HEADER MUTATOR PROTEIN 05-DEC-96 1TUM
TITLE MUTT PYROPHOSPHOHYDROLASE-METAL-NUCLEOTIDE-METAL COMPLEX, NMR, 16
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUTATOR MUTT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MUTTQC, DGTP PYROPHOSPHOHYDROLASE, 7,8-DIHYDRO-8-OXOGUANINE-
COMPND 5 TRIPHOSPHATASE;
COMPND 6 EC: 3.6.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: MUTT-MG(2+)-AMPCPP-MG(2+) COMPLEX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: K12-I7023;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET MUTT, T7 PROMOTER;
SOURCE 9 EXPRESSION_SYSTEM_GENE: MUTT
KEYWDS MUTATOR PROTEIN, QUATERNARY COMPLEX, NUCLEOSIDE TRIPHOSPHATE
KEYWDS 2 PYROPHOSPHOHYDROLASE, MUTT PYROPHOSPHOHYDROLASE-METAL-SUBSTRATE
KEYWDS 3 ANALOG COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR J.LIN,C.ABEYGUNAWARDANA,D.N.FRICK,M.J.BESSMAN,A.S.MILDVAN
REVDAT 3 02-MAR-22 1TUM 1 REMARK LINK
REVDAT 2 24-FEB-09 1TUM 1 VERSN
REVDAT 1 15-MAY-97 1TUM 0
JRNL AUTH J.LIN,C.ABEYGUNAWARDANA,D.N.FRICK,M.J.BESSMAN,A.S.MILDVAN
JRNL TITL SOLUTION STRUCTURE OF THE QUATERNARY MUTT-M2+-AMPCPP-M2+
JRNL TITL 2 COMPLEX AND MECHANISM OF ITS PYROPHOSPHOHYDROLASE ACTION.
JRNL REF BIOCHEMISTRY V. 36 1199 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9063868
JRNL DOI 10.1021/BI962619C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.N.FRICK,D.J.WEBER,C.ABEYGUNAWARDANA,A.G.GITTIS,
REMARK 1 AUTH 2 M.J.BESSMAN,A.S.MILDVAN
REMARK 1 TITL NMR STUDIES OF THE CONFORMATIONS AND LOCATION OF NUCLEOTIDES
REMARK 1 TITL 2 BOUND TO THE E.COLI MUTT ENZYME
REMARK 1 REF BIOCHEMISTRY V. 34 5577 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.ABEYGUNAWARDANA,D.J.WEBER,A.G.GITTIS,D.N.FRICK,J.LIN,
REMARK 1 AUTH 2 A.F.MILLER,M.J.BESSMAN,A.S.MILDVAN
REMARK 1 TITL SOLUTION STRUCTURE OF THE MUTT ENZYME, A NUCLEOSIDE
REMARK 1 TITL 2 TRIPHOSPHATE PYROPHOSPHOHYDROLASE
REMARK 1 REF BIOCHEMISTRY V. 34 14997 1995
REMARK 1 REFN ISSN 0006-2960
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 1TUM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176861.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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
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 VAL A 8 -79.57 -79.21
REMARK 500 1 ILE A 10 169.51 -49.43
REMARK 500 1 ASN A 13 0.23 -158.58
REMARK 500 1 ASN A 15 -48.49 -163.79
REMARK 500 1 ASN A 16 37.40 -161.74
REMARK 500 1 PHE A 19 41.94 -82.98
REMARK 500 1 THR A 21 95.05 -64.39
REMARK 500 1 ARG A 22 78.95 -104.82
REMARK 500 1 ARG A 23 76.44 25.33
REMARK 500 1 ALA A 30 18.65 -156.78
REMARK 500 1 LYS A 32 39.50 -81.52
REMARK 500 1 GLU A 34 -128.61 -91.16
REMARK 500 1 PRO A 36 88.26 -61.01
REMARK 500 1 LYS A 39 102.32 69.91
REMARK 500 1 GLU A 41 -32.55 -171.64
REMARK 500 1 GLU A 44 25.03 -168.99
REMARK 500 1 PRO A 46 -16.43 -48.37
REMARK 500 1 GLU A 47 -72.71 -78.60
REMARK 500 1 GLU A 57 -83.03 -80.21
REMARK 500 1 VAL A 58 -80.02 -80.27
REMARK 500 1 ILE A 60 -159.64 -94.27
REMARK 500 1 THR A 61 -70.87 -135.45
REMARK 500 1 PRO A 62 -171.99 -59.30
REMARK 500 1 GLN A 63 -22.08 144.03
REMARK 500 1 HIS A 64 72.12 43.82
REMARK 500 1 PHE A 68 -51.72 81.35
REMARK 500 1 GLU A 69 179.12 167.74
REMARK 500 1 GLU A 72 89.69 -154.84
REMARK 500 1 ASP A 77 33.05 -141.26
REMARK 500 1 LEU A 82 85.23 -157.31
REMARK 500 1 PHE A 84 70.73 -101.57
REMARK 500 1 GLU A 88 17.37 -149.55
REMARK 500 1 ARG A 89 67.51 -160.26
REMARK 500 1 PRO A 94 -158.15 -73.94
REMARK 500 1 TRP A 95 112.53 177.53
REMARK 500 1 GLU A 98 -111.36 -74.70
REMARK 500 1 VAL A 108 98.84 103.75
REMARK 500 1 LEU A 110 153.03 -29.96
REMARK 500 1 ALA A 112 -3.26 73.88
REMARK 500 1 ASN A 119 45.30 -85.82
REMARK 500 2 LYS A 2 -131.05 -159.05
REMARK 500 2 VAL A 8 -73.65 -78.83
REMARK 500 2 ILE A 10 172.54 -48.04
REMARK 500 2 ASN A 13 62.20 -161.66
REMARK 500 2 GLU A 14 -49.55 -148.70
REMARK 500 2 ASN A 15 -48.54 -161.17
REMARK 500 2 ASN A 16 42.52 -162.34
REMARK 500 2 PHE A 19 47.73 -83.15
REMARK 500 2 ARG A 23 76.81 24.49
REMARK 500 2 MET A 29 -106.33 -121.29
REMARK 500
REMARK 500 THIS ENTRY HAS 624 RAMACHANDRAN OUTLIERS.
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 1 ARG A 12 0.30 SIDE CHAIN
REMARK 500 1 ARG A 22 0.24 SIDE CHAIN
REMARK 500 1 ARG A 23 0.31 SIDE CHAIN
REMARK 500 1 ARG A 52 0.31 SIDE CHAIN
REMARK 500 1 ARG A 78 0.21 SIDE CHAIN
REMARK 500 1 ARG A 89 0.24 SIDE CHAIN
REMARK 500 1 ARG A 128 0.19 SIDE CHAIN
REMARK 500 2 ARG A 12 0.31 SIDE CHAIN
REMARK 500 2 ARG A 23 0.17 SIDE CHAIN
REMARK 500 2 ARG A 52 0.25 SIDE CHAIN
REMARK 500 2 ARG A 78 0.27 SIDE CHAIN
REMARK 500 2 ARG A 89 0.28 SIDE CHAIN
REMARK 500 2 ARG A 128 0.26 SIDE CHAIN
REMARK 500 3 ARG A 12 0.21 SIDE CHAIN
REMARK 500 3 ARG A 23 0.25 SIDE CHAIN
REMARK 500 3 ARG A 78 0.31 SIDE CHAIN
REMARK 500 3 ARG A 89 0.30 SIDE CHAIN
REMARK 500 4 ARG A 12 0.18 SIDE CHAIN
REMARK 500 4 ARG A 23 0.32 SIDE CHAIN
REMARK 500 4 ARG A 52 0.32 SIDE CHAIN
REMARK 500 4 ARG A 78 0.25 SIDE CHAIN
REMARK 500 4 ARG A 128 0.22 SIDE CHAIN
REMARK 500 5 ARG A 12 0.32 SIDE CHAIN
REMARK 500 5 ARG A 22 0.18 SIDE CHAIN
REMARK 500 5 ARG A 23 0.32 SIDE CHAIN
REMARK 500 5 ARG A 52 0.12 SIDE CHAIN
REMARK 500 5 ARG A 78 0.27 SIDE CHAIN
REMARK 500 5 ARG A 89 0.31 SIDE CHAIN
REMARK 500 5 ARG A 128 0.21 SIDE CHAIN
REMARK 500 6 ARG A 12 0.28 SIDE CHAIN
REMARK 500 6 ARG A 22 0.30 SIDE CHAIN
REMARK 500 6 ARG A 23 0.13 SIDE CHAIN
REMARK 500 6 ARG A 78 0.32 SIDE CHAIN
REMARK 500 6 ARG A 128 0.28 SIDE CHAIN
REMARK 500 7 ARG A 12 0.31 SIDE CHAIN
REMARK 500 7 ARG A 23 0.14 SIDE CHAIN
REMARK 500 7 ARG A 52 0.23 SIDE CHAIN
REMARK 500 7 ARG A 78 0.25 SIDE CHAIN
REMARK 500 7 ARG A 89 0.12 SIDE CHAIN
REMARK 500 7 ARG A 128 0.10 SIDE CHAIN
REMARK 500 8 ARG A 22 0.30 SIDE CHAIN
REMARK 500 8 ARG A 23 0.22 SIDE CHAIN
REMARK 500 8 ARG A 52 0.30 SIDE CHAIN
REMARK 500 8 ARG A 78 0.20 SIDE CHAIN
REMARK 500 8 ARG A 89 0.32 SIDE CHAIN
REMARK 500 8 ARG A 128 0.22 SIDE CHAIN
REMARK 500 9 ARG A 12 0.14 SIDE CHAIN
REMARK 500 9 ARG A 22 0.24 SIDE CHAIN
REMARK 500 9 ARG A 23 0.15 SIDE CHAIN
REMARK 500 9 ARG A 52 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 98 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 132 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 38 O
REMARK 620 2 GLU A 56 OE2 115.0
REMARK 620 3 GLU A 57 OE2 113.1 74.3
REMARK 620 4 GLU A 98 OE1 98.6 141.0 74.6
REMARK 620 5 HOH A 133 O 61.6 97.7 168.0 116.2
REMARK 620 6 HOH A 134 O 147.3 80.7 98.4 81.1 88.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CON A 131 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APC A 130 O1G
REMARK 620 2 CON A 131 N1 178.8
REMARK 620 3 CON A 131 N2 90.9 90.2
REMARK 620 4 CON A 131 N3 90.5 90.0 90.1
REMARK 620 5 CON A 131 N4 89.4 90.1 90.2 179.7
REMARK 620 6 APC A 130 O1B 88.6 90.3 179.5 90.0 89.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CON A 131
DBREF 1TUM A 1 129 UNP P08337 MUTT_ECOLI 1 129
SEQRES 1 A 129 MET LYS LYS LEU GLN ILE ALA VAL GLY ILE ILE ARG ASN
SEQRES 2 A 129 GLU ASN ASN GLU ILE PHE ILE THR ARG ARG ALA ALA ASP
SEQRES 3 A 129 ALA HIS MET ALA ASN LYS LEU GLU PHE PRO GLY GLY LYS
SEQRES 4 A 129 ILE GLU MET GLY GLU THR PRO GLU GLN ALA VAL VAL ARG
SEQRES 5 A 129 GLU LEU GLN GLU GLU VAL GLY ILE THR PRO GLN HIS PHE
SEQRES 6 A 129 SER LEU PHE GLU LYS LEU GLU TYR GLU PHE PRO ASP ARG
SEQRES 7 A 129 HIS ILE THR LEU TRP PHE TRP LEU VAL GLU ARG TRP GLU
SEQRES 8 A 129 GLY GLU PRO TRP GLY LYS GLU GLY GLN PRO GLY GLU TRP
SEQRES 9 A 129 MET SER LEU VAL GLY LEU ASN ALA ASP ASP PHE PRO PRO
SEQRES 10 A 129 ALA ASN GLU PRO VAL ILE ALA LYS LEU LYS ARG LEU
HET MG A 132 1
HET APC A 130 46
HET CON A 131 17
HETNAM MG MAGNESIUM ION
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM CON COBALT TETRAAMMINE ION
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 APC C11 H18 N5 O12 P3
FORMUL 4 CON CO H12 N4 3+
FORMUL 5 HOH *2(H2 O)
HELIX 1 1 PRO A 46 GLN A 55 1 10
HELIX 2 2 GLU A 120 LYS A 127 1 8
SHEET 1 A 2 SER A 66 LEU A 71 0
SHEET 2 A 2 LEU A 82 LEU A 86 -1 N LEU A 86 O SER A 66
LINK O GLY A 38 MG MG A 132 1555 1555 2.47
LINK OE2 GLU A 56 MG MG A 132 1555 1555 2.45
LINK OE2 GLU A 57 MG MG A 132 1555 1555 2.43
LINK OE1 GLU A 98 MG MG A 132 1555 1555 2.43
LINK O1G APC A 130 CO CON A 131 1555 1555 2.10
LINK O1B APC A 130 CO CON A 131 1555 1555 2.11
LINK MG MG A 132 O HOH A 133 1555 1555 2.11
LINK MG MG A 132 O HOH A 134 1555 1555 2.11
SITE 1 AC1 8 GLY A 38 GLU A 53 GLU A 56 GLU A 57
SITE 2 AC1 8 GLU A 98 APC A 130 HOH A 133 HOH A 134
SITE 1 AC2 12 LEU A 4 ILE A 6 GLY A 38 LYS A 39
SITE 2 AC2 12 GLU A 41 ILE A 80 LEU A 82 GLU A 98
SITE 3 AC2 12 CON A 131 MG A 132 HOH A 133 HOH A 134
SITE 1 AC3 1 APC A 130
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
(ATOM LINES ARE NOT SHOWN.)
END
