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Solution Structure of a 8.3 kDa Protein (gene MTH1184) from Methanobacterium thermoautotrophicum
Authors
Kozlov, G., Ekiel, I., Gehring, K.
Assembly
MTH1184 monomer
Entity
1. MTH1184 monomer (polymer, Thiol state: all free), 71 monomers, 8325.424 Da Detail

MYIIFRCDCG RALYSREGAK TRKCVCGRTV NVKDRRIFGR ADDFEEASEL VRKLQEEKYG SCHFTNPSKR E


Formula weight
8325.424 Da
Source organism
Methanothermobacter thermautotrophicus
Exptl. method
NMR
Refine. method
SIMULATED ANNEALING
Data set
assigned_chemical_shifts, coupling_constants
Chem. Shift Complete
Sequence coverage: 97.2 %, Completeness: 58.5 %, Completeness (bb): 75.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All58.5 % (491 of 839)64.9 % (289 of 445)41.7 % (134 of 321)93.2 % (68 of 73)
Backbone75.2 % (319 of 424)96.6 % (141 of 146)52.9 % (110 of 208)97.1 % (68 of 70)
Sidechain44.7 % (215 of 481)49.5 % (148 of 299)37.4 % (67 of 179) 0.0 % (0 of 3)
Aromatic 8.8 % (6 of 68)17.6 % (6 of 34) 0.0 % (0 of 34)
Methyl87.0 % (47 of 54)88.9 % (24 of 27)85.2 % (23 of 27)

1. 8.3 KDA PROTEIN (GENE MTH1184)

MYIIFRCDCG RALYSREGAK TRKCVCGRTV NVKDRRIFGR ADDFEEASEL VRKLQEEKYG SCHFTNPSKR E

Sample #1

Temperature 305 (±0.1) K, pH 6.3 (±0.1)


#NameIsotope labelingTypeConcentration
18.3 KDA PROTEIN (GENE MTH1184)[U-13C; U-15N]1.0 ~ 2.0 mM
2phosphate buffer50 mM
3NaCl0.15 M
4DTT1 mM
Sample #2

Temperature 305 (±0.1) K, pH 6.3 (±0.1)


#NameIsotope labelingTypeConcentration
58.3 KDA PROTEIN (GENE MTH1184)[U-13C]1.0 ~ 2.0 mM
6phosphate buffer50 mM
7NaCl0.15 M
8DTT1 mM
Sample #3

Temperature 305 (±0.1) K, pH 6.3 (±0.1)


#NameIsotope labelingTypeConcentration
98.3 KDA PROTEIN (GENE MTH1184)[U-15N]1.0 ~ 2.0 mM
10phosphate buffer50 mM
11NaCl0.15 M
12DTT1 mM
Sample #4

Temperature 305 (±0.1) K, pH 6.3 (±0.1)


#NameIsotope labelingTypeConcentration
138.3 KDA PROTEIN (GENE MTH1184)1.0 ~ 2.0 mM
14phosphate buffer50 mM
15NaCl0.15 M
16DTT1 mM

LACS Plot; CA
Referencing offset: 0.07 ppm, Outliers: 3 Detail
LACS Plot; CB
Referencing offset: 0.07 ppm, Outliers: 3 Detail
LACS Plot; HA
Referencing offset: 0.06 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 1GH9, Strand ID: A Detail


Coupling constant
60 J values in 1 lists
Temperature 305 (±0.1) K, pH 6.3 (±0.1) Detail
Release date
2002-03-31
Citation
Structural proteomics of an archaeon
Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Savchenko, A., Cort, J.R., Booth, V., Mackereth, C.D., Saridakis, V., Ekiel, I., Kozlov, G., Maxwell, K.L., Wu, N., Mcintosh, L.P., Gehring, K., Kennedy, M.A., Davidson, A.R., Pai, E.F., Gerstein, M., Edwards, A.M., Arrowsmith, C.H.
Nat. Struct. Biol. (2000), 7, 903-909, PubMed 11017201 , DOI 10.1038/82823 ,
Entries sharing articles BMRB: 2, Swiss-Prot: 4 entries Detail
  BMRB: 5629 released on 2003-04-07
    Title 1H, 13C, and 15N resonance assignments and topology of MTH187, a conserved protein from Methanobacterium thermoautotrophicum
  BMRB: 4674 released on 2002-09-22
    Title Structural Proteomics of M. thermoautotrophicum: A global survey of non-membrane protein expression, solubility and structure
  Swiss-Prot: O26255 released on 2001-02-21
    Title P152_METTH Entity Protein MTH_152
  Swiss-Prot: O27252 released on 2001-01-24
    Title PA84_METTH Entity Protein MTH_1184
  Swiss-Prot: O26253 released on 2000-12-01
    Title NADM_METTH Entity Nicotinamide-nucleotide adenylyltransferase
  Swiss-Prot: O27652 released on 2000-05-30
    Title DNBP_METTH Entity DNA-binding protein MTH_1615
Related entities 1. MTH1184 monomer, : 1 : 1 entities Detail
Experiments performed 4 experiments Detail
nullKeywords BETA+ALPHA COMPLEX STRUCTURE