Header list of 1ao8.pdb file
Complete list - b 16 2 Bytes
HEADER OXIDOREDUCTASE 22-JUL-97 1AO8
TITLE DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE, NMR, 21
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHFR;
COMPND 5 EC: 1.5.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;
SOURCE 3 ORGANISM_TAXID: 1582;
SOURCE 4 STRAIN: METHOTREXATE-RESISTANT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NF1;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMT702
KEYWDS OXIDOREDUCTASE, INHIBITOR-ENZYME COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR A.R.GARGARO,A.SOTERIOU,T.A.FRENKIEL,C.J.BAUER,B.BIRDSALL,
AUTHOR 2 V.I.POLSHAKOV,I.L.BARSUKOV,G.C.K.ROBERTS,J.FEENEY
REVDAT 3 16-FEB-22 1AO8 1 REMARK
REVDAT 2 24-FEB-09 1AO8 1 VERSN
REVDAT 1 25-FEB-98 1AO8 0
JRNL AUTH A.R.GARGARO,A.SOTERIOU,T.A.FRENKIEL,C.J.BAUER,B.BIRDSALL,
JRNL AUTH 2 V.I.POLSHAKOV,I.L.BARSUKOV,G.C.ROBERTS,J.FEENEY
JRNL TITL THE SOLUTION STRUCTURE OF THE COMPLEX OF LACTOBACILLUS CASEI
JRNL TITL 2 DIHYDROFOLATE REDUCTASE WITH METHOTREXATE.
JRNL REF J.MOL.BIOL. V. 277 119 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514736
JRNL DOI 10.1006/JMBI.1997.1560
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS
REMARK 1 TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 A RESOLUTION.
REMARK 1 TITL 3 I. GENERAL FEATURES AND BINDING OF METHOTREXATE
REMARK 1 REF J.BIOL.CHEM. V. 257 13650 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 J. MOL. BIOL. PAPER, GARGARO ET AL. CITED ABOVE.
REMARK 4
REMARK 4 1AO8 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_1000171053.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; NOESY; ROESY; HNHA; HNHB;
REMARK 210 HSQC; 3D-1H/13C-NOESY-HMQC; 3D-
REMARK 210 1H/ 15N-HMQC-NOESY-HMQC; 1H/15N-
REMARK 210 NOESY-HSQC; 4D-13C/ 13C-EDITED-
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 21
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATION
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 1 LEU A 23 78.79 -113.87
REMARK 500 1 GLN A 33 32.92 -98.61
REMARK 500 1 THR A 34 -48.26 -150.30
REMARK 500 1 GLU A 56 -11.31 80.52
REMARK 500 1 ASP A 67 31.55 -148.17
REMARK 500 1 ALA A 70 110.46 -165.50
REMARK 500 1 HIS A 77 36.02 -144.34
REMARK 500 1 PHE A 106 56.77 -94.83
REMARK 500 1 ASP A 108 34.13 -98.27
REMARK 500 1 ASP A 109 76.92 -163.66
REMARK 500 1 ASP A 135 38.25 -97.26
REMARK 500 1 ASP A 146 -167.06 -115.62
