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- PDB-6d6i: Ube2V1 in complex with ubiquitin variant Ubv.V1.1 and Ube2N/Ubc13 -

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Basic information

Entry
Database: PDB / ID: 6d6i
TitleUbe2V1 in complex with ubiquitin variant Ubv.V1.1 and Ube2N/Ubc13
Components
  • Ubiquitin-conjugating enzyme E2 N
  • Ubiquitin-conjugating enzyme E2 variant 1
  • Ubv.V1.1
KeywordsTRANSFERASE / Ubiquitin / Ubiquitin conjugating enzyme / Ubiquitin variant / Ube2V1
Function / homology
Function and homology information


: / UBC13-MMS2 complex / ubiquitin conjugating enzyme complex / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / DNA double-strand break processing / postreplication repair / positive regulation of double-strand break repair / positive regulation of intracellular signal transduction / E2 ubiquitin-conjugating enzyme ...: / UBC13-MMS2 complex / ubiquitin conjugating enzyme complex / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / DNA double-strand break processing / postreplication repair / positive regulation of double-strand break repair / positive regulation of intracellular signal transduction / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K63-linked ubiquitination / antiviral innate immune response / regulation of DNA repair / ubiquitin ligase complex / negative regulation of TORC1 signaling / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / positive regulation of DNA repair / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / ubiquitin binding / activated TAK1 mediates p38 MAPK activation / Nonhomologous End-Joining (NHEJ) / double-strand break repair via homologous recombination / TAK1-dependent IKK and NF-kappa-B activation / NOD1/2 Signaling Pathway / G2/M DNA damage checkpoint / ISG15 antiviral mechanism / CLEC7A (Dectin-1) signaling / Formation of Incision Complex in GG-NER / FCERI mediated NF-kB activation / Aggrephagy / modification-dependent protein catabolic process / Interleukin-1 signaling / protein polyubiquitination / ubiquitin-protein transferase activity / protein tag activity / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / positive regulation of NF-kappaB transcription factor activity / T cell receptor signaling pathway / Processing of DNA double-strand break ends / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / cell differentiation / protein ubiquitination / ubiquitin protein ligase binding / regulation of DNA-templated transcription / SARS-CoV-2 activates/modulates innate and adaptive immune responses / positive regulation of DNA-templated transcription / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Ubiquitin domain signature. ...Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 N / Ubiquitin-conjugating enzyme E2 variant 1 / UBC protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.551 Å
AuthorsCeccarelli, D.F. / Garg, P. / Keszei, A. / Sidhu, S. / Sicheri, F.
Funding support Canada, 2items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)MOP-136956 Canada
Canadian Institutes of Health Research (CIHR)MOP-126129 Canada
CitationJournal: J.Mol.Biol. / Year: 2020
Title: Structural and Functional Analysis of Ubiquitin-based Inhibitors That Target the Backsides of E2 Enzymes.
Authors: Garg, P. / Ceccarelli, D.F. / Keszei, A.F.A. / Kurinov, I. / Sicheri, F. / Sidhu, S.S.
History
DepositionApr 21, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 17, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 6, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Mar 11, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation.year / _citation_author.name
Revision 1.4Oct 4, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 variant 1
B: Ubiquitin-conjugating enzyme E2 N
C: Ubv.V1.1
D: Ubiquitin-conjugating enzyme E2 variant 1
E: Ubiquitin-conjugating enzyme E2 N
F: Ubv.V1.1


Theoretical massNumber of molelcules
Total (without water)87,0836
Polymers87,0836
Non-polymers00
Water00
1
A: Ubiquitin-conjugating enzyme E2 variant 1
B: Ubiquitin-conjugating enzyme E2 N
C: Ubv.V1.1


Theoretical massNumber of molelcules
Total (without water)43,5423
Polymers43,5423
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Ubiquitin-conjugating enzyme E2 variant 1
E: Ubiquitin-conjugating enzyme E2 N
F: Ubv.V1.1


