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- PDB-3tga: Crystal structure of L130R mutant of Nitrophorin 4 from Rhodnius ... -

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Basic information

Entry
Database: PDB / ID: 3tga
TitleCrystal structure of L130R mutant of Nitrophorin 4 from Rhodnius prolixus at pH 7.4
ComponentsNitrophorin-4
KeywordsMETAL BINDING PROTEIN / heme / lipocalin / nitrophorin
Function / homology
Function and homology information


nitrite dismutase / histamine binding / nitric oxide binding / vasodilation / oxidoreductase activity / extracellular region / metal ion binding
Similarity search - Function
Nitrophorin / Nitrophorin domain / Nitrophorin / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Nitrophorin-4
Similarity search - Component
Biological speciesRhodnius prolixus (insect)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å
AuthorsOgata, H. / He, C. / Knipp, M.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2012
Title: Guanidine-Ferroheme Coordination in the Mutant Protein Nitrophorin 4(L130R).
Authors: He, C. / Fuchs, M.R. / Ogata, H. / Knipp, M.
History
DepositionAug 17, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 30, 2012Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Nitrophorin-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9532
Polymers20,3371
Non-polymers6161
Water3,189177
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)69.890, 43.061, 52.585
Angle α, β, γ (deg.)90.00, 94.36, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-242-

HOH

21A-277-

HOH

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Components

#1: Protein Nitrophorin-4 / NP4


Mass: 20336.699 Da / Num. of mol.: 1 / Mutation: L130R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodnius prolixus (insect) / Production host: Escherichia coli (E. coli) / References: UniProt: Q94734
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 177 / 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: 1.94 Å3/Da / Density % sol: 36.59 %
Crystal growTemperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: Ammonium phosphate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 297K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.91841 Å
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Dec 15, 2010
RadiationMonochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91841 Å / Relative weight: 1
ReflectionResolution: 1.3→30.61 Å / Num. obs: 38430 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.035
Reflection shellResolution: 1.3→1.33 Å / Rmerge(I) obs: 0.312 / % possible all: 99.9

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Processing

Software
NameClassification
XDSdata scaling
MOLREPphasing
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.3→30.608 Å / SU ML: 0.13 / σ(F): 2 / Phase error: 14.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.172 1922 5 %RANDOM
Rwork0.1452 ---
obs0.1466 36507 99.85 %-
all-38429 --
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 44.182 Å2 / ksol: 0.428 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-3.1494 Å2-0 Å2-1.5029 Å2
2---1.453 Å2-0 Å2
3----1.6964 Å2
Refinement stepCycle: LAST / Resolution: 1.3→30.608 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1431 0 43 177 1651
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0071687
X-RAY DIFFRACTIONf_angle_d1.1222315
X-RAY DIFFRACTIONf_dihedral_angle_d12.419606
X-RAY DIFFRACTIONf_chiral_restr0.079243
X-RAY DIFFRACTIONf_plane_restr0.004304
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.3-1.33250.21351370.17232605X-RAY DIFFRACTION100
1.3325-1.36860.19671370.16012605X-RAY DIFFRACTION100
1.3686-1.40880.23851370.14872588X-RAY DIFFRACTION100
1.4088-1.45430.17151350.13772577X-RAY DIFFRACTION100
1.4543-1.50630.18131370.11552598X-RAY DIFFRACTION100
1.5063-1.56660.17481350.11482575X-RAY DIFFRACTION100
1.5666-1.63790.16151380.11372615X-RAY DIFFRACTION100
1.6379-1.72420.16591370.11872597X-RAY DIFFRACTION100
1.7242-1.83220.16531360.11832596X-RAY DIFFRACTION100
1.8322-1.97370.13921390.12482625X-RAY DIFFRACTION100
1.9737-2.17220.15011370.12642604X-RAY DIFFRACTION100
2.1722-2.48650.16721370.13932606X-RAY DIFFRACTION100
2.4865-3.13220.17351380.17182636X-RAY DIFFRACTION100
3.1322-30.61680.181420.16892680X-RAY DIFFRACTION100

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