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- PDB-6i4z: Crystal structure of the disease-causing P453L mutant of the huma... -

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Basic information

Entry
Database: PDB / ID: 6i4z
TitleCrystal structure of the disease-causing P453L mutant of the human dihydrolipoamide dehydrogenase
ComponentsDihydrolipoyl dehydrogenase, mitochondrial
KeywordsOXIDOREDUCTASE / Lipoamide dehydrogenase / Pathogenic mutation / E3 deficiency / Alpha-ketoglutarate dehydrogenase complex / 2-oxoglutarate dehydrogenase complex / Pyruvate dehydrogenase complex
Function / homology
Function and homology information


acetyltransferase complex / acrosomal matrix / OGDH complex synthesizes succinyl-CoA from 2-OG / OADH complex synthesizes glutaryl-CoA from 2-OA / oxoadipate dehydrogenase complex / Glycine degradation / branched-chain alpha-ketoacid dehydrogenase complex / BCKDH synthesizes BCAA-CoA from KIC, KMVA, KIV / Loss-of-function mutations in DBT cause MSUD2 / Loss-of-function mutations in DLD cause MSUD3/DLDD ...acetyltransferase complex / acrosomal matrix / OGDH complex synthesizes succinyl-CoA from 2-OG / OADH complex synthesizes glutaryl-CoA from 2-OA / oxoadipate dehydrogenase complex / Glycine degradation / branched-chain alpha-ketoacid dehydrogenase complex / BCKDH synthesizes BCAA-CoA from KIC, KMVA, KIV / Loss-of-function mutations in DBT cause MSUD2 / Loss-of-function mutations in DLD cause MSUD3/DLDD / H139Hfs13* PPM1K causes a mild variant of MSUD / PDH complex synthesizes acetyl-CoA from PYR / Branched-chain ketoacid dehydrogenase kinase deficiency / dihydrolipoyl dehydrogenase / dihydrolipoyl dehydrogenase (NADH) activity / Regulation of pyruvate dehydrogenase (PDH) complex / oxoglutarate dehydrogenase complex / pyruvate decarboxylation to acetyl-CoA / pyruvate dehydrogenase complex / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / 2-oxoglutarate metabolic process / pyruvate metabolic process / Signaling by Retinoic Acid / motile cilium / sperm capacitation / mitochondrial electron transport, NADH to ubiquinone / gastrulation / Mitochondrial protein degradation / regulation of membrane potential / flavin adenine dinucleotide binding / mitochondrial matrix / mitochondrion / proteolysis / nucleus
Similarity search - Function
Dihydrolipoamide dehydrogenase / : / Pyridine nucleotide-disulphide oxidoreductase, class I / FAD/NAD-linked reductase, C-terminal dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, class I, active site / Pyridine nucleotide-disulphide oxidoreductases class-I active site. / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / FAD/NAD-linked reductase, dimerisation domain superfamily / FAD/NAD(P)-binding domain ...Dihydrolipoamide dehydrogenase / : / Pyridine nucleotide-disulphide oxidoreductase, class I / FAD/NAD-linked reductase, C-terminal dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, class I, active site / Pyridine nucleotide-disulphide oxidoreductases class-I active site. / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain / FAD/NAD-linked reductase, dimerisation domain superfamily / FAD/NAD(P)-binding domain / Pyridine nucleotide-disulphide oxidoreductase / Enolase-like; domain 1 / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / Dihydrolipoyl dehydrogenase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.342 Å
AuthorsSzabo, E. / Wilk, P. / Torocsik, B. / Weiss, M.S. / Adam-Vizi, V. / Ambrus, A.
