REMARK 2 REMARK 2 RESOLUTION. 3.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 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) : 3.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 26003 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) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2603 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 25 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.35 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.42 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1350 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2320 REMARK 3 BIN FREE R VALUE SET COUNT : 145 REMARK 3 BIN FREE R VALUE : 0.2830 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8149 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 42.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.29 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.20000 REMARK 3 B22 (A**2) : -1.20000 REMARK 3 B33 (A**2) : 1.79000 REMARK 3 B12 (A**2) : -0.60000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.573 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.456 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.186 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.859 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.777 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8237 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 6998 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11217 ; 1.339 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): 16420 ; 0.899 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1045 ; 7.480 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1243 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9193 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1654 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1576 ; 0.210 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8196 ; 0.226 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 5359 ; 0.088 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 118 ; 0.170 ; 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): 17 ; 0.207 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 78 ; 0.250 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.275 ; 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): 5249 ; 2.152 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8485 ; 3.666 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2988 ; 2.491 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2732 ; 3.932 ; 5.000 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 : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A L REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 109 5 REMARK 3 1 L 1 L 109 5 REMARK 3 2 A 110 A 213 5 REMARK 3 2 L 110 L 213 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 1254 ; 1.26 ; 0.50 REMARK 3 LOOSE POSITIONAL 1 A (A): 1798 ; 1.43 ; 5.00 REMARK 3 MEDIUM THERMAL 1 A (A**2): 1254 ; 0.62 ; 2.00 REMARK 3 LOOSE THERMAL 1 A (A**2): 1798 ; 1.42 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 113 5 REMARK 3 1 H 1 H 113 5 REMARK 3 2 B 114 B 214 5 REMARK 3 2 H 114 H 214 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 B (A): 1311 ; 1.77 ; 0.50 REMARK 3 LOOSE POSITIONAL 2 B (A): 1859 ; 1.93 ; 5.00 REMARK 3 MEDIUM THERMAL 2 B (A**2): 1311 ; 0.63 ; 2.00 REMARK 3 LOOSE THERMAL 2 B (A**2): 1859 ; 1.50 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : R S REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 R 22 R 86 5 REMARK 3 1 S 22 S 86 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 R (A): 381 ; 0.20 ; 0.50 REMARK 3 LOOSE POSITIONAL 3 R (A): 534 ; 0.68 ; 5.00 REMARK 3 MEDIUM THERMAL 3 R (A**2): 381 ; 0.64 ; 2.00 REMARK 3 LOOSE THERMAL 3 R (A**2): 534 ; 2.42 ; 10.00 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 1 A 109 REMARK 3 ORIGIN FOR THE GROUP (A): 38.1426 56.9145 39.7317 REMARK 3 T TENSOR REMARK 3 T11: 0.6789 T22: 0.8021 REMARK 3 T33: 0.6222 T12: -0.0425 REMARK 3 T13: 0.0107 T23: -0.2614 REMARK 3 L TENSOR REMARK 3 L11: 6.7184 L22: 5.5958 REMARK 3 L33: 4.8503 L12: -1.7623 REMARK 3 L13: 1.0756 L23: 2.5589 REMARK 3 S TENSOR REMARK 3 S11: -0.0739 S12: -0.3625 S13: -0.1619 REMARK 3 S21: -0.0679 S22: -0.0557 S23: 0.3593 REMARK 3 S31: 0.3556 S32: -0.2674 S33: 0.1295 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 1 B 115 REMARK 3 ORIGIN FOR THE GROUP (A): 40.8532 43.5002 21.9088 REMARK 3 T TENSOR REMARK 3 T11: 0.8477 T22: 0.5102 REMARK 3 T33: 0.6232 T12: 0.0375 REMARK 3 T13: 0.0185 T23: -0.1189 REMARK 3 L TENSOR REMARK 3 L11: 12.0818 L22: 3.9871 REMARK 3 L33: 4.5344 L12: -0.5416 REMARK 3 L13: 1.1722 L23: 2.0429 REMARK 3 S TENSOR REMARK 3 S11: 0.0938 S12: 0.1464 S13: -0.1677 REMARK 3 S21: -0.4343 S22: -0.2663 S23: -0.0450 REMARK 3 S31: -0.2173 S32: -0.3376 S33: 0.1725 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 : A 110 A 213 REMARK 3 ORIGIN FOR THE GROUP (A): 5.3581 65.5547 26.0365 REMARK 3 T TENSOR REMARK 3 T11: 0.8416 T22: 0.8518 REMARK 3 T33: 0.9071 T12: 0.2468 REMARK 3 T13: -0.3312 T23: -0.3333 REMARK 3 L TENSOR REMARK 3 L11: 10.6546 L22: 5.2923 REMARK 3 L33: 9.2896 L12: 3.3089 REMARK 3 L13: 5.5863 L23: 3.8651 REMARK 3 S TENSOR REMARK 3 S11: -0.3198 S12: -0.5017 S13: 0.9107 REMARK 3 S21: -0.6519 S22: -0.1706 S23: 0.8432 REMARK 3 S31: -0.1072 S32: -0.7653 S33: 0.4904 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 116 B 214 REMARK 3 ORIGIN FOR THE GROUP (A): 16.3911 63.6388 13.9699 REMARK 3 T TENSOR REMARK 3 T11: 0.8642 T22: 1.1119 REMARK 3 T33: 0.8574 T12: 0.0015 REMARK 3 T13: -0.3998 T23: -0.1910 REMARK 3 L TENSOR REMARK 3 L11: 5.5589 L22: 11.8925 REMARK 3 L33: 7.8794 L12: 0.1101 REMARK 3 L13: 1.2246 L23: 0.6941 REMARK 3 S TENSOR REMARK 3 S11: -0.7974 S12: 1.2399 S13: 1.0400 REMARK 3 S21: -0.9517 S22: 0.6460 S23: -0.0201 REMARK 3 S31: -1.2122 S32: 0.4352 S33: 0.1514 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 : L 1 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): -26.9015 51.4519 -2.2203 REMARK 3 T TENSOR REMARK 3 T11: 0.6219 T22: 0.7338 REMARK 3 T33: 0.6170 T12: -0.0042 REMARK 3 T13: -0.0497 T23: -0.2641 REMARK 3 L TENSOR REMARK 3 L11: 7.7881 L22: 5.2716 REMARK 3 L33: 9.6667 L12: -0.7099 REMARK 3 L13: -1.3690 L23: 0.2777 REMARK 3 S TENSOR REMARK 3 S11: 0.2160 S12: -0.2921 S13: 0.5020 REMARK 3 S21: 0.6007 S22: -0.0106 S23: 0.1057 REMARK 3 S31: 0.2932 S32: -0.1350 S33: -0.2054 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 : H 1 H 115 REMARK 3 ORIGIN FOR THE GROUP (A): -6.7674 46.8311 -11.0679 REMARK 3 T TENSOR REMARK 3 T11: 0.5347 T22: 0.7451 REMARK 3 T33: 0.7840 T12: 0.0104 REMARK 3 T13: -0.0005 T23: -0.1707 REMARK 3 L TENSOR REMARK 3 L11: 4.9923 L22: 5.0262 REMARK 3 L33: 9.6666 L12: -0.2136 REMARK 3 L13: 2.4336 L23: 0.3563 REMARK 3 S TENSOR REMARK 3 S11: -0.1327 S12: -0.3489 S13: 0.3054 REMARK 3 S21: 0.2352 S22: 0.2934 S23: -0.4069 REMARK 3 S31: 0.3879 S32: 0.4834 S33: -0.1607 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 : L 110 L 213 REMARK 3 ORIGIN FOR THE GROUP (A): -13.1890 43.8572 30.3005 REMARK 3 T TENSOR REMARK 3 T11: 1.1954 T22: 1.6404 REMARK 3 T33: 0.8599 T12: -0.2840 REMARK 3 T13: -0.1650 T23: 0.3371 REMARK 3 L TENSOR REMARK 3 L11: 24.8239 L22: 2.8957 REMARK 3 L33: 9.8398 L12: -2.2439 REMARK 3 L13: 8.2261 L23: -1.6226 REMARK 3 S TENSOR REMARK 3 S11: 0.6544 S12: -3.5063 S13: -1.1512 REMARK 3 S21: 0.7132 S22: -0.2663 S23: -0.4873 REMARK 3 S31: 0.3295 S32: -0.4808 S33: -0.3881 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 : H 116 H 214 REMARK 3 ORIGIN FOR THE GROUP (A): -8.3386 31.0354 21.5542 REMARK 3 T TENSOR REMARK 3 T11: 1.3366 T22: 1.1030 REMARK 3 T33: 2.3951 T12: 0.0060 REMARK 3 T13: -0.4481 T23: 0.1150 REMARK 3 L TENSOR REMARK 3 L11: 27.1075 L22: 9.3622 REMARK 3 L33: 6.7878 L12: 8.1352 REMARK 3 L13: -4.2171 L23: -4.0664 REMARK 3 S TENSOR REMARK 3 S11: 0.0554 S12: -0.9486 S13: -5.7637 REMARK 3 S21: 0.6350 S22: 0.1344 S23: -0.5611 REMARK 3 S31: 1.7304 S32: 0.0695 S33: -0.1897 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 : R 22 R 86 REMARK 3 ORIGIN FOR THE GROUP (A): -11.6615 67.2178 -22.6713 REMARK 3 T TENSOR REMARK 3 T11: 0.1313 T22: 0.1290 REMARK 3 T33: 0.1932 T12: -0.0505 REMARK 3 T13: 0.0967 T23: -0.0548 REMARK 3 L TENSOR REMARK 3 L11: 12.3367 L22: 4.4530 REMARK 3 L33: 2.9905 L12: 4.8785 REMARK 3 L13: 3.6245 L23: 1.5893 REMARK 3 S TENSOR REMARK 3 S11: 0.1215 S12: -1.0411 S13: 0.8238 REMARK 3 S21: -0.1397 S22: -0.4123 S23: 0.2601 REMARK 3 S31: -0.2426 S32: -0.2615 S33: 0.2908 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 : S 22 S 86 REMARK 3 ORIGIN FOR THE GROUP (A): 53.8838 31.0796 37.4982 REMARK 3 T TENSOR REMARK 3 T11: 0.2416 T22: 0.0945 REMARK 3 T33: 0.2879 T12: 0.0364 REMARK 3 T13: 0.1291 T23: -0.1068 REMARK 3 L TENSOR REMARK 3 L11: 7.0163 L22: 11.7644 REMARK 3 L33: 2.9267 L12: 6.9364 REMARK 3 L13: 1.0498 L23: 0.1537 REMARK 3 S TENSOR REMARK 3 S11: 0.2997 S12: -0.3219 S13: -0.0146 REMARK 3 S21: 1.0815 S22: -0.3678 S23: -0.0053 REMARK 3 S31: -0.2398 S32: 0.0093 S33: 0.0681 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 : R 87 R 123 REMARK 3 ORIGIN FOR THE GROUP (A): 11.4513 77.2524 -6.7575 REMARK 3 T TENSOR REMARK 3 T11: 1.3159 T22: 1.3783 REMARK 3 T33: 0.8798 T12: -0.1768 REMARK 3 T13: 0.0251 T23: -0.5348 REMARK 3 L TENSOR REMARK 3 L11: 105.5975 L22: 13.8180 REMARK 3 L33: 49.7826 L12: -45.6197 REMARK 3 L13: 19.3915 L23: -22.6445 REMARK 3 S TENSOR REMARK 3 S11: -3.1624 S12: -3.6949 S13: 0.9033 REMARK 3 S21: 3.8157 S22: 1.0595 S23: -1.4331 REMARK 3 S31: -4.1175 S32: 1.2187 S33: 2.1029 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 : S 87 S 126 REMARK 3 ORIGIN FOR THE GROUP (A): 27.0541 10.1551 29.8876 REMARK 3 T TENSOR REMARK 3 T11: 0.7265 T22: 0.9904 REMARK 3 T33: 0.8132 T12: -0.2037 REMARK 3 T13: 0.2440 T23: 0.0936 REMARK 3 L TENSOR REMARK 3 L11: 55.5881 L22: 22.9349 REMARK 3 L33: 41.9804 L12: 20.9703 REMARK 3 L13: 22.1428 L23: 17.8230 REMARK 3 S TENSOR REMARK 3 S11: 0.8166 S12: 0.8027 S13: -0.2582 REMARK 3 S21: -0.7144 S22: 0.4574 S23: 1.3963 REMARK 3 S31: -0.3488 S32: -1.6305 S33: -1.2740 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 REMARK 4 REMARK 4 1ZA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-05. REMARK 100 THE RCSB ID CODE IS RCSB032488. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-JUN-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.92086 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SAGITTALLY REMARK 200 FOCUSED MONOCHROMOETER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26539 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.12400 REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.47 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.33800 REMARK 200 FOR SHELL : 4.200 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: 1FVE VARIANTS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.2M MGACETATE, 0.1M REMARK 280 NACACODYLATE PH 6.2-6.6, PH 6.4, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.63133 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.31567 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.31567 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 96.63133 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 APPLY THE FOLLOWING TO CHAINS: A, B, S 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 APPLY THE FOLLOWING TO CHAINS: R, L, 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 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 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 THR B 219 REMARK 465 HIS B 220 REMARK 465 GLY R -3 REMARK 465 SER R -2 REMARK 465 HIS R -1 REMARK 465 MET R 0 REMARK 465 ALA R 1 REMARK 465 LEU R 2 REMARK 465 ILE R 3 REMARK 465 THR R 4 REMARK 465 GLN R 5 REMARK 465 GLN R 6 REMARK 465 ASP R 7 REMARK 465 LEU R 8 REMARK 465 ALA R 9 REMARK 465 PRO R 10 REMARK 465 GLN R 11 REMARK 465 GLN R 12 REMARK 465 ARG R 13 REMARK 465 ALA R 14 REMARK 465 ALA R 15 REMARK 465 PRO R 16 REMARK 465 GLN R 17 REMARK 465 GLN R 18 REMARK 465 LYS R 19 REMARK 465 ARG R 20 REMARK 465 ARG R 104 REMARK 465 THR R 105 REMARK 465 GLY R 106 REMARK 465 CYS R 107 REMARK 465 PRO R 108 REMARK 465 ARG R 109 REMARK 465 GLY R 110 REMARK 465 MET R 111 REMARK 465 VAL R 112 REMARK 465 LYS R 113 REMARK 465 VAL R 114 REMARK 465 GLY R 115 REMARK 465 GLU R 124 REMARK 465 CYS R 125 REMARK 465 VAL R 126 REMARK 465 HIS R 127 REMARK 465 LYS R 128 REMARK 465 GLU R 129 REMARK 465 SER R 130 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 GLY S -3 REMARK 465 SER S -2 REMARK 465 HIS S -1 REMARK 465 MET S 0 REMARK 465 ALA S 1 REMARK 465 LEU S 2 REMARK 465 ILE S 3 REMARK 465 THR S 4 REMARK 465 GLN S 5 REMARK 465 GLN S 6 REMARK 465 ASP S 7 REMARK 465 LEU S 8 REMARK 465 ALA S 9 REMARK 465 PRO S 10 REMARK 465 GLN S 11 REMARK 465 GLN S 12 REMARK 465 ARG S 13 REMARK 465 ALA S 14 REMARK 465 ALA S 15 REMARK 465 PRO S 16 REMARK 465 GLN S 17 REMARK 465 GLN S 18 REMARK 465 LYS S 19 REMARK 465 ARG S 20 REMARK 465 HIS S 127 REMARK 465 LYS S 128 REMARK 465 GLU S 129 REMARK 465 SER S 130 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 B 214 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ REMARK 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 ARG R 92 REMARK 475 GLU R 93 REMARK 475 GLU R 94 REMARK 475 ASP R 95 REMARK 475 SER R 96 REMARK 475 PRO R 97 REMARK 475 GLU R 98 REMARK 475 MET R 99 REMARK 475 GLU S 93 REMARK 475 GLU S 94 REMARK 475 ASP S 95 REMARK 475 SER S 96 REMARK 475 PRO S 97 REMARK 475 GLU S 98 REMARK 475 MET S 99 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 OE2 GLU R 70 NH2 ARG R 92 0.88 REMARK 500 O MET R 99 N CYS R 100 1.14 REMARK 500 O PHE R 91 N ARG R 92 1.52 REMARK 500 OE2 GLU R 70 CZ ARG R 92 1.56 REMARK 500 CD GLU R 70 NH2 ARG R 92 1.89 REMARK 500 OE2 GLU R 70 NH1 ARG R 92 1.98 REMARK 500 CG GLU R 70 NH1 ARG R 92 2.