REMARK 500 1 LEU A 151 31.17 -96.40
REMARK 500 2 GLN A 33 37.28 -98.78
REMARK 500 2 THR A 34 -45.28 -146.41
REMARK 500 2 HIS A 77 36.16 -150.24
REMARK 500 2 PHE A 106 52.13 -94.88
REMARK 500 2 ASP A 109 67.69 -109.92
REMARK 500 2 ASP A 111 -64.21 -133.76
REMARK 500 2 ASP A 135 35.81 -99.27
REMARK 500 2 LEU A 151 31.46 -96.72
REMARK 500 3 ILE A 13 28.70 -145.72
REMARK 500 3 LYS A 15 114.86 -163.58
REMARK 500 3 GLN A 33 41.17 -103.10
REMARK 500 3 THR A 34 -46.20 -149.99
REMARK 500 3 HIS A 77 36.48 -149.88
REMARK 500 3 ASP A 78 127.19 -170.55
REMARK 500 3 PHE A 106 47.47 -98.15
REMARK 500 3 ASP A 111 -69.56 -130.64
REMARK 500 3 ASP A 135 35.40 -97.96
REMARK 500 4 ILE A 13 30.86 -140.08
REMARK 500 4 GLN A 33 36.03 -97.17
REMARK 500 4 THR A 34 -46.90 -150.07
REMARK 500 4 HIS A 77 33.08 -149.91
REMARK 500 4 PHE A 106 40.29 -102.23
REMARK 500 4 ASP A 108 31.40 -98.61
REMARK 500 4 ASP A 109 77.10 -160.93
REMARK 500 4 ASP A 111 -55.21 -128.86
REMARK 500 4 ASP A 135 30.59 -98.02
REMARK 500 4 SER A 141 97.43 -165.98
REMARK 500 4 ASP A 146 -166.84 -119.48
REMARK 500 5 THR A 34 -45.41 -146.87
REMARK 500 5 ARG A 57 144.70 -177.29
REMARK 500 5 HIS A 64 35.82 -99.69
REMARK 500 5 ASP A 78 136.39 -176.15
REMARK 500 5 ASP A 109 51.39 -157.27
REMARK 500 5 ASP A 135 40.20 -96.80
REMARK 500 5 SER A 141 116.42 -169.72
REMARK 500 5 ASP A 146 -168.66 -101.08
REMARK 500 5 LEU A 151 33.83 -96.35
REMARK 500
REMARK 500 THIS ENTRY HAS 183 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 170
DBREF 1AO8 A 1 162 UNP P00381 DYR_LACCA 1 162
SEQRES 1 A 162 THR ALA PHE LEU TRP ALA GLN ASP ARG ASP GLY LEU ILE
SEQRES 2 A 162 GLY LYS ASP GLY HIS LEU PRO TRP HIS LEU PRO ASP ASP
SEQRES 3 A 162 LEU HIS TYR PHE ARG ALA GLN THR VAL GLY LYS ILE MET
SEQRES 4 A 162 VAL VAL GLY ARG ARG THR TYR GLU SER PHE PRO LYS ARG
SEQRES 5 A 162 PRO LEU PRO GLU ARG THR ASN VAL VAL LEU THR HIS GLN
SEQRES 6 A 162 GLU ASP TYR GLN ALA GLN GLY ALA VAL VAL VAL HIS ASP
SEQRES 7 A 162 VAL ALA ALA VAL PHE ALA TYR ALA LYS GLN HIS PRO ASP
SEQRES 8 A 162 GLN GLU LEU VAL ILE ALA GLY GLY ALA GLN ILE PHE THR
SEQRES 9 A 162 ALA PHE LYS ASP ASP VAL ASP THR LEU LEU VAL THR ARG
SEQRES 10 A 162 LEU ALA GLY SER PHE GLU GLY ASP THR LYS MET ILE PRO
SEQRES 11 A 162 LEU ASN TRP ASP ASP PHE THR LYS VAL SER SER ARG THR
SEQRES 12 A 162 VAL GLU ASP THR ASN PRO ALA LEU THR HIS THR TYR GLU
SEQRES 13 A 162 VAL TRP GLN LYS LYS ALA
HET MTX A 170 54
HETNAM MTX METHOTREXATE
FORMUL 2 MTX C20 H22 N8 O5
HELIX 1 HB PRO A 24 ALA A 32 1 9
HELIX 2 HC ARG A 43 SER A 48 1 6
HELIX 3 HE VAL A 79 GLN A 88 1 10
HELIX 4 HF ALA A 100 ALA A 105 1 6
SHEET 1 S1 8 VAL A 74 VAL A 76 0
SHEET 2 S1 8 THR A 58 LEU A 62 1 N VAL A 61 O VAL A 74
SHEET 3 S1 8 ILE A 38 VAL A 41 1 N MET A 39 O THR A 58
SHEET 4 S1 8 LEU A 94 GLY A 98 1 N VAL A 95 O ILE A 38
SHEET 5 S1 8 ALA A 2 GLN A 7 1 N ALA A 2 O LEU A 94
SHEET 6 S1 8 THR A 112 LEU A 118 1 O THR A 112 N PHE A 3
SHEET 7 S1 8 HIS A 153 LYS A 160 -1 N TRP A 158 O LEU A 113
SHEET 8 S1 8 PHE A 136 VAL A 144 -1 N PHE A 136 O GLN A 159
CISPEP 1 ARG A 52 PRO A 53 1 -0.01
CISPEP 2 GLY A 98 GLY A 99 1 -0.02
CISPEP 3 ARG A 52 PRO A 53 2 -0.32
CISPEP 4 GLY A 98 GLY A 99 2 0.14
CISPEP 5 ARG A 52 PRO A 53 3 -0.20
CISPEP 6 GLY A 98 GLY A 99 3 0.03
CISPEP 7 ARG A 52 PRO A 53 4 -0.33
CISPEP 8 GLY A 98 GLY A 99 4 0.05
CISPEP 9 ARG A 52 PRO A 53 5 -0.18
CISPEP 10 GLY A 98 GLY A 99 5 0.00
CISPEP 11 ARG A 52 PRO A 53 6 -0.23
CISPEP 12 GLY A 98 GLY A 99 6 0.11
CISPEP 13 ARG A 52 PRO A 53 7 -0.33
CISPEP 14 GLY A 98 GLY A 99 7 -0.08
CISPEP 15 ARG A 52 PRO A 53 8 -0.14
CISPEP 16 GLY A 98 GLY A 99 8 0.09
CISPEP 17 ARG A 52 PRO A 53 9 -0.25
CISPEP 18 GLY A 98 GLY A 99 9 -0.05
CISPEP 19 ARG A 52 PRO A 53 10 -0.42
CISPEP 20 GLY A 98 GLY A 99 10 0.04
CISPEP 21 ARG A 52 PRO A 53 11 -0.20
CISPEP 22 GLY A 98 GLY A 99 11 -0.01
CISPEP 23 ARG A 52 PRO A 53 12 -0.04
CISPEP 24 GLY A 98 GLY A 99 12 0.07
CISPEP 25 ARG A 52 PRO A 53 13 -0.17
CISPEP 26 GLY A 98 GLY A 99 13 0.03
CISPEP 27 ARG A 52 PRO A 53 14 -0.32
CISPEP 28 GLY A 98 GLY A 99 14 0.00
CISPEP 29 ARG A 52 PRO A 53 15 -0.27
CISPEP 30 GLY A 98 GLY A 99 15 0.14
CISPEP 31 ARG A 52 PRO A 53 16 -0.24
CISPEP 32 GLY A 98 GLY A 99 16 0.00
CISPEP 33 ARG A 52 PRO A 53 17 -0.33
CISPEP 34 GLY A 98 GLY A 99 17 0.06
CISPEP 35 ARG A 52 PRO A 53 18 -0.42
CISPEP 36 GLY A 98 GLY A 99 18 0.07
CISPEP 37 ARG A 52 PRO A 53 19 -0.14
CISPEP 38 GLY A 98 GLY A 99 19 0.02
CISPEP 39 ARG A 52 PRO A 53 20 -0.43
CISPEP 40 GLY A 98 GLY A 99 20 -0.11
CISPEP 41 ARG A 52 PRO A 53 21 -0.35
CISPEP 42 GLY A 98 GLY A 99 21 0.01
SITE 1 AC1 13 LEU A 4 TRP A 5 ALA A 6 LEU A 19
SITE 2 AC1 13 ASP A 26 LEU A 27 PHE A 30 ARG A 31
SITE 3 AC1 13 SER A 48 PHE A 49 ARG A 57 ALA A 97
SITE 4 AC1 13 THR A 116
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 16 2 Bytes