REMARK 2 REMARK 2 RESOLUTION. 2.63 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0036 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) : 2.63 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 204.12 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 75243 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3976 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) : 2.63 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.70 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5433 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.25 REMARK 3 BIN R VALUE (WORKING SET) : 0.2530 REMARK 3 BIN FREE R VALUE SET COUNT : 297 REMARK 3 BIN FREE R VALUE : 0.3320 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15395 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 60 REMARK 3 SOLVENT ATOMS : 214 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) : 19.75 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.49000 REMARK 3 B22 (A**2) : -1.56000 REMARK 3 B33 (A**2) : -0.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.72000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.635 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.323 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.577 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15829 ; 0.011 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21603 ; 1.361 ; 1.956 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2022 ; 6.672 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 595 ;35.263 ;24.017 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2438 ;19.628 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;22.308 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2449 ; 0.089 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11874 ; 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): 10170 ; 0.355 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16481 ; 0.644 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5659 ; 0.888 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5122 ; 1.394 ; 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 : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : H I J K REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 1 H 213 5 REMARK 3 1 I 1 I 213 5 REMARK 3 1 J 1 J 213 5 REMARK 3 1 K 1 K 213 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 H (A): 844 ; 0.65 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 I (A): 844 ; 0.52 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 J (A): 844 ; 0.47 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 K (A): 844 ; 0.55 ; 0.50 REMARK 3 LOOSE POSITIONAL 1 H (A): 717 ; 0.82 ; 5.00 REMARK 3 LOOSE POSITIONAL 1 I (A): 717 ; 0.72 ; 5.00 REMARK 3 LOOSE POSITIONAL 1 J (A): 717 ; 0.68 ; 5.00 REMARK 3 LOOSE POSITIONAL 1 K (A): 717 ; 0.69 ; 5.00 REMARK 3 MEDIUM THERMAL 1 H (A**2): 844 ; 0.43 ; 2.00 REMARK 3 MEDIUM THERMAL 1 I (A**2): 844 ; 0.44 ; 2.00 REMARK 3 