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Basic information

Entry
Database: PDB / ID: 3rc4
TitleMolecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease
Components
  • NS3/4A Protease
  • Product TRIF
KeywordsHYDROLASE/HYDROLASE INHIBITOR / drug resistance / drug design / Protease inhibitors / serine protease / HYDROLASE / chymotrypsin-like / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


TICAM1 deficiency - HSE / TRAF3 deficiency - HSE / positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / ripoptosome / Toll-like receptor 2 binding / MyD88-independent TLR4 cascade / Toll Like Receptor 3 (TLR3) Cascade / TRIF-mediated programmed cell death ...TICAM1 deficiency - HSE / TRAF3 deficiency - HSE / positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / ripoptosome / Toll-like receptor 2 binding / MyD88-independent TLR4 cascade / Toll Like Receptor 3 (TLR3) Cascade / TRIF-mediated programmed cell death / TLR3-mediated TICAM1-dependent programmed cell death / positive regulation of myeloid dendritic cell cytokine production / cellular response to oxidised low-density lipoprotein particle stimulus / Caspase activation via Death Receptors in the presence of ligand / toll-like receptor 3 signaling pathway / TRIF-dependent toll-like receptor signaling pathway / RIP-mediated NFkB activation via ZBP1 / viral capsid assembly / macrophage activation involved in immune response / positive regulation of cytokine production involved in inflammatory response / positive regulation of natural killer cell activation / adhesion receptor-mediated virion attachment to host cell / TBC/RABGAPs / positive regulation of macrophage cytokine production / hepacivirin / toll-like receptor 4 signaling pathway / toll-like receptor signaling pathway / host cell mitochondrial membrane / response to exogenous dsRNA / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / B cell proliferation / transformation of host cell by virus / positive regulation of cytokinesis / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / regulation of protein-containing complex assembly / negative regulation of protein secretion / host cell membrane / positive regulation of type I interferon production / autophagosome / signaling adaptor activity / positive regulation of autophagy / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / positive regulation of B cell proliferation / positive regulation of chemokine production / lipopolysaccharide-mediated signaling pathway / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / TRAF6-mediated induction of TAK1 complex within TLR4 complex / nitric oxide biosynthetic process / positive regulation of interferon-beta production / endoplasmic reticulum-Golgi intermediate compartment membrane / serine-type peptidase activity / TICAM1, RIP1-mediated IKK complex recruitment / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / positive regulation of protein ubiquitination / virion component / apoptotic signaling pathway / SH3 domain binding / kinase binding / positive regulation of interleukin-6 production / : / positive regulation of nitric oxide biosynthetic process / nucleoside-triphosphate phosphatase / positive regulation of tumor necrosis factor production / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / defense response to virus / viral nucleocapsid / positive regulation of canonical NF-kappaB signal transduction / cellular response to lipopolysaccharide / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / entry receptor-mediated virion attachment to host cell / RNA helicase activity / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / molecular adaptor activity / early endosome / endosome membrane / RNA helicase / endosome / induction by virus of host autophagy / RNA-directed RNA polymerase / inflammatory response / symbiont entry into host cell / ribonucleoprotein complex / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / innate immune response / fusion of virus membrane with host endosome membrane / viral envelope / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / structural molecule activity
Similarity search - Function
TIR domain-containing adapter molecule 1 / TRIF, N-terminal / : / TRIF N-terminal domain / RHIM domain / RIP homotypic interaction motif / Thrombin, subunit H - #120 / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily ...TIR domain-containing adapter molecule 1 / TRIF, N-terminal / : / TRIF N-terminal domain / RHIM domain / RIP homotypic interaction motif / Thrombin, subunit H - #120 / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / 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 / DNA/RNA polymerase superfamily / Peptidase S1, PA clan / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Polyprotein / Genome polyprotein / TIR domain-containing adapter molecule 1
Similarity search - Component
Biological speciesHepatitis C virus subtype 1a
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsRomano, K.P. / Schiffer, C.A.
CitationJournal: J.Virol. / Year: 2011
Title: Molecular mechanisms of viral and host cell substrate recognition by hepatitis C virus NS3/4A protease.
Authors: Romano, K.P. / Laine, J.M. / Deveau, L.M. / Cao, H. / Massi, F. / Schiffer, C.A.
History
DepositionMar 30, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 4, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jun 28, 2017Group: Database references / Source and taxonomy / Structure summary
Category: entity / entity_name_com ...entity / entity_name_com / entity_src_gen / pdbx_entity_src_syn / struct / 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 / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_seq_type / _pdbx_entity_src_syn.pdbx_beg_seq_num / _pdbx_entity_src_syn.pdbx_end_seq_num / _struct.pdbx_descriptor
Revision 1.3Nov 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 1.4Jul 26, 2023Group: Database references / Derived calculations
Category: citation / database_2 ...citation / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Sep 13, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NS3/4A Protease
B: Product TRIF
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,9194
Polymers22,7582
Non-polymers1612
Water2,774154
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area830 Å2
ΔGint-19 kcal/mol
Surface area10010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.900, 58.146, 61.300
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein NS3/4A Protease


