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- PDB-3o65: Crystal structure of a Josephin-ubiquitin complex: Evolutionary r... -

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Basic information

Entry
Database: PDB / ID: 3o65
TitleCrystal structure of a Josephin-ubiquitin complex: Evolutionary restraints on ataxin-3 deubiquitinating activity
Components
  • Putative ataxin-3-like protein
  • Ubiquitin
Keywordshydrolase/protein binding / Papain-like fold / Ubiquitin thiolesterase / hydrolase-protein binding complex
Function / homology
Function and homology information


hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / mitochondrion transport along microtubule / fat pad development / female gonad development / seminiferous tubule development / male meiosis I / protein deubiquitination / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator ...hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / mitochondrion transport along microtubule / fat pad development / female gonad development / seminiferous tubule development / male meiosis I / protein deubiquitination / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / regulation of proteasomal protein catabolic process / energy homeostasis / regulation of neuron apoptotic 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 / Membrane binding and targetting of GAG proteins / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of FZD by ubiquitination / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / 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 / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / Translesion synthesis by REV1 / NF-kB is activated and signals survival / Regulation of PTEN localization / Translesion synthesis by POLK / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / neuron projection morphogenesis / regulation of mitochondrial membrane potential / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / positive regulation of protein ubiquitination / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / Regulation of NF-kappa B signaling / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Recognition of DNA damage by PCNA-containing replication complex / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Peroxisomal protein import / Termination of translesion DNA synthesis / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity
Similarity search - Function
Cathepsin B; Chain A - #40 / Machado-Joseph disease protein / Josephin domain / Josephin / Josephin domain profile. / Josephin / Ubiquitin interaction motif / S15/NS1, RNA-binding / Ubiquitin-interacting motif. / Ubiquitin interacting motif ...Cathepsin B; Chain A - #40 / Machado-Joseph disease protein / Josephin domain / Josephin / Josephin domain profile. / Josephin / Ubiquitin interaction motif / S15/NS1, RNA-binding / Ubiquitin-interacting motif. / Ubiquitin interacting motif / Ubiquitin-interacting motif (UIM) domain profile. / Cathepsin B; Chain A / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Helix Hairpins / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-B / Polyubiquitin-C / Ataxin-3-like protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.7 Å
AuthorsWeeks, S.D. / Grasty, K.C. / Hernandez-Cuebas, L. / Loll, P.J.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Crystal Structure of a Josephin-Ubiquitin Complex: EVOLUTIONARY RESTRAINTS ON ATAXIN-3 DEUBIQUITINATING ACTIVITY.
Authors: Weeks, S.D. / Grasty, K.C. / Hernandez-Cuebas, L. / Loll, P.J.
History
DepositionJul 28, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Putative ataxin-3-like protein
B: Ubiquitin
C: Putative ataxin-3-like protein
D: Ubiquitin
E: Putative ataxin-3-like protein
F: Ubiquitin
G: Putative ataxin-3-like protein
H: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,3009
Polymers123,2778
Non-polymers231
Water2,738152
1
A: Putative ataxin-3-like protein
B: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,8423
Polymers30,8192
Non-polymers231
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2930 Å2
ΔGint-17 kcal/mol
Surface area12510 Å2
MethodPISA
2
C: Putative ataxin-3-like protein
D: Ubiquitin


Theoretical massNumber of molelcules
Total (without water)30,8192
Polymers30,8192
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2690 Å2
ΔGint-9 kcal/mol
Surface area13340 Å2
MethodPISA
3
E: Putative ataxin-3-like protein
F: Ubiquitin


Theoretical massNumber of molelcules
Total (without water)30,8192
Polymers30,8192
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2720 Å2
ΔGint-8 kcal/mol
Surface area13460 Å2
MethodPISA
4
G: Putative ataxin-3-like protein
H: Ubiquitin


