REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.40 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3 REMARK 3 NUMBER OF REFLECTIONS : 56514 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) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3020 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4254 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.04 REMARK 3 BIN R VALUE (WORKING SET) : 0.3200 REMARK 3 BIN FREE R VALUE SET COUNT : 247 REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15323 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 27 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 65.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.25000 REMARK 3 B22 (A**2) : -1.23000 REMARK 3 B33 (A**2) : -1.95000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.99000 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): 0.408 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.271 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.456 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15719 ; 0.013 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21442 ; 1.624 ; 1.953 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2022 ; 7.650 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 611 ;38.169 ;24.566 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2423 ;21.787 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;22.560 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2414 ; 0.114 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11892 ; 0.008 ; 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): 10136 ; 0.533 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16401 ; 0.828 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5583 ; 0.624 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5041 ; 0.882 ; 3.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : K I J REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 K 2 K 220 1 REMARK 3 1 I 2 I 220 1 REMARK 3 1 J 2 J 220 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 K (A): 1607 ; 0.09 ; 0.05 REMARK 3 TIGHT POSITIONAL 1 I (A): 1607 ; 0.06 ; 0.05 REMARK 3 TIGHT POSITIONAL 1 J (A): 1607 ; 0.07 ; 0.05 REMARK 3 TIGHT THERMAL 1 K (A**2): 1607 ; 0.15 ; 0.50 REMARK 3 TIGHT THERMAL 1 I (A**2): 1607 ; 0.14 ; 0.50 REMARK 3 TIGHT THERMAL 1 J (A**2): 1607 ; 0.13 ; 0.50 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : O M N L REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 O 2 O 213 1 REMARK 3 1 M 2 M 213 1 REMARK 3 1 N 2 N 213 1 REMARK 3 1 L 2 L 213 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 O (A): 1558 ; 0.09 ; 0.05 REMARK 3 TIGHT POSITIONAL 2 M (A): 1558 ; 0.08 ; 0.05 REMARK 3 TIGHT POSITIONAL 2 N (A): 1558 ; 0.11 ; 0.05 REMARK 3 TIGHT POSITIONAL 2 L (A): 1558 ; 0.11 ; 0.05 REMARK 3 TIGHT THERMAL 2 O (A**2): 1558 ; 0.14 ; 0.50 REMARK 3 TIGHT THERMAL 2 M (A**2): 1558 ; 0.13 ; 0.50 REMARK 3 TIGHT THERMAL 2 N (A**2): 1558 ; 0.12 ; 0.50 REMARK 3 TIGHT THERMAL 2 L (A**2): 1558 ; 0.13 ; 0.50 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : D A B C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 D 34 D 117 1 REMARK 3 1 A 34 A 117 1 REMARK 3 1 B 34 B 117 1 REMARK 3 1 C 34 C 117 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 3 D (A): 647 ; 0.06 ; 0.05 REMARK 3 TIGHT POSITIONAL 3 A (A): 647 ; 0.06 ; 0.05 REMARK 3 TIGHT POSITIONAL 3 B (A): 647 ; 0.06 ; 0.05 REMARK 3 TIGHT POSITIONAL 3 C (A): 647 ; 0.09 ; 0.05 REMARK 3 TIGHT THERMAL 3 D (A**2): 647 ; 0.12 ; 0.50 REMARK 3 TIGHT THERMAL 3 A (A**2): 647 ; 0.12 ; 0.50 REMARK 3 TIGHT THERMAL 3 B (A**2): 647 ; 0.10 ; 0.50 REMARK 3 TIGHT THERMAL 3 C (A**2): 647 ; 0.11 ; 0.50 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 : H 1 H 120 REMARK 3 ORIGIN FOR THE GROUP (A): 29.7142 12.0719 11.7351 REMARK 3 T TENSOR REMARK 3 T11: 0.2877 T22: 0.0192 REMARK 3 T33: 0.0612 T12: -0.0134 REMARK 3 T13: 0.0524 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 5.9582 L22: 2.0181 REMARK 3 L33: 3.0161 L12: -1.9450 REMARK 3 L13: -1.3853 L23: 0.6764 REMARK 3 S TENSOR REMARK 3 S11: -0.1575 S12: 0.0545 S13: -0.3080 REMARK 3 S21: 0.0023 S22: 0.0983 S23: 0.0500 REMARK 3 S31: 0.5116 S32: -0.1319 S33: 0.0592 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 121 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): 65.0894 12.1356 28.5886 REMARK 3 T TENSOR REMARK 3 T11: 0.8183 T22: 0.4102 REMARK 3 T33: 0.7688 T12: 0.4228 REMARK 3 T13: 0.2154 T23: 0.0902 REMARK 3 L TENSOR REMARK 3 L11: 9.6518 L22: 4.3688 REMARK 3 L33: 11.2272 L12: -3.9644 REMARK 3 L13: -2.2925 L23: -4.3497 REMARK 3 S TENSOR REMARK 3 S11: -0.0849 S12: 0.2838 S13: -0.3900 REMARK 3 S21: -0.7515 S22: -0.7328 S23: -0.5093 REMARK 3 S31: 1.4626 S32: 1.0614 S33: 0.8177 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 2 L 120 REMARK 3 ORIGIN FOR THE GROUP (A): 29.1985 23.4730 31.1107 REMARK 3 T TENSOR REMARK 3 T11: 0.3184 T22: 0.0496 REMARK 3 T33: 0.0785 T12: 0.0375 REMARK 3 T13: 0.0450 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 7.0582 L22: 2.5391 REMARK 3 L33: 1.7146 L12: -0.7727 REMARK 3 L13: 1.4871 L23: 0.5866 REMARK 3 S TENSOR REMARK 3 S11: -0.1363 S12: -0.1191 S13: 0.2061 REMARK 3 S21: 0.0100 S22: 0.0762 S23: 0.1442 REMARK 3 S31: 0.3451 S32: -0.0732 S33: 0.0601 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 121 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): 57.2605 27.2719 28.6114 REMARK 3 T TENSOR REMARK 3 T11: 0.1618 T22: 0.2630 REMARK 3 T33: 0.3002 T12: 0.1718 REMARK 3 T13: -0.1156 T23: -0.0609 REMARK 3 L TENSOR REMARK 3 L11: 8.5889 L22: 4.4082 REMARK 3 L33: 12.0414 L12: 3.6623 REMARK 3 L13: -6.3144 L23: -4.0861 REMARK 3 S TENSOR REMARK 3 S11: -0.1535 S12: -0.0695 S13: 0.1126 REMARK 3 S21: 0.1098 S22: 0.0585 S23: -0.5047 REMARK 3 S31: -0.1682 S32: 0.3477 S33: 0.0950 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 34 A 118 REMARK 3 ORIGIN FOR THE GROUP (A): 5.2895 24.8434 20.7751 REMARK 3 T TENSOR REMARK 3 T11: 0.2743 T22: 0.3848 REMARK 3 T33: 0.3174 T12: -0.0094 REMARK 3 T13: 0.1213 T23: 0.0910 REMARK 3 L TENSOR REMARK 3 L11: 4.6180 L22: 12.3164 REMARK 3 L33: 3.4431 L12: -1.9701 REMARK 3 L13: -1.3215 L23: 1.5026 REMARK 3 S TENSOR REMARK 3 S11: -0.2072 S12: -0.2744 S13: -0.1765 REMARK 3 S21: 1.3357 S22: -0.0299 S23: 1.2369 REMARK 3 S31: 0.1204 S32: -0.6274 S33: 0.2371 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 : I 1 I 120 REMARK 3 ORIGIN FOR THE GROUP (A): 3.2745 -0.0425 40.0704 REMARK 3 T TENSOR REMARK 3 T11: 0.0570 T22: 0.2101 REMARK 3 T33: 0.0539 T12: 0.0792 REMARK 3 T13: -0.0052 T23: 0.0283 REMARK 3 L TENSOR REMARK 3 L11: 6.3623 L22: 2.8405 REMARK 3 L33: 2.2302 L12: 1.0436 REMARK 3 L13: -2.2907 L23: -0.6284 REMARK 3 S TENSOR REMARK 3 S11: 0.2459 S12: 0.6113 S13: 0.3765 REMARK 3 S21: -0.2146 S22: -0.0922 S23: 0.0583 REMARK 3 S31: -0.0467 S32: -0.4121 S33: -0.1538 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 : I 121 I 221 REMARK 3 ORIGIN FOR THE GROUP (A): 42.0932 -12.2583 36.1155 REMARK 3 T TENSOR REMARK 3 T11: 0.0727 T22: 0.2544 REMARK 3 T33: 0.3263 T12: 0.1233 REMARK 3 T13: 0.0511 T23: 0.0236 REMARK 3 L TENSOR REMARK 3 L11: 7.9486 L22: 13.6483 REMARK 3 L33: 5.5589 L12: -2.3689 REMARK 3 L13: -2.0998 L23: -2.4810 REMARK 3 S TENSOR REMARK 3 S11: 0.3677 S12: 0.6438 S13: 0.1721 REMARK 3 S21: -0.3868 S22: -0.1797 S23: -0.5349 REMARK 3 S31: 0.1007 S32: 0.3728 S33: -0.1880 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 2 M 120 REMARK 3 ORIGIN FOR THE GROUP (A): 6.5818 -20.6450 48.0805 REMARK 3 T TENSOR REMARK 3 T11: 0.1236 T22: 0.1196 REMARK 3 T33: 0.1410 T12: -0.0753 REMARK 3 T13: -0.0567 T23: 0.0045 REMARK 3 L TENSOR REMARK 3 L11: 7.2127 L22: 1.2917 REMARK 3 L33: 2.4547 L12: -0.1925 REMARK 3 L13: 0.0854 L23: -0.8295 REMARK 3 S TENSOR REMARK 3 S11: 0.0339 S12: 0.1463 S13: -0.4384 REMARK 3 S21: 0.1387 S22: -0.1205 S23: 0.0242 REMARK 3 S31: 0.1957 S32: -0.3151 S33: 0.0866 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 121 M 211 REMARK 3 ORIGIN FOR THE GROUP (A): 34.3121 -15.0704 50.7749 REMARK 3 T TENSOR REMARK 3 T11: 0.1209 T22: 0.1638 REMARK 3 T33: 0.3275 T12: 0.1133 REMARK 3 T13: -0.0593 T23: 0.0258 REMARK 3 L TENSOR REMARK 3 L11: 7.4446 L22: 9.4330 REMARK 3 L33: 4.7383 L12: 5.7482 REMARK 3 L13: 1.8703 L23: 4.5922 REMARK 3 S TENSOR REMARK 3 S11: 0.2861 S12: -0.0859 S13: 0.0024 REMARK 3 S21: 0.1377 S22: -0.0639 S23: -0.2126 REMARK 3 S31: 0.2823 S32: 0.1718 S33: -0.2222 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 34 B 118 REMARK 3 ORIGIN FOR THE GROUP (A): -18.3269 -14.4180 53.1237 REMARK 3 T TENSOR REMARK 3 T11: 0.2343 T22: 0.4796 REMARK 3 T33: 0.3342 T12: -0.1707 REMARK 3 T13: 0.0508 T23: -0.1285 REMARK 3 L TENSOR REMARK 3 L11: 6.1630 L22: 7.5604 REMARK 3 L33: 12.4945 L12: 2.7399 REMARK 3 L13: 0.4299 L23: -2.0888 REMARK 3 S TENSOR REMARK 3 S11: 0.1113 S12: 0.4202 S13: -0.6463 REMARK 3 S21: 0.5878 S22: 0.1899 S23: 0.5169 REMARK 3 S31: 1.2475 S32: -1.0145 S33: -0.3011 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 : J 1 J 120 REMARK 3 ORIGIN FOR THE GROUP (A): 44.8445 31.4542 91.6261 REMARK 3 T TENSOR REMARK 3 T11: 0.3466 T22: 0.0677 REMARK 3 T33: 0.1204 T12: -0.1109 REMARK 3 T13: 0.0459 T23: -0.0442 REMARK 3 L TENSOR REMARK 3 L11: 5.7044 L22: 4.4006 REMARK 3 L33: 2.3637 L12: 1.9767 REMARK 3 L13: 1.6423 L23: 1.2911 REMARK 3 S TENSOR REMARK 3 S11: 0.0560 S12: 0.2569 S13: -0.2458 REMARK 3 S21: -0.2764 S22: 0.0347 S23: -0.2812 REMARK 3 S31: 0.3386 S32: 0.0116 S33: -0.0907 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 : J 121 J 221 REMARK 3 ORIGIN FOR THE GROUP (A): 5.6662 43.6119 86.3455 REMARK 3 T TENSOR REMARK 3 T11: 0.2589 T22: 0.6442 REMARK 3 T33: 0.1870 T12: -0.1072 REMARK 3 T13: -0.0711 T23: 0.1495 REMARK 3 L TENSOR REMARK 3 L11: 7.0717 L22: 10.5388 REMARK 3 L33: 5.1518 L12: -1.9794 REMARK 3 L13: 1.2043 L23: 1.3620 REMARK 3 S TENSOR REMARK 3 S11: -0.0509 S12: 0.7992 S13: 0.2404 REMARK 3 S21: -0.3991 S22: 0.1372 S23: 0.4209 REMARK 3 S31: -0.2095 S32: -0.6014 S33: -0.0863 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 2 N 120 REMARK 3 ORIGIN FOR THE GROUP (A): 40.6341 51.8384 100.1256 REMARK 3 T TENSOR REMARK 3 T11: 0.3507 T22: 0.1021 REMARK 3 T33: 0.1766 T12: -0.1011 REMARK 3 T13: 0.0131 T23: -0.0944 REMARK 3 L TENSOR REMARK 3 L11: 7.2151 L22: 0.1516 REMARK 3 L33: 2.3569 L12: 0.5959 REMARK 3 L13: 0.4101 L23: 0.0398 REMARK 3 S TENSOR REMARK 3 S11: -0.0892 S12: -0.0511 S13: 0.3045 REMARK 3 S21: -0.1196 S22: 0.1083 S23: -0.0770 REMARK 3 S31: 0.1993 S32: -0.0090 S33: -0.0191 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 : N 121 N 211 REMARK 3 ORIGIN FOR THE GROUP (A): 12.8281 45.5453 100.8181 REMARK 3 T TENSOR REMARK 3 T11: 0.1318 T22: 0.2467 REMARK 3 T33: 0.1221 T12: 0.0695 REMARK 3 T13: -0.0741 T23: 0.0829 REMARK 3 L TENSOR REMARK 3 L11: 6.4106 L22: 8.4982 REMARK 3 L33: 5.1503 L12: 4.3100 REMARK 3 L13: -1.7346 L23: -2.5642 REMARK 3 S TENSOR REMARK 3 S11: -0.1324 S12: 0.2768 S13: 0.1790 REMARK 3 S21: 0.1171 S22: 0.2816 S23: 0.1017 REMARK 3 S31: -0.1127 S32: -0.1620 S33: -0.1492 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 : C 34 C 118 REMARK 3 ORIGIN FOR THE GROUP (A): 65.5627 45.7734 106.6455 REMARK 3 T TENSOR REMARK 3 T11: 0.3969 T22: 0.2298 REMARK 3 T33: 0.5518 T12: -0.1216 REMARK 3 T13: -0.0724 T23: -0.0220 REMARK 3 L TENSOR REMARK 3 L11: 4.9400 L22: 4.3356 REMARK 3 L33: 11.4795 L12: 2.0612 REMARK 3 L13: -0.0578 L23: 2.6324 REMARK 3 S TENSOR REMARK 3 S11: 0.0617 S12: -0.1569 S13: 0.1444 REMARK 3 S21: 0.3280 S22: 0.0501 S23: -0.6807 REMARK 3 S31: -1.2140 S32: 0.7685 S33: -0.1118 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 : K 1 K 120 REMARK 3 ORIGIN FOR THE GROUP (A): 21.1941 18.9658 61.4381 REMARK 3 T TENSOR REMARK 3 T11: 0.1202 T22: 0.0730 REMARK 3 T33: 0.0556 T12: 0.0097 REMARK 3 T13: 0.0305 T23: 0.0013 REMARK 3 L TENSOR REMARK 3 L11: 5.9177 L22: 2.1095 REMARK 3 L33: 2.7318 L12: -1.3626 REMARK 3 L13: -0.1332 L23: 0.3013 REMARK 3 S TENSOR REMARK 3 S11: 0.3122 S12: 0.0526 S13: 0.1330 REMARK 3 S21: -0.0478 S22: -0.0552 S23: 0.0715 REMARK 3 S31: -0.4374 S32: -0.1395 S33: -0.2570 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 : K 121 K 221 REMARK 3 ORIGIN FOR THE GROUP (A): -16.8534 18.0937 76.6165 REMARK 3 T TENSOR REMARK 3 T11: 0.2724 T22: 0.2004 REMARK 3 T33: 0.3956 T12: 0.0128 REMARK 3 T13: 0.1469 T23: -0.0531 REMARK 3 L TENSOR REMARK 3 L11: 4.0469 L22: 4.4784 REMARK 3 L33: 6.3889 L12: -0.2777 REMARK 3 L13: 0.0452 L23: -1.6347 REMARK 3 S TENSOR REMARK 3 S11: 0.3495 S12: -0.0942 S13: 0.3730 REMARK 3 S21: 0.8599 S22: -0.2190 S23: 0.5876 REMARK 3 S31: -0.2001 S32: -0.6276 S33: -0.1305 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 : O 2 O 120 REMARK 3 ORIGIN FOR THE GROUP (A): 20.0323 7.5787 80.6345 REMARK 3 T TENSOR REMARK 3 T11: 0.3172 T22: 0.1123 REMARK 3 T33: 0.0919 T12: -0.1253 REMARK 3 T13: -0.0927 T23: 0.0102 REMARK 3 L TENSOR REMARK 3 L11: 5.6543 L22: 1.6715 REMARK 3 L33: 1.5478 L12: 0.2645 REMARK 3 L13: -0.9928 L23: -0.8076 REMARK 3 S TENSOR REMARK 3 S11: 0.1978 S12: -0.2130 S13: -0.2877 REMARK 3 S21: 0.2501 S22: -0.1560 S23: -0.2317 REMARK 3 S31: 0.2812 S32: 0.0912 S33: -0.0418 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 : O 121 O 211 REMARK 3 ORIGIN FOR THE GROUP (A): -7.7697 3.9319 76.1770 REMARK 3 T TENSOR REMARK 3 T11: 0.2033 T22: 0.1013 REMARK 3 T33: 0.1120 T12: -0.0745 REMARK 3 T13: 0.0895 T23: 0.0123 REMARK 3 L TENSOR REMARK 3 L11: 7.9935 L22: 2.6879 REMARK 3 L33: 7.9973 L12: 1.4186 REMARK 3 L13: 4.6411 L23: 2.3636 REMARK 3 S TENSOR REMARK 3 S11: 0.4519 S12: -0.0551 S13: -0.1543 REMARK 3 S21: 0.5318 S22: -0.3325 S23: 0.2290 REMARK 3 S31: 0.2412 S32: -0.0544 S33: -0.1194 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 : D 34 D 118 REMARK 3 ORIGIN FOR THE GROUP (A): 44.5764 5.0289 72.3083 REMARK 3 T TENSOR REMARK 3 T11: 0.1813 T22: 0.6571 REMARK 3 T33: 0.3086 T12: -0.0176 REMARK 3 T13: -0.2000 T23: -0.1140 REMARK 3 L TENSOR REMARK 3 L11: 3.7119 L22: 19.7372 REMARK 3 L33: 7.0829 L12: -3.0908 REMARK 3 L13: -0.3813 L23: -2.6050 REMARK 3 S TENSOR REMARK 3 S11: 0.1678 S12: -1.0385 S13: -0.0543 REMARK 3 S21: 1.2650 S22: 0.0242 S23: -1.4256 REMARK 3 S31: 0.3164 S32: 0.9904 S33: -0.1920 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 : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3NH7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-10. REMARK 100 THE RCSB ID CODE IS RCSB059824. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 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 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : VARIMAX CU HIGHRES REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59539 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 30.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : 0.08000 REMARK 200 FOR THE DATA SET : 8.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.60 REMARK 200 R MERGE FOR SHELL (I) : 0.34100 REMARK 200 R SYM FOR SHELL (I) : 0.34100 REMARK 200 FOR SHELL : 2.700 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: PDB ENTRY 1AQK REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 7.0, 20% (W/V) PEG REMARK 280 8000 AND 10% (W/V) GLUCOSE , VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 294K 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 64.62750 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, 4 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: 5750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A 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: 5690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, N, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, O, 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS H 136 REMARK 465 SER H 137 REMARK 465 THR H 138 REMARK 465 SER H 139 REMARK 465 GLY H 140 REMARK 465 GLY H 141 REMARK 465 THR H 142 REMARK 465 SER H 194 REMARK 465 SER H 195 REMARK 465 LEU H 196 REMARK 465 GLY H 197 REMARK 465 THR H 198 REMARK 465 GLN H 199 REMARK 465 LYS H 221 REMARK 465 SER H 222 REMARK 465 GLU H 223 REMARK 465 PHE H 224 REMARK 465 SER H 225 REMARK 465 ALA H 226 REMARK 465 TRP H 227 REMARK 465 SER H 228 REMARK 465 HIS H 229 REMARK 465 PRO H 230 REMARK 465 GLN H 231 REMARK 465 PHE H 232 REMARK 465 GLU H 233 REMARK 465 LYS H 234 REMARK 465 ASP L 1 REMARK 465 GLU L 212 REMARK 465 ALA L 213 REMARK 465 GLN A 1 REMARK 465 ASN A 2 REMARK 465 LEU A 3 REMARK 465 ASP A 4 REMARK 465 SER A 5 REMARK 465 MET A 6 REMARK 465 LEU A 7 REMARK 465 HIS A 8 REMARK 465 GLY A 9 REMARK 465 THR A 10 REMARK 465 GLY A 11 REMARK 465 MET A 12 REMARK 465 LYS A 13 REMARK 465 SER A 14 REMARK 465 ASP A 15 REMARK 465 SER A 16 REMARK 465 ASP A 17 REMARK 465 GLN A 18 REMARK 465 LYS A 19 REMARK 465 LYS A 20 REMARK 465 SER A 21 REMARK 465 GLU A 22 REMARK 465 ASN A 23 REMARK 465 GLY A 24 REMARK 465 VAL A 25 REMARK 465 THR A 26 REMARK 465 LEU A 27 REMARK 465 ALA A 28 REMARK 465 PRO A 29 REMARK 465 GLU A 30 REMARK 465 ASP A 31 REMARK 465 THR A 32 REMARK 465 LEU A 33 REMARK 465 VAL A 119 REMARK 465 ILE A 120 REMARK 465 GLY A 121 REMARK 465 PRO A 122 REMARK 465 PHE A 123 REMARK 465 PHE A 124 REMARK 465 ASP A 125 REMARK 465 GLY A 126 REMARK 465 SER A 127 REMARK 465 ILE A 128 REMARK 465 ARG A 129 REMARK 465 LYS I 136 REMARK 465 SER I 137 REMARK 465 THR I 138 REMARK 465 SER I 139 REMARK 465 GLY I 140 REMARK 465 LYS I 221 REMARK 465 SER I 222 REMARK 465 GLU I 223 REMARK 465 PHE I 224 REMARK 465 SER I 225 REMARK 465 ALA I 226 REMARK 465 TRP I 227 REMARK 465 SER I 228 REMARK 465 HIS I 229 REMARK 465 PRO I 230 REMARK 465 GLN I 231 REMARK 465 PHE I 232 REMARK 465 GLU I 233 REMARK 465 LYS I 234 REMARK 465 ASP M 1 REMARK 465 GLU M 212 REMARK 465 ALA M 213 REMARK 465 GLN B 1 REMARK 465 ASN B 2 REMARK 465 LEU B 3 REMARK 465 ASP B 4 REMARK 465 SER B 5 REMARK 465 MET B 6 REMARK 465 LEU B 7 REMARK 465 HIS B 8 REMARK 465 GLY B 9 REMARK 465 THR B 10 REMARK 465 GLY B 11 REMARK 465 MET B 12 REMARK 465 LYS B 13 REMARK 465 SER B 14 REMARK 465 ASP B 15 REMARK 465 SER B 16 REMARK 465 ASP B 17 REMARK 465 GLN B 18 REMARK 465 LYS B 19 REMARK 465 LYS B 20 REMARK 465 SER B 21 REMARK 465 GLU B 22 REMARK 465 ASN B 23 REMARK 465 GLY B 24 REMARK 465 VAL B 25 REMARK 465 THR B 26 REMARK 465 LEU B 27 REMARK 465 ALA B 28 REMARK 465 PRO B 29 REMARK 465 GLU B 30 REMARK 465 ASP B 31 REMARK 465 THR B 32 REMARK 465 LEU B 33 REMARK 465 VAL B 119 REMARK 465 ILE B 120 REMARK 465 GLY B 121 REMARK 465 PRO B 122 REMARK 465 PHE B 123 REMARK 465 PHE B 124 REMARK 465 ASP B 125 REMARK 465 GLY B 126 REMARK 465 SER B 127 REMARK 465 ILE B 128 REMARK 465 ARG B 129 REMARK 465 SER J 222 REMARK 465 GLU J 223 REMARK 465 PHE J 224 REMARK 465 SER J 225 REMARK 465 ALA J 226 REMARK 465 TRP J 227 REMARK 465 SER J 228 REMARK 465 HIS J 229 REMARK 465 PRO J 230 REMARK 465 GLN J 231 REMARK 465 PHE J 232 REMARK 465 GLU J 233 REMARK 465 LYS J 234 REMARK 465 ASP N 1 REMARK 465 GLU N 212 REMARK 465 ALA N 213 REMARK 465 GLN C 1 REMARK 465 ASN C 2 REMARK 465 LEU C 3 REMARK 465 ASP C 4 REMARK 465 SER C 5 REMARK 465 MET C 6 REMARK 