REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0081 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 68587 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) : 0.165 REMARK 3 R VALUE (WORKING SET) : 0.164 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500 REMARK 3 FREE R VALUE TEST SET COUNT : 1014 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) : 3.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4974 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.2510 REMARK 3 BIN FREE R VALUE SET COUNT : 70 REMARK 3 BIN FREE R VALUE : 0.2710 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 24414 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 13 REMARK 3 SOLVENT ATOMS : 42 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.31 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.12000 REMARK 3 B22 (A**2) : 0.12000 REMARK 3 B33 (A**2) : -0.17000 REMARK 3 B12 (A**2) : 0.06000 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): 0.422 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.316 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.979 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25030 ; 0.013 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34035 ; 1.527 ; 1.942 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3158 ; 6.682 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1022 ;37.130 ;23.806 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4033 ;18.703 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 123 ;18.633 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3790 ; 0.099 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18855 ; 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 : 3 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 633 1 REMARK 3 1 B 1 B 633 1 REMARK 3 1 C 1 C 633 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : L M N REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 2 L 212 1 REMARK 3 1 M 2 M 212 1 REMARK 3 1 N 2 N 212 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : H I J REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 2 H 222 1 REMARK 3 1 I 2 I 222 1 REMARK 3 1 J 2 J 222 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 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 633 REMARK 3 ORIGIN FOR THE GROUP (A): 14.6080 14.3470 0.2560 REMARK 3 T TENSOR REMARK 3 T11: 0.1813 T22: 0.0865 REMARK 3 T33: 0.0920 T12: 0.0179 REMARK 3 T13: 0.0080 T23: -0.0814 REMARK 3 L TENSOR REMARK 3 L11: 1.1604 L22: 0.9099 REMARK 3 L33: 1.6799 L12: 0.3800 REMARK 3 L13: -0.6646 L23: -0.5634 REMARK 3 S TENSOR REMARK 3 S11: 0.1003 S12: -0.1939 S13: 0.1630 REMARK 3 S21: 0.0378 S22: -0.0331 S23: -0.0576 REMARK 3 S31: 0.0079 S32: 0.1691 S33: -0.0671 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 633 REMARK 3 ORIGIN FOR THE GROUP (A): 86.5840 31.3660 -35.1240 REMARK 3 T TENSOR REMARK 3 T11: 0.2164 T22: 0.1804 REMARK 3 T33: 0.1333 T12: -0.1047 REMARK 3 T13: -0.1481 T23: 0.1090 REMARK 3 L TENSOR REMARK 3 L11: 1.0307 L22: 1.4894 REMARK 3 L33: 1.5560 L12: 0.1451 REMARK 3 L13: 0.1887 L23: 0.6295 REMARK 3 S TENSOR REMARK 3 S11: 0.2031 S12: -0.2889 S13: -0.1434 REMARK 3 S21: -0.0199 S22: -0.0373 S23: 0.1359 REMARK 3 S31: 0.1800 S32: -0.1383 S33: -0.1659 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 633 REMARK 3 ORIGIN FOR THE GROUP (A): 71.8870 -41.2160 3.4970 REMARK 3 T TENSOR REMARK 3 T11: 0.2326 T22: 0.1809 