Header list of 1fmf.pdb file
Complete list - n 24 2 Bytes
HEADER ISOMERASE 17-AUG-00 1FMF TITLE REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING TITLE 2 SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: METHYLASPARTATE MUTASE S CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GLUTAMATE MUTASE, MUTS; COMPND 5 EC: 5.4.99.1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM TETANOMORPHUM; SOURCE 3 ORGANISM_TAXID: 1553; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMUTSX KEYWDS NUCLEOTIDE BINDING FOLD, ROSSMANN FOLD, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR B.HOFFMANN,R.KONRAT,M.TOLLINGER,M.HUHTA,E.N.G.MARSH,B.KRAEUTLER REVDAT 5 24-JAN-18 1FMF 1 AUTHOR REVDAT 4 01-FEB-17 1FMF 1 AUTHOR VERSN REVDAT 3 24-FEB-09 1FMF 1 VERSN REVDAT 2 01-APR-03 1FMF 1 JRNL REVDAT 1 15-FEB-02 1FMF 0 JRNL AUTH B.HOFFMANN,M.TOLLINGER,R.KONRAT,M.HUHTA,E.N.MARSH,B.KRAUTLER JRNL TITL A PROTEIN PRE-ORGANIZED TO TRAP THE NUCLEOTIDE MOIETY OF JRNL TITL 2 COENZYME B(12): REFINED SOLUTION STRUCTURE OF THE JRNL TITL 3 B(12)-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM JRNL TITL 4 TETANOMORPHUM. JRNL REF CHEMBIOCHEM V. 2 643 2001 JRNL REFN ISSN 1439-4227 JRNL PMID 11828501 JRNL DOI 10.1002/1439-7633(20010903)2:9<643::AID-CBIC643>3.0.CO;2-J REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.TOLLINGER,R.KONRAT,B.H.HILBERT,E.N.G.MARSH,B.KRAEUTLER REMARK 1 TITL HOW A PROTEIN PREPARES FOR B12-BINDING: STRUCTURE AND REMARK 1 TITL 2 DYNAMICS OF THE B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM REMARK 1 TITL 3 CLOSTRIDIUM TETANOMORPHUM REMARK 1 REF STRUCTURE V. 6 1021 1998 REMARK 1 REFN ISSN 0969-2126 REMARK 1 DOI 10.1016/S0969-2126(98)00103-8 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.E.HOLLOWAY,E.N.G.MARSH REMARK 1 TITL ADENOSYLCOBALAMIN-DEPENDENT GLUTAMATE MUTASE FROM REMARK 1 TITL 2 CLOSTRIDIUM TETANOMORPHUM. OVEREXPRESSION IN ESCHERICHIA REMARK 1 TITL 3 COLI, PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT REMARK 1 TITL 4 ENZYME REMARK 1 REF J.BIOL.CHEM. V. 269 20425 1994 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.8.5.1 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUENGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE MUTS STRUCTURE MODELS 1-15 ARE BASED ON A TOTAL OF 1792 REMARK 3 RESTRAINTS, 1553 ARE NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 184 DIHEDRAL ANGLE RESTRAINTS, 55 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. BACKBONE DIHEDRAL ANGLES PHI AND PSI WERE REMARK 3 OBTAINED BY REMARK 3 EMPLOYING TALOS SOFTWARE [G. CORNILESCU ET AL., J. BIOMOL. NMR REMARK 3 1999, 13, 289-302]. REMARK 3 PHI AND PSI TORSION ANGLE RESTRAINTS FOR THE MUTS RESIDUES 23-30, REMARK 3 WHICH FORM A "NASCENT" HELIX [M. TOLLINGER ET AL., STRUCTURE 1998, REMARK 3 6, 1021-1033], REMARK 3 WERE NOT USED IN STRUCTURE REMARK 3 CALCULATIONS FOR MUTS MODELS 16-30. REMARK 4 REMARK 4 1FMF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-00. REMARK 100 THE DEPOSITION ID IS D_1000011712. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 299 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 11MM KXH3-XPO4 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM MUTS U-98% 15N,13C; 11MM REMARK 210 PHOSPHATE BUFFER; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ANSIG 3.3, X-PLOR 3.8.5.1, TALOS REMARK 210 98.040.21.02 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, SIMULATED ANNEALING REMARK 210 REFINEMENT, ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HG1 THR A 5 HG1 THR A 53 1.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 15 HIS A 25 CG HIS A 25 CD2 0.055 REMARK 500 18 SER A 41 CB SER A 41 OG 0.085 REMARK 500 22 SER A 41 CB SER A 41 OG 0.087 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 3 THR A 53 CA - CB - CG2 ANGL. DEV. = -11.1 DEGREES REMARK 500 22 THR A 53 CA - CB - CG2 ANGL. DEV. = -10.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 CYS A 15 108.42 -164.28 REMARK 500 1 ALA A 17 27.00 176.13 REMARK 500 1 ASN A 20 55.41 -163.70 REMARK 500 1 LYS A 21 -37.58 -149.21 REMARK 500 1 LEU A 40 106.75 64.41 REMARK 500 1 LYS A 54 78.45 90.60 REMARK 500 1 TYR A 64 1.56 -160.66 REMARK 500 1 LEU A 83 48.30 -145.17 REMARK 500 1 LYS A 98 129.63 -171.40 REMARK 500 1 GLN A 99 -112.88 -73.80 REMARK 500 1 TRP A 101 -58.41 -7.47 REMARK 500 1 PRO A 118 -177.11 -63.66 REMARK 500 2 ASP A 14 98.44 71.01 REMARK 500 2 ASN A 20 35.26 -168.22 REMARK 500 2 ILE A 22 -34.18 87.07 REMARK 500 2 LEU A 40 73.57 60.78 REMARK 500 2 LYS A 54 71.35 87.18 REMARK 500 2 LEU A 63 -68.12 -102.34 REMARK 500 2 LEU A 83 48.72 -142.24 REMARK 500 2 VAL A 96 155.35 -46.77 REMARK 500 2 TRP A 101 -62.37 6.84 REMARK 500 2 PRO A 118 176.19 -54.53 REMARK 500 3 GLU A 2 74.09 -115.37 REMARK 500 3 SER A 13 167.72 58.90 REMARK 500 3 CYS A 15 -152.23 -164.85 REMARK 500 3 VAL A 18 101.35 47.22 REMARK 500 3 LYS A 21 -53.04 103.42 REMARK 500 3 LEU A 40 148.88 174.67 REMARK 500 3 SER A 42 117.54 178.17 REMARK 500 3 LYS A 54 61.74 79.45 REMARK 500 3 LEU A 83 35.54 -142.14 REMARK 500 3 VAL A 96 88.94 -68.50 REMARK 500 3 LYS A 98 164.58 73.75 REMARK 500 3 PRO A 118 -179.08 -54.91 REMARK 500 3 SER A 122 151.61 -44.45 REMARK 500 4 SER A 13 118.94 -175.81 REMARK 500 4 ASP A 14 85.47 -61.25 REMARK 500 4 CYS A 15 -65.07 -172.96 REMARK 500 4 ILE A 22 -45.94 177.95 REMARK 500 4 LEU A 40 83.74 -177.07 REMARK 500 4 SER A 41 -156.39 87.68 REMARK 500 4 SER A 42 -147.67 -117.35 REMARK 500 4 LYS A 54 58.84 91.86 REMARK 500 4 ILE A 94 16.23 53.35 REMARK 500 4 VAL A 96 31.68 -96.60 REMARK 500 4 GLN A 99 126.57 92.71 REMARK 500 4 TRP A 101 -79.92 27.63 REMARK 500 4 PRO A 118 177.68 -55.77 REMARK 500 5 GLU A 2 83.49 61.66 REMARK 500 5 SER A 13 -148.07 -162.15 REMARK 500 REMARK 500 THIS ENTRY HAS 416 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASP A 70 CYS A 71 1 -149.56 REMARK 500 TRP A 101 PRO A 102 5 125.09 REMARK 500 SER A 62 LEU A 63 6 -142.49 REMARK 500 ILE A 22 LEU A 23 8 -143.76 REMARK 500 ILE A 22 LEU A 23 12 147.15 REMARK 500 LEU A 23 ASP A 24 22 147.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 2 TYR A 64 0.09 SIDE CHAIN REMARK 500 2 TYR A 117 0.07 SIDE CHAIN REMARK 500 5 TYR A 64 0.09 SIDE CHAIN REMARK 500 6 TYR A 117 0.09 SIDE CHAIN REMARK 500 8 TYR A 117 0.08 SIDE CHAIN REMARK 500 10 TYR A 64 0.07 SIDE CHAIN REMARK 500 11 TYR A 64 0.11 SIDE CHAIN REMARK 500 16 TYR A 117 0.10 SIDE CHAIN REMARK 500 17 TYR A 117 0.07 SIDE CHAIN REMARK 500 20 TYR A 117 0.11 SIDE CHAIN REMARK 500 24 TYR A 117 0.07 SIDE CHAIN REMARK 500 26 TYR A 117 0.08 SIDE CHAIN REMARK 500 27 TYR A 117 0.08 SIDE CHAIN REMARK 500 28 TYR A 117 0.09 SIDE CHAIN REMARK 500 29 TYR A 117 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BE1 RELATED DB: PDB REMARK 900 1BE1 CONTAINS THE NMR STRUCTURE OF 15N-LABELED MUTS DBREF 1FMF A 1 137 UNP Q05488 MAMA_CLOTT 1 137 SEQRES 1 A 137 MET GLU LYS LYS THR ILE VAL LEU GLY VAL ILE GLY SER SEQRES 2 A 137 ASP CYS HIS ALA VAL GLY ASN LYS ILE LEU ASP HIS SER SEQRES 3 A 137 PHE THR ASN ALA GLY PHE ASN VAL VAL ASN ILE GLY VAL SEQRES 4 A 137 LEU SER SER GLN GLU ASP PHE ILE ASN ALA ALA ILE GLU SEQRES 5 A 137 THR LYS ALA ASP LEU ILE CYS VAL SER SER LEU TYR GLY SEQRES 6 A 137 GLN GLY GLU ILE ASP CYS LYS GLY LEU ARG GLU LYS CYS SEQRES 7 A 137 ASP GLU ALA GLY LEU LYS GLY ILE LYS LEU PHE VAL GLY SEQRES 8 A 137 GLY ASN ILE VAL VAL GLY LYS GLN ASN TRP PRO ASP VAL SEQRES 9 A 137 GLU GLN ARG PHE LYS ALA MET GLY PHE ASP ARG VAL TYR SEQRES 10 A 137 PRO PRO GLY THR SER PRO GLU THR THR ILE ALA ASP MET SEQRES 11 A 137 LYS GLU VAL LEU GLY VAL GLU HELIX 1 1 ILE A 22 ASN A 29 1 8 HELIX 2 2 SER A 42 LYS A 54 1 13 HELIX 3 3 GLN A 66 LYS A 72 1 7 HELIX 4 4 GLY A 73 ALA A 81 1 9 HELIX 5 5 ASN A 100 GLY A 112 1 13 HELIX 6 6 PRO A 123 LEU A 134 1 12 SHEET 1 A 5 ASN A 33 SER A 41 0 SHEET 2 A 5 THR A 5 ILE A 11 1 N ILE A 6 O ASN A 33 SHEET 3 A 5 ALA A 55 SER A 62 1 N ASP A 56 O THR A 5 SHEET 4 A 5 LYS A 87 GLY A 92 1 N LYS A 87 O ASP A 56 SHEET 5 A 5 ARG A 115 TYR A 117 1 O ARG A 115 N VAL A 90 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 MODEL 1
Complete list - n 24 2 Bytes