[English] 日本語
Yorodumi
- PDB-2pe8: Crystal structure of the UHM domain of human SPF45 (free form) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2pe8
TitleCrystal structure of the UHM domain of human SPF45 (free form)
ComponentsSplicing factor 45
KeywordsPROTEIN BINDING / RRM
Function / homology
Function and homology information


alternative mRNA splicing, via spliceosome / mRNA cis splicing, via spliceosome / mRNA Splicing - Major Pathway / spliceosomal complex / RNA binding / nucleoplasm
Similarity search - Function
SPF45, RNA recognition motif / Splicing factor 45 / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / RNA recognition motif domain, eukaryote / RNA recognition motif / RRM (RNA recognition motif) domain / RNA recognition motif ...SPF45, RNA recognition motif / Splicing factor 45 / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / RNA recognition motif domain, eukaryote / RNA recognition motif / RRM (RNA recognition motif) domain / RNA recognition motif / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsCorsini, L. / Basquin, J. / Hothorn, M. / Sattler, M.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2007
Title: U2AF-homology motif interactions are required for alternative splicing regulation by SPF45.
Authors: Corsini, L. / Bonna, S. / Basquin, J. / Hothorn, M. / Scheffzek, K. / Valcarcel, J. / Sattler, M.
History
DepositionApr 2, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 26, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Aug 30, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Splicing factor 45


Theoretical massNumber of molelcules
Total (without water)11,6901
Polymers11,6901
Non-polymers00
Water54030
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)63.900, 90.200, 99.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number22
Space group name H-MF222

-
Components

#1: Protein Splicing factor 45 / / 45 kDa-splicing factor / RNA-binding motif protein 17


Mass: 11690.481 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBM17, SPF45 / Plasmid: pETM30 / Production host: Escherichia coli (E. coli) / Strain (production host): K12 BL21(DE3) pLysS / References: UniProt: Q96I25
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 30 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.05 Å3/Da / Density % sol: 59.71 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 22% PEG 3,350, 0.2 M MgCl2, 0.1 M Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.976 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 1, 2005
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976 Å / Relative weight: 1
ReflectionResolution: 2→15 Å / Num. all: 9819 / Num. obs: 9819 / % possible obs: 99.5 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 7.57 % / Biso Wilson estimate: 46.5 Å2 / Rmerge(I) obs: 0.057 / Rsym value: 0.053 / Net I/σ(I): 20.13
Reflection shellResolution: 2→2.05 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.474 / Mean I/σ(I) obs: 4.67 / Num. unique all: 719 / Rsym value: 0.44 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
ADSCQuantumdata collection
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: UHM domain homology model based on PDB-ID 1o0p
Resolution: 2→19.58 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.956 / SU B: 12.328 / SU ML: 0.169 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): -3 / σ(I): -3 / ESU R: 0.169 / ESU R Free: 0.145 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24348 488 5 %RANDOM
Rwork0.23143 ---
all0.23204 9294 --
obs0.23204 9294 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 46.965 Å2
Baniso -1Baniso -2Baniso -3
1-3.65 Å20 Å20 Å2
2---0.39 Å20 Å2
3----3.27 Å2
Refinement stepCycle: LAST / Resolution: 2→19.58 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms761 0 0 30 791
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.022771
X-RAY DIFFRACTIONr_bond_other_d0.0010.02528
X-RAY DIFFRACTIONr_angle_refined_deg1.2361.9821037
X-RAY DIFFRACTIONr_angle_other_deg0.88231286
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.614599
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.96424.06232
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.49915133
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.04155
X-RAY DIFFRACTIONr_chiral_restr0.0660.2118
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02863
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02158
X-RAY DIFFRACTIONr_nbd_refined0.1960.2136
X-RAY DIFFRACTIONr_nbd_other0.1860.2518
X-RAY DIFFRACTIONr_nbtor_refined0.1680.2369
X-RAY DIFFRACTIONr_nbtor_other0.0810.2424
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1760.226
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1020.23
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2820.26
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0640.22
X-RAY DIFFRACTIONr_mcbond_it0.721.5642
X-RAY DIFFRACTIONr_mcbond_other0.1181.5207
X-RAY DIFFRACTIONr_mcangle_it0.8182788
X-RAY DIFFRACTIONr_scbond_it1.3913320
X-RAY DIFFRACTIONr_scangle_it1.9124.5249
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.416 32 -
Rwork0.357 669 -
obs--100 %
Refinement TLS params.Method: refined / Origin x: 15.6378 Å / Origin y: -6.1278 Å / Origin z: -11.5434 Å
111213212223313233
T-0.1143 Å20.1558 Å20.0131 Å2--0.2062 Å2-0.0514 Å2---0.2934 Å2
L7.0967 °2-1.4879 °2-2.0088 °2-10.7401 °2-1.0198 °2--10.6791 °2
S-0.6095 Å °-0.5825 Å °-0.2448 Å °1.0327 Å °0.4732 Å °0.0056 Å °-0.5017 Å °0.3891 Å °0.1363 Å °

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more