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Biological Magnetic Resonance Data Bank


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BMRB Entry 11504

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11504
MolProbity Validation Chart

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Title: Structure of SPOC domain of the human transcriptional corepressor SHARP   PubMed: 24268649

Deposition date: 2012-05-22 Original release date: 2013-12-02

Authors: Mikami, Suzuka; Kanaba, Teppei; Mishima, Masaki

Citation: Mikami, Suzuka; Kanaba, Teppei; Mishima, Masaki. "Structural Insights into the Recruitment of SMRT by the Corepressor SHARP under Phosphorylative Regulation"  Structure ., .-. (2013).

Assembly members:
SHARP, polymer, 169 residues, 18471.535 Da.
SMRT, polymer, 8 residues, 1102.889 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):
SHARP: VDMVQLLKKYPIVWQGLLAL KNDTAAVQLHFVSGNNVLAH RSLPLSEGGPPLRIAQRMRL EATQLEGVARRMTVETDYCL LLALPCGRDQEDVVSQTESL KAAFITYLQAKQAAGIINVP NPGSNQPAYVLQIFPPCEFS ESHLSRLAPDLLASISNISP HLMIVIASV
SMRT: YETLXDXE

Data sets:
Data typeCount
13C chemical shifts723
15N chemical shifts163
1H chemical shifts1137

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 169 residues - 18471.535 Da.

1   VALASPMETVALGLNLEULEULYSLYSTYR
2   PROILEVALTRPGLNGLYLEULEUALALEU
3   LYSASNASPTHRALAALAVALGLNLEUHIS
4   PHEVALSERGLYASNASNVALLEUALAHIS
5   ARGSERLEUPROLEUSERGLUGLYGLYPRO
6   PROLEUARGILEALAGLNARGMETARGLEU
7   GLUALATHRGLNLEUGLUGLYVALALAARG
8   ARGMETTHRVALGLUTHRASPTYRCYSLEU
9   LEULEUALALEUPROCYSGLYARGASPGLN
10   GLUASPVALVALSERGLNTHRGLUSERLEU
11   LYSALAALAPHEILETHRTYRLEUGLNALA
12   LYSGLNALAALAGLYILEILEASNVALPRO
13   ASNPROGLYSERASNGLNPROALATYRVAL
14   LEUGLNILEPHEPROPROCYSGLUPHESER
15   GLUSERHISLEUSERARGLEUALAPROASP
16   LEULEUALASERILESERASNILESERPRO
17   HISLEUMETILEVALILEALASERVAL

Entity 2, entity_2 8 residues - 1102.889 Da.

YETL(SEP)D(SEP)E

1   TYRGLUTHRLEUSEPASPSEPGLU

Samples:

sample_1: SHARP, [U-100% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; H2O 93%; D2O 7%

sample_2: SHARP, [U-15% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; H2O 93%; D2O 7%

sample_3: SMRT, [U-13C; U-15N]-Leu, Glu, Tyr, Asp, 0.9 mM; SHARP 0.9 mM; H2O 93%; D2O 7%

sample_4: SHARP, [U-100% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; D2O 100%

sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
4D HC(CO)NHsample_1isotropicsample_conditions_1
3D 13C edited NOESY-HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HN(CO)NBsample_2isotropicsample_conditions_1
15N edited NOESY-HSQCsample_1isotropicsample_conditions_1
2D 15N filtered 1H NOESYsample_3isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAA76773 BAB32786 BAG10400
EMBL CAB51072
GB AAD55931 AAI72907 AAK52750 EAW51756 EDL80993
REF NP_001258424 NP_055816 NP_062737 XP_002694185 XP_002750362
SP Q62504 Q96T58
TPG DAA21211

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