Header list of 1diu.pdb file
Complete list - b 16 2 Bytes
HEADER OXIDOREDUCTASE 01-AUG-95 1DIU 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 NUMMDL 18 AUTHOR W.D.MORGAN,B.BIRDSALL,V.I.POLSHAKOV,D.SALI,I.KOMPIS,J.FEENEY REVDAT 3 16-FEB-22 1DIU 1 KEYWDS REMARK REVDAT 2 24-FEB-09 1DIU 1 VERSN REVDAT 1 14-NOV-95 1DIU 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 1DIU 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_1000172808. 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 : 18 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 O HIS A 89 CD PRO A 90 0.79 REMARK 500 O HIS A 89 HD3 PRO A 90 0.80 REMARK 500 HD2 PRO A 90 OD1 ASP A 91 1.46 REMARK 500 HD1 HIS A 28 OX5 BDM A 163 1.56 REMARK 500 O LEU A 151 HD1 HIS A 153 1.57 REMARK 500 HH12 ARG A 57 OXW BDM A 163 1.58 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 1 PHE A 3 CG PHE A 3 CD1 0.114 REMARK 500 1 ARG A 9 CG ARG A 9 CD 0.167 REMARK 500 1 ARG A 9 CZ ARG A 9 NH1 0.088 REMARK 500 1 ARG A 9 CZ ARG A 9 NH2 0.093 REMARK 500 1 GLY A 14 CA GLY A 14 C 0.117 REMARK 500 1 ASP A 16 CA ASP A 16 CB 0.150 REMARK 500 1 GLY A 17 N GLY A 17 CA 0.113 REMARK 500 1 HIS A 18 CG HIS A 18 ND1 0.139 REMARK 500 1 HIS A 18 NE2 HIS A 18 CD2 0.199 REMARK 500 1 LEU A 19 C LEU A 19 O -0.130 REMARK 500 1 LEU A 19 C PRO A 20 N 0.217 REMARK 500 1 PRO A 20 N PRO A 20 CA 0.120 REMARK 500 1 PRO A 20 CD PRO A 20 N 0.182 REMARK 500 1 HIS A 22 CG HIS A 22 CD2 0.116 REMARK 500 1 LEU A 23 C LEU A 23 O -0.141 REMARK 500 1 LEU A 23 C PRO A 24 N 0.167 REMARK 500 1 PRO A 24 CD PRO A 24 N 0.305 REMARK 500 1 HIS A 28 CG HIS A 28 CD2 0.054 REMARK 500 1 ARG A 44 CD ARG A 44 NE -0.143 REMARK 500 1 ARG A 44 CZ ARG A 44 NH1 0.123 REMARK 500 1 ARG A 44 CZ ARG A 44 NH2 0.079 REMARK 500 1 TYR A 46 CG TYR A 46 CD1 0.080 REMARK 500 1 PRO A 55 CD PRO A 55 N 0.213 REMARK 500 1 GLU A 56 CB GLU A 56 CG 0.155 REMARK 500 1 GLU A 56 CD GLU A 56 OE1 0.079 REMARK 500 1 HIS A 64 CG HIS A 64 CD2 0.060 REMARK 500 1 HIS A 64 CG HIS A 64 ND1 -0.107 REMARK 500 1 GLN A 65 CD GLN A 65 NE2 0.173 REMARK 500 1 GLU A 66 CB GLU A 66 CG 0.126 REMARK 500 1 GLU A 66 CD GLU A 66 OE2 0.074 REMARK 500 1 ASP A 67 CA ASP A 67 CB 0.335 REMARK 500 1 ASP A 67 CG ASP A 67 OD1 0.249 REMARK 500 1 ASP A 67 CG ASP A 67 OD2 0.224 REMARK 500 1 ASP A 67 C TYR A 68 N 0.142 REMARK 500 1 TYR A 68 CE1 TYR A 68 CZ 0.092 REMARK 500 1 HIS A 77 CA HIS A 77 CB 0.135 REMARK 500 1 HIS A 77 CG HIS A 77 CD2 0.055 REMARK 500 1 ASP A 78 CG ASP A 78 OD2 0.180 REMARK 500 1 ASP A 