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
	28649	3trx	2958	cing	recoord	1-original	MR format	comment

*HEADER   R3TRXMR   17-DEC-90
*COMPND   THIOREDOXIN (E.C.1.6.4.5) (REDUCED FORM)                              
*SOURCE   HUMAN (HOMO $SAPIENS) RECOMBINANT IN (ESCHERICHIA $COLI)
*EXPDTA   NMR               
*AUTHOR   J.D.FORMAN-*KAY,G.M.CLORE,A.M.GRONENBORN                              
*COORDS   3TRX
*REMARK                                                                         
*REMARK    HYDROGEN ATOMS IN THIS ENTRY HAVE BEEN ASSIGNED NAMES                
*REMARK    CONSISTENT WITH THE RECOMMENDATIONS OF THE IUPAC-IUB                 
*REMARK    COMMISSION ON BIOCHEMICAL NOMENCLATURE (SEE,E.G., J.MOL.             
*REMARK    BIOL. 52, 1 (1970)).  THE PROTEIN DATA BANK HAS FOLLOWED             
*REMARK    RULE 4.4 OF THE RECOMMENDATIONS WITH THE FOLLOWING                   
*REMARK    MODIFICATION - WHEN MORE THAN ONE HYDROGEN ATOM IS BONDED            
*REMARK    TO A SINGLE NON-HYDROGEN ATOM, THE HYDROGEN ATOM NUMBER              
*REMARK    DESIGNATION IS GIVEN AS THE FIRST CHARACTER OF THE ATOM              
*REMARK    NAME RATHER THAN AS THE LAST CHARACTER (E.G. H*BETA*1 IS             
*REMARK    DENOTED AS 1HB).  
*REMARK
REMARK Experimental restraints used in the computation of the
REMARK high resolution three-dimensional structure of
REMARK reduced recombinant human thioredoxin in solution.
REMARK 
REMARK Authors: J.D. Forman-Kay, G.M. Clore and A.M. Gronenborn
REMARK
REMARK References
REMARK 1. The high resolution three-dimensional structure of
REMARK    reduced recombinant human thioeredoxin in solution
REMARK    Forman-Kay, J.D., Clore, G.M.*, Wingfield, P.T. & Gronenborn, A.M.*
REMARK    Biochemistry (1990) in press
REMARK
REMARK 2. Studies on the solution conformation of human thioredoxin using 
REMARK    15N-1H nuclear magnetic resonance spectroscopy. 
REMARK    Forman-Kay, J.D., Gronenborn, A.M.*, Wingfield, P.T. & Clore,, G.M.*
REMARK    Biochemistry 29, 1566-1572.
REMARK
REMARK 3. A proton nuclear magnetic resonance assignment and secondary
REMARK    structure determination of recombinant human thioredoxin.
REMARK    Forman-Kay, J.D., Clore, G.M.*, Driscoll, P.C., Wingfield, P.T.,
REMARK    Richards, F.M. & Gronenborn, A.M.*
REMARK    Biochemistry 28, 7088-7097
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 1983 interproton distance restraints
REMARK    derived from NOE measurements; 52 hydrogen-bonding distance
REMARK    restraints for 26 hydrogen-bonds identified on the basis of the
REMARK    NOE and amide proton exchange data, as well as the initial structure
REMARK    calculations; and 98 phi and 71 psi backbone torsion angle restraints
REMARK    and 72 chi1 sidechain torsion angle restraints derived from
REMARK    coupling constants and NOE data. The latter are obtained using
REMARK    the conformationa grid search program STEREOSEARCH [Nilges, M.,
REMARK    Clore, G.M. & Gronenborn, A.M. (1990) Biopolymers 29, 813-822
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    All the coordinates
REMARK    are included here as a separate file: Hum_trx.pdb
REMARK
REMARK
REMARK
REMARK

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