+Open data
-Basic information
Entry | Database: PDB / ID: 2kqk | ||||||
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Title | Solution structure of apo-IscU(D39A) | ||||||
Components | NifU-like protein | ||||||
Keywords | METAL BINDING PROTEIN / IscU / iron-sulfur cluster / scaffold protein / isc system | ||||||
Function / homology | Function and homology information IscS-IscU complex / L-cysteine catabolic process / iron-sulfur cluster assembly / ferrous iron binding / 2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / intracellular iron ion homeostasis / copper ion binding / zinc ion binding / identical protein binding ...IscS-IscU complex / L-cysteine catabolic process / iron-sulfur cluster assembly / ferrous iron binding / 2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / intracellular iron ion homeostasis / copper ion binding / zinc ion binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing, torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Kim, J.H. / Fuzery, A.K. / Tonelli, M. / Vickery, L.E. / Markley, J.L. | ||||||
Citation | Journal: Biochemistry / Year: 2012 Title: Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli. Authors: Kim, J.H. / Tonelli, M. / Kim, T. / Markley, J.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kqk.cif.gz | 747.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kqk.ent.gz | 632.7 KB | Display | PDB format |
PDBx/mmJSON format | 2kqk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kq/2kqk ftp://data.pdbj.org/pub/pdb/validation_reports/kq/2kqk | HTTPS FTP |
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-Related structure data
Related structure data | 2l4xC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13821.562 Da / Num. of mol.: 1 / Mutation: D39A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: b2529, icsU, iscu, JW2513, nifU, yfhN / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P0ACD4 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 8.0 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing, torsion angle dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2102 / NOE intraresidue total count: 305 / NOE long range total count: 713 / NOE medium range total count: 525 / NOE sequential total count: 559 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 77 / Protein psi angle constraints total count: 77 | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 200 / Conformers submitted total number: 20 |