A 62  ? 0.5671 0.7370 0.7478 -0.0232 0.0314  -0.0624 268 GLU   A CD  
510  O OE1 . GLU   A 62  ? 0.6050 0.7735 0.7904 -0.0204 0.0261  -0.0643 268 GLU   A OE1 
511  O OE2 . GLU   A 62  ? 0.5275 0.7080 0.7131 -0.0236 0.0360  -0.0654 268 GLU   A OE2 
512  N N   . LYS   A 63  ? 0.6040 0.7581 0.7652 -0.0489 0.0414  -0.0428 269 LYS   A N   
513  C CA  . LYS   A 63  ? 0.7185 0.8731 0.8799 -0.0577 0.0440  -0.0382 269 LYS   A CA  
514  C C   . LYS   A 63  ? 0.7455 0.8873 0.8947 -0.0597 0.0435  -0.0321 269 LYS   A C   
515  O O   . LYS   A 63  ? 0.6359 0.7745 0.7768 -0.0560 0.0446  -0.0317 269 LYS   A O   
516  C CB  . LYS   A 63  ? 0.6787 0.8343 0.8495 -0.0608 0.0408  -0.0390 269 LYS   A CB  
517  C CG  . LYS   A 63  ? 0.6893 0.8558 0.8718 -0.0571 0.0397  -0.0454 269 LYS   A CG  
518  C CD  . LYS   A 63  ? 0.7444 0.9266 0.9361 -0.0623 0.0452  -0.0475 269 LYS   A CD  
519  C CE  . LYS   A 63  ? 0.7961 0.9779 0.9890 -0.0720 0.0469  -0.0428 269 LYS   A CE  
520  N NZ  . LYS   A 63  ? 0.8461 1.0394 1.0395 -0.0783 0.0543  -0.0418 269 LYS   A NZ  
521  N N   . LYS   A 64  ? 0.7980 0.9323 0.9461 -0.0654 0.0416  -0.0274 270 LYS   A N   
522  C CA  . LYS   A 64  ? 0.8029 0.9257 0.9403 -0.0680 0.0410  -0.0213 270 LYS   A CA  
523  C C   . LYS   A 64  ? 0.7718 0.8836 0.9025 -0.0608 0.0368  -0.0218 270 LYS   A C   
524  O O   . LYS   A 64  ? 0.7832 0.8909 0.9175 -0.0568 0.0323  -0.0245 270 LYS   A O   
525  C CB  . LYS   A 64  ? 0.8629 0.9789 1.0020 -0.0751 0.0385  -0.0166 270 LYS   A CB  
526  C CG  . LYS   A 64  ? 0.9217 1.0482 1.0688 -0.0828 0.0419  -0.0161 270 LYS   A CG  
527  C CD  . LYS   A 64  ? 1.0250 1.1439 1.1767 -0.0878 0.0375  -0.0133 270 LYS   A CD  
528  C CE  . LYS   A 64  ? 1.1179 1.2471 1.2778 -0.0963 0.0407  -0.0125 270 LYS   A CE  
529  N NZ  . LYS   A 64  ? 1.1705 1.2916 1.3354 -0.1011 0.0359  -0.0100 270 LYS   A NZ  
530  N N   . GLY   A 65  ? 0.8459 0.9534 0.9668 -0.0596 0.0383  -0.0192 271 GLY   A N   
531  C CA  . GLY   A 65  ? 0.8154 0.9137 0.9299 -0.0532 0.0350  -0.0198 271 GLY   A CA  
532  C C   . GLY   A 65  ? 0.7051 0.8081 0.8211 -0.0459 0.0349  -0.0252 271 GLY   A C   
533  O O   . GLY   A 65  ? 0.7316 0.8274 0.8422 -0.0408 0.0323  -0.0258 271 GLY   A O   
534  N N   . GLY   A 66  ? 0.6420 0.7567 0.7652 -0.0454 0.0376  -0.0292 272 GLY   A N   
535  C CA  . GLY   A 66  ? 0.6133 0.7321 0.7389 -0.0385 0.0367  -0.0343 272 GLY   A CA  
536  C C   . GLY   A 66  ? 0.5367 0.6571 0.6558 -0.0354 0.0396  -0.0350 272 GLY   A C   
537  O O   . GLY   A 66  ? 0.5171 0.6359 0.6292 -0.0384 0.0426  -0.0317 272 GLY   A O   
538  N N   . LEU   A 67  ? 0.4337 0.5571 0.5552 -0.0293 0.0384  -0.0395 273 LEU   A N   
539  C CA  . LEU   A 67  ? 0.4343 0.5572 0.5495 -0.0254 0.0400  -0.0405 273 LEU   A CA  
540  C C   . LEU   A 67  ? 0.4525 0.5852 0.5682 -0.0282 0.0458  -0.0416 273 LEU   A C   
541  O O   . LEU   A 67  ? 0.4471 0.5775 0.5546 -0.0284 0.0481  -0.0399 273 LEU   A O   
542  C CB  . LEU   A 67  ? 0.4365 0.5597 0.5547 -0.0185 0.0366  -0.0449 273 LEU   A CB  
543  C CG  . LEU   A 67  ? 0.4078 0.5291 0.5203 -0.0137 0.0371  -0.0464 273 LEU   A CG  
544  C CD1 . LEU   A 67  ? 0.3703 0.4810 0.4716 -0.0141 0.0365  -0.0421 273 LEU   A CD1 
545  C CD2 . LEU   A 67  ? 0.3687 0.4895 0.4849 -0.0077 0.0328  -0.0501 273 LEU   A CD2 
546  N N   . LYS   A 68  ? 0.4644 0.6087 0.5898 -0.0305 0.0483  -0.0446 274 LYS   A N   
547  C CA  . LYS   A 68  ? 0.4444 0.6000 0.5709 -0.0337 0.0545  -0.0463 274 LYS   A CA  
548  C C   . LYS   A 68  ? 0.4040 0.5564 0.5218 -0.0408 0.0576  -0.0403 274 LYS   A C   
549  O O   . LYS   A 68  ? 0.4330 0.5877 0.5441 -0.0419 0.0614  -0.0399 274 LYS   A O   
550  C CB  . LYS   A 68  ? 0.4182 0.5872 0.5575 -0.0357 0.0565  -0.0505 274 LYS   A CB  
551  C CG  . LYS   A 68  ? 0.4673 0.6499 0.6089 -0.0394 0.0634  -0.0531 274 LYS   A CG  
552  C CD  . LYS   A 68  ? 0.4717 0.6686 0.6276 -0.0406 0.0651  -0.0582 274 LYS   A CD  
553  C CE  . LYS   A 68  ? 0.5029 0.7143 0.6609 -0.0463 0.0727  -0.0601 274 LYS   A CE  
554  N NZ  . LYS   A 68  ? 0.6326 0.8581 0.8051 -0.0488 0.0745  -0.0645 274 LYS   A NZ  
555  N N   . GLU   A 69  ? 0.4380 0.5842 0.5555 -0.0456 0.0556  -0.0356 275 GLU   A N   
556  C CA  . GLU   A 69  ? 0.4684 0.6097 0.5774 -0.0523 0.0574  -0.0292 275 GLU   A CA  
557  C C   . GLU   A 69  ? 0.4673 0.5982 0.5646 -0.0495 0.0559  -0.0263 275 GLU   A C   
558  O O   . GLU   A 69  ? 0.5002 0.6317 0.5895 -0.0529 0.0592  -0.0236 275 GLU   A O   
559  C CB  . GLU   A 69  ? 0.5313 0.6662 0.6432 -0.0570 0.0541  -0.0250 275 GLU   A CB  
560  C CG  . GLU   A 69  ? 0.6671 0.7968 0.7718 -0.0649 0.0553  -0.0180 275 GLU   A CG  
561  C CD  . GLU   A 69  ? 0.7400 0.8651 0.8499 -0.0699 0.0521  -0.0148 275 GLU   A CD  
562  O OE1 . GLU   A 69  ? 0.7285 0.8420 0.8375 -0.0672 0.0467  -0.0134 275 GLU   A OE1 
563  O OE2 . GLU   A 69  ? 0.9655 1.0989 1.0808 -0.0765 0.0552  -0.0141 275 GLU   A OE2 
564  N N   . LEU   A 70  ? 0.4413 0.5628 0.5371 -0.0435 0.0510  -0.0270 276 LEU   A N   
565  C CA  . LEU   A 70  ? 0.4084 0.5205 0.4941 -0.0406 0.0493  -0.0247 276 LEU   A CA  
566  C C   . LEU   A 70  ? 0.3575 0.4755 0.4391 -0.0383 0.0531  -0.0276 276 LEU   A C   
567  O O   . LEU   A 70  ? 0.4453 0.5602 0.5178 -0.0402 0.0546  -0.0245 276 LEU   A O   
568  C CB  . LEU   A 70  ? 0.4268 0.5304 0.5130 -0.0346 0.0440  -0.0261 276 LEU   A CB  
569  C CG  . LEU   A 70  ? 0.5928 0.6874 0.6798 -0.0363 0.0397  -0.0229 276 LEU   A CG  
570  C CD1 . LEU   A 70  ? 0.5187 0.6090 0.6084 -0.0305 0.0354  -0.0260 276 LEU   A CD1 
571  C CD2 . LEU   A 70  ? 0.5460 0.6310 0.6240 -0.0387 0.0387  -0.0175 276 LEU   A CD2 
572  N N   . PHE   A 71  ? 0.4049 0.5312 0.4934 -0.0339 0.0541  -0.0336 277 PHE   A N   
573  C CA  . PHE   A 71  ? 0.3848 0.5166 0.4707 -0.0307 0.0571  -0.0374 277 PHE   A CA  
574  C C   . PHE   A 71  ? 0.4143 0.5548 0.4970 -0.0367 0.0631  -0.0367 277 PHE   A C   
575  O O   . PHE   A 71  ? 0.4087 0.5491 0.4836 -0.0363 0.0652  -0.0367 277 PHE   A O   
576  C CB  . PHE   A 71  ? 0.4341 0.5733 0.5297 -0.0250 0.0564  -0.0443 277 PHE   A CB  
577  C CG  . PHE   A 71  ? 0.4258 0.5688 0.5195 -0.0205 0.0582  -0.0489 277 PHE   A CG  
578  C CD1 . PHE   A 71  ? 0.4126 0.5463 0.5000 -0.0155 0.0549  -0.0487 277 PHE   A CD1 
579  C CD2 . PHE   A 71  ? 0.4051 0.5613 0.5037 -0.0215 0.0632  -0.0538 277 PHE   A CD2 
580  C CE1 . PHE   A 71  ? 0.4278 0.5644 0.5137 -0.0114 0.0562  -0.0531 277 PHE   A CE1 
581  C CE2 . PHE   A 71  ? 0.4501 0.6099 0.5476 -0.0171 0.0647  -0.0588 277 PHE   A CE2 
582  C CZ  . PHE   A 71  ? 0.4375 0.5870 0.5286 -0.0120 0.0610  -0.0583 277 PHE   A CZ  
583  N N   . GLY   A 72  ? 0.4640 0.6122 0.5523 -0.0426 0.0658  -0.0359 278 GLY   A N   
584  C CA  . GLY   A 72  ? 0.4482 0.6052 0.5329 -0.0494 0.0718  -0.0346 278 GLY   A CA  
585  C C   . GLY   A 72  ? 0.4870 0.6348 0.5587 -0.0542 0.0716  -0.0274 278 GLY   A C   
586  O O   . GLY   A 72  ? 0.5444 0.6971 0.6090 -0.0575 0.0758  -0.0270 278 GLY   A O   
587  N N   . LYS   A 73  ? 0.5212 0.6559 0.5898 -0.0545 0.0665  -0.0220 279 LYS   A N   
588  C CA  . LYS   A 73  ? 0.4904 0.6154 0.5472 -0.0583 0.0652  -0.0153 279 LYS   A CA  
589  C C   . LYS   A 73  ? 0.4900 0.6099 0.5387 -0.0530 0.0641  -0.0164 279 LYS   A C   
590  O O   . LYS   A 73  ? 0.5178 0.6337 0.5562 -0.0561 0.0646  -0.0122 279 LYS   A O   
591  C CB  . LYS   A 73  ? 0.4796 0.5924 0.5368 -0.0597 0.0596  -0.0100 279 LYS   A CB  
592  C CG  . LYS   A 73  ? 0.6582 0.7738 0.7206 -0.0670 0.0604  -0.0069 279 LYS   A CG  
593  C CD  . LYS   A 73  ? 0.6296 0.7314 0.6904 -0.0690 0.0547  -0.0010 279 LYS   A CD  
594  C CE  . LYS   A 73  ? 0.6909 0.7949 0.7572 -0.0765 0.0550  0.0021  279 LYS   A CE  
595  N NZ  . LYS   A 73  ? 0.7343 0.8244 0.7993 -0.0786 0.0490  0.0077  279 LYS   A NZ  
596  N N   . GLY   A 74  ? 0.4783 0.5979 0.5314 -0.0453 0.0623  -0.0217 280 GLY   A N   
597  C CA  . GLY   A 74  ? 0.4687 0.5840 0.5153 -0.0401 0.0612  -0.0234 280 GLY   A CA  
598  C C   . GLY   A 74  ? 0.5360 0.6374 0.5751 -0.0392 0.0564  -0.0183 280 GLY   A C   
599  O O   . GLY   A 74  ? 0.5017 0.5960 0.5419 -0.0414 0.0531  -0.0142 280 GLY   A O   
600  N N   . PRO   A 75  ? 0.4893 0.5868 0.5213 -0.0358 0.0557  -0.0190 281 PRO   A N   
601  C CA  . PRO   A 75  ? 0.4863 0.5906 0.5169 -0.0325 0.0587  -0.0243 281 PRO   A CA  
602  C C   . PRO   A 75  ? 0.5556 0.6630 0.5950 -0.0260 0.0576  -0.0306 281 PRO   A C   
603  O O   . PRO   A 75  ? 0.4515 0.5520 0.4939 -0.0223 0.0533  -0.0303 281 PRO   A O   
604  C CB  . PRO   A 75  ? 0.4965 0.5922 0.5172 -0.0309 0.0564  -0.0220 281 PRO   A CB  
605  C CG  . PRO   A 75  ? 0.4443 0.5286 0.4649 -0.0300 0.0510  -0.0177 281 PRO   A CG  
606  C CD  . PRO   A 75  ? 0.4686 0.5540 0.4938 -0.0351 0.0512  -0.0145 281 PRO   A CD  
607  N N   . GLN   A 76  ? 0.4624 0.5804 0.5059 -0.0245 0.0613  -0.0364 282 GLN   A N   
608  C CA  . GLN   A 76  ? 0.4817 0.6031 0.5348 -0.0187 0.0598  -0.0421 282 GLN   A CA  
609  C C   . GLN   A 76  ? 0.4515 0.5648 0.5020 -0.0124 0.0558  -0.0437 282 GLN   A C   
610  O O   . GLN   A 76  ? 0.4608 0.5727 0.5178 -0.0078 0.0527  -0.0464 282 GLN   A O   
611  C CB  . GLN   A 76  ? 0.5080 0.6433 0.5673 -0.0187 0.0647  -0.0484 282 GLN   A CB  
612  C CG  . GLN   A 76  ? 0.6066 0.7507 0.6690 -0.0256 0.0688  -0.0467 282 GLN   A CG  
613  C CD  . GLN   A 76  ? 0.7655 0.9250 0.8359 -0.0258 0.0739  -0.0535 282 GLN   A CD  
614  O OE1 . GLN   A 76  ? 0.7062 0.8700 0.7800 -0.0203 0.0742  -0.0600 282 GLN   A OE1 
615  N NE2 . GLN   A 76  ? 0.7243 0.8925 0.7986 -0.0320 0.0776  -0.0525 282 GLN   A NE2 
616  N N   . ASN   A 77  ? 0.3937 0.5014 0.4347 -0.0124 0.0555  -0.0417 283 ASN   A N   
617  C CA  . ASN   A 77  ? 0.4223 0.5220 0.4606 -0.0071 0.0517  -0.0428 283 ASN   A CA  
618  C C   . ASN   A 77  ? 0.4310 0.5205 0.4687 -0.0061 0.0469  -0.0388 283 ASN   A C   
619  O O   . ASN   A 77  ? 0.3677 0.4508 0.4037 -0.0022 0.0436  -0.0394 283 ASN   A O   
620  C CB  . ASN   A 77  ? 0.4486 0.5460 0.4773 -0.0076 0.0529  -0.0423 283 ASN   A CB  
621  C CG  . ASN   A 77  ? 0.5481 0.6390 0.5682 -0.0121 0.0522  -0.0357 283 ASN   A CG  
622  O OD1 . ASN   A 77  ? 0.5260 0.6147 0.5474 -0.0154 0.0513  -0.0315 283 ASN   A OD1 
623  N ND2 . ASN   A 77  ? 0.6432 0.7308 0.6549 -0.0121 0.0521  -0.0349 283 ASN   A ND2 
624  N N   . ALA   A 78  ? 0.3887 0.4769 0.4282 -0.0097 0.0464  -0.0350 284 ALA   A N   
625  C CA  . ALA   A 78  ? 0.3628 0.4426 0.4028 -0.0088 0.0421  -0.0321 284 ALA   A CA  
626  C C   . ALA   A 78  ? 0.3177 0.3992 0.3662 -0.0063 0.0400  -0.0347 284 ALA   A C   
627  O O   . ALA   A 78  ? 0.3554 0.4308 0.4045 -0.0056 0.0366  -0.0329 284 ALA   A O   
628  C CB  . ALA   A 78  ? 0.3189 0.3952 0.3562 -0.0140 0.0420  -0.0268 284 ALA   A CB  
629  N N   . PHE   A 79  ? 0.3043 0.3940 0.3594 -0.0048 0.0417  -0.0390 285 PHE   A N   
630  C CA  . PHE   A 79  ? 0.3228 0.4151 0.3866 -0.0031 0.0397  -0.0412 285 PHE   A CA  
631  C C   . PHE   A 79  ? 0.2929 0.3841 0.3591 0.0026  0.0368  -0.0450 285 PHE   A C   
632  O O   . PHE   A 79  ? 0.2820 0.3773 0.3491 0.0051  0.0382  -0.0487 285 PHE   A O   
633  C CB  . PHE   A 79  ? 0.2894 0.3923 0.3607 -0.0059 0.0431  -0.0432 285 PHE   A CB  
634  C CG  . PHE   A 79  ? 0.3377 0.4405 0.4081 -0.0119 0.0446  -0.0389 285 PHE   A CG  
635  C CD1 . PHE   A 79  ? 0.3702 0.4718 0.4332 -0.0161 0.0473  -0.0354 285 PHE   A CD1 
636  C CD2 . PHE   A 79  ? 0.3107 0.4139 0.3875 -0.0134 0.0428  -0.0382 285 PHE   A CD2 
637  C CE1 . PHE   A 79  ? 0.2958 0.3960 0.3578 -0.0218 0.0479  -0.0309 285 PHE   A CE1 
638  C CE2 . PHE   A 79  ? 0.3593 0.4614 0.4356 -0.0190 0.0436  -0.0342 285 PHE   A CE2 
639  C CZ  . PHE   A 79  ? 0.3465 0.4468 0.4155 -0.0233 0.0460  -0.0303 285 PHE   A CZ  
640  N N   . PHE   A 80  ? 0.2736 0.3593 0.3409 0.0045  0.0325  -0.0442 286 PHE   A N   
641  C CA  . PHE   A 80  ? 0.2709 0.3540 0.3396 0.0093  0.0289  -0.0467 286 PHE   A CA  
642  C C   . PHE   A 80  ? 0.3029 0.3873 0.3783 0.0103  0.0256  -0.0476 286 PHE   A C   
643  O O   . PHE   A 80  ? 0.2607 0.3441 0.3371 0.0076  0.0251  -0.0455 286 PHE   A O   
644  C CB  . PHE   A 80  ? 0.2861 0.3598 0.3466 0.0104  0.0264  -0.0441 286 PHE   A CB  
645  C CG  . PHE   A 80  ? 0.3168 0.3887 0.3706 0.0095  0.0289  -0.0431 286 PHE   A CG  
646  C CD1 . PHE   A 80  ? 0.3060 0.3760 0.3550 0.0058  0.0308  -0.0396 286 PHE   A CD1 
647  C CD2 . PHE   A 80  ? 0.3196 0.3911 0.3716 0.0125  0.0288  -0.0457 286 PHE   A CD2 
648  C CE1 . PHE   A 80  ? 0.3022 0.3705 0.3446 0.0049  0.0326  -0.0385 286 PHE   A CE1 
649  C CE2 . PHE   A 80  ? 0.3405 0.4105 0.3859 0.0117  0.0309  -0.0450 286 PHE   A CE2 
650  C CZ  . PHE   A 80  ? 0.3608 0.4294 0.4012 0.0078  0.0328  -0.0413 286 PHE   A CZ  
651  N N   . LEU   A 81  ? 0.2363 0.3218 0.3160 0.0143  0.0229  -0.0509 287 LEU   A N   
652  C CA  . LEU   A 81  ? 0.2392 0.3236 0.3231 0.0160  0.0184  -0.0514 287 LEU   A CA  
653  C C   . LEU   A 81  ? 0.2667 0.3422 0.3441 0.0183  0.0143  -0.0498 287 LEU   A C   
654  O O   . LEU   A 81  ? 0.2733 0.3463 0.3482 0.0208  0.0137  -0.0509 287 LEU   A O   
655  C CB  . LEU   A 81  ? 0.2754 0.3674 0.3693 0.0189  0.0174  -0.0560 287 LEU   A CB  
656  C CG  . LEU   A 81  ? 0.3272 0.4180 0.4258 0.0216  0.0117  -0.0571 287 LEU   A CG  
657  C CD1 . LEU   A 81  ? 0.3331 0.4260 0.4349 0.0186  0.0111  -0.0558 287 LEU   A CD1 
658  C CD2 . LEU   A 81  ? 0.3982 0.4956 0.5062 0.0254  0.0105  -0.0621 287 LEU   A CD2 
659  N N   . VAL   A 82  ? 0.2221 0.2929 0.2967 0.0171  0.0115  -0.0474 288 VAL   A N   
660  C CA  . VAL   A 82  ? 0.2543 0.3173 0.3222 0.0184  0.0079  -0.0456 288 VAL   A CA  
661  C C   . VAL   A 82  ? 0.2865 0.3488 0.3570 0.0194  0.0031  -0.0459 288 VAL   A C   
662  O O   . VAL   A 82  ? 0.2910 0.3551 0.3635 0.0174  0.0027  -0.0455 288 VAL   A O   
663  C CB  . VAL   A 82  ? 0.2558 0.3137 0.3161 0.0158  0.0092  -0.0425 288 VAL   A CB  
664  C CG1 . VAL   A 82  ? 0.2700 0.3210 0.3237 0.0168  0.0060  -0.0410 288 VAL   A CG1 
665  C CG2 . VAL   A 82  ? 0.2852 0.3439 0.3430 0.0145  0.0136  -0.0419 288 VAL   A CG2 
666  N N   . LYS   A 83  ? 0.2478 0.3070 0.3179 0.0224  -0.0010 -0.0466 289 LYS   A N   
667  C CA  . LYS   A 83  ? 0.2636 0.3209 0.3345 0.0233  -0.0064 -0.0463 289 LYS   A CA  
668  C C   . LYS   A 83  ? 0.3067 0.3566 0.3680 0.0216  -0.0085 -0.0430 289 LYS   A C   
669  O O   . LYS   A 83  ? 0.2936 0.3386 0.3493 0.0221  -0.0085 -0.0417 289 LYS   A O   
670  C CB  . LYS   A 83  ? 0.2735 0.3309 0.3495 0.0273  -0.0104 -0.0485 289 LYS   A CB  
671  C CG  . LYS   A 83  ? 0.3226 0.3769 0.3982 0.0281  -0.0169 -0.0475 289 LYS   A CG  
672  C CD  . LYS   A 83  ? 0.4407 0.4971 0.5248 0.0322  -0.0213 -0.0504 289 LYS   A CD  
673  C CE  . LYS   A 83  ? 0.4026 0.4551 0.4854 0.0327  -0.0285 -0.0488 289 LYS   A CE  
674  N NZ  . LYS   A 83  ? 0.5045 0.5611 0.5981 0.0366  -0.0329 -0.0522 289 LYS   A NZ  
675  N N   . PHE   A 84  ? 0.2764 0.3260 0.3359 0.0196  -0.0102 -0.0419 290 PHE   A N   
676  C CA  . PHE   A 84  ? 0.2859 0.3301 0.3365 0.0176  -0.0120 -0.0394 290 PHE   A CA  
677  C C   . PHE   A 84  ? 0.3021 0.3439 0.3511 0.0181  -0.0180 -0.0386 290 PHE   A C   
678  O O   . PHE   A 84  ? 0.2945 0.3399 0.3490 0.0187  -0.0203 -0.0400 290 PHE   A O   
679  C CB  . PHE   A 84  ? 0.2372 0.2829 0.2860 0.0145  -0.0092 -0.0392 290 PHE   A CB  
680  C CG  . PHE   A 84  ? 0.2810 0.3269 0.3290 0.0134  -0.0042 -0.0389 290 PHE   A CG  
681  C CD1 . PHE   A 84  ? 0.2145 0.2650 0.2687 0.0133  -0.0010 -0.0401 290 PHE   A CD1 
682  C CD2 . PHE   A 84  ? 0.2681 0.3100 0.3092 0.0123  -0.0030 -0.0373 290 PHE   A CD2 
683  C CE1 . PHE   A 84  ? 0.2632 0.3134 0.3160 0.0120  0.0030  -0.0394 290 PHE   A CE1 
684  C CE2 . PHE   A 84  ? 0.2825 0.3245 0.3230 0.0114  0.0010  -0.0370 290 PHE   A CE2 
685  C CZ  . PHE   A 84  ? 0.2554 0.3012 0.3014 0.0113  0.0038  -0.0378 290 PHE   A CZ  
686  N N   . TRP   A 85  ? 0.2714 0.3072 0.3126 0.0174  -0.0206 -0.0362 291 TRP   A N   
687  C CA  . TRP   A 85  ? 0.3437 0.3763 0.3807 0.0167  -0.0263 -0.0344 291 TRP   A CA  
688  C C   . TRP   A 85  ? 0.3101 0.3422 0.3392 0.0127  -0.0251 -0.0331 291 TRP   A C   
689  O O   . TRP   A 85  ? 0.3020 0.3315 0.3251 0.0109  -0.0225 -0.0317 291 TRP   A O   
690  C CB  . TRP   A 85  ? 0.3365 0.3624 0.3696 0.0180  -0.0304 -0.0322 291 TRP   A CB  
691  C CG  . TRP   A 85  ? 0.3665 0.3928 0.4078 0.0222  -0.0335 -0.0341 291 TRP   A CG  
692  C CD1 . TRP   A 85  ? 0.4082 0.4334 0.4528 0.0242  -0.0400 -0.0341 291 TRP   A CD1 
693  C CD2 . TRP   A 85  ? 0.3666 0.3951 0.4144 0.0252  -0.0304 -0.0367 291 TRP   A CD2 
694  N NE1 . TRP   A 85  ? 0.3861 0.4127 0.4397 0.0285  -0.0411 -0.0369 291 TRP   A NE1 
695  C CE2 . TRP   A 85  ? 0.3951 0.4241 0.4506 0.0291  -0.0351 -0.0388 291 TRP   A CE2 
696  C CE3 . TRP   A 85  ? 0.3146 0.3448 0.3623 0.0249  -0.0244 -0.0378 291 TRP   A CE3 
697  C CZ2 . TRP   A 85  ? 0.3781 0.4101 0.4415 0.0328  -0.0334 -0.0423 291 TRP   A CZ2 
698  C CZ3 . TRP   A 85  ? 0.3753 0.4081 0.4298 0.0282  -0.0228 -0.0408 291 TRP   A CZ3 
699  C CH2 . TRP   A 85  ? 0.3387 0.3727 0.4011 0.0321  -0.0270 -0.0433 291 TRP   A CH2 
700  N N   . ALA   A 86  ? 0.2897 0.3247 0.3194 0.0114  -0.0268 -0.0339 292 ALA   A N   
701  C CA  . ALA   A 86  ? 0.3207 0.3566 0.3442 0.0078  -0.0253 -0.0339 292 ALA   A CA  
702  C C   . ALA   A 86  ? 0.3977 0.4299 0.4117 0.0054  -0.0297 -0.0312 292 ALA   A C   
703  O O   . ALA   A 86  ? 0.3614 0.3914 0.3751 0.0062  -0.0352 -0.0299 292 ALA   A O   
704  C CB  . ALA   A 86  ? 0.3374 0.3787 0.3663 0.0073  -0.0249 -0.0367 292 ALA   A CB  
705  N N   . ASP   A 87  ? 0.3246 0.3561 0.3310 0.0022  -0.0272 -0.0305 293 ASP   A N   
706  C CA  . ASP   A 87  ? 0.3647 0.3935 0.3609 -0.0013 -0.0303 -0.0279 293 ASP   A CA  
707  C C   . ASP   A 87  ? 0.4021 0.4355 0.3958 -0.0039 -0.0302 -0.0301 293 ASP   A C   
708  O O   . ASP   A 87  ? 0.3317 0.3686 0.3251 -0.0054 -0.0258 -0.0327 293 ASP   A O   
709  C CB  . ASP   A 87  ? 0.3516 0.3779 0.3411 -0.0036 -0.0274 -0.0262 293 ASP   A CB  
710  C CG  . ASP   A 87  ? 0.3959 0.4196 0.3742 -0.0080 -0.0304 -0.0230 293 ASP   A CG  
711  O OD1 . ASP   A 87  ? 0.3989 0.4238 0.3734 -0.0099 -0.0338 -0.0228 293 ASP   A OD1 
712  O OD2 . ASP   A 87  ? 0.4384 0.4589 0.4115 -0.0099 -0.0294 -0.0207 293 ASP   A OD2 
713  N N   . LEU   A 88  ? 0.3853 0.4185 0.3772 -0.0044 -0.0355 -0.0294 294 LEU   A N   
714  C CA  . LEU   A 88  ? 0.4557 0.4932 0.4448 -0.0069 -0.0361 -0.0317 294 LEU   A CA  
715  C C   . LEU   A 88  ? 0.4646 0.5008 0.4411 -0.0115 -0.0389 -0.0292 294 LEU   A C   
716  O O   . LEU   A 88  ? 0.5131 0.5527 0.4859 -0.0138 -0.0403 -0.0309 294 LEU   A O   
717  C CB  . LEU   A 88  ? 0.3842 0.4237 0.3805 -0.0045 -0.0401 -0.0332 294 LEU   A CB  
718  C CG  . LEU   A 88  ? 0.4277 0.4697 0.4366 -0.0006 -0.0375 -0.0357 294 LEU   A CG  
719  C CD1 . LEU   A 88  ? 0.5063 0.5504 0.5217 0.0012  -0.0422 -0.0368 294 LEU   A CD1 
720  C CD2 . LEU   A 88  ? 0.4694 0.5154 0.4816 -0.0014 -0.0318 -0.0392 294 LEU   A CD2 
721  N N   . ASN   A 89  ? 0.4985 0.5298 0.4680 -0.0132 -0.0395 -0.0252 295 ASN   A N   
722  C CA  . ASN   A 89  ? 0.5380 0.5680 0.4947 -0.0185 -0.0417 -0.0222 295 ASN   A CA  
723  C C   . ASN   A 89  ? 0.4335 0.4690 0.3859 -0.0220 -0.0356 -0.0252 295 ASN   A C   
724  O O   . ASN   A 89  ? 0.5264 0.5611 0.4757 -0.0237 -0.0322 -0.0241 295 ASN   A O   
725  C CB  . ASN   A 89  ? 0.5069 0.5292 0.4585 -0.0193 -0.0450 -0.0167 295 ASN   A CB  
726  C CG  . ASN   A 89  ? 0.7970 0.8137 0.7532 -0.0156 -0.0517 -0.0142 295 ASN   A CG  
727  O OD1 . ASN   A 89  ? 0.8732 0.8913 0.8312 -0.0146 -0.0560 -0.0149 295 ASN   A OD1 
728  N ND2 . ASN   A 89  ? 0.7093 0.7201 0.6684 -0.0131 -0.0529 -0.0118 295 ASN   A ND2 
729  N N   . CYS   A 90  ? 0.4798 0.5214 0.4325 -0.0231 -0.0343 -0.0294 296 CYS   A N   
730  C CA  A CYS   A 90  ? 0.5110 0.5589 0.4615 -0.0258 -0.0286 -0.0336 296 CYS   A CA  
731  C CA  B CYS   A 90  ? 0.5114 0.5591 0.4613 -0.0259 -0.0287 -0.0334 296 CYS   A CA  
732  C C   . CYS   A 90  ? 0.5620 0.6150 0.5069 -0.0289 -0.0301 -0.0366 296 CYS   A C   
733  O O   . CYS   A 90  ? 0.6005 0.6542 0.5498 -0.0269 -0.0332 -0.0382 296 CYS   A O   
734  C CB  A CYS   A 90  ? 0.5135 0.5638 0.4754 -0.0218 -0.0238 -0.0380 296 CYS   A CB  
735  C CB  B CYS   A 90  ? 0.5136 0.5638 0.4745 -0.0222 -0.0235 -0.0376 296 CYS   A CB  
736  S SG  A CYS   A 90  ? 0.4549 0.5130 0.4174 -0.0237 -0.0177 -0.0445 296 CYS   A SG  
737  S SG  B CYS   A 90  ? 0.5159 0.5702 0.4869 -0.0192 -0.0233 -0.0431 296 CYS   A SG  
738  N N   . ASN   A 91  ? 0.6386 0.6957 0.5741 -0.0339 -0.0278 -0.0375 297 ASN   A N   
739  C CA  . ASN   A 91  ? 0.5918 0.6551 0.5214 -0.0373 -0.0283 -0.0413 297 ASN   A CA  
740  C C   . ASN   A 91  ? 0.6010 0.6709 0.5388 -0.0353 -0.0233 -0.0490 297 ASN   A C   
741  O O   . ASN   A 91  ? 0.6092 0.6828 0.5480 -0.0361 -0.0180 -0.0520 297 ASN   A O   
742  C CB  . ASN   A 91  ? 0.6876 0.7533 0.6031 -0.0440 -0.0277 -0.0393 297 ASN   A CB  
743  C CG  . ASN   A 91  ? 0.7802 0.8528 0.6885 -0.0479 -0.0282 -0.0433 297 ASN   A CG  
744  O OD1 . ASN   A 91  ? 0.7932 0.8661 0.7045 -0.0459 -0.0317 -0.0454 297 ASN   A OD1 
745  N ND2 . ASN   A 91  ? 0.9305 1.0093 0.8295 -0.0535 -0.0245 -0.0451 297 ASN   A ND2 
746  N N   . ILE   A 92  ? 0.5188 0.5900 0.4628 -0.0329 -0.0254 -0.0524 298 ILE   A N   
747  C CA  . ILE   A 92  ? 0.6004 0.6769 0.5527 -0.0310 -0.0216 -0.0598 298 ILE   A CA  
748  C C   . ILE   A 92  ? 0.7067 0.7904 0.6509 -0.0353 -0.0210 -0.0646 298 ILE   A C   
749  O O   . ILE   A 92  ? 0.6816 0.7665 0.6223 -0.0365 -0.0250 -0.0655 298 ILE   A O   
750  C CB  . ILE   A 92  ? 0.6112 0.6857 0.5748 -0.0266 -0.0239 -0.0612 298 ILE   A CB  
751  C CG1 . ILE   A 92  ? 0.5283 0.5967 0.4992 -0.0227 -0.0238 -0.0567 298 ILE   A CG1 
752  C CG2 . ILE   A 92  ? 0.6798 0.7587 0.6520 -0.0250 -0.0205 -0.0684 298 ILE   A CG2 
753  C CD1 . ILE   A 92  ? 0.6170 0.6837 0.5983 -0.0190 -0.0263 -0.0570 298 ILE   A CD1 
754  N N   . GLN   A 93  ? 0.7039 0.7929 0.6449 -0.0378 -0.0160 -0.0681 299 GLN   A N   
755  C CA  . GLN   A 93  ? 0.8129 0.9102 0.7455 -0.0424 -0.0143 -0.0732 299 GLN   A CA  
756  C C   . GLN   A 93  ? 0.7651 0.8675 0.7046 -0.0406 -0.0137 -0.0817 299 GLN   A C   
757  O O   . GLN   A 93  ? 0.6840 0.7848 0.6359 -0.0360 -0.0125 -0.0848 299 GLN   A O   
758  C CB  . GLN   A 93  ? 0.7862 0.8884 0.7153 -0.0453 -0.0087 -0.0748 299 GLN   A CB  
759  C CG  . GLN   A 93  ? 0.9028 0.9996 0.8257 -0.0473 -0.0091 -0.0666 299 GLN   A CG  
760  C CD  . GLN   A 93  ? 0.8005 0.9009 0.7253 -0.0482 -0.0033 -0.0683 299 GLN   A CD  
761  O OE1 . GLN   A 93  ? 0.9210 1.0300 0.8470 -0.0495 0.0010  -0.0753 299 GLN   A OE1 
762  N NE2 . GLN   A 93  ? 0.8557 0.9497 0.7812 -0.0473 -0.0035 -0.0621 299 GLN   A NE2 
763  N N   . GLY   A 97  ? 0.5031 0.6235 0.4845 -0.0299 0.0069  -0.1118 303 GLY   A N   
764  C CA  . GLY   A 97  ? 0.5586 0.6749 0.5524 -0.0251 0.0078  -0.1127 303 GLY   A CA  
765  C C   . GLY   A 97  ? 0.6249 0.7320 0.6193 -0.0234 0.0062  -0.1032 303 GLY   A C   
766  O O   . GLY   A 97  ? 0.5486 0.6551 0.5362 -0.0256 0.0075  -0.0979 303 GLY   A O   
767  N N   . ALA   A 98  ? 0.4140 0.5143 0.4162 -0.0199 0.0034  -0.1011 304 ALA   A N   
768  C CA  . ALA   A 98  ? 0.3768 0.4692 0.3793 -0.0185 0.0016  -0.0927 304 ALA   A CA  
769  C C   . ALA   A 98  ? 0.3931 0.4802 0.4072 -0.0143 0.0015  -0.0925 304 ALA   A C   
770  O O   . ALA   A 98  ? 0.4247 0.5117 0.4465 -0.0125 0.0004  -0.0972 304 ALA   A O   
771  C CB  . ALA   A 98  ? 0.3567 0.4463 0.3548 -0.0194 -0.0023 -0.0889 304 ALA   A CB  
772  N N   . PHE   A 99  ? 0.3544 0.4367 0.3693 -0.0130 0.0023  -0.0868 305 PHE   A N   
773  C CA  . PHE   A 99  ? 0.3284 0.4053 0.3527 -0.0096 0.0020  -0.0852 305 PHE   A CA  
774  C C   . PHE   A 99  ? 0.3729 0.4441 0.3954 -0.0090 0.0007  -0.0777 305 PHE   A C   
775  O O   . PHE   A 99  ? 0.3025 0.3727 0.3190 -0.0100 0.0015  -0.0734 305 PHE   A O   
776  C CB  . PHE   A 99  ? 0.3359 0.4133 0.3642 -0.0082 0.0046  -0.0869 305 PHE   A CB  
777  C CG  . PHE   A 99  ? 0.3668 0.4381 0.4035 -0.0052 0.0039  -0.0846 305 PHE   A CG  
778  C CD1 . PHE   A 99  ? 0.3121 0.3817 0.3575 -0.0034 0.0023  -0.0884 305 PHE   A CD1 
779  C CD2 . PHE   A 99  ? 0.3296 0.3965 0.3651 -0.0044 0.0046  -0.0785 305 PHE   A CD2 
780  C CE1 . PHE   A 99  ? 0.3344 0.3979 0.3867 -0.0013 0.0014  -0.0856 305 PHE   A CE1 
781  C CE2 . PHE   A 99  ? 0.3517 0.4132 0.3939 -0.0021 0.0039  -0.0762 305 PHE   A CE2 
782  C CZ  . PHE   A 99  ? 0.3221 0.3819 0.3725 -0.0008 0.0024  -0.0794 305 PHE   A CZ  
783  N N   . TYR   A 100 ? 0.2653 0.3332 0.2932 -0.0076 -0.0015 -0.0764 306 TYR   A N   
784  C CA  . TYR   A 100 ? 0.3125 0.3760 0.3409 -0.0066 -0.0025 -0.0703 306 TYR   A CA  
785  C C   . TYR   A 100 ? 0.3114 0.3711 0.3467 -0.0045 -0.0011 -0.0689 306 TYR   A C   
786  O O   . TYR   A 100 ? 0.3316 0.3906 0.3739 -0.0036 -0.0014 -0.0719 306 TYR   A O   
787  C CB  . TYR   A 100 ? 0.2660 0.3292 0.2970 -0.0067 -0.0055 -0.0701 306 TYR   A CB  
788  C CG  . TYR   A 100 ? 0.2813 0.3476 0.3049 -0.0088 -0.0076 -0.0708 306 TYR   A CG  
789  C CD1 . TYR   A 100 ? 0.3134 0.3841 0.3351 -0.0104 -0.0080 -0.0764 306 TYR   A CD1 
790  C CD2 . TYR   A 100 ? 0.3220 0.3867 0.3406 -0.0092 -0.0097 -0.0661 306 TYR   A CD2 
791  C CE1 . TYR   A 100 ? 0.3611 0.4348 0.3751 -0.0128 -0.0102 -0.0768 306 TYR   A CE1 
792  C CE2 . TYR   A 100 ? 0.3214 0.3883 0.3329 -0.0114 -0.0124 -0.0662 306 TYR   A CE2 
793  C CZ  . TYR   A 100 ? 0.3739 0.4454 0.3827 -0.0134 -0.0126 -0.0714 306 TYR   A CZ  
794  O OH  . TYR   A 100 ? 0.4057 0.4794 0.4063 -0.0160 -0.0154 -0.0713 306 TYR   A OH  
795  N N   . GLY   A 101 ? 0.3049 0.3619 0.3379 -0.0039 0.0001  -0.0643 307 GLY   A N   
796  C CA  . GLY   A 101 ? 0.2997 0.3533 0.3377 -0.0022 0.0015  -0.0628 307 GLY   A CA  
797  C C   . GLY   A 101 ? 0.3246 0.3748 0.3618 -0.0014 0.0018  -0.0573 307 GLY   A C   
798  O O   . GLY   A 101 ? 0.2976 0.3479 0.3303 -0.0018 0.0010  -0.0547 307 GLY   A O   
799  N N   . VAL   A 102 ? 0.2914 0.3386 0.3333 -0.0002 0.0026  -0.0558 308 VAL   A N   
800  C CA  . VAL   A 102 ? 0.3326 0.3771 0.3741 0.0006  0.0034  -0.0513 308 VAL   A CA  
801  C C   . VAL   A 102 ? 0.3632 0.4054 0.4048 0.0013  0.0049  -0.0502 308 VAL   A C   
802  O O   . VAL   A 102 ? 0.3869 0.4282 0.4327 0.0016  0.0048  -0.0522 308 VAL   A O   
803  C CB  . VAL   A 102 ? 0.3093 0.3529 0.3565 0.0006  0.0028  -0.0499 308 VAL   A CB  
804  C CG1 . VAL   A 102 ? 0.3989 0.4410 0.4453 0.0013  0.0041  -0.0459 308 VAL   A CG1 
805  C CG2 . VAL   A 102 ? 0.3152 0.3615 0.3632 0.0000  0.0009  -0.0513 308 VAL   A CG2 
806  N N   . THR   A 103 ? 0.3291 0.3701 0.3664 0.0017  0.0060  -0.0473 309 THR   A N   
807  C CA  . THR   A 103 ? 0.4085 0.4474 0.4457 0.0023  0.0071  -0.0461 309 THR   A CA  
808  C C   . THR   A 103 ? 0.3625 0.3991 0.3987 0.0029  0.0079  -0.0422 309 THR   A C   
809  O O   . THR   A 103 ? 0.3348 0.3718 0.3684 0.0031  0.0078  -0.0407 309 THR   A O   
810  C CB  . THR   A 103 ? 0.3622 0.4026 0.3948 0.0019  0.0078  -0.0473 309 THR   A CB  
811  O OG1 . THR   A 103 ? 0.3965 0.4399 0.4313 0.0015  0.0075  -0.0517 309 THR   A OG1 
812  C CG2 . THR   A 103 ? 0.3809 0.4193 0.4128 0.0026  0.0087  -0.0455 309 THR   A CG2 
813  N N   . SER   A 104 ? 0.3591 0.3932 0.3975 0.0032  0.0084  -0.0407 310 SER   A N   
814  C CA  . SER   A 104 ? 0.3124 0.3450 0.3489 0.0035  0.0095  -0.0375 310 SER   A CA  
815  C C   . SER   A 104 ? 0.3870 0.4169 0.4230 0.0038  0.0098  -0.0361 310 SER   A C   
816  O O   . SER   A 104 ? 0.3512 0.3799 0.3901 0.0038  0.0088  -0.0373 310 SER   A O   
817  C CB  . SER   A 104 ? 0.3502 0.3835 0.3902 0.0030  0.0097  -0.0362 310 SER   A CB  
818  O OG  . SER   A 104 ? 0.4472 0.4794 0.4919 0.0020  0.0089  -0.0368 310 SER   A OG  
819  N N   . GLN   A 105 ? 0.3421 0.3711 0.3744 0.0042  0.0108  -0.0339 311 GLN   A N   
820  C CA  . GLN   A 105 ? 0.3117 0.3382 0.3427 0.0043  0.0109  -0.0322 311 GLN   A CA  
821  C C   . GLN   A 105 ? 0.3317 0.3576 0.3604 0.0040  0.0123  -0.0296 311 GLN   A C   
822  O O   . GLN   A 105 ? 0.3448 0.3721 0.3713 0.0046  0.0132  -0.0295 311 GLN   A O   
823  C CB  . GLN   A 105 ? 0.3158 0.3423 0.3438 0.0049  0.0107  -0.0333 311 GLN   A CB  
824  C CG  . GLN   A 105 ? 0.3667 0.3906 0.3929 0.0052  0.0105  -0.0315 311 GLN   A CG  
825  C CD  . GLN   A 105 ? 0.4182 0.4427 0.4435 0.0056  0.0100  -0.0331 311 GLN   A CD  
826  O OE1 . GLN   A 105 ? 0.4697 0.4962 0.4976 0.0056  0.0094  -0.0359 311 GLN   A OE1 
827  N NE2 . GLN   A 105 ? 0.4217 0.4450 0.4433 0.0058  0.0102  -0.0317 311 GLN   A NE2 
828  N N   . TYR   A 106 ? 0.2861 0.3100 0.3154 0.0031  0.0121  -0.0275 312 TYR   A N   
829  C CA  . TYR   A 106 ? 0.2879 0.3117 0.3143 0.0023  0.0136  -0.0250 312 TYR   A CA  
830  C C   . TYR   A 106 ? 0.3170 0.3378 0.3399 0.0024  0.0128  -0.0235 312 TYR   A C   
831  O O   . TYR   A 106 ? 0.3124 0.3310 0.3368 0.0028  0.0108  -0.0239 312 TYR   A O   
832  C CB  . TYR   A 106 ? 0.2848 0.3088 0.3140 0.0001  0.0141  -0.0232 312 TYR   A CB  
833  C CG  . TYR   A 106 ? 0.3125 0.3395 0.3461 -0.0001 0.0145  -0.0248 312 TYR   A CG  
834  C CD1 . TYR   A 106 ? 0.3824 0.4087 0.4203 -0.0001 0.0126  -0.0265 312 TYR   A CD1 
835  C CD2 . TYR   A 106 ? 0.3321 0.3631 0.3662 -0.0003 0.0165  -0.0251 312 TYR   A CD2 
836  C CE1 . TYR   A 106 ? 0.3861 0.4152 0.4279 -0.0005 0.0126  -0.0281 312 TYR   A CE1 
837  C CE2 . TYR   A 106 ? 0.4117 0.4457 0.4503 -0.0005 0.0164  -0.0266 312 TYR   A CE2 
838  C CZ  . TYR   A 106 ? 0.4859 0.5188 0.5281 -0.0007 0.0144  -0.0280 312 TYR   A CZ  
839  O OH  . TYR   A 106 ? 0.5003 0.5362 0.5468 -0.0009 0.0140  -0.0296 312 TYR   A OH  
840  N N   . GLU   A 107 ? 0.2948 0.3159 0.3134 0.0021  0.0143  -0.0220 313 GLU   A N   
841  C CA  . GLU   A 107 ? 0.3686 0.3871 0.3831 0.0020  0.0134  -0.0204 313 GLU   A CA  
842  C C   . GLU   A 107 ? 0.3894 0.4082 0.4002 0.0001  0.0149  -0.0178 313 GLU   A C   
843  O O   . GLU   A 107 ? 0.3532 0.3755 0.3638 -0.0004 0.0174  -0.0182 313 GLU   A O   
844  C CB  . GLU   A 107 ? 0.3465 0.3653 0.3579 0.0037  0.0135  -0.0220 313 GLU   A CB  
845  C CG  . GLU   A 107 ? 0.5163 0.5350 0.5302 0.0048  0.0121  -0.0242 313 GLU   A CG  
846  C CD  . GLU   A 107 ? 0.5184 0.5375 0.5294 0.0057  0.0123  -0.0256 313 GLU   A CD  
847  O OE1 . GLU   A 107 ? 0.5856 0.6043 0.5927 0.0059  0.0131  -0.0250 313 GLU   A OE1 
848  O OE2 . GLU   A 107 ? 0.5595 0.5795 0.5721 0.0060  0.0116  -0.0274 313 GLU   A OE2 
849  N N   A SER   A 108 ? 0.3582 0.3738 0.3662 -0.0009 0.0132  -0.0153 314 SER   A N   
850  N N   B SER   A 108 ? 0.3660 0.3816 0.3740 -0.0010 0.0132  -0.0153 314 SER   A N   
851  C CA  A SER   A 108 ? 0.4107 0.4264 0.4140 -0.0034 0.0143  -0.0124 314 SER   A CA  
852  C CA  B SER   A 108 ? 0.4131 0.4288 0.4164 -0.0035 0.0143  -0.0123 314 SER   A CA  
853  C C   A SER   A 108 ? 0.4387 0.4511 0.4371 -0.0034 0.0121  -0.0107 314 SER   A C   
854  C C   B SER   A 108 ? 0.4383 0.4504 0.4368 -0.0036 0.0120  -0.0104 314 SER   A C   
855  O O   A SER   A 108 ? 0.3886 0.3982 0.3888 -0.0018 0.0093  -0.0113 314 SER   A O   
856  O O   B SER   A 108 ? 0.3911 0.4001 0.3917 -0.0022 0.0089  -0.0107 314 SER   A O   
857  C CB  A SER   A 108 ? 0.4130 0.4276 0.4183 -0.0064 0.0140  -0.0095 314 SER   A CB  
858  C CB  B SER   A 108 ? 0.4127 0.4275 0.4185 -0.0064 0.0141  -0.0096 314 SER   A CB  
859  O OG  A SER   A 108 ? 0.4310 0.4460 0.4305 -0.0094 0.0152  -0.0063 314 SER   A OG  
860  O OG  B SER   A 108 ? 0.4062 0.4155 0.4129 -0.0071 0.0103  -0.0071 314 SER   A OG  
861  N N   . SER   A 109 ? 0.4226 0.4359 0.4149 -0.0053 0.0136  -0.0089 315 SER   A N   
862  C CA  . SER   A 109 ? 0.5275 0.5376 0.5142 -0.0061 0.0113  -0.0065 315 SER   A CA  
863  C C   . SER   A 109 ? 0.4713 0.4771 0.4571 -0.0090 0.0085  -0.0019 315 SER   A C   
864  O O   . SER   A 109 ? 0.5490 0.5507 0.5315 -0.0093 0.0051  0.0004  315 SER   A O   
865  C CB  . SER   A 109 ? 0.5635 0.5768 0.5431 -0.0071 0.0141  -0.0069 315 SER   A CB  
866  O OG  . SER   A 109 ? 0.7802 0.7976 0.7591 -0.0098 0.0176  -0.0061 315 SER   A OG  
867  N N   . GLU   A 110 ? 0.4801 0.4863 0.4689 -0.0112 0.0094  -0.0003 316 GLU   A N   
868  C CA  . GLU   A 110 ? 0.5250 0.5264 0.5131 -0.0144 0.0065  0.0045  316 GLU   A CA  
869  C C   . GLU   A 110 ? 0.5181 0.5156 0.5143 -0.0130 0.0031  0.0039  316 GLU   A C   
870  O O   . GLU   A 110 ? 0.4929 0.4930 0.4952 -0.0108 0.0045  0.0002  316 GLU   A O   
871  C CB  . GLU   A 110 ? 0.5675 0.5722 0.5527 -0.0189 0.0099  0.0070  316 GLU   A CB  
872  C CG  . GLU   A 110 ? 0.7853 0.7948 0.7625 -0.0205 0.0135  0.0069  316 GLU   A CG  
873  C CD  . GLU   A 110 ? 1.0378 1.0485 1.0095 -0.0262 0.0151  0.0114  316 GLU   A CD  
874  O OE1 . GLU   A 110 ? 1.1747 1.1848 1.1378 -0.0286 0.0148  0.0140  316 GLU   A OE1 
875  O OE2 . GLU   A 110 ? 1.0849 1.0973 1.0606 -0.0287 0.0167  0.0124  316 GLU   A OE2 
876  N N   . ASN   A 111 ? 0.4849 0.4759 0.4812 -0.0142 -0.0017 0.0075  317 ASN   A N   
877  C CA  . ASN   A 111 ? 0.4558 0.4423 0.4602 -0.0129 -0.0057 0.0069  317 ASN   A CA  
878  C C   . ASN   A 111 ? 0.4976 0.4833 0.5041 -0.0166 -0.0049 0.0095  317 ASN   A C   
879  O O   . ASN   A 111 ? 0.5038 0.4863 0.5057 -0.0208 -0.0061 0.0148  317 ASN   A O   
880  C CB  . ASN   A 111 ? 0.4411 0.4207 0.4455 -0.0122 -0.0118 0.0094  317 ASN   A CB  
881  C CG  . ASN   A 111 ? 0.6255 0.6006 0.6393 -0.0100 -0.0163 0.0076  317 ASN   A CG  
882  O OD1 . ASN   A 111 ? 0.5125 0.4894 0.5322 -0.0097 -0.0148 0.0051  317 ASN   A OD1 
883  N ND2 . ASN   A 111 ? 0.7383 0.7080 0.7540 -0.0084 -0.0220 0.0084  317 ASN   A ND2 
884  N N   . MET   A 112 ? 0.3745 0.3633 0.3876 -0.0153 -0.0030 0.0059  318 MET   A N   
885  C CA  . MET   A 112 ? 0.4024 0.3921 0.4182 -0.0186 -0.0015 0.0073  318 MET   A CA  
886  C C   . MET   A 112 ? 0.4268 0.4147 0.4517 -0.0164 -0.0038 0.0039  318 MET   A C   
887  O O   . MET   A 112 ? 0.4121 0.4009 0.4407 -0.0122 -0.0047 -0.0005 318 MET   A O   
888  C CB  . MET   A 112 ? 0.4358 0.4338 0.4500 -0.0193 0.0045  0.0053  318 MET   A CB  
889  C CG  . MET   A 112 ? 0.4456 0.4471 0.4515 -0.0209 0.0077  0.0069  318 MET   A CG  
890  S SD  . MET   A 112 ? 0.5019 0.5131 0.5086 -0.0218 0.0140  0.0041  318 MET   A SD  
891  C CE  . MET   A 112 ? 0.3742 0.3879 0.3827 -0.0158 0.0147  -0.0017 318 MET   A CE  
892  N N   . THR   A 113 ? 0.3889 0.3748 0.4174 -0.0194 -0.0046 0.0058  319 THR   A N   
893  C CA  . THR   A 113 ? 0.4017 0.3880 0.4386 -0.0178 -0.0055 0.0018  319 THR   A CA  
894  C C   . THR   A 113 ? 0.3545 0.3481 0.3920 -0.0194 -0.0005 0.0005  319 THR   A C   
895  O O   . THR   A 113 ? 0.3865 0.3818 0.4208 -0.0237 0.0018  0.0042  319 THR   A O   
896  C CB  . THR   A 113 ? 0.4170 0.3954 0.4587 -0.0200 -0.0106 0.0045  319 THR   A CB  
897  O OG1 . THR   A 113 ? 0.4733 0.4453 0.5157 -0.0176 -0.0157 0.0049  319 THR   A OG1 
898  C CG2 . THR   A 113 ? 0.4849 0.4642 0.5352 -0.0185 -0.0113 -0.0001 319 THR   A CG2 
899  N N   . VAL   A 114 ? 0.3382 0.3365 0.3793 -0.0162 0.0013  -0.0048 320 VAL   A N   
900  C CA  . VAL   A 114 ? 0.3938 0.3992 0.4358 -0.0170 0.0055  -0.0064 320 VAL   A CA  
901  C C   . VAL   A 114 ? 0.3898 0.3957 0.4394 -0.0168 0.0043  -0.0094 320 VAL   A C   
902  O O   . VAL   A 114 ? 0.3862 0.3886 0.4400 -0.0145 0.0011  -0.0121 320 VAL   A O   
903  C CB  . VAL   A 114 ? 0.3868 0.3980 0.4257 -0.0138 0.0087  -0.0096 320 VAL   A CB  
904  C CG1 . VAL   A 114 ? 0.3100 0.3209 0.3415 -0.0141 0.0099  -0.0072 320 VAL   A CG1 
905  C CG2 . VAL   A 114 ? 0.3205 0.3312 0.3622 -0.0097 0.0070  -0.0141 320 VAL   A CG2 
906  N N   . THR   A 115 ? 0.3032 0.3139 0.3547 -0.0192 0.0069  -0.0094 321 THR   A N   
907  C CA  . THR   A 115 ? 0.3832 0.3957 0.4416 -0.0189 0.0062  -0.0127 321 THR   A CA  
908  C C   . THR   A 115 ? 0.3943 0.4145 0.4527 -0.0169 0.0095  -0.0160 321 THR   A C   
909  O O   . THR   A 115 ? 0.3940 0.4190 0.4497 -0.0182 0.0129  -0.0147 321 THR   A O   
910  C CB  . THR   A 115 ? 0.4446 0.4559 0.5069 -0.0237 0.0056  -0.0099 321 THR   A CB  
911  O OG1 . THR   A 115 ? 0.5848 0.6014 0.6440 -0.0270 0.0096  -0.0071 321 THR   A OG1 
912  C CG2 . THR   A 115 ? 0.4615 0.4638 0.5240 -0.0257 0.0014  -0.0063 321 THR   A CG2 
913  N N   . CYS   A 116 ? 0.3457 0.3672 0.4071 -0.0139 0.0084  -0.0204 322 CYS   A N   
914  C CA  A CYS   A 116 ? 0.3706 0.3984 0.4321 -0.0119 0.0105  -0.0234 322 CYS   A CA  
915  C CA  B CYS   A 116 ? 0.3708 0.3986 0.4323 -0.0119 0.0105  -0.0234 322 CYS   A CA  
916  C C   . CYS   A 116 ? 0.3730 0.4033 0.4408 -0.0130 0.0096  -0.0256 322 CYS   A C   
917  O O   . CYS   A 116 ? 0.3727 0.4005 0.4438 -0.0122 0.0069  -0.0282 322 CYS   A O   
918  C CB  A CYS   A 116 ? 0.3847 0.4124 0.4433 -0.0081 0.0099  -0.0263 322 CYS   A CB  
919  C CB  B CYS   A 116 ? 0.3846 0.4120 0.4432 -0.0081 0.0098  -0.0263 322 CYS   A CB  
920  S SG  A CYS   A 116 ? 0.4890 0.5230 0.5474 -0.0059 0.0113  -0.0294 322 CYS   A SG  
921  S SG  B CYS   A 116 ? 0.4124 0.4360 0.4647 -0.0069 0.0098  -0.0241 322 CYS   A SG  
922  N N   . SER   A 117 ? 0.3344 0.3702 0.4043 -0.0147 0.0119  -0.0252 323 SER   A N   
923  C CA  . SER   A 117 ? 0.3660 0.4052 0.4423 -0.0159 0.0111  -0.0273 323 SER   A CA  
924  C C   . SER   A 117 ? 0.3356 0.3801 0.4121 -0.0128 0.0116  -0.0307 323 SER   A C   
925  O O   . SER   A 117 ? 0.3531 0.4016 0.4274 -0.0117 0.0139  -0.0305 323 SER   A O   
926  C CB  . SER   A 117 ? 0.3060 0.3482 0.3855 -0.0203 0.0131  -0.0246 323 SER   A CB  
927  O OG  . SER   A 117 ? 0.4471 0.4945 0.5330 -0.0211 0.0128  -0.0271 323 SER   A OG  
928  N N   . THR   A 118 ? 0.2996 0.3441 0.3788 -0.0115 0.0090  -0.0340 324 THR   A N   
929  C CA  . THR   A 118 ? 0.3194 0.3683 0.3988 -0.0091 0.0085  -0.0369 324 THR   A CA  
930  C C   . THR   A 118 ? 0.3738 0.4264 0.4601 -0.0108 0.0072  -0.0386 324 THR   A C   
931  O O   . THR   A 118 ? 0.3794 0.4295 0.4688 -0.0120 0.0050  -0.0400 324 THR   A O   
932  C CB  . THR   A 118 ? 0.3740 0.4202 0.4497 -0.0066 0.0063  -0.0393 324 THR   A CB  
933  O OG1 . THR   A 118 ? 0.4049 0.4476 0.4750 -0.0053 0.0073  -0.0379 324 THR   A OG1 
934  C CG2 . THR   A 118 ? 0.2991 0.3492 0.3738 -0.0045 0.0053  -0.0415 324 THR   A CG2 
935  N N   . LYS   A 119 ? 0.2719 0.3306 0.3613 -0.0108 0.0085  -0.0389 325 LYS   A N   
936  C CA  . LYS   A 119 ? 0.3101 0.3734 0.4067 -0.0122 0.0072  -0.0409 325 LYS   A CA  
937  C C   . LYS   A 119 ? 0.3168 0.3837 0.4134 -0.0091 0.0053  -0.0436 325 LYS   A C   
938  O O   . LYS   A 119 ? 0.3361 0.4060 0.4315 -0.0070 0.0066  -0.0434 325 LYS   A O   
939  C CB  . LYS   A 119 ? 0.3017 0.3701 0.4033 -0.0153 0.0101  -0.0392 325 LYS   A CB  
940  C CG  . LYS   A 119 ? 0.3402 0.4048 0.4428 -0.0196 0.0109  -0.0363 325 LYS   A CG  
