Component-ID: _ / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: ILE / End label comp-ID: ILE / Refine code: _ / Auth seq-ID: 3 - 233 / Label seq-ID: 4 - 234
Dom-ID
Ens-ID
Auth asym-ID
Label asym-ID
1
1
A
A
2
1
B
B
1
2
A
A
2
2
C
C
1
3
A
A
2
3
D
D
NCS ensembles :
ID
1
2
3
-
Components
#1: Protein
NUCLEOCAPSIDPROTEIN
Mass: 26295.369 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SCHMALLENBERG VIRUS Description: CODON-OPTIMISED CDNA ENCODING THE SBV NUCLEOCAPSID PROTEIN WAS CHEMICALLY SYNTHESISED (DUNDEE CELL PRODUCTS). Variant: BH80/11-1 ISOLATE / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIL / References: UniProt: H2AM13
Mass: 18.015 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE INITIAL AMINO ACID (S)IS THE REMNANT OF CUTTING AN N- TERMINAL 6-HIS-SUMO TAG OFF BY USING U1P ...THE INITIAL AMINO ACID (S)IS THE REMNANT OF CUTTING AN N- TERMINAL 6-HIS-SUMO TAG OFF BY USING U1P SUMO PROTEASE.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.31 Å3/Da / Density % sol: 46.88 % Description: THE MOLECULAR REPLACEMENT MODEL CAME FROM A LOWER RESOLUTION STRUCTURE SOLVED VIA SAD FROM A CRYSTAL OF SELENOMETHIONINE-SUBSTITUTED SBV NUCLEOCAPSID PROTEIN.
Crystal grow
pH: 8 Details: CRYSTALLISATION CONDITION: 17% PEG10000, 100 MM BIS-TRIS PH 5.5, 100 MM AMMONIUM ACETATE. CRYO CONDITION: 20% GLYCEROL
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9464 Å / Relative weight: 1
Reflection twin
Crystal-ID
ID
Operator
Domain-ID
Fraction
1
1
H, K, L
1
0.652
1
1
-h,-k,l
2
0.348
Reflection
Resolution: 3.2→61.59 Å / Num. obs: 24459 / % possible obs: 99.8 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 8.7
Reflection shell
Resolution: 2.75→2.9 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 2 / % possible all: 100
-
Processing
Software
Name
Version
Classification
REFMAC
5.7.0029
refinement
MOSFLM
datareduction
Aimless
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: SBV NUCLEOCAPSID PROTEIN Resolution: 2.75→61.59 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.942 / SU B: 18.302 / SU ML: 0.187 / Cross valid method: THROUGHOUT / ESU R Free: 0.066 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.20129
1219
5 %
RANDOM
Rwork
0.16411
-
-
-
obs
0.16601
23228
99.72 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK