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- PDB-3su4: Crystal structure of NS3/4A protease variant R155K in complex wit... -

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Basic information

Entry
Database: PDB / ID: 3su4
TitleCrystal structure of NS3/4A protease variant R155K in complex with vaniprevir
ComponentsNS3 protease,NS4A protein
KeywordsHYDROLASE/INHIBITOR / drug resistance / drug design / Protease inhibitors / serine protease / VIRAL PROTEIN / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated transformation of host cell / symbiont-mediated suppression of host TRAF-mediated signal transduction / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / host cell membrane / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / serine-type peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity ...hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated transformation of host cell / symbiont-mediated suppression of host TRAF-mediated signal transduction / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / host cell membrane / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / serine-type peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / SH3 domain binding / viral capsid / host cell / nucleoside-triphosphate phosphatase / channel activity / viral nucleocapsid / monoatomic ion transmembrane transport / clathrin-dependent endocytosis of virus by host cell / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ribonucleoprotein complex / viral translational frameshifting / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / serine-type endopeptidase activity / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
Thrombin, subunit H - #120 / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus core protein, chain A superfamily ...Thrombin, subunit H - #120 / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus core protein, chain A superfamily / : / Hepatitis C virus non-structural protein NS4b / Hepatitis C virus capsid protein / Hepatitis C virus, Non-structural protein NS2 / Hepatitis C virus, Non-structural 5a protein / Hepatitis C virus, Non-structural 5a protein, domain 1a / Hepatitis C virus non-structural 5a, 1B domain / NS5A domain 1a superfamily / : / Hepatitis C virus non-structural 5a protein membrane anchor / Hepatitis C virus non-structural 5a zinc finger domain / Hepatitis C virus non-structural 5a domain 1b / NS3 RNA helicase, C-terminal helical domain / Hepacivirus nonstructural protein 2 (NS2) protease domain profile. / Hepatitis C virus, Non-structural protein NS4a / Hepatitis C virus non-structural protein NS4a / Hepatitis C virus, Core protein, C-terminal / Hepatitis C virus core protein / Hepatitis C virus, Non-structural protein E2/NS1 / Hepatitis C virus non-structural protein E2/NS1 / Hepatitis C virus, Envelope glycoprotein E1 / Hepatitis C virus envelope glycoprotein E1 / RNA dependent RNA polymerase, hepatitis C virus / Viral RNA dependent RNA polymerase / Hepatitis C virus, NS3 protease, Peptidase S29 / Hepatitis C virus NS3 protease / Hepacivirus/Pegivirus NS3 protease domain profile. / DEAD box, Flavivirus / Flavivirus DEAD domain / helicase superfamily c-terminal domain / Trypsin-like serine proteases / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Thrombin, subunit H / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Chem-SU3 / Genome polyprotein / Polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesHepatitis C virus subtype 1a
Hepatitis C virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.255 Å
AuthorsSchiffer, C.A. / Romano, K.P.
CitationJournal: Plos Pathog. / Year: 2012
Title: The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors.
Authors: Romano, K.P. / Ali, A. / Aydin, C. / Soumana, D. / Ozen, A. / Deveau, L.M. / Silver, C. / Cao, H. / Newton, A. / Petropoulos, C.J. / Huang, W. / Schiffer, C.A.
History
DepositionJul 11, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 5, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 21, 2017Group: Database references / Source and taxonomy / Structure summary
Category: entity / entity_src_gen ...entity / entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity.pdbx_fragment ..._entity.pdbx_description / _entity.pdbx_fragment / _entity.pdbx_mutation / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3Feb 28, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NS3 protease,NS4A protein
B: NS3 protease,NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,7578
Polymers42,9192
Non-polymers1,8396
Water2,360131
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A: NS3 protease,NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,4755
Polymers21,4591
Non-polymers1,0154
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: NS3 protease,NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,2833
Polymers21,4591
Non-polymers8232
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1380 Å2
ΔGint-29 kcal/mol
Surface area15620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.762, 85.762, 97.414
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number169
Space group name H-MP61

