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- PDB-5r46: Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, roo... -

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Basic information

Entry
Database: PDB / ID: 5r46
TitleCrystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, room temperature
Components
  • (gamma-chymotrypsin) x 3
  • peptide SWPW
  • peptide TPGVY
KeywordsHYDROLASE / serine protease / hydrolase-peptide complex
Function / homology
Function and homology information


chymotrypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase activity / proteolysis / extracellular region
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 family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
IODIDE ION / Chymotrypsinogen A
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.05 Å
AuthorsKreinbring, C.A. / Wilson, M.A. / Kovalevsky, A.Y. / Blakeley, M.P. / Fisher, S.Z. / Lazar, L.M. / Moulin, A.G. / Novak, W.R. / Petsko, G.A. / Ringe, D.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM32415 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM26788 United States
CitationJournal: To be published
Title: Effect of Temperature and pH on Ionizable Residues in gamma-Chymotrypsin: a X-ray and Neutron Crystallography Study
Authors: Kreinbring, C.A. / Wilson, M.A. / Kovalevsky, A.Y. / Blakeley, M.P. / Fisher, S.Z. / Lazar, L.M. / Moulin, A.G. / Novak, W.R. / Petsko, G.A. / Ringe, D.
History
DepositionFeb 18, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 1, 2021Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: gamma-chymotrypsin
B: gamma-chymotrypsin
C: gamma-chymotrypsin
D: peptide SWPW
E: peptide TPGVY
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,6928
Polymers26,3735
Non-polymers3193
Water2,972165
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)69.447, 69.447, 97.863
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number94
Space group name H-MP42212
Components on special symmetry positions
IDModelComponents
11B-201-

IOD

21B-343-

HOH

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Components

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Protein/peptide , 3 types, 3 molecules ADE

#1: Protein/peptide gamma-chymotrypsin


Mass: 1253.511 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin
#4: Protein/peptide peptide SWPW


Mass: 574.627 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle)
#5: Protein/peptide peptide TPGVY


Mass: 535.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle)

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Protein , 2 types, 2 molecules BC

#2: Protein gamma-chymotrypsin


Mass: 13934.556 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin
#3: Protein gamma-chymotrypsin


Mass: 10074.495 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin

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Non-polymers , 3 types, 168 molecules

#6: Chemical ChemComp-IOD / IODIDE ION


Mass: 126.904 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: I
#7: Chemical ChemComp-SO4 / SULFATE ION


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


Mass: 18.015 Da / Num. of mol.: 165 / 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: 2.24 Å3/Da / Density % sol: 45.02 %
Crystal growTemperature: 297 K / Method: vapor diffusion, sitting drop
Details: 45% saturated ammonium sulfate, 0.75% saturated cetyltrimethylammonium bromide, 100 mM sodium iodide; sodium malonate
PH range: 10 mM sodium cacodylate pH 6.0

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Data collection

DiffractionMean temperature: 297 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.9 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jul 15, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.05→50 Å / Num. obs: 111717 / % possible obs: 99.6 % / Redundancy: 39.3 % / Rmerge(I) obs: 0.109 / Χ2: 1.125 / Net I/σ(I): 13.1 / Num. measured all: 4389000
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsΧ2Diffraction-ID% possible all
1.05-1.0950.726106591.864196.2
1.09-1.1311.40.629110271.356199.8
1.13-1.18240.59110741.3351100
1.18-1.24360.557111081.3111100
1.24-1.3245.20.492111251.5131100
1.32-1.4351.80.367111521.0031100
1.43-1.5755.80.253111820.9931100
1.57-1.856.90.147112580.9961100
1.8-2.2657.10.107113631.021100
2.26-5046.80.087117690.986199.6

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Processing

Software
NameVersionClassificationNB
HKL-2000data reduction
SCALEPACKdata scaling
REFMAC5.8.0158refinement
PDB_EXTRACT3.25data extraction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 1GCT

1gct


Resolution: 1.05→56.64 Å / Cor.coef. Fo:Fc: 0.984 / Cor.coef. Fo:Fc free: 0.982 / SU B: 0.484 / SU ML: 0.011 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.019 / ESU R Free: 0.018 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1216 5564 5 %RANDOM
Rwork0.1108 ---
obs0.1113 104954 98.78 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 107.66 Å2 / Biso mean: 17.772 Å2 / Biso min: 8.97 Å2
Baniso -1Baniso -2Baniso -3
1-0.09 Å20 Å20 Å2
2--0.09 Å20 Å2
3----0.19 Å2
Refinement stepCycle: final / Resolution: 1.05→56.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1817 0 11 165 1993
Biso mean--31.49 37.6 -
Num. residues----245
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.021991
X-RAY DIFFRACTIONr_bond_other_d0.0030.021829
X-RAY DIFFRACTIONr_angle_refined_deg1.5431.9482751
X-RAY DIFFRACTIONr_angle_other_deg1.44734289
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6935277
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.12525.53865
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.99415317
X-RAY DIFFRACTIONr_dihedral_angle_4_deg8.966153
X-RAY DIFFRACTIONr_chiral_restr0.1050.2326
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0212228
X-RAY DIFFRACTIONr_gen_planes_other0.0040.02375
X-RAY DIFFRACTIONr_rigid_bond_restr1.98833817
X-RAY DIFFRACTIONr_sphericity_free28.9375130
X-RAY DIFFRACTIONr_sphericity_bonded8.32153793
LS refinement shellResolution: 1.05→1.077 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.253 405 -
Rwork0.224 6986 -
all-7391 -
obs--90.66 %

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