BMRB Entry 34958

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34958
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Cdc42 in complex with inhibitory peptide
Deposition date:
2024-09-11
Original release date:
2026-01-18
Authors:
Mott, H.; Owen, D.; Murphy, N.
Citation:

Citation: Murphy, N.; Tetley, G.; Revell, J.; Mott, H.; Owen, D.. "Cyclized peptide inhibitors of the small G protein Cdc42 mimic binding of effector proteins"  To be published ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 184 residues, 20438.555 Da.
entity_2, polymer, 16 residues, 1941.242 Da.
entity_GNP, non-polymer, 522.196 Da.
entity_MG, non-polymer, 24.305 Da.
entity_HOH, water, 18.015 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQTIKCVVVGDGAVGKTCLL ISYTTNKFPSEYVPTVFDNY AVTVMIGGEPYTLGLFDTAG LEDYDRLRPLSYPQTDVFLV CFSVVSPSSFENVKEKWVPE ITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPE TAEKLARDLKAVKYVECSAL TQKGLKNVFDEAILAALEPP EPKK
entity_2: PSICHVHRPDWPCAYR

Data sets:
Data typeCount
13C chemical shifts595
15N chemical shifts176
1H chemical shifts1279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_33
4unit_44
5unit_55

Entities:

Entity 1, unit_1 184 residues - 20438.555 Da.

1   METGLNTHRILELYSCYSVALVALVALGLY
2   ASPGLYALAVALGLYLYSTHRCYSLEULEU
3   ILESERTYRTHRTHRASNLYSPHEPROSER
4   GLUTYRVALPROTHRVALPHEASPASNTYR
5   ALAVALTHRVALMETILEGLYGLYGLUPRO
6   TYRTHRLEUGLYLEUPHEASPTHRALAGLY
7   LEUGLUASPTYRASPARGLEUARGPROLEU
8   SERTYRPROGLNTHRASPVALPHELEUVAL
9   CYSPHESERVALVALSERPROSERSERPHE
10   GLUASNVALLYSGLULYSTRPVALPROGLU
11   ILETHRHISHISCYSPROLYSTHRPROPHE
12   LEULEUVALGLYTHRGLNILEASPLEUARG
13   ASPASPPROSERTHRILEGLULYSLEUALA
14   LYSASNLYSGLNLYSPROILETHRPROGLU
15   THRALAGLULYSLEUALAARGASPLEULYS
16   ALAVALLYSTYRVALGLUCYSSERALALEU
17   THRGLNLYSGLYLEULYSASNVALPHEASP
18   GLUALAILELEUALAALALEUGLUPROPRO
19   GLUPROLYSLYS

Entity 2, unit_2 16 residues - 1941.242 Da.

1   PROSERILECYSHISVALHISARGPROASP
2   TRPPROCYSALATYRARG

Entity 3, unit_3 - C10 H17 N6 O13 P3 - 522.196 Da.

1   GNP

Entity 4, unit_4 - Mg - 24.305 Da.

1   MG

Entity 5, unit_5 - 18.015 Da.

1   HOH

Samples:

sample_1: Cdc42, [U-100% 15N], 0.48 mM; Peptide, None, 0.58 mM; sodium phosphate, None, 50 mM; sodium chloride, None, 150 mM

sample_2: Cdc42, [U-13C; U-15N], 0.4 mM; Peptide, None, 0.45 mM; sodium phosphate, None, 50 mM; sodium chloride, None, 150 mM

sample_3: Cdc42, None, 0.45 mM; Peptide, [U-100% 15N], 0.415 mM; sodium phosphate, None, 50 mM; sodium chloride, None, 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D X-filtered NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4, CCPN - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 600 MHz

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