BMRB Entry 15352

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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/BMR15352
MolProbity Validation Chart

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Title:
NMR Structure of protein Q6N9A4_RHOPA:Northeast Structural Genomics Consortium Target RpT8
Deposition date:
2007-06-29
Original release date:
2007-08-29
Authors:
SINGARAPU, KIRAN KUMAR; WU, YIBING; YEE, ADELINDA; ELETSKY, ALEX; SUKUMARAN, DINESH; GARCIA, MAITE; XIAO, RONG; BANSAL, SONAL; BARAN, MICHAEL; GAETANO, MONTELIONE; JAMES, PRESTEGARD; ARROWSMITH, CHERYL; SZYPERSKI, THOMAS
Citation:

Citation: SINGARAPU, KIRAN KUMAR; WU, YIBING; YEE, ADELINDA; ELETSKY, ALEX; SUKUMARAN, DINESH; GARCIA, MAITE; XIAO, RONG; BANSAL, SONAL; BARAN, MICHAEL; GAETANO, MONTELIONE; JAMES, PRESTEGARD; ARROWSMITH, CHERYL; SZYPERSKI, THOMAS. "NMR Structure of protein Q6N9A4_RHOPA"  .

Assembly members:

Assembly members:
rpt8 dimer, polymer, 192 residues, 20891.723 Da.

Natural source:

Natural source:   Common Name: Rhodopseudomonas palustris   Taxonomy ID: 1076   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustris

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: E. coli - cell free   Vector: pet21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rpt8 dimer: MGSSHHHHHHSSGRENLYFQ GMTDTAAEDVRKIATALLKT AIEIVSEEDGGAHNQCKLCG ASVPWLQTGDEIKHADDCPV VIAKQILSSRPKLHAVMGSS HHHHHHSSGRENLYFQGMTD TAAEDVRKIATALLKTAIEI VSEEDGGAHNQCKLCGASVP WLQTGDEIKHADDCPVVIAK QILSSRPKLHAV

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts87
1H chemical shifts586

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chain11
2chain21

Entities:

Entity 1, chain1 192 residues - 20891.723 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYMETTHRASPTHRALAALAGLUASPVAL
4   ARGLYSILEALATHRALALEULEULYSTHR
5   ALAILEGLUILEVALSERGLUGLUASPGLY
6   GLYALAHISASNGLNCYSLYSLEUCYSGLY
7   ALASERVALPROTRPLEUGLNTHRGLYASP
8   GLUILELYSHISALAASPASPCYSPROVAL
9   VALILEALALYSGLNILELEUSERSERARG
10   PROLYSLEUHISALAVALMETGLYSERSER
11   HISHISHISHISHISHISSERSERGLYARG
12   GLUASNLEUTYRPHEGLNGLYMETTHRASP
13   THRALAALAGLUASPVALARGLYSILEALA
14   THRALALEULEULYSTHRALAILEGLUILE
15   VALSERGLUGLUASPGLYGLYALAHISASN
16   GLNCYSLYSLEUCYSGLYALASERVALPRO
17   TRPLEUGLNTHRGLYASPGLUILELYSHIS
18   ALAASPASPCYSPROVALVALILEALALYS
19   GLNILELEUSERSERARGPROLYSLEUHIS
20   ALAVAL

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM

sample_2: entity, [U-50% 13C; U-50% 15N], 0.5 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D simNOESYsample_1isotropicsample_conditions_1
3D filtered NOESYsample_1isotropicsample_conditions_1
3D HCCH COSYsample_1isotropicsample_conditions_1

Software:

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

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

VNMR, Varian - collection

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

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

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB

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