HEADER DEOXYRIBONUCLEIC ACID 19-JUL-92 DDB034 TITLE LOW TEMPERATURE STRUCTURES OF DCPG-PROFLAVINE: TITLE 2 CONFORMATIONAL AND HYDRATION EFFECTS COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'-D(*CP*G)-3'); COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES KEYWDS RIGHT HANDED DNA, DOUBLE HELIX, COMPLEXED WITH DRUG EXPDTA X-RAY DIFFRACTION AUTHOR B.SCHNEIDER,S.L.GINELL,H.M.BERMAN REVDAT 2 21-SEP-01 5 REVDAT 1 19-JUL-92 0 JRNL AUTH B.SCHNEIDER,S.L.GINELL,H.M.BERMAN JRNL TITL LOW TEMPERATURE STRUCTURES OF DCPG-PROFLAVINE: JRNL TITL 2 CONFORMATIONAL AND HYDRATION EFFECTS JRNL REF BIOPHYS.J. V. 63 1572 1992 JRNL REFN ASTM BIOJAU US ISSN 0006-3495 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 0.93 ANGSTROM. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELX-76 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.122 REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.122 REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 5125 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 0 REMARK 3 NUCLEIC ACID ATOMS : 79 REMARK 3 HETEROGEN ATOMS : 32 REMARK 3 SOLVENT ATOMS : 34 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 ANGLE DISTANCES (A) : NULL REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL 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) : 143.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE 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 : 6688 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.930 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 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: NH4 SULFATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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-X,1/2+Y,-Z REMARK 290 4555 1/2+X,1/2-Y,-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 -1.000000 0.000000 0.000000 16.42650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 10.88000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.42650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 10.88000 REMARK 290 SMTRY3 4 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 2 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, B 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 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 7 LIES ON A SPECIAL POSITION. REMARK 375 HOH 32 LIES ON A SPECIAL POSITION. REMARK 375 HOH 34 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 12 O HOH 13 0.91 REMARK 500 O HOH 34 O HOH 35 1.50 REMARK 500 O HOH 36 O HOH 37 1.52 REMARK 500 O HOH 12 O HOH 40 2.18 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 34 DISTANCE = 12.04 ANGSTROMS REMARK 525 0 HOH 39 DISTANCE = 9.15 ANGSTROMS SEQRES 1 A 2 C G SEQRES 1 B 2 C G HET PF 5 16 HET PF 6 16 HETNAM PF PROFLAVINE FORMUL 3 PF 2(C13 H12 N3 1+) FORMUL 5 HOH *34(H2 O1) CRYST1 32.853 21.760 13.296 90.00 90.00 90.00 P 21 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 0.030439 0.000000 0.000000 0.00000 SCALE2 0.000000 0.045956 0.000000 0.00000 SCALE3 0.000000 0.000000 0.075211 0.00000 ATOM 1 O5* C A 1 22.343 5.170 -0.185 1.00 10.00 O ANISOU 1 O5* C A 1 4851 2961 3423 -229 821 973 O ATOM 2 C5* C A 1 21.943 3.819 -0.419 1.00 10.00 C ANISOU 2 C5* C A 1 2827 3012 5925 456 963 1579 C ATOM 3 C4* C A 1 23.014 2.824 -0.081 1.00 10.00 C ANISOU 3 C4* C A 1 2300 6523 2205 2202 1473 133 C ATOM 4 O4* C A 1 24.196 3.146 -0.955 1.00 10.00 O ANISOU 4 O4* C A 1 1011 6655 3532 -225 -221 -32 O ATOM 5 C3* C A 1 23.579 2.864 1.306 1.00 10.00 C ANISOU 5 C3* C A 1 2615 3019 3017 -664 -1496 1207 C ATOM 6 O3* C A 1 22.672 2.139 2.170 1.00 10.00 O ANISOU 6 O3* C A 1 990 3217 5608 392 122 300 O ATOM 7 C2* C A 1 24.945 2.152 1.078 1.00 10.00 C ANISOU 7 C2* C A 1 1826 4239 4475 1027 -252 731 C ATOM 8 C1* C A 1 25.363 2.709 -0.255 1.00 10.00 C ANISOU 8 C1* C A 1 1951 2782 4260 -353 156 661 C ATOM 9 N1 C A 1 26.230 3.928 -0.120 1.00 10.00 N ANISOU 9 N1 C A 1 2797 3570 3188 -604 646 -104 N ATOM 10 C2 C A 1 27.567 3.699 0.082 1.00 10.00 C ANISOU 10 C2 C A 1 3137 3947 1768 -57 1586 866 C ATOM 11 O2 C A 1 27.945 2.494 0.223 1.00 10.00 O ANISOU 11 O2 C A 1 2041 3564 3235 -533 70 952 O ATOM 12 N3 C A 1 28.428 4.705 0.225 1.00 10.00 N ANISOU 12 N3 C A 1 1419 1393 3627 -640 608 -45 N ATOM 13 C4 C A 1 28.014 5.984 0.148 1.00 10.00 C ANISOU 13 C4 C A 1 1832 5831 4754 440 -329 2067 C ATOM 14 N4 C A 1 28.845 7.007 0.182 1.00 10.00 N ANISOU 14 N4 C A 1 2515 2413 7478 -2 -1550 194 N ATOM 15 C5 C A 1 26.516 6.271 -0.015 1.00 10.00 C ANISOU 15 C5 C A 1 2709 4330 8058 1263 712 1702 C ATOM 16 C6 C A 1 25.734 5.188 -0.179 1.00 10.00 C ANISOU 16 C6 C A 1 1966 3230 9687 1549 -119 1552 C ATOM 17 P G A 2 22.616 2.363 3.699 1.00 10.00 P ANISOU 17 P G A 2 4699 3768 3529 474 352 1047 P ATOM 18 O1P G A 2 21.499 1.471 4.172 1.00 10.00 O ANISOU 18 O1P G A 2 5277 6934 4741 2550 2167 1175 O ATOM 19 O2P G A 2 22.570 3.795 3.993 1.00 10.00 O ANISOU 19 O2P G A 2 5951 3647 4139 -406 825 1338 O ATOM 20 O5* G A 2 24.035 1.863 4.280 1.00 10.00 O ANISOU 20 O5* G A 2 4373 4892 6149 20 -874 416 O ATOM 21 C5* G A 2 24.236 0.403 4.279 1.00 10.00 C ANISOU 21 C5* G A 2 11309 1228 9819 -2244 -3727 866 C ATOM 22 C4* G A 2 25.008 0.083 5.566 1.00 10.00 C ANISOU 22 C4* G A 2 4382 7531 8238 1433 -4641 -4026 C ATOM 23 O4* G A 2 26.358 0.753 5.506 1.00 10.00 O ANISOU 23 O4* G A 2 2954 5669 5480 -1591 -1005 1611 O ATOM 24 C3*A G A 2 24.328 0.387 6.870 0.20 1.54 C ATOM 25 C3*B G A 2 24.489 0.764 6.859 0.80 4.05 C ATOM 26 O3*A G A 2 24.659 -1.042 7.354 0.20 1.39 O ATOM 27 O3*B G A 2 23.414 -0.109 7.506 0.80 5.95 O ATOM 28 C2*A G A 2 25.248 1.571 7.214 0.20 1.30 C ATOM 29 C2*B G A 2 25.622 0.788 7.926 0.80 4.07 C ATOM 30 C1* G A 2 26.709 1.066 6.830 1.00 10.00 C ANISOU 30 C1* G A 2 5961 7985 3459 -920 -1640 -5429 C ATOM 31 N9 G A 2 27.261 2.465 6.794 1.00 10.00 N ANISOU 31 N9 G A 2 2948 8379 3308 -1320 -1034 596 N ATOM 32 C8 G A 2 26.558 3.636 6.772 1.00 10.00 C ANISOU 32 C8 G A 2 3233 9267 3054 -878 -1083 -1536 C ATOM 33 N7 G A 2 27.380 4.711 6.766 1.00 10.00 N ANISOU 33 N7 G A 2 4537 7379 2661 -570 -437 1634 N ATOM 34 C5 G A 2 28.687 4.161 6.845 1.00 10.00 C ANISOU 34 C5 G A 2 4738 5563 3440 1133 606 2061 C ATOM 35 C6 G A 2 29.909 4.789 6.909 1.00 10.00 C ANISOU 35 C6 G A 2 4678 2496 2978 -977 1822 -276 C ATOM 36 O6 G A 2 30.192 6.010 6.853 1.00 10.00 O ANISOU 36 O6 G A 2 2792 6020 3648 -211 -168 -523 O ATOM 37 N1 G A 2 30.974 3.906 6.886 1.00 10.00 N ANISOU 37 N1 G A 2 3676 4799 2315 381 -264 421 N ATOM 38 C2 G A 2 30.829 2.539 6.887 1.00 10.00 C ANISOU 38 C2 G A 2 3763 2986 4460 1480 378 377 C ATOM 39 N2 G A 2 31.900 1.758 6.879 1.00 10.00 N ANISOU 39 N2 G A 2 2198 4691 12357 1122 -2662 -773 N ATOM 40 N3 G A 2 29.614 1.897 6.885 1.00 10.00 N ANISOU 40 N3 G A 2 2804 4699 3305 -626 -1192 793 N ATOM 41 C4 G A 2 28.631 2.774 6.831 1.00 10.00 C ANISOU 41 C4 G A 2 4132 3755 2158 -138 359 -1776 C TER 42 G A 2 ATOM 43 O5* C B 3 39.716 6.415 6.746 1.00 10.00 O ANISOU 43 O5* C B 3 3918 5267 6057 -900 -172 -1361 O ATOM 44 C5* C B 3 40.314 5.166 6.930 1.00 10.00 C ANISOU 44 C5* C B 3 2620 4570 7970 -365 -2153 -370 C ATOM 45 C4* C B 3 39.315 3.949 6.813 1.00 10.00 C ANISOU 45 C4* C B 3 3310 8550 2728 -962 390 321 C ATOM 46 O4* C B 3 38.241 4.178 7.710 1.00 10.00 O ANISOU 46 O4* C B 3 3652 6174 3642 -227 -233 17 O ATOM 47 C3* C B 3 38.602 3.808 5.451 1.00 10.00 C ANISOU 47 C3* C B 3 4287 5045 3214 -441 -7 23 C ATOM 48 O3* C B 3 39.512 3.188 4.570 1.00 10.00 O ANISOU 48 O3* C B 3 2781 3924 5923 -1224 266 1076 O ATOM 49 C2* C B 3 37.364 2.920 5.846 1.00 10.00 C ANISOU 49 C2* C B 3 6870 3079 3004 -560 -655 1648 C ATOM 50 C1* C B 3 37.032 3.514 7.210 1.00 10.00 C ANISOU 50 C1* C B 3 3003 4974 10844 -2536 -2077 1912 C ATOM 51 N1 C B 3 35.981 4.596 7.092 1.00 10.00 N ANISOU 51 N1 C B 3 2156 4687 5362 567 1123 -1207 N ATOM 52 C2 C B 3 34.660 4.141 6.998 1.00 10.00 C ANISOU 52 C2 C B 3 5472 2416 5014 298 -1344 1131 C ATOM 53 O2 C B 3 34.496 2.879 6.883 1.00 10.00 O ANISOU 53 O2 C B 3 2110 5754 5670 -898 -959 343 O ATOM 54 N3 C B 3 33.625 4.950 6.911 1.00 10.00 N ANISOU 54 N3 C B 3 2754 3175 4929 -795 305 -1187 N ATOM 55 C4 C B 3 33.829 6.278 6.994 1.00 10.00 C ANISOU 55 C4 C B 3 4206 6232 1848 917 -446 -1112 C ATOM 56 N4 C B 3 32.856 7.118 6.941 1.00 10.00 N ANISOU 56 N4 C B 3 3450 5433 5332 277 718 2218 N ATOM 57 C5 C B 3 35.222 6.854 7.072 1.00 10.00 C ANISOU 57 C5 C B 3 3245 4274 3422 -146 883 -2369 C ATOM 58 C6 C B 3 36.224 5.930 7.143 1.00 10.00 C ANISOU 58 C6 C B 3 7273 2440 4859 -3124 -1917 1551 C ATOM 59 P G B 4 39.361 3.345 2.981 1.00 10.00 P ANISOU 59 P G B 4 6160 4719 3202 -597 -589 369 P ATOM 60 O1P G B 4 40.501 2.513 2.399 1.00 10.00 O ANISOU 60 O1P G B 4 5896 7913 5258 -2042 2107 967 O ATOM 61 O2P G B 4 39.259 4.778 2.605 1.00 10.00 O ANISOU 61 O2P G B 4 9032 6860 3832 -26 -1934 12 O ATOM 62 O5* G B 4 37.971 2.692 2.599 1.00 10.00 O ANISOU 62 O5* G B 4 6762 4495 5384 -167 -3384 -366 O ATOM 63 C5* G B 4 37.755 1.258 2.715 1.00 10.00 C ANISOU 63 C5* G B 4 6548 2497 7248 -3106 -2761 2281 C ATOM 64 C4* G B 4 37.124 0.759 1.441 1.00 10.00 C ANISOU 64 C4* G B 4 4197 2633 3449 1778 144 1912 C ATOM 65 O4* G B 4 35.843 1.436 1.239 1.00 10.00 O ANISOU 65 O4* G B 4 2740 6184 4350 775 1079 1278 O ATOM 66 C3* G B 4 37.853 0.955 0.125 1.00 10.00 C ANISOU 66 C3* G B 4 2839 3340 4114 -748 -851 795 C ATOM 67 O3* G B 4 37.495 0.004 -0.834 1.00 10.00 O ANISOU 67 O3* G B 4 1681 2760 5578 -63 -80 302 O ATOM 68 C2* G B 4 37.321 2.330 -0.396 1.00 10.00 C ANISOU 68 C2* G B 4 1358 3551 5432 -293 38 845 C ATOM 69 C1* G B 4 35.872 2.154 -0.003 1.00 10.00 C ANISOU 69 C1* G B 4 1489 3985 2771 680 492 2138 C ATOM 70 N9 G B 4 35.126 3.429 0.217 1.00 10.00 N ANISOU 70 N9 G B 4 2652 1389 3092 202 824 -110 N ATOM 71 C8 G B 4 35.642 4.724 0.219 1.00 10.00 C ANISOU 71 C8 G B 4 1685 4061 2953 -631 547 -290 C ATOM 72 N7 G B 4 34.699 5.621 0.285 1.00 10.00 N ANISOU 72 N7 G B 4 1346 3049 3244 -444 82 -750 N ATOM 73 C5 G B 4 33.503 4.872 0.324 1.00 10.00 C ANISOU 73 C5 G B 4 3405 2172 2559 799 -1229 520 C ATOM 74 C6 G B 4 32.163 5.283 0.336 1.00 10.00 C ANISOU 74 C6 G B 4 2051 4992 2431 444 340 574 C ATOM 75 O6 G B 4 31.680 6.450 0.360 1.00 10.00 O ANISOU 75 O6 G B 4 3396 1558 5675 -195 -236 565 O ATOM 76 N1 G B 4 31.283 4.206 0.327 1.00 10.00 N ANISOU 76 N1 G B 4 1213 2604 3161 -381 -54 -571 N ATOM 77 C2 G B 4 31.664 2.927 0.306 1.00 10.00 C ANISOU 77 C2 G B 4 1784 1977 4372 17 46 -114 C ATOM 78 N2 G B 4 30.668 1.952 0.283 1.00 10.00 N ANISOU 78 N2 G B 4 1651 3721 4703 -219 -317 752 N ATOM 79 N3 G B 4 32.929 2.509 0.274 1.00 10.00 N ANISOU 79 N3 G B 4 2359 2892 3094 -60 -248 -420 N ATOM 80 C4 G B 4 33.776 3.547 0.274 1.00 10.00 C ANISOU 80 C4 G B 4 1645 2320 1597 -322 146 -759 C TER 81 G B 4 HETATM 82 C1 PF 5 34.193 3.791 3.535 1.00 10.00 C ANISOU 82 C1 PF 5 10203 9783 3437 -612 457 -471 C HETATM 83 C2 PF 5 35.179 4.866 3.513 1.00 10.00 C ANISOU 83 C2 PF 5 10203 9783 3437 -612 457 -471 C HETATM 84 C3 PF 5 34.765 6.202 