BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 34439

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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/BMR34439
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title: NMR structure of repeat domain 13 of the fibrillar adhesin CshA from Streptococcus gordonii.   PubMed: 32229583

Deposition date: 2019-10-02 Original release date: 2020-04-03

Authors: Higman, V.; Back, C.; Crump, M.; Race, P.

Citation: Back, C.; Higman, V.; LeVay, K.; Patel, V.; Parnell, A.; Frankel, D.; Jenkinson, H.; Burston, S.; Crump, M.; Nobbs, A.; Race, P.. "The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture"  J. Biol. Chem. 295, 6689-6699 (2020).

Assembly members:
Surface-associated protein CshA, polymer, 118 residues, 12480.738 Da.

Natural source:   Common Name: Streptococcus gordonii   Taxonomy ID: 467705   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus gordonii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pOPINF

Entity Sequences (FASTA):
Surface-associated protein CshA: MAHHHHHHSSGLEVLFQGPT GTGATSTGPQGLPQTGTPTF QGGDPLVPIDETVEPTFEDG SKEKTIPGQGTYTIVPDGTV TFTPDKQFVGKPDPVTVKRV DKNGTPVTATYSPEFTKV

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts61
1H chemical shifts483

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 118 residues - 12480.738 Da.

1   METALAHISHISHISHISHISHISSERSER
2   GLYLEUGLUVALLEUPHEGLNGLYPROTHR
3   GLYTHRGLYALATHRSERTHRGLYPROGLN
4   GLYLEUPROGLNTHRGLYTHRPROTHRPHE
5   GLNGLYGLYASPPROLEUVALPROILEASP
6   GLUTHRVALGLUPROTHRPHEGLUASPGLY
7   SERLYSGLULYSTHRILEPROGLYGLNGLY
8   THRTYRTHRILEVALPROASPGLYTHRVAL
9   THRPHETHRPROASPLYSGLNPHEVALGLY
10   LYSPROASPPROVALTHRVALLYSARGVAL
11   ASPLYSASNGLYTHRPROVALTHRALATHR
12   TYRSERPROGLUPHETHRLYSVAL

Samples:

sample_1: CshA_RD13, [U-15N], 20 mg/mL; sodium chloride 50 mM; potassium phosphate 20 mM

sample_2: CshA_RD13, [U-13C; U-15N], 20 mg/mL; sodium chloride 50 mM; potassium phosphate 20 mM

sample_3: CshA_RD13, [U-15N], 20 mg/mL; sodium chloride 50 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
HN(CA)COsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
15N TOCSY-HSQCsample_1isotropicsample_conditions_1
15N NOESY-HSQCsample_1isotropicsample_conditions_1
13C NOESY-HSQCsample_2isotropicsample_conditions_1
13C NOESY-HSQC aromaticsample_2isotropicsample_conditions_1
15N NOESY-HSQCsample_2isotropicsample_conditions_1
13C NOESY-HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian INOVA 900 MHz

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