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 25029

Title: Specific and Non-Specific Interactions in Ultra-Weak Protein-Protein Associations Revealed by Solvent Paramagnetic Relaxation Enhancements   PubMed: 24969589

Deposition date: 2014-06-19 Original release date: 2014-06-24

Authors: Johansson, Helle; Jensen, Malene; Gesmar, Henrik; Meier, Sebastian; Vinther, Joachim; Keeler, Camille; Hodsdon, Michael; Led, Jens

Citation: Johansson, Helle; Jensen, Malene Ringkjobing; Gesmar, Henrik; Meier, Sebastian; Vinther, Joachim; Keeler, Camille; Hodsdon, Michael; Led, Jens. "Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements."  J. Am. Chem. Soc. 136, 10277-10286 (2014).

Assembly members:
hGH, polymer, 191 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
hGH: FPTIPLSRLFDNAMLRAHRL HQLAFDTYQEFEEAYIPKEQ KYSFLQNPQTSLCFSESIPT PSNREETQQKSNLELLRISL LLIQSWLEPVQFLRSVFANS LVYGASDSNVYDLLKDLEEG IQTLMGRLEDGSPRTGQIFK QTYSKFDTNSHNDDALLKNY GLLYCFRKDMDKVETFLRIV QCRSVEGSCGF

Data sets:
Data typeCount
13C chemical shifts455
1H chemical shifts148
15N chemical shifts148

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hGH1

Entities:

Entity 1, hGH 191 residues - Formula weight is not available

1   PHEPROTHRILEPROLEUSERARGLEUPHE
2   ASPASNALAMETLEUARGALAHISARGLEU
3   HISGLNLEUALAPHEASPTHRTYRGLNGLU
4   PHEGLUGLUALATYRILEPROLYSGLUGLN
5   LYSTYRSERPHELEUGLNASNPROGLNTHR
6   SERLEUCYSPHESERGLUSERILEPROTHR
7   PROSERASNARGGLUGLUTHRGLNGLNLYS
8   SERASNLEUGLULEULEUARGILESERLEU
9   LEULEUILEGLNSERTRPLEUGLUPROVAL
10   GLNPHELEUARGSERVALPHEALAASNSER
11   LEUVALTYRGLYALASERASPSERASNVAL
12   TYRASPLEULEULYSASPLEUGLUGLUGLY
13   ILEGLNTHRLEUMETGLYARGLEUGLUASP
14   GLYSERPROARGTHRGLYGLNILEPHELYS
15   GLNTHRTYRSERLYSPHEASPTHRASNSER
16   HISASNASPASPALALEULEULYSASNTYR
17   GLYLEULEUTYRCYSPHEARGLYSASPMET
18   ASPLYSVALGLUTHRPHELEUARGILEVAL
19   GLNCYSARGSERVALGLUGLYSERCYSGLY
20   PHE

Samples:

sample_1: hGH, [U-100% 13C; U-100% 15N], 0.175 mM; NaCl 25 mM; NaH2PO4 15.4 mM; Na2HPO4 9.5 mM; NaN3 1.54 mM

sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 0.0706 M

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 4689
PDB
DBJ BAJ21175
EMBL CAA23778 CAA23779
GB AAA52549 AAA72260 AAA98618 AAC42099 AAF23135
PRF 1403262B
REF NP_000506 NP_001184093 NP_001277233 XP_002827754 XP_003262698
SP P01241 P58756
TPE CDW51387 CDW51389 CDW51391 CDW51396 CDW51399

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