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- PDB-7ojx: E2 UBE2K covalently linked to donor Ub, acceptor di-Ub, and RING ... -

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Basic information

Entry
Database: PDB / ID: 7ojx
TitleE2 UBE2K covalently linked to donor Ub, acceptor di-Ub, and RING E3 primed for K48-linked Ub chain synthesis
Components
  • (Polyubiquitin- ...) x 3
  • E3 ubiquitin-protein ligase RNF38
  • Ubiquitin-conjugating enzyme E2 K
KeywordsLIGASE / UBIQUITIN / RING E3 / E2
Function / homology
Function and homology information


free ubiquitin chain polymerization / regulation of proteasomal ubiquitin-dependent protein catabolic process / filopodium tip / positive regulation of type I interferon-mediated signaling pathway / positive regulation of tumor necrosis factor-mediated signaling pathway / hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of peptidyl-threonine phosphorylation / positive regulation of protein monoubiquitination / fat pad development ...free ubiquitin chain polymerization / regulation of proteasomal ubiquitin-dependent protein catabolic process / filopodium tip / positive regulation of type I interferon-mediated signaling pathway / positive regulation of tumor necrosis factor-mediated signaling pathway / hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of peptidyl-threonine phosphorylation / positive regulation of protein monoubiquitination / fat pad development / mitochondrion transport along microtubule / ubiquitin-ubiquitin ligase activity / E2 ubiquitin-conjugating enzyme / female gonad development / seminiferous tubule development / male meiosis I / ubiquitin conjugating enzyme activity / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / sperm flagellum / protein K48-linked ubiquitination / cellular response to interferon-beta / energy homeostasis / regulation of neuron apoptotic process / neuron projection morphogenesis / regulation of proteasomal protein catabolic process / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / Regulation of FZD by ubiquitination / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Regulation of innate immune responses to cytosolic DNA / Pexophagy / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / VLDLR internalisation and degradation / Regulation of PTEN localization / Regulation of BACH1 activity / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by REV1 / TICAM1, RIP1-mediated IKK complex recruitment / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Josephin domain DUBs / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / IKK complex recruitment mediated by RIP1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / positive regulation of protein ubiquitination / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / TCF dependent signaling in response to WNT / APC/C:Cdc20 mediated degradation of Securin / regulation of mitochondrial membrane potential / Regulation of NF-kappa B signaling / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / activated TAK1 mediates p38 MAPK activation / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / Negative regulators of DDX58/IFIH1 signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / Deactivation of the beta-catenin transactivating complex
Similarity search - Function
Vertebrate ubiquitin-conjugating enzyme E2 K, UBA domain / Ring finger domain / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 ...Vertebrate ubiquitin-conjugating enzyme E2 K, UBA domain / Ring finger domain / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione) / Polyubiquitin-B / Ubiquitin-conjugating enzyme E2 K / E3 ubiquitin-protein ligase RNF38
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsMajorek, K.A. / Nakasone, M.A. / Huang, D.T.
Funding supportEuropean Union, United Kingdom, 2items
OrganizationGrant numberCountry
European Research Council (ERC)647849European Union
Cancer Research UKA23278/A29256 United Kingdom
CitationJournal: Nat.Chem.Biol. / Year: 2022
Title: Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension.
Authors: Nakasone, M.A. / Majorek, K.A. / Gabrielsen, M. / Sibbet, G.J. / Smith, B.O. / Huang, D.T.
History
DepositionMay 17, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 12, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 26, 2022Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Feb 23, 2022Group: Author supporting evidence / Category: pdbx_audit_support
Item: _pdbx_audit_support.country / _pdbx_audit_support.grant_number
Revision 1.3Apr 13, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.5Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase RNF38
B: Ubiquitin-conjugating enzyme E2 K
C: Polyubiquitin-B
D: Polyubiquitin-B
E: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,9938
Polymers57,6425
Non-polymers3513
Water90150
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4920 Å2
ΔGint-25 kcal/mol
Surface area23260 Å2
Unit cell
Length a, b, c (Å)85.835, 85.835, 167.354
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein E3 ubiquitin-protein ligase RNF38 / RING finger protein 38 / RING-type E3 ubiquitin transferase RNF38