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Components

#1: Protein NS3 protease,NS4A protein


Mass: 21459.316 Da / Num. of mol.: 2
Fragment: NS4A (UNP residues 1674-1687), NS3 (UNP residues 29-211)
Mutation: A1027S, P1028G, I1029D, L1039E, L1040E, I1043Q, I1044E, L1047Q, C1073S, C1078L, I1098T, P1112Q, S1165A, C1185S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hepatitis C virus subtype 1a, (gene. exp.) Hepatitis C virus
Plasmid: PET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: A8DG50, UniProt: B4YYL7, UniProt: P26664*PLUS
#2: Chemical ChemComp-SU3 / (5R,7S,10S)-10-tert-butyl-N-{(1R,2R)-1-[(cyclopropylsulfonyl)carbamoyl]-2-ethylcyclopropyl}-15,15-dimethyl-3,9,12-trioxo-6,7,9,10,11,12,14,15,16,17,18,19-dodecahydro-1H,5H-2,23:5,8-dimethano-4,13,2,8,11-benzodioxatriazacyclohenicosine-7(3H)-carboxamide / vaniprevir / MK-7009


Mass: 757.936 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C38H55N5O9S
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 131 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer detailsVANIPREVIR (MK-7009) IS A MACROCYCLIC, PEPTIDOMIMETIC HCV NS3/4A PROTEASE INHIBITOR FROM MERCK. THE ...VANIPREVIR (MK-7009) IS A MACROCYCLIC, PEPTIDOMIMETIC HCV NS3/4A PROTEASE INHIBITOR FROM MERCK. THE DRUG MIMICS THE PEPTIDE BACKBONE OF PROTEINS, ALTHOUGH THE DRUG MOIETIES CANNOT BE SEQUENCED USING AMINO ACID NOMENCLATURE.
Sequence detailsTHE COFACTOR 4A RESIDUES 990-1000 (GLY SER VAL VAL ILE VAL GLY ARG ILE ASN LEU) IN THIS ENTRY ...THE COFACTOR 4A RESIDUES 990-1000 (GLY SER VAL VAL ILE VAL GLY ARG ILE ASN LEU) IN THIS ENTRY CORRESPOND TO RESIDUES NUMBERING 1678-1688 OF DATABASE SEQUENCE REFERENCE (UNP A8DG50). THIS PEPTIDE IS COVALENTLY LINKED TO THE N-TERMINUS OF NS3. C1679S MUTATION WAS ENGINEERED TO PREVENT DISULFIDE FORMATION. THE V1686I AND I1687N WERE ENGINEERED TO OPTIMIZE THE LINKER BETWEEN THE COFACTOR 4A AND NS3

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.41 Å3/Da / Density % sol: 48.95 %
Crystal growTemperature: 295 K / Method: hanging drop, vapor diffusion / pH: 6.2
Details: 20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, hanging drop, vapor diffusion, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorDate: Dec 7, 2010
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.25→50 Å / Num. obs: 19213 / % possible obs: 99.9 % / Redundancy: 7.9 % / Rmerge(I) obs: 0.103 / Χ2: 1 / Net I/σ(I): 7.2
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.25-2.337.90.436190911100
2.33-2.4280.356191011100
2.42-2.5380.308191411100
2.53-2.677.90.257191511100
2.67-2.8380.186192611100
2.83-3.0580.137191911100
3.05-3.3680.10919021199.9
3.36-3.857.90.0919461199.8
3.85-4.857.90.06819101199.7
4.85-507.80.04519621.001199

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACT3.1data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.255→42.88 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.926 / WRfactor Rfree: 0.2198 / WRfactor Rwork: 0.1713 / Occupancy max: 1 / Occupancy min: 0.25 / FOM work R set: 0.8725 / SU B: 9.359 / SU ML: 0.123 / SU R Cruickshank DPI: 0.2609 / SU Rfree: 0.2067 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.207 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2233 987 5.1 %RANDOM
Rwork0.1668 ---
obs0.1695 19181 99.85 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso max: 79 Å2 / Biso mean: 30.6072 Å2 / Biso min: 12.9 Å2
Baniso -1Baniso -2Baniso -3
1--1.07 Å2-0.54 Å20 Å2
2---1.07 Å20 Å2
3---1.61 Å2
Refinement stepCycle: LAST / Resolution: 2.255→42.88 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2707 0 118 131 2956
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0222879
X-RAY DIFFRACTIONr_bond_other_d0.0010.021833
X-RAY DIFFRACTIONr_angle_refined_deg1.2632.0043960
X-RAY DIFFRACTIONr_angle_other_deg0.7913.0064388
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1195382
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.91422.47185
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.84115388
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.9751519
X-RAY DIFFRACTIONr_chiral_restr0.0660.2478
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0213217
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02544
X-RAY DIFFRACTIONr_mcbond_it0.4581.51908
X-RAY DIFFRACTIONr_mcbond_other0.0891.5792
X-RAY DIFFRACTIONr_mcangle_it0.84423052
X-RAY DIFFRACTIONr_scbond_it1.1763971
X-RAY DIFFRACTIONr_scangle_it1.8274.5896
LS refinement shellResolution: 2.255→2.314 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.274 98 -
Rwork0.191 1321 -
all-1419 -
obs--99.72 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
1-3.7228-6.98680.06915.132-0.24423.4989-0.16740.11040.37570.0169-0.0862-0.2063-0.63730.39180.25350.2267-0.0002-0.05460.13550.07380.08734.650516.8861-3.0039
24.87346.7884-2.68221.1634-1.32017.52280.2456-0.00170.7597-0.3355-0.21022.21390.1264-1.059-0.03540.06720.0467-0.08970.3901-0.01170.337616.05645.295-0.7005
38.36652.9665-3.73015.66430.292919.3194-0.28260.0834-0.0134-0.5377-0.25560.2813-0.3711-0.41220.53820.09520.0758-0.08390.1450.00220.075923.454211.7277-9.0428
43.75473.27262.44553.03893.73168.7016-0.11970.21490.1676-0.26510.14930.031-0.69970.4179-0.02960.23520.042-0.03470.12960.09550.110431.108519.6637-8.6951
5-0.9455-0.5894-1.497530.2437-18.641114.96280.2490.0270.104-0.7192-0.06680.3508-0.2847-1.2707-0.18220.2440.1374-0.11680.43-0.0920.22719.32513.65571.5644
65.747-3.3844-0.49456.0207-0.32266.1413-0.43330.88060.1696-0.50320.099-0.27330.03190.02420.33430.2222-0.0212-0.01810.1872-0.00890.075132.86749.5248-3.5126
7-0.15580.25031.07981.5346-0.4711.29390.0204-0.01410.0671-0.0859-0.0740.0173-0.065-0.05820.05360.130.0109-0.00610.109-0.01410.12231.141310.73497.166
812.6925-8.46525.55836.4388-5.20464.40460.10020.13860.4453-0.4483-0.2382-0.5116-0.13050.03450.1380.24120.00670.00970.08510.04780.159635.388118.96381.1022
