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- PDB-5wwg: Crystal structure of hnRNPA2B1 in complex with AAGGACUUGC -

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Basic information

Entry
Database: PDB / ID: 5wwg
TitleCrystal structure of hnRNPA2B1 in complex with AAGGACUUGC
Components
  • Heterogeneous nuclear ribonucleoproteins A2/B1
  • RNA (5'-R(*AP*AP*GP*GP*AP*CP*UP*U)-3')
KeywordsRNA BINDING PROTEIN/RNA / HNRNP / RRM / RNA BINDING PROTEIN-RNA complex
Function / homology
Function and homology information


positive regulation of telomerase RNA reverse transcriptase activity / miRNA transport / positive regulation of telomere maintenance via telomere lengthening / RNA transport / G-quadruplex DNA unwinding / primary miRNA processing / single-stranded telomeric DNA binding / N6-methyladenosine-containing RNA reader activity / G-rich strand telomeric DNA binding / miRNA binding ...positive regulation of telomerase RNA reverse transcriptase activity / miRNA transport / positive regulation of telomere maintenance via telomere lengthening / RNA transport / G-quadruplex DNA unwinding / primary miRNA processing / single-stranded telomeric DNA binding / N6-methyladenosine-containing RNA reader activity / G-rich strand telomeric DNA binding / miRNA binding / negative regulation of mRNA splicing, via spliceosome / Processing of Capped Intron-Containing Pre-mRNA / mRNA transport / Cajal body / mRNA export from nucleus / pre-mRNA intronic binding / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / catalytic step 2 spliceosome / molecular condensate scaffold activity / mRNA Splicing - Major Pathway / mRNA 3'-UTR binding / spliceosomal complex / mRNA processing / mRNA splicing, via spliceosome / nuclear matrix / chromosome, telomeric region / ribonucleoprotein complex / negative regulation of transcription by RNA polymerase II / RNA binding / extracellular exosome / nucleoplasm / membrane / identical protein binding / nucleus / cytoplasm
Similarity search - Function
hnRNP A2/B1, RNA recognition motif 1 / Heterogeneous nuclear ribonucleoprotein A1/A2, C-terminal / Heterogeneous nuclear ribonucleoprotein A1, LC domain / RRM (RNA recognition motif) domain / 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 ...hnRNP A2/B1, RNA recognition motif 1 / Heterogeneous nuclear ribonucleoprotein A1/A2, C-terminal / Heterogeneous nuclear ribonucleoprotein A1, LC domain / RRM (RNA recognition motif) domain / 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 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
RNA / Heterogeneous nuclear ribonucleoproteins A2/B1
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.03 Å
AuthorsWu, B.X. / Su, S.C. / Ma, J.B.
CitationJournal: Nat Commun / Year: 2018
Title: Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.
Authors: Wu, B. / Su, S. / Patil, D.P. / Liu, H. / Gan, J. / Jaffrey, S.R. / Ma, J.
History
DepositionJan 1, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 17, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2018Group: Database references / Category: 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.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Feb 14, 2018Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Nov 22, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Heterogeneous nuclear ribonucleoproteins A2/B1
B: RNA (5'-R(*AP*AP*GP*GP*AP*CP*UP*U)-3')


Theoretical massNumber of molelcules
Total (without water)24,4082
Polymers24,4082
Non-polymers00
Water59433
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1420 Å2
ΔGint-1 kcal/mol
Surface area11880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)132.810, 46.228, 33.994
Angle α, β, γ (deg.)90.00, 102.22, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Heterogeneous nuclear ribonucleoproteins A2/B1 / hnRNP A2/B1


Mass: 21206.969 Da / Num. of mol.: 1 / Fragment: RRMs (UNP RESIDUES 12-195)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HNRNPA2B1, HNRPA2B1 / Production host: Escherichia coli (E. coli) / References: UniProt: P22626
#2: RNA chain RNA (5'-R(*AP*AP*GP*GP*AP*CP*UP*U)-3')


Mass: 3200.972 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 33 / Source method: isolated from a natural source / Formula: H2O

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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: 2.13 Å3/Da / Density % sol: 42.35 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9
Details: 25% (w/v) PEG 1500, 0.1M MMT/Sodium hydroxide pH 9.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97776 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: CCD / Date: Oct 13, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97776 Å / Relative weight: 1
ReflectionResolution: 2.03→50 Å / Num. obs: 14087 / % possible obs: 95.9 % / Redundancy: 4.9 % / Net I/σ(I): 2.4
Reflection shellResolution: 2.03→2.082 Å

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Processing

Software
NameVersionClassification
REFMAC5.8.0135refinement
DENZOdata reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5EN1

5en1


Resolution: 2.03→30 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.934 / SU B: 6.235 / SU ML: 0.163 / Cross valid method: THROUGHOUT / ESU R: 0.237 / ESU R Free: 0.201 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25628 616 4.8 %RANDOM
Rwork0.19868 ---
obs0.20145 12210 97.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 42.795 Å2
Baniso -1Baniso -2Baniso -3
1--0.09 Å20 Å2-1.01 Å2
2--2.35 Å20 Å2
3----1.67 Å2
Refinement stepCycle: 1 / Resolution: 2.03→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1491 169 0 33 1693
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0181754
X-RAY DIFFRACTIONr_bond_other_d0.0020.021579
X-RAY DIFFRACTIONr_angle_refined_deg1.8311.8592390
X-RAY DIFFRACTIONr_angle_other_deg1.11533649
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.8955192
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.66622.8481
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.66515297
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.6841517
X-RAY DIFFRACTIONr_chiral_restr0.1110.2248
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.021868
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02421
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.4993.882760
X-RAY DIFFRACTIONr_mcbond_other3.4853.88759
X-RAY DIFFRACTIONr_mcangle_it4.7815.799953
X-RAY DIFFRACTIONr_mcangle_other4.785.802954
X-RAY DIFFRACTIONr_scbond_it4.3884.505994
X-RAY DIFFRACTIONr_scbond_other4.3894.503993
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.596.5691437
X-RAY DIFFRACTIONr_long_range_B_refined8.12532.3062008
X-RAY DIFFRACTIONr_long_range_B_other8.12732.2852005
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.03→2.082 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.307 41 -
Rwork0.264 874 -
obs--94.72 %

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