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 4374

Title: Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality

Deposition date: 1999-08-05 Original release date: 2002-04-08

Authors: Zao, X.; Goergieva, B.; Chabes, Andrej; Domkin, Vladimir; Ippel, Hans; Schleucher, Juergen; Wijmenga, Sybren; Thelander, Lars; Rothstein, R.

Citation: Zao, X.; Goergieva, B.; Chabes, Andrej; Domkin, Vladimir; Ippel, Hans; Schleucher, Juergen; Wijmenga, Sybren; Thelander, Lars; Rothstein, R.. "Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality"  Mol. Cell. Biol. 20, 9076-9083 (2000).

Assembly members:
Sml1, polymer, 104 residues, 11834.19 Da.

Natural source:   Common Name: yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: not available Saccharomyces

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Sml1: MQNSQDYFYAQNRCQQQQAP STLRTVTMAEFRRVPLPPMA EVPMLSTQNSMGSSASASAS SLEMWEKDLEERLNSIDHDM NNNKFGSGELKSMFNQGKVE EMDF

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts96
1H chemical shifts641
coupling constants97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sml1 protein1

Entities:

Entity 1, Sml1 protein 104 residues - 11834.19 Da.

1   METGLNASNSERGLNASPTYRPHETYRALA
2   GLNASNARGCYSGLNGLNGLNGLNALAPRO
3   SERTHRLEUARGTHRVALTHRMETALAGLU
4   PHEARGARGVALPROLEUPROPROMETALA
5   GLUVALPROMETLEUSERTHRGLNASNSER
6   METGLYSERSERALASERALASERALASER
7   SERLEUGLUMETTRPGLULYSASPLEUGLU
8   GLUARGLEUASNSERILEASPHISASPMET
9   ASNASNASNLYSPHEGLYSERGLYGLULEU
10   LYSSERMETPHEASNGLNGLYLYSVALGLU
11   GLUMETASPPHE

Samples:

sample_one: Sml1 0.6 mM; H2O 90%; D2O 10%

sample_2: Sml1, [U-15N], 0.4 mM; H2O 90%; D2O 10%; sodium-phosphate buffer 25 mM; NaCl 25 mM; Dithio-threitol 10 mM

sample_3: Sml1, [U-13C; U-15N], 0.6 mM; H2O 90%; D2O 10%

conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 bar; temperature: 275 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availableconditions_1

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

Related Database Links:

DBJ GAA25391
EMBL CAA86717 CAY81764
GB AAS56287 AHY76409 AJP40654 AJS61834 AJS62260
REF NP_013653
SP Q04964
TPG DAA09840
AlphaFold Q04964

Download HSQC peak lists in one of the following formats:
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