REMARK 2 REMARK 2 RESOLUTION. 3.79 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) : 3.79 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 49884 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) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2686 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) : 3.79 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.89 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3416 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.37 REMARK 3 BIN R VALUE (WORKING SET) : 0.2520 REMARK 3 BIN FREE R VALUE SET COUNT : 180 REMARK 3 BIN FREE R VALUE : 0.3080 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 26981 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.12 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.59000 REMARK 3 B22 (A**2) : 0.88000 REMARK 3 B33 (A**2) : -0.29000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.10000 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): 0.802 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.630 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 94.958 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.878 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.829 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27604 ; 0.018 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 37422 ; 1.569 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3388 ; 7.767 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1322 ;38.719 ;24.962 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4690 ;19.868 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 114 ;17.425 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4108 ; 0.104 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21046 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 12786 ; 0.245 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 18672 ; 0.323 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 924 ; 0.173 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.296 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 102 ; 0.221 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.179 ; 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): 17294 ; 0.490 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 27308 ; 0.866 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11893 ; 0.975 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10114 ; 1.607 ; 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 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 2 A 431 REMARK 3 ORIGIN FOR THE GROUP (A): 50.8612 -17.6767 10.3281 REMARK 3 T TENSOR REMARK 3 T11: -0.4688 T22: -0.3915 REMARK 3 T33: -0.3865 T12: 0.0322 REMARK 3 T13: 0.0734 T23: -0.0072 REMARK 3 L TENSOR REMARK 3 L11: 4.7069 L22: 2.7265 REMARK 3 L33: 2.6265 L12: -0.4811 REMARK 3 L13: 1.4151 L23: 0.9229 REMARK 3 S TENSOR REMARK 3 S11: 0.0449 S12: 0.1040 S13: -0.1849 REMARK 3 S21: -0.0731 S22: 0.1942 S23: -0.0596 REMARK 3 S31: -0.0083 S32: 0.0839 S33: -0.2390 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 453 A 488 REMARK 3 ORIGIN FOR THE GROUP (A): 27.4704 -4.7601 8.2607 REMARK 3 T TENSOR REMARK 3 T11: -0.4772 T22: -0.1818 REMARK 3 T33: -0.4680 T12: 0.2575 REMARK 3 T13: 0.0701 T23: 0.0551 REMARK 3 L TENSOR REMARK 3 L11: 23.0181 L22: 15.7230 REMARK 3 L33: 27.2390 L12: 18.7078 REMARK 3 L13: 23.1964 L23: 19.6610 REMARK 3 S TENSOR REMARK 3 S11: 0.5666 S12: 0.2927 S13: -0.1033 REMARK 3 S21: -0.2365 S22: 0.2921 S23: -0.9445 REMARK 3 S31: 0.0763 S32: 0.0035 S33: -0.8587 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 493 A 621 REMARK 3 ORIGIN FOR THE GROUP (A): 40.6452 -4.9468 30.2930 REMARK 3 T TENSOR REMARK 3 T11: -0.2639 T22: 0.6956 REMARK 3 T33: -0.1916 T12: -0.0943 REMARK 3 T13: -0.0627 T23: -0.1017 REMARK 3 L TENSOR REMARK 3 L11: 4.1078 L22: 2.7105 REMARK 3 L33: 3.7256 L12: -1.2857 REMARK 3 L13: -1.4834 L23: 1.3153 REMARK 3 S TENSOR REMARK 3 S11: 0.1314 S12: -1.2866 S13: 0.4512 REMARK 3 S21: 0.0470 S22: 0.0648 S23: -0.4127 REMARK 3 S31: -0.3594 S32: -0.0029 S33: -0.1962 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 : A 627 A 872 REMARK 3 ORIGIN FOR THE GROUP (A): 19.3816 -10.7147 20.3912 REMARK 3 T TENSOR REMARK 3 T11: -0.5399 T22: 0.0054 REMARK 3 T33: -0.5063 T12: 0.0738 REMARK 3 T13: 0.1039 T23: 0.0098 REMARK 3 L TENSOR REMARK 3 L11: 8.0773 L22: 3.0209 REMARK 3 L33: 12.0024 L12: 2.2429 REMARK 3 L13: 7.2597 L23: 3.4509 REMARK 3 S TENSOR REMARK 3 S11: 0.4689 S12: -1.2309 S13: -0.2988 REMARK 3 S21: 0.2503 S22: -0.3111 S23: 0.0776 REMARK 3 S31: 0.6789 S32: -0.3881 S33: -0.1578 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 : A 873 A 1091 REMARK 3 ORIGIN FOR THE GROUP (A): -10.0677 -4.8968 24.8086 REMARK 3 T TENSOR REMARK 3 T11: -0.5918 T22: -0.3548 REMARK 3 T33: -0.4871 T12: 0.0701 REMARK 3 T13: -0.0039 T23: -0.1329 REMARK 3 L TENSOR REMARK 3 L11: 7.4685 L22: 3.8694 REMARK 3 L33: 4.2814 L12: 0.7639 REMARK 3 L13: -1.9729 L23: 0.9602 REMARK 3 S TENSOR REMARK 3 S11: 0.0812 S12: 0.7428 S13: -0.4332 REMARK 3 S21: -0.3884 S22: 0.1325 S23: -0.2549 REMARK 3 S31: -0.2173 S32: 0.2008 S33: -0.2136 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 : A 1092 A 1294 REMARK 3 ORIGIN FOR THE GROUP (A): -13.7535 -12.7175 57.8989 REMARK 3 T TENSOR REMARK 3 T11: -0.2639 T22: -0.5691 REMARK 3 T33: -0.3205 T12: 0.0524 REMARK 3 T13: -0.0613 T23: -0.0158 REMARK 3 L TENSOR REMARK 3 L11: 8.7706 L22: 4.3111 REMARK 3 L33: 8.7396 L12: -1.5088 REMARK 3 L13: 3.2125 L23: -3.0638 REMARK 3 S TENSOR REMARK 3 S11: 0.1072 S12: -0.2093 S13: -0.5144 REMARK 3 S21: 0.7423 S22: -0.0954 S23: -0.3570 REMARK 3 S31: -0.0560 S32: 0.1291 S33: -0.0118 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 2 B 431 REMARK 3 ORIGIN FOR THE GROUP (A): -1.2868 45.9869 82.6825 REMARK 3 T TENSOR REMARK 3 T11: -0.5411 