941  C CD  . LYS   A 119 ? 0.4927 0.5627 0.5985 -0.0233 0.0145  -0.0341 325 LYS   A CD  
942  C CE  . LYS   A 119 ? 0.4550 0.5201 0.5607 -0.0281 0.0147  -0.0303 325 LYS   A CE  
943  N NZ  . LYS   A 119 ? 0.6246 0.6949 0.7315 -0.0324 0.0186  -0.0275 325 LYS   A NZ  
944  N N   . VAL   A 120 ? 0.3120 0.3783 0.4098 -0.0087 0.0020  -0.0461 326 VAL   A N   
945  C CA  . VAL   A 120 ? 0.3299 0.3991 0.4274 -0.0063 -0.0006 -0.0484 326 VAL   A CA  
946  C C   . VAL   A 120 ? 0.3228 0.3983 0.4290 -0.0075 -0.0015 -0.0499 326 VAL   A C   
947  O O   . VAL   A 120 ? 0.3069 0.3831 0.4184 -0.0103 -0.0020 -0.0505 326 VAL   A O   
948  C CB  . VAL   A 120 ? 0.3404 0.4063 0.4338 -0.0056 -0.0037 -0.0505 326 VAL   A CB  
949  C CG1 . VAL   A 120 ? 0.3392 0.4079 0.4319 -0.0038 -0.0070 -0.0524 326 VAL   A CG1 
950  C CG2 . VAL   A 120 ? 0.3646 0.4253 0.4503 -0.0046 -0.0026 -0.0495 326 VAL   A CG2 
951  N N   . CYS   A 121 ? 0.2876 0.3678 0.3957 -0.0053 -0.0019 -0.0505 327 CYS   A N   
952  C CA  . CYS   A 121 ? 0.2897 0.3772 0.4072 -0.0062 -0.0022 -0.0521 327 CYS   A CA  
953  C C   . CYS   A 121 ? 0.3784 0.4689 0.4979 -0.0035 -0.0066 -0.0545 327 CYS   A C   
954  O O   . CYS   A 121 ? 0.3494 0.4376 0.4634 -0.0004 -0.0085 -0.0543 327 CYS   A O   
955  C CB  . CYS   A 121 ? 0.3186 0.4111 0.4395 -0.0064 0.0019  -0.0512 327 CYS   A CB  
956  S SG  . CYS   A 121 ? 0.4064 0.4954 0.5239 -0.0099 0.0067  -0.0477 327 CYS   A SG  
957  N N   . SER   A 122 ? 0.3368 0.4322 0.4644 -0.0051 -0.0086 -0.0566 328 SER   A N   
958  C CA  . SER   A 122 ? 0.3909 0.4897 0.5218 -0.0029 -0.0134 -0.0590 328 SER   A CA  
959  C C   . SER   A 122 ? 0.4145 0.5223 0.5569 -0.0033 -0.0126 -0.0608 328 SER   A C   
960  O O   . SER   A 122 ? 0.4197 0.5310 0.5687 -0.0070 -0.0105 -0.0612 328 SER   A O   
961  C CB  . SER   A 122 ? 0.4189 0.5155 0.5487 -0.0044 -0.0173 -0.0607 328 SER   A CB  
962  O OG  . SER   A 122 ? 0.4272 0.5262 0.5581 -0.0022 -0.0225 -0.0626 328 SER   A OG  
963  N N   . PHE   A 123 ? 0.4002 0.5117 0.5453 0.0002  -0.0142 -0.0619 329 PHE   A N   
964  C CA  . PHE   A 123 ? 0.3641 0.4854 0.5210 0.0004  -0.0131 -0.0643 329 PHE   A CA  
965  C C   . PHE   A 123 ? 0.4243 0.5493 0.5842 -0.0028 -0.0064 -0.0633 329 PHE   A C   
966  O O   . PHE   A 123 ? 0.4217 0.5546 0.5912 -0.0056 -0.0045 -0.0648 329 PHE   A O   
967  C CB  . PHE   A 123 ? 0.3803 0.5068 0.5459 -0.0009 -0.0170 -0.0670 329 PHE   A CB  
968  C CG  . PHE   A 123 ? 0.3491 0.4740 0.5131 0.0027  -0.0240 -0.0684 329 PHE   A CG  
969  C CD1 . PHE   A 123 ? 0.3900 0.5078 0.5452 0.0023  -0.0276 -0.0674 329 PHE   A CD1 
970  C CD2 . PHE   A 123 ? 0.3977 0.5278 0.5683 0.0066  -0.0269 -0.0705 329 PHE   A CD2 
971  C CE1 . PHE   A 123 ? 0.4330 0.5491 0.5853 0.0050  -0.0341 -0.0681 329 PHE   A CE1 
972  C CE2 . PHE   A 123 ? 0.4226 0.5501 0.5908 0.0097  -0.0339 -0.0710 329 PHE   A CE2 
973  C CZ  . PHE   A 123 ? 0.3937 0.5141 0.5523 0.0087  -0.0375 -0.0695 329 PHE   A CZ  
974  N N   . GLY   A 124 ? 0.3833 0.5027 0.5347 -0.0029 -0.0029 -0.0605 330 GLY   A N   
975  C CA  . GLY   A 124 ? 0.3854 0.5076 0.5378 -0.0061 0.0031  -0.0590 330 GLY   A CA  
976  C C   . GLY   A 124 ? 0.4208 0.5403 0.5725 -0.0114 0.0051  -0.0567 330 GLY   A C   
977  O O   . GLY   A 124 ? 0.4442 0.5649 0.5953 -0.0147 0.0098  -0.0546 330 GLY   A O   
978  N N   . LYS   A 125 ? 0.3893 0.5047 0.5407 -0.0126 0.0014  -0.0570 331 LYS   A N   
979  C CA  . LYS   A 125 ? 0.4421 0.5540 0.5939 -0.0175 0.0024  -0.0552 331 LYS   A CA  
980  C C   . LYS   A 125 ? 0.3719 0.4734 0.5140 -0.0168 0.0009  -0.0534 331 LYS   A C   
981  O O   . LYS   A 125 ? 0.3590 0.4571 0.4966 -0.0135 -0.0026 -0.0548 331 LYS   A O   
982  C CB  . LYS   A 125 ? 0.4141 0.5301 0.5747 -0.0198 -0.0006 -0.0576 331 LYS   A CB  
983  C CG  . LYS   A 125 ? 0.5678 0.6950 0.7390 -0.0195 -0.0005 -0.0605 331 LYS   A CG  
984  C CD  . LYS   A 125 ? 0.5679 0.7012 0.7484 -0.0253 0.0019  -0.0604 331 LYS   A CD  
985  C CE  . LYS   A 125 ? 0.5482 0.6940 0.7404 -0.0248 0.0021  -0.0640 331 LYS   A CE  
986  N NZ  . LYS   A 125 ? 0.5373 0.6885 0.7293 -0.0215 0.0054  -0.0648 331 LYS   A NZ  
987  N N   . GLN   A 126 ? 0.3763 0.4730 0.5156 -0.0201 0.0034  -0.0505 332 GLN   A N   
988  C CA  . GLN   A 126 ? 0.3935 0.4809 0.5251 -0.0195 0.0021  -0.0492 332 GLN   A CA  
989  C C   . GLN   A 126 ? 0.3799 0.4646 0.5133 -0.0197 -0.0023 -0.0519 332 GLN   A C   
990  O O   . GLN   A 126 ? 0.3821 0.4685 0.5224 -0.0231 -0.0034 -0.0528 332 GLN   A O   
991  C CB  . GLN   A 126 ? 0.4508 0.5339 0.5808 -0.0233 0.0049  -0.0456 332 GLN   A CB  
992  C CG  . GLN   A 126 ? 0.4750 0.5488 0.5983 -0.0225 0.0034  -0.0445 332 GLN   A CG  
993  C CD  . GLN   A 126 ? 0.5282 0.5973 0.6522 -0.0269 0.0045  -0.0412 332 GLN   A CD  
994  O OE1 . GLN   A 126 ? 0.5899 0.6608 0.7133 -0.0294 0.0079  -0.0380 332 GLN   A OE1 
995  N NE2 . GLN   A 126 ? 0.5306 0.5934 0.6556 -0.0279 0.0014  -0.0421 332 GLN   A NE2 
996  N N   . VAL   A 127 ? 0.3180 0.3986 0.4449 -0.0165 -0.0048 -0.0534 333 VAL   A N   
997  C CA  . VAL   A 127 ? 0.3395 0.4175 0.4667 -0.0167 -0.0087 -0.0564 333 VAL   A CA  
998  C C   . VAL   A 127 ? 0.3769 0.4471 0.4990 -0.0170 -0.0089 -0.0561 333 VAL   A C   
999  O O   . VAL   A 127 ? 0.4664 0.5340 0.5917 -0.0188 -0.0110 -0.0581 333 VAL   A O   
1000 C CB  . VAL   A 127 ? 0.3038 0.3841 0.4280 -0.0134 -0.0121 -0.0590 333 VAL   A CB  
1001 C CG1 . VAL   A 127 ? 0.3586 0.4466 0.4901 -0.0133 -0.0132 -0.0601 333 VAL   A CG1 
1002 C CG2 . VAL   A 127 ? 0.3729 0.4508 0.4883 -0.0102 -0.0112 -0.0576 333 VAL   A CG2 
1003 N N   . VAL   A 128 ? 0.3283 0.3949 0.4433 -0.0151 -0.0068 -0.0540 334 VAL   A N   
1004 C CA  . VAL   A 128 ? 0.3473 0.4072 0.4588 -0.0153 -0.0067 -0.0537 334 VAL   A CA  
1005 C C   . VAL   A 128 ? 0.3555 0.4130 0.4630 -0.0152 -0.0033 -0.0496 334 VAL   A C   
1006 O O   . VAL   A 128 ? 0.3590 0.4198 0.4645 -0.0140 -0.0011 -0.0479 334 VAL   A O   
1007 C CB  . VAL   A 128 ? 0.4027 0.4604 0.5083 -0.0127 -0.0088 -0.0570 334 VAL   A CB  
1008 C CG1 . VAL   A 128 ? 0.4877 0.5467 0.5970 -0.0135 -0.0124 -0.0614 334 VAL   A CG1 
1009 C CG2 . VAL   A 128 ? 0.3835 0.4437 0.4826 -0.0099 -0.0084 -0.0565 334 VAL   A CG2 
1010 N N   . GLU   A 129 ? 0.3609 0.4124 0.4677 -0.0163 -0.0033 -0.0483 335 GLU   A N   
1011 C CA  . GLU   A 129 ? 0.3413 0.3901 0.4445 -0.0167 -0.0005 -0.0442 335 GLU   A CA  
1012 C C   . GLU   A 129 ? 0.3845 0.4264 0.4844 -0.0157 -0.0018 -0.0445 335 GLU   A C   
1013 O O   . GLU   A 129 ? 0.4207 0.4593 0.5238 -0.0161 -0.0045 -0.0471 335 GLU   A O   
1014 C CB  . GLU   A 129 ? 0.3856 0.4347 0.4932 -0.0210 0.0011  -0.0407 335 GLU   A CB  
1015 C CG  . GLU   A 129 ? 0.5247 0.5707 0.6272 -0.0215 0.0036  -0.0364 335 GLU   A CG  
1016 C CD  . GLU   A 129 ? 0.7004 0.7453 0.8053 -0.0264 0.0050  -0.0322 335 GLU   A CD  
1017 O OE1 . GLU   A 129 ? 0.7118 0.7573 0.8232 -0.0298 0.0036  -0.0324 335 GLU   A OE1 
1018 O OE2 . GLU   A 129 ? 0.6158 0.6595 0.7159 -0.0271 0.0073  -0.0286 335 GLU   A OE2 
1019 N N   . LYS   A 130 ? 0.3655 0.4055 0.4596 -0.0141 0.0001  -0.0422 336 LYS   A N   
1020 C CA  . LYS   A 130 ? 0.3742 0.4080 0.4662 -0.0133 -0.0010 -0.0420 336 LYS   A CA  
1021 C C   . LYS   A 130 ? 0.4388 0.4701 0.5273 -0.0143 0.0010  -0.0371 336 LYS   A C   
1022 O O   . LYS   A 130 ? 0.4162 0.4510 0.5013 -0.0140 0.0039  -0.0351 336 LYS   A O   
1023 C CB  . LYS   A 130 ? 0.4018 0.4358 0.4891 -0.0098 -0.0015 -0.0453 336 LYS   A CB  
1024 C CG  . LYS   A 130 ? 0.5103 0.5391 0.5989 -0.0090 -0.0037 -0.0473 336 LYS   A CG  
1025 C CD  . LYS   A 130 ? 0.5773 0.6066 0.6611 -0.0061 -0.0034 -0.0497 336 LYS   A CD  
1026 C CE  . LYS   A 130 ? 0.5746 0.6001 0.6619 -0.0051 -0.0060 -0.0535 336 LYS   A CE  
1027 N NZ  . LYS   A 130 ? 0.7196 0.7455 0.8030 -0.0026 -0.0053 -0.0555 336 LYS   A NZ  
1028 N N   . VAL   A 131 ? 0.3711 0.3959 0.4606 -0.0154 -0.0008 -0.0355 337 VAL   A N   
1029 C CA  . VAL   A 131 ? 0.4103 0.4317 0.4960 -0.0165 0.0003  -0.0308 337 VAL   A CA  
1030 C C   . VAL   A 131 ? 0.4165 0.4325 0.5005 -0.0139 -0.0019 -0.0321 337 VAL   A C   
1031 O O   . VAL   A 131 ? 0.3931 0.4051 0.4815 -0.0134 -0.0052 -0.0347 337 VAL   A O   
1032 C CB  . VAL   A 131 ? 0.3918 0.4101 0.4805 -0.0213 -0.0002 -0.0265 337 VAL   A CB  
1033 C CG1 . VAL   A 131 ? 0.4761 0.4901 0.5596 -0.0226 0.0004  -0.0215 337 VAL   A CG1 
1034 C CG2 . VAL   A 131 ? 0.4299 0.4549 0.5211 -0.0241 0.0025  -0.0257 337 VAL   A CG2 
1035 N N   . GLU   A 132 ? 0.3377 0.3543 0.4158 -0.0119 -0.0002 -0.0309 338 GLU   A N   
1036 C CA  . GLU   A 132 ? 0.3782 0.3912 0.4546 -0.0092 -0.0018 -0.0323 338 GLU   A CA  
1037 C C   . GLU   A 132 ? 0.4471 0.4562 0.5196 -0.0104 -0.0016 -0.0272 338 GLU   A C   
1038 O O   . GLU   A 132 ? 0.4110 0.4226 0.4794 -0.0120 0.0012  -0.0239 338 GLU   A O   
1039 C CB  . GLU   A 132 ? 0.4113 0.4289 0.4839 -0.0061 -0.0001 -0.0357 338 GLU   A CB  
1040 C CG  . GLU   A 132 ? 0.5642 0.5851 0.6399 -0.0051 -0.0010 -0.0408 338 GLU   A CG  
1041 C CD  . GLU   A 132 ? 0.6987 0.7250 0.7699 -0.0034 0.0009  -0.0428 338 GLU   A CD  
1042 O OE1 . GLU   A 132 ? 0.6869 0.7147 0.7575 -0.0017 0.0002  -0.0468 338 GLU   A OE1 
1043 O OE2 . GLU   A 132 ? 0.6353 0.6644 0.7037 -0.0038 0.0030  -0.0404 338 GLU   A OE2 
1044 N N   . THR   A 133 ? 0.3844 0.3875 0.4583 -0.0096 -0.0049 -0.0270 339 THR   A N   
1045 C CA  . THR   A 133 ? 0.3930 0.3916 0.4631 -0.0106 -0.0057 -0.0222 339 THR   A CA  
1046 C C   . THR   A 133 ? 0.4007 0.3991 0.4682 -0.0070 -0.0061 -0.0242 339 THR   A C   
1047 O O   . THR   A 133 ? 0.3681 0.3666 0.4394 -0.0043 -0.0079 -0.0290 339 THR   A O   
1048 C CB  . THR   A 133 ? 0.4109 0.4016 0.4850 -0.0129 -0.0101 -0.0194 339 THR   A CB  
1049 O OG1 . THR   A 133 ? 0.5185 0.5096 0.5956 -0.0167 -0.0096 -0.0178 339 THR   A OG1 
1050 C CG2 . THR   A 133 ? 0.3840 0.3698 0.4530 -0.0146 -0.0111 -0.0137 339 THR   A CG2 
1051 N N   . GLU   A 134 ? 0.3726 0.3714 0.4337 -0.0072 -0.0044 -0.0209 340 GLU   A N   
1052 C CA  . GLU   A 134 ? 0.3265 0.3259 0.3853 -0.0041 -0.0047 -0.0228 340 GLU   A CA  
1053 C C   . GLU   A 134 ? 0.3782 0.3732 0.4326 -0.0050 -0.0060 -0.0181 340 GLU   A C   
1054 O O   . GLU   A 134 ? 0.3474 0.3424 0.3970 -0.0079 -0.0043 -0.0136 340 GLU   A O   
1055 C CB  . GLU   A 134 ? 0.3721 0.3780 0.4268 -0.0025 -0.0008 -0.0250 340 GLU   A CB  
1056 C CG  . GLU   A 134 ? 0.5178 0.5276 0.5757 -0.0005 -0.0005 -0.0306 340 GLU   A CG  
1057 C CD  . GLU   A 134 ? 0.6024 0.6105 0.6655 0.0016  -0.0035 -0.0347 340 GLU   A CD  
1058 O OE1 . GLU   A 134 ? 0.5684 0.5736 0.6317 0.0029  -0.0055 -0.0343 340 GLU   A OE1 
1059 O OE2 . GLU   A 134 ? 0.6072 0.6173 0.6745 0.0021  -0.0040 -0.0389 340 GLU   A OE2 
1060 N N   . TYR   A 135 ? 0.3264 0.3181 0.3827 -0.0027 -0.0093 -0.0194 341 TYR   A N   
1061 C CA  . TYR   A 135 ? 0.3482 0.3353 0.4009 -0.0031 -0.0117 -0.0154 341 TYR   A CA  
1062 C C   . TYR   A 135 ? 0.3788 0.3698 0.4268 -0.0010 -0.0096 -0.0167 341 TYR   A C   
1063 O O   . TYR   A 135 ? 0.3698 0.3650 0.4199 0.0017  -0.0084 -0.0215 341 TYR   A O   
1064 C CB  . TYR   A 135 ? 0.3978 0.3784 0.4568 -0.0017 -0.0176 -0.0161 341 TYR   A CB  
1065 C CG  . TYR   A 135 ? 0.4363 0.4119 0.5001 -0.0040 -0.0203 -0.0147 341 TYR   A CG  
1066 C CD1 . TYR   A 135 ? 0.4739 0.4519 0.5440 -0.0032 -0.0198 -0.0195 341 TYR   A CD1 
1067 C CD2 . TYR   A 135 ? 0.5158 0.4845 0.5775 -0.0075 -0.0233 -0.0084 341 TYR   A CD2 
1068 C CE1 . TYR   A 135 ? 0.5071 0.4807 0.5818 -0.0054 -0.0223 -0.0184 341 TYR   A CE1 
1069 C CE2 . TYR   A 135 ? 0.5667 0.5306 0.6329 -0.0102 -0.0258 -0.0068 341 TYR   A CE2 
1070 C CZ  . TYR   A 135 ? 0.5546 0.5210 0.6277 -0.0090 -0.0254 -0.0120 341 TYR   A CZ  
1071 O OH  . TYR   A 135 ? 0.8834 0.8450 0.9615 -0.0117 -0.0281 -0.0108 341 TYR   A OH  
1072 N N   . ALA   A 136 ? 0.3572 0.3468 0.3984 -0.0026 -0.0091 -0.0123 342 ALA   A N   
1073 C CA  . ALA   A 136 ? 0.3953 0.3880 0.4317 -0.0010 -0.0073 -0.0131 342 ALA   A CA  
1074 C C   . ALA   A 136 ? 0.3882 0.3800 0.4285 0.0022  -0.0104 -0.0163 342 ALA   A C   
1075 O O   . ALA   A 136 ? 0.4584 0.4452 0.5029 0.0029  -0.0151 -0.0158 342 ALA   A O   
1076 C CB  . ALA   A 136 ? 0.3633 0.3539 0.3918 -0.0035 -0.0070 -0.0078 342 ALA   A CB  
1077 N N   . ARG   A 137 ? 0.4197 0.4165 0.4589 0.0042  -0.0080 -0.0198 343 ARG   A N   
1078 C CA  . ARG   A 137 ? 0.4434 0.4413 0.4858 0.0068  -0.0100 -0.0230 343 ARG   A CA  
1079 C C   . ARG   A 137 ? 0.4234 0.4227 0.4591 0.0068  -0.0086 -0.0216 343 ARG   A C   
1080 O O   . ARG   A 137 ? 0.3700 0.3728 0.4011 0.0061  -0.0047 -0.0217 343 ARG   A O   
1081 C CB  . ARG   A 137 ? 0.4432 0.4463 0.4904 0.0085  -0.0083 -0.0289 343 ARG   A CB  
1082 C CG  . ARG   A 137 ? 0.6022 0.6084 0.6523 0.0108  -0.0093 -0.0328 343 ARG   A CG  
1083 C CD  . ARG   A 137 ? 0.6923 0.7041 0.7474 0.0119  -0.0077 -0.0388 343 ARG   A CD  
1084 N NE  . ARG   A 137 ? 0.8101 0.8250 0.8701 0.0139  -0.0092 -0.0431 343 ARG   A NE  
1085 C CZ  . ARG   A 137 ? 0.8711 0.8920 0.9357 0.0148  -0.0079 -0.0489 343 ARG   A CZ  
1086 N NH1 . ARG   A 137 ? 0.9386 0.9623 1.0028 0.0139  -0.0054 -0.0510 343 ARG   A NH1 
1087 N NH2 . ARG   A 137 ? 1.0071 1.0316 1.0766 0.0165  -0.0091 -0.0530 343 ARG   A NH2 
1088 N N   . PHE   A 138 ? 0.3776 0.3741 0.4132 0.0075  -0.0120 -0.0204 344 PHE   A N   
1089 C CA  . PHE   A 138 ? 0.3881 0.3859 0.4176 0.0075  -0.0111 -0.0193 344 PHE   A CA  
1090 C C   . PHE   A 138 ? 0.3611 0.3644 0.3929 0.0092  -0.0093 -0.0240 344 PHE   A C   
1091 O O   . PHE   A 138 ? 0.4730 0.4778 0.5114 0.0111  -0.0113 -0.0277 344 PHE   A O   
1092 C CB  . PHE   A 138 ? 0.5107 0.5038 0.5390 0.0076  -0.0157 -0.0163 344 PHE   A CB  
1093 C CG  . PHE   A 138 ? 0.4803 0.4746 0.5018 0.0072  -0.0149 -0.0151 344 PHE   A CG  
1094 C CD1 . PHE   A 138 ? 0.4901 0.4841 0.5031 0.0049  -0.0122 -0.0118 344 PHE   A CD1 
1095 C CD2 . PHE   A 138 ? 0.4932 0.4895 0.5172 0.0092  -0.0166 -0.0179 344 PHE   A CD2 
1096 C CE1 . PHE   A 138 ? 0.4653 0.4603 0.4722 0.0047  -0.0116 -0.0113 344 PHE   A CE1 
1097 C CE2 . PHE   A 138 ? 0.4646 0.4618 0.4826 0.0087  -0.0161 -0.0170 344 PHE   A CE2 
1098 C CZ  . PHE   A 138 ? 0.5125 0.5088 0.5218 0.0066  -0.0137 -0.0137 344 PHE   A CZ  
1099 N N   . GLU   A 139 ? 0.3996 0.4059 0.4259 0.0084  -0.0056 -0.0241 345 GLU   A N   
1100 C CA  . GLU   A 139 ? 0.4469 0.4580 0.4743 0.0092  -0.0037 -0.0279 345 GLU   A CA  
1101 C C   . GLU   A 139 ? 0.4530 0.4646 0.4737 0.0085  -0.0021 -0.0265 345 GLU   A C   
1102 O O   . GLU   A 139 ? 0.4740 0.4853 0.4897 0.0075  0.0004  -0.0248 345 GLU   A O   
1103 C CB  . GLU   A 139 ? 0.5061 0.5206 0.5350 0.0089  -0.0007 -0.0303 345 GLU   A CB  
1104 C CG  . GLU   A 139 ? 0.6857 0.7025 0.7221 0.0100  -0.0017 -0.0342 345 GLU   A CG  
1105 C CD  . GLU   A 139 ? 0.7257 0.7453 0.7623 0.0093  0.0010  -0.0360 345 GLU   A CD  
1106 O OE1 . GLU   A 139 ? 0.8287 0.8478 0.8700 0.0096  0.0000  -0.0374 345 GLU   A OE1 
1107 O OE2 . GLU   A 139 ? 0.7375 0.7593 0.7697 0.0084  0.0036  -0.0359 345 GLU   A OE2 
1108 N N   . ASN   A 140 ? 0.4428 0.4554 0.4640 0.0092  -0.0037 -0.0278 346 ASN   A N   
1109 C CA  . ASN   A 140 ? 0.4679 0.4812 0.4836 0.0085  -0.0025 -0.0274 346 ASN   A CA  
1110 C C   . ASN   A 140 ? 0.4066 0.4168 0.4151 0.0075  -0.0017 -0.0239 346 ASN   A C   
1111 O O   . ASN   A 140 ? 0.4699 0.4809 0.4739 0.0070  0.0007  -0.0240 346 ASN   A O   
1112 C CB  . ASN   A 140 ? 0.4376 0.4545 0.4530 0.0080  0.0005  -0.0298 346 ASN   A CB  
1113 C CG  . ASN   A 140 ? 0.5112 0.5323 0.5327 0.0083  0.0002  -0.0335 346 ASN   A CG  
1114 O OD1 . ASN   A 140 ? 0.5664 0.5886 0.5911 0.0090  -0.0020 -0.0349 346 ASN   A OD1 
1115 N ND2 . ASN   A 140 ? 0.6694 0.6935 0.6927 0.0078  0.0023  -0.0355 346 ASN   A ND2 
1116 N N   . GLY   A 141 ? 0.3788 0.3856 0.3862 0.0072  -0.0039 -0.0210 347 GLY   A N   
1117 C CA  . GLY   A 141 ? 0.3844 0.3891 0.3846 0.0058  -0.0034 -0.0178 347 GLY   A CA  
1118 C C   . GLY   A 141 ? 0.3950 0.3993 0.3933 0.0044  -0.0010 -0.0158 347 GLY   A C   
1119 O O   . GLY   A 141 ? 0.4000 0.4032 0.3923 0.0029  -0.0004 -0.0132 347 GLY   A O   
1120 N N   . ARG   A 142 ? 0.4229 0.4285 0.4260 0.0047  0.0003  -0.0170 348 ARG   A N   
1121 C CA  . ARG   A 142 ? 0.4191 0.4250 0.4211 0.0032  0.0026  -0.0153 348 ARG   A CA  
1122 C C   . ARG   A 142 ? 0.3907 0.3957 0.3993 0.0034  0.0013  -0.0157 348 ARG   A C   
1123 O O   . ARG   A 142 ? 0.4052 0.4100 0.4190 0.0049  -0.0008 -0.0179 348 ARG   A O   
1124 C CB  . ARG   A 142 ? 0.4195 0.4289 0.4197 0.0035  0.0064  -0.0172 348 ARG   A CB  
1125 C CG  . ARG   A 142 ? 0.4623 0.4739 0.4675 0.0045  0.0073  -0.0200 348 ARG   A CG  
1126 C CD  . ARG   A 142 ? 0.5520 0.5649 0.5579 0.0057  0.0071  -0.0227 348 ARG   A CD  
1127 N NE  . ARG   A 142 ? 0.5447 0.5601 0.5529 0.0061  0.0086  -0.0248 348 ARG   A NE  
1128 C CZ  . ARG   A 142 ? 0.6706 0.6876 0.6817 0.0065  0.0081  -0.0271 348 ARG   A CZ  
1129 N NH1 . ARG   A 142 ? 0.6857 0.7027 0.6991 0.0068  0.0062  -0.0281 348 ARG   A NH1 
1130 N NH2 . ARG   A 142 ? 0.7250 0.7440 0.7368 0.0063  0.0094  -0.0286 348 ARG   A NH2 
1131 N N   . PHE   A 143 ? 0.3605 0.3653 0.3691 0.0017  0.0026  -0.0139 349 PHE   A N   
1132 C CA  . PHE   A 143 ? 0.4030 0.4066 0.4178 0.0015  0.0013  -0.0142 349 PHE   A CA  
1133 C C   . PHE   A 143 ? 0.4083 0.4158 0.4261 0.0022  0.0041  -0.0172 349 PHE   A C   
1134 O O   . PHE   A 143 ? 0.3396 0.3499 0.3545 0.0016  0.0071  -0.0172 349 PHE   A O   
1135 C CB  . PHE   A 143 ? 0.3568 0.3571 0.3699 -0.0013 0.0004  -0.0099 349 PHE   A CB  
1136 C CG  . PHE   A 143 ? 0.4115 0.4071 0.4215 -0.0021 -0.0032 -0.0064 349 PHE   A CG  
1137 C CD1 . PHE   A 143 ? 0.3980 0.3895 0.4131 -0.0008 -0.0079 -0.0066 349 PHE   A CD1 
1138 C CD2 . PHE   A 143 ? 0.4085 0.4042 0.4106 -0.0039 -0.0022 -0.0037 349 PHE   A CD2 
1139 C CE1 . PHE   A 143 ? 0.4191 0.4060 0.4315 -0.0013 -0.0121 -0.0035 349 PHE   A CE1 
1140 C CE2 . PHE   A 143 ? 0.4398 0.4311 0.4383 -0.0047 -0.0060 -0.0004 349 PHE   A CE2 
1141 C CZ  . PHE   A 143 ? 0.4620 0.4486 0.4657 -0.0034 -0.0112 -0.0001 349 PHE   A CZ  
1142 N N   . VAL   A 144 ? 0.3264 0.3343 0.3500 0.0035  0.0027  -0.0201 350 VAL   A N   
1143 C CA  . VAL   A 144 ? 0.3957 0.4073 0.4221 0.0041  0.0047  -0.0232 350 VAL   A CA  
1144 C C   . VAL   A 144 ? 0.3069 0.3174 0.3387 0.0034  0.0035  -0.0237 350 VAL   A C   
1145 O O   . VAL   A 144 ? 0.3330 0.3403 0.3688 0.0037  0.0005  -0.0236 350 VAL   A O   
1146 C CB  . VAL   A 144 ? 0.4090 0.4229 0.4368 0.0058  0.0044  -0.0269 350 VAL   A CB  
1147 C CG1 . VAL   A 144 ? 0.4527 0.4702 0.4827 0.0060  0.0059  -0.0299 350 VAL   A CG1 
1148 C CG2 . VAL   A 144 ? 0.4238 0.4384 0.4462 0.0060  0.0055  -0.0262 350 VAL   A CG2 
1149 N N   . TYR   A 145 ? 0.3293 0.3423 0.3617 0.0027  0.0056  -0.0243 351 TYR   A N   
1150 C CA  . TYR   A 145 ? 0.3149 0.3276 0.3525 0.0019  0.0047  -0.0251 351 TYR   A CA  
1151 C C   . TYR   A 145 ? 0.3141 0.3308 0.3536 0.0031  0.0058  -0.0291 351 TYR   A C   
1152 O O   . TYR   A 145 ? 0.3403 0.3600 0.3774 0.0028  0.0079  -0.0292 351 TYR   A O   
1153 C CB  . TYR   A 145 ? 0.3072 0.3199 0.3440 -0.0005 0.0062  -0.0221 351 TYR   A CB  
1154 C CG  . TYR   A 145 ? 0.3396 0.3492 0.3725 -0.0023 0.0058  -0.0178 351 TYR   A CG  
1155 C CD1 . TYR   A 145 ? 0.3294 0.3406 0.3563 -0.0023 0.0078  -0.0164 351 TYR   A CD1 
1156 C CD2 . TYR   A 145 ? 0.3049 0.3097 0.3399 -0.0040 0.0029  -0.0151 351 TYR   A CD2 
1157 C CE1 . TYR   A 145 ? 0.3750 0.3837 0.3974 -0.0042 0.0074  -0.0126 351 TYR   A CE1 
1158 C CE2 . TYR   A 145 ? 0.3067 0.3084 0.3371 -0.0061 0.0022  -0.0106 351 TYR   A CE2 
1159 C CZ  . TYR   A 145 ? 0.3900 0.3940 0.4138 -0.0062 0.0046  -0.0095 351 TYR   A CZ  
1160 O OH  . TYR   A 145 ? 0.3871 0.3883 0.4055 -0.0086 0.0039  -0.0051 351 TYR   A OH  
1161 N N   . ARG   A 146 ? 0.3263 0.3432 0.3700 0.0042  0.0041  -0.0326 352 ARG   A N   
1162 C CA  A ARG   A 146 ? 0.3937 0.4149 0.4381 0.0048  0.0051  -0.0365 352 ARG   A CA  
1163 C CA  B ARG   A 146 ? 0.3935 0.4146 0.4380 0.0049  0.0050  -0.0366 352 ARG   A CA  
1164 C C   . ARG   A 146 ? 0.4110 0.4325 0.4608 0.0045  0.0038  -0.0391 352 ARG   A C   
1165 O O   . ARG   A 146 ? 0.4715 0.4905 0.5263 0.0050  0.0014  -0.0404 352 ARG   A O   
1166 C CB  A ARG   A 146 ? 0.3756 0.3988 0.4197 0.0061  0.0049  -0.0395 352 ARG   A CB  
1167 C CB  B ARG   A 146 ? 0.3777 0.4005 0.4228 0.0062  0.0044  -0.0397 352 ARG   A CB  
1168 C CG  A ARG   A 146 ? 0.4029 0.4309 0.4462 0.0060  0.0062  -0.0430 352 ARG   A CG  
1169 C CG  B ARG   A 146 ? 0.4034 0.4290 0.4431 0.0062  0.0064  -0.0396 352 ARG   A CG  
1170 C CD  A ARG   A 146 ? 0.4218 0.4529 0.4635 0.0063  0.0068  -0.0453 352 ARG   A CD  
1171 C CD  B ARG   A 146 ? 0.4346 0.4634 0.4756 0.0068  0.0063  -0.0434 352 ARG   A CD  
1172 N NE  A ARG   A 146 ? 0.4620 0.4974 0.5013 0.0053  0.0081  -0.0478 352 ARG   A NE  
1173 N NE  B ARG   A 146 ? 0.4687 0.4979 0.5055 0.0067  0.0071  -0.0421 352 ARG   A NE  
1174 C CZ  A ARG   A 146 ? 0.4899 0.5260 0.5235 0.0043  0.0094  -0.0458 352 ARG   A CZ  
1175 C CZ  B ARG   A 146 ? 0.4452 0.4722 0.4823 0.0075  0.0059  -0.0409 352 ARG   A CZ  
1176 N NH1 A ARG   A 146 ? 0.4851 0.5183 0.5154 0.0045  0.0098  -0.0420 352 ARG   A NH1 
1177 N NH1 B ARG   A 146 ? 0.4112 0.4352 0.4526 0.0084  0.0035  -0.0405 352 ARG   A NH1 
1178 N NH2 A ARG   A 146 ? 0.5174 0.5571 0.5486 0.0031  0.0100  -0.0478 352 ARG   A NH2 
1179 N NH2 B ARG   A 146 ? 0.4635 0.4910 0.4966 0.0072  0.0067  -0.0398 352 ARG   A NH2 
1180 N N   . ILE   A 147 ? 0.3760 0.4004 0.4249 0.0039  0.0051  -0.0398 353 ILE   A N   
1181 C CA  . ILE   A 147 ? 0.4489 0.4746 0.5023 0.0035  0.0041  -0.0429 353 ILE   A CA  
1182 C C   . ILE   A 147 ? 0.3848 0.4150 0.4360 0.0041  0.0049  -0.0467 353 ILE   A C   
1183 O O   . ILE   A 147 ? 0.4521 0.4847 0.4994 0.0036  0.0061  -0.0460 353 ILE   A O   
1184 C CB  . ILE   A 147 ? 0.4688 0.4948 0.5230 0.0020  0.0046  -0.0409 353 ILE   A CB  
1185 C CG1 . ILE   A 147 ? 0.4275 0.4499 0.4823 0.0007  0.0045  -0.0365 353 ILE   A CG1 
1186 C CG2 . ILE   A 147 ? 0.4784 0.5053 0.5377 0.0016  0.0030  -0.0442 353 ILE   A CG2 
1187 C CD1 . ILE   A 147 ? 0.4820 0.5058 0.5379 -0.0011 0.0056  -0.0346 353 ILE   A CD1 
1188 N N   . ASN   A 148 ? 0.4442 0.4758 0.4978 0.0050  0.0041  -0.0506 354 ASN   A N   
1189 C CA  . ASN   A 148 ? 0.5370 0.5735 0.5876 0.0048  0.0053  -0.0539 354 ASN   A CA  
1190 C C   . ASN   A 148 ? 0.4656 0.5052 0.5184 0.0043  0.0048  -0.0582 354 ASN   A C   
1191 O O   . ASN   A 148 ? 0.4605 0.4991 0.5193 0.0049  0.0031  -0.0613 354 ASN   A O   
1192 C CB  . ASN   A 148 ? 0.5160 0.5538 0.5680 0.0059  0.0053  -0.0565 354 ASN   A CB  
1193 C CG  . ASN   A 148 ? 0.5515 0.5948 0.5990 0.0049  0.0072  -0.0587 354 ASN   A CG  
1194 O OD1 . ASN   A 148 ? 0.7319 0.7756 0.7732 0.0037  0.0085  -0.0559 354 ASN   A OD1 
1195 N ND2 . ASN   A 148 ? 0.5263 0.5737 0.5769 0.0053  0.0074  -0.0639 354 ASN   A ND2 
1196 N N   . ARG   A 149 ? 0.4658 0.5087 0.5136 0.0031  0.0057  -0.0584 355 ARG   A N   
1197 C CA  . ARG   A 149 ? 0.4336 0.4806 0.4815 0.0022  0.0054  -0.0629 355 ARG   A CA  
1198 C C   . ARG   A 149 ? 0.4235 0.4688 0.4778 0.0026  0.0034  -0.0648 355 ARG   A C   
1199 O O   . ARG   A 149 ? 0.5231 0.5699 0.5820 0.0030  0.0024  -0.0699 355 ARG   A O   
1200 C CB  . ARG   A 149 ? 0.4494 0.5009 0.4976 0.0023  0.0062  -0.0679 355 ARG   A CB  
1201 C CG  . ARG   A 149 ? 0.5488 0.6060 0.5930 0.0004  0.0069  -0.0716 355 ARG   A CG  
1202 C CD  . ARG   A 149 ? 0.4708 0.5338 0.5132 -0.0004 0.0088  -0.0755 355 ARG   A CD  
1203 N NE  . ARG   A 149 ? 0.4896 0.5584 0.5293 -0.0023 0.0092  -0.0802 355 ARG   A NE  
1204 C CZ  . ARG   A 149 ? 0.5776 0.6489 0.6228 -0.0015 0.0084  -0.0863 355 ARG   A CZ  
1205 N NH1 . ARG   A 149 ? 0.5702 0.6381 0.6243 0.0012  0.0067  -0.0882 355 ARG   A NH1 
1206 N NH2 . ARG   A 149 ? 0.5471 0.6242 0.5888 -0.0035 0.0089  -0.0906 355 ARG   A NH2 
1207 N N   . SER   A 150 ? 0.4122 0.4545 0.4674 0.0022  0.0028  -0.0609 356 SER   A N   
1208 C CA  . SER   A 150 ? 0.4076 0.4482 0.4687 0.0019  0.0010  -0.0622 356 SER   A CA  
1209 C C   . SER   A 150 ? 0.3640 0.4085 0.4236 0.0009  0.0003  -0.0648 356 SER   A C   
1210 O O   . SER   A 150 ? 0.3463 0.3926 0.4004 0.0002  0.0010  -0.0626 356 SER   A O   
1211 C CB  . SER   A 150 ? 0.4216 0.4583 0.4844 0.0015  0.0009  -0.0570 356 SER   A CB  
1212 O OG  . SER   A 150 ? 0.5871 0.6228 0.6549 0.0004  -0.0006 -0.0574 356 SER   A OG  
1213 N N   . PRO   A 151 ? 0.3660 0.4115 0.4300 0.0007  -0.0013 -0.0697 357 PRO   A N   
1214 C CA  . PRO   A 151 ? 0.3237 0.3731 0.3857 -0.0004 -0.0022 -0.0723 357 PRO   A CA  
1215 C C   . PRO   A 151 ? 0.3086 0.3571 0.3706 -0.0013 -0.0029 -0.0682 357 PRO   A C   
1216 O O   . PRO   A 151 ? 0.3202 0.3653 0.3870 -0.0014 -0.0033 -0.0655 357 PRO   A O   
1217 C CB  . PRO   A 151 ? 0.3613 0.4109 0.4297 -0.0002 -0.0041 -0.0783 357 PRO   A CB  
1218 C CG  . PRO   A 151 ? 0.4462 0.4907 0.5210 0.0010  -0.0048 -0.0775 357 PRO   A CG  
1219 C CD  . PRO   A 151 ? 0.3982 0.4413 0.4693 0.0018  -0.0028 -0.0733 357 PRO   A CD  
1220 N N   . MET   A 152 ? 0.3266 0.3782 0.3831 -0.0020 -0.0031 -0.0675 358 MET   A N   
1221 C CA  . MET   A 152 ? 0.3200 0.3718 0.3772 -0.0025 -0.0043 -0.0649 358 MET   A CA  
1222 C C   . MET   A 152 ? 0.2979 0.3503 0.3615 -0.0033 -0.0065 -0.0681 358 MET   A C   
1223 O O   . MET   A 152 ? 0.2880 0.3422 0.3518 -0.0037 -0.0075 -0.0731 358 MET   A O   
1224 C CB  . MET   A 152 ? 0.3173 0.3719 0.3672 -0.0030 -0.0050 -0.0641 358 MET   A CB  
1225 C CG  . MET   A 152 ? 0.4405 0.4943 0.4890 -0.0025 -0.0053 -0.0594 358 MET   A CG  
1226 S SD  . MET   A 152 ? 0.3609 0.4169 0.4014 -0.0033 -0.0076 -0.0586 358 MET   A SD  
1227 C CE  . MET   A 152 ? 0.2938 0.3478 0.3269 -0.0031 -0.0054 -0.0557 358 MET   A CE  
1228 N N   . CYS   A 153 ? 0.3303 0.3817 0.3989 -0.0038 -0.0071 -0.0656 359 CYS   A N   
1229 C CA  . CYS   A 153 ? 0.3674 0.4193 0.4424 -0.0049 -0.0094 -0.0686 359 CYS   A CA  
1230 C C   . CYS   A 153 ? 0.3622 0.4181 0.4341 -0.0055 -0.0116 -0.0713 359 CYS   A C   
1231 O O   . CYS   A 153 ? 0.3116 0.3696 0.3776 -0.0052 -0.0117 -0.0694 359 CYS   A O   
1232 C CB  . CYS   A 153 ? 0.3611 0.4116 0.4424 -0.0059 -0.0093 -0.0652 359 CYS   A CB  
1233 S SG  . CYS   A 153 ? 0.4230 0.4770 0.5026 -0.0057 -0.0089 -0.0613 359 CYS   A SG  
1234 N N   . GLU   A 154 ? 0.3201 0.3769 0.3960 -0.0064 -0.0138 -0.0760 360 GLU   A N   
1235 C CA  . GLU   A 154 ? 0.3555 0.4164 0.4283 -0.0071 -0.0163 -0.0791 360 GLU   A CA  
1236 C C   . GLU   A 154 ? 0.3062 0.3689 0.3792 -0.0074 -0.0178 -0.0757 360 GLU   A C   
1237 O O   . GLU   A 154 ? 0.3163 0.3818 0.3835 -0.0076 -0.0196 -0.0758 360 GLU   A O   
1238 C CB  . GLU   A 154 ? 0.4729 0.5341 0.5514 -0.0080 -0.0186 -0.0848 360 GLU   A CB  
1239 C CG  . GLU   A 154 ? 0.6560 0.7166 0.7340 -0.0074 -0.0178 -0.0900 360 GLU   A CG  
1240 C CD  . GLU   A 154 ? 0.7491 0.8142 0.8179 -0.0076 -0.0172 -0.0930 360 GLU   A CD  
1241 O OE1 . GLU   A 154 ? 0.7793 0.8477 0.8426 -0.0087 -0.0187 -0.0923 360 GLU   A OE1 
1242 O OE2 . GLU   A 154 ? 0.7248 0.7904 0.7919 -0.0069 -0.0153 -0.0958 360 GLU   A OE2 
1243 N N   . TYR   A 155 ? 0.3240 0.3856 0.4039 -0.0075 -0.0172 -0.0726 361 TYR   A N   
1244 C CA  . TYR   A 155 ? 0.2912 0.3555 0.3729 -0.0075 -0.0186 -0.0701 361 TYR   A CA  
1245 C C   . TYR   A 155 ? 0.2999 0.3647 0.3738 -0.0060 -0.0182 -0.0670 361 TYR   A C   
1246 O O   . TYR   A 155 ? 0.2728 0.3400 0.3439 -0.0058 -0.0210 -0.0669 361 TYR   A O   
1247 C CB  . TYR   A 155 ? 0.3458 0.4096 0.4355 -0.0081 -0.0170 -0.0672 361 TYR   A CB  
1248 C CG  . TYR   A 155 ? 0.3477 0.4154 0.4407 -0.0078 -0.0180 -0.0653 361 TYR   A CG  
1249 C CD1 . TYR   A 155 ? 0.3769 0.4452 0.4664 -0.0060 -0.0169 -0.0621 361 TYR   A CD1 
1250 C CD2 . TYR   A 155 ? 0.3479 0.4188 0.4483 -0.0092 -0.0204 -0.0671 361 TYR   A CD2 
1251 C CE1 . TYR   A 155 ? 0.3312 0.4034 0.4247 -0.0052 -0.0182 -0.0611 361 TYR   A CE1 
1252 C CE2 . TYR   A 155 ? 0.3649 0.4403 0.4695 -0.0087 -0.0216 -0.0660 361 TYR   A CE2 
1253 C CZ  . TYR   A 155 ? 0.3830 0.4591 0.4843 -0.0065 -0.0205 -0.0631 361 TYR   A CZ  
1254 O OH  . TYR   A 155 ? 0.4376 0.5183 0.5439 -0.0055 -0.0219 -0.0625 361 TYR   A OH  
1255 N N   . MET   A 156 ? 0.3017 0.3639 0.3721 -0.0051 -0.0152 -0.0644 362 MET   A N   
1256 C CA  . MET   A 156 ? 0.2961 0.3579 0.3593 -0.0039 -0.0149 -0.0615 362 MET   A CA  
1257 C C   . MET   A 156 ? 0.2748 0.3374 0.3292 -0.0045 -0.0165 -0.0631 362 MET   A C   
1258 O O   . MET   A 156 ? 0.3032 0.3661 0.3525 -0.0041 -0.0184 -0.0610 362 MET   A O   
1259 C CB  . MET   A 156 ? 0.2134 0.2723 0.2755 -0.0029 -0.0113 -0.0585 362 MET   A CB  
1260 C CG  . MET   A 156 ? 0.2323 0.2909 0.3003 -0.0024 -0.0095 -0.0557 362 MET   A CG  
1261 S SD  . MET   A 156 ? 0.3872 0.4497 0.4587 -0.0015 -0.0121 -0.0548 362 MET   A SD  
1262 C CE  . MET   A 156 ? 0.3851 0.4455 0.4477 0.0004  -0.0125 -0.0521 362 MET   A CE  
1263 N N   . ILE   A 157 ? 0.2836 0.3466 0.3362 -0.0055 -0.0158 -0.0669 363 ILE   A N   
1264 C CA  . ILE   A 157 ? 0.2739 0.3388 0.3177 -0.0067 -0.0170 -0.0688 363 ILE   A CA  
1265 C C   . ILE   A 157 ? 0.3082 0.3755 0.3505 -0.0076 -0.0212 -0.0695 363 ILE   A C   
1266 O O   . ILE   A 157 ? 0.3317 0.3995 0.3664 -0.0083 -0.0233 -0.0676 363 ILE   A O   
1267 C CB  . ILE   A 157 ? 0.3115 0.3776 0.3551 -0.0076 -0.0155 -0.0740 363 ILE   A CB  
1268 C CG1 . ILE   A 157 ? 0.3266 0.3902 0.3719 -0.0065 -0.0120 -0.0734 363 ILE   A CG1 
1269 C CG2 . ILE   A 157 ? 0.2877 0.3572 0.3219 -0.0095 -0.0165 -0.0765 363 ILE   A CG2 
1270 C CD1 . ILE   A 157 ? 0.3521 0.4170 0.3998 -0.0067 -0.0109 -0.0792 363 ILE   A CD1 
1271 N N   . ASN   A 158 ? 0.2941 0.3627 0.3440 -0.0078 -0.0229 -0.0722 364 ASN   A N   
1272 C CA  . ASN   A 158 ? 0.3104 0.3816 0.3603 -0.0085 -0.0273 -0.0732 364 ASN   A CA  
1273 C C   . ASN   A 158 ? 0.3064 0.3773 0.3566 -0.0072 -0.0295 -0.0686 364 ASN   A C   
1274 O O   . ASN   A 158 ? 0.3314 0.4033 0.3761 -0.0077 -0.0334 -0.0678 364 ASN   A O   
1275 C CB  . ASN   A 158 ? 0.2971 0.3696 0.3566 -0.0090 -0.0283 -0.0768 364 ASN   A CB  
1276 C CG  . ASN   A 158 ? 0.4235 0.4991 0.4838 -0.0099 -0.0332 -0.0787 364 ASN   A CG  
1277 O OD1 . ASN   A 158 ? 0.5560 0.6327 0.6231 -0.0093 -0.0350 -0.0771 364 ASN   A OD1 
1278 N ND2 . ASN   A 158 ? 0.4765 0.5541 0.5295 -0.0114 -0.0352 -0.0820 364 ASN   A ND2 
1279 N N   . PHE   A 159 ? 0.2675 0.3369 0.3237 -0.0056 -0.0273 -0.0657 365 PHE   A N   
1280 C CA  . PHE   A 159 ? 0.3039 0.3733 0.3614 -0.0039 -0.0292 -0.0621 365 PHE   A CA  
1281 C C   . PHE   A 159 ? 0.3287 0.3956 0.3761 -0.0036 -0.0303 -0.0591 365 PHE   A C   
1282 O O   . PHE   A 159 ? 0.3392 0.4061 0.3843 -0.0030 -0.0346 -0.0573 365 PHE   A O   
1283 C CB  . PHE   A 159 ? 0.3186 0.3874 0.3838 -0.0025 -0.0257 -0.0602 365 PHE   A CB  
1284 C CG  . PHE   A 159 ? 0.3499 0.4193 0.4175 -0.0004 -0.0269 -0.0573 365 PHE   A CG  
1285 C CD1 . PHE   A 159 ? 0.3687 0.4415 0.4424 0.0004  -0.0306 -0.0581 365 PHE   A CD1 
1286 C CD2 . PHE   A 159 ? 0.4131 0.4798 0.4777 0.0011  -0.0245 -0.0544 365 PHE   A CD2 
1287 C CE1 . PHE   A 159 ? 0.3972 0.4709 0.4743 0.0028  -0.0320 -0.0562 365 PHE   A CE1 
1288 C CE2 . PHE   A 159 ? 0.4031 0.4703 0.4706 0.0034  -0.0259 -0.0525 365 PHE   A CE2 
1289 C CZ  . PHE   A 159 ? 0.3543 0.4251 0.4283 0.0044  -0.0296 -0.0536 365 PHE   A CZ  
1290 N N   . ILE   A 160 ? 0.3252 0.3898 0.3666 -0.0041 -0.0269 -0.0584 366 ILE   A N   
1291 C CA  . ILE   A 160 ? 0.3111 0.3733 0.3425 -0.0046 -0.0278 -0.0555 366 ILE   A CA  
1292 C C   . ILE   A 160 ? 0.2749 0.3385 0.2983 -0.0068 -0.0319 -0.0563 366 ILE   A C   
1293 O O   . ILE   A 160 ? 0.2969 0.3585 0.3142 -0.0071 -0.0356 -0.0531 366 ILE   A O   
1294 C CB  . ILE   A 160 ? 0.2747 0.3353 0.3021 -0.0052 -0.0231 -0.0554 366 ILE   A CB  
1295 C CG1 . ILE   A 160 ? 0.2755 0.3340 0.3088 -0.0031 -0.0199 -0.0533 366 ILE   A CG1 
1296 C CG2 . ILE   A 160 ? 0.2752 0.3342 0.2914 -0.0069 -0.0240 -0.0531 366 ILE   A CG2 
1297 C CD1 . ILE   A 160 ? 0.2805 0.3377 0.3117 -0.0035 -0.0155 -0.0538 366 ILE   A CD1 
1298 N N   . HIS   A 161 ? 0.3209 0.3875 0.3439 -0.0086 -0.0318 -0.0607 367 HIS   A N   
1299 C CA  . HIS   A 161 ? 0.3342 0.4027 0.3487 -0.0112 -0.0356 -0.0618 367 HIS   A CA  
1300 C C   . HIS   A 161 ? 0.3706 0.4392 0.3871 -0.0103 -0.0415 -0.0602 367 HIS   A C   
1301 O O   . HIS   A 161 ? 0.4024 0.4698 0.4105 -0.0116 -0.0458 -0.0576 367 HIS   A O   
1302 C CB  . HIS   A 161 ? 0.3303 0.4026 0.3453 -0.0129 -0.0344 -0.0678 367 HIS   A CB  
1303 C CG  . HIS   A 161 ? 0.4400 0.5132 0.4509 -0.0142 -0.0297 -0.0702 367 HIS   A CG  
1304 N ND1 . HIS   A 161 ? 0.6132 0.6900 0.6245 -0.0155 -0.0283 -0.0763 367 HIS   A ND1 
1305 C CD2 . HIS   A 161 ? 0.5072 0.5785 0.5144 -0.0141 -0.0262 -0.0677 367 HIS   A CD2 
1306 C CE1 . HIS   A 161 ? 0.5941 0.6716 0.6024 -0.0161 -0.0241 -0.0776 367 HIS   A CE1 
1307 N NE2 . HIS   A 161 ? 0.4896 0.5638 0.4953 -0.0154 -0.0228 -0.0723 367 HIS   A NE2 
1308 N N   . LYS   A 162 ? 0.2968 0.3670 0.3246 -0.0084 -0.0422 -0.0616 368 LYS   A N   
1309 C CA  . LYS   A 162 ? 0.3624 0.4336 0.3937 -0.0074 -0.0480 -0.0608 368 LYS   A CA  
1310 C C   . LYS   A 162 ? 0.3660 0.4340 0.3972 -0.0052 -0.0503 -0.0560 368 LYS   A C   
1311 O O   . LYS   A 162 ? 0.3716 0.4387 0.3997 -0.0049 -0.0562 -0.0541 368 LYS   A O   
1312 C CB  . LYS   A 162 ? 0.3801 0.4546 0.4241 -0.0064 -0.0476 -0.0640 368 LYS   A CB  
1313 C CG  . LYS   A 162 ? 0.4505 0.5276 0.4945 -0.0087 -0.0468 -0.0691 368 LYS   A CG  
1314 C CD  . LYS   A 162 ? 0.5001 0.5800 0.5562 -0.0083 -0.0473 -0.0721 368 LYS   A CD  
1315 C CE  . LYS   A 162 ? 0.5865 0.6684 0.6424 -0.0105 -0.0473 -0.0775 368 LYS   A CE  
1316 N NZ  . LYS   A 162 ? 0.6035 0.6868 0.6721 -0.0105 -0.0463 -0.0800 368 LYS   A NZ  
1317 N N   . LEU   A 163 ? 0.3421 0.4078 0.3761 -0.0034 -0.0461 -0.0540 369 LEU   A N   
1318 C CA  . LEU   A 163 ? 0.3543 0.4165 0.3878 -0.0011 -0.0481 -0.0499 369 LEU   A CA  
1319 C C   . LEU   A 163 ? 0.4091 0.4672 0.4297 -0.0030 -0.0514 -0.0465 369 LEU   A C   
1320 O O   . LEU   A 163 ? 0.4283 0.4838 0.4472 -0.0019 -0.0571 -0.0436 369 LEU   A O   
1321 C CB  . LEU   A 163 ? 0.3300 0.3909 0.3678 0.0005  -0.0424 -0.0490 369 LEU   A CB  
1322 C CG  . LEU   A 163 ? 0.4573 0.5159 0.4991 0.0037  -0.0433 -0.0464 369 LEU   A CG  
1323 C CD1 . LEU   A 163 ? 0.3044 0.3666 0.3570 0.0062  -0.0467 -0.0478 369 LEU   A CD1 
1324 C CD2 . LEU   A 163 ? 0.3489 0.4069 0.3937 0.0045  -0.0369 -0.0463 369 LEU   A CD2 
1325 N N   . LYS   A 164 ? 0.3659 0.4236 0.3774 -0.0060 -0.0481 -0.0468 370 LYS   A N   
1326 C CA  . LYS   A 164 ? 0.5096 0.5639 0.5081 -0.0088 -0.0505 -0.0434 370 LYS   A CA  
1327 C C   . LYS   A 164 ? 0.4144 0.4694 0.4064 -0.0109 -0.0570 -0.0430 370 LYS   A C   
1328 O O   . LYS   A 164 ? 0.4668 0.5179 0.4491 -0.0128 -0.0611 -0.0388 370 LYS   A O   
1329 C CB  . LYS   A 164 ? 0.3641 0.4197 0.3552 -0.0119 -0.0451 -0.0448 370 LYS   A CB  
1330 C CG  . LYS   A 164 ? 0.5397 0.5929 0.5326 -0.0106 -0.0400 -0.0434 370 LYS   A CG  
1331 C CD  . LYS   A 164 ? 0.5734 0.6286 0.5594 -0.0137 -0.0353 -0.0452 370 LYS   A CD  
1332 C CE  . LYS   A 164 ? 0.5200 0.5751 0.4927 -0.0182 -0.0378 -0.0433 370 LYS   A CE  
1333 N NZ  . LYS   A 164 ? 0.5773 0.6263 0.5444 -0.0184 -0.0421 -0.0372 370 LYS   A NZ  
1334 N N   . HIS   A 165 ? 0.4100 0.4696 0.4067 -0.0111 -0.0580 -0.0471 371 HIS   A N   
1335 C CA  . HIS   A 165 ? 0.4442 0.5050 0.4350 -0.0132 -0.0643 -0.0473 371 HIS   A CA  
1336 C C   . HIS   A 165 ? 0.4472 0.5052 0.4416 -0.0107 -0.0718 -0.0440 371 HIS   A C   
1337 O O   . HIS   A 165 ? 0.5075 0.5649 0.4950 -0.0125 -0.0782 -0.0427 371 HIS   A O   
1338 C CB  . HIS   A 165 ? 0.5172 0.5838 0.5135 -0.0138 -0.0629 -0.0533 371 HIS   A CB  
1339 C CG  . HIS   A 165 ? 0.6883 0.7572 0.6768 -0.0168 -0.0681 -0.0548 371 HIS   A CG  
1340 N ND1 . HIS   A 165 ? 0.6621 0.7311 0.6360 -0.0212 -0.0685 -0.0539 371 HIS   A ND1 
1341 C CD2 . HIS   A 165 ? 0.6485 0.7204 0.6419 -0.0164 -0.0730 -0.0573 371 HIS   A CD2 
1342 C CE1 . HIS   A 165 ? 0.7457 0.8173 0.7150 -0.0233 -0.0736 -0.0557 371 HIS   A CE1 
1343 N NE2 . HIS   A 165 ? 0.6706 0.7438 0.6517 -0.0203 -0.0765 -0.0579 371 HIS   A NE2 
1344 N N   . LEU   A 166 ? 0.4140 0.4703 0.4188 -0.0065 -0.0713 -0.0429 372 LEU   A N   
1345 C CA  . LEU   A 166 ? 0.3826 0.4366 0.3920 -0.0036 -0.0786 -0.0403 372 LEU   A CA  
1346 C C   . LEU   A 166 ? 0.4434 0.4903 0.4411 -0.0050 -0.0834 -0.0346 372 LEU   A C   
1347 O O   . LEU   A 166 ? 0.4685 0.5121 0.4587 -0.0069 -0.0796 -0.0322 372 LEU   A O   
1348 C CB  . LEU   A 166 ? 0.3374 0.3922 0.3609 0.0011  -0.0760 -0.0413 372 LEU   A CB  
1349 C CG  . LEU   A 166 ? 0.3507 0.4123 0.3868 0.0022  -0.0723 -0.0463 372 LEU   A CG  
1350 C CD1 . LEU   A 166 ? 0.3463 0.4095 0.3951 0.0061  -0.0691 -0.0471 372 LEU   A CD1 
1351 C CD2 . LEU   A 166 ? 0.3289 0.3942 0.3690 0.0023  -0.0788 -0.0484 372 LEU   A CD2 
1352 N N   . PRO   A 167 ? 0.4748 0.5190 0.4704 -0.0046 -0.0922 -0.0320 373 PRO   A N   
1353 C CA  . PRO   A 167 ? 0.4237 0.4603 0.4068 -0.0068 -0.0976 -0.0259 373 PRO   A CA  
1354 C C   . PRO   A 167 ? 0.5033 0.5337 0.4909 -0.0032 -0.0992 -0.0225 373 PRO   A C   
1355 O O   . PRO   A 167 ? 0.5351 0.5584 0.5122 -0.0054 -0.1024 -0.0173 373 PRO   A O   
1356 C CB  . PRO   A 167 ? 0.4343 0.4704 0.4142 -0.0076 -0.1072 -0.0246 373 PRO   A CB  
1357 C CG  . PRO   A 167 ? 0.4741 0.5159 0.4700 -0.0031 -0.1081 -0.0294 373 PRO   A CG  
1358 C CD  . PRO   A 167 ? 0.4580 0.5060 0.4614 -0.0028 -0.0981 -0.0344 373 PRO   A CD  
1359 N N   . GLU   A 168 ? 0.4549 0.4875 0.4574 0.0021  -0.0974 -0.0254 374 GLU   A N   
1360 C CA  . GLU   A 168 ? 0.4477 0.4749 0.4555 0.0060  -0.0996 -0.0231 374 GLU   A CA  
1361 C C   . GLU   A 168 ? 0.4860 0.5165 0.5034 0.0088  -0.0910 -0.0263 374 GLU   A C   
1362 O O   . GLU   A 168 ? 0.3980 0.4357 0.4240 0.0096  -0.0858 -0.0309 374 GLU   A O   
1363 C CB  . GLU   A 168 ? 0.4723 0.4987 0.4899 0.0105  -0.1084 -0.0234 374 GLU   A CB  
1364 C CG  . GLU   A 168 ? 0.5501 0.5728 0.5588 0.0081  -0.1181 -0.0198 374 GLU   A CG  
1365 C CD  . GLU   A 168 ? 0.7127 0.7253 0.7074 0.0052  -0.1228 -0.0131 374 GLU   A CD  
1366 O OE1 . GLU   A 168 ? 0.7481 0.7556 0.7443 0.0070  -0.1212 -0.0113 374 GLU   A OE1 
1367 O OE2 . GLU   A 168 ? 0.8215 0.8313 0.8032 0.0006  -0.1280 -0.0095 374 GLU   A OE2 
1368 N N   . LYS   A 169 ? 0.4671 0.4918 0.4828 0.0099  -0.0901 -0.0237 375 LYS   A N   
1369 C CA  . LYS   A 169 ? 0.4685 0.4954 0.4922 0.0126  -0.0827 -0.0263 375 LYS   A CA  
1370 C C   . LYS   A 169 ? 0.4172 0.4500 0.4571 0.0175  -0.0825 -0.0307 375 LYS   A C   
1371 O O   . LYS   A 169 ? 0.3713 0.4098 0.4184 0.0183  -0.0752 -0.0342 375 LYS   A O   
1372 C CB  . LYS   A 169 ? 0.4266 0.4455 0.4460 0.0133  -0.0837 -0.0226 375 LYS   A CB  
1373 C CG  . LYS   A 169 ? 0.5509 0.5714 0.5765 0.0156  -0.0765 -0.0249 375 LYS   A CG  
1374 C CD  . LYS   A 169 ? 0.7590 0.7717 0.7761 0.0142  -0.0762 -0.0210 375 LYS   A CD  
1375 C CE  . LYS   A 169 ? 0.9127 0.9187 0.9342 0.0182  -0.0837 -0.0194 375 LYS   A CE  
1376 N NZ  . LYS   A 169 ? 1.0286 1.0390 1.0656 0.0243  -0.0833 -0.0241 375 LYS   A NZ  
1377 N N   . TYR   A 170 ? 0.3889 0.4208 0.4351 0.0208  -0.0904 -0.0307 376 TYR   A N   
1378 C CA  A TYR   A 170 ? 0.4153 0.4539 0.4779 0.0255  -0.0900 -0.0354 376 TYR   A CA  
1379 C CA  B TYR   A 170 ? 0.4153 0.4539 0.4779 0.0255  -0.0900 -0.0354 376 TYR   A CA  
1380 C C   . TYR   A 170 ? 0.3698 0.4176 0.4386 0.0241  -0.0861 -0.0394 376 TYR   A C   
1381 O O   . TYR   A 170 ? 0.3523 0.4069 0.4328 0.0262  -0.0812 -0.0434 376 TYR   A O   
1382 C CB  A TYR   A 170 ? 0.4012 0.4369 0.4700 0.0296  -0.1000 -0.0350 376 TYR   A CB  
1383 C CB  B TYR   A 170 ? 0.4012 0.4369 0.4700 0.0296  -0.1000 -0.0350 376 TYR   A CB  
1384 C CG  A TYR   A 170 ? 0.4814 0.5182 0.5490 0.0285  -0.1076 -0.0344 376 TYR   A CG  
1385 C CG  B TYR   A 170 ? 0.4814 0.5182 0.5490 0.0285  -0.1076 -0.0344 376 TYR   A CG  
1386 C CD1 A TYR   A 170 ? 0.5009 0.5468 0.5806 0.0301  -0.1078 -0.0391 376 TYR   A CD1 
1387 C CD1 B TYR   A 170 ? 0.5010 0.5469 0.5806 0.0301  -0.1078 -0.0391 376 TYR   A CD1 
1388 C CD2 A TYR   A 170 ? 0.5231 0.5519 0.5777 0.0257  -0.1151 -0.0292 376 TYR   A CD2 
1389 C CD2 B TYR   A 170 ? 0.5231 0.5519 0.5777 0.0257  -0.1151 -0.0292 376 TYR   A CD2 
1390 C CE1 A TYR   A 170 ? 0.5310 0.5780 0.6098 0.0292  -0.1152 -0.0388 376 TYR   A CE1 
1391 C CE1 B TYR   A 170 ? 0.5310 0.5780 0.6098 0.0292  -0.1152 -0.0388 376 TYR   A CE1 
1392 C CE2 A TYR   A 170 ? 0.5086 0.5383 0.5614 0.0246  -0.1225 -0.0286 376 TYR   A CE2 
1393 C CE2 B TYR   A 170 ? 0.5086 0.5383 0.5614 0.0246  -0.1225 -0.0286 376 TYR   A CE2 
1394 C CZ  A TYR   A 170 ? 0.5465 0.5853 0.6115 0.0266  -0.1227 -0.0335 376 TYR   A CZ  
1395 C CZ  B TYR   A 170 ? 0.5465 0.5853 0.6116 0.0266  -0.1227 -0.0335 376 TYR   A CZ  
1396 O OH  A TYR   A 170 ? 0.6426 0.6825 0.7061 0.0255  -0.1303 -0.0332 376 TYR   A OH  
1397 O OH  B TYR   A 170 ? 0.6426 0.6825 0.7061 0.0255  -0.1303 -0.0332 376 TYR   A OH  
1398 N N   . MET   A 171 ? 0.3703 0.4184 0.4311 0.0203  -0.0879 -0.0385 377 MET   A N   
1399 C CA  . MET   A 171 ? 0.4117 0.4678 0.4783 0.0187  -0.0843 -0.0425 377 MET   A CA  
1400 C C   . MET   A 171 ? 0.3255 0.3841 0.3916 0.0168  -0.0744 -0.0439 377 MET   A C   
1401 O O   . MET   A 171 ? 0.3539 0.4191 0.4297 0.0171  -0.0699 -0.0475 377 MET   A O   
1402 C CB  . MET   A 171 ? 0.3825 0.4384 0.4403 0.0150  -0.0886 -0.0417 377 MET   A CB  
1403 C CG  . MET   A 171 ? 0.3980 0.4503 0.4534 0.0161  -0.0993 -0.0392 377 MET   A CG  
1404 S SD  . MET   A 171 ? 0.4009 0.4518 0.4414 0.0107  -0.1039 -0.0374 377 MET   A SD  
1405 C CE  . MET   A 171 ? 0.3800 0.4253 0.4193 0.0129  -0.1171 -0.0338 377 MET   A CE  
1406 N N   . MET   A 172 ? 0.3641 0.4173 0.4190 0.0146  -0.0713 -0.0410 378 MET   A N   
1407 C CA  . MET   A 172 ? 0.3274 0.3819 0.3815 0.0131  -0.0627 -0.0420 378 MET   A CA  
1408 C C   . MET   A 172 ? 0.2808 0.3380 0.3458 0.0165  -0.0587 -0.0438 378 MET   A C   
1409 O O   . MET   A 172 ? 0.3238 0.3860 0.3953 0.0161  -0.0529 -0.0464 378 MET   A O   
1410 C CB  . MET   A 172 ? 0.3940 0.4419 0.4347 0.0107  -0.0617 -0.0383 378 MET   A CB  
1411 C CG  . MET   A 172 ? 0.4376 0.4844 0.4666 0.0064  -0.0635 -0.0372 378 MET   A CG  
1412 S SD  . MET   A 172 ? 0.4585 0.4998 0.4731 0.0028  -0.0604 -0.0336 378 MET   A SD  
1413 C CE  . MET   A 172 ? 0.3736 0.4138 0.3746 -0.0020 -0.0656 -0.0318 378 MET   A CE  
1414 N N   . ASN   A 173 ? 0.3022 0.3562 0.3696 0.0199  -0.0621 -0.0426 379 ASN   A N   
1415 C CA  . ASN   A 173 ? 0.3355 0.3927 0.4131 0.0232  -0.0584 -0.0448 379 ASN   A CA  
1416 C C   . ASN   A 173 ? 0.3832 0.4493 0.4744 0.0246  -0.0577 -0.0490 379 ASN   A C   
1417 O O   . ASN   A 173 ? 0.3460 0.4172 0.4444 0.0251  -0.0516 -0.0513 379 ASN   A O   
1418 C CB  . ASN   A 173 ? 0.3122 0.3640 0.3902 0.0268  -0.0631 -0.0433 379 ASN   A CB  
1419 C CG  . ASN   A 173 ? 0.3857 0.4302 0.4531 0.0254  -0.0608 -0.0399 379 ASN   A CG  
1420 O OD1 . ASN   A 173 ? 0.3497 0.3948 0.4125 0.0228  -0.0543 -0.0397 379 ASN   A OD1 
1421 N ND2 . ASN   A 173 ? 0.3384 0.3756 0.4018 0.0270  -0.0665 -0.0372 379 ASN   A ND2 
1422 N N   . SER   A 174 ? 0.3309 0.3993 0.4255 0.0249  -0.0637 -0.0500 380 SER   A N   
1423 C CA  . SER   A 174 ? 0.3398 0.4174 0.4478 0.0257  -0.0630 -0.0541 380 SER   A CA  
1424 C C   . SER   A 174 ? 0.3359 0.4177 0.4444 0.0220  -0.0563 -0.0555 380 SER   A C   
1425 O O   . SER   A 174 ? 0.3682 0.4571 0.4872 0.0221  -0.0520 -0.0584 380 SER   A O   
1426 C CB  . SER   A 174 ? 0.3694 0.4483 0.4803 0.0265  -0.0713 -0.0548 380 SER   A CB  
1427 O OG  . SER   A 174 ? 0.4586 0.5355 0.5742 0.0309  -0.0776 -0.0546 380 SER   A OG  
1428 N N   . VAL   A 175 ? 0.3139 0.3917 0.4116 0.0185  -0.0555 -0.0536 381 VAL   A N   
1429 C CA  . VAL   A 175 ? 0.3454 0.4260 0.4435 0.0151  -0.0496 -0.0550 381 VAL   A CA  
1430 C C   . VAL   A 175 ? 0.3850 0.4653 0.4837 0.0151  -0.0422 -0.0545 381 VAL   A C   
1431 O O   . VAL   A 175 ? 0.3655 0.4505 0.4710 0.0137  -0.0375 -0.0563 381 VAL   A O   
1432 C CB  . VAL   A 175 ? 0.3256 0.4020 0.4119 0.0118  -0.0508 -0.0538 381 VAL   A CB  
1433 C CG1 . VAL   A 175 ? 0.3163 0.3940 0.4023 0.0088  -0.0447 -0.0552 381 VAL   A CG1 
1434 C CG2 . VAL   A 175 ? 0.2865 0.3640 0.3719 0.0113  -0.0579 -0.0546 381 VAL   A CG2 
1435 N N   . LEU   A 176 ? 0.3262 0.4008 0.4175 0.0162  -0.0415 -0.0520 382 LEU   A N   
1436 C CA  . LEU   A 176 ? 0.3187 0.3926 0.4093 0.0161  -0.0349 -0.0513 382 LEU   A CA  
1437 C C   . LEU   A 176 ? 0.3454 0.4248 0.4468 0.0184  -0.0323 -0.0534 382 LEU   A C   
1438 O O   . LEU   A 176 ? 0.3542 0.4348 0.4564 0.0175  -0.0265 -0.0534 382 LEU   A O   
1439 C CB  . LEU   A 176 ? 0.2889 0.3554 0.3692 0.0166  -0.0352 -0.0483 382 LEU   A CB  
1440 C CG  . LEU   A 176 ? 0.2845 0.3467 0.3537 0.0136  -0.0359 -0.0465 382 LEU   A CG  
1441 C CD1 . LEU   A 176 ? 0.3620 0.4174 0.4215 0.0138  -0.0370 -0.0433 382 LEU   A CD1 
1442 C CD2 . LEU   A 176 ? 0.3113 0.3751 0.3802 0.0109  -0.0302 -0.0475 382 LEU   A CD2 
1443 N N   . GLU   A 177 ? 0.3465 0.4298 0.4562 0.0212  -0.0366 -0.0554 383 GLU   A N   
1444 C CA  . GLU   A 177 ? 0.3808 0.4712 0.5019 0.0233  -0.0339 -0.0583 383 GLU   A CA  
1445 C C   . GLU   A 177 ? 0.3886 0.4857 0.5159 0.0201  -0.0282 -0.0599 383 GLU   A C   
1446 O O   . GLU   A 177 ? 0.3470 0.4495 0.4806 0.0202  -0.0235 -0.0615 383 GLU   A O   
1447 C CB  . GLU   A 177 ? 0.4130 0.5074 0.5433 0.0267  -0.0402 -0.0608 383 GLU   A CB  
1448 C CG  . GLU   A 177 ? 0.4909 0.5815 0.6213 0.0311  -0.0444 -0.0607 383 GLU   A CG  
1449 C CD  . GLU   A 177 ? 0.6476 0.7409 0.7863 0.0343  -0.0522 -0.0628 383 GLU   A CD  
1450 O OE1 . GLU   A 177 ? 0.5988 0.7005 0.7476 0.0337  -0.0520 -0.0659 383 GLU   A OE1 
1451 O OE2 . GLU   A 177 ? 0.6785 0.7651 0.8132 0.0368  -0.0590 -0.0610 383 GLU   A OE2 
1452 N N   . ASN   A 178 ? 0.3512 0.4481 0.4768 0.0169  -0.0289 -0.0596 384 ASN   A N   
1453 C CA  . ASN   A 178 ? 0.3751 0.4774 0.5067 0.0134  -0.0244 -0.0608 384 ASN   A CA  
1454 C C   . ASN   A 178 ? 0.3933 0.4905 0.5168 0.0100  -0.0203 -0.0585 384 ASN   A C   
1455 O O   . ASN   A 178 ? 0.3374 0.4371 0.4645 0.0067  -0.0175 -0.0589 384 ASN   A O   
1456 C CB  . ASN   A 178 ? 0.4153 0.5220 0.5535 0.0123  -0.0286 -0.0630 384 ASN   A CB  
1457 C CG  . ASN   A 178 ? 0.4855 0.5976 0.6328 0.0159  -0.0333 -0.0655 384 ASN   A CG  
1458 O OD1 . ASN   A 178 ? 0.3773 0.4961 0.5337 0.0173  -0.0307 -0.0677 384 ASN   A OD1 
1459 N ND2 . ASN   A 178 ? 0.4488 0.5581 0.5936 0.0174  -0.0404 -0.0654 384 ASN   A ND2 
1460 N N   . PHE   A 179 ? 0.3082 0.3982 0.4212 0.0108  -0.0202 -0.0561 385 PHE   A N   
1461 C CA  . PHE   A 179 ? 0.3192 0.4043 0.4247 0.0082  -0.0168 -0.0542 385 PHE   A CA  
1462 C C   . PHE   A 179 ? 0.2815 0.3650 0.3844 0.0087  -0.0120 -0.0526 385 PHE   A C   
1463 O O   . PHE   A 179 ? 0.3292 0.4102 0.4286 0.0114  -0.0128 -0.0518 385 PHE   A O   
1464 C CB  . PHE   A 179 ? 0.2947 0.3737 0.3903 0.0082  -0.0203 -0.0531 385 PHE   A CB  
1465 C CG  . PHE   A 179 ? 0.3592 0.4336 0.4475 0.0062  -0.0171 -0.0518 385 PHE   A CG  
1466 C CD1 . PHE   A 179 ? 0.3671 0.4417 0.4565 0.0034  -0.0162 -0.0530 385 PHE   A CD1 
1467 C CD2 . PHE   A 179 ? 0.2657 0.3354 0.3466 0.0071  -0.0152 -0.0496 385 PHE   A CD2 
1468 C CE1 . PHE   A 179 ? 0.3363 0.4067 0.4200 0.0020  -0.0137 -0.0523 385 PHE   A CE1 
1469 C CE2 . PHE   A 179 ? 0.3229 0.3889 0.3981 0.0054  -0.0125 -0.0488 385 PHE   A CE2 
1470 C CZ  . PHE   A 179 ? 0.3010 0.3674 0.3777 0.0030  -0.0118 -0.0501 385 PHE   A CZ  
1471 N N   . THR   A 180 ? 0.2950 0.3795 0.3995 0.0060  -0.0074 -0.0520 386 THR   A N   
1472 C CA  . THR   A 180 ? 0.3159 0.3987 0.4170 0.0061  -0.0030 -0.0503 386 THR   A CA  
1473 C C   . THR   A 180 ? 0.2921 0.3707 0.3888 0.0031  -0.0003 -0.0484 386 THR   A C   
1474 O O   . THR   A 180 ? 0.2866 0.3648 0.3850 0.0008  -0.0011 -0.0489 386 THR   A O   
1475 C CB  . THR   A 180 ? 0.2928 0.3827 0.4017 0.0060  0.0004  -0.0514 386 THR   A CB  
1476 O OG1 . THR   A 180 ? 0.2942 0.3883 0.4094 0.0024  0.0021  -0.0519 386 THR   A OG1 
1477 C CG2 . THR   A 180 ? 0.2812 0.3757 0.3959 0.0096  -0.0024 -0.0540 386 THR   A CG2 
1478 N N   . ILE   A 181 ? 0.2844 0.3597 0.3757 0.0033  0.0027  -0.0465 387 ILE   A N   
1479 C CA  . ILE   A 181 ? 0.2293 0.3004 0.3167 0.0008  0.0050  -0.0446 387 ILE   A CA  
1480 C C   . ILE   A 181 ? 0.2400 0.3125 0.3274 -0.0001 0.0092  -0.0430 387 ILE   A C   
1481 O O   . ILE   A 181 ? 0.3032 0.3765 0.3887 0.0021  0.0103  -0.0430 387 ILE   A O   
1482 C CB  . ILE   A 181 ? 0.2283 0.2931 0.3074 0.0018  0.0036  -0.0438 387 ILE   A CB  
1483 C CG1 . ILE   A 181 ? 0.2567 0.3209 0.3351 0.0020  -0.0003 -0.0456 387 ILE   A CG1 
1484 C CG2 . ILE   A 181 ? 0.2231 0.2839 0.2993 -0.0001 0.0058  -0.0421 387 ILE   A CG2 
1485 C CD1 . ILE   A 181 ? 0.2341 0.2933 0.3043 0.0024  -0.0015 -0.0453 387 ILE   A CD1 
1486 N N   . LEU   A 182 ? 0.2771 0.3496 0.3665 -0.0035 0.0114  -0.0415 388 LEU   A N   
1487 C CA  . LEU   A 182 ? 0.2410 0.3146 0.3291 -0.0052 0.0153  -0.0395 388 LEU   A CA  
1488 C C   . LEU   A 182 ? 0.3735 0.4400 0.4554 -0.0065 0.0156  -0.0368 388 LEU   A C   
1489 O O   . LEU   A 182 ? 0.3222 0.3855 0.4053 -0.0086 0.0143  -0.0362 388 LEU   A O   
1490 C CB  . LEU   A 182 ? 0.2300 0.3095 0.3251 -0.0089 0.0176  -0.0394 388 LEU   A CB  
1491 C CG  . LEU   A 182 ? 0.2733 0.3551 0.3666 -0.0114 0.0219  -0.0372 388 LEU   A CG  
1492 C CD1 . LEU   A 182 ? 0.2904 0.3763 0.3823 -0.0083 0.0239  -0.0390 388 LEU   A CD1 
1493 C CD2 . LEU   A 182 ? 0.2752 0.3627 0.3752 -0.0160 0.0240  -0.0367 388 LEU   A CD2 
1494 N N   . LEU   A 183 ? 0.2789 0.3428 0.3546 -0.0050 0.0170  -0.0356 389 LEU   A N   
1495 C CA  A LEU   A 183 ? 0.2959 0.3536 0.3661 -0.0058 0.0171  -0.0332 389 LEU   A CA  
1496 C CA  B LEU   A 183 ? 0.2958 0.3534 0.3659 -0.0058 0.0171  -0.0332 389 LEU   A CA  
1497 C C   . LEU   A 183 ? 0.3255 0.3841 0.3939 -0.0083 0.0203  -0.0306 389 LEU   A C   
1498 O O   . LEU   A 183 ? 0.3394 0.4020 0.4069 -0.0075 0.0227  -0.0311 389 LEU   A O   
1499 C CB  A LEU   A 183 ? 0.3299 0.3839 0.3940 -0.0026 0.0159  -0.0338 389 LEU   A CB  
1500 C CB  B LEU   A 183 ? 0.3382 0.3922 0.4021 -0.0026 0.0160  -0.0337 389 LEU   A CB  
1501 C CG  A LEU   A 183 ? 0.3042 0.3524 0.3626 -0.0027 0.0159  -0.0318 389 LEU   A CG  
1502 C CG  B LEU   A 183 ? 0.2954 0.3483 0.3587 -0.0003 0.0130  -0.0358 389 LEU   A CG  
1503 C CD1 A LEU   A 183 ? 0.4196 0.4644 0.4769 -0.0016 0.0131  -0.0333 389 LEU   A CD1 
1504 C CD1 B LEU   A 183 ? 0.3472 0.3972 0.4041 0.0021  0.0127  -0.0356 389 LEU   A CD1 
1505 C CD2 A LEU   A 183 ? 0.3483 0.3959 0.4014 -0.0010 0.0173  -0.0312 389 LEU   A CD2 
1506 C CD2 B LEU   A 183 ? 0.3216 0.3716 0.3859 -0.0015 0.0110  -0.0365 389 LEU   A CD2 
1507 N N   . VAL   A 184 ? 0.2409 0.2959 0.3091 -0.0115 0.0202  -0.0280 390 VAL   A N   
1508 C CA  . VAL   A 184 ? 0.2746 0.3297 0.3399 -0.0147 0.0228  -0.0247 390 VAL   A CA  
1509 C C   . VAL   A 184 ? 0.3735 0.4208 0.4338 -0.0152 0.0211  -0.0219 390 VAL   A C   
1510 O O   . VAL   A 184 ? 0.3737 0.4163 0.4362 -0.0159 0.0183  -0.0215 390 VAL   A O   
1511 C CB  . VAL   A 184 ? 0.3264 0.3854 0.3968 -0.0193 0.0244  -0.0233 390 VAL   A CB  
1512 C CG1 . VAL   A 184 ? 0.3036 0.3625 0.3695 -0.0231 0.0270  -0.0195 390 VAL   A CG1 
1513 C CG2 . VAL   A 184 ? 0.3376 0.4056 0.4142 -0.0187 0.0260  -0.0266 390 VAL   A CG2 
1514 N N   . VAL   A 185 ? 0.3239 0.3699 0.3780 -0.0147 0.0225  -0.0203 391 VAL   A N   
1515 C CA  . VAL   A 185 ? 0.2939 0.3328 0.3434 -0.0152 0.0207  -0.0175 391 VAL   A CA  
1516 C C   . VAL   A 185 ? 0.3494 0.3881 0.3956 -0.0195 0.0224  -0.0134 391 VAL   A C   
1517 O O   . VAL   A 185 ? 0.3368 0.3807 0.3802 -0.0204 0.0258  -0.0132 391 VAL   A O   
1518 C CB  . VAL   A 185 ? 0.3444 0.3812 0.3890 -0.0114 0.0201  -0.0188 391 VAL   A CB  
1519 C CG1 . VAL   A 185 ? 0.3068 0.3366 0.3482 -0.0116 0.0176  -0.0165 391 VAL   A CG1 
1520 C CG2 . VAL   A 185 ? 0.3036 0.3415 0.3508 -0.0079 0.0187  -0.0226 391 VAL   A CG2 
1521 N N   . THR   A 186 ? 0.3477 0.3803 0.3939 -0.0222 0.0199  -0.0101 392 THR   A N   
1522 C CA  . THR   A 186 ? 0.3491 0.3806 0.3923 -0.0273 0.0208  -0.0053 392 THR   A CA  
1523 C C   . THR   A 186 ? 0.3915 0.4147 0.4298 -0.0274 0.0175  -0.0019 392 THR   A C   
1524 O O   . THR   A 186 ? 0.4229 0.4405 0.4636 -0.0248 0.0137  -0.0031 392 THR   A O   
1525 C CB  . THR   A 186 ? 0.3761 0.4077 0.4254 -0.0315 0.0200  -0.0039 392 THR   A CB  
1526 O OG1 . THR   A 186 ? 0.4291 0.4688 0.4838 -0.0311 0.0227  -0.0074 392 THR   A OG1 
1527 C CG2 . THR   A 186 ? 0.3981 0.4283 0.4436 -0.0377 0.0209  0.0017  392 THR   A CG2 
1528 N N   . ASN   A 187 ? 0.3569 0.3797 0.3884 -0.0305 0.0188  0.0020  393 ASN   A N   
1529 C CA  . ASN   A 187 ? 0.4213 0.4358 0.4482 -0.0316 0.0150  0.0062  393 ASN   A CA  
1530 C C   . ASN   A 187 ? 0.4620 0.4708 0.4927 -0.0357 0.0118  0.0098  393 ASN   A C   
1531 O O   . ASN   A 187 ? 0.4246 0.4360 0.4549 -0.0410 0.0138  0.0128  393 ASN   A O   
1532 C CB  . ASN   A 187 ? 0.4940 0.5103 0.5119 -0.0342 0.0174  0.0093  393 ASN   A CB  
1533 C CG  . ASN   A 187 ? 0.5364 0.5441 0.5488 -0.0356 0.0130  0.0141  393 ASN   A CG  
1534 O OD1 . ASN   A 187 ? 0.5743 0.5745 0.5896 -0.0368 0.0084  0.0168  393 ASN   A OD1 
1535 N ND2 . ASN   A 187 ? 0.5475 0.5562 0.5520 -0.0353 0.0142  0.0151  393 ASN   A ND2 
1536 N N   . ARG   A 188 ? 0.4186 0.4200 0.4535 -0.0334 0.0068  0.0091  394 ARG   A N   
1537 C CA  . ARG   A 188 ? 0.5171 0.5131 0.5572 -0.0368 0.0034  0.0116  394 ARG   A CA  
1538 C C   . ARG   A 188 ? 0.5300 0.5206 0.5648 -0.0429 0.0016  0.0188  394 ARG   A C   
1539 O O   . ARG   A 188 ? 0.7041 0.6926 0.7418 -0.0478 0.0006  0.0219  394 ARG   A O   
1540 C CB  . ARG   A 188 ? 0.4762 0.4655 0.5224 -0.0328 -0.0018 0.0086  394 ARG   A CB  
1541 C CG  . ARG   A 188 ? 0.5465 0.5307 0.5997 -0.0355 -0.0054 0.0095  394 ARG   A CG  
1542 C CD  . ARG   A 188 ? 0.5047 0.4830 0.5639 -0.0311 -0.0104 0.0058  394 ARG   A CD  
1543 N NE  . ARG   A 188 ? 0.4841 0.4538 0.5411 -0.0305 -0.0154 0.0089  394 ARG   A NE  
1544 C CZ  . ARG   A 188 ? 0.4405 0.4040 0.5035 -0.0271 -0.0207 0.0061  394 ARG   A CZ  
1545 N NH1 . ARG   A 188 ? 0.4770 0.4416 0.5477 -0.0245 -0.0215 0.0004  394 ARG   A NH1 
1546 N NH2 . ARG   A 188 ? 0.4751 0.4313 0.5363 -0.0260 -0.0253 0.0086  394 ARG   A NH2 
1547 N N   . ASP   A 189 ? 0.5715 0.5600 0.5983 -0.0431 0.0012  0.0219  395 ASP   A N   
1548 C CA  . ASP   A 189 ? 0.6988 0.6810 0.7197 -0.0488 -0.0015 0.0292  395 ASP   A CA  
1549 C C   . ASP   A 189 ? 0.7113 0.7005 0.7255 -0.0551 0.0040  0.0327  395 ASP   A C   
1550 O O   . ASP   A 189 ? 0.8330 0.8186 0.8447 -0.0617 0.0026  0.0387  395 ASP   A O   
1551 C CB  . ASP   A 189 ? 0.7314 0.7071 0.7468 -0.0462 -0.0056 0.0311  395 ASP   A CB  
1552 C CG  . ASP   A 189 ? 0.9802 0.9492 1.0031 -0.0405 -0.0112 0.0275  395 ASP   A CG  
1553 O OD1 . ASP   A 189 ? 0.9235 0.8894 0.9545 -0.0404 -0.0136 0.0260  395 ASP   A OD1 
1554 O OD2 . ASP   A 189 ? 0.8881 0.8555 0.9091 -0.0361 -0.0130 0.0257  395 ASP   A OD2 
1555 N N   . THR   A 190 ? 0.6882 0.6878 0.7001 -0.0533 0.0100  0.0288  396 THR   A N   
1556 C CA  . THR   A 190 ? 0.5109 0.5191 0.5177 -0.0588 0.0158  0.0306  396 THR   A CA  
1557 C C   . THR   A 190 ? 0.5859 0.6035 0.6001 -0.0595 0.0205  0.0266  396 THR   A C   
1558 O O   . THR   A 190 ? 0.5462 0.5720 0.5579 -0.0644 0.0255  0.0276  396 THR   A O   
1559 C CB  . THR   A 190 ? 0.6261 0.6398 0.6252 -0.0565 0.0194  0.0287  396 THR   A CB  
1560 O OG1 . THR   A 190 ? 0.6300 0.6490 0.6342 -0.0498 0.0215  0.0216  396 THR   A OG1 
1561 C CG2 . THR   A 190 ? 0.7146 0.7195 0.7069 -0.0552 0.0145  0.0320  396 THR   A CG2 
1562 N N   . GLN   A 191 ? 0.5162 0.5334 0.5393 -0.0548 0.0190  0.0219  397 GLN   A N   
1563 C CA  . GLN   A 191 ? 0.4747 0.5005 0.5056 -0.0543 0.0225  0.0173  397 GLN   A CA  
1564 C C   . GLN   A 191 ? 0.4662 0.5032 0.4956 -0.0522 0.0283  0.0129  397 GLN   A C   
1565 O O   . GLN   A 191 ? 0.4711 0.5167 0.5064 -0.0527 0.0317  0.0097  397 GLN   A O   
1566 C CB  . GLN   A 191 ? 0.4796 0.5067 0.5139 -0.0615 0.0232  0.0208  397 GLN   A CB  
1567 C CG  . GLN   A 191 ? 0.5733 0.5899 0.6127 -0.0622 0.0170  0.0231  397 GLN   A CG  
1568 C CD  . GLN   A 191 ? 0.7246 0.7413 0.7729 -0.0563 0.0152  0.0169  397 GLN   A CD  
1569 O OE1 . GLN   A 191 ? 0.7116 0.7368 0.7654 -0.0553 0.0184  0.0126  397 GLN   A OE1 
1570 N NE2 . GLN   A 191 ? 0.7852 0.7928 0.8349 -0.0522 0.0099  0.0161  397 GLN   A NE2 
1571 N N   . GLU   A 192 ? 0.4270 0.4642 0.4495 -0.0494 0.0292  0.0123  398 GLU   A N   
1572 C CA  . GLU   A 192 ? 0.4829 0.5300 0.5048 -0.0466 0.0342  0.0074  398 GLU   A CA  
1573 C C   . GLU   A 192 ? 0.5090 0.5572 0.5376 -0.0398 0.0332  0.0015  398 GLU   A C   
1574 O O   . GLU   A 192 ? 0.4075 0.4485 0.4368 -0.0359 0.0291  0.0010  398 GLU   A O   
1575 C CB  . GLU   A 192 ? 0.5451 0.5921 0.5574 -0.0460 0.0354  0.0083  398 GLU   A CB  
1576 C CG  . GLU   A 192 ? 0.7080 0.7479 0.7182 -0.0402 0.0316  0.0070  398 GLU   A CG  
1577 C CD  . GLU   A 192 ? 0.8520 0.8926 0.8531 -0.0395 0.0328  0.0073  398 GLU   A CD  
1578 O OE1 . GLU   A 192 ? 0.8510 0.8837 0.8467 -0.0398 0.0290  0.0109  398 GLU   A OE1 
1579 O OE2 . GLU   A 192 ? 0.7641 0.8131 0.7637 -0.0390 0.0374  0.0038  398 GLU   A OE2 
1580 N N   . THR   A 193 ? 0.4321 0.4897 0.4655 -0.0384 0.0368  -0.0030 399 THR   A N   
1581 C CA  . THR   A 193 ? 0.3870 0.4459 0.4254 -0.0322 0.0359  -0.0083 399 THR   A CA  
1582 C C   . THR   A 193 ? 0.4182 0.4753 0.4508 -0.0278 0.0357  -0.0100 399 THR   A C   
1583 O O   . THR   A 193 ? 0.3998 0.4616 0.4278 -0.0283 0.0389  -0.0107 399 THR   A O   
1584 C CB  . THR   A 193 ? 0.4040 0.4733 0.4493 -0.0320 0.0393  -0.0124 399 THR   A CB  
1585 O OG1 . THR   A 193 ? 0.4100 0.4806 0.4614 -0.0363 0.0390  -0.0108 399 THR   A OG1 
1586 C CG2 . THR   A 193 ? 0.3431 0.4135 0.3929 -0.0257 0.0378  -0.0175 399 THR   A CG2 
1587 N N   . LEU   A 194 ? 0.3624 0.4128 0.3951 -0.0238 0.0319  -0.0108 400 LEU   A N   
1588 C CA  . LEU   A 194 ? 0.3271 0.3752 0.3548 -0.0198 0.0313  -0.0123 400 LEU   A CA  
1589 C C   . LEU   A 194 ? 0.3462 0.3986 0.3775 -0.0152 0.0320  -0.0173 400 LEU   A C   
1590 O O   . LEU   A 194 ? 0.3311 0.3854 0.3589 -0.0129 0.0334  -0.0193 400 LEU   A O   
1591 C CB  . LEU   A 194 ? 0.2957 0.3350 0.3218 -0.0182 0.0270  -0.0105 400 LEU   A CB  
1592 C CG  . LEU   A 194 ? 0.3749 0.4083 0.3968 -0.0219 0.0250  -0.0054 400 LEU   A CG  
1593 C CD1 . LEU   A 194 ? 0.3168 0.3423 0.3397 -0.0196 0.0203  -0.0050 400 LEU   A CD1 
1594 C CD2 . LEU   A 194 ? 0.3909 0.4253 0.4045 -0.0236 0.0269  -0.0034 400 LEU   A CD2 
1595 N N   . LEU   A 195 ? 0.3294 0.3830 0.3674 -0.0140 0.0308  -0.0193 401 LEU   A N   
1596 C CA  . LEU   A 195 ? 0.3343 0.3908 0.3757 -0.0098 0.0305  -0.0235 401 LEU   A CA  
1597 C C   . LEU   A 195 ? 0.3353 0.3955 0.3845 -0.0103 0.0300  -0.0252 401 LEU   A C   
1598 O O   . LEU   A 195 ? 0.3241 0.3813 0.3758 -0.0122 0.0281  -0.0235 401 LEU   A O   
1599 C CB  . LEU   A 195 ? 0.2966 0.3469 0.3352 -0.0063 0.0273  -0.0241 401 LEU   A CB  
1600 C CG  . LEU   A 195 ? 0.4007 0.4521 0.4413 -0.0023 0.0260  -0.0276 401 LEU   A CG  
1601 C CD1 . LEU   A 195 ? 0.3620 0.4182 0.4021 -0.0006 0.0282  -0.0300 401 LEU   A CD1 
1602 C CD2 . LEU   A 195 ? 0.3787 0.4241 0.4156 -0.0002 0.0233  -0.0274 401 LEU   A CD2 
1603 N N   . CYS   A 196 ? 0.2652 0.3319 0.3188 -0.0084 0.0313  -0.0286 402 CYS   A N   
1604 C CA  . CYS   A 196 ? 0.2560 0.3266 0.3174 -0.0082 0.0302  -0.0307 402 CYS   A CA  
1605 C C   . CYS   A 196 ? 0.3169 0.3888 0.3803 -0.0035 0.0285  -0.0343 402 CYS   A C   
1606 O O   . CYS   A 196 ? 0.3521 0.4273 0.4149 -0.0014 0.0300  -0.0365 402 CYS   A O   
1607 C CB  . CYS   A 196 ? 0.2469 0.3256 0.3134 -0.0117 0.0335  -0.0311 402 CYS   A CB  
1608 S SG  . CYS   A 196 ? 0.3441 0.4285 0.4211 -0.0110 0.0320  -0.0343 402 CYS   A SG  
1609 N N   . MET   A 197 ? 0.2768 0.3457 0.3421 -0.0018 0.0250  -0.0350 403 MET   A N   
1610 C CA  . MET   A 197 ? 0.2837 0.3528 0.3503 0.0022  0.0225  -0.0377 403 MET   A CA  
1611 C C   . MET   A 197 ? 0.2483 0.3213 0.3223 0.0021  0.0206  -0.0396 403 MET   A C   
1612 O O   . MET   A 197 ? 0.3158 0.3863 0.3906 0.0007  0.0187  -0.0387 403 MET   A O   
1613 C CB  . MET   A 197 ? 0.2655 0.3273 0.3261 0.0040  0.0197  -0.0368 403 MET   A CB  
1614 C CG  . MET   A 197 ? 0.3895 0.4479 0.4434 0.0047  0.0209  -0.0356 403 MET   A CG  
1615 S SD  . MET   A 197 ? 0.5066 0.5572 0.5541 0.0056  0.0182  -0.0342 403 MET   A SD  
1616 C CE  . MET   A 197 ? 0.4365 0.4874 0.4865 0.0078  0.0145  -0.0362 403 MET   A CE  
1617 N N   . ALA   A 198 ? 0.2456 0.3249 0.3253 0.0039  0.0209  -0.0425 404 ALA   A N   
1618 C CA  . ALA   A 198 ? 0.2358 0.3192 0.3230 0.0047  0.0185  -0.0447 404 ALA   A CA  
1619 C C   . ALA   A 198 ? 0.2903 0.3696 0.3753 0.0084  0.0140  -0.0456 404 ALA   A C   
1620 O O   . ALA   A 198 ? 0.2885 0.3675 0.3725 0.0115  0.0134  -0.0470 404 ALA   A O   
1621 C CB  . ALA   A 198 ? 0.2092 0.3021 0.3043 0.0048  0.0209  -0.0477 404 ALA   A CB  
1622 N N   . CYS   A 199 ? 0.2333 0.3090 0.3171 0.0080  0.0107  -0.0449 405 CYS   A N   
1623 C CA  . CYS   A 199 ? 0.2733 0.3441 0.3529 0.0105  0.0066  -0.0449 405 CYS   A CA  
1624 C C   . CYS   A 199 ? 0.3159 0.3899 0.4014 0.0121  0.0026  -0.0470 405 CYS   A C   
1625 O O   . CYS   A 199 ? 0.2705 0.3477 0.3607 0.0102  0.0021  -0.0477 405 CYS   A O   
1626 C CB  . CYS   A 199 ? 0.2451 0.3100 0.3180 0.0089  0.0056  -0.0429 405 CYS   A CB  
1627 S SG  . CYS   A 199 ? 0.3117 0.3729 0.3789 0.0070  0.0096  -0.0405 405 CYS   A SG  
1628 N N   . VAL   A 200 ? 0.2602 0.3328 0.3451 0.0154  -0.0007 -0.0478 406 VAL   A N   
1629 C CA  . VAL   A 200 ? 0.2365 0.3106 0.3257 0.0172  -0.0058 -0.0493 406 VAL   A CA  
1630 C C   . VAL   A 200 ? 0.2480 0.3147 0.3290 0.0182  -0.0101 -0.0473 406 VAL   A C   
1631 O O   . VAL   A 200 ? 0.2711 0.3325 0.3447 0.0181  -0.0091 -0.0454 406 VAL   A O   
1632 C CB  . VAL   A 200 ? 0.2924 0.3725 0.3906 0.0203  -0.0065 -0.0525 406 VAL   A CB  
1633 C CG1 . VAL   A 200 ? 0.3289 0.4173 0.4350 0.0183  -0.0017 -0.0544 406 VAL   A CG1 
1634 C CG2 . VAL   A 200 ? 0.2263 0.3035 0.3220 0.0232  -0.0063 -0.0528 406 VAL   A CG2 
1635 N N   . PHE   A 201 ? 0.2641 0.3306 0.3463 0.0188  -0.0153 -0.0477 407 PHE   A N   
1636 C CA  . PHE   A 201 ? 0.2874 0.3476 0.3607 0.0182  -0.0192 -0.0454 407 PHE   A CA  
1637 C C   . PHE   A 201 ? 0.3143 0.3732 0.3889 0.0204  -0.0259 -0.0455 407 PHE   A C   
1638 O O   . PHE   A 201 ? 0.2820 0.3456 0.3647 0.0218  -0.0284 -0.0476 407 PHE   A O   
1639 C CB  . PHE   A 201 ? 0.2236 0.2839 0.2936 0.0148  -0.0187 -0.0451 407 PHE   A CB  
1640 C CG  . PHE   A 201 ? 0.2656 0.3257 0.3338 0.0126  -0.0132 -0.0447 407 PHE   A CG  
1641 C CD1 . PHE   A 201 ? 0.2630 0.3279 0.3382 0.0116  -0.0097 -0.0460 407 PHE   A CD1 
1642 C CD2 . PHE   A 201 ? 0.2183 0.2736 0.2780 0.0114  -0.0118 -0.0428 407 PHE   A CD2 
1643 C CE1 . PHE   A 201 ? 0.2579 0.3218 0.3313 0.0095  -0.0054 -0.0451 407 PHE   A CE1 
1644 C CE2 . PHE   A 201 ? 0.2400 0.2949 0.2986 0.0097  -0.0074 -0.0425 407 PHE   A CE2 
1645 C CZ  . PHE   A 201 ? 0.3043 0.3630 0.3695 0.0088  -0.0045 -0.0435 407 PHE   A CZ  
1646 N N   . GLU   A 202 ? 0.3178 0.3698 0.3837 0.0204  -0.0290 -0.0428 408 GLU   A N   
1647 C CA  . GLU   A 202 ? 0.3214 0.3698 0.3853 0.0217  -0.0361 -0.0416 408 GLU   A CA  
1648 C C   . GLU   A 202 ? 0.3773 0.4197 0.4288 0.0186  -0.0375 -0.0382 408 GLU   A C   
1649 O O   . GLU   A 202 ? 0.3950 0.4359 0.4409 0.0164  -0.0330 -0.0372 408 GLU   A O   
1650 C CB  . GLU   A 202 ? 0.3410 0.3869 0.4086 0.0256  -0.0385 -0.0420 408 GLU   A CB  
1651 C CG  . GLU   A 202 ? 0.5454 0.5868 0.6126 0.0278  -0.0466 -0.0407 408 GLU   A CG  
1652 C CD  . GLU   A 202 ? 0.6458 0.6870 0.7211 0.0325  -0.0485 -0.0430 408 GLU   A CD  
1653 O OE1 . GLU   A 202 ? 0.5650 0.6136 0.6505 0.0346  -0.0449 -0.0470 408 GLU   A OE1 
1654 O OE2 . GLU   A 202 ? 0.7974 0.8312 0.8689 0.0340  -0.0538 -0.0409 408 GLU   A OE2 
1655 N N   . VAL   A 203 ? 0.3162 0.3554 0.3635 0.0181  -0.0439 -0.0364 409 VAL   A N   
1656 C CA  . VAL   A 203 ? 0.3545 0.3883 0.3895 0.0147  -0.0456 -0.0330 409 VAL   A CA  
1657 C C   . VAL   A 203 ? 0.3891 0.4158 0.4192 0.0155  -0.0476 -0.0300 409 VAL   A C   
1658 O O   . VAL   A 203 ? 0.4115 0.4356 0.4464 0.0189  -0.0518 -0.0300 409 VAL   A O   
1659 C CB  . VAL   A 203 ? 0.4108 0.4443 0.4422 0.0131  -0.0518 -0.0320 409 VAL   A CB  
1660 C CG1 . VAL   A 203 ? 0.4531 0.4810 0.4712 0.0094  -0.0542 -0.0281 409 VAL   A CG1 
1661 C CG2 . VAL   A 203 ? 0.3220 0.3621 0.3566 0.0115  -0.0494 -0.0350 409 VAL   A CG2 
1662 N N   . SER   A 204 ? 0.3474 0.3709 0.3684 0.0124  -0.0447 -0.0279 410 SER   A N   
1663 C CA  . SER   A 204 ? 0.4576 0.4740 0.4732 0.0124  -0.0465 -0.0248 410 SER   A CA  
1664 C C   . SER   A 204 ? 0.5257 0.5361 0.5368 0.0120  -0.0548 -0.0215 410 SER   A C   
1665 O O   . SER   A 204 ? 0.5118 0.5225 0.5175 0.0093  -0.0580 -0.0201 410 SER   A O   
1666 C CB  . SER   A 204 ? 0.5048 0.5199 0.5114 0.0084  -0.0421 -0.0232 410 SER   A CB  
1667 O OG  . SER   A 204 ? 0.7121 0.7265 0.7093 0.0041  -0.0443 -0.0210 410 SER   A OG  
1668 N N   . ASN   A 205 ? 0.7715 0.7762 0.7848 0.0149  -0.0586 -0.0203 411 ASN   A N   
1669 C CA  . ASN   A 205 ? 0.8957 0.8928 0.9051 0.0149  -0.0672 -0.0166 411 ASN   A CA  
1670 C C   . ASN   A 205 ? 0.9773 0.9659 0.9777 0.0123  -0.0686 -0.0124 411 ASN   A C   
1671 O O   . ASN   A 205 ? 1.0065 0.9893 0.9975 0.0087  -0.0739 -0.0078 411 ASN   A O   
1672 C CB  . ASN   A 205 ? 0.9224 0.9193 0.9436 0.0208  -0.0721 -0.0192 411 ASN   A CB  
1673 C CG  . ASN   A 205 ? 1.0151 1.0167 1.0466 0.0249  -0.0663 -0.0239 411 ASN   A CG  
1674 O OD1 . ASN   A 205 ? 1.0211 1.0215 1.0497 0.0239  -0.0612 -0.0238 411 ASN   A OD1 
1675 N ND2 . ASN   A 205 ? 1.0004 1.0080 1.0439 0.0291  -0.0669 -0.0282 411 ASN   A ND2 
1676 N N   . SER   A 206 ? 1.1420 1.1301 1.1445 0.0135  -0.0638 -0.0138 412 SER   A N   
1677 C CA  . SER   A 206 ? 1.2422 1.2227 1.2367 0.0108  -0.0647 -0.0100 412 SER   A CA  
1678 C C   . SER   A 206 ? 1.1280 1.1102 1.1116 0.0045  -0.0605 -0.0077 412 SER   A C   
1679 O O   . SER   A 206 ? 1.0348 1.0245 1.0195 0.0036  -0.0540 -0.0104 412 SER   A O   
1680 C CB  . SER   A 206 ? 1.0989 1.0789 1.0991 0.0140  -0.0607 -0.0127 412 SER   A CB  
1681 O OG  . SER   A 206 ? 0.9267 0.9118 0.9246 0.0117  -0.0526 -0.0141 412 SER   A OG  
1682 N N   . GLU   A 207 ? 1.0443 1.0197 1.0177 0.0001  -0.0643 -0.0026 413 GLU   A N   
1683 C CA  . GLU   A 207 ? 0.9612 0.9393 0.9245 -0.0062 -0.0602 -0.0008 413 GLU   A CA  
1684 C C   . GLU   A 207 ? 0.9080 0.8879 0.8714 -0.0070 -0.0533 -0.0022 413 GLU   A C   
1685 O O   . GLU   A 207 ? 0.9286 0.9093 0.8836 -0.0123 -0.0506 -0.0003 413 GLU   A O   
1686 C CB  . GLU   A 207 ? 1.0477 1.0187 0.9993 -0.0116 -0.0663 0.0053  413 GLU   A CB  
1687 C CG  . GLU   A 207 ? 1.1293 1.0994 1.0791 -0.0117 -0.0730 0.0070  413 GLU   A CG  
1688 C CD  . GLU   A 207 ? 1.1007 1.0800 1.0579 -0.0086 -0.0700 0.0019  413 GLU   A CD  
1689 O OE1 . GLU   A 207 ? 1.0675 1.0463 1.0310 -0.0048 -0.0752 0.0009  413 GLU   A OE1 
1690 O OE2 . GLU   A 207 ? 1.0711 1.0581 1.0286 -0.0099 -0.0626 -0.0014 413 GLU   A OE2 
1691 N N   . HIS   A 208 ? 1.0210 1.0021 0.9936 -0.0021 -0.0504 -0.0058 414 HIS   A N   
1692 C CA  . HIS   A 208 ? 1.0394 1.0247 1.0133 -0.0024 -0.0431 -0.0082 414 HIS   A CA  
1693 C C   . HIS   A 208 ? 0.9084 0.9027 0.8868 -0.0015 -0.0375 -0.0122 414 HIS   A C   
1694 O O   . HIS   A 208 ? 0.9705 0.9686 0.9506 -0.0015 -0.0317 -0.0144 414 HIS   A O   
1695 C CB  . HIS   A 208 ? 0.9214 0.9034 0.9018 0.0019  -0.0427 -0.0099 414 HIS   A CB  
1696 C CG  . HIS   A 208 ? 0.8832 0.8651 0.8609 0.0000  -0.0380 -0.0099 414 HIS   A CG  
1697 N ND1 . HIS   A 208 ? 0.9061 0.8807 0.8804 -0.0012 -0.0406 -0.0074 414 HIS   A ND1 
1698 C CD2 . HIS   A 208 ? 0.8499 0.8379 0.8278 -0.0012 -0.0315 -0.0121 414 HIS   A CD2 
1699 C CE1 . HIS   A 208 ? 0.8892 0.8659 0.8620 -0.0029 -0.0356 -0.0083 414 HIS   A CE1 
1700 N NE2 . HIS   A 208 ? 0.8505 0.8353 0.8254 -0.0028 -0.0301 -0.0110 414 HIS   A NE2 
1701 N N   . GLY   A 209 ? 0.7641 0.7616 0.7446 -0.0007 -0.0396 -0.0132 415 GLY   A N   
1702 C CA  . GLY   A 209 ? 0.6170 0.6225 0.6006 -0.0009 -0.0351 -0.0166 415 GLY   A CA  
1703 C C   . GLY   A 209 ? 0.4938 0.5036 0.4879 0.0036  -0.0317 -0.0204 415 GLY   A C   
1704 O O   . GLY   A 209 ? 0.3585 0.3669 0.3591 0.0074  -0.0342 -0.0213 415 GLY   A O   
1705 N N   . ALA   A 210 ? 0.3797 0.3948 0.3756 0.0029  -0.0261 -0.0229 416 ALA   A N   
1706 C CA  . ALA   A 210 ? 0.3500 0.3693 0.3548 0.0060  -0.0226 -0.0261 416 ALA   A CA  
1707 C C   . ALA   A 210 ? 0.3448 0.3619 0.3528 0.0086  -0.0209 -0.0264 416 ALA   A C   
1708 O O   . ALA   A 210 ? 0.3566 0.3703 0.3598 0.0073  -0.0200 -0.0248 416 ALA   A O   
1709 C CB  . ALA   A 210 ? 0.2819 0.3063 0.2870 0.0042  -0.0178 -0.0283 416 ALA   A CB  
1710 N N   . GLN   A 211 ? 0.3234 0.3430 0.3396 0.0121  -0.0203 -0.0286 417 GLN   A N   
1711 C CA  . GLN   A 211 ? 0.3079 0.3263 0.3276 0.0148  -0.0187 -0.0297 417 GLN   A CA  
1712 C C   . GLN   A 211 ? 0.2988 0.3234 0.3267 0.0168  -0.0153 -0.0327 417 GLN   A C   
1713 O O   . GLN   A 211 ? 0.3342 0.3631 0.3658 0.0164  -0.0152 -0.0338 417 GLN   A O   
1714 C CB  . GLN   A 211 ? 0.3227 0.3359 0.3432 0.0172  -0.0241 -0.0289 417 GLN   A CB  
1715 C CG  . GLN   A 211 ? 0.5058 0.5119 0.5176 0.0146  -0.0277 -0.0252 417 GLN   A CG  
1716 C CD  . GLN   A 211 ? 0.5645 0.5641 0.5772 0.0170  -0.0338 -0.0241 417 GLN   A CD  
1717 O OE1 . GLN   A 211 ? 0.4841 0.4845 0.5044 0.0212  -0.0347 -0.0269 417 GLN   A OE1 
1718 N NE2 . GLN   A 211 ? 0.6218 0.6149 0.6268 0.0142  -0.0381 -0.0202 417 GLN   A NE2 
1719 N N   . HIS   A 212 ? 0.2754 0.3007 0.3063 0.0187  -0.0126 -0.0341 418 HIS   A N   
1720 C CA  . HIS   A 212 ? 0.2654 0.2969 0.3038 0.0202  -0.0093 -0.0369 418 HIS   A CA  
1721 C C   . HIS   A 212 ? 0.2956 0.3274 0.3378 0.0232  -0.0088 -0.0390 418 HIS   A C   
1722 O O   . HIS   A 212 ? 0.2891 0.3159 0.3275 0.0239  -0.0100 -0.0383 418 HIS   A O   
1723 C CB  . HIS   A 212 ? 0.2698 0.3043 0.3073 0.0177  -0.0043 -0.0367 418 HIS   A CB  
1724 C CG  . HIS   A 212 ? 0.3264 0.3587 0.3599 0.0173  -0.0014 -0.0360 418 HIS   A CG  
1725 N ND1 . HIS   A 212 ? 0.2677 0.2949 0.2943 0.0160  -0.0023 -0.0341 418 HIS   A ND1 
1726 C CD2 . HIS   A 212 ? 0.2673 0.3019 0.3024 0.0177  0.0024  -0.0370 418 HIS   A CD2 
1727 C CE1 . HIS   A 212 ? 0.3195 0.3461 0.3443 0.0159  0.0005  -0.0341 418 HIS   A CE1 
1728 N NE2 . HIS   A 212 ? 0.2689 0.2996 0.2983 0.0169  0.0033  -0.0358 418 HIS   A NE2 
1729 N N   . HIS   A 213 ? 0.2650 0.3031 0.3149 0.0248  -0.0068 -0.0419 419 HIS   A N   
1730 C CA  . HIS   A 213 ? 0.2748 0.3152 0.3294 0.0278  -0.0057 -0.0450 419 HIS   A CA  
1731 C C   . HIS   A 213 ? 0.2629 0.3108 0.3216 0.0268  -0.0001 -0.0469 419 HIS   A C   
1732 O O   . HIS   A 213 ? 0.3032 0.3560 0.3659 0.0254  0.0010  -0.0471 419 HIS   A O   
1733 C CB  . HIS   A 213 ? 0.2628 0.3038 0.3243 0.0314  -0.0106 -0.0474 419 HIS   A CB  
1734 C CG  . HIS   A 213 ? 0.3998 0.4411 0.4651 0.0350  -0.0108 -0.0509 419 HIS   A CG  
1735 N ND1 . HIS   A 213 ? 0.4912 0.5249 0.5540 0.0370  -0.0154 -0.0504 419 HIS   A ND1 
1736 C CD2 . HIS   A 213 ? 0.3952 0.4433 0.4662 0.0365  -0.0067 -0.0549 419 HIS   A CD2 
1737 C CE1 . HIS   A 213 ? 0.4686 0.5044 0.5360 0.0401  -0.0144 -0.0546 419 HIS   A CE1 
1738 N NE2 . HIS   A 213 ? 0.4440 0.4889 0.5163 0.0399  -0.0090 -0.0575 419 HIS   A NE2 
1739 N N   . ILE   A 214 ? 0.2501 0.2990 0.3074 0.0271  0.0034  -0.0481 420 ILE   A N   
1740 C CA  . ILE   A 214 ? 0.2576 0.3128 0.3164 0.0252  0.0089  -0.0490 420 ILE   A CA  
1741 C C   . ILE   A 214 ? 0.3226 0.3847 0.3886 0.0277  0.0106  -0.0536 420 ILE   A C   
1742 O O   . ILE   A 214 ? 0.3130 0.3734 0.3800 0.0308  0.0089  -0.0562 420 ILE   A O   
1743 C CB  . ILE   A 214 ? 0.3179 0.3695 0.3689 0.0232  0.0116  -0.0468 420 ILE   A CB  
1744 C CG1 . ILE   A 214 ? 0.2814 0.3267 0.3261 0.0211  0.0098  -0.0430 420 ILE   A CG1 
1745 C CG2 . ILE   A 214 ? 0.3143 0.3716 0.3658 0.0208  0.0168  -0.0470 420 ILE   A CG2 
1746 C CD1 . ILE   A 214 ? 0.3881 0.4283 0.4255 0.0204  0.0105  -0.0413 420 ILE   A CD1 
1747 N N   . TYR   A 215 ? 0.2693 0.3395 0.3405 0.0260  0.0143  -0.0549 421 TYR   A N   
1748 C CA  . TYR   A 215 ? 0.2949 0.3740 0.3731 0.0273  0.0173  -0.0596 421 TYR   A CA  
1749 C C   . TYR   A 215 ? 0.3372 0.4216 0.4133 0.0231  0.0232  -0.0585 421 TYR   A C   
1750 O O   . TYR   A 215 ? 0.3238 0.4072 0.3978 0.0196  0.0241  -0.0549 421 TYR   A O   
1751 C CB  . TYR   A 215 ? 0.2901 0.3756 0.3788 0.0291  0.0153  -0.0627 421 TYR   A CB  
1752 C CG  . TYR   A 215 ? 0.3145 0.3948 0.4058 0.0330  0.0087  -0.0634 421 TYR   A CG  
1753 C CD1 . TYR   A 215 ? 0.3139 0.3886 0.4023 0.0319  0.0047  -0.0597 421 TYR   A CD1 
1754 C CD2 . TYR   A 215 ? 0.3606 0.4415 0.4571 0.0376  0.0061  -0.0678 421 TYR   A CD2 
1755 C CE1 . TYR   A 215 ? 0.3714 0.4410 0.4611 0.0349  -0.0017 -0.0596 421 TYR   A CE1 
1756 C CE2 . TYR   A 215 ? 0.3418 0.4168 0.4403 0.0410  -0.0008 -0.0678 421 TYR   A CE2 
1757 C CZ  . TYR   A 215 ? 0.3709 0.4404 0.4656 0.0393  -0.0047 -0.0634 421 TYR   A CZ  
1758 O OH  . TYR   A 215 ? 0.4371 0.5004 0.5327 0.0421  -0.0118 -0.0628 421 TYR   A OH  
1759 N N   . ARG   A 216 ? 0.2784 0.3687 0.3554 0.0233  0.0271  -0.0618 422 ARG   A N   
1760 C CA  A ARG   A 216 ? 0.3274 0.4244 0.4031 0.0189  0.0328  -0.0611 422 ARG   A CA  
1761 C CA  B ARG   A 216 ? 0.3404 0.4372 0.4160 0.0189  0.0327  -0.0610 422 ARG   A CA  
1762 C C   . ARG   A 216 ? 0.3266 0.4338 0.4122 0.0179  0.0347  -0.0639 422 ARG   A C   
1763 O O   . ARG   A 216 ? 0.3255 0.4377 0.4196 0.0216  0.0332  -0.0688 422 ARG   A O   
1764 C CB  A ARG   A 216 ? 0.3509 0.4512 0.4232 0.0193  0.0364  -0.0641 422 ARG   A CB  
1765 C CB  B ARG   A 216 ? 0.3527 0.4520 0.4239 0.0188  0.0363  -0.0632 422 ARG   A CB  
1766 C CG  A ARG   A 216 ? 0.3920 0.4838 0.4541 0.0190  0.0357  -0.0613 422 ARG   A CG  
1767 C CG  B ARG   A 216 ? 0.3873 0.4769 0.4482 0.0186  0.0349  -0.0598 422 ARG   A CG  
1768 C CD  A ARG   A 216 ? 0.3792 0.4756 0.4390 0.0197  0.0391  -0.0653 422 ARG   A CD  
1769 C CD  B ARG   A 216 ? 0.4099 0.5024 0.4650 0.0171  0.0390  -0.0611 422 ARG   A CD  
1770 N NE  A ARG   A 216 ? 0.3816 0.4816 0.4489 0.0247  0.0376  -0.0718 422 ARG   A NE  
1771 N NE  B ARG   A 216 ? 0.4411 0.5335 0.4900 0.0117  0.0420  -0.0562 422 ARG   A NE  
1772 C CZ  A ARG   A 216 ? 0.3797 0.4909 0.4544 0.0254  0.0409  -0.0776 422 ARG   A CZ  
1773 C CZ  B ARG   A 216 ? 0.3575 0.4421 0.3978 0.0101  0.0409  -0.0518 422 ARG   A CZ  
1774 N NH1 A ARG   A 216 ? 0.3110 0.4311 0.3860 0.0209  0.0463  -0.0773 422 ARG   A NH1 
1775 N NH1 B ARG   A 216 ? 0.3581 0.4348 0.3949 0.0130  0.0374  -0.0515 422 ARG   A NH1 
1776 N NH2 A ARG   A 216 ? 0.3920 0.5054 0.4742 0.0307  0.0386  -0.0838 422 ARG   A NH2 
1777 N NH2 B ARG   A 216 ? 0.4353 0.5199 0.4708 0.0054  0.0431  -0.0476 422 ARG   A NH2 
1778 N N   . LEU   A 217 ? 0.3268 0.4370 0.4118 0.0130  0.0376  -0.0608 423 LEU   A N   
1779 C CA  . LEU   A 217 ? 0.3119 0.4325 0.4062 0.0110  0.0399  -0.0631 423 LEU   A CA  
1780 C C   . LEU   A 217 ? 0.3426 0.4729 0.4369 0.0082  0.0462  -0.0656 423 LEU   A C   
1781 O O   . LEU   A 217 ? 0.3238 0.4519 0.4095 0.0042  0.0491  -0.0620 423 LEU   A O   
1782 C CB  . LEU   A 217 ? 0.2792 0.3974 0.3732 0.0068  0.0394  -0.0584 423 LEU   A CB  
1783 C CG  . LEU   A 217 ? 0.2958 0.4081 0.3925 0.0091  0.0337  -0.0573 423 LEU   A CG  
1784 C CD1 . LEU   A 217 ? 0.2311 0.3402 0.3261 0.0046  0.0335  -0.0529 423 LEU   A CD1 
1785 C CD2 . LEU   A 217 ? 0.3137 0.4332 0.4217 0.0124  0.0317  -0.0623 423 LEU   A CD2 
1786 N N   . VAL   A 218 ? 0.2665 0.4078 0.3704 0.0102  0.0481  -0.0719 424 VAL   A N   
1787 C CA  . VAL   A 218 ? 0.3644 0.5172 0.4694 0.0075  0.0544  -0.0754 424 VAL   A CA  
1788 C C   . VAL   A 218 ? 0.4427 0.6082 0.5589 0.0051  0.0573  -0.0785 424 VAL   A C   
1789 O O   . VAL   A 218 ? 0.3693 0.5357 0.4943 0.0073  0.0537  -0.0797 424 VAL   A O   
1790 C CB  . VAL   A 218 ? 0.3610 0.5166 0.4672 0.0126  0.0548  -0.0819 424 VAL   A CB  
1791 C CG1 . VAL   A 218 ? 0.3378 0.4810 0.4331 0.0146  0.0521  -0.0790 424 VAL   A CG1 
1792 C CG2 . VAL   A 218 ? 0.3520 0.5109 0.4705 0.0188  0.0507  -0.0879 424 VAL   A CG2 
1793 N N   . LYS   A 219 ? 0.3723 0.5484 0.4880 0.0001  0.0638  -0.0797 425 LYS   A N   
1794 C CA  . LYS   A 219 ? 0.4672 0.6561 0.5927 -0.0037 0.0674  -0.0819 425 LYS   A CA  
1795 C C   . LYS   A 219 ? 0.5459 0.7478 0.6841 0.0008  0.0686  -0.0913 425 LYS   A C   
1796 O O   . LYS   A 219 ? 0.5799 0.7828 0.7174 0.0053  0.0689  -0.0963 425 LYS   A O   
1797 C CB  . LYS   A 219 ? 0.5663 0.7611 0.6854 -0.0121 0.0739  -0.0785 425 LYS   A CB  
1798 C CG  . LYS   A 219 ? 0.7343 0.9352 0.8474 -0.0127 0.0790  -0.0819 425 LYS   A CG  
1799 C CD  . LYS   A 219 ? 0.7473 0.9485 0.8490 -0.0212 0.0837  -0.0759 425 LYS   A CD  
1800 C CE  . LYS   A 219 ? 0.8373 1.0459 0.9330 -0.0220 0.0890  -0.0800 425 LYS   A CE  
1801 N NZ  . LYS   A 219 ? 0.8075 1.0076 0.8980 -0.0153 0.0856  -0.0823 425 LYS   A NZ  
1802 N N   . GLY   B 1   ? 0.6316 0.6644 0.6164 0.0160  0.0248  -0.0481 207 GLY   B N   
1803 C CA  . GLY   B 1   ? 0.5990 0.6289 0.5892 0.0172  0.0226  -0.0469 207 GLY   B CA  
1804 C C   . GLY   B 1   ? 0.5646 0.5922 0.5543 0.0150  0.0218  -0.0419 207 GLY   B C   
1805 O O   . GLY   B 1   ? 0.6050 0.6347 0.5925 0.0126  0.0235  -0.0394 207 GLY   B O   
1806 N N   . PRO   B 2   ? 0.5110 0.5343 0.5027 0.0156  0.0190  -0.0406 208 PRO   B N   
1807 C CA  . PRO   B 2   ? 0.4747 0.4967 0.4671 0.0138  0.0184  -0.0369 208 PRO   B CA  
1808 C C   . PRO   B 2   ? 0.4798 0.4991 0.4679 0.0121  0.0175  -0.0346 208 PRO   B C   
1809 O O   . PRO   B 2   ? 0.4487 0.4664 0.4331 0.0122  0.0168  -0.0355 208 PRO   B O   
1810 C CB  . PRO   B 2   ? 0.5320 0.5508 0.5274 0.0150  0.0158  -0.0370 208 PRO   B CB  
1811 C CG  . PRO   B 2   ? 0.5611 0.5767 0.5549 0.0166  0.0140  -0.0394 208 PRO   B CG  
1812 C CD  . PRO   B 2   ? 0.5568 0.5763 0.5505 0.0179  0.0162  -0.0426 208 PRO   B CD  
1813 N N   . ARG   B 3   ? 0.3755 0.3946 0.3648 0.0106  0.0171  -0.0318 209 ARG   B N   
1814 C CA  . ARG   B 3   ? 0.4262 0.4429 0.4131 0.0093  0.0157  -0.0299 209 ARG   B CA  
1815 C C   . ARG   B 3   ? 0.4395 0.4531 0.4268 0.0097  0.0134  -0.0303 209 ARG   B C   
1816 O O   . ARG   B 3   ? 0.3675 0.3793 0.3522 0.0092  0.0121  -0.0302 209 ARG   B O   
1817 C CB  . ARG   B 3   ? 0.4207 0.4383 0.4098 0.0079  0.0159  -0.0274 209 ARG   B CB  
1818 C CG  . ARG   B 3   ? 0.4121 0.4275 0.3997 0.0069  0.0140  -0.0255 209 ARG   B CG  
1819 C CD  . ARG   B 3   ? 0.4331 0.4485 0.4247 0.0061  0.0133  -0.0239 209 ARG   B CD  
1820 N NE  . ARG   B 3   ? 0.4845 0.5007 0.4801 0.0068  0.0133  -0.0252 209 ARG   B NE  
1821 C CZ  . ARG   B 3   ? 0.5871 0.6025 0.5837 0.0071  0.0120  -0.0262 209 ARG   B CZ  
1822 N NH1 . ARG   B 3   ? 0.4670 0.4811 0.4619 0.0069  0.0106  -0.0263 209 ARG   B NH1 
1823 N NH2 . ARG   B 3   ? 0.5377 0.5542 0.5370 0.0072  0.0122  -0.0272 209 ARG   B NH2 
1824 N N   . SER   B 4   ? 0.3361 0.3495 0.3264 0.0101  0.0129  -0.0306 210 SER   B N   
1825 C CA  . SER   B 4   ? 0.3361 0.3470 0.3262 0.0096  0.0110  -0.0306 210 SER   B CA  
1826 C C   . SER   B 4   ? 0.3428 0.3508 0.3307 0.0105  0.0097  -0.0322 210 SER   B C   
1827 O O   . SER   B 4   ? 0.3321 0.3404 0.3197 0.0120  0.0104  -0.0339 210 SER   B O   
1828 C CB  . SER   B 4   ? 0.3524 0.3637 0.3453 0.0092  0.0106  -0.0302 210 SER   B CB  
1829 O OG  . SER   B 4   ? 0.4678 0.4793 0.4621 0.0107  0.0106  -0.0312 210 SER   B OG  
1830 N N   . ILE   B 5   ? 0.3371 0.3426 0.3239 0.0093  0.0079  -0.0319 211 ILE   B N   
1831 C CA  . ILE   B 5   ? 0.2993 0.3012 0.2840 0.0097  0.0062  -0.0332 211 ILE   B CA  
1832 C C   . ILE   B 5   ? 0.3592 0.3580 0.3446 0.0091  0.0042  -0.0327 211 ILE   B C   
1833 O O   . ILE   B 5   ? 0.3417 0.3403 0.3269 0.0068  0.0035  -0.0312 211 ILE   B O   
1834 C CB  . ILE   B 5   ? 0.3458 0.3468 0.3282 0.0083  0.0054  -0.0331 211 ILE   B CB  
1835 C CG1 . ILE   B 5   ? 0.3878 0.3915 0.3691 0.0086  0.0067  -0.0329 211 ILE   B CG1 
1836 C CG2 . ILE   B 5   ? 0.3304 0.3274 0.3108 0.0085  0.0034  -0.0346 211 ILE   B CG2 
1837 C CD1 . ILE   B 5   ? 0.3697 0.3737 0.3502 0.0072  0.0057  -0.0322 211 ILE   B CD1 
1838 N N   . GLY   B 6   ? 0.3177 0.3141 0.3038 0.0109  0.0030  -0.0341 212 GLY   B N   
1839 C CA  . GLY   B 6   ? 0.3305 0.3224 0.3165 0.0102  0.0001  -0.0332 212 GLY   B CA  
1840 C C   . GLY   B 6   ? 0.3814 0.3728 0.3702 0.0126  -0.0008 -0.0341 212 GLY   B C   
1841 O O   . GLY   B 6   ? 0.3668 0.3609 0.3577 0.0152  0.0007  -0.0364 212 GLY   B O   
1842 N N   . THR   B 7   ? 0.4073 0.3956 0.3961 0.0115  -0.0034 -0.0323 213 THR   B N   
1843 C CA  . THR   B 7   ? 0.4535 0.4406 0.4451 0.0136  -0.0055 -0.0327 213 THR   B CA  
1844 C C   . THR   B 7   ? 0.4120 0.4007 0.4033 0.0115  -0.0056 -0.0300 213 THR   B C   
1845 O O   . THR   B 7   ? 0.3759 0.3666 0.3649 0.0086  -0.0041 -0.0282 213 THR   B O   
1846 C CB  . THR   B 7   ? 0.4681 0.4479 0.4594 0.0143  -0.0100 -0.0330 213 THR   B CB  
1847 O OG1 . THR   B 7   ? 0.4323 0.4079 0.4197 0.0105  -0.0123 -0.0295 213 THR   B OG1 
1848 C CG2 . THR   B 7   ? 0.5136 0.4918 0.5048 0.0161  -0.0099 -0.0361 213 THR   B CG2 
1849 N N   . THR   B 8   ? 0.4097 0.3976 0.4036 0.0132  -0.0077 -0.0301 214 THR   B N   
1850 C CA  . THR   B 8   ? 0.4309 0.4198 0.4240 0.0113  -0.0086 -0.0277 214 THR   B CA  
1851 C C   . THR   B 8   ? 0.4348 0.4207 0.4228 0.0070  -0.0101 -0.0246 214 THR   B C   
1852 O O   . THR   B 8   ? 0.3974 0.3867 0.3836 0.0043  -0.0085 -0.0232 214 THR   B O   
1853 C CB  . THR   B 8   ? 0.4894 0.4762 0.4857 0.0138  -0.0122 -0.0281 214 THR   B CB  
1854 O OG1 . THR   B 8   ? 0.5647 0.5554 0.5664 0.0176  -0.0104 -0.0315 214 THR   B OG1 
1855 C CG2 . THR   B 8   ? 0.4900 0.4785 0.4855 0.0119  -0.0132 -0.0259 214 THR   B CG2 
1856 N N   . LYS   B 9   ? 0.4114 0.3911 0.3970 0.0062  -0.0131 -0.0237 215 LYS   B N   
1857 C CA  . LYS   B 9   ? 0.4012 0.3780 0.3818 0.0014  -0.0146 -0.0205 215 LYS   B CA  
1858 C C   . LYS   B 9   ? 0.4606 0.4426 0.4396 -0.0013 -0.0106 -0.0206 215 LYS   B C   
1859 O O   . LYS   B 9   ? 0.4351 0.4188 0.4109 -0.0054 -0.0101 -0.0186 215 LYS   B O   
1860 C CB  . LYS   B 9   ? 0.4513 0.4200 0.4302 0.0011  -0.0187 -0.0198 215 LYS   B CB  
1861 C CG  . LYS   B 9   ? 0.6311 0.5962 0.6046 -0.0045 -0.0207 -0.0160 215 LYS   B CG  
1862 C CD  . LYS   B 9   ? 0.5654 0.5215 0.5370 -0.0052 -0.0269 -0.0133 215 LYS   B CD  
1863 C CE  . LYS   B 9   ? 0.5755 0.5288 0.5406 -0.0118 -0.0286 -0.0087 215 LYS   B CE  
1864 N NZ  . LYS   B 9   ? 0.5669 0.5268 0.5290 -0.0150 -0.0259 -0.0071 215 LYS   B NZ  
1865 N N   . LEU   B 10  ? 0.3567 0.3415 0.3380 0.0007  -0.0078 -0.0231 216 LEU   B N   
1866 C CA  . LEU   B 10  ? 0.3738 0.3636 0.3547 -0.0013 -0.0045 -0.0235 216 LEU   B CA  
1867 C C   . LEU   B 10  ? 0.3521 0.3447 0.3356 0.0016  -0.0020 -0.0260 216 LEU   B C   
1868 O O   . LEU   B 10  ? 0.3682 0.3579 0.3518 0.0035  -0.0029 -0.0273 216 LEU   B O   
1869 C CB  . LEU   B 10  ? 0.2892 0.2769 0.2669 -0.0051 -0.0054 -0.0222 216 LEU   B CB  
1870 C CG  . LEU   B 10  ? 0.4076 0.4019 0.3860 -0.0074 -0.0022 -0.0228 216 LEU   B CG  
1871 C CD1 . LEU   B 10  ? 0.3933 0.3909 0.3699 -0.0108 -0.0015 -0.0214 216 LEU   B CD1 
1872 C CD2 . LEU   B 10  ? 0.4256 0.4197 0.4032 -0.0094 -0.0021 -0.0232 216 LEU   B CD2 
1873 N N   . ARG   B 11  ? 0.3558 0.3538 0.3412 0.0020  0.0008  -0.0266 217 ARG   B N   
1874 C CA  . ARG   B 11  ? 0.3825 0.3830 0.3698 0.0042  0.0029  -0.0282 217 ARG   B CA  
1875 C C   . ARG   B 11  ? 0.3526 0.3569 0.3404 0.0024  0.0046  -0.0283 217 ARG   B C   
1876 O O   . ARG   B 11  ? 0.3385 0.3458 0.3272 0.0008  0.0053  -0.0279 217 ARG   B O   
1877 C CB  . ARG   B 11  ? 0.3466 0.3499 0.3368 0.0064  0.0043  -0.0289 217 ARG   B CB  
1878 C CG  . ARG   B 11  ? 0.4750 0.4765 0.4664 0.0091  0.0035  -0.0300 217 ARG   B CG  
1879 C CD  . ARG   B 11  ? 0.4289 0.4343 0.4236 0.0105  0.0051  -0.0306 217 ARG   B CD  
1880 N NE  . ARG   B 11  ? 0.4618 0.4668 0.4588 0.0132  0.0045  -0.0323 217 ARG   B NE  
1881 C CZ  . ARG   B 11  ? 0.4593 0.4640 0.4587 0.0143  0.0028  -0.0325 217 ARG   B CZ  
1882 N NH1 . ARG   B 11  ? 0.4462 0.4506 0.4452 0.0127  0.0015  -0.0307 217 ARG   B NH1 
1883 N NH2 . ARG   B 11  ? 0.5312 0.5362 0.5337 0.0172  0.0023  -0.0348 217 ARG   B NH2 
1884 N N   . LEU   B 12  ? 0.3329 0.3372 0.3204 0.0030  0.0050  -0.0290 218 LEU   B N   
1885 C CA  . LEU   B 12  ? 0.3434 0.3512 0.3324 0.0023  0.0061  -0.0294 218 LEU   B CA  
1886 C C   . LEU   B 12  ? 0.2763 0.2862 0.2673 0.0042  0.0075  -0.0295 218 LEU   B C   
1887 O O   . LEU   B 12  ? 0.3293 0.3382 0.3194 0.0059  0.0079  -0.0297 218 LEU   B O   
1888 C CB  . LEU   B 12  ? 0.3000 0.3067 0.2877 0.0020  0.0053  -0.0299 218 LEU   B CB  
1889 C CG  . LEU   B 12  ? 0.3120 0.3218 0.3017 0.0018  0.0056  -0.0304 218 LEU   B CG  
1890 C CD1 . LEU   B 12  ? 0.2796 0.2931 0.2719 -0.0004 0.0059  -0.0309 218 LEU   B CD1 
1891 C CD2 . LEU   B 12  ? 0.3225 0.3308 0.3105 0.0020  0.0044  -0.0309 218 LEU   B CD2 
1892 N N   . VAL   B 13  ? 0.2767 0.2897 0.2706 0.0038  0.0084  -0.0295 219 VAL   B N   
1893 C CA  . VAL   B 13  ? 0.3106 0.3250 0.3066 0.0052  0.0094  -0.0294 219 VAL   B CA  
1894 C C   . VAL   B 13  ? 0.3243 0.3403 0.3225 0.0052  0.0094  -0.0295 219 VAL   B C   
1895 O O   . VAL   B 13  ? 0.3647 0.3809 0.3641 0.0060  0.0099  -0.0288 219 VAL   B O   
1896 C CB  . VAL   B 13  ? 0.3047 0.3207 0.3027 0.0051  0.0099  -0.0295 219 VAL   B CB  
1897 C CG1 . VAL   B 13  ? 0.3563 0.3702 0.3526 0.0054  0.0092  -0.0292 219 VAL   B CG1 
1898 C CG2 . VAL   B 13  ? 0.2821 0.3008 0.2819 0.0034  0.0099  -0.0303 219 VAL   B CG2 
1899 N N   . GLU   B 14  ? 0.2857 0.3028 0.2848 0.0042  0.0087  -0.0302 220 GLU   B N   
1900 C CA  . GLU   B 14  ? 0.3525 0.3711 0.3548 0.0046  0.0079  -0.0307 220 GLU   B CA  
1901 C C   . GLU   B 14  ? 0.3977 0.4167 0.3996 0.0039  0.0068  -0.0314 220 GLU   B C   
1902 O O   . GLU   B 14  ? 0.3492 0.3691 0.3503 0.0023  0.0070  -0.0322 220 GLU   B O   
1903 C CB  . GLU   B 14  ? 0.4059 0.4276 0.4128 0.0044  0.0083  -0.0321 220 GLU   B CB  
1904 C CG  . GLU   B 14  ? 0.6468 0.6686 0.6576 0.0055  0.0071  -0.0322 220 GLU   B CG  
1905 C CD  . GLU   B 14  ? 0.8645 0.8890 0.8803 0.0057  0.0074  -0.0342 220 GLU   B CD  
1906 O OE1 . GLU   B 14  ? 0.8375 0.8648 0.8535 0.0046  0.0086  -0.0358 220 GLU   B OE1 
1907 O OE2 . GLU   B 14  ? 0.8676 0.8913 0.8871 0.0067  0.0061  -0.0342 220 GLU   B OE2 
1908 N N   . PHE   B 15  ? 0.3644 0.3824 0.3664 0.0047  0.0053  -0.0309 221 PHE   B N   
1909 C CA  . PHE   B 15  ? 0.3202 0.3387 0.3224 0.0041  0.0038  -0.0317 221 PHE   B CA  
1910 C C   . PHE   B 15  ? 0.3965 0.4145 0.4006 0.0053  0.0017  -0.0312 221 PHE   B C   
1911 O O   . PHE   B 15  ? 0.3459 0.3613 0.3477 0.0061  0.0013  -0.0292 221 PHE   B O   
1912 C CB  . PHE   B 15  ? 0.3614 0.3773 0.3586 0.0036  0.0036  -0.0312 221 PHE   B CB  
1913 C CG  . PHE   B 15  ? 0.3748 0.3910 0.3723 0.0030  0.0017  -0.0320 221 PHE   B CG  
1914 C CD1 . PHE   B 15  ? 0.4134 0.4328 0.4140 0.0013  0.0015  -0.0337 221 PHE   B CD1 
1915 C CD2 . PHE   B 15  ? 0.3997 0.4140 0.3949 0.0040  -0.0001 -0.0311 221 PHE   B CD2 
1916 C CE1 . PHE   B 15  ? 0.4225 0.4430 0.4244 0.0008  -0.0004 -0.0347 221 PHE   B CE1 
1917 C CE2 . PHE   B 15  ? 0.4002 0.4151 0.3961 0.0036  -0.0023 -0.0320 221 PHE   B CE2 
1918 C CZ  . PHE   B 15  ? 0.3876 0.4057 0.3873 0.0021  -0.0025 -0.0339 221 PHE   B CZ  
1919 N N   . SER   B 16  ? 0.3151 0.3357 0.3235 0.0052  0.0000  -0.0330 222 SER   B N   
1920 C CA  . SER   B 16  ? 0.3536 0.3731 0.3636 0.0064  -0.0031 -0.0324 222 SER   B CA  
1921 C C   . SER   B 16  ? 0.3042 0.3273 0.3187 0.0061  -0.0047 -0.0349 222 SER   B C   
1922 O O   . SER   B 16  ? 0.2987 0.3263 0.3172 0.0051  -0.0033 -0.0375 222 SER   B O   
1923 C CB  . SER   B 16  ? 0.3401 0.3588 0.3539 0.0078  -0.0042 -0.0318 222 SER   B CB  
1924 O OG  . SER   B 16  ? 0.4523 0.4750 0.4737 0.0084  -0.0046 -0.0349 222 SER   B OG  
1925 N N   . ALA   B 17  ? 0.2624 0.2838 0.2760 0.0067  -0.0078 -0.0341 223 ALA   B N   
1926 C CA  . ALA   B 17  ? 0.2769 0.3018 0.2959 0.0068  -0.0103 -0.0365 223 ALA   B CA  
1927 C C   . ALA   B 17  ? 0.3029 0.3261 0.3257 0.0090  -0.0142 -0.0359 223 ALA   B C   
1928 O O   . ALA   B 17  ? 0.3403 0.3586 0.3580 0.0094  -0.0160 -0.0326 223 ALA   B O   
1929 C CB  . ALA   B 17  ? 0.2602 0.2841 0.2750 0.0056  -0.0113 -0.0363 223 ALA   B CB  
1930 N N   . PHE   B 18  ? 0.2684 0.2960 0.3003 0.0102  -0.0158 -0.0391 224 PHE   B N   
1931 C CA  . PHE   B 18  ? 0.2760 0.3013 0.3126 0.0125  -0.0197 -0.0386 224 PHE   B CA  
1932 C C   . PHE   B 18  ? 0.3113 0.3412 0.3577 0.0142  -0.0232 -0.0424 224 PHE   B C   
1933 O O   . PHE   B 18  ? 0.2781 0.3143 0.3286 0.0132  -0.0217 -0.0461 224 PHE   B O   
1934 C CB  . PHE   B 18  ? 0.2409 0.2657 0.2796 0.0131  -0.0176 -0.0388 224 PHE   B CB  
1935 C CG  . PHE   B 18  ? 0.2622 0.2939 0.3065 0.0125  -0.0142 -0.0433 224 PHE   B CG  
1936 C CD1 . PHE   B 18  ? 0.2657 0.3027 0.3202 0.0141  -0.0157 -0.0480 224 PHE   B CD1 
1937 C CD2 . PHE   B 18  ? 0.2531 0.2861 0.2925 0.0104  -0.0096 -0.0430 224 PHE   B CD2 
1938 C CE1 . PHE   B 18  ? 0.3471 0.3914 0.4060 0.0131  -0.0122 -0.0525 224 PHE   B CE1 
1939 C CE2 . PHE   B 18  ? 0.2944 0.3337 0.3377 0.0093  -0.0066 -0.0468 224 PHE   B CE2 
1940 C CZ  . PHE   B 18  ? 0.3709 0.4163 0.4237 0.0104  -0.0076 -0.0516 224 PHE   B CZ  
1941 N N   . LEU   B 19  ? 0.2939 0.3205 0.3444 0.0165  -0.0281 -0.0416 225 LEU   B N   
1942 C CA  . LEU   B 19  ? 0.2553 0.2856 0.3168 0.0189  -0.0324 -0.0455 225 LEU   B CA  
1943 C C   . LEU   B 19  ? 0.3141 0.3427 0.3825 0.0213  -0.0343 -0.0467 225 LEU   B C   
1944 O O   . LEU   B 19  ? 0.3034 0.3245 0.3676 0.0217  -0.0366 -0.0423 225 LEU   B O   
1945 C CB  . LEU   B 19  ? 0.2703 0.2966 0.3302 0.0198  -0.0384 -0.0430 225 LEU   B CB  
1946 C CG  . LEU   B 19  ? 0.3219 0.3502 0.3935 0.0230  -0.0445 -0.0463 225 LEU   B CG  
1947 C CD1 . LEU   B 19  ? 0.3686 0.4076 0.4506 0.0234  -0.0422 -0.0533 225 LEU   B CD1 
1948 C CD2 . LEU   B 19  ? 0.3365 0.3603 0.4047 0.0235  -0.0505 -0.0430 225 LEU   B CD2 
1949 N N   . GLU   B 20  ? 0.2981 0.3340 0.3769 0.0227  -0.0332 -0.0528 226 GLU   B N   
1950 C CA  . GLU   B 20  ? 0.3341 0.3692 0.4215 0.0254  -0.0357 -0.0554 226 GLU   B CA  
1951 C C   . GLU   B 20  ? 0.3674 0.4050 0.4665 0.0288  -0.0417 -0.0595 226 GLU   B C   
1952 O O   . GLU   B 20  ? 0.3114 0.3570 0.4161 0.0288  -0.0410 -0.0638 226 GLU   B O   
1953 C CB  . GLU   B 20  ? 0.3281 0.3700 0.4198 0.0249  -0.0304 -0.0605 226 GLU   B CB  
1954 C CG  . GLU   B 20  ? 0.4438 0.4836 0.5254 0.0220  -0.0249 -0.0571 226 GLU   B CG  
1955 C CD  . GLU   B 20  ? 0.6380 0.6855 0.7227 0.0209  -0.0197 -0.0621 226 GLU   B CD  
1956 O OE1 . GLU   B 20  ? 0.6488 0.7053 0.7396 0.0206  -0.0179 -0.0675 226 GLU   B OE1 
1957 O OE2 . GLU   B 20  ? 0.6343 0.6791 0.7145 0.0199  -0.0171 -0.0604 226 GLU   B OE2 
1958 N N   . GLN   B 21  ? 0.3261 0.3570 0.4295 0.0315  -0.0477 -0.0580 227 GLN   B N   
1959 C CA  . GLN   B 21  ? 0.3456 0.3774 0.4607 0.0353  -0.0548 -0.0614 227 GLN   B CA  
1960 C C   . GLN   B 21  ? 0.4583 0.4881 0.5834 0.0385  -0.0579 -0.0648 227 GLN   B C   
1961 O O   . GLN   B 21  ? 0.4236 0.4448 0.5439 0.0381  -0.0591 -0.0602 227 GLN   B O   
1962 C CB  . GLN   B 21  ? 0.4612 0.4843 0.5705 0.0354  -0.0614 -0.0551 227 GLN   B CB  
1963 C CG  . GLN   B 21  ? 0.4536 0.4795 0.5552 0.0329  -0.0595 -0.0532 227 GLN   B CG  
1964 C CD  . GLN   B 21  ? 0.5636 0.5811 0.6582 0.0327  -0.0659 -0.0469 227 GLN   B CD  
1965 O OE1 . GLN   B 21  ? 0.6074 0.6271 0.7065 0.0340  -0.0705 -0.0484 227 GLN   B OE1 
1966 N NE2 . GLN   B 21  ? 0.4641 0.4726 0.5475 0.0307  -0.0661 -0.0399 227 GLN   B NE2 
1967 N N   . GLN   B 22  ? 0.4754 0.5135 0.6146 0.0416  -0.0591 -0.0730 228 GLN   B N   
1968 C CA  . GLN   B 22  ? 0.4795 0.5157 0.6300 0.0454  -0.0632 -0.0773 228 GLN   B CA  
1969 C C   . GLN   B 22  ? 0.5840 0.6137 0.7417 0.0491  -0.0733 -0.0762 228 GLN   B C   
1970 O O   . GLN   B 22  ? 0.5365 0.5729 0.7042 0.0516  -0.0763 -0.0813 228 GLN   B O   
1971 C CB  . GLN   B 22  ? 0.5474 0.5965 0.7099 0.0470  -0.0592 -0.0877 228 GLN   B CB  
1972 C CG  . GLN   B 22  ? 0.5288 0.5762 0.7035 0.0511  -0.0634 -0.0930 228 GLN   B CG  
1973 C CD  . GLN   B 22  ? 0.4880 0.5357 0.6591 0.0494  -0.0578 -0.0940 228 GLN   B CD  
1974 O OE1 . GLN   B 22  ? 0.5196 0.5695 0.6794 0.0452  -0.0507 -0.0910 228 GLN   B OE1 
1975 N NE2 . GLN   B 22  ? 0.4343 0.4793 0.6148 0.0528  -0.0614 -0.0983 228 GLN   B NE2 
1976 N N   . ARG   B 23  ? 0.8996 0.9170 1.0529 0.0493  -0.0785 -0.0697 229 ARG   B N   
1977 C CA  . ARG   B 23  ? 0.9065 0.9158 1.0648 0.0523  -0.0888 -0.0671 229 ARG   B CA  
1978 C C   . ARG   B 23  ? 0.8320 0.8414 1.0074 0.0577  -0.0950 -0.0741 229 ARG   B C   
1979 O O   . ARG   B 23  ? 0.8748 0.8859 1.0610 0.0614  -0.1017 -0.0777 229 ARG   B O   
1980 C CB  . ARG   B 23  ? 0.9843 0.9799 1.1292 0.0494  -0.0914 -0.0566 229 ARG   B CB  
1981 C CG  . ARG   B 23  ? 0.9149 0.9084 1.0522 0.0464  -0.0847 -0.0544 229 ARG   B CG  
1982 C CD  . ARG   B 23  ? 0.9265 0.9074 1.0517 0.0432  -0.0873 -0.0444 229 ARG   B CD  
1983 N NE  . ARG   B 23  ? 1.1001 1.0716 1.2322 0.0453  -0.0946 -0.0434 229 ARG   B NE  
1984 C CZ  . ARG   B 23  ? 1.2160 1.1758 1.3445 0.0448  -0.1029 -0.0361 229 ARG   B CZ  
1985 N NH1 . ARG   B 23  ? 1.2639 1.2205 1.3815 0.0423  -0.1046 -0.0295 229 ARG   B NH1 
1986 N NH2 . ARG   B 23  ? 1.2530 1.2040 1.3887 0.0467  -0.1097 -0.0355 229 ARG   B NH2 
1987 N N   . ASP   B 24  ? 0.7737 0.7817 0.9522 0.0582  -0.0930 -0.0766 230 ASP   B N   
1988 C CA  . ASP   B 24  ? 0.7097 0.7165 0.9041 0.0632  -0.0989 -0.0833 230 ASP   B CA  
1989 C C   . ASP   B 24  ? 0.6063 0.6240 0.8066 0.0634  -0.0910 -0.0922 230 ASP   B C   
1990 O O   . ASP   B 24  ? 0.5757 0.5996 0.7662 0.0593  -0.0818 -0.0914 230 ASP   B O   
1991 C CB  . ASP   B 24  ? 0.7433 0.7340 0.9344 0.0631  -0.1060 -0.0760 230 ASP   B CB  
1992 C CG  . ASP   B 24  ? 0.9691 0.9486 1.1514 0.0617  -0.1132 -0.0660 230 ASP   B CG  
1993 O OD1 . ASP   B 24  ? 1.0219 1.0037 1.2102 0.0644  -0.1186 -0.0678 230 ASP   B OD1 
1994 O OD2 . ASP   B 24  ? 0.9547 0.9234 1.1242 0.0578  -0.1137 -0.0566 230 ASP   B OD2 
1995 N N   . PRO   B 25  ? 0.5993 0.6197 0.8152 0.0680  -0.0943 -0.1010 231 PRO   B N   
1996 C CA  . PRO   B 25  ? 0.5353 0.5677 0.7561 0.0679  -0.0863 -0.1101 231 PRO   B CA  
1997 C C   . PRO   B 25  ? 0.4809 0.5092 0.6903 0.0639  -0.0803 -0.1061 231 PRO   B C   
1998 O O   . PRO   B 25  ? 0.4786 0.5174 0.6865 0.0620  -0.0720 -0.1111 231 PRO   B O   
1999 C CB  . PRO   B 25  ? 0.6019 0.6365 0.8424 0.0742  -0.0926 -0.1204 231 PRO   B CB  
2000 C CG  . PRO   B 25  ? 0.6115 0.6353 0.8579 0.0778  -0.1041 -0.1165 231 PRO   B CG  
2001 C CD  . PRO   B 25  ? 0.6088 0.6226 0.8390 0.0737  -0.1055 -0.1038 231 PRO   B CD  
2002 N N   . ASP   B 26  ? 0.3867 0.4007 0.5881 0.0624  -0.0842 -0.0971 232 ASP   B N   
2003 C CA  . ASP   B 26  ? 0.3682 0.3791 0.5600 0.0587  -0.0786 -0.0938 232 ASP   B CA  
2004 C C   . ASP   B 26  ? 0.3875 0.3916 0.5616 0.0534  -0.0756 -0.0824 232 ASP   B C   
2005 O O   . ASP   B 26  ? 0.3388 0.3372 0.5052 0.0505  -0.0732 -0.0779 232 ASP   B O   
2006 C CB  . ASP   B 26  ? 0.3454 0.3468 0.5443 0.0609  -0.0844 -0.0948 232 ASP   B CB  
2007 C CG  . ASP   B 26  ? 0.4344 0.4430 0.6511 0.0663  -0.0868 -0.1071 232 ASP   B CG  
2008 O OD1 . ASP   B 26  ? 0.3871 0.4091 0.6065 0.0660  -0.0794 -0.1152 232 ASP   B OD1 
2009 O OD2 . ASP   B 26  ? 0.4115 0.4126 0.6393 0.0705  -0.0961 -0.1087 232 ASP   B OD2 
2010 N N   . SER   B 27  ? 0.3905 0.3953 0.5583 0.0521  -0.0758 -0.0780 233 SER   B N   
2011 C CA  . SER   B 27  ? 0.4627 0.4609 0.6141 0.0474  -0.0734 -0.0678 233 SER   B CA  
2012 C C   . SER   B 27  ? 0.4956 0.5017 0.6404 0.0454  -0.0685 -0.0672 233 SER   B C   
2013 O O   . SER   B 27  ? 0.4240 0.4371 0.5766 0.0478  -0.0699 -0.0724 233 SER   B O   
2014 C CB  . SER   B 27  ? 0.5232 0.5075 0.6711 0.0473  -0.0819 -0.0594 233 SER   B CB  
2015 O OG  . SER   B 27  ? 0.6995 0.6836 0.8528 0.0500  -0.0883 -0.0600 233 SER   B OG  
2016 N N   . TYR   B 28  ? 0.3771 0.3821 0.5078 0.0410  -0.0627 -0.0612 234 TYR   B N   
2017 C CA  . TYR   B 28  ? 0.4758 0.4861 0.5991 0.0388  -0.0588 -0.0596 234 TYR   B CA  
2018 C C   . TYR   B 28  ? 0.4759 0.4784 0.5839 0.0350  -0.0577 -0.0501 234 TYR   B C   
2019 O O   . TYR   B 28  ? 0.4035 0.3990 0.5062 0.0333  -0.0575 -0.0455 234 TYR   B O   
2020 C CB  . TYR   B 28  ? 0.5282 0.5503 0.6519 0.0375  -0.0507 -0.0655 234 TYR   B CB  
2021 C CG  . TYR   B 28  ? 0.3763 0.3982 0.4906 0.0342  -0.0440 -0.0630 234 TYR   B CG  
2022 C CD1 . TYR   B 28  ? 0.4270 0.4495 0.5456 0.0347  -0.0424 -0.0664 234 TYR   B CD1 
2023 C CD2 . TYR   B 28  ? 0.4608 0.4820 0.5625 0.0306  -0.0396 -0.0576 234 TYR   B CD2 
2024 C CE1 . TYR   B 28  ? 0.4490 0.4716 0.5595 0.0318  -0.0368 -0.0641 234 TYR   B CE1 
2025 C CE2 . TYR   B 28  ? 0.4408 0.4619 0.5348 0.0278  -0.0340 -0.0555 234 TYR   B CE2 
2026 C CZ  . TYR   B 28  ? 0.4940 0.5158 0.5924 0.0284  -0.0327 -0.0587 234 TYR   B CZ  
2027 O OH  . TYR   B 28  ? 0.5969 0.6189 0.6882 0.0258  -0.0276 -0.0568 234 TYR   B OH  
2028 N N   . ASN   B 29  ? 0.3460 0.3504 0.4478 0.0336  -0.0569 -0.0478 235 ASN   B N   
2029 C CA  . ASN   B 29  ? 0.4499 0.4494 0.5374 0.0300  -0.0552 -0.0402 235 ASN   B CA  
2030 C C   . ASN   B 29  ? 0.3812 0.3882 0.4625 0.0276  -0.0473 -0.0417 235 ASN   B C   
2031 O O   . ASN   B 29  ? 0.3695 0.3850 0.4566 0.0284  -0.0451 -0.0473 235 ASN   B O   
2032 C CB  . ASN   B 29  ? 0.5019 0.4973 0.5867 0.0304  -0.0612 -0.0365 235 ASN   B CB  
2033 C CG  . ASN   B 29  ? 0.7690 0.7540 0.8549 0.0314  -0.0693 -0.0318 235 ASN   B CG  
2034 O OD1 . ASN   B 29  ? 0.8283 0.8069 0.9104 0.0298  -0.0693 -0.0279 235 ASN   B OD1 
2035 N ND2 . ASN   B 29  ? 0.8848 0.8678 0.9758 0.0338  -0.0767 -0.0320 235 ASN   B ND2 
2036 N N   . LYS   B 30  ? 0.3611 0.3648 0.4309 0.0244  -0.0434 -0.0366 236 LYS   B N   
2037 C CA  . LYS   B 30  ? 0.3109 0.3198 0.3737 0.0221  -0.0371 -0.0369 236 LYS   B CA  
2038 C C   . LYS   B 30  ? 0.3827 0.3861 0.4334 0.0197  -0.0372 -0.0305 236 LYS   B C   
2039 O O   . LYS   B 30  ? 0.3569 0.3540 0.4022 0.0184  -0.0381 -0.0257 236 LYS   B O   
2040 C CB  . LYS   B 30  ? 0.3361 0.3484 0.3980 0.0208  -0.0310 -0.0388 236 LYS   B CB  
2041 C CG  . LYS   B 30  ? 0.3836 0.4006 0.4389 0.0185  -0.0252 -0.0392 236 LYS   B CG  
2042 C CD  . LYS   B 30  ? 0.4073 0.4285 0.4632 0.0176  -0.0201 -0.0419 236 LYS   B CD  
2043 C CE  . LYS   B 30  ? 0.4586 0.4831 0.5078 0.0153  -0.0153 -0.0416 236 LYS   B CE  
2044 N NZ  . LYS   B 30  ? 0.4958 0.5249 0.5458 0.0142  -0.0109 -0.0444 236 LYS   B NZ  
2045 N N   . HIS   B 31  ? 0.3122 0.3183 0.3591 0.0189  -0.0365 -0.0307 237 HIS   B N   
2046 C CA  . HIS   B 31  ? 0.3014 0.3035 0.3368 0.0167  -0.0363 -0.0257 237 HIS   B CA  
2047 C C   . HIS   B 31  ? 0.2889 0.2954 0.3189 0.0149  -0.0303 -0.0270 237 HIS   B C   
2048 O O   . HIS   B 31  ? 0.3056 0.3178 0.3400 0.0152  -0.0288 -0.0312 237 HIS   B O   
2049 C CB  . HIS   B 31  ? 0.3098 0.3099 0.3447 0.0174  -0.0420 -0.0244 237 HIS   B CB  
2050 C CG  . HIS   B 31  ? 0.3985 0.3959 0.4214 0.0150  -0.0413 -0.0204 237 HIS   B CG  
2051 N ND1 . HIS   B 31  ? 0.4330 0.4240 0.4472 0.0132  -0.0429 -0.0147 237 HIS   B ND1 
2052 C CD2 . HIS   B 31  ? 0.3648 0.3652 0.3829 0.0139  -0.0390 -0.0215 237 HIS   B CD2 
2053 C CE1 . HIS   B 31  ? 0.4314 0.4222 0.4360 0.0113  -0.0414 -0.0129 237 HIS   B CE1 
2054 N NE2 . HIS   B 31  ? 0.3986 0.3947 0.4055 0.0118  -0.0394 -0.0170 237 HIS   B NE2 
2055 N N   . LEU   B 32  ? 0.2948 0.2985 0.3155 0.0128  -0.0272 -0.0236 238 LEU   B N   
2056 C CA  . LEU   B 32  ? 0.3061 0.3128 0.3215 0.0113  -0.0221 -0.0246 238 LEU   B CA  
2057 C C   . LEU   B 32  ? 0.3283 0.3333 0.3359 0.0102  -0.0232 -0.0227 238 LEU   B C   
2058 O O   . LEU   B 32  ? 0.3362 0.3370 0.3368 0.0092  -0.0246 -0.0189 238 LEU   B O   
2059 C CB  . LEU   B 32  ? 0.2986 0.3041 0.3099 0.0101  -0.0179 -0.0229 238 LEU   B CB  
2060 C CG  . LEU   B 32  ? 0.3753 0.3836 0.3921 0.0106  -0.0150 -0.0253 238 LEU   B CG  
2061 C CD1 . LEU   B 32  ? 0.3629 0.3726 0.3894 0.0124  -0.0179 -0.0280 238 LEU   B CD1 
2062 C CD2 . LEU   B 32  ? 0.3982 0.4041 0.4110 0.0094  -0.0124 -0.0226 238 LEU   B CD2 
2063 N N   . PHE   B 33  ? 0.2961 0.3045 0.3045 0.0101  -0.0226 -0.0255 239 PHE   B N   
2064 C CA  . PHE   B 33  ? 0.2943 0.3013 0.2954 0.0090  -0.0234 -0.0245 239 PHE   B CA  
2065 C C   . PHE   B 33  ? 0.2946 0.3007 0.2877 0.0075  -0.0190 -0.0236 239 PHE   B C   
2066 O O   . PHE   B 33  ? 0.3041 0.3075 0.2893 0.0066  -0.0193 -0.0213 239 PHE   B O   
2067 C CB  . PHE   B 33  ? 0.2706 0.2817 0.2760 0.0091  -0.0245 -0.0280 239 PHE   B CB  
2068 C CG  . PHE   B 33  ? 0.3227 0.3357 0.3368 0.0107  -0.0291 -0.0297 239 PHE   B CG  
2069 C CD1 . PHE   B 33  ? 0.2961 0.3060 0.3087 0.0115  -0.0347 -0.0276 239 PHE   B CD1 
2070 C CD2 . PHE   B 33  ? 0.2988 0.3172 0.3225 0.0115  -0.0281 -0.0336 239 PHE   B CD2 
2071 C CE1 . PHE   B 33  ? 0.3245 0.3362 0.3462 0.0134  -0.0395 -0.0295 239 PHE   B CE1 
2072 C CE2 . PHE   B 33  ? 0.3508 0.3721 0.3840 0.0134  -0.0323 -0.0361 239 PHE   B CE2 
2073 C CZ  . PHE   B 33  ? 0.2945 0.3122 0.3271 0.0146  -0.0382 -0.0340 239 PHE   B CZ  
2074 N N   . VAL   B 34  ? 0.2986 0.3072 0.2938 0.0073  -0.0150 -0.0257 240 VAL   B N   
2075 C CA  . VAL   B 34  ? 0.2910 0.2988 0.2804 0.0064  -0.0111 -0.0253 240 VAL   B CA  
2076 C C   . VAL   B 34  ? 0.3066 0.3159 0.2997 0.0066  -0.0079 -0.0259 240 VAL   B C   
2077 O O   . VAL   B 34  ? 0.3358 0.3478 0.3356 0.0071  -0.0081 -0.0276 240 VAL   B O   
2078 C CB  . VAL   B 34  ? 0.3193 0.3279 0.3063 0.0056  -0.0102 -0.0275 240 VAL   B CB  
2079 C CG1 . VAL   B 34  ? 0.3844 0.3911 0.3660 0.0053  -0.0129 -0.0269 240 VAL   B CG1 
2080 C CG2 . VAL   B 34  ? 0.3572 0.3693 0.3509 0.0053  -0.0104 -0.0301 240 VAL   B CG2 
2081 N N   . HIS   B 35  ? 0.2575 0.2659 0.2464 0.0062  -0.0050 -0.0249 241 HIS   B N   
2082 C CA  . HIS   B 35  ? 0.3157 0.3254 0.3076 0.0063  -0.0022 -0.0254 241 HIS   B CA  
2083 C C   . HIS   B 35  ? 0.3170 0.3259 0.3038 0.0060  0.0006  -0.0249 241 HIS   B C   
2084 O O   . HIS   B 35  ? 0.3320 0.3395 0.3133 0.0057  0.0006  -0.0242 241 HIS   B O   
2085 C CB  . HIS   B 35  ? 0.2238 0.2332 0.2198 0.0068  -0.0032 -0.0241 241 HIS   B CB  
2086 C CG  . HIS   B 35  ? 0.2900 0.2965 0.2818 0.0063  -0.0042 -0.0208 241 HIS   B CG  
2087 N ND1 . HIS   B 35  ? 0.2746 0.2807 0.2618 0.0054  -0.0015 -0.0194 241 HIS   B ND1 
2088 C CD2 . HIS   B 35  ? 0.3041 0.3080 0.2957 0.0062  -0.0077 -0.0186 241 HIS   B CD2 
2089 C CE1 . HIS   B 35  ? 0.3274 0.3311 0.3111 0.0043  -0.0029 -0.0163 241 HIS   B CE1 
2090 N NE2 . HIS   B 35  ? 0.3266 0.3285 0.3125 0.0048  -0.0070 -0.0154 241 HIS   B NE2 
2091 N N   . ILE   B 36  ? 0.2875 0.2975 0.2765 0.0062  0.0029  -0.0256 242 ILE   B N   
2092 C CA  . ILE   B 36  ? 0.2554 0.2653 0.2412 0.0063  0.0053  -0.0256 242 ILE   B CA  
2093 C C   . ILE   B 36  ? 0.2620 0.2726 0.2493 0.0062  0.0068  -0.0241 242 ILE   B C   
2094 O O   . ILE   B 36  ? 0.2973 0.3089 0.2849 0.0064  0.0089  -0.0247 242 ILE   B O   
2095 C CB  . ILE   B 36  ? 0.3339 0.3440 0.3202 0.0065  0.0064  -0.0274 242 ILE   B CB  
2096 C CG1 . ILE   B 36  ? 0.3040 0.3158 0.2950 0.0062  0.0068  -0.0279 242 ILE   B CG1 
2097 C CG2 . ILE   B 36  ? 0.2802 0.2890 0.2643 0.0061  0.0049  -0.0287 242 ILE   B CG2 
2098 C CD1 . ILE   B 36  ? 0.3176 0.3290 0.3083 0.0060  0.0076  -0.0289 242 ILE   B CD1 
2099 N N   . GLY   B 37  ? 0.3224 0.3321 0.3107 0.0057  0.0053  -0.0222 243 GLY   B N   
2100 C CA  . GLY   B 37  ? 0.3450 0.3548 0.3347 0.0051  0.0062  -0.0205 243 GLY   B CA  
2101 C C   . GLY   B 37  ? 0.4097 0.4196 0.3944 0.0038  0.0076  -0.0185 243 GLY   B C   
2102 O O   . GLY   B 37  ? 0.3779 0.3886 0.3639 0.0029  0.0091  -0.0173 243 GLY   B O   
2103 N N   . HIS   B 38  ? 0.3393 0.3486 0.3182 0.0034  0.0074  -0.0183 244 HIS   B N   
2104 C CA  . HIS   B 38  ? 0.3467 0.3567 0.3199 0.0016  0.0088  -0.0165 244 HIS   B CA  
2105 C C   . HIS   B 38  ? 0.3504 0.3623 0.3192 0.0022  0.0108  -0.0191 244 HIS   B C   
2106 O O   . HIS   B 38  ? 0.3634 0.3742 0.3274 0.0020  0.0093  -0.0194 244 HIS   B O   
2107 C CB  . HIS   B 38  ? 0.3792 0.3863 0.3489 0.0001  0.0057  -0.0131 244 HIS   B CB  
2108 C CG  . HIS   B 38  ? 0.4463 0.4540 0.4098 -0.0027 0.0070  -0.0103 244 HIS   B CG  
2109 N ND1 . HIS   B 38  ? 0.5624 0.5734 0.5204 -0.0035 0.0101  -0.0118 244 HIS   B ND1 
2110 C CD2 . HIS   B 38  ? 0.4748 0.4801 0.4363 -0.0052 0.0052  -0.0060 244 HIS   B CD2 
2111 C CE1 . HIS   B 38  ? 0.5041 0.5157 0.4569 -0.0067 0.0109  -0.0087 244 HIS   B CE1 
2112 N NE2 . HIS   B 38  ? 0.6081 0.6158 0.5625 -0.0080 0.0078  -0.0047 244 HIS   B NE2 
2113 N N   . ALA   B 39  ? 0.4167 0.4313 0.3872 0.0030  0.0137  -0.0214 245 ALA   B N   
2114 C CA  . ALA   B 39  ? 0.3692 0.3856 0.3365 0.0039  0.0154  -0.0246 245 ALA   B CA  
2115 C C   . ALA   B 39  ? 0.3777 0.3960 0.3382 0.0019  0.0167  -0.0239 245 ALA   B C   
2116 O O   . ALA   B 39  ? 0.4464 0.4667 0.4055 -0.0003 0.0183  -0.0216 245 ALA   B O   
2117 C CB  . ALA   B 39  ? 0.3658 0.3850 0.3375 0.0053  0.0178  -0.0271 245 ALA   B CB  
2118 N N   . ASN   B 40  ? 0.3974 0.4150 0.3531 0.0023  0.0157  -0.0257 246 ASN   B N   
2119 C CA  . ASN   B 40  ? 0.4713 0.4913 0.4195 0.0006  0.0171  -0.0261 246 ASN   B CA  
2120 C C   . ASN   B 40  ? 0.5592 0.5842 0.5076 0.0014  0.0210  -0.0304 246 ASN   B C   
2121 O O   . ASN   B 40  ? 0.4903 0.5194 0.4336 -0.0007 0.0236  -0.0307 246 ASN   B O   
2122 C CB  . ASN   B 40  ? 0.5021 0.5192 0.4458 0.0010  0.0141  -0.0271 246 ASN   B CB  
2123 C CG  . ASN   B 40  ? 0.6298 0.6493 0.5649 -0.0009 0.0151  -0.0278 246 ASN   B CG  
2124 O OD1 . ASN   B 40  ? 0.6612 0.6828 0.5941 0.0002  0.0165  -0.0323 246 ASN   B OD1 
2125 N ND2 . ASN   B 40  ? 0.6125 0.6312 0.5422 -0.0038 0.0138  -0.0234 246 ASN   B ND2 
2126 N N   . HIS   B 41  ? 0.4992 0.5242 0.4534 0.0043  0.0213  -0.0337 247 HIS   B N   
2127 C CA  . HIS   B 41  ? 0.5204 0.5501 0.4765 0.0057  0.0244  -0.0382 247 HIS   B CA  
2128 C C   . HIS   B 41  ? 0.5606 0.5942 0.5212 0.0048  0.0271  -0.0370 247 HIS   B C   
2129 O O   . HIS   B 41  ? 0.5671 0.5986 0.5304 0.0038  0.0260  -0.0331 247 HIS   B O   
2130 C CB  . HIS   B 41  ? 0.5175 0.5445 0.4782 0.0091  0.0228  -0.0420 247 HIS   B CB  
2131 C CG  . HIS   B 41  ? 0.4551 0.4782 0.4213 0.0100  0.0205  -0.0397 247 HIS   B CG  
2132 N ND1 . HIS   B 41  ? 0.3750 0.3935 0.3406 0.0094  0.0175  -0.0370 247 HIS   B ND1 
2133 C CD2 . HIS   B 41  ? 0.5483 0.5719 0.5207 0.0112  0.0209  -0.0400 247 HIS   B CD2 
2134 C CE1 . HIS   B 41  ? 0.3765 0.3933 0.3472 0.0100  0.0166  -0.0359 247 HIS   B CE1 
2135 N NE2 . HIS   B 41  ? 0.5335 0.5530 0.5081 0.0111  0.0184  -0.0374 247 HIS   B NE2 
2136 N N   . SER   B 42  ? 0.5820 0.6216 0.5441 0.0053  0.0305  -0.0407 248 SER   B N   
2137 C CA  . SER   B 42  ? 0.6949 0.7394 0.6613 0.0040  0.0333  -0.0399 248 SER   B CA  
2138 C C   . SER   B 42  ? 0.6514 0.6944 0.6263 0.0068  0.0320  -0.0408 248 SER   B C   
2139 O O   . SER   B 42  ? 0.6627 0.7043 0.6409 0.0101  0.0307  -0.0444 248 SER   B O   
2140 C CB  . SER   B 42  ? 0.7487 0.8015 0.7142 0.0034  0.0376  -0.0442 248 SER   B CB  
2141 O OG  . SER   B 42  ? 0.8552 0.9134 0.8257 0.0020  0.0404  -0.0436 248 SER   B OG  
2142 N N   . TYR   B 43  ? 0.7282 0.7715 0.7065 0.0052  0.0322  -0.0373 249 TYR   B N   
2143 C CA  . TYR   B 43  ? 0.7109 0.7542 0.6969 0.0073  0.0315  -0.0383 249 TYR   B CA  
2144 C C   . TYR   B 43  ? 0.7729 0.8236 0.7639 0.0083  0.0346  -0.0425 249 TYR   B C   
2145 O O   . TYR   B 43  ? 0.7897 0.8408 0.7874 0.0108  0.0336  -0.0443 249 TYR   B O   
2146 C CB  . TYR   B 43  ? 0.8224 0.8635 0.8105 0.0054  0.0305  -0.0338 249 TYR   B CB  
2147 C CG  . TYR   B 43  ? 0.8419 0.8822 0.8371 0.0072  0.0291  -0.0342 249 TYR   B CG  
2148 C CD1 . TYR   B 43  ? 0.8606 0.9060 0.8613 0.0070  0.0310  -0.0353 249 TYR   B CD1 
2149 C CD2 . TYR   B 43  ? 0.7496 0.7845 0.7456 0.0088  0.0258  -0.0336 249 TYR   B CD2 
2150 C CE1 . TYR   B 43  ? 0.8008 0.8454 0.8075 0.0086  0.0293  -0.0357 249 TYR   B CE1 
2151 C CE2 . TYR   B 43  ? 0.7675 0.8018 0.7688 0.0101  0.0245  -0.0339 249 TYR   B CE2 
2152 C CZ  . TYR   B 43  ? 0.9231 0.9620 0.9296 0.0101  0.0260  -0.0349 249 TYR   B CZ  
2153 O OH  . TYR   B 43  ? 0.7985 0.8367 0.8098 0.0113  0.0242  -0.0352 249 TYR   B OH  
2154 N N   . SER   B 44  ? 0.8381 0.8951 0.8260 0.0065  0.0382  -0.0443 250 SER   B N   
2155 C CA  . SER   B 44  ? 0.8219 0.8875 0.8151 0.0071  0.0416  -0.0488 250 SER   B CA  
2156 C C   . SER   B 44  ? 0.7791 0.8455 0.7763 0.0118  0.0407  -0.0551 250 SER   B C   
2157 O O   . SER   B 44  ? 0.8657 0.9357 0.8709 0.0143  0.0408  -0.0585 250 SER   B O   
2158 C CB  . SER   B 44  ? 0.7751 0.8479 0.7632 0.0031  0.0461  -0.0488 250 SER   B CB  
2159 O OG  . SER   B 44  ? 0.9294 1.0028 0.9166 -0.0013 0.0471  -0.0435 250 SER   B OG  
2160 N N   . ASP   B 45  ? 0.7190 0.7823 0.7112 0.0131  0.0395  -0.0571 251 ASP   B N   
2161 C CA  . ASP   B 45  ? 0.7470 0.8087 0.7434 0.0178  0.0374  -0.0627 251 ASP   B CA  
2162 C C   . ASP   B 45  ? 0.6339 0.6877 0.6341 0.0198  0.0328  -0.0601 251 ASP   B C   
2163 O O   . ASP   B 45  ? 0.6647 0.7121 0.6606 0.0184  0.0305  -0.0555 251 ASP   B O   
2164 C CB  . ASP   B 45  ? 0.7351 0.7943 0.7255 0.0186  0.0366  -0.0655 251 ASP   B CB  
2165 C CG  . ASP   B 45  ? 0.8575 0.9223 0.8401 0.0150  0.0404  -0.0655 251 ASP   B CG  
2166 O OD1 . ASP   B 45  ? 0.9143 0.9880 0.8980 0.0132  0.0448  -0.0674 251 ASP   B OD1 
2167 O OD2 . ASP   B 45  ? 0.8324 0.8927 0.8074 0.0138  0.0390  -0.0638 251 ASP   B OD2 
2168 N N   . PRO   B 46  ? 0.7233 0.7776 0.7313 0.0230  0.0311  -0.0628 252 PRO   B N   
2169 C CA  . PRO   B 46  ? 0.7090 0.7553 0.7191 0.0246  0.0264  -0.0603 252 PRO   B CA  
2170 C C   . PRO   B 46  ? 0.6695 0.7086 0.6765 0.0264  0.0230  -0.0614 252 PRO   B C   
2171 O O   . PRO   B 46  ? 0.6295 0.6615 0.6353 0.0262  0.0195  -0.0580 252 PRO   B O   
2172 C CB  . PRO   B 46  ? 0.7122 0.7616 0.7314 0.0275  0.0254  -0.0633 252 PRO   B CB  
2173 C CG  . PRO   B 46  ? 0.7703 0.8300 0.7926 0.0264  0.0302  -0.0658 252 PRO   B CG  
2174 C CD  . PRO   B 46  ? 0.7888 0.8518 0.8045 0.0245  0.0336  -0.0673 252 PRO   B CD  
2175 N N   . LEU   B 47  ? 0.6115 0.6525 0.6170 0.0278  0.0239  -0.0662 253 LEU   B N   
2176 C CA  . LEU   B 47  ? 0.5737 0.6078 0.5770 0.0297  0.0204  -0.0682 253 LEU   B CA  
2177 C C   . LEU   B 47  ? 0.5734 0.6048 0.5683 0.0269  0.0208  -0.0656 253 LEU   B C   
2178 O O   . LEU   B 47  ? 0.5804 0.6169 0.5707 0.0248  0.0243  -0.0657 253 LEU   B O   
2179 C CB  . LEU   B 47  ? 0.5189 0.5565 0.5259 0.0332  0.0207  -0.0757 253 LEU   B CB  
2180 C CG  . LEU   B 47  ? 0.6664 0.7023 0.6823 0.0374  0.0173  -0.0791 253 LEU   B CG  
2181 C CD1 . LEU   B 47  ? 0.5748 0.6201 0.5970 0.0379  0.0207  -0.0811 253 LEU   B CD1 
2182 C CD2 . LEU   B 47  ? 0.5914 0.6246 0.6096 0.0412  0.0146  -0.0857 253 LEU   B CD2 
2183 N N   . LEU   B 48  ? 0.4839 0.5072 0.4767 0.0269  0.0169  -0.0635 254 LEU   B N   
2184 C CA  . LEU   B 48  ? 0.4563 0.4765 0.4420 0.0247  0.0164  -0.0616 254 LEU   B CA  
2185 C C   . LEU   B 48  ? 0.4776 0.4981 0.4610 0.0263  0.0163  -0.0671 254 LEU   B C   
2186 O O   . LEU   B 48  ? 0.4752 0.4943 0.4630 0.0295  0.0145  -0.0719 254 LEU   B O   
2187 C CB  . LEU   B 48  ? 0.4940 0.5064 0.4790 0.0238  0.0125  -0.0577 254 LEU   B CB  
2188 C CG  . LEU   B 48  ? 0.4943 0.5066 0.4802 0.0217  0.0127  -0.0524 254 LEU   B CG  
2189 C CD1 . LEU   B 48  ? 0.5090 0.5147 0.4953 0.0210  0.0090  -0.0496 254 LEU   B CD1 
2190 C CD2 . LEU   B 48  ? 0.4254 0.4408 0.4069 0.0189  0.0152  -0.0493 254 LEU   B CD2 
2191 N N   . GLU   B 49  ? 0.3838 0.4058 0.3604 0.0240  0.0178  -0.0666 255 GLU   B N   
2192 C CA  . GLU   B 49  ? 0.3981 0.4190 0.3711 0.0250  0.0169  -0.0712 255 GLU   B CA  
2193 C C   . GLU   B 49  ? 0.4573 0.4694 0.4312 0.0259  0.0120  -0.0708 255 GLU   B C   
2194 O O   . GLU   B 49  ? 0.4574 0.4648 0.4320 0.0245  0.0098  -0.0658 255 GLU   B O   
2195 C CB  . GLU   B 49  ? 0.4716 0.4951 0.4362 0.0218  0.0188  -0.0693 255 GLU   B CB  
2196 C CG  . GLU   B 49  ? 0.5536 0.5858 0.5158 0.0199  0.0236  -0.0693 255 GLU   B CG  
2197 C CD  . GLU   B 49  ? 0.6099 0.6426 0.5638 0.0160  0.0243  -0.0647 255 GLU   B CD  
2198 O OE1 . GLU   B 49  ? 0.6362 0.6697 0.5837 0.0152  0.0243  -0.0670 255 GLU   B OE1 
2199 O OE2 . GLU   B 49  ? 0.6284 0.6602 0.5823 0.0139  0.0243  -0.0588 255 GLU   B OE2 
2200 N N   . SER   B 50  ? 0.4528 0.4627 0.4266 0.0279  0.0102  -0.0762 256 SER   B N   
2201 C CA  . SER   B 50  ? 0.4703 0.4715 0.4451 0.0284  0.0053  -0.0761 256 SER   B CA  
2202 C C   . SER   B 50  ? 0.5104 0.5099 0.4789 0.0270  0.0043  -0.0776 256 SER   B C   
2203 O O   . SER   B 50  ? 0.5109 0.5160 0.4747 0.0265  0.0071  -0.0803 256 SER   B O   
2204 C CB  . SER   B 50  ? 0.4641 0.4622 0.4455 0.0324  0.0026  -0.0813 256 SER   B CB  
2205 O OG  . SER   B 50  ? 0.5659 0.5686 0.5471 0.0346  0.0043  -0.0886 256 SER   B OG  
2206 N N   . VAL   B 51  ? 0.4266 0.4187 0.3947 0.0258  0.0003  -0.0754 257 VAL   B N   
2207 C CA  . VAL   B 51  ? 0.4362 0.4256 0.3994 0.0243  -0.0016 -0.0763 257 VAL   B CA  
2208 C C   . VAL   B 51  ? 0.4649 0.4459 0.4315 0.0253  -0.0066 -0.0782 257 VAL   B C   
2209 O O   . VAL   B 51  ? 0.4001 0.3762 0.3705 0.0248  -0.0089 -0.0747 257 VAL   B O   
2210 C CB  . VAL   B 51  ? 0.4858 0.4755 0.4450 0.0206  -0.0015 -0.0702 257 VAL   B CB  
2211 C CG1 . VAL   B 51  ? 0.4818 0.4667 0.4382 0.0191  -0.0050 -0.0708 257 VAL   B CG1 
2212 C CG2 . VAL   B 51  ? 0.4995 0.4963 0.4538 0.0194  0.0024  -0.0691 257 VAL   B CG2 
2213 N N   . ASP   B 52  ? 0.4743 0.4535 0.4394 0.0266  -0.0083 -0.0839 258 ASP   B N   
2214 C CA  . ASP   B 52  ? 0.4706 0.4411 0.4387 0.0274  -0.0134 -0.0862 258 ASP   B CA  
2215 C C   . ASP   B 52  ? 0.3933 0.3587 0.3593 0.0235  -0.0161 -0.0809 258 ASP   B C   
2216 O O   . ASP   B 52  ? 0.4542 0.4220 0.4153 0.0212  -0.0155 -0.0801 258 ASP   B O   
2217 C CB  . ASP   B 52  ? 0.4881 0.4590 0.4548 0.0297  -0.0142 -0.0942 258 ASP   B CB  
2218 C CG  . ASP   B 52  ? 0.5671 0.5283 0.5363 0.0301  -0.0200 -0.0968 258 ASP   B CG  
2219 O OD1 . ASP   B 52  ? 0.5194 0.4732 0.4926 0.0294  -0.0236 -0.0932 258 ASP   B OD1 
2220 O OD2 . ASP   B 52  ? 0.7179 0.6788 0.6847 0.0309  -0.0211 -0.1025 258 ASP   B OD2 
2221 N N   . ILE   B 53  ? 0.4454 0.4043 0.4152 0.0224  -0.0193 -0.0772 259 ILE   B N   
2222 C CA  . ILE   B 53  ? 0.4470 0.4027 0.4153 0.0181  -0.0211 -0.0718 259 ILE   B CA  
2223 C C   . ILE   B 53  ? 0.4928 0.4443 0.4590 0.0166  -0.0243 -0.0743 259 ILE   B C   
2224 O O   . ILE   B 53  ? 0.4629 0.4148 0.4270 0.0131  -0.0248 -0.0711 259 ILE   B O   
2225 C CB  . ILE   B 53  ? 0.4417 0.3918 0.4138 0.0167  -0.0236 -0.0674 259 ILE   B CB  
2226 C CG1 . ILE   B 53  ? 0.4107 0.3614 0.3813 0.0120  -0.0233 -0.0613 259 ILE   B CG1 
2227 C CG2 . ILE   B 53  ? 0.4349 0.3755 0.4099 0.0176  -0.0290 -0.0700 259 ILE   B CG2 
2228 C CD1 . ILE   B 53  ? 0.4391 0.3852 0.4120 0.0098  -0.0253 -0.0567 259 ILE   B CD1 
2229 N N   . ARG   B 54  ? 0.4707 0.4185 0.4380 0.0193  -0.0268 -0.0805 260 ARG   B N   
2230 C CA  . ARG   B 54  ? 0.5596 0.5028 0.5253 0.0179  -0.0303 -0.0834 260 ARG   B CA  
2231 C C   . ARG   B 54  ? 0.5361 0.4856 0.4961 0.0164  -0.0281 -0.0840 260 ARG   B C   
2232 O O   . ARG   B 54  ? 0.5521 0.4989 0.5104 0.0137  -0.0308 -0.0838 260 ARG   B O   
2233 C CB  . ARG   B 54  ? 0.4787 0.4170 0.4471 0.0217  -0.0333 -0.0909 260 ARG   B CB  
2234 C CG  . ARG   B 54  ? 0.5830 0.5131 0.5575 0.0229  -0.0371 -0.0898 260 ARG   B CG  
2235 C CD  . ARG   B 54  ? 0.7446 0.6713 0.7234 0.0279  -0.0397 -0.0977 260 ARG   B CD  
