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- PDB-5nhg: Crystal structure of the human dihydrolipoamide dehydrogenase -

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Basic information

Entry
Database: PDB / ID: 5nhg
TitleCrystal structure of the human dihydrolipoamide dehydrogenase
ComponentsDihydrolipoyl dehydrogenase, mitochondrialDihydrolipoamide dehydrogenase
KeywordsOXIDOREDUCTASE / dihydrolipoamide dehydrogenase / E3 subunit / pyruvate dehydrogenase complex / alpha-ketoglutarate dehydrogenase complex
Function / homology
Function and homology information


acetyltransferase complex / acrosomal matrix / Glycine degradation / : / oxoglutarate dehydrogenase complex / dihydrolipoyl dehydrogenase / dihydrolipoyl dehydrogenase activity / : / Lysine catabolism / acetyl-CoA biosynthetic process from pyruvate ...acetyltransferase complex / acrosomal matrix / Glycine degradation / : / oxoglutarate dehydrogenase complex / dihydrolipoyl dehydrogenase / dihydrolipoyl dehydrogenase activity / : / Lysine catabolism / acetyl-CoA biosynthetic process from pyruvate / pyruvate dehydrogenase complex / branched-chain amino acid catabolic process / : / Citric acid cycle (TCA cycle) / Branched-chain amino acid catabolism / Pyruvate metabolism / Glyoxylate metabolism and glycine degradation / Regulation of pyruvate dehydrogenase (PDH) complex / motile cilium / sperm capacitation / Signaling by Retinoic Acid / mitochondrial electron transport, NADH to ubiquinone / gastrulation / 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 / Pyridine nucleotide-disulphide oxidoreductase ...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 / Resolution: 2.27 Å
AuthorsSzabo, E. / Mizsei, R. / Wilk, P. / Zambo, Z. / Torocsik, B. / Weiss, M.S. / Adam-Vizi, V. / Ambrus, A.
Funding support Hungary, Germany, 6items
OrganizationGrant numberCountry
Hungarian Academy of Sciences02001 Hungary
Hungarian Scientific Research Fund112230 Hungary
Hungarian Brain Research ProgramKTIA_13_NAP-A-III/6 Hungary
Hungarian Academy of SciencesBolyai Fellowship [to A.A.] Hungary
European Molecular Biology OrganizationShort-term Fellowship [to A.A.] Hungary
Helmholtz-Zentrum Berlin16204087-ST, BESSY: 362 [to E.Sz., A.A.] Germany
CitationJournal: Free Radic. Biol. Med. / Year: 2018
Title: Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase.
Authors: Szabo, E. / Mizsei, R. / Wilk, P. / Zambo, Z. / Torocsik, B. / Weiss, M.S. / Adam-Vizi, V. / Ambrus, A.
History
DepositionMar 21, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 16, 2018Provider: repository / Type: Initial release
Revision 1.1Jul 4, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name
Revision 1.2Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _citation.country / _database_2.pdbx_DOI ..._citation.country / _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: 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)427,39624
Polymers420,0488
Non-polymers7,34916
Water4,954275
1
A: Dihydrolipoyl dehydrogenase, mitochondrial
B: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


