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 | in_dress | stage | program | type |
|
|
31726 |
1eza   |
4106 | cing | recoord | dress | 2-parsed | STAR | comment |
data_1eza_MR_file_constraints
save_Conversion_project
_Study_list.Sf_category study_list
_Study_list.Entry_ID parsed_1eza
_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_1eza 1
stop_
save_
save_entry_information
_Entry.Sf_category entry_information
_Entry.ID parsed_1eza
_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 1eza "Master copy" parsed_1eza
stop_
save_
save_global_Org_file_characteristics
_Constraint_stat_list.Sf_category constraint_statistics
_Constraint_stat_list.Entry_ID parsed_1eza
_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 1eza.mr . . "MR format" 1 comment "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . XPLOR/CNS 2 distance NOE ambi 0 parsed_1eza 1
1 1eza.mr . . XPLOR/CNS 3 distance "hydrogen bond" simple 0 parsed_1eza 1
1 1eza.mr . . n/a 4 comment "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . XPLOR/CNS 5 "coupling constant" "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . n/a 6 comment "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . XPLOR/CNS 7 "chemical shift" "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . n/a 8 comment "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . XPLOR/CNS 9 "dihedral angle" "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . n/a 10 comment "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . PIPP 11 "chemical shift" "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . unknown 12 "chemical shift" "Not applicable" "Not applicable" 0 parsed_1eza 1
1 1eza.mr . . "MR format" 13 "nomenclature mapping" "Not applicable" "Not applicable" 0 parsed_1eza 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_1eza
_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 PHOSPHOTRANSFERASE 01-JAN-97 1EZA
*TITLE AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI
*TITLE 2 NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
*COMPND MOL_ID: 1;
*COMPND 2 MOLECULE: ENZYME I;
*COMPND 3 CHAIN: NULL;
*COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259;
*COMPND 5 EC: 2.7.3.9;
*COMPND 6 ENGINEERED: YES;
*COMPND 7 BIOLOGICAL_UNIT: HOMODIMER
*SOURCE MOL_ID: 1;
*SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
*SOURCE 3 STRAIN: GI698;
*SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
*SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PLP2
*KEYWDS PHOSPHOTRANSFERASE
*EXPDTA NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
*AUTHOR D.S.GARRETT,A.M.GRONENBORN,G.M.CLORE
*REVDAT 1 07-JAN-98 1EZA 0
EXPERIMENTAL RESTRAINTS
HEADER PHOSPHOTRANSFERASE
TITLE AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENZYME I;
COMPND 3 CHAIN: A
COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN RESIDUES 1 - 259;
COMPND 5 EC: 2.7.3.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 STRAIN: GI698;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PLP2
KEYWDS PHOSPHOTRANSFERASE
EXPDTA NMR, 1 REGULARIZED MEAN STRUCTURE
AUTHOR D.S. GARRETT, A.M. GRONENBORN, G.M. CLORE
JRNL AUTH D.S. GARRETT, Y.-J. SEOK, D.-I. LIAO, A. PETERKOFSKY,
JRNL AUTH 2 A.M. GRONENBORN AND G.M. CLORE
JRNL TITL 1 SOLUTION STRUCTURE OF THE 30 KDA N-TERMINAL DOMAIN OF
JRNL TITL 2 ENZYME I OF THE ESCHERICHIA COLI PHOPHOENOLPYRUVATE:SUGAR
JRNL TITL 3 PHOPHOTRANSFERASE SYSTEM BY MULTIDIMENSIONAL NMR
JRNL REF BIOCHEMISTRY (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 EIN WAS SOLVED BY
REMARK 5 MULTI-DIMENSIONAL HETERONUCLEAR NMR AND
REMARK 5 IS BASED ON 4251 EXPERIMENTAL NMR RESTRAINTS: (A) INTRA-
REMARK 5 PROTEIN: 952 SEQUENTIAL (|I- J|=1), 809 MEDIUM RANGE (1 <
REMARK 5 |I-J| <=5) AND 586 LONG RANGE (|I-J| >5) INTERRESIDUES AND
REMARK 5 471 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE
REMARK 5 RESTRAINTS; 230 DISTANCES FOR 115 BACKBONE HYDROGEN BONDS;
REMARK 5 140 TORSION ANGLE RESTRAINTS; 163 THREE-BOND HN-HA COUPLING CONSTANT
REMARK 5 RESTRAINTS; AND 498 (258 CALPHA AND 241 CBETA) 13C SHIFT
REMARK 5 RESTRAINTS. (NUMBERS OF RESIDUES 1-259)
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) PROETIN SCI. 5, 1067-1080
REMARK 7
REMARK 7 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
REMARK 7 ENTRY .... AND 50 STRUCTURES ARE PRESENTED IN ENTRY ...
REMARK 7 IN THE RESTRAINED REGULARIZED MEAN COORDINATES THE LAST COLUMN
REMARK 7 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 HAS NO MEANING. BEST FITTING TO GENERATE THE
REMARK 7 AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 1-246 OF
REMARK 7 (RESIDUES 250-259 ARE DISORDERED IN SOLUTION)
REMARK 7 NOTE THE OCCUPANCY FIELD HAS NO MEANING.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 40 C
REMARK 210 PH :7 TO 8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : Triple resonance for assignment of
REMARK protein;
REMARK quantitative J correlation for coupling constants
REMARK 3D AND 4D HETERONUCLEAR SEPARATED NOE EXPERIMENTS.
REMARK 3D 13C-SEPARATED/12C-FILTERED NOE EXPERIMENTS FOR
REMARK REVERSE LABELED AROMATIC SAMPLES
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 : 50
REMARK 210
REMARK 210 REMARK:
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
REMARK 900 THIS ENTRY IS THE RESTRAINED REGULARIZED MEAN STRUCTURE
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
A. NOEs
;
save_
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