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 16380

Title: NMR solution structure of A2LD1 (gi:13879369)   PubMed: 20944236

Deposition date: 2009-06-30 Original release date: 2009-08-07

Authors: Pedrini, Bill; Serrano, Pedro; Mohanty, Biswaranjan; Geralt, Michael; Herrmann, Torsten; Wuthrich, Kurt; Wilson, Ian

Citation: Serrano, Pedro; Pedrini, Bill; Geralt, Michael; Jaudzems, Kristaps; Mohanty, Biswaranjan; Horst, Reto; Herrmann, Torsten; Elsliger, Marc-Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites"  Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun. 66, 1393-1405 (2010).

Assembly members:
gi-13879369, polymer, 149 residues, 17099.287 Da.

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):
gi-13879369: MAHIFVYGTLKRGQPNHKVM LDHSHGLAAFRGRGCTVESF PLVIAGEHNIPWLLYLPGKG HCVTGEIYEVDEQMLRFLDD FEDCPSMYQRTALQVQVLEW EGDGDPGDSVQCFVYTTATY APEWLFLPYHESYDSEGPHG LRYNPRENR

Data sets:
Data typeCount
13C chemical shifts471
15N chemical shifts153
1H chemical shifts951

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gi-138793691

Entities:

Entity 1, gi-13879369 149 residues - 17099.287 Da.

1   METALAHISILEPHEVALTYRGLYTHRLEU
2   LYSARGGLYGLNPROASNHISLYSVALMET
3   LEUASPHISSERHISGLYLEUALAALAPHE
4   ARGGLYARGGLYCYSTHRVALGLUSERPHE
5   PROLEUVALILEALAGLYGLUHISASNILE
6   PROTRPLEULEUTYRLEUPROGLYLYSGLY
7   HISCYSVALTHRGLYGLUILETYRGLUVAL
8   ASPGLUGLNMETLEUARGPHELEUASPASP
9   PHEGLUASPCYSPROSERMETTYRGLNARG
10   THRALALEUGLNVALGLNVALLEUGLUTRP
11   GLUGLYASPGLYASPPROGLYASPSERVAL
12   GLNCYSPHEVALTYRTHRTHRALATHRTYR
13   ALAPROGLUTRPLEUPHELEUPROTYRHIS
14   GLUSERTYRASPSERGLUGLYPROHISGLY
15   LEUARGTYRASNPROARGGLUASNARG

Samples:

sample_1: gi-13879369, [U-100% 13C; U-100% 15N], 1.1 ± 0.1 mM; sodium phosphate 25 mM; sodium chloride 50 mM; DTT, [U-100% 2H], 4.5 mM; DTT 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 80.25 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
5D APSY CBCACONHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
3D APSY (HA)CANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D aliphatic 1H-13C NOESYsample_1isotropicsample_conditions_1
3D aromatic 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - collection of distance restraints

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

GAPRO, Hiller, Fiorito, Wider Wuthrich - Geometric analysis of 2D APSY projections

MATCH, Volk, Herrmann, Wuthrich - Backbione assignment from APSY peaks

ASCAN, Fiorito, Herrmann, Wuthrich - Sidechain assignment with NOESY spectra

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC34147
GB AAH06662 EDL00632 EDL00634
REF NP_663441 XP_006518983
SP Q923B0

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