Funding support Hungary, United States, Germany, 10items
OrganizationGrant numberCountry
Hungarian Academy of Sciences02001 [to A.-V.V.] Hungary
Hungarian Scientific Research Fund, grant#112230 [to A.-V.V.] Hungary
Hungarian Brain Research Program, grant#KTIA_13_NAP_III/6 and 2017-1.2.1-NKP-2017-00002 [to A.-V.V.] Hungary
Hungarian Academy of SciencesBolyai Fellowship [to A.A.] Hungary
European Molecular Biology OrganizationShort-term Fellowship [to A.A.] Hungary
Semmelweis University, Young Investigator Research Grant [to A.A.] Hungary
Gedeon Richter PIc., Young Investigator Research Grant [to A.A.] Hungary
Fulbright Commission, Fulbright Fellowship [to A.A.] United States
European Union and Government of Hungary, grant#EFOP-3.6.3-VEKOP-16-2017-00009 [to S.E.] Hungary
European Union CALIPSOplus, grant#16204087-ST [to S.E. and A.A.] Germany
CitationJournal: Hum.Mol.Genet. / Year: 2019
Title: Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants.
Authors: Szabo, E. / Wilk, P. / Nagy, B. / Zambo, Z. / Bui, D. / Weichsel, A. / Arjunan, P. / Torocsik, B. / Hubert, A. / Furey, W. / Montfort, W.R. / Jordan, F. / Weiss, M.S. / Adam-Vizi, V. / Ambrus, A.
History
DepositionNov 12, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 20, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 11, 2019Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 24, 2024Group: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Dihydrolipoyl dehydrogenase, mitochondrial
B: Dihydrolipoyl dehydrogenase, mitochondrial
C: Dihydrolipoyl dehydrogenase, mitochondrial
D: Dihydrolipoyl dehydrogenase, mitochondrial
E: Dihydrolipoyl dehydrogenase, mitochondrial
F: Dihydrolipoyl dehydrogenase, mitochondrial
G: Dihydrolipoyl dehydrogenase, mitochondrial
H: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)430,10443
Polymers421,2268
Non-polymers8,87835
Water8,143452
1
A: Dihydrolipoyl dehydrogenase, mitochondrial
B: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,55011
Polymers105,3062
Non-polymers2,2449
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11880 Å2
ΔGint-138 kcal/mol
Surface area35950 Å2
MethodPISA
2
C: Dihydrolipoyl dehydrogenase, mitochondrial
D: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,83814
Polymers105,3062
Non-polymers2,53212
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12380 Å2
ΔGint-167 kcal/mol
Surface area35720 Å2
MethodPISA
3
E: Dihydrolipoyl dehydrogenase, mitochondrial
F: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,3589
Polymers105,3062
Non-polymers2,0517
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11520 Å2
ΔGint-124 kcal/mol
Surface area35780 Å2
MethodPISA
4
G: Dihydrolipoyl dehydrogenase, mitochondrial
H: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,3589
Polymers105,3062
Non-polymers2,0517
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11410 Å2
ΔGint-122 kcal/mol
Surface area35680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.560, 123.390, 158.410
Angle α, β, γ (deg.)105.950, 91.310, 90.000
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 through 331 or resid 333 through 474 or resid 500))
21(chain B and (resid 3 through 331 or resid 333 through 474 or resid 500))