REMARK 3 T33: 0.3356 T12: 0.0079 REMARK 3 T13: -0.0947 T23: 0.0547 REMARK 3 L TENSOR REMARK 3 L11: 1.7513 L22: 0.6920 REMARK 3 L33: 1.5382 L12: -0.1354 REMARK 3 L13: -0.9279 L23: 0.1788 REMARK 3 S TENSOR REMARK 3 S11: -0.0390 S12: 0.2614 S13: 0.1718 REMARK 3 S21: -0.0822 S22: -0.0308 S23: 0.0627 REMARK 3 S31: -0.0957 S32: -0.2482 S33: 0.0698 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 1 L 106 REMARK 3 ORIGIN FOR THE GROUP (A): 35.4840 0.2960 -33.3700 REMARK 3 T TENSOR REMARK 3 T11: 0.1000 T22: 0.2218 REMARK 3 T33: 0.2248 T12: 0.0812 REMARK 3 T13: 0.0134 T23: -0.0820 REMARK 3 L TENSOR REMARK 3 L11: 1.2980 L22: 3.0271 REMARK 3 L33: 4.7619 L12: 1.5384 REMARK 3 L13: 0.7932 L23: 2.7113 REMARK 3 S TENSOR REMARK 3 S11: 0.0292 S12: 0.0584 S13: -0.0934 REMARK 3 S21: 0.0669 S22: -0.1412 S23: 0.2664 REMARK 3 S31: 0.1526 S32: -0.2157 S33: 0.1120 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 107 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): 54.1360 -28.3800 -47.3360 REMARK 3 T TENSOR REMARK 3 T11: 0.1629 T22: 0.3385 REMARK 3 T33: 0.1886 T12: 0.0763 REMARK 3 T13: 0.0200 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 6.5360 L22: 3.2798 REMARK 3 L33: 2.0284 L12: -1.8450 REMARK 3 L13: 1.9288 L23: 0.7249 REMARK 3 S TENSOR REMARK 3 S11: 0.0036 S12: -0.3430 S13: -0.6429 REMARK 3 S21: 0.0578 S22: 0.0475 S23: 0.1647 REMARK 3 S31: 0.3746 S32: 0.0421 S33: -0.0511 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 2 H 118 REMARK 3 ORIGIN FOR THE GROUP (A): 54.1520 5.4170 -23.4210 REMARK 3 T TENSOR REMARK 3 T11: 0.1517 T22: 0.4012 REMARK 3 T33: 0.1907 T12: 0.0306 REMARK 3 T13: 0.0254 T23: -0.1372 REMARK 3 L TENSOR REMARK 3 L11: 4.3921 L22: 5.5084 REMARK 3 L33: 4.0728 L12: -3.0150 REMARK 3 L13: 0.2828 L23: 1.5350 REMARK 3 S TENSOR REMARK 3 S11: 0.1355 S12: -0.1228 S13: 0.3676 REMARK 3 S21: 0.1646 S22: 0.0506 S23: -0.3562 REMARK 3 S31: -0.0683 S32: 0.8126 S33: -0.1861 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 : H 119 H 222 REMARK 3 ORIGIN FOR THE GROUP (A): 64.5910 -16.6910 -48.5930 REMARK 3 T TENSOR REMARK 3 T11: 0.0677 T22: 0.3327 REMARK 3 T33: 0.3347 T12: 0.0496 REMARK 3 T13: 0.0245 T23: -0.0080 REMARK 3 L TENSOR REMARK 3 L11: 3.9994 L22: 5.0881 REMARK 3 L33: 9.4820 L12: -0.8467 REMARK 3 L13: 0.7225 L23: 1.8462 REMARK 3 S TENSOR REMARK 3 S11: -0.1525 S12: 0.2084 S13: 0.2248 REMARK 3 S21: -0.3671 S22: 0.1889 S23: -0.1652 REMARK 3 S31: 0.0207 S32: -0.0391 S33: -0.0364 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 : M 1 M 106 REMARK 3 ORIGIN FOR THE GROUP (A): 61.7780 29.0050 -68.8030 REMARK 3 T TENSOR REMARK 3 T11: 0.1861 T22: 0.1775 REMARK 3 T33: 0.1923 T12: -0.0725 REMARK 3 T13: -0.1272 T23: 0.1070 REMARK 3 L TENSOR REMARK 3 L11: 2.9883 L22: 4.2698 REMARK 3 L33: 2.7814 L12: -0.7496 REMARK 3 L13: 1.7138 L23: -2.1559 REMARK 3 S TENSOR REMARK 3 S11: 0.3899 S12: 0.0796 S13: -0.1128 REMARK 3 S21: -0.1145 S22: -0.1280 S23: 0.1364 REMARK 3 S31: 0.1992 S32: -0.2423 S33: -0.2618 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 : M 107 M 212 REMARK 3 ORIGIN FOR THE GROUP (A): 29.0800 37.9110 -83.9530 REMARK 3 T TENSOR REMARK 3 T11: 0.2587 T22: 0.4510 REMARK 3 T33: 0.2658 T12: -0.0647 REMARK 3 T13: -0.0645 T23: 0.0112 REMARK 3 L TENSOR REMARK 3 L11: 6.3630 L22: 3.3658 REMARK 3 L33: 2.1127 L12: 1.0126 REMARK 3 L13: -0.4443 L23: -0.7111 REMARK 3 S TENSOR REMARK 3 S11: 0.3455 S12: -0.1227 S13: 0.2179 REMARK 3 S21: -0.0265 S22: -0.2316 S23: 0.5665 REMARK 3 S31: 0.0175 S32: -0.6408 S33: -0.1139 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 : I 4 I 118 REMARK 3 ORIGIN FOR THE GROUP (A): 50.4950 13.0770 -59.2390 REMARK 3 T TENSOR REMARK 3 T11: 0.8007 T22: 0.5188 REMARK 3 T33: 0.5172 T12: -0.5089 REMARK 3 T13: -0.2980 T23: 0.3101 REMARK 3 L TENSOR REMARK 3 L11: 7.6962 L22: 1.3800 REMARK 3 L33: 3.0338 L12: 0.8831 REMARK 3 L13: 3.0719 L23: -1.0050 REMARK 3 S TENSOR REMARK 3 S11: 0.6777 S12: -0.6073 S13: -1.0142 REMARK 3 S21: 0.0656 S22: 0.0757 S23: 0.1714 REMARK 3 S31: 0.7679 S32: -0.7279 S33: -0.7533 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 119 I 219 REMARK 3 ORIGIN FOR THE GROUP (A): 30.4670 22.3650 -85.2290 REMARK 3 T TENSOR REMARK 3 T11: 0.4412 T22: 0.3968 REMARK 3 T33: 0.5207 T12: -0.1784 REMARK 3 T13: -0.1487 T23: -0.0540 REMARK 3 L TENSOR REMARK 3 L11: 6.5314 L22: 3.1988 REMARK 3 L33: 9.2308 L12: 1.5190 REMARK 3 L13: -1.5735 L23: -2.1195 REMARK 3 S TENSOR REMARK 3 S11: 0.1611 S12: 0.2600 S13: -0.6911 REMARK 3 S21: -0.5476 S22: -0.0353 S23: -0.0151 REMARK 3 S31: 0.5758 S32: -0.5439 S33: -0.1257 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 : N 1 N 106 REMARK 3 ORIGIN FOR THE GROUP (A): 54.4970 -59.7600 36.5930 REMARK 3 T TENSOR REMARK 3 T11: 0.1205 T22: 0.3403 REMARK 3 T33: 0.4511 T12: -0.1056 REMARK 3 T13: -0.0552 T23: -0.0685 REMARK 3 L TENSOR REMARK 3 L11: 2.4421 L22: 4.3015 REMARK 3 L33: 2.4072 L12: -2.1315 REMARK 3 L13: 0.1027 L23: -2.0183 REMARK 3 S TENSOR REMARK 3 S11: -0.1112 S12: -0.1946 S13: -0.1918 REMARK 3 S21: 0.2820 S22: -0.0596 S23: -0.0698 REMARK 3 S31: 0.0880 S32: -0.2684 S33: 0.1708 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 : N 107 N 212 REMARK 3 ORIGIN FOR THE GROUP (A): 42.5210 -92.0660 50.4770 REMARK 3 T TENSOR REMARK 3 T11: 0.6518 T22: 0.8631 REMARK 3 T33: 1.3002 T12: -0.3419 REMARK 3 T13: -0.1898 T23: 0.2014 REMARK 3 L TENSOR REMARK 3 L11: 0.9531 L22: 1.8491 REMARK 3 L33: 2.6115 L12: -1.2709 REMARK 3 L13: 0.4757 L23: -0.2078 REMARK 3 S TENSOR REMARK 3 S11: 0.1953 S12: -0.2587 S13: -0.7034 REMARK 3 S21: -0.0089 S22: 0.3991 S23: 0.6940 REMARK 3 S31: 0.9190 S32: -0.8044 S33: -0.5944 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 : J 2 J 118 REMARK 3 ORIGIN FOR THE GROUP (A): 35.1840 -59.0910 26.6860 REMARK 3 T TENSOR REMARK 3 T11: 0.1665 T22: 0.5624 REMARK 3 T33: 0.5363 T12: -0.0099 REMARK 3 T13: -0.0271 T23: -0.0329 REMARK 3 L TENSOR REMARK 3 L11: 3.7166 L22: 4.3000 REMARK 3 L33: 3.9523 L12: 1.5676 REMARK 3 L13: 0.0285 L23: -2.4015 REMARK 3 S TENSOR REMARK 3 S11: 0.0804 S12: -0.0202 S13: 0.0567 REMARK 3 S21: 0.0356 S22: -0.0383 S23: 0.5052 REMARK 3 S31: -0.1999 S32: -0.7778 S33: -0.0421 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : J 119 J 219 REMARK 3 ORIGIN FOR THE GROUP (A): 30.2880 -82.2050 51.6740 REMARK 3 T TENSOR REMARK 3 T11: 0.4690 T22: 1.3815 REMARK 3 T33: 1.2887 T12: -0.2361 REMARK 3 T13: 0.1462 T23: 0.3196 REMARK 3 L TENSOR REMARK 3 L11: 3.3926 L22: 2.2553 REMARK 3 L33: 9.7014 L12: -0.8639 REMARK 3 L13: 5.0845 L23: -0.9976 REMARK 3 S TENSOR REMARK 3 S11: 0.0903 S12: -0.9570 S13: -0.7619 REMARK 3 S21: 0.3209 S22: 0.6934 S23: 0.8561 REMARK 3 S31: 0.4843 S32: -0.9796 S33: -0.7837 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: U VALUES : WITH TLS COMPONENT REMARK 3 INCLUDED REMARK 4 REMARK 4 3OPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-10. REMARK 100 THE RCSB ID CODE IS RCSB061427. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-APR-09 REMARK 200 TEMPERATURE (KELVIN) : 108 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : MULTILAYER MIRRORS (VARIMAX HF) REMARK 200 OPTICS : VARIMAX HF MULTILAYER MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68611 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 154.273 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.19000 REMARK 200 FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.51600 REMARK 200 R SYM FOR SHELL (I) : 0.51600 REMARK 200 FOR SHELL : 1.500 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 (%): 66.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINA, 10 % PEG 20000, 4% 1,4- REMARK 280 DIOXANO, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,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 46.90333 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 93.80667 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTRIMER, WITH THREE REMARK 300 TRIMERS IN THE ASU (CHAINS A-H-L, B-I-M AND C-J-N). EACH REMARK 300 HETEROTRIMERS CORRESPONDS TO A STABLE BINARY COMPLEX BETWEEN TRANS- REMARK 300 SIALIDASE (E.G. CHAIN A) AND A FAB IGG FRAGMENT, ITSELF A REMARK 300 HETERODIMER (CHAINS H AND L). 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, 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 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 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 MET A -13 REMARK 465 GLY A -12 REMARK 465 GLY A -11 REMARK 465 SER A -10 REMARK 465 HIS A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 GLY A -3 REMARK 465 MET A -2 REMARK 465 ALA A -1 REMARK 465 ASP A 400 REMARK 465 PRO A 401 REMARK 465 ALA A 402 REMARK 465 ALA A 403 REMARK 465 SER A 404 REMARK 465 SER A 405 REMARK 465 SER A 406 REMARK 465 GLU A 407 REMARK 465 ARG A 408 REMARK 465 ASP A 634 REMARK 465 MET B -13 REMARK 465 GLY B -12 REMARK 465 GLY B -11 REMARK 465 SER B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 GLY B -3 REMARK 465 MET B -2 REMARK 465 ALA B -1 REMARK 465 ASP B 400 REMARK 465 PRO B 401 REMARK 465 ALA B 402 REMARK 465 ALA B 403 REMARK 465 SER B 404 REMARK 465 SER B 405 REMARK 465 SER B 406 REMARK 465 GLU B 407 REMARK 465 ARG B 408 REMARK 465 ASP B 634 REMARK 465 MET C -13 REMARK 465 GLY C -12 REMARK 465 GLY C -11 REMARK 465 SER C -10 REMARK 465 HIS C -9 REMARK 465 HIS C -8 REMARK 465 HIS C -7 REMARK 465 HIS C -6 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 GLY C -3 REMARK 465 MET C -2 REMARK 465 ALA C -1 REMARK 465 ASP C 400 REMARK 465 PRO C 401 REMARK 465 ALA C 402 REMARK 465 ALA C 403 REMARK 465 SER C 404 REMARK 465 SER C 405 REMARK 465 SER C 406 REMARK 465 GLU C 407 REMARK 465 ARG C 408 REMARK 465 ASP C 634 REMARK 465 THR H 28 REMARK 465 ILE H 223 REMARK 465 SER I 138 REMARK 465 ILE I 223 REMARK 465 ILE J 223 REMARK 465 CYS L 213 REMARK 465 CYS M 213 REMARK 465 CYS N 213 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 SER A 0 OG REMARK 470 SER B 0 OG REMARK 470 SER C 0 OG REMARK 470 TYR H 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE H 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR H 30 OG1 CG2 REMARK 470 TYR H 31 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 TYR I 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS I 65 CG CD CE NZ REMARK 470 ASP I 136 CG OD1 OD2 REMARK 470 TYR J 