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- PDB-1fj3: THERMOLYSIN (50% ACETONE SOAKED) -

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Basic information

Entry
Database: PDB / ID: 1fj3
TitleTHERMOLYSIN (50% ACETONE SOAKED)
ComponentsTHERMOLYSIN
KeywordsHYDROLASE / METALLOPROTEINASE / ORGANIC SOLVENT
Function / homology
Function and homology information


thermolysin / metalloendopeptidase activity / extracellular region / metal ion binding
Thermolysin metallopeptidase, alpha-helical domain / Peptidase M4, C-terminal / FTP domain / Peptidase M4 domain / Peptidase M4 / PepSY domain / Peptidase M4/M1, CTD superfamily / Thermolysin metallopeptidase, catalytic domain / Elastase; domain 1 - #10 / Elastase; domain 1 ...Thermolysin metallopeptidase, alpha-helical domain / Peptidase M4, C-terminal / FTP domain / Peptidase M4 domain / Peptidase M4 / PepSY domain / Peptidase M4/M1, CTD superfamily / Thermolysin metallopeptidase, catalytic domain / Elastase; domain 1 - #10 / Elastase; domain 1 / Neutral Protease Domain 2 / Neutral Protease; domain 2 / Roll / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Thermolysin
Biological speciesBacillus thermoproteolyticus (bacteria)
MethodX-RAY DIFFRACTION / isomorphous replacement / Resolution: 2 Å
AuthorsEnglish, A.C. / Groom, C.R. / Hubbard, R.E.
CitationJournal: Protein Eng. / Year: 2001
Title: Experimental and computational mapping of the binding surface of a crystalline protein.
Authors: English, A.C. / Groom, C.R. / Hubbard, R.E.
Validation Report
SummaryFull reportAbout validation report
History
DepositionAug 7, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 18, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: THERMOLYSIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,7829
Polymers34,3621
Non-polymers4208
Water2,432135
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)94.010, 94.010, 131.030
Angle α, β, γ (deg.)90, 90, 120
Int Tables number178
Space group name H-MP6122

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Components

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Protein , 1 types, 1 molecules A

#1: Protein THERMOLYSIN /


Mass: 34362.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus thermoproteolyticus (bacteria) / References: UniProt: P00800, thermolysin

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Non-polymers , 5 types, 143 molecules

#2: Chemical ChemComp-ZN / ZINC ION / Zinc


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-CA / CALCIUM ION / Calcium


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Chemical ChemComp-ACN / ACETONE / Acetone


Mass: 58.079 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H6O
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 135 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49.41 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 4.6MM THERMOLYSIN, 45% DMSO, 50MM TRIS-HCL, 2.5M CSCL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Crystal grow
*PLUS
Method: unknown
Details: English, A.C., (1999) Proteins Struct.Funct.Genet., 37, 628.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
14.6 mMprotein11
245 %DMSO11
350 mMTris-HCl11
42.5 M11CsCl

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: AREA DETECTOR / Date: Jan 22, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. all: 312589 / Num. obs: 23648 / % possible obs: 93 % / Observed criterion σ(I): 2 / Redundancy: 6.4 % / Biso Wilson estimate: 24 Å2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 6.4
Reflection shellResolution: 2→2.06 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.266 / Num. unique all: 3285 / % possible all: 91
Reflection shell
*PLUS
% possible obs: 91 % / Mean I/σ(I) obs: 2.8

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Processing

Software
NameVersionClassification
REFMACrefinement
MAR345data collection
CCP4(SCALA)data scaling
RefinementMethod to determine structure: isomorphous replacement / Resolution: 2→20 Å / Stereochemistry target values: Engh & Huber / Details: used maximum likelihood procedure
RfactorNum. reflection% reflection
Rfree0.205 1219 5 %
Rwork0.16 --
All0.163 --
Obs-23648 93 %
Refinement stepCycle: LAST / Resolution: 2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2458 0 9 143 2610
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.033
X-RAY DIFFRACTIONp_angle_d0.014

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