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- PDB-1n1x: Crystal Structure Analysis of the monomeric [S-carboxyamidomethyl... -

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Basic information

Entry
Database: PDB / ID: 1n1x
TitleCrystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] Bovine seminal ribonuclease
ComponentsRibonuclease, seminal
KeywordsHYDROLASE
Function / homology
Function and homology information


pancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / metabolic process / nucleic acid binding / lyase activity / defense response to Gram-positive bacterium / extracellular region / identical protein binding
Similarity search - Function
P-30 Protein / Ribonuclease A-like domain / Pancreatic ribonuclease / Ribonuclease A, active site / Ribonuclease A-domain / Ribonuclease A-like domain superfamily / Pancreatic ribonuclease / Pancreatic ribonuclease family signature. / Pancreatic ribonuclease / Roll / Alpha Beta
Similarity search - Domain/homology
Seminal ribonuclease
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsSica, F. / Di Fiore, A. / Zagari, A. / Mazzarella, L.
Citation
Journal: Proteins / Year: 2003
Title: The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative
Authors: Sica, F. / Di Fiore, A. / Zagari, A. / Mazzarella, L.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1993
Title: Bovine seminal ribonuclease: structure at 1.9 A resolution
Authors: Mazzarella, L. / Capasso, S. / Demasi, D. / Di Lorenzo, G. / Mattia, C.A. / Zagari, A.
#2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1995
Title: Swapping structural determinants of ribonucleases: an energetic analysis of the hinge peptide 16-22
Authors: Mazzarella, L. / Vitagliano, L. / Zagari, A.
#3: Journal: J.CRYST.GROWTH / Year: 1999
Title: Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state.
Authors: Sica, F. / Adinolfi, S. / Berisio, R. / De Lorenzo, C. / Mazzarella, L. / Piccoli, R. / Vitagliano, L. / Zagari, A.
#4: Journal: Eur.J.Biochem. / Year: 1995
Title: Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra
Authors: D'Ursi, A. / Oschkinat, H. / Cieslar, C. / Picone, D. / D'Alessio, G. / Amodeo, P. / Temussi, P.
History
DepositionOct 21, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 26, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Ribonuclease, seminal


Theoretical massNumber of molelcules
Total (without water)13,7471
Polymers13,7471
Non-polymers00
Water2,630146
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)70.39, 28.73, 67.41
Angle α, β, γ (deg.)90.00, 119.0, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Ribonuclease, seminal / Seminal RNase / Ribonuclease BS-1


Mass: 13746.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: seminal fluid / Source: (natural) Bos taurus (cattle) / References: UniProt: P00669, EC: 3.1.27.5
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 146 / 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: 2.22 Å3/Da / Density % sol: 43.25 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.7
Details: PEG 4000, TRIS-HCl, sodium acetate, acetonitrile, glycerol (cryoprotectant), pH 8.7, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K
Crystal grow
*PLUS
Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
17.5 mg/mlprotein1drop
228 %(w/v)PEG40001reservoir
30.1 MTris-HCl1reservoirpH8.7
40.2 Msodium acetate1reservoir
515 %(v/v)acetonitrile1reservoirpH8.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.45→18 Å / Num. all: 21157 / Num. obs: 21157 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 14.73 Å2 / Rmerge(I) obs: 0.028 / Net I/σ(I): 42
Reflection shellResolution: 1.45→1.47 Å / Rmerge(I) obs: 0.076 / Mean I/σ(I) obs: 17 / % possible all: 99.1
Reflection
*PLUS
Num. measured all: 93751
Reflection shell
*PLUS
% possible obs: 99.1 %

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLOR3.851refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1BSR

1bsr


Resolution: 1.45→18 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.258 2044 10 %RANDOM
Rwork0.205 ---
all0.207 21157 --
obs0.207 20831 99.5 %-
Displacement parametersBiso mean: 17.8 Å2
Refinement stepCycle: LAST / Resolution: 1.45→18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms955 0 0 146 1101
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.017
X-RAY DIFFRACTIONx_angle_deg1.8
X-RAY DIFFRACTIONx_dihedral_angle_d25.5
LS refinement shellResolution: 1.45→1.47 Å
RfactorNum. reflection% reflection
Rfree0.29 98 -
Rwork0.271 --
obs--99.1 %
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.5

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