[English] 日本語
Yorodumi- PDB-1fa4: ELUCIDATION OF THE PARAMAGNETIC RELAXATION OF HETERONUCLEI AND PR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fa4 | ||||||
---|---|---|---|---|---|---|---|
Title | ELUCIDATION OF THE PARAMAGNETIC RELAXATION OF HETERONUCLEI AND PROTONS IN CU(II) PLASTOCYANIN FROM ANABAENA VARIABILIS | ||||||
Components | PLASTOCYANIN | ||||||
Keywords | ELECTRON TRANSPORT / PLASTOCYANIN / ANABAENA VARIABILIS | ||||||
Function / homology | Function and homology information thylakoid membrane / plasma membrane-derived thylakoid membrane / electron transfer activity / copper ion binding Similarity search - Function | ||||||
Biological species | Anabaena variabilis (bacteria) | ||||||
Method | SOLUTION NMR / Distance geometry, simulated annealing, restrained energy minimization | ||||||
Authors | Ma, L. / Jorgensen, A.M. / Sorensen, G.O. / Ulstrup, J. / Led, J.J. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2000 Title: Elucidation of the Paramagnetic R1 Relaxation of Heteronuclei and Protons in Cu(II) Plastocyanin from Anabaena Variabilis Authors: Ma, L. / Jorgensen, A.M. / Soerensen, G.O. / Ulstrup, J. / Led, J.J. #1: Journal: Biochemistry / Year: 1996 Title: Solution Structure of Reduced Plastocyanin from the Blue-Green Alga Anabaena variabilis Authors: Badsberg, U. / Jorgensen, A.M. / Gesmar, H. / Led, J.J. / Hammerstad, J.M. / Jespersen, L.L. / Ulstrup, J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1fa4.cif.gz | 613.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1fa4.ent.gz | 507.7 KB | Display | PDB format |
PDBx/mmJSON format | 1fa4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fa4_validation.pdf.gz | 349.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1fa4_full_validation.pdf.gz | 549.8 KB | Display | |
Data in XML | 1fa4_validation.xml.gz | 63.6 KB | Display | |
Data in CIF | 1fa4_validation.cif.gz | 82.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fa/1fa4 ftp://data.pdbj.org/pub/pdb/validation_reports/fa/1fa4 | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 11116.643 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Anabaena variabilis (bacteria) / References: UniProt: P00301, UniProt: Q3M9H8*PLUS |
---|---|
#2: Chemical | ChemComp-CU / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: INPUT DATA FOR STRUCTURE CALCULATION: 595 INTRARESIDUAL RESTRAINTS, 279 SEQUENTIAL RESTRAINTS, 585 INTERRESIDUAL RESTRAINTS, 49 DIHEDRAL (PHI) RESTRAINTS, 29 DIHEDRAL (CHI) RESTRAINTS, 9 ...Text: INPUT DATA FOR STRUCTURE CALCULATION: 595 INTRARESIDUAL RESTRAINTS, 279 SEQUENTIAL RESTRAINTS, 585 INTERRESIDUAL RESTRAINTS, 49 DIHEDRAL (PHI) RESTRAINTS, 29 DIHEDRAL (CHI) RESTRAINTS, 9 DIHEDRAL (OMIGA_PROLIN) RESTRAINTS, 0 HYDROGEN BOND RESTRAINTS, 4 COPPER RESTRAINTS. THE RMS DEVIATION FROM IDEALIZED GEOMETRY: BONDS:0.0031 ANGSTROMS, ANGLES:1.06 ANGSTROMS, IMPROPERS:0.42 ANGSTROMS. |
-Sample preparation
Details |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions |
| |||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: Distance geometry, simulated annealing, restrained energy minimization Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 20 |