NMR Restraints Grid

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

image	mrblock_id	pdb_id	cing	stage	program	type
	2916	1ctl	cing	1-original	MR format	comment

*HEADER   METAL-BINDING PROTEIN                   06-JAN-95   1CTL    
*COMPND   MOLECULE: AVIAN CYSTEINE RICH PROTEIN;                      
*COMPND  2 DOMAIN: C-TERMINAL LIM DOMAIN;                             
*COMPND  3 SYNONYMS: LIM2, ZN-LIM2, CCRP-LIM2, CRP-LIM2,              
*COMPND  4 ZN(II)-CRP-LIM2;                                           
*COMPND  5 EXPERIMENT: NMR, 18 STRUCTURES                             
*SOURCE   MOLECULE: AVIAN CYSTEINE RICH PROTEIN;                      
*SOURCE  2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                        
*SOURCE  3 ORGANISM_COMMON: CHICKEN; TISSUE: SMOOTH MUSCLE;           
*SOURCE  4 ORGAN: GIZZARD;                                            
*SOURCE  5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                       
*SOURCE  6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                       
*SOURCE  7 EXPRESSION_SYSTEM_PLASMID: PAED4-LIM2                      
*KEYWDS   LIM DOMAIN CONTAINING PROTEINS                              
*EXPDTA   NMR, 18 STRUCTURES                                          
*AUTHOR   G.C.PEREZ-ALVARADO,C.MILES,J.W.MICHELSEN,H.A.LOUIS,         
*AUTHOR  2 D.R.WINGE,M.C.BECKERLE,M.F.SUMMERS                         
*REVDAT  1   03-JUN-95 1CTL    0                                      

References:
G.C. Perez-Alvarado, C. Miles, J.W. Michelsen, H. A. Louis,
D. R. Winge, M.C. Beckerle and M.F. Summers (1994) Structure
of the carboxy-terminal LIM domain from the Cysteine Rich Protein CRP
Nature Struct. Biol., 1, p388-398.

The solution NMR 3D structure of the C-terminal LIM domain
from CRP (LIM2) is based on 239 distance restraints derived 
from the NOE data and 17 metal restraints. A complete list
of experimental restraints follows:

List of residues with corresponding numbering in the sequence
of the MODELS:

Met-1  Ala-2  Gln-3  Lys-4  Val-5  Gly-6  Gly-7  Ser-8  Asp-9  Gly-10  
Cys-11 Pro-12 Arg-13 Cys-14 Gly-15 Gln-16 Ala-17 Val-18 Tyr-19 Ala-20 
Ala-21 Glu-22 Lys-23 Val-24 Ile-25 Gly-26 Ala-27 Gly-28 Lys-29 Ser-30 
Trp-31 His-32 Lys-33 Ser-34 Cys-35 Phe-36 Arg-37 Cys-38 Ala-39 Lys-40 
Cys-41 Gly-42 Lys-43 Ser-44 Leu-45 Glu-46 Ser-47 Thr-48 Thr-49 Leu-50 
Ala-51 Asp-52 Lys-53 Asp-54 Gly-55 Glu-56 Ile-57 Tyr-58 Cys-59 Lys-60 
Gly-61 Cys-62 Tyr-63 Ala-64 Lys-65 Asn-66 Phe-67 Gly-68 Pro-69 Lys-70 
Gly-71 Phe-72 Gly-73 Phe-74 Gly-75 Gln-76 Gly-77 Ala-78 Gly-79 Ala-80 
Leu-81 Ile-82 His-83 Ser-84 Gln-85

*NOTE: Met-1 is removed post-translationally, but eventhough it is in
the MODELS, it was not employed for structure calculations.
The correct sequencing is found in the referenced paper, using the
numbering corresponding to the residues within the sequence of CRP.


NOE Interproton distance restraints. Distances are in Angstroms (A)

Strong 1.8 - 2.7 A
Medium 1.8 - 3.3 A
Weak   1.8 - 5.0 A


Metal restraints used to enforce Zn-S and Zn-N bond distances,
and to ensure proper hybridization of the His-Nd and Cys-Sg atoms
(distances in A)

LB= Lower Bound
UB= Upper Bound

 ATOM 1  ATOM 2  distance

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