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- PDB-3fbv: Crystal structure of the oligomer formed by the kinase-ribonuclea... -

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Basic information

Entry
Database: PDB / ID: 3fbv
TitleCrystal structure of the oligomer formed by the kinase-ribonuclease domain of Ire1
ComponentsSerine/threonine-protein kinase/endoribonuclease IRE1
KeywordsTRANSFERASE / HYDROLASE / IRE1 / RNase / ribonuclease / complex / kinase / inhibitor / oligomer / cytoplasmic / APY29 / aminopyrazole / ATP-binding / Endoplasmic reticulum / Glycoprotein / Magnesium / Membrane / Metal-binding / Multifunctional enzyme / Nucleotide-binding / Phosphoprotein / Serine/threonine-protein kinase / Transcription / Transcription regulation / Transmembrane / Unfolded protein response
Function / homology
Function and homology information


IRE1alpha activates chaperones / Ire1 complex / IRE1-TRAF2-ASK1 complex / fungal-type cell wall organization / inositol metabolic process / protein localization to Golgi apparatus / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / IRE1-mediated unfolded protein response / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / endoplasmic reticulum unfolded protein response ...IRE1alpha activates chaperones / Ire1 complex / IRE1-TRAF2-ASK1 complex / fungal-type cell wall organization / inositol metabolic process / protein localization to Golgi apparatus / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / IRE1-mediated unfolded protein response / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / endoplasmic reticulum unfolded protein response / RNA endonuclease activity / response to endoplasmic reticulum stress / mRNA processing / unfolded protein binding / non-specific serine/threonine protein kinase / protein kinase activity / protein serine kinase activity / protein serine/threonine kinase activity / endoplasmic reticulum membrane / endoplasmic reticulum / ATP binding / metal ion binding / identical protein binding / nucleus
Similarity search - Function
KEN domain / Serine/threonine-protein kinase/endoribonuclease IRE1/2-like / KEN domain / KEN domain superfamily / Ribonuclease 2-5A / KEN domain profile. / domain in protein kinases, N-glycanases and other nuclear proteins / de novo design (two linked rop proteins) / Pyrrolo-quinoline quinone beta-propeller repeat / beta-propeller repeat ...KEN domain / Serine/threonine-protein kinase/endoribonuclease IRE1/2-like / KEN domain / KEN domain superfamily / Ribonuclease 2-5A / KEN domain profile. / domain in protein kinases, N-glycanases and other nuclear proteins / de novo design (two linked rop proteins) / Pyrrolo-quinoline quinone beta-propeller repeat / beta-propeller repeat / Quinoprotein alcohol dehydrogenase-like superfamily / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Up-down Bundle / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-APJ / Serine/threonine-protein kinase/endoribonuclease IRE1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsKorennykh, A.V. / Egea, P.F. / Korostelev, A.A. / Finer-Moore, J. / Zhang, C. / Shokat, K.M. / Stroud, R.M. / Walter, P.
CitationJournal: Nature / Year: 2009
Title: The unfolded protein response signals through high-order assembly of Ire1.
Authors: Korennykh, A.V. / Egea, P.F. / Korostelev, A.A. / Finer-Moore, J. / Zhang, C. / Shokat, K.M. / Stroud, R.M. / Walter, P.
History
DepositionNov 19, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 16, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software / Item: _software.classification
Revision 1.3Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.4Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Serine/threonine-protein kinase/endoribonuclease IRE1
B: Serine/threonine-protein kinase/endoribonuclease IRE1
C: Serine/threonine-protein kinase/endoribonuclease IRE1
D: Serine/threonine-protein kinase/endoribonuclease IRE1
E: Serine/threonine-protein kinase/endoribonuclease IRE1
F: Serine/threonine-protein kinase/endoribonuclease IRE1
G: Serine/threonine-protein kinase/endoribonuclease IRE1
H: Serine/threonine-protein kinase/endoribonuclease IRE1
I: Serine/threonine-protein kinase/endoribonuclease IRE1
J: Serine/threonine-protein kinase/endoribonuclease IRE1
K: Serine/threonine-protein kinase/endoribonuclease IRE1
L: Serine/threonine-protein kinase/endoribonuclease IRE1
M: Serine/threonine-protein kinase/endoribonuclease IRE1
N: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)731,02128
Polymers726,36714
Non-polymers4,65314
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Serine/threonine-protein kinase/endoribonuclease IRE1
B: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3800 Å2
ΔGint-7 kcal/mol
Surface area36840 Å2
MethodPISA
3
C: Serine/threonine-protein kinase/endoribonuclease IRE1
D: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3690 Å2
ΔGint-7 kcal/mol
Surface area37220 Å2
MethodPISA
4
E: Serine/threonine-protein kinase/endoribonuclease IRE1
F: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3770 Å2
ΔGint-7 kcal/mol
Surface area36990 Å2
MethodPISA
5
G: Serine/threonine-protein kinase/endoribonuclease IRE1
H: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3830 Å2
ΔGint-7 kcal/mol
Surface area36880 Å2
MethodPISA
6
I: Serine/threonine-protein kinase/endoribonuclease IRE1
J: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3640 Å2
ΔGint-7 kcal/mol
Surface area36780 Å2
MethodPISA
7
K: Serine/threonine-protein kinase/endoribonuclease IRE1
L: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3630 Å2
ΔGint-6 kcal/mol
Surface area37390 Å2
MethodPISA
8
M: Serine/threonine-protein kinase/endoribonuclease IRE1
N: Serine/threonine-protein kinase/endoribonuclease IRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,4324
Polymers103,7672
Non-polymers6652
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3780 Å2
ΔGint-7 kcal/mol
Surface area37000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)156.820, 163.470, 292.830
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
111
121
131
141
12
22
32
42
52
62
72
82
92
102
112
122
132

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and not resi 1037:1045 and not resi 660:680
211chain B and not resi 1037:1045 and not resi 660:680
311chain C and not resi 1037:1045 and not resi 660:680
411chain D and not resi 1037:1045 and not resi 660:680
511chain E and not resi 1037:1045 and not resi 660:680
611chain F and not resi 1037:1045 and not resi 660:680
711chain G and not resi 1037:1045 and not resi 660:680
811chain H and not resi 1037:1045 and not resi 660:680
911chain I and not resi 1037:1045 and not resi 660:680
1011chain J and not resi 1037:1045 and not resi 660:680
1111chain K and not resi 1037:1045 and not resi 660:680
1211chain L and not resi 1037:1045 and not resi 660:680
1311chain M and not resi 1037:1045 and not resi 660:680
1411chain N and not resi 1037:1045 and not resi 660:680
112chain B and resi 1037:1045
212resid 1037:1045 and chain C
312resid 1037:1045 and chain E
412resid 1037:1045 and chain M
512resid 1037:1045 and chain I
612resid 1037:1045 and chain N
712resid 1037:1045 and chain D
812resid 1037:1045 and chain F
912resid 1037:1045 and chain H
1012resid 1037:1045 and chain J
1112resid 1037:1045 and chain L
1212resid 1037:1045 and chain K
1312resid 1037:1045 and chain G

NCS ensembles :
ID
1
2

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Components

#1: Protein
Serine/threonine-protein kinase/endoribonuclease IRE1


Mass: 51883.391 Da / Num. of mol.: 14 / Fragment: Ire1 Kinase-RNase domain: UNP residues 641-1115 / Mutation: Amino acids 865-892 deleted
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: S288c / Gene: IRE1, ERN1 / Plasmid: pGEX-6P-2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIPL
References: UniProt: P32361, non-specific serine/threonine protein kinase, Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters
#2: Chemical
ChemComp-APJ / N~2~-1H-benzimidazol-5-yl-N~4~-(3-cyclopropyl-1H-pyrazol-5-yl)pyrimidine-2,4-diamine


Mass: 332.363 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C17H16N8
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 3

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Sample preparation

CrystalDensity Matthews: 2.58 Å3/Da / Density % sol: 52.39 %
Crystal growTemperature: 298 K / Method: vapor diffusion / pH: 5.6
Details: Sodium citrate, pH 5.6, VAPOR DIFFUSION, temperature 298K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 30, 2008 / Details: Mirrors
RadiationMonochromator: KOHZU: Double Crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→20 Å / Num. obs: 123887 / % possible obs: 100 % / Redundancy: 23.2 % / Rmerge(I) obs: 0.053 / Net I/σ(I): 16
Reflection shellResolution: 3.2→3.31 Å / Redundancy: 23 % / Rmerge(I) obs: 0.342 / Mean I/σ(I) obs: 2.2 / % possible all: 100

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Processing

Software
NameClassification
ELVESrefinement
PHASERphasing
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2RIO

2rio


Resolution: 3.2→19.983 Å / SU ML: 0.6 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflection
Rfree0.2835 6727 5.43 %
Rwork0.2352 --
obs0.2374 123887 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 60.707 Å2 / ksol: 0.24 e/Å3
Refinement stepCycle: LAST / Resolution: 3.2→19.983 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms47668 0 350 0 48018
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3249X-RAY DIFFRACTIONPOSITIONAL
12B3249X-RAY DIFFRACTIONPOSITIONAL0.026
13C3249X-RAY DIFFRACTIONPOSITIONAL0.027
14D3249X-RAY DIFFRACTIONPOSITIONAL0.026
15E3249X-RAY DIFFRACTIONPOSITIONAL0.024
16F3249X-RAY DIFFRACTIONPOSITIONAL0.026
17G3249X-RAY DIFFRACTIONPOSITIONAL0.023
18H3249X-RAY DIFFRACTIONPOSITIONAL0.022
19I3249X-RAY DIFFRACTIONPOSITIONAL0.023
110J3249X-RAY DIFFRACTIONPOSITIONAL0.021
111K3249X-RAY DIFFRACTIONPOSITIONAL0.022
112L3249X-RAY DIFFRACTIONPOSITIONAL0.022
113M3249X-RAY DIFFRACTIONPOSITIONAL0.025
114N3249X-RAY DIFFRACTIONPOSITIONAL0.026
21B88X-RAY DIFFRACTIONPOSITIONAL
22C88X-RAY DIFFRACTIONPOSITIONAL0.033
23E88X-RAY DIFFRACTIONPOSITIONAL0.016
24M88X-RAY DIFFRACTIONPOSITIONAL0.035
25I88X-RAY DIFFRACTIONPOSITIONAL0.017
26N88X-RAY DIFFRACTIONPOSITIONAL0.027
27D88X-RAY DIFFRACTIONPOSITIONAL0.019
28F88X-RAY DIFFRACTIONPOSITIONAL0.018
29H88X-RAY DIFFRACTIONPOSITIONAL0.018
210J88X-RAY DIFFRACTIONPOSITIONAL0.04
211L88X-RAY DIFFRACTIONPOSITIONAL0.016
212K88X-RAY DIFFRACTIONPOSITIONAL0.013
213G88X-RAY DIFFRACTIONPOSITIONAL0.031
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
3.2-3.236200.40024045
3.2362-3.27410.392510630.40573065
3.2741-3.31390.40021390.3983873
3.3139-3.355600.38444124
3.3556-3.399600.37014105
3.3996-3.44590.35287890.36093273
3.4459-3.49490.38562790.35073843
3.4949-3.546800.34154089
3.5468-3.601900.31864075
3.6019-3.66060.31779060.32223222
3.6606-3.72330.3606970.30443992
3.7233-3.790600.29284078
3.7906-3.86300.28634103
3.863-3.94120.31038660.27213230
3.9412-4.026200.26794150
4.0262-4.119100.2564114
4.1191-4.22120.25896060.24053477
4.2212-4.33420.26611130.22824003
4.3342-4.460400.21744117
4.4604-4.60260.2262560.21253878
4.6026-4.7650.23423770.19623750
4.765-4.95300.18494140
