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 16355

Title: NMR Solution Structure of a Putative Uncharacterized Protein obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium target AR3449A

Authors: Mani, Rajeswari; Gurla, Swapna; Shastry, Ritu; Ciccosanti, Colleen; Foote, Erica; Jiang, Mei; Xiao, Rong; Nair, Rajesh; Everett, John; Huang, Yuanpeng; Acton, Tom; Rost, Burkhard; Montelione, Gaetano

Citation: Mani, Rajeswari; Gurla, Swapna; Shastry, Ritu; Ciccosanti, Colleen; Foote, Erica; Jiang, Mei; Xiao, Rong; Nair, Rajesh; Everett, John; Huang, Yuanpeng; Acton, Tom; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of a Putative Uncharacterized Protein obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium Target AR3449A"  Not known ., .-..

Assembly members:
AR3449A, polymer, 84 residues, 9679.103 Da.

Natural source:   Common Name: thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
AR3449A: MGHHHHHHSHMKFLVENLNG SSFELEVDYRDTLLVVKQKI ERSQHIPVSKQTLIVDGIVI LREDLTVEQCQIVPTSDIQL EVSS

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts81
1H chemical shifts552

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AR3449A1

Entities:

Entity 1, AR3449A 84 residues - 9679.103 Da.

1-10 residues MGHHHHHHSH is a N-terminal tag

1   METGLYHISHISHISHISHISHISSERHIS
2   METLYSPHELEUVALGLUASNLEUASNGLY
3   SERSERPHEGLULEUGLUVALASPTYRARG
4   ASPTHRLEULEUVALVALLYSGLNLYSILE
5   GLUARGSERGLNHISILEPROVALSERLYS
6   GLNTHRLEUILEVALASPGLYILEVALILE
7   LEUARGGLUASPLEUTHRVALGLUGLNCYS
8   GLNILEVALPROTHRSERASPILEGLNLEU
9   GLUVALSERSER

Samples:

sample_1: AR3449A, [U-100% 13C; U-100% 15N], 1.11 mM; H2O 90%; D2O 10%; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 10 mM; MES 20 mM; DDT 10 mM

sample_2: AR3449A, [U-10% 13C; U-100% 15N], 1.22 mM; H2O 90%; D2O 10%; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 10 mM; MES 20 mM; DDT 10 mM

sample_conditions_1: ionic strength: . M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aliphatic NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aromatic NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
(4,3)D GFT-HNNCABCAsample_1isotropicsample_conditions_1
(4,3)D GFT-CABCA(CO)NHNsample_1isotropicsample_conditions_1
3D GFT-HNNCABCAsample_1isotropicsample_conditions_1
3D GFT-CABCA(CO)NHNsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1

Software:

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

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
EMBL CAB81069
GB AEE82498
REF NP_192436