NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
40589 | 1vrc | 4264 | cing | 2-parsed | STAR | comment |
data_1vrc_MR_file_constraints save_Conversion_project _Study_list.Sf_category study_list _Study_list.Entry_ID parsed_1vrc _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_1vrc 1 stop_ save_ save_entry_information _Entry.Sf_category entry_information _Entry.ID parsed_1vrc _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 1vrc "Master copy" parsed_1vrc stop_ save_ save_global_Org_file_characteristics _Constraint_stat_list.Sf_category constraint_statistics _Constraint_stat_list.Entry_ID parsed_1vrc _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 1vrc.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . n/a 2 comment "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . XPLOR/CNS 3 distance NOE simple 0 parsed_1vrc 1 1 1vrc.mr . . n/a 4 comment "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . XPLOR/CNS 5 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . n/a 6 comment "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . XPLOR/CNS 7 "dipolar coupling" "Not applicable" "Not applicable" 0 parsed_1vrc 1 1 1vrc.mr . . "MR format" 8 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_1vrc 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_1vrc _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 TRANSFERASE 21-FEB-05 1VRC *TITLE COMPLEX OF ENZYME IIAMANNOSE AND THE HISTIDINE-CONTAINING *TITLE 2 PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, *TITLE 3 RESTRAINED REGULARIZED MEAN STRUCTURE *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PTS SYSTEM, MANNOSE-SPECIFIC IIAB COMPONENT; *COMPND 3 CHAIN: A, B; *COMPND 4 FRAGMENT: EIIA DOMAIN; *COMPND 5 SYNONYM: EIIAB-MAN, MANNOSE-PERMEASE IIAB COMPONENT, *COMPND 6 PHOSPHOTRANSFERASE ENZYME II, AB COMPONENT, EIII-MAN; *COMPND 7 EC: 2.7.1.69; *COMPND 8 ENGINEERED: YES; *COMPND 9 MOL_ID: 2; *COMPND 10 MOLECULE: PHOSPHOCARRIER PROTEIN HPR; *COMPND 11 CHAIN: C, D; *COMPND 12 SYNONYM: HISTIDINE-CONTAINING PROTEIN; *COMPND 13 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; *SOURCE 3 ORGANISM_COMMON: BACTERIA; *SOURCE 4 GENE: MANX, GPTB, PTSL; *SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; *SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; *SOURCE 7 MOL_ID: 2; *SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; *SOURCE 9 ORGANISM_COMMON: BACTERIA; *SOURCE 10 GENE: PTSH, HPR; *SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; *SOURCE 12 EXPRESSION_SYSTEM_COMMON: BACTERIA *KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT, *KEYWDS 2 COMPLEX (TRANSFERASE/PHOSPHOCARRIER) *EXPDTA NMR, RESTRAINED REGULARIZED MEAN STRUCTURE *AUTHOR G.M.CLORE, D.C.WILLIAMS *REVDAT 1 19-APR-05 1VRC 0 ! CHAIN A: SUBUNIT A OF IIAMAN (RESIDUES 2-130 AND SEGID A) ! CHAIN B: SUBUNIT B OF IIAMAN (RESIDUES 2-130 AND SEGID B) ! CHAIN C: MOLECULE 1 OF HPR (RESIDUES 201-285 AND SEGID C) ! CHAIN D: MOLECULE 2 OF HPR (RESIDUES 201-285 AND SEGID D) ; save_
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