+Open data
-Basic information
Entry | Database: PDB / ID: 1u0i | ||||||
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Title | IAAL-E3/K3 heterodimer | ||||||
Components |
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Keywords | DE NOVO PROTEIN / coiled-coil | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, CHEMICAL-SHIFT AUTO -ASSIGNMENT, DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
Authors | Lindhout, D.A. / Litowski, J.R. / Mercier, P. / Hodges, R.S. / Sykes, B.D. | ||||||
Citation | Journal: Biopolymers / Year: 2004 Title: NMR solution structure of a highly stable de novo heterodimeric coiled-coil Authors: Lindhout, D.A. / Litowski, J.R. / Mercier, P. / Hodges, R.S. / Sykes, B.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1u0i.cif.gz | 294 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1u0i.ent.gz | 261.5 KB | Display | PDB format |
PDBx/mmJSON format | 1u0i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u0/1u0i ftp://data.pdbj.org/pub/pdb/validation_reports/u0/1u0i | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2285.651 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized using t-butyloxycarbonyl solid-phase technique |
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#2: Protein/peptide | Mass: 2285.849 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized using t-butyloxycarbonyl solid-phase technique |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1MM IAAL-E3/K3 COILED-COIL, NA-15N, PH 6.7, 100MM KCL, 50MM KPO4,90%/10% H2O/D2O, 23.1% TFE-D3 |
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Sample conditions | Ionic strength: 0.15 / pH: 6.7 / Pressure: AMBIENT / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING, CHEMICAL-SHIFT AUTO -ASSIGNMENT, DISTANCE GEOMETRY, SIMULATED ANNEALING Software ordinal: 1 Details: SOFTWARE USED WAS CYANA AND ITS INTEGRATED AUTO-ASSIGNMENT MODULE CANDID. THE CHEMICAL SHIFT IDENTIFICATION TOLERANCE AND TRANSPOSE ERRORS WERE SET TO 0.015 PPM IN BOTH PROTON DIMENSIONS. ...Details: SOFTWARE USED WAS CYANA AND ITS INTEGRATED AUTO-ASSIGNMENT MODULE CANDID. THE CHEMICAL SHIFT IDENTIFICATION TOLERANCE AND TRANSPOSE ERRORS WERE SET TO 0.015 PPM IN BOTH PROTON DIMENSIONS. STARTING WITH DISTANCE RESTRAINTS DERIVED FROM MANUALLY ASSIGNED NOE CROSS-PEAKS IN NMRVIEW, A TOTAL NUMBER OF 100 STRUCTURES WERE GENERATED PER CANDID ROUND WITH 8000 STEPS IN THE CYANA ANNEALING PROTOCOL. FOR EACH CANDID RUN, TALOS DERIVED ANGLE RESTRAINTS WERE INCORPORATED (WITH A MINIMUM ERROR SET MANUALLY TO 20 DEGREES) . THE BEST 20 LOW TARGET FUNCTION VALUE STRUCTURES OF CANDIDS FINAL ROUND WERE KEPT AS AN ENSEMBLE REPRESENTATION OF THE FAMILY OF GENERATED STRUCTURES. | ||||||||||||
NMR ensemble | Conformer selection criteria: back calculated data agree with experimental NOESY spectrum Conformers calculated total number: 100 / Conformers submitted total number: 20 |