MEDIUM THERMAL 1 J (A**2): 844 ; 0.36 ; 2.00 REMARK 3 MEDIUM THERMAL 1 K (A**2): 844 ; 0.45 ; 2.00 REMARK 3 LOOSE THERMAL 1 H (A**2): 717 ; 0.87 ; 10.00 REMARK 3 LOOSE THERMAL 1 I (A**2): 717 ; 0.82 ; 10.00 REMARK 3 LOOSE THERMAL 1 J (A**2): 717 ; 0.54 ; 10.00 REMARK 3 LOOSE THERMAL 1 K (A**2): 717 ; 0.74 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : L M N O REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 1 L 210 5 REMARK 3 1 N 1 N 210 5 REMARK 3 1 M 1 M 210 5 REMARK 3 1 O 1 O 210 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 L (A): 848 ; 0.39 ; 0.50 REMARK 3 MEDIUM POSITIONAL 2 M (A): 848 ; 0.31 ; 0.50 REMARK 3 MEDIUM POSITIONAL 2 N (A): 848 ; 0.31 ; 0.50 REMARK 3 MEDIUM POSITIONAL 2 O (A): 848 ; 0.34 ; 0.50 REMARK 3 LOOSE POSITIONAL 2 L (A): 753 ; 0.64 ; 5.00 REMARK 3 LOOSE POSITIONAL 2 M (A): 753 ; 0.60 ; 5.00 REMARK 3 LOOSE POSITIONAL 2 N (A): 753 ; 0.61 ; 5.00 REMARK 3 LOOSE POSITIONAL 2 O (A): 753 ; 0.66 ; 5.00 REMARK 3 MEDIUM THERMAL 2 L (A**2): 848 ; 0.35 ; 2.00 REMARK 3 MEDIUM THERMAL 2 M (A**2): 848 ; 0.27 ; 2.00 REMARK 3 MEDIUM THERMAL 2 N (A**2): 848 ; 0.36 ; 2.00 REMARK 3 MEDIUM THERMAL 2 O (A**2): 848 ; 0.36 ; 2.00 REMARK 3 LOOSE THERMAL 2 L (A**2): 753 ; 0.54 ; 10.00 REMARK 3 LOOSE THERMAL 2 M (A**2): 753 ; 0.43 ; 10.00 REMARK 3 LOOSE THERMAL 2 N (A**2): 753 ; 0.53 ; 10.00 REMARK 3 LOOSE THERMAL 2 O (A**2): 753 ; 0.58 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A B C D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 128 5 REMARK 3 1 B 1 B 128 5 REMARK 3 1 C 1 C 128 5 REMARK 3 1 D 1 D 128 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 A (A): 300 ; 0.25 ; 0.50 REMARK 3 MEDIUM POSITIONAL 3 B (A): 300 ; 0.25 ; 0.50 REMARK 3 MEDIUM POSITIONAL 3 C (A): 300 ; 0.27 ; 0.50 REMARK 3 MEDIUM POSITIONAL 3 D (A): 300 ; 0.28 ; 0.50 REMARK 3 LOOSE POSITIONAL 3 A (A): 297 ; 0.62 ; 5.00 REMARK 3 LOOSE POSITIONAL 3 B (A): 297 ; 0.75 ; 5.00 REMARK 3 LOOSE POSITIONAL 3 C (A): 297 ; 0.77 ; 5.00 REMARK 3 LOOSE POSITIONAL 3 D (A): 297 ; 0.69 ; 5.00 REMARK 3 MEDIUM THERMAL 3 A (A**2): 300 ; 0.42 ; 2.00 REMARK 3 MEDIUM THERMAL 3 B (A**2): 300 ; 0.35 ; 2.00 REMARK 3 MEDIUM THERMAL 3 C (A**2): 300 ; 0.41 ; 2.00 REMARK 3 MEDIUM THERMAL 3 D (A**2): 300 ; 0.30 ; 2.00 REMARK 3 LOOSE THERMAL 3 A (A**2): 297 ; 0.69 ; 10.00 REMARK 3 LOOSE THERMAL 3 B (A**2): 297 ; 0.51 ; 10.00 REMARK 3 LOOSE THERMAL 3 C (A**2): 297 ; 0.75 ; 10.00 REMARK 3 LOOSE THERMAL 3 D (A**2): 297 ; 0.48 ; 10.00 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 118 REMARK 3 ORIGIN FOR THE GROUP (A): 113.2523 -0.8011 -29.9810 REMARK 3 T TENSOR REMARK 3 T11: 0.1104 T22: 0.1548 REMARK 3 T33: 0.1887 T12: 0.0021 REMARK 3 T13: 0.0302 T23: 0.0320 REMARK 3 L TENSOR REMARK 3 L11: 4.1069 L22: 1.5791 REMARK 3 L33: 1.0894 L12: -0.3823 REMARK 3 L13: -0.0920 L23: 0.0826 REMARK 3 S TENSOR REMARK 3 S11: 0.0750 S12: 0.1042 S13: 0.0354 REMARK 3 S21: -0.1769 S22: -0.0847 S23: -0.0900 REMARK 3 S31: 0.0140 S32: 0.0098 S33: 0.0096 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 119 H 216 REMARK 3 ORIGIN FOR THE GROUP (A): 122.2990 -30.6071 -25.9188 REMARK 3 T TENSOR REMARK 3 T11: 0.2107 T22: 0.2151 REMARK 3 T33: 0.3350 T12: -0.0440 REMARK 3 T13: -0.0626 T23: 0.0769 REMARK 3 L TENSOR REMARK 3 L11: 3.0577 L22: 3.8354 REMARK 3 L33: 2.1827 L12: 2.0398 REMARK 3 L13: -0.9525 L23: -0.7893 REMARK 3 S TENSOR REMARK 3 S11: 0.0637 S12: 0.0863 S13: -0.3725 REMARK 3 S21: -0.2397 S22: 0.0148 S23: -0.0604 REMARK 3 S31: 0.4257 S32: -0.2668 S33: -0.0785 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 112 REMARK 3 ORIGIN FOR THE GROUP (A): 105.9176 -1.3621 -9.1952 REMARK 3 T TENSOR REMARK 3 T11: 0.0950 T22: 0.2514 REMARK 3 T33: 0.1323 T12: -0.0966 REMARK 3 T13: 0.0190 T23: -0.0208 REMARK 3 L TENSOR REMARK 3 L11: 1.3308 L22: 3.9703 REMARK 3 L33: 2.1327 L12: -0.5522 REMARK 3 L13: 0.7437 L23: -1.3181 REMARK 3 S TENSOR REMARK 3 S11: -0.0119 S12: -0.2247 S13: 0.0583 REMARK 3 S21: 0.2999 S22: -0.1110 S23: -0.0629 REMARK 3 S31: -0.0146 S32: -0.2394 S33: 0.1230 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 113 L 210 REMARK 3 ORIGIN FOR THE GROUP (A): 130.3353 -31.4628 -11.4917 REMARK 3 T TENSOR REMARK 3 T11: 0.1114 T22: 0.1458 REMARK 3 T33: 0.2353 T12: -0.0893 REMARK 3 T13: -0.0753 T23: 0.1463 REMARK 3 L TENSOR REMARK 3 L11: 3.0383 L22: 2.4124 REMARK 3 L33: 2.0651 L12: -0.7142 REMARK 3 L13: -0.7841 L23: 0.2542 REMARK 3 S TENSOR REMARK 3 S11: 0.0952 S12: -0.1712 S13: -0.3151 REMARK 3 S21: 0.0135 S22: -0.0421 S23: -0.0193 REMARK 3 S31: 0.2273 S32: 0.0654 S33: -0.0531 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 : I 2 I 118 REMARK 3 ORIGIN FOR THE GROUP (A): 66.1690 31.9504 -31.1849 REMARK 3 T TENSOR REMARK 3 T11: 0.1727 T22: 0.0978 REMARK 3 T33: 0.1503 T12: -0.0157 REMARK 3 T13: -0.0471 T23: -0.0090 REMARK 3 L TENSOR REMARK 3 L11: 3.3518 L22: 1.8288 REMARK 3 L33: 1.2083 L12: -1.0525 REMARK 3 L13: -0.0930 L23: 0.0750 REMARK 3 S TENSOR REMARK 3 S11: -0.0673 S12: 0.0860 S13: 0.1072 REMARK 3 S21: -0.1248 S22: 0.0361 S23: 0.0172 REMARK 3 S31: -0.0276 S32: 0.0278 S33: 0.0312 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 119 I 216 REMARK 3 ORIGIN FOR THE GROUP (A): 58.4317 64.4989 -30.7628 REMARK 3 T TENSOR REMARK 3 T11: 0.0620 T22: 0.1025 REMARK 3 T33: 0.1635 T12: 0.0324 REMARK 3 T13: 0.0200 T23: -0.0350 REMARK 3 L TENSOR REMARK 3 L11: 1.4454 L22: 3.7832 REMARK 3 L33: 1.6006 L12: 1.8466 REMARK 3 L13: 0.7444 L23: -0.2836 REMARK 3 S TENSOR REMARK 3 S11: -0.0457 S12: -0.0330 S13: 0.0262 REMARK 3 S21: -0.0780 S22: 0.0873 S23: 0.0369 REMARK 3 S31: 0.0133 S32: -0.0126 S33: -0.0416 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 : M 2 M 112 REMARK 3 ORIGIN FOR THE GROUP (A): 76.2907 36.0370 -11.7471 REMARK 3 T TENSOR REMARK 3 T11: 0.1128 T22: 0.1581 REMARK 3 T33: 0.1622 T12: 0.0633 REMARK 3 T13: -0.0619 T23: -0.0520 REMARK 3 L TENSOR REMARK 3 L11: 0.8429 L22: 3.5794 REMARK 3 L33: 1.1578 L12: 0.3768 REMARK 3 L13: 0.1465 L23: 0.8271 REMARK 3 S TENSOR REMARK 3 S11: -0.1682 S12: -0.1779 S13: 0.1193 REMARK 3 S21: 0.0540 S22: 0.1013 S23: -0.1314 REMARK 3 S31: -0.0332 S32: -0.0301 S33: 0.0669 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 113 M 212 REMARK 3 ORIGIN FOR THE GROUP (A): 52.0811 66.5542 -15.9861 REMARK 3 T TENSOR REMARK 3 T11: 0.0365 T22: 0.0663 REMARK 3 T33: 0.0897 T12: 0.0149 REMARK 3 T13: 0.0354 T23: -0.0240 REMARK 3 L TENSOR REMARK 3 L11: 3.4768 L22: 1.9692 REMARK 3 L33: 3.7868 L12: -0.9247 REMARK 3 L13: 2.1171 L23: -0.7698 REMARK 3 S TENSOR REMARK 3 S11: 0.0622 S12: -0.0704 S13: 0.1616 REMARK 3 S21: 0.1510 S22: 0.0409 S23: 0.0016 REMARK 3 S31: -0.0436 S32: -0.1156 S33: -0.1031 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 : J 1 J 118 REMARK 3 ORIGIN FOR THE GROUP (A): 84.7860 -8.1587 -92.7582 REMARK 3 T TENSOR REMARK 3 T11: 0.2787 T22: 0.3832 REMARK 3 T33: 0.3352 T12: 0.0292 REMARK 3 T13: 0.0194 T23: 0.0500 REMARK 3 L TENSOR REMARK 3 L11: 2.6508 L22: 2.1846 REMARK 3 L33: 2.8323 L12: 0.5877 REMARK 3 L13: -0.9730 L23: -0.6313 REMARK 3 S TENSOR REMARK 3 S11: 0.0308 S12: -0.0385 S13: 0.0813 REMARK 3 S21: -0.0387 S22: -0.1979 S23: -0.4202 REMARK 3 S31: 0.0794 S32: 0.3318 S33: 0.1671 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 : J 119 J 213 REMARK 3 ORIGIN FOR THE GROUP (A): 88.2008 20.9330-102.3358 REMARK 3 T TENSOR REMARK 3 T11: 0.5187 T22: 0.5258 REMARK 3 T33: 0.4465 T12: 0.0810 REMARK 3 T13: -0.0174 T23: 0.0080 REMARK 3 L TENSOR REMARK 3 L11: 4.8919 L22: 5.0427 REMARK 3 L33: 1.5416 L12: -2.6730 REMARK 3 L13: -0.6978 L23: 0.6905 REMARK 3 S TENSOR REMARK 3 S11: -0.1416 S12: -0.4425 S13: 0.4126 REMARK 3 S21: 0.3285 S22: 0.0873 S23: -0.3475 REMARK 3 S31: -0.3977 S32: -0.1362 S33: 0.0543 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 : N 2 N 112 REMARK 3 ORIGIN FOR THE GROUP (A): 64.4522 -7.3669-101.4024 REMARK 3 T TENSOR REMARK 3 T11: 0.2724 T22: 0.3611 REMARK 3 T33: 0.1608 T12: 0.0512 REMARK 3 T13: 0.0065 T23: -0.0961 REMARK 3 L TENSOR REMARK 3 L11: 2.2851 L22: 3.8443 REMARK 3 L33: 2.6723 L12: -0.9722 REMARK 3 L13: 1.1160 L23: -1.6281 REMARK 3 S TENSOR REMARK 3 S11: 0.0970 S12: 0.0061 S13: -0.1212 REMARK 3 S21: -0.2992 S22: -0.1275 S23: 0.2826 REMARK 3 S31: 0.1659 S32: -0.2301 S33: 0.0305 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 113 N 210 REMARK 3 ORIGIN FOR THE GROUP (A): 82.6159 22.5404-118.0550 REMARK 3 T TENSOR REMARK 3 T11: 0.4894 T22: 0.5171 REMARK 3 T33: 0.3331 T12: 0.0827 REMARK 3 T13: -0.0117 T23: 0.0651 REMARK 3 L TENSOR REMARK 3 L11: 2.8259 L22: 3.3345 REMARK 3 L33: 2.5929 L12: 0.1713 REMARK 3 L13: -0.4069 L23: -0.2114 REMARK 3 S TENSOR REMARK 3 S11: -0.0585 S12: 0.5506 S13: 0.3409 REMARK 3 S21: -0.1905 S22: -0.0136 S23: -0.1818 REMARK 3 S31: -0.4405 S32: 0.0740 S33: 0.0721 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 : K 2 K 118 REMARK 3 ORIGIN FOR THE GROUP (A): 54.3974 -41.4758 -57.4069 REMARK 3 T TENSOR REMARK 3 T11: 0.3065 T22: 0.1458 REMARK 3 T33: 0.1265 T12: 0.0314 REMARK 3 T13: -0.0290 T23: -0.0249 REMARK 3 L TENSOR REMARK 3 L11: 2.0660 L22: 1.8886 REMARK 3 L33: 2.0681 L12: 0.7427 REMARK 3 L13: -0.7255 L23: -0.9670 REMARK 3 S TENSOR REMARK 3 S11: -0.0165 S12: 0.0181 S13: -0.0414 REMARK 3 S21: 0.0180 S22: 0.0254 S23: -0.0742 REMARK 3 S31: 0.0521 S32: 0.1046 S33: -0.0089 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 : K 119 K 215 REMARK 3 ORIGIN FOR THE GROUP (A): 48.8883 -73.3439 -51.7623 REMARK 3 T TENSOR REMARK 3 T11: 0.1675 T22: 0.0882 REMARK 3 T33: 0.1020 T12: -0.0232 REMARK 3 T13: 0.0193 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.7182 L22: 5.5751 REMARK 3 L33: 2.6568 L12: -1.1781 REMARK 3 L13: -0.2491 L23: 2.0737 REMARK 3 S TENSOR REMARK 3 S11: -0.0255 S12: 0.1146 S13: 0.0573 REMARK 3 S21: -0.2001 S22: 0.0724 S23: 0.1328 REMARK 3 S31: -0.0696 S32: -0.0539 S33: -0.0469 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 : O 2 O 112 REMARK 3 ORIGIN FOR THE GROUP (A): 46.8362 -45.4845 -77.9642 REMARK 3 T TENSOR REMARK 3 T11: 0.3300 T22: 0.1822 REMARK 3 T33: 0.1016 T12: -0.0050 REMARK 3 T13: -0.0193 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 1.2629 L22: 3.1067 REMARK 3 L33: 1.8336 L12: 0.5619 REMARK 3 L13: 0.7587 L23: 0.5166 REMARK 3 S TENSOR REMARK 3 S11: 0.0404 S12: 0.2118 S13: -0.0494 REMARK 3 S21: -0.2316 S22: 0.0492 S23: -0.0225 REMARK 3 S31: 0.2856 S32: -0.0672 S33: -0.0896 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 : O 113 O 212 REMARK 3 ORIGIN FOR THE GROUP (A): 33.6491 -75.9459 -57.2492 REMARK 3 T TENSOR REMARK 3 T11: 0.1601 T22: 0.0955 REMARK 3 T33: 0.2113 T12: -0.0406 REMARK 3 T13: -0.0921 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 1.7311 L22: 2.7033 REMARK 3 L33: 5.6314 L12: 0.0265 REMARK 3 L13: -0.4576 L23: -0.9508 REMARK 3 S TENSOR REMARK 3 S11: -0.1217 S12: 0.1266 S13: -0.1039 REMARK 3 S21: -0.3525 S22: 0.0732 S23: 0.3733 REMARK 3 S31: -0.0220 S32: -0.2016 S33: 0.0485 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 : A 36 A 128 REMARK 3 ORIGIN FOR THE GROUP (A): 83.7452 10.3533 -37.5294 REMARK 3 T TENSOR REMARK 3 T11: 0.1315 T22: 0.2150 REMARK 3 T33: 0.2387 T12: -0.0231 REMARK 3 T13: -0.0553 T23: -0.0563 REMARK 3 L TENSOR REMARK 3 L11: 2.5097 L22: 3.8839 REMARK 3 L33: 4.2612 L12: -0.9289 REMARK 3 L13: -1.2358 L23: 2.0292 REMARK 3 S TENSOR REMARK 3 S11: -0.1301 S12: 0.4172 S13: -0.2409 REMARK 3 S21: -0.4336 S22: 0.0261 S23: 0.1023 REMARK 3 S31: 0.1728 S32: -0.1999 S33: 0.1040 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 : B 37 B 128 REMARK 3 ORIGIN FOR THE GROUP (A): 94.9125 17.9148 -37.6337 REMARK 3 T TENSOR REMARK 3 T11: 0.1532 T22: 0.2137 REMARK 3 T33: 0.2010 T12: -0.0297 REMARK 3 T13: 0.0569 T23: -0.0183 REMARK 3 L TENSOR REMARK 3 L11: 2.4132 L22: 2.7945 REMARK 3 L33: 2.9572 L12: -0.7008 REMARK 3 L13: 0.4319 L23: -0.4584 REMARK 3 S TENSOR REMARK 3 S11: -0.0073 