91.7993-2.55485.29961.58-3.635912.2364-0.1475-0.16150.0958-0.030.1788-0.0548-0.478-0.3637-0.03140.2209-0.0098-0.05290.0705-0.01220.246832.793922.2985.8563
104.0907-2.5087-1.27122.18590.9170.92380.0505-0.06630.2881-0.0151-0.0209-0.258-0.1158-0.0186-0.02960.1123-0.0044-0.01580.0938-0.0130.138634.838413.415310.6864
112.06590.21950.30958.3621-2.02394.6977-0.0767-0.0445-0.12520.8260.07840.6564-0.0188-0.585-0.00180.0633-0.02730.07740.1726-0.06220.097219.45954.477714.3072
1212.82911.88-0.44193.8208-7.842419.55940.08880.31130.0643-0.4357-0.46250.188-0.12660.44010.37370.21210.0784-0.02950.1125-0.06740.136925.1174-0.06440.3435
137.2907-5.38328.790310.8884-5.56664.27680.2944-0.3982-0.0796-0.3667-0.26860.53030.5757-0.6187-0.02580.1912-0.08310.03410.2056-0.05930.154522.2648-6.21797.3772
1416.29847.61422.91696.7726-6.27516.1738-0.2907-0.479-0.30020.29520.0615-0.30030.43070.33990.22920.4190.0708-0.0120.18310.03660.038730.5082-5.108918.5082
150.9008-1.43624.37768.729214.050231.60880.1917-0.2683-0.28880.5009-0.19960.72861.2719-0.91210.00790.2259-0.09060.01850.0974-0.03720.177426.8598-11.38937.5907
163.3676-7.44962.124921.03943.69734.51860.01930.25-0.3106-0.2702-0.07350.2543-0.27410.05260.05410.1475-0.0099-0.02690.1117-0.04570.194131.5835-6.0985-1.0911
177.69541.9955-5.46471.6228-1.87627.80920.2453-0.18980.24630.1113-0.21030.2263-0.0583-0.1755-0.0350.1176-0.00760.00690.1319-0.03390.115223.56941.50768.9619
180.60390.5078-0.8164.15611.25850.88140.1274-0.1382-0.07390.1319-0.08490.12320.1191-0.0736-0.04250.167-0.0083-0.04390.1650.02060.10829.06050.19510.8062
193.3554-0.6256-1.6842.92053.13444.73390.0335-0.0466-0.32780.5105-0.11430.09140.5971-0.15410.08080.1604-0.0016-0.03530.07750.02750.109232.8043-4.778710.2881
209.5472-7.5305-0.927713.34821.47377.36870.1287-0.43530.00970.4703-0.21150.09580.173-0.47590.08280.1222-0.0041-0.02210.1456-0.03810.125330.300511.609120.246
215.0423-1.3045-2.38691.92494.8451.562-0.1214-0.1434-0.1932-0.0951-0.2024-0.01820.4843-0.10630.32390.4726-0.04210.01510.1293-0.03170.097554.3573-13.4153-3.131
224.555611.09648.879225.22379.739114.3907-0.36650.4874-0.9908-0.54190.7828-2.0117-0.36581.1182-0.41620.12060.05970.10550.2512-0.01560.313470.5588-4.73432.4353
232.84444.74362.944221.76968.48177.2763-0.19680.6236-0.4128-0.47310.3537-1.3140.36850.6982-0.15690.23430.04540.13150.21590.00190.132667.1365-5.9586-4.5947
246.81221.97550.73171.18822.90657.3615-0.40790.8229-0.1647-0.17830.1109-0.12710.68980.12930.29710.4619-0.0070.05050.1231-0.06460.139157.8206-16.9522-6.4422
2511.5154-0.323.35455.8092-2.81786.3493-0.01920.3969-0.1513-0.2438-0.1078-0.16360.25090.77660.1270.15980.00640.06470.0741-0.02230.077561.0642-8.26571.4782
2612.96744.74992.072419.61690.91817.0584-0.46440.361-0.2845-1.19060.66660.19710.0128-0.9074-0.20220.2064-0.0245-0.05870.19380.04560.069950.6296-6.1128-3.4758
270.1350.1003-0.65981.61780.43570.31370.0614-0.0556-0.037-0.1795-0.0441-0.06870.0034-0.0072-0.01720.15850.0007-0.02340.11760.02010.134954.7627-9.20228.4138
2819.984-6.0588-7.29194.50128.08087.4684-0.6464-0.1915-0.118-0.47970.44040.25220.00860.13340.2060.4078-0.1521-0.07680.06740.01710.113550.6291-16.7871.1295
290.27850.2286-3.3416-0.6088-1.371412.5841-0.2252-0.1673-0.1227-0.08880.1874-0.0781.19270.0790.03780.3156-0.0284-0.00880.1592-0.04620.322552.7666-20.31395.9488