465 LEU C 7 REMARK 465 HIS C 8 REMARK 465 GLY C 9 REMARK 465 THR C 10 REMARK 465 GLY C 11 REMARK 465 MET C 12 REMARK 465 LYS C 13 REMARK 465 SER C 14 REMARK 465 ASP C 15 REMARK 465 SER C 16 REMARK 465 ASP C 17 REMARK 465 GLN C 18 REMARK 465 LYS C 19 REMARK 465 LYS C 20 REMARK 465 SER C 21 REMARK 465 GLU C 22 REMARK 465 ASN C 23 REMARK 465 GLY C 24 REMARK 465 VAL C 25 REMARK 465 THR C 26 REMARK 465 LEU C 27 REMARK 465 ALA C 28 REMARK 465 PRO C 29 REMARK 465 GLU C 30 REMARK 465 ASP C 31 REMARK 465 THR C 32 REMARK 465 LEU C 33 REMARK 465 VAL C 119 REMARK 465 ILE C 120 REMARK 465 GLY C 121 REMARK 465 PRO C 122 REMARK 465 PHE C 123 REMARK 465 PHE C 124 REMARK 465 ASP C 125 REMARK 465 GLY C 126 REMARK 465 SER C 127 REMARK 465 ILE C 128 REMARK 465 ARG C 129 REMARK 465 LYS K 136 REMARK 465 SER K 137 REMARK 465 THR K 138 REMARK 465 SER K 139 REMARK 465 GLY K 140 REMARK 465 GLY K 141 REMARK 465 SER K 222 REMARK 465 GLU K 223 REMARK 465 PHE K 224 REMARK 465 SER K 225 REMARK 465 ALA K 226 REMARK 465 TRP K 227 REMARK 465 SER K 228 REMARK 465 HIS K 229 REMARK 465 PRO K 230 REMARK 465 GLN K 231 REMARK 465 PHE K 232 REMARK 465 GLU K 233 REMARK 465 LYS K 234 REMARK 465 ASP O 1 REMARK 465 GLU O 212 REMARK 465 ALA O 213 REMARK 465 GLN D 1 REMARK 465 ASN D 2 REMARK 465 LEU D 3 REMARK 465 ASP D 4 REMARK 465 SER D 5 REMARK 465 MET D 6 REMARK 465 LEU D 7 REMARK 465 HIS D 8 REMARK 465 GLY D 9 REMARK 465 THR D 10 REMARK 465 GLY D 11 REMARK 465 MET D 12 REMARK 465 LYS D 13 REMARK 465 SER D 14 REMARK 465 ASP D 15 REMARK 465 SER D 16 REMARK 465 ASP D 17 REMARK 465 GLN D 18 REMARK 465 LYS D 19 REMARK 465 LYS D 20 REMARK 465 SER D 21 REMARK 465 GLU D 22 REMARK 465 ASN D 23 REMARK 465 GLY D 24 REMARK 465 VAL D 25 REMARK 465 THR D 26 REMARK 465 LEU D 27 REMARK 465 ALA D 28 REMARK 465 PRO D 29 REMARK 465 GLU D 30 REMARK 465 ASP D 31 REMARK 465 THR D 32 REMARK 465 LEU D 33 REMARK 465 VAL D 119 REMARK 465 ILE D 120 REMARK 465 GLY D 121 REMARK 465 PRO D 122 REMARK 465 PHE D 123 REMARK 465 PHE D 124 REMARK 465 ASP D 125 REMARK 465 GLY D 126 REMARK 465 SER D 127 REMARK 465 ILE D 128 REMARK 465 ARG D 129 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 M 60 OD2 ASP M 81 1.88 REMARK 500 ND2 ASN O 52 CD2 HIS D 43 1.99 REMARK 500 NH1 ARG O 60 OD2 ASP O 81 2.02 REMARK 500 NH1 ARG L 60 OD2 ASP L 81 2.04 REMARK 500 NH1 ARG N 60 OD2 ASP N 81 2.05 REMARK 500 ND2 ASN L 52 CD2 HIS A 43 2.07 REMARK 500 CD2 HIS H 207 OG SER H 210 2.10 REMARK 500 OH TYR M 179 O HOH M 216 2.11 REMARK 500 ND2 ASN M 52 CD2 HIS B 43 2.12 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 ARG L 191 CZ ARG L 191 NH2 0.080 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 ASP L 49 N - CA - C ANGL. DEV. = -16.2 DEGREES REMARK 500 ARG L 191 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES REMARK 500 ARG L 191 NE - CZ - NH2 ANGL. DEV. = 11.8 DEGREES REMARK 500 ARG M 191 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES REMARK 500 PRO J 220 C - N - CA ANGL. DEV. = 10.9 DEGREES REMARK 500 ASP N 49 N - CA - C ANGL. DEV. = -19.5 DEGREES REMARK 500 ASP N 50 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES REMARK 500 ARG N 191 NE - CZ - NH1 