REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.53 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 23086 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) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1244 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1478 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.3730 REMARK 3 BIN FREE R VALUE SET COUNT : 91 REMARK 3 BIN FREE R VALUE : 0.4150 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3593 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 59 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.52 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.50000 REMARK 3 B22 (A**2) : 3.50000 REMARK 3 B33 (A**2) : -7.01000 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): 0.332 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.215 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.425 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3673 ; 0.009 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): 2458 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4987 ; 1.328 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5963 ; 0.839 ; 3.001 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 465 ; 6.186 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 165 ;33.651 ;23.636 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 570 ;15.755 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.450 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 553 ; 0.081 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4152 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 777 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 10 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 4 A 128 REMARK 3 ORIGIN FOR THE GROUP (A): -0.4488 -0.9022 14.9919 REMARK 3 T TENSOR REMARK 3 T11: 0.3326 T22: 0.5176 REMARK 3 T33: 0.1558 T12: -0.0963 REMARK 3 T13: 0.0080 T23: 0.0291 REMARK 3 L TENSOR REMARK 3 L11: 3.2679 L22: 2.6303 REMARK 3 L33: 6.4166 L12: 1.4138 REMARK 3 L13: 0.3069 L23: -0.8210 REMARK 3 S TENSOR REMARK 3 S11: -0.3216 S12: 0.1485 S13: 0.0772 REMARK 3 S21: -0.4340 S22: 0.1820 S23: -0.0110 REMARK 3 S31: -0.0749 S32: -0.1507 S33: 0.1397 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 : B 3 B 128 REMARK 3 ORIGIN FOR THE GROUP (A): -21.1618 -17.3657 31.3578 REMARK 3 T TENSOR REMARK 3 T11: 0.0455 T22: 0.3361 REMARK 3 T33: 0.1588 T12: -0.0019 REMARK 3 T13: 0.0674 T23: -0.0345 REMARK 3 L TENSOR REMARK 3 L11: 4.8934 L22: 2.4595 REMARK 3 L33: 5.8554 L12: 1.5000 REMARK 3 L13: 1.4437 L23: 1.3259 REMARK 3 S TENSOR REMARK 3 S11: -0.1041 S12: -0.0479 S13: 0.0720 REMARK 3 S21: 0.0005 S22: -0.0567 S23: 0.0913 REMARK 3 S31: 0.0902 S32: -0.0493 S33: 0.1608 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 : C 283 C 292 REMARK 3 ORIGIN FOR THE GROUP (A): 7.7028 -4.4617 54.1780 REMARK 3 T TENSOR REMARK 3 T11: 0.9580 T22: 1.2280 REMARK 3 T33: 0.8361 T12: 0.3100 REMARK 3 T13: 0.3242 T23: 0.4527 REMARK 3 L TENSOR REMARK 3 L11: 12.3923 L22: 24.5011 REMARK 3 L33: 14.7557 L12: -8.5514 REMARK 3 L13: -11.1675 L23: 17.0405 REMARK 3 S TENSOR REMARK 3 S11: -1.9415 S12: -2.4388 S13: -1.5369 REMARK 3 S21: 0.0771 S22: 1.6534 S23: -1.5018 REMARK 3 S31: 1.1957 S32: 2.0308 S33: 0.2881 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 : C 293 C 307 REMARK 3 ORIGIN FOR THE GROUP (A): -14.7789 -6.4400 51.2246 REMARK 3 T TENSOR REMARK 3 T11: 0.2230 T22: 0.7314 REMARK 3 T33: 0.1002 T12: 0.0599 REMARK 3 T13: 0.0452 T23: -0.0065 REMARK 3 L TENSOR REMARK 3 L11: 8.5797 L22: 24.5038 REMARK 3 L33: 4.1278 L12: 0.9155 REMARK 3 L13: 1.2929 L23: 1.6342 REMARK 3 S TENSOR REMARK 3 S11: 0.1682 S12: -0.2979 S13: 0.1215 REMARK 3 S21: 0.1695 S22: -0.1360 S23: 1.4922 REMARK 3 S31: -0.2746 S32: -0.8429 S33: -0.0322 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 308 C 338 REMARK 3 ORIGIN FOR THE GROUP (A): -10.8612 0.0482 46.5808 REMARK 3 T TENSOR REMARK 3 T11: 0.2257 T22: 0.6127 REMARK 3 T33: 0.1202 T12: 0.0734 REMARK 3 T13: -0.0505 T23: -0.1372 REMARK 3 L TENSOR REMARK 3 L11: 4.8943 L22: 7.4936 REMARK 3 L33: 5.7335 L12: 2.2899 REMARK 3 L13: -1.2831 L23: -2.4068 REMARK 3 S TENSOR REMARK 3 S11: -0.1194 S12: 0.1000 S13: 0.5631 REMARK 3 S21: -0.2625 S22: 0.1861 S23: 0.3583 REMARK 3 S31: -0.3753 S32: -0.4555 S33: -0.0667 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 339 C 393 REMARK 3 ORIGIN FOR THE GROUP (A): -9.1037 -6.8985 50.2567 REMARK 3 T TENSOR REMARK 3 T11: 0.1879 T22: 0.5584 REMARK 3 T33: 0.2275 T12: 0.0020 REMARK 3 T13: -0.0148 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 2.2878 L22: 4.0326 REMARK 3 L33: 6.2388 L12: -0.4862 REMARK 3 L13: -0.9590 L23: 2.7005 REMARK 3 S TENSOR REMARK 3 S11: -0.1289 S12: -0.5395 S13: 0.0889 REMARK 3 S21: 0.7658 S22: 0.0829 S23: 0.1455 REMARK 3 S31: 0.2231 S32: -0.1764 S33: 0.0460 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 20 D 38 REMARK 3 ORIGIN FOR THE GROUP (A): 6.4086 3.6247 41.9903 REMARK 3 T TENSOR REMARK 3 T11: 0.4021 T22: 0.5658 REMARK 3 T33: 0.2201 T12: -0.1709 REMARK 3 T13: -0.0640 T23: -0.1367 REMARK 3 L TENSOR REMARK 3 L11: 4.5466 L22: 2.8880 REMARK 3 L33: 2.8374 L12: -0.4463 REMARK 3 L13: -0.1571 L23: -2.7938 REMARK 3 S TENSOR REMARK 3 S11: -0.0968 S12: -0.6140 S13: 0.0921 REMARK 3 S21: 0.0129 S22: -0.1540 S23: -0.2952 REMARK 3 S31: -0.1234 S32: 0.3733 S33: 0.2507 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 39 D 81 REMARK 3 ORIGIN FOR THE GROUP (A): 6.4979 0.9008 41.6294 REMARK 3 T TENSOR REMARK 3 T11: 0.2219 T22: 0.5845 REMARK 3 T33: 0.1375 T12: -0.0884 REMARK 3 T13: -0.0959 T23: -0.1165 REMARK 3 L TENSOR REMARK 3 L11: 3.8607 L22: 14.3553 REMARK 3 L33: 2.5924 L12: 0.7638 REMARK 3 L13: -0.8463 L23: -2.0047 REMARK 3 S TENSOR REMARK 3 S11: 0.0372 S12: -0.1058 S13: 0.0226 REMARK 3 S21: 0.6325 S22: -0.1731 S23: -0.1823 REMARK 3 S31: -0.6745 S32: 0.4318 S33: 0.1359 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 : D 82 D 106 REMARK 3 ORIGIN FOR THE GROUP (A): 6.4277 5.2142 40.7717 REMARK 3 T TENSOR REMARK 3 T11: 0.4242 T22: 0.6621 REMARK 3 T33: 0.1672 T12: -0.0667 REMARK 3 T13: -0.0281 T23: -0.0804 REMARK 3 L TENSOR REMARK 3 L11: 6.1055 L22: 6.1062 REMARK 3 L33: 2.3707 L12: -0.0940 REMARK 3 L13: 0.4993 L23: -1.0128 REMARK 3 S TENSOR REMARK 3 S11: -0.1974 S12: 0.7006 S13: 0.6879 REMARK 3 S21: 0.1033 S22: 0.0247 S23: -0.2816 REMARK 3 S31: -0.6116 S32: 0.3101 S33: 0.1727 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 : D 107 D 132 REMARK 3 ORIGIN FOR THE GROUP (A): -0.1134 3.8760 39.1670 REMARK 3 T TENSOR REMARK 3 T11: 0.3195 T22: 0.6150 REMARK 3 T33: 0.2420 T12: -0.0013 REMARK 3 T13: 0.0469 T23: -0.0910 REMARK 3 L TENSOR REMARK 3 L11: 3.8599 L22: 4.1012 REMARK 3 L33: 4.5453 L12: 2.3441 REMARK 3 L13: 3.0304 L23: 0.8033 REMARK 3 S TENSOR REMARK 3 S11: -0.3602 S12: -0.2538 S13: 0.7007 REMARK 3 S21: 0.0660 S22: -0.1583 S23: 0.1959 REMARK 3 S31: -0.8425 S32: 0.0924 S33: 0.5185 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3STB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-11. REMARK 100 THE RCSB ID CODE IS RCSB066625. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10; NULL REMARK 200 TEMPERATURE (KELVIN) : 77; NULL REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; NULL REMARK 200 RADIATION SOURCE : SSRL; NULL REMARK 200 BEAMLINE : BL12-2; NULL REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792, 0.9794, 0.9116; NULL REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE REMARK 200 CRYSTAL; LIQUID NITROGEN-COOLED REMARK 200 DOUBLE CRYSTAL REMARK 200 OPTICS : RH COATED; NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL; NULL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M; NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 54.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.12500 REMARK 200 R SYM (I) : 0.12500 REMARK 200 FOR THE DATA SET : 17.4900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.80 REMARK 200 R MERGE FOR SHELL (I) : 0.36100 REMARK 200 R SYM FOR SHELL (I) : 0.36100 REMARK 200 FOR SHELL : 2.333 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 10% 2-PROPANOL, REMARK 280 22% W/V PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 119.94500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.27000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.27000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 179.91750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.27000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.27000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.97250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.27000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.27000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 179.91750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.27000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.27000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.97250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 119.94500 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 18250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, B, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 119.94500 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, B, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLN A 3 REMARK 465 HIS A 129 REMARK 465 HIS A 130 REMARK 465 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 REMARK 465 HIS A 134 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 HIS B 133 REMARK 465 HIS B 134 REMARK 465 MET C 246 REMARK 465 ARG C 247 REMARK 465 SER C 248 REMARK 465 ALA C 249 REMARK 465 MET C 250 REMARK 465 GLY C 251 REMARK 465 THR C 252 REMARK 465 GLN C 253 REMARK 465 TYR C 254 REMARK 465 VAL C 255 REMARK 465 HIS C 256 REMARK 465 GLY C 257 REMARK 465 GLN C 258 REMARK 465 GLU C 259 REMARK 465 THR C 260 REMARK 465 ILE C 261 REMARK 465 LEU C 262 REMARK 465 PRO C 263 REMARK 465 GLN C 264 REMARK 465 ALA C 265 REMARK 465 PRO C 266 REMARK 465 GLN C 267 REMARK 465 TYR C 268 REMARK 465 HIS C 269 REMARK 465 LEU C 270 REMARK 465 ASP C 271 REMARK 465 VAL C 272 REMARK 465 ALA C 273 REMARK 465 PRO C 274 REMARK 465 ASN C 275 REMARK 465 ALA C 276 REMARK 465 PRO C 277 REMARK 465 GLU C 278 REMARK 465 GLU C 279 REMARK 465 GLY C 280 REMARK 465 GLU C 281 REMARK 465 VAL C 282 REMARK 465 HIS D 58 REMARK 465 PRO D 59 REMARK 465 THR D 60 REMARK 465 GLN D 61 REMARK 465 GLU D 62 REMARK 465 ASP D 133 REMARK 465 ARG D 134 REMARK 465 ARG D 135 REMARK 465 THR D 136 REMARK 465 VAL D 137 REMARK 465 PRO D 138 REMARK 465 ALA D 139 REMARK 465 ALA D 140 REMARK 465 VAL D 141 REMARK 465 ASN D 142 REMARK 465 PRO D 143 REMARK 465 ALA D 144 REMARK 465 VAL D 145 REMARK 465 GLU D 146 REMARK 465 ASP D 147 REMARK 465 ILE D 148 REMARK 465 LYS D 149 REMARK 465 SER D 150 REMARK 465 GLU D 151 REMARK 465 LYS D 152 REMARK 465 GLU D 153 REMARK 465 GLY D 154 REMARK 465 SER D 155 REMARK 465 GLY D 156 REMARK 465 GLY D 157 REMARK 465 ASP D 158 REMARK 465 GLN D 159 REMARK 465 SER D 160 REMARK 465 GLY D 161 REMARK 465 VAL D 162 REMARK 465 PRO D 163 REMARK 465 SER D 164 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 HIS C 285 CG ND1 CD2 CE1 NE2 REMARK 470 TRP C 286 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 286 CZ3 CH2 REMARK 470 ARG C 287 CG CD NE CZ NH1 NH2 REMARK 470 CYS C 288 SG REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 GLN D 104 CG CD OE1 NE2 REMARK 470 HIS D 131 CG ND1 CD2 CE1 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 ARG B 68 -39.57 -137.91 REMARK 500 SER B 86 57.77 36.61 REMARK 500 TRP C 286 -165.01 -105.16 REMARK 500 ARG C 287 -72.63 -67.93 REMARK 500 PHE C 307 -110.21 56.38 REMARK 500 GLU C 321 -70.75 -65.55 REMARK 500 PRO C 325 -69.10 -25.72 REMARK 500 ASP C 339 107.90 74.80 REMARK 500 VAL D 39 -69.81 -95.87 REMARK 500 TYR D 40 -89.08 -117.51 REMARK 500 HIS D 124 68.09 -68.90 REMARK 500 REMARK 500 REMARK: NULL