[English] 日本語
Yorodumi
- PDB-7pdv: Crystal structure of RBM5 RRM1-zinc finger in complex with RNA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7pdv
TitleCrystal structure of RBM5 RRM1-zinc finger in complex with RNA
Components
  • RNA (5'-R(P*UP*GP*GP*CP*UP*CP*UP*UP*CP*U)-3')
  • RNA binding motif protein 5 isoform 1
KeywordsRNA BINDING PROTEIN / RRM domain / Zinc finger / Splicing
Function / homology
Function and homology information


spliceosomal complex / mRNA splicing, via spliceosome / RNA binding / metal ion binding
Similarity search - Function
RNA-binding protein 5, RNA recognition motif 1 / RNA-binding protein 5, RNA recognition motif 2 / OCRE domain / OCRE domain / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger, RanBP2-type superfamily / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type ...RNA-binding protein 5, RNA recognition motif 1 / RNA-binding protein 5, RNA recognition motif 2 / OCRE domain / OCRE domain / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger, RanBP2-type superfamily / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
RNA / RNA binding motif protein 5 isoform 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.49 Å
AuthorsSoni, K. / Jagtap, P.K.A. / Sattler, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
CitationJournal: Nat Commun / Year: 2023
Title: Structural basis for specific RNA recognition by the alternative splicing factor RBM5.
Authors: Soni, K. / Jagtap, P.K.A. / Martinez-Lumbreras, S. / Bonnal, S. / Geerlof, A. / Stehle, R. / Simon, B. / Valcarcel, J. / Sattler, M.
History
DepositionAug 8, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 24, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 31, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: RNA binding motif protein 5 isoform 1
C: RNA binding motif protein 5 isoform 1
E: RNA binding motif protein 5 isoform 1
F: RNA (5'-R(P*UP*GP*GP*CP*UP*CP*UP*UP*CP*U)-3')
G: RNA binding motif protein 5 isoform 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,0869
Polymers58,8255
Non-polymers2624
Water00
1
A: RNA binding motif protein 5 isoform 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,9992
Polymers13,9331
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area7950 Å2
MethodPISA
2
C: RNA binding motif protein 5 isoform 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,9992
Polymers13,9331
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area8100 Å2
MethodPISA
3
E: RNA binding motif protein 5 isoform 1
F: RNA (5'-R(P*UP*GP*GP*CP*UP*CP*UP*UP*CP*U)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,0903
Polymers17,0252
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1480 Å2
ΔGint-12 kcal/mol
Surface area9170 Å2
MethodPISA
4
G: RNA binding motif protein 5 isoform 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,9992
Polymers13,9331
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area8310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.230, 65.890, 94.910
Angle α, β, γ (deg.)90.000, 90.050, 90.000
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
RNA binding motif protein 5 isoform 1


Mass: 13933.171 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBM5 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0S2Z549
#2: RNA chain RNA (5'-R(P*UP*GP*GP*CP*UP*CP*UP*UP*CP*U)-3')


Mass: 3091.828 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.72 Å3/Da / Density % sol: 54.83 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.05M Sodium cacodylate, 18mM CaCl2, 2.7 mM spermine, 9% 2-propanol

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 1.27982 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 20, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.27982 Å / Relative weight: 1
Reflection twinOperator: h,-k,-l / Fraction: 0.5
ReflectionResolution: 3.49→47.45 Å / Num. obs: 14244 / % possible obs: 90.7 % / Redundancy: 1.803 % / CC1/2: 0.94 / Rmerge(I) obs: 0.288 / Rrim(I) all: 0.397 / Χ2: 0.727 / Net I/σ(I): 1.9 / Num. measured all: 25689 / Scaling rejects: 8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
3.49-3.591.8250.9280.861863113810210.5361.26889.7
3.59-3.681.850.80911896114510250.5041.11189.5
3.68-3.791.8170.6171.291841111210130.6780.84591.1
3.79-3.911.7830.6631.06170810579580.6850.91290.6
3.91-4.041.7790.4361.53164210289230.8060.689.8
4.04-4.181.7360.4941.41163210599400.7790.67888.8
4.18-4.331.8190.3231.7614849398160.8870.44586.9
4.33-4.511.820.3561.8315789498670.8560.49491.4
4.51-4.711.8260.2811.8314798948100.9330.38990.6
4.71-4.941.7990.222.2913718197620.9460.30293
4.94-5.211.7860.2352.3113728247680.9260.32593.2
5.21-5.531.7360.2172.212227857040.9350.30189.7
5.53-5.911.8490.2672.1211856966410.9350.36992.1
5.91-6.381.8470.212.5212177046590.9390.29293.6
6.38-6.991.830.162.6610526025750.9610.22395.5
6.99-7.811.7640.1572.838915465050.9480.2292.5
7.81-9.021.8040.1163.287925114390.9830.16285.9
9.02-11.051.7980.0973.766874033820.9770.13594.8
11.05-15.631.7610.0893.675163292930.9740.12489.1
15.63-47.451.8250.0694.352611731430.9860.09682.7

