BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17530

Title: Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242

Authors: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242"  Not known ., .-..

Assembly members:
AHSA1-like_protein_RHE_CH02687_(1-152)_from_Rhizobium_etli, polymer, 160 residues, 17575.8 Da.

Natural source:   Common Name: Rhizobium etli   Taxonomy ID: 29449   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhizobium etli

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

Entity Sequences (FASTA):
AHSA1-like_protein_RHE_CH02687_(1-152)_from_Rhizobium_etli: MEKAMPESFVVRREAHLAAP PAAVFALMTDPEKILRWMGT EAEVEPEPGGLYLVNVTGAR FARGSFREVVPVHRLAYSFG WDGSEVVPPGSSLVEIDLIE QGGGTLLRLTHSGLPSAEQC AGHEEGWAHYLGRLTEVAAG RDPGPDPFYGRRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts639
15N chemical shifts154
1H chemical shifts1017

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AHSA1-like protein RHE_CH02687 (1-152)1

Entities:

Entity 1, AHSA1-like protein RHE_CH02687 (1-152) 160 residues - 17575.8 Da.

1   METGLULYSALAMETPROGLUSERPHEVAL
2   VALARGARGGLUALAHISLEUALAALAPRO
3   PROALAALAVALPHEALALEUMETTHRASP
4   PROGLULYSILELEUARGTRPMETGLYTHR
5   GLUALAGLUVALGLUPROGLUPROGLYGLY
6   LEUTYRLEUVALASNVALTHRGLYALAARG
7   PHEALAARGGLYSERPHEARGGLUVALVAL
8   PROVALHISARGLEUALATYRSERPHEGLY
9   TRPASPGLYSERGLUVALVALPROPROGLY
10   SERSERLEUVALGLUILEASPLEUILEGLU
11   GLNGLYGLYGLYTHRLEULEUARGLEUTHR
12   HISSERGLYLEUPROSERALAGLUGLNCYS
13   ALAGLYHISGLUGLUGLYTRPALAHISTYR
14   LEUGLYARGLEUTHRGLUVALALAALAGLY
15   ARGASPPROGLYPROASPPROPHETYRGLY
16   ARGARGLEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-100% 13C; U-100% 15N], 0.72 ± 0.07 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 mM; DTT 10 ± 0.5 mM

NC5_sample: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-5% 13C; U-100% 15N], 0.76 ± 0.07 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 mM

NC_sample_in_D2O: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-100% 13C; U-100% 15N], 0.72 ± 0.07 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

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 NOESYNC5_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 HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_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

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 v1.2, 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 v5.1, (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 ABC91458 AGS22491
REF WP_041678693