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Yorodumi- PDB-1ezc: AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ezc | ||||||
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Title | AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17 STRUCTURES | ||||||
Components | ENZYME I | ||||||
Keywords | PHOSPHOTRANSFERASE / KINASE / SUGAR TRANSPORT | ||||||
Function / homology | Function and homology information phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / kinase activity / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Garrett, D.S. / Gronenborn, A.M. / Clore, G.M. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Authors: Garrett, D.S. / Seok, Y.J. / Liao, D.I. / Peterkofsky, A. / Gronenborn, A.M. / 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 | 1ezc.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1ezc.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 1ezc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ezc_validation.pdf.gz | 342.6 KB | Display | wwPDB validaton report |
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Full document | 1ezc_full_validation.pdf.gz | 450.8 KB | Display | |
Data in XML | 1ezc_validation.xml.gz | 81.8 KB | Display | |
Data in CIF | 1ezc_validation.cif.gz | 25.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ez/1ezc ftp://data.pdbj.org/pub/pdb/validation_reports/ez/1ezc | 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: 28381.316 Da / Num. of mol.: 1 / Fragment: AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: GI698 / Plasmid: PLP2 / Production host: Escherichia coli (E. coli) References: UniProt: P08839, phosphoenolpyruvate-protein phosphotransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 7 / Temperature: 313 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: THE 3D STRUCTURE OF THE EIN WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 4251 EXPERIMENTAL NMR RESTRAINTS: (A) INTRAPROTEIN: 952 SEQUENTIAL (|I- J|=1), 809 MEDIUM RANGE ...Details: THE 3D STRUCTURE OF THE EIN WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 4251 EXPERIMENTAL NMR RESTRAINTS: (A) INTRAPROTEIN: 952 SEQUENTIAL (|I- J|=1), 809 MEDIUM RANGE (1 < |I-J| <=5) AND 586 LONG RANGE (|I-J| >5) INTERRESIDUES AND 471 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 230 DISTANCES FOR 115 BACKBONE HYDROGEN BONDS; 140 TORSION ANGLE RESTRAINTS; 163 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 498 (258 CALPHA AND 241 CBETA) 13C SHIFT RESTRAINTS. (NUMBERS OF RESIDUES 1 - 259). THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE POTENTIAL (KUSZEWSKI ET AL.(1996) PROTEIN SCI. 5, 1067-1080 IN THE RESTRAINED REGULARIZED MEAN COORDINATES THE TEMPERATURE FACTOR FIELD REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO MEANING. BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 1 - 246 (RESIDUES 250 - 259 ARE DISORDERED IN SOLUTION) NOTE THE OCCUPANCY FIELD HAS NO MEANING. | ||||||||||||
NMR ensemble | Conformers submitted total number: 17 |