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Open data
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Basic information
| Entry | Database: PDB / ID: 2jv2 | |||||||||
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| Title | Solution Structure of the N-terminal Domain of PH1500 | |||||||||
Components | Putative uncharacterized protein PH1500 | |||||||||
Keywords | UNKNOWN FUNCTION / AAA ATPASE NC-DOMAIN-LIKE | |||||||||
| Function / homology | Function and homology information: / Domain of unknown function (DUF6849) / Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Roll / Alpha Beta Similarity search - Domain/homology | |||||||||
| Biological species | ![]() Pyrococcus horikoshii (archaea) | |||||||||
| Method | SOLUTION NMR / simulated annealing | |||||||||
| Model type details | minimized average | |||||||||
Authors | Varnay, I. / Truffault, V. / Coles, M. | |||||||||
Citation | Journal: To be PublishedTitle: The Solution Structure of Ph1500-N Authors: Varnay, I. / Djuranovic, S. / Truffault, V. / Lupas, A. / Kessler, H. / Coles, M. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2jv2.cif.gz | 536 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2jv2.ent.gz | 452.5 KB | Display | PDB format |
| PDBx/mmJSON format | 2jv2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2jv2_validation.pdf.gz | 345.6 KB | Display | wwPDB validaton report |
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| Full document | 2jv2_full_validation.pdf.gz | 477.3 KB | Display | |
| Data in XML | 2jv2_validation.xml.gz | 23.5 KB | Display | |
| Data in CIF | 2jv2_validation.cif.gz | 40.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jv/2jv2 ftp://data.pdbj.org/pub/pdb/validation_reports/jv/2jv2 | HTTPS FTP |
-Related structure data
| Similar structure data | |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 9449.224 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: cis-P66, cis-P68 / Source: (gene. exp.) ![]() Pyrococcus horikoshii (archaea) / Gene: PH1500 / Production host: ![]() |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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| NMR experiment |
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Sample preparation
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| Sample conditions | Ionic strength: 50 / pH: 7 / Pressure: AMBIENT / Temperature: 300 K |
-NMR measurement
| NMR spectrometer |
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Processing
| NMR software |
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| Refinement | Method: simulated annealing / Software ordinal: 1 Details: Protocol including conformational database potential, BASED ON 748 DISTANCE RESTRAINTS, TALOS RESTRAINTS FOR 55 RESIDUES, 47 SIDECHAIN CHI1 AND 11 SIDECHAIN CHI2 DIHEDRAL RESTRAINTS, 34 ...Details: Protocol including conformational database potential, BASED ON 748 DISTANCE RESTRAINTS, TALOS RESTRAINTS FOR 55 RESIDUES, 47 SIDECHAIN CHI1 AND 11 SIDECHAIN CHI2 DIHEDRAL RESTRAINTS, 34 HBOND RESTRAINTS AND 51 PHI AND 16 PSI J-COUPLING RESTRAINTS. | ||||||||||||||||||||||||
| NMR constraints | NOE constraints total: 786 / NOE intraresidue total count: 194 / NOE long range total count: 193 / NOE medium range total count: 96 / NOE sequential total count: 269 / Protein chi angle constraints total count: 51 / Protein other angle constraints total count: 19 / Protein phi angle constraints total count: 58 / Protein psi angle constraints total count: 58 | ||||||||||||||||||||||||
| NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
| NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 22 |
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Pyrococcus horikoshii (archaea)
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