REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 99.23 REMARK 3 NUMBER OF REFLECTIONS : 62651 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) : 0.20135 REMARK 3 R VALUE (WORKING SET) : 0.19862 REMARK 3 FREE R VALUE : 0.25403 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 3298 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) : 2.300 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.358 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4200 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91 REMARK 3 BIN R VALUE (WORKING SET) : 0.269 REMARK 3 BIN FREE R VALUE SET COUNT : 219 REMARK 3 BIN FREE R VALUE : 0.316 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11603 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 51 REMARK 3 SOLVENT ATOMS : 210 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.6 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.863 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.58 REMARK 3 B22 (A**2) : -0.47 REMARK 3 B33 (A**2) : -0.23 REMARK 3 B12 (A**2) : -0.00 REMARK 3 B13 (A**2) : -2.39 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.412 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.469 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11986 ; 0.010 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16335 ; 1.365 ; 1.953 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1508 ; 6.682 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 502 ;33.588 ;23.685 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1876 ;16.718 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;18.007 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1771 ; 0.093 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9162 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL 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 : 5 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 65 5 REMARK 3 1 B 1 B 65 5 REMARK 3 1 C 1 C 65 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 255 ; 0.07 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 B (A): 255 ; 0.08 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 C (A): 255 ; 0.06 ; 0.50 REMARK 3 LOOSE POSITIONAL 1 A (A): 257 ; 0.49 ; 5.00 REMARK 3 LOOSE POSITIONAL 1 B (A): 257 ; 0.61 ; 5.00 REMARK 3 LOOSE POSITIONAL 1 C (A): 257 ; 0.41 ; 5.00 REMARK 3 MEDIUM THERMAL 1 A (A**2): 255 ; 1.06 ; 2.00 REMARK 3 MEDIUM THERMAL 1 B (A**2): 255 ; 1.29 ; 2.00 REMARK 3 MEDIUM THERMAL 1 C (A**2): 255 ; 0.77 ; 2.00 REMARK 3 LOOSE THERMAL 1 A (A**2): 257 ; 1.77 ; 10.00 REMARK 3 LOOSE THERMAL 1 B (A**2): 257 ; 2.23 ; 10.00 REMARK 3 LOOSE THERMAL 1 C (A**2): 257 ; 1.16 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : L N M REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 1 L 113 5 REMARK 3 1 N 1 N 113 5 REMARK 3 1 M 1 M 113 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 L (A): 443 ; 0.21 ; 0.50 REMARK 3 MEDIUM POSITIONAL 2 M (A): 443 ; 0.13 ; 0.50 REMARK 3 MEDIUM POSITIONAL 2 N (A): 443 ; 0.14 ; 0.50 REMARK 3 LOOSE POSITIONAL 2 L (A): 399 ; 0.61 ; 5.00 REMARK 3 