BMRB Entry 15085

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15085
MolProbity Validation Chart

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Title:
Complete Assignment of a hypothetical portein RP4601 (NESG ID: RpT2)from Rhodopseudomonas palustris.
Deposition date:
2006-12-22
Original release date:
2007-02-09
Authors:
Lemak, Alexander; Srisailam, Sampath; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl
Citation:

Citation: Lemak, Alexander. "Assignment of a hypothetical protein RP4601 from Rhodopseudomonas palustris"  The BMRB entry is the only known published source for the data..

Assembly members:

Assembly members:
RP4601, polymer, 66 residues, 7260.643 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21 DE3 Gold Magic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RP4601: MKVMIRKTATGHSAYVAKKD LEELIVEMENPALWGGKVTL ANGWQLELPAMAADTPLPIT VEARKL

Data sets:
Data typeCount
13C chemical shifts267
15N chemical shifts62
1H chemical shifts460

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RP4601_aasem1

Entities:

Entity 1, RP4601_aasem 66 residues - 7260.643 Da.

1   METLYSVALMETILEARGLYSTHRALATHR
2   GLYHISSERALATYRVALALALYSLYSASP
3   LEUGLUGLULEUILEVALGLUMETGLUASN
4   PROALALEUTRPGLYGLYLYSVALTHRLEU
5   ALAASNGLYTRPGLNLEUGLULEUPROALA
6   METALAALAASPTHRPROLEUPROILETHR
7   VALGLUALAARGLYSLEU

Samples:

RP4601_sample1: RP4601, [U-100% 13C; U-100% 15N], 0.7 – 1.2 mM; NaN3 0.01%; Zn 10 uM; DTT 10 mM; H2O 90%; D2O 10%; Benzamidine 1 mM

RP4601_sample2: RP4601, [U-100% 13C; U-100% 15N], 0.6 – 1.1 mM; D2O 100%; NaN3 0.01%; Zn 10 uM; DTT 10 mM; Benzamidine 1 mM

rp4601_conditions_1: ionic strength: 500 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRP4601_sample1isotropicrp4601_conditions_1
2D 1H-13C HSQCRP4601_sample1isotropicrp4601_conditions_1
3D HNCARP4601_sample1isotropicrp4601_conditions_1
3D CBCA(CO)NHRP4601_sample1isotropicrp4601_conditions_1
3D H(CCO)NHRP4601_sample1isotropicrp4601_conditions_1
HBHACBCAcoNH 4D projection ReconstructionRP4601_sample1isotropicrp4601_conditions_1
HCCCcoNH Tocsy 4D Projection ReconstructionRP4601_sample1isotropicrp4601_conditions_1
3D 1H-15N NOESYRP4601_sample1isotropicrp4601_conditions_1
3D 1H-13C NOESYRP4601_sample1isotropicrp4601_conditions_1
3D HN(COCA)CBRP4601_sample1isotropicrp4601_conditions_1
3D HCCH-TOCSY (H-Tocsy)RP4601_sample2isotropicrp4601_conditions_1
HCCH-TOCSY (C-Tocsy)RP4601_sample2isotropicrp4601_conditions_1
3D 1H-13C NOESYRP4601_sample2isotropicrp4601_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

NMRPipe v2.6, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.106, Goddard - chemical shift assignment, data analysis, peak picking

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

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAE30063
GB ACF03593
REF WP_011160155

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