78 C ASP A 78 O 0.153 REMARK 500 1 TYR A 85 CG TYR A 85 CD2 0.094 REMARK 500 1 LYS A 87 CD LYS A 87 CE 0.181 REMARK 500 1 HIS A 89 C HIS A 89 O 0.343 REMARK 500 1 HIS A 89 C PRO A 90 N -0.373 REMARK 500 1 PRO A 90 N PRO A 90 CA 0.175 REMARK 500 1 PRO A 90 CD PRO A 90 N 1.022 REMARK 500 1 ASP A 91 CA ASP A 91 CB 0.171 REMARK 500 1 GLU A 93 CD GLU A 93 OE1 0.100 REMARK 500 1 GLY A 99 CA GLY A 99 C -0.122 REMARK 500 1 ALA A 105 C ALA A 105 O 0.186 REMARK 500 1 PHE A 106 CZ PHE A 106 CE2 0.143 REMARK 500 REMARK 500 THIS ENTRY HAS 1541 BOND DEVIATIONS. 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 1 THR A 1 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES REMARK 500 1 PHE A 3 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 PHE A 3 CD1 - CG - CD2 ANGL. DEV. = -14.1 DEGREES REMARK 500 1 PHE A 3 CB - CG - CD1 ANGL. DEV. = 9.8 DEGREES REMARK 500 1 PHE A 3 CG - CD2 - CE2 ANGL. DEV. = 21.4 DEGREES REMARK 500 1 PHE A 3 CD1 - CE1 - CZ ANGL. DEV. = 8.8 DEGREES REMARK 500 1 ASP A 8 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 8 CA - C - O ANGL. DEV. = 14.2 DEGREES REMARK 500 1 ARG A 9 CG - CD - NE ANGL. DEV. = -20.3 DEGREES REMARK 500 1 ARG A 9 CD - NE - CZ ANGL. DEV. = 42.1 DEGREES REMARK 500 1 ARG A 9 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES REMARK 500 1 ASP A 10 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 LEU A 12 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES REMARK 500 1 ASP A 16 CB - CG - OD1 ANGL. DEV. = 9.2 DEGREES REMARK 500 1 LEU A 19 CA - C - O ANGL. DEV. = 19.7 DEGREES REMARK 500 1 LEU A 19 CA - C - N ANGL. DEV. = -17.1 DEGREES REMARK 500 1 PRO A 20 C - N - CA ANGL. DEV. = -15.3 DEGREES REMARK 500 1 PRO A 20 C - N - CD ANGL. DEV. = 24.1 DEGREES REMARK 500 1 PRO A 20 CA - N - CD ANGL. DEV. = -9.8 DEGREES REMARK 500 1 PRO A 20 CB - CA - C ANGL. DEV. = -13.7 DEGREES REMARK 500 1 PRO A 20 O - C - N ANGL. DEV. = -10.2 DEGREES REMARK 500 1 TRP A 21 CB - CG - CD2 ANGL. DEV. = -12.7 DEGREES REMARK 500 1 TRP A 21 CB - CG - CD1 ANGL. DEV. = 14.0 DEGREES REMARK 500 1 HIS A 22 CA - C - O ANGL. DEV. = 17.4 DEGREES REMARK 500 1 HIS A 22 CA - C - N ANGL. DEV. = -14.0 DEGREES REMARK 500 1 LEU A 23 CA - C - O ANGL. DEV. = 14.3 DEGREES REMARK 500 1 LEU A 23 CA - C - N ANGL. DEV. = -19.2 DEGREES REMARK 500 1 PRO A 24 C - N - CA ANGL. DEV. = -12.1 DEGREES REMARK 500 1 PRO A 24 C - N - CD ANGL. DEV. = 25.5 DEGREES REMARK 500 1 PRO A 24 CA - N - CD ANGL. DEV. = -13.1 DEGREES REMARK 500 1 PRO A 24 CA - C - N ANGL. DEV. = 