ANGL. DEV. = -14.2 DEGREES REMARK 500 ARG N 191 NE - CZ - NH2 ANGL. DEV. = 9.3 DEGREES REMARK 500 ASP C 47 CB - CA - C ANGL. DEV. = -12.8 DEGREES REMARK 500 ASP C 47 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES REMARK 500 ARG K 98 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG K 98 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES REMARK 500 ASP O 49 N - CA - C ANGL. DEV. = -20.6 DEGREES REMARK 500 ARG O 191 NE - CZ - NH1 ANGL. DEV. = -3.5 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 THR H 28 90.03 -67.94 REMARK 500 SER H 30 7.60 -62.49 REMARK 500 LYS H 43 -157.13 -102.47 REMARK 500 ASP H 62 -38.99 -35.69 REMARK 500 LYS H 65 130.64 -34.43 REMARK 500 LYS H 76 -167.27 -66.43 REMARK 500 HIS H 102 -96.17 -101.07 REMARK 500 SER H 122 95.50 -169.11 REMARK 500 THR H 123 110.46 44.94 REMARK 500 ASP H 151 35.35 71.78 REMARK 500 PHE H 153 143.48 177.90 REMARK 500 ASN H 162 71.09 26.04 REMARK 500 SER H 163 50.99 24.57 REMARK 500 PRO H 209 -17.20 -44.97 REMARK 500 SER H 210 36.13 -144.66 REMARK 500 ASN H 211 46.21 28.35 REMARK 500 SER L 51 28.90 -150.09 REMARK 500 LEU L 108 106.60 -41.82 REMARK 500 PHE A 35 11.86 -156.71 REMARK 500 ASP A 47 44.87 -104.85 REMARK 500 GLN A 86 118.61 -162.17 REMARK 500 CYS A 87 -69.77 -124.99 REMARK 500 TYR A 110 45.75 -73.33 REMARK 500 GLN A 112 51.49 -143.39 REMARK 500 PRO I 41 124.49 -38.20 REMARK 500 LYS I 43 -167.39 -110.49 REMARK 500 LYS I 76 -169.63 -65.12 REMARK 500 HIS I 102 -98.28 -100.48 REMARK 500 SER M 51 27.95 -149.72 REMARK 500 LEU M 108 110.00 -38.98 REMARK 500 PHE B 35 14.93 -160.17 REMARK 500 ASP B 47 44.88 -103.65 REMARK 500 CYS B 87 -67.35 -127.42 REMARK 500 TYR B 110 42.26 -72.16 REMARK 500 GLN B 112 48.76 -148.71 REMARK 500 PRO J 41 122.32 -36.62 REMARK 500 LYS J 76 -175.43 -69.94 REMARK 500 HIS J 102 -96.18 -107.67 REMARK 500 SER J 135 -5.17 -51.03 REMARK 500 SER J 139 -53.55 -132.37 REMARK 500 ASP J 151 63.63 62.85 REMARK 500 SER N 51 31.68 -153.20 REMARK 500 ARG N 60 -38.60 -35.20 REMARK 500 LEU N 108 107.51 -43.54 REMARK 500 PHE C 35 17.21 -157.35 REMARK 500 ASP C 46 27.11 -71.15 REMARK 500 CYS C 87 -68.96 -128.25 REMARK 500 GLN C 94 157.15 -49.34 REMARK 500 TYR C 110 41.16 -71.83 REMARK 500 GLN C 112 53.30 -143.15 REMARK 500 REMARK 500 THIS ENTRY HAS 62 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 SER L 93 GLY L 94 -60.82 REMARK 500 ALA A 48 ILE A 49 146.63 REMARK 500 ALA B 48 ILE B 49 145.81 REMARK 500 ALA C 48 ILE C 49 145.85 REMARK 500 ALA D 48 ILE D 49 145.33 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 VAL H 5 24.2 L L OUTSIDE RANGE REMARK 500 TYR L 48 21.9 L L OUTSIDE RANGE REMARK 500 TYR M 48 21.8 L L OUTSIDE RANGE REMARK 500 ASP M 50 21.1 L L OUTSIDE RANGE REMARK 500 TYR N 48 19.8 L L OUTSIDE RANGE REMARK 500 TYR O 48 20.4 L L OUTSIDE RANGE REMARK 500 ASP O 49 45.2 L L OUTSIDE RANGE REMARK 500 ASP O 50 22.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1REW RELATED DB: PDB REMARK 900 COMPLEX OF THE BMP TYPE I RECEPTOR BMPR-IA BOUND TO ITS REMARK 900 LIGAND BMP-2 REMARK 900 RELATED ID: 2K3G RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE FREE BMP TYPE I RECEPTOR BMPR-IA