REMARK 2 REMARK 2 RESOLUTION. 2.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 3 NUMBER OF REFLECTIONS : 110627 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) : 0.209 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 5547 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 : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.56 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7385 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2169 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7008 REMARK 3 BIN R VALUE (WORKING SET) : 0.2143 REMARK 3 BIN FREE R VALUE : 0.2647 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 377 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 : 20129 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 70 REMARK 3 SOLVENT ATOMS : 431 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 54.99 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.16 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.09700 REMARK 3 B22 (A**2) : 0.85890 REMARK 3 B33 (A**2) : 1.23810 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -4.12920 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.41 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 20755 ; 2.000 ; NULL REMARK 3 BOND ANGLES : 28336 ; 2.000 ; NULL REMARK 3 TORSION ANGLES : 6558 ; 2.000 ; NULL REMARK 3 TRIGONAL CARBON PLANES : 387 ; 2.000 ; NULL REMARK 3 GENERAL PLANES : 3107 ; 5.000 ; NULL REMARK 3 ISOTROPIC THERMAL FACTORS : 20755 ; 20.000 ; NULL REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 2748 ; 5.000 ; NULL REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 21524 ; 4.000 ; NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.25 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.21 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.47 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: A 505 A 505 REMARK 3 ORIGIN FOR THE GROUP (A): 2.4375 -5.4760 78.2172 REMARK 3 T TENSOR REMARK 3 T11: -0.2038 T22: -0.0740 REMARK 3 T33: 0.0481 T12: 0.0875 REMARK 3 T13: 0.0028 T23: 0.0713 REMARK 3 L TENSOR REMARK 3 L11: 0.5306 L22: 3.8680 REMARK 3 L33: 0.8685 L12: 0.7032 REMARK 3 L13: 0.4568 L23: -1.2508 REMARK 3 S TENSOR REMARK 3 S11: -0.0136 S12: 0.4041 S13: -0.0735 REMARK 3 S21: -0.2764 S22: 0.3049 S23: 0.5682 REMARK 3 S31: -0.0316 S32: -0.2664 S33: -0.2913 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: B 1 B 239 REMARK 3 ORIGIN FOR THE GROUP (A): 17.0404 -8.0825 85.1011 REMARK 3 T TENSOR REMARK 3 T11: -0.1715 T22: -0.0202 REMARK 3 T33: -0.0866 T12: 0.0103 REMARK 3 T13: -0.0069 T23: -0.0513 REMARK 3 L TENSOR REMARK 3 L11: 0.2332 L22: 7.4128 REMARK 3 L33: 1.2569 L12: 0.3487 REMARK 3 L13: 0.0480 L23: -3.0936 REMARK 3 S TENSOR REMARK 3 S11: 0.0626 S12: 0.1217 S13: -0.4625 REMARK 3 S21: 0.2331 S22: -0.1627 S23: -0.3913 REMARK 3 S31: 0.2690 S32: 0.1192 S33: 0.1001 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: C 505 C 506 REMARK 3 ORIGIN FOR THE GROUP (A): -8.7877 22.5523 51.3891 REMARK 3 T TENSOR REMARK 3 T11: 0.0319 T22: -0.1724 REMARK 3 T33: -0.1515 T12: -0.1543 REMARK 3 T13: 0.1126 T23: -0.0308 REMARK 3 L TENSOR REMARK 3 L11: 1.2290 L22: 1.1306 REMARK 3 L33: 4.4062 L12: -0.0697 REMARK 3 L13: -0.2547 L23: 0.3006 REMARK 3 S TENSOR REMARK 3 S11: -0.2324 S12: 0.3612 S13: -0.2559 REMARK 3 S21: -0.7133 S22: 0.3301 S23: -0.5792 REMARK 3 S31: -0.5113 S32: -0.0260 S33: -0.0977 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: D 1 D 239 REMARK 3 ORIGIN FOR THE GROUP (A): -23.9980 28.9464 48.9179 REMARK 3 T TENSOR REMARK 3 T11: 0.0350 T22: -0.2112 REMARK 3 T33: -0.3069 T12: -0.0730 REMARK 3 T13: -0.0171 T23: -0.0027 REMARK 3 L TENSOR REMARK 3 L11: 1.3227 L22: 0.9276 REMARK 3 L33: 6.3038 L12: -0.7280 REMARK 3 L13: 0.8134 L23: -0.9850 REMARK 3 S TENSOR REMARK 3 S11: -0.0479 S12: 0.2608 S13: 0.1161 REMARK 3 S21: -0.4978 S22: 0.1286 S23: -0.1197 REMARK 3 S31: -0.8096 S32: -0.3838 S33: -0.0807 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: E 3 E 213 REMARK 3 ORIGIN FOR THE GROUP (A): 21.3742 6.9602 15.4766 REMARK 3 T TENSOR REMARK 3 T11: 0.5672 T22: -0.3054 REMARK 3 T33: -0.2971 T12: -0.0329 REMARK 3 T13: -0.0311 T23: -0.0301 REMARK 3 L TENSOR REMARK 3 L11: 0.5989 L22: 0.6148 REMARK 3 L33: 1.6810 L12: -0.5405 REMARK 3 L13: -0.8512 L23: 0.4062 REMARK 3 S TENSOR REMARK 3 S11: -0.1721 S12: -0.0236 S13: -0.2012 REMARK 3 S21: -0.2668 S22: -0.0184 S23: 0.1053 REMARK 3 S31: -0.0925 S32: -0.2286 S33: 0.1905 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: F 1 F 238 REMARK 3 ORIGIN FOR THE GROUP (A): 22.1935 -6.8065 21.2707 REMARK 3 T TENSOR REMARK 3 T11: 0.6695 T22: -0.4610 REMARK 3 T33: -0.3597 T12: -0.0957 REMARK 3 T13: 0.0504 T23: -0.0275 REMARK 3 L TENSOR REMARK 3 L11: 1.6826 L22: 0.9993 REMARK 3 L33: 3.8018 L12: -0.6894 REMARK 3 L13: -1.6909 L23: 0.1949 REMARK 3 S TENSOR REMARK 3 S11: -0.3322 S12: -0.2024 S13: -0.1286 REMARK 3 S21: 0.1638 S22: 0.1289 S23: 0.1739 REMARK 3 S31: 0.3686 S32: -0.0662 S33: 0.2032 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: G 2 G 213 REMARK 3 ORIGIN FOR THE GROUP (A): 66.9400 -5.4646 78.8636 REMARK 3 T TENSOR REMARK 3 T11: -0.1291 T22: -0.0796 REMARK 3 T33: -0.1242 T12: 0.1126 REMARK 3 T13: -0.0100 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 0.6608 L22: 3.4988 REMARK 3 L33: 1.1232 L12: 0.4091 REMARK 3 L13: 0.0608 L23: -1.1907 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: 0.3312 S13: -0.0879 REMARK 3 S21: -0.0260 S22: 0.2315 S23: 0.2976 REMARK 3 S31: -0.0418 S32: -0.3160 S33: -0.2315 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: H 1 H 239 REMARK 3 ORIGIN FOR THE GROUP (A): 81.6913 -8.0405 85.3118 REMARK 3 T TENSOR REMARK 3 T11: -0.1092 T22: -0.0732 REMARK 3 T33: -0.1216 T12: 0.0420 REMARK 3 T13: 0.0015 T23: -0.0446 REMARK 3 L TENSOR REMARK 3 L11: 0.1291 L22: 6.7982 REMARK 3 L33: 1.2503 L12: -0.3566 REMARK 3 L13: 0.3518 L23: -2.8783 REMARK 3 S TENSOR REMARK 3 S11: 0.0792 S12: 0.0982 S13: -0.3078 REMARK 3 S21: 0.1983 S22: -0.2758 S23: -0.3838 REMARK 3 S31: 0.2203 S32: 0.1869 S33: 0.1966 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: I 505 I 506 REMARK 3 ORIGIN FOR THE GROUP (A): 56.2847 22.4127 52.0197 REMARK 3 T TENSOR REMARK 3 T11: -0.0772 T22: -0.2144 REMARK 3 T33: -0.1836 T12: -0.0041 REMARK 3 T13: -0.0101 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 0.9476 L22: 1.2303 REMARK 3 L33: 3.6616 L12: -0.0394 REMARK 3 L13: -0.6355 L23: -0.9837 REMARK 3 S TENSOR REMARK 3 S11: -0.0434 S12: 0.0748 S13: -0.0370 REMARK 3 S21: -0.2825 S22: -0.0164 S23: -0.1212 REMARK 3 S31: -0.0169 S32: -0.1831 S33: 0.0598 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: J 1 J 239 REMARK 3 ORIGIN FOR THE GROUP (A): 41.7092 28.7453 49.0009 REMARK 3 T TENSOR REMARK 3 T11: -0.0029 T22: -0.1890 REMARK 3 T33: -0.2437 T12: 0.0239 REMARK 3 T13: 0.0156 T23: -0.0607 REMARK 3 L TENSOR REMARK 3 L11: 0.9164 L22: 0.9105 REMARK 3 L33: 5.3464 L12: -0.4635 REMARK 3 L13: 0.6757 L23: -1.5596 REMARK 3 S TENSOR REMARK 3 S11: -0.0188 S12: 0.0533 S13: 0.2963 REMARK 3 S21: -0.3536 S22: 0.0438 S23: -0.0093 REMARK 3 S31: -0.3388 S32: -0.5472 S33: -0.0250 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: K 3 K 213 REMARK 3 ORIGIN FOR THE GROUP (A): 83.5459 6.9815 15.8096 REMARK 3 T TENSOR REMARK 3 T11: 0.4866 T22: -0.2903 REMARK 3 T33: -0.2835 T12: -0.0348 REMARK 3 T13: -0.0129 T23: -0.0164 REMARK 3 L TENSOR REMARK 3 L11: 0.7679 L22: 0.6761 REMARK 3 L33: 1.5902 L12: -0.4726 REMARK 3 L13: -1.4537 L23: 0.0135 REMARK 3 S TENSOR REMARK 3 S11: -0.0824 S12: 0.0036 S13: -0.1539 REMARK 3 S21: -0.1454 S22: -0.0543 S23: 0.0537 REMARK 3 S31: 0.0608 S32: -0.1665 S33: 0.1366 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: L 1 L 238 REMARK 3 ORIGIN FOR THE GROUP (A): 84.6857 -6.8023 21.7007 REMARK 3 T TENSOR REMARK 3 T11: 0.5837 T22: -0.3936 REMARK 3 T33: -0.3080 T12: -0.0210 REMARK 3 T13: 0.0318 T23: 0.0273 REMARK 3 L TENSOR REMARK 3 L11: 1.5686 L22: 0.4156 REMARK 3 L33: 3.0297 L12: -0.5026 REMARK 3 L13: -1.9741 L23: 0.3858 REMARK 3 S TENSOR REMARK 3 S11: -0.1818 S12: -0.0630 S13: -0.1179 REMARK 3 S21: -0.0194 S22: 0.0192 S23: 0.1155 REMARK 3 S31: 0.2901 S32: -0.0028 S33: 0.1626 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3MUG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-10. REMARK 100 THE RCSB ID CODE IS RCSB059007. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110752 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490 REMARK 200 RESOLUTION RANGE LOW (A) : 24.970 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09700 REMARK 200 FOR THE DATA SET : 7.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.50700 REMARK 200 FOR SHELL : 2.400 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: PDB ENTRY 7FAB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 400, 0.08M SODIUM CHLORIDE, REMARK 280 0.1M CHES, PH 9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.12500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 PCA A 1 REMARK 465 GLU A 213 REMARK 465 CYS A 214 REMARK 465 SER A 215 REMARK 465 CYS B 233 REMARK 465 ASP