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- PDB-3oqz: Semi-synthetic ribonuclease S: meta-cyano-phenylalanine at position 8 -

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Basic information

Entry
Database: PDB / ID: 3oqz
TitleSemi-synthetic ribonuclease S: meta-cyano-phenylalanine at position 8
Components(Ribonuclease pancreaticPancreatic ribonuclease family) x 2
KeywordsHYDROLASE / artificial / non-natural / vibrational / probe / nitrile / cyano / cyanophenylalanine
Function / homology
Function and homology information


pancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / lyase activity / defense response to Gram-positive bacterium / extracellular region
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
Ribonuclease pancreatic
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsFafarman, A.T. / Boxer, S.G.
CitationJournal: J.Phys.Chem.B / Year: 2010
Title: Nitrile bonds as infrared probes of electrostatics in ribonuclease S.
Authors: Fafarman, A.T. / Boxer, S.G.
History
DepositionSep 4, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 20, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
a: Ribonuclease pancreatic
A: Ribonuclease pancreatic
b: Ribonuclease pancreatic
B: Ribonuclease pancreatic


Theoretical massNumber of molelcules
Total (without water)26,6684
Polymers26,6684
Non-polymers00
Water25214
1
a: Ribonuclease pancreatic
A: Ribonuclease pancreatic


Theoretical massNumber of molelcules
Total (without water)13,3342
Polymers13,3342
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
b: Ribonuclease pancreatic
B: Ribonuclease pancreatic


Theoretical massNumber of molelcules
Total (without water)13,3342
Polymers13,3342
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)99.850, 31.679, 69.171
Angle α, β, γ (deg.)90.00, 90.93, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein/peptide Ribonuclease pancreatic / Pancreatic ribonuclease family / RNase 1 / RNase A


Mass: 1777.954 Da / Num. of mol.: 2 / Fragment: UNP residues 27-41 / Source method: obtained synthetically / Details: Made by solid phase peptide synthesis / Source: (synth.) Bos taurus (cattle) / References: UniProt: P61823, EC: 3.1.27.5
#2: Protein Ribonuclease pancreatic / Pancreatic ribonuclease family / RNase 1 / RNase A


Mass: 11555.981 Da / Num. of mol.: 2 / Fragment: UNP residues 47-150 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P61823, EC: 3.1.27.5
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 14 / 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: 2.05 Å3/Da / Density % sol: 40.03 %
Crystal growTemperature: 279 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 25% PEG 4000, 0.08M ammonium acetate, 0.1 M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 279K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å
DetectorDate: Mar 15, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.5→69.171 Å / Num. all: 7887 / Num. obs: 7757 / % possible obs: 99.9 % / Redundancy: 3.2 % / Biso Wilson estimate: 38.8 Å2

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1RNV

1rnv


Resolution: 2.5→40.792 Å / SU ML: 0.46 / σ(F): 1.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.268 356 4.59 %5%, random
Rwork0.2038 ---
obs0.2067 7753 99.83 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.604 Å2 / ksol: 0.384 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--3.8517 Å20 Å22.3524 Å2
2--11.5454 Å2-0 Å2
3----7.6937 Å2
Refinement stepCycle: LAST / Resolution: 2.5→40.792 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1832 0 0 14 1846
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0071900
X-RAY DIFFRACTIONf_angle_d1.0452560
X-RAY DIFFRACTIONf_dihedral_angle_d18.095704
X-RAY DIFFRACTIONf_chiral_restr0.069278
X-RAY DIFFRACTIONf_plane_restr0.012340
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5-2.86170.27561220.23632426X-RAY DIFFRACTION100
2.8617-3.60510.31741170.21112446X-RAY DIFFRACTION100
3.6051-40.79760.22591170.17952525X-RAY DIFFRACTION100

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