2236 N NE  . ARG   B 54  ? 0.6152 0.5511 0.5942 0.0319  -0.0349 -0.1025 260 ARG   B NE  
2237 C CZ  . ARG   B 54  ? 0.8011 0.7371 0.7843 0.0368  -0.0357 -0.1103 260 ARG   B CZ  
2238 N NH1 . ARG   B 54  ? 0.6812 0.6079 0.6692 0.0388  -0.0416 -0.1145 260 ARG   B NH1 
2239 N NH2 . ARG   B 54  ? 0.7256 0.6716 0.7087 0.0396  -0.0305 -0.1142 260 ARG   B NH2 
2240 N N   . GLN   B 55  ? 0.5177 0.4754 0.4745 0.0176  -0.0236 -0.0842 261 GLN   B N   
2241 C CA  . GLN   B 55  ? 0.6000 0.5629 0.5507 0.0160  -0.0221 -0.0842 261 GLN   B CA  
2242 C C   . GLN   B 55  ? 0.5908 0.5564 0.5406 0.0127  -0.0212 -0.0773 261 GLN   B C   
2243 O O   . GLN   B 55  ? 0.5909 0.5608 0.5359 0.0115  -0.0203 -0.0767 261 GLN   B O   
2244 C CB  . GLN   B 55  ? 0.7047 0.6750 0.6515 0.0184  -0.0180 -0.0879 261 GLN   B CB  
2245 C CG  . GLN   B 55  ? 0.6679 0.6439 0.6151 0.0188  -0.0136 -0.0842 261 GLN   B CG  
2246 C CD  . GLN   B 55  ? 0.9125 0.8955 0.8567 0.0210  -0.0097 -0.0890 261 GLN   B CD  
2247 O OE1 . GLN   B 55  ? 0.9902 0.9793 0.9321 0.0203  -0.0059 -0.0861 261 GLN   B OE1 
2248 N NE2 . GLN   B 55  ? 0.8584 0.8407 0.8025 0.0234  -0.0106 -0.0964 261 GLN   B NE2 
2249 N N   . ILE   B 56  ? 0.4734 0.4366 0.4274 0.0111  -0.0216 -0.0724 262 ILE   B N   
2250 C CA  . ILE   B 56  ? 0.5207 0.4864 0.4748 0.0080  -0.0212 -0.0669 262 ILE   B CA  
2251 C C   . ILE   B 56  ? 0.5040 0.4648 0.4615 0.0048  -0.0245 -0.0646 262 ILE   B C   
2252 O O   . ILE   B 56  ? 0.4572 0.4206 0.4158 0.0021  -0.0241 -0.0606 262 ILE   B O   
2253 C CB  . ILE   B 56  ? 0.5134 0.4835 0.4689 0.0084  -0.0175 -0.0628 262 ILE   B CB  
2254 C CG1 . ILE   B 56  ? 0.4395 0.4059 0.3996 0.0087  -0.0179 -0.0611 262 ILE   B CG1 
2255 C CG2 . ILE   B 56  ? 0.5485 0.5239 0.5008 0.0109  -0.0141 -0.0647 262 ILE   B CG2 
2256 C CD1 . ILE   B 56  ? 0.4514 0.4212 0.4134 0.0075  -0.0155 -0.0561 262 ILE   B CD1 
2257 N N   . TYR   B 57  ? 0.4765 0.4303 0.4359 0.0048  -0.0278 -0.0671 263 TYR   B N   
2258 C CA  . TYR   B 57  ? 0.5179 0.4667 0.4801 0.0010  -0.0310 -0.0646 263 TYR   B CA  
2259 C C   . TYR   B 57  ? 0.4835 0.4350 0.4448 -0.0023 -0.0322 -0.0638 263 TYR   B C   
2260 O O   . TYR   B 57  ? 0.5088 0.4605 0.4727 -0.0060 -0.0328 -0.0601 263 TYR   B O   
2261 C CB  . TYR   B 57  ? 0.5475 0.4875 0.5113 0.0017  -0.0352 -0.0681 263 TYR   B CB  
2262 C CG  . TYR   B 57  ? 0.5057 0.4410 0.4724 0.0036  -0.0357 -0.0673 263 TYR   B CG  
2263 C CD1 . TYR   B 57  ? 0.5455 0.4829 0.5135 0.0026  -0.0335 -0.0622 263 TYR   B CD1 
2264 C CD2 . TYR   B 57  ? 0.5658 0.4944 0.5342 0.0065  -0.0388 -0.0720 263 TYR   B CD2 
2265 C CE1 . TYR   B 57  ? 0.5554 0.4886 0.5259 0.0042  -0.0344 -0.0614 263 TYR   B CE1 
2266 C CE2 . TYR   B 57  ? 0.5034 0.4275 0.4750 0.0085  -0.0400 -0.0714 263 TYR   B CE2 
2267 C CZ  . TYR   B 57  ? 0.5336 0.4600 0.5061 0.0072  -0.0379 -0.0658 263 TYR   B CZ  
2268 O OH  . TYR   B 57  ? 0.6429 0.5649 0.6184 0.0091  -0.0395 -0.0649 263 TYR   B OH  
2269 N N   . ASP   B 58  ? 0.5287 0.4827 0.4864 -0.0010 -0.0325 -0.0673 264 ASP   B N   
2270 C CA  . ASP   B 58  ? 0.4652 0.4214 0.4227 -0.0041 -0.0345 -0.0667 264 ASP   B CA  
2271 C C   . ASP   B 58  ? 0.5795 0.5431 0.5373 -0.0049 -0.0320 -0.0628 264 ASP   B C   
2272 O O   . ASP   B 58  ? 0.5381 0.5043 0.4971 -0.0074 -0.0337 -0.0620 264 ASP   B O   
2273 C CB  . ASP   B 58  ? 0.5706 0.5262 0.5240 -0.0029 -0.0367 -0.0719 264 ASP   B CB  
2274 C CG  . ASP   B 58  ? 0.6954 0.6561 0.6434 0.0003  -0.0340 -0.0737 264 ASP   B CG  
2275 O OD1 . ASP   B 58  ? 0.9283 0.8900 0.8717 0.0008  -0.0353 -0.0774 264 ASP   B OD1 
2276 O OD2 . ASP   B 58  ? 0.8691 0.8328 0.8171 0.0019  -0.0304 -0.0714 264 ASP   B OD2 
2277 N N   . LYS   B 59  ? 0.4691 0.4360 0.4264 -0.0030 -0.0284 -0.0606 265 LYS   B N   
2278 C CA  . LYS   B 59  ? 0.4691 0.4423 0.4275 -0.0037 -0.0265 -0.0570 265 LYS   B CA  
2279 C C   . LYS   B 59  ? 0.4744 0.4485 0.4380 -0.0061 -0.0254 -0.0532 265 LYS   B C   
2280 O O   . LYS   B 59  ? 0.4307 0.4100 0.3963 -0.0066 -0.0238 -0.0507 265 LYS   B O   
2281 C CB  . LYS   B 59  ? 0.5136 0.4902 0.4686 -0.0007 -0.0233 -0.0566 265 LYS   B CB  
2282 C CG  . LYS   B 59  ? 0.5913 0.5681 0.5402 0.0012  -0.0238 -0.0603 265 LYS   B CG  
2283 C CD  . LYS   B 59  ? 0.5611 0.5418 0.5064 0.0034  -0.0204 -0.0596 265 LYS   B CD  
2284 C CE  . LYS   B 59  ? 0.7515 0.7335 0.6898 0.0044  -0.0207 -0.0630 265 LYS   B CE  
2285 N NZ  . LYS   B 59  ? 0.8686 0.8473 0.8061 0.0061  -0.0210 -0.0684 265 LYS   B NZ  
2286 N N   . PHE   B 60  ? 0.3920 0.3612 0.3577 -0.0077 -0.0264 -0.0529 266 PHE   B N   
2287 C CA  . PHE   B 60  ? 0.4272 0.3972 0.3966 -0.0104 -0.0252 -0.0493 266 PHE   B CA  
2288 C C   . PHE   B 60  ? 0.4890 0.4544 0.4603 -0.0145 -0.0281 -0.0490 266 PHE   B C   
2289 O O   . PHE   B 60  ? 0.4674 0.4278 0.4375 -0.0145 -0.0312 -0.0518 266 PHE   B O   
2290 C CB  . PHE   B 60  ? 0.4144 0.3827 0.3833 -0.0081 -0.0230 -0.0480 266 PHE   B CB  
2291 C CG  . PHE   B 60  ? 0.3786 0.3521 0.3463 -0.0050 -0.0199 -0.0476 266 PHE   B CG  
2292 C CD1 . PHE   B 60  ? 0.3838 0.3628 0.3538 -0.0059 -0.0177 -0.0449 266 PHE   B CD1 
2293 C CD2 . PHE   B 60  ? 0.3968 0.3699 0.3610 -0.0016 -0.0192 -0.0503 266 PHE   B CD2 
2294 C CE1 . PHE   B 60  ? 0.2987 0.2817 0.2676 -0.0034 -0.0153 -0.0443 266 PHE   B CE1 
2295 C CE2 . PHE   B 60  ? 0.4196 0.3974 0.3823 0.0005  -0.0165 -0.0495 266 PHE   B CE2 
2296 C CZ  . PHE   B 60  ? 0.3949 0.3771 0.3599 -0.0005 -0.0147 -0.0463 266 PHE   B CZ  
2297 N N   . PRO   B 61  ? 0.5024 0.4697 0.4768 -0.0183 -0.0273 -0.0458 267 PRO   B N   
2298 C CA  . PRO   B 61  ? 0.4914 0.4546 0.4674 -0.0233 -0.0300 -0.0450 267 PRO   B CA  
2299 C C   . PRO   B 61  ? 0.5322 0.4855 0.5063 -0.0228 -0.0330 -0.0456 267 PRO   B C   
2300 O O   . PRO   B 61  ? 0.5331 0.4832 0.5058 -0.0197 -0.0322 -0.0454 267 PRO   B O   
2301 C CB  . PRO   B 61  ? 0.5557 0.5236 0.5343 -0.0271 -0.0276 -0.0412 267 PRO   B CB  
2302 C CG  . PRO   B 61  ? 0.5374 0.5134 0.5171 -0.0243 -0.0242 -0.0412 267 PRO   B CG  
2303 C CD  . PRO   B 61  ? 0.4767 0.4504 0.4531 -0.0188 -0.0239 -0.0430 267 PRO   B CD  
2304 N N   . GLU   B 62  ? 0.5282 0.4763 0.5029 -0.0260 -0.0366 -0.0466 268 GLU   B N   
2305 C CA  . GLU   B 62  ? 0.6071 0.5448 0.5807 -0.0253 -0.0405 -0.0479 268 GLU   B CA  
2306 C C   . GLU   B 62  ? 0.6480 0.5802 0.6230 -0.0316 -0.0433 -0.0446 268 GLU   B C   
2307 O O   . GLU   B 62  ? 0.6899 0.6273 0.6665 -0.0366 -0.0417 -0.0415 268 GLU   B O   
2308 C CB  . GLU   B 62  ? 0.6462 0.5813 0.6187 -0.0225 -0.0431 -0.0533 268 GLU   B CB  
2309 C CG  . GLU   B 62  ? 0.6229 0.5623 0.5928 -0.0166 -0.0405 -0.0565 268 GLU   B CG  
2310 C CD  . GLU   B 62  ? 0.7101 0.6473 0.6779 -0.0140 -0.0428 -0.0621 268 GLU   B CD  
2311 O OE1 . GLU   B 62  ? 0.6987 0.6406 0.6656 -0.0148 -0.0430 -0.0634 268 GLU   B OE1 
2312 O OE2 . GLU   B 62  ? 0.7510 0.6819 0.7180 -0.0111 -0.0447 -0.0655 268 GLU   B OE2 
2313 N N   . LYS   B 63  ? 0.6881 0.6097 0.6625 -0.0313 -0.0475 -0.0453 269 LYS   B N   
2314 C CA  . LYS   B 63  ? 0.7430 0.6570 0.7179 -0.0374 -0.0510 -0.0416 269 LYS   B CA  
2315 C C   . LYS   B 63  ? 0.7497 0.6662 0.7238 -0.0404 -0.0486 -0.0359 269 LYS   B C   
2316 O O   . LYS   B 63  ? 0.6331 0.5523 0.6062 -0.0362 -0.0458 -0.0355 269 LYS   B O   
2317 C CB  . LYS   B 63  ? 0.8422 0.7576 0.8190 -0.0428 -0.0527 -0.0419 269 LYS   B CB  
2318 C CG  . LYS   B 63  ? 0.7681 0.6815 0.7453 -0.0397 -0.0553 -0.0478 269 LYS   B CG  
2319 C CD  . LYS   B 63  ? 0.7851 0.7067 0.7642 -0.0427 -0.0543 -0.0490 269 LYS   B CD  
2320 C CE  . LYS   B 63  ? 0.7988 0.7239 0.7768 -0.0373 -0.0541 -0.0546 269 LYS   B CE  
2321 N NZ  . LYS   B 63  ? 0.8173 0.7539 0.7966 -0.0376 -0.0509 -0.0545 269 LYS   B NZ  
2322 N N   . LYS   B 64  ? 0.7389 0.6545 0.7131 -0.0478 -0.0495 -0.0315 270 LYS   B N   
2323 C CA  . LYS   B 64  ? 0.6869 0.6032 0.6592 -0.0514 -0.0479 -0.0261 270 LYS   B CA  
2324 C C   . LYS   B 64  ? 0.7359 0.6639 0.7084 -0.0490 -0.0420 -0.0260 270 LYS   B C   
2325 O O   . LYS   B 64  ? 0.7486 0.6861 0.7233 -0.0489 -0.0388 -0.0281 270 LYS   B O   
2326 C CB  . LYS   B 64  ? 0.8591 0.7749 0.8311 -0.0607 -0.0490 -0.0218 270 LYS   B CB  
2327 C CG  . LYS   B 64  ? 0.8571 0.7750 0.8263 -0.0657 -0.0471 -0.0160 270 LYS   B CG  
2328 C CD  . LYS   B 64  ? 1.0285 0.9391 0.9956 -0.0746 -0.0508 -0.0109 270 LYS   B CD  
2329 C CE  . LYS   B 64  ? 0.9898 0.9057 0.9535 -0.0809 -0.0478 -0.0054 270 LYS   B CE  
2330 N NZ  . LYS   B 64  ? 1.0602 0.9650 1.0195 -0.0877 -0.0526 0.0008  270 LYS   B NZ  
2331 N N   . GLY   B 65  ? 0.7511 0.6781 0.7217 -0.0467 -0.0409 -0.0239 271 GLY   B N   
2332 C CA  . GLY   B 65  ? 0.7634 0.7004 0.7343 -0.0441 -0.0357 -0.0239 271 GLY   B CA  
2333 C C   . GLY   B 65  ? 0.6501 0.5914 0.6224 -0.0369 -0.0336 -0.0285 271 GLY   B C   
2334 O O   . GLY   B 65  ? 0.7208 0.6699 0.6936 -0.0346 -0.0295 -0.0286 271 GLY   B O   
2335 N N   . GLY   B 66  ? 0.5791 0.5156 0.5518 -0.0335 -0.0362 -0.0324 272 GLY   B N   
2336 C CA  . GLY   B 66  ? 0.6006 0.5412 0.5736 -0.0274 -0.0342 -0.0365 272 GLY   B CA  
2337 C C   . GLY   B 66  ? 0.6143 0.5525 0.5863 -0.0218 -0.0337 -0.0376 272 GLY   B C   
2338 O O   . GLY   B 66  ? 0.5353 0.4686 0.5068 -0.0220 -0.0350 -0.0351 272 GLY   B O   
2339 N N   . LEU   B 67  ? 0.5430 0.4851 0.5148 -0.0167 -0.0318 -0.0413 273 LEU   B N   
2340 C CA  . LEU   B 67  ? 0.4759 0.4184 0.4473 -0.0117 -0.0301 -0.0424 273 LEU   B CA  
2341 C C   . LEU   B 67  ? 0.4672 0.4007 0.4390 -0.0092 -0.0339 -0.0442 273 LEU   B C   
2342 O O   . LEU   B 67  ? 0.4898 0.4218 0.4623 -0.0071 -0.0337 -0.0431 273 LEU   B O   
2343 C CB  . LEU   B 67  ? 0.3978 0.3466 0.3683 -0.0078 -0.0273 -0.0458 273 LEU   B CB  
2344 C CG  . LEU   B 67  ? 0.3982 0.3495 0.3684 -0.0031 -0.0247 -0.0470 273 LEU   B CG  
2345 C CD1 . LEU   B 67  ? 0.3604 0.3149 0.3317 -0.0039 -0.0224 -0.0430 273 LEU   B CD1 
2346 C CD2 . LEU   B 67  ? 0.3925 0.3500 0.3610 -0.0007 -0.0223 -0.0496 273 LEU   B CD2 
2347 N N   . LYS   B 68  ? 0.4929 0.4203 0.4648 -0.0093 -0.0376 -0.0472 274 LYS   B N   
2348 C CA  . LYS   B 68  ? 0.4707 0.3892 0.4439 -0.0064 -0.0417 -0.0498 274 LYS   B CA  
2349 C C   . LYS   B 68  ? 0.5206 0.4320 0.4945 -0.0094 -0.0449 -0.0450 274 LYS   B C   
2350 O O   . LYS   B 68  ? 0.4893 0.3965 0.4646 -0.0062 -0.0466 -0.0453 274 LYS   B O   
2351 C CB  . LYS   B 68  ? 0.5321 0.4453 0.5055 -0.0063 -0.0453 -0.0541 274 LYS   B CB  
2352 C CG  . LYS   B 68  ? 0.5544 0.4581 0.5301 -0.0031 -0.0501 -0.0578 274 LYS   B CG  
2353 C CD  . LYS   B 68  ? 0.6150 0.5147 0.5906 -0.0030 -0.0532 -0.0628 274 LYS   B CD  
2354 C CE  . LYS   B 68  ? 0.7051 0.5932 0.6837 -0.0009 -0.0594 -0.0660 274 LYS   B CE  
2355 N NZ  . LYS   B 68  ? 0.7876 0.6710 0.7665 -0.0019 -0.0630 -0.0704 274 LYS   B NZ  
2356 N N   . GLU   B 69  ? 0.4992 0.4096 0.4719 -0.0157 -0.0457 -0.0404 275 GLU   B N   
2357 C CA  . GLU   B 69  ? 0.5884 0.4924 0.5604 -0.0197 -0.0486 -0.0351 275 GLU   B CA  
2358 C C   . GLU   B 69  ? 0.5608 0.4699 0.5321 -0.0186 -0.0454 -0.0320 275 GLU   B C   
2359 O O   . GLU   B 69  ? 0.5220 0.4249 0.4932 -0.0183 -0.0484 -0.0296 275 GLU   B O   
2360 C CB  . GLU   B 69  ? 0.6208 0.5243 0.5914 -0.0275 -0.0495 -0.0310 275 GLU   B CB  
2361 C CG  . GLU   B 69  ? 0.7783 0.6722 0.7475 -0.0324 -0.0542 -0.0258 275 GLU   B CG  
2362 C CD  . GLU   B 69  ? 0.9030 0.8003 0.8700 -0.0409 -0.0528 -0.0205 275 GLU   B CD  
2363 O OE1 . GLU   B 69  ? 0.8540 0.7584 0.8219 -0.0433 -0.0501 -0.0219 275 GLU   B OE1 
2364 O OE2 . GLU   B 69  ? 1.0698 0.9627 1.0342 -0.0453 -0.0548 -0.0152 275 GLU   B OE2 
2365 N N   . LEU   B 70  ? 0.5157 0.4355 0.4866 -0.0182 -0.0398 -0.0320 276 LEU   B N   
2366 C CA  . LEU   B 70  ? 0.4920 0.4168 0.4626 -0.0168 -0.0368 -0.0298 276 LEU   B CA  
2367 C C   . LEU   B 70  ? 0.4644 0.3866 0.4368 -0.0104 -0.0377 -0.0327 276 LEU   B C   
2368 O O   . LEU   B 70  ? 0.4450 0.3644 0.4176 -0.0098 -0.0392 -0.0304 276 LEU   B O   
2369 C CB  . LEU   B 70  ? 0.4607 0.3968 0.4314 -0.0167 -0.0311 -0.0303 276 LEU   B CB  
2370 C CG  . LEU   B 70  ? 0.5294 0.4706 0.4993 -0.0229 -0.0292 -0.0271 276 LEU   B CG  
2371 C CD1 . LEU   B 70  ? 0.5370 0.4883 0.5083 -0.0216 -0.0248 -0.0291 276 LEU   B CD1 
2372 C CD2 . LEU   B 70  ? 0.4786 0.4200 0.4468 -0.0261 -0.0289 -0.0226 276 LEU   B CD2 
2373 N N   . PHE   B 71  ? 0.3875 0.3115 0.3615 -0.0057 -0.0368 -0.0381 277 PHE   B N   
2374 C CA  . PHE   B 71  ? 0.4743 0.3976 0.4506 0.0004  -0.0370 -0.0419 277 PHE   B CA  
2375 C C   . PHE   B 71  ? 0.4644 0.3771 0.4428 0.0015  -0.0431 -0.0421 277 PHE   B C   
2376 O O   . PHE   B 71  ? 0.4796 0.3911 0.4603 0.0050  -0.0440 -0.0426 277 PHE   B O   
2377 C CB  . PHE   B 71  ? 0.4158 0.3431 0.3926 0.0043  -0.0350 -0.0478 277 PHE   B CB  
2378 C CG  . PHE   B 71  ? 0.4593 0.3888 0.4387 0.0102  -0.0339 -0.0522 277 PHE   B CG  
2379 C CD1 . PHE   B 71  ? 0.4061 0.3435 0.3858 0.0119  -0.0293 -0.0514 277 PHE   B CD1 
2380 C CD2 . PHE   B 71  ? 0.4799 0.4039 0.4620 0.0139  -0.0373 -0.0574 277 PHE   B CD2 
2381 C CE1 . PHE   B 71  ? 0.5045 0.4448 0.4869 0.0169  -0.0280 -0.0555 277 PHE   B CE1 
2382 C CE2 . PHE   B 71  ? 0.4767 0.4040 0.4620 0.0193  -0.0360 -0.0621 277 PHE   B CE2 
2383 C CZ  . PHE   B 71  ? 0.5341 0.4698 0.5195 0.0206  -0.0312 -0.0611 277 PHE   B CZ  
2384 N N   . GLY   B 72  ? 0.4948 0.3993 0.4727 -0.0013 -0.0476 -0.0418 278 GLY   B N   
2385 C CA  . GLY   B 72  ? 0.4626 0.3556 0.4426 -0.0006 -0.0542 -0.0416 278 GLY   B CA  
2386 C C   . GLY   B 72  ? 0.5556 0.4449 0.5343 -0.0035 -0.0564 -0.0352 278 GLY   B C   
2387 O O   . GLY   B 72  ? 0.6313 0.5137 0.6125 -0.0006 -0.0610 -0.0354 278 GLY   B O   
2388 N N   . LYS   B 73  ? 0.5434 0.4375 0.5182 -0.0091 -0.0534 -0.0299 279 LYS   B N   
2389 C CA  . LYS   B 73  ? 0.5075 0.3992 0.4802 -0.0122 -0.0551 -0.0240 279 LYS   B CA  
2390 C C   . LYS   B 73  ? 0.5062 0.4041 0.4805 -0.0076 -0.0522 -0.0249 279 LYS   B C   
2391 O O   . LYS   B 73  ? 0.6581 0.5516 0.6323 -0.0075 -0.0555 -0.0219 279 LYS   B O   
2392 C CB  . LYS   B 73  ? 0.6028 0.4983 0.5708 -0.0199 -0.0526 -0.0185 279 LYS   B CB  
2393 C CG  . LYS   B 73  ? 0.7107 0.6005 0.6774 -0.0253 -0.0556 -0.0172 279 LYS   B CG  
2394 C CD  . LYS   B 73  ? 0.8953 0.7873 0.8575 -0.0338 -0.0545 -0.0110 279 LYS   B CD  
2395 C CE  . LYS   B 73  ? 0.8645 0.7594 0.8265 -0.0385 -0.0529 -0.0115 279 LYS   B CE  
2396 N NZ  . LYS   B 73  ? 0.9559 0.8491 0.9138 -0.0477 -0.0540 -0.0054 279 LYS   B NZ  
2397 N N   . GLY   B 74  ? 0.5190 0.4268 0.4949 -0.0040 -0.0465 -0.0288 280 GLY   B N   
2398 C CA  . GLY   B 74  ? 0.4862 0.3999 0.4642 0.0003  -0.0437 -0.0301 280 GLY   B CA  
2399 C C   . GLY   B 74  ? 0.4968 0.4162 0.4719 -0.0032 -0.0407 -0.0253 280 GLY   B C   
2400 O O   . GLY   B 74  ? 0.4932 0.4137 0.4647 -0.0090 -0.0398 -0.0214 280 GLY   B O   
2401 N N   . PRO   B 75  ? 0.4942 0.4182 0.4714 0.0002  -0.0389 -0.0259 281 PRO   B N   
2402 C CA  . PRO   B 75  ? 0.4566 0.3813 0.4388 0.0069  -0.0393 -0.0307 281 PRO   B CA  
2403 C C   . PRO   B 75  ? 0.4917 0.4235 0.4756 0.0101  -0.0346 -0.0359 281 PRO   B C   
2404 O O   . PRO   B 75  ? 0.4861 0.4254 0.4681 0.0084  -0.0297 -0.0353 281 PRO   B O   
2405 C CB  . PRO   B 75  ? 0.4662 0.3954 0.4491 0.0076  -0.0379 -0.0286 281 PRO   B CB  
2406 C CG  . PRO   B 75  ? 0.4268 0.3617 0.4053 0.0025  -0.0340 -0.0247 281 PRO   B CG  
2407 C CD  . PRO   B 75  ? 0.4271 0.3565 0.4018 -0.0028 -0.0363 -0.0220 281 PRO   B CD  
2408 N N   . GLN   B 76  ? 0.4337 0.3634 0.4213 0.0148  -0.0361 -0.0412 282 GLN   B N   
2409 C CA  . GLN   B 76  ? 0.4591 0.3951 0.4470 0.0170  -0.0319 -0.0460 282 GLN   B CA  
2410 C C   . GLN   B 76  ? 0.4670 0.4130 0.4557 0.0188  -0.0263 -0.0468 282 GLN   B C   
2411 O O   . GLN   B 76  ? 0.4763 0.4285 0.4635 0.0190  -0.0222 -0.0488 282 GLN   B O   
2412 C CB  . GLN   B 76  ? 0.5150 0.4469 0.5067 0.0215  -0.0349 -0.0521 282 GLN   B CB  
2413 C CG  . GLN   B 76  ? 0.5780 0.4992 0.5689 0.0195  -0.0408 -0.0513 282 GLN   B CG  
2414 C CD  . GLN   B 76  ? 0.6656 0.5824 0.6603 0.0239  -0.0439 -0.0581 282 GLN   B CD  
2415 O OE1 . GLN   B 76  ? 0.6828 0.6046 0.6815 0.0290  -0.0420 -0.0637 282 GLN   B OE1 
2416 N NE2 . GLN   B 76  ? 0.7726 0.6801 0.7666 0.0219  -0.0489 -0.0579 282 GLN   B NE2 
2417 N N   . ASN   B 77  ? 0.4297 0.3774 0.4205 0.0197  -0.0263 -0.0449 283 ASN   B N   
2418 C CA  . ASN   B 77  ? 0.4452 0.4022 0.4370 0.0210  -0.0212 -0.0455 283 ASN   B CA  
2419 C C   . ASN   B 77  ? 0.4453 0.4071 0.4333 0.0170  -0.0175 -0.0416 283 ASN   B C   
2420 O O   . ASN   B 77  ? 0.4024 0.3713 0.3909 0.0176  -0.0134 -0.0418 283 ASN   B O   
2421 C CB  . ASN   B 77  ? 0.4853 0.4431 0.4814 0.0235  -0.0225 -0.0455 283 ASN   B CB  
2422 C CG  . ASN   B 77  ? 0.5778 0.5322 0.5719 0.0202  -0.0249 -0.0398 283 ASN   B CG  
2423 O OD1 . ASN   B 77  ? 0.5828 0.5332 0.5726 0.0159  -0.0264 -0.0361 283 ASN   B OD1 
2424 N ND2 . ASN   B 77  ? 0.6831 0.6401 0.6801 0.0217  -0.0251 -0.0392 283 ASN   B ND2 
2425 N N   . ALA   B 78  ? 0.3720 0.3301 0.3565 0.0128  -0.0191 -0.0383 284 ALA   B N   
2426 C CA  . ALA   B 78  ? 0.4046 0.3674 0.3864 0.0091  -0.0159 -0.0352 284 ALA   B CA  
2427 C C   . ALA   B 78  ? 0.3962 0.3618 0.3762 0.0083  -0.0138 -0.0368 284 ALA   B C   
2428 O O   . ALA   B 78  ? 0.3621 0.3315 0.3406 0.0055  -0.0116 -0.0348 284 ALA   B O   
2429 C CB  . ALA   B 78  ? 0.3927 0.3513 0.3719 0.0045  -0.0185 -0.0309 284 ALA   B CB  
2430 N N   . PHE   B 79  ? 0.3374 0.3013 0.3177 0.0108  -0.0144 -0.0407 285 PHE   B N   
2431 C CA  . PHE   B 79  ? 0.3655 0.3309 0.3436 0.0099  -0.0134 -0.0422 285 PHE   B CA  
2432 C C   . PHE   B 79  ? 0.3606 0.3324 0.3383 0.0124  -0.0098 -0.0448 285 PHE   B C   
2433 O O   . PHE   B 79  ? 0.3478 0.3206 0.3270 0.0157  -0.0092 -0.0482 285 PHE   B O   
2434 C CB  . PHE   B 79  ? 0.3499 0.3083 0.3275 0.0100  -0.0173 -0.0445 285 PHE   B CB  
2435 C CG  . PHE   B 79  ? 0.3766 0.3289 0.3533 0.0059  -0.0208 -0.0410 285 PHE   B CG  
2436 C CD1 . PHE   B 79  ? 0.3510 0.2985 0.3286 0.0051  -0.0236 -0.0383 285 PHE   B CD1 
2437 C CD2 . PHE   B 79  ? 0.3697 0.3216 0.3445 0.0023  -0.0213 -0.0402 285 PHE   B CD2 
2438 C CE1 . PHE   B 79  ? 0.3995 0.3419 0.3754 0.0004  -0.0265 -0.0345 285 PHE   B CE1 
2439 C CE2 . PHE   B 79  ? 0.3663 0.3136 0.3402 -0.0022 -0.0240 -0.0369 285 PHE   B CE2 
2440 C CZ  . PHE   B 79  ? 0.3696 0.3120 0.3436 -0.0034 -0.0265 -0.0338 285 PHE   B CZ  
2441 N N   . PHE   B 80  ? 0.3069 0.2831 0.2826 0.0106  -0.0075 -0.0434 286 PHE   B N   
2442 C CA  . PHE   B 80  ? 0.3095 0.2913 0.2840 0.0120  -0.0043 -0.0448 286 PHE   B CA  
2443 C C   . PHE   B 80  ? 0.3373 0.3201 0.3088 0.0105  -0.0045 -0.0450 286 PHE   B C   
2444 O O   . PHE   B 80  ? 0.3439 0.3252 0.3152 0.0078  -0.0060 -0.0432 286 PHE   B O   
2445 C CB  . PHE   B 80  ? 0.2857 0.2724 0.2616 0.0117  -0.0016 -0.0421 286 PHE   B CB  
2446 C CG  . PHE   B 80  ? 0.2947 0.2811 0.2737 0.0131  -0.0015 -0.0418 286 PHE   B CG  
2447 C CD1 . PHE   B 80  ? 0.2995 0.2828 0.2797 0.0115  -0.0035 -0.0393 286 PHE   B CD1 
2448 C CD2 . PHE   B 80  ? 0.3016 0.2914 0.2823 0.0157  0.0005  -0.0439 286 PHE   B CD2 
2449 C CE1 . PHE   B 80  ? 0.3497 0.3325 0.3326 0.0128  -0.0040 -0.0389 286 PHE   B CE1 
2450 C CE2 . PHE   B 80  ? 0.3892 0.3791 0.3734 0.0172  0.0002  -0.0439 286 PHE   B CE2 
2451 C CZ  . PHE   B 80  ? 0.3434 0.3294 0.3286 0.0159  -0.0023 -0.0413 286 PHE   B CZ  
2452 N N   . LEU   B 81  ? 0.3255 0.3112 0.2945 0.0119  -0.0029 -0.0474 287 LEU   B N   
2453 C CA  . LEU   B 81  ? 0.2962 0.2839 0.2618 0.0106  -0.0029 -0.0472 287 LEU   B CA  
2454 C C   . LEU   B 81  ? 0.3264 0.3192 0.2913 0.0105  -0.0001 -0.0449 287 LEU   B C   
2455 O O   . LEU   B 81  ? 0.3154 0.3109 0.2802 0.0120  0.0023  -0.0458 287 LEU   B O   
2456 C CB  . LEU   B 81  ? 0.3323 0.3193 0.2943 0.0120  -0.0035 -0.0514 287 LEU   B CB  
2457 C CG  . LEU   B 81  ? 0.3838 0.3732 0.3411 0.0109  -0.0035 -0.0516 287 LEU   B CG  
2458 C CD1 . LEU   B 81  ? 0.3398 0.3265 0.2974 0.0087  -0.0065 -0.0504 287 LEU   B CD1 
2459 C CD2 . LEU   B 81  ? 0.5127 0.5027 0.4663 0.0126  -0.0031 -0.0564 287 LEU   B CD2 
2460 N N   . VAL   B 82  ? 0.2705 0.2646 0.2354 0.0086  -0.0006 -0.0421 288 VAL   B N   
2461 C CA  . VAL   B 82  ? 0.3318 0.3297 0.2965 0.0084  0.0013  -0.0397 288 VAL   B CA  
2462 C C   . VAL   B 82  ? 0.3252 0.3240 0.2865 0.0074  -0.0001 -0.0391 288 VAL   B C   
2463 O O   . VAL   B 82  ? 0.3094 0.3070 0.2716 0.0062  -0.0024 -0.0388 288 VAL   B O   
2464 C CB  . VAL   B 82  ? 0.3539 0.3527 0.3231 0.0075  0.0016  -0.0370 288 VAL   B CB  
2465 C CG1 . VAL   B 82  ? 0.3392 0.3412 0.3087 0.0075  0.0032  -0.0348 288 VAL   B CG1 
2466 C CG2 . VAL   B 82  ? 0.3226 0.3201 0.2945 0.0082  0.0022  -0.0374 288 VAL   B CG2 
2467 N N   . LYS   B 83  ? 0.3107 0.3116 0.2680 0.0076  0.0012  -0.0390 289 LYS   B N   
2468 C CA  . LYS   B 83  ? 0.3092 0.3106 0.2624 0.0065  -0.0005 -0.0377 289 LYS   B CA  
2469 C C   . LYS   B 83  ? 0.3495 0.3524 0.3048 0.0058  -0.0004 -0.0340 289 LYS   B C   
2470 O O   . LYS   B 83  ? 0.2930 0.2974 0.2491 0.0060  0.0020  -0.0327 289 LYS   B O   
2471 C CB  . LYS   B 83  ? 0.3322 0.3351 0.2787 0.0066  0.0007  -0.0394 289 LYS   B CB  
2472 C CG  . LYS   B 83  ? 0.4034 0.4064 0.3446 0.0051  -0.0016 -0.0377 289 LYS   B CG  
2473 C CD  . LYS   B 83  ? 0.5099 0.5144 0.4435 0.0048  -0.0007 -0.0403 289 LYS   B CD  
2474 C CE  . LYS   B 83  ? 0.5785 0.5827 0.5059 0.0031  -0.0036 -0.0383 289 LYS   B CE  
2475 N NZ  . LYS   B 83  ? 0.6146 0.6200 0.5343 0.0026  -0.0034 -0.0418 289 LYS   B NZ  
2476 N N   . PHE   B 84  ? 0.2913 0.2936 0.2480 0.0051  -0.0033 -0.0325 290 PHE   B N   
2477 C CA  . PHE   B 84  ? 0.3065 0.3097 0.2660 0.0047  -0.0042 -0.0294 290 PHE   B CA  
2478 C C   . PHE   B 84  ? 0.3513 0.3539 0.3058 0.0039  -0.0069 -0.0276 290 PHE   B C   
2479 O O   . PHE   B 84  ? 0.3300 0.3317 0.2819 0.0036  -0.0094 -0.0289 290 PHE   B O   
2480 C CB  . PHE   B 84  ? 0.2677 0.2713 0.2340 0.0047  -0.0059 -0.0296 290 PHE   B CB  
2481 C CG  . PHE   B 84  ? 0.3176 0.3219 0.2886 0.0049  -0.0035 -0.0305 290 PHE   B CG  
2482 C CD1 . PHE   B 84  ? 0.2961 0.2993 0.2672 0.0046  -0.0033 -0.0326 290 PHE   B CD1 
2483 C CD2 . PHE   B 84  ? 0.3045 0.3102 0.2794 0.0052  -0.0021 -0.0291 290 PHE   B CD2 
2484 C CE1 . PHE   B 84  ? 0.3089 0.3122 0.2834 0.0045  -0.0017 -0.0329 290 PHE   B CE1 
2485 C CE2 . PHE   B 84  ? 0.2762 0.2826 0.2545 0.0052  -0.0002 -0.0299 290 PHE   B CE2 
2486 C CZ  . PHE   B 84  ? 0.3144 0.3195 0.2922 0.0048  -0.0001 -0.0316 290 PHE   B CZ  
2487 N N   . TRP   B 85  ? 0.3039 0.3065 0.2571 0.0033  -0.0068 -0.0245 291 TRP   B N   
2488 C CA  . TRP   B 85  ? 0.3577 0.3589 0.3070 0.0022  -0.0103 -0.0217 291 TRP   B CA  
2489 C C   . TRP   B 85  ? 0.3226 0.3232 0.2792 0.0029  -0.0133 -0.0201 291 TRP   B C   
2490 O O   . TRP   B 85  ? 0.3500 0.3509 0.3114 0.0034  -0.0119 -0.0192 291 TRP   B O   
2491 C CB  . TRP   B 85  ? 0.3348 0.3361 0.2779 0.0006  -0.0087 -0.0188 291 TRP   B CB  
2492 C CG  . TRP   B 85  ? 0.4051 0.4079 0.3402 -0.0002 -0.0064 -0.0207 291 TRP   B CG  
2493 C CD1 . TRP   B 85  ? 0.4067 0.4091 0.3334 -0.0017 -0.0083 -0.0203 291 TRP   B CD1 
2494 C CD2 . TRP   B 85  ? 0.3311 0.3364 0.2661 0.0005  -0.0020 -0.0241 291 TRP   B CD2 
2495 N NE1 . TRP   B 85  ? 0.3970 0.4019 0.3184 -0.0020 -0.0049 -0.0235 291 TRP   B NE1 
2496 C CE2 . TRP   B 85  ? 0.4045 0.4112 0.3314 -0.0005 -0.0011 -0.0260 291 TRP   B CE2 
2497 C CE3 . TRP   B 85  ? 0.3633 0.3697 0.3044 0.0019  0.0010  -0.0259 291 TRP   B CE3 
2498 C CZ2 . TRP   B 85  ? 0.4650 0.4744 0.3906 0.0003  0.0027  -0.0301 291 TRP   B CZ2 
2499 C CZ3 . TRP   B 85  ? 0.4261 0.4347 0.3658 0.0027  0.0043  -0.0294 291 TRP   B CZ3 
2500 C CH2 . TRP   B 85  ? 0.4432 0.4534 0.3758 0.0020  0.0052  -0.0317 291 TRP   B CH2 
2501 N N   . ALA   B 86  ? 0.3170 0.3170 0.2750 0.0032  -0.0175 -0.0205 292 ALA   B N   
2502 C CA  . ALA   B 86  ? 0.3016 0.3019 0.2678 0.0043  -0.0207 -0.0202 292 ALA   B CA  
2503 C C   . ALA   B 86  ? 0.3202 0.3178 0.2851 0.0040  -0.0248 -0.0164 292 ALA   B C   
2504 O O   . ALA   B 86  ? 0.3623 0.3577 0.3197 0.0028  -0.0273 -0.0143 292 ALA   B O   
2505 C CB  . ALA   B 86  ? 0.3096 0.3113 0.2793 0.0047  -0.0233 -0.0230 292 ALA   B CB  
2506 N N   . ASP   B 87  ? 0.3437 0.3409 0.3156 0.0050  -0.0258 -0.0155 293 ASP   B N   
2507 C CA  . ASP   B 87  ? 0.3352 0.3288 0.3072 0.0049  -0.0305 -0.0117 293 ASP   B CA  
2508 C C   . ASP   B 87  ? 0.3699 0.3642 0.3498 0.0068  -0.0357 -0.0135 293 ASP   B C   
2509 O O   . ASP   B 87  ? 0.3488 0.3459 0.3385 0.0085  -0.0353 -0.0164 293 ASP   B O   
2510 C CB  . ASP   B 87  ? 0.3501 0.3426 0.3257 0.0049  -0.0288 -0.0100 293 ASP   B CB  
2511 C CG  . ASP   B 87  ? 0.4260 0.4135 0.4014 0.0045  -0.0340 -0.0056 293 ASP   B CG  
2512 O OD1 . ASP   B 87  ? 0.4152 0.4005 0.3905 0.0050  -0.0397 -0.0045 293 ASP   B OD1 
2513 O OD2 . ASP   B 87  ? 0.4252 0.4107 0.4005 0.0035  -0.0328 -0.0031 293 ASP   B OD2 
2514 N N   . LEU   B 88  ? 0.3570 0.3492 0.3328 0.0064  -0.0406 -0.0119 294 LEU   B N   
2515 C CA  . LEU   B 88  ? 0.4185 0.4118 0.4020 0.0083  -0.0461 -0.0138 294 LEU   B CA  
2516 C C   . LEU   B 88  ? 0.4575 0.4461 0.4434 0.0092  -0.0527 -0.0103 294 LEU   B C   
2517 O O   . LEU   B 88  ? 0.4839 0.4727 0.4757 0.0109  -0.0584 -0.0114 294 LEU   B O   
2518 C CB  . LEU   B 88  ? 0.3921 0.3864 0.3708 0.0076  -0.0480 -0.0150 294 LEU   B CB  
2519 C CG  . LEU   B 88  ? 0.4701 0.4679 0.4464 0.0067  -0.0426 -0.0185 294 LEU   B CG  
2520 C CD1 . LEU   B 88  ? 0.4571 0.4548 0.4277 0.0058  -0.0453 -0.0194 294 LEU   B CD1 
2521 C CD2 . LEU   B 88  ? 0.4404 0.4430 0.4276 0.0079  -0.0403 -0.0228 294 LEU   B CD2 
2522 N N   . ASN   B 89  ? 0.4655 0.4497 0.4473 0.0079  -0.0524 -0.0060 295 ASN   B N   
2523 C CA  . ASN   B 89  ? 0.4520 0.4305 0.4354 0.0083  -0.0590 -0.0019 295 ASN   B CA  
2524 C C   . ASN   B 89  ? 0.4998 0.4793 0.4969 0.0113  -0.0603 -0.0048 295 ASN   B C   
2525 O O   . ASN   B 89  ? 0.5752 0.5531 0.5746 0.0112  -0.0582 -0.0038 295 ASN   B O   
2526 C CB  . ASN   B 89  ? 0.5392 0.5128 0.5126 0.0051  -0.0578 0.0039  295 ASN   B CB  
2527 C CG  . ASN   B 89  ? 0.6385 0.6120 0.5982 0.0019  -0.0560 0.0062  295 ASN   B CG  
2528 O OD1 . ASN   B 89  ? 0.8138 0.7871 0.7697 0.0019  -0.0599 0.0062  295 ASN   B OD1 
2529 N ND2 . ASN   B 89  ? 0.7312 0.7054 0.6835 -0.0007 -0.0501 0.0077  295 ASN   B ND2 
2530 N N   . CYS   B 90  ? 0.5082 0.4911 0.5150 0.0141  -0.0637 -0.0090 296 CYS   B N   
2531 C CA  A CYS   B 90  ? 0.5070 0.4924 0.5277 0.0172  -0.0648 -0.0130 296 CYS   B CA  
2532 C CA  B CYS   B 90  ? 0.5071 0.4927 0.5278 0.0172  -0.0646 -0.0132 296 CYS   B CA  
2533 C C   . CYS   B 90  ? 0.5233 0.5092 0.5529 0.0200  -0.0724 -0.0151 296 CYS   B C   
2534 O O   . CYS   B 90  ? 0.5295 0.5181 0.5577 0.0199  -0.0740 -0.0164 296 CYS   B O   
2535 C CB  A CYS   B 90  ? 0.4995 0.4925 0.5252 0.0175  -0.0574 -0.0185 296 CYS   B CB  
2536 C CB  B CYS   B 90  ? 0.4984 0.4919 0.5239 0.0175  -0.0573 -0.0188 296 CYS   B CB  
2537 S SG  A CYS   B 90  ? 0.4958 0.4964 0.5238 0.0176  -0.0558 -0.0235 296 CYS   B SG  
2538 S SG  B CYS   B 90  ? 0.4960 0.4960 0.5386 0.0209  -0.0576 -0.0258 296 CYS   B SG  
2539 N N   . ASN   B 91  ? 0.5847 0.5677 0.6237 0.0226  -0.0776 -0.0154 297 ASN   B N   
2540 C CA  . ASN   B 91  ? 0.5984 0.5820 0.6478 0.0260  -0.0854 -0.0180 297 ASN   B CA  
2541 C C   . ASN   B 91  ? 0.6233 0.6170 0.6863 0.0286  -0.0822 -0.0264 297 ASN   B C   
2542 O O   . ASN   B 91  ? 0.7131 0.7091 0.7844 0.0301  -0.0798 -0.0298 297 ASN   B O   
2543 C CB  . ASN   B 91  ? 0.6229 0.5983 0.6769 0.0278  -0.0933 -0.0148 297 ASN   B CB  
2544 C CG  . ASN   B 91  ? 0.7444 0.7209 0.8117 0.0321  -0.1017 -0.0185 297 ASN   B CG  
2545 O OD1 . ASN   B 91  ? 0.7414 0.7226 0.8105 0.0327  -0.1035 -0.0209 297 ASN   B OD1 
2546 N ND2 . ASN   B 91  ? 0.8844 0.8568 0.9618 0.0350  -0.1071 -0.0193 297 ASN   B ND2 
2547 N N   . ILE   B 92  ? 0.6118 0.6117 0.6768 0.0286  -0.0821 -0.0297 298 ILE   B N   
2548 C CA  . ILE   B 92  ? 0.6427 0.6532 0.7201 0.0303  -0.0790 -0.0376 298 ILE   B CA  
2549 C C   . ILE   B 92  ? 0.7819 0.7938 0.8740 0.0346  -0.0869 -0.0413 298 ILE   B C   
2550 O O   . ILE   B 92  ? 0.7888 0.8009 0.8831 0.0357  -0.0930 -0.0414 298 ILE   B O   
2551 C CB  . ILE   B 92  ? 0.5998 0.6163 0.6732 0.0280  -0.0753 -0.0394 298 ILE   B CB  
2552 C CG1 . ILE   B 92  ? 0.5751 0.5917 0.6377 0.0245  -0.0666 -0.0376 298 ILE   B CG1 
2553 C CG2 . ILE   B 92  ? 0.7226 0.7498 0.8101 0.0297  -0.0748 -0.0471 298 ILE   B CG2 
2554 C CD1 . ILE   B 92  ? 0.6489 0.6679 0.7040 0.0218  -0.0638 -0.0376 298 ILE   B CD1 
2555 N N   . GLN   B 93  ? 0.7094 0.7227 0.8121 0.0373  -0.0871 -0.0450 299 GLN   B N   
2556 C CA  . GLN   B 93  ? 0.8055 0.8188 0.9229 0.0419  -0.0950 -0.0487 299 GLN   B CA  
2557 C C   . GLN   B 93  ? 0.8538 0.8796 0.9853 0.0441  -0.0946 -0.0574 299 GLN   B C   
2558 O O   . GLN   B 93  ? 0.8111 0.8461 0.9424 0.0418  -0.0870 -0.0612 299 GLN   B O   
2559 C CB  . GLN   B 93  ? 0.8552 0.8654 0.9787 0.0439  -0.0948 -0.0500 299 GLN   B CB  
2560 C CG  . GLN   B 93  ? 0.8825 0.8812 0.9931 0.0413  -0.0945 -0.0418 299 GLN   B CG  
2561 C CD  . GLN   B 93  ? 0.9578 0.9562 1.0731 0.0420  -0.0909 -0.0441 299 GLN   B CD  
2562 O OE1 . GLN   B 93  ? 1.0211 1.0247 1.1506 0.0456  -0.0919 -0.0512 299 GLN   B OE1 
2563 N NE2 . GLN   B 93  ? 0.8686 0.8611 0.9719 0.0387  -0.0867 -0.0384 299 GLN   B NE2 
2564 N N   . ASP   B 94  ? 0.8948 0.9209 1.0393 0.0484  -0.1031 -0.0606 300 ASP   B N   
2565 C CA  . ASP   B 94  ? 0.9150 0.9536 1.0754 0.0510  -0.1036 -0.0696 300 ASP   B CA  
2566 C C   . ASP   B 94  ? 0.9251 0.9703 1.0995 0.0540  -0.1011 -0.0774 300 ASP   B C   
2567 O O   . ASP   B 94  ? 0.9189 0.9569 1.0975 0.0569  -0.1058 -0.0766 300 ASP   B O   
2568 C CB  . ASP   B 94  ? 0.8219 0.8582 0.9902 0.0545  -0.1147 -0.0697 300 ASP   B CB  
2569 C CG  . ASP   B 94  ? 0.8662 0.8960 1.0203 0.0516  -0.1177 -0.0623 300 ASP   B CG  
2570 O OD1 . ASP   B 94  ? 0.8652 0.8961 1.0066 0.0470  -0.1104 -0.0595 300 ASP   B OD1 
2571 O OD2 . ASP   B 94  ? 0.8762 0.8997 1.0320 0.0538  -0.1277 -0.0594 300 ASP   B OD2 
2572 N N   . ASP   B 95  ? 0.9540 1.0130 1.1355 0.0530  -0.0938 -0.0849 301 ASP   B N   
2573 C CA  . ASP   B 95  ? 0.9776 1.0454 1.1720 0.0552  -0.0902 -0.0934 301 ASP   B CA  
2574 C C   . ASP   B 95  ? 0.9749 1.0347 1.1624 0.0547  -0.0872 -0.0901 301 ASP   B C   
2575 O O   . ASP   B 95  ? 0.9286 0.9823 1.1229 0.0584  -0.0927 -0.0909 301 ASP   B O   
2576 C CB  . ASP   B 95  ? 0.8802 0.9519 1.0940 0.0613  -0.0985 -0.1006 301 ASP   B CB  
2577 C CG  . ASP   B 95  ? 0.9274 1.0097 1.1504 0.0619  -0.1004 -0.1056 301 ASP   B CG  
2578 O OD1 . ASP   B 95  ? 0.9329 1.0160 1.1455 0.0577  -0.0976 -0.1014 301 ASP   B OD1 
2579 O OD2 . ASP   B 95  ? 0.9352 1.0253 1.1764 0.0665  -0.1049 -0.1139 301 ASP   B OD2 
2580 N N   . ALA   B 96  ? 0.8843 0.9441 1.0583 0.0498  -0.0787 -0.0865 302 ALA   B N   
2581 C CA  . ALA   B 96  ? 0.8663 0.9193 1.0330 0.0487  -0.0754 -0.0831 302 ALA   B CA  
2582 C C   . ALA   B 96  ? 0.8184 0.8799 0.9817 0.0454  -0.0651 -0.0864 302 ALA   B C   
2583 O O   . ALA   B 96  ? 0.6722 0.7280 0.8254 0.0431  -0.0611 -0.0820 302 ALA   B O   
2584 C CB  . ALA   B 96  ? 0.7659 0.8053 0.9161 0.0462  -0.0772 -0.0724 302 ALA   B CB  
2585 N N   . GLY   B 97  ? 0.5981 0.6731 0.7694 0.0447  -0.0608 -0.0938 303 GLY   B N   
2586 C CA  . GLY   B 97  ? 0.5702 0.6535 0.7376 0.0409  -0.0514 -0.0966 303 GLY   B CA  
2587 C C   . GLY   B 97  ? 0.5093 0.5863 0.6593 0.0362  -0.0464 -0.0887 303 GLY   B C   
2588 O O   . GLY   B 97  ? 0.6198 0.6981 0.7644 0.0338  -0.0403 -0.0887 303 GLY   B O   
2589 N N   . ALA   B 98  ? 0.3839 0.4543 0.5253 0.0349  -0.0492 -0.0824 304 ALA   B N   
2590 C CA  . ALA   B 98  ? 0.4237 0.4872 0.5490 0.0311  -0.0455 -0.0750 304 ALA   B CA  
2591 C C   . ALA   B 98  ? 0.3782 0.4491 0.4987 0.0268  -0.0372 -0.0767 304 ALA   B C   
2592 O O   . ALA   B 98  ? 0.3405 0.4215 0.4668 0.0254  -0.0347 -0.0816 304 ALA   B O   
2593 C CB  . ALA   B 98  ? 0.3205 0.3787 0.4393 0.0304  -0.0497 -0.0700 304 ALA   B CB  
2594 N N   . PHE   B 99  ? 0.2892 0.3549 0.3992 0.0246  -0.0330 -0.0724 305 PHE   B N   
2595 C CA  . PHE   B 99  ? 0.2871 0.3573 0.3903 0.0204  -0.0260 -0.0724 305 PHE   B CA  
2596 C C   . PHE   B 99  ? 0.3008 0.3621 0.3900 0.0181  -0.0251 -0.0650 305 PHE   B C   
2597 O O   . PHE   B 99  ? 0.2731 0.3260 0.3562 0.0189  -0.0262 -0.0606 305 PHE   B O   
2598 C CB  . PHE   B 99  ? 0.2813 0.3549 0.3861 0.0200  -0.0216 -0.0754 305 PHE   B CB  
2599 C CG  . PHE   B 99  ? 0.3588 0.4360 0.4559 0.0155  -0.0150 -0.0746 305 PHE   B CG  
2600 C CD1 . PHE   B 99  ? 0.3419 0.4291 0.4422 0.0126  -0.0116 -0.0787 305 PHE   B CD1 
2601 C CD2 . PHE   B 99  ? 0.2944 0.3646 0.3809 0.0140  -0.0126 -0.0695 305 PHE   B CD2 
2602 C CE1 . PHE   B 99  ? 0.3174 0.4070 0.4100 0.0080  -0.0062 -0.0773 305 PHE   B CE1 
2603 C CE2 . PHE   B 99  ? 0.3918 0.4644 0.4712 0.0100  -0.0074 -0.0685 305 PHE   B CE2 
2604 C CZ  . PHE   B 99  ? 0.2956 0.3775 0.3778 0.0069  -0.0044 -0.0722 305 PHE   B CZ  
2605 N N   . TYR   B 100 ? 0.2428 0.3062 0.3273 0.0152  -0.0233 -0.0642 306 TYR   B N   
2606 C CA  . TYR   B 100 ? 0.2716 0.3281 0.3437 0.0129  -0.0220 -0.0584 306 TYR   B CA  
2607 C C   . TYR   B 100 ? 0.3097 0.3686 0.3767 0.0096  -0.0158 -0.0585 306 TYR   B C   
2608 O O   . TYR   B 100 ? 0.2937 0.3604 0.3640 0.0071  -0.0129 -0.0619 306 TYR   B O   
2609 C CB  . TYR   B 100 ? 0.2345 0.2915 0.3049 0.0116  -0.0242 -0.0578 306 TYR   B CB  
2610 C CG  . TYR   B 100 ? 0.2835 0.3371 0.3570 0.0145  -0.0308 -0.0569 306 TYR   B CG  
2611 C CD1 . TYR   B 100 ? 0.2938 0.3532 0.3795 0.0170  -0.0345 -0.0616 306 TYR   B CD1 
2612 C CD2 . TYR   B 100 ? 0.3243 0.3690 0.3883 0.0147  -0.0337 -0.0515 306 TYR   B CD2 
2613 C CE1 . TYR   B 100 ? 0.2831 0.3389 0.3718 0.0197  -0.0414 -0.0605 306 TYR   B CE1 
2614 C CE2 . TYR   B 100 ? 0.3803 0.4216 0.4462 0.0170  -0.0403 -0.0502 306 TYR   B CE2 
2615 C CZ  . TYR   B 100 ? 0.3935 0.4400 0.4718 0.0196  -0.0444 -0.0545 306 TYR   B CZ  
2616 O OH  . TYR   B 100 ? 0.4843 0.5269 0.5646 0.0219  -0.0516 -0.0530 306 TYR   B OH  
2617 N N   . GLY   B 101 ? 0.2622 0.3150 0.3215 0.0094  -0.0139 -0.0547 307 GLY   B N   
2618 C CA  . GLY   B 101 ? 0.2604 0.3150 0.3153 0.0066  -0.0088 -0.0547 307 GLY   B CA  
2619 C C   . GLY   B 101 ? 0.3202 0.3674 0.3641 0.0054  -0.0074 -0.0496 307 GLY   B C   
2620 O O   . GLY   B 101 ? 0.2783 0.3191 0.3176 0.0067  -0.0099 -0.0463 307 GLY   B O   
2621 N N   . VAL   B 102 ? 0.2451 0.2938 0.2851 0.0026  -0.0036 -0.0494 308 VAL   B N   
2622 C CA  A VAL   B 102 ? 0.3248 0.3674 0.3556 0.0016  -0.0020 -0.0455 308 VAL   B CA  
2623 C CA  B VAL   B 102 ? 0.3072 0.3496 0.3381 0.0017  -0.0021 -0.0455 308 VAL   B CA  
2624 C C   . VAL   B 102 ? 0.3251 0.3689 0.3549 0.0007  0.0011  -0.0458 308 VAL   B C   
2625 O O   . VAL   B 102 ? 0.3445 0.3946 0.3776 -0.0012 0.0032  -0.0486 308 VAL   B O   
2626 C CB  A VAL   B 102 ? 0.3166 0.3584 0.3427 -0.0012 -0.0015 -0.0445 308 VAL   B CB  
2627 C CB  B VAL   B 102 ? 0.3164 0.3572 0.3419 -0.0009 -0.0017 -0.0441 308 VAL   B CB  
2628 C CG1 A VAL   B 102 ? 0.3015 0.3366 0.3192 -0.0015 -0.0006 -0.0410 308 VAL   B CG1 
2629 C CG1 B VAL   B 102 ? 0.3141 0.3514 0.3381 0.0004  -0.0052 -0.0429 308 VAL   B CG1 
2630 C CG2 A VAL   B 102 ? 0.3081 0.3502 0.3362 -0.0008 -0.0046 -0.0452 308 VAL   B CG2 
2631 C CG2 B VAL   B 102 ? 0.3190 0.3666 0.3480 -0.0041 -0.0001 -0.0469 308 VAL   B CG2 
2632 N N   . THR   B 103 ? 0.2820 0.3205 0.3073 0.0019  0.0015  -0.0430 309 THR   B N   
2633 C CA  . THR   B 103 ? 0.2896 0.3287 0.3135 0.0012  0.0040  -0.0430 309 THR   B CA  
2634 C C   . THR   B 103 ? 0.3729 0.4067 0.3892 0.0004  0.0049  -0.0396 309 THR   B C   
2635 O O   . THR   B 103 ? 0.3156 0.3446 0.3285 0.0017  0.0037  -0.0373 309 THR   B O   
2636 C CB  . THR   B 103 ? 0.3425 0.3811 0.3705 0.0036  0.0033  -0.0436 309 THR   B CB  
2637 O OG1 . THR   B 103 ? 0.3919 0.4363 0.4279 0.0043  0.0026  -0.0478 309 THR   B OG1 
2638 C CG2 . THR   B 103 ? 0.3880 0.4261 0.4136 0.0030  0.0055  -0.0430 309 THR   B CG2 
2639 N N   . SER   B 104 ? 0.3083 0.3431 0.3219 -0.0017 0.0069  -0.0394 310 SER   B N   
2640 C CA  . SER   B 104 ? 0.3710 0.4007 0.3786 -0.0019 0.0073  -0.0366 310 SER   B CA  
2641 C C   . SER   B 104 ? 0.3863 0.4171 0.3927 -0.0030 0.0089  -0.0366 310 SER   B C   
2642 O O   . SER   B 104 ? 0.3470 0.3827 0.3556 -0.0048 0.0101  -0.0386 310 SER   B O   
2643 C CB  . SER   B 104 ? 0.3475 0.3746 0.3511 -0.0037 0.0066  -0.0355 310 SER   B CB  
2644 O OG  . SER   B 104 ? 0.4707 0.5018 0.4753 -0.0069 0.0072  -0.0368 310 SER   B OG  
2645 N N   . GLN   B 105 ? 0.3533 0.3799 0.3564 -0.0020 0.0089  -0.0345 311 GLN   B N   
2646 C CA  . GLN   B 105 ? 0.3726 0.3995 0.3741 -0.0029 0.0098  -0.0341 311 GLN   B CA  
2647 C C   . GLN   B 105 ? 0.3482 0.3700 0.3451 -0.0027 0.0090  -0.0318 311 GLN   B C   
2648 O O   . GLN   B 105 ? 0.3432 0.3618 0.3393 -0.0006 0.0084  -0.0310 311 GLN   B O   
2649 C CB  . GLN   B 105 ? 0.3383 0.3665 0.3430 -0.0011 0.0103  -0.0349 311 GLN   B CB  
2650 C CG  . GLN   B 105 ? 0.4051 0.4329 0.4079 -0.0016 0.0107  -0.0342 311 GLN   B CG  
2651 C CD  . GLN   B 105 ? 0.5424 0.5726 0.5490 -0.0005 0.0113  -0.0357 311 GLN   B CD  
2652 O OE1 . GLN   B 105 ? 0.5442 0.5781 0.5550 -0.0005 0.0116  -0.0382 311 GLN   B OE1 
2653 N NE2 . GLN   B 105 ? 0.4921 0.5206 0.4981 0.0004  0.0112  -0.0346 311 GLN   B NE2 
2654 N N   . TYR   B 106 ? 0.2893 0.3106 0.2833 -0.0050 0.0088  -0.0309 312 TYR   B N   
2655 C CA  . TYR   B 106 ? 0.2916 0.3077 0.2820 -0.0047 0.0074  -0.0290 312 TYR   B CA  
2656 C C   . TYR   B 106 ? 0.3791 0.3957 0.3690 -0.0048 0.0073  -0.0284 312 TYR   B C   
2657 O O   . TYR   B 106 ? 0.3259 0.3467 0.3166 -0.0064 0.0083  -0.0294 312 TYR   B O   
2658 C CB  . TYR   B 106 ? 0.3136 0.3272 0.3005 -0.0077 0.0060  -0.0277 312 TYR   B CB  
2659 C CG  . TYR   B 106 ? 0.3701 0.3835 0.3575 -0.0080 0.0058  -0.0284 312 TYR   B CG  
2660 C CD1 . TYR   B 106 ? 0.3660 0.3845 0.3557 -0.0100 0.0069  -0.0299 312 TYR   B CD1 
2661 C CD2 . TYR   B 106 ? 0.3807 0.3891 0.3666 -0.0065 0.0043  -0.0279 312 TYR   B CD2 
2662 C CE1 . TYR   B 106 ? 0.4479 0.4665 0.4385 -0.0104 0.0063  -0.0306 312 TYR   B CE1 
2663 C CE2 . TYR   B 106 ? 0.4114 0.4195 0.3974 -0.0069 0.0037  -0.0287 312 TYR   B CE2 
2664 C CZ  . TYR   B 106 ? 0.4143 0.4274 0.4027 -0.0090 0.0046  -0.0298 312 TYR   B CZ  
2665 O OH  . TYR   B 106 ? 0.5153 0.5283 0.5043 -0.0094 0.0038  -0.0306 312 TYR   B OH  
2666 N N   . GLU   B 107 ? 0.3085 0.3211 0.2972 -0.0032 0.0059  -0.0272 313 GLU   B N   
2667 C CA  . GLU   B 107 ? 0.3668 0.3792 0.3550 -0.0031 0.0050  -0.0265 313 GLU   B CA  
