NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | in_dress | stage | program | type |
29728 | 1bbn | 4094 | cing | dress | 2-parsed | STAR | comment |
data_1bbn_MR_file_constraints save_Conversion_project _Study_list.Sf_category study_list _Study_list.Entry_ID parsed_1bbn _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_1bbn 1 stop_ save_ save_entry_information _Entry.Sf_category entry_information _Entry.ID parsed_1bbn _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 1bbn "Master copy" parsed_1bbn stop_ save_ save_global_Org_file_characteristics _Constraint_stat_list.Sf_category constraint_statistics _Constraint_stat_list.Entry_ID parsed_1bbn _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 1bbn.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_1bbn 1 1 1bbn.mr . . XPLOR/CNS 2 distance NOE simple 0 parsed_1bbn 1 1 1bbn.mr . . XPLOR/CNS 3 distance NOE simple 0 parsed_1bbn 1 1 1bbn.mr . . XPLOR/CNS 4 distance "hydrogen bond" simple 0 parsed_1bbn 1 1 1bbn.mr . . n/a 5 comment "Not applicable" "Not applicable" 0 parsed_1bbn 1 1 1bbn.mr . . XPLOR/CNS 6 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_1bbn 1 1 1bbn.mr . . "MR format" 7 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_1bbn 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_1bbn _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 1BBN *COMPND INTERLEUKIN 4 (NMR, MINIMIZED AVERAGE STRUCTURE) *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 1BBN 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 All the coordinates REMARK are included here as a separate file: il4_brookhaven.pdb 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 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. Appropriate corrections to the upper limits for distances involving methyl, methylene and Tyr and Phe aromatic ring protons, to account for centre averaging, are carried out as described by Wuthrich et al. [J. Mol. Biol. 169, 949-961 (1983)]. 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 centreaverages. 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. ; save_
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