REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 37098 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) : 0.190 REMARK 3 R VALUE (WORKING SET) : 0.187 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1947 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) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2345 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.37 REMARK 3 BIN R VALUE (WORKING SET) : 0.2650 REMARK 3 BIN FREE R VALUE SET COUNT : 135 REMARK 3 BIN FREE R VALUE : 0.3640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6603 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 6 REMARK 3 SOLVENT ATOMS : 367 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.91 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.32000 REMARK 3 B22 (A**2) : -0.18000 REMARK 3 B33 (A**2) : -1.51000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.82000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.384 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.251 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.185 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.973 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6779 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4517 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9238 ; 1.061 ; 1.952 REMARK 3 BOND ANGLES OTHERS (DEGREES): 11060 ; 0.766 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 853 ; 5.870 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 264 ;35.580 ;24.394 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1085 ;13.755 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.290 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1030 ; 0.062 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7499 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1313 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1069 ; 0.175 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4416 ; 0.186 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3129 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3577 ; 0.082 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 274 ; 0.140 ; 0.200 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): 34 ; 0.140 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 78 ; 0.170 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.143 ; 0.200 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): 5473 ; 3.352 ; 4.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1719 ; 0.839 ; 4.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6955 ; 4.297 ; 6.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3022 ; 5.270 ; 6.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2283 ; 7.107 ;10.000 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 : 4 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 3 A 93 5 REMARK 3 1 C 3 C 93 5 REMARK 3 2 A 99 A 107 5 REMARK 3 2 C 99 C 107 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 585 ; 0.16 ; 0.50 REMARK 3 LOOSE POSITIONAL 1 A (A): 682 ; 0.63 ; 5.00 REMARK 3 MEDIUM THERMAL 1 A (A**2): 585 ; 2.37 ; 20.00 REMARK 3 LOOSE THERMAL 1 A (A**2): 682 ; 3.32 ; 30.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 112 A 210 5 REMARK 3 1 C 112 C 210 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 A (A): 585 ; 0.18 ; 0.50 REMARK 3 LOOSE POSITIONAL 2 A (A): 698 ; 0.80 ; 5.00 REMARK 3 MEDIUM THERMAL 2 A (A**2): 585 ; 2.39 ; 20.00 REMARK 3 LOOSE THERMAL 2 A (A**2): 698 ; 3.79 ; 30.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : B D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 2 B 61 5 REMARK 3 1 D 2 D 61 5 REMARK 3 2 B 67 B 116 5 REMARK 3 2 D 67 D 116 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 B (A): 646 ; 0.17 ; 0.50 REMARK 3 LOOSE POSITIONAL 3 B (A): 813 ; 0.64 ; 5.00 REMARK 3 MEDIUM THERMAL 3 B (A**2): 646 ; 2.31 ; 20.00 REMARK 3 LOOSE THERMAL 3 B (A**2): 813 ; 3.30 ; 30.