Theoretical massNumber of molelcules
Total (without water)30,8192
Polymers30,8192
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2510 Å2
ΔGint-9 kcal/mol
Surface area13570 Å2
MethodPISA
5
A: Putative ataxin-3-like protein
B: Ubiquitin
C: Putative ataxin-3-like protein
D: Ubiquitin
E: Putative ataxin-3-like protein
F: Ubiquitin
G: Putative ataxin-3-like protein
H: Ubiquitin
hetero molecules

A: Putative ataxin-3-like protein
B: Ubiquitin
C: Putative ataxin-3-like protein
D: Ubiquitin
E: Putative ataxin-3-like protein
F: Ubiquitin
G: Putative ataxin-3-like protein
H: Ubiquitin
hetero molecules

A: Putative ataxin-3-like protein
B: Ubiquitin
C: Putative ataxin-3-like protein
D: Ubiquitin
E: Putative ataxin-3-like protein
F: Ubiquitin
G: Putative ataxin-3-like protein
H: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)369,89927
Polymers369,83024
Non-polymers693
Water27015
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area64220 Å2
ΔGint-319 kcal/mol
Surface area126990 Å2
MethodPISA
6
A: Putative ataxin-3-like protein
B: Ubiquitin
C: Putative ataxin-3-like protein
D: Ubiquitin
E: Putative ataxin-3-like protein
F: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,4817
Polymers92,4586
Non-polymers231
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11160 Å2
ΔGint-58 kcal/mol
Surface area36490 Å2
MethodPISA
7
A: Putative ataxin-3-like protein
C: Putative ataxin-3-like protein
E: Putative ataxin-3-like protein
G: Putative ataxin-3-like protein
hetero molecules

A: Putative ataxin-3-like protein
C: Putative ataxin-3-like protein
E: Putative ataxin-3-like protein
G: Putative ataxin-3-like protein
hetero molecules

A: Putative ataxin-3-like protein
C: Putative ataxin-3-like protein
E: Putative ataxin-3-like protein
G: Putative ataxin-3-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)267,33715
Polymers267,26812
Non-polymers693
Water1629
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area33800 Å2
ΔGint-239 kcal/mol
Surface area99650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)159.150, 159.150, 146.290
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number150
Space group name H-MP321

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Components

#1: Protein
Putative ataxin-3-like protein / Machado-Joseph disease protein 1-like


Mass: 22272.348 Da / Num. of mol.: 4 / Fragment: Josephin domain
Source method: isolated from a genetically manipulated source
Details: Protein expressed as a SUMO fusion. The isolated protein has an additional non-native glycine residue on the N-terminus that was necessary to facilitate cleavage of the SUMO fusion partner.
Source: (gene. exp.) Homo sapiens (human) / Gene: ATX3L, ATXN3L, MJDL / Plasmid: pETHSUL / Production host: Escherichia coli (E. coli) / Strain (production host): B834(DE3) / References: UniProt: Q9H3M9, EC: 3.1.2.15
#2: Protein
Ubiquitin /


Mass: 8546.848 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Protein expressed as a fusion with M. xenopii intein. Fusion cleaved with MESNA to generate Ubiqutitn 1-75 thioester. This was reacted with 2-chloroethylamine to yield a suicide substrate ...Details: Protein expressed as a fusion with M. xenopii intein. Fusion cleaved with MESNA to generate Ubiqutitn 1-75 thioester. This was reacted with 2-chloroethylamine to yield a suicide substrate suitable for complex formation.
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pETXSH / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta(DE3) / References: UniProt: P0CG47, UniProt: P0CG48*PLUS
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 152 / Source method: isolated from a natural source / Formula: H2O

