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.
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.
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.
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.
Gathers information of experimental input (structures, analyses) in an annotated and verified collection. NRG-CING contains only the release Protein Data Bank (PDB) entries. This tools contains eleven programs that list for each entry, the potential inconsistencies between the coordinates and the available experimental Nuclear Magnetic Resonance (NMR) data.