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- PDB-5r67: PanDDA analysis group deposition -- Crystal Structure of HUMAN CL... -

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Basic information

Entry
Database: PDB / ID: 5r67
TitlePanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in complex with FMOPL000589a
ComponentsCleavage and polyadenylation specificity factor subunit 5
KeywordsRNA BINDING PROTEIN / PanDDA / SGC - Diamond I04-1 fragment screening / NUDIX domain / XChemExplorer / CPSF5 / RNA PROCESSING / CLEAVAGE FACTOR / MRNA PROCESSING / NUCLEUS / PHOSPHOPROTEIN / RNA-BINDING
Function / homology
Function and homology information


positive regulation of pro-B cell differentiation / mRNA cleavage factor complex / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / Processing of Intronless Pre-mRNAs / positive regulation of stem cell differentiation / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / paraspeckles / mRNA 3'-UTR AU-rich region binding / mRNA 3'-end processing ...positive regulation of pro-B cell differentiation / mRNA cleavage factor complex / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / Processing of Intronless Pre-mRNAs / positive regulation of stem cell differentiation / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / paraspeckles / mRNA 3'-UTR AU-rich region binding / mRNA 3'-end processing / mRNA 3'-end processing / RNA Polymerase II Transcription Termination / protein heterotetramerization / post-transcriptional regulation of gene expression / Processing of Capped Intron-Containing Pre-mRNA / centriolar satellite / protein tetramerization / histone deacetylase binding / mRNA processing / cell differentiation / nuclear body / mRNA binding / centrosome / chromatin binding / protein homodimerization activity / RNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Cleavage/polyadenylation specificity factor subunit 5 / Nucleotide hydrolase / Nucleoside Triphosphate Pyrophosphohydrolase / Nucleoside Triphosphate Pyrophosphohydrolase / Nudix hydrolase domain profile. / NUDIX hydrolase domain / NUDIX hydrolase-like domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / Chem-S6V / Cleavage and polyadenylation specificity factor subunit 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / molecular replacement / Resolution: 1.52 Å
AuthorsTalon, R. / Krojer, T. / Diaz-Saez, L. / Bradley, A.R. / Aimon, A. / Fairhead, M. / Arrowsmith, C.H. / Bountra, C. / Edwards, A.M. / Huber, K.V.M. / von Delft, F.
CitationJournal: To Be Published
Title: PanDDA analysis group deposition
Authors: Talon, R. / Krojer, T. / Diaz-Saez, L. / Bradley, A.R. / Aimon, A. / Fairhead, M. / Arrowsmith, C.H. / Bountra, C. / Edwards, A.M. / Huber, K.V.M. / von Delft, F.
History
DepositionFeb 28, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 15, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cleavage and polyadenylation specificity factor subunit 5
B: Cleavage and polyadenylation specificity factor subunit 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,56612
Polymers45,7492
Non-polymers81710
Water4,612256
1
A: Cleavage and polyadenylation specificity factor subunit 5
hetero molecules

A: Cleavage and polyadenylation specificity factor subunit 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,74112
Polymers45,7492
Non-polymers99210
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555y,x,-z1
2
B: Cleavage and polyadenylation specificity factor subunit 5
hetero molecules

B: Cleavage and polyadenylation specificity factor subunit 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,39012
Polymers45,7492
Non-polymers64110
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_554-x,-x+y,-z-1/31
Unit cell
Length a, b, c (Å)59.770, 59.770, 214.230
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein Cleavage and polyadenylation specificity factor subunit 5 / Cleavage and polyadenylation specificity factor 25 kDa subunit / CPSF 25 kDa subunit / Cleavage ...Cleavage and polyadenylation specificity factor 25 kDa subunit / CPSF 25 kDa subunit / Cleavage factor Im complex 25 kDa subunit / CFIm25 / Nucleoside diphosphate-linked moiety X motif 21 / Nudix motif 21 / Nudix hydrolase 21 / Pre-mRNA cleavage factor Im 68 kDa subunit


Mass: 22874.393 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NUDT21, CFIM25, CPSF25, CPSF5 / Production host: escherichia coli (E. coli) / References: UniProt: O43809
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical ChemComp-S6V / 1-[2-(2-oxidanylidenepyrrolidin-1-yl)ethyl]-3-phenyl-urea


Mass: 247.293 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C13H17N3O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 256 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.24 Å3/Da / Density % sol: 45.16 % / Mosaicity: 0 °
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.1 / Details: 0.1M acetate pH 5.1, 0.0025M ZnAC, 6% PEG3K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92819 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 8, 2017
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92819 Å / Relative weight: 1
ReflectionResolution: 1.52→46.61 Å / Num. obs: 69626 / % possible obs: 99.9 % / Redundancy: 9.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.06 / Rpim(I) all: 0.02 / Rrim(I) all: 0.063 / Net I/σ(I): 17.5 / Num. measured all: 672004 / Scaling rejects: 0
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique allCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.52-1.568.52.2234283450360.4990.8072.3671100
6.8-46.618.70.03780829320.9990.0130.03960.999.7

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
REFMAC5.8.0238refinement
Aimless0.5.32data scaling
PDB_EXTRACT3.23data extraction
XDSdata reduction
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 3BAP

3bap


Resolution: 1.52→46.65 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.952 / SU B: 2.3 / SU ML: 0.08 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.088 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2452 3481 5 %RANDOM
Rwork0.2089 ---
obs0.2108 66050 99.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 123.05 Å2 / Biso mean: 30.202 Å2 / Biso min: 14.24 Å2
Baniso -1Baniso -2Baniso -3
1-0.5 Å20.25 Å20 Å2
2--0.5 Å2-0 Å2
3----1.61 Å2
Refinement stepCycle: final / Resolution: 1.52→46.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3160 0 36 256 3452
Biso mean--47.15 40.03 -
Num. residues----394
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0133894
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173353
X-RAY DIFFRACTIONr_angle_refined_deg2.0671.6554993
X-RAY DIFFRACTIONr_angle_other_deg1.3771.577809
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.9575458
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.45121.856194
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.59915609
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.311523
X-RAY DIFFRACTIONr_chiral_restr0.1120.2453
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.024227
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02794
X-RAY DIFFRACTIONr_mcbond_it3.2563.0521865
X-RAY DIFFRACTIONr_mcbond_other3.253.0491847
X-RAY DIFFRACTIONr_mcangle_it4.6474.6032234
LS refinement shellResolution: 1.52→1.559 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 256 -
Rwork0.343 4777 -
all-5033 -
obs--100 %

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