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Biological Magnetic Resonance Data Bank


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BMRB Entry 19755

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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/BMR19755
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Title: Structure determination of substrate binding domain of MecA

Deposition date: 2014-01-29 Original release date: 2015-02-09

Authors: Zhang, Yong-hui; Zhang, Yi; Jin, Changwen; Shi, Yigong

Citation: Zhang, Yong-hui; Zhang, Yi; Jin, Changwen; Shi, Yigong. "NMR structure and interaction analysis of the substrate binding domain of MecA"  Nat. Struct. Biol. ., .-..

Assembly members:
MecA-NTD, polymer, 90 residues, 10904.278 Da.

Natural source:   Common Name: firmicutes   Taxonomy ID: 703612   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

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

Entity Sequences (FASTA):
MecA-NTD: MEIERINEHTVKFYMSYGDI EDRGFDREEIWYNRERSEEL FWEVMDEVHEEEEFAVEGPL WIQVQALDKGLEIIVTKAQL SKDLDKLVPR

Data sets:
Data typeCount
13C chemical shifts409
15N chemical shifts90
1H chemical shifts618

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MecA1

Entities:

Entity 1, MecA 90 residues - 10904.278 Da.

1   METGLUILEGLUARGILEASNGLUHISTHR
2   VALLYSPHETYRMETSERTYRGLYASPILE
3   GLUASPARGGLYPHEASPARGGLUGLUILE
4   TRPTYRASNARGGLUARGSERGLUGLULEU
5   PHETRPGLUVALMETASPGLUVALHISGLU
6   GLUGLUGLUPHEALAVALGLUGLYPROLEU
7   TRPILEGLNVALGLNALALEUASPLYSGLY
8   LEUGLUILEILEVALTHRLYSALAGLNLEU
9   SERLYSASPLEUASPLYSLEUVALPROARG

Samples:

sample_1: MecA-NTD, [U-13C; U-15N], 1.0 mM; sodium chloride 140 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 7.3; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

CCPN_Analysis v2, CCPN - chemical shift assignment, data analysis, peak picking

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

MARS, Markus Zweckstetter - chemical shift assignment

CYANA v2, Guntert, Mumenthaler and Wuthrich - geometry optimization

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAI84705 BAM50072 BAM57340 GAK78855
EMBL CAB13009 CCU57623 CDH96423 CEI56289 CEJ76712
GB AAC36956 ADM37217 ADP31634 ADV96142 AEP86108
REF NP_389034 WP_003224603 WP_003232942 WP_003239278 WP_003245194
SP P37958

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