BMRB Entry 19942

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19942
MolProbity Validation Chart

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Title:
Solution structure of the terminal Ig-like domain from Leptospira interrogans LigB
Deposition date:
2014-04-25
Original release date:
2014-08-26
Authors:
Ptak, Christopher; Hsieh, Ching-Lin; Lin, Yi-Pin; Maltsev, Alexander; Raman, Rajeev; Sharma, Yogendra; Oswald, Robert; Chang, Yung-Fu
Citation:

Citation: Ptak, Christopher; Hsieh, Ching-Lin; Lin, Yi-Pin; Maltsev, Alexander; Raman, Rajeev; Sharma, Yogendra; Oswald, Robert; Chang, Yung-Fu. "The NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB"  Biochemistry 53, 5249-5260 (2014).
PubMed: 25068811

Assembly members:

Assembly members:
entity, polymer, 95 residues, 9641.579 Da.

Natural source:

Natural source:   Common Name: Leptospira Interrogans   Taxonomy ID: 173   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Leptospira Interrogans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-His-Sumo

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SAATLSSISISPINTNINTT VSKQFFAVGTYSDGTKADLT SSVTWSSSNQSQAKVSNASE TKGLVTGIASGNPTIIATYG SVSGNTILTVNKTDT

Data sets:
Data typeCount
1H chemical shifts561
13C chemical shifts368
15N chemical shifts91

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 95 residues - 9641.579 Da.

1   SERALAALATHRLEUSERSERILESERILE
2   SERPROILEASNTHRASNILEASNTHRTHR
3   VALSERLYSGLNPHEPHEALAVALGLYTHR
4   TYRSERASPGLYTHRLYSALAASPLEUTHR
5   SERSERVALTHRTRPSERSERSERASNGLN
6   SERGLNALALYSVALSERASNALASERGLU
7   THRLYSGLYLEUVALTHRGLYILEALASER
8   GLYASNPROTHRILEILEALATHRTYRGLY
9   SERVALSERGLYASNTHRILELEUTHRVAL
10   ASNLYSTHRASPTHR

Samples:

sample_1: Protein, [U-95% 13C; U-95% 15N], 0.5 mM; sodium chloride 137 mM; sodium phosphate 10 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM

sample_2: Protein, [U-95% 15N], 0.5 mM; sodium chloride 137 mM; sodium phosphate 10 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM

sample_conditions_1: temperature: 286 K; pH: 7; pressure: 1 atm; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCBCACOsample_1isotropicsample_conditions_1
3D CCONHsample_1isotropicsample_conditions_1
3D HCCONHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

NCBI ACH89908.1
BMRB 25032
PDB

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