216L

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Replaces:  116L

Summary for 216L

Related2LZM 3LZM
DescriptorT4 LYSOZYME (2 entities in total)
Functional Keywordshydrolase(o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm  P00720
Total number of polymer chains2
Total molecular weight37454.99
Authors
Blaber, M.,Matthews, B.W. (deposition date: 1994-05-10, release date: 1994-07-31, Last modification date: 2017-11-29)
Primary citation
Blaber, M.,Zhang, X.J.,Matthews, B.W.
Structural basis of amino acid alpha helix propensity.
Science, 260:1637-1640, 1993
PubMed: 8503008 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers370.6%15.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 216l
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Molmil generated image of 216l
rotated about x axis by 90°
Molmil generated image of 216l
rotated about y axis by 90°

More Biological unit images

Molmil generated image of 216l
no rotation
Molmil generated image of 216l
rotated about x axis by 90°
Molmil generated image of 216l
rotated about y axis by 90°
(*)In the case of coarse surface representation, the asymmetric unit is shown as red ribbon representation.
Coordinate files for Biological unit (216l.pdb2.gz [28.22 KB])
Coordinate files for Biological unit (216l.pdb1.gz [27.71 KB])
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