Mass: 21487.330 Da / Num. of mol.: 1 / Fragment: UNP residues 36-218
Mutation: A1027S, P1028G, I1029D, L1039E, L1040E, I1043Q, V1044E, L1047Q, C1073S, C1078L, I1098T, P1112Q, S1165A, C1185S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hepatitis C virus subtype 1a / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: D6MZ98, UniProt: P27958*PLUS
#2: Protein/peptide Product TRIF


Mass: 1270.451 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q8IUC6*PLUS
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


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.: 1 / Source method: obtained synthetically / Formula: Zn
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 154 / Source method: isolated from a natural source / Formula: H2O
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: 2.12 Å3/Da / Density % sol: 41.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 14-BM-C
DetectorDate: Oct 28, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 1.5→20 Å / Num. obs: 27770 / % possible obs: 87.4 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 13.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obs% possible all
1.5-1.554.70.33293.1
1.55-1.624.70.24792.1
1.62-1.694.80.18892.7
1.69-1.784.80.14591.9
1.78-1.894.90.11391.2
1.89-2.0450.08990.5
2.04-2.245.10.07189.4
2.24-2.565.10.05788.1
2.56-3.235.10.04385
3.23-205.10.03962.6

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACT3.1data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3M5M

3m5m


Resolution: 1.5→17.24 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.944 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 2.929 / SU ML: 0.051 / SU R Cruickshank DPI: 0.0855 / Cross valid method: THROUGHOUT / ESU R: 0.086 / ESU R Free: 0.086 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21549 1416 5.1 %RANDOM
Rwork0.18641 ---
obs0.18789 26246 87.11 %-
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: 23.043 Å2
Baniso -1Baniso -2Baniso -3
1-0.35 Å20 Å20 Å2
2---1.53 Å20 Å2
3---1.18 Å2
Refinement stepCycle: LAST / Resolution: 1.5→17.24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1477 0 6 154 1637
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0221510
X-RAY DIFFRACTIONr_bond_other_d0.0010.021005
X-RAY DIFFRACTIONr_angle_refined_deg1.281.9672057
X-RAY DIFFRACTIONr_angle_other_deg0.82632453
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4125205
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.7622.04149
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.78715231
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.6441513
X-RAY DIFFRACTIONr_chiral_restr0.0710.2245
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0211699
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02296
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_it0.5971.51017
X-RAY DIFFRACTIONr_mcbond_other0.161.5422
X-RAY DIFFRACTIONr_mcangle_it1.02121633
X-RAY DIFFRACTIONr_scbond_it1.5193493
X-RAY DIFFRACTIONr_scangle_it2.3434.5423
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.5→1.535 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.283 96 -
Rwork0.224 2004 -
obs--91.03 %
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)
1-1.78230.71021.66560.98445.062810.03730.21910.19870.3847-0.23490.1366-0.21720.2994-0.0441-0.35570.82060.09330.29560.31120.08930.3276.5914-19.02210.0618
23.2661-0.4576-1.02165.07041.92736.10390.1252-0.3630.22420.39220.0349-0.1878-0.26340.1646-0.16020.1475-0.02970.0080.08990.01050.0812.29442.222824.0661
