REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.173 REMARK 3 R VALUE (WORKING SET) : 0.171 REMARK 3 FREE R VALUE : 0.213 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6729 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00 REMARK 3 REFLECTION IN BIN (WORKING SET) : 9261 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.2540 REMARK 3 BIN FREE R VALUE SET COUNT : 494 REMARK 3 BIN FREE R VALUE : 0.2890 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9486 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 177 REMARK 3 SOLVENT ATOMS : 851 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.39 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.06000 REMARK 3 B22 (A**2) : -0.58000 REMARK 3 B33 (A**2) : -2.48000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.120 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.891 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9879 ; 0.023 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6643 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13399 ; 1.840 ; 1.959 REMARK 3 BOND ANGLES OTHERS (DEGREES): 16236 ; 0.971 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1209 ; 7.593 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 383 ;35.733 ;24.256 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1572 ;13.547 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;19.748 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1509 ; 0.126 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10720 ; 0.010 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1893 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6134 ; 3.760 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2449 ; 1.535 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9982 ; 5.198 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3745 ; 7.340 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3417 ; 9.297 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 431 A 533 REMARK 3 ORIGIN FOR THE GROUP (A): 47.1401 40.3999 -6.3344 REMARK 3 T TENSOR REMARK 3 T11: 0.1644 T22: 0.0928 REMARK 3 T33: 0.0498 T12: 0.0260 REMARK 3 T13: -0.0076 T23: 0.0021 REMARK 3 L TENSOR REMARK 3 L11: 0.5756 L22: 0.2765 REMARK 3 L33: 1.3628 L12: -0.3849 REMARK 3 L13: -0.0549 L23: 0.1699 REMARK 3 S TENSOR REMARK 3 S11: -0.0086 S12: -0.0127 S13: 0.0153 REMARK 3 S21: 0.0472 S22: 0.0446 S23: -0.0006 REMARK 3 S31: 0.3160 S32: 0.1176 S33: -0.0360 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 534 A 701 REMARK 3 ORIGIN FOR THE GROUP (A): 71.6880 49.8452 16.4967 REMARK 3 T TENSOR REMARK 3 T11: 0.0535 T22: 0.1912 REMARK 3 T33: 0.0948 T12: 0.0272 REMARK 3 T13: -0.0712 T23: -0.0367 REMARK 3 L TENSOR REMARK 3 L11: 6.2909 L22: 0.1040 REMARK 3 L33: 2.1677 L12: -0.7761 REMARK 3 L13: 3.6901 L23: -0.4523 REMARK 3 S TENSOR REMARK 3 S11: -0.1661 S12: 0.2046 S13: 0.2064 REMARK 3 S21: 0.0294 S22: 0.0249 S23: -0.0354 REMARK 3 S31: -0.1107 S32: 0.1343 S33: 0.1413 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 430 B 533 REMARK 3 ORIGIN FOR THE GROUP (A): 40.4948 69.7290 5.7121 REMARK 3 T TENSOR REMARK 3 T11: 0.2051 T22: 0.0489 REMARK 3 T33: 0.0585 T12: 0.0396 REMARK 3 T13: 0.0163 T23: -0.0011 REMARK 3 L TENSOR REMARK 3 L11: 0.3086 L22: 0.8811 REMARK 3 L33: 1.3373 L12: 0.5091 REMARK 3 L13: -0.1572 L23: -0.0984 REMARK 3 S TENSOR REMARK 3 S11: 0.0277 S12: 0.0158 S13: 0.0148 REMARK 3 S21: 0.0094 S22: 0.0142 S23: 0.0545 REMARK 3 S31: -0.3762 S32: -0.0600 S33: -0.0418 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 534 B 1001 REMARK 3 ORIGIN FOR THE GROUP (A): 66.6445 70.8737 -17.5072 REMARK 3 T TENSOR REMARK 3 T11: 0.3189 T22: 0.1063 REMARK 3 T33: 0.0934 T12: -0.0579 REMARK 3 T13: 0.1447 T23: 0.0085 REMARK 3 L TENSOR REMARK 3 L11: 7.8527 L22: 3.2828 REMARK 3 L33: 4.2211 L12: 5.0629 REMARK 3 L13: -5.6470 L23: -3.5866 REMARK 3 S TENSOR REMARK 3 S11: -0.2508 S12: 0.1700 S13: -0.3972 REMARK 3 S21: -0.2202 S22: 0.0877 S23: -0.2930 REMARK 3 S31: -0.0185 S32: -0.1563 S33: 0.1630 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 3 C 119 REMARK 3 ORIGIN FOR THE GROUP (A): 42.1843 51.5662 -31.9768 REMARK 3 T TENSOR REMARK 3 T11: 0.0536 T22: 0.0976 REMARK 3 T33: 0.0616 T12: 0.0031 REMARK 3 T13: -0.0079 T23: 0.0100 REMARK 3 L TENSOR REMARK 3 L11: 0.1904 L22: 0.4135 REMARK 3 L33: 1.9338 L12: 0.0514 REMARK 3 L13: -0.0007 L23: -0.1413 REMARK 3 S TENSOR REMARK 3 S11: 0.0062 S12: -0.0466 S13: -0.0247 REMARK 3 S21: -0.0932 S22: 0.0125 S23: 0.0159 REMARK 3 S31: 0.0022 S32: 0.0670 S33: -0.0188 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 120 C 222 REMARK 3 ORIGIN FOR THE GROUP (A): 44.0877 79.6554 -47.4473 REMARK 3 T TENSOR REMARK 3 T11: 0.0831 T22: 0.0680 REMARK 3 T33: 0.0975 T12: -0.0033 REMARK 3 T13: -0.0303 T23: 0.0279 REMARK 3 L TENSOR REMARK 3 L11: 0.1057 L22: 2.0165 REMARK 3 L33: 0.3970 L12: 0.4594 REMARK 3 L13: -0.0099 L23: -0.0964 REMARK 3 S TENSOR REMARK 3 S11: 0.0039 S12: -0.0165 S13: -0.0156 REMARK 3 S21: 0.0468 S22: -0.0975 S23: -0.1045 REMARK 3 S31: 0.0307 S32: 0.0743 S33: 0.0936 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 3 D 119 REMARK 3 ORIGIN FOR THE GROUP (A): 41.7388 56.3095 31.0013 REMARK 3 T TENSOR REMARK 3 T11: 0.1469 T22: 0.0744 REMARK 3 T33: 0.0490 T12: 0.0120 REMARK 3 T13: 0.0184 T23: -0.0028 REMARK 3 L TENSOR REMARK 3 L11: 0.1233 L22: 0.7446 REMARK 3 L33: 1.4736 L12: 0.2930 REMARK 3 L13: -0.0443 L23: -0.2435 REMARK 3 S TENSOR REMARK 3 S11: 0.0397 S12: 0.0335 S13: -0.0095 REMARK 3 S21: 0.1682 S22: 0.0382 S23: -0.0007 REMARK 3 S31: -0.1566 S32: -0.0604 S33: -0.0779 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 120 D 221 REMARK 3 ORIGIN FOR THE GROUP (A): 53.7546 31.6742 45.9256 REMARK 3 T TENSOR REMARK 3 T11: 0.0780 T22: 0.0779 REMARK 3 T33: 0.1462 T12: -0.0549 REMARK 3 T13: -0.0105 T23: 0.0736 REMARK 3 L TENSOR REMARK 3 L11: 0.1016 L22: 2.6376 REMARK 3 L33: 1.6223 L12: -0.4434 REMARK 3 L13: -0.2459 L23: 0.2906 REMARK 3 S TENSOR REMARK 3 S11: 0.0320 S12: 0.0033 S13: 0.0001 REMARK 3 S21: -0.0564 S22: -0.2219 S23: -0.2560 REMARK 3 S31: -0.2461 S32: 0.2075 S33: 0.1898 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 4 E 106 REMARK 3 ORIGIN FOR THE GROUP (A): 30.6998 64.2918 -18.2720 REMARK 3 T TENSOR REMARK 3 T11: 0.0877 T22: 0.1446 REMARK 3 T33: 0.0731 T12: 0.0577 REMARK 3 T13: 0.0055 T23: 0.0204 REMARK 3 L TENSOR REMARK 3 L11: 0.0397 L22: 1.2691 REMARK 3 L33: 0.9642 L12: -0.1238 REMARK 3 L13: 0.1590 L23: -0.3101 REMARK 3 S TENSOR REMARK 3 S11: -0.0404 S12: -0.0395 S13: -0.0313 REMARK 3 S21: 0.0866 S22: 0.0835 S23: 0.0082 REMARK 3 S31: -0.2556 S32: -0.2655 S33: -0.0431 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 107 E 216 REMARK 3 ORIGIN FOR THE GROUP (A): 30.2803 86.3012 -48.7786 REMARK 3 T TENSOR REMARK 3 T11: 0.1881 T22: 0.0615 REMARK 3 T33: 0.0747 T12: -0.0205 REMARK 3 T13: -0.0660 T23: 0.0510 REMARK 3 L TENSOR REMARK 3 L11: 0.2365 L22: 0.6937 REMARK 3 L33: 1.6005 L12: -0.1097 REMARK 3 L13: -0.2214 L23: -0.7047 REMARK 3 S TENSOR REMARK 3 S11: -0.1806 S12: 0.0221 S13: 0.0580 REMARK 3 S21: 0.1303 S22: 0.1236 S23: -0.0116 REMARK 3 S31: -0.0069 S32: -0.1027 S33: 0.0570 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 4 F 106 REMARK 3 ORIGIN FOR THE GROUP (A): 36.0080 40.1922 17.3735 REMARK 3 T TENSOR REMARK 3 T11: 0.0742 T22: 0.0994 REMARK 3 T33: 0.0674 T12: -0.0255 REMARK 3 T13: -0.0013 T23: 0.0114 REMARK 3 L TENSOR REMARK 3 L11: 0.0442 L22: 1.7518 REMARK 3 L33: 1.0009 L12: -0.2698 REMARK 3 L13: 0.0614 L23: -0.5981 REMARK 3 S TENSOR REMARK 3 S11: 0.0021 S12: -0.0115 S13: 0.0040 REMARK 3 S21: -0.0938 S22: 0.0738 S23: 0.0341 REMARK 3 S31: 0.1854 S32: -0.1760 S33: -0.0759 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 107 F 216 REMARK 3 ORIGIN FOR THE GROUP (A): 43.5243 19.5911 47.5619 REMARK 3 T TENSOR REMARK 3 T11: 0.1345 T22: 0.0408 REMARK 3 T33: 0.0734 T12: 0.0186 REMARK 3 T13: 0.0124 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 0.0953 L22: 1.0711 REMARK 3 L33: 1.8592 L12: 0.0987 REMARK 3 L13: 0.3013 L23: -0.6128 REMARK 3 S TENSOR REMARK 3 S11: -0.0302 S12: -0.0170 S13: -0.0138 REMARK 3 S21: -0.0308 S22: -0.0008 S23: -0.0638 REMARK 3 S31: -0.0408 S32: -0.0540 S33: 0.0310 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS; U VALUES: WITH TLS ADDED REMARK 4 REMARK 4 3V6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-12. REMARK 100 THE RCSB ID CODE IS RCSB069662. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-APR-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127050 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 49.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07400 REMARK 200 R SYM (I) : 0.07400 REMARK 200 FOR THE DATA SET : 15.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.55600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG-4000, PH 4.6, REMARK 280 VAPOR DIFFUSION, TEMPERATURE 281K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-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 44.90700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.64050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.41450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.64050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.90700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.41450 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29270 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ILE A 428 REMARK 465 ASP A 429 REMARK 465 VAL A 430 REMARK 465 SER A 452 REMARK 465 THR A 453 REMARK 465 ILE A 454 REMARK 465 GLN A 455 REMARK 465 SER A 456 REMARK 465 LEU A 457 REMARK 465 ALA A 458 REMARK 465 GLU A 459 REMARK 465 HIS A 517 REMARK 465 SER A 518 REMARK 465 LEU A 519 REMARK 465 GLU A 559 REMARK 465 LYS A 560 REMARK 465 PRO A 561 REMARK 465 VAL A 562 REMARK 465 PHE A 563 REMARK 465 PRO A 564 REMARK 465 GLU A 565 REMARK 465 ASN A 566 REMARK 465 ALA A 591 REMARK 465 LYS A 592 REMARK 465 SER A 593 REMARK 465 ILE B 428 REMARK 465 ASP B 429 REMARK 465 ILE B 454 REMARK 465 GLN B 455 REMARK 465 SER B 456 REMARK 465 LEU B 457 REMARK 465 ALA B 458 REMARK 465 GLU B 459 REMARK 465 LYS B 560 REMARK 465 PRO B 561 REMARK 465 VAL B 562 REMARK 465 PHE B 563 REMARK 465 PRO B 564 REMARK 465 GLU B 565 REMARK 465 TYR B 589 REMARK 465 ASP B 