BMRB Entry 17203

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17203
MolProbity Validation Chart

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Title:
NMR structure of Acyl carrier protein from Brucella melitensis. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Deposition date:
2010-09-23
Original release date:
2010-11-01
Authors:
Barnwal, Ravi pratap; Varani, Gabriele
Citation:

Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "NMR assignment of acyl carrier protein from Brucella melitensis."  .

Assembly members:

Assembly members:
entity, polymer, 79 residues, 8395.351 Da.

Natural source:

Natural source:   Common Name: Brucella melitensis   Taxonomy ID: 29459   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Brucella melitensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SMSDTAERVKKIVVEHLGVD ADKVTEGASFIDDLGADSLD TVELVMAFEEEFGVEIPDDA AETILTVGDAVKFIDKASA

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts74
1H chemical shifts448

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Acyl carrier protein1

Entities:

Entity 1, Acyl carrier protein 79 residues - 8395.351 Da.

1   SERMETSERASPTHRALAGLUARGVALLYS
2   LYSILEVALVALGLUHISLEUGLYVALASP
3   ALAASPLYSVALTHRGLUGLYALASERPHE
4   ILEASPASPLEUGLYALAASPSERLEUASP
5   THRVALGLULEUVALMETALAPHEGLUGLU
6   GLUPHEGLYVALGLUILEPROASPASPALA
7   ALAGLUTHRILELEUTHRVALGLYASPALA
8   VALLYSPHEILEASPLYSALASERALA

Samples:

sample_1: acyl carrir protein, [U-98% 15N], 1.2-1.4 mM; H2O 93%; D2O 7%

sample_2: acyl carrir protein, [U-95% 13C; U-95% 15N], 1.2 mM; H2O 93%; D2O 7%

sample_3: acyl carrir protein 1.5 mM; H2O 93%; D2O 7%

sample_conditions_1: 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
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
EMBL CAJ10440 CDL75871
GB AAL52656 AAN29402 AAX73876 ABQ60146 ABS13303
REF WP_002963616 WP_008039152 WP_018427111 WP_024848545 WP_035033204
SP A5VP30 A9M8Y2 B0CKE3 B2S9V7 C0RHG7
AlphaFold A5VP30 A9M8Y2 B0CKE3 B2S9V7 C0RHG7

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