4.953-5.17470.22664640.18713668
5.1747-5.44230.2434260.19974138
5.4423-5.775500.20414163
5.7755-6.2090.24453650.19613807
6.209-6.811300.18364197
6.8113-7.74620.22072560.17253941
7.7462-9.577100.1424248
9.5771-19.9830.17371250.16794252
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)
13.7793-0.658-0.3308-0.68910.6072.3037-0.3203-0.1198-1.2026-0.00750.3210.53420.63760.10580.05740.89890.19450.15970.30150.09751.150619.940930.5055121.1772
22.145-1.2527-0.37516.1796-0.28542.4165-0.1617-0.1369-0.0434-0.59610.0557-0.43510.14240.72870.11530.61360.34930.21110.87560.10670.733849.977747.3744114.0723
36.23391.2029-1.24032.8196-0.59653.76090.2727-0.3432-1.0150.157-0.0911-0.48580.47990.3918-0.16410.4590.0849-0.1560.20110.1990.724140.785127.7862161.7662
43.74982.0737-0.49035.4596-0.86272.3182-0.1686-0.2608-0.28490.39950.0517-0.4051-0.2648-0.00730.10360.99880.0175-0.01760.5677-0.1210.68753.013640.5813206.081
56.33860.33190.05950.55240.00281.90710.00220.12720.56020.30390.0947-0.0926-0.6301-0.1522-0.15091.22330.17950.14360.5824-0.14390.745830.319366.6357199.0838
64.851-1.68920.7534.27-0.55112.54150.18080.30880.4623-0.0414-0.0823-0.6454-0.47420.441-0.06480.5699-0.12360.10.42670.10930.661147.242762.1432157.0477
71.50961.2478-0.50363.16070.1783-1.4654-0.09810.01590.17910.0150.14680.16160.0162-0.04980.00721.5960.50340.06771.57-0.28040.946314.131358.6196239.7544
81.8662-0.9134-0.87862.5595-0.7645-1.8836-0.267-0.65440.1970.56380.2241-0.21330.1465-0.03390.02291.70370.019-0.12611.6782-0.41230.902548.552159.8916247.1684
91.3402-0.98210.92192.7352-1.6793-2.0160.3825-0.46460.0474-0.2876-0.36330.07550.09240.1777-0.01291.7681-0.02260.17892.451-0.42750.968210.844643.6479282.0171
102.1015-0.0833-0.01990.3744-0.8428-1.6721-0.1204-1.23110.3259-0.0198-0.13120.03670.09990.46490.00582.2119-0.21630.11242.25-0.79621.302931.370972.3381286.8238
114.5328-0.40310.41181.19450.2204-2.8026-0.01181.0054-0.1659-0.0768-0.09880.0443-0.0554-0.05760.11861.5543-0.40980.12261.9493-0.33030.75620.805233.000531.1
123.36032.4405-0.30553.74720.1130.0565-0.04070.2430.66430.2517-0.140.90220.04910.29880.15371.3441-0.430.09331.8779-0.16441.388813.058566.994537.0922
134.93261.8205-0.30452.1016-0.11761.3857-0.27260.2647-0.5414-0.27860.2531-0.1730.53290.1120.06121.28560.22340.27280.7923-0.13620.846938.639133.756172.6915
141.91250.02920.31845.07961.06322.0098-0.2180.1315-0.1017-0.00760.19150.12650.19430.01530.05151.19190.12780.21330.58070.00640.75757.314648.138979.9111
153.24540.25560.36952.34320.32392.6872-0.0805-0.05190.3158-0.13390.25060.3454-0.201-0.2603-0.12490.58140.0849-0.00190.38360.11190.93167.571764.9776124.1199
164.0935-1.7042-0.51911.82820.87153.1463-0.0692-0.32870.6477-0.41530.137-0.24-0.50460.1095-0.04970.6539-0.02130.03490.3808-0.00150.766828.449677.0842116.5238
171.9470.36481.0712.93381.03693.49470.1341-0.18980.31430.0335-0.01360.72950.1542-1.0355-0.07740.466-0.085-0.05550.62090.23451.07155.865738.8605164.2838
182.551-0.3449-1.63171.93670.52481.3777-0.2826-0.0983-0.40750.16280.05710.20350.0346-0.02930.20050.93410.03820.24980.7586-0.01471.067622.236720.4561206.8227