T22: -0.6436 REMARK 3 T33: -0.2945 T12: -0.0328 REMARK 3 T13: -0.0550 T23: 0.0468 REMARK 3 L TENSOR REMARK 3 L11: 3.9586 L22: 2.9630 REMARK 3 L33: 3.2768 L12: -0.3619 REMARK 3 L13: -0.8674 L23: -1.4475 REMARK 3 S TENSOR REMARK 3 S11: 0.0623 S12: -0.1087 S13: -0.2362 REMARK 3 S21: -0.1673 S22: 0.1628 S23: 0.2426 REMARK 3 S31: 0.1417 S32: 0.0668 S33: -0.2251 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 453 B 488 REMARK 3 ORIGIN FOR THE GROUP (A): 22.2444 32.9935 80.5497 REMARK 3 T TENSOR REMARK 3 T11: -0.4542 T22: -0.1738 REMARK 3 T33: -0.0318 T12: 0.0817 REMARK 3 T13: -0.2244 T23: 0.1795 REMARK 3 L TENSOR REMARK 3 L11: 18.3722 L22: 16.1267 REMARK 3 L33: 29.0487 L12: 16.4855 REMARK 3 L13: -22.7388 L23: -21.0772 REMARK 3 S TENSOR REMARK 3 S11: 0.5042 S12: 0.3088 S13: -0.1124 REMARK 3 S21: -0.4040 S22: 0.2795 S23: 0.8159 REMARK 3 S31: -0.0167 S32: -0.0215 S33: -0.7838 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 : B 493 B 621 REMARK 3 ORIGIN FOR THE GROUP (A): 9.0438 33.3591 102.5012 REMARK 3 T TENSOR REMARK 3 T11: -0.3076 T22: 0.6014 REMARK 3 T33: -0.0544 T12: -0.0643 REMARK 3 T13: 0.2156 T23: 0.2275 REMARK 3 L TENSOR REMARK 3 L11: 3.7085 L22: 3.6882 REMARK 3 L33: 4.4292 L12: -1.2443 REMARK 3 L13: 2.2397 L23: -2.6955 REMARK 3 S TENSOR REMARK 3 S11: 0.0647 S12: -1.3187 S13: -0.7392 REMARK 3 S21: 0.2920 S22: 0.0215 S23: 0.2054 REMARK 3 S31: 0.2542 S32: -0.0575 S33: -0.0862 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 : B 627 B 872 REMARK 3 ORIGIN FOR THE GROUP (A): 30.3681 38.9866 92.6388 REMARK 3 T TENSOR REMARK 3 T11: -0.5752 T22: -0.2156 REMARK 3 T33: -0.2009 T12: 0.0410 REMARK 3 T13: -0.0435 T23: 0.1705 REMARK 3 L TENSOR REMARK 3 L11: 5.7485 L22: 3.1426 REMARK 3 L33: 11.2521 L12: 1.4250 REMARK 3 L13: -5.2736 L23: -3.1556 REMARK 3 S TENSOR REMARK 3 S11: 0.3943 S12: -1.1932 S13: 0.2707 REMARK 3 S21: 0.1249 S22: -0.2655 S23: -0.0899 REMARK 3 S31: -0.5251 S32: 0.4300 S33: -0.1287 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 : B 873 B 1091 REMARK 3 ORIGIN FOR THE GROUP (A): 59.7387 33.2504 97.2806 REMARK 3 T TENSOR REMARK 3 T11: -0.6236 T22: -0.5796 REMARK 3 T33: -0.1210 T12: 0.0024 REMARK 3 T13: 0.0812 T23: 0.2302 REMARK 3 L TENSOR REMARK 3 L11: 7.2287 L22: 4.7107 REMARK 3 L33: 4.5001 L12: 0.2835 REMARK 3 L13: 2.0665 L23: -1.6164 REMARK 3 S TENSOR REMARK 3 S11: 0.1447 S12: 0.4219 S13: 0.5088 REMARK 3 S21: -0.1044 S22: 0.1479 S23: 0.1120 REMARK 3 S31: 0.0405 S32: -0.3045 S33: -0.2926 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 : B 1092 B 1294 REMARK 3 ORIGIN FOR THE GROUP (A): 63.7410 40.7874 130.5810 REMARK 3 T TENSOR REMARK 3 T11: 0.2809 T22: -0.3026 REMARK 3 T33: 0.1152 T12: 0.1191 REMARK 3 T13: 0.0180 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 6.9235 L22: 4.5299 REMARK 3 L33: 12.8413 L12: -0.6527 REMARK 3 L13: -2.9485 L23: 3.4354 REMARK 3 S TENSOR REMARK 3 S11: 0.1520 S12: -0.9857 