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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: 4.33 Å3/Da / Density % sol: 71.59 %
Crystal growTemperature: 291 K / pH: 6.5
Details: The protein complex was at 8 mg/ml in 10 mM Tris pH 7,5mm DTT. 2 microlitres drops were set up under paraffin oil. To 1.1 microlitres of precipitant (1.6 M sodium citrate pH 6.5, pH adjusted ...Details: The protein complex was at 8 mg/ml in 10 mM Tris pH 7,5mm DTT. 2 microlitres drops were set up under paraffin oil. To 1.1 microlitres of precipitant (1.6 M sodium citrate pH 6.5, pH adjusted with HCl) 0.9 microlitres of protein was added, the final concentration of precipitant was therefore 0.88 M sodium citrate. For cryo crystals were passed through the 1.6 M sodium citrate pH 6.5 preciptant solution and then flash frozen in liquid nitrogen, microbatch under paraffin oil, temperature 291K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 0.978 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 10, 2008 / Details: Toroidal focusing mirror
RadiationMonochromator: Si(111) channel cut monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionHighest resolution: 2.7 Å / Num. obs: 112055 / % possible obs: 98.4 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 54.522 Å2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 15.42
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.7-2.770.5881.622307779892.9
2.77-2.850.5022.6398938260100
2.85-2.930.4533.552077792299.9
2.93-3.020.3375.871942771199.8
3.02-3.120.2847.273491757599.6
3.12-3.230.2239.269140713499.2
3.23-3.350.17911.666655692198.8
3.35-3.490.14813.963873665898.2
3.49-3.640.12216.959639627997.8
3.64-3.820.10719.457832613798.4
3.82-4.030.092353835576798.2
4.03-4.270.08224.351298550398.8
4.27-4.560.07326.547718514698.6
4.56-4.930.0682844600482599.1
4.93-5.40.06727.741918446099.6
5.4-6.040.06328.438501404099.8
6.04-6.970.06129.534109358199.9
6.97-8.540.05232.3284663006100
8.54-12.080.04337219212340100
12.080.0437.3907699277.4

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Phasing

PhasingMethod: SAD
Phasing dmFOM : 0.64 / FOM acentric: 0.64 / FOM centric: 0.66 / Reflection: 54832 / Reflection acentric: 51372 / Reflection centric: 3460
Phasing dm shell
Resolution (Å)FOM FOM acentricFOM centricReflectionReflection acentricReflection centric
7.7-19.9030.930.950.8725292085444
4.8-7.70.880.890.7978507066784
3.9-4.80.870.870.8395328903629
3.4-3.90.750.760.6891988699499
2.9-3.40.510.510.441601215304708
2.7-2.90.260.260.2397119315396

