BMRB Entry 27534

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27534

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Title:
Solution NMR Structure of PALB2 Colied-coil Domain (PALB2cc)
Deposition date:
2018-07-05
Original release date:
2018-11-16
Authors:
Song, Fei; Li, Minxing; Liu, Gaohua; Swapna, G.V.T.; Xia, Bing; Bunting, Samuel; Montelione, Gaetano
Citation:

Citation: Song, Fei; Li, Minxing; Liu, Gaohua; Swapna, G.V.T.; Daigham, Nourhan; Xia, Bing; Montelione, Gaetano; Bunting, Samuel. "Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2"  Biochemistry 57, 6581-6591 (2018).
PubMed: 30289697

Assembly members:

Assembly members:
PALB2cc, polymer, 68 residues, 7926.10 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   Vector: pET21-NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PALB2cc: MEELSGKPLSYAEKEKLKEK LAFLKKEYSRTLARLQRAKR AEKAKNSKKAIEDGVPQPEA LEHHHHHH

Data sets:
Data typeCount

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PALB2cc, chain 11
2PALB2cc, chain 21

Entities:

Entity 1, PALB2cc, chain 1 68 residues - 7926.10 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; sodium azide 0.02%; H2O 90%; DSS 10%

sample_2: PALB2cc, [U-100% 13C; U-100% 15N], 1 X; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; DSS 10%; PALB2cc 2 X

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D TROSY-HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCOCAsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HNCOCACBsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HBHACONHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
AROMATIC 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

Software:

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

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

SPARKY, Goddard - Processing, chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

Autoassign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

AVS, Moseley and Montelione - chemical shift assignment, data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

xeasy, C. Bartels, T.-h. Xia, M. Billeter, P. Guntert, and K. Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz