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- PDB-1hyt: RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ... -

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Basic information

Entry
Database: PDB / ID: 1hyt
TitleRE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A
ComponentsTHERMOLYSIN
KeywordsHYDROLASE(METALLOPROTEINASE)
Function / homology
Function and homology information


thermolysin / metalloendopeptidase activity / extracellular region / metal ion binding
Peptidase M4/M1, CTD superfamily / Peptidase M4 domain / PepSY domain / Peptidase M4 / Peptidase M4, C-terminal / FTP domain / Elastase; domain 1 - #10 / Elastase; domain 1 / Neutral Protease Domain 2 / Neutral Protease; domain 2 ...Peptidase M4/M1, CTD superfamily / Peptidase M4 domain / PepSY domain / Peptidase M4 / Peptidase M4, C-terminal / FTP 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 / MOLECULAR SUBSTITUTION / Resolution: 1.7 Å
AuthorsHausrath, A.C. / Matthews, B.W.
Citation
Journal: J.Biol.Chem. / Year: 1994
Title: Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.
Authors: Hausrath, A.C. / Matthews, B.W.
#1: Journal: Biochemistry / Year: 1984
Title: Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined by X-Ray Crystallography: A Novel Class of Transition-State Analogues for Zinc Peptidases
Authors: Monzingo, A.F. / Matthews, B.W.
#2: Journal: J.Mol.Biol. / Year: 1982
Title: Structure of Thermolysin Refined at 1.6 Angstroms Resolution
Authors: Holmes, M.A. / Matthews, B.W.
#3: Journal: J.Biol.Chem. / Year: 1974
Title: The Conformation of Thermolysin
Authors: Matthews, B.W. / Weaver, L.H. / Kester, W.R.
#4: Journal: Nature New Biol. / Year: 1972
Title: Structure of Thermolysin
Authors: Matthews, B.W. / Colman, P.M. / Jansonius, J.N. / Titani, K. / Walsh, K.A. / Neurath, H.
#5: Journal: Nature New Biol. / Year: 1972
Title: Three Dimensional Structure of Thermolysin
Authors: Matthews, B.W. / Jansonius, J.N. / Colman, P.M. / Schoenborn, B.P. / Duporque, D.
Validation Report
SummaryFull reportAbout validation report
History
DepositionMay 4, 1994Processing site: BNL
Revision 1.0Jul 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 13, 2012Group: Derived calculations
Revision 1.4Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.5Apr 4, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type

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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)34,8748
Polymers34,3621
Non-polymers5127
Water2,828157
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)93.691, 93.691, 131.503
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122
Atom site foot note1: CIS PROLINE - PRO 51

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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 genetically manipulated source
Source: (gene. exp.) Bacillus thermoproteolyticus (bacteria)
References: UniProt: P00800, thermolysin

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Non-polymers , 5 types, 164 molecules

#2: Chemical
ChemComp-CA / CALCIUM ION / Calcium


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-ZN / ZINC ION / Zinc


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#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-BZS / L-BENZYLSUCCINIC ACID


Mass: 208.211 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H12O4
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 157 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.42 Å3/Da / Density % sol: 49.25 %
Crystal growpH: 7.2 / Details: pH 7.2
Crystal grow
*PLUS
Method: unknown / Details: Holmes, M.A., (1982) J.Mol.Biol., 160, 623.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
12.5 M11CsCl
20.01 Mcalcium acetate12
30.01 MTris12
47 %(v/v)dimethylsulphoxide12

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
DetectorType: XUONG-HAMLIN / Detector: MULTIWIRE AREA DETECTOR
RadiationMonochromator: GRAPHITE / Protocol: SINGLE CRYSTAL / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
Reflection
*PLUS
Highest resolution: 1.7 Å / Num. obs: 35931 / % possible obs: 94 % / Rmerge(I) obs: 0.045

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Processing

Software
NameVersionClassification
TNTrefinement
XENGEN(HOWARDdata reduction
NIELSENdata reduction
XUONG)data reduction
XENGEN(HOWARDdata scaling
NIELSENdata scaling
XUONG)data scaling
RefinementMethod to determine structure: MOLECULAR SUBSTITUTION / Resolution: 1.7→20 Å / σ(F): 4 /
RfactorNum. reflection
Obs0.157 35975
Refinement stepCycle: LAST / Resolution: 1.7→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2432 0 24 157 2613
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.015
X-RAY DIFFRACTIONt_angle_deg1.9
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd
Software
*PLUS
Name: TNT / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.157
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 30.1 Å2
Refine LS restraints
*PLUS
Type: t_angle_d / Dev ideal: 1.9

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