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 6052

Title: Backbone and side chain 1H, 13C, and 15N chemical shift assignments for Haemophilus human protein HR969

Authors: Ramelot, Theresa; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Montelione, Gaetano; Kennedy, Michael. "Backbone and side chain 1H, 13C, and 15N chemical shift assignments for Haemophilus human protein HR969"  . ., .-..

Assembly members:
HR969, polymer, 149 residues, 16800 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
HR969: MGHHHHHHSHMETDCNPMEL SSMSGFEEGSELNGFEGTDM KDMRLEAEAVVNDVLFAVNN MFVSKSLRCADDVAYINVET KERNRYCLELTEAGLKVVGY AFDQVDDHLQTPYHETVYSL LDTLSPAYREAFGNALLQRL EALKRDGQS

Data sets:
Data typeCount
1H chemical shifts926
13C chemical shifts583
15N chemical shifts143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR9691

Entities:

Entity 1, HR969 149 residues - 16800 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METGLUTHRASPCYSASNPROMETGLULEU
3   SERSERMETSERGLYPHEGLUGLUGLYSER
4   GLULEUASNGLYPHEGLUGLYTHRASPMET
5   LYSASPMETARGLEUGLUALAGLUALAVAL
6   VALASNASPVALLEUPHEALAVALASNASN
7   METPHEVALSERLYSSERLEUARGCYSALA
8   ASPASPVALALATYRILEASNVALGLUTHR
9   LYSGLUARGASNARGTYRCYSLEUGLULEU
10   THRGLUALAGLYLEULYSVALVALGLYTYR
11   ALAPHEASPGLNVALASPASPHISLEUGLN
12   THRPROTYRHISGLUTHRVALTYRSERLEU
13   LEUASPTHRLEUSERPROALATYRARGGLU
14   ALAPHEGLYASNALALEULEUGLNARGLEU
15   GLUALALEULYSARGASPGLYGLNSER

Samples:

sample_1: HR969, [U-15N; U-13C], 1 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM

sample_2: HR969, [U-15N], 1 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM

sample_3: HR969, [U-5% 13C; U-100% 15N], 1 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM

cond_1: pH: 6.5; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablecond_1
1H-13C HSQC (aliph)not availablenot availablecond_1
15N-edited NOESY-HQSCnot availablenot availablecond_1
HCC-TOCSY-NNHnot availablenot availablecond_1
HCCH-TOCSYnot availablenot availablecond_1
13C-edited-NOESY-HSQC (aliph)not availablenot availablecond_1
CBCACOCAHAnot availablenot availablecond_1
HNCAnot availablenot availablecond_1
HN(CO)CAnot availablenot availablecond_1
HNCOnot availablenot availablecond_1
HNCACBnot availablenot availablecond_1
CBCA(CO)NHnot availablenot availablecond_1
CC-TOCSY-NNHnot availablenot availablecond_1
HNHAnot availablenot availablecond_1
4D CC-NOESYnot availablenot availablecond_1
1H-13C HSQC (arom)not availablenot availablecond_1
1H-13C HSQC (alpha)not availablenot availablecond_1
13C-edited-NOESY-HSQC (arom)not availablenot availablecond_1

Software:

Felix v98 - processing data

Sparky v3.98 - analyzing, peak picking spectra

Autostructure v2 - assigning noe peaks

XPLOR NIH v2.0.6 - structure calculations

NMR spectrometers:

  • Varian Inova 500 MHz
  • Varian Inova 600 MHz
  • Varian Inova 750 MHz
  • Varian Inova 800 MHz

Related Database Links:

PDB
DBJ BAA91380 BAE00760 BAG52902
GB AAF36130 AAH04818 AIC51518 EAW81634 EAW81635
REF NP_001181120 NP_001229499 NP_001258833 NP_001258834 NP_001258835
SP Q4R812 Q9P0R6