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Yorodumi- PDB-1fcl: DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fcl | ||||||
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Title | DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G | ||||||
Components | IMMUNOGLOBULIN G BINDING PROTEIN G | ||||||
Keywords | PROTEIN BINDING / Designed Core Mutant / Streptococcal Protein G | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptococcus sp. (bacteria) | ||||||
Method | SOLUTION NMR / Standard Distance Geometry, simulated Annealing Methods | ||||||
Authors | Ross, S.A. / Sarisky, C.A. / Su, A. / Mayo, S.L. | ||||||
Citation | Journal: Protein Sci. / Year: 2001 Title: Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification. Authors: Ross, S.A. / Sarisky, C.A. / Su, A. / Mayo, S.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fcl.cif.gz | 658.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fcl.ent.gz | 554.7 KB | Display | PDB format |
PDBx/mmJSON format | 1fcl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fcl_validation.pdf.gz | 341.1 KB | Display | wwPDB validaton report |
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Full document | 1fcl_full_validation.pdf.gz | 582.3 KB | Display | |
Data in XML | 1fcl_validation.xml.gz | 37.1 KB | Display | |
Data in CIF | 1fcl_validation.cif.gz | 61.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fc/1fcl ftp://data.pdbj.org/pub/pdb/validation_reports/fc/1fcl | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Antibody | Mass: 6216.819 Da / Num. of mol.: 1 / Fragment: GB1_DELTA1.5 / Mutation: Y3F, L7I, F30L, A34I, V39I, F52W Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus sp. (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P19909 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: none |
-Sample preparation
Details | Contents: 1 mM unlabeled protein in 50 mM sodium phosphate, pH 6.0 Solvent system: either D2O or 90:10 H2O:D2O |
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Sample conditions | Ionic strength: 50 mM sodium phosphate / pH: 6 / Pressure: Atmospheric atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: Standard Distance Geometry, simulated Annealing Methods Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Structures with the Least Restraint Violations, Structures with the Lowest Energy Conformers calculated total number: 100 / Conformers submitted total number: 40 |