B 234 REMARK 465 PCA C 1 REMARK 465 GLU C 213 REMARK 465 CYS C 214 REMARK 465 SER C 215 REMARK 465 CYS D 233 REMARK 465 ASP D 234 REMARK 465 PCA E 1 REMARK 465 SER E 2 REMARK 465 GLU E 213 REMARK 465 CYS E 214 REMARK 465 SER E 215 REMARK 465 SER F 229 REMARK 465 CYS F 230 REMARK 465 ASP F 231 REMARK 465 PCA G 1 REMARK 465 GLU G 213 REMARK 465 CYS G 214 REMARK 465 SER G 215 REMARK 465 CYS H 233 REMARK 465 ASP H 234 REMARK 465 GLU I 213 REMARK 465 CYS I 214 REMARK 465 SER I 215 REMARK 465 CYS J 233 REMARK 465 ASP J 234 REMARK 465 PCA K 1 REMARK 465 SER K 2 REMARK 465 CYS K 214 REMARK 465 SER K 215 REMARK 465 SER L 229 REMARK 465 CYS L 230 REMARK 465 ASP L 231 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 LYS A 45 CG CD CE NZ REMARK 470 LYS A 190 CG CD CE NZ REMARK 470 TRP B 64 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 64 CZ3 CH2 REMARK 470 VAL B 67 CG1 CG2 REMARK 470 LYS B 83 CG CD CE NZ REMARK 470 VAL B 84 CG1 CG2 REMARK 470 LYS B 105 CG CD CE NZ REMARK 470 LYS B 129 CG CD CE NZ REMARK 470 SER B 134 OG REMARK 470 LYS B 213 CG CD CE NZ REMARK 470 LYS B 218 CG CD CE NZ REMARK 470 LYS B 228 CG CD CE NZ REMARK 470 LYS C 42 CG CD CE NZ REMARK 470 LYS C 45 CG CD CE NZ REMARK 470 LYS C 103 CG CD CE NZ REMARK 470 LYS C 190 CG CD CE NZ REMARK 470 LYS D 83 CG CD CE NZ REMARK 470 VAL D 84 CG1 CG2 REMARK 470 LYS D 105 CG CD CE NZ REMARK 470 LYS D 129 CG CD CE NZ REMARK 470 SER D 134 OG REMARK 470 LYS D 213 CG CD CE NZ REMARK 470 LYS D 218 CG CD CE NZ REMARK 470 LYS D 228 CG CD CE NZ REMARK 470 LYS E 190 CG CD CE NZ REMARK 470 TRP F 64 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 64 CZ3 CH2 REMARK 470 LYS F 75 CG CD CE NZ REMARK 470 LYS F 83 CG CD CE NZ REMARK 470 LYS F 105 CG CD CE NZ REMARK 470 SER F 127 OG REMARK 470 SER F 128 OG REMARK 470 SER F 130 OG REMARK 470 SER F 134 OG REMARK 470 THR F 137 OG1 CG2 REMARK 470 LYS F 228 CG CD CE NZ REMARK 470 LYS G 190 CG CD CE NZ REMARK 470 TRP H 64 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 64 CZ3 CH2 REMARK 470 VAL H 67 CG1 CG2 REMARK 470 LYS H 83 CG CD CE NZ REMARK 470 VAL H 84 CG1 CG2 REMARK 470 LYS H 105 CG CD CE NZ REMARK 470 SER H 134 OG REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 LYS H 228 CG CD CE NZ REMARK 470 LYS I 42 CG CD CE NZ REMARK 470 LYS I 190 CG CD CE NZ REMARK 470 LYS J 83 CG CD CE NZ REMARK 470 VAL J 84 CG1 CG2 REMARK 470 LYS J 105 CG CD CE NZ REMARK 470 LYS J 129 CG CD CE NZ REMARK 470 SER J 134 OG REMARK 470 LYS J 213 CG CD CE NZ REMARK 470 LYS J 218 CG CD CE NZ REMARK 470 LYS J 228 CG CD CE NZ REMARK 470 LYS K 190 CG CD CE NZ REMARK 470 GLU K 213 CG CD OE1 OE2 REMARK 470 TRP L 64 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP L 64 CZ3 CH2 REMARK 470 GLN L 81 CG CD OE1 NE2 REMARK 470 LYS L 83 CG CD CE NZ REMARK 470 LYS L 105 CG CD CE NZ REMARK 470 SER L 127 OG REMARK 470 SER L 128 OG REMARK 470 LYS L 129 CG CD CE NZ REMARK 470 SER L 130 OG REMARK 470 SER L 134 OG REMARK 470 THR L 137 OG1 CG2 REMARK 470 GLN L 203 CG CD OE1 NE2 