A: OLIGOPEPTIDASSE B B: OLIGOPEPTIDASSE B C: OLIGOPEPTIDASSE B D: OLIGOPEPTIDASSE B E: OLIGOPEPTIDASSE B F: OLIGOPEPTIDASSE B G: ANTIPAIN H: ANTIPAIN I: ANTIPAIN J: ANTIPAIN K: ANTIPAIN L: ANTIPAIN
Mass: 18.015 Da / Num. of mol.: 344 / Source method: isolated from a natural source / Formula: H2O
Compound details
ANTIPAIN HYDROCHLORIDE IS A REVERSIBLE INHIBITOR OF SERINE/CYSTEINE PROTEASES AND SOME TRYPSIN-LIKE ...ANTIPAIN HYDROCHLORIDE IS A REVERSIBLE INHIBITOR OF SERINE/CYSTEINE PROTEASES AND SOME TRYPSIN-LIKE SERINE PROTEASES. ITS ACTION RESEMBLES LEUPEPTIN; HOWEVER, ITS PLASMIN INHIBITION IS LESS AND ITS CATHEPSIN A INHIBITION IS MORE THAN THAT OBSERVED WITH LEUPEPTIN. IT IS AN INHIBITOR OF TRYPSIN-LIKE PROTEASES (E.G. TRYPSIN, PAPAIN, CATHEPSIN B); CATHEPSIN A, A CARBOXYPEPTIDASE IS INHIBITED TOO, WHICH IS NOT TRUE FOR OTHER INHIBITORS FROM ACTINOMYCES.THE NAME IS DERIVED FROM ANTI-PAPAIN. GROUP: 1 NAME: ANTIPAIN CHAIN: G, H, I, J, K, L COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 4 DESCRIPTION: ANTIPAIN FORMS A COVALENT LINKAGE BETWEEN THE ARGINAL RESIDUE OF THE INHIBITOR AND SER RESIDUE OF THE PROTEIN.THE PROTEASE INHIBITOR ANTIPAIN INCREASES THE EFFECTIVENESSOF UV IRRADIATION ON CESSATION OF RESPIRATION AND CELL KILLING IN ESCHERICHIA COLI B/R CULTURES WITHOUT AFFECTING EXCISION OF PYRIMIDINE DIMERS. THE ACTIONS ARE SIMILAR TO THOSE CAUSED BY CYCLIC AMP IN IRRADIATED CULTURES.
Nonpolymer details
ANTIPAIN: COVALENTLY BOUND TO THE CATALYTIC SER563
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3 Å3/Da / Density % sol: 59 % Description: STARTING MODEL IS ALSO BEING CURRENTLY DEPOSITED
Crystal grow
pH: 5 Details: 10 % PEG 4000, 0.2 M CALCIUM ACETATE, 0.1 M SODIUM ACETATE PH 5
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9778 Å / Relative weight: 1
Reflection
Resolution: 2.85→59 Å / Num. obs: 127053 / % possible obs: 96.7 % / Observed criterion σ(I): -3 / Redundancy: 6.5 % / Biso Wilson estimate: 45.4 Å2 / Rmerge(I) obs: 0.22 / Net I/σ(I): 8.3
Reflection shell
Resolution: 2.85→3 Å / Redundancy: 6.6 % / Rmerge(I) obs: 1.12 / Mean I/σ(I) obs: 2.2 / % possible all: 97.7
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Processing
Software
Name
Version
Classification
REFMAC
5.5.0109
refinement
XDS
datareduction
XDS
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.85→58.59 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.882 / SU B: 43.636 / SU ML: 0.381 / Cross valid method: THROUGHOUT / ESU R Free: 0.436 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.28074
5162
4.1 %
RANDOM
Rwork
0.21333
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obs
0.21609
121891
96.75 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK