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
36358 1ner 287 cing recoord 2-parsed STAR comment


data_1ner_MR_file_constraints


save_Conversion_project
    _Study_list.Sf_category  study_list 
    _Study_list.Entry_ID     parsed_1ner 
    _Study_list.ID           1 

    loop_
        _Study.ID 
        _Study.Name 
        _Study.Type 
        _Study.Details 
        _Study.Entry_ID 
        _Study.Study_list_ID 

        1   "Conversion project"    NMR   .   parsed_1ner   1   
    stop_

save_


save_entry_information
    _Entry.Sf_category                  entry_information 
    _Entry.ID                           parsed_1ner 
    _Entry.Title                       "Original constraint list(s)" 
    _Entry.Version_type                 original 
    _Entry.Submission_date              . 
    _Entry.Accession_date               . 
    _Entry.Last_release_date            . 
    _Entry.Original_release_date        . 
    _Entry.Origination                  . 
    _Entry.NMR_STAR_version             3.1 
    _Entry.Original_NMR_STAR_version    . 
    _Entry.Experimental_method          NMR 
    _Entry.Experimental_method_subtype  . 

    loop_
        _Related_entries.Database_name 
        _Related_entries.Database_accession_code 
        _Related_entries.Relationship 
        _Related_entries.Entry_ID 

        PDB   1ner   "Master copy"    parsed_1ner   
    stop_

save_


save_global_Org_file_characteristics
    _Constraint_stat_list.Sf_category  constraint_statistics 
    _Constraint_stat_list.Entry_ID     parsed_1ner 
    _Constraint_stat_list.ID           1 

    loop_
        _Constraint_file.ID 
        _Constraint_file.Constraint_filename 
        _Constraint_file.Software_ID 
        _Constraint_file.Software_label 
        _Constraint_file.Software_name 
        _Constraint_file.Block_ID 
        _Constraint_file.Constraint_type 
        _Constraint_file.Constraint_subtype 
        _Constraint_file.Constraint_subsubtype 
        _Constraint_file.Constraint_number 
        _Constraint_file.Entry_ID 
        _Constraint_file.Constraint_stat_list_ID 

        1   1ner.mr   .   .   "MR format"     1    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS      2    distance                  NOE                 simple             0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS      3    distance                 "hydrogen bond"      simple             0   parsed_1ner   1   
        1   1ner.mr   .   .    n/a            4    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS      5   "dihedral angle"          "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    n/a            6    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS      7   "coupling constant"       "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    n/a            8    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS      9   "chemical shift"          "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    n/a           10    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    XPLOR/CNS     11   "chemical shift"          "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    n/a           12    comment                  "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .    PIPP          13   "chemical shift"          "Not applicable"    "Not applicable"    0   parsed_1ner   1   
        1   1ner.mr   .   .   "MR format"    14   "nomenclature mapping"    "Not applicable"    "Not applicable"    0   parsed_1ner   1   
    stop_

save_


save_MR_file_comment_1
    _Org_constr_file_comment.Sf_category         org_constr_file_comment 
    _Org_constr_file_comment.Entry_ID            parsed_1ner 
    _Org_constr_file_comment.ID                  1 
    _Org_constr_file_comment.Constraint_file_ID  1 
    _Org_constr_file_comment.Block_ID            1 
    _Org_constr_file_comment.Details            "Generated by Wattos" 
    _Org_constr_file_comment.Comment            
;
*HEADER   DNA-BINDING PROTEIN                     24-AUG-95   1NER    
*TITLE    SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL
*TITLE   2 NMR                                                        
*COMPND   MOL_ID: 1;                                                  
*COMPND  2 MOLECULE: DNA-BINDING PROTEIN NER;                         
*COMPND  3 CHAIN: NULL                                                
*SOURCE   MOL_ID: 1;                                                  
*SOURCE  2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE MU                      
*EXPDTA   NMR, 30 STRUCTURES                                          
*AUTHOR   G.M.CLORE,T.E.STRZELECKA,A.M.GRONENBORN                     
*REVDAT  1   07-DEC-95 1NER    0                                      



