BMRB Entry 15835

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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/BMR15835
MolProbity Validation Chart

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Title:
Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195
Deposition date:
2008-06-27
Original release date:
2008-08-19
Authors:
SINGARAPU, KIRAN KUMAR; ELETSKY, ALEX; SATHYAMOORTHY, BHARATHWAJ; SUKUMARAN, DINESH; Wang, Dongyan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS
Citation:

Citation: SINGARAPU, KIRAN KUMAR; ELETSKY, ALEX; SATHYAMOORTHY, BHARATHWAJ; SUKUMARAN, DINESH; Wang, Dongyan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS. "Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195"  .

Assembly members:

Assembly members:
BpR195, polymer, 191 residues, 21168.037 Da.

Natural source:

Natural source:   Common Name: Bordetella parapertussis   Taxonomy ID: 519   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella parapertussis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21-23c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BpR195: MTSPSSAFPDGHGARLDAQS IRFERLLPGPIERVWAWLAD ADKRARWLAGGELPRQPGQT FELHFNHAALTAETAPARYA QYDRPIVARHTLLRCEPPRV LALTWGGGAGEAPSEVLFEL SEAGEQVRLVLTHTRLADRA AMLDVAGGWHAHLAVLAGKL AGQAPPPFWTTLAQAEQDYE QRLLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts738
15N chemical shifts175
1H chemical shifts1224

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BpR1951

Entities:

Entity 1, BpR195 191 residues - 21168.037 Da.

1   METTHRSERPROSERSERALAPHEPROASP
2   GLYHISGLYALAARGLEUASPALAGLNSER
3   ILEARGPHEGLUARGLEULEUPROGLYPRO
4   ILEGLUARGVALTRPALATRPLEUALAASP
5   ALAASPLYSARGALAARGTRPLEUALAGLY
6   GLYGLULEUPROARGGLNPROGLYGLNTHR
7   PHEGLULEUHISPHEASNHISALAALALEU
8   THRALAGLUTHRALAPROALAARGTYRALA
9   GLNTYRASPARGPROILEVALALAARGHIS
10   THRLEULEUARGCYSGLUPROPROARGVAL
11   LEUALALEUTHRTRPGLYGLYGLYALAGLY
12   GLUALAPROSERGLUVALLEUPHEGLULEU
13   SERGLUALAGLYGLUGLNVALARGLEUVAL
14   LEUTHRHISTHRARGLEUALAASPARGALA
15   ALAMETLEUASPVALALAGLYGLYTRPHIS
16   ALAHISLEUALAVALLEUALAGLYLYSLEU
17   ALAGLYGLNALAPROPROPROPHETRPTHR
18   THRLEUALAGLNALAGLUGLNASPTYRGLU
19   GLNARGLEULEUGLUHISHISHISHISHIS
20   HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.069 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_2: entity, [U-100% 15N; U-5% 13C], 1.1 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
4,3D GFT HCCH COSYsample_1isotropicsample_conditions_1
3D 15N-13C simultanious NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

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

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMRJ, Varian - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAO68965
EMBL CAE32895 CAE36637 CAE42423 CCJ49648 CCJ52144
GB AEE67412 AIW92288 AIW95609 AJB27454 ALH49292
REF NP_880798 WP_003812218 WP_003816973 WP_010927985 WP_010930760

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