199L

THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME

Summary for 199L

DescriptorLYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
Functional Keywordscavities, core-packing, protein stability, hydrolase (o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm  P00720
Total number of polymer chains1
Total molecular weight18873.57
Authors
Baldwin, E.,Xu, J.,Hajiseyedjavadi, O.,Matthews, B.W. (deposition date: 1995-11-06, release date: 1996-03-08, Last modification date: 2017-11-29)
Primary citation
Baldwin, E.,Xu, J.,Hajiseyedjavadi, O.,Baase, W.A.,Matthews, B.W.
Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.
J.Mol.Biol., 259:542-559, 1996
PubMed: 8676387 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1996.0338
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.85 Å)
NMR Information
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers1104.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 199l
no rotation
Molmil generated image of 199l
rotated about x axis by 90°
Molmil generated image of 199l
rotated about y axis by 90°