BMRB Entry 16006

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16006
MolProbity Validation Chart

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Title:
NMR structure of the protein TM1112
Deposition date:
2008-10-27
Original release date:
2009-04-14
Authors:
Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Geralt, Michel; Horst, Reto; Wilson, Ian; Wuthrich, Kurt
Citation:

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Pedrini, Bill; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Herrmann, Torsten; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures for the proteins TM1112 and TM1367."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1381-1392 (2010).
PubMed: 20944235

Assembly members:

Assembly members:
TM1112, polymer, 89 residues, 10757.4 Da.

Natural source:

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: Thermotogae   Genus/species: Thermotoga maritima

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TM1112: MEVKIEKPTPEKLKELSVEK WPIWEKEVSEFDWYYDTNET CYILEGKVEVTTEDGKKYVI EKGDLVTFPKGLRCRWKVLE PVRKHYNLF

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts91
1H chemical shifts676

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM11121

Entities:

Entity 1, TM1112 89 residues - 10757.4 Da.

1   METGLUVALLYSILEGLULYSPROTHRPRO
2   GLULYSLEULYSGLULEUSERVALGLULYS
3   TRPPROILETRPGLULYSGLUVALSERGLU
4   PHEASPTRPTYRTYRASPTHRASNGLUTHR
5   CYSTYRILELEUGLUGLYLYSVALGLUVAL
6   THRTHRGLUASPGLYLYSLYSTYRVALILE
7   GLULYSGLYASPLEUVALTHRPHEPROLYS
8   GLYLEUARGCYSARGTRPLYSVALLEUGLU
9   PROVALARGLYSHISTYRASNLEUPHE

Samples:

sample_1: TM1112, [U-98% 13C; U-98% 15N], 1.3 mM; D10-DTT 4.5 mM; DTT 0.5 mM; potassium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.03%; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D [15N,1H] HSQCsample_1isotropicsample_conditions_1
2D [13C,1H] HSQCsample_1isotropicsample_conditions_1
4D-APSY-HACANHsample_1isotropicsample_conditions_1
5D-APSY-HACACONHsample_1isotropicsample_conditions_1
5D-APSY-CBCACONHsample_1isotropicsample_conditions_1
3D 15N - resolved [1H,1H] NOESYsample_1isotropicsample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aromatic 13Csample_1isotropicsample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aliphatic 13Csample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

ASCAN, ASCAN Fiorito, Herrmann, Damberger and Wuthrich - data analysis

CARA, Keller and Wuthrich - data analysis

TOPSPIN v1.3, Bruker Biospin - collection, data analysis

MATCH, Volk, Herrmann and Wuthrich - chemical shift assignment

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAD36188 ABQ47637 ACB10038 ACM23631 ADA67724
REF NP_228918 WP_004080314 WP_012311288 WP_012896586 WP_038067843

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