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 15243

Title: 1H, 15N, 13C chemical shifts of human translationally controlled tumor protein   PubMed: 17897616

Authors: Feng, Yingang; Yao, Hongwei; Liu, Dongsheng; Wang, Jinfeng

Citation: Feng, Yingang; Liu, Dongsheng; Yao, Hongwei; Wang, Jinfeng. "Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR"  Arch. Biochem. Biophys. 467, 48-57 (2007).

Assembly members:
TCTP, polymer, 180 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

Entity Sequences (FASTA):
TCTP: MIIYRDLISHDEMFSDIYKI REIADGLCLEVEGKMVSRTE GNIDDSLIGGNASAEGPEGE GTESTVITGVDIVMNHHLQE TSFTKEAYKKYIKDYMKSIK GKLEEQRPERVKPFMTGAAE QIKHILANFKNYQFFIGENM NPDGMVALLDYREDGVTPYM IFFKDGLEMEKCLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts757
15N chemical shifts180
1H chemical shifts1204

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TCTP1

Entities:

Entity 1, TCTP 180 residues - Formula weight is not available

1   METILEILETYRARGASPLEUILESERHIS
2   ASPGLUMETPHESERASPILETYRLYSILE
3   ARGGLUILEALAASPGLYLEUCYSLEUGLU
4   VALGLUGLYLYSMETVALSERARGTHRGLU
5   GLYASNILEASPASPSERLEUILEGLYGLY
6   ASNALASERALAGLUGLYPROGLUGLYGLU
7   GLYTHRGLUSERTHRVALILETHRGLYVAL
8   ASPILEVALMETASNHISHISLEUGLNGLU
9   THRSERPHETHRLYSGLUALATYRLYSLYS
10   TYRILELYSASPTYRMETLYSSERILELYS
11   GLYLYSLEUGLUGLUGLNARGPROGLUARG
12   VALLYSPROPHEMETTHRGLYALAALAGLU
13   GLNILELYSHISILELEUALAASNPHELYS
14   ASNTYRGLNPHEPHEILEGLYGLUASNMET
15   ASNPROASPGLYMETVALALALEULEUASP
16   TYRARGGLUASPGLYVALTHRPROTYRMET
17   ILEPHEPHELYSASPGLYLEUGLUMETGLU
18   LYSCYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: TCTP, [U-13C; U-15N], 1.0 – 2.0 mM; sodium phosphate 50 mM; sodium chloride 200 mM; D2O 10%; DSS 0.01%; sodium azide 0.01%

sample_conditions_1: ionic strength: 250 mM; pH: 7.8; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CBCA)(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-COSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC for aliphatic regionsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC for aromatic regionsample_1isotropicsample_conditions_1

Software:

FELIX, Accelrys Software Inc. - chemical shift assignment, processing

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAC56439 BAC56463 BAC56506 BAC56521 BAE01619
EMBL CAA12650 CAA34200 CAB41990 CAB87812 CAC01240
GB AAH03352 AAH12431 AAH22436 AAH52333 AAI04563
REF NP_001014410 NP_001075598 NP_001092016 NP_001166553 NP_001253308
SP A5A6K2 P13693 P43348 P61288 Q5E984
TPG DAA15695 DAA20369 DAA23903 DAA25240