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Open data
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Basic information
Entry | Database: PDB / ID: 1qou | ||||||
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Title | CEN (Centroradialis) protein from Antirrhinum | ||||||
![]() | CEN | ||||||
![]() | PLANT PROTEIN / INFLUORESCENCE DETERMINATION IN FLOWERING PLANT MERISTEM / SIGNALLING / MEMBER OF THE PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FAMILY | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Banfield, M.J. / Brady, R.L. | ||||||
![]() | ![]() Title: The Structure of Antirrhinum Centroradialis Protein (Cen) Suggests a Role as a Kinase Regulator Authors: Banfield, M.J. / Brady, R.L. #1: ![]() Title: Function from Structure? the Crystal Structure of Human Phosphatidylethanolamine Binding Protein Suggests a Role in Membrane Signal Transduction Authors: Banfield, M.J. / Barker, J.J. / Perry, A. / Brady, R.L. #2: ![]() Title: Crystal Structure of Bovine Phosphatidylethanolamine-Binding Proteins from Bovine Brain: A Novel Structural Class of Phospholipid-Binding Proteins. Authors: Serre, L. / Vallee, B. / Bureaud, N. / Schoentgen, F. / Zelwer, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 81.4 KB | Display | ![]() |
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PDB format | ![]() | 59.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1bd9S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.997832, 0.065499, 0.006386), Vector: Details | IN THE CRYSTAL THE PROTEIN FORMS A HOMO- DIMER THROUGHAN INTER-CHAIN DISULPHIDE BOND. THIS OLIGOMERIC STATEIS NOT EXPECTED TO REPRESENT THE FUNCTIONAL STATE.HOWEVER, A ROLE FOR THIS DIMERIC ASSOCIATION IN PROTEINFUNCTION CANNOT BE RULED OUT . | |
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Components
#1: Protein | Mass: 20350.279 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: INTER-MOLECULAR DISULPHIDE BOND FORMED IN THE CRYSTAL, BETWEEN RESIDUES A145 AND B145. Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | AMINO ACID NUMBERING: FOR EASE OF COMPARISON, THE NUMBERING SCHEME ADOPTED FOR THIS ENTRY IS BASED ...AMINO ACID NUMBERING: FOR EASE OF COMPARISON | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 39.3 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: 1:1 MIX OF 13MG/ML CEN SOLUTION (10MM HEPES, 50MM NACL. PH 7) WITH 1.8 - 2.1 M NACL BUFFERED WITH 100MM SODIUM ACETATE AT PH 5.4 - 5.6 | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 15, 1999 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 28860 / % possible obs: 94.9 % / Redundancy: 4.2 % / Biso Wilson estimate: 19.29 Å2 / Rmerge(I) obs: 0.057 / Net I/σ(I): 22.4 |
Reflection shell | Resolution: 1.9→1.99 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.226 / Mean I/σ(I) obs: 4.6 / % possible all: 91.4 |
Reflection shell | *PLUS % possible obs: 91.4 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: 1BD9 Resolution: 1.9→40 Å / SU B: 3.65 / SU ML: 0.11 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.17 / ESU R Free: 0.16 Details: THE REFINED MODEL OF THE A-CHAIN CONTAINS THE FOLLOWING RESIDUES OF THE SEQUENCE LISTED REFINED MODEL OF THE B-CHAIN CONTAINS THE FOLLOWING RESIDUES B32B- B130, B143-B175.
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Displacement parameters | Biso mean: 27.44 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→40 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.212 / Rfactor Rfree: 0.25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.303 / Rfactor obs: 0.259 |