S12: 0.3976 S13: 0.2647 REMARK 3 S21: -0.5306 S22: -0.0656 S23: -0.1563 REMARK 3 S31: -0.1515 S32: -0.0005 S33: 0.0729 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 : C 39 C 128 REMARK 3 ORIGIN FOR THE GROUP (A): 70.2710 -20.0440 -66.6011 REMARK 3 T TENSOR REMARK 3 T11: 0.3827 T22: 0.3383 REMARK 3 T33: 0.1390 T12: -0.0172 REMARK 3 T13: 0.0120 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 4.1687 L22: 3.1242 REMARK 3 L33: 1.2288 L12: 1.9481 REMARK 3 L13: 0.2493 L23: 0.6239 REMARK 3 S TENSOR REMARK 3 S11: 0.0916 S12: -0.4063 S13: 0.0477 REMARK 3 S21: 0.2772 S22: -0.0018 S23: -0.3097 REMARK 3 S31: -0.2454 S32: 0.3017 S33: -0.0897 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 38 D 128 REMARK 3 ORIGIN FOR THE GROUP (A): 77.8900 -27.5661 -74.9587 REMARK 3 T TENSOR REMARK 3 T11: 0.2400 T22: 0.3482 REMARK 3 T33: 0.2913 T12: 0.0416 REMARK 3 T13: 0.0642 T23: -0.0380 REMARK 3 L TENSOR REMARK 3 L11: 2.0587 L22: 3.1652 REMARK 3 L33: 3.5909 L12: 1.0419 REMARK 3 L13: 0.2497 L23: -0.4019 REMARK 3 S TENSOR REMARK 3 S11: -0.0303 S12: -0.2253 S13: -0.1763 REMARK 3 S21: 0.1997 S22: -0.0769 S23: -0.5039 REMARK 3 S31: 0.1692 S32: 0.4276 S33: 0.1072 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS.U VALUES RESIDUAL ONLY REMARK 4 REMARK 4 2VXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-09. REMARK 100 THE PDBE ID CODE IS EBI-36823. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : TOROIDAL MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79235 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.63 REMARK 200 RESOLUTION RANGE LOW (A) : 102.10 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.0 REMARK 200 R MERGE (I) : 0.13 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.70 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.9 REMARK 200 R MERGE FOR SHELL (I) : 0.46 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.70 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 1AQK REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 90.9 MM PCTP BUFFER PH 4.0, 9.1 REMARK 280 MM PCTP BUFFER PH 9.5, 100 MM AMMONIUM SULPHATE, 14% W/V REMARK 280 PEG3350 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 33.35400 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 14020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 54580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, K, D, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 15220 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 56350 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS:L, H, I, M, A, 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 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 -4 REMARK 465 ILE A -3 REMARK 465 VAL A -2 REMARK 465 LYS A -1 REMARK 465 ALA A 0 REMARK 465 GLY A 1 REMARK 465 ILE A 2 REMARK 465 THR A 3 REMARK 465 ILE A 4 REMARK 465 PRO A 5 REMARK 465 ARG A 6 REMARK 465 ASN A 7 REMARK 465 PRO A 8 REMARK 465 GLY A 9 REMARK 465 CYS A 