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
RESOLVE2.14phasing
PHENIX1.6.1_357refinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.7→19.903 Å / Occupancy max: 1 / Occupancy min: 0.56 / FOM work R set: 0.8532 / SU ML: 0.33 / σ(F): 0.04 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2242 2011 3.67 %
Rwork0.1763 --
obs0.1781 54826 93.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.243 Å2 / ksol: 0.293 e/Å3
Displacement parametersBiso max: 414.67 Å2 / Biso mean: 78.9387 Å2 / Biso min: 12.01 Å2
Baniso -1Baniso -2Baniso -3
1-1.9061 Å2-0 Å2-0 Å2
2--1.9061 Å2-0 Å2
3----3.8123 Å2
Refinement stepCycle: LAST / Resolution: 2.7→19.903 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8343 0 1 152 8496
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0098515
X-RAY DIFFRACTIONf_angle_d1.1411494
X-RAY DIFFRACTIONf_chiral_restr0.0741250
X-RAY DIFFRACTIONf_plane_restr0.0041509
X-RAY DIFFRACTIONf_dihedral_angle_d15.8883170
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.7002-2.79650.2881870.23614884507187
2.7965-2.90810.28351970.21785060525791
2.9081-3.040.24241960.20835129532591
3.04-3.19970.2561910.20955124531591
3.1997-3.39920.24571910.20175119531091
3.3992-3.66020.26011990.18885217541692
3.6602-4.02580.22152050.15785326553194
4.0258-4.6020.18032090.14295494570396
4.602-5.77450.19482170.14885607582498
5.7745-19.90350.20532190.15995855607499
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)
11.555-0.0037-0.26270.1463-0.21880.3650.39030.27620.4297-0.1489-0.2714-0.3176-0.1671-0.0979-0.15080.1620.06830.03740.04910.02210.432113.039382.7079-7.1956
21.98011.2459-3.15210.8564-2.57948.4835-0.05120.091-0.5763-0.09180.34090.01850.6416-0.5576-0.30420.0910.0009-0.07760.0850.06350.735-0.982864.57818.7309
30.012-0.0975-0.01740.7811-0.76382.43050.1123-0.04820.03090.2090.19920.42420.2191-0.6483-0.1822-0.09110.10720.0017-0.119-0.02580.4413.164671.70747.2943
41.9406-0.4841-1.27680.904-0.20941.21340.0789-0.31350.20010.16920.0599-0.4732-0.1350.2239-0.00120.0230.0359-0.04740.0419-0.04260.487521.671983.92236.0919
50.1041-0.4999-0.00435.9997-2.241.4546-0.344-0.11910.1446-0.23410.0048-1.77340.29530.10880.23150.08210.03680.09420.1047-0.10360.599727.656977.4564-9.9296
63.07340.2964-2.78790.6155-0.27992.53830.0056-0.695-0.6332-0.088-0.1333-0.42920.39470.96240.27650.09340.1349-0.01390.29820.16540.696414.685362.875621.0116
78.8176-0.2641-0.80321.0677-0.21980.1287-0.2196-1.37560.58020.23650.2374-0.1199-0.04920.15620.04310.04510.085-0.03070.2411-0.03690.192113.269771.160528.1042
82.8512-3.00121.19614.3989-0.74440.7974-0.4897-0.89-0.54090.50090.81180.7716-0.163-0.1244-0.28190.12070.07770.03080.17870.13980.43625.056270.153821.2223
90.0938-0.6110.12125.1707-1.93481.9768-0.3633-0.6403-0.62440.33650.7761.4121-0.1178-0.4378-0.390.11740.04740.15510.46520.20460.49482.269466.463530.4808
101.98180.0723-0.80660.6546-0.10860.61290.0888-0.4638-0.3076-0.10380.27060.81550.04490.0761-0.22480.08030.0833-0.04860.13110.05440.49777.88866.937819.2017
110.4788-1.53661.23545.2451-4.12393.64520.05290.12210.0542-1.2154-0.1093-0.17570.86280.01970.05640.3444-0.04420.25460.046-0.03190.611722.3566105.1325-17.4812
