REMARK 2 REMARK 2 RESOLUTION. 2.70 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.33 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 42077 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) : 0.238 REMARK 3 R VALUE (WORKING SET) : 0.235 REMARK 3 FREE R VALUE : 0.284 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2216 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3110 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76 REMARK 3 BIN R VALUE (WORKING SET) : 0.3500 REMARK 3 BIN FREE R VALUE SET COUNT : 176 REMARK 3 BIN FREE R VALUE : 0.4090 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10234 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 36 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : UNVERIFIED REMARK 3 FROM WILSON PLOT (A**2) : 70.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.35 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.44000 REMARK 3 B22 (A**2) : 2.26000 REMARK 3 B33 (A**2) : 1.17000 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): 2.220 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.389 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.327 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.285 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10500 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7042 ; 0.007 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14262 ; 1.576 ; 1.957 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17238 ; 0.907 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1316 ; 7.612 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 412 ;33.958 ;24.417 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1768 ;15.508 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.609 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1626 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11534 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2058 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1903 ; 0.238 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6879 ; 0.215 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4915 ; 0.188 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5890 ; 0.091 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 255 ; 0.172 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.083 ; 0.200 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): 19 ; 0.312 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.277 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.244 ; 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): 8295 ; 2.452 ; 3.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2656 ; 0.324 ; 3.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10730 ; 2.847 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4653 ; 5.145 ; 8.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3532 ; 6.595 ;11.000 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 : 6 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : L D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 5 L 100 6 REMARK 3 2 D 5 D 100 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 1 L (A): 1232 ; 0.340 ; 5.000 REMARK 3 LOOSE THERMAL 1 L (A**2): 1232 ; 2.190 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : L D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 110 L 200 6 REMARK 3 2 D 110 D 200 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 2 L (A): 1182 ; 0.410 ; 5.000 REMARK 3 LOOSE THERMAL 2 L (A**2): 1182 ; 3.090 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 5 H 110 6 REMARK 3 2 B 5 B 117 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 3 H (A): 1400 ; 0.370 ; 5.000 REMARK 3 LOOSE THERMAL 3 H (A**2): 1400 ; 2.330 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 120 H 210 