LOOSE POSITIONAL 2 M (A): 399 ; 0.56 ; 5.00 REMARK 3 LOOSE POSITIONAL 2 N (A): 399 ; 0.53 ; 5.00 REMARK 3 MEDIUM THERMAL 2 L (A**2): 443 ; 1.68 ; 2.00 REMARK 3 MEDIUM THERMAL 2 M (A**2): 443 ; 2.89 ; 2.00 REMARK 3 MEDIUM THERMAL 2 N (A**2): 443 ; 2.63 ; 2.00 REMARK 3 LOOSE THERMAL 2 L (A**2): 399 ; 2.18 ; 10.00 REMARK 3 LOOSE THERMAL 2 M (A**2): 399 ; 3.15 ; 10.00 REMARK 3 LOOSE THERMAL 2 N (A**2): 399 ; 2.85 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : L N M REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 114 L 216 5 REMARK 3 1 N 114 N 216 5 REMARK 3 1 M 114 M 216 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 L (A): 396 ; 0.21 ; 0.50 REMARK 3 MEDIUM POSITIONAL 3 M (A): 396 ; 0.22 ; 0.50 REMARK 3 MEDIUM POSITIONAL 3 N (A): 396 ; 0.20 ; 0.50 REMARK 3 LOOSE POSITIONAL 3 L (A): 371 ; 0.52 ; 5.00 REMARK 3 LOOSE POSITIONAL 3 M (A): 371 ; 0.54 ; 5.00 REMARK 3 LOOSE POSITIONAL 3 N (A): 371 ; 0.58 ; 5.00 REMARK 3 MEDIUM THERMAL 3 L (A**2): 396 ; 6.50 ; 2.00 REMARK 3 MEDIUM THERMAL 3 M (A**2): 396 ; 6.68 ; 2.00 REMARK 3 MEDIUM THERMAL 3 N (A**2): 396 ; 2.77 ; 2.00 REMARK 3 LOOSE THERMAL 3 L (A**2): 371 ; 6.36 ; 10.00 REMARK 3 LOOSE THERMAL 3 M (A**2): 371 ; 6.04 ; 10.00 REMARK 3 LOOSE THERMAL 3 N (A**2): 371 ; 2.87 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : H J I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 1 H 120 5 REMARK 3 1 J 1 J 120 5 REMARK 3 1 I 1 I 120 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 4 H (A): 472 ; 0.12 ; 0.50 REMARK 3 MEDIUM POSITIONAL 4 J (A): 472 ; 0.16 ; 0.50 REMARK 3 MEDIUM POSITIONAL 4 I (A): 472 ; 0.13 ; 0.50 REMARK 3 LOOSE POSITIONAL 4 H (A): 455 ; 0.37 ; 5.00 REMARK 3 LOOSE POSITIONAL 4 J (A): 455 ; 0.38 ; 5.00 REMARK 3 LOOSE POSITIONAL 4 I (A): 455 ; 0.43 ; 5.00 REMARK 3 MEDIUM THERMAL 4 H (A**2): 472 ; 1.62 ; 2.00 REMARK 3 MEDIUM THERMAL 4 J (A**2): 472 ; 2.88 ; 2.00 REMARK 3 MEDIUM THERMAL 4 I (A**2): 472 ; 2.04 ; 2.00 REMARK 3 LOOSE THERMAL 4 H (A**2): 455 ; 2.05 ; 10.00 REMARK 3 LOOSE THERMAL 4 J (A**2): 455 ; 2.77 ; 10.00 REMARK 3 LOOSE THERMAL 4 I (A**2): 455 ; 2.48 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : H J I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 121 H 216 5 REMARK 3 1 J 121 J 216 5 REMARK 3 1 I 121 I 216 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 5 H (A): 344 ; 0.20 ; 0.50 REMARK 3 MEDIUM POSITIONAL 5 J (A): 344 ; 0.24 ; 0.50 REMARK 3 MEDIUM POSITIONAL 5 I (A): 344 ; 0.29 ; 0.50 REMARK 3 LOOSE POSITIONAL 5 H (A): 290 ; 0.48 ; 5.00 REMARK 3 LOOSE POSITIONAL 5 J (A): 290 ; 0.55 ; 5.00 REMARK 3 LOOSE POSITIONAL 5 I (A): 290 ; 0.67 ; 5.00 REMARK 3 MEDIUM THERMAL 5 H (A**2): 344 ; 6.22 ; 2.00 REMARK 3 MEDIUM THERMAL 5 J (A**2): 344 ; 6.22 ; 2.00 REMARK 3 MEDIUM THERMAL 5 I (A**2): 344 ; 3.34 ; 2.00 REMARK 3 LOOSE THERMAL 5 H (A**2): 290 ; 6.06 ; 10.00 REMARK 3 LOOSE THERMAL 5 J (A**2): 290 ; 6.33 ; 10.00 REMARK 3 LOOSE THERMAL 5 I (A**2): 290 ; 3.98 ; 10.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 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 65 REMARK 3 ORIGIN FOR THE GROUP (A): 57.7666 15.3766 31.5451 REMARK 3 T TENSOR REMARK 3 T11: 0.1279 T22: 0.0435 REMARK 3 T33: 0.0409 T12: -0.0136 REMARK 3 T13: 0.0267 T23: 0.0097 REMARK 3 L TENSOR REMARK 3 L11: 2.1517 L22: 1.9545 REMARK 3 L33: 2.3903 L12: 0.0687 REMARK 3 L13: 0.0456 L23: -0.4315 REMARK 3 S TENSOR REMARK 3 S11: -0.0355 S12: 0.0288 S13: 0.0891 REMARK 3 S21: -0.1830 S22: 0.0901 S23: 0.1911 REMARK 3 S31: 0.0364 S32: -0.2871 S33: -0.0546 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 65 REMARK 3 ORIGIN FOR THE GROUP (A): 63.0949 34.7074 70.9147 REMARK 3 T TENSOR REMARK 3 T11: 0.1730 T22: 0.0513 REMARK 3 T33: 0.0593 T12: -0.0184 REMARK 3 T13: 0.0701 T23: 0.0047 REMARK 3 L TENSOR REMARK 3 L11: 2.7587 L22: 2.1138 REMARK 3 L33: 3.1449 L12: -0.2976 REMARK 3 L13: 0.6397 L23: -0.0663 REMARK 3 S TENSOR REMARK 3 S11: 0.0749 S12: 0.0627 S13: 0.0916 REMARK 3 S21: 0.2313 S22: -0.0639 S23: -0.1379 REMARK 3 S31: -0.0805 S32: 0.2365 S33: -0.0110 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 1 C 65 REMARK 3 ORIGIN FOR THE GROUP (A): 64.2187 -4.0034 19.6871 REMARK 3 T TENSOR REMARK 3 T11: 0.1433 T22: 0.0735 REMARK 3 T33: 0.0110 T12: -0.0241 REMARK 3 T13: 0.0117 T23: 0.0122 REMARK 3 L TENSOR REMARK 3 L11: 2.6070 L22: 2.4582 REMARK 3 L33: 3.0778 L12: -0.1320 REMARK 3 L13: 0.5770 L23: 0.7654 REMARK 3 S TENSOR REMARK 3 S11: -0.0054 S12: -0.0296 S13: 0.0829 REMARK 3 S21: 0.0116 S22: 0.0457 S23: -0.0239 REMARK 3 S31: -0.0695 S32: 0.2080 S33: -0.0403 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 113 REMARK 3 RESIDUE RANGE : H 1 H 120 REMARK 3 ORIGIN FOR THE GROUP (A): 79.7740 17.7184 47.9018 REMARK 3 T TENSOR REMARK 3 T11: 0.0737 T22: 0.0451 REMARK 3 T33: 0.0786 T12: 0.0369 REMARK 3 T13: 0.0233 T23: -0.0193 REMARK 3 L TENSOR REMARK 3 L11: 2.2533 L22: 1.2944 REMARK 3 L33: 0.8389 L12: 0.3844 REMARK 3 L13: 0.6291 L23: -0.3535 REMARK 3 S TENSOR REMARK 3 S11: -0.1435 S12: -0.0989 S13: 0.0376 REMARK 3 S21: 0.0509 S22: 0.0310 S23: -0.1737 REMARK 3 S31: -0.0449 S32: -0.0608 S33: 0.1125 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 114 L 218 REMARK 3 RESIDUE RANGE : H 121 H 220 REMARK 3 ORIGIN FOR THE GROUP (A): 109.8591 17.5694 64.3670 REMARK 3 T TENSOR REMARK 3 T11: 0.0854 T22: 0.1116 REMARK 3 T33: 0.2338 T12: 0.0245 REMARK 3 T13: -0.0080 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 1.5508 L22: 1.5972 REMARK 3 L33: 1.4213 L12: 0.3188 REMARK 3 L13: 0.2884 L23: -0.3526 REMARK 3 S TENSOR REMARK 3 S11: -0.0141 S12: -0.2173 S13: 0.0228 REMARK 3 S21: 0.0783 S22: -0.0571 S23: -0.0527 REMARK 3 S31: -0.0031 S32: 0.0221 S33: 0.0713 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 1 M 113 REMARK 3 RESIDUE RANGE : I 1 I 120 REMARK 3 ORIGIN FOR THE GROUP (A): 40.6420 37.7566 55.3839 REMARK 3 T TENSOR REMARK 3 T11: 0.0939 T22: 0.0841 REMARK 3 T33: 0.1305 T12: -0.0301 REMARK 3 T13: 0.0547 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 2.4996 L22: 1.4688 REMARK 3 L33: 1.5347 L12: -0.6574 REMARK 3 L13: 0.6757 L23: 0.1258 REMARK 3 S TENSOR REMARK 3 S11: -0.0739 S12: 0.0652 S13: 0.0192 REMARK 3 S21: -0.0312 S22: 0.0320 S23: 0.2826 REMARK 3 S31: 0.0185 S32: -0.0527 S33: 0.0419 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 114 M 217 REMARK 3 RESIDUE RANGE : I 121 I 219 REMARK 3 ORIGIN FOR THE GROUP (A): 9.9788 39.7576 40.4435 REMARK 3 T TENSOR REMARK 3 T11: 0.2106 T22: 0.3616 REMARK 3 T33: 0.3210 T12: 0.0378 REMARK 3 T13: -0.0162 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 3.2223 L22: 1.7893 REMARK 3 L33: 1.7587 L12: -1.1112 REMARK 3 L13: -0.2339 L23: 0.7917 REMARK 3 S TENSOR REMARK 3 S11: 0.2250 S12: 0.4629 S13: -0.2077 REMARK 3 S21: -0.2048 S22: -0.2062 S23: 0.1131 REMARK 3 S31: -0.0875 S32: -0.1311 S33: -0.0188 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : N 1 N 113 REMARK 3 RESIDUE RANGE : J 1 J 120 REMARK 3 ORIGIN FOR THE GROUP (A): 42.1409 -1.4595 3.3795 REMARK 3 T TENSOR REMARK 3 T11: 0.1658 T22: 0.1305 REMARK 3 T33: 0.0968 T12: -0.0221 REMARK 3 T13: -0.0779 T23: 0.0278 REMARK 3 L TENSOR REMARK 3 L11: 2.5674 L22: 1.3031 REMARK 3 L33: 1.9150 L12: -0.3086 REMARK 3 L13: 0.6016 L23: 0.3119 REMARK 3 S TENSOR REMARK 3 S11: -0.1882 S12: 0.1176 S13: 0.1015 REMARK 3 S21: -0.1363 S22: 0.0249 S23: 0.2588 REMARK 3 S31: -0.1232 S32: -0.1657 S33: 0.1632 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : N 114 N 217 REMARK 3 RESIDUE RANGE : J 121 J 218 REMARK 3 ORIGIN FOR THE GROUP (A): 12.0751 -1.0120 -12.0954 REMARK 3 T TENSOR REMARK 3 T11: 0.4231 T22: 0.7709 REMARK 3 T33: 0.4395 T12: -0.0615 REMARK 3 T13: -0.1940 T23: -0.0591 REMARK 3 L TENSOR REMARK 3 L11: 1.9192 L22: 2.6964 REMARK 3 L33: 1.6190 L12: -0.6986 REMARK 3 L13: 0.6589 L23: 1.2798 REMARK 3 S TENSOR REMARK 3 S11: -0.1041 S12: 0.1570 S13: 0.1052 REMARK 3 S21: -0.2181 S22: -0.1527 S23: 0.3652 REMARK 3 S31: -0.0508 S32: -0.4973 S33: 0.2568 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 RIDING REMARK 3 POSITIONS. U VALUES WITH TLS ADDED. HYDROGENS HAVE BEEN USED IF REMARK 3 PRESENT IN THE INPUT REMARK 4 REMARK 4 4AEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-12. REMARK 100 THE PDBE ID CODE IS EBI-50923. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4) REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65949 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30 REMARK 200 RESOLUTION RANGE LOW (A) : 13.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 4.0 REMARK 200 R MERGE (I) : 0.09 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.80 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) : 2.35 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.1 REMARK 200 R MERGE FOR SHELL (I) : 0.43 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.45 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 1PTX REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 2000 MME, 0.1 M HEPES PH REMARK 280 8.0, 0.1 M NACL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 19.37000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.3 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, M 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22270 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J, N 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 CYS H 222 REMARK 465 GLY H 223 REMARK 465 CYS H 224 REMARK 465 LYS H 225 REMARK 465 PRO H 226 REMARK 465 CYS H 227 REMARK 465 ILE H 228 REMARK 465 CYS H 229 REMARK 465 GLY I 134 REMARK 465 SER I 135 REMARK 465 ALA I 136 REMARK 465 ALA I 137 REMARK 465 GLN I 138 REMARK 465 THR I 139 REMARK 465 ASN I 140 REMARK 465 SER I 141 REMARK 465 MET I 142 REMARK 465 ARG I 220 REMARK 465 ASP I 221 REMARK 465 CYS I 222 REMARK 465 GLY I 223 REMARK 465 CYS I 224 REMARK 465 LYS I 225 REMARK 465 PRO I 226 REMARK 465 CYS I 227 REMARK 465 ILE I 228 REMARK 465 CYS I 229 REMARK 465 PRO J 133 REMARK 465 GLY J 134 REMARK 465 SER J 135 REMARK 465 ALA J 136 REMARK 465 ALA J 137 REMARK 465 GLN J 138 REMARK 465 THR J 139 REMARK 465 ASN J 140 REMARK 465 SER J 141 REMARK 465 MET J 142 REMARK 465 PRO J 219 REMARK 465 ARG J 220 REMARK 465 ASP J 221 REMARK 465 CYS J 222 REMARK 465 GLY J 223 REMARK 465 CYS J 224 REMARK 465 LYS J 225 REMARK 465 PRO J 226 REMARK 465 CYS J 227 REMARK 465 ILE J 228 REMARK 465 CYS J 229 REMARK 465 CYS L 219 REMARK 465 GLU M 218 REMARK 465 CYS M 219 REMARK 465 GLU N 218 REMARK 465 CYS N 219 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 CYS H 147 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 LEU L 88 CA - CB - CG ANGL. DEV. = 19.7 DEGREES REMARK 500 CYS L 139 CA - CB - SG ANGL. DEV. = 6.8 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 SER A 33 -179.59 -170.11 REMARK 500 ASP B 8 -168.93 -74.99 REMARK 500 ASP C 8 -167.38 -74.95 REMARK 500 SER H 119 149.29 -175.02 REMARK 500 GLN H 138 39.39 -76.36 REMARK 500 SER I 85 48.36 38.77 REMARK 500 ALA I 92 165.52 174.89 REMARK 500 TYR J 102 -70.06 -74.46 REMARK 500 PRO J 196 35.50 -91.27 REMARK 500 PRO L 8 -169.59 -72.81 REMARK 500 VAL L 56 -48.53 81.70 REMARK 500 LYS M 55 57.46 34.02 REMARK 500 VAL M 56 -56.37 78.47 REMARK 500 VAL N 56 -49.07 82.37 REMARK 500 SER N 57 -1.70 -141.32 REMARK 500 SER N 132 -73.12 -65.81 REMARK 500 ASP N 175 -1.14 -141.34 REMARK 500 ASN N 195 -53.80 -122.37 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 CL A1065 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1065 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1065 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A1066 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B1066 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE C1066 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SEG RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A TOXIN CHIMERA BETWEEN LQH-ALPHA REMARK 900 -ITFROM THE SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS REMARK 900 ANDAAH2 FROM ANDROCTONUS AUSTRALIS HECTOR REMARK 900 RELATED ID: 1PTX RELATED DB: PDB REMARK 900 SCORPION TOXIN II REMARK 900 RELATED ID: 1AHO RELATED DB: PDB REMARK 900 THE AB INITIO STRUCTURE DETERMINATION AND REFINEMENT OF REMARK 900 ASCORPION PROTEIN TOXIN REMARK 900 RELATED ID: 4AEH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-AAHI FAB9C2 ANTIBODY REMARK 999 REMARK 999 SEQUENCE REMARK 999 AMIDATED HIS64