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 ASP A 27B -93.59 -141.77 REMARK 500 ASP A 31 54.02 -100.02 REMARK 500 VAL A 51 -64.40 73.00 REMARK 500 ASP A 151 -112.59 67.60 REMARK 500 GLN A 167 42.76 -99.29 REMARK 500 SER A 168 -47.50 73.69 REMARK 500 ASN A 171 -4.75 67.01 REMARK 500 SER B 82B 82.67 33.01 REMARK 500 ASP B 100L 15.77 55.38 REMARK 500 SER B 134 61.29 -104.87 REMARK 500 ALA C 3 171.95 -59.95 REMARK 500 ASP C 27B -80.62 -136.64 REMARK 500 PHE C 30 -159.14 -81.98 REMARK 500 ASP C 31 29.89 -151.99 REMARK 500 SER C 32 65.98 -112.22 REMARK 500 VAL C 51 -66.84 72.58 REMARK 500 SER C 95 20.77 80.46 REMARK 500 ASP C 151 -110.75 65.40 REMARK 500 GLN C 167 45.21 -104.80 REMARK 500 SER C 168 -35.05 70.36 REMARK 500 ASN C 170 33.59 -97.29 REMARK 500 ASN C 171 -20.21 60.90 REMARK 500 VAL D 48 -60.94 -102.55 REMARK 500 SER D 82B 81.84 25.24 REMARK 500 GLU D 150 -58.90 -29.36 REMARK 500 ASP E 27B -93.95 -141.14 REMARK 500 ASP E 31 53.38 -101.57 REMARK 500 VAL E 51 -65.16 73.10 REMARK 500 ASP E 151 -110.61 65.28 REMARK 500 SER F 82B 82.48 61.53 REMARK 500 ASN F 100K 34.73 72.82 REMARK 500 PHE F 148 -77.20 -98.35 REMARK 500 ASP G 27B -93.34 -141.69 REMARK 500 ASP G 31 53.94 -99.40 REMARK 500 VAL G 51 -63.82 72.61 REMARK 500 ASP G 151 -116.63 70.82 REMARK 500 GLN G 167 61.93 -111.14 REMARK 500 SER G 168 -47.57 61.38 REMARK 500 ASN G 171 -6.55 67.15 REMARK 500 SER H 82B 83.08 33.17 REMARK 500 ASP H 146 70.17 41.57 REMARK 500 ASP I 27B -94.54 -143.38 REMARK 500 ASP I 31 51.30 -99.41 REMARK 500 VAL I 51 -66.02 74.67 REMARK 500 ASP I 151 -110.49 64.59 REMARK 500 SER I 168 -52.01 67.99 REMARK 500 ASN I 170 49.80 -80.90 REMARK 500 ASN I 171 -14.10 37.86 REMARK 500 SER J 82B 81.18 33.29 REMARK 500 ASP J 100L 13.93 59.15 REMARK 500 REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS. 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 GLU B 150 22.3 L L OUTSIDE RANGE REMARK 500 GLU D 150 22.1 L L OUTSIDE RANGE REMARK 500 THR E 145 23.0 L L OUTSIDE RANGE REMARK 500 PHE F 148 20.4 L L OUTSIDE RANGE REMARK 500 GLU F 150 24.5 L L OUTSIDE RANGE REMARK 500 LEU F 198 24.7 L L OUTSIDE RANGE REMARK 500 ILE G 80 24.9 L L OUTSIDE RANGE REMARK 500 ASN G 171 24.9 L L OUTSIDE RANGE REMARK 500 HIS H 100R 24.3 L L OUTSIDE RANGE REMARK 500 THR H 108 24.3 L L OUTSIDE RANGE REMARK 500 GLU H 150 22.9 L L OUTSIDE RANGE REMARK 500 THR I 5 24.7 L L OUTSIDE RANGE REMARK 500 ASN I 171 23.8 L L OUTSIDE RANGE REMARK 500 GLU J 150 21.6 L L OUTSIDE RANGE REMARK 500 THR K 18 24.9 L L OUTSIDE RANGE REMARK 500 ASN K 171 24.5 L L OUTSIDE RANGE REMARK 500 ASN L 100K 23.9 L L OUTSIDE RANGE REMARK 500 THR L 108 25.0 L L OUTSIDE RANGE REMARK 500 ALA L 114 21.9 L L OUTSIDE RANGE REMARK 500 PHE L 148 19.4 L L OUTSIDE RANGE REMARK 500 GLU L 150 23.5 L L OUTSIDE RANGE REMARK 500 LEU L 198 23.5 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 626 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH L 640 DISTANCE = 5.40 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3MUH RELATED DB: PDB