BMRB Entry 4899

Title:
SMN Tudor Domain Structure and its Interaction with the Sm Proteins
Deposition date:
2000-11-15
Original release date:
2001-05-03
Authors:
Selenko, Philipp; Sprangers, Remco; Stier, Gunter; Buehler, Dirk; Fischer, Utz; Sattler, Michael
Citation:

Citation: Selenko, Philipp; Sprangers, Remco; Stier, Gunter; Buehler, Dirk; Fischer, Utz; Sattler, Michael. "SMN Tudor Domain Structure and its Interaction with the Sm Proteins"  Nat. Struct. Biol. 8, 27-31 (2001).
PubMed: 11135666

Assembly members:

Assembly members:
Survival of Motor Neurons protein, polymer, 91 residues, 10049.0 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9d

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts61
1H chemical shifts373

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tudor1

Entities:

Entity 1, tudor 91 residues - 10049.0 Da.

1   GLYALAMETLYSLYSASNTHRALAALASER
2   LEUGLNGLNTRPLYSVALGLYASPLYSCYS
3   SERALAILETRPSERGLUASPGLYCYSILE
4   TYRPROALATHRILEALASERILEASPPHE
5   LYSARGGLUTHRCYSVALVALVALTYRTHR
6   GLYTYRGLYASNARGGLUGLUGLNASNLEU
7   SERASPLEULEUSERPROILECYSGLUVAL
8   ALAASNASNILEGLUGLNASNALAGLNGLU
9   ASNGLUASNGLUSERGLNVALSERTHRASP
10   GLU

Samples:

sample_1: Survival of Motor Neurons protein, [U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; H2O 95%; D2O 5%

sample_2: Survival of Motor Neurons protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; H2O 95%; D2O 5%

sample_3: Survival of Motor Neurons protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; D2O 100%

Cond_sample_1: pH: 6.3; pressure: 1 atm; temperature: 295 K

Cond_sample_2: pH: 6.3; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
H(C)CH TOCSYnot availablenot availablenot available
CCH TOCSYnot availablenot availablenot available
15N edited NOESYnot availablenot availablenot available
13C edited NOESYnot availablenot availablenot available
IPAP (dipolar couplings)not availablenot availablenot available

Software:

xwinnmr v2.6 - recording experiments

NMRPipe - processing spectra

XEASY - chemical shift assignment

CNS - structure calculations

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 18005 18007
PDB
DBJ BAF82358 BAJ21116
EMBL CAH89989
GB AAA64505 AAA66242 AAC50473 AAC52048 AAC62262
REF NP_000335 NP_001124942 NP_001284644 NP_059107 NP_075012
SP Q16637 Q5RE18
AlphaFold Q16637 Q5RE18

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