HEADER DEOXYRIBONUCLEIC ACID 18-AUG-88 DDB011 TITLE THE STRUCTURE OF A PSEUDO INTERCALATED COMPLEX BETWEEN TITLE 2 ACTINOMYCIN AND THE DNA BINDING SEQUENCE D(GPC) COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'-D(*GP*C)-3'); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1 KEYWDS U-DNA, SINGLE STRAND, OPEN, COMPLEXED WITH DRUG EXPDTA X-RAY DIFFRACTION AUTHOR F.TAKUSAGAWA,M.DABROW,S.NEIDLE,H.M.BERMAN REVDAT 2 21-SEP-01 5 REVDAT 1 18-AUG-88 0 JRNL AUTH F.TAKUSAGAWA,M.DABROW,S.NEIDLE,H.M.BERMAN JRNL TITL THE STRUCTURE OF A PSEUDO INTERCALATED COMPLEX JRNL TITL 2 BETWEEN ACTINOMYCIN AND THE DNA BINDING SEQUENCE JRNL TITL 3 D(GPC) JRNL REF NATURE V. 296 466 1982 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH F.TAKUSAGAWA,H.M.BERMAN REMARK 1 TITL SOME NEW ASPECTS OF ACTINOMYCIN D-NUCLEIC ACID REMARK 1 TITL 2 BINDING REMARK 1 REF COLD SPRING HARBOR SYMP. V. 47 315 1983 REMARK 1 REF 2 QUANT.BIOL. REMARK 1 REFN ASTM CSHSAZ US ISSN 0091-7451 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 967 REMARK 3 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.150 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 0 REMARK 3 NUCLEIC ACID ATOMS : 38 REMARK 3 HETEROGEN ATOMS : 47 REMARK 3 SOLVENT ATOMS : 84 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: TRANSLATION FOR G-C FOR REMARK 3 SYMMETRY 1) 0,0,0 TRANSLATION FOR G-C FOR SYMMETRY 2) 1, REMARK 3 0,-1 TRANSLATION FOR AMD FOR SYMMETRY 1) 0,0,0 REMARK 3 TRANSLATION FOR AMD FOR SYMMETRY 5) 0,0,1 REMARK 4 REMARK 4 NULL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 105 REMARK 105 THE PROTEIN DATA BANK HAS ADOPTED THE SACCHARIDE CHEMISTS REMARK 105 NOMENCLATURE FOR ATOMS OF THE DEOXYRIBOSE/RIBOSE MOIETY REMARK 105 RATHER THAN THAT OF THE NUCLEOSIDE CHEMISTS. THE RING REMARK 105 OXYGEN ATOM IS LABELLED O4* INSTEAD OF O1*. REMARK 106 REMARK 106 ALL HYDROGEN BONDS BETWEEN BASE PAIRS NOT MENTIONED IN REMARK 106 REMARKS 102 AND 103 FOLLOW THE CONVENTIONAL WATSON-CRICK REMARK 106 HYDROGEN BONDING PATTERN. THEY HAVE NOT BEEN PRESENTED ON REMARK 106 *CONECT* RECORDS IN THIS ENTRY. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 273.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : DIFFRACTOMETER REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 1668 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,-X+Y,2/3-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.46667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.73333 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 18.73333 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.46667 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 16.57700 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -18.73333 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 74.93333 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 O5 PXZ B 3 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 14 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O HOH A 39 O HOH B 69 1.08 REMARK 500 O HOH A 40 O HOH B 73 1.13 REMARK 500 O HOH A 38 O HOH B 64 1.16 REMARK 500 O HOH A 47 O HOH B 83 1.17 REMARK 500 O HOH A 36 O HOH B 76 1.24 REMARK 500 C SAR B 7 N MVA B 8 1.28 REMARK 500 O HOH A 19 O HOH B 83 1.30 REMARK 500 C DTH A 4 N DVA B 5 1.32 REMARK 500 C MVA B 8 OG1 DTH A 4 1.33 REMARK 500 C DVA B 5 N DPR B 6 1.35 REMARK 500 N SAR B 7 C DPR B 6 1.36 REMARK 500 C PXZ B 3 N DTH A 4 1.36 REMARK 500 O HOH A 11 O HOH B 56 1.49 REMARK 500 O HOH B 49 O HOH B 64 1.53 REMARK 500 O HOH A 23 O HOH B 75 1.60 REMARK 500 O1P C A 2 O HOH A 10 1.62 REMARK 500 O HOH A 41 O HOH B 52 1.69 REMARK 500 O HOH A 40 O HOH B 75 1.69 REMARK 500 O HOH A 26 O HOH B 68 1.70 REMARK 500 O HOH A 34 O HOH B 52 1.72 REMARK 500 O HOH B 73 O HOH B 80 1.73 REMARK 500 O HOH A 45 O HOH B 70 1.76 REMARK 500 O HOH A 34 O HOH A 43 1.77 REMARK 500 O HOH A 12 O HOH B 73 1.78 REMARK 500 O DPR B 6 O HOH B 67 1.87 REMARK 500 O HOH B 55 O HOH B 57 1.87 REMARK 500 O5* C A 2 O HOH A 10 1.87 REMARK 500 P C A 2 O HOH A 10 1.87 REMARK 500 O HOH A 43 O HOH B 80 1.90 REMARK 500 O HOH A 46 O HOH B 56 1.91 REMARK 500 O HOH A 28 O HOH B 81 1.93 REMARK 500 O HOH A 28 O HOH A 33 1.94 REMARK 500 O HOH A 22 O HOH B 52 1.94 REMARK 500 O HOH A 45 O HOH B 63 1.96 REMARK 500 O HOH A 23 O HOH A 40 1.96 REMARK 500 O HOH A 39 O HOH B 73 2.00 REMARK 500 O HOH B 59 O HOH B 66 2.02 REMARK 500 O2P C A 2 O HOH B 74 2.04 REMARK 500 O HOH A 33 O HOH B 50 2.11 REMARK 500 O HOH A 44 O HOH B 74 2.12 REMARK 500 O HOH A 28 O HOH B 71 2.13 REMARK 500 O HOH A 43 O HOH B 73 2.14 REMARK 500 O HOH A 17 O HOH A 43 2.15 REMARK 500 O HOH A 46 O HOH B 65 2.16 REMARK 500 O HOH A 23 O HOH A 41 2.16 REMARK 500 O HOH A 26 O HOH B 51 2.16 REMARK 500 O HOH A 40 O HOH B 53 2.17 REMARK 500 O HOH B 53 O HOH B 73 2.17 REMARK 500 O HOH A 36 