Header list of 1g11.pdb file
Complete list - b 23 2 Bytes
HEADER OXIDOREDUCTASE 10-OCT-00 1G11
TITLE TOLUENE-4-MONOOXYGENASE CATALYTIC EFFECTOR PROTEIN NMR STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLUENE-4-MONOOXYGENASE CATALYTIC EFFECTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TOLUENE-4-MONOOXYGENASE SYSTEM PROTEIN D, T4MOD;
COMPND 5 EC: 1.14.13.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS MENDOCINA;
SOURCE 3 ORGANISM_TAXID: 300;
SOURCE 4 STRAIN: KR1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS AROMATIC HYDROCARBON CATABOLISM, OXIDOREDUCTASE, MONOOXYGENASE,
KEYWDS 2 TOLUENE OXIDATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.HEMMI,J.M.STUDTS,Y.K.CHAE,J.SONG,J.L.MARKLEY,B.G.FOX
REVDAT 4 23-FEB-22 1G11 1 REMARK
REVDAT 3 24-FEB-09 1G11 1 VERSN
REVDAT 2 11-OCT-05 1G11 1 REMARK
REVDAT 1 09-MAY-01 1G11 0
JRNL AUTH H.HEMMI,J.M.STUDTS,Y.K.CHAE,J.SONG,J.L.MARKLEY,B.G.FOX
JRNL TITL SOLUTION STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE EFFECTOR
JRNL TITL 2 PROTEIN (T4MOD).
JRNL REF BIOCHEMISTRY V. 40 3512 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11297417
JRNL DOI 10.1021/BI0013703
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.HEMMI,J.M.STUDTS,Y.K.CHAE,B.G.FOX,J.L.MARKLEY
REMARK 1 TITL ASSIGNMENT OF 1H, 13C AND 15N NMR SIGNALS IN THE TOLUENE
REMARK 1 TITL 2 4-MONOOXYGENASE EFFECTOR PROTEIN
REMARK 1 REF J.BIOMOL.NMR V. 16 359 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008333115661
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.M.STUDTS,B.G.FOX
REMARK 1 TITL APPLICATION OF FED-BATCH FERMENTATION TO THE PREPARATION OF
REMARK 1 TITL 2 ISOTOPICALY LABELED OR SELENOMETHIONYL-LABELED PROTEINS
REMARK 1 REF PROTEIN EXPR.PURIF. V. 16 109 1999
REMARK 1 REFN ISSN 1046-5928
REMARK 1 DOI 10.1006/PREP.1999.1067
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.XIA,J.D.PIKUS,W.XIA,K.MCCLAY,R.J.STEFFAN,Y.K.CHAE,
REMARK 1 AUTH 2 M.M.WESTLER,J.L.MARKLEY,B.G.FOX
REMARK 1 TITL DETECTION AND CLASSIFICATION OF HYPERFINE-SHIFTED 1H, 2H,
REMARK 1 TITL 2 AND 15N RESONANCES OF THE RIESKE FERREDOXIN COMPONENT FROM
REMARK 1 TITL 3 TOLUENE 4-MONOOXYGENASE
REMARK 1 REF BIOCHEMISTRY V. 38 727 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI981851A
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.D.PIKUS,J.M STUDTS,C.ACHIM,K.E.KAUFFMANN,E.MUNCK,
REMARK 1 AUTH 2 R.J.STEFFAN,K.MCCLAY,B.G.FOX
REMARK 1 TITL RECOMBINANT TOLUENE-4-MONOOXYGENASE: CATALYTIC AND MOSSBAUER
REMARK 1 TITL 2 STUDIES OF THE PURIFIED DIIRON AND RIESKE COMPONENTS OF A
REMARK 1 TITL 3 FOUR-PROTEIN COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 35 9106 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI960456M
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.M.WHITED,D.T.GIBSON
REMARK 1 TITL TOLUENE-4-MONOOXYGENASE, A THREE COMPONENT ENZYME SYSTEM
REMARK 1 TITL 2 THAT CATALYZES THE OXIDATION OF TOLUENE TO P-CRESOL IN
REMARK 1 TITL 3 PSEUDOMONAS MENDOCINA KR1
REMARK 1 REF J.BACTERIOL. V. 173 3010 1991
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843, DYANA 1.5
REMARK 3 AUTHORS : BRUNGER (X-PLOR), GUNTER, MUMENTHALER, WUTRICH
REMARK 3 (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1339
REMARK 3 INTERPROTON RESTRAINTS. THESE COMPRISED 367 INTRARESIDUE, 424
REMARK 3 SEQUENTIAL, 195 MEDIUM-RANGE, AND 273 LONG-RANGE NOE DISTANCE
REMARK 3 RESTRAINTS AND 128 DIHEDRAL ANGLE RESTRAINTS (78 PSI, 26 PHI,
REMARK 3 AND 24 CHI), AND 80 HYDROGEN BONDING RESTRAINTS.
REMARK 4
REMARK 4 1G11 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012099.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 67 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1 MM [U-13C,U-15N] T4MOD; 3.0
REMARK 210 MM [NA] T4MOD
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N
REMARK 210 HSQC,HNCA,HN(CO)CA,C(CO)NH,HNCACB,HCCH-COSY,HCCH-TOCSY,2D_1H-
REMARK 210 NOESY,2D_1H-TOCSY,CT-13C-HSQC,3D_NOESY-CT-HSCQ,3D_TOCSY-CT-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 123 1H-15N CROSS PEAKS WERE ASSIGNED OUT OF THE EXPECTED
REMARK 210 129 CROSS PEAKS (95% COMPLETE). 386 BACKBONE RESONANCES WERE
REMARK 210 ASSIGNED OUT OF THE EXPECTED 400 RESONANCES (97% COMPLETE). 789
REMARK 210 SIDECHAIN RESONANCES WERE ASSIGNED OUT OF THE EXPECTED 901
REMARK 210 RESONANCES (88% COMPLETE). ARG SIDECHAIN ATOMS ACCOUNT FOR 51 OF
REMARK 210 112 UNASSIGNED SIDECHAIN ATOMS (51%).
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 OD2 ASP A 33 H THR A 59 1.52
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 ALA A 7 44.34 -146.80
REMARK 500 1 ASN A 11 -74.26 -139.57
REMARK 500 1 LYS A 37 46.13 -85.02
REMARK 500 1 GLU A 38 49.54 179.49
REMARK 500 1 ARG A 45 -47.53 162.66
REMARK 500 1 ARG A 60 33.18 -88.05
REMARK 500 1 PHE A 71 -157.01 -160.16
REMARK 500 1 ALA A 81 -52.24 -122.47
REMARK 500 1 ALA A 84 -45.14 -131.13
REMARK 500 1 ASP A 92 59.75 -149.72
REMARK 500 1 LYS A 100 -79.32 -78.32
REMARK 500 2 THR A 2 124.55 61.76
REMARK 500 2 ASP A 5 110.83 -166.49
REMARK 500 2 ALA A 7 65.86 -154.18
REMARK 500 2 LEU A 8 -63.30 -137.49
REMARK 500 2 HIS A 9 175.15 -57.08
REMARK 500 2 ASN A 11 -48.59 -139.31
REMARK 500 2 ASN A 12 147.50 179.94
REMARK 500 2 ARG A 18 -167.14 -78.88
REMARK 500 2 ASP A 21 -147.55 -179.61
REMARK 500 2 GLU A 38 43.82 179.08
REMARK 500 2 ARG A 44 -71.18 -81.16
REMARK 500 2 ARG A 45 -42.62 168.04
REMARK 500 2 GLU A 55 87.95 -178.46
REMARK 500 2 ARG A 60 45.46 -84.18
REMARK 500 2 PHE A 71 -159.07 -160.23
REMARK 500 2 ALA A 81 -66.27 -128.64
REMARK 500 2 ASP A 92 61.77 -151.17
REMARK 500 2 LYS A 100 -65.59 -103.85
REMARK 500 3 ALA A 7 101.11 -175.57
REMARK 500 3 HIS A 9 162.13 172.13
REMARK 500 3 ASN A 11 -88.93 -149.10
REMARK 500 3 LYS A 37 39.66 -88.27
REMARK 500 3 GLU A 38 37.64 179.40
REMARK 500 3 ARG A 45 -55.26 161.16
REMARK 500 3 THR A 59 19.40 -149.73
REMARK 500 3 ARG A 60 46.21 -87.55
REMARK 500 3 PHE A 71 -157.73 -160.15
REMARK 500 3 ASN A 72 -169.83 -163.58
REMARK 500 3 LEU A 80 80.44 -159.43
REMARK 500 3 ASP A 92 64.15 -153.54
REMARK 500 3 THR A 101 140.78 -37.02
REMARK 500 4 THR A 2 97.66 58.30
REMARK 500 4 ALA A 7 48.96 -109.20
REMARK 500 4 HIS A 9 169.38 172.96
REMARK 500 4 ASN A 11 -69.74 -161.68
REMARK 500 4 ASN A 12 146.69 -172.90
REMARK 500 4 ASP A 21 130.40 179.96
REMARK 500 4 GLU A 38 51.23 178.95
REMARK 500 4 ARG A 45 -50.43 160.16
REMARK 500
REMARK 500 THIS ENTRY HAS 348 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4560 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS
REMARK 900 RELATED ID: 1G10 RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1G11 A 1 102 UNP Q00459 TMOD_PSEME 1 102
SEQRES 1 A 102 SER THR LEU ALA ASP GLN ALA LEU HIS ASN ASN ASN VAL
SEQRES 2 A 102 GLY PRO ILE ILE ARG ALA GLY ASP LEU VAL GLU PRO VAL
SEQRES 3 A 102 ILE GLU THR ALA GLU ILE ASP ASN PRO GLY LYS GLU ILE
SEQRES 4 A 102 THR VAL GLU ASP ARG ARG ALA TYR VAL ARG ILE ALA ALA
SEQRES 5 A 102 GLU GLY GLU LEU ILE LEU THR ARG LYS THR LEU GLU GLU
SEQRES 6 A 102 GLN LEU GLY ARG PRO PHE ASN MET GLN GLU LEU GLU ILE
SEQRES 7 A 102 ASN LEU ALA SER PHE ALA GLY GLN ILE GLN ALA ASP GLU
SEQRES 8 A 102 ASP GLN ILE ARG PHE TYR PHE ASP LYS THR MET
HELIX 1 1 LEU A 22 ASP A 33 1 12
HELIX 2 2 ARG A 60 LEU A 67 1 8
HELIX 3 3 MET A 73 ASN A 79 1 7
SHEET 1 A 3 ILE A 16 ARG A 18 0
SHEET 2 A 3 TYR A 47 ALA A 51 -1 N VAL A 48 O ILE A 17
SHEET 3 A 3 THR A 40 ASP A 43 -1 O THR A 40 N ALA A 51
SHEET 1 B 3 LEU A 56 LEU A 58 0
SHEET 2 B 3 GLN A 93 TYR A 97 -1 N ILE A 94 O LEU A 58
SHEET 3 B 3 GLN A 86 ASP A 90 -1 N GLN A 86 O TYR A 97
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 - b 23 2 Bytes