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 16444

Title: NMR Chemical Shifts of GB1-SC35   PubMed: 20703835

Authors: Clayton, Jonathan; Goult, Benjamin; Lian, Lu-Yun

Citation: Clayton, Jonathan; Phelan, Marie; Goult, Benjamin; Hautbergue, Guillaume; Wilson, Stuart; Lian, Lu-Yun. "The (1)H, (13)C and (15)N backbone and side-chain assignment of the RRM domain of SC35, a regulator of pre-mRNA splicing."  Biomol. NMR Assignments 5, 7-10 (2011).

Assembly members:
SC35, polymer, 158 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):
SC35: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTEGSHH HHHHMDVEGMTSLKVDNLTY RTSPDTLRRVFEKYGRVGDV YIPRDRYTKESRGFAFVRFH DKRDAEDAMDAMDGAVLDGR ELRVQMARYGRPPDSHHS

Data sets:
Data typeCount
13C chemical shifts668
15N chemical shifts155
1H chemical shifts1028

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SC351

Entities:

Entity 1, SC35 158 residues - Formula weight is not available

Residues 1-65 represent a Protein GB1 solubility tag plus a hexa-His tag for purification.

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLUGLYSERHISHIS
7   HISHISHISHISMETASPVALGLUGLYMET
8   THRSERLEULYSVALASPASNLEUTHRTYR
9   ARGTHRSERPROASPTHRLEUARGARGVAL
10   PHEGLULYSTYRGLYARGVALGLYASPVAL
11   TYRILEPROARGASPARGTYRTHRLYSGLU
12   SERARGGLYPHEALAPHEVALARGPHEHIS
13   ASPLYSARGASPALAGLUASPALAMETASP
14   ALAMETASPGLYALAVALLEUASPGLYARG
15   GLULEUARGVALGLNMETALAARGTYRGLY
16   ARGPROPROASPSERHISHISSER

Samples:

cn_H2O: SC35, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

cn_D2O: SC35, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 100%; NaCl 100 mM

n_H2O: SC35, [U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

un_D2O: SC35 0.5 mM; D2O 100%; NaCl 100 mM

un_H2O: SC35 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCcn_H2Oisotropicsample_conditions_1
2D 1H-13C HSQCcn_D2Oisotropicsample_conditions_1
3D CBCA(CO)NHcn_H2Oisotropicsample_conditions_1
3D HNCOcn_H2Oisotropicsample_conditions_1
3D HNCAcn_H2Oisotropicsample_conditions_1
3D HNCACBcn_H2Oisotropicsample_conditions_1
3D HBHA(CO)NHcn_H2Oisotropicsample_conditions_1
3D HN(CO)CAcn_H2Oisotropicsample_conditions_1
3D HBHANHcn_H2Oisotropicsample_conditions_1
3D HCCH-TOCSYcn_D2Oisotropicsample_conditions_1
2D 1H-1H TOCSYun_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYun_D2Oisotropicsample_conditions_1
3D 1H-15N NOESYn_H2Oisotropicsample_conditions_1
3D 1H-13C NOESYcn_H2Oisotropicsample_conditions_1
3D 1H-13C NOESYcn_D2Oisotropicsample_conditions_1
3D HN(CA)COcn_H2Oisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN_Analysis v1, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17705 17706 17707
PDB
DBJ BAC03903 BAC36346 BAC39610 BAC40111 BAD74033
EMBL CAA44306 CAA44307 CAA53383 CAA67134 CAJ82901
GB AAA60306 AAC71000 AAH00339 AAH01303 AAH05493
PIR A42701
PRF 1805195A 1805195B
REF NP_001001305 NP_001009720 NP_001029290 NP_001029490 NP_001070697
SP P30352 Q01130 Q06A98 Q3MHR5 Q5R1W5
TPG DAA18198