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 15995

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15995
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Structure of TM1_TM2 in LPPG micelles   PubMed: 19383463

Deposition date: 2008-10-21 Original release date: 2009-05-18

Authors: Neumoin, Alexey; Zerbe, Oliver; Fred, Naider

Citation: Neumoin, Alexey; Cohen, Leah; Arshava, Boris; Tantry, Subramanyam; Becker, Jeffey; Zerbe, Oliver; Naider, Fred. "STRUCTURE OF A DOUBLE TRANSMEMBRANE FRAGMENT OF A G PROTEIN-COUPLED RECEPTOR IN MICELLES"  Biophys J. 96, 3187-3196 (2009).

Assembly members:
TM1_TM2 in LPPG micelles, polymer, 80 residues, 8757.232 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
TM1_TM2 in LPPG micelles: GNGSTITFDELQGLVNSTVT QAILFGVRSGAAALTLIVVW ITSRSRKTPIFIINQVSLFL IILHSALYFKYLLSNYSSVT

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts76
1H chemical shifts533

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM1_TM2 in LPPG micelles1

Entities:

Entity 1, TM1_TM2 in LPPG micelles 80 residues - 8757.232 Da.

fragment comprising part of the N-terminal domain, TM1, I1, TM2, E1

1   GLYASNGLYSERTHRILETHRPHEASPGLU
2   LEUGLNGLYLEUVALASNSERTHRVALTHR
3   GLNALAILELEUPHEGLYVALARGSERGLY
4   ALAALAALALEUTHRLEUILEVALVALTRP
5   ILETHRSERARGSERARGLYSTHRPROILE
6   PHEILEILEASNGLNVALSERLEUPHELEU
7   ILEILELEUHISSERALALEUTYRPHELYS
8   TYRLEULEUSERASNTYRSERSERVALTHR

Samples:

TM1-TM2_BBassign: LPPG 200 mM; Na-phosphate buffer 20 mM; TM1-TM2 peptide, [U-100% 13C; U-100% 15N], 0.4 mM; H2O 90%; D2O 10%

TM1-TM2_15N: LPPG 200 mM; Na-phosphate buffer 20 mM; TM1-TM2 peptide, [U-100% 15N], 0.4 mM; H2O 90%; D2O 10%

TM1-TM2_15N2H: LPPG 200 mM; Na-phosphate buffer 20 mM; TM1-TM2 peptide, [U-100% 15N; 80% 2H], 0.4 mM; H2O 90%; D2O 10%

TM1-TM2_13C: LPPG, [>85% 2H], 200 mM; Na-phosphate buffer 20 mM; TM1-TM2 peptide, [U-100% 13C; U-100% 15N], 0.4 mM; H2O 90%; D2O 10%

TM1-TM2_13C2H1H(Me): LPPG, [>85% 2H], 200 mM; Na-phosphate buffer 20 mM; TM1-TM2 peptide, [U-100% 13C; U-100% 15N; >98% 2H; Me(Ile(Hd1),Leu(Hd),Val(Hg)) 1H], 0.4 mM; D2O 100%

TM1-TM2_conditions: pH: 6.4; pressure: 1 atm; temperature: 320 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTM1-TM2_BBassignisotropicTM1-TM2_conditions
2D 1H-13C HSQCTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HNCOTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HNCATM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HNCACBTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HBHA(CO)NHTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D CBCA(CO)NHTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HN(CO)CATM1-TM2_BBassignisotropicTM1-TM2_conditions
3D HN(CA)COTM1-TM2_BBassignisotropicTM1-TM2_conditions
3D 1H-15N NOESYTM1-TM2_15NisotropicTM1-TM2_conditions
3D 1H-15N NOESYTM1-TM2_15N2HisotropicTM1-TM2_conditions
3D 1H-13C NOESYTM1-TM2_13CisotropicTM1-TM2_conditions
3D 1H-13C NOESYTM1-TM2_13C2H1H(Me)isotropicTM1-TM2_conditions

Software:

CYANA v3.0, P.GUNTERT ET AL. - refinement

XEASY v55, Bartels et al. - structure solution

CARA, Keller et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 17211 17593
PDB

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