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Biological Magnetic Resonance Data Bank


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BMRB Entry 16019

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16019
MolProbity Validation Chart

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Title: NMR Structure of the protein TM1081   PubMed: 20944236

Deposition date: 2008-11-04 Original release date: 2012-05-31

Authors: Serrano, Pedro; Geralt, Micheal; Mohanty, Biswaranjan; Pedrini, Bill; Horst, Reto; Wuthrich, Kurt; Wilson, Ian

Citation: Serrano, Pedro; Pedrini, Bill; Geralt, Michael; Jaudzems, Kristaps; Mohanty, Biswaranjan; Horst, Reto; Herrmann, Torsten; Elsliger, Marc-Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites"  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1393-1405 (2010).

Assembly members:
TM1081, polymer, 125 residues, Formula weight is not available

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

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

Entity Sequences (FASTA):
TM1081: MGSDKIHHHHHHMFPYKIVD DVVILMPNKELNIENAHLFK KWVFDEFLNKGYNKIFLVLS DVESIDSFSLGVIVNILKSI SSSGGFFALVSPNEKVERVL SLTNLDRIVKIYDTISEAME EVRRK

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts118
1H chemical shifts843

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1TM10811

Entities:

Entity 1, TM1081 125 residues - Formula weight is not available

1   METGLYSERASPLYSILEHISHISHISHIS
2   HISHISMETPHEPROTYRLYSILEVALASP
3   ASPVALVALILELEUMETPROASNLYSGLU
4   LEUASNILEGLUASNALAHISLEUPHELYS
5   LYSTRPVALPHEASPGLUPHELEUASNLYS
6   GLYTYRASNLYSILEPHELEUVALLEUSER
7   ASPVALGLUSERILEASPSERPHESERLEU
8   GLYVALILEVALASNILELEULYSSERILE
9   SERSERSERGLYGLYPHEPHEALALEUVAL
10   SERPROASNGLULYSVALGLUARGVALLEU
11   SERLEUTHRASNLEUASPARGILEVALLYS
12   ILETYRASPTHRILESERGLUALAMETGLU
13   GLUVALARGARGLYS

Samples:

sample_1: TM1081, [U-98% 13C; U-98% 15N], 1.3 mM; sodium azide 0.3%; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 190 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

ASCAN, Fiorito, F., Herrmann, T. Damberger, F. Fred, Wuthrich, K. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, data analysis

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAD36158 ABQ47668 ACB10069 AGL50009 AHD19011
REF NP_228887 WP_004080402 WP_011944077 WP_012311312 WP_039446238
SP Q9X0H0

Download simulated HSQC data in one of the following formats:
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