BMRB Entry 30493

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30493
MolProbity Validation Chart

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Title:
Solution NMR Structure of the Colied-coil PALB2 Homodimer
Deposition date:
2018-07-17
Original release date:
2018-10-08
Authors:
Song, F.; Li, M.; Liu, G.; Swapna, G.; Xia, B.; Bunting, S.; Montelione, G.
Citation:

Citation: Song, F.; Li, M.; Liu, G.; Swapna, G.; Daigham, N.; Xia, B.; Montelione, G.; Bunting, S.. "Antiparallel Coiled-Coil Interactions Mediate Homodimerization of the DNA Damage Repair Protein, PALB2"  Biochemistry 57, 6581-6591 (2018).
PubMed: 30289697

Assembly members:

Assembly members:
entity_1, polymer, 68 residues, 7948.166 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEELSGKPLSYAEKEKLKEK LAFLKKEYSRTLARLQRAKR AEKAKNSKKAIEDGVPQPEA LEHHHHHH

Data typeCount
13C chemical shifts211
15N chemical shifts59
1H chemical shifts426

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 68 residues - 7948.166 Da.

1   METGLUGLULEUSERGLYLYSPROLEUSER
2   TYRALAGLULYSGLULYSLEULYSGLULYS
3   LEUALAPHELEULYSLYSGLUTYRSERARG
4   THRLEUALAARGLEUGLNARGALALYSARG
5   ALAGLULYSALALYSASNSERLYSLYSALA
6   ILEGLUASPGLYVALPROGLNPROGLUALA
7   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: PALB2cc, [U-100% 13C; U-100% 15N], 1.2 mM; MES 20 mM; sodium chloride 200 mM; Calcium Chloride 5 mM; DTT 10 mM; DSS 10%; sodium azide 0.02%

sample_2: PALB2cc, [U-100% 13C; U-100% 15N], 1 v/v; MES 20 mM; sodium chloride 200 mM; Calcium Chloride 5 mM; DTT 10 mM; DSS 10%; sodium azide 0.02%; unlabeled PALB2cc 2 v/v

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D TROSY-HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D TROSY-HNCOCAsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HNCOCACBsample_1isotropicsample_conditions_1
3D TROSY-HBHACONHsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
AROMATIC CCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D simultaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
X-filtered noesy (pulse sequence: noesyhsqcgpwgx13d)sample_2isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AVS, Moseley and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - data analysis

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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