S13: 0.7697 REMARK 3 S21: 0.9998 S22: 0.0541 S23: 0.4297 REMARK 3 S31: -1.0665 S32: -0.2986 S33: -0.2061 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 : C 1 C 120 REMARK 3 ORIGIN FOR THE GROUP (A): -36.9907 23.4468 44.4781 REMARK 3 T TENSOR REMARK 3 T11: 0.9996 T22: -0.0041 REMARK 3 T33: -0.4481 T12: 0.6478 REMARK 3 T13: 0.2536 T23: 0.3499 REMARK 3 L TENSOR REMARK 3 L11: 8.3992 L22: 6.1728 REMARK 3 L33: 4.6327 L12: -6.5107 REMARK 3 L13: -3.1369 L23: 1.7395 REMARK 3 S TENSOR REMARK 3 S11: 0.0180 S12: -0.6132 S13: -0.1653 REMARK 3 S21: 0.9891 S22: 0.7174 S23: 0.5809 REMARK 3 S31: -2.0689 S32: -0.9945 S33: -0.7354 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 : C 121 C 216 REMARK 3 ORIGIN FOR THE GROUP (A): -61.2034 49.3819 35.9956 REMARK 3 T TENSOR REMARK 3 T11: 0.0703 T22: -0.1322 REMARK 3 T33: 0.1143 T12: 0.0232 REMARK 3 T13: 0.1032 T23: 0.2432 REMARK 3 L TENSOR REMARK 3 L11: 6.7792 L22: 5.9082 REMARK 3 L33: 24.9774 L12: -0.8134 REMARK 3 L13: 0.7672 L23: -6.4258 REMARK 3 S TENSOR REMARK 3 S11: 0.2328 S12: 0.2941 S13: -0.0191 REMARK 3 S21: -0.7515 S22: 0.2050 S23: 1.0306 REMARK 3 S31: 0.7619 S32: -0.9432 S33: -0.4378 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 : E 1 E 120 REMARK 3 ORIGIN FOR THE GROUP (A): 86.1353 4.7275 117.3314 REMARK 3 T TENSOR REMARK 3 T11: 0.3935 T22: -0.0201 REMARK 3 T33: -0.4621 T12: 0.3364 REMARK 3 T13: -0.1487 T23: -0.1106 REMARK 3 L TENSOR REMARK 3 L11: 6.4343 L22: 9.2660 REMARK 3 L33: 0.8473 L12: -6.9300 REMARK 3 L13: 2.0148 L23: -2.7945 REMARK 3 S TENSOR REMARK 3 S11: -0.5311 S12: -0.7147 S13: 0.3222 REMARK 3 S21: 1.0639 S22: 0.9323 S23: -0.0527 REMARK 3 S31: 0.6413 S32: 0.5090 S33: -0.4012 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 121 E 216 REMARK 3 ORIGIN FOR THE GROUP (A): 108.4955 -22.5335 110.0845 REMARK 3 T TENSOR REMARK 3 T11: -0.1791 T22: -0.1642 REMARK 3 T33: -0.3129 T12: 0.1177 REMARK 3 T13: -0.2072 T23: -0.0876 REMARK 3 L TENSOR REMARK 3 L11: 5.5312 L22: 7.8221 REMARK 3 L33: 27.3887 L12: -3.9970 REMARK 3 L13: -5.4778 L23: 8.7957 REMARK 3 S TENSOR REMARK 3 S11: 0.0599 S12: 0.1688 S13: -0.2919 REMARK 3 S21: -0.5127 S22: 0.0890 S23: -0.5528 REMARK 3 S31: -0.5896 S32: 1.0219 S33: -0.1489 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 2 D 109 REMARK 3 ORIGIN FOR THE GROUP (A): -28.2116 24.4078 23.8547 REMARK 3 T TENSOR REMARK 3 T11: 0.4149 T22: -0.2986 REMARK 3 T33: -0.6104 T12: 0.2646 REMARK 3 T13: 0.1877 T23: 0.0215 REMARK 3 L TENSOR REMARK 3 L11: 3.6958 L22: 9.0602 REMARK 3 L33: 14.1502 L12: -3.5201 REMARK 3 L13: 1.1359 L23: -3.8785 REMARK 3 S TENSOR REMARK 3 S11: 0.1801 S12: 0.3049 S13: -0.0595 REMARK 3 S21: -0.2359 S22: 0.1791 S23: 0.1902 REMARK 3 S31: -2.5132 S32: -0.0740 S33: -0.3592 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 110 D 218 REMARK 3 ORIGIN FOR THE GROUP (A): -45.9429 52.1152 29.3406 REMARK 3 T TENSOR REMARK 3 T11: 0.1812 T22: 0.1047 REMARK 3 T33: -0.2331 T12: 0.3711 REMARK 3 T13: 0.0479 T23: 0.5628 REMARK 3 L TENSOR REMARK 3 L11: 5.8516 L22: 14.0372 REMARK 3 L33: 9.2288 L12: -1.1251 REMARK 3 L13: -0.7441 L23: 0.9930 REMARK 3 S TENSOR REMARK 3 S11: 0.2082 S12: 0.1086 S13: 0.4036 REMARK 3 S21: 0.0678 S22: -0.4997 S23: -0.3112 REMARK 3 S31: 0.1374 S32: 1.4599 S33: 0.2915 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 2 F 109 REMARK 3 ORIGIN FOR THE GROUP (A): 77.6303 3.6650 96.5770 REMARK 3 T TENSOR REMARK 3 T11: -0.1783 T22: -0.4400 REMARK 3 T33: -0.4986 T12: 0.1340 REMARK 3 T13: -0.2432 T23: 0.1638 REMARK 3 L TENSOR REMARK 3 L11: 8.5232 L22: 8.5922 REMARK 3 L33: 9.8480 L12: -4.4767 REMARK 3 L13: -4.9403 L23: 2.2923 REMARK 3 S TENSOR REMARK 3 S11: 0.1551 S12: 0.3637 S13: -0.0797 REMARK 3 S21: -0.1721 S22: 0.2710 S23: 0.2092 REMARK 3 S31: 1.2988 S32: 0.2491 S33: -0.4260 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 110 F 218 REMARK 3 ORIGIN FOR THE GROUP (A): 93.3426 -24.3898 102.9857 REMARK 3 T TENSOR REMARK 3 T11: -0.0137 T22: -0.1488 REMARK 3 T33: -0.4255 T12: 0.2634 REMARK 3 T13: -0.1624 T23: -0.4277 REMARK 3 L TENSOR REMARK 3 L11: 7.4398 L22: 11.4729 REMARK 3 L33: 13.1773 L12: 0.9773 REMARK 3 L13: -0.8952 L23: -3.5481 REMARK 3 S TENSOR REMARK 3 S11: 0.3119 S12: 0.1627 S13: -0.7215 REMARK 3 S21: -0.4222 S22: -0.3053 S23: -0.0661 REMARK 3 S31: 1.2951 S32: -0.3976 S33: -0.0066 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2NZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-06. REMARK 100 THE RCSB ID CODE IS RCSB040487. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 214725 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.5 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 59.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.45000 REMARK 200 FOR SHELL : 1.700 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 3BTA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 20000, 8% PEG 550 MME, 200 MM REMARK 280 CALCIUM ACETATE, 100 MM SODIUM ACETATE, PH 5.60, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 297K 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 98.79800 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 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: 5890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 70520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 5830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 70520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLY A 433 REMARK 465 ILE A 434 REMARK 465 ILE A 435 REMARK 465 THR A 436 REMARK 465 SER A 437 REMARK 465 LYS A 438 REMARK 465 THR A 439 REMARK 465 LYS A 440 REMARK 465 SER A 441 REMARK 465 LEU A 442 REMARK 465 ASP A 443 REMARK 465 LYS A 444 REMARK 465 GLY A 445 REMARK 465 TYR A 446 REMARK 465 ASN A 447 REMARK 465 LYS A 448 REMARK 465 ALA A 449 REMARK 465 LEU A 450 REMARK 465 ASN A 451 REMARK 465 ASP A 452 REMARK 465 ALA A 490 REMARK 465 GLU A 491 REMARK 465 GLU A 492 REMARK 465 THR A 623 REMARK 465 THR A 624 REMARK 465 ASP A 625 REMARK 465 LYS A 626 REMARK 465 LEU A 1296 REMARK 465 GLY B 433 REMARK 465 ILE B 434 REMARK 465 ILE B 435 REMARK 465 THR B 436 REMARK 465 SER B 437 REMARK 465 LYS B 438 REMARK 465 THR B 439 REMARK 465 LYS B 440 REMARK 465 SER B 441 REMARK 465 LEU B 442 REMARK 465 ASP B 443 REMARK 465 LYS B 444 REMARK 465 GLY B 445 REMARK 465 TYR B 446 REMARK 465 ASN B 447 REMARK 465 LYS B 448 REMARK 465 ALA B 449 REMARK 465 LEU B 450 REMARK 465 ASN B 451 REMARK 465 ASP B 452 REMARK 465 ALA B 490 REMARK 465 GLU B 491 REMARK 465 GLU B 492 REMARK 465 THR B 623 REMARK 465 THR B 624 REMARK 465 ASP B 625 REMARK 465 LYS B 626 REMARK 465 LEU B 1296 REMARK 465 GLU C 217 REMARK 465 CYS C 218 REMARK 465 GLN D 1 REMARK 465 LYS D 219 REMARK 465 SER D 220 REMARK 465 CYS D 221 REMARK 465 ASP D 222 REMARK 465 LYS D 223 REMARK 465 THR D 224 REMARK 465 GLU E 217 REMARK 465 CYS E 218 REMARK 465 GLN F 1 REMARK 465 LYS F 219 REMARK 465 SER F 220 REMARK 465 CYS F 221 REMARK 465 ASP F 222 REMARK 465 LYS F 223 REMARK 465 THR F 224 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 542 CD CE NZ REMARK 470 LYS A 547 CG CD CE NZ REMARK 470 GLU A 560 CB CG CD OE1 OE2 REMARK 470 HIS A 561 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 563 CB CG CD CE NZ REMARK 470 SER A 564 CB OG REMARK 470 ARG A 565 CB CG CD NE CZ NH1 NH2 REMARK 470 ILE A 566 CB CG1 CG2 CD1 REMARK 470 ASN A 645 CB CG OD1 REMARK 470 MET A 646 CB CG SD CE REMARK 470 LEU A 647 CG CD1 CD2 REMARK 470 TYR A 648 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 648 OH REMARK 470 LYS A 649 CB CG CD CE NZ REMARK 470 ASP A 650 CB CG OD1 OD2 REMARK 470 TYR A 754 CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR A 755 CB OG1 CG2 REMARK 470 GLU A 756 CB CG CD OE1 OE2 REMARK 470 GLU A 757 CB CG CD OE1 OE2 REMARK 470 GLU A 758 CB CG CD OE1 OE2 REMARK 470 LYS A 759 CB CG CD CE NZ REMARK 470 ASN A 760 CB CG OD1 REMARK 470 ASN A 761 CB CG OD1 REMARK 470 ASP A 989 CB CG OD1 OD2 REMARK 470 GLN A 991 CG CD OE1 NE2 REMARK 470 GLU A 992 CB CG CD OE1 OE2 REMARK 470 ASN A1046 CG OD1 REMARK 470 ILE A1047 CG1 CG2 CD1 REMARK 470 SER A1167 CB OG REMARK 470 ASN A1169 CB CG OD1 REMARK 470 LYS A1170 CB CG CD CE NZ REMARK 470 LYS B 542 CD CE NZ REMARK 470 LYS B 547 CG CD CE NZ REMARK 470 GLU B 560 CB CG CD OE1 OE2 REMARK 470 HIS B 561 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 563 CB CG CD CE NZ REMARK 470 SER B 564 CB OG REMARK 470 ARG B 565 CB CG CD NE CZ NH1 NH2 REMARK 470 ILE B 566 CB CG1 CG2 CD1 REMARK 470 ASN B 645 CB CG OD1 REMARK 470 MET B 646 CB CG SD CE REMARK 470 LEU B 647 CG CD1 CD2 REMARK 470 TYR B 648 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 648 OH REMARK 470 LYS B 649 CB CG CD CE NZ REMARK 470 ASP B 650 CB CG OD1 OD2 REMARK 470 THR B 755 CB OG1 CG2 REMARK 470 GLU B 756 CB CG CD OE1 OE2 REMARK 470 GLU B 757 CB CG CD OE1 OE2 REMARK 470 GLU B 758 CB CG CD OE1 OE2 REMARK 470 LYS B 759 CB CG CD CE NZ REMARK 470 ASN B 760 CB CG OD1 REMARK 470 ASN B 761 CB CG OD1 REMARK 470 ASP B 989 CB CG OD1 OD2 REMARK 470 GLN B 991 CG CD OE1 NE2 REMARK 470 GLU B 992 CB CG CD OE1 OE2 REMARK 470 ILE B 993 CG1 CG2 CD1 REMARK 470 ASN B1046 CG OD1 REMARK 470 ILE B1047 CG1 CG2 CD1 REMARK 470 SER B1167 CB OG REMARK 470 ASN B1169 CB CG OD1 REMARK 470 LYS B1170 CB CG CD CE NZ REMARK 470 ASP C 171 CG OD1 OD2 REMARK 470 LYS C 173 CB CG CD CE NZ REMARK 470 LYS D 134 CG CD CE NZ REMARK 470 SER D 137 CB OG REMARK 470 ASP E 171 CG OD1 OD2 REMARK 470 LYS E 173 CB CG CD CE NZ REMARK 470 LYS F 134 CG CD CE NZ REMARK 470 SER F 137 CB OG 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 PRO B1212 C - N - CD ANGL. DEV. = -14.6 DEGREES REMARK 500 PRO D 154 C - N - CD ANGL. DEV. = -18.3 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 ASP A 18 -3.85 -140.21 REMARK 500 ASN A 40 117.16 -39.45 REMARK 500 LYS A 41 -14.70 86.47 REMARK 500 ASP A 49 93.99 -59.18 REMARK 500 SER A 121 103.63 23.59 REMARK 500 SER A 157 -156.49 -75.67 REMARK 500 ARG A 177 32.11 -142.31 REMARK 500 ASN A 178 12.83 -148.93 REMARK 500 SER A 199 46.96 -144.10 REMARK 500 THR A 204 -52.08 -127.51 REMARK 500 ALA A 210 -57.61 175.85 REMARK 500 ASN A 238 133.20 -39.17 REMARK 500 THR A 247 4.19 -161.02 REMARK 500 SER A 254 -63.03 -17.59 REMARK 500 LEU A 256 122.18 167.83 REMARK 500 ASP A 326 -153.02 -85.74 REMARK 500 ALA A 399 -151.32 -64.41 REMARK 500 ASN A 400 77.00 -54.01 REMARK 500 PHE A 401 24.32 40.14 REMARK 500 ASP A 509 -146.55 -131.91 REMARK 500 ASN A 533 -17.80 92.72 REMARK 500 LYS A 541 94.51 87.73 REMARK 500 GLU A 560 -25.11 159.18 REMARK 500 HIS A 561 13.36 -162.73 REMARK 500 LYS A 563 -121.35 -84.13 REMARK 500 SER A 564 90.92 -41.37 REMARK 500 ILE A 566 -118.40 -71.13 REMARK 500 ALA A 567 81.57 40.94 REMARK 500 VAL A 572 77.42 61.53 REMARK 500 LEU A 576 -71.84 2.07 REMARK 500 LEU A 577 34.46 -66.12 REMARK 500 ASN A 578 -151.13 -127.39 REMARK 500 ARG A 581 85.02 -68.17 REMARK 500 SER A 588 -56.86 -30.00 REMARK 500 ASP A 589 -38.57 -32.51 REMARK 500 ALA A 597 41.88 86.38 REMARK 500 TRP A 606 -51.13 -16.55 REMARK 500 VAL A 607 -71.38 -73.62 REMARK 500 GLU A 608 -65.97 -20.34 REMARK 500 ALA A 640 -71.29 -51.59 REMARK 500 ASN A 645 3.11 101.74 REMARK 500 VAL A 662 -14.59 -49.98 REMARK 500 TYR A 710 -70.72 -51.55 REMARK 500 TYR A 754 -144.84 -112.33 REMARK 500 THR A 755 -80.64 -11.76 REMARK 500 GLU A 757 -137.37 62.78 REMARK 500 LYS A 759 -133.16 70.54 REMARK 500 ASN A 760 49.09 -54.02 REMARK 500 ASN A 761 -29.37 -148.06 REMARK 500 ASN A 763 123.55 -33.54 REMARK 500 REMARK 500 THIS ENTRY HAS 252 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 TRP A 118 GLY A 119 46.69 REMARK 500 GLY A 119 GLY A 120 -146.40 REMARK 500 ASP A 484 THR A 485 -143.54 REMARK 500 ASN A 507 PHE A 508 -148.15 REMARK 500 LYS A 547 TYR A 548 147.15 REMARK 500 SER A 564 ARG A 565 115.31 REMARK 500 ASN A 573 GLU A 574 48.88 REMARK 500 GLU A 574 ALA A 575 134.86 REMARK 500 ASN A 578 PRO A 579 50.60 REMARK 500 LYS A 596 ALA A 597 42.27 REMARK 500 THR A 598 GLU A 599 147.60 REMARK 500 LEU A 604 GLY A 605 51.15 REMARK 500 GLY A 644 ASN A 645 -69.02 REMARK 500 ASN A 645 MET A 646 -139.30 REMARK 500 GLN A 753 TYR A 754 -143.09 REMARK 500 THR A 847 ASP A 848 127.60 REMARK 500 ASP A 989 THR A 990 -56.05 REMARK 500 GLU A 992 ILE A 993 59.12 REMARK 500 PRO A 1139 ARG A 1140 143.89 REMARK 500 SER A 1167 GLY A 1168 -125.96 REMARK 500 LYS A 1226 ASN A 1227 143.26 REMARK 500 ASN A 1227 ASP A 1228 147.85 REMARK 500 ASP A 1228 GLN A 1229 142.39 REMARK 500 THR A 1232 ASN A 1233 -144.03 REMARK 500 GLN A 1254 PHE A 1255 140.97 REMARK 500 ASN A 1257 ILE A 1258 -145.64 REMARK 500 TRP B 118 GLY B 119 86.37 REMARK 500 GLY B 119 GLY B 120 -147.11 REMARK 500 GLY B 120 SER B 121 149.37 REMARK 500 GLU B 148 LEU B 149 -144.25 REMARK 500 ILE B 487 GLU B 488 148.51 REMARK 500 PRO B 532 ASN B 533 39.88 REMARK 500 PHE B 559 GLU B 560 47.08 REMARK 500 SER B 564 ARG B 565 144.03 REMARK 500 ASN B 573 GLU B 574 51.51 REMARK 500 GLU B 574 ALA B 575 134.74 REMARK 500 ASN B 578 PRO B 579 35.33 REMARK 500 LYS B 596 ALA B 597 55.94 REMARK 500 LEU B 604 GLY B 605 43.58 REMARK 500 GLY B 644 ASN B 645 -70.79 REMARK 500 ASN B 645 MET B 646 -144.46 REMARK 500 LYS B 649 ASP B 650 -146.78 REMARK 500 ASP B 650 ASP B 651 143.10 REMARK 500 GLN B 753 TYR B 754 -135.85 REMARK 500 THR B 847 ASP B 848 147.25 REMARK 500 ASP B 989 THR B 990 -38.97 REMARK 500 THR B 990 GLN B 991 -130.58 REMARK 500 GLN B 991 GLU B 992 129.67 REMARK 500 LYS B 994 GLN B 995 141.29 REMARK 500 ASP B 1228 GLN B 1229 89.42 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 1 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 262 OE1 REMARK 620 2 GLU A 262 OE2 56.7 REMARK 620 3 HIS A 227 NE2 71.2 88.4 REMARK 620 4 HIS A 223 NE2 125.9 76.0 83.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B1297 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 262 OE2 REMARK 620 2 HIS B 223 NE2 81.6 REMARK 620 3 GLU B 262 OE1 62.2 141.9 REMARK 620 4 HIS B 227 NE2 91.5 92.4 78.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B1298 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS B 711 NZ REMARK 620 2 GLU B 279 OE1 76.3 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1297 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1297 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1298 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2NYY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE A COMPLEXED REMARK 900 WITH MONOCLONAL ANTIBODY CR1 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE AVAILABLE REMARK 999 FOR THE CR1 MONOCLONAL ANTIBODY LIGHT AND HEAVY CHAINS