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O GLY A 16 OG1 THR L 20 5665 2.19 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 PHE R 91 C ARG R 92 N -0.328 REMARK 500 MET R 99 C CYS R 100 N -0.451 REMARK 500 MET S 99 C CYS S 100 N -0.354 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 ASP A 28 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 ASP R 40 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 ASP R 56 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES REMARK 500 PHE R 91 CA - C - N ANGL. DEV. = 19.1 DEGREES REMARK 500 PHE R 91 O - C - N ANGL. DEV. = -37.2 DEGREES REMARK 500 MET R 99 CA - C - N ANGL. DEV. = 16.1 DEGREES REMARK 500 MET R 99 O - C - N ANGL. DEV. = -60.2 DEGREES REMARK 500 ASP L 28 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP S 37 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 ARG S 92 CA - C - N ANGL. DEV. = -25.5 DEGREES REMARK 500 ARG S 92 O - C - N ANGL. DEV. = 16.4 DEGREES REMARK 500 GLU S 93 C - N - CA ANGL. DEV. = -29.2 DEGREES REMARK 500 MET S 99 O - C - N ANGL. DEV. = -14.9 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 ASN A 30 -118.96 61.15 REMARK 500 ALA A 32 33.37 -146.16 REMARK 500 ALA A 50 -27.10 71.24 REMARK 500 ALA A 51 -49.99 138.83 REMARK 500 SER A 65 57.50 -158.65 REMARK 500 SER A 67 120.37 -171.49 REMARK 500 SER A 76 -63.00 -99.25 REMARK 500 SER A 77 67.26 -116.74 REMARK 500 LEU A 78 132.17 -37.44 REMARK 500 SER A 91 -72.03 -69.88 REMARK 500 SER A 93 -114.90 -110.21 REMARK 500 TYR A 95 42.96 -104.53 REMARK 500 SER A 126 4.17 -63.32 REMARK 500 ASN A 137 64.82 60.95 REMARK 500 SER A 155 -78.25 -111.16 REMARK 500 GLU A 212 66.49 39.49 REMARK 500 LEU B 18 106.94 -171.10 REMARK 500 VAL B 48 -63.03 -97.56 REMARK 500 SER B 62 12.75 -69.37 REMARK 500 VAL B 63 -12.60 -148.96 REMARK 500 SER B 82B 55.28 32.80 REMARK 500 SER B 97 -142.95 -105.26 REMARK 500 TYR B 100C -77.12 -76.34 REMARK 500 ASP B 144 66.98 62.73 REMARK 500 PHE B 146 139.50 -179.94 REMARK 500 THR R 77 -159.58 -126.42 REMARK 500 MET R 99 38.28 -147.13 REMARK 500 CYS R 100 160.65 26.92 REMARK 500 ASN L 30 -130.27 46.56 REMARK 500 ALA L 50 -18.52 57.34 REMARK 500 ALA L 51 -38.17 128.44 REMARK 500 SER L 65 44.95 -165.88 REMARK 500 SER L 67 117.80 172.06 REMARK 500 SER L 91 -98.19 -66.00 REMARK 500 SER L 92 -3.29 -41.58 REMARK 500 SER L 93 -91.87 -117.16 REMARK 500 ASN L 137 71.09 51.04 REMARK 500 ASN L 151 17.12 56.22 REMARK 500 SER L 155 -85.86 -104.42 REMARK 500 LYS L 168 -45.66 -140.66 REMARK 500 LYS L 189 -62.87 -92.94 REMARK 500 ARG L 210 119.84 -35.35 REMARK 500 LEU H 18 122.09 -173.58 REMARK 500 ILE H 29 -34.69 -27.05 REMARK 500 VAL H 63 -12.50 -147.67 REMARK 500 SER H 82B 66.21 24.56 REMARK 500 ALA H 88 174.45 174.41 REMARK 500 SER H 97 -146.78 -99.90 REMARK 500 SER H 100 -36.26 -38.81 REMARK 500 TYR H 100J 46.77 35.41 REMARK 500 REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS. 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 SER A 93 PRO A 94 149.56 REMARK 500 SER L 93 PRO L 94 144.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PHE R 91 -38.85 REMARK 500 MET R 99 67.25 REMARK 500 ARG S 92 11.07 REMARK 500 MET S 99 23.02 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 GLN L 79 16.2 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1D0G RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF HDR5 BOUND TO APO2L/TRAIL REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE HEAVY AND LIGHT CHAIN FAB FRAGMENTS WERE ISOLATED REMARK 999 FROM A PHAGE LIBRARY, AND HAVE NO CORRESPONDING ENTRIES REMARK 999 IN THE STANDARD DATABASES.