BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27617

Title: 1H, 13C, and 15N backbone chemical shift assignments of KPC-2   PubMed: 30552637

Deposition date: 2018-09-19 Original release date: 2018-12-14

Authors: VanPelt, Jamie; Ramelot, Theresa; Page, Richard

Citation: VanPelt, Jamie; Shurina, Ben; Ramelot, Theresa; Bonomo, Robert; Page, Richard. "."  Biomol NMR Assign 13, 139-142 (2019).

Assembly members:
KPC-2, polymer, 265 residues, Formula weight is not available

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):
KPC-2: LTNLVAEPFAKLEQDFGGSI GVYAMDTGSGATVSYRAEER FPLCSSFKGFLAAAVLARSQ QQAGLLDTPIRYGKNALVPW SPISEKYLTTGMTVAELSAA AVQYSDNAAANLLLKELGGP AGLTAFMRSIGDTTFRLDRW ELELNSAIPGDARDTSSPRA VTESLQKLTLGSALAAPQRQ QFVDWLKGNTTGNHRIRAAV PADWAVGDKTGTCGVYGTAN DYAVVWPTGRAPIVLAVYTR APNKDDKHSEAVIAAAARLA LEGLG

Data sets:
Data typeCount
13C chemical shifts761
15N chemical shifts248
1H chemical shifts248

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KPC-21

Entities:

Entity 1, KPC-2 265 residues - Formula weight is not available

1   LEUTHRASNLEUVALALAGLUPROPHEALA
2   LYSLEUGLUGLNASPPHEGLYGLYSERILE
3   GLYVALTYRALAMETASPTHRGLYSERGLY
4   ALATHRVALSERTYRARGALAGLUGLUARG
5   PHEPROLEUCYSSERSERPHELYSGLYPHE
6   LEUALAALAALAVALLEUALAARGSERGLN
7   GLNGLNALAGLYLEULEUASPTHRPROILE
8   ARGTYRGLYLYSASNALALEUVALPROTRP
9   SERPROILESERGLULYSTYRLEUTHRTHR
10   GLYMETTHRVALALAGLULEUSERALAALA
11   ALAVALGLNTYRSERASPASNALAALAALA
12   ASNLEULEULEULYSGLULEUGLYGLYPRO
13   ALAGLYLEUTHRALAPHEMETARGSERILE
14   GLYASPTHRTHRPHEARGLEUASPARGTRP
15   GLULEUGLULEUASNSERALAILEPROGLY
16   ASPALAARGASPTHRSERSERPROARGALA
17   VALTHRGLUSERLEUGLNLYSLEUTHRLEU
18   GLYSERALALEUALAALAPROGLNARGGLN
19   GLNPHEVALASPTRPLEULYSGLYASNTHR
20   THRGLYASNHISARGILEARGALAALAVAL
21   PROALAASPTRPALAVALGLYASPLYSTHR
22   GLYTHRCYSGLYVALTYRGLYTHRALAASN
23   ASPTYRALAVALVALTRPPROTHRGLYARG
24   ALAPROILEVALLEUALAVALTYRTHRARG
25   ALAPROASNLYSASPASPLYSHISSERGLU
26   ALAVALILEALAALAALAALAARGLEUALA
27   LEUGLUGLYLEUGLY

Samples:

sample_1: KPC-2, [U-100% 13C; U-100% 15N], 0.55 mM; potassium phosphate 20 mM; sodium chloride 50 mM; glycerol 3%

sample_conditions_1: ionic strength: 70 mM; pH: 5.9; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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