BMRB Entry 16808

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16808
MolProbity Validation Chart

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Title:
Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H
Deposition date:
2010-03-31
Original release date:
2010-04-28
Authors:
Ertekin, Asli; Aramini, James; Rossi, Paolo; Ramelot, Theresa; Lee, Hsiau-Wei; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Swapna, Gurla; Rost, Burkhard; Everett, John; Acton, Thomas; Prestegard, James; Montelione, Gaetano
Citation:

Citation: Ertekin, Asli; Aramini, James; Rossi, Paolo; Lee, Hsiau-Wei; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Swapna, Gurla; Rost, Burkhard; Everett, John; Acton, Thomas; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H"  To be published ., .-..

Assembly members:

Assembly members:
HR3057H, polymer, 65 residues, 14863.186 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):
HR3057H: MGHHHHHHSHSKYAELLAII EELGKEIRPTYAGSKSAMER LKRGIIHARGLVRECLAETE RNARS

Data sets:
Data typeCount
13C chemical shifts241
15N chemical shifts54
1H chemical shifts388

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR3057H1

Entities:

Entity 1, HR3057H 65 residues - 14863.186 Da.

the protein is a dimer in solution

1   METGLYHISHISHISHISHISHISSERHIS
2   SERLYSTYRALAGLULEULEUALAILEILE
3   GLUGLULEUGLYLYSGLUILEARGPROTHR
4   TYRALAGLYSERLYSSERALAMETGLUARG
5   LEULYSARGGLYILEILEHISALAARGGLY
6   LEUVALARGGLUCYSLEUALAGLUTHRGLU
7   ARGASNALAARGSER

Samples:

sample_2: HR3057H, [U-5% 13C; U-100% 15N], 0.68 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_3: HR3057H, [U-100% 13C; U-100% 15N], 0.92 mM; HR3057H, unlabeled, 0.92 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_4: HR3057H, [U-5% 13C; U-100% 15N], 0.68 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; Polyacrylamide Gel 7%; H2O 95%; D2O 5%

sample_5: HR3057H, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; PEG 4.2%; H2O 95%; D2O 5%

sample_1: HR3057H, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-15N hetNOEsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC high res. (L/V methyl stereospecific assignment)sample_2isotropicsample_conditions_1
2D 1H-15N T1 relaxationsample_2isotropicsample_conditions_1
2D 1H-15N T2 relaxationsample_2isotropicsample_conditions_1
2D 1H-15N hetNOEsample_2isotropicsample_conditions_1
X-filtered 13C NOESYsample_3isotropicsample_conditions_1
2D 1H-15N TROSYsample_4isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_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 - data analysis,chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY v3, Goddard - data analysis, peak picking

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

PSVS v1.4, Bhattacharya and Montelione - structure quality analysis

TALOS v+, Cornilescu, Delaglio and Bax - Dihedral Angle Constraints

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

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