NMR Restraints Grid

Result table
 (Save to zip file containing files for each block)

image	mrblock_id	pdb_id	bmrb_id	cing	in_recoord	stage	program	type
	2068	1bcn	4094	cing	recoord	1-original	MR format	comment

*HEADER   CYTOKINE                                01-MAY-92   1BCN    
*COMPND   INTERLEUKIN 4 (NMR, 22 STRUCTURES)                          
*SOURCE   HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN YEAST    
*SOURCE  2 (SACCHAROMYCES CEREVISIAE)                                 
*AUTHOR   G.M.CLORE,B.POWERS,D.S.GARRETT,A.M.GRONENBORN               
*REVDAT  1   31-OCT-93 1BCN    0                                      

REMARK Experimental NMR restraints used for the three-dimensional structure 
REMARK determination of recombinant human interleukin-4
REMARK 
REMARK
REMARK Authors: G.M. Clore, B. Powers, D.S. Garrett and A.M. Gronenborn
REMARK
REMARK References
REMARK
REMARK 1.  R. Powers, D.S. Garrett, C.J. March, E.A. Frieden, A.M. Gronenborn
REMARK     and G.M. Clore (1992) Three dimensional solution structure of 
REMARK     human interleukin-4 by multidimensional heteronuclear magnetic 
REMARK     resonance spectroscopy. Science in press
REMARK
REMARK 2.  R. Powers, D.S. Garrett, C.J. March, E.A. Frieden, A.M. Gronenborn
REMARK     and G.M. Clore (1992) 1H, 15N, 13C and 13CO assignments of human
REMARK     interleukin-4 using three-dimensional double- and triple-resonance
REMARK     hetronuclear magnetic resonance spectroscopy. Biochemistry 31, issue
REMARK     18, in press
REMARK
REMARK 3.  D.S. Garrett, R. Powers, C.J. March, E.A. Frieden, G.M. Clore
REMARK     and A.M. Gronenborn (1992) Determination of the secondary structure
REMARK     and folding topology of human interleukin-4 using three-dimensional
REMARK     heteronuclear magnetic resonance spectroscopy. Biochemistry 31,
REMARK     issue 18, in press
REMARK
REMARK     The numbering scheme in this structure includes the four-residue
REMARK     sequence Glu-Ala-Glu-Ala at the N-terminus of the recombinant
REMARK     protein which is not part of the natural human IL-4; the natural
REMARK     IL-4 sequence therefore starts at residue 5.
REMARK
REMARK    Details of the structure determination and all structural
REMARK    statistics are given in ref. 1 (i.e. agreement with experimental
REMARK    restraints, deviations from ideality for bond lengths, angles,
REMARK    planes and chirality, non-bonded contacts, atomic rms differences
REMARK    between the calculated structures).
REMARK    The structures are based on 823 interproton distance restraints
REMARK    derived from NOE measurements; 98 hydrogen-bonding distance
REMARK    restraints for 49 hydrogen-bonds identified on the basis of the
REMARK    NOE and amide proton exchange data, as well as the initial structure
REMARK    calculations; and 101 phi and 82 psi backbone torsion angle 
REMARK    restraints derived from oupling constants, NOE data, and 13C
REMARK    secondary chemical shifts. 
REMARK
REMARK    The method used to determine the structures
REMARK    is the hybrid metric matrix distance geometry-dynamical simulated
REMARK    annealing method  [Nilges, M., Clore, G.M. & Gronenborn, A.M.
REMARK    FEBS Lett. 229, 317-324 (1988)].
REMARK
REMARK
REMARK
REMARK    The NOE restraints are given in (A) and the torsion angle restraints
REMARK    in (B).
REMARK
REMARK

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