REMARK  Experimental restraints used for the solution structure determination
REMARK  of the Mu Ner Protein by multidimensional NMR
REMARK
REMARK   Authors: G.M. Clore, T.E. Strzelecka and A.M. Gronenborn
REMARK            Laboratory of Chemical Physics, Bldg 5, Rm 132
REMARK            NIDDK, National Institutes of Health
REMARK            Bethesda, MD 20892
REMARK  Tel: (301) 496 0782; FAX (301) 496 0825; 
REMARK  e-mail: clore@vger.niddk.nih.gov
REMARK  
REMARK   References:
REMARK   Strzelecka, T.E., Clore, G.M. & Gronenborn, A.M. (1995)
REMARK   The solution structure of the Mu Ner Protein reveals a helix-turn-
REMARK   helix DNA recognition motif. Structure in press.
REMARK
REMARK   Related references:
REMARK   Gronenborn, A.M., Wingfield, P.T. & Clore, G.M. (1989)
REMARK   Determination of the secondary structure of the DNA binding protein
REMARK   Ner from phage Mu using 1H homonuclear and 15N-1H heteronuclear
REMARK   NMR spectroscopy. Biochemistry 28, 5081-5089.
REMARK
REMARK   The 3D structure of the Mu Ner protein by
REMARK   multi-dimensional heteronuclear NMR
REMARK   is based on 1546 experimental restraints comprising the following:
REMARK   944 interproton distance restraints [251 sequential; 202 short
REMARK   range (1<|i-j|<=5; 157 long range (|i-j|>5); and 334 intraresidue];
REMARK   40 distance restraints for 20 backbone hydrogen bonds;
REMARK   89 torsion angle restraints 56 phi, 27 ch1 and 6 chi2);
REMARK   46 3 bond HN-Ha coupling constants; 140 secondary 13C shifts
REMARK   (72 Ca and 68 Cb); 287 1H chemical shifts (74 Ha, 39 methyl
REMARK   and 174 other, with no exchangeable proton shifts).
REMARK
REMARK
REMARK   The structure was determined by simulated annealing [Nilges,
REMARK   Clore & Gronenborn (1988) FEBS Lett. 229, 317-324] using the
REMARK   program XPLOR (Brunger) modified to incorporate coupling constant
REMARK   [Garrett et al. & Clore (1994) J. Magn. Reson. B104, 99-103],
REMARK   carbon chemical shift [Kuszewski, Qin, Gronenborn & Clore (1995)
REMARK   J. Magn. Reson. B106, 92-96] and proton chemical shift
REMARK   [Kuszewski, Gronenborn & Clore (1995) J. Magn. Reson. B107, 293-297]
REMARK   restraints.

REMARK    The structures have been provided in a separate files:
REMARK    ner_brookhaven.pdb
REMARK
REMARK    The NOE restraints are given in (A), the torsion angle restraints
REMARK    in (B), the coupling constant restraints in (C), the
REMARK    carbon chemical shift restraints in (D), the 1H chemical shift
REMARK    restraints in (E).
REMARK    The complete set of 1H, 15N and 13C assignments is given in F.
REMARK
REMARK

A. NOE interproton distance restraints

The restraints are represented by square-well potentials with the upper (u)
and lower (l) limits given  by u=i+k and l=i-j where the numbers are
entered in the order i,j,k. [Clore et al. (1986) EMBO J. 5, 2729-2735]

The NOEs are classified into three distance ranges corresponding to
strong, medium and weak NOEs.  These are 1.8-2.7 A, 1.8-3.3 A and 1.8-5.0 A,
respectively.  
In addition, an extra 0.5 A is added
to the upper limits of distances involving methyl protons [Clore et al.
(1983) Biochemistry 26, 8012-8023; Wagner et al. (1987) 
J. Mol. Biol. 196, 611-640].

The atom notation follows standard PDB format.  The # indicates a single
wild card, and the * a full wild card. e.g. For Leu, HD* representes all the
methyl protons; for a normal methylene beta proton, HB# represents the 
two protons.  In these cases, the distances are calculated as 
sigma-1/6 sums

Note that the hard sphere van der Waals repulsion term ensures that
the minimum lower limit for all distances is the sum of the relevant
hard sphere atom radii.

B. Torsion angle restraints

The torsion angle restraints are derived from coupling constant and NOE data
using the conformational grid search program STEREOSEARCH [Nilges, M.,
Clore, G.M. & Gronenborn, A.M. (1990) Biopolymers 29, 813-822].
They are represented by a square well potential
[Clore et al. (1986) EMBO J. 5, 2729-2735].  The upper and lower limits are 
given by i+j and i-j respectively, where the numbers are entered in the order
x,i,j,m.  x is the force constant and m the exponent used to compute the
torsion angle restraints target function.

C. Three-bond HN-HA coupling constant restraints.
The value of the coupling constant is given by the first number, and the
second number has no meaning.

D. Ca and Cb carbon chemical shift restraints: the Ca shift is given 
by the first number and the Cb one by the second.

E. 1H chemical shift restraints

F. Complete list of 1H, 15N and 13C assignments


A. interproton distance restraints

;

save_





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