O HOH A 43 2.19 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 12 O HOH A 30 6666 1.26 REMARK 500 O HOH A 48 O HOH B 50 2554 1.35 REMARK 500 N10 PXZ B 3 C11 PXZ B 3 5556 1.35 REMARK 500 O5 PXZ B 3 C12 PXZ B 3 5556 1.38 REMARK 500 O HOH A 26 O HOH B 74 6656 1.47 REMARK 500 O HOH A 26 O HOH B 80 6656 1.60 REMARK 500 O HOH A 41 O HOH B 49 6666 1.64 REMARK 500 O HOH A 18 O HOH B 79 4556 1.70 REMARK 500 O HOH B 71 O HOH A 27 3555 1.70 REMARK 500 O HOH B 63 O HOH A 48 3555 1.73 REMARK 500 O HOH A 17 O HOH B 51 6666 1.74 REMARK 500 O HOH A 24 O HOH B 63 6656 1.75 REMARK 500 O HOH A 10 O HOH A 31 6656 1.77 REMARK 500 O HOH A 30 O HOH B 73 6656 1.80 REMARK 500 C15 PXZ B 3 O HOH B 82 1655 1.81 REMARK 500 O HOH A 20 O HOH B 68 6666 1.86 REMARK 500 O HOH A 24 O HOH A 44 6656 1.86 REMARK 500 C4* G A 1 O HOH A 37 5666 1.88 REMARK 500 O HOH A 15 O HOH A 20 6656 1.89 REMARK 500 O HOH A 30 O HOH A 34 6656 1.89 REMARK 500 O HOH A 19 O HOH B 71 2554 1.98 REMARK 500 O HOH A 27 O HOH B 77 5556 1.98 REMARK 500 O HOH A 42 O HOH B 80 6656 1.99 REMARK 500 O HOH A 27 O HOH B 54 4556 2.01 REMARK 500 O HOH A 34 O HOH B 56 6666 2.01 REMARK 500 O HOH A 19 O HOH B 81 2554 2.03 REMARK 500 C5* G A 1 O HOH B 85 6656 2.04 REMARK 500 O5* G A 1 O HOH A 37 5666 2.06 REMARK 500 O HOH A 30 O HOH A 41 6656 2.06 REMARK 500 O HOH A 18 O HOH B 54 4556 2.09 REMARK 500 O HOH A 29 O HOH B 60 6656 2.09 REMARK 500 O HOH A 47 O HOH A 28 2554 2.10 REMARK 500 O HOH A 31 O HOH B 68 6666 2.11 REMARK 500 O HOH B 83 O HOH A 28 2554 2.12 REMARK 500 O HOH A 22 O HOH B 56 6666 2.13 REMARK 500 O HOH A 30 O HOH A 40 6656 2.15 REMARK 500 O HOH A 30 O HOH B 52 6656 2.15 REMARK 500 O HOH B 62 O HOH A 19 3555 2.17 REMARK 500 O HOH A 46 O HOH B 76 6656 2.19 SEQRES 1 A 2 G C FTNOTE 1 THESE ATOMS ARE THE AMINO ACID RESIDUES OF ACTINOMYCIN D. HET PXZ B 3 13 HET SAR B 7 5 HET MVA B 8 8 HETNAM PXZ 2-AMINO-1,9-DICARBONYL-4,6-DIMETHYL-10-DEHYDRO- HETNAM 2 PXZ PHENOXAZIN-3-ONE HETNAM SAR SARCOSINE HETNAM MVA N-METHYLVALINE HETNAM THR THREONINE HETNAM VAL VALINE HETNAM PRO PROLINE HETSYN PXZ PHENOXAZINE FORMUL 2 PXZ C16 H12 N2 O4 FORMUL 3 SAR C3 H7 N1 O2 FORMUL 4 MVA C6 H13 N1 O2 FORMUL 5 THR C4 H9 N1 O3 FORMUL 6 VAL C5 H11 N1 O2 FORMUL 7 PRO C5 H10 N1 O2 FORMUL 8 HOH *84(H2 O1) CRYST1 16.577 16.577 56.200 90.00 90.00 120.00 P 32 2 1 6 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 0.060325 0.034828 0.000000 0.00000 SCALE2 0.000000 0.069657 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017794 0.00000 ATOM 1 O5* G A 1 10.371 7.160 43.621 1.00 34.69 O ATOM 2 C5* G A 1 9.853 5.988 43.017 1.00 23.89 C ATOM 3 C4* G A 1 8.369 5.805 43.004 1.00 11.53 C ATOM 4 O4* G A 1 8.272 5.535 41.565 1.00 22.41 O ATOM 5 C3* G A 1 7.970 4.530 43.678 1.00 26.16 C ATOM 6 O3* G A 1 6.578 4.411 43.847 1.00 30.05 O ATOM 7 C2* G A 1 8.499 3.499 42.614 1.00 26.54 C ATOM 8 C1* G A 1 8.281 4.135 41.367 1.00 13.95 C ATOM 9 N9 G A 1 9.438 3.668 40.495 1.00 14.15 N ATOM 10 C8 G A 1 10.775 3.929 40.752 1.00 15.16 C ATOM 11 N7 G A 1 11.557 3.733 39.732 1.00 18.35 N ATOM 12 C5 G A 1 10.700 3.424 38.681 1.00 12.47 C ATOM 13 C6 G A 1 10.965 3.347 37.280 1.00 12.61 C ATOM 14 O6 G A 1 12.022 3.337 36.695 1.00 17.67 O ATOM 15 N1 G A 1 9.767 3.203 36.573 1.00 14.13 N ATOM 16 C2 G A 1 8.502 3.113 37.113 1.00 17.87 C ATOM 17 N2 G A 1 7.512 2.933 36.244 1.00 16.24 N ATOM 18 N3 G A 1 8.245 3.445 38.385 1.00 18.89 N ATOM 19 C4 G A 1 9.393 3.546 39.107 1.00 7.93 C ATOM 20 P C A 2 5.931 3.846 45.215 1.00 26.90 P ATOM 21 O1P C A 2 6.427 2.454 45.437 1.00 19.30 O ATOM 22 O2P C A 2 4.469 3.991 45.161 1.00 22.73 O ATOM 23 O5* C A 2 6.556 4.776 46.317 1.00 24.09 O ATOM 24 C5* C A 2 6.034 6.087 46.488 1.00 19.98 C ATOM 25 C4* C A 2 6.788 6.782 47.553 1.00 25.11 C ATOM 26 O4* C A 2 6.214 6.634 48.875 1.00 26.71 O ATOM 27 C3* C A 2 8.187 6.250 47.603 1.00 34.31 C ATOM 28 O3* C A 2 9.101 7.266 48.035 1.00 26.59 O ATOM 29 C2* C A 2 7.893 5.052 48.529 1.00 28.98 C ATOM 30 C1* C A 2 7.029 5.770 49.513 1.00 21.68 C ATOM 31 N1 C A 2 6.228 4.915 50.361 1.00 19.32 N ATOM 32 C2 C A 2 6.522 4.916 51.714 1.00 17.52 C ATOM 33 O2 C A 2 7.352 5.732 52.127 1.00 19.24 O ATOM 34 N3 C A 2 5.864 4.029 52.497 1.00 16.73 N ATOM 35 C4 C A 2 5.266 2.942 51.976 1.00 9.98 C ATOM 36 N4 C A 2 4.854 1.988 52.771 1.00 23.18 N ATOM 37 C5 C A 2 4.923 2.915 50.581 1.00 17.32 C ATOM 38 C6 C A 2 5.367 3.970 49.844 1.00 12.37 C TER 39 C A 2 HETATM 40 C1 PXZ B 3 8.278 0.209 39.831 1.00 16.81 C HETATM 41 C PXZ B 3 6.805 0.228 39.899 1.00 16.23 C HETATM 42 O PXZ B 3 6.170 -0.587 40.580 1.00 27.27 O HETATM 43 C2 PXZ B 3 8.989 0.033 40.998 1.00 17.01 C HETATM 44 N2 PXZ B 3 8.273 0.233 42.262 0.50 12.49 N HETATM 45 C3 PXZ B 3 10.393 0.235 40.985 1.00 13.52 C HETATM 46 O3 PXZ B 3 10.994 0.198 42.094 0.50 20.80 O HETATM 