2668 C C   . GLU   B 107 ? 0.3442 0.3509 0.3291 -0.0034 0.0022  -0.0247 313 GLU   B C   
2669 O O   . GLU   B 107 ? 0.3578 0.3608 0.3424 -0.0021 0.0011  -0.0246 313 GLU   B O   
2670 C CB  . GLU   B 107 ? 0.3049 0.3186 0.2967 0.0000  0.0059  -0.0275 313 GLU   B CB  
2671 C CG  . GLU   B 107 ? 0.4433 0.4614 0.4384 0.0001  0.0080  -0.0291 313 GLU   B CG  
2672 C CD  . GLU   B 107 ? 0.4148 0.4336 0.4134 0.0026  0.0087  -0.0296 313 GLU   B CD  
2673 O OE1 . GLU   B 107 ? 0.4503 0.4672 0.4490 0.0042  0.0080  -0.0290 313 GLU   B OE1 
2674 O OE2 . GLU   B 107 ? 0.5867 0.6084 0.5883 0.0027  0.0098  -0.0307 313 GLU   B OE2 
2675 N N   . SER   B 108 ? 0.3471 0.3533 0.3298 -0.0051 0.0006  -0.0233 314 SER   B N   
2676 C CA  . SER   B 108 ? 0.3713 0.3714 0.3510 -0.0056 -0.0031 -0.0211 314 SER   B CA  
2677 C C   . SER   B 108 ? 0.3632 0.3635 0.3427 -0.0053 -0.0048 -0.0203 314 SER   B C   
2678 O O   . SER   B 108 ? 0.3426 0.3477 0.3225 -0.0063 -0.0032 -0.0211 314 SER   B O   
2679 C CB  . SER   B 108 ? 0.4077 0.4056 0.3825 -0.0101 -0.0043 -0.0189 314 SER   B CB  
2680 O OG  . SER   B 108 ? 0.5044 0.4952 0.4763 -0.0106 -0.0085 -0.0164 314 SER   B OG  
2681 N N   . SER   B 109 ? 0.3754 0.3701 0.3545 -0.0038 -0.0086 -0.0190 315 SER   B N   
2682 C CA  . SER   B 109 ? 0.3675 0.3612 0.3458 -0.0038 -0.0115 -0.0177 315 SER   B CA  
2683 C C   . SER   B 109 ? 0.4446 0.4358 0.4161 -0.0087 -0.0140 -0.0143 315 SER   B C   
2684 O O   . SER   B 109 ? 0.4028 0.3942 0.3722 -0.0098 -0.0162 -0.0130 315 SER   B O   
2685 C CB  . SER   B 109 ? 0.4475 0.4365 0.4292 0.0002  -0.0150 -0.0180 315 SER   B CB  
2686 O OG  . SER   B 109 ? 0.4822 0.4650 0.4623 0.0001  -0.0174 -0.0170 315 SER   B OG  
2687 N N   . GLU   B 110 ? 0.4097 0.3986 0.3774 -0.0121 -0.0139 -0.0128 316 GLU   B N   
2688 C CA  . GLU   B 110 ? 0.4745 0.4610 0.4351 -0.0176 -0.0163 -0.0092 316 GLU   B CA  
2689 C C   . GLU   B 110 ? 0.4834 0.4766 0.4414 -0.0221 -0.0121 -0.0099 316 GLU   B C   
2690 O O   . GLU   B 110 ? 0.4032 0.4007 0.3649 -0.0209 -0.0083 -0.0127 316 GLU   B O   
2691 C CB  . GLU   B 110 ? 0.5747 0.5522 0.5329 -0.0185 -0.0206 -0.0064 316 GLU   B CB  
2692 C CG  . GLU   B 110 ? 0.6698 0.6412 0.6321 -0.0133 -0.0248 -0.0068 316 GLU   B CG  
2693 C CD  . GLU   B 110 ? 0.8416 0.8039 0.7997 -0.0153 -0.0314 -0.0026 316 GLU   B CD  
2694 O OE1 . GLU   B 110 ? 1.0317 0.9869 0.9910 -0.0140 -0.0345 -0.0023 316 GLU   B OE1 
2695 O OE2 . GLU   B 110 ? 1.0550 1.0168 1.0085 -0.0182 -0.0339 0.0003  316 GLU   B OE2 
2696 N N   . ASN   B 111 ? 0.4219 0.4164 0.3736 -0.0273 -0.0129 -0.0075 317 ASN   B N   
2697 C CA  . ASN   B 111 ? 0.4443 0.4462 0.3932 -0.0321 -0.0089 -0.0085 317 ASN   B CA  
2698 C C   . ASN   B 111 ? 0.5206 0.5193 0.4654 -0.0368 -0.0097 -0.0058 317 ASN   B C   
2699 O O   . ASN   B 111 ? 0.5262 0.5188 0.4648 -0.0406 -0.0137 -0.0014 317 ASN   B O   
2700 C CB  . ASN   B 111 ? 0.4307 0.4364 0.3743 -0.0357 -0.0092 -0.0076 317 ASN   B CB  
2701 C CG  . ASN   B 111 ? 0.5427 0.5582 0.4848 -0.0400 -0.0043 -0.0103 317 ASN   B CG  
2702 O OD1 . ASN   B 111 ? 0.5576 0.5770 0.5028 -0.0405 -0.0011 -0.0124 317 ASN   B OD1 
2703 N ND2 . ASN   B 111 ? 0.5587 0.5788 0.4963 -0.0430 -0.0040 -0.0105 317 ASN   B ND2 
2704 N N   . MET   B 112 ? 0.4027 0.4056 0.3510 -0.0370 -0.0062 -0.0083 318 MET   B N   
2705 C CA  . MET   B 112 ? 0.4533 0.4520 0.3999 -0.0399 -0.0073 -0.0063 318 MET   B CA  
2706 C C   . MET   B 112 ? 0.4005 0.4084 0.3487 -0.0431 -0.0025 -0.0091 318 MET   B C   
2707 O O   . MET   B 112 ? 0.4683 0.4840 0.4209 -0.0409 0.0012  -0.0132 318 MET   B O   
2708 C CB  . MET   B 112 ? 0.4930 0.4862 0.4450 -0.0340 -0.0087 -0.0077 318 MET   B CB  
2709 C CG  . MET   B 112 ? 0.5221 0.5060 0.4738 -0.0309 -0.0137 -0.0055 318 MET   B CG  
2710 S SD  . MET   B 112 ? 0.4913 0.4685 0.4468 -0.0272 -0.0155 -0.0065 318 MET   B SD  
2711 C CE  . MET   B 112 ? 0.4464 0.4303 0.4090 -0.0208 -0.0113 -0.0115 318 MET   B CE  
2712 N N   . THR   B 113 ? 0.4224 0.4294 0.3675 -0.0483 -0.0027 -0.0071 319 THR   B N   
2713 C CA  . THR   B 113 ? 0.4090 0.4237 0.3578 -0.0501 0.0012  -0.0103 319 THR   B CA  
2714 C C   . THR   B 113 ? 0.4053 0.4142 0.3579 -0.0470 -0.0004 -0.0105 319 THR   B C   
2715 O O   . THR   B 113 ? 0.4199 0.4196 0.3694 -0.0481 -0.0044 -0.0070 319 THR   B O   
2716 C CB  . THR   B 113 ? 0.4983 0.5174 0.4416 -0.0586 0.0026  -0.0083 319 THR   B CB  
2717 O OG1 . THR   B 113 ? 0.5717 0.5976 0.5115 -0.0613 0.0047  -0.0090 319 THR   B OG1 
2718 C CG2 . THR   B 113 ? 0.4734 0.5003 0.4217 -0.0604 0.0062  -0.0117 319 THR   B CG2 
2719 N N   . VAL   B 114 ? 0.3611 0.3746 0.3204 -0.0429 0.0021  -0.0146 320 VAL   B N   
2720 C CA  . VAL   B 114 ? 0.3502 0.3583 0.3127 -0.0395 0.0004  -0.0151 320 VAL   B CA  
2721 C C   . VAL   B 114 ? 0.3885 0.4023 0.3544 -0.0417 0.0026  -0.0174 320 VAL   B C   
2722 O O   . VAL   B 114 ? 0.3997 0.4230 0.3683 -0.0433 0.0061  -0.0202 320 VAL   B O   
2723 C CB  . VAL   B 114 ? 0.4068 0.4133 0.3737 -0.0321 0.0004  -0.0175 320 VAL   B CB  
2724 C CG1 . VAL   B 114 ? 0.4188 0.4207 0.3835 -0.0298 -0.0017 -0.0157 320 VAL   B CG1 
2725 C CG2 . VAL   B 114 ? 0.3781 0.3936 0.3504 -0.0299 0.0041  -0.0215 320 VAL   B CG2 
2726 N N   . THR   B 115 ? 0.4167 0.4247 0.3829 -0.0414 0.0003  -0.0167 321 THR   B N   
2727 C CA  . THR   B 115 ? 0.4231 0.4354 0.3930 -0.0430 0.0015  -0.0188 321 THR   B CA  
2728 C C   . THR   B 115 ? 0.4041 0.4139 0.3782 -0.0367 0.0008  -0.0212 321 THR   B C   
2729 O O   . THR   B 115 ? 0.3805 0.3820 0.3530 -0.0338 -0.0021 -0.0201 321 THR   B O   
2730 C CB  . THR   B 115 ? 0.4407 0.4477 0.4070 -0.0486 -0.0010 -0.0157 321 THR   B CB  
2731 O OG1 . THR   B 115 ? 0.5919 0.6020 0.5536 -0.0553 0.0000  -0.0131 321 THR   B OG1 
2732 C CG2 . THR   B 115 ? 0.5086 0.5200 0.4792 -0.0499 0.0000  -0.0181 321 THR   B CG2 
2733 N N   . CYS   B 116 ? 0.3664 0.3835 0.3458 -0.0347 0.0031  -0.0247 322 CYS   B N   
2734 C CA  A CYS   B 116 ? 0.3813 0.3969 0.3641 -0.0292 0.0025  -0.0268 322 CYS   B CA  
2735 C CA  B CYS   B 116 ? 0.3958 0.4114 0.3786 -0.0293 0.0024  -0.0268 322 CYS   B CA  
2736 C C   . CYS   B 116 ? 0.4646 0.4819 0.4500 -0.0308 0.0018  -0.0282 322 CYS   B C   
2737 O O   . CYS   B 116 ? 0.3973 0.4227 0.3868 -0.0329 0.0037  -0.0304 322 CYS   B O   
2738 C CB  A CYS   B 116 ? 0.4193 0.4408 0.4062 -0.0255 0.0047  -0.0293 322 CYS   B CB  
2739 C CB  B CYS   B 116 ? 0.4195 0.4408 0.4064 -0.0254 0.0047  -0.0293 322 CYS   B CB  
2740 S SG  A CYS   B 116 ? 0.6315 0.6506 0.6212 -0.0193 0.0038  -0.0309 322 CYS   B SG  
2741 S SG  B CYS   B 116 ? 0.4475 0.4676 0.4321 -0.0236 0.0054  -0.0281 322 CYS   B SG  
2742 N N   . SER   B 117 ? 0.3799 0.3900 0.3636 -0.0297 -0.0010 -0.0275 323 SER   B N   
2743 C CA  . SER   B 117 ? 0.3798 0.3906 0.3656 -0.0312 -0.0022 -0.0289 323 SER   B CA  
2744 C C   . SER   B 117 ? 0.4534 0.4638 0.4413 -0.0259 -0.0029 -0.0311 323 SER   B C   
2745 O O   . SER   B 117 ? 0.4269 0.4315 0.4124 -0.0222 -0.0041 -0.0308 323 SER   B O   
2746 C CB  . SER   B 117 ? 0.3884 0.3911 0.3703 -0.0343 -0.0052 -0.0266 323 SER   B CB  
2747 O OG  . SER   B 117 ? 0.4368 0.4386 0.4205 -0.0346 -0.0070 -0.0282 323 SER   B OG  
2748 N N   . THR   B 118 ? 0.3307 0.3476 0.3234 -0.0257 -0.0023 -0.0335 324 THR   B N   
2749 C CA  . THR   B 118 ? 0.3708 0.3873 0.3652 -0.0215 -0.0037 -0.0352 324 THR   B CA  
2750 C C   . THR   B 118 ? 0.3806 0.3970 0.3762 -0.0236 -0.0059 -0.0364 324 THR   B C   
2751 O O   . THR   B 118 ? 0.4201 0.4428 0.4200 -0.0269 -0.0053 -0.0376 324 THR   B O   
2752 C CB  . THR   B 118 ? 0.3700 0.3933 0.3693 -0.0190 -0.0022 -0.0371 324 THR   B CB  
2753 O OG1 . THR   B 118 ? 0.4121 0.4356 0.4105 -0.0174 -0.0003 -0.0362 324 THR   B OG1 
2754 C CG2 . THR   B 118 ? 0.3964 0.4181 0.3960 -0.0151 -0.0042 -0.0380 324 THR   B CG2 
2755 N N   . LYS   B 119 ? 0.3108 0.3206 0.3031 -0.0217 -0.0083 -0.0365 325 LYS   B N   
2756 C CA  . LYS   B 119 ? 0.3712 0.3804 0.3644 -0.0232 -0.0109 -0.0378 325 LYS   B CA  
2757 C C   . LYS   B 119 ? 0.3828 0.3921 0.3760 -0.0191 -0.0123 -0.0395 325 LYS   B C   
2758 O O   . LYS   B 119 ? 0.3537 0.3583 0.3427 -0.0157 -0.0127 -0.0392 325 LYS   B O   
2759 C CB  . LYS   B 119 ? 0.3572 0.3583 0.3463 -0.0252 -0.0131 -0.0369 325 LYS   B CB  
2760 C CG  . LYS   B 119 ? 0.4499 0.4507 0.4390 -0.0307 -0.0126 -0.0349 325 LYS   B CG  
2761 C CD  . LYS   B 119 ? 0.4906 0.4818 0.4756 -0.0322 -0.0155 -0.0336 325 LYS   B CD  
2762 C CE  . LYS   B 119 ? 0.5788 0.5693 0.5630 -0.0383 -0.0153 -0.0307 325 LYS   B CE  
2763 N NZ  . LYS   B 119 ? 0.7428 0.7226 0.7230 -0.0395 -0.0186 -0.0289 325 LYS   B NZ  
2764 N N   . VAL   B 120 ? 0.2772 0.2924 0.2752 -0.0194 -0.0132 -0.0412 326 VAL   B N   
2765 C CA  . VAL   B 120 ? 0.2954 0.3107 0.2932 -0.0160 -0.0154 -0.0423 326 VAL   B CA  
2766 C C   . VAL   B 120 ? 0.3517 0.3636 0.3476 -0.0173 -0.0185 -0.0436 326 VAL   B C   
2767 O O   . VAL   B 120 ? 0.4102 0.4243 0.4094 -0.0211 -0.0194 -0.0444 326 VAL   B O   
2768 C CB  . VAL   B 120 ? 0.3541 0.3772 0.3588 -0.0153 -0.0156 -0.0436 326 VAL   B CB  
2769 C CG1 . VAL   B 120 ? 0.3932 0.4157 0.3974 -0.0122 -0.0188 -0.0444 326 VAL   B CG1 
2770 C CG2 . VAL   B 120 ? 0.3006 0.3266 0.3073 -0.0138 -0.0127 -0.0429 326 VAL   B CG2 
2771 N N   . CYS   B 121 ? 0.3365 0.3433 0.3270 -0.0145 -0.0202 -0.0439 327 CYS   B N   
2772 C CA  . CYS   B 121 ? 0.3486 0.3514 0.3365 -0.0156 -0.0231 -0.0455 327 CYS   B CA  
2773 C C   . CYS   B 121 ? 0.3687 0.3721 0.3547 -0.0133 -0.0259 -0.0468 327 CYS   B C   
2774 O O   . CYS   B 121 ? 0.3509 0.3548 0.3345 -0.0102 -0.0254 -0.0460 327 CYS   B O   
2775 C CB  . CYS   B 121 ? 0.3691 0.3643 0.3515 -0.0151 -0.0229 -0.0454 327 CYS   B CB  
2776 S SG  . CYS   B 121 ? 0.4728 0.4658 0.4561 -0.0176 -0.0205 -0.0432 327 CYS   B SG  
2777 N N   . SER   B 122 ? 0.3746 0.3776 0.3613 -0.0151 -0.0290 -0.0487 328 SER   B N   
2778 C CA  . SER   B 122 ? 0.4497 0.4528 0.4340 -0.0135 -0.0325 -0.0502 328 SER   B CA  
2779 C C   . SER   B 122 ? 0.3948 0.3922 0.3745 -0.0144 -0.0347 -0.0524 328 SER   B C   
2780 O O   . SER   B 122 ? 0.4098 0.4062 0.3924 -0.0177 -0.0358 -0.0534 328 SER   B O   
2781 C CB  . SER   B 122 ? 0.4156 0.4252 0.4069 -0.0149 -0.0349 -0.0511 328 SER   B CB  
2782 O OG  . SER   B 122 ? 0.4215 0.4309 0.4101 -0.0132 -0.0387 -0.0521 328 SER   B OG  
2783 N N   . PHE   B 123 ? 0.3827 0.3766 0.3552 -0.0117 -0.0353 -0.0534 329 PHE   B N   
2784 C CA  . PHE   B 123 ? 0.4874 0.4758 0.4552 -0.0119 -0.0371 -0.0562 329 PHE   B CA  
2785 C C   . PHE   B 123 ? 0.4448 0.4284 0.4139 -0.0135 -0.0358 -0.0564 329 PHE   B C   
2786 O O   . PHE   B 123 ? 0.4715 0.4512 0.4410 -0.0155 -0.0382 -0.0584 329 PHE   B O   
2787 C CB  . PHE   B 123 ? 0.4483 0.4375 0.4170 -0.0137 -0.0415 -0.0586 329 PHE   B CB  
2788 C CG  . PHE   B 123 ? 0.4099 0.4017 0.3746 -0.0117 -0.0438 -0.0589 329 PHE   B CG  
2789 C CD1 . PHE   B 123 ? 0.4443 0.4416 0.4134 -0.0116 -0.0449 -0.0570 329 PHE   B CD1 
2790 C CD2 . PHE   B 123 ? 0.4652 0.4540 0.4217 -0.0100 -0.0449 -0.0610 329 PHE   B CD2 
2791 C CE1 . PHE   B 123 ? 0.4042 0.4030 0.3693 -0.0099 -0.0477 -0.0567 329 PHE   B CE1 
2792 C CE2 . PHE   B 123 ? 0.4778 0.4687 0.4294 -0.0087 -0.0471 -0.0607 329 PHE   B CE2 
2793 C CZ  . PHE   B 123 ? 0.4365 0.4319 0.3923 -0.0087 -0.0488 -0.0582 329 PHE   B CZ  
2794 N N   . GLY   B 124 ? 0.4355 0.4191 0.4054 -0.0126 -0.0324 -0.0540 330 GLY   B N   
2795 C CA  . GLY   B 124 ? 0.4682 0.4468 0.4388 -0.0138 -0.0315 -0.0535 330 GLY   B CA  
2796 C C   . GLY   B 124 ? 0.5067 0.4860 0.4827 -0.0184 -0.0319 -0.0518 330 GLY   B C   
2797 O O   . GLY   B 124 ? 0.5602 0.5346 0.5363 -0.0200 -0.0317 -0.0508 330 GLY   B O   
2798 N N   . LYS   B 125 ? 0.4154 0.4008 0.3958 -0.0206 -0.0324 -0.0515 331 LYS   B N   
2799 C CA  . LYS   B 125 ? 0.4139 0.4017 0.3996 -0.0254 -0.0323 -0.0502 331 LYS   B CA  
2800 C C   . LYS   B 125 ? 0.4760 0.4713 0.4661 -0.0260 -0.0291 -0.0481 331 LYS   B C   
2801 O O   . LYS   B 125 ? 0.4061 0.4068 0.3980 -0.0237 -0.0287 -0.0486 331 LYS   B O   
2802 C CB  . LYS   B 125 ? 0.4505 0.4403 0.4394 -0.0284 -0.0356 -0.0522 331 LYS   B CB  
2803 C CG  . LYS   B 125 ? 0.6464 0.6292 0.6312 -0.0278 -0.0392 -0.0549 331 LYS   B CG  
2804 C CD  . LYS   B 125 ? 0.7879 0.7690 0.7761 -0.0330 -0.0420 -0.0557 331 LYS   B CD  
2805 C CE  . LYS   B 125 ? 0.8899 0.8650 0.8747 -0.0322 -0.0461 -0.0593 331 LYS   B CE  
2806 N NZ  . LYS   B 125 ? 1.1228 1.0995 1.1121 -0.0368 -0.0493 -0.0606 331 LYS   B NZ  
2807 N N   . GLN   B 126 ? 0.4526 0.4483 0.4446 -0.0295 -0.0271 -0.0461 332 GLN   B N   
2808 C CA  . GLN   B 126 ? 0.4506 0.4539 0.4467 -0.0305 -0.0239 -0.0448 332 GLN   B CA  
2809 C C   . GLN   B 126 ? 0.4370 0.4491 0.4399 -0.0323 -0.0244 -0.0465 332 GLN   B C   
2810 O O   . GLN   B 126 ? 0.4388 0.4520 0.4445 -0.0363 -0.0261 -0.0474 332 GLN   B O   
2811 C CB  . GLN   B 126 ? 0.4819 0.4838 0.4777 -0.0347 -0.0220 -0.0422 332 GLN   B CB  
2812 C CG  . GLN   B 126 ? 0.4555 0.4648 0.4544 -0.0355 -0.0182 -0.0411 332 GLN   B CG  
2813 C CD  . GLN   B 126 ? 0.5688 0.5788 0.5679 -0.0415 -0.0168 -0.0388 332 GLN   B CD  
2814 O OE1 . GLN   B 126 ? 0.6161 0.6189 0.6105 -0.0426 -0.0171 -0.0363 332 GLN   B OE1 
2815 N NE2 . GLN   B 126 ? 0.5853 0.6042 0.5898 -0.0456 -0.0152 -0.0397 332 GLN   B NE2 
2816 N N   . VAL   B 127 ? 0.3942 0.4123 0.4001 -0.0292 -0.0231 -0.0471 333 VAL   B N   
2817 C CA  . VAL   B 127 ? 0.4145 0.4418 0.4283 -0.0303 -0.0237 -0.0492 333 VAL   B CA  
2818 C C   . VAL   B 127 ? 0.4636 0.4990 0.4830 -0.0322 -0.0199 -0.0491 333 VAL   B C   
2819 O O   . VAL   B 127 ? 0.4042 0.4473 0.4302 -0.0360 -0.0194 -0.0508 333 VAL   B O   
2820 C CB  . VAL   B 127 ? 0.4459 0.4747 0.4607 -0.0256 -0.0263 -0.0506 333 VAL   B CB  
2821 C CG1 . VAL   B 127 ? 0.4600 0.4830 0.4702 -0.0250 -0.0303 -0.0515 333 VAL   B CG1 
2822 C CG2 . VAL   B 127 ? 0.4992 0.5257 0.5103 -0.0211 -0.0248 -0.0490 333 VAL   B CG2 
2823 N N   . VAL   B 128 ? 0.3944 0.4289 0.4114 -0.0299 -0.0172 -0.0475 334 VAL   B N   
2824 C CA  . VAL   B 128 ? 0.4147 0.4562 0.4356 -0.0320 -0.0135 -0.0476 334 VAL   B CA  
2825 C C   . VAL   B 128 ? 0.4690 0.5049 0.4836 -0.0317 -0.0111 -0.0447 334 VAL   B C   
2826 O O   . VAL   B 128 ? 0.4079 0.4359 0.4166 -0.0284 -0.0121 -0.0432 334 VAL   B O   
2827 C CB  . VAL   B 128 ? 0.4889 0.5386 0.5170 -0.0286 -0.0129 -0.0501 334 VAL   B CB  
2828 C CG1 . VAL   B 128 ? 0.4775 0.5349 0.5139 -0.0296 -0.0150 -0.0535 334 VAL   B CG1 
2829 C CG2 . VAL   B 128 ? 0.4374 0.4819 0.4621 -0.0228 -0.0143 -0.0491 334 VAL   B CG2 
2830 N N   . GLU   B 129 ? 0.4507 0.4912 0.4666 -0.0354 -0.0079 -0.0442 335 GLU   B N   
2831 C CA  . GLU   B 129 ? 0.4712 0.5069 0.4813 -0.0359 -0.0061 -0.0413 335 GLU   B CA  
2832 C C   . GLU   B 129 ? 0.4701 0.5139 0.4832 -0.0374 -0.0023 -0.0420 335 GLU   B C   
2833 O O   . GLU   B 129 ? 0.4502 0.5035 0.4695 -0.0403 -0.0008 -0.0445 335 GLU   B O   
2834 C CB  . GLU   B 129 ? 0.4933 0.5220 0.4982 -0.0405 -0.0072 -0.0385 335 GLU   B CB  
2835 C CG  . GLU   B 129 ? 0.6193 0.6421 0.6182 -0.0406 -0.0061 -0.0354 335 GLU   B CG  
2836 C CD  . GLU   B 129 ? 0.6576 0.6759 0.6526 -0.0466 -0.0069 -0.0324 335 GLU   B CD  
2837 O OE1 . GLU   B 129 ? 0.7525 0.7735 0.7498 -0.0515 -0.0076 -0.0328 335 GLU   B OE1 
2838 O OE2 . GLU   B 129 ? 0.7146 0.7259 0.7042 -0.0464 -0.0074 -0.0296 335 GLU   B OE2 
2839 N N   . LYS   B 130 ? 0.3945 0.4350 0.4037 -0.0354 -0.0009 -0.0402 336 LYS   B N   
2840 C CA  . LYS   B 130 ? 0.4476 0.4949 0.4585 -0.0368 0.0025  -0.0409 336 LYS   B CA  
2841 C C   . LYS   B 130 ? 0.4524 0.4933 0.4560 -0.0382 0.0031  -0.0372 336 LYS   B C   
2842 O O   . LYS   B 130 ? 0.4218 0.4542 0.4210 -0.0348 0.0014  -0.0353 336 LYS   B O   
2843 C CB  . LYS   B 130 ? 0.4490 0.5005 0.4646 -0.0315 0.0032  -0.0434 336 LYS   B CB  
2844 C CG  . LYS   B 130 ? 0.5316 0.5942 0.5532 -0.0331 0.0064  -0.0467 336 LYS   B CG  
2845 C CD  . LYS   B 130 ? 0.5966 0.6597 0.6194 -0.0286 0.0074  -0.0476 336 LYS   B CD  
2846 C CE  . LYS   B 130 ? 0.7161 0.7892 0.7428 -0.0310 0.0109  -0.0506 336 LYS   B CE  
2847 N NZ  . LYS   B 130 ? 0.8190 0.8937 0.8496 -0.0260 0.0111  -0.0528 336 LYS   B NZ  
2848 N N   . VAL   B 131 ? 0.3957 0.4411 0.3981 -0.0433 0.0055  -0.0365 337 VAL   B N   
2849 C CA  . VAL   B 131 ? 0.3843 0.4246 0.3799 -0.0450 0.0059  -0.0330 337 VAL   B CA  
2850 C C   . VAL   B 131 ? 0.4415 0.4899 0.4388 -0.0452 0.0093  -0.0348 337 VAL   B C   
2851 O O   . VAL   B 131 ? 0.4688 0.5273 0.4703 -0.0485 0.0119  -0.0375 337 VAL   B O   
2852 C CB  . VAL   B 131 ? 0.4729 0.5098 0.4638 -0.0519 0.0049  -0.0297 337 VAL   B CB  
2853 C CG1 . VAL   B 131 ? 0.4940 0.5259 0.4780 -0.0539 0.0048  -0.0259 337 VAL   B CG1 
2854 C CG2 . VAL   B 131 ? 0.4780 0.5062 0.4675 -0.0513 0.0012  -0.0284 337 VAL   B CG2 
2855 N N   . GLU   B 132 ? 0.3816 0.4262 0.3764 -0.0413 0.0093  -0.0338 338 GLU   B N   
2856 C CA  . GLU   B 132 ? 0.4481 0.4991 0.4439 -0.0411 0.0121  -0.0355 338 GLU   B CA  
2857 C C   . GLU   B 132 ? 0.4178 0.4634 0.4060 -0.0432 0.0117  -0.0317 338 GLU   B C   
2858 O O   . GLU   B 132 ? 0.4387 0.4745 0.4225 -0.0418 0.0089  -0.0283 338 GLU   B O   
2859 C CB  . GLU   B 132 ? 0.4537 0.5057 0.4543 -0.0344 0.0122  -0.0382 338 GLU   B CB  
2860 C CG  . GLU   B 132 ? 0.6374 0.6964 0.6464 -0.0323 0.0125  -0.0424 338 GLU   B CG  
2861 C CD  . GLU   B 132 ? 0.7437 0.7984 0.7553 -0.0259 0.0104  -0.0430 338 GLU   B CD  
2862 O OE1 . GLU   B 132 ? 0.7994 0.8454 0.8064 -0.0238 0.0084  -0.0401 338 GLU   B OE1 
2863 O OE2 . GLU   B 132 ? 0.8295 0.8897 0.8478 -0.0231 0.0107  -0.0464 338 GLU   B OE2 
2864 N N   . THR   B 133 ? 0.4106 0.4628 0.3976 -0.0465 0.0144  -0.0324 339 THR   B N   
2865 C CA  . THR   B 133 ? 0.3864 0.4345 0.3662 -0.0487 0.0139  -0.0290 339 THR   B CA  
2866 C C   . THR   B 133 ? 0.4036 0.4554 0.3854 -0.0448 0.0154  -0.0315 339 THR   B C   
2867 O O   . THR   B 133 ? 0.4090 0.4702 0.3961 -0.0444 0.0183  -0.0360 339 THR   B O   
2868 C CB  . THR   B 133 ? 0.5220 0.5749 0.4971 -0.0569 0.0154  -0.0274 339 THR   B CB  
2869 O OG1 . THR   B 133 ? 0.4795 0.5291 0.4537 -0.0606 0.0139  -0.0253 339 THR   B OG1 
2870 C CG2 . THR   B 133 ? 0.3733 0.4207 0.3399 -0.0594 0.0140  -0.0231 339 THR   B CG2 
2871 N N   . GLU   B 134 ? 0.3799 0.4242 0.3581 -0.0417 0.0134  -0.0290 340 GLU   B N   
2872 C CA  . GLU   B 134 ? 0.3789 0.4259 0.3590 -0.0382 0.0146  -0.0311 340 GLU   B CA  
2873 C C   . GLU   B 134 ? 0.3845 0.4277 0.3577 -0.0401 0.0134  -0.0278 340 GLU   B C   
2874 O O   . GLU   B 134 ? 0.3801 0.4151 0.3480 -0.0415 0.0104  -0.0235 340 GLU   B O   
2875 C CB  . GLU   B 134 ? 0.4353 0.4783 0.4200 -0.0313 0.0134  -0.0322 340 GLU   B CB  
2876 C CG  . GLU   B 134 ? 0.5727 0.6217 0.5651 -0.0287 0.0148  -0.0364 340 GLU   B CG  
2877 C CD  . GLU   B 134 ? 0.5650 0.6243 0.5618 -0.0297 0.0177  -0.0409 340 GLU   B CD  
2878 O OE1 . GLU   B 134 ? 0.5710 0.6322 0.5654 -0.0305 0.0187  -0.0413 340 GLU   B OE1 
2879 O OE2 . GLU   B 134 ? 0.7297 0.7953 0.7326 -0.0296 0.0188  -0.0444 340 GLU   B OE2 
2880 N N   . TYR   B 135 ? 0.3772 0.4261 0.3509 -0.0399 0.0153  -0.0302 341 TYR   B N   
2881 C CA  . TYR   B 135 ? 0.3366 0.3834 0.3039 -0.0419 0.0142  -0.0277 341 TYR   B CA  
2882 C C   . TYR   B 135 ? 0.3845 0.4294 0.3547 -0.0363 0.0135  -0.0289 341 TYR   B C   
2883 O O   . TYR   B 135 ? 0.3674 0.4166 0.3442 -0.0325 0.0152  -0.0330 341 TYR   B O   
2884 C CB  . TYR   B 135 ? 0.3616 0.4179 0.3259 -0.0478 0.0172  -0.0296 341 TYR   B CB  
2885 C CG  . TYR   B 135 ? 0.4069 0.4667 0.3688 -0.0541 0.0185  -0.0286 341 TYR   B CG  
2886 C CD1 . TYR   B 135 ? 0.4165 0.4832 0.3853 -0.0539 0.0210  -0.0325 341 TYR   B CD1 
2887 C CD2 . TYR   B 135 ? 0.4371 0.4926 0.3903 -0.0602 0.0166  -0.0233 341 TYR   B CD2 
2888 C CE1 . TYR   B 135 ? 0.4100 0.4804 0.3773 -0.0600 0.0222  -0.0317 341 TYR   B CE1 
2889 C CE2 . TYR   B 135 ? 0.4899 0.5481 0.4409 -0.0665 0.0177  -0.0220 341 TYR   B CE2 
2890 C CZ  . TYR   B 135 ? 0.4258 0.4918 0.3840 -0.0664 0.0207  -0.0264 341 TYR   B CZ  
2891 O OH  . TYR   B 135 ? 0.6856 0.7551 0.6422 -0.0730 0.0218  -0.0253 341 TYR   B OH  
2892 N N   . ALA   B 136 ? 0.3444 0.3826 0.3100 -0.0358 0.0106  -0.0254 342 ALA   B N   
2893 C CA  . ALA   B 136 ? 0.4133 0.4490 0.3818 -0.0305 0.0096  -0.0262 342 ALA   B CA  
2894 C C   . ALA   B 136 ? 0.4990 0.5418 0.4688 -0.0306 0.0117  -0.0296 342 ALA   B C   
2895 O O   . ALA   B 136 ? 0.4939 0.5412 0.4590 -0.0352 0.0126  -0.0298 342 ALA   B O   
2896 C CB  . ALA   B 136 ? 0.4418 0.4689 0.4057 -0.0300 0.0056  -0.0218 342 ALA   B CB  
2897 N N   . ARG   B 137 ? 0.4243 0.4674 0.4000 -0.0257 0.0120  -0.0321 343 ARG   B N   
2898 C CA  . ARG   B 137 ? 0.4880 0.5362 0.4657 -0.0249 0.0132  -0.0353 343 ARG   B CA  
2899 C C   . ARG   B 137 ? 0.4268 0.4693 0.4051 -0.0212 0.0107  -0.0335 343 ARG   B C   
2900 O O   . ARG   B 137 ? 0.3938 0.4322 0.3759 -0.0174 0.0100  -0.0329 343 ARG   B O   
2901 C CB  . ARG   B 137 ? 0.4646 0.5182 0.4500 -0.0223 0.0156  -0.0402 343 ARG   B CB  
2902 C CG  . ARG   B 137 ? 0.5977 0.6565 0.5858 -0.0215 0.0166  -0.0442 343 ARG   B CG  
2903 C CD  . ARG   B 137 ? 0.7226 0.7864 0.7190 -0.0190 0.0184  -0.0492 343 ARG   B CD  
2904 N NE  . ARG   B 137 ? 0.8548 0.9208 0.8551 -0.0168 0.0184  -0.0526 343 ARG   B NE  
2905 C CZ  . ARG   B 137 ? 0.9656 1.0366 0.9731 -0.0150 0.0195  -0.0579 343 ARG   B CZ  
2906 N NH1 . ARG   B 137 ? 1.0561 1.1310 1.0680 -0.0148 0.0208  -0.0605 343 ARG   B NH1 
2907 N NH2 . ARG   B 137 ? 1.0435 1.1156 1.0544 -0.0132 0.0191  -0.0608 343 ARG   B NH2 
2908 N N   . PHE   B 138 ? 0.4455 0.4883 0.4201 -0.0226 0.0094  -0.0329 344 PHE   B N   
2909 C CA  . PHE   B 138 ? 0.4364 0.4747 0.4123 -0.0193 0.0069  -0.0315 344 PHE   B CA  
2910 C C   . PHE   B 138 ? 0.3622 0.4035 0.3454 -0.0157 0.0084  -0.0352 344 PHE   B C   
2911 O O   . PHE   B 138 ? 0.4916 0.5388 0.4764 -0.0166 0.0101  -0.0389 344 PHE   B O   
2912 C CB  . PHE   B 138 ? 0.5227 0.5603 0.4924 -0.0220 0.0045  -0.0295 344 PHE   B CB  
2913 C CG  . PHE   B 138 ? 0.4210 0.4543 0.3926 -0.0186 0.0014  -0.0281 344 PHE   B CG  
2914 C CD1 . PHE   B 138 ? 0.4011 0.4274 0.3727 -0.0166 -0.0013 -0.0249 344 PHE   B CD1 
2915 C CD2 . PHE   B 138 ? 0.4228 0.4593 0.3969 -0.0174 0.0014  -0.0306 344 PHE   B CD2 
2916 C CE1 . PHE   B 138 ? 0.4627 0.4860 0.4371 -0.0133 -0.0040 -0.0242 344 PHE   B CE1 
2917 C CE2 . PHE   B 138 ? 0.3345 0.3677 0.3112 -0.0144 -0.0013 -0.0296 344 PHE   B CE2 
2918 C CZ  . PHE   B 138 ? 0.3790 0.4060 0.3561 -0.0124 -0.0039 -0.0265 344 PHE   B CZ  
2919 N N   . GLU   B 139 ? 0.3717 0.4092 0.3595 -0.0117 0.0078  -0.0345 345 GLU   B N   
2920 C CA  . GLU   B 139 ? 0.3984 0.4377 0.3929 -0.0087 0.0089  -0.0372 345 GLU   B CA  
2921 C C   . GLU   B 139 ? 0.4438 0.4790 0.4406 -0.0057 0.0073  -0.0354 345 GLU   B C   
2922 O O   . GLU   B 139 ? 0.3687 0.4000 0.3656 -0.0042 0.0067  -0.0333 345 GLU   B O   
2923 C CB  . GLU   B 139 ? 0.3987 0.4388 0.3975 -0.0073 0.0107  -0.0387 345 GLU   B CB  
2924 C CG  . GLU   B 139 ? 0.5631 0.6089 0.5629 -0.0092 0.0126  -0.0421 345 GLU   B CG  
2925 C CD  . GLU   B 139 ? 0.6288 0.6749 0.6332 -0.0075 0.0135  -0.0433 345 GLU   B CD  
2926 O OE1 . GLU   B 139 ? 0.5706 0.6126 0.5776 -0.0048 0.0128  -0.0417 345 GLU   B OE1 
2927 O OE2 . GLU   B 139 ? 0.7837 0.8343 0.7891 -0.0091 0.0149  -0.0457 345 GLU   B OE2 
2928 N N   . ASN   B 140 ? 0.4783 0.5150 0.4775 -0.0050 0.0066  -0.0367 346 ASN   B N   
2929 C CA  . ASN   B 140 ? 0.4541 0.4887 0.4572 -0.0023 0.0055  -0.0358 346 ASN   B CA  
2930 C C   . ASN   B 140 ? 0.3424 0.3727 0.3431 -0.0014 0.0036  -0.0328 346 ASN   B C   
2931 O O   . ASN   B 140 ? 0.4073 0.4356 0.4110 0.0010  0.0038  -0.0321 346 ASN   B O   
2932 C CB  . ASN   B 140 ? 0.4694 0.5040 0.4781 -0.0002 0.0073  -0.0368 346 ASN   B CB  
2933 C CG  . ASN   B 140 ? 0.5542 0.5922 0.5666 -0.0006 0.0084  -0.0401 346 ASN   B CG  
2934 O OD1 . ASN   B 140 ? 0.6086 0.6490 0.6220 -0.0012 0.0077  -0.0420 346 ASN   B OD1 
2935 N ND2 . ASN   B 140 ? 0.6164 0.6546 0.6312 0.0000  0.0096  -0.0411 346 ASN   B ND2 
2936 N N   . GLY   B 141 ? 0.3344 0.3631 0.3295 -0.0035 0.0015  -0.0311 347 GLY   B N   
2937 C CA  . GLY   B 141 ? 0.3461 0.3702 0.3395 -0.0024 -0.0014 -0.0285 347 GLY   B CA  
2938 C C   . GLY   B 141 ? 0.3801 0.4001 0.3703 -0.0028 -0.0018 -0.0265 347 GLY   B C   
2939 O O   . GLY   B 141 ? 0.3808 0.3964 0.3699 -0.0019 -0.0047 -0.0246 347 GLY   B O   
2940 N N   . ARG   B 142 ? 0.3328 0.3541 0.3222 -0.0041 0.0007  -0.0272 348 ARG   B N   
2941 C CA  A ARG   B 142 ? 0.4130 0.4308 0.3999 -0.0047 0.0005  -0.0256 348 ARG   B CA  
2942 C CA  B ARG   B 142 ? 0.4128 0.4303 0.3992 -0.0049 0.0002  -0.0255 348 ARG   B CA  
2943 C C   . ARG   B 142 ? 0.3229 0.3433 0.3063 -0.0084 0.0021  -0.0259 348 ARG   B C   
2944 O O   . ARG   B 142 ? 0.3721 0.3977 0.3565 -0.0096 0.0041  -0.0282 348 ARG   B O   
2945 C CB  A ARG   B 142 ? 0.3750 0.3918 0.3660 -0.0016 0.0021  -0.0265 348 ARG   B CB  
2946 C CB  B ARG   B 142 ? 0.3737 0.3896 0.3641 -0.0017 0.0013  -0.0261 348 ARG   B CB  
2947 C CG  A ARG   B 142 ? 0.3845 0.4038 0.3811 0.0011  0.0035  -0.0282 348 ARG   B CG  
2948 C CG  B ARG   B 142 ? 0.3607 0.3799 0.3538 -0.0014 0.0044  -0.0279 348 ARG   B CG  
2949 C CD  A ARG   B 142 ? 0.4132 0.4324 0.4123 0.0029  0.0056  -0.0289 348 ARG   B CD  
2950 C CD  B ARG   B 142 ? 0.4084 0.4306 0.4065 0.0006  0.0058  -0.0296 348 ARG   B CD  
2951 N NE  A ARG   B 142 ? 0.4341 0.4526 0.4364 0.0056  0.0057  -0.0291 348 ARG   B NE  
2952 N NE  B ARG   B 142 ? 0.4741 0.4977 0.4750 0.0014  0.0079  -0.0308 348 ARG   B NE  
2953 C CZ  A ARG   B 142 ? 0.4318 0.4530 0.4382 0.0067  0.0070  -0.0300 348 ARG   B CZ  
2954 C CZ  B ARG   B 142 ? 0.4102 0.4372 0.4138 0.0009  0.0092  -0.0326 348 ARG   B CZ  
2955 N NH1 A ARG   B 142 ? 0.3925 0.4165 0.4008 0.0057  0.0079  -0.0309 348 ARG   B NH1 
2956 N NH1 B ARG   B 142 ? 0.4219 0.4518 0.4256 -0.0005 0.0091  -0.0340 348 ARG   B NH1 
2957 N NH2 A ARG   B 142 ? 0.4350 0.4565 0.4440 0.0087  0.0075  -0.0304 348 ARG   B NH2 
2958 N NH2 B ARG   B 142 ? 0.4523 0.4796 0.4584 0.0018  0.0103  -0.0332 348 ARG   B NH2 
2959 N N   . PHE   B 143 ? 0.3390 0.3562 0.3190 -0.0101 0.0013  -0.0241 349 PHE   B N   
2960 C CA  . PHE   B 143 ? 0.3310 0.3513 0.3085 -0.0138 0.0031  -0.0245 349 PHE   B CA  
2961 C C   . PHE   B 143 ? 0.3421 0.3636 0.3237 -0.0120 0.0053  -0.0263 349 PHE   B C   
2962 O O   . PHE   B 143 ? 0.3371 0.3545 0.3200 -0.0095 0.0045  -0.0255 349 PHE   B O   
2963 C CB  . PHE   B 143 ? 0.3379 0.3538 0.3091 -0.0175 0.0006  -0.0211 349 PHE   B CB  
2964 C CG  . PHE   B 143 ? 0.3439 0.3584 0.3103 -0.0197 -0.0021 -0.0189 349 PHE   B CG  
2965 C CD1 . PHE   B 143 ? 0.3957 0.4158 0.3586 -0.0236 -0.0007 -0.0196 349 PHE   B CD1 
2966 C CD2 . PHE   B 143 ? 0.3224 0.3307 0.2884 -0.0175 -0.0060 -0.0167 349 PHE   B CD2 
2967 C CE1 . PHE   B 143 ? 0.4613 0.4802 0.4191 -0.0257 -0.0034 -0.0176 349 PHE   B CE1 
2968 C CE2 . PHE   B 143 ? 0.4143 0.4211 0.3761 -0.0193 -0.0091 -0.0146 349 PHE   B CE2 
2969 C CZ  . PHE   B 143 ? 0.4654 0.4774 0.4226 -0.0236 -0.0079 -0.0148 349 PHE   B CZ  
2970 N N   . VAL   B 144 ? 0.2971 0.3246 0.2810 -0.0130 0.0079  -0.0290 350 VAL   B N   
2971 C CA  . VAL   B 144 ? 0.3416 0.3708 0.3302 -0.0111 0.0095  -0.0310 350 VAL   B CA  
2972 C C   . VAL   B 144 ? 0.3672 0.3997 0.3548 -0.0144 0.0107  -0.0317 350 VAL   B C   
2973 O O   . VAL   B 144 ? 0.3450 0.3818 0.3301 -0.0180 0.0116  -0.0325 350 VAL   B O   
2974 C CB  . VAL   B 144 ? 0.4018 0.4350 0.3958 -0.0088 0.0109  -0.0339 350 VAL   B CB  
2975 C CG1 . VAL   B 144 ? 0.3757 0.4104 0.3742 -0.0072 0.0119  -0.0357 350 VAL   B CG1 
2976 C CG2 . VAL   B 144 ? 0.3664 0.3966 0.3618 -0.0059 0.0099  -0.0330 350 VAL   B CG2 
2977 N N   . TYR   B 145 ? 0.2958 0.3266 0.2848 -0.0135 0.0106  -0.0316 351 TYR   B N   
2978 C CA  . TYR   B 145 ? 0.2839 0.3179 0.2731 -0.0163 0.0115  -0.0325 351 TYR   B CA  
2979 C C   . TYR   B 145 ? 0.3651 0.4018 0.3603 -0.0135 0.0123  -0.0352 351 TYR   B C   
2980 O O   . TYR   B 145 ? 0.3916 0.4241 0.3879 -0.0106 0.0112  -0.0343 351 TYR   B O   
2981 C CB  . TYR   B 145 ? 0.3317 0.3600 0.3168 -0.0180 0.0096  -0.0296 351 TYR   B CB  
2982 C CG  . TYR   B 145 ? 0.3277 0.3513 0.3070 -0.0202 0.0076  -0.0263 351 TYR   B CG  
2983 C CD1 . TYR   B 145 ? 0.2968 0.3149 0.2754 -0.0171 0.0057  -0.0248 351 TYR   B CD1 
2984 C CD2 . TYR   B 145 ? 0.3678 0.3925 0.3424 -0.0256 0.0075  -0.0247 351 TYR   B CD2 
2985 C CE1 . TYR   B 145 ? 0.3353 0.3487 0.3093 -0.0186 0.0031  -0.0219 351 TYR   B CE1 
2986 C CE2 . TYR   B 145 ? 0.3415 0.3607 0.3103 -0.0277 0.0048  -0.0211 351 TYR   B CE2 
2987 C CZ  . TYR   B 145 ? 0.4229 0.4363 0.3918 -0.0239 0.0023  -0.0198 351 TYR   B CZ  
2988 O OH  . TYR   B 145 ? 0.4312 0.4390 0.3952 -0.0255 -0.0010 -0.0164 351 TYR   B OH  
2989 N N   . ARG   B 146 ? 0.3457 0.3894 0.3450 -0.0145 0.0140  -0.0386 352 ARG   B N   
2990 C CA  . ARG   B 146 ? 0.3841 0.4302 0.3899 -0.0116 0.0141  -0.0414 352 ARG   B CA  
2991 C C   . ARG   B 146 ? 0.4209 0.4718 0.4292 -0.0136 0.0147  -0.0433 352 ARG   B C   
2992 O O   . ARG   B 146 ? 0.4282 0.4851 0.4363 -0.0172 0.0164  -0.0451 352 ARG   B O   
2993 C CB  . ARG   B 146 ? 0.3611 0.4117 0.3719 -0.0099 0.0150  -0.0448 352 ARG   B CB  
2994 C CG  . ARG   B 146 ? 0.5425 0.5887 0.5535 -0.0070 0.0141  -0.0435 352 ARG   B CG  
2995 C CD  . ARG   B 146 ? 0.5573 0.6076 0.5741 -0.0054 0.0145  -0.0472 352 ARG   B CD  
2996 N NE  . ARG   B 146 ? 0.5923 0.6385 0.6091 -0.0032 0.0137  -0.0457 352 ARG   B NE  
2997 C CZ  . ARG   B 146 ? 0.5744 0.6210 0.5889 -0.0041 0.0141  -0.0456 352 ARG   B CZ  
2998 N NH1 . ARG   B 146 ? 0.5694 0.6202 0.5808 -0.0071 0.0153  -0.0468 352 ARG   B NH1 
2999 N NH2 . ARG   B 146 ? 0.6212 0.6642 0.6363 -0.0021 0.0133  -0.0442 352 ARG   B NH2 
3000 N N   . ILE   B 147 ? 0.3377 0.3863 0.3485 -0.0115 0.0133  -0.0431 353 ILE   B N   
3001 C CA  . ILE   B 147 ? 0.3991 0.4526 0.4143 -0.0125 0.0133  -0.0456 353 ILE   B CA  
3002 C C   . ILE   B 147 ? 0.4245 0.4791 0.4465 -0.0084 0.0121  -0.0480 353 ILE   B C   
3003 O O   . ILE   B 147 ? 0.3836 0.4330 0.4055 -0.0058 0.0100  -0.0462 353 ILE   B O   
3004 C CB  . ILE   B 147 ? 0.4868 0.5362 0.4987 -0.0138 0.0119  -0.0431 353 ILE   B CB  
3005 C CG1 . ILE   B 147 ? 0.4495 0.4947 0.4541 -0.0170 0.0120  -0.0397 353 ILE   B CG1 
3006 C CG2 . ILE   B 147 ? 0.6067 0.6624 0.6233 -0.0158 0.0122  -0.0459 353 ILE   B CG2 
3007 C CD1 . ILE   B 147 ? 0.5211 0.5636 0.5230 -0.0196 0.0109  -0.0381 353 ILE   B CD1 
3008 N N   . ASN   B 148 ? 0.4168 0.4778 0.4447 -0.0079 0.0131  -0.0521 354 ASN   B N   
3009 C CA  . ASN   B 148 ? 0.4616 0.5225 0.4961 -0.0039 0.0113  -0.0543 354 ASN   B CA  
3010 C C   . ASN   B 148 ? 0.4465 0.5124 0.4883 -0.0031 0.0101  -0.0577 354 ASN   B C   
3011 O O   . ASN   B 148 ? 0.4973 0.5712 0.5423 -0.0056 0.0119  -0.0613 354 ASN   B O   
3012 C CB  . ASN   B 148 ? 0.4792 0.5437 0.5171 -0.0031 0.0125  -0.0575 354 ASN   B CB  
3013 C CG  . ASN   B 148 ? 0.6648 0.7260 0.7081 0.0010  0.0100  -0.0582 354 ASN   B CG  
3014 O OD1 . ASN   B 148 ? 0.7336 0.7878 0.7747 0.0029  0.0079  -0.0544 354 ASN   B OD1 
3015 N ND2 . ASN   B 148 ? 0.6304 0.6966 0.6807 0.0023  0.0101  -0.0631 354 ASN   B ND2 
3016 N N   . ARG   B 149 ? 0.4148 0.4762 0.4590 0.0000  0.0069  -0.0565 355 ARG   B N   
3017 C CA  . ARG   B 149 ? 0.4207 0.4861 0.4732 0.0018  0.0046  -0.0599 355 ARG   B CA  
3018 C C   . ARG   B 149 ? 0.3574 0.4293 0.4115 -0.0012 0.0058  -0.0620 355 ARG   B C   
3019 O O   . ARG   B 149 ? 0.4197 0.5000 0.4818 -0.0013 0.0062  -0.0671 355 ARG   B O   
3020 C CB  . ARG   B 149 ? 0.3790 0.4493 0.4402 0.0041  0.0043  -0.0650 355 ARG   B CB  
3021 C CG  . ARG   B 149 ? 0.4998 0.5700 0.5696 0.0078  0.0001  -0.0671 355 ARG   B CG  
3022 C CD  . ARG   B 149 ? 0.4622 0.5319 0.5391 0.0112  -0.0018 -0.0701 355 ARG   B CD  
3023 N NE  . ARG   B 149 ? 0.5286 0.6003 0.6155 0.0144  -0.0060 -0.0736 355 ARG   B NE  
3024 C CZ  . ARG   B 149 ? 0.4831 0.5644 0.5786 0.0144  -0.0055 -0.0797 355 ARG   B CZ  
3025 N NH1 . ARG   B 149 ? 0.4671 0.5576 0.5626 0.0112  -0.0007 -0.0834 355 ARG   B NH1 
3026 N NH2 . ARG   B 149 ? 0.5275 0.6095 0.6318 0.0176  -0.0101 -0.0821 355 ARG   B NH2 
3027 N N   . SER   B 150 ? 0.3317 0.3998 0.3787 -0.0036 0.0061  -0.0582 356 SER   B N   
3028 C CA  . SER   B 150 ? 0.3782 0.4515 0.4263 -0.0069 0.0068  -0.0596 356 SER   B CA  
3029 C C   . SER   B 150 ? 0.3526 0.4256 0.4059 -0.0046 0.0031  -0.0605 356 SER   B C   
3030 O O   . SER   B 150 ? 0.3525 0.4179 0.4027 -0.0020 0.0002  -0.0572 356 SER   B O   
3031 C CB  . SER   B 150 ? 0.3705 0.4387 0.4091 -0.0104 0.0080  -0.0552 356 SER   B CB  
3032 O OG  . SER   B 150 ? 0.5958 0.6672 0.6349 -0.0136 0.0080  -0.0556 356 SER   B OG  
3033 N N   . PRO   B 151 ? 0.3389 0.4206 0.4002 -0.0055 0.0031  -0.0649 357 PRO   B N   
3034 C CA  . PRO   B 151 ? 0.3655 0.4471 0.4322 -0.0031 -0.0011 -0.0658 357 PRO   B CA  
3035 C C   . PRO   B 151 ? 0.3457 0.4208 0.4051 -0.0046 -0.0027 -0.0615 357 PRO   B C   
3036 O O   . PRO   B 151 ? 0.3297 0.4043 0.3832 -0.0086 -0.0003 -0.0598 357 PRO   B O   
3037 C CB  . PRO   B 151 ? 0.3749 0.4686 0.4515 -0.0048 0.0001  -0.0719 357 PRO   B CB  
3038 C CG  . PRO   B 151 ? 0.3529 0.4523 0.4262 -0.0096 0.0054  -0.0729 357 PRO   B CG  
3039 C CD  . PRO   B 151 ? 0.3413 0.4339 0.4072 -0.0088 0.0068  -0.0696 357 PRO   B CD  
3040 N N   . MET   B 152 ? 0.2720 0.3417 0.3314 -0.0015 -0.0070 -0.0599 358 MET   B N   
3041 C CA  . MET   B 152 ? 0.3237 0.3884 0.3772 -0.0028 -0.0089 -0.0569 358 MET   B CA  
3042 C C   . MET   B 152 ? 0.3391 0.4111 0.3981 -0.0055 -0.0092 -0.0600 358 MET   B C   
3043 O O   . MET   B 152 ? 0.3166 0.3965 0.3857 -0.0045 -0.0102 -0.0644 358 MET   B O   
3044 C CB  . MET   B 152 ? 0.2976 0.3558 0.3497 0.0008  -0.0137 -0.0547 358 MET   B CB  
3045 C CG  . MET   B 152 ? 0.3362 0.3857 0.3801 0.0024  -0.0138 -0.0504 358 MET   B CG  
3046 S SD  . MET   B 152 ? 0.3391 0.3825 0.3809 0.0053  -0.0198 -0.0479 358 MET   B SD  
3047 C CE  . MET   B 152 ? 0.2472 0.2834 0.2832 0.0074  -0.0195 -0.0440 358 MET   B CE  
3048 N N   . CYS   B 153 ? 0.3072 0.3766 0.3603 -0.0090 -0.0086 -0.0580 359 CYS   B N   
3049 C CA  . CYS   B 153 ? 0.3593 0.4352 0.4176 -0.0119 -0.0092 -0.0606 359 CYS   B CA  
3050 C C   . CYS   B 153 ? 0.3301 0.4062 0.3938 -0.0086 -0.0144 -0.0620 359 CYS   B C   
3051 O O   . CYS   B 153 ? 0.3324 0.4013 0.3924 -0.0051 -0.0177 -0.0595 359 CYS   B O   
3052 C CB  . CYS   B 153 ? 0.3706 0.4423 0.4212 -0.0162 -0.0082 -0.0578 359 CYS   B CB  
3053 S SG  . CYS   B 153 ? 0.4737 0.5327 0.5140 -0.0141 -0.0116 -0.0534 359 CYS   B SG  
3054 N N   . GLU   B 154 ? 0.3314 0.4161 0.4037 -0.0102 -0.0153 -0.0659 360 GLU   B N   
3055 C CA  . GLU   B 154 ? 0.3849 0.4705 0.4634 -0.0071 -0.0208 -0.0676 360 GLU   B CA  
3056 C C   . GLU   B 154 ? 0.3827 0.4590 0.4524 -0.0068 -0.0243 -0.0636 360 GLU   B C   
3057 O O   . GLU   B 154 ? 0.3576 0.4299 0.4275 -0.0032 -0.0292 -0.0627 360 GLU   B O   
3058 C CB  . GLU   B 154 ? 0.4040 0.5012 0.4936 -0.0094 -0.0209 -0.0728 360 GLU   B CB  
3059 C CG  . GLU   B 154 ? 0.4978 0.5977 0.5967 -0.0053 -0.0269 -0.0755 360 GLU   B CG  
3060 C CD  . GLU   B 154 ? 0.4297 0.5289 0.5338 0.0000  -0.0291 -0.0768 360 GLU   B CD  
3061 O OE1 . GLU   B 154 ? 0.4304 0.5353 0.5392 0.0001  -0.0253 -0.0796 360 GLU   B OE1 
3062 O OE2 . GLU   B 154 ? 0.4211 0.5140 0.5246 0.0039  -0.0348 -0.0748 360 GLU   B OE2 
3063 N N   . TYR   B 155 ? 0.3723 0.4446 0.4340 -0.0106 -0.0222 -0.0613 361 TYR   B N   
3064 C CA  . TYR   B 155 ? 0.4038 0.4675 0.4571 -0.0102 -0.0253 -0.0582 361 TYR   B CA  
3065 C C   . TYR   B 155 ? 0.3781 0.4336 0.4245 -0.0062 -0.0269 -0.0549 361 TYR   B C   
3066 O O   . TYR   B 155 ? 0.3417 0.3929 0.3853 -0.0040 -0.0313 -0.0537 361 TYR   B O   
3067 C CB  . TYR   B 155 ? 0.4293 0.4891 0.4752 -0.0145 -0.0227 -0.0564 361 TYR   B CB  
3068 C CG  . TYR   B 155 ? 0.4345 0.4858 0.4720 -0.0141 -0.0258 -0.0542 361 TYR   B CG  
3069 C CD1 . TYR   B 155 ? 0.3934 0.4361 0.4216 -0.0117 -0.0257 -0.0511 361 TYR   B CD1 
3070 C CD2 . TYR   B 155 ? 0.4903 0.5428 0.5296 -0.0161 -0.0289 -0.0558 361 TYR   B CD2 
3071 C CE1 . TYR   B 155 ? 0.4803 0.5163 0.5010 -0.0113 -0.0283 -0.0499 361 TYR   B CE1 
3072 C CE2 . TYR   B 155 ? 0.4349 0.4800 0.4666 -0.0156 -0.0319 -0.0544 361 TYR   B CE2 
3073 C CZ  . TYR   B 155 ? 0.4766 0.5137 0.4989 -0.0132 -0.0314 -0.0517 361 TYR   B CZ  
3074 O OH  . TYR   B 155 ? 0.4798 0.5105 0.4946 -0.0128 -0.0341 -0.0511 361 TYR   B OH  
3075 N N   . MET   B 156 ? 0.3362 0.3896 0.3797 -0.0054 -0.0235 -0.0534 362 MET   B N   
3076 C CA  . MET   B 156 ? 0.2965 0.3424 0.3334 -0.0022 -0.0246 -0.0501 362 MET   B CA  
3077 C C   . MET   B 156 ? 0.3537 0.4007 0.3964 0.0015  -0.0285 -0.0507 362 MET   B C   
3078 O O   . MET   B 156 ? 0.3134 0.3543 0.3509 0.0036  -0.0317 -0.0479 362 MET   B O   
3079 C CB  . MET   B 156 ? 0.3299 0.3732 0.3622 -0.0026 -0.0202 -0.0482 362 MET   B CB  
3080 C CG  . MET   B 156 ? 0.3734 0.4126 0.3980 -0.0055 -0.0178 -0.0467 362 MET   B CG  
3081 S SD  . MET   B 156 ? 0.4284 0.4591 0.4432 -0.0042 -0.0206 -0.0442 362 MET   B SD  
3082 C CE  . MET   B 156 ? 0.3466 0.3738 0.3590 -0.0004 -0.0218 -0.0418 362 MET   B CE  
3083 N N   . ILE   B 157 ? 0.3254 0.3800 0.3789 0.0023  -0.0285 -0.0543 363 ILE   B N   
3084 C CA  . ILE   B 157 ? 0.3271 0.3821 0.3873 0.0062  -0.0331 -0.0552 363 ILE   B CA  
3085 C C   . ILE   B 157 ? 0.3408 0.3942 0.4011 0.0071  -0.0390 -0.0548 363 ILE   B C   
3086 O O   . ILE   B 157 ? 0.3686 0.4162 0.4261 0.0097  -0.0436 -0.0521 363 ILE   B O   
3087 C CB  . ILE   B 157 ? 0.3489 0.4135 0.4220 0.0069  -0.0320 -0.0604 363 ILE   B CB  
3088 C CG1 . ILE   B 157 ? 0.2995 0.3656 0.3713 0.0058  -0.0262 -0.0608 363 ILE   B CG1 
3089 C CG2 . ILE   B 157 ? 0.3729 0.4372 0.4539 0.0114  -0.0377 -0.0616 363 ILE   B CG2 
3090 C CD1 . ILE   B 157 ? 0.3179 0.3946 0.4013 0.0058  -0.0239 -0.0666 363 ILE   B CD1 
3091 N N   . ASN   B 158 ? 0.3936 0.4517 0.4566 0.0046  -0.0391 -0.0572 364 ASN   B N   
3092 C CA  . ASN   B 158 ? 0.3435 0.4005 0.4067 0.0052  -0.0449 -0.0572 364 ASN   B CA  
3093 C C   . ASN   B 158 ? 0.3541 0.4015 0.4039 0.0050  -0.0464 -0.0525 364 ASN   B C   
3094 O O   . ASN   B 158 ? 0.3547 0.3981 0.4020 0.0069  -0.0519 -0.0507 364 ASN   B O   
3095 C CB  . ASN   B 158 ? 0.3790 0.4437 0.4481 0.0018  -0.0438 -0.0609 364 ASN   B CB  
3096 C CG  . ASN   B 158 ? 0.5321 0.5953 0.5998 0.0016  -0.0492 -0.0609 364 ASN   B CG  
3097 O OD1 . ASN   B 158 ? 0.6020 0.6609 0.6613 -0.0009 -0.0487 -0.0592 364 ASN   B OD1 
3098 N ND2 . ASN   B 158 ? 0.5586 0.6250 0.6349 0.0045  -0.0551 -0.0628 364 ASN   B ND2 
3099 N N   . PHE   B 159 ? 0.3029 0.3465 0.3439 0.0027  -0.0417 -0.0506 365 PHE   B N   