3.550 1.00 10.00 C ANISOU 84 C3 PF 5 10203 9783 3437 -612 457 -471 C HETATM 85 C4 PF 5 33.336 6.567 3.551 1.00 10.00 C ANISOU 85 C4 PF 5 10203 9783 3437 -612 457 -471 C HETATM 86 C5 PF 5 28.737 5.420 3.583 1.00 10.00 C ANISOU 86 C5 PF 5 10203 9783 3437 -612 457 -471 C HETATM 87 C6 PF 5 27.767 4.300 3.555 1.00 10.00 C ANISOU 87 C6 PF 5 10203 9783 3437 -612 457 -471 C HETATM 88 C7 PF 5 28.086 2.981 3.578 1.00 10.00 C ANISOU 88 C7 PF 5 10203 9783 3437 -612 457 -471 C HETATM 89 C8 PF 5 29.420 2.559 3.594 1.00 10.00 C ANISOU 89 C8 PF 5 10203 9783 3437 -612 457 -471 C HETATM 90 C9 PF 5 31.808 3.212 3.634 1.00 10.00 C ANISOU 90 C9 PF 5 10203 9783 3437 -612 457 -471 C HETATM 91 N10 PF 5 31.076 5.847 3.618 1.00 10.00 N ANISOU 91 N10 PF 5 10203 9783 3437 -612 457 -471 N HETATM 92 C11 PF 5 32.439 5.484 3.541 1.00 10.00 C ANISOU 92 C11 PF 5 10203 9783 3437 -612 457 -471 C HETATM 93 C12 PF 5 30.530 3.545 3.558 1.00 10.00 C ANISOU 93 C12 PF 5 10203 9783 3437 -612 457 -471 C HETATM 94 C13 PF 5 32.745 4.156 3.562 1.00 10.00 C ANISOU 94 C13 PF 5 10203 9783 3437 -612 457 -471 C HETATM 95 C14 PF 5 30.083 4.946 3.590 1.00 10.00 C ANISOU 95 C14 PF 5 10203 9783 3437 -612 457 -471 C HETATM 96 N15 PF 5 35.770 7.250 3.579 1.00 10.00 N ANISOU 96 N15 PF 5 10203 9783 3437 -612 457 -471 N HETATM 97 N16 PF 5 26.420 4.715 3.498 1.00 10.00 N ANISOU 97 N16 PF 5 10203 9783 3437 -612 457 -471 N HETATM 98 C1 PF 6 33.714 3.277 10.314 1.00 10.00 C ANISOU 98 C1 PF 6 9685 8836 2781 656 -809 1310 C HETATM 99 C2 PF 6 34.775 4.147 10.312 1.00 10.00 C ANISOU 99 C2 PF 6 9685 8836 2781 656 -809 1310 C HETATM 100 C3 PF 6 34.597 5.418 10.282 1.00 10.00 C ANISOU 100 C3 PF 6 9685 8836 2781 656 -809 1310 C HETATM 101 C4 PF 6 33.290 6.080 10.237 1.00 10.00 C ANISOU 101 C4 PF 6 9685 8836 2781 656 -809 1310 C HETATM 102 C5 PF 6 28.562 5.544 10.062 1.00 10.00 C ANISOU 102 C5 PF 6 9685 8836 2781 656 -809 1310 C HETATM 103 C6 PF 6 27.429 4.755 10.033 1.00 10.00 C ANISOU 103 C6 PF 6 9685 8836 2781 656 -809 1310 C HETATM 104 C7 PF 6 27.468 3.299 10.097 1.00 10.00 C ANISOU 104 C7 PF 6 9685 8836 2781 656 -809 1310 C HETATM 105 C8 PF 6 28.796 2.796 10.185 1.00 10.00 C ANISOU 105 C8 PF 6 9685 8836 2781 656 -809 1310 C HETATM 106 C9 PF 6 31.227 3.012 10.242 1.00 10.00 C ANISOU 106 C9 PF 6 9685 8836 2781 656 -809 1310 C HETATM 107 N10 PF 6 30.954 5.751 10.155 1.00 10.00 N ANISOU 107 N10 PF 6 9685 8836 2781 656 -809 1310 N HETATM 108 C11 PF 6 32.226 5.205 10.173 1.00 10.00 C ANISOU 108 C11 PF 6 9685 8836 2781 656 -809 1310 C HETATM 109 C12 PF 6 29.992 3.527 10.183 1.00 10.00 C ANISOU 109 C12 PF 6 9685 8836 2781 656 -809 1310 C HETATM 110 C13 PF 6 32.331 3.817 10.287 1.00 10.00 C ANISOU 110 C13 PF 6 9685 8836 2781 656 -809 1310 C HETATM 