31(chain C and (resid 3 through 331 or resid 333 through 474 or resid 500))
41(chain D and (resid 3 through 331 or resid 333 through 474 or resid 500))
51(chain E and (resid 3 through 331 or resid 333 through 474 or resid 500))
61(chain F and (resid 3 through 331 or resid 333 through 474 or resid 500))
71(chain G and (resid 3 through 331 or resid 333 through 474 or resid 500))
81(chain H and (resid 3 through 331 or resid 333 through 474 or resid 500))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 3 through 331 or resid 333 through 474 or resid 500))A3 - 331
121(chain A and (resid 3 through 331 or resid 333 through 474 or resid 500))A333 - 474
131(chain A and (resid 3 through 331 or resid 333 through 474 or resid 500))A500
211(chain B and (resid 3 through 331 or resid 333 through 474 or resid 500))B3 - 331
221(chain B and (resid 3 through 331 or resid 333 through 474 or resid 500))B333 - 474
231(chain B and (resid 3 through 331 or resid 333 through 474 or resid 500))B500
311(chain C and (resid 3 through 331 or resid 333 through 474 or resid 500))C3 - 331
321(chain C and (resid 3 through 331 or resid 333 through 474 or resid 500))C333 - 474
331(chain C and (resid 3 through 331 or resid 333 through 474 or resid 500))C500
411(chain D and (resid 3 through 331 or resid 333 through 474 or resid 500))D3 - 331
421(chain D and (resid 3 through 331 or resid 333 through 474 or resid 500))D333 - 474
431(chain D and (resid 3 through 331 or resid 333 through 474 or resid 500))D500
511(chain E and (resid 3 through 331 or resid 333 through 474 or resid 500))E3 - 331
521(chain E and (resid 3 through 331 or resid 333 through 474 or resid 500))E333 - 474
531(chain E and (resid 3 through 331 or resid 333 through 474 or resid 500))E500
611(chain F and (resid 3 through 331 or resid 333 through 474 or resid 500))F3 - 331
621(chain F and (resid 3 through 331 or resid 333 through 474 or resid 500))F333 - 474
631(chain F and (resid 3 through 331 or resid 333 through 474 or resid 500))F500
711(chain G and (resid 3 through 331 or resid 333 through 474 or resid 500))G3 - 331
721(chain G and (resid 3 through 331 or resid 333 through 474 or resid 500))G333 - 474
731(chain G and (resid 3 through 331 or resid 333 through 474 or resid 500))G500
811(chain H and (resid 3 through 331 or resid 333 through 474 or resid 500))H3 - 331
821(chain H and (resid 3 through 331 or resid 333 through 474 or resid 500))H333 - 474
831(chain H and (resid 3 through 331 or resid 333 through 474 or resid 500))H500

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Components

#1: Protein
Dihydrolipoyl dehydrogenase, mitochondrial / Dihydrolipoamide dehydrogenase / Glycine cleavage system L protein


Mass: 52653.215 Da / Num. of mol.: 8 / Mutation: P453L
Source method: isolated from a genetically manipulated source
Details: Sequence of the Strep-tag with the linker amino acids: MASWSHPQFEKGALEVLFQGPG
Source: (gene. exp.) Homo sapiens (human) / Gene: DLD, GCSL, LAD, PHE3 / Plasmid: pET52b+ / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P09622, dihydrolipoyl dehydrogenase
#2: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 27 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 452 / Source method: isolated from a natural source / Formula: H2O
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: 2.61 Å3/Da / Density % sol: 52.81 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.3
Details: 2 M ammonium sulfate, 1.5 (v/v)% PEG 400, 0.1 M Hepes (pH7.3)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 26, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.34→46.567 Å / Num. obs: 164477 / % possible obs: 96.6 % / Redundancy: 4.972 % / Biso Wilson estimate: 47.64 Å2 / CC1/2: 0.993 / Rmerge(I) obs: 0.144 / Rrim(I) all: 0.161 / Χ2: 0.97 / Net I/σ(I): 7.45
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.34-2.43.6010.9721.22107870.6021.13485.6
2.4-2.473.7370.8271.47115720.6690.96194.6
2.47-2.543.7310.6911.73113570.7520.80494.8
2.54-2.625.3530.6572.29115350.8380.72999.5
2.62-2.75.2770.5352.79111060.8740.59499.2
2.7-2.84.910.4213.34106950.9070.47198
2.8-2.95.5870.3554.25104770.9480.39199.6
2.9-3.025.5820.2795.35100260.9650.30899.5
3.02-3.165.5410.2276.5596170.9740.25199.6
3.16-3.315.4970.1758.392390.9830.19499.5
3.31-3.495.3520.1459.8787320.9850.16199.1
3.49-3.74.4560.13810.4173970.9760.15888.5
3.7-3.965.3630.12612.2571300.9880.1491.2
3.96-4.285.4930.09415.772170.9910.10499.3
4.28-4.685.3550.08517.4266370.9920.09499.3
4.68-5.245.0360.08616.3959430.990.09698.9
5.24-6.055.270.0915.9352530.9930.198
6.05-7.415.5340.08617.0444780.9930.09599.5
7.41-10.474.9440.06719.8434230.9950.07597.5
10.47-46.5675.1260.05821.3318560.9960.06497.6

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Phasing

PhasingMethod: molecular replacement
Phasing MRR rigid body: 0.586
Highest resolutionLowest resolution
Rotation46.57 Å2.76 Å

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Processing

Software
NameVersionClassification
MxCuBEdata collection
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
PHENIXrefinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1ZMD

1zmd


Resolution: 2.342→46.567 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.93 / Phase error: 28.01
Details: TLS groups, NCS torsion-angle restraints and occupancy refinement were included, hydrogen atoms were added to the final model during refinement
RfactorNum. reflection% reflection
Rfree0.249 2465 1.5 %
Rwork0.2272 --
obs0.2276 164323 96.56 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 173.35 Å2 / Biso mean: 64.3838 Å2 / Biso min: 15.98 Å2
Refinement stepCycle: final / Resolution: 2.342→46.567 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28064 0 807 452 29323
Biso mean--55.03 45.04 -
Num. residues----3776
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A17708X-RAY DIFFRACTION14.242TORSIONAL
12B17708X-RAY DIFFRACTION14.242TORSIONAL
13C17708X-RAY DIFFRACTION14.242TORSIONAL
14D17708X-RAY DIFFRACTION14.242TORSIONAL
15E17708X-RAY DIFFRACTION14.242TORSIONAL
16F17708X-RAY DIFFRACTION14.242TORSIONAL
17G17708X-RAY DIFFRACTION14.242TORSIONAL
18H17708X-RAY DIFFRACTION14.242TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 18

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.342-2.3870.31841170.30957633775082
2.387-2.43580.31981340.2998827896195
2.4358-2.48870.30941350.28568854898995
2.4887-2.54660.30151350.28328848898395
2.5466-2.61030.28311410.269492579398100
2.6103-2.68090.32181410.26649258939999
2.6809-2.75970.26871400.25519182932298
2.7597-2.84880.27081390.24829134927399
2.8488-2.95060.30091410.253193289469100
2.9506-3.06870.29111420.254292939435100
3.0687-3.20840.27981400.245892299369100
3.2084-3.37750.27441420.23679298944099
3.3775-3.5890.25471390.22129121926099
3.589-3.8660.32211190.28427890800984
3.866-4.25480.20641400.19629193933398
4.2548-4.86990.1861400.16689191933199
4.8699-6.13340.22941400.19449211935198
6.1334-46.57640.18011400.19379111925198
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)
10.3792-0.5745-0.12171.20810.38890.3584-0.09560.30180.05790.19680.0487-0.17650.12410.0102-0.20830.05570.00710.00520.46370.03690.388118.1685-7.0516-7.7046
21.5987-0.44420.05522.52690.35141.8193-0.23120.14020.29250.761-0.0893-0.1086-0.23040.02390.0790.29420.0557-0.0740.29710.06590.4278-0.735423.951.9589
31.1483-0.69980.10481.23370.03220.8078-0.0480.14160.0704-0.029-0.0206-0.06720.0120.02990.06010.1668-0.02590.02530.41360.04950.34477.1691.8803-12.0489
41.62660.09050.57850.5806-0.04010.361-0.20140.09640.0610.02920.23880.1362-0.2047-0.35290.07280.04070.03190.00940.4787-0.00160.367-16.52467.2477-5.5398
50.6813-0.6029-0.09710.68650.02750.6364-0.05150.0744-0.12020.09380.05130.10550.05290.04160.02260.1289-0.03470.01370.33410.00280.35731.7791-10.8645-5.2792
61.1382-0.1340.62231.7765-0.49651.3987-0.2168-0.13510.01880.55330.1160.1466-0.088-0.21940.03640.33710.07220.06810.4008-0.01120.3375-6.02331.636219.9745
70.31520.20480.07071.95090.00161.8832-0.1474-0.46590.11540.76430.15720.5082-0.0944-0.12590.25891.28960.39550.09160.752-0.12310.4202-8.363816.251842.2442
81.4811-0.1940.11861.50490.59792.1505-0.17840.02940.34620.2716-0.0859-0.4048-0.28720.37390.23930.44550.0752-0.16160.26850.01220.47815.331428.59079.4101
93.32241.5903-1.09791.4866-1.62012.2973-0.6126-0.22890.39270.48820.5650.2516-0.4199-0.41950.04980.87320.3332-0.07190.5262-0.06990.4418-8.066625.496226.6879
101.0217-0.03030.16590.4131-0.38770.6505-0.5182-0.48670.99141.3360.39780.1862-0.7293-0.22880.03711.78250.5508-0.20010.7445-0.32490.4026-0.728926.329943.4854
110.44950.28530.07920.57640.40580.3593-0.46840.18990.28490.73440.0324-0.2776-0.65410.1733-0.06451.0009-0.0298-0.47560.4747-0.04830.765217.918527.136425.1176
120.36090.6048-0.10161.1058-0.02990.0623-0.3933-0.04340.60410.5884-0.3298-0.8314-0.67770.0262-1.12631.0949-0.0803-0.65660.4884-0.10591.043924.255232.03526.7618
130.4910.21830.20830.543-0.39080.5554-0.3403-0.71760.24480.6570.062-0.0155-0.3245-0.2319-0.19861.84320.3299-0.4930.6209-0.26250.40568.547317.565849.7986
140.65880.0864-0.66840.0166-0.20961.9103-0.3218-0.3512-0.05881.14520.1163-0.1108-0.15850.11120.07571.06280.294-0.07710.5188-0.01950.46944.02927.546141.0278
151.3411-0.1470.11032.1252-0.84971.3259-0.11820.01470.10240.39030.0174-0.335-0.17110.10350.21030.27680.0222-0.09970.3802-0.05230.424716.51072.961917.2021
160.66040.8772-0.18741.6804-0.08340.5875-0.1269-0.0452-0.0435-0.18530.05-0.0703-0.05210.1373-0.02690.07030.03010.02340.40250.01020.3454-11.5082-14.4782-45.6052
