NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | in_recoord | stage | program | type |
19976 | 2ezh | 4090 | cing | recoord | 1-original | MR format | 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
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