[English] 日本語
Yorodumi
- PDB-5f5t: Crystal structure of the Prp38-MFAP1 complex of Chaetomium thermo... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5f5t
TitleCrystal structure of the Prp38-MFAP1 complex of Chaetomium thermophilum
Components(Putative uncharacterized protein) x 2
KeywordsSPLICING / B-specific protein / pre-mRNA splicing / SAH / TRANSCRIPTION
Function / homology
Function and homology information


U2-type spliceosomal complex / precatalytic spliceosome / mRNA splicing, via spliceosome / RNA binding
Similarity search - Function
Micro-fibrillar-associated protein 1, C-terminal / Microfibrillar-associated protein 1 / Microfibril-associated/Pre-mRNA processing / Pre-mRNA-splicing factor 38 / PRP38 family
Similarity search - Domain/homology
Pre-mRNA-splicing factor 38 / Micro-fibrillar-associated protein 1 C-terminal domain-containing protein
Similarity search - Component
Biological speciesChaetomium thermophilum (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.55 Å
AuthorsUlrich, A.K.C. / Wahl, M.C.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationWA1126/7-1 Germany
CitationJournal: Structure / Year: 2016
Title: Scaffolding in the Spliceosome via Single alpha Helices.
Authors: Ulrich, A.K.C. / Seeger, M. / Schutze, T. / Bartlick, N. / Wahl, M.C.
History
DepositionDec 4, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Oct 12, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 6, 2017Group: Author supporting evidence / Data collection / Category: diffrn_source / pdbx_audit_support
Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_audit_support.funding_organization
Revision 1.2Apr 18, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_id_ISSN / _citation.journal_volume ..._citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Jan 10, 2024Group: 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_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Putative uncharacterized protein
B: Putative uncharacterized protein
C: Putative uncharacterized protein
D: Putative uncharacterized protein


Theoretical massNumber of molelcules
Total (without water)71,5134
Polymers71,5134
Non-polymers00
Water2,504139
1
A: Putative uncharacterized protein
C: Putative uncharacterized protein


Theoretical massNumber of molelcules
Total (without water)35,7572
Polymers35,7572
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint-1 kcal/mol
Surface area16900 Å2
MethodPISA
2
B: Putative uncharacterized protein
D: Putative uncharacterized protein


Theoretical massNumber of molelcules
Total (without water)35,7572
Polymers35,7572
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2110 Å2
ΔGint-0 kcal/mol
Surface area15110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)195.550, 52.150, 104.600
Angle α, β, γ (deg.)90.000, 102.510, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: PRO / Beg label comp-ID: PRO

Dom-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1ASPASPchain AAA4 - 2187 - 221
2GLUGLUchain BBB4 - 2177 - 220

-
Components

#1: Protein Putative uncharacterized protein


Mass: 25617.205 Da / Num. of mol.: 2 / Fragment: NTR
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: CTHT_0013190 / Plasmid: pETM11 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): RIL / References: UniProt: G0S1D3
#2: Protein Putative uncharacterized protein


Mass: 10139.329 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum (fungus) / Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: CTHT_0069660 / Plasmid: pETM11 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): RIL / References: UniProt: G0SHD7
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 139 / 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: 3.64 Å3/Da / Density % sol: 66.21 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion / pH: 8.5
Details: 0.1 M Tris-HCl, pH 8.5, 0.2 M ammonium acetate, and 20 % (v/v) isopropanol

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P14 (MX2) / Wavelength: 0.976 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 22, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976 Å / Relative weight: 1
ReflectionResolution: 2.55→95.454 Å / Num. obs: 33726 / % possible obs: 98.9 % / Redundancy: 3.8 % / Rsym value: 0.044 / Net I/σ(I): 17.9
Reflection shellResolution: 2.55→2.62 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 1.9 / % possible all: 98.4

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.15data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4rz9
Resolution: 2.55→95.454 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 26.98 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2233 1706 5.06 %Random selection
Rwork0.1955 32013 --
obs0.1969 33719 98.9 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 292.36 Å2 / Biso mean: 102.4795 Å2 / Biso min: 35.71 Å2
Refinement stepCycle: final / Resolution: 2.55→95.454 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4418 0 0 139 4557
Biso mean---87.93 -
Num. residues----537
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0034493
X-RAY DIFFRACTIONf_angle_d0.8146043
X-RAY DIFFRACTIONf_chiral_restr0.033648
X-RAY DIFFRACTIONf_plane_restr0.004799
X-RAY DIFFRACTIONf_dihedral_angle_d14.8571775
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2034X-RAY DIFFRACTION13.221TORSIONAL
12B2034X-RAY DIFFRACTION13.221TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.55-2.62510.32291290.31032633276298
2.6251-2.70980.3671480.29222641278999
2.7098-2.80670.30831380.29752635277399
2.8067-2.91910.27831330.26332662279599
2.9191-3.05190.30511330.2262664279799
3.0519-3.21280.24691180.22672668278699
3.2128-3.41410.2681400.20962664280499
3.4141-3.67770.24411420.19312647278998
3.6777-4.04790.16891420.16132692283499
4.0479-4.63360.18111440.15212677282199
4.6336-5.83770.21511720.18232680285299
5.8377-95.52130.20531670.19582750291798
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.09140.9917-4.37775.6961-3.20335.99010.05392.9519-0.5397-0.6439-0.0664-1.64321.30141.0148-0.15291.4287-0.0471-0.20611.8801-0.33281.2588235.9104-29.8655-17.2825
26.54360.3191-0.96624.6216-0.19846.4569-0.26620.5701-0.4047-0.69110.3358-0.40060.0182-0.0823-0.05260.5073-0.1070.07410.5228-0.09090.5026241.366-23.1282-7.3159
31.02030.6585-1.12678.4898-4.32855.7736-0.38370.28850.35680.2616-0.11270.0234-0.46810.34690.38630.46230.0569-0.04380.53260.0060.6231238.0967-13.389-1.169
44.98640.5136-2.8592.4025-0.72064.8897-0.33180.2483-0.4087-0.26850.2211-0.04920.9937-0.40590.0610.4508-0.0537-0.04890.4096-0.07270.5029231.5778-30.98272.3026
57.00730.38850.9331.82410.26725.25860.070.15350.4489-0.09660.02640.590.1373-0.6722-0.0880.38970.0244-0.02340.46550.0230.522222.322-23.4576.7441
64.03311.399-0.05448.49964.81572.90841.1506-0.3741-0.29973.10640.2493-0.50770.248-1.1071-0.81481.75550.01070.01041.55880.12781.23213.3686-24.698333.6192
75.86543.62314.97886.9117-0.59939.61852.1392-2.8892-0.04481.977-0.4297-1.2693-0.6236-1.8194-1.33312.23160.14340.32841.9037-0.2721.5731217.4412-2.392862.7029
84.74350.81890.09884.44650.37891.7128-0.5704-1.14650.14382.00740.52350.8506-0.0773-0.43820.04081.52730.21910.4551.2059-0.00890.829217.8097-13.088157.8732
94.650.83360.52483.22912.3154.91940.0438-0.43320.44080.90220.23630.0432-1.68060.0332-0.2521.4530.02760.10190.7147-0.09270.5326228.9026-6.144450.7169
107.54580.61390.69613.01171.04138.17310.2636-0.24250.44820.29740.08690.2386-0.8958-0.6542-0.37920.81070.18080.10480.4744-0.01350.5139221.9994-7.271138.0645
113.81470.0617-0.52462.51471.51981.14480.75470.00040.5879-0.2904-0.22321.167-1.0198-1.6325-0.43791.00280.41430.21571.20790.09091.0465209.311-3.624435.1181
127.3469-2.90850.34812.07631.61917.8644-0.74540.53910.7984-1.27221.01-0.0867-0.63640.77060.06771.6255-0.0709-0.1371.80470.11841.1947218.8514-5.84418.1816
132.4961-0.8114-2.1269.02014.07113.3346-2.0460.78483.0929-1.15141.9708-0.98910.22361.13-0.1311.1586-0.3177-0.39731.4883-0.08511.4706238.6819-18.507719.7827
146.34780.52643.86020.07320.22951.48080.1104-0.2490.823-0.1386-0.29530.3810.1828-0.54520.2110.52210.069-0.06531.0771-0.05480.8218201.4075-19.52199.5602
152.5215-2.47351.60278.12291.98353.5530.499-2.0976-2.42160.09391.69171.0929-1.9321-0.3887-2.01951.07130.3446-0.03881.4688-0.08321.7268236.6578-12.12229.089
161.8526-0.0587-1.72623.9071.28872.22190.41260.11240.7996-0.1723-0.39081.5065-0.361-1.1668-0.30080.77090.2689-0.02381.1997-0.03321.1023208.0668-10.226422.9075
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 30 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 31 through 68 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 69 through 83 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 84 through 142 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 143 through 202 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 203 through 218 )A0
7X-RAY DIFFRACTION7chain 'B' and (resid 6 through 30 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 31 through 45 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 46 through 112 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 113 through 169 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 170 through 202 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 203 through 217 )B0
13X-RAY DIFFRACTION13chain 'C' and (resid 215 through 222 )C0
14X-RAY DIFFRACTION14chain 'C' and (resid 223 through 277 )C0
15X-RAY DIFFRACTION15chain 'D' and (resid 216 through 222 )D0
16X-RAY DIFFRACTION16chain 'D' and (resid 223 through 259 )D0

+
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://pdbjlvh1.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