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BMRB Entry 15750

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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/BMR15750
MolProbity Validation Chart

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Title: Solution NMR structure of the folded 79 residue fragment of Lin0334 fromListeria innocua. Northeast Structural Genomics Consortium target LkR15.

Deposition date: 2008-05-02 Original release date: 2008-05-12

Authors: Ramelot, Theresa; Zhao, Li; Jiang, Mei; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Zhao, Li; Jiang, Mei; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the folded 79 residue fragment of Lin0334 from Listeria innocua. Northeast Structural Genomics Consortium target LkR15."  . ., .-..

Assembly members:
Lin0334, polymer, 87 residues, 10237 Da.

Natural source:   Common Name: Listeria innocua   Taxonomy ID: 1642   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Listeria innocua

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

Entity Sequences (FASTA):
Lin0334: AFFNEQKEKVTLYLKHNIPD FNTVTFTNEEFNPIGISIDG YINNDKNLSFTAGKDVKIFS SSEELDKMFQEPRKGYDEIL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts88
1H chemical shifts589

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lin03341

Entities:

Entity 1, Lin0334 87 residues - 10237 Da.

residues 12-90 of Lin0334 followed by 8 non-native C-terminal residues (LEHHHH)

1   ALAPHEPHEASNGLUGLNLYSGLULYSVAL
2   THRLEUTYRLEULYSHISASNILEPROASP
3   PHEASNTHRVALTHRPHETHRASNGLUGLU
4   PHEASNPROILEGLYILESERILEASPGLY
5   TYRILEASNASNASPLYSASNLEUSERPHE
6   THRALAGLYLYSASPVALLYSILEPHESER
7   SERSERGLUGLULEUASPLYSMETPHEGLN
8   GLUPROARGLYSGLYTYRASPGLUILELEU
9   GLUHISHISHISHISHISHIS

Samples:

NC_sample: entity, [U-100% 13C; U-100% 15N], 0.94 ± .1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± 0.001 %; D2O 10%; H2O 90%

NC5_sample: entity, [U-5% 13C; U-100% 15N], 1.0 ± .1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± 0.001 %; D2O 10%; H2O 90%

NC_sample_in_D2O: entity, [U-100% 13C; U-100% 15N], 0.9 ± .1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± 0.001 %; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availableisotropicsample_conditions_1
2D 1H-13C HSQC (aliph)not availableisotropicsample_conditions_1
2D 1H-13C HSQCnot availableisotropicsample_conditions_1
3D 1H-15N NOESYnot availableisotropicsample_conditions_1
3D 1H-13C NOESY (aliph)not availableisotropicsample_conditions_1
3D 1H-13C NOESYnot availableisotropicsample_conditions_1
3D HNCOnot availableisotropicsample_conditions_1
3D HNCAnot availableisotropicsample_conditions_1
3D HNCACBnot availableisotropicsample_conditions_1
3D CBCA(CO)NHnot availableisotropicsample_conditions_1
3D HBHA(CO)NHnot availableisotropicsample_conditions_1
3D HCCH-TOCSYnot availableisotropicsample_conditions_1
4D CC NOESYnot availableisotropicsample_conditions_1
3D HNHAnot availableisotropicsample_conditions_1
2D 1H-13C HSQC (arom)not availableisotropicsample_conditions_1
3D 1H-13C NOESY (arom)not availableisotropicsample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.19.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure solution

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB

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