BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15820

Title: RRM1 of hnRNPLL   PubMed: 19100700

Authors: Otting, Gottfried

Citation: Wu, Zuopeng; Jia, Xinying; de la Cruz, Laura; Su, Xun-Cheng; Marzolf, Bruz; Troisch, Pamela; Zak, Daniel; Hamilton, Adam; Whittle, Belinda; Yu, Di; Sheahan, Daniel; Bertram, Edward; Alderem, Alan; Otting, Gottfried; Goodnow, Christopher; Hoyne, Gerard. "Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL"  Immunity 29, 863-875 (2008).

Assembly members:
RRM1, polymer, 112 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
RRM1: MHHHHHHMLSTEGGGSHHKV SVSPVVHVRGLCESVVEADL VEALEKFGTICYVMMMPFKR QALVEFENIDSAKECVTFAA DVPVYIAGQQAFFNYSTSKR ITRPGNTDDPSG

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts96
1H chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM1 of hnRNPLL1

Entities:

Entity 1, RRM1 of hnRNPLL 112 residues - Formula weight is not available

1   METHISHISHISHISHISHISMETLEUSER
2   THRGLUGLYGLYGLYSERHISHISLYSVAL
3   SERVALSERPROVALVALHISVALARGGLY
4   LEUCYSGLUSERVALVALGLUALAASPLEU
5   VALGLUALALEUGLULYSPHEGLYTHRILE
6   CYSTYRVALMETMETMETPROPHELYSARG
7   GLNALALEUVALGLUPHEGLUASNILEASP
8   SERALALYSGLUCYSVALTHRPHEALAALA
9   ASPVALPROVALTYRILEALAGLYGLNGLN
10   ALAPHEPHEASNTYRSERTHRSERLYSARG
11   ILETHRARGPROGLYASNTHRASPASPPRO
12   SERGLY

Samples:

sample_1: RRM1, [U-100% 13C; U-100% 15N], 0.5-0.8 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: RRM1, [U-100% 15N], 0.5-0.8 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAB28521 BAC28858 BAE02506 BAE27500 BAE42243
EMBL CAH56358
GB AAH08217 AAH12849 AAH17480 AAI23452 AAN76189
REF NP_001070368 NP_001136122 NP_001267087 NP_612403 NP_659051
SP Q8WVV9 Q921F4
TPG DAA24711