BMRB Entry 18707

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18707
MolProbity Validation Chart

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Title:
Solution structure of TamA POTRA domain I
Deposition date:
2012-09-11
Original release date:
2014-03-10
Authors:
Headey, Stephen; Belousoff, Matthew; Lithgow, Trevor
Citation:

Citation: Selkrig, Joel; Headey, Stephen; Belousoff, Matthew; Celik, Nermin; Phan, Minh-Duy; Schembri, Mark; Scanlon, Martin; Lithgow, Trevor. "The C-terminal beta-signal-like motif of TamB facilitates efficient autotransporter secretion."  .

Assembly members:

Assembly members:
entity, polymer, 89 residues, 10157.640 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: ANVRLQVEGLSGQLEKNVRA QLSTIESDEVTPDRRFRARV DDAIREGLKALGYYQPTIEF DLRPPPKKGRQVLIAKVTPG VLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts77
1H chemical shifts591

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TamA POTRA domain I1

Entities:

Entity 1, TamA POTRA domain I 89 residues - 10157.640 Da.

1   ALAASNVALARGLEUGLNVALGLUGLYLEU
2   SERGLYGLNLEUGLULYSASNVALARGALA
3   GLNLEUSERTHRILEGLUSERASPGLUVAL
4   THRPROASPARGARGPHEARGALAARGVAL
5   ASPASPALAILEARGGLUGLYLEULYSALA
6   LEUGLYTYRTYRGLNPROTHRILEGLUPHE
7   ASPLEUARGPROPROPROLYSLYSGLYARG
8   GLNVALLEUILEALALYSVALTHRPROGLY
9   VALLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: TamA domain I, [U-99% 13C; U-99% 15N], 1.8 ± 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.4; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D (H)C(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

ATHNOS-CANDID v2.0.2, Herrmann, Guntert and Wuthrich - structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB38621 BAE78221 BAG80050 BAI28525 BAI33699
EMBL CAP78741 CAQ34571 CAR01195 CAR05962 CAR11033
GB AAA97116 AAC77177 AAG59418 AAN45685 AAN83739
PIR F86119
REF NP_313225 NP_418641 NP_709978 WP_000338225 WP_001269283
SP P0ADE4 P0ADE5
AlphaFold P0ADE4 P0ADE5

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