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BMRB Entry 25081

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25081
MolProbity Validation Chart

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Title: Fyn SH2 bound

Deposition date: 2014-07-09 Original release date: 2015-07-13

Authors: Huculeci, Radu; Buts, Lieven; Lenaerts, Tom; van Nuland, Nico

Citation: Huculeci, Radu; Cilia, Elisa; Buts, Lieven; Houben, Klaartje; van Nuland, Nico; Lenaerts, Tom. "Dynamically coupled residues within the SH2 domain of FYN are key to unlock its activity"  Not known ., .-..

Assembly members:
FynSH2_bound, polymer, 112 residues, 11690.439 Da.

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):
FynSH2_bound: SSGLVPRGSHMEWYFGKLGR KDAERQLLSFGNPRGTFLIR ESETTKGAYSLSIRDWDDMK GDHVKHYKIRKLDNGGYYIT TRAQFETLQQLVQHYSERAA GLCCRLVVPCHK

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts115
1H chemical shifts774

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fyn SH2 bound1

Entities:

Entity 1, Fyn SH2 bound 112 residues - 11690.439 Da.

1   SERSERGLYLEUVALPROARGGLYSERHIS
2   METGLUTRPTYRPHEGLYLYSLEUGLYARG
3   LYSASPALAGLUARGGLNLEULEUSERPHE
4   GLYASNPROARGGLYTHRPHELEUILEARG
5   GLUSERGLUTHRTHRLYSGLYALATYRSER
6   LEUSERILEARGASPTRPASPASPMETLYS
7   GLYASPHISVALLYSHISTYRLYSILEARG
8   LYSLEUASPASNGLYGLYTYRTYRILETHR
9   THRARGALAGLNPHEGLUTHRLEUGLNGLN
10   LEUVALGLNHISTYRSERGLUARGALAALA
11   GLYLEUCYSCYSARGLEUVALVALPROCYS
12   HISLYS

Samples:

sample_1: FynSH2 bound, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.50; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

CCPNMR, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian Varian NMR Systems 600 MHz
  • Varian Varian NMR Systems 800 MHz

Related Database Links:

BMRB 17368 17369 25082
PDB
DBJ BAE33766 BAG70107 BAG70240 BAI46902
EMBL CAA36435
GB AAA36615 AAA49719 AAA82942 AAC08285 AAH32496
REF NP_001071440 NP_001073675 NP_001079077 NP_001080120 NP_001116365
SP A0JNB0 A1Y2K1 P06241 P13406 P39688
TPG DAA26259

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