111 C14 PF 6 29.814 4.963 10.171 1.00 10.00 C ANISOU 111 C14 PF 6 9685 8836 2781 656 -809 1310 C HETATM 112 N15 PF 6 35.685 6.295 10.336 1.00 10.00 N ANISOU 112 N15 PF 6 9685 8836 2781 656 -809 1310 N HETATM 113 N16 PF 6 26.158 5.375 9.964 1.00 10.00 N ANISOU 113 N16 PF 6 9685 8836 2781 656 -809 1310 N HETATM 114 O HOH 7 16.427 10.880 14.229 0.50 5.69 O HETATM 115 O HOH 8 25.254 9.635 12.892 1.00 7.87 O HETATM 116 O HOH 9 26.880 7.470 20.036 1.00 6.39 O HETATM 117 O HOH 10 18.963 10.334 21.173 1.00 8.27 O HETATM 118 O HOH 11 17.741 10.662 23.602 1.00 8.51 O HETATM 119 O HOH 12 30.550 13.395 13.073 0.50 3.40 O HETATM 120 O HOH 13 30.501 13.413 13.982 0.50 8.89 O HETATM 121 O HOH 14 28.418 11.518 19.948 1.00 11.23 O HETATM 122 O HOH 15 26.374 8.249 9.424 1.00 4.99 O HETATM 123 O HOH 16 26.480 11.968 16.486 1.00 11.14 O HETATM 124 O HOH 17 22.130 6.036 15.776 1.00 4.55 O HETATM 125 O HOH 18 30.737 8.567 9.695 1.00 9.55 O HETATM 126 O HOH 19 25.934 14.734 17.289 1.00 11.61 O HETATM 127 O HOH 20 30.461 8.543 17.209 1.00 15.49 O HETATM 128 O HOH 21 27.951 9.746 13.043 1.00 5.72 O HETATM 129 O HOH 22 25.960 7.562 17.398 1.00 10.08 O HETATM 130 O HOH 23 23.289 8.447 16.648 1.00 7.84 O HETATM 131 O HOH 24 28.894 11.700 14.757 1.00 8.59 O HETATM 132 O HOH 25 30.336 12.577 10.213 1.00 14.11 O HETATM 133 O HOH 26 18.575 10.253 18.122 1.00 11.86 O HETATM 134 O HOH 27 29.449 8.785 19.959 1.00 8.81 O HETATM 135 O HOH 28 21.118 10.123 16.882 1.00 8.43 O HETATM 136 O HOH 29 24.275 10.762 15.204 1.00 7.37 O HETATM 137 O HOH 30 33.385 12.740 13.332 1.00 11.95 O HETATM 138 O HOH 31 28.385 9.870 10.335 1.00 6.27 O HETATM 139 O HOH 32 16.427 10.880 16.686 0.50 17.22 O HETATM 140 O HOH 33 30.833 11.807 17.936 1.00 26.89 O HETATM 141 O HOH 34 32.853 10.880 21.097 0.25 5.45 O HETATM 142 O HOH 35 32.173 11.790 20.118 0.25 1.57 O HETATM 143 O HOH 36 32.232 11.087 7.791 0.25 0.31 O HETATM 144 O HOH 37 32.508 11.894 9.048 0.25 3.00 O HETATM 145 O HOH 38 27.840 9.091 16.443 1.00 19.09 O HETATM 146 O HOH 39 15.030 0.807 11.050 1.00 31.10 O HETATM 147 O HOH 40 31.522 11.618 12.279 0.50 20.63 O CONECT 82 83 94 CONECT 83 82 84 CONECT 84 83 85 96 CONECT 85 84 92 CONECT 86 87 95 CONECT 87 86 88 97 CONECT 88 87 89 CONECT 89 88 93 CONECT 90 93 94 CONECT 91 92 95 CONECT 92 85 91 94 CONECT 93 89 90 95 CONECT 94 82 90 92 CONECT 95 86 91 93 CONECT 96 84 CONECT 97 87 CONECT 98 99 110 CONECT 99 98 100 CONECT 100 99 101 112 CONECT 101 100 108 CONECT 102 103 111 CONECT 103 102 104 113 CONECT 104 103 105 CONECT 105 104 109 CONECT 106 109 110 CONECT 107 108 111 CONECT 108 101 107 110 CONECT 109 105 106 111 CONECT 110 98 106 108 CONECT 111 102 107 109 CONECT 112 100 CONECT 113 103 MASTER 212 0 2 0 0 0 0 6 145 2 32 2 END