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Yorodumi- PDB-1lc2: Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Ace... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lc2 | ||||||
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Title | Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures | ||||||
Components | CYTOCHROME C | ||||||
Keywords | ELECTRON TRANSPORT / CYTOCHROME C / ORGANIC SOLVENT | ||||||
Function / homology | Function and homology information cytochrome c-heme linkage / cytochrome complex / positive regulation of cysteine-type endopeptidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / : / mitochondrial intermembrane space / electron transfer activity / positive regulation of apoptotic process ...cytochrome c-heme linkage / cytochrome complex / positive regulation of cysteine-type endopeptidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / : / mitochondrial intermembrane space / electron transfer activity / positive regulation of apoptotic process / lipid binding / apoptotic process / heme binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Equus caballus (horse) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, TORSION ANGLE DYNAMICS, RESTRAINED ENERGY MINIMIZATION | ||||||
Authors | Sivakolundu, S.G. / Mabrouk, P.A. | ||||||
Citation | Journal: J.BIOL.INORG.CHEM. / Year: 2003 Title: Structure function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution Authors: Sivakolundu, S.G. / Mabrouk, P.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lc2.cif.gz | 1019.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lc2.ent.gz | 876 KB | Display | PDB format |
PDBx/mmJSON format | 1lc2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lc2_validation.pdf.gz | 465.2 KB | Display | wwPDB validaton report |
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Full document | 1lc2_full_validation.pdf.gz | 628.8 KB | Display | |
Data in XML | 1lc2_validation.xml.gz | 48.5 KB | Display | |
Data in CIF | 1lc2_validation.cif.gz | 81.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lc/1lc2 ftp://data.pdbj.org/pub/pdb/validation_reports/lc/1lc2 | 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: 11725.598 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Equus caballus (horse) / Organ: heart / References: UniProt: P00004 |
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#2: Chemical | ChemComp-HEC / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques |
-Sample preparation
Details | Contents: 5mM FERROCYTOCHROME C 1H; 50mM PHOSPHATE BUFFER; 70% H2O, 30% CD3CN Solvent system: 70% H2O, 30% CD3CN |
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Sample conditions | Ionic strength: 50mM / pH: 7.2 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Home-built HOME BUILT / Manufacturer: Home-built / Model: HOME BUILT / Field strength: 591.1 MHz |
-Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING, TORSION ANGLE DYNAMICS, RESTRAINED ENERGY MINIMIZATION Software ordinal: 1 Details: The structures are based on a total of 2232 NOE-based distance restraints and 73 dihedral angle restraints | ||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 30 / Conformers submitted total number: 30 |