NMR structure refinement databases | Protein structure data analysis

A database that contains recalculated structures for 500+ protein entries from the Protein Data Bank (PDB). RECOORD can be used by the structural biology community for further development of calculation protocols, validation tools, structure-based statistical approaches and modeling.

Contains detailed information about the extent of disorder in more than 100 curated protein data entries. CheZOD database is a repository of experimentally validated disordered proteins. The inspection and systematic analysis of the entries highlighted several trends and variations. This repository can contribute to a more detailed understanding of the relationship between primary sequence and disorder/structure and function.

A repository for solution NMR structures refined in explicit solvent. DRESS presents a uniformly refined and validated set of structural models that hopefully improves the value of these NMR structures as input for experimental and theoretical studies in many fields of research. Currently there are 100 refined PDB files in the database.

Allows users to integrate high resolution accurate mass (HRAM) mass spectrometry (MS) and complementary nuclear magnetic resonance (NMR) data for unrivalled structure verification. Bruker FUSION-SV allows access to joint spectroscopic data allowing projects to be shared by collaborating scientists. In addition, individuals can work on multiple projects in parallel. The software also delivers to lab managers information ensuring visibility of workflow within the laboratory and providing an overview of on-going projects.

A public database of 2405 refined NMR solution structures from the Protein Data Bank (PDB). A simulated annealing protocol was employed to obtain refined structures with target potentials, including the newly developed STAP. The refined database was extensively analysed using various quality indicators from several assessment programs to determine the nuclear Overhauser effect (NOE) completeness, Ramachandran appearance, chi(1)-chi(2) rotamer normality, various parameters for protein stability and other indicators.