BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17033

Title: Solution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B

Deposition date: 2010-06-30 Original release date: 2010-07-09

Authors: Mani, Rajeswari; Mao, Lei; Ciccosanti, Colleen; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Swapna, G.V.T; Everett, John; Montelione, Gaetano

Citation: Mani, Rajeswari; Mao, Lei; Ciccosanti, Colleen; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Swapna, G.V.T; Everett, John; Montelione, Gaetano. "olution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B"  Not known ., .-..

Assembly members:
entity, polymer, 97 residues, 11596.293 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: MGHHHHHHSHMVVIRRLPPG LTKEQLEEQLRPLPAHDYFE FFAADLSLYPHLYSRAYINF RNPDDILLFRDRFDGYIFLD SKGLEYPAVVEFAPFQK

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts75
1H chemical shifts552

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nonsense mRNA reducing factor1

Entities:

Entity 1, Nonsense mRNA reducing factor 97 residues - 11596.293 Da.

First 10 residue, MGHHHHHHSH is a N-terminal tag.

1   METGLYHISHISHISHISHISHISSERHIS
2   METVALVALILEARGARGLEUPROPROGLY
3   LEUTHRLYSGLUGLNLEUGLUGLUGLNLEU
4   ARGPROLEUPROALAHISASPTYRPHEGLU
5   PHEPHEALAALAASPLEUSERLEUTYRPRO
6   HISLEUTYRSERARGALATYRILEASNPHE
7   ARGASNPROASPASPILELEULEUPHEARG
8   ASPARGPHEASPGLYTYRILEPHELEUASP
9   SERLYSGLYLEUGLUTYRPROALAVALVAL
10   GLUPHEALAPROPHEGLNLYS

Samples:

sample_1: HR4714B, [U-100% 13C; U-100% 15N], 0.82 mM; H2O 90%; D2O 10%; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl 10 mM

sample_2: HR4714B, [U-10% 13C; U-99% 15N], 0.9 mM; H2O 90%; D2O 10%; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl 10 mM

sample_conditions_1: ionic strength: 110 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_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 HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D simul NOESYsample_1isotropicsample_conditions_1
3D arom NOESYsample_1isotropicsample_conditions_1

Software:

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAE02295 BAG57751
GB AAG48510 AAG60690 EAX09248 EAX09249 EAX09250
REF NP_001272234 NP_075387 XP_002742608 XP_002824527 XP_003281173
SP Q9H1J1

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts