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- PDB-3m5o: Crystal structure of HCV NS3/4A protease in complex with N-termin... -

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Basic information

Entry
Database: PDB / ID: 3m5o
TitleCrystal structure of HCV NS3/4A protease in complex with N-terminal product 5A5B
Components
  • NS3/4A
  • TEDVVCC peptide
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


host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / symbiont-mediated transformation of host cell / 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 / channel activity / viral nucleocapsid ...host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / symbiont-mediated transformation of host cell / 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 / channel activity / viral nucleocapsid / monoatomic ion transmembrane transport / clathrin-dependent endocytosis of virus by host cell / RNA helicase activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ribonucleoprotein complex / symbiont-mediated activation of host autophagy / 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 / virion attachment to host cell / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule 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 / 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 / Genome polyprotein
Similarity search - Component
Biological speciesHepatitis C virus subtype 1a
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.6 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: Advisory / Derived calculations ...Advisory / Derived calculations / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_distant_solvent_atoms ...entity_src_gen / pdbx_distant_solvent_atoms / software / struct_conn / struct_conn_type
Revision 1.3Nov 27, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_value_order / _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_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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: TEDVVCC peptide
D: TEDVVCC peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,7897
Polymers44,5624
Non-polymers2273
Water8,341463
1
A: NS3/4A
C: TEDVVCC peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,4434
Polymers22,2812
Non-polymers1612
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: NS3/4A
D: TEDVVCC peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,3473
Polymers22,2812
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)47.272, 58.885, 67.058
Angle α, β, γ (deg.)90.000, 99.220, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#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 / Strain: genotype 1a BID-V318 / Gene: NS3 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A8DG50, hepacivirin
#2: Protein/peptide TEDVVCC peptide


Mass: 793.906 Da / Num. of mol.: 2 / Fragment: UNP residues 2414-2420 / Source method: obtained synthetically / Source: (synth.) Hepatitis C virus subtype 1a / References: UniProt: A8DG50, UniProt: B3TKQ3*PLUS
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / 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.: 463 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.07 Å3/Da / Density % sol: 40.5 %
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-ID-B / Wavelength: 1.033 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Mar 10, 2009
RadiationMonochromator: Si (111) double-crystal monochromator / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionRedundancy: 3.3 % / Number: 150463 / Rmerge(I) obs: 0.054 / Χ2: 1.06 / D res high: 1.6 Å / D res low: 50 Å / Num. obs: 45685 / % possible obs: 94.7
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
3.455059.910.0521.0172.4
2.743.4592.510.0431.0343.1
2.392.749910.0481.083.4
2.172.3999.310.0551.0853.4
2.022.1799.510.0581.0923.4
1.92.0299.610.0671.0713.4
1.81.999.610.0781.0653.4
1.721.899.610.0811.0343.4
1.661.7299.510.091.0583.4
1.61.6699.110.0971.0363.3
ReflectionResolution: 1.6→50 Å / Num. obs: 45685 / % possible obs: 94.7 % / Redundancy: 3.3 % / Rsym value: 0.074 / Net I/σ(I): 17.4
Reflection shellResolution: 1.6→1.66 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 13.303 / Rsym value: 0.106 / % possible all: 99.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
HKL-2000data reduction
PHASERphasing
REFMAC5.5.0102refinement
PDB_EXTRACT3.1data extraction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.6→50 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.917 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 3.156 / SU ML: 0.056 / SU R Cruickshank DPI: 0.103 / Cross valid method: THROUGHOUT / ESU R: 0.104 / ESU R Free: 0.107 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22625 2294 5 %RANDOM
Rwork0.17982 ---
obs0.18214 43288 94.36 %-
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: 23.238 Å2
Baniso -1Baniso -2Baniso -3
1--0.22 Å20 Å2-0.21 Å2
2---0.56 Å20 Å2
3---0.71 Å2
Refinement stepCycle: LAST / Resolution: 1.6→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3022 0 7 463 3492
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0223116
X-RAY DIFFRACTIONr_bond_other_d0.0010.022090
X-RAY DIFFRACTIONr_angle_refined_deg1.261.9634244
X-RAY DIFFRACTIONr_angle_other_deg0.82835108
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0235422
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.94222.632114
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.74415506
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.4991528
X-RAY DIFFRACTIONr_chiral_restr0.0780.2500
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213508
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02612
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_it0.5721.52054
X-RAY DIFFRACTIONr_mcbond_other0.1591.5850
X-RAY DIFFRACTIONr_mcangle_it1.06623316
X-RAY DIFFRACTIONr_scbond_it1.83731062
X-RAY DIFFRACTIONr_scangle_it2.9994.5920
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.6→1.639 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.19 163 -
Rwork0.161 3286 -
obs--96.96 %
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)
14.1207-11.6087-2.782622.46647.4303-0.96140.483-0.40611.8536-1.20650.645-3.3072-0.5245-0.057-1.1280.0947-0.02090.25350.2368-0.28780.883622.8884-10.4572-37.2359
22.1854-0.06740.43563.52220.18540.3939-0.0574-0.06890.0680.10010.0576-0.0544-0.02620.0338-0.00020.0332-0.00190.00220.02910.00080.0296.51046.5383-28.5609
322.865911.5884-5.985811.6201-14.243115.72070.9607-1.45383.16611.4406-0.12151.7182-1.4694-0.6288-0.83920.20070.10.11890.5162-0.3580.6049-7.078617.9154-25.5271
44.4118-1.82651.07053.2287-0.39351.16030.0268-0.12010.0222-0.0139-0.0404-0.06870.0080.03670.01350.0626-0.0118-0.00430.02070.00070.06158.689414.2124-29.2892
57.8513-0.1346-1.74794.9315-2.33013.3770.15790.1034-0.136-0.0715-0.2001-0.09130.02850.15140.04220.01350.0068-0.00460.02080.0070.080717.64753.7552-29.5488
615.1069-23.8627-8.135941.00448.29387.3153-0.3271-0.74310.73890.87030.5424-1.3351-0.26670.745-0.21530.18250.0896-0.09350.2924-0.07860.104614.13414.8005-21.2991
74.3647-0.5572-0.53233.2683-0.02884.628-0.052-0.34860.17640.4393-0.0189-0.0356-0.03590.00080.07090.073-0.01540.00310.0396-0.02650.04381.26788.6676-23.2621
83.64340.428-0.14252.2685-0.93171.3135-0.04470.2691-0.0319-0.07240.0069-0.0360.131-0.08070.03780.0336-0.00550.00530.0298-0.00840.01562.17912.8676-32.1504
91.7076-0.63140.41221.14350.43290.55660.04030.0065-0.1040.0175-0.03190.02530.00660.0121-0.00850.0391-0.0020.00030.01680.01260.04081.393-3.8333-32.1767
104.44952.45781.95595.36831.75071.49690.1391-0.3319-0.04860.3446-0.1127-0.15350.1405-0.0432-0.02650.0563-0.0096-0.01750.04930.0190.0379.0031-4.1262-23.1812
112.50130.5610.2283.39670.24670.27710.05020.0202-0.07520.0749-0.11570.16280.0137-0.08480.06550.04050.001-0.00370.0373-0.01340.0635-2.9728-9.4441-33.446
123.41940.1883-0.59655.16454.19933.45010.0465-0.35280.10850.33730.1421-0.1910.24160.1865-0.18860.14750.0025-0.00770.0730.00170.04392.3062-0.5586-20.7803
1310.4183-2.22734.17511.0592-0.97681.6160.0276-0.6693-0.0445-0.01280.02280.13260.0264-0.252-0.05040.0534-0.00920.02980.12710.01280.0656-15.53324.2224-24.7223
1410.72771.6489-0.33222.17-0.16311.693-0.1026-0.00150.2639-0.03310.0674-0.0255-0.0881-0.00660.03520.0391-0.0024-0.00790.03150.00750.0404-8.169711.8963-35.2859
152.3024-0.44810.23093.50310.47632.15560.0770.1635-0.0601-0.1371-0.00370.2786-0.0135-0.0842-0.07330.0177-0.0015-0.01010.064-0.00170.0625-17.30625.7897-40.799
162.1394-2.0225.34531.8771-5.159713.8078-0.19460.11620.12240.1293-0.0377-0.1031-0.36660.0770.23230.1146-0.0267-0.00110.08750.01890.061-3.99879.4532-43.2714
174.703-2.309-0.95744.53971.09430.7158-0.0699-0.20030.02310.17520.11950.12010.0880.0025-0.04950.024-0.01460.01110.06860.00340.0367-13.38375.8893-29.2692
181.87911.34533.94391.4341.39219.7682-0.0647-0.01060.053-0.1063-0.0873-0.0158-0.08590.11130.1520.0970.0453-0.01330.0818-0.00470.0518-7.94951.7234-43.2236
190.7820.2282-0.88591.8129-2.13445.92190.02440.1522-0.0644-0.14640.12380.13180.0163-0.2307-0.14820.0384-0.0108-0.02470.0637-0.00620.0548-11.21653.2115-45.4375
209.0615-0.57644.52177.5123-4.21083.8465-0.0073-0.5495-0.36010.37580.31060.3733-0.1764-0.4247-0.30330.0947-0.01440.05470.08630.02730.1278-11.2529-7.7093-27.2442
216.038414.7077.266527.296515.05147.35591.4406-0.5098-1.47482.7728-0.5245-1.9961.7595-0.6787-0.91610.3455-0.1425-0.30320.6393-0.28330.437216.273436.90089.3693
222.99610.53580.73993.88110.07842.1786-0.09260.1199-0.1593-0.10410.109-0.06420.08280.0525-0.01630.06410.0090.01880.01-0.00060.03112.141819.8308-3.4622
235.6773-3.22261.43065.7178-1.28261.19550.11440.7326-0.4471-1.1219-0.01230.31570.4107-0.0856-0.10210.3845-0.1154-0.04990.2112-0.06290.1115-7.42237.9427-9.5636
243.6654-0.5543-1.15586.0142-0.46810.23780.21770.06780.36580.3775-0.2295-0.4199-0.10450.12030.01180.1416-0.02630.0040.13330.04520.1497.710613.5123-1.4738
254.60550.3347-0.47881.89-0.78282.2353-0.0944-0.0712-0.40620.17090.0154-0.45030.31890.41860.0790.15080.1116-0.02160.1162-0.00840.163911.780521.636-4.7365
264.42540.39542.57444.61752.33237.84810.0455-0.0865-0.0901-0.0325-0.0853-0.0973-0.0322-0.00940.03980.0703-0.0010.00650.01070.01380.0233-0.52219.7793-2.4835
272.17520.6797-0.48831.6146-0.68450.39110.03740.06780.1116-0.0940.00380.03650.0696-0.0154-0.04120.07780.0063-0.01020.02310.01770.0184-5.162126.9232-3.7872
283.4773-0.6406-0.74443.98630.35022.16140.08520.25290.1224-0.199-0.0475-0.28520.02180.0685-0.03770.08040.00680.01530.0280.01830.04695.731330.1062-6.7147
294.07110.7908-0.38251.71040.53651.79760.13610.01120.3131-0.1247-0.09360.2828-0.043-0.1275-0.04250.07480.01910.00830.01650.00780.089-8.206135.2544-1.9581
302.127-0.37030.03676.35774.51637.47120.19750.35420.0975-0.45670.2832-0.4815-0.10270.4315-0.48070.09970.00940.02230.0909-0.00550.06120.707727.3136-11.7375
3111.12950.4441.51792.5057-0.14330.13090.04140.4738-0.1971-0.04570.01370.10850.01940.0626-0.05510.11440.0089-0.05030.11530.01450.028-16.543321.706-13.4328
326.7525-1.96981.98242.1584-0.79342.6518-0.02150.1239-0.2147-0.07360.09670.05540.0926-0.1697-0.07530.0882-0.0224-0.0090.04630.02240.0521-14.407913.7434-2.2755
331.31350.26760.05685.0357-0.02070.4285-0.0336-0.21460.09620.14420.12230.26080.0205-0.1656-0.08860.05170.0107-0.02330.13130.04520.0699-24.2321.4493-0.9357
341.7568-1.62031.37235.0828-2.67781.43570.0153-0.1322-0.0362-0.11150.1570.34940.0442-0.1245-0.17230.09040.0048-0.0060.15470.05550.0627-22.504916.41234.8659
358.06216.528-7.28566.1264-4.65577.74140.0393-0.1969-0.160.0715-0.1282-0.17040.02320.18590.08890.0780.0171-0.01280.08180.04480.0532-11.583215.64477.9254
3612.8483.67759.45083.08794.12358.02990.03950.0327-0.0797-0.09180.0754-0.0006-0.1098-0.0798-0.11490.09540.0245-0.0150.13960.08090.0505-15.523119.3461-6.0796
372.31591.17180.90130.61510.33054.3863-0.05880.1040.1043-0.01970.03650.1171-0.07740.16470.02220.07150.019-0.00940.05460.00840.0873-15.712222.7985-4.1535
380.7432-1.68733.5499.2082-7.527911.7337-0.04950.03360.16661.02910.10680.7189-0.60760.0022-0.05720.22910.04010.16810.08710.05650.2777-20.335819.270914.6682
392.1781.7517-1.65833.8601-2.61554.93460.0158-0.19150.18130.11660.1530.2594-0.0364-0.1638-0.16880.05380.01850.00090.09420.0440.0958-19.102824.951.7519
4018.0998-3.0913.55411.1651-2.12711.22950.03941.40061.5697-0.1597-0.16760.0450.10590.06020.12820.09470.0778-0.02350.23850.15480.2385-14.431434.3466-9.3645
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A982 - 989
2X-RAY DIFFRACTION2A990 - 998
3X-RAY DIFFRACTION3A999 - 1005
4X-RAY DIFFRACTION4A1006 - 1014
5X-RAY DIFFRACTION5A1015 - 1022
6X-RAY DIFFRACTION6A1023 - 1027
7X-RAY DIFFRACTION7A1028 - 1035
8X-RAY DIFFRACTION8A1036 - 1049
9X-RAY DIFFRACTION9A1050 - 1062
10X-RAY DIFFRACTION10A1063 - 1074
11X-RAY DIFFRACTION11A1075 - 1083
12X-RAY DIFFRACTION12A1084 - 1091
13X-RAY DIFFRACTION13A1092 - 1102
14X-RAY DIFFRACTION14A1103 - 1113
15X-RAY DIFFRACTION15A1114 - 1129
16X-RAY DIFFRACTION16A1130 - 1140
17X-RAY DIFFRACTION17A1141 - 1153
18X-RAY DIFFRACTION18A1154 - 1159
19X-RAY DIFFRACTION19A1160 - 1171
20X-RAY DIFFRACTION20A1172 - 1179
21X-RAY DIFFRACTION21B982 - 988
22X-RAY DIFFRACTION22B989 - 999
23X-RAY DIFFRACTION23B1000 - 1008
24X-RAY DIFFRACTION24B1009 - 1014
25X-RAY DIFFRACTION25B1015 - 1029
26X-RAY DIFFRACTION26B1030 - 1041
27X-RAY DIFFRACTION27B1042 - 1061
28X-RAY DIFFRACTION28B1062 - 1074
29X-RAY DIFFRACTION29B1075 - 1083
30X-RAY DIFFRACTION30B1084 - 1089
31X-RAY DIFFRACTION31B1090 - 1102
32X-RAY DIFFRACTION32B1103 - 1113
33X-RAY DIFFRACTION33B1114 - 1122
34X-RAY DIFFRACTION34B1123 - 1130
35X-RAY DIFFRACTION35B1131 - 1138
36X-RAY DIFFRACTION36B1139 - 1146
37X-RAY DIFFRACTION37B1147 - 1157
38X-RAY DIFFRACTION38B1158 - 1164
39X-RAY DIFFRACTION39B1165 - 1171
40X-RAY DIFFRACTION40B1172 - 1179

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