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 16519

Title: Solution structure of human SDF1-alpha H25R

Deposition date: 2009-09-24 Original release date: 2012-08-03

Authors: Volkman, B.; Ziarek, J.; Peterson, F.

Citation: Ziarek, J.; Veldkamp, C.; Peterson, F.; Volkman, B.. "TBD"  To be published ., .-..

Assembly members:
SDF1a_H25R, polymer, 68 residues, 7997.572 Da.

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: pQE30-8HT

Entity Sequences (FASTA):
SDF1a_H25R: KPVSLSYRCPCRFFESHVAR ANVKRLKILNTPNCALQIVA RLKNNNRQVCIDPKLKWIQE YLEKALNK

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts77
1H chemical shifts531

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SDF1a H25R1

Entities:

Entity 1, SDF1a H25R 68 residues - 7997.572 Da.

1   LYSPROVALSERLEUSERTYRARGCYSPRO
2   CYSARGPHEPHEGLUSERHISVALALAARG
3   ALAASNVALLYSARGLEULYSILELEUASN
4   THRPROASNCYSALALEUGLNILEVALALA
5   ARGLEULYSASNASNASNARGGLNVALCYS
6   ILEASPPROLYSLEULYSTRPILEGLNGLU
7   TYRLEUGLULYSALALEUASNLYS

Samples:

sample_1: SDF1a H25R, [U-100% 13C; U-100% 15N], 3.3 mM; MES, [U-99% 2H], 25 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

SPSCAN v1.1.0, R.W. Glaser - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16142 16143 16145
PDB
DBJ BAA04648 BAA07862 BAA07863 BAA28601 BAA28602
EMBL CAG29279 CAH91884 CAJ18596
GB AAA40100 AAA40101 AAA97434 AAB32650 AAB39332
PIR I53416
REF NP_000600 NP_001009847 NP_001012495 NP_001028106 NP_001029058
SP O62657 P40224 P48061
AlphaFold P40224 O62657 P48061

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