5KW0

T. danielli thaumatin at 100K, Data set 5

Summary for 5KW0

Related5KUL 5KUN 5KUO 5KUQ 5KUR 5KUS 5KUU 5KUV 5KUW 5KUZ 5KV0 5KV1 5KV2 5KV3 5KV4 5KV5 5KV6 5KV7 5KVW 5KVX 5KVZ 5KW3 5KW4 5KW5 5KW7 5KW8
DescriptorThaumatin-1, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total)
Functional Keywordsconformational variation, radiation damage, plant protein
Biological sourceThaumatococcus daniellii (Katemfe)
Cellular locationCytoplasmic vesicle P02883
Total number of polymer chains1
Total molecular weight22469.24
Authors
Russi, S.,Gonzalez, A.,Kenner, L.R.,Keedy, D.A.,Fraser, J.S.,van den Bedem, H. (deposition date: 2016-07-15, release date: 2016-08-17, Last modification date: 2017-09-27)
Primary citation
Russi, S.,Gonzalez, A.,Kenner, L.R.,Keedy, D.A.,Fraser, J.S.,van den Bedem, H.
Conformational variation of proteins at room temperature is not dominated by radiation damage.
J Synchrotron Radiat, 24:73-82, 2017
PubMed: 28009548 (PDB entries with the same primary citation)
DOI: 10.1107/S1600577516017343
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.594 Å)
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.224902.4%8.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution