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Yorodumi- PDB-2kjz: Solution NMR structure of protein ATC0852 from Agrobacterium tume... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kjz | ||||||
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Title | Solution NMR structure of protein ATC0852 from Agrobacterium tumefaciens. Northeast Structural Genomics Consortium (NESG) target AtT2. | ||||||
Components | ATC0852 | ||||||
Keywords | UNKNOWN FUNCTION / protein of unknown function / dimer / Structural Genomics / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | Function and homology information Signal recognition particle alu RNA binding heterodimer, srp9/1 - #120 / Glyoxalase/dioxygenase/EhpR / Signal recognition particle alu RNA binding heterodimer, srp9/1 - #110 / Signal recognition particle alu RNA binding heterodimer, srp9/1 / Glyoxalase/fosfomycin resistance/dioxygenase domain / Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily / Vicinal oxygen chelate (VOC) domain / Vicinal oxygen chelate (VOC) domain profile. / Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | Agrobacterium tumefaciens (bacteria) | ||||||
Method | SOLUTION NMR / restrained molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Lemak, A. / Yee, A. / Gutmanas, A. / Fares, C. / Garcia, M. / Montelione, G. / Arrowsmith, C. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: To be Published Title: Solution structure of protein ATC0852 from Agrobacterium tumefaciens Authors: Lemak, A. / Yee, A. / Gutmanas, A. / Fares, C. / Garcia, M. / Montelione, G. / Arrowsmith, C. #1: Journal: J.Biomol.Nmr / Year: 2011 Title: A novel strategy for NMR resonance assignment and protein structure determination. Authors: Lemak, A. / Gutmanas, A. / Chitayat, S. / Karra, M. / Fares, C. / Sunnerhagen, M. / Arrowsmith, C.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kjz.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2kjz.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 2kjz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kjz_validation.pdf.gz | 424.1 KB | Display | wwPDB validaton report |
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Full document | 2kjz_full_validation.pdf.gz | 634.2 KB | Display | |
Data in XML | 2kjz_validation.xml.gz | 75.3 KB | Display | |
Data in CIF | 2kjz_validation.cif.gz | 119.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kj/2kjz ftp://data.pdbj.org/pub/pdb/validation_reports/kj/2kjz | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15828.633 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Agrobacterium tumefaciens (bacteria) / Strain: C58 / Gene: AGR_C_1587, Atu0869 / Plasmid: p15Tv lic / Production host: Escherichia coli (E. coli) / Strain (production host): C58 / References: UniProt: A9CJT2 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM [U-13C; U-15N] atc0852-1, 10 mM TRIS-2, 300 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-7, 10 % D2O-8, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 300 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: restrained molecular dynamics / Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |