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 16795

Title: Solution NMR of Putative excisionase from Klebsiella pneumoniae, Northeast Structural Genomics Consortium Target Target KpR49

Deposition date: 2010-03-28 Original release date: 2010-04-26

Authors: Liu, G.; Hamilton, H.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.

Citation: Liu, G.; Hamilton, H.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.. "Northeast Structural Genomics Consortium Target KpR49"  To be published ., .-..

Assembly members:
KpR49, polymer, 78 residues, 9304.643 Da.

Natural source:   Common Name: Klebsiella pneumoniae   Taxonomy ID: 573   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Klebsiella pneumoniae

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

Entity Sequences (FASTA):
KpR49: MAQIIFNEEWMVEKALMVRT GLGARQIESYRQGAWIEGVH FKRVSPSGEKTLRGTTWYNY PEINKFIRDSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts77
1H chemical shifts522

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KpR491

Entities:

Entity 1, KpR49 78 residues - 9304.643 Da.

1   METALAGLNILEILEPHEASNGLUGLUTRP
2   METVALGLULYSALALEUMETVALARGTHR
3   GLYLEUGLYALAARGGLNILEGLUSERTYR
4   ARGGLNGLYALATRPILEGLUGLYVALHIS
5   PHELYSARGVALSERPROSERGLYGLULYS
6   THRLEUARGGLYTHRTHRTRPTYRASNTYR
7   PROGLUILEASNLYSPHEILEARGASPSER
8   LEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: KpR49, [U-100% 13C; U-100% 15N], 0.7 mM

sample_nc5: KpR49, [U-10% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_nc5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1

Software:

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CEL82146 CEL85567 CEP30669 CTQ13220 CTQ20086
GB ABR76809 ALD08109 ALD56363 EKB75770 ESA97574
REF WP_004179593 WP_023159475

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