BMRB Entry 15574

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15574
MolProbity Validation Chart

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Title:
NMR solution structure of KP-TerB, a tellurite resistance protein from Klebsiella pneumoniae
Deposition date:
2007-11-30
Original release date:
2008-06-27
Authors:
Sheng-Kuo, Chiang; Yuan-Chao, Lou; Chinpan, Chen
Citation:

Citation: Chiang, Sheng-Kuo; Lou, Yuan-Chao; Chen, Chinpan. "NMR solution structure of KP-TerB, a tellurite-resistance protein from Klebsiella pneumoniae"  Protein Sci. 17, 785-789 (2008).
PubMed: 18305192

Assembly members:

Assembly members:
KP-TerB, polymer, 159 residues, 17753.1 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KP-TerB: MSFFDKVKGALTSGREELTR QVGRYKNKKFMQGTVAVCAR IAVASDGVSSEEKQKMIGFL RSSEELKVFDTAEVIEFFNK LVTSFDFDLEIGKGETMKYI LALKDQPEAAQLALRVGIAV AKSDGNFDDDEKSAVREIAR SLGFDPAEFGLLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts684
15N chemical shifts156
1H chemical shifts1058

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1KP-TerB1

Entities:

Entity 1, KP-TerB 159 residues - 17753.1 Da.

Residues 152-159 are tag residues.

1   METSERPHEPHEASPLYSVALLYSGLYALA
2   LEUTHRSERGLYARGGLUGLULEUTHRARG
3   GLNVALGLYARGTYRLYSASNLYSLYSPHE
4   METGLNGLYTHRVALALAVALCYSALAARG
5   ILEALAVALALASERASPGLYVALSERSER
6   GLUGLULYSGLNLYSMETILEGLYPHELEU
7   ARGSERSERGLUGLULEULYSVALPHEASP
8   THRALAGLUVALILEGLUPHEPHEASNLYS
9   LEUVALTHRSERPHEASPPHEASPLEUGLU
10   ILEGLYLYSGLYGLUTHRMETLYSTYRILE
11   LEUALALEULYSASPGLNPROGLUALAALA
12   GLNLEUALALEUARGVALGLYILEALAVAL
13   ALALYSSERASPGLYASNPHEASPASPASP
14   GLULYSSERALAVALARGGLUILEALAARG
15   SERLEUGLYPHEASPPROALAGLUPHEGLY
16   LEULEUGLUHISHISHISHISHISHIS

Samples:

sample_1: KP-TerB, [U-99% 13C; U-99% 15N], 1 – 2 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AURELIA, Bruker Biospin, Neidig, Geyer, Gorler, Antz, Saffrich, Beneicke, Kalbitzer, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, collection, refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAH66155
EMBL CDI26599 CDM79665 CEO83280 CEP33512
GB AAA98290 AAR07675 ACI12150 AFB82882 AHE47496
REF NP_943325 WP_004026604 WP_011154616 WP_014386550 WP_023287202
SP P18779
AlphaFold P18779

Download HSQC peak lists in one of the following formats:
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