BMRB Entry 16884

Title:
1H, 13C and 15N Chemical Shift assignments for RRM3 of Brunol-3.
Deposition date:
2010-04-20
Original release date:
2011-12-15
Authors:
Kashyap, Maruthi; Bhatt, Harshesh; Bhavesh, Neel Sarovar
Citation:

Citation: Kashyap, Maruthi; Bhatt, Harshesh; Bhavesh, Neel Sarovar. "1H, 13C and 15N NMR assignments of RNA recognizing motifs 1 and 2 of BRUNOL-3 protein from human involved in myotonic dystrophy"  Biomol. NMR Assignments 4, 143-145 (2010).
PubMed: 20443086

Assembly members:

Assembly members:
RRM3, polymer, 97 residues, Formula weight is not available

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: pET28a

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts107
1H chemical shifts562

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM31

Entities:

Entity 1, RRM3 97 residues - Formula weight is not available

1   GLYSERHISMETGLNLYSGLUGLYPROGLU
2   GLYALAASNLEUPHEILETYRHISLEUPRO
3   GLNGLUPHEGLYASPGLNASPILELEUGLN
4   METPHEMETPROPHEGLYASNVALILESER
5   ALALYSVALPHEILEASPLYSGLNTHRASN
6   LEUSERLYSCYSPHEGLYPHEVALSERTYR
7   ASPASNPROVALSERALAGLNALAALAILE
8   GLNALAMETASNGLYPHEGLNILEGLYMET
9   LYSARGLEULYSVALGLNLEULYSARGSER
10   LYSASNASPSERLYSPROTYR

Samples:

sample_1: BRUNOL-3, [U-13C; U-15N], 1 – 1.2 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 50 ± 0.5 mM; sodium azide 0.1%; D2O, [U-99% 2H], 5%; D2O 95%

sample_conditions_1: pH: 6.5; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1
3D HN(C)Nsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 19685
PDB
DBJ BAE36341 BAG58428 BAG59778 BAG63913
EMBL CAF96701 CDQ91280
GB AAF89096 AAH45035 AAI36077 AAP57761 AAP57762
REF NP_001079593 NP_001096417 NP_001279263 XP_004574118 XP_004574119
SP A4IIM2 Q7T2T1 Q7ZXE2
AlphaFold A4IIM2 Q7T2T1 Q7ZXE2

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