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : B D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 122 B 131 5 REMARK 3 1 D 122 D 131 5 REMARK 3 2 B 140 B 191 5 REMARK 3 2 D 140 D 191 5 REMARK 3 3 B 199 B 216 5 REMARK 3 3 D 199 D 216 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 4 B (A): 468 ; 0.14 ; 0.50 REMARK 3 LOOSE POSITIONAL 4 B (A): 500 ; 0.45 ; 5.00 REMARK 3 MEDIUM THERMAL 4 B (A**2): 468 ; 2.98 ; 20.00 REMARK 3 LOOSE THERMAL 4 B (A**2): 500 ; 2.88 ; 30.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 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 1 A 112 REMARK 3 ORIGIN FOR THE GROUP (A): -34.0703 -34.0703 -13.5987 REMARK 3 T TENSOR REMARK 3 T11: -0.1428 T22: -0.1201 REMARK 3 T33: -0.1311 T12: 0.0264 REMARK 3 T13: 0.0092 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 2.1519 L22: 1.8484 REMARK 3 L33: 5.7700 L12: -0.0587 REMARK 3 L13: 2.3527 L23: -1.4099 REMARK 3 S TENSOR REMARK 3 S11: 0.1477 S12: 0.1627 S13: -0.1395 REMARK 3 S21: 0.1322 S22: 0.0599 S23: 0.0928 REMARK 3 S31: 0.2444 S32: 0.1669 S33: -0.2077 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 113 A 217 REMARK 3 ORIGIN FOR THE GROUP (A): -18.5979 -18.5979 21.8864 REMARK 3 T TENSOR REMARK 3 T11: -0.1675 T22: -0.1526 REMARK 3 T33: -0.1140 T12: 0.0290 REMARK 3 T13: 0.0072 T23: -0.0097 REMARK 3 L TENSOR REMARK 3 L11: 1.5952 L22: 2.2118 REMARK 3 L33: 5.4393 L12: 0.9190 REMARK 3 L13: 1.5979 L23: 1.9351 REMARK 3 S TENSOR REMARK 3 S11: 0.2229 S12: -0.1117 S13: -0.1626 REMARK 3 S21: 0.0822 S22: -0.0763 S23: -0.0085 REMARK 3 S31: 0.3893 S32: -0.1213 S33: -0.1467 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 1 B 112 REMARK 3 ORIGIN FOR THE GROUP (A): -26.3690 -80.2680 -12.4260 REMARK 3 T TENSOR REMARK 3 T11: -0.1915 T22: -0.1047 REMARK 3 T33: -0.0840 T12: -0.0354 REMARK 3 T13: -0.0151 T23: 0.0438 REMARK 3 L TENSOR REMARK 3 L11: 1.1675 L22: 2.5559 REMARK 3 L33: 3.7428 L12: -0.1804 REMARK 3 L13: 0.5741 L23: -0.1581 REMARK 3 S TENSOR REMARK 3 S11: -0.0925 S12: 0.0731 S13: 0.0722 REMARK 3 S21: 0.0589 S22: -0.1215 S23: -0.2332 REMARK 3 S31: -0.1057 S32: 0.1657 S33: 0.2141 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 113 B 219 REMARK 3 ORIGIN FOR THE GROUP (A): -9.5070 -93.5510 11.2770 REMARK 3 T TENSOR REMARK 3 T11: -0.0718 T22: 0.0405 REMARK 3 T33: -0.1042 T12: -0.0392 REMARK 3 T13: 0.1280 T23: -0.0031 REMARK 3 L TENSOR REMARK 3 L11: 3.5878 L22: 7.3172 REMARK 3 L33: 4.2688 L12: -0.7146 REMARK 3 L13: 2.5101 L23: -2.3594 REMARK 3 S TENSOR REMARK 3 S11: -0.1472 S12: 0.3879 S13: -0.1035 REMARK 3 S21: -0.2833 S22: -0.1416 S23: -0.7579 REMARK 3 S31: -0.0755 S32: 0.6900 S33: 0.2888 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 1 C 112 REMARK 3 ORIGIN FOR THE GROUP (A): -37.5330 -75.7980 -41.2150 REMARK 3 T TENSOR REMARK 3 T11: -0.2077 T22: -0.0620 REMARK 3 T33: -0.1500 T12: -0.0199 REMARK 3 T13: -0.0028 T23: -0.0241 REMARK 3 L TENSOR REMARK 3 L11: 2.0804 L22: 2.2385 REMARK 3 L33: 5.2178 L12: 0.0111 REMARK 3 L13: 0.6639 L23: -1.0905 REMARK 3 S TENSOR REMARK 3 S11: -0.0521 S12: -0.0082 S13: 0.0431 REMARK 3 S21: 0.1136 S22: -0.0118 S23: 0.0384 REMARK 3 S31: -0.1859 S32: 0.2911 S33: 0.0639 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 113 C 215 REMARK 3 ORIGIN FOR THE GROUP (A): -58.2680 -66.9590 -70.1960 REMARK 3 T TENSOR REMARK 3 T11: -0.0825 T22: 0.0050 REMARK 3 T33: 0.0216 T12: 0.0940 REMARK 3 T13: -0.0151 T23: -0.0670 REMARK 3 L TENSOR REMARK 3 L11: 10.0091 L22: 2.0694 REMARK 3 L33: 7.1708 L12: 1.3155 REMARK 3 L13: 6.7810 L23: 0.8095 REMARK 3 S TENSOR REMARK 3 S11: -0.3418 S12: -0.9321 S13: 0.6497 REMARK 3 S21: 0.0352 S22: -0.1114 S23: 0.3333 REMARK 3 S31: -0.5876 S32: -0.7946 S33: 0.4531 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 1 D 112 REMARK 3 ORIGIN FOR THE GROUP (A): -44.8270 -96.6850 -44.0050 REMARK 3 T TENSOR REMARK 3 T11: -0.1075 T22: -0.1188 REMARK 3 T33: -0.1688 T12: -0.0404 REMARK 3 T13: 0.0579 T23: -0.0367 REMARK 3 L TENSOR REMARK 3 L11: 4.9185 L22: 2.4059 REMARK 3 L33: 3.0559 L12: 0.5688 REMARK 3 L13: 0.4165 L23: -0.7231 REMARK 3 S TENSOR REMARK 3 S11: -0.3418 S12: 0.2209 S13: -0.2533 REMARK 3 S21: -0.2086 S22: 0.2462 S23: -0.1335 REMARK 3 S31: 0.2119 S32: -0.0036 S33: 0.0956 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 113 D 220 REMARK 3 ORIGIN FOR THE GROUP (A): -50.8690 -80.3050 -75.7440 REMARK 3 T TENSOR REMARK 3 T11: -0.2102 T22: -0.0883 REMARK 3 T33: -0.1412 T12: 0.0267 REMARK 3 T13: 0.0198 T23: -0.0239 REMARK 3 L TENSOR REMARK 3 L11: 5.0567 L22: 4.7074 REMARK 3 L33: 2.5180 L12: 1.7361 REMARK 3 L13: 1.7259 L23: -0.4224 REMARK 3 S TENSOR REMARK 3 S11: 0.0366 S12: 0.2106 S13: 0.3156 REMARK 3 S21: -0.2663 S22: -0.0344 S23: 0.1649 REMARK 3 S31: 0.0795 S32: 0.0597 S33: -0.0022 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 3DGG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-08. REMARK 100 THE RCSB ID CODE IS RCSB048007. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39870 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.10100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : 0.64900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 32C2 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 5% V/V REMARK 280 ISOPROPANOL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: 3340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.8 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: 3450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLY B 133 REMARK 465 SER B 134 REMARK 465 ALA B 135 REMARK 465 ALA B 136 REMARK 465 GLN B 137 REMARK 465 THR B 138 REMARK 465 ASN B 139 REMARK 465 ASP B 220 REMARK 465 CYS B 221 REMARK 465 GLY B 222 REMARK 465 LYS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS B 229 REMARK 465 GLU C 216 REMARK 465 CYS C 217 REMARK 465 ALA D 135 REMARK 465 ALA D 136 REMARK 465 GLN D 137 REMARK 465 THR D 138 REMARK 465 ASN D 139 REMARK 465 CYS D 221 REMARK 465 GLY D 222 REMARK 465 LYS D 223 REMARK 465 HIS D 224 REMARK 465 HIS D 225 REMARK 465 HIS D 226 REMARK 465 HIS D 227 REMARK 465 HIS D 228 REMARK 465 HIS D 229 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 OD2 ASP B 100 O HOH B 249 2.12 REMARK 500 OD2 ASP D 100 O HOH D 508 2.14 REMARK 500 OE2 GLU B 154 O HOH B 237 2.18 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 ALA A 55 -46.25 75.19 REMARK 500 HIS A 80 116.67 -167.54 REMARK 500 SER A 95 -90.39 -109.39 REMARK 500 ARG A 96 -74.01 45.34 REMARK 500 GLU A 97 -73.20 -113.01 REMARK 500 ASP A 154 44.00 39.92 REMARK 500 ASN A 215 33.37 -87.22 REMARK 500 PRO B 41 120.72 -39.79 REMARK 500 SER B 166 -32.54 -37.88 REMARK 500 ALA C 55 -43.41 78.77 REMARK 500 GLU C 97 -57.70 56.61 REMARK 500 TYR D 102 94.30 -68.33 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 D 482 DISTANCE = 7.05 ANGSTROMS REMARK 525 HOH A 461 DISTANCE = 5.16 ANGSTROMS REMARK 525 HOH B 251 DISTANCE = 6.90 ANGSTROMS REMARK 525 HOH D 502 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH D 546 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH C 529 DISTANCE = 6.07 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 456 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF ENTITIES 1 AND 2 WAS NOT AVAILABLE AT REMARK 999 THE UNIPROT KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE REMARK 999 TIME OF DEPOSITION.