BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 15423

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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/BMR15423
MolProbity Validation Chart

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Title: Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments for FimA

Deposition date: 2007-08-08 Original release date: 2009-10-20

Authors: Erilov, Denis; Wider, Gerhard; Glockshuber, Rudi; Puorger, Chasper; Vetsch, Michael

Citation: Erilov, Denis; Puorger, Chasper; Vetsch, Michael; Wider, Gerhard; Glockshuber, Rudi. "Structure, Folding and Stability of FimA"  J. Mol. Biol. ., .-..

Assembly members:
FimA, polymer, 184 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
FimA: AATTVNGGTVHFKGEVVNAA CAVDAGSVDQTVQLGQVRTA SLAQEGATSSAVGFNIQLND CDTNVASKAAVAFLGTAIDA GHTNVLALQSSAAGSATNVG VQILDRTGAALTLDGATFSS ETTLNNGTNTIPFQARYFAT GAATPGAANADATFKVQYQG GGGGGAATTVNGGTVHFKGE VVNA

Data sets:
Data typeCount
13C chemical shifts680
15N chemical shifts206
1H chemical shifts1046

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FimA1

Entities:

Entity 1, FimA 184 residues - Formula weight is not available

1   ALAALATHRTHRVALASNGLYGLYTHRVAL
2   HISPHELYSGLYGLUVALVALASNALAALA
3   CYSALAVALASPALAGLYSERVALASPGLN
4   THRVALGLNLEUGLYGLNVALARGTHRALA
5   SERLEUALAGLNGLUGLYALATHRSERSER
6   ALAVALGLYPHEASNILEGLNLEUASNASP
7   CYSASPTHRASNVALALASERLYSALAALA
8   VALALAPHELEUGLYTHRALAILEASPALA
9   GLYHISTHRASNVALLEUALALEUGLNSER
10   SERALAALAGLYSERALATHRASNVALGLY
11   VALGLNILELEUASPARGTHRGLYALAALA
12   LEUTHRLEUASPGLYALATHRPHESERSER
13   GLUTHRTHRLEUASNASNGLYTHRASNTHR
14   ILEPROPHEGLNALAARGTYRPHEALATHR
15   GLYALAALATHRPROGLYALAALAASNALA
16   ASPALATHRPHELYSVALGLNTYRGLNGLY
17   GLYGLYGLYGLYGLYALAALATHRTHRVAL
18   ASNGLYGLYTHRVALHISPHELYSGLYGLU
19   VALVALASNALA

Samples:

sample_1: FimA, [U-98% 13C; U-98% 15N], 1.7 mM; sodium phosphate 10 mM; H2O 50 M; D2O 5 M

sample_conditions_1: ionic strength: 18 mM; pH: 7.0; 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 HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HcCH TOCSYsample_1isotropicsample_conditions_1
CBHDsample_1isotropicsample_conditions_1
3D 1H-13C NOESY arosample_1isotropicsample_conditions_1
2D 1H-13C HSQC arosample_1isotropicsample_conditions_1

Software:

CYANA, Peter Guntert - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker DRX 750 MHz

Related Database Links:

PDB
DBJ BAE78307 BAJ46028
EMBL CAA25489 CAQ34662 CAR16032 CAS12169 CCJ47011
GB AAA24389 AAA97210 AAC77270 AAG35683 AAO84630
REF NP_418734 WP_000695553 WP_000695557 WP_000695559 WP_000695560
SP P04128

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts