BMRB Entry 50412

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50412

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Title:
Backbone and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor
Deposition date:
2020-07-27
Original release date:
2020-08-04
Authors:
Singh, Amrinder; Dyson, Jane; Wright, Peter
Citation:

Citation: Singh, Amrinder; Dyson, Jane. "Backbone and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor"  Biomol. NMR Assign. 15, 29-33 (2021).
PubMed: 32936430

Assembly members:

Assembly members:
entity_1, polymer, 210 residues, Formula weight is not available
entity_2, polymer, 107 residues, Formula weight is not available

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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGPYLQILEQPKQRGFRFRY VCEGPSHGGLPGASSEKNKK SYPQVKICNYVGPAKVIVQL VTNGKNIHLHAHSLVGKHCE DGVCTVTAGPKDMVVGFANL GILHVTKKKVFETLEARMTE ACIRGYNPGLLVHSDLAYLQ AEGGGDRQLTDREKEIIRQA AVQQTKEMDLSVVRLMFTAF LPDSTGSFTRRLEPVVSDAI YDSKAPNASN
entity_2: MASNLKIVRMDRTAGCVTGG EEIYLLCDKVQKDDIQIRFY EEEENGGVWEGFGDFSPTDV HRQFAIVFKTPKYKDVNITK PASVFVQLRRKSDLETSEPK PFLYYPE

Data sets:
Data typeCount
13C chemical shifts1069
15N chemical shifts283
1H chemical shifts1708

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p50 DNA binding domain1
2p50 Dimerization Domain2

Entities:

Entity 1, p50 DNA binding domain 210 residues - Formula weight is not available

1   METGLYPROTYRLEUGLNILELEUGLUGLN
2   PROLYSGLNARGGLYPHEARGPHEARGTYR
3   VALCYSGLUGLYPROSERHISGLYGLYLEU
4   PROGLYALASERSERGLULYSASNLYSLYS
5   SERTYRPROGLNVALLYSILECYSASNTYR
6   VALGLYPROALALYSVALILEVALGLNLEU
7   VALTHRASNGLYLYSASNILEHISLEUHIS
8   ALAHISSERLEUVALGLYLYSHISCYSGLU
9   ASPGLYVALCYSTHRVALTHRALAGLYPRO
10   LYSASPMETVALVALGLYPHEALAASNLEU
11   GLYILELEUHISVALTHRLYSLYSLYSVAL
12   PHEGLUTHRLEUGLUALAARGMETTHRGLU
13   ALACYSILEARGGLYTYRASNPROGLYLEU
14   LEUVALHISSERASPLEUALATYRLEUGLN
15   ALAGLUGLYGLYGLYASPARGGLNLEUTHR
16   ASPARGGLULYSGLUILEILEARGGLNALA
17   ALAVALGLNGLNTHRLYSGLUMETASPLEU
18   SERVALVALARGLEUMETPHETHRALAPHE
19   LEUPROASPSERTHRGLYSERPHETHRARG
20   ARGLEUGLUPROVALVALSERASPALAILE
21   TYRASPSERLYSALAPROASNALASERASN

Entity 2, p50 Dimerization Domain 107 residues - Formula weight is not available

1   METALASERASNLEULYSILEVALARGMET
2   ASPARGTHRALAGLYCYSVALTHRGLYGLY
3   GLUGLUILETYRLEULEUCYSASPLYSVAL
4   GLNLYSASPASPILEGLNILEARGPHETYR
5   GLUGLUGLUGLUASNGLYGLYVALTRPGLU
6   GLYPHEGLYASPPHESERPROTHRASPVAL
7   HISARGGLNPHEALAILEVALPHELYSTHR
8   PROLYSTYRLYSASPVALASNILETHRLYS
9   PROALASERVALPHEVALGLNLEUARGARG
10   LYSSERASPLEUGLUTHRSERGLUPROLYS
11   PROPHELEUTYRTYRPROGLU

Samples:

sample_1: entity_1, [U-13C; U-15N; U-2H], 0.8 ± 0.01 mM; NaCl 150 mM

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 ± 0.01 mM; NaCl 150 mM

sample_3: entity_2, [U-100% 13C; U-100% 15N], 0.800 ± 0.01 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.8; temperature: 290 K

sample_conditions_2: ionic strength: 0.15 M; pH: 6.8; temperature: 300 K

sample_conditions_3: ionic strength: 0.15 M; pH: 6.8; temperature: 315 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-15N TOCSYsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_2
3D HCCH-COSYsample_1isotropicsample_conditions_2
3D H(CCO)NHsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
3D HCCH-TOCSYsample_3isotropicsample_conditions_3
3D HCCH-COSYsample_3isotropicsample_conditions_3
3D H(CCO)NHsample_3isotropicsample_conditions_3
3D 1H-15N TOCSYsample_3isotropicsample_conditions_3
3D 1H-15N NOESYsample_3isotropicsample_conditions_3
3D HNCAsample_3isotropicsample_conditions_3

Software:

NMRPipe - processing

CcpNMR - data analysis

NMRView - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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