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR J 28 OG1 CG2 REMARK 470 PHE J 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS J 65 CG CD CE NZ REMARK 470 THR L 9 OG1 CG2 REMARK 470 THR M 9 OG1 CG2 REMARK 470 THR N 9 OG1 CG2 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 CG2 VAL J 2 CB TYR J 27 1.82 REMARK 500 O SER J 140 CB SER J 191 1.83 REMARK 500 NZ LYS H 23 O SER H 76 1.95 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 GLU C 576 CG GLU C 576 CD 0.092 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 13 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.1 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 15 -63.50 -144.86 REMARK 500 ARG A 87 9.21 59.91 REMARK 500 GLU A 168 101.43 -36.59 REMARK 500 ASN A 173 -73.10 -118.92 REMARK 500 ALA A 179 174.74 69.77 REMARK 500 ASP A 258 51.37 -115.75 REMARK 500 THR A 269 -82.60 -132.10 REMARK 500 ARG A 311 -137.88 45.99 REMARK 500 ARG A 316 68.74 61.99 REMARK 500 GLN A 325 -62.63 -130.49 REMARK 500 ASP A 337 23.88 -79.30 REMARK 500 SER A 340 85.63 -159.45 REMARK 500 SER A 424 -121.84 -137.46 REMARK 500 VAL A 466 -71.65 -117.65 REMARK 500 PRO A 532 130.70 -37.85 REMARK 500 ASP A 575 -176.34 -65.95 REMARK 500 ASN A 604 73.25 39.70 REMARK 500 ALA B 2 152.61 -43.27 REMARK 500 SER B 15 -61.68 -143.13 REMARK 500 ARG B 87 12.27 59.11 REMARK 500 SER B 115 7.45 -152.62 REMARK 500 GLU B 168 103.41 -35.89 REMARK 500 ASN B 173 -70.32 -118.45 REMARK 500 ALA B 179 174.69 69.74 REMARK 500 ASP B 258 51.95 -116.23 REMARK 500 THR B 269 -80.59 -130.93 REMARK 500 ARG B 311 -139.71 50.96 REMARK 500 ARG B 316 68.84 61.65 REMARK 500 GLN B 325 -61.93 -131.04 REMARK 500 ASP B 337 28.27 -79.92 REMARK 500 SER B 340 88.10 -159.16 REMARK 500 SER B 424 -121.03 -139.17 REMARK 500 VAL B 466 -71.84 -118.45 REMARK 500 PRO B 532 129.66 -39.85 REMARK 500 GLU B 576 -10.08 -44.83 REMARK 500 ASN B 604 72.72 35.80 REMARK 500 HIS B 632 0.69 -66.79 REMARK 500 SER C 15 -61.74 -145.11 REMARK 500 ARG C 87 11.69 58.92 REMARK 500 SER C 115 8.05 -150.53 REMARK 500 GLU C 168 104.08 -40.71 REMARK 500 ASN C 173 -71.63 -119.35 REMARK 500 ALA C 179 173.21 70.14 REMARK 500 ASP C 258 51.49 -117.57 REMARK 500 THR C 269 -81.81 -131.77 REMARK 500 ARG C 311 -137.02 48.20 REMARK 500 ARG C 316 67.95 63.49 REMARK 500 GLN C 325 -60.93 -131.82 REMARK 500 ASP C 337 23.91 -76.65 REMARK 500 SER C 340 86.52 -159.81 REMARK 500 REMARK 500 THIS ENTRY HAS 86 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 I 135 ASP I 136 138.19 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 ALA H 24 24.3 L L OUTSIDE RANGE REMARK 500 LEU H 180 22.8 L L OUTSIDE RANGE REMARK 500 LEU I 180 23.8 L L OUTSIDE RANGE REMARK 500 LEU J 180 23.2 L L OUTSIDE RANGE REMARK 500 ASN L 144 24.6 L L OUTSIDE RANGE 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 NA A 635 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 636 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 635 REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS STATE THAT UNIPROT ENTRY Q26966 HAS FOUR SEQUENCE ERRORS. REMARK 999 THESE DISCREPANCIES HAVE BEEN REPEATEDLY INDICATED IN ALL PROVIOUS REMARK 999 XRAY STRUCTURES RELATED TO TRYPANOSOMA CRUZI TRANS-SIALIDASE. THESE REMARK 999 ERRORS CONCERN RESIDUES 262 (INDEED A THR), 476 (A HIS), 484 (A REMARK 999 LEU) AND 558 (A VAL). HENCE, THESE DISCREPANCIES IN CHAINS A, B AND REMARK 999 C, ARE NOT THE RESULT OF PROTEIN ENGINEERING.