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Yorodumi- PDB-2gb1: A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2gb1 | ||||||
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Title | A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G | ||||||
Components | PROTEIN G | ||||||
Keywords | IMMUNOGLOBULIN BINDING PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptococcus sp. 'group G' (bacteria) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Gronenborn, A.M. / Clore, G.M. | ||||||
Citation | Journal: Science / Year: 1991 Title: A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Authors: Gronenborn, A.M. / Filpula, D.R. / Essig, N.Z. / Achari, A. / Whitlow, M. / Wingfield, P.T. / Clore, G.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2gb1.cif.gz | 28.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2gb1.ent.gz | 18.9 KB | Display | PDB format |
PDBx/mmJSON format | 2gb1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2gb1_validation.pdf.gz | 240.1 KB | Display | wwPDB validaton report |
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Full document | 2gb1_full_validation.pdf.gz | 239.9 KB | Display | |
Data in XML | 2gb1_validation.xml.gz | 2.8 KB | Display | |
Data in CIF | 2gb1_validation.cif.gz | 3.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gb/2gb1 ftp://data.pdbj.org/pub/pdb/validation_reports/gb/2gb1 | 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: Protein | Mass: 6201.784 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus sp. 'group G' (bacteria) / References: UniProt: P06654 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software |
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Refinement | Software ordinal: 1 Details: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON THE JRNL RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM ...Details: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON THE JRNL RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES BETWEEN THE CALCULATED STRUCTURES). THE STRUCTURES ARE BASED ON 854 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 60 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 30 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE CALCULATIONS; AND 54 PHI AND 51 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 39 CHI1 SIDE CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE DATA. THE LATTER ARE OBTAINED USING THE CONFORMATIONAL GRID SEARCH PROGRAM STEREOSEARCH [NILGES, M., CLORE, G.M. & GRONENBORN, A.M. (1990) BIOPOLYMERS 29, 813-822. THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD [NILGES, M., CLORE, G.M. & GRONENBORN, A.M. FEBS LETT. 229, 317-324 (1988)]. A TOTAL OF 60 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE PRESENTED IN PROTEIN DATA BANK ENTRY 2GB1. THIS WAS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE 60 STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1GB1. THE QUANTITY PRESENTED IN THE B VALUE FIELD (COLUMNS 61 - 66 OF THE ATOM AND HETATM RECORDS BELOW) REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS. | |||||||||
NMR ensemble | Conformers submitted total number: 1 |