590 REMARK 465 ALA B 591 REMARK 465 LYS B 592 REMARK 465 SER B 593 REMARK 465 LYS B 594 REMARK 465 VAL B 997 REMARK 465 VAL B 998 REMARK 465 ALA C 2 REMARK 465 ALA D 2 REMARK 465 ALA D 136 REMARK 465 GLN D 137 REMARK 465 THR D 138 REMARK 465 ASN D 139 REMARK 465 THR D 222 REMARK 465 ALA E 2 REMARK 465 GLU E 3 REMARK 465 ALA F 2 REMARK 465 GLU F 3 REMARK 465 SER F 9 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 VAL B 430 CG1 CG2 REMARK 470 GLU C 3 CG CD OE1 OE2 REMARK 470 THR C 222 CA C O CB OG1 CG2 REMARK 470 GLU D 3 CG CD OE1 OE2 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 DISTANCE REMARK 500 O HOH B 1184 O HOH C 556 2.17 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 CYS B 498 CB CYS B 498 SG 0.107 REMARK 500 GLU C 83 CG GLU C 83 CD 0.094 REMARK 500 CYS C 97 CB CYS C 97 SG -0.130 REMARK 500 CYS C 146 CB CYS C 146 SG -0.108 REMARK 500 CYS C 201 CB CYS C 201 SG -0.118 REMARK 500 CYS E 196 CB CYS E 196 SG -0.108 REMARK 500 CYS F 196 CB CYS F 196 SG -0.099 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 C 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 MET C 84 CG - SD - CE ANGL. DEV. = -9.8 DEGREES REMARK 500 CYS E 25 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 ARG E 32 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 MET E 177 CG - SD - CE ANGL. DEV. = -13.0 DEGREES REMARK 500 CYS F 25 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 ARG F 32 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG F 56 NE - CZ - NH2 ANGL. DEV. = -3.2 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 LEU A 471 -126.80 -119.30 REMARK 500 TYR A 472 -141.40 -110.58 REMARK 500 LYS A 579 -103.14 178.44 REMARK 500 SER B 452 -44.28 -25.93 REMARK 500 LEU B 471 -130.83 -123.24 REMARK 500 TYR B 472 -139.48 -107.37 REMARK 500 SER B 518 -126.05 47.24 REMARK 500 LEU B 519 52.94 -113.99 REMARK 500 SER C 17 -3.90 76.12 REMARK 500 SER C 166 -34.22 -130.18 REMARK 500 SER C 178 62.91 74.30 REMARK 500 ASP C 179 13.31 57.52 REMARK 500 SER D 17 -6.65 74.25 REMARK 500 SER D 86 70.56 50.91 REMARK 500 SER D 134 93.55 -65.44 REMARK 500 ASN D 161 56.74 36.11 REMARK 500 SER D 162 27.28 49.97 REMARK 500 ASP D 179 21.60 48.91 REMARK 500 ARG E 32 -116.16 56.52 REMARK 500 ALA E 53 -32.28 71.83 REMARK 500 ARG F 32 -122.86 58.52 REMARK 500 ALA F 53 -33.29 70.33 REMARK 500 SER F 173 18.79 59.75 REMARK 500 ASN F 214 68.54 -68.95 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 LYS A 579 GLU A 580 144.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ILE B 551 24.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 305 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER C 191 O REMARK 620 2 TRP C 194 O 87.4 REMARK 620 3 HOH C 555 O 86.0 81.9 REMARK 620 4 HOH C 554 O 91.1 103.3 174.0 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS A 701 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 705 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 706 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 707 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 708 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 709 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS B 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1004 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1005 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1006 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 309