305.363-3.3219-0.26283.07010.21663.09480.09630.0416-0.3111-0.1467-0.04440.21950.1062-0.035-0.05190.1267-0.0206-0.020.0570.03380.130651.6569-12.025310.3746
312.4150.1802-0.31675.29340.27162.7797-0.0109-0.10890.06680.36420.1338-0.5131-0.14890.5063-0.1230.1336-0.0142-0.03950.10270.00970.084865.8605-1.970515.9011
3213.96532.97782.0127.242416.23682.7386-0.11920.68930.1035-0.2720.03610.0206-0.39530.38120.08310.1528-0.02990.00230.11980.05840.1662.10511.68150.4839
33-0.4832-0.83441.61473.92690.74777.5899-0.10540.0438-0.04830.39190.03180.033-0.30530.13310.07360.1879-0.05860.02130.0709-0.0140.154260.43337.36114.7023
34-0.00370.0525-1.13891.3586-0.31934.56890.04220.0080.13860.0618-0.12980.0149-0.0753-0.07750.08760.1683-0.03510.03290.1412-0.01080.183357.238911.18037.5713
359.14137.327-3.638211.0215-7.00697.3815-0.06460.1460.2949-0.66230.01290.36980.11930.01430.05180.12930.01690.00810.1065-0.00630.098855.98254.10920.6269
366.03462.62161.81152.51721.86224.89230.1067-0.12890.05640.1021-0.071-0.0879-0.0370.2148-0.03570.12190.002-0.00870.11990.01220.129764.0558-1.293813.9111
378.3241-2.45873.4669.2664-0.6711.6670.1539-0.17080.52930.0811-0.0614-0.3-0.2053-0.2065-0.09240.17040.03540.07050.07150.02060.13951.2246.82638.7808
385.5271-0.610.27016.7866-3.67629.24670.1550.00050.56570.16450.27780.1593-0.5127-0.0426-0.43280.1188-0.01930.05390.0832-0.00420.216252.8111.15718.2717
391.447-0.6842.88259.8128-2.34060.2956-0.2101-0.15390.04050.33550.1635-0.1469-0.31150.07360.04660.1999-0.01460.01670.13680.02430.14455.3153-3.919817.773
4010.5934-4.1681-2.03376.3159-2.62969.44780.0483-0.6474-0.17920.5288-0.10760.02040.22470.07140.05940.13980.0088-0.00530.14420.04030.151354.3096-12.592421.7737
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A990 - 995
2X-RAY DIFFRACTION2A996 - 1007
3X-RAY DIFFRACTION3A1008 - 1012
4X-RAY DIFFRACTION4A1013 - 1027
5X-RAY DIFFRACTION5A1028 - 1033
6X-RAY DIFFRACTION6A1034 - 1042
7X-RAY DIFFRACTION7A1043 - 1060
8X-RAY DIFFRACTION8A1061 - 1066
9X-RAY DIFFRACTION9A1067 - 1075
10X-RAY DIFFRACTION10A1076 - 1088
11X-RAY DIFFRACTION11A1089 - 1105
12X-RAY DIFFRACTION12A1106 - 1110
13X-RAY DIFFRACTION13A1111 - 1117
14X-RAY DIFFRACTION14A1118 - 1123
15X-RAY DIFFRACTION15A1124 - 1130
16X-RAY DIFFRACTION16A1131 - 1136
17X-RAY DIFFRACTION17A1137 - 1147
18X-RAY DIFFRACTION18A1148 - 1159
19X-RAY DIFFRACTION19A1160 - 1172
20X-RAY DIFFRACTION20A1173 - 1180
21X-RAY DIFFRACTION21B990 - 996
22X-RAY DIFFRACTION22B997 - 1003
23X-RAY DIFFRACTION23B1004 - 1012
24X-RAY DIFFRACTION24B1013 - 1031
25X-RAY DIFFRACTION25B1032 - 1037
26X-RAY DIFFRACTION26B1038 - 1043
27X-RAY DIFFRACTION27B1044 - 1060
28X-RAY DIFFRACTION28B1061 - 1066
29X-RAY DIFFRACTION29B1067 - 1075
30X-RAY DIFFRACTION30B1076 - 1089
31X-RAY DIFFRACTION31B1090 - 1106
32X-RAY DIFFRACTION32B1107 - 1111
33X-RAY DIFFRACTION33B1112 - 1122
34X-RAY DIFFRACTION34B1123 - 1133
35X-RAY DIFFRACTION35B1134 - 1139
36X-RAY DIFFRACTION36B1140 - 1153
37X-RAY DIFFRACTION37B1154 - 1160
38X-RAY DIFFRACTION38B1161 - 1168
39X-RAY DIFFRACTION39B1169 - 1175
40X-RAY DIFFRACTION40B1176 - 1180

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