15.6 DEGREES REMARK 500 1 ASP A 25 OD1 - CG - OD2 ANGL. DEV. = -15.7 DEGREES REMARK 500 1 ASP A 25 CB - CG - OD1 ANGL. DEV. = 14.4 DEGREES REMARK 500 1 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 LYS A 37 CD - CE - NZ ANGL. DEV. = 17.5 DEGREES REMARK 500 1 ARG A 43 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES REMARK 500 1 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 1 ARG A 44 N - CA - CB ANGL. DEV. = -18.3 DEGREES REMARK 500 1 ARG A 44 CG - CD - NE ANGL. DEV. = 22.7 DEGREES REMARK 500 1 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES REMARK 500 1 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -10.7 DEGREES REMARK 500 1 ARG A 44 O - C - N ANGL. DEV. = -10.1 DEGREES REMARK 500 1 THR A 45 CA - CB - OG1 ANGL. DEV. = -14.7 DEGREES REMARK 500 1 TYR A 46 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 1 TYR A 46 CG - CD2 - CE2 ANGL. DEV. = -6.2 DEGREES REMARK 500 1 TYR A 46 O - C - N ANGL. DEV. = -9.6 DEGREES REMARK 500 1 GLU A 47 CA - CB - CG ANGL. DEV. = -15.1 DEGREES REMARK 500 1 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 PRO A 55 CA - N - CD ANGL. DEV. = -11.4 DEGREES REMARK 500 1 GLU A 56 OE1 - CD - OE2 ANGL. DEV. = 36.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 4050 ANGLE DEVIATIONS. 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 HIS A 89 -113.71 -100.97 REMARK 500 1 PRO A 90 -67.47 132.53 REMARK 500 2 HIS A 89 -113.71 -100.97 REMARK 500 2 PRO A 90 -67.47 132.53 REMARK 500 3 HIS A 89 -113.71 -100.97 REMARK 500 3 PRO A 90 -67.47 132.53 REMARK 500 4 HIS A 89 -113.71 -100.97 REMARK 500 4 PRO A 90 -67.47 132.53 REMARK 500 5 HIS A 89 -113.71 -100.97 REMARK 500 5 PRO A 90 -67.47 132.53 REMARK 500 6 HIS A 89 -113.71 -100.97 REMARK 500 6 PRO A 90 -67.47 132.53 REMARK 500 7 HIS A 89 -113.71 -100.97 REMARK 500 7 PRO A 90 -67.47 132.53 REMARK 500 8 HIS A 89 -113.71 -100.97 REMARK 500 8 PRO A 90 -67.47 132.53 REMARK 500 9 THR A 34 71.48 -110.60 REMARK 500 9 HIS A 89 -113.71 -100.97 REMARK 500 9 PRO A 90 -67.47 132.53 REMARK 500 10 HIS A 89 -113.71 -100.97 REMARK 500 10 PRO A 90 -67.47 132.53 REMARK 500 11 HIS A 89 -113.71 -100.97 REMARK 500 11 PRO A 90 -67.47 132.53 REMARK 500 12 THR A 34 62.58 -118.57 REMARK 500 12 HIS A 89 -113.71 -100.97 REMARK 500 12 PRO A 90 -67.47 132.53 REMARK 500 13 HIS A 89 -113.71 -100.97 REMARK 500 13 PRO A 90 -67.47 132.53 REMARK 500 14 HIS A 89 -113.71 -100.97 REMARK 500 14 PRO A 90 -67.47 132.53 REMARK 500 15 HIS A 89 -113.71 -100.97 REMARK 500 15 PRO A 90 -67.47 132.53 REMARK 500 16 HIS A 89 -113.71 -100.97 REMARK 500 16 PRO A 90 -67.47 132.53 REMARK 500 17 HIS A 89 -113.71 -100.97 REMARK 500 17 PRO A 90 -67.47 132.53 REMARK 500 18 HIS A 89 -113.71 -100.97 REMARK 500 18 PRO A 90 -67.47 132.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR A 34 VAL A 35 3 143.95 REMARK 500 THR A 34 VAL A 35 7 137.20 REMARK 500 THR A 34 VAL A 35 9 135.63 REMARK 500 THR A 34 VAL A 35 12 143.15 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 9 0.07 SIDE CHAIN REMARK 500 1 ARG A 44 0.09 SIDE CHAIN REMARK 500 2 ARG A 9 0.07 SIDE CHAIN REMARK 500 2 ARG A 44 0.09 SIDE CHAIN REMARK 500 3 ARG A 9 0.07 SIDE CHAIN REMARK 500 3 ARG A 44 0.09 SIDE CHAIN REMARK 500 4 ARG A 9 0.07 SIDE CHAIN REMARK 500 4 ARG A 44 0.09 SIDE CHAIN REMARK 500 5 ARG A 9 0.07 SIDE CHAIN REMARK 500 5 ARG A 44 0.09 SIDE CHAIN REMARK 500 6 ARG A 9 0.07 SIDE CHAIN REMARK 500 6 ARG A 44 0.09 SIDE CHAIN REMARK 500 7 ARG A 9 0.07 SIDE CHAIN REMARK 500 7 ARG A 44 0.09 SIDE CHAIN REMARK 500 8 ARG A 9 0.07 SIDE CHAIN REMARK 500 8 ARG A 44 0.09 SIDE CHAIN REMARK 500 9 ARG A 9 0.07 SIDE CHAIN REMARK 500 9 ARG A 44 0.09 SIDE CHAIN REMARK 500 10 ARG A 9 0.07 SIDE CHAIN REMARK 500 10 ARG A 44 0.09 SIDE CHAIN REMARK 500 11 ARG A 9 0.07 SIDE CHAIN REMARK 500 11 ARG A 44 0.09 SIDE CHAIN REMARK 500 12 ARG A 9 0.07 SIDE CHAIN REMARK 500 12 ARG A 44 0.09 SIDE CHAIN REMARK 500 12 ARG A 57 0.07 SIDE CHAIN REMARK 500 13 ARG A 9 0.07 SIDE CHAIN REMARK 500 13 ARG A 44 0.09 SIDE CHAIN REMARK 500 14 ARG A 9 0.07 SIDE CHAIN REMARK 500 14 ARG A 44 0.09 SIDE CHAIN REMARK 500 15 ARG A 9 0.07 SIDE CHAIN REMARK 500 15 ARG A 44 0.09 SIDE CHAIN REMARK 500 16 ARG A 9 0.07 SIDE CHAIN REMARK 500 16 ARG A 44 0.09 SIDE CHAIN REMARK 500 17 ARG A 9 0.07 SIDE CHAIN REMARK 500 17 ARG A 44 0.09 SIDE CHAIN REMARK 500 17 ARG A 57 0.08 SIDE CHAIN REMARK 500 18 ARG A 9 0.07 SIDE CHAIN REMARK 500 18 ARG A 44 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 1 TRP A 21 -11.24 REMARK 500 1 ASP A 78 -12.18 REMARK 500 1 GLU A 145 10.90 REMARK 500 2 TRP A 21 -11.24 REMARK 500 2 ASP A 78 -12.18 REMARK 500 2 GLU A 145 10.90 REMARK 500 3 TRP A 21 -11.24 REMARK 500 3 ASP A 78 -12.18 REMARK 500 3 GLU A 145 10.90 REMARK 500 4 TRP A 21 -11.24 REMARK 500 4 ASP A 25 10.07 REMARK 500 4 ASP A 78 -12.18 REMARK 500 4 GLU A 145 10.90 REMARK 500 5 TRP A 21 -11.24 REMARK 500 5 ASP A 78 -12.18 REMARK 500 5 GLU A 145 10.90 REMARK 500 6 TRP A 21 -11.24 REMARK 500 6 ASP A 25 10.26 REMARK 500 6 ASP A 78 -12.18 REMARK 500 6 GLU A 145 10.90 REMARK 500 7 TRP A 21 -11.24 REMARK 500 7 ASP A 78 -12.18 REMARK 500 7 GLU A 145 10.90 REMARK 500 8 TRP A 21 -11.24 REMARK 500 8 ASP A 78 -12.18 REMARK 500 8 GLU A 145 10.90 REMARK 500 9 TRP A 21 -11.24 REMARK 500 9 ASP A 78 -12.18 REMARK 500 9 GLU A 145 10.90 REMARK 500 10 TRP A 21 -11.24 REMARK 500 10 ASP A 78 -12.18 REMARK 500 10 GLU A 145 10.90 REMARK 500 11 TRP A 21 -11.24 REMARK 500 11 ASP A 78 -12.18 REMARK 500 11 GLU A 145 10.90 REMARK 500 12 TRP A 21 -11.24 REMARK 500 12 ASP A 78 -12.18 REMARK 500 12 GLU A 145 10.90 REMARK 500 13 TRP A 21 -11.24 REMARK 500 13 ASP A 78 -12.18 REMARK 500 13 GLU A 145 10.90 REMARK 500 14 TRP A 21 -11.24 REMARK 500 14 ASP A 25 10.24 REMARK 500 14 ASP A 78 -12.18 REMARK 500 14 GLU A 145 10.90 REMARK 500 15 TRP A 21 -11.24 REMARK 500 15 ASP A 78 -12.18 REMARK 500 15 GLU A 145 10.90 REMARK 500 16 TRP A 21 -11.24 REMARK 500 16 ASP A 78 -12.18 REMARK 500 REMARK 500 THIS ENTRY HAS 57 MAIN CHAIN PLANARITY DEVIATIONS. 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: 1DIS RELATED DB: PDB DBREF 1DIU 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 1 2.74 CISPEP 2 GLY A 98 GLY A 99 1 2.29 CISPEP 3 ARG A 52 PRO A 53 2 2.39 CISPEP 4 GLY A 98 GLY A 99 2 2.29 CISPEP 5 ARG A 52 PRO A 53 3 2.38 CISPEP 6 GLY A 98 GLY A 99 3 2.29 CISPEP 7 ARG A 52 PRO A 53 4 2.44 CISPEP 8 GLY A 98 GLY A 99 4 2.29 CISPEP 9 ARG A 52 PRO A 53 5 1.83 CISPEP 10 GLY A 98 GLY A 99 5 2.29 CISPEP 11 ARG A 52 PRO A 53 6 2.05 CISPEP 12 GLY A 98 GLY A 99 6 2.29 CISPEP 13 ARG A 52 PRO A 53 7 2.02 CISPEP 14 GLY A 98 GLY A 99 7 2.29 CISPEP 15 ARG A 52 PRO A 53 8 2.38 CISPEP 16 GLY A 98 GLY A 99 8 2.29 CISPEP 17 ARG A 52 PRO A 53 9 2.11 CISPEP 18 GLY A 98 GLY A 99 9 2.29 CISPEP 19 ARG A 52 PRO A 53 10 2.40 CISPEP 20 GLY A 98 GLY A 99 10 2.29 CISPEP 21 ARG A 52 PRO A 53 11 2.47 CISPEP 22 GLY A 98 GLY A 99 11 2.29 CISPEP 23 ARG A 52 PRO A 53 12 2.27 CISPEP 24 GLY A 98 GLY A 99 12 2.29 CISPEP 25 ARG A 52 PRO A 53 13 1.71 CISPEP 26 GLY A 98 GLY A 99 13 2.29 CISPEP 27 ARG A 52 PRO A 53 14 2.17 CISPEP 28 GLY A 98 GLY A 99 14 2.29 CISPEP 29 ARG A 52 PRO A 53 15 2.45 CISPEP 30 GLY A 98 GLY A 99 15 2.29 CISPEP 31 ARG A 52 PRO A 53 16 2.32 CISPEP 32 GLY A 98 GLY A 99 16 2.29 CISPEP 33 ARG A 52 PRO A 53 17 2.25 CISPEP 34 GLY A 98 GLY A 99 17 2.29 CISPEP 35 ARG A 52 PRO A 53 18 2.14 CISPEP 36 GLY A 98 GLY A 99 18 2.29 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 LEU A 54 ARG A 57 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