47 C4 PXZ B 3 11.122 0.308 39.778 1.00 19.12 C HETATM 48 O5 PXZ B 3 11.109 0.000 37.467 0.50 9.98 O HETATM 49 N10 PXZ B 3 8.268 0.000 37.467 0.50 18.19 N HETATM 50 C11 PXZ B 3 8.990 0.125 38.604 1.00 11.81 C HETATM 51 C12 PXZ B 3 10.388 0.267 38.613 1.00 12.75 C HETATM 52 C15 PXZ B 3 12.659 0.157 39.767 1.00 19.36 C HETATM 53 N SAR B 7 3.204 5.962 35.695 1.00 22.17 N HETATM 54 CA SAR B 7 4.456 5.952 36.406 1.00 21.30 C HETATM 55 C SAR B 7 4.150 5.649 37.948 1.00 11.71 C HETATM 56 O SAR B 7 2.968 5.635 38.345 1.00 16.21 O HETATM 57 CN SAR B 7 2.468 7.269 35.720 1.00 19.13 C HETATM 58 N MVA B 8 5.093 6.040 38.725 1.00 13.91 N HETATM 59 CN MVA B 8 6.466 6.181 38.288 1.00 23.58 C HETATM 60 CA MVA B 8 4.963 5.987 40.213 1.00 14.98 C HETATM 61 CB MVA B 8 4.478 7.400 40.778 1.00 24.83 C HETATM 62 CG1 MVA B 8 5.289 8.423 39.958 1.00 23.96 C HETATM 63 CG2 MVA B 8 3.021 7.503 40.517 1.00 48.88 C HETATM 64 C MVA B 8 4.687 4.698 40.807 1.00 20.36 C HETATM 65 O MVA B 8 3.578 4.745 41.369 1.00 33.02 O HETATM 66 N DTH A 4 6.195 1.324 39.385 1.00 14.64 N HETATM 67 CA DTH A 4 4.723 1.375 39.394 1.00 11.41 C HETATM 68 C DTH A 4 4.218 1.734 38.036 1.00 15.50 C HETATM 69 O DTH A 4 4.977 2.323 37.220 1.00 23.47 O HETATM 70 CB DTH A 4 4.169 2.416 40.376 1.00 10.15 C HETATM 71 OG1 DTH A 4 5.114 3.531 40.320 1.00 26.42 O HETATM 72 CG2 DTH A 4 4.215 1.941 41.863 1.00 18.46 C HETATM 73 N DVA B 5 2.919 1.617 37.826 1.00 18.34 N HETATM 74 CA DVA B 5 2.026 2.261 36.864 1.00 30.18 C HETATM 75 C DVA B 5 2.351 1.684 35.471 1.00 17.97 C HETATM 76 O DVA B 5 1.930 0.512 35.258 1.00 16.57 O HETATM 77 CB DVA B 5 0.606 2.097 37.468 1.00 24.94 C HETATM 78 CG1 DVA B 5 -0.365 2.694 36.446 1.00 25.15 C HETATM 79 CG2 DVA B 5 0.409 2.752 38.840 1.00 51.54 C HETATM 80 N DPR B 6 2.779 2.523 34.502 1.00 14.67 N HETATM 81 CA DPR B 6 3.448 3.772 34.719 1.00 28.50 C HETATM 82 C DPR B 6 2.824 5.063 34.755 1.00 17.90 C HETATM 83 O DPR B 6 1.619 5.044 34.378 1.00 19.91 O HETATM 84 CB DPR B 6 4.477 3.853 33.559 1.00 16.41 C HETATM 85 CG DPR B 6 3.661 3.123 32.395 1.00 14.33 C HETATM 86 CD DPR B 6 2.960 1.981 33.088 1.00 11.81 C HETATM 87 O HOH A 9 5.897 0.155 43.819 1.00 23.65 O HETATM 88 O HOH A 10 7.694 3.426 45.694 0.50 27.90 O HETATM 89 O HOH A 11 9.683 4.850 52.672 1.00 27.95 O HETATM 90 O HOH A 12 0.819 4.091 41.396 0.50 29.77 O HETATM 91 O HOH A 13 -2.919 4.887 28.851 1.00 37.65 O HETATM 92 O HOH A 14 -2.337 0.000 37.466 0.50 48.69 O HETATM 93 O HOH A 15 7.387 1.557 47.792 1.00 42.24 O HETATM 94 O HOH A 16 -4.198 8.084 44.892 0.50 31.96 O HETATM 95 O HOH A 17 -0.603 3.635 46.204 1.00 32.87 O HETATM 96 O HOH A 18 -0.304 5.066 30.616 1.00 28.85 O HETATM 97 O HOH A 19 -1.471 0.944 32.237 1.00 30.46 O HETATM 98 O HOH A 20 1.888 8.234 44.667 1.00 36.22 O HETATM 99 O HOH A 21 3.822 0.127 30.079 1.00 33.28 O HETATM 100 O HOH A 22 -3.249 6.900 42.247 1.00 34.35 O HETATM 101 O HOH A 23 -2.379 2.803 41.537 0.50 29.23 O HETATM 102 O HOH A 24 9.790 0.371 45.161 1.00 40.01 O HETATM 103 O HOH A 25 -3.341 5.135 38.053 0.50 32.41 O HETATM 104 O HOH A 26 11.272 0.903 48.703 1.00 44.67 O HETATM 105 O HOH A 27 0.327 1.575 29.151 1.00 34.62 O HETATM 106 O HOH A 28 2.189 1.064 48.033 1.00 33.04 O HETATM 107 O HOH A 29 10.700 4.322 46.420 1.00 34.94 O HETATM 108 O HOH A 30 12.483 2.541 51.939 1.00 27.59 O HETATM 109 O HOH A 31 1.686 7.755 47.365 1.00 28.87 O HETATM 110 O HOH A 32 -4.843 5.084 44.310 0.50 26.71 O HETATM 111 O HOH A 33 3.290 1.341 46.457 1.00 34.57 O HETATM 112 O HOH A 34 -1.402 5.589 42.919 1.00 35.19 O HETATM 113 O HOH A 35 1.438 5.888 39.988 0.50 33.36 O HETATM 114 O HOH A 36 -2.070 5.845 45.846 0.50 41.04 O HETATM 115 O HOH A 37 0.180 7.288 30.538 0.50 25.97 O HETATM 116 O HOH A 38 10.602 3.363 54.758 0.50 44.69 O HETATM 117 O HOH A 39 1.767 2.652 43.720 0.50 37.12 O HETATM 118 O HOH A 40 -0.905 3.111 42.797 1.00 43.65 O HETATM 119 O HOH A 41 -1.581 4.387 40.306 1.00 58.98 O HETATM 120 O HOH A 42 10.223 2.285 50.781 1.00 33.46 O HETATM 121 O HOH A 43 -0.931 4.701 44.371 0.50 24.23 O HETATM 122 O HOH A 44 3.732 5.806 46.781 0.50 31.10 O HETATM 123 O HOH A 45 0.312 3.873 49.461 0.50 33.95 O HETATM 124 O HOH A 46 10.190 5.578 50.133 1.00 48.48 O HETATM 125 O HOH A 47 -1.211 -0.358 30.190 0.50 56.20 O HETATM 126 O HOH A 48 -4.290 0.281 29.053 1.00 36.16 O HETATM 127 O HOH B 49 12.900 4.124 54.750 0.50 20.30 O HETATM 128 O HOH B 50 3.624 3.056 47.641 0.50 43.59 O HETATM 129 O HOH B 51 12.110 1.922 46.988 0.50 26.00 O HETATM 130 O HOH B 52 -2.131 5.581 41.361 0.50 30.94 O HETATM 131 O HOH B 53 -0.182 2.153 44.599 0.50 24.09 O HETATM 132 O HOH B 54 2.865 2.175 26.828 0.50 31.98 O HETATM 133 O HOH B 55 12.135 3.322 44.717 0.50 32.45 O HETATM 134 O HOH B 56 10.812 4.698 51.712 0.50 35.88 O HETATM 135 O HOH B 57 11.875 3.010 42.893 0.50 28.10 O HETATM 136 O HOH B 58 -1.599 5.866 32.353 0.50 32.05 O HETATM 137 O HOH B 59 3.083 3.128 29.135 0.50 27.55 O HETATM 138 O HOH B 60 -2.710 6.688 47.889 0.50 36.65 O HETATM 139 O HOH B 61 1.039 1.807 31.620 0.50 54.52 O HETATM 140 O HOH B 62 2.628 -0.374 52.440 0.50 39.47 O HETATM 141 O HOH B 63 1.978 4.775 48.959 0.50 34.56 O HETATM 142 O HOH B 64 11.724 3.167 54.554 0.50 31.46 O HETATM 143 O HOH B 65 10.884 3.942 48.910 0.50 46.42 O HETATM 144 O HOH B 66 2.766 5.088 29.521 0.50 70.73 O HETATM 145 O HOH B 67 0.748 5.536 35.954 0.50 61.56 O HETATM 146 O HOH B 68 9.929 1.726 48.072 0.50 27.96 O HETATM 147 O HOH B 69 2.066 2.424 42.706 0.50 27.27 O HETATM 148 O HOH B 70 -0.570 2.578 48.657 0.50 43.43 O HETATM 149 O HOH B 71 1.545 -0.418 49.417 0.50 37.56 O HETATM 150 O HOH B 72 -2.374 3.346 37.147 0.50 51.35 O HETATM 151 O HOH B 73 0.141 3.523 42.944 0.50 33.47 O HETATM 152 O HOH B 74 3.228 5.561 44.741 0.50 27.34 O HETATM 153 O HOH B 75 -1.311 1.698 41.968 0.50 39.20 O HETATM 154 O HOH B 76 -1.883 6.643 44.915 0.50 37.54 O HETATM 155 O HOH B 77 -0.263 0.280 46.166 0.50 27.45 O HETATM 156 O HOH B 78 -1.116 3.419 32.283 0.50 34.24 O HETATM 157 O HOH B 79 4.997 3.638 26.481 0.50 20.28 O HETATM 158 O HOH B 80 0.851 4.882 43.739 0.50 35.68 O HETATM 159 O HOH B 81 2.906 1.662 49.717 0.50 65.94 O HETATM 160 O HOH B 82 -4.078 1.179 41.250 0.50 75.52 O HETATM 161 O HOH B 83 -1.505 0.339 31.082 0.50 48.05 O HETATM 162 O HOH B 84 -3.368 6.643 30.835 0.50 45.95 O HETATM 163 O HOH B 85 -0.561 7.507 49.729 0.50 38.43 O HETATM 164 8H7 HOH B 86 5.762 9.891 25.262 1.00 36.13 H HETATM 165 9H7 HOH B 87 0.482 0.941 41.869 1.00 21.92 H HETATM 166 0H8 HOH B 88 8.290 -0.144 45.280 1.00 37.28 H HETATM 167 1H8 HOH B 89 0.322 3.805 32.273 1.00 27.58 H HETATM 168 2H8 HOH B 90 1.810 0.529 44.467 1.00 22.38 H HETATM 169 3H8 HOH B 91 -2.720 4.953 30.301 1.00 34.95 H HETATM 170 4H8 HOH B 92 3.233 1.516 29.418 0.50 53.46 H CONECT 40 41 43 50 CONECT 41 40 42 CONECT 42 41 CONECT 43 40 44 45 CONECT 44 43 CONECT 45 43 46 47 CONECT 46 45 CONECT 47 45 51 52 CONECT 48 51 CONECT 49 50 CONECT 50 40 49 51 CONECT 51 47 48 50 CONECT 52 47 CONECT 53 54 57 CONECT 54 53 55 CONECT 55 54 56 CONECT 56 55 CONECT 57 53 CONECT 58 59 60 CONECT 59 58 CONECT 60 58 61 64 CONECT 61 60 62 63 CONECT 62 61 CONECT 63 61 CONECT 64 60 65 CONECT 65 64 MASTER 357 1 3 0 0 0 0 6 169 1 26 1 END