NMR Restraints Grid
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NMR Restraints Grid |
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Result table
| image | mrblock_id | pdb_id | cing | stage | program | type |
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43723 |
2bbm   |
cing | 2-parsed | STAR | comment |
data_2bbm_MR_file_constraints
save_Conversion_project
_Study_list.Sf_category study_list
_Study_list.Entry_ID parsed_2bbm
_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_2bbm 1
stop_
save_
save_entry_information
_Entry.Sf_category entry_information
_Entry.ID parsed_2bbm
_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 2bbm "Master copy" parsed_2bbm
stop_
save_
save_global_Org_file_characteristics
_Constraint_stat_list.Sf_category constraint_statistics
_Constraint_stat_list.Entry_ID parsed_2bbm
_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 2bbm.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_2bbm 1
1 2bbm.mr . . n/a 2 comment "Not applicable" "Not applicable" 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 3 distance NOE simple 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 4 distance "hydrogen bond" simple 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 5 distance NOE simple 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 6 distance "hydrogen bond" simple 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 7 distance NOE simple 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 8 distance "hydrogen bond" simple 0 parsed_2bbm 1
1 2bbm.mr . . n/a 9 comment "Not applicable" "Not applicable" 0 parsed_2bbm 1
1 2bbm.mr . . XPLOR/CNS 10 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_2bbm 1
1 2bbm.mr . . "MR format" 11 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_2bbm 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_2bbm
_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 CALCIUM-BINDING PROTEIN 16-JUL-92 2BBM
*COMPND CALMODULIN (CALCIUM-BOUND) COMPLEXED WITH RABBIT SKELETAL
*COMPND 2 MYOSIN LIGHT CHAIN KINASE (CALMODULIN-BINDING DOMAIN)
*COMPND 3 (NMR, MINIMIZED AVERAGE STRUCTURE)
*SOURCE CALMODULIN: (DROSOPHILA MELANOGASTER); PEPTIDE: SYNTHETIC
*AUTHOR G.M.CLORE,A.BAX,M.IKURA,A.M.GRONENBORN
*REVDAT 1 31-JAN-94 2BBM 0
REMARK Ident code 1BBM Revised restraints list
REMARK Experimental NMR restraints used to determine the
REMARK three-dimensional structure of the complex of drosophila
REMARK calmodulin with a 26 residue peptide comprising the calmodulin
REMARK binding domain of skeltal muscle myosin light chain kinase.
REMARKS
REMARKS
REMARK Authors: M. Ikura, G.M. Clore, A. Bax and A.M. Gronenborn
REMARK
REMARK References
REMARK
REMARK 1. M. Ikura, G.M. Clore*, A.M. Gronenborn*, G. Zhu, C.B. Klee & A. Bax*
REMARK (1992) Solution structure of a ccalmodulin-target peptide complex by
REMARK multidimensional NMR. Science in press
REMARK
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 1827 interproton distance restraints
REMARK derived from NOE measurements; 148 hydrogen-bonding distance
REMARK restraints for 74 hydrogen-bonds identified on the basis of the
REMARK NOE and amide proton exchange data, as well as the initial structure
REMARK calculations; 24 restraints for the 4 calcium ions, and 113 phi
REMARK torsion angle restraints derived from oupling constants, NOE data,
REMARK and 13C 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 All the coordinates
REMARK are included here as a separate file: cam_brookhaven.pdb
REMARK
REMARK The NOE restraints are given in (A) and the torsion angle restraints
REMARK in (B).
REMARK
REMARK
;
save_
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