120.02690.0670.23150.16390.41411.16120.02610.08410.2519-0.1192-0.01670.0993-0.1415-0.0225-0.23940.0932-0.01960.15280.04580.04010.595214.671127.7457-15.3318
130.40140.5086-0.62644.4256-0.74252.11820.3027-0.12950.3322-0.1968-0.3222-1.7134-0.00460.49880.00090.16210.02940.33840.0610.04980.927835.0421112.9655-15.5507
140.1170.06930.36170.18680.27921.3894-0.5330.5482-0.2018-0.1372-0.03650.0753-0.00950.940.49050.4793-0.12790.48390.86820.14511.802243.615115.4187-21.0017
153.2039-0.99030.64830.85740.61661.41590.2907-0.63260.18370.4386-0.0987-0.03020.31240.3653-0.1520.16-0.03310.080.1595-0.00910.717531.9812105.6802-6.4661
161.01882.2858-1.93246.7766-3.99324.0889-0.1344-0.32330.0976-0.2751-0.2789-1.1983-0.00430.65760.3490.1055-0.03910.00760.15010.0410.948630.8367140.3428-7.8202
172.41640.6485-1.68020.9356-0.02292.33190.1837-0.12840.1404-0.28010.0002-1.0758-0.06230.3695-0.05910.1438-0.03650.31180.13260.07971.081634.3388139.5995-16.9948
181.8981.59390.64992.49421.53541.0734-0.36250.1935-0.7703-0.59830.2024-0.3079-0.34770.06430.02710.2049-0.04410.25820.04070.09220.852327.2907137.3883-16.8109
190.5211-0.60730.73071.0965-1.29362.3108-0.11590.00330.3693-0.2062-0.3039-1.1841-0.39780.06230.35410.3551-0.10550.17390.06920.08040.87326.5793148.9405-11.1526
200.39790.1253-0.08741.6888-1.85212.04750.1935-0.0208-0.3614-0.52950.236-0.85250.2409-0.1738-0.39390.0978-0.01240.14830.02570.06070.619823.5422130.425-17.303
211.23460.24770.56090.23460.21260.33120.0843-0.3973-0.0173-0.0579-0.2117-0.20640.0113-0.44210.20110.35180.12450.22540.50290.00970.237619.693982.9611-33.5285
220.6302-0.33690.2660.7219-0.19640.13180.13220.6269-0.2006-1.2357-0.2433-0.0402-0.54540.34240.01451.10130.12390.34381.1315-0.11490.23224.748375.5774-61.0736
232.8001-0.3746-1.67942.00181.52993.75160.09210.5935-0.4682-0.55890.2032-1.00830.03430.2919-0.17790.39260.07040.33550.4214-0.07540.553130.565976.6593-35.8933
240.7206-0.5771-0.33140.55290.33520.33460.04880.0673-0.3055-0.25640.0367-0.24220.01740.19480.06340.32430.14310.31180.2122-0.01470.628732.400678.3661-30.3963
252.2018-3.2705-1.6525.49851.86171.78760.0854-0.05310.3503-0.1884-0.3006-0.23870.25690.27850.17760.16840.11430.28970.2034-0.00570.880740.340792.3197-14.6939
262.06750.5914-0.90110.458-0.77551.31470.32540.23930.2816-0.0653-0.7105-0.17320.52280.74320.41590.73940.36790.3371.60720.00390.706843.693974.4681-55.654
270.5407-0.38580.54951.1533-1.18091.27920.66021.3997-0.1835-0.2595-1.1352-0.080.10690.54110.20321.3030.54030.45511.4913-0.27670.870644.824663.4817-52.7889
284.1587-3.9343-3.52883.72813.33463.09040.71260.9626-0.0301-0.8961-0.5621-0.084-0.783-0.9672-0.10141.19190.40120.64961.4339-0.45511.067633.967265.2889-51.9529
290.21820.3134-0.38651.3324-1.54111.84840.0970.5607-0.2315-0.9937-1.0281-0.0330.95810.47080.76691.32330.38980.46341.7042-0.27060.992340.830964.5956-64.1752
301.96980.04961.1230.91570.47350.8730.48151.793-0.2026-0.9822-0.3172-0.0828-0.98230.065-0.29050.9106-0.13830.40551.4393-0.46050.621229.623770.3552-51.3881
310.7549-0.0334-0.19760.64060.15710.08770.09010.55780.0217-0.5062-0.135-0.04190.0284-0.31810.01670.85710.13360.2750.74890.14990.219918.482298.4105-45.8908
