[English] 日本語
Yorodumi
- PDB-3nfg: Crystal structure of Dimerization module of RNA polymerase I subc... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3nfg
TitleCrystal structure of Dimerization module of RNA polymerase I subcomplex A49/A34.5
Components
  • DNA-directed RNA polymerase I subunit RPA34
  • DNA-directed RNA polymerase I subunit RPA49
KeywordsTRANSCRIPTION / triple barrel / RNA polymerase / Dimerization
Function / homology
Function and homology information


termination of RNA polymerase I transcription / transcription initiation at RNA polymerase I promoter / transcription elongation by RNA polymerase I / RNA polymerase I complex / RNA polymerase I activity / DNA binding
Similarity search - Function
Double Stranded RNA Binding Domain - #70 / Double Stranded RNA Binding Domain / : / DNA-directed RNA polymerase I, subunit RPA34.5 / DNA-directed RNA polymerase I subunit RPA34.5 / RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor / Other non-globular / Special
Similarity search - Domain/homology
Candida glabrata strain CBS138 chromosome J complete sequence / Candida glabrata strain CBS138 chromosome I complete sequence
Similarity search - Component
Biological speciesCandida glabrata (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.51 Å
AuthorsGeiger, S.R.
CitationJournal: Mol.Cell / Year: 2010
Title: RNA Polymerase I Contains a TFIIF-Related DNA-Binding Subcomplex.
Authors: Geiger, S.R. / Lorenzen, K. / Schreieck, A. / Hanecker, P. / Kostrewa, D. / Heck, A.J. / Cramer, P.
History
DepositionJun 10, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DNA-directed RNA polymerase I subunit RPA49
B: DNA-directed RNA polymerase I subunit RPA34
C: DNA-directed RNA polymerase I subunit RPA49
D: DNA-directed RNA polymerase I subunit RPA34
E: DNA-directed RNA polymerase I subunit RPA49
F: DNA-directed RNA polymerase I subunit RPA34
G: DNA-directed RNA polymerase I subunit RPA49
H: DNA-directed RNA polymerase I subunit RPA34
I: DNA-directed RNA polymerase I subunit RPA49
J: DNA-directed RNA polymerase I subunit RPA34
K: DNA-directed RNA polymerase I subunit RPA49
L: DNA-directed RNA polymerase I subunit RPA34
M: DNA-directed RNA polymerase I subunit RPA49
N: DNA-directed RNA polymerase I subunit RPA34
O: DNA-directed RNA polymerase I subunit RPA49
P: DNA-directed RNA polymerase I subunit RPA34


Theoretical massNumber of molelcules
Total (without water)205,35616
Polymers205,35616
Non-polymers00
Water1,964109
1
A: DNA-directed RNA polymerase I subunit RPA49
B: DNA-directed RNA polymerase I subunit RPA34
O: DNA-directed RNA polymerase I subunit RPA49
P: DNA-directed RNA polymerase I subunit RPA34


Theoretical massNumber of molelcules
Total (without water)51,3394
Polymers51,3394
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17420 Å2
ΔGint-101 kcal/mol
Surface area22350 Å2
MethodPISA
2
C: DNA-directed RNA polymerase I subunit RPA49
D: DNA-directed RNA polymerase I subunit RPA34
I: DNA-directed RNA polymerase I subunit RPA49
J: DNA-directed RNA polymerase I subunit RPA34


Theoretical massNumber of molelcules
Total (without water)51,3394
Polymers51,3394
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17420 Å2
ΔGint-99 kcal/mol
Surface area22590 Å2
MethodPISA
3
E: DNA-directed RNA polymerase I subunit RPA49
F: DNA-directed RNA polymerase I subunit RPA34
G: DNA-directed RNA polymerase I subunit RPA49
H: DNA-directed RNA polymerase I subunit RPA34


Theoretical massNumber of molelcules
Total (without water)51,3394
Polymers51,3394
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17090 Å2
ΔGint-98 kcal/mol
Surface area22460 Å2
MethodPISA
4
K: DNA-directed RNA polymerase I subunit RPA49
L: DNA-directed RNA polymerase I subunit RPA34
M: DNA-directed RNA polymerase I subunit RPA49
N: DNA-directed RNA polymerase I subunit RPA34


Theoretical massNumber of molelcules
Total (without water)51,3394
Polymers51,3394
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17100 Å2
ΔGint-100 kcal/mol
Surface area22420 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.426, 132.920, 118.286
Angle α, β, γ (deg.)90.00, 102.84, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
DNA-directed RNA polymerase I subunit RPA49


Mass: 11848.159 Da / Num. of mol.: 8 / Fragment: UNP residues 1-99, N-terminal domain / Mutation: V72M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida glabrata (fungus) / Gene: CAGL0J07766g, rpa49 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL 21 (DE) RIL / References: UniProt: Q6FNZ9, DNA-directed RNA polymerase
#2: Protein
DNA-directed RNA polymerase I subunit RPA34


Mass: 13821.366 Da / Num. of mol.: 8 / Fragment: UNP residues 25-143 / Mutation: L55M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida glabrata (fungus) / Gene: CAGL0I06006g, rpa34 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL 21 (DE) RIL / References: UniProt: Q6FQI3, DNA-directed RNA polymerase
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 109 / 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: 2.64 Å3/Da / Density % sol: 53.49 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 22% PEG 3350, 250 mM sodium flouride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 70 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9792 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jun 18, 2008 / Details: Dynamically bendable mirror
RadiationMonochromator: Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.51→50 Å / Num. all: 88325 / Num. obs: 88325 / % possible obs: 97.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Biso Wilson estimate: 61.64 Å2 / Rmerge(I) obs: 0.037 / Rsym value: 0.037 / Net I/σ(I): 15.61
Reflection shellResolution: 2.5→2.56 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.651 / Mean I/σ(I) obs: 3.3 / Rsym value: 0.651 / % possible all: 97.6

-
Processing

Software
NameVersionClassification
SHARPphasing
BUSTER2.9.2refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: SAD / Resolution: 2.51→49.68 Å / Cor.coef. Fo:Fc: 0.9455 / Cor.coef. Fo:Fc free: 0.9161 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2434 3519 5.08 %RANDOM
Rwork0.1941 ---
obs0.1966 69255 --
all-69255 --
Displacement parametersBiso mean: 83.97 Å2
Baniso -1Baniso -2Baniso -3
1--4.9661 Å20 Å2-7.5494 Å2
2---0.8186 Å20 Å2
3---5.7847 Å2
Refine analyzeLuzzati coordinate error obs: 0.493 Å
Refinement stepCycle: LAST / Resolution: 2.51→49.68 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13685 0 0 109 13794
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0113920HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.2818803HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d5017SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes425HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1916HARMONIC5
X-RAY DIFFRACTIONt_it13920HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.16
X-RAY DIFFRACTIONt_other_torsion20.61
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion18455
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact139004
LS refinement shellResolution: 2.5→2.56 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.297 242 5.1 %
Rwork0.2655 4502 -
all0.267 4744 -
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)
17.0794-0.0145-0.21763.15870.3845.23940.1323-0.52630.5607-0.0314-0.22320.3831-0.4085-0.14010.0909-0.32590.0108-0.0237-0.1326-0.14010.325968.4254120.055-24.6106
25.0567-0.9166-0.25963.53220.45915.1290.12390.38520.56960.0554-0.1809-0.5456-0.3498-0.0630.0569-0.31510.0339-0.0449-0.0250.01030.3037104.4945119.069-20.6476
37.9395-1.0386-1.40533.98020.74016.09430.0448-0.1543-0.48-0.530.1776-0.12390.60850.4574-0.22240.103-0.1442-0.0587-0.304-0.0512-0.236248.2279153.3925.9101
45.94380.6751-1.59882.806-0.37994.10440.0991-0.1414-0.18830.1592-0.05720.14380.06070.0669-0.0419-0.12580.0379-0.0114-0.1689-0.0237-0.166259.9005153.45738.9526
53.97360.3021.81574.41711.33565.4968-0.0359-0.01810.20120.0517-0.0820.23280.2148-0.31030.1179-0.19140.104-0.0145-0.05080.0345-0.268722.7256122.95926.9767
62.05510.95151.05952.95170.79033.7013-0.1899-0.4097-0.5761-0.10650.24730.53390.5124-0.6516-0.05740.03290.0188-0.1302-0.08440.1602-0.127124.366193.526448.7898
71.81620.34830.51297.017-1.47414.91210.3059-0.0828-0.40170.2244-0.1493-0.45670.65710.4482-0.1566-0.1660.0312-0.1927-0.2429-0.0894-0.065958.8705119.49638.9028
83.12370.22461.3534.6492-1.15294.60560.06590.4734-0.4589-0.4097-0.3725-0.65160.49380.37210.30660.11430.1043-0.1728-0.304-0.13210.193950.745489.475422.0643
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{N|* K|43 - K|99 M|5 - 42}N43 - 99
2X-RAY DIFFRACTION1{N|* K|43 - K|99 M|5 - 42}K5 - 42
3X-RAY DIFFRACTION2{L|* M|43 - M|98 K|5 - 42}L43 - 98
4X-RAY DIFFRACTION2{L|* M|43 - M|98 K|5 - 42}M5 - 42
5X-RAY DIFFRACTION3{P|* A|43 - A|98 O|6 - 42}P43 - 98
6X-RAY DIFFRACTION3{P|* A|43 - A|98 O|6 - 42}A6 - 42
7X-RAY DIFFRACTION4{B|* O|43 - O|98 A|5 - 42}B43 - 98
8X-RAY DIFFRACTION4{B|* O|43 - O|98 A|5 - 42}O5 - 42
9X-RAY DIFFRACTION5{F|* G|43 - G|99 E|4 - 42}F43 - 99
10X-RAY DIFFRACTION5{F|* G|43 - G|99 E|4 - 42}G4 - 42
11X-RAY DIFFRACTION6{H|* E|43 - E|99 G|5 - 42}H43 - 99
12X-RAY DIFFRACTION6{H|* E|43 - E|99 G|5 - 42}E5 - 42
13X-RAY DIFFRACTION7{D|* I|43 - I|98 C|5 - 42}D43 - 98
14X-RAY DIFFRACTION7{D|* I|43 - I|98 C|5 - 42}I5 - 42
15X-RAY DIFFRACTION8{J|* C|43 - C|99 I|5 - 42}J43 - 99
16X-RAY DIFFRACTION8{J|* C|43 - C|99 I|5 - 42}C5 - 42

+
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