BMRB Entry 5902

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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/BMR5902
MolProbity Validation Chart

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Title:
1H, 13C, and 15N Resonance Assignments of the Hath-Domain of Hepatoma-derived Growth Factor
Deposition date:
2003-08-13
Original release date:
2007-01-24
Authors:
Sue, Shih-Che; Huang, Tai-huang
Citation:

Citation: Sue, Shih-Che; Chen, Jeou-Yuan; Huang, Tai-huang. "Letter to Editor: Sequence specific 1H, 13C and 15N Resonance Assignments of the Hath-Domain of Human Hepatoma-Derived Growth Factor "  J. Biomol. NMR 29, 95-96 (2004).
PubMed: 15017145

Assembly members:

Assembly members:
hath domain of hHDGF, polymer, 110 residues, 12772.5 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET6H

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hath domain of hHDGF: MHHHHHHAMAMSRSNRQKEY KCGDLVFAKMKGYPHWPARI DEMPEAAVKSTANKYQVFFF GTHETAFLGPKDLFPYEESK EKFGKPNKRKGFSEGLWEIE NNPTVKASGY

Data sets:
Data typeCount
1H chemical shifts683
13C chemical shifts455
15N chemical shifts102

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1hath domain1

Entities:

Entity 1, hath domain 110 residues - 12772.5 Da.

1   METHISHISHISHISHISHISALAMETALA
2   METSERARGSERASNARGGLNLYSGLUTYR
3   LYSCYSGLYASPLEUVALPHEALALYSMET
4   LYSGLYTYRPROHISTRPPROALAARGILE
5   ASPGLUMETPROGLUALAALAVALLYSSER
6   THRALAASNLYSTYRGLNVALPHEPHEPHE
7   GLYTHRHISGLUTHRALAPHELEUGLYPRO
8   LYSASPLEUPHEPROTYRGLUGLUSERLYS
9   GLULYSPHEGLYLYSPROASNLYSARGLYS
10   GLYPHESERGLUGLYLEUTRPGLUILEGLU
11   ASNASNPROTHRVALLYSALASERGLYTYR

Samples:

sample_1: hath domain of hHDGF, [U-13C; U-15N], 2.0 mM; Na2HPO4 100 mM; NaCl 150 mM

sample_2: hath domain of hHDGF, [U-13C; U-15N], 1.0 mM; Na2HPO4 100 mM; NaCl 150 mM; D2O 100%

EX-condition: pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availableEX-condition
HNCAnot availablenot availableEX-condition
HN(CO)CAnot availablenot availableEX-condition
HNCOnot availablenot availableEX-condition
HN(CA)COnot availablenot availableEX-condition
CBCANHnot availablenot availableEX-condition
CBCA(CO)NHnot availablenot availableEX-condition
HBHA(CO)NHnot availablenot availableEX-condition
1H-15N TOCSYnot availablenot availableEX-condition
H(CC)(CO)NHnot availablenot availableEX-condition
CC(CO)NHnot availablenot availableEX-condition
HCCH-TOCSYnot availablenot availableEX-condition

Software:

XWINNMR v3.1 - NMR data processing

Aurelia v2.8 - NMR data processing, peak picking

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 500 MHz

Related Database Links:

PDB
DBJ BAA03903 BAA09838 BAB30979 BAC26466 BAC36126
EMBL CAB40626 CAH92417
GB AAF65469 AAH05713 AAH18991 AAH21654 AAH70943
REF NP_001119522 NP_001119523 NP_004485 NP_032257 NP_446159
SP P51858 P51859 Q8VHK7 Q9XSK7
TPG DAA31759
AlphaFold P51858 P51859 Q8VHK7 Q9XSK7 P51858 P51859 Q8VHK7 Q9XSK7 P51858 P51859 Q8VHK7 Q9XSK7

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks