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 15914

Title: Backbone 1H, 13C and 15N Chemical Shift Assignments for Binder of Arl2 (BART)   PubMed: 18981177

Authors: Bailey, Laura; Campbell, Louise; Evetts, Katrina; Littlefield, Keily; Rajendra, Eeson; Nietlispach, Daniel; Owen, Darerca; Mott, Helen

Citation: Bailey, Laura; Campbell, Louise; Evetts, Katrina; Littlefield, Keily; Rajendra, Eeson; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: Implications for function."  J. Biol. Chem. 284, 992-999 (2009).

Assembly members:
Binder of Arl2, polymer, 137 residues, 16024.985 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):
Binder of Arl2: HMDALEGESFALSFSSASDA EFDAVVGYLEDIIMDDEFQL LQRNFMDKYYLEFEDTEENK LIYTPIFNEYISLVEKYIEE QLLQRIPEFNMAAFTTTLQH HKDEVAGDIFDMLLTFTDFL AFKEMFLDYRAEKEGRG

Data sets:
Data typeCount
13C chemical shifts576
15N chemical shifts133
1H chemical shifts906

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Binder of Arl21

Entities:

Entity 1, Binder of Arl2 137 residues - 16024.985 Da.

1   HISMETASPALALEUGLUGLYGLUSERPHE
2   ALALEUSERPHESERSERALASERASPALA
3   GLUPHEASPALAVALVALGLYTYRLEUGLU
4   ASPILEILEMETASPASPGLUPHEGLNLEU
5   LEUGLNARGASNPHEMETASPLYSTYRTYR
6   LEUGLUPHEGLUASPTHRGLUGLUASNLYS
7   LEUILETYRTHRPROILEPHEASNGLUTYR
8   ILESERLEUVALGLULYSTYRILEGLUGLU
9   GLNLEULEUGLNARGILEPROGLUPHEASN
10   METALAALAPHETHRTHRTHRLEUGLNHIS
11   HISLYSASPGLUVALALAGLYASPILEPHE
12   ASPMETLEULEUTHRPHETHRASPPHELEU
13   ALAPHELYSGLUMETPHELEUASPTYRARG
14   ALAGLULYSGLUGLYARGGLY

Samples:

sample_2: entity, [U-100% 15N], 1 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.05%; H2O 90%

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.05%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ANALYSIS, CCPN - chemical shift assignment, chemical shift calculation, peak picking

AZARA, Boucher - processing

TALOS, Cornilescu, Delaglio and Bax - Torsion angle prediction

Tensor2, P. Dosset, J-C. Hus, M. Blackledge, D. Marion - Model free analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAE00391 BAG52057 BAG60900 BAK62297
EMBL CAH91552
GB AAD20633 AAH03087 AIC50989 EAW82913 EAW82914
REF NP_001125911 NP_001233387 NP_001253957 NP_001271553 NP_036238
SP Q4R930 Q5R9K8 Q9Y2Y0