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 4 H (A): 1069 ; 0.400 ; 5.000 REMARK 3 LOOSE THERMAL 4 H (A**2): 1069 ; 3.480 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : C A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 5 C 105 6 REMARK 3 2 A 5 A 105 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 5 C (A): 1381 ; 0.490 ; 5.000 REMARK 3 LOOSE THERMAL 5 C (A**2): 1381 ; 2.000 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : F E REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 E 4 E 121 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 6 F (A): 1340 ; 0.400 ; 5.000 REMARK 3 LOOSE THERMAL 6 F (A**2): 1340 ; 2.200 ;10.000 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 : L 1 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): -11.4570 -52.9930 28.9880 REMARK 3 T TENSOR REMARK 3 T11: 0.0436 T22: -0.2441 REMARK 3 T33: -0.1367 T12: -0.0537 REMARK 3 T13: 0.0256 T23: -0.0368 REMARK 3 L TENSOR REMARK 3 L11: 2.0470 L22: 2.3459 REMARK 3 L33: 3.7626 L12: -0.1580 REMARK 3 L13: -0.1148 L23: -1.3918 REMARK 3 S TENSOR REMARK 3 S11: -0.0641 S12: 0.1236 S13: -0.2313 REMARK 3 S21: -0.0954 S22: 0.1119 S23: 0.1992 REMARK 3 S31: 0.1850 S32: -0.0949 S33: -0.0478 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 : H 1 H 110 REMARK 3 ORIGIN FOR THE GROUP (A): -10.8930 -31.5770 22.6460 REMARK 3 T TENSOR REMARK 3 T11: 0.1454 T22: -0.1790 REMARK 3 T33: -0.1106 T12: -0.0606 REMARK 3 T13: -0.0434 T23: 0.0246 REMARK 3 L TENSOR REMARK 3 L11: 3.7105 L22: 2.8598 REMARK 3 L33: 4.2374 L12: -1.3326 REMARK 3 L13: -1.1487 L23: 0.1486 REMARK 3 S TENSOR REMARK 3 S11: 0.0189 S12: 0.0748 S13: 0.2389 REMARK 3 S21: 0.0694 S22: -0.0448 S23: -0.0833 REMARK 3 S31: -0.3646 S32: -0.0258 S33: 0.0259 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 : H 121 H 210 REMARK 3 ORIGIN FOR THE GROUP (A): -24.7700 -31.2030 57.4380 REMARK 3 T TENSOR REMARK 3 T11: 0.4023 T22: -0.6488 REMARK 3 T33: -0.1420 T12: -0.0933 REMARK 3 T13: 0.3270 T23: 0.0556 REMARK 3 L TENSOR REMARK 3 L11: 5.2663 L22: 7.3194 REMARK 3 L33: 3.5586 L12: 1.0535 REMARK 3 L13: -1.5055 L23: -0.1706 REMARK 3 S TENSOR REMARK 3 S11: 0.1363 S12: -0.5768 S13: -0.1706 REMARK 3 S21: 1.8856 S22: -0.2249 S23: 0.9634 REMARK 3 S31: -0.1394 S32: 0.1280 S33: 0.0886 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 : L 110 L 210 REMARK 3 ORIGIN FOR THE GROUP (A): -35.8220 -41.3740 53.5510 REMARK 3 T TENSOR REMARK 3 T11: 0.0298 T22: -0.7258 REMARK 3 T33: 0.5240 T12: -0.1130 REMARK 3 T13: 0.3965 T23: 0.0654 REMARK 3 L TENSOR REMARK 3 L11: 3.6763 L22: 9.7319 REMARK 3 L33: 4.3508 L12: -3.4059 REMARK 3 L13: -1.4777 L23: 1.6069 REMARK 3 S TENSOR REMARK 3 S11: 0.0091 S12: 0.0265 S13: -0.0652 REMARK 3 S21: 0.5449 S22: 0.2888 S23: 2.2957 REMARK 3 S31: 0.0067 S32: -0.3773 S33: -0.2979 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 : D 1 D 109 REMARK 3 ORIGIN FOR THE GROUP (A): -11.5740 -99.0670 43.4310 REMARK 3 T TENSOR REMARK 3 T11: 0.0400 T22: -0.3486 REMARK 3 T33: -0.1880 T12: -0.0270 REMARK 3 T13: 0.0343 T23: -0.0589 REMARK 3 L TENSOR REMARK 3 L11: 2.9065 L22: 2.9795 REMARK 3 L33: 4.5673 L12: 0.2779 REMARK 3 L13: -0.4172 L23: -1.8200 REMARK 3 S TENSOR REMARK 3 S11: -0.0378 S12: 0.0716 S13: -0.1050 REMARK 3 S21: -0.0562 S22: -0.0122 S23: 0.0896 REMARK 3 S31: 0.2621 S32: 0.0149 S33: 0.0500 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 : D 110 D 210 REMARK 3 ORIGIN FOR THE GROUP (A): -36.8170 -89.7160 67.2720 REMARK 3 T TENSOR REMARK 3 T11: 0.4413 T22: -0.2132 REMARK 3 T33: 0.3543 T12: 0.2939 REMARK 3 T13: 0.5748 T23: 0.3422 REMARK 3 L TENSOR REMARK 3 L11: 7.7354 L22: 10.0169 REMARK 3 L33: 1.4374 L12: -3.4514 REMARK 3 L13: -2.5049 L23: 2.9611 REMARK 3 S TENSOR REMARK 3 S11: -0.4197 S12: -0.1947 S13: -0.1464 REMARK 3 S21: 1.6106 S22: 0.6861 S23: 2.2848 REMARK 3 S31: -0.4335 S32: -0.6874 S33: -0.2664 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 : B 1 B 110 REMARK 3 ORIGIN FOR THE GROUP (A): -11.1830 -77.4850 37.8970 REMARK 3 T TENSOR REMARK 3 T11: 0.0866 T22: -0.2327 REMARK 3 T33: -0.0740 T12: -0.0102 REMARK 3 T13: 0.0429 T23: 0.0277 REMARK 3 L TENSOR REMARK 3 L11: 0.8145 L22: 4.0813 REMARK 3 L33: 4.4951 L12: -0.0568 REMARK 3 L13: -1.5649 L23: 0.1708 REMARK 3 S TENSOR REMARK 3 S11: 0.1635 S12: 0.0144 S13: 0.1612 REMARK 3 S21: 0.2156 S22: 0.0381 S23: 0.0749 REMARK 3 S31: -0.3888 S32: -0.0256 S33: -0.2016 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 : B 121 B 210 REMARK 3 ORIGIN FOR THE GROUP (A): -26.6530 -78.6780 72.1630 REMARK 3 T TENSOR REMARK 3 T11: 1.1369 T22: -0.3599 REMARK 3 T33: -0.0221 T12: 0.4372 REMARK 3 T13: 0.1779 T23: -0.1631 REMARK 3 L TENSOR REMARK 3 L11: 8.1254 L22: 12.4945 REMARK 3 L33: 17.5056 L12: -2.3329 REMARK 3 L13: 0.2196 L23: -8.8831 REMARK 3 S TENSOR REMARK 3 S11: -0.6291 S12: -1.1141 S13: 0.3608 REMARK 3 S21: 3.3012 S22: 0.9273 S23: -0.3995 REMARK 3 S31: -1.6252 S32: 0.1229 S33: -0.2983 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 : A 4 A 110 REMARK 3 ORIGIN FOR THE GROUP (A): 15.7770 -95.2170 5.4700 REMARK 3 T TENSOR REMARK 3 T11: -0.2476 T22: -0.0530 REMARK 3 T33: -0.2797 T12: 0.0221 REMARK 3 T13: 0.0262 T23: -0.0634 REMARK 3 L TENSOR REMARK 3 L11: 8.9485 L22: 3.6503 REMARK 3 L33: 5.6359 L12: -1.7767 REMARK 3 L13: -1.8237 L23: 1.0932 REMARK 3 S TENSOR REMARK 3 S11: 0.1660 S12: 0.9206 S13: -0.6294 REMARK 3 S21: -0.0664 S22: -0.1756 S23: 0.2895 REMARK 3 S31: 0.1987 S32: 0.0377 S33: 0.0096 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 : C 4 C 110 REMARK 3 ORIGIN FOR THE GROUP (A): 15.7680 -50.3200 -9.3730 REMARK 3 T TENSOR REMARK 3 T11: -0.2584 T22: 0.0135 REMARK 3 T33: -0.2960 T12: -0.0060 REMARK 3 T13: 0.0327 T23: -0.0908 REMARK 3 L TENSOR REMARK 3 L11: 6.9845 L22: 4.3443 REMARK 3 L33: 4.8589 L12: -0.4207 REMARK 3 L13: -1.2056 L23: 1.0365 REMARK 3 S TENSOR REMARK 3 S11: 0.0437 S12: 0.6617 S13: -0.7042 REMARK 3 S21: 0.0213 S22: -0.2563 S23: 0.2572 REMARK 3 S31: 0.3271 S32: -0.0237 S33: 0.2127 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 : E 4 E 110 REMARK 3 ORIGIN FOR THE GROUP (A): -2.7920 -84.8550 11.9020 REMARK 3 T TENSOR REMARK 3 T11: -0.0816 T22: 0.0179 REMARK 3 T33: -0.1830 T12: -0.0113 REMARK 3 T13: 0.0832 T23: 0.0225 REMARK 3 L TENSOR REMARK 3 L11: 3.4630 L22: 2.1955 REMARK 3 L33: 2.4565 L12: 0.6504 REMARK 3 L13: 0.6124 L23: 0.4226 REMARK 3 S TENSOR REMARK 3 S11: -0.1372 S12: 0.5288 S13: 0.2586 REMARK 3 S21: -0.1433 S22: 0.0543 S23: -0.0315 REMARK 3 S31: -0.1897 S32: 0.1635 S33: 0.0829 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 : R 1 R 110 REMARK 3 ORIGIN FOR THE GROUP (A): -2.6770 -39.8730 -3.0380 REMARK 3 T TENSOR REMARK 3 T11: -0.0845 T22: 0.0048 REMARK 3 T33: -0.2449 T12: -0.0141 REMARK 3 T13: 0.0558 T23: 0.0381 REMARK 3 L TENSOR REMARK 3 L11: 3.6786 L22: 2.0390 REMARK 3 L33: 4.2916 L12: 0.1600 REMARK 3 L13: 0.5550 L23: 0.4550 REMARK 3 S TENSOR REMARK 3 S11: -0.0083 S12: 0.6705 S13: 0.2767 REMARK 3 S21: -0.2049 S22: -0.0372 S23: -0.0261 REMARK 3 S31: -0.2429 S32: 0.3204 S33: 0.0455 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 3B9K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-07. REMARK 100 THE RCSB ID CODE IS RCSB045249. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-JUL-05 REMARK 200 TEMPERATURE (KELVIN) : 93.2 REMARK 200 PH : 6.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945 REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45395 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.13100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.170 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, 0.1 M NA/K PHOSPHATE, 0.2 M REMARK 280 NACL, PH 6.2, SITTING DROP, TEMPERATURE 296K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 45.88950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.15500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.37350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.15500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.88950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.37350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 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 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC 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 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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: 6 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 LYS A 1 REMARK 465 PRO A 2 REMARK 465 GLN A 3 REMARK 465 VAL A 122 REMARK 465 ASN A 123 REMARK 465 SER A 124 REMARK 465 SER A 125 REMARK 465 ALA A 126 REMARK 465 ASP A 127 REMARK 465 LEU A 128 REMARK 465 VAL A 129 REMARK 465 PRO A 130 REMARK 465 ARG A 131 REMARK 465 SER B 118 REMARK 465 SER B 119 REMARK 465 ALA B 120 REMARK 465 ASP B 121 REMARK 465 LEU B 122 REMARK 465 VAL B 123 REMARK 465 PRO B 124 REMARK 465 ARG B 125 REMARK 465 LYS E 1 REMARK 465 PRO E 2 REMARK 465 GLN E 3 REMARK 465 VAL E 122 REMARK 465 ASN E 123 REMARK 465 SER E 124 REMARK 465 SER E 125 REMARK 465 ALA E 126 REMARK 465 ASP E 127 REMARK 465 LEU E 128 REMARK 465 VAL E 129 REMARK 465 PRO E 130 REMARK 465 ARG E 131 REMARK 465 SER F 118 REMARK 465 SER F 119 REMARK 465 ALA F 120 REMARK 465 ASP F 121 REMARK 465 LEU F 122 REMARK 465 VAL F 123 REMARK 465 PRO F 124 REMARK 465 ARG F 125 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 GLU H 58 CD GLU H 58 OE2 0.076 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU L 15 124.54 -37.47 REMARK 500 GLN L 27 142.05 173.93 REMARK 500 ASP L 30 55.79 36.34 REMARK 500 THR L 51 -51.61 76.34 REMARK 500 LEU L 94 -136.94 36.72 REMARK 500 ALA L 130 115.61 -164.50 REMARK 500 LYS H 64 -47.65 -25.66 REMARK 500 SER H 76 56.00 35.32 REMARK 500 SER H 82B 72.16 61.57 REMARK 500 PRO H 123 155.75 -46.85 REMARK 500 CYS H 128 34.50 39.83 REMARK 500 PHE H 148 139.39 -171.41 REMARK 500 SER H 161 21.21 47.70 REMARK 500 SER H 165 50.97 -160.19 REMARK 500 SER H 180 65.34 -152.80 REMARK 500 VAL H 193 131.43 -176.14 REMARK 500 TRP H 198 -70.28 -60.43 REMARK 500 SER A 31 91.51 -62.04 REMARK 500 SER A 33 -54.64 -145.06 REMARK 500 LYS A 46 91.89 -57.56 REMARK 500 VAL A 53 -66.57 -97.96 REMARK 500 ASP A 66 98.45 -62.18 REMARK 500 THR A 81 -147.21 53.83 REMARK 500 ASN A 90 -80.78 -67.51 REMARK 500 VAL A 118 71.68 -117.47 REMARK 500 LYS B 41 39.86 -76.43 REMARK 500 SER B 62 44.01 -98.00 REMARK 500 MET B 84 -78.60 -87.50 REMARK 500 ASN B 85 56.61 -91.87 REMARK 500 LYS B 103 121.58 8.11 REMARK 500 LYS C 31 -5.60 73.31 REMARK 500 TYR C 50 54.17 35.89 REMARK 500 THR C 51 -52.69 72.30 REMARK 500 ALA C 84 -169.73 -174.75 REMARK 500 LEU C 94 -128.90 35.68 REMARK 500 ALA C 130 120.54 -178.54 REMARK 500 PRO C 204 150.46 -46.00 REMARK 500 SER D 15 -12.45 82.36 REMARK 500 THR D 116 104.83 -53.32 REMARK 500 CYS D 128 30.84 38.10 REMARK 500 SER D 161 -4.88 66.05 REMARK 500 LEU D 164 73.60 -101.10 REMARK 500 GLN D 179 -60.91 -103.56 REMARK 500 SER D 180 56.27 -148.87 REMARK 500 PRO D 200 -13.12 -48.37 REMARK 500 LEU E 18 97.27 -69.73 REMARK 500 SER E 31 90.62 -61.94 REMARK 500 SER E 33 -52.52 -147.14 REMARK 500 SER E 45 70.59 47.57 REMARK 500 LYS E 46 90.54 -57.00 REMARK 500 REMARK 500 THIS ENTRY HAS 61 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 GLY B 109 THR B 110 142.67 REMARK 500 REMARK 500 REMARK: NULL 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 242 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 242