Click here to see the 3D structure Header list of 1tum.pdb file

Complete list - r 2 2 Bytes
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
Complete list - r 2 2 Bytes