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- EMDB-3352: Activation of NMDA receptors and the mechanism of inhibition by i... -

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Basic information

Entry
Database: EMDB / ID: 3352
TitleActivation of NMDA receptors and the mechanism of inhibition by ifenprodil - Active confirmation
KeywordsNMDA receptor / glutamate receptor / GluN1 / GluN2B / ion channel
SampleNMDA Receptor
SourceRattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /
Map dataActive Conformation - Unsharpened, unmasked map.
Methodsingle particle reconstruction, at 6.8 Å resolution
AuthorsTajima N / Karakas E / Grant T / Simorowski N / Diaz-Avalos R / Grigorieff N / Furukawa H
CitationNature, 2016, 534, 63-68

Nature, 2016, 534, 63-68 Yorodumi Papers
Activation of NMDA receptors and the mechanism of inhibition by ifenprodil.
Nami Tajima / Erkan Karakas / Timothy Grant / Noriko Simorowski / Ruben Diaz-Avalos / Nikolaus Grigorieff / Hiro Furukawa

Validation ReportPDB-ID: 5fxg

SummaryFull reportAbout validation report
DateDeposition: Mar 1, 2016 / Header (metadata) release: Apr 6, 2016 / Map release: May 11, 2016 / Last update: Jun 15, 2016

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.035
  • Imaged by UCSF CHIMERA
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  • Surface view colored by height
  • Surface level: 0.035
  • Imaged by UCSF CHIMERA
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  • Surface view with fitted model
  • Atomic models: : PDB-5fxg
  • Surface level: 0.035
  • Imaged by UCSF CHIMERA
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Supplemental images

Downloads & links

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Map

Fileemd_3352.map.gz (map file in CCP4 format, 65537 KB)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
256 pix
1.31 Å/pix.
= 335.36 Å
256 pix
1.31 Å/pix.
= 335.36 Å
256 pix
1.31 Å/pix.
= 335.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider package.

Voxel sizeX=Y=Z: 1.31 Å
Density
Contour Level:0.025 (by author), 0.035 (movie #1):
Minimum - Maximum-0.02085609 - 0.0761986
Average (Standard dev.)-0.00057818 (0.00617342)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions256256256
Origin000
Limit255255255
Spacing256256256
CellA=B=C: 335.36 Å
α=β=γ: 90 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.311.311.31
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z335.360335.360335.360
α/β/γ90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.0210.076-0.001

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Supplemental data

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Sample components

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Entire NMDA Receptor

EntireName: NMDA Receptor
Details: The sample was purified in the presence of agonists Glycine and L-glutamate.
Number of components: 2
Oligomeric State: One heterotetramer of 2 GluN1 and 2 GluN2B subunits
MassTheoretical: 370 kDa

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Component #1: protein, N-methyl-D-aspartate receptor GluN1

ProteinName: N-methyl-D-aspartate receptor GluN1 / a.k.a: GluN1, NR1 / Oligomeric Details: dimer / Number of Copies: 2 / Recombinant expression: Yes
MassTheoretical: 93 kDa
SourceSpecies: Rattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /
Source (engineered)Expression System: Spodoptera frugiperda / arthropod / Vector: Modified pFL and pUCDM / Cell of expression system: Sf9 / Strain: Sf9 CRL-1711
Source (natural)Location in cell: Plasma membane
External referencesUniProt: UniProt: P35439

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Component #2: protein, N-methyl-D-aspartate receptor GluN2B

ProteinName: N-methyl-D-aspartate receptor GluN2B / a.k.a: GluN2B, NR2B / Oligomeric Details: Dimer / Recombinant expression: Yes / Number of Copies: 2
MassTheoretical: 92 kDa
SourceSpecies: Rattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /
Source (engineered)Expression System: Spodoptera frugiperda / arthropod / Vector: Modified pFL and pUCDM / Cell of expression system: Sf9 / Strain: Sf9 CRL-1711
Source (natural)Location in cell: Plasma membane
External referencesUniProt: UniProt: Q00960

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Experimental details

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Sample preparation

Specimen stateparticle
Sample solutionSpecimen conc.: 2 mg/ml
Buffer solution: 200 mM NaCl, 20 mM HEPES pH 7.0, 10 mM Glycine, 10 mM L-Glutamate, 0.002% MNG-3
pH: 7
Support filmC-flat 1.2/1.3 Cu 400
VitrificationInstrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 90 % / Method: 3s Blot time

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS / Date: Aug 10, 2015
Details: 21s exposure into 70 frames, with an exposure rate of ~8 electrons/pixel/s on the camera.
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 100 e/Å2 / Electron beam tilt params: 0 / Illumination mode: FLOOD BEAM
LensMagnification: 22500 X (nominal), 38168 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1000 - 2500 nm
Specimen HolderModel: FEI TITAN KRIOS AUTOGRID HOLDER
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

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Image acquisition

Image acquisitionNumber of digital images: 1200

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Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 12000
3D reconstructionAlgorithm: FREALIGN / Software: Unblur, CTFFIND4, FREALIGN / CTF correction: Each Particle
Details: The highest resolution included in the refinement was 12A.
Resolution: 6.8 Å / Resolution method: FSC 0.143, semi-independent

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Atomic model buiding

Modeling #1Software: Coot / Refinement protocol: flexible / Target criteria: Real Space / Refinement space: REAL
Details: The individual domains were initially fitted using coot and real space refinement was performed using Phenix
Input PDB model: 4PE5
Chain ID: A, B, C, D
Output model

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