Theoretical massNumber of molelcules
Total (without water)43,5423
Polymers43,5423
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)91.444, 91.444, 92.446
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number145
Space group name H-MP32
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 12 through 133 or (resid 134...
21(chain D and (resid 12 through 25 or (resid 26...
12(chain B and (resid 3 through 25 or (resid 26...
22(chain E and (resid 3 or (resid 4 and (name...
13(chain C and (resid 1 or (resid 2 and (name...
23(chain F and (resid 1 through 19 or (resid 20...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111PROPROASNASN(chain A and (resid 12 through 133 or (resid 134...AA12 - 1338 - 129
121METMETLEULEU(chain A and (resid 12 through 133 or (resid 134...AA134 - 136130 - 132
131PROPROASNASN(chain A and (resid 12 through 133 or (resid 134...AA12 - 1478 - 143
141PROPROASNASN(chain A and (resid 12 through 133 or (resid 134...AA12 - 1478 - 143
151PROPROASNASN(chain A and (resid 12 through 133 or (resid 134...AA12 - 1478 - 143
161PROPROASNASN(chain A and (resid 12 through 133 or (resid 134...AA12 - 1478 - 143
211PROPROGLNGLN(chain D and (resid 12 through 25 or (resid 26...DD12 - 258 - 21
221LYSLYSLYSLYS(chain D and (resid 12 through 25 or (resid 26...DD2622
231PROPROASNASN(chain D and (resid 12 through 25 or (resid 26...DD12 - 1478 - 143
241PROPROASNASN(chain D and (resid 12 through 25 or (resid 26...DD12 - 1478 - 143
251PROPROASNASN(chain D and (resid 12 through 25 or (resid 26...DD12 - 1478 - 143
261PROPROASNASN(chain D and (resid 12 through 25 or (resid 26...DD12 - 1478 - 143
112GLYGLYALAALA(chain B and (resid 3 through 25 or (resid 26...BB3 - 256 - 28
122GLUGLUGLUGLU(chain B and (resid 3 through 25 or (resid 26...BB2629
132GLYGLYASNASN(chain B and (resid 3 through 25 or (resid 26...BB3 - 1506 - 153
142GLYGLYASNASN(chain B and (resid 3 through 25 or (resid 26...BB3 - 1506 - 153
152GLYGLYASNASN(chain B and (resid 3 through 25 or (resid 26...BB3 - 1506 - 153
162GLYGLYASNASN(chain B and (resid 3 through 25 or (resid 26...BB3 - 1506 - 153
212GLYGLYGLYGLY(chain E and (resid 3 or (resid 4 and (name...EE36
222LEULEULEULEU(chain E and (resid 3 or (resid 4 and (name...EE47
232GLYGLYASNASN(chain E and (resid 3 or (resid 4 and (name...EE3 - 1506 - 153
242GLYGLYASNASN(chain E and (resid 3 or (resid 4 and (name...EE3 - 1506 - 153
252GLYGLYASNASN(chain E and (resid 3 or (resid 4 and (name...EE3 - 1506 - 153
262GLYGLYASNASN(chain E and (resid 3 or (resid 4 and (name...EE3 - 1506 - 153
113METMETMETMET(chain C and (resid 1 or (resid 2 and (name...CC113
123GLNGLNGLNGLN(chain C and (resid 1 or (resid 2 and (name...CC214
133METMETLEULEU(chain C and (resid 1 or (resid 2 and (name...CC1 - 7313 - 85
143METMETLEULEU(chain C and (resid 1 or (resid 2 and (name...CC1 - 7313 - 85
153METMETLEULEU(chain C and (resid 1 or (resid 2 and (name...CC1 - 7313 - 85
163METMETLEULEU(chain C and (resid 1 or (resid 2 and (name...CC1 - 7313 - 85
213METMETPROPRO(chain F and (resid 1 through 19 or (resid 20...FF1 - 1913 - 31
223SERSERSERSER(chain F and (resid 1 through 19 or (resid 20...FF2032
233METMETLEULEU(chain F and (resid 1 through 19 or (resid 20...FF1 - 7313 - 85
243METMETLEULEU(chain F and (resid 1 through 19 or (resid 20...FF1 - 7313 - 85
253METMETLEULEU(chain F and (resid 1 through 19 or (resid 20...FF1 - 7313 - 85

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Ubiquitin-conjugating enzyme E2 variant 1 / UEV-1 / CROC-1 / TRAF6-regulated IKK activator 1 beta Uev1A


