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PDBsum entry 1bus
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Proteinase inhibitor PDB id
1bus

 

 

 

 

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Contents
Protein chain
57 a.a. *
* Residue conservation analysis
PDB id:
1bus
Name: Proteinase inhibitor
Title: Solution conformation of proteinase inhibitor iia from bull seminal plasma by 1h nuclear magnetic resonance and distance geometry
Structure: Proteinase inhibitor iia. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913
NMR struc: 5 models
Authors: P.Guntert,M.P.Williamson,T.F.Havel,K.Wuthrich
Key ref:
M.P.Williamson et al. (1985). Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. J Mol Biol, 182, 295-315. PubMed id: 3839023 DOI: 10.1016/0022-2836(85)90347-X
Date:
14-May-90     Release date:   15-Apr-91    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01001  (ISK6_BOVIN) -  Serine protease inhibitor Kazal-type 6 from Bos taurus
Seq:
Struc: 		80 a.a.
57 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.1016/0022-2836(85)90347-X J Mol Biol 182:295-315 (1985)
PubMed id: 3839023  
 
 
Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.
M.P.Williamson, T.F.Havel, K.Wüthrich.
 
  ABSTRACT  
 
A determination of the solution conformation of the proteinase inhibitor IIA from bull seminal plasma (BUSI IIA) is described. Two-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain a list of 202 distance constraints between individually assigned hydrogen atoms of the polypeptide chain, to identify the positions of the three disulfide bridges, and to locate the single cis peptide bond. Supplementary geometric constraints were derived from the vicinal spin-spin couplings and the locations of certain hydrogen bonds, as determined by nuclear magnetic resonance (n.m.r.). Using a new distance geometry program (DISGEO) which is capable of computing all-atom structures for proteins the size of BUSI IIA, five conformers were computed from the NOE distance constraints alone, and another five were computed with the supplementary constraints included. Comparison of the different structures computed from the n.m.r. data among themselves and with the crystal structures of two homologous proteins shows that the global features of the conformation of BUSI IIA (i.e. the overall dimensions of the molecule and the threading of the polypeptide chain) were well-defined by the available n.m.r. data. In the Appendix, we describe a preliminary energy refinement of the structure, which showed that the constraints derived from the n.m.r. data are compatible with a low energy spatial structure.
 
  Selected figure(s)  
 
Figure 2.
FIG. 2. 		Figure 7.
Figure 7. Schematic drawing of the polypeptide backbone ``topology'' which was obtained in all 10 of te BUS1 IIA structures computed from the n.m.r. data presented.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1985, 182, 295-315) copyright 1985.  
  Figures were selected by an automated process.  

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The sampling properties of some distance geometry algorithms applied to unconstrained polypeptide chains: a study of 1830 independently computed conformations.
  Biopolymers, 29, 1565-1585.  
1964810 T.O.Matsunaga, C.A.Gehrig, and V.J.Hruby (1990).
1H-NMR assignments and conformational studies of melanin concentrating hormone in water using two-dimensional NMR.
  Biopolymers, 30, 1291-1295.  
  2676353 G.M.Clore, and A.M.Gronenborn (1989).
Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy.
  Crit Rev Biochem Mol Biol, 24, 479-564.  
2585001 M.Sanner, A.Widmer, H.Senn, and W.Braun (1989).
GEOM: a new tool for molecular modelling based on distance geometry calculations with NMR data.
  J Comput Aided Mol Des, 3, 195-210.  
2831051 G.M.Clore, M.Nilges, A.Brünger, and A.M.Gronenborn (1988).
Determination of the backbone conformation of secretin by restrained molecular dynamics on the basis of interproton distance data.
  Eur J Biochem, 171, 479-484.  
3047742 J.de Vlieg, R.M.Scheek, W.F.van Gunsteren, H.J.Berendsen, R.Kaptein, and J.Thomason (1988).
Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: application to the DNA binding domain of lac repressor from Escherichia coli.
  Proteins, 3, 209-218.  
3186691 P.R.Gooley, S.A.Carter, P.E.Fagerness, and N.E.MacKenzie (1988).
Preferred conformational state of the N-terminus section of a bovine growth hormone fragment (residues 96-133) in water is an omega loop.
  Proteins, 4, 48-55.  
3345756 W.E.Steinmetz, P.E.Bougis, H.Rochat, O.D.Redwine, W.Braun, and K.Wüthrich (1988).
1H nuclear-magnetic-resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins.
  Eur J Biochem, 172, 101-116.  
3324162 B.R.Reid (1987).
Sequence-specific assignments and their use in NMR studies of DNA structure.
  Q Rev Biophys, 20, 1.  
2448843 D.J.Patel, L.Shapiro, and D.Hare (1987).
DNA and RNA: NMR studies of conformations and dynamics in solution.
  Q Rev Biophys, 20, 35.  
  3608994 G.M.Clore, A.M.Gronenborn, M.Nilges, D.K.Sukumaran, and J.Zarbock (1987).
The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
  EMBO J, 6, 1833-1842.  
  15981339 G.M.Clore, D.K.Sukumaran, M.Nilges, J.Zarbock, and A.M.Gronenborn (1987).
The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
  EMBO J, 6, 529-537.  
3496602 G.T.Montelione, K.Wüthrich, E.C.Nice, A.W.Burgess, and H.A.Scheraga (1987).
Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.
  Proc Natl Acad Sci U S A, 84, 5226-5230.  
3447178 P.J.Kraulis, and T.A.Jones (1987).
Determination of three-dimensional protein structures from nuclear magnetic resonance data using fragments of known structures.
  Proteins, 2, 188-201.  
3032625 S.G.Hyberts, W.Märki, and G.Wagner (1987).
Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c.
  Eur J Biochem, 164, 625-635.  
3310077 W.Braun (1987).
Distance geometry and related methods for protein structure determination from NMR data.
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3459158 A.T.Brünger, G.M.Clore, A.M.Gronenborn, and M.Karplus (1986).
Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin.
  Proc Natl Acad Sci U S A, 83, 3801-3805.  
  16453716 G.M.Clore, M.Nilges, D.K.Sukumaran, A.T.Brünger, M.Karplus, and A.M.Gronenborn (1986).
The three-dimensional structure of alpha1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
  EMBO J, 5, 2729-2735.  
2835760 H.Roder, and K.Wüthrich (1986).
Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons.
  Proteins, 1, 34-42.  
3006046 M.A.Weiss, A.G.Redfield, and R.H.Griffey (1986).
Isotope-detected 1H NMR studies of proteins: a general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage lambda repressor.
  Proc Natl Acad Sci U S A, 83, 1325-1329.  
2992961 D.Neuhaus, G.Wagner, M.Vasák, J.H.Kägi, and K.Wüthrich (1985).
Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Rabbit metallothionein-2.
  Eur J Biochem, 151, 257-273.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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