BMRB Entry 16816

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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/BMR16816
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:
2010-03-31
Original release date:
2010-09-17
Authors:
Liu, Gaohua; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Acton, Thomas; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR4547E"  To be published ., .-..

Assembly members:

Assembly members:
HR4547E, 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):
HR4547E: 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
  • Hide all

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

sample_nc5_rdc: HR4547E, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 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
2D 1H-15N HSQCsample_nc5_rdcisotropicsample_conditions_1

Software:

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

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

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

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16792
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