NMR Restraints Grid
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NMR Restraints Grid |
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Result table
| image | mrblock_id | pdb_id | bmrb_id | cing | in_recoord | stage | program | type |
|
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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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