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- PDB-1nsf: D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF) -

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Basic information

Entry
Database: PDB / ID: 1nsf
TitleD2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)
ComponentsN-ETHYLMALEIMIDE SENSITIVE FACTOR
KeywordsPROTEIN TRANSPORT / ENDOPLASMIC RETICULUM / GOLGI STACK / ATP-BINDING
Function / homology
Function and homology information


SNARE complex disassembly / vesicle-fusing ATPase / positive regulation of receptor recycling / syntaxin-1 binding / ionotropic glutamate receptor binding / SNARE binding / potassium ion transport / ATPase activity, coupled / PDZ domain binding / positive regulation of protein catabolic process ...SNARE complex disassembly / vesicle-fusing ATPase / positive regulation of receptor recycling / syntaxin-1 binding / ionotropic glutamate receptor binding / SNARE binding / potassium ion transport / ATPase activity, coupled / PDZ domain binding / positive regulation of protein catabolic process / intracellular protein transport / midbody / ATPase activity / protein-containing complex binding / protein kinase binding / ATP binding / identical protein binding / plasma membrane / metal ion binding / cytosol
CDC48, N-terminal subdomain / ATPase family associated with various cellular activities (AAA) / AAA ATPase, AAA+ lid domain / Vesicle-fusing ATPase / CDC48 domain 2-like superfamily / P-loop containing nucleoside triphosphate hydrolase / Aspartate decarboxylase-like domain superfamily / CDC48, domain 2 / ATPase, AAA-type, conserved site / ATPase, AAA-type, core ...CDC48, N-terminal subdomain / ATPase family associated with various cellular activities (AAA) / AAA ATPase, AAA+ lid domain / Vesicle-fusing ATPase / CDC48 domain 2-like superfamily / P-loop containing nucleoside triphosphate hydrolase / Aspartate decarboxylase-like domain superfamily / CDC48, domain 2 / ATPase, AAA-type, conserved site / ATPase, AAA-type, core / AAA+ ATPase domain / Helicase, Ruva Protein; domain 3 - #60 / Helicase, Ruva Protein; domain 3 / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Vesicle-fusing ATPase
Biological speciesCricetulus griseus (Chinese hamster)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.9 Å
AuthorsYu, R.C. / Hanson, P.I. / Jahn, R. / Brunger, A.T.
Citation
Journal: Nat.Struct.Biol. / Year: 1998
Title: Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.
Authors: Yu, R.C. / Hanson, P.I. / Jahn, R. / Brunger, A.T.
#1: Journal: J.Biol.Chem. / Year: 1993
Title: Domain Structure of an N-Ethylmaleimide-Sensitive Fusion Protein Involved in Vesicular Transport
Authors: Tagaya, M. / Wilson, D.W. / Brunner, M. / Arango, N. / Rothman, J.E.
Validation Report
SummaryFull reportAbout validation report
History
DepositionJun 26, 1998Processing site: BNL
Revision 1.0Nov 25, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: N-ETHYLMALEIMIDE SENSITIVE FACTOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,0183
Polymers30,4861
Non-polymers5312
Water2,198122
1
A: N-ETHYLMALEIMIDE SENSITIVE FACTOR
hetero molecules
x 6


Theoretical massNumber of molelcules
Total (without water)186,10818
Polymers182,9196
Non-polymers3,18912
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
crystal symmetry operation4_555-x,-y,z1
crystal symmetry operation5_555y,-x+y,z1
crystal symmetry operation6_555x-y,x,z1
Buried area22840 Å2
ΔGint-157 kcal/mol
Surface area60170 Å2
MethodPISA, PQS
Unit cell
γ
α
β
Length a, b, c (Å)115.996, 115.996, 44.130
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number168
Space group name H-MP6

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Components

#1: Protein N-ETHYLMALEIMIDE SENSITIVE FACTOR / VESICULAR-FUSION PROTEIN NSF


Mass: 30486.451 Da / Num. of mol.: 1 / Fragment: D2 HEXAMERIZATION DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Cricetulus griseus (Chinese hamster) / Cell line: CHO / Plasmid: PET28B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P18708
#2: Chemical ChemComp-MG / MAGNESIUM ION / Magnesium


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 122 / 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: 3

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Sample preparation

CrystalDensity Matthews: 2.81 Å3/Da / Density % sol: 56.23 %
Crystal growpH: 6.05 / Details: pH 6.05
Crystal grow
*PLUS
Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, hanging drop
Details: drop contains equal volume of protein and reservoir solutions
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
115 mg/mlprotein1drop
220 mMHEPES1drop
3100 mM1dropNaCl
420 mMADP1drop
55 mM1dropMgCl2
62 %glycerol1drop
720 mMdithiothreitol1drop
8100 mMMES1reservoir
90.5 %PEG60001reservoir

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Data collection

DiffractionMean temperature: 80 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL1-5 / Wavelength: 1
DetectorType: ADSC QUANTUM / Detector: CCD / Date: Mar 1, 1998 / Details: BENT MIRROR
RadiationMonochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→500 Å / Num. obs: 50548 / % possible obs: 96.5 % / Observed criterion σ(I): 3 / Redundancy: 6.7 % / Biso Wilson estimate: 20.7 Å2 / Rmerge(I) obs: 0.053 / Rsym value: 0.053 / Net I/σ(I): 33.3
Reflection shellResolution: 1.9→1.97 Å / Redundancy: 5 % / Rmerge(I) obs: 0.334 / Mean I/σ(I) obs: 4.8 / Rsym value: 0.334 / % possible all: 97.5

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Processing

Software
NameVersionClassification
CNS0.4refinement
DENZOdata reduction
SCALEPACKdata scaling
CNS0.4phasing
RefinementMethod to determine structure: MAD / Resolution: 1.9→500 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 1105949.83 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflectionSelection details
Rfree0.244 4947 9.8 %RANDOM
Rwork0.224 ---
Obs0.224 50548 96.4 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 70.69 Å2 / ksol: 0.374 e/Å3
Displacement parametersBiso mean: 35.5 Å2
Baniso -1Baniso -2Baniso -3
1--8.49 Å2-3.54 Å20 Å2
2---8.49 Å20 Å2
3---16.99 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.27 Å0.24 Å
Luzzati d res low-5 Å
Luzzati sigma a0.26 Å0.21 Å
Refinement stepCycle: LAST / Resolution: 1.9→500 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1942 0 32 122 2096
Refine LS restraints
Refinement-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.2
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d20.7
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.76
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.681.5
X-RAY DIFFRACTIONc_mcangle_it2.392
X-RAY DIFFRACTIONc_scbond_it2.972
X-RAY DIFFRACTIONc_scangle_it4.192.5
LS refinement shellResolution: 1.9→1.97 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.335 451 9.8 %
Rwork0.287 4169 -
Obs--88.1 %
Xplor file
Refinement-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2ATP.PARATP.TOP
X-RAY DIFFRACTION3WATER_REP.PARAMTOPMG.PRO
X-RAY DIFFRACTION4PAR_MG.PRO
Software
*PLUS
Name: CNS / Version: 0.4 / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.26
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg20.7
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.77
LS refinement shell
*PLUS
Rfactor Rfree: 0.333 / Rfactor obs: 0.288

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