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- PDB-1nzp: Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nzp | ||||||
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Title | Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda | ||||||
![]() | DNA polymerase lambda | ||||||
![]() | DNA BINDING PROTEIN/TRANSFERASE / DNA POLYMERASE LAMBDA / POL LAMBDA / LYASE DOMAIN / 8 kDa DOMAIN / POL BETA-LIKE / DNA BINDING PROTEIN-TRANSFERASE COMPLEX | ||||||
Function / homology | ![]() DNA biosynthetic process / Lyases; Carbon-oxygen lyases; Other carbon-oxygen lyases / 5'-deoxyribose-5-phosphate lyase activity / somatic hypermutation of immunoglobulin genes / base-excision repair, gap-filling / double-strand break repair via homologous recombination / nucleotide-excision repair / Nonhomologous End-Joining (NHEJ) / double-strand break repair via nonhomologous end joining / site of double-strand break ...DNA biosynthetic process / Lyases; Carbon-oxygen lyases; Other carbon-oxygen lyases / 5'-deoxyribose-5-phosphate lyase activity / somatic hypermutation of immunoglobulin genes / base-excision repair, gap-filling / double-strand break repair via homologous recombination / nucleotide-excision repair / Nonhomologous End-Joining (NHEJ) / double-strand break repair via nonhomologous end joining / site of double-strand break / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA replication / DNA binding / nucleoplasm / metal ion binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing torsion angle dynamics follow by cartesian dynamics | ||||||
Model type details | minimized average | ||||||
![]() | DeRose, E.F. / Kirby, T.W. / Mueller, G.A. / Bebenek, K. / Garcia-Diaz, M. / Blanco, L. / Kunkel, T.A. / London, R.E. | ||||||
![]() | ![]() Title: Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda Authors: DeRose, E.F. / Kirby, T.W. / Mueller, G.A. / Bebenek, K. / Garcia-Diaz, M. / Blanco, L. / Kunkel, T.A. / London, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 227.7 KB | Display | ![]() |
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PDB format | ![]() | 188.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 350.7 KB | Display | ![]() |
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Full document | ![]() | 407.3 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 19.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 9715.243 Da / Num. of mol.: 1 Fragment: POLYMERASE LAMBDA LYASE DOMAIN(RESIDUES 242 - 327) 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: Chemical shift assigments were made from 3D HNCACB, CBCA(CO)NH, HNCO, H(CCO)NH, and (H)C(CO)NH experiments. Aromatic resonances were assigned using 2D (HB)CB(CGCD)HD and (HB)CB(CGCDCE)HE experiments. |
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Sample preparation
Details | Contents: 2mM pol lambda 8 kDa domain U-15N,13C; 5mM Tris-d11; 100mM NaCl; 1mM DTT; 5mM NaN3 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 5mM Tris, 100mM NaCl, 5mM NaN3 / pH: 7 / Pressure: ambient / 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 INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing torsion angle dynamics follow by cartesian dynamics Software ordinal: 1 Details: The structure was computed using default ARIA parameters. 281 manually assigned NOE distance restraints were used in addition to the NOE restraints automatically assigned by ARIA. ARIA ...Details: The structure was computed using default ARIA parameters. 281 manually assigned NOE distance restraints were used in addition to the NOE restraints automatically assigned by ARIA. ARIA assigned 790 unambiguous and 191 ambiguous NOE restraints. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 8 |