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- PDB-5r66: PanDDA analysis group deposition -- Crystal Structure of HUMAN CL... -

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Basic information

Entry
Database: PDB / ID: 5r66
TitlePanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in complex with FMOPL000198a
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 / Processing of Intronless Pre-mRNAs / positive regulation of stem cell differentiation / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / mRNA 3'-UTR AU-rich region binding / paraspeckles / mRNA 3'-end processing ...positive regulation of pro-B cell differentiation / : / mRNA cleavage factor complex / Processing of Intronless Pre-mRNAs / positive regulation of stem cell differentiation / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / mRNA 3'-UTR AU-rich region binding / paraspeckles / mRNA 3'-end processing / mRNA 3'-end processing / protein heterotetramerization / RNA Polymerase II Transcription Termination / post-transcriptional regulation of gene expression / : / Processing of Capped Intron-Containing Pre-mRNA / centriolar satellite / protein tetramerization / mRNA processing / histone deacetylase binding / 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-NT7 / Cleavage and polyadenylation specificity factor subunit 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / molecular replacement / Resolution: 2.02 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_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_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)46,50811
Polymers45,7492
Non-polymers7599
Water4,522251
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)46,24710
Polymers45,7492
Non-polymers4988
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)46,76912
Polymers45,7492
Non-polymers1,02010
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)59.690, 59.690, 214.740
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 / Acetate


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical ChemComp-NT7 / N-(2,3-dimethylphenyl)-2-(morpholin-4-yl)acetamide


Mass: 248.321 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H20N2O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 251 / 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: 45.14 % / 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: 2.02→50.26 Å / Num. obs: 30176 / % possible obs: 99.9 % / Redundancy: 9.2 % / CC1/2: 0.998 / Rmerge(I) obs: 0.151 / Rpim(I) all: 0.053 / Rrim(I) all: 0.16 / Net I/σ(I): 12.8 / Num. measured all: 277678 / 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
2.02-2.079.92.8212168421870.6410.9372.9761.2100
9.03-50.268.10.03734714290.9990.0130.03942.899.5

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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: 2.02→50.31 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.928 / SU B: 6.564 / SU ML: 0.168 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.237 / ESU R Free: 0.197 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2592 1487 4.9 %RANDOM
Rwork0.2101 ---
obs0.2126 28623 99.77 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 194.85 Å2 / Biso mean: 37.412 Å2 / Biso min: 19.4 Å2
Baniso -1Baniso -2Baniso -3
1-0.67 Å20.34 Å20 Å2
2--0.67 Å2-0 Å2
3----2.18 Å2
Refinement stepCycle: final / Resolution: 2.02→50.31 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3160 0 32 251 3443
Biso mean--73.75 45.72 -
Num. residues----394
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0134116
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173418
X-RAY DIFFRACTIONr_angle_refined_deg1.5551.6545166
X-RAY DIFFRACTIONr_angle_other_deg1.2171.5687950
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.1465470
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.46922.161199
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.34415597
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.081523
X-RAY DIFFRACTIONr_chiral_restr0.0760.2465
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.024360
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02821
X-RAY DIFFRACTIONr_mcbond_it3.0363.8941976
X-RAY DIFFRACTIONr_mcbond_other3.0243.891956
X-RAY DIFFRACTIONr_mcangle_it4.7445.8492300
LS refinement shellResolution: 2.02→2.072 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.401 100 -
Rwork0.356 2082 -
all-2182 -
obs--99.77 %

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