Mass: 9135.328 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RNF38 / Plasmid: pRSF-DUET1 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q9H0F5, RING-type E3 ubiquitin transferase
#2: Protein Ubiquitin-conjugating enzyme E2 K / E2 ubiquitin-conjugating enzyme K / Huntingtin-interacting protein 2 / HIP-2 / Ubiquitin carrier ...E2 ubiquitin-conjugating enzyme K / Huntingtin-interacting protein 2 / HIP-2 / Ubiquitin carrier protein / Ubiquitin-conjugating enzyme E2-25 kDa / Ubiquitin-conjugating enzyme E2(25K) / Ubiquitin-conjugating enzyme E2-25K / Ubiquitin-protein ligase


Mass: 22600.762 Da / Num. of mol.: 1 / Mutation: C92K, K97R, D124C, C170S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2K, HIP2, LIG / Plasmid: pRSF-DUET1 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P61086, E2 ubiquitin-conjugating enzyme

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Polyubiquitin- ... , 3 types, 3 molecules CDE

#3: Protein Polyubiquitin-B


Mass: 8778.012 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pRSF-DUET1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0CG47
#4: Protein Polyubiquitin-B


Mass: 8550.794 Da / Num. of mol.: 1 / Mutation: K48C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pRSF-DUET1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0CG47
#5: Protein Polyubiquitin-B


Mass: 8576.831 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pRSF-DUET1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0CG47

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Non-polymers , 3 types, 53 molecules

#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#7: Chemical ChemComp-ME7 / 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione)


Mass: 220.182 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H8N2O4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 50 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 3.1 Å3/Da / Density % sol: 60.35 %
Crystal growTemperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: Crystals were grown in: 0.2 M sodium citrate, 0.1 M Bis Tris propane 7.5 and 20 % (w/v) PEG 3350. The crystallization drops were set as a 1:1 mixture of the protein complex solution and the precipitant solution.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9119 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 9, 2020
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9119 Å / Relative weight: 1
ReflectionResolution: 2.4→74.34 Å / Num. obs: 28670 / % possible obs: 100 % / Redundancy: 8.6 % / Biso Wilson estimate: 62.67 Å2 / Rpim(I) all: 0.02 / Rrim(I) all: 0.06 / Net I/σ(I): 19.1 / Num. measured all: 246998
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique obsRpim(I) allRrim(I) all% possible all
2.4-2.448.80.714190.371.10299.9
6.51-74.377.974.415870.0120.034100

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.27data extraction
DIALSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1YLA, 1UBQ, 4V3L

1yla

1ubq

4v3l


Resolution: 2.4→74.34 Å / SU ML: 0.37 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 26 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.236 1412 4.93 %
Rwork0.1878 27214 -
obs0.1902 28626 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 237.02 Å2 / Biso mean: 94.6641 Å2 / Biso min: 42.81 Å2
Refinement stepCycle: final / Resolution: 2.4→74.34 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3663 0 18 50 3731
Biso mean--112.88 75.34 -
Num. residues----488
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 10 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.4-2.490.3491590.297326322791
2.49-2.590.36041250.317427132838
2.59-2.70.35271490.285426662815
2.7-2.850.26851270.257927032830
2.85-3.020.32791360.266226862822
3.02-3.260.29211180.254427092827
3.26-3.590.2841600.214127212881
3.59-4.10.23251510.174827202871
4.1-5.170.19351440.141827492893
5.17-74.340.18531430.154629153058
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)
10.5691-1.5826-0.78184.44432.25491.15820.0595-0.414-1.29951.328-2.1989-4.05290.41663.52581.98820.99520.0165-0.44811.35690.31551.3276-28.98442.88275.2108
23.98813.79915.24334.40865.22696.89430.1529-0.9906-1.41250.1093-0.5412-1.41071.3031-0.84540.37681.21040.1488-0.16970.60310.03220.8694-41.0668-11.53244.1523
3-0.0040.0278-0.04751.2417-2.40474.67541.7485-0.98422.2382-1.3057-0.5265-1.55081.6306-1.0605-0.83261.5603-0.1812-0.25310.57350.11681.4072-47.2277-5.92247.0561
44.59343.0787-3.90397.6339-0.10417.92270.0842-0.173-0.5847-0.36520.33230.89230.4839-0.2201-0.49450.82510.1019-0.0870.8090.10860.6751-46.5274-1.5579-3.8999
52.423-0.0382-0.5945.03025.08415.25320.56180.5387-0.6772-0.9522-0.2542-0.62211.1711-0.7213-0.64890.99230.0833-0.11770.5561-0.07370.8234-38.8953-6.78480.0751
65.8259-4.4223.43863.418-2.97442.421-0.36920.47850.5840.9822-0.2196-1.0624-0.1224-0.54030.70620.77290.0519-0.11330.5343-0.01750.7288-37.98593.73780.783
79.51283.6787-4.67638.08993.29548.9026-0.6063-0.47050.67150.52870.4424-0.7091-0.21140.0860.28010.95190.1042-0.15150.54550.04120.8144-38.733211.1774.2704
82.7121.93083.46123.5117-0.46428.49671.03910.7066-0.4671-1.0347-0.80760.44530.8908-0.1722-0.32371.2871-0.0637-0.1290.6409-0.06440.7627-48.78572.9196-13.6469
93.1688-4.09910.18848.734.22098.85560.01330.0762-0.4764-0.8130.50780.3280.28570.3805-0.22651.003-0.1248-0.19060.78270.0270.7417-57.305212.6503-17.6248
102.75561.62562.63433.93564.02774.6719-0.3991-1.0760.03450.56260.10722.12870.9846-1.8540.23230.68340.02080.06760.80430.09670.8867-65.486227.7197-6.8556
117.5093-3.18036.05187.7205-5.45476.2459-0.12010.51830.1976-0.3807-0.3836-0.58060.69810.33990.41590.72320.09830.00730.4995-0.07540.4488-47.765215.1142-15.1373
123.0727-1.0346-1.62182.7279-0.85181.49050.0547-0.0597-0.2139-0.19830.28060.55260.15230.535-0.35080.5338-0.0051-0.02450.68010.05130.4082-52.441329.1032-15.1611
136.1902-5.29580.77046.9097-1.44678.52450.1531-0.3984-0.25530.6807-0.0218-0.05390.74470.1679-0.19520.68750.0057-0.0990.45510.04220.4662-49.532118.4169-6.376
143.4973.8926-0.6125.24191.64417.0358-0.0355-0.89830.48841.08220.55990.16390.21260.7319-0.58170.570.1282-0.00150.72510.07830.4674-49.630133.1516-4.4819
155.20884.167-5.17963.4602-4.02085.22720.6177-1.2194-0.04421.4659-0.5194-0.1551-1.1615-0.3483-0.09150.6492-0.02040.01980.67770.04230.5406-53.772141.3496-6.0783
168.48512.48814.33974.75296.24878.5691-0.031-0.3873-0.30830.34530.03781.02050.0759-0.7349-0.00060.59650.0578-0.02980.71990.16960.5717-63.356336.6514-12.5878
174.8896-3.90630.94633.1472-1.07052.0893-0.22530.4530.25910.13280.72670.3838-0.2068-0.6998-0.53640.58210.0394-0.06710.80810.04330.7529-68.041642.2909-19.3025
187.5334-1.9863.09138.6588-4.75373.10540.1860.69480.6032-0.4468-0.3671-0.36530.10560.79880.23680.64620.0831-0.02750.63190.13330.6169-57.236147.0394-22.3489
198.48353.9503-1.11886.0148-2.4547.5484-0.70080.7312-0.3313-0.13981.2582-0.3632.0537-2.6203-0.33111.0034-0.10040.2940.82480.38451.5482-65.46226.67815.7983
202.96361.54351.54531.20440.19611.6842-1.57741.8642-5.198-3.18481.6722-3.37921.8130.63390.3611.044-0.13140.50151.2784-0.69232.5763-54.75114.63660.5438
215.2597-6.53530.07878.38460.7942.83130.1175-1.7399-0.67791.06840.80113.2299-1.9853-0.8024-0.73531.69650.31210.61381.0940.15941.2879-65.60769.688712.1871
227.4262-4.19054.74682.4391-2.69453.25960.2802-1.3907-1.38153.57170.84011.2645-1.03390.1579-1.18821.65060.2460.15940.76070.13070.8441-57.572711.355512.8569
234.6344-4.3195-2.54236.5428-0.2534.1861-1.28-0.5954-0.21361.73851.4019-0.7566-2.3517-0.2435-0.29811.80870.2789-0.2090.8266-0.20781.0516-50.553111.05359.0497
244.6855-4.9473-4.37445.12714.58174.3589-0.25-0.60570.6177-0.49121.31780.7107-2.14760.7368-0.98751.15210.09240.06850.77810.09311.176-60.745819.47544.632
259.2643.5124-2.81173.53571.373.6950.7183-0.4693-1.2021-0.16190.20163.0604-0.1778-0.8784-0.7721.01160.1780.04131.13220.46221.9091-69.886315.67467.1441
265.50865.2478-6.10685.111-5.64058.434-0.46791.06191.3613-0.01260.97351.5181-0.20850.2808-0.3640.7573-0.06480.04360.66860.07040.9997-53.70617.72270.4106
277.15025.0972-3.96829.6066-1.1727.6566-0.51190.13870.6846-0.79520.3933-0.4478-0.51570.20380.11780.59820.02380.01160.77120.22570.7598-34.401244.8589-22.2035
287.6778-2.78292.88047.27090.74128.6070.09490.854-0.3927-1.0259-0.2261-0.27110.08640.98870.090.62250.03640.03620.90030.22450.6615-30.236135.6255-22.5965
299.57815.29522.60498.0845.26143.80440.1991-0.9338-0.42630.1627-0.2679-0.24360.6509-0.18550.0150.70060.0057-0.02960.83280.1050.7288-38.184236.4744-12.9932
305.76735.6134-5.01215.4242-4.86784.35320.06270.5531.3588-0.29840.10181.6074-0.6825-0.4208-0.16630.59940.0335-0.0750.57360.08030.7977-43.054644.2609-16.1953
315.3131-1.097-5.02885.12865.45338.7452-0.4672-3.23630.6193-0.620.8892-1.2612-0.17941.707-0.42640.51470.0301-0.0160.96550.39710.8283-28.94942.1363-15.486
325.0545-4.4142-5.08955.15951.6112.00251.87631.4228-5.52923.37820.991-6.82741.16011.0749-1.87991.8598-0.0705-0.06751.1951-0.40222.4346-19.464329.7078-15.8416
334.5636-4.01315.13623.7527-5.06947.5146-0.67610.434-0.30381.46791.48080.7486-0.2567-2.1247-0.72581.4868-0.21270.0581.25180.17090.9499-28.104316.1478-18.7744
342.00119.121-2.93831.9989-5.0693.0416-0.0465-1.0012-2.0465-0.8031-0.5683-0.75091.3135-5.10910.70511.9831-0.4338-0.19482.54080.56451.0827-27.356915.994-31.703
351.89732.6336-1.66039.648-0.20495.49440.5102-0.01340.8981.14450.33721.5335-1.1235-0.9241-0.52291.3289-0.36230.03381.55940.4911.578-26.081511.7367-15.6276
365.1913.21470.72953.68552.13393.2081-0.4151.3167-2.0143-1.85881.69262.16652.9924-2.22960.13772.8625-1.52460.42360.75360.6811.9665-22.03326.149-20.8553
373.47093.76884.06794.46974.3774.64750.9264-0.4118-1.87650.6383-1.0803-1.49663.63930.3107-0.21381.7971-0.02440.13980.90750.19291.3019-16.506514.2486-24.3736
386.8257.02283.79129.23062.31793.46110.6617-1.11421.3072-0.1259-0.8493-3.57571.6892-1.63190.26721.34080.13280.09111.1470.31081.1445-18.612717.0214-13.7596
393.9878-3.51090.19216.41413.36164.0703-0.17280.28481.9568-1.10961.2672-1.12791.4711-0.4333-1.24071.2044-0.26610.25931.11320.19971.1418-18.960216.5613-26.4376
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 392 through 397 )A392 - 397
2X-RAY DIFFRACTION2chain 'A' and (resid 398 through 405 )A398 - 405
3X-RAY DIFFRACTION3chain 'A' and (resid 406 through 410 )A406 - 410
4X-RAY DIFFRACTION4chain 'A' and (resid 411 through 420 )A411 - 420
5X-RAY DIFFRACTION5chain 'A' and (resid 421 through 428 )A421 - 428
6X-RAY DIFFRACTION6chain 'A' and (resid 429 through 446 )A429 - 446
7X-RAY DIFFRACTION7chain 'A' and (resid 447 through 459 )A447 - 459
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 18 )B1 - 18
9X-RAY DIFFRACTION9chain 'B' and (resid 19 through 44 )B19 - 44
10X-RAY DIFFRACTION10chain 'B' and (resid 45 through 54 )B45 - 54
11X-RAY DIFFRACTION11chain 'B' and (resid 55 through 71 )B55 - 71
12X-RAY DIFFRACTION12chain 'B' and (resid 72 through 90 )B72 - 90
13X-RAY DIFFRACTION13chain 'B' and (resid 91 through 117 )B91 - 117
14X-RAY DIFFRACTION14chain 'B' and (resid 118 through 127 )B118 - 127
15X-RAY DIFFRACTION15chain 'B' and (resid 128 through 137 )B128 - 137
16X-RAY DIFFRACTION16chain 'B' and (resid 138 through 153 )B138 - 153
17X-RAY DIFFRACTION17chain 'B' and (resid 154 through 171 )B154 - 171
18X-RAY DIFFRACTION18chain 'B' and (resid 172 through 200 )B172 - 200
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 6 )C1 - 6
20X-RAY DIFFRACTION20chain 'C' and (resid 7 through 12 )C7 - 12
21X-RAY DIFFRACTION21chain 'C' and (resid 13 through 22 )C13 - 22
22X-RAY DIFFRACTION22chain 'C' and (resid 23 through 32 )C23 - 32
23X-RAY DIFFRACTION23chain 'C' and (resid 33 through 40 )C33 - 40
24X-RAY DIFFRACTION24chain 'C' and (resid 41 through 54 )C41 - 54
25X-RAY DIFFRACTION25chain 'C' and (resid 55 through 65 )C55 - 65
26X-RAY DIFFRACTION26chain 'C' and (resid 66 through 76 )C66 - 76
27X-RAY DIFFRACTION27chain 'D' and (resid 1 through 22 )D1 - 22
28X-RAY DIFFRACTION28chain 'D' and (resid 23 through 44 )D23 - 44
29X-RAY DIFFRACTION29chain 'D' and (resid 45 through 56 )D45 - 56
30X-RAY DIFFRACTION30chain 'D' and (resid 57 through 65 )D57 - 65
31X-RAY DIFFRACTION31chain 'D' and (resid 66 through 71 )D66 - 71
32X-RAY DIFFRACTION32chain 'D' and (resid 72 through 76 )D72 - 76
33X-RAY DIFFRACTION33chain 'E' and (resid 1 through 6 )E1 - 6
34X-RAY DIFFRACTION34chain 'E' and (resid 7 through 11 )E7 - 11
35X-RAY DIFFRACTION35chain 'E' and (resid 12 through 22 )E12 - 22
36X-RAY DIFFRACTION36chain 'E' and (resid 23 through 34 )E23 - 34
37X-RAY DIFFRACTION37chain 'E' and (resid 35 through 49 )E35 - 49
38X-RAY DIFFRACTION38chain 'E' and (resid 50 through 65 )E50 - 65
39X-RAY DIFFRACTION39chain 'E' and (resid 66 through 72 )E66 - 72

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