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 15928

Title: Human ARNT C-Terminal PAS Domain, 3 Residue IB slip   PubMed: 19196990

Authors: Evans, Matthew; Card, Paul; Gardner, Kevin

Citation: Evans, Matthew; Card, Paul; Gardner, Kevin. "ARNT PAS-B has a fragile native state structure with an alternative {beta}-sheet register nearby in sequence space."  Proc. Natl. Acad. Sci. U.S.A. 106, 2617-2622 (2009).

Assembly members:
ARNT_PAS-B_Slipped_IB_Strand, polymer, 119 residues, 13799.596 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):
ARNT_PAS-B_Slipped_IB_Strand: GAMDNVCQPTEFISRHNIEG IFTFVDHRCVATVGYQPQEL LGKNIVEFCHPEDQQLLRDS FQQVVKLKGQVLSVMFRFRS KNQEWLWMRTSSQTAQNPYS DEIETIICTNTNVKNSSQE

Data sets:
Data typeCount
13C chemical shifts492
15N chemical shifts122
1H chemical shifts772

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ARNT_PAS-B_Slipped_IB_Strand1

Entities:

Entity 1, ARNT_PAS-B_Slipped_IB_Strand 119 residues - 13799.596 Da.

First four residues (GAMD) is a cloning artifact

1   GLYALAMETASPASNVALCYSGLNPROTHR
2   GLUPHEILESERARGHISASNILEGLUGLY
3   ILEPHETHRPHEVALASPHISARGCYSVAL
4   ALATHRVALGLYTYRGLNPROGLNGLULEU
5   LEUGLYLYSASNILEVALGLUPHECYSHIS
6   PROGLUASPGLNGLNLEULEUARGASPSER
7   PHEGLNGLNVALVALLYSLEULYSGLYGLN
8   VALLEUSERVALMETPHEARGPHEARGSER
9   LYSASNGLNGLUTRPLEUTRPMETARGTHR
10   SERSERGLNTHRALAGLNASNPROTYRSER
11   ASPGLUILEGLUTHRILEILECYSTHRASN
12   THRASNVALLYSASNSERSERGLNGLU

Samples:

sample_1: ARNT PAS-B Slipped IB Strand, [U-98% 13C; U-98% 15N], 900 uM; TRIS 50 mM; sodium chloride 17 mM; DTT 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 17 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

ARIA v2.1, Linge, O, . - chemical shift assignment, structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

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