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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29775 |
1bcn   |
4094 | cing | recoord | 2-parsed | STAR | comment |
data_1bcn_MR_file_constraints
save_Conversion_project
_Study_list.Sf_category study_list
_Study_list.Entry_ID parsed_1bcn
_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_1bcn 1
stop_
save_
save_entry_information
_Entry.Sf_category entry_information
_Entry.ID parsed_1bcn
_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 1bcn "Master copy" parsed_1bcn
stop_
save_
save_global_Org_file_characteristics
_Constraint_stat_list.Sf_category constraint_statistics
_Constraint_stat_list.Entry_ID parsed_1bcn
_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 1bcn.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_1bcn 1
1 1bcn.mr . . n/a 2 comment "Not applicable" "Not applicable" 0 parsed_1bcn 1
1 1bcn.mr . . XPLOR/CNS 3 distance NOE simple 0 parsed_1bcn 1
1 1bcn.mr . . XPLOR/CNS 4 distance "hydrogen bond" simple 0 parsed_1bcn 1
1 1bcn.mr . . n/a 5 comment "Not applicable" "Not applicable" 0 parsed_1bcn 1
1 1bcn.mr . . XPLOR/CNS 6 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_1bcn 1
1 1bcn.mr . . "MR format" 7 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_1bcn 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_1bcn
_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 CYTOKINE 01-MAY-92 1BCN
*COMPND INTERLEUKIN 4 (NMR, 22 STRUCTURES)
*SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN YEAST
*SOURCE 2 (SACCHAROMYCES CEREVISIAE)
*AUTHOR G.M.CLORE,B.POWERS,D.S.GARRETT,A.M.GRONENBORN
*REVDAT 1 31-OCT-93 1BCN 0
REMARK Experimental NMR restraints used for the three-dimensional structure
REMARK determination of recombinant human interleukin-4
REMARK
REMARK
REMARK Authors: G.M. Clore, B. Powers, D.S. Garrett and A.M. Gronenborn
REMARK
REMARK References
REMARK
REMARK 1. R. Powers, D.S. Garrett, C.J. March, E.A. Frieden, A.M. Gronenborn
REMARK and G.M. Clore (1992) Three dimensional solution structure of
REMARK human interleukin-4 by multidimensional heteronuclear magnetic
REMARK resonance spectroscopy. Science in press
REMARK
REMARK 2. R. Powers, D.S. Garrett, C.J. March, E.A. Frieden, A.M. Gronenborn
REMARK and G.M. Clore (1992) 1H, 15N, 13C and 13CO assignments of human
REMARK interleukin-4 using three-dimensional double- and triple-resonance
REMARK hetronuclear magnetic resonance spectroscopy. Biochemistry 31, issue
REMARK 18, in press
REMARK
REMARK 3. D.S. Garrett, R. Powers, C.J. March, E.A. Frieden, G.M. Clore
REMARK and A.M. Gronenborn (1992) Determination of the secondary structure
REMARK and folding topology of human interleukin-4 using three-dimensional
REMARK heteronuclear magnetic resonance spectroscopy. Biochemistry 31,
REMARK issue 18, in press
REMARK
REMARK The numbering scheme in this structure includes the four-residue
REMARK sequence Glu-Ala-Glu-Ala at the N-terminus of the recombinant
REMARK protein which is not part of the natural human IL-4; the natural
REMARK IL-4 sequence therefore starts at residue 5.
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 823 interproton distance restraints
REMARK derived from NOE measurements; 98 hydrogen-bonding distance
REMARK restraints for 49 hydrogen-bonds identified on the basis of the
REMARK NOE and amide proton exchange data, as well as the initial structure
REMARK calculations; and 101 phi and 82 psi backbone torsion angle
REMARK restraints derived from oupling constants, NOE data, and 13C
REMARK 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
REMARK The NOE restraints are given in (A) and the torsion angle restraints
REMARK in (B).
REMARK
REMARK
;
save_
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