BMRB Entry 16860

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16860
MolProbity Validation Chart

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Title:
Solution NMR structure of holo acyl carrier protein from Geobacter metallireducens refined with NH RDCs. Northeast Structural Genomics Consortium Target GmR141.
Deposition date:
2010-04-13
Original release date:
2010-04-29
Authors:
Ramelot, Theresa; Smola, Matthew; Zhao, Li; Ciccosanti, Colleen; Foote, Erica; Hamilton, Keith; Nair, Rajesh; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Smola, Matthew; Zhao, Li; Ciccosanti, Colleen; Foote, Erica; Hamilton, Keith; Nair, Rajesh; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of holo acyl carrier protein from Geobacter metallireducens refined with NH RDCs. Northeast Structural Genomics Consortium Target GmR141."  .

Assembly members:

Assembly members:
holo acyl carrier protein, polymer, 86 residues, 10006 Da.
PNS, non-polymer, 358.348 Da.

Natural source:

Natural source:   Common Name: Geobacter metallireducens   Taxonomy ID: 28232   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacter metallireducens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
holo acyl carrier protein: PTLDALTPIFRQVFDDDSIV LTRETSANDIDAWDSLSHMN LIVSLEVHYKIKFALGELQK LKNVGDLADLVDKKLARKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts383
15N chemical shifts90
1H chemical shifts630

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2PNS2

Entities:

Entity 1, protein 86 residues - 10006 Da.

1   PROTHRLEUASPALALEUTHRPROILEPHE
2   ARGGLNVALPHEASPASPASPSERILEVAL
3   LEUTHRARGGLUTHRSERALAASNASPILE
4   ASPALATRPASPSERLEUSERHISMETASN
5   LEUILEVALSERLEUGLUVALHISTYRLYS
6   ILELYSPHEALALEUGLYGLULEUGLNLYS
7   LEULYSASNVALGLYASPLEUALAASPLEU
8   VALASPLYSLYSLEUALAARGLYSLEUGLU
9   HISHISHISHISHISHIS

Entity 2, PNS - C11 H23 N2 O7 P S - 358.348 Da.

1   PNS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.74 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], .74 ± .05 mM; D2O 100%

holo_NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 0.83 ± .05 mM; H2O 95%; D2O 5%

holo_NC_sample_in_neutral_stretch_gel: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.5 ± .05 mM; H2O 95%; D2O 5%

holo_NC5_sample_in_negative_compressed_gel: MES 20 ± 1 mM; sodium chloride 5400 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 0.5 ± .05 mM; H2O 95%; D2O 5%

holo_NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.74 ± .05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

sample_25K: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYholo_NC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYholo_NC_sampleisotropicsample_conditions_1
4D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCholo_NC5_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
2D J-mod 1H-15N HSQCholo_NC_sample_in_neutral_stretch_gelanisotropicsample_25K
2D J-mod 1H-15N HSQCholo_NC5_sample_in_negative_compressed_gelanisotropicsample_25K
2D 1H-15N HSQCholo_NC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCholo_NC_sampleisotropicsample_conditions_1

Software:

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

VNMR v6.1C, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

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

X-PLOR_NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

Cyana v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB ABB32564 EHP86409
REF WP_004513281

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