3100 C CA  . PHE   B 159 ? 0.3808 0.4162 0.4094 0.0026  -0.0425 -0.0471 365 PHE   B CA  
3101 C C   . PHE   B 159 ? 0.3576 0.3877 0.3818 0.0053  -0.0445 -0.0436 365 PHE   B C   
3102 O O   . PHE   B 159 ? 0.3429 0.3681 0.3599 0.0059  -0.0482 -0.0412 365 PHE   B O   
3103 C CB  . PHE   B 159 ? 0.3688 0.4018 0.3908 0.0002  -0.0370 -0.0463 365 PHE   B CB  
3104 C CG  . PHE   B 159 ? 0.4299 0.4556 0.4401 0.0002  -0.0370 -0.0437 365 PHE   B CG  
3105 C CD1 . PHE   B 159 ? 0.4167 0.4403 0.4223 -0.0008 -0.0401 -0.0442 365 PHE   B CD1 
3106 C CD2 . PHE   B 159 ? 0.4505 0.4720 0.4545 0.0010  -0.0340 -0.0411 365 PHE   B CD2 
3107 C CE1 . PHE   B 159 ? 0.4392 0.4568 0.4340 -0.0008 -0.0398 -0.0426 365 PHE   B CE1 
3108 C CE2 . PHE   B 159 ? 0.4231 0.4391 0.4168 0.0010  -0.0336 -0.0394 365 PHE   B CE2 
3109 C CZ  . PHE   B 159 ? 0.3581 0.3723 0.3471 0.0001  -0.0365 -0.0402 365 PHE   B CZ  
3110 N N   . ILE   B 160 ? 0.3535 0.3844 0.3813 0.0067  -0.0422 -0.0432 366 ILE   B N   
3111 C CA  . ILE   B 160 ? 0.2963 0.3220 0.3208 0.0088  -0.0442 -0.0397 366 ILE   B CA  
3112 C C   . ILE   B 160 ? 0.3818 0.4068 0.4104 0.0110  -0.0514 -0.0393 366 ILE   B C   
3113 O O   . ILE   B 160 ? 0.3740 0.3929 0.3955 0.0117  -0.0549 -0.0354 366 ILE   B O   
3114 C CB  . ILE   B 160 ? 0.3176 0.3449 0.3471 0.0098  -0.0407 -0.0402 366 ILE   B CB  
3115 C CG1 . ILE   B 160 ? 0.2990 0.3252 0.3224 0.0079  -0.0343 -0.0395 366 ILE   B CG1 
3116 C CG2 . ILE   B 160 ? 0.3170 0.3395 0.3460 0.0121  -0.0441 -0.0371 366 ILE   B CG2 
3117 C CD1 . ILE   B 160 ? 0.2833 0.3123 0.3122 0.0085  -0.0306 -0.0407 366 ILE   B CD1 
3118 N N   . HIS   B 161 ? 0.3215 0.3529 0.3618 0.0120  -0.0539 -0.0433 367 HIS   B N   
3119 C CA  . HIS   B 161 ? 0.3785 0.4094 0.4238 0.0144  -0.0616 -0.0433 367 HIS   B CA  
3120 C C   . HIS   B 161 ? 0.3768 0.4041 0.4136 0.0132  -0.0655 -0.0413 367 HIS   B C   
3121 O O   . HIS   B 161 ? 0.4019 0.4240 0.4344 0.0143  -0.0713 -0.0380 367 HIS   B O   
3122 C CB  . HIS   B 161 ? 0.3743 0.4143 0.4350 0.0157  -0.0633 -0.0489 367 HIS   B CB  
3123 C CG  . HIS   B 161 ? 0.5859 0.6297 0.6563 0.0177  -0.0612 -0.0515 367 HIS   B CG  
3124 N ND1 . HIS   B 161 ? 0.6592 0.7127 0.7434 0.0184  -0.0605 -0.0576 367 HIS   B ND1 
3125 C CD2 . HIS   B 161 ? 0.6042 0.6439 0.6723 0.0187  -0.0591 -0.0494 367 HIS   B CD2 
3126 C CE1 . HIS   B 161 ? 0.5721 0.6272 0.6620 0.0202  -0.0584 -0.0592 367 HIS   B CE1 
3127 N NE2 . HIS   B 161 ? 0.6190 0.6654 0.6994 0.0204  -0.0576 -0.0542 367 HIS   B NE2 
3128 N N   . LYS   B 162 ? 0.3963 0.4263 0.4305 0.0106  -0.0628 -0.0433 368 LYS   B N   
3129 C CA  A LYS   B 162 ? 0.4032 0.4301 0.4290 0.0092  -0.0661 -0.0421 368 LYS   B CA  
3130 C CA  B LYS   B 162 ? 0.4030 0.4298 0.4290 0.0094  -0.0664 -0.0420 368 LYS   B CA  
3131 C C   . LYS   B 162 ? 0.4119 0.4307 0.4235 0.0088  -0.0659 -0.0372 368 LYS   B C   
3132 O O   . LYS   B 162 ? 0.4010 0.4158 0.4060 0.0089  -0.0711 -0.0348 368 LYS   B O   
3133 C CB  A LYS   B 162 ? 0.4114 0.4414 0.4361 0.0062  -0.0621 -0.0450 368 LYS   B CB  
3134 C CB  B LYS   B 162 ? 0.4161 0.4467 0.4424 0.0065  -0.0633 -0.0453 368 LYS   B CB  
3135 C CG  A LYS   B 162 ? 0.4219 0.4598 0.4582 0.0053  -0.0633 -0.0496 368 LYS   B CG  
3136 C CG  B LYS   B 162 ? 0.4023 0.4413 0.4420 0.0064  -0.0653 -0.0499 368 LYS   B CG  
3137 C CD  A LYS   B 162 ? 0.4640 0.5032 0.4974 0.0017  -0.0584 -0.0513 368 LYS   B CD  
3138 C CD  B LYS   B 162 ? 0.5148 0.5573 0.5547 0.0028  -0.0613 -0.0526 368 LYS   B CD  
3139 C CE  A LYS   B 162 ? 0.5469 0.5930 0.5888 -0.0004 -0.0603 -0.0554 368 LYS   B CE  
3140 C CE  B LYS   B 162 ? 0.5260 0.5776 0.5790 0.0020  -0.0632 -0.0573 368 LYS   B CE  
3141 N NZ  A LYS   B 162 ? 0.5195 0.5744 0.5758 0.0006  -0.0603 -0.0588 368 LYS   B NZ  
3142 N NZ  B LYS   B 162 ? 0.5374 0.5928 0.5915 -0.0022 -0.0581 -0.0595 368 LYS   B NZ  
3143 N N   . LEU   B 163 ? 0.3740 0.3909 0.3808 0.0080  -0.0598 -0.0359 369 LEU   B N   
3144 C CA  . LEU   B 163 ? 0.3551 0.3658 0.3490 0.0072  -0.0585 -0.0319 369 LEU   B CA  
3145 C C   . LEU   B 163 ? 0.4066 0.4129 0.3983 0.0086  -0.0633 -0.0278 369 LEU   B C   
3146 O O   . LEU   B 163 ? 0.4147 0.4165 0.3959 0.0077  -0.0661 -0.0245 369 LEU   B O   
3147 C CB  . LEU   B 163 ? 0.3590 0.3696 0.3510 0.0064  -0.0512 -0.0320 369 LEU   B CB  
3148 C CG  . LEU   B 163 ? 0.4803 0.4869 0.4604 0.0051  -0.0474 -0.0300 369 LEU   B CG  
3149 C CD1 . LEU   B 163 ? 0.4023 0.4085 0.3763 0.0035  -0.0479 -0.0320 369 LEU   B CD1 
3150 C CD2 . LEU   B 163 ? 0.4512 0.4590 0.4335 0.0049  -0.0409 -0.0308 369 LEU   B CD2 
3151 N N   . LYS   B 164 ? 0.4023 0.4098 0.4037 0.0107  -0.0648 -0.0279 370 LYS   B N   
3152 C CA  . LYS   B 164 ? 0.4304 0.4329 0.4307 0.0120  -0.0699 -0.0237 370 LYS   B CA  
3153 C C   . LYS   B 164 ? 0.4354 0.4362 0.4361 0.0129  -0.0785 -0.0226 370 LYS   B C   
3154 O O   . LYS   B 164 ? 0.5180 0.5129 0.5130 0.0129  -0.0834 -0.0179 370 LYS   B O   
3155 C CB  . LYS   B 164 ? 0.4163 0.4206 0.4281 0.0143  -0.0692 -0.0250 370 LYS   B CB  
3156 C CG  . LYS   B 164 ? 0.4629 0.4661 0.4715 0.0134  -0.0623 -0.0238 370 LYS   B CG  
3157 C CD  . LYS   B 164 ? 0.5787 0.5823 0.5974 0.0157  -0.0628 -0.0246 370 LYS   B CD  
3158 C CE  . LYS   B 164 ? 0.5266 0.5239 0.5454 0.0170  -0.0698 -0.0205 370 LYS   B CE  
3159 N NZ  . LYS   B 164 ? 0.7052 0.6963 0.7105 0.0148  -0.0727 -0.0150 370 LYS   B NZ  
3160 N N   . HIS   B 165 ? 0.4365 0.4424 0.4441 0.0134  -0.0808 -0.0268 371 HIS   B N   
3161 C CA  A HIS   B 165 ? 0.4864 0.4911 0.4948 0.0143  -0.0894 -0.0261 371 HIS   B CA  
3162 C CA  B HIS   B 165 ? 0.4864 0.4912 0.4949 0.0143  -0.0894 -0.0262 371 HIS   B CA  
3163 C C   . HIS   B 165 ? 0.4640 0.4651 0.4581 0.0117  -0.0910 -0.0237 371 HIS   B C   
3164 O O   . HIS   B 165 ? 0.5456 0.5453 0.5385 0.0121  -0.0984 -0.0228 371 HIS   B O   
3165 C CB  A HIS   B 165 ? 0.4911 0.5036 0.5140 0.0159  -0.0914 -0.0319 371 HIS   B CB  
3166 C CB  B HIS   B 165 ? 0.4908 0.5035 0.5134 0.0157  -0.0914 -0.0321 371 HIS   B CB  
3167 C CG  A HIS   B 165 ? 0.5213 0.5371 0.5590 0.0191  -0.0930 -0.0343 371 HIS   B CG  
3168 C CG  B HIS   B 165 ? 0.5395 0.5517 0.5669 0.0176  -0.1011 -0.0319 371 HIS   B CG  
3169 N ND1 A HIS   B 165 ? 0.4663 0.4905 0.5161 0.0196  -0.0884 -0.0399 371 HIS   B ND1 
3170 N ND1 B HIS   B 165 ? 0.5916 0.6042 0.6147 0.0164  -0.1052 -0.0325 371 HIS   B ND1 
3171 C CD2 A HIS   B 165 ? 0.4958 0.5075 0.5377 0.0217  -0.0987 -0.0319 371 HIS   B CD2 
3172 C CD2 B HIS   B 165 ? 0.5266 0.5373 0.5627 0.0208  -0.1081 -0.0311 371 HIS   B CD2 
3173 C CE1 A HIS   B 165 ? 0.5325 0.5583 0.5938 0.0228  -0.0910 -0.0416 371 HIS   B CE1 
3174 C CE1 B HIS   B 165 ? 0.5313 0.5431 0.5603 0.0187  -0.1143 -0.0320 371 HIS   B CE1 
3175 N NE2 A HIS   B 165 ? 0.5672 0.5851 0.6244 0.0243  -0.0975 -0.0368 371 HIS   B NE2 
3176 N NE2 B HIS   B 165 ? 0.5023 0.5128 0.5394 0.0215  -0.1163 -0.0311 371 HIS   B NE2 
3177 N N   . LEU   B 166 ? 0.4806 0.4804 0.4640 0.0093  -0.0845 -0.0230 372 LEU   B N   
3178 C CA  . LEU   B 166 ? 0.4521 0.4488 0.4215 0.0069  -0.0857 -0.0213 372 LEU   B CA  
3179 C C   . LEU   B 166 ? 0.5180 0.5082 0.4773 0.0061  -0.0903 -0.0151 372 LEU   B C   
3180 O O   . LEU   B 166 ? 0.5682 0.5554 0.5273 0.0064  -0.0890 -0.0117 372 LEU   B O   
3181 C CB  . LEU   B 166 ? 0.4099 0.4072 0.3716 0.0049  -0.0775 -0.0227 372 LEU   B CB  
3182 C CG  . LEU   B 166 ? 0.4320 0.4344 0.4007 0.0047  -0.0732 -0.0281 372 LEU   B CG  
3183 C CD1 . LEU   B 166 ? 0.3968 0.3983 0.3574 0.0030  -0.0661 -0.0290 372 LEU   B CD1 
3184 C CD2 . LEU   B 166 ? 0.4382 0.4428 0.4090 0.0043  -0.0782 -0.0309 372 LEU   B CD2 
3185 N N   . PRO   B 167 ? 0.5700 0.5577 0.5198 0.0047  -0.0958 -0.0133 373 PRO   B N   
3186 C CA  . PRO   B 167 ? 0.5525 0.5338 0.4921 0.0034  -0.1010 -0.0068 373 PRO   B CA  
3187 C C   . PRO   B 167 ? 0.6705 0.6490 0.5956 0.0002  -0.0955 -0.0033 373 PRO   B C   
3188 O O   . PRO   B 167 ? 0.6938 0.6672 0.6120 -0.0012 -0.0987 0.0027  373 PRO   B O   
3189 C CB  . PRO   B 167 ? 0.5916 0.5722 0.5264 0.0028  -0.1088 -0.0067 373 PRO   B CB  
3190 C CG  . PRO   B 167 ? 0.5421 0.5279 0.4779 0.0024  -0.1049 -0.0126 373 PRO   B CG  
3191 C CD  . PRO   B 167 ? 0.5164 0.5070 0.4653 0.0042  -0.0984 -0.0170 373 PRO   B CD  
3192 N N   . GLU   B 168 ? 0.5543 0.5360 0.4747 -0.0011 -0.0878 -0.0067 374 GLU   B N   
3193 C CA  . GLU   B 168 ? 0.5161 0.4964 0.4230 -0.0040 -0.0825 -0.0043 374 GLU   B CA  
3194 C C   . GLU   B 168 ? 0.4769 0.4602 0.3879 -0.0035 -0.0735 -0.0072 374 GLU   B C   
3195 O O   . GLU   B 168 ? 0.5020 0.4889 0.4219 -0.0018 -0.0706 -0.0122 374 GLU   B O   
3196 C CB  . GLU   B 168 ? 0.5547 0.5357 0.4485 -0.0065 -0.0828 -0.0058 374 GLU   B CB  
3197 C CG  . GLU   B 168 ? 0.6442 0.6226 0.5328 -0.0073 -0.0919 -0.0034 374 GLU   B CG  
3198 C CD  . GLU   B 168 ? 0.6788 0.6518 0.5585 -0.0095 -0.0965 0.0042  374 GLU   B CD  
3199 O OE1 . GLU   B 168 ? 0.9208 0.8906 0.7993 -0.0095 -0.1054 0.0073  374 GLU   B OE1 
3200 O OE2 . GLU   B 168 ? 0.8535 0.8254 0.7274 -0.0115 -0.0914 0.0072  374 GLU   B OE2 
3201 N N   . LYS   B 169 ? 0.4684 0.4503 0.3723 -0.0054 -0.0692 -0.0040 375 LYS   B N   
3202 C CA  . LYS   B 169 ? 0.5410 0.5256 0.4482 -0.0049 -0.0609 -0.0066 375 LYS   B CA  
3203 C C   . LYS   B 169 ? 0.4916 0.4796 0.3954 -0.0052 -0.0564 -0.0121 375 LYS   B C   
3204 O O   . LYS   B 169 ? 0.4493 0.4398 0.3606 -0.0036 -0.0518 -0.0159 375 LYS   B O   
3205 C CB  . LYS   B 169 ? 0.5526 0.5355 0.4526 -0.0072 -0.0573 -0.0023 375 LYS   B CB  
3206 C CG  . LYS   B 169 ? 0.5906 0.5763 0.4966 -0.0061 -0.0497 -0.0049 375 LYS   B CG  
3207 C CD  . LYS   B 169 ? 0.7010 0.6880 0.5975 -0.0088 -0.0437 -0.0037 375 LYS   B CD  
3208 C CE  . LYS   B 169 ? 0.8513 0.8357 0.7466 -0.0106 -0.0437 0.0020  375 LYS   B CE  
3209 N NZ  . LYS   B 169 ? 0.7931 0.7805 0.6821 -0.0127 -0.0365 0.0016  375 LYS   B NZ  
3210 N N   . TYR   B 170 ? 0.4860 0.4739 0.3785 -0.0072 -0.0579 -0.0125 376 TYR   B N   
3211 C CA  A TYR   B 170 ? 0.4892 0.4800 0.3786 -0.0073 -0.0538 -0.0182 376 TYR   B CA  
3212 C CA  B TYR   B 170 ? 0.4893 0.4800 0.3786 -0.0073 -0.0538 -0.0182 376 TYR   B CA  
3213 C C   . TYR   B 170 ? 0.4107 0.4027 0.3104 -0.0052 -0.0555 -0.0227 376 TYR   B C   
3214 O O   . TYR   B 170 ? 0.4404 0.4341 0.3426 -0.0045 -0.0513 -0.0273 376 TYR   B O   
3215 C CB  A TYR   B 170 ? 0.4719 0.4627 0.3468 -0.0099 -0.0553 -0.0184 376 TYR   B CB  
3216 C CB  B TYR   B 170 ? 0.4719 0.4627 0.3468 -0.0099 -0.0553 -0.0184 376 TYR   B CB  
3217 C CG  A TYR   B 170 ? 0.5171 0.5066 0.3898 -0.0101 -0.0629 -0.0187 376 TYR   B CG  
3218 C CG  B TYR   B 170 ? 0.5171 0.5066 0.3898 -0.0101 -0.0629 -0.0186 376 TYR   B CG  
3219 C CD1 A TYR   B 170 ? 0.5002 0.4913 0.3761 -0.0091 -0.0638 -0.0243 376 TYR   B CD1 
3220 C CD1 B TYR   B 170 ? 0.5003 0.4914 0.3761 -0.0091 -0.0638 -0.0243 376 TYR   B CD1 
3221 C CD2 A TYR   B 170 ? 0.5349 0.5214 0.4017 -0.0117 -0.0694 -0.0131 376 TYR   B CD2 
3222 C CD2 B TYR   B 170 ? 0.5349 0.5214 0.4017 -0.0117 -0.0694 -0.0131 376 TYR   B CD2 
3223 C CE1 A TYR   B 170 ? 0.5064 0.4967 0.3805 -0.0095 -0.0708 -0.0247 376 TYR   B CE1 
3224 C CE1 B TYR   B 170 ? 0.5064 0.4967 0.3805 -0.0095 -0.0708 -0.0247 376 TYR   B CE1 
3225 C CE2 A TYR   B 170 ? 0.5298 0.5153 0.3946 -0.0118 -0.0768 -0.0134 376 TYR   B CE2 
3226 C CE2 B TYR   B 170 ? 0.5298 0.5153 0.3946 -0.0118 -0.0768 -0.0134 376 TYR   B CE2 
3227 C CZ  A TYR   B 170 ? 0.5117 0.4995 0.3803 -0.0107 -0.0773 -0.0194 376 TYR   B CZ  
3228 C CZ  B TYR   B 170 ? 0.5117 0.4995 0.3803 -0.0107 -0.0773 -0.0193 376 TYR   B CZ  
3229 O OH  A TYR   B 170 ? 0.5093 0.4964 0.3763 -0.0109 -0.0848 -0.0199 376 TYR   B OH  
3230 O OH  B TYR   B 170 ? 0.5093 0.4964 0.3763 -0.0109 -0.0848 -0.0198 376 TYR   B OH  
3231 N N   . MET   B 171 ? 0.4464 0.4377 0.3526 -0.0042 -0.0618 -0.0215 377 MET   B N   
3232 C CA  . MET   B 171 ? 0.4419 0.4354 0.3588 -0.0026 -0.0631 -0.0257 377 MET   B CA  
3233 C C   . MET   B 171 ? 0.3699 0.3652 0.2979 -0.0011 -0.0584 -0.0270 377 MET   B C   
3234 O O   . MET   B 171 ? 0.4056 0.4030 0.3393 -0.0008 -0.0560 -0.0310 377 MET   B O   
3235 C CB  . MET   B 171 ? 0.3630 0.3562 0.2848 -0.0019 -0.0711 -0.0243 377 MET   B CB  
3236 C CG  . MET   B 171 ? 0.4607 0.4521 0.3715 -0.0035 -0.0767 -0.0236 377 MET   B CG  
3237 S SD  . MET   B 171 ? 0.5732 0.5642 0.4915 -0.0022 -0.0869 -0.0218 377 MET   B SD  
3238 C CE  . MET   B 171 ? 0.4624 0.4580 0.3915 -0.0014 -0.0875 -0.0284 377 MET   B CE  
3239 N N   . MET   B 172 ? 0.3687 0.3631 0.2994 -0.0005 -0.0570 -0.0234 378 MET   B N   
3240 C CA  . MET   B 172 ? 0.4124 0.4086 0.3521 0.0007  -0.0521 -0.0246 378 MET   B CA  
3241 C C   . MET   B 172 ? 0.3628 0.3596 0.2984 0.0001  -0.0455 -0.0270 378 MET   B C   
3242 O O   . MET   B 172 ? 0.3614 0.3599 0.3036 0.0006  -0.0424 -0.0300 378 MET   B O   
3243 C CB  . MET   B 172 ? 0.3952 0.3899 0.3379 0.0015  -0.0522 -0.0205 378 MET   B CB  
3244 C CG  . MET   B 172 ? 0.4215 0.4157 0.3716 0.0029  -0.0589 -0.0188 378 MET   B CG  
3245 S SD  . MET   B 172 ? 0.5042 0.4942 0.4538 0.0032  -0.0605 -0.0131 378 MET   B SD  
3246 C CE  . MET   B 172 ? 0.4730 0.4613 0.4290 0.0049  -0.0705 -0.0115 378 MET   B CE  
3247 N N   . ASN   B 173 ? 0.3303 0.3257 0.2550 -0.0012 -0.0435 -0.0258 379 ASN   B N   
3248 C CA  . ASN   B 173 ? 0.3779 0.3742 0.2991 -0.0014 -0.0377 -0.0288 379 ASN   B CA  
3249 C C   . ASN   B 173 ? 0.3921 0.3888 0.3140 -0.0014 -0.0382 -0.0338 379 ASN   B C   
3250 O O   . ASN   B 173 ? 0.3961 0.3932 0.3218 -0.0008 -0.0345 -0.0367 379 ASN   B O   
3251 C CB  . ASN   B 173 ? 0.3666 0.3626 0.2762 -0.0030 -0.0357 -0.0272 379 ASN   B CB  
3252 C CG  . ASN   B 173 ? 0.4646 0.4606 0.3748 -0.0032 -0.0322 -0.0237 379 ASN   B CG  
3253 O OD1 . ASN   B 173 ? 0.4579 0.4545 0.3766 -0.0018 -0.0297 -0.0241 379 ASN   B OD1 
3254 N ND2 . ASN   B 173 ? 0.4614 0.4568 0.3626 -0.0053 -0.0324 -0.0202 379 ASN   B ND2 
3255 N N   . SER   B 174 ? 0.3454 0.3417 0.2640 -0.0021 -0.0431 -0.0346 380 SER   B N   
3256 C CA  . SER   B 174 ? 0.3539 0.3504 0.2742 -0.0023 -0.0443 -0.0393 380 SER   B CA  
3257 C C   . SER   B 174 ? 0.3647 0.3623 0.2968 -0.0016 -0.0436 -0.0408 380 SER   B C   
3258 O O   . SER   B 174 ? 0.3670 0.3642 0.3014 -0.0018 -0.0410 -0.0440 380 SER   B O   
3259 C CB  . SER   B 174 ? 0.3682 0.3644 0.2847 -0.0031 -0.0507 -0.0394 380 SER   B CB  
3260 O OG  . SER   B 174 ? 0.4250 0.4205 0.3288 -0.0043 -0.0509 -0.0392 380 SER   B OG  
3261 N N   . VAL   B 175 ? 0.2981 0.2973 0.2381 -0.0011 -0.0461 -0.0386 381 VAL   B N   
3262 C CA  . VAL   B 175 ? 0.2971 0.2986 0.2482 -0.0010 -0.0453 -0.0402 381 VAL   B CA  
3263 C C   . VAL   B 175 ? 0.3514 0.3528 0.3051 -0.0007 -0.0394 -0.0402 381 VAL   B C   
3264 O O   . VAL   B 175 ? 0.3423 0.3440 0.3001 -0.0014 -0.0375 -0.0425 381 VAL   B O   
3265 C CB  . VAL   B 175 ? 0.3534 0.3575 0.3127 -0.0002 -0.0491 -0.0385 381 VAL   B CB  
3266 C CG1 . VAL   B 175 ? 0.3609 0.3686 0.3316 -0.0003 -0.0470 -0.0402 381 VAL   B CG1 
3267 C CG2 . VAL   B 175 ? 0.4113 0.4157 0.3695 -0.0006 -0.0555 -0.0393 381 VAL   B CG2 
3268 N N   . LEU   B 176 ? 0.3490 0.3497 0.2998 0.0002  -0.0369 -0.0374 382 LEU   B N   
3269 C CA  . LEU   B 176 ? 0.3775 0.3782 0.3309 0.0006  -0.0317 -0.0374 382 LEU   B CA  
3270 C C   . LEU   B 176 ? 0.3998 0.3986 0.3485 0.0003  -0.0288 -0.0401 382 LEU   B C   
3271 O O   . LEU   B 176 ? 0.3657 0.3642 0.3181 0.0004  -0.0257 -0.0410 382 LEU   B O   
3272 C CB  . LEU   B 176 ? 0.3525 0.3529 0.3038 0.0014  -0.0299 -0.0339 382 LEU   B CB  
3273 C CG  . LEU   B 176 ? 0.3163 0.3182 0.2751 0.0022  -0.0317 -0.0316 382 LEU   B CG  
3274 C CD1 . LEU   B 176 ? 0.3659 0.3666 0.3218 0.0026  -0.0301 -0.0281 382 LEU   B CD1 
3275 C CD2 . LEU   B 176 ? 0.3457 0.3503 0.3139 0.0023  -0.0296 -0.0335 382 LEU   B CD2 
3276 N N   . GLU   B 177 ? 0.3658 0.3632 0.3067 0.0000  -0.0302 -0.0417 383 GLU   B N   
3277 C CA  . GLU   B 177 ? 0.4181 0.4137 0.3551 0.0001  -0.0279 -0.0452 383 GLU   B CA  
3278 C C   . GLU   B 177 ? 0.4277 0.4220 0.3704 -0.0006 -0.0286 -0.0479 383 GLU   B C   
3279 O O   . GLU   B 177 ? 0.4096 0.4018 0.3524 -0.0002 -0.0262 -0.0500 383 GLU   B O   
3280 C CB  . GLU   B 177 ? 0.3966 0.3918 0.3240 -0.0002 -0.0294 -0.0469 383 GLU   B CB  
3281 C CG  . GLU   B 177 ? 0.5376 0.5314 0.4605 0.0003  -0.0271 -0.0512 383 GLU   B CG  
3282 C CD  . GLU   B 177 ? 0.6678 0.6621 0.5808 -0.0003 -0.0288 -0.0533 383 GLU   B CD  
3283 O OE1 . GLU   B 177 ? 0.6697 0.6631 0.5816 -0.0011 -0.0327 -0.0554 383 GLU   B OE1 
3284 O OE2 . GLU   B 177 ? 0.7615 0.7576 0.6678 -0.0003 -0.0261 -0.0529 383 GLU   B OE2 
3285 N N   . ASN   B 178 ? 0.3387 0.3341 0.2866 -0.0018 -0.0318 -0.0478 384 ASN   B N   
3286 C CA  . ASN   B 178 ? 0.3849 0.3793 0.3382 -0.0033 -0.0325 -0.0500 384 ASN   B CA  
3287 C C   . ASN   B 178 ? 0.3965 0.3933 0.3583 -0.0041 -0.0308 -0.0482 384 ASN   B C   
3288 O O   . ASN   B 178 ? 0.3915 0.3883 0.3582 -0.0061 -0.0314 -0.0493 384 ASN   B O   
3289 C CB  . ASN   B 178 ? 0.3516 0.3464 0.3051 -0.0046 -0.0371 -0.0520 384 ASN   B CB  
3290 C CG  . ASN   B 178 ? 0.3930 0.3858 0.3374 -0.0040 -0.0388 -0.0541 384 ASN   B CG  
3291 O OD1 . ASN   B 178 ? 0.4487 0.4385 0.3892 -0.0036 -0.0375 -0.0570 384 ASN   B OD1 
3292 N ND2 . ASN   B 178 ? 0.4058 0.4003 0.3466 -0.0038 -0.0419 -0.0528 384 ASN   B ND2 
3293 N N   . PHE   B 179 ? 0.3361 0.3349 0.2994 -0.0029 -0.0287 -0.0455 385 PHE   B N   
3294 C CA  . PHE   B 179 ? 0.3326 0.3341 0.3032 -0.0035 -0.0266 -0.0441 385 PHE   B CA  
3295 C C   . PHE   B 179 ? 0.3325 0.3320 0.3017 -0.0027 -0.0226 -0.0433 385 PHE   B C   
3296 O O   . PHE   B 179 ? 0.3844 0.3829 0.3491 -0.0010 -0.0209 -0.0423 385 PHE   B O   
3297 C CB  . PHE   B 179 ? 0.3141 0.3192 0.2880 -0.0023 -0.0277 -0.0421 385 PHE   B CB  
3298 C CG  . PHE   B 179 ? 0.3776 0.3860 0.3587 -0.0025 -0.0253 -0.0411 385 PHE   B CG  
3299 C CD1 . PHE   B 179 ? 0.3881 0.4006 0.3768 -0.0042 -0.0259 -0.0425 385 PHE   B CD1 
3300 C CD2 . PHE   B 179 ? 0.3778 0.3857 0.3580 -0.0011 -0.0223 -0.0392 385 PHE   B CD2 
3301 C CE1 . PHE   B 179 ? 0.3698 0.3861 0.3647 -0.0045 -0.0235 -0.0422 385 PHE   B CE1 
3302 C CE2 . PHE   B 179 ? 0.3558 0.3669 0.3423 -0.0013 -0.0202 -0.0388 385 PHE   B CE2 
3303 C CZ  . PHE   B 179 ? 0.3840 0.3994 0.3776 -0.0030 -0.0207 -0.0404 385 PHE   B CZ  
3304 N N   . THR   B 180 ? 0.2974 0.2964 0.2703 -0.0044 -0.0212 -0.0437 386 THR   B N   
3305 C CA  . THR   B 180 ? 0.2888 0.2858 0.2608 -0.0037 -0.0180 -0.0428 386 THR   B CA  
3306 C C   . THR   B 180 ? 0.3169 0.3162 0.2946 -0.0056 -0.0164 -0.0416 386 THR   B C   
3307 O O   . THR   B 180 ? 0.3430 0.3451 0.3252 -0.0080 -0.0175 -0.0421 386 THR   B O   
3308 C CB  . THR   B 180 ? 0.3074 0.2990 0.2755 -0.0036 -0.0182 -0.0448 386 THR   B CB  
3309 O OG1 . THR   B 180 ? 0.3487 0.3387 0.3193 -0.0063 -0.0203 -0.0458 386 THR   B OG1 
3310 C CG2 . THR   B 180 ? 0.3504 0.3404 0.3123 -0.0016 -0.0191 -0.0467 386 THR   B CG2 
3311 N N   . ILE   B 181 ? 0.3022 0.3009 0.2798 -0.0047 -0.0137 -0.0403 387 ILE   B N   
3312 C CA  . ILE   B 181 ? 0.2476 0.2485 0.2294 -0.0067 -0.0120 -0.0391 387 ILE   B CA  
3313 C C   . ILE   B 181 ? 0.2903 0.2867 0.2697 -0.0068 -0.0109 -0.0386 387 ILE   B C   
3314 O O   . ILE   B 181 ? 0.3225 0.3166 0.2989 -0.0043 -0.0100 -0.0386 387 ILE   B O   
3315 C CB  . ILE   B 181 ? 0.2519 0.2576 0.2371 -0.0055 -0.0102 -0.0380 387 ILE   B CB  
3316 C CG1 . ILE   B 181 ? 0.2814 0.2912 0.2701 -0.0053 -0.0121 -0.0388 387 ILE   B CG1 
3317 C CG2 . ILE   B 181 ? 0.2638 0.2718 0.2523 -0.0077 -0.0080 -0.0372 387 ILE   B CG2 
3318 C CD1 . ILE   B 181 ? 0.3042 0.3182 0.2972 -0.0039 -0.0112 -0.0382 387 ILE   B CD1 
3319 N N   . LEU   B 182 ? 0.3167 0.3119 0.2975 -0.0100 -0.0112 -0.0380 388 LEU   B N   
3320 C CA  . LEU   B 182 ? 0.3358 0.3262 0.3147 -0.0103 -0.0110 -0.0370 388 LEU   B CA  
3321 C C   . LEU   B 182 ? 0.3359 0.3296 0.3171 -0.0122 -0.0089 -0.0350 388 LEU   B C   
3322 O O   . LEU   B 182 ? 0.3779 0.3752 0.3616 -0.0158 -0.0086 -0.0345 388 LEU   B O   
3323 C CB  . LEU   B 182 ? 0.3426 0.3275 0.3203 -0.0128 -0.0137 -0.0375 388 LEU   B CB  
3324 C CG  . LEU   B 182 ? 0.3849 0.3635 0.3608 -0.0127 -0.0146 -0.0364 388 LEU   B CG  
3325 C CD1 . LEU   B 182 ? 0.3744 0.3502 0.3481 -0.0080 -0.0144 -0.0383 388 LEU   B CD1 
3326 C CD2 . LEU   B 182 ? 0.3991 0.3718 0.3744 -0.0162 -0.0178 -0.0363 388 LEU   B CD2 
3327 N N   A LEU   B 183 ? 0.3483 0.3414 0.3286 -0.0100 -0.0073 -0.0341 389 LEU   B N   
3328 N N   B LEU   B 183 ? 0.3530 0.3463 0.3333 -0.0099 -0.0073 -0.0341 389 LEU   B N   
3329 C CA  A LEU   B 183 ? 0.3723 0.3682 0.3539 -0.0114 -0.0054 -0.0324 389 LEU   B CA  
3330 C CA  B LEU   B 183 ? 0.3645 0.3605 0.3462 -0.0114 -0.0054 -0.0324 389 LEU   B CA  
3331 C C   A LEU   B 183 ? 0.3820 0.3722 0.3611 -0.0123 -0.0065 -0.0308 389 LEU   B C   
3332 C C   B LEU   B 183 ? 0.3762 0.3662 0.3553 -0.0124 -0.0067 -0.0309 389 LEU   B C   
3333 O O   A LEU   B 183 ? 0.4000 0.3858 0.3775 -0.0094 -0.0074 -0.0313 389 LEU   B O   
3334 O O   B LEU   B 183 ? 0.3974 0.3826 0.3747 -0.0096 -0.0077 -0.0315 389 LEU   B O   
3335 C CB  A LEU   B 183 ? 0.3911 0.3906 0.3740 -0.0083 -0.0033 -0.0325 389 LEU   B CB  
3336 C CB  B LEU   B 183 ? 0.3913 0.3906 0.3741 -0.0084 -0.0032 -0.0324 389 LEU   B CB  
3337 C CG  A LEU   B 183 ? 0.4177 0.4198 0.4018 -0.0089 -0.0014 -0.0313 389 LEU   B CG  
3338 C CG  B LEU   B 183 ? 0.4256 0.4297 0.4110 -0.0068 -0.0026 -0.0335 389 LEU   B CG  
3339 C CD1 A LEU   B 183 ? 0.3987 0.4052 0.3848 -0.0129 -0.0007 -0.0311 389 LEU   B CD1 
3340 C CD1 B LEU   B 183 ? 0.4074 0.4117 0.3923 -0.0035 -0.0013 -0.0332 389 LEU   B CD1 
3341 C CD2 A LEU   B 183 ? 0.4184 0.4239 0.4044 -0.0059 0.0003  -0.0317 389 LEU   B CD2 
3342 C CD2 B LEU   B 183 ? 0.4296 0.4399 0.4194 -0.0090 -0.0017 -0.0339 389 LEU   B CD2 
3343 N N   . VAL   B 184 ? 0.3489 0.3393 0.3278 -0.0166 -0.0068 -0.0290 390 VAL   B N   
3344 C CA  . VAL   B 184 ? 0.3916 0.3759 0.3677 -0.0181 -0.0086 -0.0268 390 VAL   B CA  
3345 C C   . VAL   B 184 ? 0.3979 0.3862 0.3738 -0.0207 -0.0068 -0.0248 390 VAL   B C   
3346 O O   . VAL   B 184 ? 0.3495 0.3434 0.3265 -0.0246 -0.0052 -0.0246 390 VAL   B O   
3347 C CB  . VAL   B 184 ? 0.3621 0.3407 0.3366 -0.0217 -0.0117 -0.0259 390 VAL   B CB  
3348 C CG1 . VAL   B 184 ? 0.3973 0.3687 0.3690 -0.0230 -0.0143 -0.0233 390 VAL   B CG1 
3349 C CG2 . VAL   B 184 ? 0.3720 0.3470 0.3468 -0.0190 -0.0136 -0.0286 390 VAL   B CG2 
3350 N N   . VAL   B 185 ? 0.3718 0.3579 0.3465 -0.0187 -0.0069 -0.0238 391 VAL   B N   
3351 C CA  . VAL   B 185 ? 0.3553 0.3444 0.3290 -0.0212 -0.0056 -0.0218 391 VAL   B CA  
3352 C C   . VAL   B 185 ? 0.4074 0.3891 0.3773 -0.0235 -0.0090 -0.0188 391 VAL   B C   
3353 O O   . VAL   B 185 ? 0.3781 0.3532 0.3475 -0.0202 -0.0116 -0.0188 391 VAL   B O   
3354 C CB  . VAL   B 185 ? 0.4064 0.3992 0.3819 -0.0174 -0.0035 -0.0229 391 VAL   B CB  
3355 C CG1 . VAL   B 185 ? 0.3806 0.3776 0.3549 -0.0204 -0.0021 -0.0215 391 VAL   B CG1 
3356 C CG2 . VAL   B 185 ? 0.3585 0.3566 0.3376 -0.0146 -0.0012 -0.0256 391 VAL   B CG2 
3357 N N   . THR   B 186 ? 0.3914 0.3742 0.3585 -0.0292 -0.0091 -0.0163 392 THR   B N   
3358 C CA  A THR   B 186 ? 0.4045 0.3799 0.3672 -0.0328 -0.0128 -0.0125 392 THR   B CA  
3359 C CA  B THR   B 186 ? 0.4067 0.3819 0.3695 -0.0324 -0.0128 -0.0126 392 THR   B CA  
3360 C C   . THR   B 186 ? 0.4201 0.3987 0.3795 -0.0360 -0.0118 -0.0101 392 THR   B C   
3361 O O   . THR   B 186 ? 0.3613 0.3488 0.3216 -0.0380 -0.0080 -0.0113 392 THR   B O   
3362 C CB  A THR   B 186 ? 0.3996 0.3729 0.3608 -0.0383 -0.0141 -0.0112 392 THR   B CB  
3363 C CB  B THR   B 186 ? 0.4086 0.3798 0.3695 -0.0374 -0.0150 -0.0109 392 THR   B CB  
3364 O OG1 A THR   B 186 ? 0.3841 0.3554 0.3484 -0.0352 -0.0149 -0.0139 392 THR   B OG1 
3365 O OG1 B THR   B 186 ? 0.4363 0.4158 0.3971 -0.0428 -0.0118 -0.0108 392 THR   B OG1 
3366 C CG2 A THR   B 186 ? 0.4597 0.4239 0.4161 -0.0424 -0.0187 -0.0067 392 THR   B CG2 
3367 C CG2 B THR   B 186 ? 0.4129 0.3811 0.3769 -0.0341 -0.0161 -0.0138 392 THR   B CG2 
3368 N N   . ASN   B 187 ? 0.3890 0.3603 0.3449 -0.0365 -0.0156 -0.0069 393 ASN   B N   
3369 C CA  . ASN   B 187 ? 0.4181 0.3912 0.3693 -0.0406 -0.0156 -0.0038 393 ASN   B CA  
3370 C C   . ASN   B 187 ? 0.4720 0.4459 0.4188 -0.0487 -0.0156 -0.0009 393 ASN   B C   
3371 O O   . ASN   B 187 ? 0.5081 0.4737 0.4525 -0.0515 -0.0196 0.0020  393 ASN   B O   
3372 C CB  . ASN   B 187 ? 0.4511 0.4153 0.4000 -0.0385 -0.0206 -0.0011 393 ASN   B CB  
3373 C CG  . ASN   B 187 ? 0.5382 0.5036 0.4814 -0.0429 -0.0214 0.0024  393 ASN   B CG  
3374 O OD1 . ASN   B 187 ? 0.4907 0.4605 0.4296 -0.0494 -0.0195 0.0043  393 ASN   B OD1 
3375 N ND2 . ASN   B 187 ? 0.4913 0.4530 0.4345 -0.0393 -0.0242 0.0031  393 ASN   B ND2 
3376 N N   . ARG   B 188 ? 0.4572 0.4415 0.4037 -0.0525 -0.0110 -0.0021 394 ARG   B N   
3377 C CA  . ARG   B 188 ? 0.5137 0.5008 0.4571 -0.0604 -0.0101 -0.0002 394 ARG   B CA  
3378 C C   . ARG   B 188 ? 0.5615 0.5412 0.4969 -0.0667 -0.0142 0.0059  394 ARG   B C   
3379 O O   . ARG   B 188 ? 0.6281 0.6049 0.5608 -0.0727 -0.0157 0.0087  394 ARG   B O   
3380 C CB  . ARG   B 188 ? 0.4765 0.4772 0.4216 -0.0630 -0.0043 -0.0033 394 ARG   B CB  
3381 C CG  . ARG   B 188 ? 0.5711 0.5774 0.5143 -0.0712 -0.0023 -0.0023 394 ARG   B CG  
3382 C CD  . ARG   B 188 ? 0.6130 0.6331 0.5575 -0.0736 0.0032  -0.0057 394 ARG   B CD  
3383 N NE  . ARG   B 188 ? 0.7718 0.8004 0.7177 -0.0799 0.0063  -0.0070 394 ARG   B NE  
3384 C CZ  . ARG   B 188 ? 0.9991 1.0402 0.9453 -0.0841 0.0110  -0.0098 394 ARG   B CZ  
3385 N NH1 . ARG   B 188 ? 0.8789 0.9254 0.8240 -0.0825 0.0132  -0.0117 394 ARG   B NH1 
3386 N NH2 . ARG   B 188 ? 1.0577 1.1068 1.0057 -0.0901 0.0137  -0.0110 394 ARG   B NH2 
3387 N N   . ASP   B 189 ? 0.5165 0.4926 0.4480 -0.0656 -0.0165 0.0083  395 ASP   B N   
3388 C CA  . ASP   B 189 ? 0.6041 0.5731 0.5272 -0.0720 -0.0208 0.0145  395 ASP   B CA  
3389 C C   . ASP   B 189 ? 0.6576 0.6119 0.5801 -0.0705 -0.0279 0.0179  395 ASP   B C   
3390 O O   . ASP   B 189 ? 0.6462 0.5937 0.5628 -0.0772 -0.0316 0.0230  395 ASP   B O   
3391 C CB  . ASP   B 189 ? 0.5903 0.5613 0.5092 -0.0717 -0.0211 0.0158  395 ASP   B CB  
3392 C CG  . ASP   B 189 ? 0.8017 0.7871 0.7207 -0.0741 -0.0144 0.0124  395 ASP   B CG  
3393 O OD1 . ASP   B 189 ? 0.7673 0.7598 0.6848 -0.0804 -0.0109 0.0121  395 ASP   B OD1 
3394 O OD2 . ASP   B 189 ? 0.8111 0.8010 0.7320 -0.0696 -0.0128 0.0096  395 ASP   B OD2 
3395 N N   . THR   B 190 ? 0.6052 0.5544 0.5335 -0.0622 -0.0299 0.0149  396 THR   B N   
3396 C CA  . THR   B 190 ? 0.5701 0.5059 0.4990 -0.0599 -0.0367 0.0170  396 THR   B CA  
3397 C C   . THR   B 190 ? 0.6228 0.5560 0.5569 -0.0576 -0.0367 0.0138  396 THR   B C   
3398 O O   . THR   B 190 ? 0.6362 0.5582 0.5710 -0.0561 -0.0424 0.0150  396 THR   B O   
3399 C CB  . THR   B 190 ? 0.6057 0.5370 0.5377 -0.0521 -0.0397 0.0155  396 THR   B CB  
3400 O OG1 . THR   B 190 ? 0.6517 0.5895 0.5910 -0.0451 -0.0354 0.0094  396 THR   B OG1 
3401 C CG2 . THR   B 190 ? 0.5916 0.5261 0.5192 -0.0537 -0.0396 0.0179  396 THR   B CG2 
3402 N N   . GLN   B 191 ? 0.5638 0.5068 0.5019 -0.0567 -0.0310 0.0096  397 GLN   B N   
3403 C CA  . GLN   B 191 ? 0.5969 0.5393 0.5400 -0.0541 -0.0305 0.0060  397 GLN   B CA  
3404 C C   . GLN   B 191 ? 0.5257 0.4629 0.4737 -0.0455 -0.0326 0.0023  397 GLN   B C   
3405 O O   . GLN   B 191 ? 0.5752 0.5097 0.5265 -0.0432 -0.0334 -0.0004 397 GLN   B O   
3406 C CB  . GLN   B 191 ? 0.6096 0.5449 0.5501 -0.0605 -0.0340 0.0092  397 GLN   B CB  
3407 C CG  . GLN   B 191 ? 0.5981 0.5416 0.5352 -0.0691 -0.0303 0.0113  397 GLN   B CG  
3408 C CD  . GLN   B 191 ? 0.7430 0.6989 0.6854 -0.0677 -0.0242 0.0062  397 GLN   B CD  
3409 O OE1 . GLN   B 191 ? 0.8799 0.8352 0.8271 -0.0641 -0.0242 0.0028  397 GLN   B OE1 
3410 N NE2 . GLN   B 191 ? 0.6435 0.6108 0.5853 -0.0701 -0.0191 0.0054  397 GLN   B NE2 
3411 N N   . GLU   B 192 ? 0.4926 0.4293 0.4413 -0.0407 -0.0332 0.0019  398 GLU   B N   
3412 C CA  . GLU   B 192 ? 0.5663 0.5003 0.5202 -0.0327 -0.0343 -0.0021 398 GLU   B CA  
3413 C C   . GLU   B 192 ? 0.4953 0.4386 0.4535 -0.0288 -0.0287 -0.0070 398 GLU   B C   
3414 O O   . GLU   B 192 ? 0.4487 0.4012 0.4069 -0.0299 -0.0241 -0.0076 398 GLU   B O   
3415 C CB  . GLU   B 192 ? 0.5156 0.4475 0.4695 -0.0293 -0.0364 -0.0012 398 GLU   B CB  
3416 C CG  . GLU   B 192 ? 0.7700 0.6904 0.7207 -0.0314 -0.0436 0.0031  398 GLU   B CG  
3417 C CD  . GLU   B 192 ? 0.9979 0.9160 0.9503 -0.0267 -0.0464 0.0030  398 GLU   B CD  
3418 O OE1 . GLU   B 192 ? 1.0336 0.9593 0.9899 -0.0219 -0.0425 -0.0006 398 GLU   B OE1 
3419 O OE2 . GLU   B 192 ? 1.0908 0.9994 1.0408 -0.0280 -0.0529 0.0068  398 GLU   B OE2 
3420 N N   . THR   B 193 ? 0.4586 0.3995 0.4205 -0.0241 -0.0294 -0.0108 399 THR   B N   
3421 C CA  . THR   B 193 ? 0.4349 0.3836 0.4002 -0.0202 -0.0248 -0.0150 399 THR   B CA  
3422 C C   . THR   B 193 ? 0.3960 0.3485 0.3635 -0.0154 -0.0229 -0.0165 399 THR   B C   
3423 O O   . THR   B 193 ? 0.4586 0.4060 0.4274 -0.0117 -0.0259 -0.0171 399 THR   B O   
3424 C CB  . THR   B 193 ? 0.4304 0.3755 0.3980 -0.0171 -0.0262 -0.0186 399 THR   B CB  
3425 O OG1 . THR   B 193 ? 0.4836 0.4256 0.4496 -0.0219 -0.0278 -0.0173 399 THR   B OG1 
3426 C CG2 . THR   B 193 ? 0.4000 0.3527 0.3702 -0.0133 -0.0218 -0.0224 399 THR   B CG2 
3427 N N   . LEU   B 194 ? 0.3916 0.3530 0.3599 -0.0154 -0.0183 -0.0172 400 LEU   B N   
3428 C CA  . LEU   B 194 ? 0.3550 0.3204 0.3255 -0.0114 -0.0163 -0.0186 400 LEU   B CA  
3429 C C   . LEU   B 194 ? 0.4061 0.3751 0.3800 -0.0067 -0.0138 -0.0224 400 LEU   B C   
3430 O O   . LEU   B 194 ? 0.3693 0.3386 0.3456 -0.0025 -0.0136 -0.0241 400 LEU   B O   
3431 C CB  . LEU   B 194 ? 0.3715 0.3442 0.3410 -0.0143 -0.0131 -0.0172 400 LEU   B CB  
3432 C CG  . LEU   B 194 ? 0.3915 0.3623 0.3567 -0.0193 -0.0150 -0.0134 400 LEU   B CG  
3433 C CD1 . LEU   B 194 ? 0.3626 0.3420 0.3270 -0.0223 -0.0112 -0.0132 400 LEU   B CD1 
3434 C CD2 . LEU   B 194 ? 0.4365 0.4016 0.4010 -0.0172 -0.0188 -0.0118 400 LEU   B CD2 
3435 N N   . LEU   B 195 ? 0.3267 0.2987 0.3009 -0.0077 -0.0119 -0.0238 401 LEU   B N   
3436 C CA  . LEU   B 195 ? 0.3508 0.3264 0.3270 -0.0041 -0.0095 -0.0268 401 LEU   B CA  
3437 C C   . LEU   B 195 ? 0.3470 0.3223 0.3226 -0.0056 -0.0098 -0.0279 401 LEU   B C   
3438 O O   . LEU   B 195 ? 0.3367 0.3139 0.3116 -0.0096 -0.0095 -0.0265 401 LEU   B O   
3439 C CB  . LEU   B 195 ? 0.3294 0.3125 0.3072 -0.0035 -0.0058 -0.0270 401 LEU   B CB  
3440 C CG  . LEU   B 195 ? 0.3759 0.3629 0.3553 -0.0006 -0.0034 -0.0292 401 LEU   B CG  
3441 C CD1 . LEU   B 195 ? 0.3637 0.3487 0.3436 0.0033  -0.0038 -0.0313 401 LEU   B CD1 
3442 C CD2 . LEU   B 195 ? 0.3690 0.3621 0.3503 -0.0006 -0.0006 -0.0288 401 LEU   B CD2 
3443 N N   . CYS   B 196 ? 0.3298 0.3035 0.3057 -0.0026 -0.0102 -0.0307 402 CYS   B N   
3444 C CA  . CYS   B 196 ? 0.3745 0.3484 0.3497 -0.0036 -0.0106 -0.0321 402 CYS   B CA  
3445 C C   . CYS   B 196 ? 0.3838 0.3613 0.3592 -0.0002 -0.0085 -0.0347 402 CYS   B C   
3446 O O   . CYS   B 196 ? 0.3470 0.3235 0.3226 0.0032  -0.0083 -0.0367 402 CYS   B O   
3447 C CB  . CYS   B 196 ? 0.3568 0.3232 0.3309 -0.0045 -0.0144 -0.0328 402 CYS   B CB  
3448 S SG  . CYS   B 196 ? 0.3862 0.3528 0.3597 -0.0052 -0.0151 -0.0354 402 CYS   B SG  
3449 N N   . MET   B 197 ? 0.3358 0.3182 0.3116 -0.0012 -0.0069 -0.0346 403 MET   B N   
3450 C CA  . MET   B 197 ? 0.3654 0.3511 0.3406 0.0012  -0.0053 -0.0362 403 MET   B CA  
3451 C C   . MET   B 197 ? 0.3644 0.3501 0.3384 0.0001  -0.0067 -0.0374 403 MET   B C   
3452 O O   . MET   B 197 ? 0.3355 0.3236 0.3111 -0.0024 -0.0070 -0.0364 403 MET   B O   
3453 C CB  . MET   B 197 ? 0.3394 0.3307 0.3164 0.0015  -0.0028 -0.0348 403 MET   B CB  
3454 C CG  . MET   B 197 ? 0.5230 0.5149 0.5012 0.0026  -0.0014 -0.0338 403 MET   B CG  
3455 S SD  . MET   B 197 ? 0.5403 0.5382 0.5211 0.0025  0.0011  -0.0324 403 MET   B SD  
3456 C CE  . MET   B 197 ? 0.3751 0.3747 0.3546 0.0032  0.0009  -0.0333 403 MET   B CE  
3457 N N   . ALA   B 198 ? 0.3539 0.3374 0.3257 0.0020  -0.0076 -0.0399 404 ALA   B N   
3458 C CA  . ALA   B 198 ? 0.3058 0.2893 0.2757 0.0015  -0.0091 -0.0415 404 ALA   B CA  
3459 C C   . ALA   B 198 ? 0.3713 0.3593 0.3398 0.0028  -0.0074 -0.0414 404 ALA   B C   
3460 O O   . ALA   B 198 ? 0.3580 0.3469 0.3245 0.0051  -0.0058 -0.0423 404 ALA   B O   
3461 C CB  . ALA   B 198 ? 0.2870 0.2656 0.2548 0.0028  -0.0111 -0.0447 404 ALA   B CB  
3462 N N   . CYS   B 199 ? 0.2956 0.2866 0.2652 0.0014  -0.0080 -0.0402 405 CYS   B N   
3463 C CA  . CYS   B 199 ? 0.3061 0.3008 0.2748 0.0024  -0.0071 -0.0392 405 CYS   B CA  
3464 C C   . CYS   B 199 ? 0.3321 0.3268 0.2976 0.0023  -0.0092 -0.0404 405 CYS   B C   
3465 O O   . CYS   B 199 ? 0.3276 0.3219 0.2943 0.0007  -0.0115 -0.0411 405 CYS   B O   
3466 C CB  . CYS   B 199 ? 0.2630 0.2613 0.2363 0.0013  -0.0066 -0.0371 405 CYS   B CB  
3467 S SG  . CYS   B 199 ? 0.3758 0.3745 0.3526 0.0007  -0.0044 -0.0358 405 CYS   B SG  
3468 N N   . VAL   B 200 ? 0.3136 0.3090 0.2746 0.0037  -0.0085 -0.0406 406 VAL   B N   
3469 C CA  . VAL   B 200 ? 0.3075 0.3032 0.2643 0.0035  -0.0106 -0.0413 406 VAL   B CA  
3470 C C   . VAL   B 200 ? 0.3287 0.3269 0.2843 0.0037  -0.0104 -0.0385 406 VAL   B C   
3471 O O   . VAL   B 200 ? 0.2946 0.2941 0.2520 0.0042  -0.0081 -0.0366 406 VAL   B O   
3472 C CB  . VAL   B 200 ? 0.3490 0.3430 0.3001 0.0044  -0.0103 -0.0445 406 VAL   B CB  
3473 C CG1 . VAL   B 200 ? 0.3447 0.3351 0.2976 0.0044  -0.0113 -0.0473 406 VAL   B CG1 
3474 C CG2 . VAL   B 200 ? 0.3329 0.3284 0.2818 0.0059  -0.0069 -0.0445 406 VAL   B CG2 
3475 N N   . PHE   B 201 ? 0.3220 0.3206 0.2747 0.0031  -0.0132 -0.0380 407 PHE   B N   
3476 C CA  . PHE   B 201 ? 0.3447 0.3447 0.2976 0.0030  -0.0144 -0.0349 407 PHE   B CA  
3477 C C   . PHE   B 201 ? 0.3418 0.3414 0.2871 0.0025  -0.0165 -0.0341 407 PHE   B C   
3478 O O   . PHE   B 201 ? 0.3562 0.3550 0.2977 0.0021  -0.0184 -0.0364 407 PHE   B O   
3479 C CB  . PHE   B 201 ? 0.3361 0.3375 0.2960 0.0027  -0.0171 -0.0342 407 PHE   B CB  
3480 C CG  . PHE   B 201 ? 0.3170 0.3196 0.2839 0.0025  -0.0150 -0.0347 407 PHE   B CG  
3481 C CD1 . PHE   B 201 ? 0.2555 0.2577 0.2245 0.0015  -0.0148 -0.0368 407 PHE   B CD1 
3482 C CD2 . PHE   B 201 ? 0.2664 0.2706 0.2372 0.0031  -0.0134 -0.0329 407 PHE   B CD2 
3483 C CE1 . PHE   B 201 ? 0.2600 0.2633 0.2342 0.0008  -0.0129 -0.0368 407 PHE   B CE1 
3484 C CE2 . PHE   B 201 ? 0.2687 0.2744 0.2451 0.0028  -0.0114 -0.0334 407 PHE   B CE2 
3485 C CZ  . PHE   B 201 ? 0.2913 0.2967 0.2689 0.0015  -0.0111 -0.0352 407 PHE   B CZ  
3486 N N   . GLU   B 202 ? 0.3365 0.3365 0.2800 0.0023  -0.0166 -0.0308 408 GLU   B N   
3487 C CA  . GLU   B 202 ? 0.3617 0.3611 0.2974 0.0013  -0.0188 -0.0288 408 GLU   B CA  
3488 C C   . GLU   B 202 ? 0.3980 0.3969 0.3366 0.0011  -0.0209 -0.0245 408 GLU   B C   
3489 O O   . GLU   B 202 ? 0.3452 0.3446 0.2905 0.0019  -0.0193 -0.0237 408 GLU   B O   
3490 C CB  . GLU   B 202 ? 0.3365 0.3368 0.2643 0.0006  -0.0152 -0.0294 408 GLU   B CB  
3491 C CG  . GLU   B 202 ? 0.6109 0.6112 0.5287 -0.0011 -0.0170 -0.0285 408 GLU   B CG  
3492 C CD  . GLU   B 202 ? 0.6797 0.6824 0.5908 -0.0018 -0.0125 -0.0303 408 GLU   B CD  
3493 O OE1 . GLU   B 202 ? 0.7503 0.7538 0.6614 -0.0007 -0.0105 -0.0351 408 GLU   B OE1 
3494 O OE2 . GLU   B 202 ? 0.7879 0.7917 0.6938 -0.0036 -0.0111 -0.0271 408 GLU   B OE2 
3495 N N   . VAL   B 203 ? 0.3637 0.3611 0.2971 0.0001  -0.0248 -0.0218 409 VAL   B N   
3496 C CA  . VAL   B 203 ? 0.4258 0.4215 0.3615 0.0000  -0.0276 -0.0175 409 VAL   B CA  
3497 C C   . VAL   B 203 ? 0.4257 0.4211 0.3562 -0.0015 -0.0245 -0.0144 409 VAL   B C   
3498 O O   . VAL   B 203 ? 0.4206 0.4168 0.3422 -0.0032 -0.0222 -0.0145 409 VAL   B O   
3499 C CB  . VAL   B 203 ? 0.4695 0.4632 0.4021 -0.0006 -0.0340 -0.0154 409 VAL   B CB  
3500 C CG1 . VAL   B 203 ? 0.4789 0.4698 0.4131 -0.0008 -0.0375 -0.0106 409 VAL   B CG1 
3501 C CG2 . VAL   B 203 ? 0.4150 0.4099 0.3546 0.0008  -0.0371 -0.0186 409 VAL   B CG2 
3502 N N   . SER   B 204 ? 0.3550 0.3495 0.2912 -0.0011 -0.0242 -0.0119 410 SER   B N   
3503 C CA  . SER   B 204 ? 0.4124 0.4065 0.3444 -0.0030 -0.0215 -0.0087 410 SER   B CA  
3504 C C   . SER   B 204 ? 0.4878 0.4795 0.4100 -0.0058 -0.0246 -0.0042 410 SER   B C   
3505 O O   . SER   B 204 ? 0.5128 0.5018 0.4338 -0.0058 -0.0303 -0.0024 410 SER   B O   
3506 C CB  . SER   B 204 ? 0.4824 0.4754 0.4229 -0.0020 -0.0216 -0.0069 410 SER   B CB  
3507 O OG  . SER   B 204 ? 0.5387 0.5286 0.4833 -0.0013 -0.0276 -0.0048 410 SER   B OG  
3508 N N   . ASN   B 205 ? 0.4915 0.4845 0.4068 -0.0084 -0.0209 -0.0025 411 ASN   B N   
3509 C CA  . ASN   B 205 ? 0.7426 0.7339 0.6470 -0.0120 -0.0230 0.0020  411 ASN   B CA  
3510 C C   . ASN   B 205 ? 0.8634 0.8511 0.7675 -0.0142 -0.0250 0.0080  411 ASN   B C   
3511 O O   . ASN   B 205 ? 0.8376 0.8264 0.7458 -0.0145 -0.0213 0.0084  411 ASN   B O   
3512 C CB  . ASN   B 205 ? 0.7482 0.7441 0.6435 -0.0142 -0.0176 -0.0002 411 ASN   B CB  
3513 C CG  . ASN   B 205 ? 0.7989 0.7974 0.6930 -0.0123 -0.0166 -0.0061 411 ASN   B CG  
3514 O OD1 . ASN   B 205 ? 0.7651 0.7673 0.6606 -0.0111 -0.0116 -0.0106 411 ASN   B OD1 
3515 N ND2 . ASN   B 205 ? 0.7787 0.7748 0.6703 -0.0119 -0.0218 -0.0060 411 ASN   B ND2 
3516 N N   . SER   B 206 ? 0.9513 0.9343 0.8508 -0.0159 -0.0313 0.0127  412 SER   B N   
3517 C CA  . SER   B 206 ? 1.0297 1.0076 0.9280 -0.0185 -0.0349 0.0193  412 SER   B CA  
3518 C C   . SER   B 206 ? 1.0999 1.0762 1.0109 -0.0159 -0.0349 0.0190  412 SER   B C   
3519 O O   . SER   B 206 ? 0.9590 0.9348 0.8799 -0.0119 -0.0374 0.0159  412 SER   B O   
3520 C CB  . SER   B 206 ? 1.1139 1.0936 1.0010 -0.0237 -0.0308 0.0227  412 SER   B CB  
3521 O OG  . SER   B 206 ? 1.2439 1.2177 1.1248 -0.0275 -0.0361 0.0302  412 SER   B OG  
3522 N N   . GLU   B 207 ? 1.0519 1.0278 0.9628 -0.0183 -0.0320 0.0219  413 GLU   B N   
3523 C CA  . GLU   B 207 ? 1.0046 0.9789 0.9268 -0.0162 -0.0319 0.0215  413 GLU   B CA  
3524 C C   . GLU   B 207 ? 0.9216 0.9019 0.8481 -0.0152 -0.0242 0.0171  413 GLU   B C   
3525 O O   . GLU   B 207 ? 0.8663 0.8460 0.7993 -0.0151 -0.0229 0.0176  413 GLU   B O   
3526 C CB  . GLU   B 207 ? 0.9759 0.9442 0.8965 -0.0195 -0.0355 0.0282  413 GLU   B CB  
3527 C CG  . GLU   B 207 ? 1.0119 0.9729 0.9321 -0.0193 -0.0446 0.0324  413 GLU   B CG  
3528 C CD  . GLU   B 207 ? 0.9996 0.9595 0.9328 -0.0138 -0.0487 0.0283  413 GLU   B CD  
3529 O OE1 . GLU   B 207 ? 0.9722 0.9334 0.9158 -0.0113 -0.0464 0.0252  413 GLU   B OE1 
3530 O OE2 . GLU   B 207 ? 1.0039 0.9621 0.9369 -0.0121 -0.0540 0.0279  413 GLU   B OE2 
3531 N N   . HIS   B 208 ? 0.8280 0.8137 0.7512 -0.0145 -0.0197 0.0127  414 HIS   B N   
3532 C CA  . HIS   B 208 ? 0.8640 0.8548 0.7918 -0.0131 -0.0133 0.0084  414 HIS   B CA  
3533 C C   . HIS   B 208 ? 0.7298 0.7210 0.6689 -0.0088 -0.0136 0.0043  414 HIS   B C   
3534 O O   . HIS   B 208 ? 0.7720 0.7659 0.7165 -0.0077 -0.0096 0.0018  414 HIS   B O   
3535 C CB  . HIS   B 208 ? 0.7070 0.7030 0.6277 -0.0138 -0.0088 0.0049  414 HIS   B CB  
3536 C CG  . HIS   B 208 ? 0.8964 0.8938 0.8060 -0.0185 -0.0071 0.0083  414 HIS   B CG  
3537 N ND1 . HIS   B 208 ? 0.9938 0.9904 0.8933 -0.0206 -0.0096 0.0098  414 HIS   B ND1 
3538 C CD2 . HIS   B 208 ? 0.8607 0.8607 0.7676 -0.0219 -0.0032 0.0104  414 HIS   B CD2 
3539 C CE1 . HIS   B 208 ? 0.9379 0.9366 0.8283 -0.0253 -0.0072 0.0128  414 HIS   B CE1 
3540 N NE2 . HIS   B 208 ? 0.9394 0.9404 0.8343 -0.0262 -0.0031 0.0132  414 HIS   B NE2 
3541 N N   . GLY   B 209 ? 0.5962 0.5849 0.5388 -0.0066 -0.0184 0.0035  415 GLY   B N   
3542 C CA  . GLY   B 209 ? 0.6005 0.5902 0.5536 -0.0032 -0.0188 -0.0002 415 GLY   B CA  
3543 C C   . GLY   B 209 ? 0.4479 0.4419 0.4021 -0.0016 -0.0146 -0.0052 415 GLY   B C   
3544 O O   . GLY   B 209 ? 0.4047 0.4008 0.3522 -0.0026 -0.0119 -0.0064 415 GLY   B O   
3545 N N   . ALA   B 210 ? 0.4025 0.3979 0.3655 0.0008  -0.0144 -0.0082 416 ALA   B N   
3546 C CA  . ALA   B 210 ? 0.3338 0.3324 0.2984 0.0021  -0.0113 -0.0125 416 ALA   B CA  
3547 C C   . ALA   B 210 ? 0.3522 0.3531 0.3150 0.0015  -0.0061 -0.0134 416 ALA   B C   
3548 O O   . ALA   B 210 ? 0.3403 0.3412 0.3049 0.0008  -0.0046 -0.0117 416 ALA   B O   
3549 C CB  . ALA   B 210 ? 0.2771 0.2770 0.2511 0.0041  -0.0122 -0.0152 416 ALA   B CB  
3550 N N   . GLN   B 211 ? 0.2869 0.2896 0.2466 0.0019  -0.0037 -0.0163 417 GLN   B N   
3551 C CA  . GLN   B 211 ? 0.3101 0.3152 0.2686 0.0019  0.0008  -0.0179 417 GLN   B CA  
3552 C C   . GLN   B 211 ? 0.3690 0.3750 0.3286 0.0033  0.0018  -0.0218 417 GLN   B C   
3553 O O   . GLN   B 211 ? 0.3415 0.3464 0.3014 0.0038  -0.0007 -0.0230 417 GLN   B O   
3554 C CB  . GLN   B 211 ? 0.3841 0.3905 0.3348 -0.0001 0.0026  -0.0166 417 GLN   B CB  
3555 C CG  . GLN   B 211 ? 0.4384 0.4436 0.3876 -0.0024 0.0020  -0.0121 417 GLN   B CG  
3556 C CD  . GLN   B 211 ? 0.4949 0.5023 0.4358 -0.0052 0.0043  -0.0107 417 GLN   B CD  
3557 O OE1 . GLN   B 211 ? 0.5296 0.5405 0.4674 -0.0050 0.0076  -0.0140 417 GLN   B OE1 
3558 N NE2 . GLN   B 211 ? 0.5932 0.5985 0.5304 -0.0080 0.0025  -0.0060 417 GLN   B NE2 
3559 N N   . HIS   B 212 ? 0.3256 0.3334 0.2860 0.0040  0.0051  -0.0239 418 HIS   B N   
3560 C CA  . HIS   B 212 ? 0.3225 0.3301 0.2834 0.0053  0.0055  -0.0274 418 HIS   B CA  
3561 C C   . HIS   B 212 ? 0.3557 0.3654 0.3143 0.0058  0.0086  -0.0297 418 HIS   B C   
3562 O O   . HIS   B 212 ? 0.3410 0.3531 0.2996 0.0053  0.0110  -0.0288 418 HIS   B O   
3563 C CB  . HIS   B 212 ? 0.2552 0.2622 0.2226 0.0061  0.0051  -0.0281 418 HIS   B CB  
3564 C CG  . HIS   B 212 ? 0.3099 0.3184 0.2810 0.0066  0.0074  -0.0280 418 HIS   B CG  
3565 N ND1 . HIS   B 212 ? 0.3038 0.3133 0.2768 0.0061  0.0082  -0.0258 418 HIS   B ND1 
3566 C CD2 . HIS   B 212 ? 0.2869 0.2955 0.2604 0.0076  0.0087  -0.0299 418 HIS   B CD2 
3567 C CE1 . HIS   B 212 ? 0.3090 0.3199 0.2853 0.0067  0.0101  -0.0265 418 HIS   B CE1 
3568 N NE2 . HIS   B 212 ? 0.3301 0.3404 0.3067 0.0077  0.0103  -0.0289 418 HIS   B NE2 
3569 N N   . HIS   B 213 ? 0.3107 0.3196 0.2679 0.0069  0.0083  -0.0330 419 HIS   B N   
3570 C CA  . HIS   B 213 ? 0.3200 0.3309 0.2760 0.0080  0.0108  -0.0364 419 HIS   B CA  
3571 C C   . HIS   B 213 ? 0.3070 0.3155 0.2668 0.0098  0.0098  -0.0392 419 HIS   B C   
3572 O O   . HIS   B 213 ? 0.3358 0.3412 0.2948 0.0097  0.0073  -0.0400 419 HIS   B O   
3573 C CB  . HIS   B 213 ? 0.3595 0.3719 0.3085 0.0073  0.0113  -0.0382 419 HIS   B CB  
3574 C CG  . HIS   B 213 ? 0.4558 0.4723 0.4037 0.0081  0.0146  -0.0418 419 HIS   B CG  
3575 N ND1 . HIS   B 213 ? 0.5091 0.5300 0.4523 0.0063  0.0173  -0.0412 419 HIS   B ND1 
3576 C CD2 . HIS   B 213 ? 0.3896 0.4067 0.3410 0.0105  0.0156  -0.0462 419 HIS   B CD2 
3577 C CE1 . HIS   B 213 ? 0.4960 0.5210 0.4401 0.0075  0.0203  -0.0456 419 HIS   B CE1 
3578 N NE2 . HIS   B 213 ? 0.4590 0.4815 0.4084 0.0104  0.0190  -0.0488 419 HIS   B NE2 
3579 N N   . ILE   B 214 ? 0.3174 0.3269 0.2811 0.0112  0.0114  -0.0407 420 ILE   B N   
3580 C CA  . ILE   B 214 ? 0.3209 0.3273 0.2883 0.0127  0.0098  -0.0426 420 ILE   B CA  
3581 C C   . ILE   B 214 ? 0.3480 0.3545 0.3148 0.0148  0.0102  -0.0473 420 ILE   B C   
3582 O O   . ILE   B 214 ? 0.3542 0.3651 0.3208 0.0156  0.0129  -0.0493 420 ILE   B O   
3583 C CB  . ILE   B 214 ? 0.3417 0.3484 0.3142 0.0132  0.0104  -0.0410 420 ILE   B CB  
3584 C CG1 . ILE   B 214 ? 0.3827 0.3898 0.3564 0.0114  0.0101  -0.0372 420 ILE   B CG1 
3585 C CG2 . ILE   B 214 ? 0.3059 0.3085 0.2813 0.0143  0.0081  -0.0424 420 ILE   B CG2 
3586 C CD1 . ILE   B 214 ? 0.3772 0.3855 0.3553 0.0116  0.0110  -0.0359 420 ILE   B CD1 
3587 N N   . TYR   B 215 ? 0.3170 0.3190 0.2841 0.0155  0.0074  -0.0493 421 TYR   B N   
3588 C CA  . TYR   B 215 ? 0.3343 0.3351 0.3021 0.0179  0.0068  -0.0543 421 TYR   B CA  
3589 C C   . TYR   B 215 ? 0.3968 0.3921 0.3690 0.0188  0.0037  -0.0543 421 TYR   B C   
3590 O O   . TYR   B 215 ? 0.3625 0.3540 0.3346 0.0169  0.0015  -0.0513 421 TYR   B O   
3591 C CB  . TYR   B 215 ? 0.3740 0.3735 0.3370 0.0175  0.0055  -0.0569 421 TYR   B CB  
3592 C CG  . TYR   B 215 ? 0.3838 0.3880 0.3411 0.0161  0.0078  -0.0565 421 TYR   B CG  
3593 C CD1 . TYR   B 215 ? 0.4160 0.4252 0.3711 0.0170  0.0106  -0.0603 421 TYR   B CD1 
3594 C CD2 . TYR   B 215 ? 0.3677 0.3716 0.3218 0.0136  0.0069  -0.0524 421 TYR   B CD2 
3595 C CE1 . TYR   B 215 ? 0.3957 0.4091 0.3445 0.0150  0.0126  -0.0595 421 TYR   B CE1 
3596 C CE2 . TYR   B 215 ? 0.3599 0.3672 0.3082 0.0120  0.0083  -0.0515 421 TYR   B CE2 
3597 C CZ  . TYR   B 215 ? 0.4442 0.4562 0.3893 0.0125  0.0112  -0.0549 421 TYR   B CZ  
3598 O OH  . TYR   B 215 ? 0.4531 0.4685 0.3914 0.0104  0.0126  -0.0537 421 TYR   B OH  
3599 N N   . ARG   B 216 ? 0.3773 0.3721 0.3532 0.0216  0.0032  -0.0577 422 ARG   B N   
3600 C CA  . ARG   B 216 ? 0.3848 0.3730 0.3640 0.0224  -0.0007 -0.0579 422 ARG   B CA  
3601 C C   . ARG   B 216 ? 0.3916 0.3750 0.3689 0.0227  -0.0035 -0.0610 422 ARG   B C   
3602 O O   . ARG   B 216 ? 0.4091 0.3951 0.3844 0.0241  -0.0023 -0.0654 422 ARG   B O   
3603 C CB  . ARG   B 216 ? 0.4461 0.4350 0.4309 0.0256  -0.0010 -0.0604 422 ARG   B CB  
3604 C CG  . ARG   B 216 ? 0.6379 0.6199 0.6259 0.0257  -0.0052 -0.0583 422 ARG   B CG  
3605 C CD  . ARG   B 216 ? 0.8459 0.8295 0.8398 0.0288  -0.0056 -0.0601 422 ARG   B CD  
3606 N NE  . ARG   B 216 ? 0.8028 0.7913 0.7978 0.0277  -0.0030 -0.0567 422 ARG   B NE  
3607 C CZ  . ARG   B 216 ? 0.7683 0.7542 0.7637 0.0260  -0.0047 -0.0523 422 ARG   B CZ  
3608 N NH1 . ARG   B 216 ? 0.7388 0.7173 0.7333 0.0247  -0.0089 -0.0500 422 ARG   B NH1 
3609 N NH2 . ARG   B 216 ? 0.7398 0.7307 0.7364 0.0252  -0.0021 -0.0501 422 ARG   B NH2 
3610 N N   . LEU   B 217 ? 0.3621 0.3387 0.3394 0.0210  -0.0072 -0.0587 423 LEU   B N   
3611 C CA  . LEU   B 217 ? 0.3857 0.3568 0.3618 0.0209  -0.0106 -0.0615 423 LEU   B CA  
3612 C C   . LEU   B 217 ? 0.4289 0.3945 0.4095 0.0239  -0.0140 -0.0649 423 LEU   B C   
3613 O O   . LEU   B 217 ? 0.4012 0.3632 0.3847 0.0238  -0.0161 -0.0621 423 LEU   B O   
3614 C CB  . LEU   B 217 ? 0.3143 0.2811 0.2886 0.0170  -0.0129 -0.0573 423 LEU   B CB  
3615 C CG  . LEU   B 217 ? 0.3756 0.3468 0.3461 0.0145  -0.0108 -0.0554 423 LEU   B CG  
3616 C CD1 . LEU   B 217 ? 0.3495 0.3179 0.3199 0.0107  -0.0127 -0.0514 423 LEU   B CD1 
3617 C CD2 . LEU   B 217 ? 0.4051 0.3774 0.3722 0.0154  -0.0108 -0.0597 423 LEU   B CD2 
3618 N N   . VAL   B 218 ? 0.4526 0.4177 0.4336 0.0266  -0.0148 -0.0710 424 VAL   B N   
3619 C CA  . VAL   B 218 ? 0.4311 0.3913 0.4173 0.0303  -0.0184 -0.0755 424 VAL   B CA  
3620 C C   . VAL   B 218 ? 0.4993 0.4530 0.4847 0.0305  -0.0222 -0.0794 424 VAL   B C   
3621 O O   . VAL   B 218 ? 0.4387 0.3934 0.4194 0.0283  -0.0215 -0.0795 424 VAL   B O   
3622 C CB  . VAL   B 218 ? 0.4766 0.4440 0.4665 0.0345  -0.0153 -0.0811 424 VAL   B CB  
3623 C CG1 . VAL   B 218 ? 0.4420 0.4153 0.4334 0.0342  -0.0120 -0.0774 424 VAL   B CG1 
3624 C CG2 . VAL   B 218 ? 0.4153 0.3893 0.4012 0.0350  -0.0117 -0.0861 424 VAL   B CG2 
3625 N N   . LYS   B 219 ? 0.5216 0.4687 0.5121 0.0335  -0.0268 -0.0829 425 LYS   B N   
3626 C CA  . LYS   B 219 ? 0.5197 0.4591 0.5110 0.0343  -0.0316 -0.0872 425 LYS   B CA  
3627 C C   . LYS   B 219 ? 0.6226 0.5545 0.6105 0.0296  -0.0350 -0.0827 425 LYS   B C   
3628 O O   . LYS   B 219 ? 0.6960 0.6224 0.6838 0.0298  -0.0384 -0.0865 425 LYS   B O   
3629 C CB  . LYS   B 219 ? 0.5547 0.4997 0.5440 0.0364  -0.0289 -0.0946 425 LYS   B CB  
3630 C CG  . LYS   B 219 ? 0.6367 0.5894 0.6296 0.0410  -0.0257 -0.1008 425 LYS   B CG  
3631 C CD  . LYS   B 219 ? 0.7167 0.6629 0.7177 0.0447  -0.0306 -0.1028 425 LYS   B CD  
3632 C CE  . LYS   B 219 ? 0.8574 0.8042 0.8632 0.0497  -0.0320 -0.1130 425 LYS   B CE  
3633 N NZ  . LYS   B 219 ? 0.6791 0.6175 0.6825 0.0484  -0.0364 -0.1149 425 LYS   B NZ  
3634 C C1  . GOL   C .   ? 0.7178 0.8187 0.7393 -0.0134 0.0151  -0.1010 501 GOL   A C1  
3635 O O1  . GOL   C .   ? 0.8058 0.9041 0.8228 -0.0146 0.0161  -0.0947 501 GOL   A O1  
3636 C C2  . GOL   C .   ? 0.7873 0.8918 0.7990 -0.0174 0.0146  -0.1009 501 GOL   A C2  
3637 O O2  . GOL   C .   ? 0.8081 0.9060 0.8140 -0.0181 0.0123  -0.0932 501 GOL   A O2  
3638 C C3  . GOL   C .   ? 0.7939 0.9008 0.8108 -0.0160 0.0132  -0.1080 501 GOL   A C3  
3639 O O3  . GOL   C .   ? 0.8371 0.9359 0.8614 -0.0124 0.0103  -0.1054 501 GOL   A O3  
3640 C C1  . A1IJL D .   ? 0.3834 0.4262 0.4557 -0.0035 -0.0008 -0.0513 502 A1IJL A C1  
3641 C C2  . A1IJL D .   ? 0.4185 0.4668 0.4833 -0.0020 -0.0017 -0.0524 502 A1IJL A C2  
3642 C C3  . A1IJL D .   ? 0.4369 0.4786 0.5083 -0.0028 -0.0019 -0.0553 502 A1IJL A C3  
3643 N N6  . A1IJL D .   ? 0.3866 0.4363 0.4396 0.0049  0.0024  -0.0408 502 A1IJL A N6  
3644 C C7  . A1IJL D .   ? 0.4039 0.4559 0.4608 -0.0009 -0.0039 -0.0519 502 A1IJL A C7  
3645 C C8  . A1IJL D .   ? 0.3549 0.4040 0.4143 -0.0001 0.0003  -0.0471 502 A1IJL A C8  
3646 C C9  . A1IJL D .   ? 0.4544 0.5021 0.5425 -0.0082 -0.0034 -0.0518 502 A1IJL A C9  
3647 C C10 . A1IJL D .   ? 0.3924 0.4451 0.4456 0.0001  -0.0048 -0.0500 502 A1IJL A C10 
3648 C C11 . A1IJL D .   ? 0.4202 0.4703 0.4762 0.0012  -0.0003 -0.0458 502 A1IJL A C11 
3649 C C12 . A1IJL D .   ? 0.4735 0.5166 0.5681 -0.0096 -0.0076 -0.0578 502 A1IJL A C12 
3650 C C13 . A1IJL D .   ? 0.4165 0.4681 0.4697 0.0013  -0.0031 -0.0471 502 A1IJL A C13 
3651 C C14 . A1IJL D .   ? 0.3502 0.4000 0.4049 0.0025  0.0010  -0.0434 502 A1IJL A C14 
3652 C C15 . A1IJL D .   ? 0.3540 0.4045 0.4059 0.0036  -0.0013 -0.0434 502 A1IJL A C15 
3653 C C16 . A1IJL D .   ? 0.3558 0.4050 0.4107 0.0032  0.0034  -0.0414 502 A1IJL A C16 
3654 C C19 . A1IJL D .   ? 0.3514 0.4052 0.4031 0.0046  -0.0091 -0.0448 502 A1IJL A C19 
3655 C C20 . A1IJL D .   ? 0.3518 0.4013 0.4043 0.0064  0.0041  -0.0394 502 A1IJL A C20 
3656 C C21 . A1IJL D .   ? 0.3718 0.4235 0.4097 0.0018  -0.0130 -0.0458 502 A1IJL A C21 
3657 C C22 . A1IJL D .   ? 0.3846 0.4386 0.4342 0.0051  -0.0133 -0.0448 502 A1IJL A C22 
3658 C C24 . A1IJL D .   ? 0.5170 0.5694 0.5562 0.0037  -0.0205 -0.0443 502 A1IJL A C24 
3659 C C17 . A1IJL D .   ? 0.3461 0.3980 0.3934 0.0032  -0.0073 -0.0452 502 A1IJL A C17 
3660 C C18 . A1IJL D .   ? 0.3607 0.4121 0.4018 0.0019  -0.0091 -0.0462 502 A1IJL A C18 
3661 C C23 . A1IJL D .   ? 0.3603 0.4129 0.4025 0.0036  -0.0155 -0.0449 502 A1IJL A C23 
3662 C C4  . A1IJL D .   ? 0.4588 0.5030 0.5375 -0.0053 -0.0021 -0.0519 502 A1IJL A C4  
3663 C C5  . A1IJL D .   ? 0.3863 0.4361 0.4465 -0.0010 -0.0016 -0.0504 502 A1IJL A C5  
3664 C C6  . A1IJL D .   ? 0.3664 0.4136 0.4482 -0.0063 -0.0016 -0.0501 502 A1IJL A C6  
3665 F F1  . A1IJL D .   ? 0.4318 0.4836 0.4742 0.0061  -0.0227 -0.0429 502 A1IJL A F1  
3666 F F2  . A1IJL D .   ? 0.5094 0.5594 0.5394 0.0021  -0.0219 -0.0430 502 A1IJL A F2  
3667 F F3  . A1IJL D .   ? 0.4695 0.5251 0.5122 0.0030  -0.0227 -0.0465 502 A1IJL A F3  
3668 N N1  . A1IJL D .   ? 0.3790 0.4244 0.4460 -0.0023 -0.0001 -0.0502 502 A1IJL A N1  
3669 N N2  . A1IJL D .   ? 0.4053 0.4480 0.4884 -0.0062 -0.0042 -0.0550 502 A1IJL A N2  
3670 N N3  . A1IJL D .   ? 0.5298 0.5743 0.6184 -0.0080 -0.0051 -0.0547 502 A1IJL A N3  
3671 N N4  . A1IJL D .   ? 0.3264 0.3777 0.3767 0.0028  -0.0039 -0.0452 502 A1IJL A N4  
3672 N N5  . A1IJL D .   ? 0.3335 0.3835 0.3847 0.0052  -0.0008 -0.0417 502 A1IJL A N5  
3673 O O1  . A1IJL D .   ? 0.3662 0.4157 0.4331 -0.0028 -0.0036 -0.0557 502 A1IJL A O1  
3674 O O2  . A1IJL D .   ? 0.5429 0.5838 0.6090 -0.0015 -0.0005 -0.0545 502 A1IJL A O2  
3675 S S   . SO4   E .   ? 0.9871 0.9798 1.0027 0.0340  -0.0084 -0.0547 503 SO4   A S   
3676 O O1  . SO4   E .   ? 0.6638 0.6656 0.6803 0.0333  -0.0029 -0.0552 503 SO4   A O1  
3677 O O2  . SO4   E .   ? 0.7315 0.7200 0.7484 0.0335  -0.0125 -0.0513 503 SO4   A O2  
3678 O O3  . SO4   E .   ? 0.8805 0.8724 0.9008 0.0381  -0.0103 -0.0605 503 SO4   A O3  
3679 O O4  . SO4   E .   ? 0.9877 0.9762 0.9965 0.0307  -0.0082 -0.0519 503 SO4   A O4  
3680 S S   . SO4   F .   ? 0.7826 0.8018 0.8509 0.0487  -0.0239 -0.0603 504 SO4   A S   
3681 O O1  . SO4   F .   ? 0.7857 0.8027 0.8485 0.0449  -0.0249 -0.0547 504 SO4   A O1  
3682 O O2  . SO4   F .   ? 0.7511 0.7819 0.8282 0.0505  -0.0195 -0.0654 504 SO4   A O2  
3683 O O3  . SO4   F .   ? 0.7286 0.7456 0.7899 0.0467  -0.0200 -0.0597 504 SO4   A O3  
3684 O O4  . SO4   F .   ? 0.8630 0.8751 0.9354 0.0526  -0.0315 -0.0618 504 SO4   A O4  
3685 S S   . SO4   G .   ? 1.2514 1.3907 1.2811 -0.0393 0.0752  -0.0353 505 SO4   A S   
3686 O O1  . SO4   G .   ? 1.1001 1.2271 1.1197 -0.0380 0.0713  -0.0309 505 SO4   A O1  
3687 O O2  . SO4   G .   ? 0.8785 1.0150 0.9141 -0.0422 0.0732  -0.0313 505 SO4   A O2  
3688 O O3  . SO4   G .   ? 1.3534 1.5040 1.3789 -0.0454 0.0814  -0.0360 505 SO4   A O3  
3689 O O4  . SO4   G .   ? 0.9757 1.1192 1.0140 -0.0319 0.0747  -0.0430 505 SO4   A O4  
3690 C C1  . GOL   H .   ? 0.7419 0.7960 0.8626 0.0313  -0.0310 -0.0778 501 GOL   B C1  
3691 O O1  . GOL   H .   ? 0.7725 0.8303 0.8878 0.0285  -0.0245 -0.0787 501 GOL   B O1  
3692 C C2  . GOL   H .   ? 0.6695 0.7345 0.8025 0.0332  -0.0317 -0.0859 501 GOL   B C2  
3693 O O2  . GOL   H .   ? 0.7942 0.8559 0.9369 0.0374  -0.0391 -0.0875 501 GOL   B O2  
3694 C C3  . GOL   H .   ? 0.6530 0.7226 0.7801 0.0300  -0.0287 -0.0842 501 GOL   B C3  
3695 O O3  . GOL   H .   ? 0.7068 0.7816 0.8445 0.0324  -0.0328 -0.0885 501 GOL   B O3  
3696 C C1  . A1IJL I .   ? 0.4394 0.4913 0.4651 -0.0156 -0.0006 -0.0474 502 A1IJL B C1  
3697 C C2  . A1IJL I .   ? 0.4218 0.4672 0.4478 -0.0084 -0.0058 -0.0466 502 A1IJL B C2  
3698 C C3  . A1IJL I .   ? 0.4322 0.4934 0.4666 -0.0152 0.0007  -0.0514 502 A1IJL B C3  
3699 N N6  . A1IJL I .   ? 0.4257 0.4388 0.4175 0.0001  -0.0054 -0.0346 502 A1IJL B N6  
3700 C C7  . A1IJL I .   ? 0.3469 0.3846 0.3701 -0.0025 -0.0112 -0.0442 502 A1IJL B C7  
3701 C C8  . A1IJL I .   ? 0.3634 0.3953 0.3765 -0.0052 -0.0064 -0.0413 502 A1IJL B C8  
3702 C C9  . A1IJL I .   ? 0.4614 0.5095 0.4838 -0.0229 -0.0049 -0.0467 502 A1IJL B C9  
3703 C C10 . A1IJL I .   ? 0.3748 0.4062 0.3922 -0.0003 -0.0130 -0.0416 502 A1IJL B C10 
3704 C C11 . A1IJL I .   ? 0.3791 0.4054 0.3873 -0.0026 -0.0078 -0.0393 502 A1IJL B C11 
3705 C C12 . A1IJL I .   ? 0.4771 0.5429 0.5126 -0.0289 -0.0025 -0.0522 502 A1IJL B C12 
3706 C C13 . A1IJL I .   ? 0.3453 0.3716 0.3553 -0.0005 -0.0109 -0.0393 502 A1IJL B C13 
3707 C C14 . A1IJL I .   ? 0.3443 0.3650 0.3457 -0.0018 -0.0068 -0.0371 502 A1IJL B C14 
3708 C C15 . A1IJL I .   ? 0.3748 0.3928 0.3735 0.0004  -0.0088 -0.0360 502 A1IJL B C15 
3709 C C16 . A1IJL I .   ? 0.3780 0.3947 0.3743 -0.0019 -0.0049 -0.0358 502 A1IJL B C16 
3710 C C19 . A1IJL I .   ? 0.3413 0.3560 0.3356 0.0025  -0.0157 -0.0349 502 A1IJL B C19 
3711 C C20 . A1IJL I .   ? 0.3702 0.3795 0.3569 0.0010  -0.0039 -0.0337 502 A1IJL B C20 
3712 C C21 . A1IJL I .   ? 0.3812 0.3991 0.3857 0.0053  -0.0216 -0.0346 502 A1IJL B C21 
3713 C C22 . A1IJL I .   ? 0.3656 0.3783 0.3568 0.0035  -0.0191 -0.0337 502 A1IJL B C22 
3714 C C24 . A1IJL I .   ? 0.4502 0.4616 0.4423 0.0054  -0.0266 -0.0313 502 A1IJL B C24 
3715 C C17 . A1IJL I .   ? 0.3242 0.3428 0.3257 0.0028  -0.0148 -0.0358 502 A1IJL B C17 
3716 C C18 . A1IJL I .   ? 0.3394 0.3600 0.3465 0.0042  -0.0176 -0.0361 502 A1IJL B C18 
3717 C C23 . A1IJL I .   ? 0.3608 0.3748 0.3568 0.0048  -0.0222 -0.0331 502 A1IJL B C23 
3718 C C4  . A1IJL I .   ? 0.3965 0.4484 0.4218 -0.0188 -0.0020 -0.0475 502 A1IJL B C4  
3719 C C5  . A1IJL I .   ? 0.3563 0.3944 0.3769 -0.0052 -0.0077 -0.0439 502 A1IJL B C5  
3720 C C6  . A1IJL I .   ? 0.4084 0.4529 0.4280 -0.0192 -0.0041 -0.0454 502 A1IJL B C6  
3721 F F1  . A1IJL I .   ? 0.4428 0.4507 0.4257 0.0048  -0.0259 -0.0300 502 A1IJL B F1  
3722 F F2  . A1IJL I .   ? 0.4476 0.4577 0.4415 0.0068  -0.0287 -0.0292 502 A1IJL B F2  
3723 F F3  . A1IJL I .   ? 0.4789 0.4923 0.4744 0.0053  -0.0301 -0.0331 502 A1IJL B F3  
3724 N N1  . A1IJL I .   ? 0.4188 0.4642 0.4417 -0.0112 -0.0028 -0.0457 502 A1IJL B N1  
3725 N N2  . A1IJL I .   ? 0.4785 0.5388 0.5100 -0.0219 -0.0012 -0.0504 502 A1IJL B N2  
3726 N N3  . A1IJL I .   ? 0.4942 0.5520 0.5238 -0.0246 -0.0029 -0.0496 502 A1IJL B N3  
3727 N N4  . A1IJL I .   ? 0.3668 0.3876 0.3703 0.0011  -0.0115 -0.0369 502 A1IJL B N4  
3728 N N5  . A1IJL I .   ? 0.3405 0.3543 0.3331 0.0013  -0.0078 -0.0345 502 A1IJL B N5  
3729 O O1  . A1IJL I .   ? 0.3864 0.4375 0.4190 -0.0088 -0.0073 -0.0493 502 A1IJL B O1  
3730 O O2  . A1IJL I .   ? 0.4654 0.5260 0.4998 -0.0126 0.0019  -0.0513 502 A1IJL B O2  
3731 S S   . SO4   J .   ? 0.5358 0.5563 0.5360 0.0108  0.0159  -0.0307 503 SO4   B S   
3732 O O1  . SO4   J .   ? 0.5519 0.5730 0.5544 0.0095  0.0158  -0.0292 503 SO4   B O1  
3733 O O2  . SO4   J .   ? 0.5967 0.6187 0.5998 0.0124  0.0158  -0.0324 503 SO4   B O2  
3734 O O3  . SO4   J .   ? 0.6535 0.6754 0.6513 0.0103  0.0176  -0.0305 503 SO4   B O3  
3735 O O4  . SO4   J .   ? 0.5897 0.6068 0.5873 0.0109  0.0140  -0.0308 503 SO4   B O4  
3736 S S   . SO4   K .   ? 1.3700 1.3789 1.3739 0.0309  0.0064  -0.0608 504 SO4   B S   
3737 O O1  . SO4   K .   ? 1.0871 1.0907 1.0925 0.0303  0.0028  -0.0569 504 SO4   B O1  
3738 O O2  . SO4   K .   ? 1.2390 1.2530 1.2490 0.0343  0.0073  -0.0663 504 SO4   B O2  
3739 O O3  . SO4   K .   ? 1.0782 1.0924 1.0786 0.0279  0.0106  -0.0579 504 SO4   B O3  
3740 O O4  . SO4   K .   ? 1.0987 1.1027 1.0987 0.0309  0.0045  -0.0624 504 SO4   B O4  
3741 S S   . SO4   L .   ? 1.2733 1.3275 1.2388 -0.0069 0.0396  -0.0299 505 SO4   B S   
3742 O O1  . SO4   L .   ? 0.9898 1.0354 0.9541 -0.0062 0.0350  -0.0261 505 SO4   B O1  
3743 O O2  . SO4   L .   ? 1.0424 1.0986 1.0158 -0.0026 0.0399  -0.0349 505 SO4   B O2  
3744 O O3  . SO4   L .   ? 1.2224 1.2803 1.1890 -0.0110 0.0419  -0.0267 505 SO4   B O3  
3745 O O4  . SO4   L .   ? 1.1180 1.1752 1.0759 -0.0079 0.0413  -0.0322 505 SO4   B O4  
3746 O O   . HOH   M .   ? 0.5047 0.5580 0.5181 -0.0155 0.0359  -0.0163 601 HOH   A O   
3747 O O   . HOH   M .   ? 0.3755 0.4091 0.4473 -0.0071 0.0052  -0.0367 602 HOH   A O   
3748 O O   . HOH   M .   ? 0.7195 0.7208 0.7473 0.0239  -0.0502 -0.0259 603 HOH   A O   
3749 O O   . HOH   M .   ? 0.5590 0.5547 0.6463 -0.0160 -0.0104 -0.0259 604 HOH   A O   
3750 O O   . HOH   M .   ? 0.4585 0.5478 0.5813 -0.0082 -0.0255 -0.0662 605 HOH   A O   
3751 O O   . HOH   M .   ? 0.4849 0.4911 0.5385 0.0039  -0.0034 -0.0306 606 HOH   A O   
3752 O O   . HOH   M .   ? 0.2841 0.3638 0.3841 0.0178  -0.0167 -0.0523 607 HOH   A O   
3753 O O   . HOH   M .   ? 0.3696 0.4401 0.3361 -0.0260 -0.0031 -0.0551 608 HOH   A O   
3754 O O   . HOH   M .   ? 0.4488 0.4839 0.4996 -0.0003 0.0103  -0.0341 609 HOH   A O   
3755 O O   . HOH   M .   ? 0.3822 0.4753 0.4398 -0.0413 0.0486  -0.0153 610 HOH   A O   
3756 O O   . HOH   M .   ? 0.5444 0.6485 0.6913 0.0281  -0.0562 -0.0654 611 HOH   A O   
3757 O O   . HOH   M .   ? 0.5002 0.5083 0.4878 0.0002  -0.0205 -0.0201 612 HOH   A O   
3758 O O   . HOH   M .   ? 0.4338 0.5743 0.5779 -0.0176 0.0326  -0.0531 613 HOH   A O   
3759 O O   . HOH   M .   ? 0.6479 0.8131 0.7341 -0.0063 0.0694  -0.0721 614 HOH   A O   
3760 O O   . HOH   M .   ? 0.5057 0.5559 0.5798 0.0489  0.0007  -0.0764 615 HOH   A O   
3761 O O   . HOH   M .   ? 0.4939 0.6072 0.6296 0.0489  0.0079  -0.0904 616 HOH   A O   
3762 O O   . HOH   M .   ? 0.5183 0.5939 0.5480 -0.0480 0.0470  -0.0022 617 HOH   A O   
3763 O O   . HOH   M .   ? 0.7482 0.7536 0.7243 -0.0040 -0.0491 -0.0133 618 HOH   A O   
3764 O O   . HOH   M .   ? 0.4962 0.5530 0.5541 -0.0369 0.0309  -0.0081 619 HOH   A O   
3765 O O   . HOH   M .   ? 0.3487 0.4092 0.4203 0.0376  0.0072  -0.0640 620 HOH   A O   
3766 O O   . HOH   M .   ? 0.5618 0.6008 0.6479 -0.0052 -0.0074 -0.0631 621 HOH   A O   
3767 O O   . HOH   M .   ? 0.5827 0.5668 0.5995 -0.0306 -0.0027 0.0175  622 HOH   A O   
3768 O O   . HOH   M .   ? 0.5689 0.5419 0.6135 -0.0015 -0.0229 -0.0066 623 HOH   A O   
3769 O O   . HOH   M .   ? 0.5355 0.6854 0.6752 -0.0454 0.0484  -0.0397 624 HOH   A O   
3770 O O   . HOH   M .   ? 0.5194 0.6093 0.6322 0.0027  -0.0265 -0.0599 625 HOH   A O   
3771 O O   . HOH   M .   ? 0.5418 0.5958 0.6072 0.0046  0.0024  -0.0822 626 HOH   A O   
3772 O O   . HOH   M .   ? 0.5574 0.6254 0.5403 -0.0187 -0.0469 -0.0564 627 HOH   A O   
3773 O O   . HOH   M .   ? 0.5593 0.5823 0.6084 0.0262  -0.0643 -0.0317 628 HOH   A O   
3774 O O   . HOH   M .   ? 0.5733 0.6013 0.6792 -0.0145 -0.0097 -0.0523 629 HOH   A O   
3775 O O   . HOH   M .   ? 0.5393 0.6353 0.5946 0.0054  0.0429  -0.0506 630 HOH   A O   
3776 O O   . HOH   M .   ? 0.2721 0.2943 0.2882 0.0115  -0.0074 -0.0305 631 HOH   A O   
3777 O O   . HOH   M .   ? 0.3627 0.4665 0.4935 0.0030  -0.0061 -0.0572 632 HOH   A O   
3778 O O   . HOH   M .   ? 0.4218 0.5445 0.5055 0.0353  0.0428  -0.0964 633 HOH   A O   
3779 O O   . HOH   M .   ? 0.5104 0.6936 0.6830 -0.0314 0.0475  -0.0604 634 HOH   A O   
3780 O O   . HOH   M .   ? 0.4212 0.4784 0.5224 0.0356  -0.0821 -0.0477 635 HOH   A O   
3781 O O   . HOH   M .   ? 0.3823 0.4109 0.4056 0.0161  0.0082  -0.0353 636 HOH   A O   
3782 O O   . HOH   M .   ? 0.5432 0.6281 0.5361 -0.0206 -0.0136 -0.0829 637 HOH   A O   
3783 O O   . HOH   M .   ? 0.6196 0.6400 0.6212 0.0068  0.0159  -0.0256 638 HOH   A O   
3784 O O   . HOH   M .   ? 0.6968 0.7215 0.6808 0.0046  0.0214  -0.0256 639 HOH   A O   
3785 O O   . HOH   M .   ? 0.3578 0.3930 0.4226 -0.0251 0.0166  -0.0140 640 HOH   A O   
3786 O O   . HOH   M .   ? 0.7176 0.7380 0.7941 0.0003  -0.0037 -0.0502 641 HOH   A O   
3787 O O   . HOH   M .   ? 0.5447 0.5987 0.6261 0.0452  -0.0040 -0.0678 642 HOH   A O   
3788 O O   . HOH   M .   ? 0.4704 0.6235 0.6298 0.0398  0.0231  -0.0977 643 HOH   A O   
3789 O O   . HOH   M .   ? 0.5169 0.6096 0.6361 0.0227  -0.0159 -0.0582 644 HOH   A O   
3790 O O   . HOH   M .   ? 0.5295 0.5347 0.5119 -0.0012 0.0049  -0.0094 645 HOH   A O   
3791 O O   . HOH   M .   ? 0.5679 0.6391 0.5760 -0.0196 0.0458  -0.0205 646 HOH   A O   
3792 O O   . HOH   M .   ? 0.6616 0.7052 0.6865 0.0248  0.0207  -0.0528 647 HOH   A O   
3793 O O   . HOH   M .   ? 0.5095 0.5431 0.5701 0.0435  -0.0056 -0.0632 648 HOH   A O   
3794 O O   . HOH   M .   ? 0.6858 0.7030 0.6296 -0.0174 -0.1093 -0.0091 649 HOH   A O   
3795 O O   . HOH   M .   ? 0.4289 0.5252 0.4986 0.0362  0.0333  -0.0856 650 HOH   A O   
3796 O O   . HOH   M .   ? 0.4621 0.4975 0.5124 0.0015  0.0060  -0.0433 651 HOH   A O   
3797 O O   . HOH   M .   ? 0.5380 0.5980 0.5508 -0.0255 0.0403  -0.0111 652 HOH   A O   
3798 O O   . HOH   M .   ? 0.6597 0.6637 0.6723 0.0150  -0.0448 -0.0221 653 HOH   A O   
3799 O O   . HOH   M .   ? 0.3899 0.4514 0.4768 -0.0172 0.0171  -0.0309 654 HOH   A O   
3800 O O   . HOH   M .   ? 0.4321 0.4466 0.4336 0.0065  0.0052  -0.0271 655 HOH   A O   
3801 O O   . HOH   M .   ? 0.6034 0.6080 0.6107 0.0156  -0.0074 -0.0299 656 HOH   A O   
3802 O O   . HOH   M .   ? 0.7385 0.7465 0.8385 -0.0116 -0.0119 -0.0446 657 HOH   A O   
3803 O O   . HOH   M .   ? 0.7168 0.7724 0.6418 -0.0398 -0.0218 -0.0326 658 HOH   A O   
3804 O O   . HOH   M .   ? 0.6746 0.7535 0.7042 -0.0140 -0.0304 -0.0843 659 HOH   A O   
3805 O O   . HOH   M .   ? 0.4926 0.5067 0.5026 0.0139  -0.0004 -0.0309 660 HOH   A O   
3806 O O   . HOH   M .   ? 0.4584 0.4805 0.4476 -0.0018 -0.0482 -0.0224 661 HOH   A O   
3807 O O   . HOH   M .   ? 0.6048 0.6630 0.6314 0.0139  0.0304  -0.0448 662 HOH   A O   
3808 O O   . HOH   M .   ? 0.4952 0.5625 0.5904 0.0269  -0.0411 -0.0504 663 HOH   A O   
3809 O O   . HOH   M .   ? 0.5108 0.5814 0.5525 0.0270  0.0301  -0.0655 664 HOH   A O   
3810 O O   . HOH   M .   ? 0.6359 0.7557 0.6637 -0.0221 0.0650  -0.0405 665 HOH   A O   
3811 O O   . HOH   M .   ? 0.6282 0.6937 0.5690 -0.0321 -0.0388 -0.0470 666 HOH   A O   
3812 O O   . HOH   M .   ? 0.5851 0.5907 0.5798 0.0064  -0.1038 -0.0118 667 HOH   A O   
3813 O O   . HOH   M .   ? 0.5876 0.7324 0.7596 -0.0164 0.0149  -0.0603 668 HOH   A O   
3814 O O   . HOH   M .   ? 0.4541 0.4960 0.5167 -0.0015 0.0044  -0.0431 669 HOH   A O   
3815 O O   . HOH   M .   ? 0.5414 0.6137 0.6349 -0.0270 0.0237  -0.0266 670 HOH   A O   
3816 O O   . HOH   M .   ? 0.7054 0.6914 0.6839 -0.0190 -0.0051 0.0158  671 HOH   A O   
3817 O O   . HOH   M .   ? 0.5752 0.6281 0.6728 0.0434  -0.0319 -0.0567 672 HOH   A O   
3818 O O   . HOH   M .   ? 0.5674 0.6564 0.7008 -0.0356 0.0153  -0.0365 673 HOH   A O   
3819 O O   . HOH   M .   ? 0.5623 0.6556 0.6785 0.0077  -0.0351 -0.0606 674 HOH   A O   
3820 O O   . HOH   M .   ? 0.4452 0.4935 0.5358 -0.0068 -0.0144 -0.0786 675 HOH   A O   
3821 O O   . HOH   M .   ? 0.5453 0.5815 0.6062 -0.0007 0.0035  -0.0456 676 HOH   A O   
3822 O O   . HOH   M .   ? 0.4681 0.5127 0.5846 -0.0193 -0.0098 -0.0542 677 HOH   A O   
3823 O O   . HOH   M .   ? 0.4916 0.6449 0.6389 -0.0303 0.0428  -0.0499 678 HOH   A O   
3824 O O   . HOH   M .   ? 0.6172 0.6293 0.6645 0.0146  -0.0142 -0.0353 679 HOH   A O   
3825 O O   . HOH   M .   ? 0.6197 0.6362 0.6249 0.0172  0.0105  -0.0367 680 HOH   A O   
3826 O O   . HOH   M .   ? 0.2949 0.3274 0.3197 0.0101  -0.0112 -0.0335 681 HOH   A O   
3827 O O   . HOH   M .   ? 0.7050 0.7334 0.7181 0.0209  0.0158  -0.0436 682 HOH   A O   
3828 O O   . HOH   M .   ? 0.5493 0.5659 0.6513 -0.0166 -0.0085 -0.0417 683 HOH   A O   
3829 O O   . HOH   M .   ? 0.6033 0.6676 0.6063 -0.0095 -0.0899 -0.0477 684 HOH   A O   
3830 O O   . HOH   M .   ? 0.4060 0.5213 0.5500 0.0099  -0.0086 -0.0622 685 HOH   A O   
3831 O O   . HOH   M .   ? 0.4984 0.5394 0.5608 0.0494  0.0017  -0.0789 686 HOH   A O   
3832 O O   . HOH   M .   ? 0.6274 0.6479 0.6950 0.0060  -0.0022 -0.0502 687 HOH   A O   
3833 O O   . HOH   M .   ? 0.6684 0.6216 0.7125 -0.0258 -0.0264 0.0166  688 HOH   A O   
3834 O O   . HOH   M .   ? 0.6193 0.6678 0.6427 -0.0013 0.0098  -0.0524 689 HOH   A O   
3835 O O   . HOH   M .   ? 0.6827 0.6505 0.6824 -0.0092 -0.0251 0.0137  690 HOH   A O   
3836 O O   . HOH   M .   ? 0.7388 0.7250 0.7491 0.0362  -0.0092 -0.0634 691 HOH   A O   
3837 O O   . HOH   M .   ? 0.5134 0.5629 0.5420 0.0144  0.0245  -0.0408 692 HOH   A O   
3838 O O   . HOH   M .   ? 0.6277 0.6408 0.6926 -0.0395 0.0084  0.0010  693 HOH   A O   
3839 O O   . HOH   M .   ? 0.7547 0.7598 0.7105 -0.0148 -0.0447 -0.0093 694 HOH   A O   
3840 O O   . HOH   M .   ? 0.5532 0.6613 0.7049 -0.0310 0.0116  -0.0467 695 HOH   A O   
3841 O O   . HOH   M .   ? 0.6551 0.7009 0.7555 0.0396  -0.1414 -0.0402 696 HOH   A O   
3842 O O   . HOH   M .   ? 0.6105 0.6440 0.6871 0.0425  -0.0291 -0.0522 697 HOH   A O   
3843 O O   . HOH   M .   ? 0.5985 0.6075 0.6253 0.0198  -0.1083 -0.0186 698 HOH   A O   
3844 O O   . HOH   M .   ? 0.7147 0.7015 0.7115 -0.0364 0.0006  0.0250  699 HOH   A O   
3845 O O   . HOH   M .   ? 0.5751 0.7056 0.7400 0.0109  -0.0130 -0.0683 700 HOH   A O   
3846 O O   . HOH   M .   ? 0.6730 0.6880 0.7400 0.0092  -0.0053 -0.0470 701 HOH   A O   
3847 O O   . HOH   M .   ? 0.6731 0.7006 0.7391 0.0088  -0.0008 -0.0562 702 HOH   A O   
3848 O O   . HOH   M .   ? 0.5414 0.6655 0.6035 0.0237  0.0520  -0.0877 703 HOH   A O   
3849 O O   . HOH   M .   ? 0.5631 0.6544 0.6136 0.0281  0.0383  -0.0770 704 HOH   A O   
3850 O O   . HOH   M .   ? 0.5829 0.6391 0.6566 -0.0400 0.0267  -0.0097 705 HOH   A O   
3851 O O   . HOH   M .   ? 0.6940 0.7089 0.7521 0.0096  -0.0039 -0.0420 706 HOH   A O   
3852 O O   . HOH   M .   ? 0.5432 0.6043 0.6275 -0.0329 0.0240  -0.0184 707 HOH   A O   
3853 O O   . HOH   M .   ? 0.7318 0.8208 0.7139 -0.0248 -0.0218 -0.0847 708 HOH   A O   
3854 O O   . HOH   M .   ? 0.7591 0.6945 0.8151 -0.0231 -0.0406 0.0170  709 HOH   A O   
3855 O O   . HOH   M .   ? 0.5355 0.5844 0.6157 0.0066  -0.0028 -0.0888 710 HOH   A O   
3856 O O   . HOH   M .   ? 0.6412 0.7170 0.6513 -0.0572 0.0506  0.0056  711 HOH   A O   
3857 O O   . HOH   M .   ? 0.6255 0.6659 0.6511 0.0218  0.0185  -0.0463 712 HOH   A O   
3858 O O   . HOH   N .   ? 0.4311 0.4819 0.4747 -0.0053 -0.0405 -0.0555 601 HOH   B O   
3859 O O   . HOH   N .   ? 0.6076 0.5478 0.6067 0.0333  -0.0317 -0.0708 602 HOH   B O   
3860 O O   . HOH   N .   ? 0.5590 0.5744 0.4893 0.0056  0.0108  -0.0450 603 HOH   B O   
3861 O O   . HOH   N .   ? 0.6813 0.5858 0.6743 0.0352  -0.0535 -0.1085 604 HOH   B O   
3862 O O   . HOH   N .   ? 0.6196 0.6508 0.5685 -0.0470 0.0063  -0.0165 605 HOH   B O   
3863 O O   . HOH   N .   ? 0.5619 0.5588 0.4644 -0.0065 -0.0239 -0.0154 606 HOH   B O   
3864 O O   . HOH   N .   ? 0.4653 0.3849 0.4289 -0.0202 -0.0409 -0.0112 607 HOH   B O   
3865 O O   . HOH   N .   ? 0.6993 0.6836 0.6868 -0.0415 -0.0237 -0.0363 608 HOH   B O   
3866 O O   . HOH   N .   ? 0.5833 0.5643 0.4342 -0.0143 -0.0983 -0.0096 609 HOH   B O   
3867 O O   . HOH   N .   ? 0.5775 0.5742 0.5460 -0.0012 -0.0074 -0.0055 610 HOH   B O   
3868 O O   . HOH   N .   ? 0.6678 0.7428 0.6323 0.0080  0.0471  -0.0670 611 HOH   B O   
3869 O O   . HOH   N .   ? 0.5158 0.5022 0.4500 -0.0536 -0.0133 0.0032  612 HOH   B O   
3870 O O   . HOH   N .   ? 0.4347 0.4361 0.4287 0.0429  0.0007  -0.1014 613 HOH   B O   
3871 O O   . HOH   N .   ? 0.4686 0.5223 0.4611 -0.0245 0.0169  -0.0396 614 HOH   B O   
3872 O O   . HOH   N .   ? 0.6734 0.6537 0.6431 0.0096  -0.0975 -0.0054 615 HOH   B O   
3873 O O   . HOH   N .   ? 0.4212 0.3467 0.3901 -0.0159 -0.0362 -0.0217 616 HOH   B O   
3874 O O   . HOH   N .   ? 0.4240 0.4526 0.4362 0.0046  0.0067  -0.0327 617 HOH   B O   
3875 O O   . HOH   N .   ? 0.5676 0.5918 0.5650 -0.0104 0.0051  -0.0343 618 HOH   B O   
3876 O O   . HOH   N .   ? 0.4865 0.4339 0.4550 -0.0094 -0.0320 -0.0529 619 HOH   B O   
3877 O O   . HOH   N .   ? 0.3526 0.3484 0.3041 0.0015  -0.0187 -0.0430 620 HOH   B O   
3878 O O   . HOH   N .   ? 0.7596 0.6577 0.7348 0.0057  -0.0564 -0.0816 621 HOH   B O   
3879 O O   . HOH   N .   ? 0.6856 0.6050 0.6558 -0.0094 -0.0465 -0.0623 622 HOH   B O   
3880 O O   . HOH   N .   ? 0.3793 0.3841 0.3470 -0.0042 -0.0430 -0.0471 623 HOH   B O   
3881 O O   . HOH   N .   ? 0.5826 0.4990 0.5551 -0.0228 -0.0452 -0.0421 624 HOH   B O   
3882 O O   . HOH   N .   ? 0.4224 0.4304 0.4031 -0.0072 -0.0372 -0.0483 625 HOH   B O   
3883 O O   . HOH   N .   ? 0.4336 0.4663 0.4335 -0.0249 0.0038  -0.0361 626 HOH   B O   
3884 O O   . HOH   N .   ? 0.4179 0.4159 0.3445 0.0004  -0.0245 -0.0364 627 HOH   B O   
3885 O O   . HOH   N .   ? 0.4441 0.4380 0.3658 -0.0028 -0.0415 -0.0524 628 HOH   B O   
3886 O O   . HOH   N .   ? 0.6995 0.7372 0.7185 -0.0485 -0.0150 -0.0454 629 HOH   B O   
3887 O O   . HOH   N .   ? 0.4171 0.4365 0.4154 -0.0074 -0.0358 -0.0475 630 HOH   B O   
3888 O O   . HOH   N .   ? 0.3721 0.3942 0.3405 0.0173  0.0192  -0.0549 631 HOH   B O   
3889 O O   . HOH   N .   ? 0.5089 0.5622 0.6171 0.0282  -0.0607 -0.0629 632 HOH   B O   
3890 O O   . HOH   N .   ? 0.5300 0.5213 0.4734 0.0023  -0.0186 -0.0497 633 HOH   B O   
3891 O O   . HOH   N .   ? 0.5470 0.5671 0.5605 0.0093  -0.0828 -0.0390 634 HOH   B O   
3892 O O   . HOH   N .   ? 0.6664 0.6244 0.6361 -0.0174 -0.0376 -0.0573 635 HOH   B O   
3893 O O   . HOH   N .   ? 0.5932 0.6098 0.5937 -0.0188 -0.0442 -0.0561 636 HOH   B O   
3894 O O   . HOH   N .   ? 0.2756 0.2830 0.2497 0.0045  0.0038  -0.0208 637 HOH   B O   
3895 O O   . HOH   N .   ? 0.6275 0.6385 0.6286 0.0354  0.0074  -0.0749 638 HOH   B O   
3896 O O   . HOH   N .   ? 0.4195 0.3973 0.4017 0.0054  -0.0089 -0.0288 639 HOH   B O   
3897 O O   . HOH   N .   ? 0.3985 0.3890 0.3670 -0.0077 -0.0267 -0.0495 640 HOH   B O   
3898 O O   . HOH   N .   ? 0.4131 0.4951 0.4601 -0.0252 0.0034  -0.0583 641 HOH   B O   
3899 O O   . HOH   N .   ? 0.6391 0.6424 0.6322 -0.0237 -0.0407 -0.0560 642 HOH   B O   
3900 O O   . HOH   N .   ? 0.4261 0.4153 0.3974 -0.0361 -0.0079 -0.0192 643 HOH   B O   
3901 O O   . HOH   N .   ? 0.5982 0.6196 0.5519 0.0238  0.0158  -0.0828 644 HOH   B O   
3902 O O   . HOH   N .   ? 0.5077 0.5944 0.5605 -0.0193 0.0057  -0.0619 645 HOH   B O   
3903 O O   . HOH   N .   ? 0.4926 0.5107 0.4725 0.0025  0.0168  -0.0205 646 HOH   B O   
3904 O O   . HOH   N .   ? 0.6370 0.6625 0.6475 0.0160  0.0151  -0.0364 647 HOH   B O   
3905 O O   . HOH   N .   ? 0.6668 0.6271 0.5980 -0.0465 -0.0284 0.0104  648 HOH   B O   
3906 O O   . HOH   N .   ? 0.4719 0.5132 0.4876 -0.0070 0.0061  -0.0421 649 HOH   B O   
3907 O O   . HOH   N .   ? 0.6658 0.6309 0.6340 -0.0176 -0.0409 -0.0614 650 HOH   B O   
3908 O O   . HOH   N .   ? 0.5897 0.5730 0.5328 -0.0292 -0.0233 -0.0005 651 HOH   B O   
3909 O O   . HOH   N .   ? 0.4701 0.4566 0.4217 0.0014  -0.0413 -0.0047 652 HOH   B O   
3910 O O   . HOH   N .   ? 0.4158 0.4066 0.3970 -0.0243 -0.0107 -0.0310 653 HOH   B O   
3911 O O   . HOH   N .   ? 0.5128 0.5459 0.5318 -0.0182 -0.0398 -0.0553 654 HOH   B O   
3912 O O   . HOH   N .   ? 0.5063 0.5652 0.5347 -0.0455 -0.0056 -0.0482 655 HOH   B O   
3913 O O   . HOH   N .   ? 0.4086 0.4174 0.4795 0.0261  -0.0521 -0.0378 656 HOH   B O   
3914 O O   . HOH   N .   ? 0.7638 0.7400 0.7194 -0.0023 -0.0395 0.0082  657 HOH   B O   
3915 O O   . HOH   N .   ? 0.6874 0.6975 0.6851 0.0067  0.0004  -0.0271 658 HOH   B O   
3916 O O   . HOH   N .   ? 0.6611 0.6546 0.6158 0.0271  -0.0015 -0.0923 659 HOH   B O   
3917 O O   . HOH   N .   ? 0.5594 0.5920 0.5344 0.0168  0.0250  -0.0544 660 HOH   B O   
3918 O O   . HOH   N .   ? 0.7145 0.6543 0.6739 -0.0378 -0.0299 -0.0091 661 HOH   B O   
3919 O O   . HOH   N .   ? 0.6541 0.6768 0.5743 0.0003  0.0153  -0.0392 662 HOH   B O   
3920 O O   . HOH   N .   ? 0.6198 0.6666 0.6169 -0.0093 0.0078  -0.0429 663 HOH   B O   
3921 O O   . HOH   N .   ? 0.6129 0.6884 0.6425 -0.0472 0.0059  -0.0495 664 HOH   B O   
3922 O O   . HOH   N .   ? 0.3249 0.3294 0.2978 0.0049  -0.0059 -0.0229 665 HOH   B O   
3923 O O   . HOH   N .   ? 0.5666 0.5686 0.5573 0.0045  -0.0020 -0.0252 666 HOH   B O   
3924 O O   . HOH   N .   ? 0.5848 0.5669 0.4533 -0.0134 -0.0645 -0.0010 667 HOH   B O   
3925 O O   . HOH   N .   ? 0.4973 0.5040 0.4911 0.0142  0.0080  -0.0348 668 HOH   B O   
3926 O O   . HOH   N .   ? 0.5679 0.5260 0.5449 0.0000  -0.0216 -0.0218 669 HOH   B O   
3927 O O   . HOH   N .   ? 0.5741 0.5514 0.5510 -0.0294 -0.0161 -0.0286 670 HOH   B O   
3928 O O   . HOH   N .   ? 0.5596 0.4909 0.5302 -0.0120 -0.0389 -0.0524 671 HOH   B O   
3929 O O   . HOH   N .   ? 0.7294 0.7236 0.7073 -0.0488 -0.0105 -0.0222 672 HOH   B O   
3930 O O   . HOH   N .   ? 0.6645 0.6080 0.6336 -0.0088 -0.0305 -0.0138 673 HOH   B O   
3931 O O   . HOH   N .   ? 0.7034 0.6119 0.6766 -0.0201 -0.0526 -0.0553 674 HOH   B O   
3932 O O   . HOH   N .   ? 0.4952 0.5633 0.5095 -0.0526 0.0099  -0.0426 675 HOH   B O   
3933 O O   . HOH   N .   ? 0.7522 0.7198 0.7339 0.0039  -0.0269 -0.0162 676 HOH   B O   
3934 O O   . HOH   N .   ? 0.5259 0.5097 0.4754 -0.0045 -0.0335 -0.0589 677 HOH   B O   
3935 O O   . HOH   N .   ? 0.5923 0.5492 0.5773 0.0093  -0.0235 -0.0275 678 HOH   B O   
3936 O O   . HOH   N .   ? 0.4482 0.4507 0.4354 0.0155  0.0072  -0.0390 679 HOH   B O   
3937 O O   . HOH   N .   ? 0.5728 0.5824 0.5692 0.0070  0.0042  -0.0282 680 HOH   B O   
3938 O O   . HOH   N .   ? 0.6692 0.6793 0.5697 -0.0066 -0.0018 -0.0247 681 HOH   B O   
3939 O O   . HOH   N .   ? 0.6163 0.6103 0.6627 0.0254  -0.0907 -0.0225 682 HOH   B O   
3940 O O   . HOH   N .   ? 0.4964 0.5780 0.5575 -0.0224 -0.0132 -0.0625 683 HOH   B O   
3941 O O   . HOH   N .   ? 0.5999 0.5755 0.5529 -0.0069 -0.0362 -0.0632 684 HOH   B O   
3942 O O   . HOH   N .   ? 0.4839 0.5173 0.4927 -0.0113 0.0006  -0.0398 685 HOH   B O   
3943 O O   . HOH   N .   ? 0.6440 0.6111 0.6351 0.0133  -0.0212 -0.0278 686 HOH   B O   
3944 O O   . HOH   N .   ? 0.6089 0.6047 0.4841 -0.0102 -0.0369 -0.0201 687 HOH   B O   
3945 O O   . HOH   N .   ? 0.6298 0.6754 0.6460 -0.0131 0.0054  -0.0433 688 HOH   B O   
3946 O O   . HOH   N .   ? 0.6524 0.6307 0.6398 -0.0364 -0.0317 -0.0446 689 HOH   B O   
3947 O O   . HOH   N .   ? 0.6573 0.6806 0.6279 -0.0021 0.0210  -0.0181 690 HOH   B O   
3948 O O   . HOH   N .   ? 0.5009 0.6012 0.5747 -0.0230 -0.0049 -0.0691 691 HOH   B O   
3949 O O   . HOH   N .   ? 0.6227 0.6931 0.6877 -0.0115 -0.0396 -0.0639 692 HOH   B O   
3950 O O   . HOH   N .   ? 0.6829 0.6633 0.6199 -0.0035 -0.0378 -0.0669 693 HOH   B O   
3951 O O   . HOH   N .   ? 0.6528 0.6945 0.5937 -0.0523 0.0083  -0.0181 694 HOH   B O   
3952 O O   . HOH   N .   ? 0.7018 0.6622 0.6822 -0.0325 -0.0387 -0.0494 695 HOH   B O   
3953 O O   . HOH   N .   ? 0.7147 0.5995 0.6908 -0.0194 -0.0639 -0.0585 696 HOH   B O   
3954 O O   . HOH   N .   ? 0.4771 0.4624 0.4316 -0.0033 -0.0274 -0.0541 697 HOH   B O   
3955 O O   . HOH   N .   ? 0.6728 0.5810 0.6436 -0.0021 -0.0525 -0.0747 698 HOH   B O   
3956 O O   . HOH   N .   ? 0.7433 0.7476 0.7095 0.0337  0.0042  -0.1008 699 HOH   B O   
3957 O O   . HOH   N .   ? 0.7033 0.7050 0.5924 -0.0053 -0.0218 -0.0331 700 HOH   B O   
3958 O O   . HOH   N .   ? 0.7854 0.7875 0.6545 -0.0106 -0.0256 -0.0270 701 HOH   B O   
3959 O O   . HOH   N .   ? 0.6599 0.6363 0.4941 -0.0192 -0.0942 0.0018  702 HOH   B O   
3960 O O   . HOH   N .   ? 0.5881 0.6672 0.7902 0.0547  -0.0599 -0.1140 703 HOH   B O   
3961 O O   . HOH   N .   ? 0.6281 0.6261 0.6001 -0.0548 -0.0073 -0.0172 704 HOH   B O   
3962 O O   . HOH   N .   ? 0.5980 0.6418 0.6301 -0.0274 -0.0364 -0.0580 705 HOH   B O   
# 
