BMRB Entry 16129

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16129
MolProbity Validation Chart

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Title:
The NMR structure of the TC10 and Cdc42 interacting domain of CIP4
Deposition date:
2009-01-22
Original release date:
2009-05-06
Authors:
Kumeta, Hiroyuki; Kanoh, Daisuke; Kobashigawa, Yoshihiro; Inagaki, Fuyuhiko
Citation:

Citation: Kobashigawa, Yoshihiro; Kumeta, Hiroyuki; Kanoh, Daisuke; Inagaki, Fuyuhiko. "The NMR structure of the TC10 and Cdc42 interacting domain of CIP4"  J. Biomol. NMR 44, 113-118 (2009).
PubMed: 19387844

Assembly members:

Assembly members:
TC10 and Cdc42, polymer, 98 residues, 11534.024 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: pGB1HPS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TC10 and Cdc42: GPHMTEDFSHLPPEQQRKRL QQQLEERSRELQKEVDQREA LKKMKDVYEKTPQMGDPASL EPQIAETLSNIERLKLEVQK YEAWLAEAESRVLSNRGD

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts110
1H chemical shifts728

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TC10 and Cdc421

Entities:

Entity 1, TC10 and Cdc42 98 residues - 11534.024 Da.

1   GLYPROHISMETTHRGLUASPPHESERHIS
2   LEUPROPROGLUGLNGLNARGLYSARGLEU
3   GLNGLNGLNLEUGLUGLUARGSERARGGLU
4   LEUGLNLYSGLUVALASPGLNARGGLUALA
5   LEULYSLYSMETLYSASPVALTYRGLULYS
6   THRPROGLNMETGLYASPPROALASERLEU
7   GLUPROGLNILEALAGLUTHRLEUSERASN
8   ILEGLUARGLEULYSLEUGLUVALGLNLYS
9   TYRGLUALATRPLEUALAGLUALAGLUSER
10   ARGVALLEUSERASNARGGLYASP

Samples:

13C15N: entity, [U-13C; U-15N], mM; MES 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC13C15Nisotropicsample_conditions_1
3D HNCO13C15Nisotropicsample_conditions_1
3D HN(CO)CA13C15Nisotropicsample_conditions_1
3D HNCA13C15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C15Nisotropicsample_conditions_1
3D HNCACB13C15Nisotropicsample_conditions_1
3D HN(CA)HA13C15Nisotropicsample_conditions_1
3D HBHA(CO)NH13C15Nisotropicsample_conditions_1
3D C(CO)NH13C15Nisotropicsample_conditions_1
3D H(CCO)NH13C15Nisotropicsample_conditions_1
3D HCCH-TOCSY13C15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY13C15Nisotropicsample_conditions_1
2D (HB)CB(CGCD)HD13C15Nisotropicsample_conditions_1
2D (HB)CB(CGCDCE)HE13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY (Aromatic)13C15Nisotropicsample_conditions_1
3D HCCH-TOCSY (Aromatic)13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC (Aromatic)13C15Nisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking, refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAE00629 BAF80144 BAG36103 BAK63850
EMBL CAA04062 CAG38751
GB AAH13002 AAK77492 AAL89588 AAM46851 AAP35344
REF NP_001275891 NP_001275892 NP_004231 XP_001092276 XP_003316087
SP Q15642
AlphaFold Q15642

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