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- PDB-5i6n: Crystal Structure of Copper Nitrite Reductase at 100K after 11.73 MGy -

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Basic information

Entry
Database: PDB / ID: 5i6n
TitleCrystal Structure of Copper Nitrite Reductase at 100K after 11.73 MGy
ComponentsCopper-containing nitrite reductase
KeywordsOXIDOREDUCTASE / Copper Nitrite Reductase / Reaction Mechanism / Serial Crystallography
Function / homology
Function and homology information


denitrification pathway / nitrite reductase (NO-forming) / nitrite reductase (NO-forming) activity / nitrate assimilation / periplasmic space / copper ion binding
Similarity search - Function
Nitrite reductase, copper-type / Multicopper oxidase, type 1 / Multicopper oxidase / Multicopper oxidase, N-terminal / Multicopper oxidase / Cupredoxins - blue copper proteins / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Cupredoxin / Immunoglobulin-like ...Nitrite reductase, copper-type / Multicopper oxidase, type 1 / Multicopper oxidase / Multicopper oxidase, N-terminal / Multicopper oxidase / Cupredoxins - blue copper proteins / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Cupredoxin / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / NITRIC OXIDE / NITRITE ION / Copper-containing nitrite reductase
Similarity search - Component
Biological speciesAchromobacter cycloclastes (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.22 Å
AuthorsHorrell, S. / Hough, M.A. / Strange, R.W.
CitationJournal: Iucrj / Year: 2016
Title: Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal.
Authors: Horrell, S. / Antonyuk, S.V. / Eady, R.R. / Hasnain, S.S. / Hough, M.A. / Strange, R.W.
History
DepositionFeb 16, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jul 13, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2016Group: Database references
Revision 1.2Sep 21, 2016Group: Database references
Revision 1.3Sep 28, 2016Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Copper-containing nitrite reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,82410
Polymers36,3911
Non-polymers4339
Water4,684260
1
A: Copper-containing nitrite reductase
hetero molecules

A: Copper-containing nitrite reductase
hetero molecules

A: Copper-containing nitrite reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)110,47230
Polymers109,1733
Non-polymers1,29927
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_555z,x,y1
crystal symmetry operation9_555y,z,x1
Buried area14890 Å2
ΔGint-76 kcal/mol
Surface area34020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)95.192, 95.192, 95.192
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number198
Space group name H-MP213
Components on special symmetry positions
IDModelComponents
11A-848-

HOH

21A-859-

HOH

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Components

#1: Protein Copper-containing nitrite reductase / Cu-NIR


Mass: 36391.008 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Achromobacter cycloclastes (bacteria) / Gene: nirK / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P25006, nitrite reductase (NO-forming)
#2: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#3: Chemical ChemComp-NO / NITRIC OXIDE / Nitrogen monoxide / Nitric oxide


Mass: 30.006 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: NO
#4: Chemical
ChemComp-NO2 / NITRITE ION / Nitrite


Mass: 46.005 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: NO2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 260 / 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: 1.99 Å3/Da / Density % sol: 38.2 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 1.7 M Ammonium Sulphate, 0.1 M Sodium Acetate pH 4.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 1.2→42.57 Å / Num. obs: 86878 / % possible obs: 97.5 % / Redundancy: 4.1 % / CC1/2: 0.999 / Rmerge(I) obs: 0.04 / Rpim(I) all: 0.021 / Rrim(I) all: 0.045 / Net I/σ(I): 16.7 / Num. measured all: 356830
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique allCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.2-1.223.91.2611728744200.4850.711.4551.199.7
6.57-42.574.70.02224015160.9980.0110.02575.487.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0135refinement
Aimless0.5.17data scaling
PDB_EXTRACT3.2data extraction
XDSdata reduction
REFMACphasing
RefinementResolution: 1.22→42.6 Å / Cor.coef. Fo:Fc: 0.978 / Cor.coef. Fo:Fc free: 0.969 / SU B: 1.346 / SU ML: 0.026 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.04 / ESU R Free: 0.041 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1652 4148 5 %RANDOM
Rwork0.1303 ---
obs0.132 78412 96.73 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 120.86 Å2 / Biso mean: 17.719 Å2 / Biso min: 9.68 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: final / Resolution: 1.22→42.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2566 0 22 262 2850
Biso mean--34.79 29.39 -
Num. residues----332
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0192852
X-RAY DIFFRACTIONr_bond_other_d0.0020.022648
X-RAY DIFFRACTIONr_angle_refined_deg1.6771.953869
X-RAY DIFFRACTIONr_angle_other_deg0.99436114
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.675359
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.09524.462130
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.01515446
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.11512
X-RAY DIFFRACTIONr_chiral_restr0.110.2421
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0213242
X-RAY DIFFRACTIONr_gen_planes_other0.0030.02640
X-RAY DIFFRACTIONr_mcbond_it1.4591.4851416
X-RAY DIFFRACTIONr_mcbond_other1.441.4821414
X-RAY DIFFRACTIONr_mcangle_it1.7962.2361772
X-RAY DIFFRACTIONr_rigid_bond_restr2.6635497
X-RAY DIFFRACTIONr_sphericity_free22.436560
X-RAY DIFFRACTIONr_sphericity_bonded8.42655623
LS refinement shellResolution: 1.22→1.252 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.282 333 -
Rwork0.265 5892 -
all-6225 -
obs--99.7 %

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