Mass: 16138.480 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2V1, CROC1, UBE2V, UEV1, P/OKcl.19 / Production host: Homo sapiens (human) / References: UniProt: Q13404
#2: Protein Ubiquitin-conjugating enzyme E2 N / Bendless-like ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme N / Ubc13 / UbcH13 / ...Bendless-like ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme N / Ubc13 / UbcH13 / Ubiquitin carrier protein N / Ubiquitin-protein ligase N


Mass: 17358.951 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2N, BLU / Plasmid: Pet28 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: P61088, E2 ubiquitin-conjugating enzyme
#3: Protein Ubv.V1.1


Mass: 10044.318 Da / Num. of mol.: 2 / Mutation: Q62H, K63W, H68L, V70W, L71W, R74L, G75I, G76A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: Uba52 / Plasmid: ProEx / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q96H31

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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: 2.77 Å3/Da / Density % sol: 55.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: 0.2M LiSO4, 25% PEG3350, 0.1 M Tris-HCl pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 5, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.55→50 Å / Num. obs: 28109 / % possible obs: 99.8 % / Redundancy: 5.1 % / Rmerge(I) obs: 0.065 / Rpim(I) all: 0.032 / Rrim(I) all: 0.072 / Χ2: 0.913 / Net I/σ(I): 7.6 / Num. measured all: 143038
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allΧ2% possible allRrim(I) all
2.55-2.594.90.9513980.5720.4770.42499.9
2.59-2.6450.79614090.6660.3920.43799.80.889
2.64-2.695.10.66414120.7480.3270.48199.80.741
2.69-2.7550.56313770.8480.280.44599.80.63
2.75-2.814.60.40514040.8840.2080.46799.60.456
2.81-2.874.90.37914170.8930.1890.46199.90.424
2.87-2.945.30.29314230.9490.1390.49799.90.325
2.94-3.025.30.22314070.9660.1060.52499.70.247
3.02-3.115.30.19313980.9720.0930.54199.80.214
3.11-3.215.20.14113650.9860.0680.5699.90.157
3.21-3.335.10.11214450.990.0550.6481000.125
3.33-3.464.60.09613870.9910.050.73699.80.108
3.46-3.625.10.07214350.9950.0350.7751000.08
3.62-3.815.40.06214130.9960.030.87399.90.069
3.81-4.055.20.05813940.9970.0281.09799.90.064
4.05-4.365.10.05214150.9970.0251.22899.90.057
4.36-4.84.90.0513970.9970.0241.58799.40.056
4.8-5.495.40.05313860.9970.0251.71999.90.059
5.49-6.9250.05814110.9960.0292.06499.80.065
6.92-505.30.04914160.9980.0232.51399.40.054

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIXrefinement
HKL-2000716.1data reduction
HKL-2000716.1data scaling
PHASER2.8.1phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5AIT