320.6793-0.0403-0.78590.02410.0870.96290.36940.13390.2549-0.1983-0.0689-0.6475-0.5797-0.0693-0.3990.95930.11620.70940.75690.24341.545340.2624110.1289-32.5203
330.67070.2315-0.61151.5183-0.22920.739-0.10840.71090.3252-0.1840.1666-0.47360.2618-0.6353-0.03441.13030.11360.51741.06430.29250.446727.5113105.0193-53.3431
341.12390.0694-0.23921.74270.340.11890.09061.09630.1424-1.35180.0577-0.2526-0.2875-0.5864-0.12521.35720.04540.13841.35980.34780.29614.1479105.2716-57.7379
350.58310.134-0.17730.2525-0.02860.0541-0.17240.70320.0052-0.52880.1603-0.0649-0.0432-0.2136-0.02061.7263-0.02330.39411.22250.29770.69315.706104.3274-61.9405
360.530.41220.41870.43250.37060.34260.06240.62910.1721-0.55510.3628-0.2869-0.59460.5268-0.27131.4378-0.32930.50991.70880.47091.294944.1963115.9426-51.8694
371.6107-0.47640.84760.1951-0.24080.4619-0.40220.2856-0.13810.0344-0.1871-0.06150.08290.90620.53811.0927-0.11410.51.28250.29550.837536.2957110.8657-47.0793
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:29)A1 - 29
2X-RAY DIFFRACTION2(chain A and resid 30:57)A30 - 57
3X-RAY DIFFRACTION3(chain A and resid 58:91)A58 - 91
4X-RAY DIFFRACTION4(chain A and resid 92:167)A92 - 167
5X-RAY DIFFRACTION5(chain A and resid 168:181)A168 - 181
6X-RAY DIFFRACTION6(chain B and resid 1:16)B1 - 16
7X-RAY DIFFRACTION7(chain B and resid 17:36)B17 - 36
8X-RAY DIFFRACTION8(chain B and resid 37:48)B37 - 48
9X-RAY DIFFRACTION9(chain B and resid 49:61)B49 - 61
10X-RAY DIFFRACTION10(chain B and resid 62:76)B62 - 76
11X-RAY DIFFRACTION11(chain C and resid 1:28)C1 - 28
12X-RAY DIFFRACTION12(chain C and resid 29:90)C29 - 90
13X-RAY DIFFRACTION13(chain C and resid 91:143)C91 - 143
14X-RAY DIFFRACTION14(chain C and resid 144:161)C144 - 161
15X-RAY DIFFRACTION15(chain C and resid 162:182)C162 - 182
16X-RAY DIFFRACTION16(chain D and resid 1:22)D1 - 22
17X-RAY DIFFRACTION17(chain D and resid 23:31)D23 - 31
18X-RAY DIFFRACTION18(chain D and resid 32:52)D32 - 52
19X-RAY DIFFRACTION19(chain D and resid 53:66)D53 - 66
20X-RAY DIFFRACTION20(chain D and resid 67:76)D67 - 76
21X-RAY DIFFRACTION21(Chain E and resid 1:28)E1 - 28
22X-RAY DIFFRACTION22(Chain E and resid 29:66)E29 - 66
23X-RAY DIFFRACTION23(Chain E and resid 67:149)E67 - 149
24X-RAY DIFFRACTION24(Chain E and resid 150:181)E150 - 181
25X-RAY DIFFRACTION25(Chain E and resid 182:187)E182 - 187
26X-RAY DIFFRACTION26(Chain F and resid 1:14)F1 - 14
27X-RAY DIFFRACTION27(Chain F and resid 15:37)F15 - 37
28X-RAY DIFFRACTION28(Chain F and resid 38:43)F38 - 43
29X-RAY DIFFRACTION29(Chain F and resid 44:67)F44 - 67
30X-RAY DIFFRACTION30(Chain F and resid 68:76)F68 - 76
31X-RAY DIFFRACTION31(Chain G and resid 2:45)G2 - 45
32X-RAY DIFFRACTION32(Chain G and resid 46:66)G46 - 66
33X-RAY DIFFRACTION33(Chain G and resid 67:107)G67 - 107
34X-RAY DIFFRACTION34(Chain G and resid 108:142)G108 - 142
35X-RAY DIFFRACTION35(Chain G and resid 143:181)G143 - 181
36X-RAY DIFFRACTION36(Chain H and resid 1:64)H1 - 64
37X-RAY DIFFRACTION37(Chain H and resid 65:76)H65 - 76

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