BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 15381

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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/BMR15381
MolProbity Validation Chart

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Title: Solution structure of the E. coli Tat proofreading chaperone protein NapD   PubMed: 17901208

Deposition date: 2007-07-17 Original release date: 2007-08-16

Authors: Spronk, Chris; Vuister, Geerten; Sargent, Frank

Citation: Maillard, Julien; Spronk, Chris; Buchanan, Grant; Lyall, Verity; Richardson, David; Palmer, Tracy; Vuister, Geerten; Sargent, Frank. "Structural diversity in twin-arginine signal peptide binding proteins"  Proc. Natl. Acad. Sci. U.S.A. 104, 15641-15646 (2007).

Assembly members:
NapD, polymer, 95 residues, 10549.718 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NapD: MHTNWQVCSLVVQAKSERIS DISTQLNAFPGCEVAVSDAP SGQLIVVVEAEDSETLIQTI ESVRNVEGVLAVSLVYHQQE EQGEETPRSHHHHHH

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts85
1H chemical shifts561

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NapD1

Entities:

Entity 1, NapD 95 residues - 10549.718 Da.

1   METHISTHRASNTRPGLNVALCYSSERLEU
2   VALVALGLNALALYSSERGLUARGILESER
3   ASPILESERTHRGLNLEUASNALAPHEPRO
4   GLYCYSGLUVALALAVALSERASPALAPRO
5   SERGLYGLNLEUILEVALVALVALGLUALA
6   GLUASPSERGLUTHRLEUILEGLNTHRILE
7   GLUSERVALARGASNVALGLUGLYVALLEU
8   ALAVALSERLEUVALTYRHISGLNGLNGLU
9   GLUGLNGLYGLUGLUTHRPROARGSERHIS
10   HISHISHISHISHIS

Samples:

NapD_13C_15N: NapD, [U-100% 13C; U-100% 15N], 0.5 mM; deuterated Tris 20 mM; DTT 1 mM

NapD_15N: NapD, [U-100% 15N], 0.5 mM; deuterated Tris 20 mM; DTT 1 mM

NapD_10%_13C_15N: NapD, [U-10% 13C; U-100% 15N], 0.5 mM; deuterated Tris 20 mM; DTT 1 mM

sample_conditions_1: pH: 7.4; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNapD_13C_15Nisotropicsample_conditions_1
3D HNCACBNapD_13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NHNapD_13C_15Nisotropicsample_conditions_1
3D HBHA(CBCACO)NHNapD_13C_15Nisotropicsample_conditions_1
3D HN(CA)HANapD_13C_15Nisotropicsample_conditions_1
3D 1H-15N NOESYNapD_13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESYNapD_13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromaticNapD_13C_15Nisotropicsample_conditions_1
3D (H)CCH-TOCSYNapD_13C_15Nisotropicsample_conditions_1
3D H(C)CH-TOCSYNapD_13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC constant timeNapD_10%_13C_15Nisotropicsample_conditions_1

Software:

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

ATHNOS-CANDID, Herrmann, T., G ntert, P. & W thrich, K. - Automated NOE assignment, data analysis, peak picking

CYANA, P Guntert, C Mumenthaler and K Wuthrich - structure calculation engine

X-PLOR NIH, CD Schwieters, JJ Kuszewski, N Tjandra and GM Clore - Structure refinement

WhatIF, G Vriend - structure validation

YASARA, E. Krieger, Yasara Biosciences - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA15990 BAB36519 BAG77999 BAI26345 BAI31453
EMBL CAP76709 CAQ32610 CAQ89798 CAQ99134 CAR03635
GB AAA16400 AAC75267 AAG57342 AAN43810 AAN81200
REF NP_311123 NP_416711 NP_708103 WP_000557371 WP_000557372
SP P0A9I5 P0A9I6 P0A9I7

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