BMRB Entry 30796

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30796
MolProbity Validation Chart

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Title:
Solution NMR Structure of the Coiled-coil BRCA1-PALB2 Heterodimer
Deposition date:
2020-09-13
Original release date:
2021-09-22
Authors:
Daigham, N.; Liu, G.; Bunting, S.; Montelione, G.
Citation:

Citation: Daigham, N.; Liu, G.; Bunting, S.; Montelione, G.. "The Structural Basis for Interactions Between PALB2 and BRCA1 that Mediate the Homologous Recombination DNA Damage Repair Process"  .

Assembly members:

Assembly members:
entity_1, polymer, 60 residues, 6935.690 Da.
entity_2, 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   Vector: MmR494A-1337-1387

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNLSEDCSQSDILTTQQRAT MKYNLIKLQQEMAHLEAVLE QRGNQPSGHSPSLEHHHHHH
entity_2: MEELSGKPLSYAEKEKLKEK LAFLKKEYSRTLARLQRAKR AEKAKNSKKAIEDGVPQPEA LEHHHHHH

Data typeCount
13C chemical shifts367
15N chemical shifts111
1H chemical shifts776

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 60 residues - 6935.690 Da.

1   METASNLEUSERGLUASPCYSSERGLNSER
2   ASPILELEUTHRTHRGLNGLNARGALATHR
3   METLYSTYRASNLEUILELYSLEUGLNGLN
4   GLUMETALAHISLEUGLUALAVALLEUGLU
5   GLNARGGLYASNGLNPROSERGLYHISSER
6   PROSERLEUGLUHISHISHISHISHISHIS

Entity 2, unit_2 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], 1.5 mM; BRCA1cc 3 mM; MES 20 mM; sodium chloride 200 mM; DTT 10 mM; CaCl2 5 mM

sample_2: PALB2cc 3 mM; BRCA1cc, [U-100% 13C; U-100% 15N], 1.5 mM; MES 20 mM; sodium chloride 200 mM; DTT 10 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

PSVS, Bhattacharya and Montelione - data analysis

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

Sparky, Goddard - chemical shift assignment

TopSpin, Bruker Biospin - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - 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

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