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Open data
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Basic information
Entry | Database: PDB / ID: 1c54 | ||||||
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Title | SOLUTION STRUCTURE OF RIBONUCLEASE SA | ||||||
![]() | RIBONUCLEASE SA | ||||||
![]() | HYDROLASE / ALPHA+BETA PROTEIN | ||||||
Function / homology | ![]() ribonuclease T1 activity / ribonuclease T1 / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Laurents, D.V. / Canadillas-Perez, J.M. / Santoro, J. / Schell, D. / Pace, C.N. / Rico, M. / Bruix, M. | ||||||
![]() | ![]() Title: Solution structure and dynamics of ribonuclease Sa. Authors: Laurents, D. / Perez-Canadillas, J.M. / Santoro, J. / Rico, M. / Schell, D. / Pace, C.N. / Bruix, M. #1: ![]() Title: Sequential Assignment and Solution Secondary Structure of Doubly Labelled Ribonuclease Sa Authors: Laurents, D.V. / Canadillas-Perez, J.M. / Santoro, J. / Schell, D. / Pace, C.N. / Rico, M. / Bruix, M. #2: ![]() Title: Ribonucelase from Streptomyces Aureofaciens at Atomic Resolution Authors: Sevcik, J. / Dauter, Z. / Lamzin, V.S. / Wilson, K.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 327.5 KB | Display | ![]() |
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PDB format | ![]() | 263.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 358.9 KB | Display | ![]() |
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Full document | ![]() | 502.7 KB | Display | |
Data in XML | ![]() | 34.2 KB | Display | |
Data in CIF | ![]() | 57.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 10582.492 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED WITH A 80MS MIXING TIME, AND STANDARD 2D HOMONUCLEAR TECHNIQUES. |
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Sample preparation
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 1924 UPPER DISTANCE RESTRAINTS, DERIVED FROM 2276 UNAMBIGUOUS NOES, AND 3 LOWER DISTANCE RESTRAINTS BASED ON THE PROTEINS C7-C96 DISULFIDE BOND. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY AND REPRESENTATIVE OF DIFFERENT CONFORMERS Conformers calculated total number: 40 / Conformers submitted total number: 20 |