BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 16313

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16313

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Title: NMR Solution Structure of a Tubulin folding cofactor B obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium target AR3436A

Deposition date: 2009-05-22 Original release date: 2009-10-20

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

Citation: Mani, Rajeswari; Gurla, Swapna; Shastry, Ritu; Foote, Erica; Ciccosanti, Colleen; Jiang, Mei; Xiao, Rong; Nair, Rajesh; Everett, John; Huang, Yuanpeng; Acton, Tom; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of Tbulin folding Cofactor B obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium"  .

Assembly members:
AR3436A, polymer, 97 residues, 10852.224 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   Vector: pET 21-23C

Entity Sequences (FASTA):
AR3436A: MGHHHHHHSHGDDSVHLHIT HANLKSFSADARFSPQMSVE AVKEKLWKKCGTSVNSMALE LYDDSGSKVAVLSDDSRPLG FFSPFDGFRLHIIDLDP

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts86
1H chemical shifts551

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AR3436A1

Entities:

Entity 1, AR3436A 97 residues - 10852.224 Da.

1-10 residues - MGHHHHHHSH is a N-terminal tag

1   METGLYHISHISHISHISHISHISSERHIS
2   GLYASPASPSERVALHISLEUHISILETHR
3   HISALAASNLEULYSSERPHESERALAASP
4   ALAARGPHESERPROGLNMETSERVALGLU
5   ALAVALLYSGLULYSLEUTRPLYSLYSCYS
6   GLYTHRSERVALASNSERMETALALEUGLU
7   LEUTYRASPASPSERGLYSERLYSVALALA
8   VALLEUSERASPASPSERARGPROLEUGLY
9   PHEPHESERPROPHEASPGLYPHEARGLEU
10   HISILEILEASPLEUASPPRO

Samples:

sample_1: AR3436A, [U-100% 13C; U-100% 15N], 0.78 mM; H2O 95%; D2O 5%; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_2: AR3436A, [U-100% 13C; U-100% 15N], 0.95 mM; H2O 95%; D2O 5%; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_3: AR3436A, [U-100% 13C; U-100% 15N], 0.4 mM; H2O 95%; D2O 5%; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_4: AR3436A, [U-10% 13C; U-100% 15N], 0.56 mM; H2O 95%; D2O 5%; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_conditions_1: ionic strength: 15 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13Caliphatic 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_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
(4,3)D GFT-HNNCABCAsample_3isotropicsample_conditions_1
(4,3)D GFT-CABCACA(CO)NHNsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNHAsample_4isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
(4,3)D GFT-HABCAB(CO)NHNsample_3isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_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
DBJ BAD43946 BAD44029 BAD44467
GB AAF02820 AAM22958 AEE74873
REF NP_187633
SP Q67Z52
AlphaFold Q67Z52

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