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- PDB-6svj: Terahertz irradiated structure of bovine trypsin (odd frames of c... -

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Basic information

Entry
Database: PDB / ID: 6svj
TitleTerahertz irradiated structure of bovine trypsin (odd frames of crystal x42)
ComponentsCationic trypsin
KeywordsHYDROLASE / bovine trypsin / Terahertz irradiation / odd frames / x42
Function / homology
Function and homology information


trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding
Similarity search - Function
Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases ...Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
BENZAMIDINE / Serine protease 1
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.16 Å
AuthorsAhlberg Gagner, V. / Lundholm, I. / Garcia-Bonete, M.J. / Rodilla, H. / Friedman, R. / Zhaunerchyk, V. / Bourenkov, G. / Schneider, T. / Stake, J. / Katona, G.
Funding support Sweden, 2items
OrganizationGrant numberCountry
Knut and Alice Wallenberg Foundation Sweden
Swedish Research Council Sweden
CitationJournal: Sci Rep / Year: 2019
Title: Clustering of atomic displacement parameters in bovine trypsin reveals a distributed lattice of atoms with shared chemical properties.
Authors: Gagner, V.A. / Lundholm, I. / Garcia-Bonete, M.J. / Rodilla, H. / Friedman, R. / Zhaunerchyk, V. / Bourenkov, G. / Schneider, T. / Stake, J. / Katona, G.
History
DepositionSep 18, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 22, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 29, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cationic trypsin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,6775
Polymers23,3241
Non-polymers3524
Water5,188288
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS GIVEN BELOW. ...Evidence: COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area780 Å2
ΔGint-30 kcal/mol
Surface area9000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.910, 57.150, 65.700
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 Cationic trypsin / Beta-trypsin


Mass: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00760, trypsin
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-BEN / BENZAMIDINE / Benzamidine


Mass: 120.152 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H8N2
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 288 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.13 Å3/Da / Density % sol: 42.15 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: protein solution - 60 mg/ml trypsin, 6 mg/ml benzamidine and 3 mM CaCl2 in a 30 mM HEPES buffer pH 7.0. Well solution - 18% PEG 8000, 200 mM (NH4)2SO4, 50 mM HEPES pH 7, 3 mM CaCl2 and 6 ...Details: protein solution - 60 mg/ml trypsin, 6 mg/ml benzamidine and 3 mM CaCl2 in a 30 mM HEPES buffer pH 7.0. Well solution - 18% PEG 8000, 200 mM (NH4)2SO4, 50 mM HEPES pH 7, 3 mM CaCl2 and 6 mg/ml benzamidine. 1:1 ratio drops

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P14 (MX2) / Wavelength: 0.8856 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 23, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8856 Å / Relative weight: 1
ReflectionResolution: 1.16→43.12 Å / Num. obs: 129370 / % possible obs: 94.6 % / Redundancy: 3.564 % / Biso Wilson estimate: 13.461 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.102 / Rrim(I) all: 0.119 / Χ2: 1.233 / Net I/σ(I): 7.91 / Num. measured all: 461067
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.16-1.191.660.7760.8472861014743880.3171.0243.2
1.19-1.222.5470.7021.3223021986590400.4910.86691.6
1.22-1.263.1860.6231.8230173957794710.6060.74498.9
1.26-1.293.6420.5532.3433929937493170.710.64899.4
1.29-1.343.7930.4762.9433799896089110.7630.55599.5
1.34-1.383.8090.4063.5333369880487610.8390.47399.5
1.38-1.443.8110.3484.231804838883450.870.40599.5
1.44-1.493.8190.2895.1730836810780750.9150.33699.6
1.49-1.563.8260.2496.129608776377380.9350.2999.7
1.56-1.643.8240.2117.3428534748274610.950.24599.7
1.64-1.733.7930.1788.5326493702769850.9640.20799.4
1.73-1.833.8560.14610.2625664670066550.9740.16999.3
1.83-1.963.8610.11512.7623875623861830.9820.13499.1
1.96-2.113.7760.09114.9321926586058060.9890.10699.1
2.11-2.313.7280.07816.4419838537553210.9920.09299
2.31-2.593.5780.06717.717275488248280.9920.07998.9
2.59-2.993.3510.05918.5614103427942080.9940.0798.3
2.99-3.663.7320.0522.6313400362735910.9960.05899
3.66-5.183.8110.04225.0710559278927710.9970.04899.4
5.18-43.123.680.04224.595575152915150.9980.04999.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 418G

418g


Resolution: 1.16→43.12 Å / Cross valid method: FREE R-VALUE
RfactorNum. reflection% reflection
Rfree0.19223 --
Rwork0.15034 --
obs-66489 95.96 %
Displacement parametersBiso mean: 12.975 Å2
Refinement stepCycle: LAST / Resolution: 1.16→43.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1629 0 20 288 1937

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