about
Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactionsRecommendations of the wwPDB NMR Validation Task ForceTraditional biomolecular structure determination by NMR spectroscopy allows for major errors.NMR structure of the pseudo-receiver domain of CikAStructure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphismCatalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinaseSolution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidisNMR Structure of the Amino-Terminal Domain of the Lambda Integrase Protein in Complex with DNA: Immobilization of a Flexible Tail Facilitates Beta-Sheet Recognition of the Major GrooveStructure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D(28K)The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulationsStructural biology by NMR: structure, dynamics, and interactions.Advances in automated NMR protein structure determination.Overview on the use of NMR to examine protein structure.Blind testing of routine, fully automated determination of protein structures from NMR dataInsights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions.Vivaldi: visualization and validation of biomacromolecular NMR structures from the PDB.How precise are reported protein coordinate data?Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements.Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments.X-ray vs. NMR structures as templates for computational protein design.An overview of tools for the validation of protein NMR structures.The structure of chromophore-grafted amyloid-β(12-28) dimers in the gas-phase: FRET-experiment guided modelling.NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.Analysis of the structural quality of the CASD-NMR 2013 entries.CING: an integrated residue-based structure validation program suite.Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity.Assessment of contact predictions in CASP12: co-evolution and deep learning coming of age.A robust method for quantitative identification of ordered cores in an ensemble of biomolecular structures by non-linear multi-dimensional scaling using inter-atomic distance variance matrix.In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design.Measurement of Structural Restraints
P2860
Q24320262-AC615703-16F6-40F6-AF5D-82323EB22D7FQ24620570-560C20AE-8C4C-4FD9-8495-3EA4E35D986DQ25257832-1BCD85CD-1AA8-4DAC-A846-F7FE1D52B52AQ27643902-4EBF4AD2-4DF7-4436-8586-64FFA882F25EQ27644071-79DA57E7-7B79-4CBC-A692-F59D0F5643C9Q27648164-1758CC8C-ED0B-4D1D-BF39-35E3980DDB22Q27653667-864DB16E-1914-488A-A2DE-CAFF8A7F73F4Q27654440-A0737669-A618-470C-B8A2-412E389D3A88Q28248378-6B067751-3755-44E5-98D7-FFDA2159CDE2Q30010196-08D08E99-0AC1-4A25-B332-D939AE1F8F2EQ30372281-32DCB7E5-45BF-4663-8B0B-124DC5DF82D0Q30400806-8BA61EC1-3ADF-4AB3-95F1-BF9645FCCDBFQ30401790-0F963D31-D2CC-4C18-89C9-6D70C3A0861DQ30412925-2F76D3A8-CF46-4487-BF27-6B349016F867Q31115351-862BBB34-1CFE-46CD-8A69-9D165F1FB5D3Q34488156-C36D2938-8DA8-4DED-B577-6D0870EE6C8EQ35111992-1D6104B5-8A07-434F-9EFD-4AC5052C75D4Q35633848-377BB97B-ACCB-4F6D-B05A-A03445C72CB7Q36791983-36D1A14B-CDCA-470D-94DA-2B4E8256F9D6Q37319930-CEADAF06-46CF-49B8-89A6-9F907CE600ECQ38123436-9274B6E8-6527-42DF-9A40-4E6291D11B98Q39924452-5B6F4915-7820-413C-9445-1A2F2425C8C7Q40175098-01E07F23-E721-4B32-9D8E-22E857AF0108Q40881375-3FE58261-7E50-48CC-A224-D1D17B4FF874Q41666652-5FEDF1A7-2DD9-4E89-B8BE-47D395AE4A80Q42732701-5D729B70-C2CB-4E93-83CD-2A1BF9F26214Q45944467-422797DA-5047-4B2E-9C01-C6291212C30AQ51127001-A6EED98B-9F20-47B1-AEFE-E132387EEE44Q52691351-C83EB7B9-CFDF-4FF9-A55F-4B9C98A25FFAQ57080179-1196195B-60D6-4947-9D4C-59DD74A07383
P2860
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Quantitative evaluation of experimental NMR restraints.
@en
Quantitative evaluation of experimental NMR restraints.
@nl
type
label
Quantitative evaluation of experimental NMR restraints.
@en
Quantitative evaluation of experimental NMR restraints.
@nl
prefLabel
Quantitative evaluation of experimental NMR restraints.
@en
Quantitative evaluation of experimental NMR restraints.
@nl
P2093
P356
P1476
Quantitative evaluation of experimental NMR restraints
@en
P2093
Chris A E M Spronk
Elmar Krieger
Gert Vriend
Hans Maassen
Sander B Nabuurs
P304
12026-12034
P356
10.1021/JA035440F
P407
P577
2003-10-01T00:00:00Z