-
Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIX1.19.2_4158refinement
PDB_EXTRACT3.27data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7PCV
Resolution: 3.49→47.45 Å / Cross valid method: THROUGHOUT / σ(F): 1.9 / Phase error: 41.13 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflection
Rfree0.39 1066 7.48 %
Rwork0.3373 13242 -
obs0.3421 14244 90.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 68.52 Å2 / Biso mean: 31.4705 Å2 / Biso min: 11.52 Å2
Refinement stepCycle: final / Resolution: 3.49→47.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3284 138 4 0 3426
Biso mean--25.04 --
Num. residues----435
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 7

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.49-3.680.4041460.32871858200483
3.68-3.910.33561270.31691898202585
3.91-4.210.39541480.31641851199982
4.21-4.630.37331370.33081906204384
4.63-5.30.40741520.33581909206186
5.3-6.680.35171520.34761919207185
6.68-47.450.4051400.37311901204185
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)
10.1568-0.0052-0.02290.0032-0.00410.01110.01080.0129-0.0422-0.00660.0132-0.0256-0.0179-0.01290.0797-0.07750.2053-0.07920.1694-0.28360.01913.9446-2.067722.8586
2-0.01860.0004-0.0087-0.0071-0.0016-0.01030.01550.00340.0862-0.01890.01860.0183-0.1331-0.04660.11-0.98790.19020.284-0.1109-0.2394-0.54424.5767-0.766818.8515
30.0007-0.0279-0.00110.3636-0.02550.04350.03320.05660.0297-0.0838-0.0176-0.0058-0.00470.00470.12780.10350.2351-0.08190.26090.01550.036821.99731.957727.9431
40.00080.02630.00570.1502-0.07680.2217-0.0232-0.00020.02030.00390.0048-0.0231-0.01320.0102-0.04770.0256-0.6654-0.15950.1297-0.0205-0.333419.2392-12.25930.7916
50.1103-0.0326-0.06420.0150.01230.0342-0.0208-0.01690.16980.0134-0.0194-0.0816-0.16410.0779-0.4143-0.5098-0.05420.73780.0703-0.2172-0.347517.16875.061926.4848
60.0015-00.03220.00540.00890.06830.03160.12160.0050.0430.0758-0.00310.08510.01820.721-0.21950.18560.08650.0857-0.0871-0.313314.78184.133714.9599
70.1856-0.07480.07950.06640.0560.2180.0281-0.0516-0.01240.03770.04930.06170.0375-0.07020.3029-0.3267-0.18060.17690.09760.29590.05978.68791.123222.8423
80.0320.03180.08720.1912-0.03780.2656-0.06330.0681-0.013-0.0424-0.05060.09060.02450.0845-0.7577-0.0375-0.1226-0.30090.28550.26730.05246.36744.073644.0085
90.1398-0.11280.01580.0818-0.01760.1334-0.0478-0.0203-0.0553-0.0180.07220.00390.05230.05640.2348-0.18970.09120.3379-0.02940.1839-0.097410.93050.459443.5128
100.0722-0.0076-0.14390.00680.02720.29630.00560.07630.0267-0.08440.02120.0051-0.0136-0.00320.06290.67060.00220.08260.33470.5740.415217.08263.791541.772
11-0.0143-0.00520.0054-0.00680.0002-0.01130.15290.0047-0.02320.06140.10790.0393-0.03310.02561.6293-0.86690.2265-0.3790.01290.2499-0.481129.1-0.693343.1086
120.3813-0.028-0.18730.00780.04570.16510.03690.10030.2334-0.0165-0.01630.0521-0.16430.0816-0.3531-0.70390.41121.01150.29040.0951-0.435733.3355-2.399635.7921
13-0.0001-0.002-0.0019-0.0034-0.0036-0.0050.01220.00170.0214-0.01260.01140.05840.0314-0.02970.2356-0.36820.01990.06280.03790.0547-0.069937.172411.214945.838
140.14780.07150.22050.03660.10720.3057-0.01770.00440.06170.02-0.0086-0.085-0.10120.17380.2310.17640.0513-0.2950.2958-0.10280.01336.0284-3.842952.7649
150.1112-0.05440.0660.1081-0.03030.03970.0168-0.0481-0.05330.09330.07280.02480.0079-0.00010.3635-0.18640.1928-0.077-0.08390.12160.023343.47871.480738.8006
160.0693-0.0754-0.12990.25080.14080.23860.0044-0.016-0.01690.0117-0.0239-0.0088-0.0251-0.0412-0.0405-0.14810.0272-0.0215-0.0053-0.25350.320347.8699-0.343619.4686
170.07940.06550.02650.0460.0150.10460.0386-0.0239-0.0320.06370.0216-0.0091-0.03390.01890.4464-0.2518-0.4680.37440.0911-0.2714-0.096939.83942.811920.4518
180.1041-0.04490.02990.1998-0.21890.24220.0258-0.06740.03960.07990.01510.0161-0.0723-0.00180.04540.6343-0.01320.14280.6048-0.07820.053533.65124.135423.7774
19-0.01290.01270.01950.05860.0632-0.01010.19970.2594-0.2777-0.20470.22480.12030.01750.12422.8841-1.7574-0.19920.30880.1542-0.4573-0.91595.357433.23816.3184
200.09180.1257-0.12380.1657-0.16850.1577-0.0031-0.02320.0225-0.01940.0312-0.0074-0.0024-0.00290.1548-0.27210.2949-0.19880.3271-0.41940.204310.92619.47681.9396
21-0.0636-0.0209-0.0184-0.1096-0.0581-0.0212-0.0067-0.0060.0731-0.0547-0.00990.04510.07260.0667-0.0367-1.39610.4718-0.2113-0.52790.6418-0.848915.283129.996212.9464
220.1267-0.05490.03560.15290.14090.20580.02150.02320.0433-0.1012-0.0118-0.0649-0.06930.0230.21540.2012-0.05120.18070.12330.0318-0.05237.982132.400315.1641
230.1018-0.1116-0.20760.16590.1080.69410.04530.0497-0.11460.0272-0.0354-0.00860.1298-0.25330.1257-0.0567-0.233-0.07280.4229-0.3202-0.192745.923737.558726.0946
240.2321-0.00580.03340.24420.26460.2728-0.05360.0303-0.0470.0102-0.0033-0.00890.01080.04-0.3812-0.75790.6058-0.09460.28560.58590.074850.237426.566630.5326
25-0.00470.00050.0051-0.0047-0.0006-0.0083-0.0053-0.03050.01560.0438-0.0178-0.0299-0.07360.0592-0.1874-0.2898-0.16690.16110.1007-0.1974-0.228242.70639.660617.7985
260.12150.0062-0.0184-0.008-0.0072-0.0066-0.01650.0561-0.03170.09320.01670.02410.10450.0848-0.0222-0.5933-0.1774-0.22820.29870.3631-0.025241.89721.392324.8457
270.42080.1480.19380.0520.05380.24990.0270.0424-0.0029-0.01560.00140.0110.022-0.00940.1341-0.1794-0.0629-0.12860.0419-0.23190.055137.468725.700535.4108
280.0091-0.02250.04390.0522-0.10150.19620.00640.0169-0.03530.0149-0.00390.01690.03270.016-0.0280.07020.203-0.1610.087-0.0590.041944.151135.743136.4296
290.0229-0.02550.00450.0214-0.00430.0050.0554-0.02220.0212-0.08620.0419-0.06580.0320.0450.4573-0.30630.00470.03510.1047-0.50240.077237.554332.877130.0226
300.0019-0.0082-0.01660.02980.07560.17440.0289-0.0279-0.00650.03410.0056-0.01710.003-0.00730.168-0.2062-0.01820.03140.1585-0.095-0.101227.56630.450213.1636
310.0484-0.16780.01780.9324-0.13270.14430.03370.0232-0.02390.0170.0624-0.03640.06690.0440.3868-0.1593-0.0938-0.0028-0.0346-0.28120.006729.242328.79984.3197
320.0090.0130.02420.0190.02540.0380.03520.00130.0111-0.09390.004-0.0256-0.0822-0.02420.3506-0.03380.0619-0.3419-0.055-0.0984-0.394136.506828.29125.8462
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 8 through 14 )A8 - 14
2X-RAY DIFFRACTION2chain 'A' and (resid 15 through 34 )A15 - 34
3X-RAY DIFFRACTION3chain 'A' and (resid 35 through 40 )A35 - 40
4X-RAY DIFFRACTION4chain 'A' and (resid 41 through 49 )A41 - 49
5X-RAY DIFFRACTION5chain 'A' and (resid 50 through 59 )A50 - 59
6X-RAY DIFFRACTION6chain 'A' and (resid 60 through 78 )A60 - 78
7X-RAY DIFFRACTION7chain 'A' and (resid 79 through 88 )A79 - 88
8X-RAY DIFFRACTION8chain 'A' and (resid 89 through 98 )A89 - 98
9X-RAY DIFFRACTION9chain 'A' and (resid 99 through 108 )A99 - 108
10X-RAY DIFFRACTION10chain 'A' and (resid 109 through 114 )A109 - 114
11X-RAY DIFFRACTION11chain 'C' and (resid 8 through 40 )C8 - 40
12X-RAY DIFFRACTION12chain 'C' and (resid 41 through 59 )C41 - 59
13X-RAY DIFFRACTION13chain 'C' and (resid 60 through 69 )C60 - 69
14X-RAY DIFFRACTION14chain 'C' and (resid 70 through 79 )C70 - 79
15X-RAY DIFFRACTION15chain 'C' and (resid 80 through 89 )C80 - 89
16X-RAY DIFFRACTION16chain 'C' and (resid 90 through 94 )C90 - 94
17X-RAY DIFFRACTION17chain 'C' and (resid 95 through 109 )C95 - 109
18X-RAY DIFFRACTION18chain 'C' and (resid 110 through 114 )C110 - 114
19X-RAY DIFFRACTION19chain 'E' and (resid 8 through 58 )E8 - 58
20X-RAY DIFFRACTION20chain 'E' and (resid 59 through 66 )E59 - 66
21X-RAY DIFFRACTION21chain 'E' and (resid 67 through 114 )E67 - 114
22X-RAY DIFFRACTION22chain 'F' and (resid 2 through 8 )F2 - 8
23X-RAY DIFFRACTION23chain 'G' and (resid 8 through 23 )G8 - 23
24X-RAY DIFFRACTION24chain 'G' and (resid 24 through 36 )G24 - 36
25X-RAY DIFFRACTION25chain 'G' and (resid 37 through 52 )G37 - 52
26X-RAY DIFFRACTION26chain 'G' and (resid 53 through 66 )G53 - 66
27X-RAY DIFFRACTION27chain 'G' and (resid 67 through 71 )G67 - 71
28X-RAY DIFFRACTION28chain 'G' and (resid 72 through 76 )G72 - 76
29X-RAY DIFFRACTION29chain 'G' and (resid 77 through 86 )G77 - 86
30X-RAY DIFFRACTION30chain 'G' and (resid 87 through 91 )G87 - 91
31X-RAY DIFFRACTION31chain 'G' and (resid 92 through 96 )G92 - 96
32X-RAY DIFFRACTION32chain 'G' and (resid 97 through 114 )G97 - 114

+
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