REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0104 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 53899 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) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2897 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) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3818 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3180 REMARK 3 BIN FREE R VALUE SET COUNT : 208 REMARK 3 BIN FREE R VALUE : 0.3520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12696 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 192 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.02000 REMARK 3 B22 (A**2) : -0.02000 REMARK 3 B33 (A**2) : 0.02000 REMARK 3 B12 (A**2) : -0.01000 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): 1.534 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.356 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.254 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.282 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13304 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18114 ; 1.057 ; 1.942 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1612 ; 5.505 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 568 ;34.933 ;24.049 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2076 ;14.380 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;13.668 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1971 ; 0.067 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10072 ; 0.004 ; 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): 8078 ; 0.095 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13074 ; 0.196 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5448 ; 0.356 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5364 ; 0.664 ; 4.500 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 D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 6 A 286 1 REMARK 3 1 D 6 D 286 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 2213 ; 0.020 ; 0.050 REMARK 3 TIGHT THERMAL 1 A (A**2): 2213 ; 0.010 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B E REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 99 1 REMARK 3 1 E 2 E 99 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 B (A): 782 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 2 B (A**2): 782 ; 0.010 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : L I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 1 L 214 1 REMARK 3 1 I 1 I 214 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 3 L (A): 1654 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 3 L (A**2): 1654 ; 0.010 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : H G REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 1 H 222 1 REMARK 3 1 G 1 G 222 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 4 H (A): 1657 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 4 H (A**2): 1657 ; 0.010 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : A D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 287 A 287 1 REMARK 3 1 D 287 D 287 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 5 A (A): 54 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 5 A (A**2): 54 ; 0.020 ; 0.500 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 6 A 185 REMARK 3 RESIDUE RANGE : A 506 A 512 REMARK 3 RESIDUE RANGE : A 287 A 287 REMARK 3 ORIGIN FOR THE GROUP (A): -58.7898 -83.4092 38.1217 REMARK 3 T TENSOR REMARK 3 T11: 0.3413 T22: 0.2304 REMARK 3 T33: 0.2471 T12: 0.1665 REMARK 3 T13: 0.0329 T23: -0.0293 REMARK 3 L TENSOR REMARK 3 L11: 4.2260 L22: 1.9824 REMARK 3 L33: 2.3445 L12: 1.2759 REMARK 3 L13: -1.4275 L23: -0.0517 REMARK 3 S TENSOR REMARK 3 S11: -0.0193 S12: 0.1875 S13: 0.2004 REMARK 3 S21: -0.3019 S22: -0.0648 S23: 0.1712 REMARK 3 S31: -0.0312 S32: -0.2028 S33: 0.0841 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 186 A 286 REMARK 3 ORIGIN FOR THE GROUP (A): -92.3617 -80.4484 57.0597 REMARK 3 T TENSOR REMARK 3 T11: 0.1890 T22: 0.1083 REMARK 3 T33: 0.4143 T12: 0.0484 REMARK 3 T13: -0.0803 T23: -0.0437 REMARK 3 L TENSOR REMARK 3 L11: 5.0724 L22: 4.0592 REMARK 3 L33: 8.2573 L12: -3.2077 REMARK 3 L13: -2.5707 L23: 3.9287 REMARK 3 S TENSOR REMARK 3 S11: -0.1558 S12: 0.3280 S13: 0.0291 REMARK 3 S21: -0.1424 S22: -0.1517 S23: 0.5085 REMARK 3 S31: -0.1090 S32: -0.4585 S33: 0.3075 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 : L 1 L 108 REMARK 3 ORIGIN FOR THE GROUP (A): -33.7866 -89.2702 20.4450 REMARK 3 T TENSOR REMARK 3 T11: 0.1871 T22: 0.1303 REMARK 3 T33: 0.1734 T12: 0.1295 REMARK 3 T13: 0.0323 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 3.6691 L22: 1.2621 REMARK 3 L33: 4.9272 L12: -0.9188 REMARK 3 L13: -0.8697 L23: 1.6764 REMARK 3 S TENSOR REMARK 3 S11: 0.3558 S12: 0.3521 S13: -0.3015 REMARK 3 S21: 0.0093 S22: -0.1858 S23: 0.1030 REMARK 3 S31: -0.1063 S32: -0.1871 S33: -0.1700 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 109 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): -0.9910 -99.6768 7.5596 REMARK 3 T TENSOR REMARK 3 T11: 0.2046 T22: 0.3960 REMARK 3 T33: 0.2784 T12: 0.1012 REMARK 3 T13: 0.0720 T23: 0.0556 REMARK 3 L TENSOR REMARK 3 L11: 7.7082 L22: 3.4106 REMARK 3 L33: 2.7745 L12: -2.5119 REMARK 3 L13: 0.5941 L23: -0.0179 REMARK 3 S TENSOR REMARK 3 S11: 0.2497 S12: -0.0347 S13: -0.3362 REMARK 3 S21: -0.1188 S22: -0.1152 S23: -0.4458 REMARK 3 S31: -0.0517 S32: 0.4307 S33: -0.1346 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 : H 1 H 120 REMARK 3 ORIGIN FOR THE GROUP (A): -22.0345 -75.7562 34.1283 REMARK 3 T TENSOR REMARK 3 T11: 0.4111 T22: 0.1930 REMARK 3 T33: 0.3063 T12: 0.0338 REMARK 3 T13: 0.1010 T23: -0.0561 REMARK 3 L TENSOR REMARK 3 L11: 7.4695 L22: 1.7997 REMARK 3 L33: 2.3242 L12: 2.1432 REMARK 3 L13: -0.1798 L23: 0.5081 REMARK 3 S TENSOR REMARK 3 S11: 0.2401 S12: -0.4840 S13: 0.8853 REMARK 3 S21: 0.1798 S22: -0.0680 S23: -0.0680 REMARK 3 S31: -0.6175 S32: 0.2679 S33: -0.1722 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 121 H 222 REMARK 3 ORIGIN FOR THE GROUP (A): 1.7080 -84.2549 5.2852 REMARK 3 T TENSOR REMARK 3 T11: 0.3800 T22: 0.4552 REMARK 3 T33: 0.5508 T12: -0.0371 REMARK 3 T13: 0.1789 T23: 0.1757 REMARK 3 L TENSOR REMARK 3 L11: 5.7874 L22: 3.7159 REMARK 3 L33: 8.4667 L12: 0.5910 REMARK 3 L13: 1.2190 L23: 2.1080 REMARK 3 S TENSOR REMARK 3 S11: -0.0467 S12: 0.3258 S13: 0.5344 REMARK 3 S21: -0.6861 S22: 0.1118 S23: -0.5253 REMARK 3 S31: -0.7894 S32: 0.7295 S33: -0.0651 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 99 REMARK 3 ORIGIN FOR THE GROUP (A): -72.6694 -88.1100 62.5438 REMARK 3 T TENSOR REMARK 3 T11: 0.2287 T22: 0.2651 REMARK 3 T33: 0.2954 T12: 0.1611 REMARK 3 T13: 0.0391 T23: -0.0976 REMARK 3 L TENSOR REMARK 3 L11: 6.3319 L22: 2.2748 REMARK 3 L33: 5.8956 L12: 2.1449 REMARK 3 L13: -3.0201 L23: -1.9832 REMARK 3 S TENSOR REMARK 3 S11: 0.2211 S12: -0.3133 S13: 0.2322 REMARK 3 S21: 0.0194 S22: -0.1591 S23: 0.0751 REMARK 3 S31: 0.2380 S32: 0.9215 S33: -0.0620 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 6 D 185 REMARK 3 RESIDUE RANGE : D 506 D 512 REMARK 3 RESIDUE RANGE : D 287 D 287 REMARK 3 ORIGIN FOR THE GROUP (A): -1.7405-102.1055 -38.2732 REMARK 3 T TENSOR REMARK 3 T11: 0.1938 T22: 0.6042 REMARK 3 T33: 0.2943 T12: -0.0023 REMARK 3 T13: 0.1510 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 2.6330 L22: 4.1031 REMARK 3 L33: 2.1507 L12: -1.1858 REMARK 3 L13: -1.0087 L23: 1.0599 REMARK 3 S TENSOR REMARK 3 S11: -0.2182 S12: -0.5288 S13: -0.1305 REMARK 3 S21: 0.3785 S22: -0.0156 S23: -0.2062 REMARK 3 S31: 0.0740 S32: 0.0345 S33: 0.2337 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 186 D 286 REMARK 3 ORIGIN FOR THE GROUP (A): 26.8810-119.5749 -57.5024 REMARK 3 T TENSOR REMARK 3 T11: 0.0969 T22: 0.2225 REMARK 3 T33: 0.3795 T12: -0.0504 REMARK 3 T13: 0.0815 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 7.7084 L22: 1.5891 REMARK 3 L33: 7.4224 L12: 0.0400 REMARK 3 L13: -4.4630 L23: -0.8859 REMARK 3 S TENSOR REMARK 3 S11: -0.2281 S12: -0.0610 S13: -0.2917 REMARK 3 S21: 0.1977 S22: 0.0325 S23: -0.1106 REMARK 3 S31: 0.1163 S32: 0.1258 S33: 0.1956 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 : E 2 E 99 REMARK 3 ORIGIN FOR THE GROUP (A): 6.5421-114.2208 -63.0070 REMARK 3 T TENSOR REMARK 3 T11: 0.1004 T22: 0.3809 REMARK 3 T33: 0.3914 T12: -0.0477 REMARK 3 T13: 0.1462 T23: -0.0311 REMARK 3 L TENSOR REMARK 3 L11: 3.6714 L22: 4.9533 REMARK 3 L33: 6.5226 L12: -2.0336 REMARK 3 L13: -0.8280 L23: 2.6523 REMARK 3 S TENSOR REMARK 3 S11: 0.0891 S12: -0.0015 S13: -0.2111 REMARK 3 S21: -0.1981 S22: -0.1632 S23: 0.2022 REMARK 3 S31: -0.3233 S32: -0.8406 S33: 0.0742 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 : I 1 I 108 REMARK 3 ORIGIN FOR THE GROUP (A): -25.3632 -92.2124 -20.5188 REMARK 3 T TENSOR REMARK 3 T11: 0.1222 T22: 0.4036 REMARK 3 T33: 0.2211 T12: 0.1185 REMARK 3 T13: 0.0266 T23: -0.0851 REMARK 3 L TENSOR REMARK 3 L11: 2.9840 L22: 0.8028 REMARK 3 L33: 5.6919 L12: -0.3620 REMARK 3 L13: -1.4718 L23: -0.7626 REMARK 3 S TENSOR REMARK 3 S11: -0.1067 S12: -0.2485 S13: -0.2803 REMARK 3 S21: -0.0684 S22: 0.1634 S23: 0.0061 REMARK 3 S31: 0.0423 S32: 0.2265 S33: -0.0568 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 : I 109 I 214 REMARK 3 ORIGIN FOR THE GROUP (A): -58.1265 -81.5100 -7.5993 REMARK 3 T TENSOR REMARK 3 T11: 0.1962 T22: 0.4538 REMARK 3 T33: 0.2419 T12: 0.1184 REMARK 3 T13: 0.0254 T23: -0.0637 REMARK 3 L TENSOR REMARK 3 L11: 6.5430 L22: 3.0258 REMARK 3 L33: 2.0115 L12: -0.8337 REMARK 3 L13: 0.8508 L23: -0.3888 REMARK 3 S TENSOR REMARK 3 S11: 0.1929 S12: -0.0526 S13: 0.1194 REMARK 3 S21: -0.1683 S22: -0.1024 S23: 0.6056 REMARK 3 S31: -0.0903 S32: -0.1772 S33: -0.0905 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : G 1 G 120 REMARK 3 ORIGIN FOR THE GROUP (A): -27.0207 -74.3405 -34.1655 REMARK 3 T TENSOR REMARK 3 T11: 0.3324 T22: 0.4380 REMARK 3 T33: 0.2519 T12: -0.0504 REMARK 3 T13: 0.1012 T23: -0.0673 REMARK 3 L TENSOR REMARK 3 L11: 3.4726 L22: 5.8176 REMARK 3 L33: 2.4577 L12: -3.4617 REMARK 3 L13: 0.2695 L23: -0.1773 REMARK 3 S TENSOR REMARK 3 S11: 0.0304 S12: 0.1998 S13: 0.5577 REMARK 3 S21: -0.3208 S22: 0.0382 S23: -0.4286 REMARK 3 S31: -0.5563 S32: 0.4557 S33: -0.0686 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : G 121 G 222 REMARK 3 ORIGIN FOR THE GROUP (A): -51.1977 -67.3728 -5.4532 REMARK 3 T TENSOR REMARK 3 T11: 0.4006 T22: 0.4061 REMARK 3 T33: 0.5104 T12: 0.0772 REMARK 3 T13: 0.0764 T23: -0.2373 REMARK 3 L TENSOR REMARK 3 L11: 4.1971 L22: 4.7221 REMARK 3 L33: 6.5589 L12: -0.3694 REMARK 3 L13: 0.1283 L23: -1.4464 REMARK 3 S TENSOR REMARK 3 S11: 0.3656 S12: -0.3554 S13: 0.7495 REMARK 3 S21: 0.3735 S22: -0.1149 S23: 0.3309 REMARK 3 S31: -1.0322 S32: 0.1776 S33: -0.2507 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 USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 3UBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-11. REMARK 100 THE RCSB ID CODE IS RCSB068560. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-FEB-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-ROOT I REMARK 200 -BEAM SINGLE CRYSTAL, ASYMMETRIC REMARK 200 CUT 4.965 DEGS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56798 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 37.890 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : 0.54900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 9.300 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 ENTRIES 2Q7Y AND 2BDN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 71.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 4% V/V TACSIMATE, PH 7.0, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-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 -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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.58600 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.58600 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 49.58600 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 39140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38880 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, I, G 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 A 1 REMARK 465 GLU A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLN A 5 REMARK 465 VAL A 196 REMARK 465 PRO A 197 REMARK 465 SER A 198 REMARK 465 SER A 199 REMARK 465 ALA A 200 REMARK 465 HIS A 201 REMARK 465 SER D 1 REMARK 465 GLU D 2 REMARK 465 ALA D 3 REMARK 465 GLN D 4 REMARK 465 GLN D 5 REMARK 465 PRO D 197 REMARK 465 SER D 198 REMARK 465 SER D 199 REMARK 465 ALA D 200 REMARK 465 HIS D 201 REMARK 465 ILE E 1 REMARK 465 ASP H 137 REMARK 465 ASP G 137 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 A 6 CG CD CE NZ REMARK 470 MET A 87 CG SD CE REMARK 470 LYS B 44 CG CD CE NZ REMARK 470 LYS D 6 CG CD CE NZ REMARK 470 MET D 87 CG SD CE REMARK 470 LYS E 58 CG CD CE NZ REMARK 470 ASN L 212 CG OD1 ND2 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 23 CG CD CE NZ REMARK 470 ASP H 180 CG OD1 OD2 REMARK 470 LYS H 212 CG CD CE NZ REMARK 470 SER I 7 OG REMARK 470 GLN G 1 CG CD OE1 NE2 REMARK 470 LYS G 23 CG CD CE NZ REMARK 470 THR G 138 OG1 CG2 REMARK 470 THR G 139 OG1 CG2 REMARK 470 GLN G 178 OE1 NE2 REMARK 470 LYS G 212 CG CD CE NZ 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 NH1 ARG L 32 O ARG H 103 2.09 REMARK 500 NH1 ARG I 32 O ARG G 103 2.12 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 ARG A 173 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG A 173 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ARG D 173 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES REMARK 500 ARG D 173 NE - CZ - NH2 ANGL. DEV. = 3.7 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 7 -120.82 -101.23 REMARK 500 ALA A 19 -76.31 -92.55 REMARK 500 SER A 22 24.86 -143.03 REMARK 500 ASP A 93 59.79 -90.31 REMARK 500 HIS A 280 -154.90 -150.21 REMARK 500 HIS A 282 -20.59 68.36 REMARK 500 TRP B 60 -1.68 76.11 REMARK 500 ASN D 7 -120.92 -101.60 REMARK 500 ALA D 19 -77.05 -92.81 REMARK 500 SER D 22 22.14 -142.87 REMARK 500 ASP D 93 59.85 -90.77 REMARK 500 ASP D 242 35.16 -99.49 REMARK 500 HIS D 280 -158.71 -151.57 REMARK 500 HIS D 281 62.22 -66.06 REMARK 500 HIS D 282 -33.56 66.52 REMARK 500 TRP E 60 -2.92 77.64 REMARK 500 TYR L 30 63.57 29.84 REMARK 500 ALA L 51 -45.56 71.17 REMARK 500 ASN L 190 -62.56 -95.17 REMARK 500 LYS L 199 -39.62 -39.92 REMARK 500 PRO H 41 112.27 -39.69 REMARK 500 ARG H 67 -23.41 82.22 REMARK 500 SER H 77 47.62 39.34 REMARK 500 CYS H 135 97.14 -66.43 REMARK 500 SER H 179 -95.40 60.07 REMARK 500 PRO H 196 30.42 -92.12 REMARK 500 TYR I 30 63.38 30.04 REMARK 500 ALA I 51 -45.63 71.33 REMARK 500 ASN I 190 -62.43 -96.57 REMARK 500 PRO G 41 110.27 -38.14 REMARK 500 ARG G 67 -20.97 80.33 REMARK 500 SER G 77 45.86 39.24 REMARK 500 GLU G 89 -8.30 -59.06 REMARK 500 CYS G 135 96.54 -66.09 REMARK 500 SER G 179 -95.70 60.45 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 09N A 287 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 09N D 287 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 512 REMARK 999 REMARK 999 SEQUENCE REMARK 999 CD1D1 D219H (CHAINS A,D) AND BETA-2-MICROGLOBULIN D105A (CHAINS B, REMARK 999 E) ARE NATURAL VARIANTS.