BMRB Entry 17809

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17809
MolProbity Validation Chart

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Title:
Solution NMR structure of the AHSA1-like protein AHA_2358 from Aeromonas hydrophila refined with NH RDCs. Northeast Structural Genomics Consortium Target AhR99.
Deposition date:
2011-07-26
Original release date:
2011-08-25
Authors:
Ramelot, Theresa; Yang, Yunhuang; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rajesh, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the AHSA1-like protein AHA_2358 from Aeromonas hydrophila refined with NH RDCs. Northeast Structural Genomics Consortium Target AhR99."  .

Assembly members:

Assembly members:
AHA_2358, polymer, 144 residues, 20270 Da.

Natural source:

Natural source:   Common Name: Aeromonas hydrophila   Taxonomy ID: 644   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aeromonas hydrophila

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AHA_2358: MKISIEAHIEQEIEAVWWAW NDPDCIARWNAASSDWHTTG SRVDLVVGGRFCHHMAAKDG SAGFDFTGTFTRVEAPTRLS FVMDDGREVDVQFASEPGGT WVQETFDAETSHTPAQQQAG WQGILDNFKRYVEAAGLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts592
15N chemical shifts158
1H chemical shifts916

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AHA_23581

Entities:

Entity 1, AHA_2358 144 residues - 20270 Da.

1   METLYSILESERILEGLUALAHISILEGLU
2   GLNGLUILEGLUALAVALTRPTRPALATRP
3   ASNASPPROASPCYSILEALAARGTRPASN
4   ALAALASERSERASPTRPHISTHRTHRGLY
5   SERARGVALASPLEUVALVALGLYGLYARG
6   PHECYSHISHISMETALAALALYSASPGLY
7   SERALAGLYPHEASPPHETHRGLYTHRPHE
8   THRARGVALGLUALAPROTHRARGLEUSER
9   PHEVALMETASPASPGLYARGGLUVALASP
10   VALGLNPHEALASERGLUPROGLYGLYTHR
11   TRPVALGLNGLUTHRPHEASPALAGLUTHR
12   SERHISTHRPROALAGLNGLNGLNALAGLY
13   TRPGLNGLYILELEUASPASNPHELYSARG
14   TYRVALGLUALAALAGLYLEUGLUHISHIS
15   HISHISHISHIS

Samples:

NC_sample: AHA_2358, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; H20 90%; D20 10%

NC5_sample: AHA_2358, U-100% 15N and 5% 13C biosynthetically directed, 1.0 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H20 90%; D20 10%

NC_sample_in_D2O: AHA_2358, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; D20 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY_aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY_aromNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N hetNOENC5_sampleisotropicsample_conditions_1
2D 1H-15N HSQC_HisNC5_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

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

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.4, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance III 850 MHz

Related Database Links:

PDB
GB ABK39236 AGM44009 AHV35281 AHX32686 AHX69484
REF WP_010634059 WP_011706200 WP_016350632 WP_017410150 WP_017780145

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