BMRB Entry 16792

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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/BMR16792
MolProbity Validation Chart

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Title:
Solution NMR Structure of SAP domain of MKL/myocardin-like protein 1 from H.sapiens, Northeast Structural Genomics Consortium Target Target HR4547E
Deposition date:
2010-03-28
Original release date:
2010-04-26
Authors:
Liu, G.; Janjua, J.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.
Citation:

Citation: Liu, G.; Janjua, J.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.. "Northeast Structural Genomics Consortium Target HR4547E"  To be published ., .-..

Assembly members:

Assembly members:
SAP domain of MKL/myocardin-like protein 1, polymer, 75 residues, 8161.478 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: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SAP domain of MKL/myocardin-like protein 1: MGHHHHHHSHMSTPLTGKPG ALPANLDDMKVAELKQELKL RSLPVSGTKTELIERLRAYQ DQISPVPGAPKAPAA

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts61
1H chemical shifts463

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HR4547E1

Entities:

Entity 1, HR4547E 75 residues - 8161.478 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METSERTHRPROLEUTHRGLYLYSPROGLY
3   ALALEUPROALAASNLEUASPASPMETLYS
4   VALALAGLULEULYSGLNGLULEULYSLEU
5   ARGSERLEUPROVALSERGLYTHRLYSTHR
6   GLULEUILEGLUARGLEUARGALATYRGLN
7   ASPGLNILESERPROVALPROGLYALAPRO
8   LYSALAPROALAALA

Samples:

sample_NC: HR4547E, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%

sample_nc5: HR4547E, [U-10% 13C; U-100% 15N], 0.82 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: ambient atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_nc5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16816
PDB
DBJ BAA92676 BAG10065
EMBL CAC38826 CAC38827 CAC38828 CAC38829 CAD28507
GB AAI15040 AAI41654 AAI41656 AAK54721 EAW60382
REF NP_001269589 NP_001269590 NP_001269591 NP_065882 XP_002831211
SP Q969V6
AlphaFold Q969V6

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