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Entry
Database: PDB / ID: 5ums
TitleCrystal structure of middle double PH domain of human FACT complex subunit SSRP1
ComponentsFACT complex subunit SSRP1FACT (biology)
KeywordsTRANSCRIPTION / Histone chaperone / Double PH domain / FACT
Function / homology
Function and homology information


FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / nucleosome binding / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat ...FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / nucleosome binding / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / nucleosome assembly / histone binding / Regulation of TP53 Activity through Phosphorylation / DNA replication / DNA repair / nucleolus / DNA binding / RNA binding / nucleoplasm / nucleus
Similarity search - Function
PH-domain like - #150 / : / FACT complex subunit SSRP1, C-terminal domain / : / SSRP1 PH domain / FACT complex subunit SSRP1/POB3 / SSRP1, dimerization domain / FACT complex subunit SSRP1/POB3, N-terminal PH domain / SSRP1 domain superfamily / Structure-specific recognition protein (SSRP1) ...PH-domain like - #150 / : / FACT complex subunit SSRP1, C-terminal domain / : / SSRP1 PH domain / FACT complex subunit SSRP1/POB3 / SSRP1, dimerization domain / FACT complex subunit SSRP1/POB3, N-terminal PH domain / SSRP1 domain superfamily / Structure-specific recognition protein (SSRP1) / POB3-like N-terminal PH domain / Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain / Histone chaperone Rttp106-like, middle domain / Histone chaperone Rttp106-like / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / PH-like domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
FACT complex subunit SSRP1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.569 Å
AuthorsSu, D. / Hu, Q. / Thompson, J.R. / Botuyan, M.V. / Mer, G.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)CA132878 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM116829 United States
CitationJournal: To Be Published
Title: Crystal structure of middle double PH domain of human FACT complex subunit SSRP1
Authors: Hu, Q. / Su, D. / Thompson, J.R. / Botuyan, M.V. / Mer, G.
History
DepositionJan 29, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 31, 2018Provider: repository / Type: Initial release
Revision 1.1Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Oct 4, 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

Downloads & links

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Assembly

Deposited unit
A: FACT complex subunit SSRP1


Theoretical massNumber of molelcules
Total (without water)30,4601
Polymers30,4601
Non-polymers00
Water3,513195
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)63.810, 82.290, 48.505
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-631-

HOH

21A-695-

HOH

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Components

#1: Protein FACT complex subunit SSRP1 / FACT (biology) / Chromatin-specific transcription elongation factor 80 kDa subunit / Facilitates chromatin ...Chromatin-specific transcription elongation factor 80 kDa subunit / Facilitates chromatin transcription complex 80 kDa subunit / FACTp80 / Facilitates chromatin transcription complex subunit SSRP1 / Recombination signal sequence recognition protein 1 / Structure-specific recognition protein 1 / hSSRP1 / T160


Mass: 30460.014 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SSRP1, FACT80 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q08945
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 195 / 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: 2.09 Å3/Da / Density % sol: 41.16 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 100 mM Bis-Tris, pH 6.5, 28% polyethylene glycol monomethyl ether 2000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 1, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.569→28.16 Å / Num. obs: 35760 / % possible obs: 93.1 % / Redundancy: 2.3 % / Net I/σ(I): 29.6

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Processing

Software
NameVersionClassification
PHENIXdev_972refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2GCL
Resolution: 1.569→28.157 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.42
RfactorNum. reflection% reflection
Rfree0.2274 602 1.69 %
Rwork0.198 --
obs0.1985 35727 98.04 %
Solvent computationShrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Bsol: 40.436 Å2 / ksol: 0.323 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.0328 Å20 Å2-0 Å2
2---8.9476 Å20 Å2
3---3.9148 Å2
Refinement stepCycle: LAST / Resolution: 1.569→28.157 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1955 0 0 195 2150
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0042067
X-RAY DIFFRACTIONf_angle_d0.6232800
X-RAY DIFFRACTIONf_dihedral_angle_d13.864801
X-RAY DIFFRACTIONf_chiral_restr0.061305
X-RAY DIFFRACTIONf_plane_restr0.004361
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5691-1.7270.27441570.26918691X-RAY DIFFRACTION99
1.727-1.97690.26191370.21138836X-RAY DIFFRACTION100
1.9769-2.49040.24261620.1868808X-RAY DIFFRACTION99
2.4904-28.16140.21191460.19458790X-RAY DIFFRACTION95

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