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 16476

Title: Solution structure of protein Atu0922 from A. tumefaciens. Northeast Structural Genomics Consortium target AtT13. Ontario Center for Structural Proteomics target ATC0905.

Authors: Gutmanas, Aleksandras; Yee, Adelinda; Lemak, Alexander; Fares, Christophe; Semesi, Anthony; Arrowsmith, Cheryl

Citation: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Semesi, Anthony; Fares, Christophe; Arrowsmith, Cheryl. "Solution NMR structure of protein atc0905 from A. tumefaciens."  To be published ., .-..

Assembly members:
ATC0905, polymer, 121 residues, Formula weight is not available

Natural source:   Common Name: Agrobacterium tumefaciens   Taxonomy ID: 358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Agrobacterium tumefaciens

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

Entity Sequences (FASTA):
ATC0905: QGHMRLKSEMFVSALIRRVF AAGGFAAVEKKGAEAAGAIF VRQRLRDGRENLYGPAPQSF ADDEDIMRAERRFETRLAGV EGEEIAALLERERRFDSDLW VVEIETDEIGTLLTLVDQPQ A

Data sets:
Data typeCount
13C chemical shifts514
15N chemical shifts122
1H chemical shifts829

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ATC09051

Entities:

Entity 1, ATC0905 121 residues - Formula weight is not available

1   GLNGLYHISMETARGLEULYSSERGLUMET
2   PHEVALSERALALEUILEARGARGVALPHE
3   ALAALAGLYGLYPHEALAALAVALGLULYS
4   LYSGLYALAGLUALAALAGLYALAILEPHE
5   VALARGGLNARGLEUARGASPGLYARGGLU
6   ASNLEUTYRGLYPROALAPROGLNSERPHE
7   ALAASPASPGLUASPILEMETARGALAGLU
8   ARGARGPHEGLUTHRARGLEUALAGLYVAL
9   GLUGLYGLUGLUILEALAALALEULEUGLU
10   ARGGLUARGARGPHEASPSERASPLEUTRP
11   VALVALGLUILEGLUTHRASPGLUILEGLY
12   THRLEULEUTHRLEUVALASPGLNPROGLN
13   ALA

Samples:

sample: ATC0905, [U-100% 13C; U-100% 15N], 1 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 uM; Roche inhibitor coctail 1 x; D2O 10%; H2O 90%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D 1H-13C arom NOESYsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H-13C NOESYsampleisotropicsample_conditions_1
3D 1H-13C aliph NOESYsampleisotropicsample_conditions_1
3D HBHA(CO)NHsampleisotropicsample_conditions_1
3D H(C)CH-TOCSY aliphaticsampleisotropicsample_conditions_1
3D CCH-TOCSY aliphaticsampleisotropicsample_conditions_1
2D 1H-13C HSQC CTsampleisotropicsample_conditions_1
2D 1H-13C HSQC aromsampleisotropicsample_conditions_1
2D HBCBCGCDHDsampleisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

ABACUS, Lemak, A - chemical shift assignment

MDDNMR, Orekhov, V. Yu. - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

Analysis, CCPN - data analysis, peak picking

NMR spectrometers:

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

Related Database Links:

PDB
GB AAK86727 EGL65971 KEY55322 KJX89147
REF NP_353942 WP_006311220 WP_010971254