34.7783-1.3893-3.70985.04441.5876.7520.048-0.2505-0.09430.0061-0.0103-0.1777-0.06280.3074-0.03760.0951-0.0140.00270.05090.01160.07924.35425.054119.1889
43.6902-2.47610.02848.62920.39029.34040.11170.0342-0.0421-0.4865-0.1232-0.593-0.2830.30210.01150.0842-0.0030.08950.0710.01870.132511.3756-5.2411.0437
527.29762.2577-6.2859.0159-0.66728.0380.2694-0.69460.71180.1737-0.1806-0.3935-0.29050.4806-0.08880.1227-0.047-0.02580.0729-0.00270.10656.2091-1.541226.4446
64.07380.58960.18537.20522.044214.35120.26310.2259-0.1387-0.487-0.04740.02780.1105-0.5606-0.21570.09290.0193-0.00820.09780.02570.1014-0.0347-5.153113.3611
72.35060.2558-0.33471.80940.44051.08010.0746-0.0101-0.03360.0044-0.0858-0.06320.0536-0.02140.01110.09490.0076-0.00320.08740.02460.0751-1.3421-11.275120.2017
87.61272.6533-1.30243.0491-0.69361.91660.2061-0.2184-0.19190.0587-0.2319-0.35480.07460.1980.02580.06990.0236-0.00020.06460.0170.12515.9188-16.449119.4225
96.62882.21712.05852.19321.25543.18560.02940.0384-0.16220.1504-0.0782-0.13740.05280.09820.04880.09450.0181-0.00590.07850.01550.0939-0.9753-15.639522.1808
1014.03231.4679-10.15982.0903-1.12367.599-0.227-0.6181-0.17080.1287-0.094-0.1479-0.04430.32850.3210.1813-0.0019-0.02990.2556-0.04130.1375-1.5202-8.059335.2373
1114.26514.6252-6.71563.0451-7.329915.88210.4853-1.16120.96960.0828-0.18020.0542-0.0590.3621-0.30510.0781-0.00780.08260.1498-0.18980.3407-14.3151-1.469133.2003
128.26427.9203-3.592117.3775-6.656317.36180.06820.39220.4473-0.74030.14421.3296-0.00920.3174-0.21240.10510.0177-0.01980.0759-0.00580.2404-6.96093.381621.2654
138.15761.8196-2.59920.8246-1.12652.76180.1627-0.360.5970.05340.15070.0792-0.1155-0.0233-0.31340.07480.00360.05430.1608-0.03230.1214-17.7132-5.571430.6129
145.2785-3.59880.556912.4215-9.15125.48410.1442-0.00980.5952-0.20930.36290.5604-0.0628-0.2844-0.50710.18010.03810.07850.18910.01530.2683-20.864-1.283126.0205
1530.8502-11.72220.80197.4563-5.9415.20080.12470.65731.64290.24770.3931-0.319-0.3014-0.5174-0.51790.13850.02710.01330.16680.11650.3248-13.76481.030716.8831
164.542-0.6767-2.3447-0.10592.133115.80110.0959-0.62740.7405-0.08170.0043-0.0264-0.34810.0912-0.10020.1497-0.03060.0390.2535-0.11590.2441-7.8018-3.771933.3199
179.6925-3.26630.436-0.113-0.40345.63940.01830.0750.0648-0.0336-0.15280.11110.22060.37270.13450.1469-0.01340.0160.15030.00180.147-10.1726-8.932126.1077
181.5419-4.17613.892410.2891-4.15328.39390.11780.5537-0.2926-0.46670.11351.2879-0.0275-0.0277-0.23140.14240.06380.0120.62760.21720.3422-21.9782-3.071517.5764
1920.0374-8.3766.52626.1854-7.333210.55610.16730.1133-0.30410.0652-0.02420.2027-0.04970.0347-0.14320.1103-0.01490.02030.11960.00990.0589-13.9468-10.671325.9813
2014.2477-3.6459-6.85954.6329-1.91773.5448-0.3471-0.8776-0.60170.25780.1360.4240.17250.14460.21110.1545-0.044-0.03220.19320.10260.114-5.9745-17.945531.7631
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A982 - 991
2X-RAY DIFFRACTION2A992 - 1004
3X-RAY DIFFRACTION3A1005 - 1012
4X-RAY DIFFRACTION4A1013 - 1027
5X-RAY DIFFRACTION5A1028 - 1033
6X-RAY DIFFRACTION6A1034 - 1041
7X-RAY DIFFRACTION7A1042 - 1063
8X-RAY DIFFRACTION8A1064 - 1078
9X-RAY DIFFRACTION9A1079 - 1088
10X-RAY DIFFRACTION10A1089 - 1101
11X-RAY DIFFRACTION11A1102 - 1106
12X-RAY DIFFRACTION12A1107 - 1112
13X-RAY DIFFRACTION13A1113 - 1122
14X-RAY DIFFRACTION14A1123 - 1129
15X-RAY DIFFRACTION15A1130 - 1139
16X-RAY DIFFRACTION16A1140 - 1149
17X-RAY DIFFRACTION17A1150 - 1155
18X-RAY DIFFRACTION18A1156 - 1166
19X-RAY DIFFRACTION19A1167 - 1171
20X-RAY DIFFRACTION20A1172 - 1179

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