5ait


Resolution: 2.551→45.722 Å / SU ML: 0.74 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 39.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2963 1423 5.07 %
Rwork0.2635 26649 -
obs0.2651 28072 99.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 327.28 Å2 / Biso mean: 114.7371 Å2 / Biso min: 42.11 Å2
Refinement stepCycle: final / Resolution: 2.551→45.722 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5118 0 0 0 5118
Num. residues----697
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1300X-RAY DIFFRACTION5.429TORSIONAL
12D1300X-RAY DIFFRACTION5.429TORSIONAL
21B1139X-RAY DIFFRACTION5.429TORSIONAL
22E1139X-RAY DIFFRACTION5.429TORSIONAL
31C620X-RAY DIFFRACTION5.429TORSIONAL
32F620X-RAY DIFFRACTION5.429TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5506-2.64170.4781230.432326782801100
2.6417-2.74750.51531380.372326452783100
2.7475-2.87250.40211470.353926742821100
2.8725-3.02390.36021540.313726662820100
3.0239-3.21330.3531290.32726412770100
3.2133-3.46140.30641260.309627132839100
3.4614-3.80950.28281760.273426692845100
3.8095-4.36040.2881480.252326552803100
4.3604-5.49220.28981290.219226552784100
5.4922-45.72930.24861530.22572653280699
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)
13.5605-0.51130.35652.2850.31096.94350.56010.8905-0.4122-0.5494-0.42340.2785-0.0418-1.6619-0.13430.51790.1773-0.07180.72510.12850.9162-30.4221-38.872-17.0894
29.61451.66692.56097.75580.43899.43580.33120.2602-1.91390.8658-0.266-0.83271.626-1.3799-0.22440.7872-0.1553-0.08720.9730.23541.0695-29.7071-46.437-6.691
33.3616-1.55712.75213.31271.59626.88-0.16110.92710.1189-0.5326-0.0163-0.9778-0.18411.3631-0.34740.39640.04080.0340.88060.18860.8967-13.1274-34.8125-17.9866
44.9304-0.50941.19653.89671.09398.95690.2312-0.32220.38570.04210.0991-0.2527-0.48860.772-0.20050.35590.02660.03110.53030.02920.8743-18.2697-32.9633-7.1309
58.1969-2.54712.47863.8562-1.08087.9049-0.05650.16951.049-0.5711-0.42880.1912-2.63820.03620.09150.81480.0085-0.09280.55270.15881.0757-20.6193-23.2527-7.2167
64.73480.32031.15835.06191.95872.18150.31720.13190.2668-1.0579-0.26230.0955-1.7449-0.6292-0.04830.76290.17760.09490.64490.1730.9203-23.5178-27.4405-15.9574
76.3932-1.85780.29123.09981.06188.1881-0.52310.57070.49650.28810.4194-0.8602-0.88921.8181-0.35570.5003-0.18650.19561.1438-0.06141.3272-5.7783-31.9088-11.511
84.5999-0.3291.5253.02492.27462.42350.418-1.0841-0.59020.5981-0.34440.14960.8635-1.55010.51590.6116-0.08910.06272.68390.24450.9726-55.7075-37.0534-8.6549
94.1539-0.0392-1.81043.01591.95462.93420.54320.34860.23750.2668-0.5283-0.34731.2082-2.18770.0520.8533-0.798-0.10941.8320.09820.7404-45.4657-47.898-10.8789
103.5145-0.4596-1.39022.22281.32891.14270.47370.9226-0.05660.4993-1.17610.10880.3137-1.6262-0.11880.9577-0.678-0.0812.5377-0.14180.9955-52.781-48.4589-17.9952
114.83180.86211.5870.36310.9822.930.2828-0.2024-0.48140.5483-0.5830.15831.103-1.22020.27351.3984-0.311-0.6761.1751-0.80062.537-45.2357-62.6274-16.8808
121.3106-2.0744-2.9453.33034.66926.6175-0.22850.4406-0.77450.0402-0.007-0.13830.5042-1.31730.36541.8745-0.3678-0.1040.7950.05181.9643-37.833-68.0202-14.0852
134.87091.253-0.87821.812-1.17771.6430.2016-0.6605-0.56050.7073-0.4861-0.67890.9233-0.48430.03381.8595-1.1488-0.30721.87810.38161.1231-41.5861-61.8123-1.1197
143.8531-1.68651.80592.8986-1.7212.29950.46960.7485-0.1838-0.8737-0.17630.53950.6168-0.46640.00070.82960.6119-0.1171.4192-0.04450.6488-22.8292-45.0636-32.1094
