BMRB Entry 15584

Title:
NMR STRUCTURE OF PUTATIVE-tRNA HYDROLASE DOMAIN FROM SALMONELLA TYPHIMURIUM: NORTH EAST STRUCTURAL GENOMICS CONSORTIUM TARGET STR220
Deposition date:
2007-12-07
Original release date:
2008-01-18
Authors:
SINGARAPU, KIRAN KUMAR; WU, YIBING; SUKUMARAN, DINESH; ELETSKY, ALEX; ZERI, ANNA; WANG, DONGYAN; JANJUA, HALEEMA; OWENS, LEAH; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; G.V.T., SWAPNA; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS
Citation:

Citation: SINGARAPU, KIRAN KUMAR; WU, YIBING; SUKUMARAN, DINESH; ELETSKY, ALEX; ZERI, ANNA; WANG, DONGYAN; JANJUA, HALEEMA; OWENS, LEAH; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; G.V.T., SWAPNA; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS. "NMR STRUCTURE OF PUTATIVE-tRNA HYDROLASE DOMAIN FROM SALMONELLA TYPHIMURIUM: NORTH EAST STRUCTURAL GENOMICS CONSORTIUM TARGET STR220"  .

Assembly members:

Assembly members:
STR220, polymer, 148 residues, 16700.322 Da.

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 602   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21

Data sets:
Data typeCount
13C chemical shifts586
15N chemical shifts139
1H chemical shifts977

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1STR2201

Entities:

Entity 1, STR220 148 residues - 16700.322 Da.

1   METILEALAILESERARGTHRVALSERILE
2   ALAASPASNGLULEUGLUILETHRALAILE
3   ARGALAGLNGLYALAGLYGLYGLNHISVAL
4   ASNLYSTHRSERSERALAILEHISLEUARG
5   PHEASPILEARGALASERGLYLEUPROGLU
6   TYRTYRLYSGLNARGLEULEUTHRALASER
7   HISHISLEUILESERASPASPGLYVALILE
8   ILEILELYSALAGLNGLUPHEARGSERGLN
9   GLULEUASNARGGLUALAALAILEALAARG
10   LEUVALALAVALILELYSGLULEUTHRALA
11   GLUGLNLYSSERARGARGALATHRARGPRO
12   THRARGALASERLYSGLUARGARGLEUSER
13   SERLYSALAGLNLYSSERSERVALLYSALA
14   LEUARGGLYLYSVALARGARGPROLEUASP
15   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.4 mM; D2O, [U-100% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HCCH COSYsample_1isotropicsample_conditions_1
3D HCCH COSYsample_1isotropicsample_conditions_1
3D SimNOESYsample_1isotropicsample_conditions_1
4,3D HABCABCONHNsample_1isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

Molmol, Koradi, Billeter and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - validation

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMRJ, Varian - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAJ35184 BAP05946
EMBL CAD08699 CAR31835 CAR36151 CAR58353 CBG23262
GB AAL19204 AAO67971 AAV76276 AAX64146 ABX22610
PIR AC0532
REF NP_454848 NP_459245 WP_000560520 WP_000560521 WP_000560522

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