  • defined by software
  • Evidence: gel filtration, Ambrus A et al., Hum. Mol. Genet., 20:2984-2995, 2011., mass spectrometry, Ambrus A et al., Hum. Mol. Genet., 20:2984-2995, 2011; Ambrus A et al., Biochim. Biophys. Acta., ...Evidence: gel filtration, Ambrus A et al., Hum. Mol. Genet., 20:2984-2995, 2011., mass spectrometry, Ambrus A et al., Hum. Mol. Genet., 20:2984-2995, 2011; Ambrus A et al., Biochim. Biophys. Acta., 1862(11):2098-2109, 2016.
  • 107 kDa, 2 polymers
  • Search similar-shape structures of this assembly by Omokage search (details)
Theoretical massNumber of molelcules
Total (without water)106,8276
Polymers105,0122
Non-polymers1,8154
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10970 Å2
ΔGint-51 kcal/mol
Surface area34500 Å2
MethodPISA
2
C: Dihydrolipoyl dehydrogenase, mitochondrial
D: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,9146
Polymers105,0122
Non-polymers1,9024
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11400 Å2
ΔGint-47 kcal/mol
Surface area34910 Å2
MethodPISA
3
E: Dihydrolipoyl dehydrogenase, mitochondrial
F: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,9497
Polymers105,0122
Non-polymers1,9385
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11740 Å2
ΔGint-44 kcal/mol
Surface area34570 Å2
MethodPISA
4
G: Dihydrolipoyl dehydrogenase, mitochondrial
H: Dihydrolipoyl dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,7055
Polymers105,0122
Non-polymers1,6933
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11140 Å2
ΔGint-52 kcal/mol
Surface area34630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.060, 113.540, 136.880
Angle α, β, γ (deg.)83.180, 84.750, 81.090
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21(chain B and resid 4 through 474)
31(chain C and resid 4 through 474)
41(chain D and resid 4 through 474)
51chain E
61chain F
71chain G
81chain H

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: PRO / Beg label comp-ID: PRO / End auth comp-ID: PHE / End label comp-ID: PHE / Auth seq-ID: 4 - 474 / Label seq-ID: 25 - 495

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1chain AAA
2(chain B and resid 4 through 474)BB
3(chain C and resid 4 through 474)CC
4(chain D and resid 4 through 474)DD
5chain EEE
6chain FFF
7chain GGG
8chain HHH

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Components

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


Mass: 52505.980 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Details: sequence of the Strep-tag with linker amino acids: ASWSHPQFEKGALEVLFQGPG
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 / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical
ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER / Tris


Mass: 122.143 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#4: Chemical ChemComp-BTB / 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / BIS-TRIS BUFFER / Bis-tris methane


Mass: 209.240 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H19NO5 / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 275 / 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: 2.28 Å3/Da / Density % sol: 46.06 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.45
Details: 0.1 M Bis-Tris (pH 7.45), 0.2 M MgCl2, 25 (w/v)% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 23, 2016
RadiationMonochromator: Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.27→46.622 Å / Num. obs: 160435 / % possible obs: 98.1 % / Observed criterion σ(I): -3 / Redundancy: 3.756 % / Biso Wilson estimate: 48.38 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.058 / Rrim(I) all: 0.068 / Χ2: 1.022 / Net I/σ(I): 13.68 / Num. measured all: 602581 / Scaling rejects: 501
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.27-2.332.1060.5411.46110680.660.73391.9
2.33-2.393.7580.5942.19116730.7830.69298.5
2.39-2.463.9950.4862.8112880.8490.56299
2.46-2.543.9210.3883.42111130.8970.4599.2
2.54-2.623.8690.3184.14107410.9180.36999.3
2.62-2.713.7750.2265.51103130.9560.26499
2.71-2.823.6740.1746.8297060.9720.20496.8
2.82-2.934.0280.1438.996270.9840.16599.2
2.93-3.064.0040.11610.9392320.9880.13499.5
3.06-3.213.9730.08814.1388360.9920.10199.3
3.21-3.383.9310.06617.9683930.9950.07799.1
3.38-3.593.710.05421.1778210.9960.06397.5
3.59-3.843.9110.04725.3473110.9970.05498
3.84-4.144.0340.04229.0369570.9980.04899.3
4.14-4.543.9570.03932.5864150.9980.04599.3
4.54-5.083.7780.03733.4257450.9980.04398.8
5.08-5.863.7050.03531.7249100.9980.04196.3
5.86-7.183.9610.03534.1443130.9980.0499.3
7.18-10.153.730.02838.6232700.9990.03397.7
10.15-46.6223.8240.02641.5117030.9990.03193.3

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Processing

Software
NameClassification
PHENIXrefinement
MxCuBEdata collection
XDSdata scaling
XDSdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1ZMD

1zmd


Resolution: 2.27→46.622 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.13 / Phase error: 25.27
Details: torsion-angle NCS restraints were used during refinement in phenix.refine
RfactorNum. reflection% reflection
Rfree0.2096 4531 1.49 %
Rwork0.1805 --
obs0.1809 304054 93.02 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 190.7 Å2 / Biso mean: 74.983 Å2 / Biso min: 28.16 Å2
Refinement stepCycle: final / Resolution: 2.27→46.622 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28011 0 735 275 29021
Biso mean--60.07 48.39 -
Num. residues----3771
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00728985
X-RAY DIFFRACTIONf_angle_d0.94239238
X-RAY DIFFRACTIONf_chiral_restr0.0594515
X-RAY DIFFRACTIONf_plane_restr0.0064993
X-RAY DIFFRACTIONf_dihedral_angle_d14.88217166
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A21863X-RAY DIFFRACTION11.317TORSIONAL
12B21863X-RAY DIFFRACTION11.317TORSIONAL
13C21863X-RAY DIFFRACTION11.317TORSIONAL
14D21863X-RAY DIFFRACTION11.317TORSIONAL
15E21863X-RAY DIFFRACTION11.317TORSIONAL
16F21863X-RAY DIFFRACTION11.317TORSIONAL
17G21863X-RAY DIFFRACTION11.317TORSIONAL
18H21863X-RAY DIFFRACTION11.317TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2701-2.29590.3628810.33615095517648
2.2959-2.32290.34191100.32466755686562
2.3229-2.35130.31551010.30967911801274
2.3513-2.3810.31981560.29939370952688
2.381-2.41230.31081370.2916104781061596
2.4123-2.44540.28231710.2834103371050897
2.4454-2.48030.37051760.2687104211059797
2.4803-2.51730.33551160.2551104551057197
2.5173-2.55670.26111230.2544103561047997
2.5567-2.59860.26121910.2503105841077597
2.5986-2.64340.24991480.2461104081055697
2.6434-2.69150.27581370.2353103451048297
2.6915-2.74320.25631450.232102631040894
2.7432-2.79920.27321310.240199651009693
2.7992-2.86010.28741800.2527105931077398
2.8601-2.92660.32181360.2321103131044998
2.9266-2.99980.26381400.2316106371077798
2.9998-3.08090.27221470.214104521059998
3.0809-3.17150.23521870.2129105301071798
3.1715-3.27380.22121750.2129105021067798
3.2738-3.39080.22562140.2011103951060998
3.3908-3.52650.24411370.1868106201075797
3.5265-3.6870.21571520.171598481000092
3.687-3.88130.16961410.158105791072099
3.8813-4.12430.16751880.1411105561074498
4.1243-4.44250.15371650.1237105211068699
4.4425-4.88910.13011830.1197105321071598
4.8891-5.59560.21041690.1322100441021394
5.5956-7.04590.16551530.1586105461069998
7.0459-46.63140.15361410.1378101121025394
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)
14.10692.4963.65322.50933.10145.63060.2209-0.03620.03090.0623-0.0272-0.20650.23770.2203-0.20040.4391-0.0096-0.06530.29580.020.495612.83960.4713-3.0052
22.70730.03521.69540.95371.02792.54110.00190.4413-0.1736-0.12950.0566-0.04140.18410.1768-0.08610.5657-0.0082-0.010.41590.02560.48335.6287-5.4614-18.6461
31.5004-0.0712-0.06491.42550.17261.26990.1897-0.2401-0.4640.32-0.014-0.07990.5314-0.0763-0.20390.7009-0.0574-0.1120.38540.06770.5370.9699-11.23531.5698
42.14571.1799-0.34943.77850.54771.12460.3958-0.6274-0.24090.7649-0.2016-0.18320.58360.0133-0.20920.7238-0.1075-0.12680.52270.09450.40665.1571-4.641312.8745
53.5294-0.8833-0.35960.9862-0.91150.65740.0979-0.50420.53330.40030.0336-0.19870.2371-0.0568-0.09160.481-0.0888-0.03320.3712-0.010.4627-2.67459.44974.8938
62.8240.26850.1253.85811.65325.80480.1818-0.03610.1324-0.0378-0.12010.3357-0.0108-0.5249-0.05020.2828-0.0439-0.00830.34660.04490.362-15.020915.3716-7.4983
73.2054-0.8832-0.53474.38672.22964.22310.20410.02060.14990.0138-0.37740.6385-0.0577-0.93090.06160.4149-0.00660.01340.59540.02550.5458-29.234626.331-24.3594
85.9506-3.99752.46955.3312-4.29323.4127-0.04950.2559-0.270.33490.0581-0.570.69870.29270.01150.49130.0235-0.06650.3815-0.04480.4324-4.2602-1.2183-30.2223
96.9745-6.4153-6.09885.96596.32037.17080.01720.2949-0.85690.4695-0.49460.9680.5623-0.82530.69640.5246-0.106-0.05690.58490.02020.584-23.89799.8708-27.3873
101.8778-0.775-0.26612.6211.33712.47040.16520.35440.0228-0.4224-0.21130.4073-0.1831-0.43830.04020.4280.0277-0.0730.45270.10280.3607-19.502723.1171-36.9613
112.02780.31211.80961.82530.28185.34940.00130.4856-0.0088-0.294-0.0326-0.1946-0.05220.56530.03240.44140.02080.08110.46780.04480.4453.746618.535-40.6478
122.4469-1.0116-1.62422.47711.50513.79310.26790.15550.3308-0.5099-0.1173-0.0524-0.4425-0.1978-0.18450.47170.0097-0.01250.36450.11140.4185-14.90133.1045-31.1075
133.1978-0.8805-0.49030.1996-0.17832.24220.1416-0.03640.34620.2216-0.0572-0.1009-0.096-0.1834-0.08130.3911-0.00670.02420.39310.0530.4213-4.987924.9611-19.5086
142.35220.1782-0.48414.77760.26993.36410.1104-0.1090.18120.10540.002-0.34240.02190.2205-0.15030.2453-0.0262-0.01090.29690.02340.36376.413919.6808-11.5853
151.59280.32840.48122.68470.43821.44390.1210.0406-0.2243-0.0985-0.0774-0.31420.17230.1854-0.08250.43120.088-0.03410.29910.04690.477411.547243.852-67.8404
161.3625-0.0480.45794.256-1.42552.75250.1718-0.0519-0.3814-0.08690.11660.85830.3199-0.138-0.26080.4745-0.0406-0.10690.34430.0370.6185-12.118237.8988-69.1966
173.77911.39771.51714.92760.4122.12850.2169-0.5048-0.07390.8199-0.1196-0.06120.3314-0.1405-0.09340.48920.06670.00450.34490.03460.34282.912146.1321-52.7544
184.92522.7865.70422.36932.5426.3687-0.516-0.28310.73730.2493-0.15320.1751-0.6242-0.2410.74220.52650.0551-0.13920.39480.00330.54266.098161.6951-60.3224
192.3505-0.54990.37414.2189-0.00243.96950.0992-0.01830.0649-0.1007-0.16350.45330.0247-0.27880.06590.35160.0186-0.04330.29930.01220.5243-13.613760.9371-72.9226
203.5591-1.4226-0.69246.10692.46094.23630.03670.26310.5337-0.4232-0.15410.2072-0.5731-0.36630.11160.53740.0701-0.04560.33210.06310.4816-9.927269.1775-78.1563
210.48130.0558-0.08191.33761.69991.71830.26190.3264-0.2163-0.865-0.40290.5939-0.0416-0.25970.03360.97790.2055-0.09620.58490.0850.5435-15.46368.7336-96.8365
220.394-0.02550.96812.1729-0.72522.3180.36960.5247-0.1456-0.9994-0.20450.06220.4196-0.0928-0.13520.9210.089-0.13880.58260.01560.489-9.120750.9093-97.2682
230.73250.58121.3431.33220.57671.6480.25080.6890.3271-1.2103-0.50520.2823-0.4574-0.19470.24071.43040.3846-0.13290.83680.24710.6242-13.798973.3187-108.0034
241.632-0.37930.55270.1335-0.43963.04250.30720.71120.3126-1.0592-0.1901-0.521-0.04960.8262-0.08831.24280.19910.29120.81440.20010.630210.451863.7863-106.5135
251.09780.33840.04880.86261.11261.32540.11570.53540.4498-1.0287-0.2345-0.3507-0.55710.07110.15181.58180.21660.1140.74770.25910.749-2.363579.684-108.3897
262.4772-0.84070.4543.644-1.7990.9748-0.14390.31750.7287-0.5282-0.1752-0.0389-0.826-0.19070.29731.17120.2022-0.09950.51950.1180.7462-11.954583.713-93.3801
273.7033-1.3208-0.46851.44410.13683.10930.3930.10090.5501-0.7165-0.5236-0.3622-0.1355-0.18990.11570.75650.09980.01010.43040.08470.5470.427173.915-88.2748
284.23461.2436-0.11716.5356-0.48335.04960.03740.11280.7898-0.83750.0373-0.4534-0.57980.5207-0.03280.45330.00750.11630.40580.03990.587413.006269.1308-82.1133
294.93880.2119-0.14945.27380.13043.49830.0493-0.37470.49440.27370.0869-0.5548-0.21810.3562-0.12790.5681-0.012-0.04460.3812-0.01570.53867.816666.7643-74.1186
302.3460.0381-0.20862.18490.71422.65670.2229-0.00460.1610.1916-0.21450.5915-0.1753-0.703-0.00460.44470.03480.03660.68-0.1430.5884-33.806341.369432.1938
311.32810.2285-0.38851.86060.54333.57030.1405-0.51890.25180.48-0.0243-0.3263-0.03180.236-0.16870.5886-0.0665-0.02930.5888-0.13880.5256-13.144741.974843.0394
324.7799-0.49690.08254.9827-0.45866.2979-0.05010.089-0.72290.4648-0.18940.30951.1185-0.78430.19450.6119-0.1801-0.00670.5342-0.08960.704-30.585419.849931.0832
337.22114.13982.56843.82161.3132.5899-0.14371.0813-0.889-0.37540.2478-0.11010.4686-0.3667-0.1670.4929-0.1296-0.01440.6575-0.22270.6329-26.700528.341119.874
342.2727-0.11540.27472.17310.32023.59110.188-0.08540.0887-0.11110.0665-0.6038-0.26290.2711-0.2490.3341-0.05050.05180.3115-0.07730.5056-6.782939.556814.5156
350.5296-0.59170.00891.20560.89880.80840.3176-0.15750.4488-0.19580.0435-0.4102-0.57340.238-0.39530.9031-0.08690.21970.4092-0.08030.90371.028260.42614.6826
360.9818-0.5573-0.05791.58030.49011.10030.35570.13810.5281-0.5759-0.1524-0.0726-0.8788-0.2898-0.14691.15120.13640.23960.43540.07510.8513-14.576467.4541-3.428
372.5647-0.8424-1.39650.15350.44250.57150.3310.36410.0919-0.367-0.1728-0.3265-0.5587-0.0922-0.23960.70680.09930.06930.41520.02940.6841-16.211849.9839-0.1638
381.70350.05111.291.46050.97958.8485-0.05390.04860.3331-0.302-0.32120.3211-1.164-0.42240.410.54230.17290.03330.4702-0.0350.6591-30.774949.0886.5179
392.0493-0.3450.74923.70781.49347.08560.16170.09580.0162-0.1972-0.20160.3157-0.1688-0.68250.00090.35950.07840.02360.4161-0.00690.4794-26.707241.30037.6715
400.91290.5820.39383.05611.20111.27790.3684-0.64630.36890.3203-0.34480.21880.0084-0.2195-0.04020.6201-0.24360.13230.6198-0.14950.5459-31.703687.9366-38.9607
411.37721.3683-0.36552.823-0.72420.44550.2257-0.61760.63980.32640.054-0.081-0.56920.1635-0.18490.7296-0.21520.28730.7526-0.36120.9833-26.5541105.3131-37.4482
421.12120.35510.19231.21090.36121.99730.541-0.96010.18510.7581-0.41590.02960.24340.0433-0.13140.8178-0.29950.03490.7953-0.09890.5575-18.044887.7424-28.2085
432.51570.04830.01250.52231.1553.35750.4033-0.9051-0.15660.5727-0.314-0.2620.45120.1714-0.08751.0089-0.2619-0.12520.76590.10020.5289-18.534676.5356-28.0221
445.12252.07222.09343.39372.96322.71220.2642-0.2444-0.30430.6026-0.12510.24260.2682-0.2156-0.11950.6589-0.21950.02340.51760.02060.5311-27.705973.3695-43.4002
459.02221.65721.10530.5417-0.76471.48450.2409-0.2443-0.80640.3458-0.3637-0.48620.4715-0.26250.13350.5503-0.13120.0260.4325-0.00570.506-15.55783.8807-47.6273
463.9094-1.2568-0.10398.222-0.41794.53310.2359-0.42160.36580.5424-0.0082-0.5235-0.0530.3744-0.21380.3078-0.0697-0.03190.4355-0.08330.5328-2.25491.9315-51.9191
474.5247-0.6949-0.49934.42741.48874.66660.22460.16880.1139-0.31070.0417-0.35930.01840.3308-0.24020.3713-0.01460.05270.2553-0.00590.5081-6.965990.5453-59.2244
480.66890.48851.20872.64171.09632.29160.5943-0.33840.6047-0.64120.4397-0.7482-0.5910.8978-0.9130.9313-0.00450.47670.5539-0.19311.54633.7894108.2324-72.7971
490.31230.3912-0.09712.655-1.78381.28710.5448-0.6090.71870.224-0.2569-0.1737-0.59370.264-0.15820.81-0.14870.37970.583-0.31321.2891-19.2513116.9154-45.2647
500.7903-0.1303-0.17633.1531.38951.53850.3796-0.09460.5348-0.69360.1865-0.6886-0.80940.661-0.5020.9455-0.17130.40230.6885-0.23441.52675.0049114.4697-69.5988
511.24010.52440.62741.7221-0.05071.52290.6660.15520.9182-0.8822-0.0786-0.1804-0.9582-0.7823-0.35861.15260.31690.54060.35230.13231.3928-23.6655121.8565-66.3128
521.0347-0.06330.47434.1050.34320.64260.68810.92330.8247-1.371-0.1903-0.0254-1.1112-0.229-0.11751.49580.35720.50660.51880.34811.2197-15.8035118.1205-79.9375
532.73261.1156-2.15393.33220.07213.05660.40760.25920.4317-0.80720.1886-0.7501-0.3908-0.0235-0.61140.74780.08520.21850.37510.01330.908-11.0363101.9437-74.6592
543.52270.28640.15514.2641.68445.88540.18690.18280.24780.0303-0.1770.56890.0116-0.5033-0.03250.3122-0.02520.02590.36170.00930.5788-28.573792.7177-60.3294
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 4 through 67 )A4 - 67
2X-RAY DIFFRACTION2chain 'A' and (resid 68 through 110 )A68 - 110
3X-RAY DIFFRACTION3chain 'A' and (resid 111 through 260 )A111 - 260
4X-RAY DIFFRACTION4chain 'A' and (resid 261 through 327 )A261 - 327
5X-RAY DIFFRACTION5chain 'A' and (resid 328 through 380 )A328 - 380
6X-RAY DIFFRACTION6chain 'A' and (resid 381 through 474 )A381 - 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 110 )B85 - 110
10X-RAY DIFFRACTION10chain 'B' and (resid 111 through 199 )B111 - 199
11X-RAY DIFFRACTION11chain 'B' and (resid 200 through 260 )B200 - 260
12X-RAY DIFFRACTION12chain 'B' and (resid 261 through 343 )B261 - 343
13X-RAY DIFFRACTION13chain 'B' and (resid 344 through 370 )B344 - 370
