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The archiving and dissemination of biological structure dataUncertainty in integrative structural modelingThe RCSB Protein Data Bank: views of structural biology for basic and applied research and educationThe Protein Data Bank archive as an open data resourceHow to make deposition of images a realityProtein structure determination by combining sparse NMR data with evolutionary couplingsOneDep: Unified wwPDB System for Deposition, Biocuration, and Validation of Macromolecular Structures in the PDB ArchiveStructural and sequencing analysis of local target DNA recognition by MLV integrase.Outcome of the First wwPDB/CCDC/D3R Ligand Validation Workshop.Quality assessment of protein NMR structures.The expanded FindCore method for identification of a core atom set for assessment of protein structure prediction.Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structuresProtein structure annotation resources.CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO.A community resource of experimental data for NMR / X-ray crystal structure pairs.The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.Structure of fully protonated proteins by proton-detected magic-angle spinning NMRA protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining.Protein Data Bank (PDB): The Single Global Macromolecular Structure Archive.TEMPy: a Python library for assessment of three-dimensional electron microscopy density fitsHow community has shaped the Protein Data Bank.Chemical annotation of small and peptide-like molecules at the Protein Data Bank.Small molecule annotation for the Protein Data Bank.NMR Exchange Format: a unified and open standard for representation of NMR restraint data.EMDataBank unified data resource for 3DEM.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.Using the Tools and Resources of the RCSB Protein Data Bank.The RCSB protein data bank: integrative view of protein, gene and 3D structural information.Deriving Structural Information from Experimentally Measured Data on Biomolecules.Mechanism of the pH-induced conformational change in the sensor domain of the DraK Histidine kinase via the E83, E105, and E107 residues.MolProbity for the masses-of data.The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013.Databases and Archiving for CryoEM.Improving NMR Structures of RNAOutcome of the First wwPDB Hybrid/Integrative Methods Task Force WorkshopProteinsPlus: a web portal for structure analysis of macromolecules.Resolution of ab initio shapes determined from small-angle scattering.Analysis of the structural quality of the CASD-NMR 2013 entries.Structure calculation, refinement and validation using CcpNmr Analysis.
P2860
Q26741934-A40F4CF0-8AEC-49E7-891D-84C6BD4E72DFQ26827375-8B31C4B2-47A7-40AD-BB42-C4626F93417BQ28650443-5AA05976-43B3-4238-9637-CC8F9781D356Q28654725-72C846D8-C429-4FA6-9BDB-C94DD90D86B9Q28654955-EDF967E6-47AD-4322-86FD-E7F25DA99D65Q28914765-8A2FE8EA-8336-4D47-B723-4318CBCB5F0CQ28950350-8DAE2135-0B63-4947-805E-5FDD5B52F130Q30009173-D41E3CBD-2746-473C-BEA6-60D96124641AQ30277026-27CD7AC3-84C0-4D82-8532-A5333080D317Q30353837-326832AF-982B-4F96-9BAD-BF3B789B3E96Q30356675-ABBE36E8-9B53-4E3F-B1C6-5E21DA96BC90Q30357564-26ED41EA-95ED-4EB5-A29D-A67365B3C700Q30369659-FAE88C8D-EA1D-4D45-88AB-F2610F579EC0Q30374174-49DC8592-B41C-4669-BD07-D258CE4F5593Q30378171-A8331BE5-F2BA-455A-B5E0-65D99C55809CQ30380211-379B12A5-AC5E-404B-9453-A14CE5163829Q30391464-ABDA54B5-4040-48CC-921B-71ACB3D2D77CQ30394410-397FBF9E-9C49-4B9E-9F07-8B910B5559C2Q30411764-BB1F467C-FA44-411F-853C-C6A40F5DA41CQ30491855-0B067ED7-CC1B-421F-879D-733DDB437F54Q30659554-5345DE74-5AC4-4CCA-8950-47D2BD93CC79Q30665362-7906B2DF-BF80-4C6E-99B7-7569FE71986CQ30704756-1CBBB317-4363-4E4F-BE21-F525D8310489Q30872013-A20DA594-C001-4D92-9891-1D57F26CE53CQ30963884-037EC542-10FF-4A58-B86C-9A07306B6D4FQ31025251-A24812CA-C0BD-46C1-A03B-CC57A8B13E74Q31035956-6C5F59B7-9E9A-4C15-9A53-42E382FEAB85Q31127140-C5394C94-CB15-4854-ADFB-EF056AB228E3Q31139806-5B3B2545-66FB-4A7D-9FFD-81C0812DA109Q31143273-2861B0A1-793B-45A6-9B8C-912B9C1553DEQ34156137-B9A5DB42-8456-4063-BC35-63E82C76FCC1Q35701346-A3E7EC46-790D-4B17-9962-E881A5D92073Q36059190-D913803A-6CDE-43FD-B6D3-AC63FA09D357Q36116327-70D71724-EEF4-47D1-AD4C-C97A5A4B6584Q36869352-675D0EF4-9D31-4606-9089-41389553A729Q37066138-68DA56AB-ACBD-4071-8B85-C69A37CD19DCQ38687678-AF265BE1-19EB-461A-A95C-11C43FE076D2Q39190593-22B29744-08E7-4C4E-B65F-657EFE5EA739Q40881375-00910B35-6524-4590-BC91-6AF6DC42ACA2Q42055587-34247047-CE42-4FAD-8C16-7046260846F3
P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Recommendations of the wwPDB NMR Validation Task Force
@ast
Recommendations of the wwPDB NMR Validation Task Force
@en
Recommendations of the wwPDB NMR Validation Task Force
@nl
type
label
Recommendations of the wwPDB NMR Validation Task Force
@ast
Recommendations of the wwPDB NMR Validation Task Force
@en
Recommendations of the wwPDB NMR Validation Task Force
@nl
prefLabel
Recommendations of the wwPDB NMR Validation Task Force
@ast
Recommendations of the wwPDB NMR Validation Task Force
@en
Recommendations of the wwPDB NMR Validation Task Force
@nl
P2860
P50
P1433
P1476
Recommendations of the wwPDB NMR Validation Task Force
@en
P2093
P2860
P304
P356
10.1016/J.STR.2013.07.021
P407
P50
P577
2013-09-03T00:00:00Z