BMRB Entry 18478

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18478
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
P75/LEDGF PWWP Domain
Deposition date:
2012-05-24
Original release date:
2013-02-27
Authors:
Crowe, Brandon; Foster, Mark
Citation:

Citation: Eidahl, Jocelyn; Crowe, Brandon; North, Justin; McKee, Christopher; Shkriabai, Nikoloz; Feng, Lei; Plumb, Matthew; Graham, Robert; Gorelick, Robert; Hess, Sonja; Poirier, Michael; Foster, Mark; Kvaratskhelia, Mamuka. "Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes."  Nucleic Acids Res. 41, 3924-3936 (2013).
PubMed: 23396443

Assembly members:

Assembly members:
entity, polymer, 97 residues, 11031.707 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pFT-1-LEDGF

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPGSMTRDFKPGDLIFAKMK GYPHWPARVDEVPDGAVKPP TNKLPIFFFGTHETAFLGPK DIFPYSENKEKYGKPNKRKG FNEGLWEIDNNPKVKFS

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts81
1H chemical shifts482

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1P75/LEDGF PWWP Domain1

Entities:

Entity 1, P75/LEDGF PWWP Domain 97 residues - 11031.707 Da.

Residues 1-4 are non native. They are left over from an affinity tag cleavage site used for purification.

1   GLYPROGLYSERMETTHRARGASPPHELYS
2   PROGLYASPLEUILEPHEALALYSMETLYS
3   GLYTYRPROHISTRPPROALAARGVALASP
4   GLUVALPROASPGLYALAVALLYSPROPRO
5   THRASNLYSLEUPROILEPHEPHEPHEGLY
6   THRHISGLUTHRALAPHELEUGLYPROLYS
7   ASPILEPHEPROTYRSERGLUASNLYSGLU
8   LYSTYRGLYLYSPROASNLYSARGLYSGLY
9   PHEASNGLUGLYLEUTRPGLUILEASPASN
10   ASNPROLYSVALLYSPHESER

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.35 – 0.45 mM; HEPES 50 mM; sodium chloride 150 mM; beta-mercaptoethanol 2 mM; DSS 0.66 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.35 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TALOS+, Cornilescu, Delaglio and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRViewJ v8.2.1, Johnson, One Moon Scientific - chemical shift assignment, peak picking

xwinnmr, Bruker Biospin - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 18878
PDB
DBJ BAB27707 BAE24079 BAE36388 BAE41251 BAJ78791
EMBL CAC34944 CAC34945
GB AAC25167 AAC97945 AAC97946 AAF25870 AAF25871
REF NP_001009372 NP_001075982 NP_001121689 NP_001137364 NP_001193405
SP O75475 Q66T72 Q812D1 Q8MJG1 Q99JF8
TPG DAA26946
AlphaFold O75475 Q66T72 Q812D1 Q8MJG1 Q99JF8

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks