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- PDB-1avt: SUBTILISIN CARLSBERG D-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID... -

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Basic information

Entry
Database: PDB / ID: 1avt
TitleSUBTILISIN CARLSBERG D-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
ComponentsSUBTILISIN CARLSBERG, TYPE VIII
KeywordsSERINE PROTEASE / HYDROLASE / BORONIC ACID INHIBITORS
Function / homology
Function and homology information


subtilisin / serine-type endopeptidase activity / extracellular region / metal ion binding
Peptidase S8, subtilisin, Ser-active site / Subtilisin Carlsberg-like catalytic domain / Subtilase family / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8 propeptide/proteinase inhibitor I9 / Peptidase S8, subtilisin-related / Peptidase S8, subtilisin, His-active site / Peptidase S8, subtilisin, Asp-active site / Peptidase S8/S53 domain superfamily ...Peptidase S8, subtilisin, Ser-active site / Subtilisin Carlsberg-like catalytic domain / Subtilase family / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8 propeptide/proteinase inhibitor I9 / Peptidase S8, subtilisin-related / Peptidase S8, subtilisin, His-active site / Peptidase S8, subtilisin, Asp-active site / Peptidase S8/S53 domain superfamily / Peptidase S8/S53 domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Subtilisin Carlsberg
Biological speciesBacillus licheniformis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / ISOSTRUCTURAL TO 1SCA / Resolution: 2 Å
AuthorsStoll, V.S. / Eger, B.T. / Hynes, R.C. / Martichonok, V. / Jones, J.B. / Pai, E.F.
Citation
Journal: Biochemistry / Year: 1998
Title: Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
Authors: Stoll, V.S. / Eger, B.T. / Hynes, R.C. / Martichonok, V. / Jones, J.B. / Pai, E.F.
#1: Journal: J.Am.Chem.Soc. / Year: 1996
Title: Probing the Specificity of the Serine Proteases Subtilisin Carlsberg and A-Chymotrypsin with Enantiomeric 1-Acetamido Boronic Acids. An Unexpected Reversal of the Normal "L"-Stereoselectivity Preference
Authors: Martichonok, V. / Jones, J.B.
#2: Journal: Bioorg.Med.Chem. / Year: 1994
Title: Probing the Specificity of the S1 Binding Site of Subtilisin Carlsberg with Boronic Acids
Authors: Seufer-Wasserthal, P. / Martichonok, V. / Keller, T.H. / Chin, B. / Martin, R. / Jones, J.B.
#3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1993
Title: Enzyme Crystal Structure in a Neat Organic Solvent
Authors: Fitzpatrick, P.A. / Steinmetz, A.C. / Ringe, D. / Klibanov, A.M.
#4: Journal: J.Mol.Biol. / Year: 1976
Title: The Structure of Subtilopeptidase A. I. X-Ray Crystallographic Data
Authors: Petsko, G.A. / Tsernoglou, D.
Validation Report
SummaryFull reportAbout validation report
History
DepositionSep 19, 1997-
Revision 1.0Mar 25, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SUBTILISIN CARLSBERG, TYPE VIII
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,5933
Polymers27,5471
Non-polymers462
Water2,738152
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)53.000, 55.400, 76.600
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein/peptide SUBTILISIN CARLSBERG, TYPE VIII / SUBTILOPEPTIDASE A


Mass: 27546.670 Da / Num. of mol.: 1 / Fragment: FULL PROTEIN / Source method: isolated from a natural source / Source: (natural) Bacillus licheniformis (bacteria) / Details: PURCHASED FROM SIGMA / References: UniProt: P00780, subtilisin
#2: Chemical ChemComp-NA / SODIUM ION / Sodium


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 152 / 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: 7

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Sample preparation

CrystalDensity Matthews: 2.2 Å3/Da / Density % sol: 41.5 %
Description: THE COORDINATES OF THE STARTING MODEL WERE RE-INDEXED TO CONFORM TO AXIS LABELING CONVENTION A
Crystal growpH: 7 / Details: AS GIVEN IN REFERENCE 4, pH 7.0
Crystal grow
*PLUS
pH: 5.6 / Method: batch method / Details: Petsko, G.A., (1976) J.Mol.Biol., 106, 453.
Components of the solutions
*PLUS

Crystal-ID: 1 / Sol-ID: 1

IDConc.Common name
10.5 %protein
217 %aqueous sodium sulfate

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Data collection

DiffractionMean temperature: 287 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918
DetectorType: FUJI / Detector: IMAGE PLATE / Date: Nov 1, 1993 / Details: MIRRORS
RadiationMonochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 15092 / % possible obs: 96 % / Redundancy: 1.7 % / Rmerge(I) obs: 0.082 / Rsym value: 0.082 / Net I/σ(I): 14
Reflection shellResolution: 2→2.09 Å / Redundancy: 1.4 % / Rmerge(I) obs: 0.083 / Mean I/σ(I) obs: 7 / Rsym value: 0.083 / % possible all: 94.3

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
DENZOdata reduction
XSCALEdata scaling
X-PLOR3.1phasing
RefinementMethod to determine structure: ISOSTRUCTURAL TO 1SCA
Starting model: PDB ENTRY 1SCA
Resolution: 2→8 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: INDIVIDUAL / Cross valid method: THROUGHOUT / σ(F): 1
RfactorNum. reflection% reflectionSelection details
Rfree0.226 1452 10 %RANDOM
Rwork0.157 ---
Obs0.157 14776 95.6 %-
Displacement parametersBiso mean: 12 Å2
Refine analyzeLuzzati d res low obs: 8 Å
Refinement stepCycle: LAST / Resolution: 2→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1920 0 16 153 2089
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.48
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d24.7
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.34
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 2→2.09 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.227 189 9.92 %
Rwork0.1808 1572 -
Obs--91.9 %
Xplor file

Refinement-ID: X-RAY DIFFRACTION

Serial noParam fileTopol file
1PARHCSDX.PROTOPHCSDX.PRO
2PARAM19.SOLTOPH19.SOL
3TOPH19.PEP
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg24.7
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.34
LS refinement shell
*PLUS
Rfactor Rfree: 0.227

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