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Yorodumi- PDB-2odg: Complex of barrier-to-autointegration factor and LEM-domain of emerin -
+Open data
-Basic information
Entry | Database: PDB / ID: 2odg | ||||||
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Title | Complex of barrier-to-autointegration factor and LEM-domain of emerin | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / PROTEIN BINDING / INNER NUCLEAR MEMBRANE PROTEIN / LEM-DOMAIN BAF MULTIDIMENSIONAL NMR DIPOLAR COUPLINGS | ||||||
Function / homology | Function and homology information TMEM240-body / nuclear membrane organization / negative regulation of protein ADP-ribosylation / Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / mitotic nuclear membrane reassembly / Initiation of Nuclear Envelope (NE) Reformation / RHOD GTPase cycle / nuclear outer membrane / regulation of canonical Wnt signaling pathway ...TMEM240-body / nuclear membrane organization / negative regulation of protein ADP-ribosylation / Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / mitotic nuclear membrane reassembly / Initiation of Nuclear Envelope (NE) Reformation / RHOD GTPase cycle / nuclear outer membrane / regulation of canonical Wnt signaling pathway / nuclear inner membrane / muscle organ development / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / negative regulation of type I interferon production / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of viral genome replication / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation / beta-tubulin binding / Vpr-mediated nuclear import of PICs / skeletal muscle cell differentiation / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / RHOG GTPase cycle / chromosome organization / RAC2 GTPase cycle / RAC3 GTPase cycle / negative regulation of fibroblast proliferation / condensed chromosome / RAC1 GTPase cycle / negative regulation of innate immune response / positive regulation of protein export from nucleus / muscle contraction / response to virus / negative regulation of canonical Wnt signaling pathway / cellular response to growth factor stimulus / DNA integration / spindle / chromatin organization / nuclear envelope / actin binding / double-stranded DNA binding / nuclear membrane / microtubule / response to oxidative stress / cadherin binding / chromatin / endoplasmic reticulum / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / CONJOINED RIGID BODY, TORSION ANGLE SIMULATED ANNEALING DYNAMICS | ||||||
Authors | Clore, G.M. / Cai, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: Solution NMR Structure of the Barrier-to-Autointegration Factor-Emerin Complex. Authors: Cai, M. / Huang, Y. / Suh, J.Y. / Louis, J.M. / Ghirlando, R. / Craigie, R. / Clore, G.M. | ||||||
History |
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Remark 7 | IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL ... IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. IT IS IMPORTANT TO NOTE THAT THE VALUES GIVEN FOR THE BACKBONE ATOMS AND NON-INTERFACIAL SIDECHAINS PROVIDE ONLY A MEASURE OF THE PRECISION WITH WHICH THE RELATIVE ORIENTATION OF THE TWO PROTEINS HAVE BEEN DETERMINED AND DOES NOT TAKE INTO ACCOUNT THE ERRORS IN THE NMR COORDINATES OF THE FREE BAF DIMER AND THE LEM-DOMAIN OF EMERIN. STRUCTURAL STATISTICS: --------------------------------------------------------- RMS DEVIATIONS FROM EXPT RESTRAINTS NOES (122) 0.016 A SIDE-CHAIN TORSION ANGLES (46) 0.025 DEG 1DNH DIPOLAR COUPLING R-FACTORS (CLORE AND GARRETT (1999) J. AM. CHEM. SOC. 121, 9008-9012): BAF (54x2) 15.2% LEM-DOMAIN: 14.8% -------------------------------------------------------- COORDINATE PRECISION BACKBONE: 0.13(+/-0.06) A INTERFACIAL SIDE-CHAIN HEAVY ATOMS: 1.02(+/-0.02) A |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2odg.cif.gz | 84.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2odg.ent.gz | 66.5 KB | Display | PDB format |
PDBx/mmJSON format | 2odg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2odg_validation.pdf.gz | 251.3 KB | Display | wwPDB validaton report |
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Full document | 2odg_full_validation.pdf.gz | 251.1 KB | Display | |
Data in XML | 2odg_validation.xml.gz | 5.9 KB | Display | |
Data in CIF | 2odg_validation.cif.gz | 8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/od/2odg ftp://data.pdbj.org/pub/pdb/validation_reports/od/2odg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10073.588 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-89 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: NUCLEUS / Gene: BANF1, BAF, BCRG1 / Production host: Escherichia coli (E. coli) / References: UniProt: O75531 #2: Protein/peptide | | Mass: 5720.397 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-47 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: NUCLEUS / Gene: EMD, EDMD, STA / Production host: Escherichia coli (E. coli) / References: UniProt: P50402 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | Ionic strength: 50 mM POTASSIUM PHOSPHATE 200 mM NACL / pH: 6.50 / Temperature: 303.00 K |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: CONJOINED RIGID BODY, TORSION ANGLE SIMULATED ANNEALING DYNAMICS Software ordinal: 1 Details: THE STRUCTURES WERE CALCULATED BY CONJOINED RIGID BODY/TORSION ANGLE DYNAMICS (SCHWIETERS & CLORE (2001) J.MAGN.RESON 152, 288-302). THE TARGET FUNCTIONS COMPRISES TERMS FOR NOE RESTRAINTS, ...Details: THE STRUCTURES WERE CALCULATED BY CONJOINED RIGID BODY/TORSION ANGLE DYNAMICS (SCHWIETERS & CLORE (2001) J.MAGN.RESON 152, 288-302). THE TARGET FUNCTIONS COMPRISES TERMS FOR NOE RESTRAINTS, SIDECHAIN TORSION ANGLE RESTRAINTS, RESIDUAL DIPOLAR COUPLING RESTRAINTS (CLORE ET AL. J.MAGN.RESON. 131, 159-162 (1998); J.MAGN.RESON.133, 216-221(1998)), A RADIUS OF GYRATION TERM (KUSZEWSKI ET AL. J.AM.CHEM.SOC. 121, 2337-2338 (1999)), A QUARTIC VAN DER WAALS REPULSION TERM (NILGES ET AL. (1988) FEBS LETT. 229, 129-136), AND A TORSION ANGLE CONFORMATIONAL DATABASE POTENTIAL OF MEAN FORCE (CLORE AND KUSZEWSKI 2002) J.AM.CHEM.SOC 124, 2866-2867). THE STARTING COORDINATE COME FROM THE NMR STRUCTURE OF THE BAF DIMER (1QCK; KUSZEWSKI ET AL. J.AM.CHEM.SOC.121, 2337-2338(1999)) AND THE LEM-DOMAIN OF EMERIN (PDB ID 2ODC; CAI ET AL) THE BACKBONE COORDINATES AND NON-INTERFACIAL SIDECHAINS ARE TREATED AS RIGID BODIES THROUGHOUT WITH THE BAF DIMER HELD FIXED, THE MOLECULES ALLOWED TO ROTATE AND TRANSLATE, AND THE AXIS OF THE SINGLE DIPOLAR COUPLING ALIGNMENT TENSOR FREE TO ROTATE. THE INTERFACIAL SIDECHAINS ARE GIVEN FULL TORSIONAL DEGREES OF FREEDOM. | |||||||||
NMR representative | Selection criteria: restrained regularized mean coordinates | |||||||||
NMR ensemble | Conformer selection criteria: RESTRAINED REGULARIZED MEAN STRUCTURE Conformers calculated total number: 180 / Conformers submitted total number: 1 |