170.63880.74950.07981.18840.16781.1715-0.1845-0.2437-0.4003-0.2210.0201-0.36870.3135-0.00130.10370.28790.02330.12230.35060.03090.4777-16.286-33.0201-48.7743
180.76770.62230.00311.11260.06270.80150.1262-0.21090.00250.196-0.1106-0.0096-0.02880.03390.09330.13020.00070.00720.42250.01720.3516-17.5429-11.0623-35.6093
192.01550.5236-1.07421.1856-0.38541.281-0.11470.0774-0.1463-0.13060.01250.19580.2963-0.40530.00050.1711-0.0540.02030.4852-0.04680.4063-38.9224-22.0419-45.7734
200.2369-0.11010.05140.3071-0.21920.23250.2827-0.2011-0.0769-0.2097-0.28640.2910.30520.12410.02430.0489-0.01560.06150.570.00930.3627-34.3168-14.0869-36.4571
210.6370.6426-0.03521.61240.2511.219-0.0381-0.1638-0.0293-0.1281-0.0150.0884-0.3575-0.12410.06460.09370.0093-0.02580.33850.0140.353-17.93541.2648-49.2881
221.2430.7352-0.60721.9812-0.4821.5187-0.31350.0830.0233-0.64380.17950.2440.131-0.31570.07150.4122-0.0984-0.06340.3933-0.00440.3304-30.0802-15.6253-70.9668
230.2835-0.397-0.28821.4176-0.10060.7992-0.28560.6113-0.1299-0.61070.16510.51930.1829-0.3202-0.08511.6413-0.8653-0.26470.6856-0.26370.3527-32.1379-30.4498-93.2677
241.29840.46850.27711.5911-0.43531.7169-0.43850.0946-0.2778-0.63020.1795-0.35460.3346-0.120.19040.7167-0.17040.23250.4283-0.0720.5249-24.116-41.381-67.2996
250.90870.5111-0.41370.62890.18911.0049-0.85640.4092-0.8575-1.39110.338-0.1970.75740.1589-1.42651.6899-0.54750.35650.5345-0.37730.5438-20.8675-41.2236-89.903
260.54510.3274-0.22690.5185-0.30050.2062-0.2943-0.1223-0.4445-0.4948-0.0373-0.53590.35920.3417-0.85430.6590.0450.56220.4352-0.10690.8462-1.3494-36.0928-73.0366
270.93170.6135-0.2121.0870.4090.4731-0.51810.3566-0.426-1.15350.2721-0.49640.4450.0548-0.08981.4107-0.24980.52460.6507-0.10960.7278-10.9625-36.32-91.1738
282.4896-0.12660.99461.0594-0.50421.3864-0.45590.0505-0.1755-1.1830.4229-0.2652-0.0811-0.1090.18610.9653-0.21210.15880.4363-0.1050.4651-13.2905-22.2534-80.0434
291.0461-0.25020.07071.59250.0380.9626-0.1507-0.0185-0.1509-0.56830.047-0.33470.00410.14690.14950.263-0.01650.13410.3866-0.03780.4242-7.3181-15.6699-67.4988
300.4113-0.0654-0.22451.37610.11670.6209-0.01470.31560.1033-0.8801-0.084-0.1612-0.5434-0.13520.06691.2365-0.06860.03930.52860.01820.4362-15.620826.681-85.5513
310.543-0.28920.48040.6638-0.86021.2145-0.2051-0.13770.2031-0.94440.02560.1178-0.0578-0.8092-0.12661.0640.1797-0.28290.6607-0.050.5917-38.270834.4289-78.882
321.0073-0.0023-0.05721.5091-0.29490.3544-0.05850.1691-0.1273-0.64180.1180.2663-0.3445-0.20560.05650.7932-0.0079-0.05210.5157-0.00320.3519-23.870613.1724-81.1455
331.5473-0.09610.09921.9934-0.10651.146-0.0085-0.17330.0671-0.16140.03580.2893-0.4943-0.24280.04640.55040.0376-0.00720.4665-0.02810.3725-25.171826.1072-55.2272
341.43610.71380.18141.6203-0.13251.17490.1515-0.52530.38810.3961-0.14860.2493-0.5186-0.1983-0.05230.8709-0.00210.12230.6473-0.12780.5338-21.241640.3988-32.9703
350.80780.31160.24550.73850.14222.2254-0.03560.12750.4949-0.40570.1174-0.0048-0.2724-0.07810.01111.0445-0.054-0.0060.46210.08840.6201-11.152950.9729-67.5039
361.62510.6068-0.06081.4879-0.37561.11940.0293-0.3440.48850.29430.0070.0767-0.6838-0.043-0.01241.0153-0.01430.03320.5899-0.12090.5775-13.184249.4213-38.252
371.47120.3398-0.06181.8112-0.05821.0942-0.0725-0.03610.1265-0.07330.005-0.3945-0.45450.33460.0410.9577-0.21960.11510.6265-0.00540.64836.927148.1531-54.6407
381.44330.7007-0.01182.043-0.6831.41770.162-0.52820.1610.051-0.3491-0.0977-0.65970.13130.02520.7847-0.16090.00730.6496-0.08530.58811.679444.0258-35.1029
391.46510.6827-0.62811.418-0.33381.3854-0.138-0.7335-0.06990.1697-0.1535-0.2229-0.4961-0.0924-0.00850.5982-0.0968-0.00590.60570.00640.3758-11.451331.3931-33.1371
402.78290.0987-0.72980.93440.77341.0051-0.07-0.2554-0.0370.1928-0.0418-0.2632-0.5590.17030.06620.7075-0.08980.06490.4176-0.04980.3819-6.183229.5903-48.7854
411.62260.30140.30771.81480.02891.2859-0.06070.0421-0.0858-0.43330.0503-0.3178-0.46210.21340.01670.6007-0.12630.10450.4604-0.00610.459-3.510422.4426-62.2428
421.70990.02390.08070.5444-0.46291.6245-0.1422-0.12570.13260.6466-0.1006-0.40610.60160.20440.11580.88810.1099-0.17520.42790.03640.403116.265-27.935835.454
430.2887-0.1941-0.26110.6672-0.28330.46150.1582-0.1209-0.37210.43210.0535-0.36270.57560.0420.11281.2942-0.0346-0.09460.55240.14050.6079.5194-55.114227.3367
440.239-0.1612-0.0640.9629-0.16291.05770.1203-0.3142-0.08931.0385-0.21280.06940.6677-0.4733-0.08711.1967-0.1630.0640.63190.00070.4294-0.7717-39.58134.02
450.6203-0.3416-0.36410.3725-0.13971.1163-0.3233-0.3019-0.30720.977-0.0846-0.0142-0.17570.0177-0.39411.4488-0.36380.4690.76470.11140.5572-17.6086-49.994836.7111
461.07160.9103-0.12372.4124-0.75730.24910.1407-0.14180.14020.9788-0.12930.4230.6546-0.3435-0.00350.9808-0.18460.21960.5-0.01460.3854-6.6952-30.801636.0648
471.20230.3922-0.15112.63011.01241.4230.0679-0.09070.12080.7109-0.1128-0.04080.3177-0.24440.02520.62750.0131-0.04290.38590.02720.37684.7661-27.332522.791
482.0825-0.4759-0.82221.92990.28112.1128-0.0462-0.10960.0128-0.00990.11680.21330.2942-0.40560.07380.414-0.1380.06250.5138-0.01310.3762-5.7767-39.78564.3475
491.70740.0494-0.26262.06640.00281.9550.03340.1008-0.1894-0.1684-0.03520.06320.8243-0.43190.07670.5346-0.05560.00550.4258-0.02550.38812.6222-39.68721.6388
501.0398-0.21090.09251.3743-0.30291.2793-0.09010.1772-0.31050.2374-0.0436-0.02680.5614-0.0108-0.1070.8464-0.10010.00090.4351-0.00310.51177.3862-59.1103-2.3026
511.3068-0.210.23561.351-0.22621.3037-0.07810.1043-0.1908-0.0230.1004-0.23340.63490.0565-0.05280.72460.01390.01670.4162-0.09340.503619.4804-59.4771-9.4001
522.4599-0.07681.04021.00650.92751.8124-0.26430.2078-0.12380.11180.0551-0.38470.18210.2021-0.00120.44920.0786-0.04450.3585-0.07770.457117.8079-43.5557-2.1331
531.73310.061-0.1122.0979-0.01361.61450.0104-0.0369-0.01010.60460.0289-0.36710.34030.2005-0.01550.46520.0822-0.10060.3507-0.01590.385320.5014-36.440211.2593
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 49 )A3 - 49
2X-RAY DIFFRACTION2chain 'A' and (resid 50 through 84 )A50 - 84
3X-RAY DIFFRACTION3chain 'A' and (resid 85 through 199 )A85 - 199
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 260 )A200 - 260
5X-RAY DIFFRACTION5chain 'A' and (resid 261 through 358 )A261 - 358
6X-RAY DIFFRACTION6chain 'A' and (resid 359 through 474 )A359 - 474
7X-RAY DIFFRACTION7chain 'B' and (resid 3 through 49 )B3 - 49
8X-RAY DIFFRACTION8chain 'B' and (resid 50 through 84 )B50 - 84
9X-RAY DIFFRACTION9chain 'B' and (resid 85 through 109 )B85 - 109
10X-RAY DIFFRACTION10chain 'B' and (resid 110 through 179 )B110 - 179
11X-RAY DIFFRACTION11chain 'B' and (resid 180 through 219 )B180 - 219
12X-RAY DIFFRACTION12chain 'B' and (resid 220 through 276 )B220 - 276
13X-RAY DIFFRACTION13chain 'B' and (resid 277 through 307 )B277 - 307
14X-RAY DIFFRACTION14chain 'B' and (resid 308 through 358 )B308 - 358
15X-RAY DIFFRACTION15chain 'B' and (resid 359 through 474 )B359 - 474
16X-RAY DIFFRACTION16chain 'C' and (resid 3 through 67 )C3 - 67
17X-RAY DIFFRACTION17chain 'C' and (resid 68 through 109 )C68 - 109
18X-RAY DIFFRACTION18chain 'C' and (resid 110 through 187 )C110 - 187
19X-RAY DIFFRACTION19chain 'C' and (resid 188 through 260 )C188 - 260
20X-RAY DIFFRACTION20chain 'C' and (resid 261 through 288 )C261 - 288
21X-RAY DIFFRACTION21chain 'C' and (resid 289 through 358 )C289 - 358
22X-RAY DIFFRACTION22chain 'C' and (resid 359 through 474 )C359 - 474
23X-RAY DIFFRACTION23chain 'D' and (resid 3 through 49 )D3 - 49
24X-RAY DIFFRACTION24chain 'D' and (resid 50 through 109 )D50 - 109
25X-RAY DIFFRACTION25chain 'D' and (resid 110 through 199 )D110 - 199
26X-RAY DIFFRACTION26chain 'D' and (resid 200 through 233 )D200 - 233
27X-RAY DIFFRACTION27chain 'D' and (resid 234 through 342 )D234 - 342
28X-RAY DIFFRACTION28chain 'D' and (resid 343 through 370 )D343 - 370
29X-RAY DIFFRACTION29chain 'D' and (resid 371 through 474 )D371 - 474
30X-RAY DIFFRACTION30chain 'E' and (resid 3 through 199 )E3 - 199
31X-RAY DIFFRACTION31chain 'E' and (resid 200 through 260 )E200 - 260
32X-RAY DIFFRACTION32chain 'E' and (resid 261 through 358 )E261 - 358
33X-RAY DIFFRACTION33chain 'E' and (resid 359 through 474 )E359 - 474
34X-RAY DIFFRACTION34chain 'F' and (resid 3 through 49 )F3 - 49
35X-RAY DIFFRACTION35chain 'F' and (resid 50 through 84 )F50 - 84
36X-RAY DIFFRACTION36chain 'F' and (resid 85 through 187 )F85 - 187
37X-RAY DIFFRACTION37chain 'F' and (resid 188 through 260 )F188 - 260
38X-RAY DIFFRACTION38chain 'F' and (resid 261 through 307 )F261 - 307
39X-RAY DIFFRACTION39chain 'F' and (resid 308 through 342 )F308 - 342
40X-RAY DIFFRACTION40chain 'F' and (resid 343 through 370 )F343 - 370
41X-RAY DIFFRACTION41chain 'F' and (resid 371 through 474 )F371 - 474
42X-RAY DIFFRACTION42chain 'G' and (resid 3 through 49 )G3 - 49
43X-RAY DIFFRACTION43chain 'G' and (resid 50 through 109 )G50 - 109
44X-RAY DIFFRACTION44chain 'G' and (resid 110 through 233 )G110 - 233
45X-RAY DIFFRACTION45chain 'G' and (resid 234 through 260 )G234 - 260
46X-RAY DIFFRACTION46chain 'G' and (resid 261 through 307 )G261 - 307
47X-RAY DIFFRACTION47chain 'G' and (resid 308 through 370 )G308 - 370
48X-RAY DIFFRACTION48chain 'G' and (resid 371 through 414 )G371 - 414
49X-RAY DIFFRACTION49chain 'G' and (resid 415 through 474 )G415 - 474
50X-RAY DIFFRACTION50chain 'H' and (resid 3 through 84 )H3 - 84
51X-RAY DIFFRACTION51chain 'H' and (resid 85 through 342 )H85 - 342
52X-RAY DIFFRACTION52chain 'H' and (resid 343 through 370 )H343 - 370
53X-RAY DIFFRACTION53chain 'H' and (resid 371 through 474 )H371 - 474

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