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Yorodumi- PDB-1e9s: Bacterial conjugative coupling protein TrwBdeltaN70. Unbound mono... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1e9s | ||||||
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Title | Bacterial conjugative coupling protein TrwBdeltaN70. Unbound monoclinic form. | ||||||
Components | CONJUGAL TRANSFER PROTEIN TRWB | ||||||
Keywords | COUPLING PROTEIN / BACTERIAL CONJUGATION / F1-ATPASE-LIKE QUATERNARY STRUCTURE / RING HELICASES | ||||||
Function / homology | Function and homology information nucleotide binding / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Gomis-Rueth, F.X. / Moncalian, G. / Cabezon, E. / de la Cruz, F. / Coll, M. | ||||||
Citation | Journal: Nature / Year: 2001 Title: The Bacterial Conjugation Protein Trwb Resembles Ring Helicases and F1-ATPase Authors: Gomis-Rueth, F.X. / Moncalian, G. / Perez-Luque, R. / Gonzalez, A. / Cabezon, E. / De La Cruz, F. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e9s.cif.gz | 979.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e9s.ent.gz | 819.9 KB | Display | PDB format |
PDBx/mmJSON format | 1e9s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e9s_validation.pdf.gz | 471.3 KB | Display | wwPDB validaton report |
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Full document | 1e9s_full_validation.pdf.gz | 624.9 KB | Display | |
Data in XML | 1e9s_validation.xml.gz | 111.7 KB | Display | |
Data in CIF | 1e9s_validation.cif.gz | 170.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e9/1e9s ftp://data.pdbj.org/pub/pdb/validation_reports/e9/1e9s | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given / Matrix: (1), |
-Components
#1: Protein | Mass: 48671.469 Da / Num. of mol.: 12 / Fragment: TRANSMEMBRANE-ANCHOR-EXCISED PROTEIN / Mutation: YES Source method: isolated from a genetically manipulated source Details: TWO HOMOHEXAMERS ARE PRESENT IN THE A.U. / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Gene: TRWB / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q04230 #2: Water | ChemComp-HOH / | Compound details | CHAIN A, B, D, E, F, G, H, I, J, K, L, M FIRST 70 RESIDUES DELETED | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.19 % | |||||||||||||||
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Crystal grow | pH: 7.5 / Details: 0.9 M POTASSIUM/SODIUM, 0.1 M HEPES PH 7.5 | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 1.053 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.053 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. obs: 728622 / % possible obs: 97 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 9.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: TRIGONAL CRYSTAL FORM Resolution: 2.5→50 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.5→50 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 40.8 Å2 |