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- PDB-6l3q: Crystal structure of Chaetomium thermophilum Utp15 C terminal domain -

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Basic information

Entry
Database: PDB / ID: 6l3q
TitleCrystal structure of Chaetomium thermophilum Utp15 C terminal domain
ComponentsWD_REPEATS_REGION domain-containing protein
KeywordsNUCLEAR PROTEIN / 90S preribosome
Function / homology
Function and homology information


rRNA processing / nucleolus
Similarity search - Function
U3 small nucleolar RNA-associated protein 15, C-terminal / UTP15 C terminal / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. ...U3 small nucleolar RNA-associated protein 15, C-terminal / UTP15 C terminal / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
U3 small nucleolar RNA-associated protein 15 C-terminal domain-containing protein
Similarity search - Component
Biological speciesChaetomium thermophilum var. thermophilum DSM 1495 (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.702 Å
AuthorsChen, R.C. / Ye, K.Q.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China91540201 China
CitationJournal: To Be Published
Title: Crystal structure of Chaetomium thermophilum Utp15 C terminal domain
Authors: Chen, R.C. / Ye, K.Q.
History
DepositionOct 14, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 15, 2020Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: WD_REPEATS_REGION domain-containing protein
B: WD_REPEATS_REGION domain-containing protein


Theoretical massNumber of molelcules
Total (without water)31,3672
Polymers31,3672
Non-polymers00
Water36020
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2170 Å2
ΔGint-17 kcal/mol
Surface area13470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.188, 106.188, 59.081
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein WD_REPEATS_REGION domain-containing protein


Mass: 15683.536 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum var. thermophilum DSM 1495 (fungus)
Strain: DSM 1495 / Gene: CTHT_0063870 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: G0SEI5
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 3.07 Å3/Da / Density % sol: 59.88 %
Crystal growTemperature: 293.15 K / Method: evaporation / pH: 6.5 / Details: 1.6M MgSO4, 0.1M Mes / PH range: 6.0-8.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 25, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 20360 / % possible obs: 99.9 % / Redundancy: 21.3 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 35.93
Reflection shellResolution: 2.7→2.75 Å / Mean I/σ(I) obs: 17.95 / Num. unique obs: 512 / CC1/2: 0.998

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Processing

Software
NameVersionClassification
PHENIX1.8.1_1168refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.702→36.286 Å / FOM work R set: 0.8188 / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 25.06 / Stereochemistry target values: ML
Details: SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS COLUMNS.
RfactorNum. reflection% reflection
Rfree0.2407 2053 10.08 %
Rwork0.1986 18307 -
obs0.2028 20360 99.75 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 149.14 Å2 / Biso mean: 36.02 Å2 / Biso min: 14.14 Å2
Refinement stepCycle: final / Resolution: 2.702→36.286 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1999 0 0 20 2019
Biso mean---25.24 -
Num. residues----254
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0082035
X-RAY DIFFRACTIONf_angle_d1.0622763
X-RAY DIFFRACTIONf_chiral_restr0.071321
X-RAY DIFFRACTIONf_plane_restr0.005353
X-RAY DIFFRACTIONf_dihedral_angle_d14.741745
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.7021-2.76490.36141360.25871207100
2.7649-2.8340.31460.25841234100
2.834-2.91060.28561340.23261215100
2.9106-2.99620.31941360.24391205100
2.9962-3.09290.28741340.23451219100
3.0929-3.20340.31411400.23091239100
3.2034-3.33160.30651420.21281236100
3.3316-3.48310.28441320.21891221100
3.4831-3.66650.30471340.19711233100
3.6665-3.8960.20911320.18361224100
3.896-4.19640.19221420.16911227100
4.1964-4.6180.1831360.17331226100
4.618-5.28440.22011420.18151223100
5.2844-6.65110.22131440.20651215100
6.6511-36.280.19071230.1726118396

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