157.09640.6689-0.94875.9714-0.03322.3547-0.36350.5033-1.30120.0039-0.0221-0.48110.7255-0.29040.28441.9762-0.1469-0.84880.7621-0.22792.1598-22.4232-59.4274-26.9648
168.5354-0.88580.30473.75693.8644.16350.27581.9224-0.6628-1.0587-0.4938-0.28610.48040.6553-0.19790.74340.4008-0.12610.9264-0.32191.3879-14.6138-53.1065-32.8326
170.0078-0.1364-0.01661.22860.0780.0020.42840.82950.2669-0.3604-0.1281-0.34150.02930.47320.13760.16251.9385-0.08161.9477-0.18370.7571-10.1018-47.5668-28.0357
185.35973.24271.48062.12371.15780.83760.83160.2811-1.547-0.1463-0.4963-0.22191.71360.7929-0.43561.0750.39710.02150.80460.1441.0246-17.3403-50.9047-18.9381
199.40441.4219-1.6034.34633.95844.53650.36060.5801-2.51950.7243-0.6612-0.47241.7369-0.5436-0.10091.09370.0395-0.10340.80890.02551.4597-26.008-53.7158-21.4211
204.426-2.64333.95912.8786-2.073.61050.54841.6895-0.1941-0.5851-0.5471-0.60530.16040.9001-0.46860.63070.42490.01761.00510.11420.8424-14.1664-42.359-26.5185
214.6432-1.0483-1.40542.9743-0.0364.7559-0.3366-1.303-0.8960.32610.1604-0.05251.56281.2240.24340.75390.2899-0.24220.7432-0.01631.0994-17.067-49.604715.496
221.2752-0.2544-1.51153.5610.34635.8516-0.2033-0.85140.15690.71620.5049-0.13490.93740.2082-0.20550.40370.0278-0.06110.7612-0.11550.8928-21.1145-39.117620.9909
238.16380.10441.26711.9742-1.37199.7578-0.3670.1449-0.2121-0.35020.64331.51281.6516-0.736-0.13331.00160.0507-0.31290.6289-0.02751.0437-25.2891-48.9086.9436
245.3324-0.8717-0.56494.5521-0.89068.74010.0277-0.75541.05790.7912-0.2470.2253-1.4472-0.5149-0.3790.75130.1961-0.16480.6548-0.10070.8588-23.5362-28.734118.213
254.8968-0.833-1.06264.6758-0.36968.79730.399-0.17910.0478-0.70870.15060.1037-0.46660.0322-0.21210.43970.119-0.02280.4099-0.00670.7967-19.3911-35.06728.0246
262.7098-1.6167-3.2084.7244-2.29548.6151-0.1003-0.33531.46680.2612-0.1918-0.7297-1.61050.7896-0.73740.68530.006-0.2140.4078-0.08261.0923-14.5976-26.83236.4568
273.7006-0.778-1.84514.7048-2.46573.15570.345-1.1038-0.46180.2167-0.2128-0.5731-0.21781.5662-0.08830.39270.0117-0.17210.877-0.18640.872-12.053-34.130316.2419
285.2261-2.4967-1.26074.8024-0.47118.62090.39450.60990.44151.04870.4385-0.13-1.66750.2584-0.45641.0860.17740.24260.5696-0.06291.1797-25.1001-21.003311.8634
291.21491.2675-1.13421.8002-1.85571.854-0.53940.3741-0.4123-0.94120.263-0.32552.26610.76960.46042.2250.90670.00071.2252-0.03441.015-4.331-66.96338.999
302.38850.598-0.79862.618-2.00482.1253-1.71350.34780.2794-1.35370.82170.44861.6803-0.4488-0.0362.3494-0.2151-0.11060.7181-0.11141.0984-19.9579-67.63875.2132
313.4695-1.8563-0.47263.1188-0.5913.497-0.0682-0.8521-0.1931-0.25220.61440.17021.9280.35520.68692.29630.368-0.23910.46260.11450.8894-18.5694-61.381813.6803
326.9615-2.3631-2.00682.8402-0.67982.6883-1.1286-0.9644-0.0637-0.01210.95210.44022.06920.35030.36932.65390.40510.19980.76690.08581.0741-15.728-69.719118.5726
331.7728-0.8742-0.97932.25322.5382.8777-0.1434-0.1819-1.1319-0.58750.39360.46782.6293-0.98030.01811.5855-0.7887-0.03831.54160.62611.4321-36.288-67.834915.9801
341.5706-1.3491.17543.6796-0.44263.2481-0.66350.81130.0656-0.95480.93221.68051.5983-1.0884-0.39392.7935-0.4758-0.34581.12690.13281.1713-32.6356-67.10121.3628
355.9059-1.91070.14621.7130.47920.8361-0.2146-1.1647-0.51910.45590.00810.43250.487-0.1237-0.28180.47970.52260.03241.71570.2240.7997-27.6069-42.230732.4022
361.5339-2.37181.28544.1376-1.33691.9934-1.217-0.9246-0.20690.28911.01622.05840.5552-1.75650.1580.8822-0.4314-0.28051.0060.04161.5689-40.5305-49.519827.0866
373.7415-1.5291-0.4471.80971.44351.5953-0.2598-0.71080.27840.47720.140.4353-0.0673-0.67270.12640.34390.78020.44881.31450.43571.6759-38.9572-39.37632.9964
382.26870.1642-1.06550.0121-0.06610.5029-0.278-0.86570.69080.91840.74970.3488-0.8065-0.8264-0.27550.9020.79030.14951.98740.20130.8902-35.817-32.671928.2708
390.58840.15640.25743.973-2.57041.9247-0.3836-0.6043-0.5984-0.13271.20911.82820.1056-1.93-0.32590.54310.0212-0.08081.35120.05831.2058-35.1102-40.606119.3433
405.07891.0438-2.86622.00051.60457.2676-1.0744-0.6408-0.54940.79081.07261.98421.1152-0.7626-0.24420.64650.148-0.14481.12770.11761.2045-31.333-42.362124.4249
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 12 through 37 )A12 - 37
2X-RAY DIFFRACTION2chain 'A' and (resid 38 through 46 )A38 - 46
3X-RAY DIFFRACTION3chain 'A' and (resid 47 through 63 )A47 - 63
4X-RAY DIFFRACTION4chain 'A' and (resid 64 through 99 )A64 - 99
5X-RAY DIFFRACTION5chain 'A' and (resid 100 through 109 )A100 - 109
6X-RAY DIFFRACTION6chain 'A' and (resid 110 through 129 )A110 - 129
7X-RAY DIFFRACTION7chain 'A' and (resid 130 through 147 )A130 - 147
8X-RAY DIFFRACTION8chain 'B' and (resid 3 through 38 )B3 - 38
9X-RAY DIFFRACTION9chain 'B' and (resid 39 through 86 )B39 - 86
10X-RAY DIFFRACTION10chain 'B' and (resid 87 through 113 )B87 - 113
11X-RAY DIFFRACTION11chain 'B' and (resid 114 through 124 )B114 - 124
12X-RAY DIFFRACTION12chain 'B' and (resid 125 through 132 )B125 - 132
13X-RAY DIFFRACTION13chain 'B' and (resid 133 through 150 )B133 - 150
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 16 )C1 - 16
15X-RAY DIFFRACTION15chain 'C' and (resid 17 through 22 )C17 - 22
16X-RAY DIFFRACTION16chain 'C' and (resid 23 through 34 )C23 - 34
17X-RAY DIFFRACTION17chain 'C' and (resid 35 through 44 )C35 - 44
18X-RAY DIFFRACTION18chain 'C' and (resid 45 through 55 )C45 - 55
19X-RAY DIFFRACTION19chain 'C' and (resid 56 through 65 )C56 - 65
20X-RAY DIFFRACTION20chain 'C' and (resid 66 through 73 )C66 - 73
21X-RAY DIFFRACTION21chain 'D' and (resid 12 through 26 )D12 - 26
22X-RAY DIFFRACTION22chain 'D' and (resid 27 through 37 )D27 - 37
23X-RAY DIFFRACTION23chain 'D' and (resid 38 through 46 )D38 - 46
24X-RAY DIFFRACTION24chain 'D' and (resid 47 through 63 )D47 - 63
25X-RAY DIFFRACTION25chain 'D' and (resid 64 through 89 )D64 - 89
26X-RAY DIFFRACTION26chain 'D' and (resid 90 through 109 )D90 - 109
27X-RAY DIFFRACTION27chain 'D' and (resid 110 through 129 )D110 - 129
28X-RAY DIFFRACTION28chain 'D' and (resid 130 through 147 )D130 - 147
29X-RAY DIFFRACTION29chain 'E' and (resid 3 through 39 )E3 - 39
30X-RAY DIFFRACTION30chain 'E' and (resid 44 through 57 )E44 - 57
31X-RAY DIFFRACTION31chain 'E' and (resid 58 through 86 )E58 - 86
32X-RAY DIFFRACTION32chain 'E' and (resid 87 through 113 )E87 - 113
33X-RAY DIFFRACTION33chain 'E' and (resid 114 through 132 )E114 - 132
34X-RAY DIFFRACTION34chain 'E' and (resid 133 through 150 )E133 - 150
35X-RAY DIFFRACTION35chain 'F' and (resid 1 through 16 )F1 - 16
36X-RAY DIFFRACTION36chain 'F' and (resid 17 through 22 )F17 - 22
37X-RAY DIFFRACTION37chain 'F' and (resid 23 through 34 )F23 - 34
38X-RAY DIFFRACTION38chain 'F' and (resid 35 through 44 )F35 - 44
39X-RAY DIFFRACTION39chain 'F' and (resid 45 through 55 )F45 - 55
40X-RAY DIFFRACTION40chain 'F' and (resid 56 through 73 )F56 - 73

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