BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 11546

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11546
MolProbity Validation Chart

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Title: 1H, 15N and 13C resonance assignments of the conserved domain in the middle of Schizosaccharomyces pombe SAPK-interacting protein 1   PubMed: 25428765

Deposition date: 2013-11-27 Original release date: 2015-07-27

Authors: Kataoka, Saori; Furuita, Kyoko; Hattori, Yoshikazu; Kobayashi, Naohiro; Ikegami, Takahisa; Shiozaki, Kazuhiro; Fujiwara, Toshimichi; Kojima, Chojiro

Citation: Furuita, Kyoko; Kataoka, Saori; Hattori, Yoshikazu; Kobayashi, Naohiro; Ikegami, Takahisa; Shiozaki, Kazuhiro; Fujiwara, Toshimichi; Kojima, Chojiro. "Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints"  Biomol. NMR Assignments 61, 55-64 (2015).

Assembly members:
sin1, polymer, 160 residues, 17037.0 Da.

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

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

Entity Sequences (FASTA):
sin1: GPGHMGSVSNAKAPTSALRA LLEHKENSSQNGPLAENFAT FSGHAESNALRLNIYFPSSE SPSKPLFVELRKNVLVSEAI GYILLQYVNQQLVPPIEDEA QNPNYWNLRIVEDDGELDED FPALDRVGPLSKFGFDAFAL VKATPAQIKENQAAYPFKSK

Data sets:
Data typeCount
13C chemical shifts559
15N chemical shifts144
1H chemical shifts890

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sin11

Entities:

Entity 1, sin1 160 residues - 17037.0 Da.

1   GLYPROGLYHISMETGLYSERVALSERASN
2   ALALYSALAPROTHRSERALALEUARGALA
3   LEULEUGLUHISLYSGLUASNSERSERGLN
4   ASNGLYPROLEUALAGLUASNPHEALATHR
5   PHESERGLYHISALAGLUSERASNALALEU
6   ARGLEUASNILETYRPHEPROSERSERGLU
7   SERPROSERLYSPROLEUPHEVALGLULEU
8   ARGLYSASNVALLEUVALSERGLUALAILE
9   GLYTYRILELEULEUGLNTYRVALASNGLN
10   GLNLEUVALPROPROILEGLUASPGLUALA
11   GLNASNPROASNTYRTRPASNLEUARGILE
12   VALGLUASPASPGLYGLULEUASPGLUASP
13   PHEPROALALEUASPARGVALGLYPROLEU
14   SERLYSPHEGLYPHEASPALAPHEALALEU
15   VALLYSALATHRPROALAGLNILELYSGLU
16   ASNGLNALAALATYRPROPHELYSSERLYS

Samples:

sample_1: sin1, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%; potassium phosphate 50 mM; potassium chloride 50 mM; DTT 1 mM

sample_2: sin1 0.5 mM; H2O 90%; D2O 10%; potassium phosphate 50 mM; potassium chloride 50 mM; DTT 1 mM

sample_conditions_1: pH: 6.8; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MagRO-NMRView, Johnson, One Moon Scientific - chemical shift assignment

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

Related Database Links:

EMBL CAB66311
GB AAD37449
PIR T51293
REF NP_594703
SP Q9P7Y9

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