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- PDB-3m5m: Avoiding drug resistance against HCV NS3/4A protease inhibitors -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 3m5m
TitleAvoiding drug resistance against HCV NS3/4A protease inhibitors
Components
  • FDEMEEC Peptide
  • NS3/4A
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HCV / Hepatitis C Virus / NS3 / protease / drug resistance / serine protease / chimera protein / fusion protein / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


symbiont-mediated suppression of host TRAF-mediated signal transduction => GO:0039527 / : / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity ...symbiont-mediated suppression of host TRAF-mediated signal transduction => GO:0039527 / : / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / lipid droplet / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / viral nucleocapsid / RNA helicase activity / membrane => GO:0016020 / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / RNA helicase / induction by virus of host autophagy / ribonucleoprotein complex / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / virion attachment to host cell / endoplasmic reticulum membrane / host cell plasma membrane / virion membrane / structural molecule activity / proteolysis / RNA binding / zinc ion binding / extracellular region / ATP binding / nucleus / plasma membrane / cytoplasm
Similarity search - Function
Thrombin, subunit H - #120 / Hepatitis C virus core protein, chain A superfamily / 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 ...Thrombin, subunit H - #120 / Hepatitis C virus core protein, chain A superfamily / 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 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 / 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 / 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 / Trypsin-like serine proteases / 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
Genome polyprotein / Capsid protein C
Similarity search - Component
Biological speciesHepatitis C virus subtype 1a
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.7 Å
AuthorsSchiffer, C.A. / Romano, K.P.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2010
Title: Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding.
Authors: Romano, K.P. / Ali, A. / Royer, W.E. / Schiffer, C.A.
History
DepositionMar 12, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 9, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 1.3Nov 8, 2017Group: Refinement description / Category: software
Remark 999The 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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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NS3/4A
B: NS3/4A
C: FDEMEEC Peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,5179
Polymers43,9033
Non-polymers6146
Water5,585310
1
A: NS3/4A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,0366
Polymers21,4871
Non-polymers5495
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: NS3/4A
C: FDEMEEC Peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,4813
Polymers22,4152
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)58.218, 60.093, 95.670
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein / Protein/peptide , 2 types, 3 molecules ABC

#1: Protein NS3/4A


Mass: 21487.330 Da / Num. of mol.: 2
Fragment: NS4A (UNP residues 1678-1688), NS3 (UNP residues 1027-1657)
Mutation: A1027S, P1028G, I1029D, L1039E, L1040E, I1043Q, I1044E, L1047Q, A1066T, C1073S, C1078L, I1098T, P1112Q, S1165A, C1185S, C1679S, V1686I, I1687N
Source method: isolated from a genetically manipulated source
Details: The protein crystallized is a single-chain construct of protease domain of hepatitis C virus NS3/4A, with cofactor 4A covalently linked at the N-terminus.
Source: (gene. exp.) Hepatitis C virus subtype 1a / Gene: NS3 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A8DG50, hepacivirin
#2: Protein/peptide FDEMEEC Peptide


Mass: 927.995 Da / Num. of mol.: 1 / Fragment: UNP residues 1706-1712 / Source method: obtained synthetically / Source: (synth.) Hepatitis C virus subtype 1a / References: UniProt: Q9WPH5

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Non-polymers , 4 types, 316 molecules

#3: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-ZN / ZINC ION


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


Mass: 18.015 Da / Num. of mol.: 310 / Source method: isolated from a natural source / Formula: H2O

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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: 1.91 Å3/Da / Density % sol: 35.46 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 100mM MES buffer pH 6.5, 4% (w/v) ammonium sulfate, 20-26% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 9, 2008
RadiationMonochromator: Bent Ge(111) monochromator / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 1.7→100 Å / Num. obs: 37615 / % possible obs: 99.8 % / Redundancy: 7.4 % / Rsym value: 0.078 / Net I/σ(I): 10.2
Reflection shellResolution: 1.7→1.76 Å / Redundancy: 7.5 % / Mean I/σ(I) obs: 4.782 / Rsym value: 0.404 / % possible all: 99.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACT3.1data extraction
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→50.9 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.954 / Occupancy max: 1 / Occupancy min: 0.38 / SU B: 4.576 / SU ML: 0.073 / SU R Cruickshank DPI: 0.117 / Cross valid method: THROUGHOUT / ESU R: 0.117 / ESU R Free: 0.108 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20565 1874 5 %RANDOM
Rwork0.17694 ---
obs0.17841 35681 99.72 %-
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 mean: 22.714 Å2
Baniso -1Baniso -2Baniso -3
1--1.81 Å20 Å20 Å2
2--3.2 Å20 Å2
3----1.39 Å2
Refinement stepCycle: LAST / Resolution: 1.7→50.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2912 0 29 310 3251
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0223011
X-RAY DIFFRACTIONr_bond_other_d0.0010.022001
X-RAY DIFFRACTIONr_angle_refined_deg1.2511.974100
X-RAY DIFFRACTIONr_angle_other_deg0.81534879
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2645404
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.53222.43107
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.87815467
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.8351527
X-RAY DIFFRACTIONr_chiral_restr0.0740.2481
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213387
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02596
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5351.51991
X-RAY DIFFRACTIONr_mcbond_other0.1461.5827
X-RAY DIFFRACTIONr_mcangle_it0.96423196
X-RAY DIFFRACTIONr_scbond_it1.58831020
X-RAY DIFFRACTIONr_scangle_it2.5534.5901
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.7→1.744 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.277 138 -
Rwork0.21 2590 -
obs--99.09 %
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)
111.0643-6.7529-13.589611.36689.16096.2641-0.08510.4205-0.2950.1201-0.090.3804-0.6358-0.65970.17510.06070.0746-0.04910.3004-0.09970.023839.807112.80775.6856
26.6864-0.8168-2.73430.64891.43144.4126-0.0019-0.0707-0.0084-0.0401-0.00450.04370.02710.03370.00640.1169-0.0055-0.00350.04340.00680.108724.616921.668320.6256
34.45224.40093.22374.07632.58167.4335-0.0768-0.27810.74870.24510.18810.4136-0.606-0.7824-0.11140.20260.11390.04350.3033-0.01580.204612.642925.859733.6209
40.88581.75231.07283.4641-4.33879.02190.0295-0.14870.0413-0.038-0.08-0.1281-0.4268-0.0540.05050.1415-0.00430.00410.1478-0.01920.146215.64722.944820.9825
58.50170.8201-0.51653.4305-0.95774.3523-0.18480.2337-0.2478-0.11490.03470.03960.1664-0.09230.15010.1326-0.01130.00560.1253-0.02590.113322.974818.69511.2474
61.52780.5976-0.13470.2869-0.00543.1289-0.0250.11560.0611-0.05150.03750.0078-0.0961-0.1842-0.01240.12260.0048-0.00210.0601-0.01230.125624.47222.705123.6814
70.9224-0.3272-0.15460.9648-0.52421.6918-0.0015-0.04170.03830.0129-0.0222-0.0515-0.04370.06870.02370.1121-0.0112-0.00080.0438-0.00760.123232.829920.533829.5068
82.5149-1.53180.242.4388-1.25083.3008-0.03420.08270.0663-0.1650.0381-0.1241-0.13730.0164-0.00380.1252-0.02110.00420.0444-0.00550.128232.545424.564318.0632
94.4859-1.64453.28122.3799-3.90426.9794-0.10020.19140.1397-0.0186-0.0964-0.1929-0.18270.36450.19650.1224-0.0290.01230.0889-0.0010.121436.773225.843420.5569
103.7414-1.5151-0.8781.2417-1.86374.1078-0.1264-0.18070.05560.1348-0.0071-0.1416-0.11690.20390.13350.1073-0.0098-0.01890.0798-0.00460.137438.805818.360631.6491
110.0419-0.48121.56714.1029-1.05674.48730.123-0.04150.3196-0.14870.0104-0.0849-0.6105-0.1145-0.13340.2470.01130.05330.03470.01220.247127.921831.08427.6801
126.84291.50211.41943.94140.77846.19-0.1048-0.0418-0.0402-0.2341-0.1476-0.1955-0.39190.11950.25240.2053-0.0033-0.0030.0918-0.0510.128327.827729.072846.6297
13-0.0531-0.70071.69532.0332.03219.91030.0423-0.0755-0.02180.10830.0228-0.0145-0.0576-0.2006-0.06510.159-0.05360.01060.1264-0.00460.09720.509419.368143.5548
142.6904-0.23765.05383.13671.61657.68560.13520.0246-0.06520.1162-0.19330.15940.3115-0.66290.05810.1007-0.02960.00120.2271-0.02630.101215.956415.765533.7358
155.4299-0.76910.51591.10720.2354.6606-0.0485-0.083-0.32830.120.0009-0.06660.352-0.00930.04760.2132-0.0338-0.01180.0533-0.00530.128926.252314.272748.0408
164.45392.6265-2.4893.9291-1.35172.435-0.030.09040.20690.08140.1370.25210.1399-0.1617-0.1070.1618-0.03610.00060.0353-0.01350.173717.66788.858537.4042
170.536-0.3549-0.09180.93772.87177.24180.0386-0.01310.0434-0.038-0.0878-0.0048-0.0916-0.25540.04930.1708-0.0157-0.00540.0472-0.0180.112824.518923.440240.7937
185.35913.6355-1.534312.1784-9.11335.58170.1424-0.3445-0.3185-0.324-0.3747-0.24880.33050.23550.23230.2024-0.0312-0.00010.06750.01120.142427.44489.407938.3506
194.72776.3352-0.50210.358-0.2638-0.47070.4038-0.2935-0.33460.5222-0.4638-0.36720.02790.10530.060.2464-0.0417-0.02430.0975-0.00130.116225.61268.198941.8429
206.04385.4452-6.99037.6109-5.246.45570.1039-0.38640.45410.4346-0.2084-0.2168-0.47650.72150.10440.2242-0.0754-0.07970.2208-0.03650.278537.7425.428839.2386
219.2849-0.9883-8.8888-1.21732.6085-0.0157-0.1090.1349-0.83450.0632-0.08330.4517-0.5683-0.49430.19230.07370.0378-0.06540.3812-0.18460.129838.87557.4355-39.507
225.87281.2302-1.8151-0.159-0.21095.8082-0.00790.05110.396-0.0104-0.00050.125-0.1912-0.10250.00840.1316-0.0077-0.00770.04890.03290.155521.771218.0329-24.0232
234.90912.54871.34212.09452.888510.5388-0.0391-0.43490.76250.24-0.07630.1844-0.6818-0.83460.11540.25740.0855-0.00140.2247-0.04610.268711.874620.7768-13.6282
246.43320.8834-2.7051.5305-2.86684.87090.1480.26160.28180.0252-0.1041-0.053-0.44370.2552-0.04390.1557-0.0378-0.02090.11950.01730.161416.12517.6484-27.5557
256.87840.2449-4.92562.9574-1.45882.1022-0.15380.4067-0.2089-0.09630.070500.1266-0.16780.08320.1223-0.036-0.00540.1981-0.00240.092523.018914.3478-35.2703
263.2121-2.3629-1.64953.5344-3.11837.820.35560.5456-0.0119-0.1597-0.310.206-1.112-0.3065-0.04560.2931-0.0012-0.05560.13340.06080.141325.237922.3581-32.7419
273.996-0.21510.18082.67310.68324.315-0.09450.1706-0.0438-0.03620.01930.02220.180.02610.07530.1161-0.0073-0.00020.05190.02280.132723.83413.9284-21.8318
282.7191-0.7604-0.09511.73560.19882.079-0.07940.15230.23770.11990.0373-0.056-0.06560.13650.04210.1076-0.0141-0.00450.05650.02410.123632.30916.2107-17.2669
292.4339-4.27181.25566.6005-3.47163.1383-0.14430.08630.1527-0.25730.1787-0.1358-0.27260.1111-0.03440.1979-0.1046-0.03740.1490.05860.148431.365820.7215-29.0198
301.0695-4.1837.92514.4095-9.222.0951-0.24710.24180.2908-0.0312-0.018-0.1475-0.52510.8590.26510.1115-0.0916-0.02910.20370.11680.199336.565820.9657-26.2525
314.0869-0.6382-0.36370.05680.08263.1042-0.110.02180.10840.04190.0712-0.0748-0.02290.16040.03880.1043-0.0085-0.00690.1140.00490.142438.756713.0885-15.3935
322.9709-3.3388-2.05293.94270.30896.75150.13350.34550.4782-0.1436-0.311-0.2154-0.78320.01420.17750.1948-0.0393-0.07280.04630.07780.338227.94725.5249-18.7402
330.5983-0.52420.24032.18211.08529.2074-0.054-0.41180.09830.2311-0.2379-0.0853-0.1974-0.20180.29190.1299-0.0089-0.02890.2118-0.04010.132423.745418.5944-0.3528
348.799-0.13231.03371.8731-0.47212.92460.04480.0726-0.1028-0.0981-0.1480.1601-0.0488-0.2920.10320.1164-0.0149-0.00640.0934-0.00740.125516.074511.1027-14.5448
354.0528-1.3823-0.17240.8363-1.54686.0159-0.0153-0.5860.01650.0798-0.084-0.09480.1745-0.17170.09920.1804-0.0696-0.00470.1831-0.01080.125725.18999.4851-0.7162
366.5693.1822-0.61041.999-0.05251.21570.1552-0.26190.23350.1703-0.10660.20370.0566-0.2668-0.04860.1733-0.0182-0.00840.09160.02980.16417.00043.2801-5.8059
371.35930.2616-0.36441.07441.90212.82310.0446-0.13510.0107-0.0634-0.1922-0.0081-0.0752-0.28230.14760.1633-0.0014-0.02140.1059-0.01570.154122.207813.4734-9.0128
382.12030.62290.27433.4316-0.13061.8279-0.0316-0.13350.0084-0.1064-0.0099-0.0577-0.03530.03260.04150.13350.0009-0.02050.0476-0.00150.105126.37919.0636-7.5232
395.80113.979-0.12025.4171-0.68781.25480.2663-0.2554-0.18440.2995-0.2481-0.13460.12070.1014-0.01810.1559-0.0123-0.01190.04990.02130.091826.87575.8759-5.409
403.4293.4914-0.391716.1665-9.01513.64960.0765-0.16560.18030.0209-0.0809-0.0362-0.55660.15570.00440.1267-0.0497-0.0030.1122-0.01130.2438.62520.3253-8.8226
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A983 - 988
2X-RAY DIFFRACTION2A989 - 997
3X-RAY DIFFRACTION3A998 - 1006
4X-RAY DIFFRACTION4A1007 - 1011
5X-RAY DIFFRACTION5A1012 - 1021
6X-RAY DIFFRACTION6A1022 - 1048
7X-RAY DIFFRACTION7A1049 - 1060
8X-RAY DIFFRACTION8A1061 - 1068
9X-RAY DIFFRACTION9A1069 - 1074
10X-RAY DIFFRACTION10A1075 - 1084
11X-RAY DIFFRACTION11A1085 - 1094
12X-RAY DIFFRACTION12A1095 - 1101
13X-RAY DIFFRACTION13A1102 - 1108
14X-RAY DIFFRACTION14A1109 - 1114
15X-RAY DIFFRACTION15A1115 - 1126
16X-RAY DIFFRACTION16A1127 - 1138
17X-RAY DIFFRACTION17A1139 - 1153
18X-RAY DIFFRACTION18A1154 - 1159
19X-RAY DIFFRACTION19A1160 - 1171
20X-RAY DIFFRACTION20A1172 - 1179
21X-RAY DIFFRACTION21B983 - 990
22X-RAY DIFFRACTION22B991 - 998
23X-RAY DIFFRACTION23B999 - 1007
24X-RAY DIFFRACTION24B1008 - 1012
25X-RAY DIFFRACTION25B1013 - 1020
26X-RAY DIFFRACTION26B1021 - 1029
27X-RAY DIFFRACTION27B1030 - 1045
28X-RAY DIFFRACTION28B1046 - 1061
29X-RAY DIFFRACTION29B1062 - 1068
30X-RAY DIFFRACTION30B1069 - 1074
31X-RAY DIFFRACTION31B1075 - 1084
32X-RAY DIFFRACTION32B1085 - 1094
33X-RAY DIFFRACTION33B1095 - 1106
34X-RAY DIFFRACTION34B1107 - 1112
35X-RAY DIFFRACTION35B1113 - 1123
36X-RAY DIFFRACTION36B1124 - 1134
37X-RAY DIFFRACTION37B1135 - 1148
38X-RAY DIFFRACTION38B1149 - 1160
39X-RAY DIFFRACTION39B1161 - 1173
40X-RAY DIFFRACTION40B1174 - 1179

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