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Open data
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Basic information
Entry | Database: PDB / ID: 2cvr | |||||||||
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Title | NMR solution structure of sso7d mutant, K12L, 12 conformers | |||||||||
![]() | DNA-binding protein 7a | |||||||||
![]() | DNA BINDING PROTEIN / DNA-binding protein / thermostable protein / Sulfolobus solfataricus / single point mutation | |||||||||
Function / homology | ![]() Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / DNA binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Model type details | minimized average | |||||||||
![]() | Arosio, I. / Recca, T. / Consonni, R. / Alberti, E. / Fusi, P. / Zetta, L. | |||||||||
![]() | ![]() Title: Structural Determinants Responsible for the Thermostability of Sso7d and its Single Point Mutants Authors: Arosio, I. / Recca, T. / Consonni, R. / Alberti, E. / Fusi, P. / Zetta, L. #1: ![]() Title: A single-point mutation in the extreme heat- and pressure-resistant sso7d protein from sulfolobus solfataricus leads to a major rearrangement of the hydrophobic core Authors: Consonni, R. / Santomo, L. / Fusi, P. / Tortora, P. / Zetta, L. #2: Journal: Biochemistry / Year: 2003 Title: Investigations of Sso7d catalytic residues by NMR titration shifts and electrostatic calculations Authors: Consonni, R. / Arosio, I. / Belloni, B. / Fogolari, F. / Fusi, P. / Shehi, E. / Zetta, L. | |||||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | |||||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 242.7 KB | Display | ![]() |
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PDB format | ![]() | 200.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 348.8 KB | Display | ![]() |
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Full document | ![]() | 414.4 KB | Display | |
Data in XML | ![]() | 13.7 KB | Display | |
Data in CIF | ![]() | 21.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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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: 7018.202 Da / Num. of mol.: 1 / Mutation: K12L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P61991, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters |
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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 conditions | pH: 4.5 / Pressure: AMBIENT / Temperature: 300 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 683 restraints, 660 are noe-derived distance constraints, 7 dihedral angle restraints, 16 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 12 |