HEADER RIBONUCLEIC ACID 18-AUG-88 DRB005 TITLE CRYSTALLOGRAPHIC STUDIES OF DRUG-NUCLEIC ACID INTERACTIONS: TITLE 2 PROFLAVINE INTERCALATION BETWEEN THE NON-COMPLEMENTARY TITLE 3 BASE-PAIRS OF CYTIDILYL-3',5'-ADENOSINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA (5'-R(*CP*A)-3'); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES KEYWDS U-RNA, DOUBLE HELIX, PARALLEL HELIX, COMPLEXED WITH DRUG EXPDTA X-RAY DIFFRACTION AUTHOR E.WESTHOF,S.T.RAO,M.SUNDARALINGAM REVDAT 2 21-SEP-01 5 REVDAT 1 18-AUG-88 0 JRNL AUTH E.WESTHOF,S.T.RAO,M.SUNDARALINGAM JRNL TITL CRYSTALLOGRAPHIC STUDIES OF DRUG-NUCLEIC ACID JRNL TITL 2 INTERACTIONS: PROFLAVINE INTERCALATION BETWEEN THE JRNL TITL 3 NON-COMPLEMENTARY BASE-PAIRS OF JRNL TITL 4 CYTIDILYL-3',5'-ADENOSINE JRNL REF J.MOL.BIOL. V. 142 331 1980 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.WESTHOF,M.SUNDARALINGAM REMARK 1 TITL X-RAY STRUCTURE OF A CYTIDYLYL-3',5'-ADENOSINE REMARK 1 TITL 2 PROFLAVINE COMPLEX: A SELF-PAIRED PARALLEL-CHAIN REMARK 1 TITL 3 DOUBLE HELICAL DIMER WITH AN INTERCALATED ACRIDINE REMARK 1 TITL 4 DYE. REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 77 1852 1980 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. 0.8 ANGSTROM. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.80 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 : 2454 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) : 0.110 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 : 39 REMARK 3 HETEROGEN ATOMS : 25 REMARK 3 SOLVENT ATOMS : 26 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: TO FORM THE PARALLEL REMARK 3 INTERCALATED DUPLEX USE THE FOLLOWING RELATIONS: REMARK 3 TRANSLATION FOR C-A FOR SYMMETRY 1) 0,0,0 TRANSLATION FOR REMARK 3 C-A FOR SYMMETRY 2) 1,0,0 TRANSLATION FOR PF25 FOR REMARK 3 SYMMETRY 1) 0,0,0 TRANSLATION FOR PF25 FOR SYMMETRY 2) 1, REMARK 3 0,0 TRANSLATION FOR PF26 FOR SYMMETRY 1) 0,0,0 REMARK 3 TRANSLATION FOR PF26 FOR SYMMETRY 2) 2,1,0 REMARK 4 REMARK 4 NULL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 103 REMARK 103 THERE ARE NON-WATSON-CRICK HYDROGEN BONDS BETWEEN THE REMARK 103 FOLLOWING ATOMS: REMARK 103 O2 C A 1 AND N4 C B 1 REMARK 103 N4 C A 1 AND O2 C B 1 REMARK 103 N7 A A 2 AND N6 A B 2 REMARK 103 N6 A A 2 AND N7 A B 2 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 283.0 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) : 1.5400 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : DIFFRACTOMETER REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS CAD4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2454 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.800 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500 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: METHANOL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 1/2-Y,1/2+X,1/2+Z REMARK 290 4555 1/2+Y,1/2-X,1/2+Z REMARK 290 5555 1/2-X,1/2+Y,1/2-Z REMARK 290 6555 1/2+X,1/2-Y,1/2-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 9.69000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 9.69000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 13.55000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 9.69000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 9.69000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.55000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 9.69000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 9.69000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 13.55000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 9.69000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 9.69000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 13.55000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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 -1.000000 0.000000 0.000000 19.38000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 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 38.76000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 19.38000 REMARK 350 BIOMT3 4 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 HOH A 23 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 30 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 6 O HOH A 24 1.03 REMARK 500 O HOH A 11 O HOH A 19 1.10 REMARK 500 O HOH A 9 O HOH A 20 1.10 REMARK 500 N15 PF A 3 O HOH A 15 1.62 REMARK 500 O HOH A 14 O HOH A 17 1.67 REMARK 500 O HOH A 16 O HOH A 23 1.87 REMARK 500 O HOH A 21 O HOH A 24 1.88 REMARK 500 O HOH A 20 O HOH A 21 2.11 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 6 O HOH A 25 6566 0.83 REMARK 500 O2* A A 2 O HOH A 29 3645 1.30 REMARK 500 N10 PF B 4 C11 PF B 4 2765 1.40 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 0 HOH A 8 DISTANCE = 5.20 ANGSTROMS REMARK 525 0 HOH A 25 DISTANCE = 14.69 ANGSTROMS REMARK 525 0 HOH A 26 DISTANCE = 10.43 ANGSTROMS REMARK 525 0 HOH A 28 DISTANCE = 16.54 ANGSTROMS REMARK 525 0 HOH A 29 DISTANCE = 11.52 ANGSTROMS REMARK 525 0 HOH A 30 DISTANCE = 7.34 ANGSTROMS SEQRES 1 A 2 C A FTNOTE 1 THESE ATOMS AND SOME WATER MOLECULES ARE DISORDERED. HET PF A 3 16 HET PF B 4 9 HETNAM PF PROFLAVINE FORMUL 2 PF 2(C13 H12 N3 1+) FORMUL 4 HOH *26(H2 O1) CRYST1 19.380 19.380 27.100 90.00 90.00 90.00 P 42 21 2 8 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 0.051600 0.000000 0.000000 0.00000 SCALE2 0.000000 0.051600 0.000000 0.00000 SCALE3 0.000000 0.000000 0.036900 0.00000 ATOM 1 O5* C A 1 11.990 -6.866 19.236 1.00 11.50 O ATOM 2 C5* C A 1 13.326 -6.950 18.723 1.00 10.10 C ATOM 3 C4* C A 1 13.851 -5.543 18.591 1.00 8.70 C ATOM 4 O4* C A 1 13.163 -4.752 17.607 1.00 7.80 O ATOM 5 C3* C A 1 13.830 -4.643 19.900 1.00 6.70 C ATOM 6 O3* C A 1 14.841 -4.971 20.769 1.00 8.30 O ATOM 7 C2* C A 1 13.861 -3.267 19.301 1.00 6.50 C ATOM 8 O2* C A 1 15.258 -2.919 18.948 1.00 9.40 O ATOM 9 C1* C A 1 13.078 -3.391 18.005 1.00 6.80 C ATOM 10 N1 C A 1 11.614 -3.064 18.165 1.00 6.10 N ATOM 11 C2 C A 1 11.273 -1.752 18.078 1.00 5.90 C ATOM 12 O2 C A 1 12.184 -0.888 18.143 1.00 6.80 O ATOM 13 N3 C A 1 9.981 -1.409 18.119 1.00 5.60 N ATOM 14 C4 C A 1 9.029 -2.310 18.143 1.00 6.00 C ATOM 15 N4 C A 1 7.783 -1.969 18.076 1.00 6.90 N ATOM 16 C5 C A 1 9.395 -3.700 18.162 1.00 6.00 C ATOM 17 C6 C A 1 10.609 -4.058 18.179 1.00 6.20 C ATOM 18 P A A 2 14.669 -4.735 22.341 1.00 8.00 P ATOM 19 O1P A A 2 15.762 -5.514 22.967 1.00 9.80 O ATOM 20 O2P A A 2 13.275 -5.023 22.742 1.00 8.60 O ATOM 21 O5* A A 2 14.855 -3.186 22.558 1.00 8.20 O ATOM 22 C5* A A 2 16.124 -2.620 22.314 1.00 9.50 C ATOM 23 C4* A A 2 16.502 -1.628 23.417 1.00 9.70 C ATOM 24 O4* A A 2 15.521 -0.630 23.542 1.00 8.20 O ATOM 25 C3* A A 2 16.607 -2.236 24.810 1.00 8.60 C ATOM 26 O3* A A 2 17.636 -1.560 25.618 1.00 13.10 O ATOM 27 C2* A A 2 15.363 -1.868 25.436 1.00 9.80 C ATOM 28 O2* A A 2 15.258 -1.940 26.824 1.00 12.50 O ATOM 29 C1* A A 2 15.157 -0.469 24.897 1.00 6.70 C ATOM 30 N9 A A 2 13.702 -0.076 24.859 1.00 6.10 N ATOM 31 C8 A A 2 12.601 -0.874 24.783 1.00 7.10 C ATOM 32 N7 A A 2 11.510 -0.172 24.764 1.00 6.10 N ATOM 33 C5 A A 2 11.890 1.114 24.867 1.00 5.70 C ATOM 34 C6 A A 2 11.194 2.388 24.899 1.00 7.40 C ATOM 35 N6 A A 2 9.814 2.366 24.918 1.00 7.50 N ATOM 36 N1 A A 2 11.872 3.483 24.965 1.00 6.50 N ATOM 37 C2 A A 2 13.165 3.432 24.994 1.00 8.00 C ATOM 38 N3 A A 2 13.987 2.349 24.951 1.00 6.80 N ATOM 39 C4 A A 2 13.285 1.200 24.883 1.00 5.60 C TER 40 A A 2 HETATM 41 C1 PF A 3 8.432 2.994 21.661 0.50 6.90 C HETATM 42 C2 PF A 3 9.209 4.101 21.623 0.50 8.30 C HETATM 43 C3 PF A 3 10.647 3.928 21.550 0.50 6.20 C HETATM 44 C4 PF A 3 11.219 2.667 21.496 0.50 5.10 C HETATM 45 C5 PF A 3 10.659 -2.143 21.639 0.50 4.50 C HETATM 46 C6 PF A 3 9.868 -3.298 21.542 0.50 7.50 C HETATM 47 C7 PF A 3 8.461 -3.109 21.458 0.50 6.70 C HETATM 48 C8 PF A 3 7.880 -1.897 21.433 0.50 6.10 C HETATM 49 C9 PF A 3 8.165 0.568 21.436 0.50 6.00 C HETATM 50 N10 PF A 3 10.911 0.267 21.401 0.50 5.30 N HETATM 51 C11 PF A 3 8.932 1.647 21.563 0.50 6.10 C HETATM 52 C12 PF A 3 10.310 1.554 21.477 0.50 5.70 C HETATM 53 C13 PF A 3 10.083 -0.907 21.577 0.50 7.70 C HETATM 54 C14 PF A 3 8.692 -0.686 21.431 0.50 4.60 C HETATM 55 N15 PF A 3 11.450 5.079 21.523 0.50 10.50 N HETATM 56 N16 PF A 3 10.380 -4.506 21.658 0.50 6.90 N HETATM 57 C1 PF B 4 19.723 6.861 25.970 1.00 10.00 C HETATM 58 C2 PF B 4 18.535 6.138 25.956 1.00 8.40 C HETATM 59 C3 PF B 4 17.190 6.705 25.916 1.00 10.00 C HETATM 60 C4 PF B 4 17.153 8.064 25.932 1.00 9.00 C HETATM 61 N10 PF B 4 18.140 10.225 25.951 1.00 8.70 N HETATM 62 C11 PF B 4 19.477 8.345 26.011 1.00 7.80 C HETATM 63 C12 PF B 4 18.248 8.862 25.954 1.00 7.20 C HETATM 64 N15 PF B 4 16.223 5.892 25.937 0.50 8.40 N HETATM 65 N16 PF B 4 18.806 4.620 25.875 0.50 10.30 N HETATM 66 O HOH A 5 2.713 16.638 25.729 1.00 10.00 O HETATM 67 O HOH A 6 11.932 15.058 25.100 1.00 15.70 O HETATM 68 O HOH A 7 13.727 -0.006 21.314 0.50 7.10 O HETATM 69 O HOH A 8 14.091 9.558 21.653 0.50 14.30 O HETATM 70 O HOH A 9 15.808 13.735 25.837 0.50 10.80 O HETATM 71 O HOH A 10 7.167 7.378 22.081 0.50 10.30 O HETATM 72 O HOH A 11 11.147 6.087 24.688 0.50 15.20 O HETATM 73 O HOH A 12 18.611 2.211 24.282 0.25 10.00 O HETATM 74 O HOH A 13 13.539 7.076 25.702 0.50 20.50 O HETATM 75 O HOH A 14 3.483 8.333 26.100 0.25 10.10 O HETATM 76 O HOH A 15 10.783 6.541 21.328 0.25 11.60 O HETATM 77 O HOH A 16 19.109 1.533 22.081 0.25 9.80 O HETATM 78 O HOH A 17 4.134 7.312 24.946 0.25 11.20 O HETATM 79 O HOH A 18 9.320 13.300 25.618 0.25 23.00 O HETATM 80 O HOH A 19 11.250 6.103 25.780 0.25 21.30 O HETATM 81 O HOH A 20 15.374 14.200 26.731 0.13 21.30 O HETATM 82 O HOH A 21 13.634 15.364 26.989 0.25 9.30 O HETATM 83 O HOH A 22 0.733 18.318 24.856 0.25 5.80 O HETATM 84 O HOH A 23 19.380 0.000 21.043 0.25 22.20 O HETATM 85 O HOH A 24 12.872 15.454 25.271 0.25 18.90 O HETATM 86 O HOH A 25 1.638 14.457 15.913 0.25 14.00 O HETATM 87 O HOH A 26 18.105 18.925 20.195 0.25 13.40 O HETATM 88 O HOH A 27 5.064 9.719 24.311 0.13 14.30 O HETATM 89 O HOH A 28 3.711 19.562 19.536 0.25 21.40 O HETATM 90 O HOH A 29 8.766 13.264 13.870 0.13 16.20 O HETATM 91 O HOH A 30 15.994 3.382 13.550 0.13 21.00 O CONECT 41 42 53 CONECT 42 41 43 CONECT 43 42 44 55 CONECT 44 43 51 CONECT 45 46 54 CONECT 46 45 47 56 CONECT 47 46 48 CONECT 48 47 52 CONECT 49 52 53 CONECT 50 51 54 CONECT 51 44 50 53 CONECT 52 48 49 54 CONECT 53 41 49 51 CONECT 54 45 50 52 CONECT 55 43 CONECT 56 46 CONECT 57 58 CONECT 58 57 59 CONECT 59 58 60 64 CONECT 60 59 62 CONECT 61 62 CONECT 62 60 61 CONECT 64 59 MASTER 305 1 2 0 0 0 0 6 90 1 23 1 END