14X-RAY DIFFRACTION14chain 'B' and (resid 371 through 474 )B371 - 474
15X-RAY DIFFRACTION15chain 'C' and (resid 3 through 187 )C3 - 187
16X-RAY DIFFRACTION16chain 'C' and (resid 188 through 260 )C188 - 260
17X-RAY DIFFRACTION17chain 'C' and (resid 261 through 327 )C261 - 327
18X-RAY DIFFRACTION18chain 'C' and (resid 328 through 358 )C328 - 358
19X-RAY DIFFRACTION19chain 'C' and (resid 359 through 424 )C359 - 424
20X-RAY DIFFRACTION20chain 'C' and (resid 425 through 474 )C425 - 474
21X-RAY DIFFRACTION21chain 'D' and (resid 4 through 67 )D4 - 67
22X-RAY DIFFRACTION22chain 'D' and (resid 68 through 109 )D68 - 109
23X-RAY DIFFRACTION23chain 'D' and (resid 110 through 187 )D110 - 187
24X-RAY DIFFRACTION24chain 'D' and (resid 188 through 260 )D188 - 260
25X-RAY DIFFRACTION25chain 'D' and (resid 261 through 307 )D261 - 307
26X-RAY DIFFRACTION26chain 'D' and (resid 308 through 342 )D308 - 342
27X-RAY DIFFRACTION27chain 'D' and (resid 343 through 370 )D343 - 370
28X-RAY DIFFRACTION28chain 'D' and (resid 371 through 424 )D371 - 424
29X-RAY DIFFRACTION29chain 'D' and (resid 425 through 474 )D425 - 474
30X-RAY DIFFRACTION30chain 'E' and (resid 4 through 167 )E4 - 167
31X-RAY DIFFRACTION31chain 'E' and (resid 168 through 288 )E168 - 288
32X-RAY DIFFRACTION32chain 'E' and (resid 289 through 327 )E289 - 327
33X-RAY DIFFRACTION33chain 'E' and (resid 328 through 358 )E328 - 358
34X-RAY DIFFRACTION34chain 'E' and (resid 359 through 474 )E359 - 474
35X-RAY DIFFRACTION35chain 'F' and (resid 4 through 152 )F4 - 152
36X-RAY DIFFRACTION36chain 'F' and (resid 153 through 342 )F153 - 342
37X-RAY DIFFRACTION37chain 'F' and (resid 343 through 370 )F343 - 370
38X-RAY DIFFRACTION38chain 'F' and (resid 371 through 402 )F371 - 402
39X-RAY DIFFRACTION39chain 'F' and (resid 403 through 474 )F403 - 474
40X-RAY DIFFRACTION40chain 'G' and (resid 4 through 67 )G4 - 67
41X-RAY DIFFRACTION41chain 'G' and (resid 68 through 110 )G68 - 110
42X-RAY DIFFRACTION42chain 'G' and (resid 111 through 260 )G111 - 260
43X-RAY DIFFRACTION43chain 'G' and (resid 261 through 307 )G261 - 307
44X-RAY DIFFRACTION44chain 'G' and (resid 308 through 342 )G308 - 342
45X-RAY DIFFRACTION45chain 'G' and (resid 343 through 370 )G343 - 370
46X-RAY DIFFRACTION46chain 'G' and (resid 371 through 402 )G371 - 402
47X-RAY DIFFRACTION47chain 'G' and (resid 403 through 474 )G403 - 474
48X-RAY DIFFRACTION48chain 'H' and (resid 4 through 49 )H4 - 49
49X-RAY DIFFRACTION49chain 'H' and (resid 50 through 84 )H50 - 84
50X-RAY DIFFRACTION50chain 'H' and (resid 85 through 141 )H85 - 141
51X-RAY DIFFRACTION51chain 'H' and (resid 142 through 260 )H142 - 260
52X-RAY DIFFRACTION52chain 'H' and (resid 261 through 307 )H261 - 307
53X-RAY DIFFRACTION53chain 'H' and (resid 308 through 368 )H308 - 368
54X-RAY DIFFRACTION54chain 'H' and (resid 369 through 474 )H369 - 474

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