Header list of 1dis.pdb file
Complete list - 16 20 Bytes
HEADER OXIDOREDUCTASE 01-AUG-95 1DIS
TITLE DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH BRODIMOPRIM-4,6-
TITLE 2 DICARBOXYLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;
SOURCE 3 ORGANISM_TAXID: 1582;
SOURCE 4 STRAIN: METHOTREXATE-RESISTANT;
SOURCE 5 GENE: POTENTIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR-ENZYME COMPLEX, OXIDO-REDUCTASE, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
AUTHOR W.D.MORGAN,B.BIRDSALL,V.I.POLSHAKOV,D.SALI,I.KOMPIS,J.FEENEY
REVDAT 3 16-FEB-22 1DIS 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1DIS 1 VERSN
REVDAT 1 14-NOV-95 1DIS 0
JRNL AUTH W.D.MORGAN,B.BIRDSALL,V.I.POLSHAKOV,D.SALI,I.KOMPIS,J.FEENEY
JRNL TITL SOLUTION STRUCTURE OF A BRODIMOPRIM ANALOGUE IN ITS COMPLEX
JRNL TITL 2 WITH LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE.
JRNL REF BIOCHEMISTRY V. 34 11690 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7547901
JRNL DOI 10.1021/BI00037A006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.MARTORELL,M.J.GRADWELL,B.BIRDSALL,C.J.BAUER,T.A.FRENKIEL,
REMARK 1 AUTH 2 H.T.A.CHEUNG,V.I.POLSHAKOV,L.KUYPER,J.FEENEY
REMARK 1 TITL SOLUTION STRUCTURE OF BOUND TRIMETHOPRIM IN ITS COMPLEX WITH
REMARK 1 TITL 2 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE
REMARK 1 REF BIOCHEMISTRY V. 33 12416 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.BIRDSALL,J.FEENEY,C.PASCUAL,G.C.K.ROBERTS,I.KOMPIS,
REMARK 1 AUTH 2 R.L.THEN,K.MUELLER,A.KROEHN
REMARK 1 TITL A 1H NMR STUDY OF THE INTERACTIONS AND CONFORMATIONS OF
REMARK 1 TITL 2 RATIONALLY DESIGNED BRODIMOPRIM ANALOGUES IN COMPLEXES WITH
REMARK 1 TITL 3 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE
REMARK 1 REF J.MED.CHEM. V. 27 1672 1984
REMARK 1 REFN ISSN 0022-2623
REMARK 1 REFERENCE 3
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 ANGSTROMS
REMARK 1 TITL 3 RESOLUTION. 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 : DISCOVER
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DIS 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_1000172806.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : 1
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 HD2 PHE A 30 H152 BDM A 163 1.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 18 CG HIS A 18 CD2 0.056
REMARK 500 HIS A 22 CG HIS A 22 CD2 0.055
REMARK 500 HIS A 28 CG HIS A 28 CD2 0.056
REMARK 500 HIS A 64 CG HIS A 64 CD2 0.055
REMARK 500 HIS A 77 CG HIS A 77 CD2 0.056
REMARK 500 HIS A 89 CG HIS A 89 CD2 0.055
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 HIS A 18 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 HIS A 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 HIS A 28 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 HIS A 64 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 HIS A 77 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 HIS A 89 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
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 GLU A 56 -0.71 73.75
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 BDM A 163
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DIU RELATED DB: PDB
DBREF 1DIS 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 BDM A 163 55
HETNAM BDM BRODIMOPRIM-4,6-DICARBOXYLATE
FORMUL 2 BDM C20 H24 BR N4 O6 1-
HELIX 1 HB PRO A 24 GLN A 33 1 10
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 GLY A 99 PHE A 106 1 8
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 GLY A 42 1 N MET A 39 O THR A 58
SHEET 4 S1 8 LEU A 94 ILE A 96 1 N VAL A 95 O ILE A 38
SHEET 5 S1 8 THR A 1 GLN A 7 1 N ALA A 2 O LEU A 94
SHEET 6 S1 8 THR A 112 LEU A 118 1 N THR A 112 O THR A 1
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 0 -16.45
CISPEP 2 GLY A 98 GLY A 99 0 7.98
SITE 1 AC1 14 LEU A 4 TRP A 5 ALA A 6 LEU A 19
SITE 2 AC1 14 ASP A 26 LEU A 27 HIS A 28 PHE A 30
SITE 3 AC1 14 ARG A 31 SER A 48 PHE A 49 PRO A 50
SITE 4 AC1 14 ARG A 57 ALA 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
Complete list - 16 20 Bytes