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 50447

Title: 1H, 15N, 13C resonance assignment of the Fam20C hyperphosphorylated human Osteopontin (17-314)   PubMed: 33876640

Deposition date: 2020-08-27 Original release date: 2021-05-27

Authors: Mateos, Borja; Platzer, Gerald; Zerko, Szymon; Kozminski, Wiktor; Konrat, Robert

Citation: Mateos, Borja; Holzinger, Julian; Conrad-Billroth, Clara; Platzer, Gerald; Zberko, Szymon; Sealey-Cardona, Marco; Anrather, Dorothea; Kozaminski, Wiktor; Konrat, Robert. "Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition"  Biochemistry 60, 1347-1355 (2021).

Assembly members:
entity_1, polymer, 302 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: enzymatic semisynthesis

Entity Sequences (FASTA):
entity_1: GAMGIPVKQADSGSSEEKQL YNKYPDAVATWLNPDPSQKQ NLLAPQNAVSSEETNDFKQE TLPSKSNESHDHMDDMDDED DDDHVDSQDSIDSNDSDDVD DTDDSHQSDESHHSDESDEL VTDFPTDLPATEVFTPVVPT VDTYDGRGDSVVYGLRSKSK KFRRPDIQYPDATDEDITSH MESEELNGAYKAIPVAQDLN APSDWDSRGKDSYETSQLDD QSAETHSHKQSRLYKRKAND ESNEHSDVIDSQELSKVSRE FHSHEFHSHEDMLVVDPKSK EEDKHLKFRISHELDSASSE VN

Data sets:
Data typeCount
13C chemical shifts686
15N chemical shifts215
1H chemical shifts214

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hyperphosphorylated human OPN1

Entities:

Entity 1, Hyperphosphorylated human OPN 302 residues - Formula weight is not available

1   GLYALAMETGLYILEPROVALLYSGLNALA
2   ASPSERGLYSERSERGLUGLULYSGLNLEU
3   TYRASNLYSTYRPROASPALAVALALATHR
4   TRPLEUASNPROASPPROSERGLNLYSGLN
5   ASNLEULEUALAPROGLNASNALAVALSER
6   SERGLUGLUTHRASNASPPHELYSGLNGLU
7   THRLEUPROSERLYSSERASNGLUSERHIS
8   ASPHISMETASPASPMETASPASPGLUASP
9   ASPASPASPHISVALASPSERGLNASPSER
10   ILEASPSERASNASPSERASPASPVALASP
11   ASPTHRASPASPSERHISGLNSERASPGLU
12   SERHISHISSERASPGLUSERASPGLULEU
13   VALTHRASPPHEPROTHRASPLEUPROALA
14   THRGLUVALPHETHRPROVALVALPROTHR
15   VALASPTHRTYRASPGLYARGGLYASPSER
16   VALVALTYRGLYLEUARGSERLYSSERLYS
17   LYSPHEARGARGPROASPILEGLNTYRPRO
18   ASPALATHRASPGLUASPILETHRSERHIS
19   METGLUSERGLUGLULEUASNGLYALATYR
20   LYSALAILEPROVALALAGLNASPLEUASN
21   ALAPROSERASPTRPASPSERARGGLYLYS
22   ASPSERTYRGLUTHRSERGLNLEUASPASP
23   GLNSERALAGLUTHRHISSERHISLYSGLN
24   SERARGLEUTYRLYSARGLYSALAASNASP
25   GLUSERASNGLUHISSERASPVALILEASP
26   SERGLNGLULEUSERLYSVALSERARGGLU
27   PHEHISSERHISGLUPHEHISSERHISGLU
28   ASPMETLEUVALVALASPPROLYSSERLYS
29   GLUGLUASPLYSHISLEULYSPHEARGILE
30   SERHISGLULEUASPSERALASERSERGLU
31   VALASN

Samples:

sample_1: Hyperphosphorylated human OPN, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.01%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)NNHsample_1isotropicsample_conditions_1
3D HN(COCA)NNHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

CcpNMR - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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