HEADER ISOMERASE 19-MAY-98 1BE1
TITLE GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B12-BINDING SUBUNIT;
COMPND 5 SYNONYM: MUTS;
COMPND 6 EC: 5.4.99.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM TETANOMORPHUM;
SOURCE 3 ORGANISM_TAXID: 1553;
SOURCE 4 STRAIN: H1;
SOURCE 5 ATCC: ATCC 15920;
SOURCE 6 COLLECTION: ATCC 15920;
SOURCE 7 GENE: MUTS;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL12 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PT7-7;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PMUTSX;
SOURCE 14 EXPRESSION_SYSTEM_GENE: MUTS
KEYWDS ISOMERASE, GLUTAMATE MUTASE, B12-BINDING SUBUNIT
EXPDTA SOLUTION NMR
AUTHOR M.TOLLINGER,R.KONRAT,B.H.HILBERT,E.N.G.MARSH,B.KRAEUTLER
REVDAT 4 16-FEB-22 1BE1 1 REMARK
REVDAT 3 24-FEB-09 1BE1 1 VERSN
REVDAT 2 01-APR-03 1BE1 1 JRNL
REVDAT 1 26-AUG-98 1BE1 0
JRNL AUTH M.TOLLINGER,R.KONRAT,B.H.HILBERT,E.N.MARSH,B.KRAUTLER
JRNL TITL HOW A PROTEIN PREPARES FOR B12 BINDING: STRUCTURE AND
JRNL TITL 2 DYNAMICS OF THE B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM
JRNL TITL 3 CLOSTRIDIUM TETANOMORPHUM
JRNL REF STRUCTURE V. 6 1021 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9739092
JRNL DOI 10.1016/S0969-2126(98)00103-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.E.HOLLOWAY,E.N.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 : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171643.
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 : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O,10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N HSQC; 2D X-FILT NOESY; 2D
REMARK 210 NOESY; 2D TOCSY; 3D 15N NOESY-
REMARK 210 HSQC; 3D 15N TOCSY-HSQC; 3D 15N
REMARK 210 HSQC-NOESY-HSQC; 3D HNHA
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 : NMRPIPE, ANSIG, FELIX, X-PLOR
REMARK 210 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 15
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 VAL A 10 -110.19 48.34
REMARK 500 ILE A 11 -119.34 -84.14
REMARK 500 ASP A 14 -42.48 -161.29
REMARK 500 CYS A 15 102.05 86.32
REMARK 500 HIS A 16 53.46 -96.20
REMARK 500 ASN A 20 -67.89 -124.33
REMARK 500 LYS A 21 -132.47 -160.37
REMARK 500 LEU A 23 53.88 78.28
REMARK 500 HIS A 25 46.17 -171.26
REMARK 500 SER A 26 -25.49 -164.88
REMARK 500 PHE A 27 -89.02 -68.20
REMARK 500 ASN A 29 -78.08 63.31
REMARK 500 LEU A 40 -104.18 71.28
REMARK 500 SER A 41 -12.94 161.57
REMARK 500 SER A 42 92.27 -30.42
REMARK 500 GLU A 52 -71.41 -64.71
REMARK 500 LYS A 54 48.89 80.59
REMARK 500 SER A 61 68.74 -100.11
REMARK 500 ALA A 81 -3.41 70.80
REMARK 500 LYS A 84 -168.78 -76.28
REMARK 500 ASN A 93 -84.05 74.46
REMARK 500 ILE A 94 -123.07 -109.74
REMARK 500 VAL A 95 -148.64 -135.68
REMARK 500 LYS A 98 -58.23 -132.19
REMARK 500 ASN A 100 64.60 70.25
REMARK 500 VAL A 104 -76.70 -54.07
REMARK 500 ARG A 115 -169.99 -110.59
REMARK 500 LYS A 131 -71.77 -82.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BE1 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 2 GLN A 43 LYS A 54 1 12
HELIX 2 3 GLU A 68 GLU A 80 1 13
HELIX 3 4 PRO A 102 MET A 111 1 10
HELIX 4 5 PRO A 123 GLY A 135 1 13
SHEET 1 1 5 ASN A 33 ILE A 37 0
SHEET 2 1 5 THR A 5 VAL A 10 1
SHEET 3 1 5 LEU A 57 SER A 62 1
SHEET 4 1 5 LYS A 87 GLY A 91 1
SHEET 5 1 5 ASP A 114 TYR A 117 1
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
(ATOM LINES ARE NOT SHOWN.)
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