Atomic resolution (0.95A) structure of purified thaumatin I grown in sodium L-tartrate at 4 C
The structure was published by Asherie, N., Jakoncic, J., Ginsberg, C., et al., Hrnjez, B.J., Blass, S., and Berger, J., in 2009 in a paper entitled "Tartrate Chirality Determines Thaumatin Crystal Habit" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 0.95 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of THAUMATIN-1. This molecule has the UniProt identifier P02883 (THM1_THADA). The sample contained 207 residues which is 100% of the natural sequence. Out of 207 residues 206 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: