Result table
| image | mrblock_id | pdb_id | bmrb_id | cing | in_recoord | stage | program | type |
|
|
46527 | 2ezh RC | 4090 | cing | recoord | 2-parsed | STAR | comment |
data_2ezh_MR_file_constraints
save_Conversion_project
_Study_list.Sf_category study_list
_Study_list.Entry_ID parsed_2ezh
_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_2ezh 1
stop_
save_
save_entry_information
_Entry.Sf_category entry_information
_Entry.ID parsed_2ezh
_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 2ezh "Master copy" parsed_2ezh
stop_
save_
save_global_Org_file_characteristics
_Constraint_stat_list.Sf_category constraint_statistics
_Constraint_stat_list.Entry_ID parsed_2ezh
_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 2ezh.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . n/a 2 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . XPLOR/CNS 3 distance NOE simple 0 parsed_2ezh 1
1 2ezh.mr . . XPLOR/CNS 4 distance "hydrogen bond" simple 0 parsed_2ezh 1
1 2ezh.mr . . n/a 5 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . XPLOR/CNS 6 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . n/a 7 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . XPLOR/CNS 8 "coupling constant" "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . n/a 9 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . XPLOR/CNS 10 "chemical shift" "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . n/a 11 comment "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . PIPP 12 "chemical shift" "Not applicable" "Not applicable" 0 parsed_2ezh 1
1 2ezh.mr . . "MR format" 13 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_2ezh 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_2ezh
_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 25-JUL-97 2EZH
*TITLE SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU
*TITLE 2 END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED
*TITLE 3 AVERAGE STRUCTURE
*COMPND MOL_ID: 1;
*COMPND 2 MOLECULE: TRANSPOSASE;
*COMPND 3 CHAIN: NULL;
*COMPND 4 FRAGMENT: IGAMMA SUBDOMAIN, RESIDUES 174 - 247;
*COMPND 5 OTHER_DETAILS: MUA OF PHAGE MU TRANSPOSASE
*SOURCE MOL_ID: 1;
*SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE MU
*KEYWDS DNA-BINDING PROTEIN, TRANSPOSITION
*EXPDTA NMR, MINIMIZED AVERAGE STRUCTURE
*AUTHOR G.M.CLORE,R.T.CLUBB,S.SCHUMAKER,A.M.GRONENBORN
*REVDAT 1 03-DEC-97 2EZH 0
SUGGESTED ID CODE 2EZHMR
RELATED ENTRIES 2EZH AND 2EZI
EXPERIMENTAL RESTRAINTS FOR
SUGGESTED ID CODE 2EZH
HEADER DNA-BINDING PROTEIN
TITLE SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE
TITLE 2 MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE.
TITLE 2 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGAMMA SUBDOMAIN OF MUA OF PHAGE MU TRANSPOSASE
COMPND 3 (RESIDUES 174-247);
COMPND 4 CHAIN: A;
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE MU;
SOURCE 3 ORGANISM_COMMON: PHAGE MU;
KEYWDS DNA-BINDING , TRANSPOSITION
EXPDTA NMR, 1 REGULARIZED MEAN STRUCTURE
AUTHOR G.M.CLORE, R.T. CLUBB, S. SCHUMAKER, A.M. GRONENBORN
JRNL AUTH R.T. CLUBB, S. SCHUMAKER, K. MIZUUCHI, A.M. GRONENBORN,
JRNL AUTH 2 G.M. CLORE
JRNL TITL SOLUTION STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END
JRNL TITL 2 DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE
JRNL REF JOURNAL OF MOLECULAR BIOLOGY (1997) IN PRESS
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4.
REMARK 3
REMARK 3 REFINEMENT. NONE.
REMARK 4
REMARK 4 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 4 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 4 *CRYST1* AND *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 4 THESE RECORDS ARE MEANINGLESS.
REMARK 5
REMARK 5 THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A TRANSPOSASE WAS
REMARK 5 SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND
REMARK 5 IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS:
REMARK 5 264 SEQUENTIAL (|I- J|=1), 282 MEDIUM RANGE (1 <
REMARK 5 |I-J| <=5) AND 178 LONG RANGE (|I-J| >5) INTERRESIDUES AND
REMARK 5 245 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE
REMARK 5 RESTRAINTS; 40 DISTANCE RESTRAINTS FOR 20 BACKBONE H-BONDS;
REMARK 5 108 TORSION ANGLE RESTRAINTS; 47 THREE-BOND HN-HA COUPLING CONSTANT
REMARK 5 RESTRAINTS; AND 129 (66 CALPHA AND 63 CBETA) 13C SHIFT
REMARK 5 RESTRAINTS.
REMARK 6
REMARK 6 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 6 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
REMARK 6 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED
REMARK 6 TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J.
REMARK 6 MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL
REMARK 6 SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B
REMARK 6 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE
REMARK 6 POTENTIAL (KUSZEWSKI ET AL.(1996) PROTEIN SCI. 5, 1067-1080;
REMARK 6 KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125, 171-177).
REMARK 7
REMARK 7 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
REMARK 7 ENTRY 2EZH AND 30 STRUCTURES ARE PRESENTED IN ENTRY 2EZI,
REMARK 7 AND THE EXPERIMENTAL RESTRAINTS IN 2EZHMR.
REMARK 7 IN THE RESTRAINED REGULARIZED MEAN COORDINATES (2EZH) THE LAST
REMARK 7 COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 7 INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
REMARK 7 COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
REMARK 7 STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE THE
REMARK 7 AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 180-240
REMARK 7 NOTE THE OCCUPANCY FIELD HAS NO MEANING.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 30 C
REMARK 210 PH :6.3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : Triple resonance for assignment of
REMARK protein: CBCA(CO)NH, CBCANH, HBHA(CO)NH, C(CO)NH,
REMARK H(CCO)NH, HCCH-COSY, HCCH-TOCSY, HNHA,
REMARK 15N-SEPARATED HOHAHA;
REMARK quantitative J correlation for coupling constants;
REMARK 3D 15N-SEPARATED NOE, 3D 13C-SEPARATED NOE AND ROE,
REMARK 4D 15N/13C-SEPARATED NOE, 4D 13C/13C-SEPARATED NOE
REMARK experiments
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 and 600 MHz
REMARK 210 SPECTROMETER MODEL : AMX500 and AMX600
REMARK 210 SPECTROMETER MANUFACTURER : Bruker
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR (see above)
REMARK 210 METHOD USED : Simulated annealing
REMARK 210
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210
REMARK 210 REMARK: RESIDUE 173 IS AN N_TERMINAL MET DUE TO CLONING.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 900
REMARK 900 RELATED ENTRIES (2EZI AND 2EZIMR)
REMARK 900 THIS ENTRY (2EZH) IS THE MINIMIZED STRUCUTURE OF THE MODEL
REMARK 900
REMARK 999
REMARK 999 SEQUENCE
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
;
save_