BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18869

Title: Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 2 (CDK2AP2, DOC-1R) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8910C

Authors: Ertekin, Asli; Janjua, Haleema; Kohan, Eitan; Shastry, Ritu; Pederson, Kari; Prestegard, James; Montelione, Gaetano

Citation: Ertekin, Asli; Janjua, Haleema; Shastry, Ritu; Pederson, Kari; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of CDK2-associated protein 2 (CDK2AP2; Deleted in Oral Cancer 1 Related protein, DOC-1R)"  Not known ., .-..

Assembly members:
HR8910C, polymer, 69 residues, 7644.846 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):
HR8910C: SHMAMKPPGAQGSQSTYTDL LSVIEEMGKEIRPTYAGSKS AMERLKRGIIHARALVRECL AETERNART

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts65
1H chemical shifts435

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8910C_11
2HR8910C_21

Entities:

Entity 1, HR8910C_1 69 residues - 7644.846 Da.

Protein is a dimer, residues 58-60 are part of N-terminal tag.

1   SERHISMETALAMETLYSPROPROGLYALA
2   GLNGLYSERGLNSERTHRTYRTHRASPLEU
3   LEUSERVALILEGLUGLUMETGLYLYSGLU
4   ILEARGPROTHRTYRALAGLYSERLYSSER
5   ALAMETGLUARGLEULYSARGGLYILEILE
6   HISALAARGALALEUVALARGGLUCYSLEU
7   ALAGLUTHRGLUARGASNALAARGTHR

Samples:

sample_1: HR8910C.003, [U-100% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%

sample_2: HR8910C, [U-100% 13C; U-100% 15N], 5.0 mg/mL; HR8910C 15.0 mg/mL; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x

sample_3: HR8910C, [U-100% 15N], 0.3 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x; PEG 4.2%

sample_4: HR8910C.005, [U-5% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; 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 HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 13C-filtered NOESY aliphaticsample_2isotropicsample_conditions_1
2D 13C-filtered NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-13C high res (L/V methyl stereospecific assignment)sample_4isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
3D HC(C)H-COSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.02, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

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

NMRPipe v2.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

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

SPARKY v3.112, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP O75956
PDB
DBJ BAB22939 BAB28046 BAB31046 BAG50926
EMBL CAG33331 CAG46839
GB AAC61745 AAH02850 AAH16704 AAH25656 AAP35555
REF NP_001030397 NP_001102968 NP_001253515 NP_001258778 NP_005842
SP O75956 Q58CN7 Q9CPY4
TPG DAA13560