191.3760.1883-0.35762.63180.98952.6518-0.0097-0.3184-0.05730.08280.42940.45990.0443-0.5245-0.24281.04140.07960.23771.13060.14221.09046.348738.7371199.4405
202.0989-1.02240.36682.44290.5222.54710.0411-0.3841-0.19890.26420.02750.6249-0.1888-0.6793-0.0720.55660.16240.19450.39550.11470.88869.866963.5065159.1052
211.9083-0.1952-0.57912.2554-0.50750.41680.3765-0.3509-0.35910.3246-0.0703-0.1025-0.5393-0.2997-0.29271.24380.25080.06791.4258-0.11820.973720.427522.4672242.0038
221.97081.21060.46533.32890.5958-1.06330.1597-0.2831-0.2240.3460.2511-0.1368-0.2627-0.0862-0.30351.48890.32440.0371.8774-0.18271.120744.41823.4196249.6015
232.694-0.14311.74991.01470.1378-1.17060.5912-0.3768-0.04980.5659-0.2357-0.3334-0.4053-0.959-0.15391.6057-0.1199-0.12952.0487-0.05411.011942.582325.6276284.5428
241.7026-0.5766-0.39242.53671.2762-1.87050.0704-0.4212-0.2548-0.27040.1757-0.1325-0.7363-0.3608-0.23041.7779-0.34050.38252.6231-0.37951.24356.690446.1791290.1072
251.15921.60810.62383.03261.45211.2038-0.54240.6801-0.04120.16460.7593-0.48260.2523-0.5568-0.23211.271-0.2599-0.01261.8082-0.32880.983255.651946.706432.5066
262.5942-0.52950.28131.32211.0386-1.6743-0.4251.06670.09370.09760.2757-0.12630.2917-0.26010.12791.6087-0.30320.15391.99990.23121.257349.589670.722338.9556
272.09380.08820.13962.17040.63321.0596-0.1226-0.01170.5642-0.09990.1526-0.07710.21970.2785-0.02691.03570.04910.23460.8051-0.0640.888349.26468.936574.1421
282.35781.02680.55451.5825-0.4671.9067-0.15960.20140.2938-0.31120.2060.145-0.63220.22010.01971.09610.13790.18430.51720.09480.914927.228179.023781.531
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1resid 1:965 and chain A
2X-RAY DIFFRACTION2resid 1:965 and chain B
3X-RAY DIFFRACTION3resid 1:965 and chain C
4X-RAY DIFFRACTION4resid 1:965 and chain F
5X-RAY DIFFRACTION5resid 1:965 and chain E
6X-RAY DIFFRACTION6resid 1:965 and chain D
7X-RAY DIFFRACTION7resid 1:965 and chain G
8X-RAY DIFFRACTION8resid 1:965 and chain H
9X-RAY DIFFRACTION9resid 1:965 and chain I
10X-RAY DIFFRACTION10resid 1:965 and chain J
11X-RAY DIFFRACTION11resid 1:965 and chain K
12X-RAY DIFFRACTION12resid 1:965 and chain L
13X-RAY DIFFRACTION13resid 1:965 and chain M
14X-RAY DIFFRACTION14resid 1:965 and chain N
15X-RAY DIFFRACTION15resid 966:2000 and chain A
16X-RAY DIFFRACTION16resid 966:2000 and chain B
17X-RAY DIFFRACTION17resid 966:2000 and chain C
18X-RAY DIFFRACTION18resid 966:2000 and chain F
19X-RAY DIFFRACTION19resid 966:2000 and chain E
20X-RAY DIFFRACTION20resid 966:2000 and chain D
21X-RAY DIFFRACTION21resid 966:2000 and chain G
22X-RAY DIFFRACTION22resid 966:2000 and chain H
23X-RAY DIFFRACTION23resid 966:2000 and chain I
24X-RAY DIFFRACTION24resid 966:2000 and chain J
25X-RAY DIFFRACTION25resid 966:2000 and chain K
26X-RAY DIFFRACTION26resid 966:2000 and chain L
27X-RAY DIFFRACTION27resid 966:2000 and chain M
28X-RAY DIFFRACTION28resid 966:2000 and chain N

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