10 REMARK 465 PRO A 11 REMARK 465 ASN A 12 REMARK 465 SER A 13 REMARK 465 GLU A 14 REMARK 465 ASP A 15 REMARK 465 LYS A 16 REMARK 465 ASN A 17 REMARK 465 PHE A 18 REMARK 465 PRO A 19 REMARK 465 ARG A 20 REMARK 465 THR A 21 REMARK 465 VAL A 22 REMARK 465 MET A 23 REMARK 465 VAL A 24 REMARK 465 ASN A 25 REMARK 465 LEU A 26 REMARK 465 ASN A 27 REMARK 465 ILE A 28 REMARK 465 HIS A 29 REMARK 465 ASN A 30 REMARK 465 ARG A 31 REMARK 465 ASN A 32 REMARK 465 THR A 33 REMARK 465 ASN A 34 REMARK 465 ARG A 100 REMARK 465 ARG A 101 REMARK 465 GLU A 102 REMARK 465 PRO A 103 REMARK 465 PRO A 104 REMARK 465 HIS A 105 REMARK 465 CYS A 106 REMARK 465 PRO A 107 REMARK 465 ASN A 108 REMARK 465 HIS A 130 REMARK 465 VAL A 131 REMARK 465 ALA A 132 REMARK 465 MET B -4 REMARK 465 ILE B -3 REMARK 465 VAL B -2 REMARK 465 LYS B -1 REMARK 465 ALA B 0 REMARK 465 GLY B 1 REMARK 465 ILE B 2 REMARK 465 THR B 3 REMARK 465 ILE B 4 REMARK 465 PRO B 5 REMARK 465 ARG B 6 REMARK 465 ASN B 7 REMARK 465 PRO B 8 REMARK 465 GLY B 9 REMARK 465 CYS B 10 REMARK 465 PRO B 11 REMARK 465 ASN B 12 REMARK 465 SER B 13 REMARK 465 GLU B 14 REMARK 465 ASP B 15 REMARK 465 LYS B 16 REMARK 465 ASN B 17 REMARK 465 PHE B 18 REMARK 465 PRO B 19 REMARK 465 ARG B 20 REMARK 465 THR B 21 REMARK 465 VAL B 22 REMARK 465 MET B 23 REMARK 465 VAL B 24 REMARK 465 ASN B 25 REMARK 465 LEU B 26 REMARK 465 ASN B 27 REMARK 465 ILE B 28 REMARK 465 HIS B 29 REMARK 465 ASN B 30 REMARK 465 ARG B 31 REMARK 465 ASN B 32 REMARK 465 THR B 33 REMARK 465 ASN B 34 REMARK 465 THR B 35 REMARK 465 PRO B 59 REMARK 465 GLU B 60 REMARK 465 ARG B 100 REMARK 465 ARG B 101 REMARK 465 GLU B 102 REMARK 465 PRO B 103 REMARK 465 PRO B 104 REMARK 465 HIS B 105 REMARK 465 CYS B 106 REMARK 465 PRO B 107 REMARK 465 ASN B 108 REMARK 465 SER B 109 REMARK 465 PHE B 110 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 VAL B 131 REMARK 465 ALA B 132 REMARK 465 MET C -4 REMARK 465 ILE C -3 REMARK 465 VAL C -2 REMARK 465 LYS C -1 REMARK 465 ALA C 0 REMARK 465 GLY C 1 REMARK 465 ILE C 2 REMARK 465 THR C 3 REMARK 465 ILE C 4 REMARK 465 PRO C 5 REMARK 465 ARG C 6 REMARK 465 ASN C 7 REMARK 465 PRO C 8 REMARK 465 GLY C 9 REMARK 465 CYS C 10 REMARK 465 PRO C 11 REMARK 465 ASN C 12 REMARK 465 SER C 13 REMARK 465 GLU C 14 REMARK 465 ASP C 15 REMARK 465 LYS C 16 REMARK 465 ASN C 17 REMARK 465 PHE C 18 REMARK 465 PRO C 19 REMARK 465 ARG C 20 REMARK 465 THR C 21 REMARK 465 VAL C 22 REMARK 465 MET C 23 REMARK 465 VAL C 24 REMARK 465 ASN C 25 REMARK 465 LEU C 26 REMARK 465 ASN C 27 REMARK 465 ILE C 28 REMARK 465 HIS C 29 REMARK 465 ASN C 30 REMARK 465 ARG C 31 REMARK 465 ASN C 32 REMARK 465 THR C 33 REMARK 465 ASN C 34 REMARK 465 THR C 35 REMARK 465 PRO C 59 REMARK 465 GLU C 60 REMARK 465 ARG C 100 REMARK 465 ARG C 101 REMARK 465 GLU C 102 REMARK 465 PRO C 103 REMARK 465 PRO C 104 REMARK 465 HIS C 105 REMARK 465 CYS C 106 REMARK 465 PRO C 107 REMARK 465 ASN C 108 REMARK 465 SER C 109 REMARK 465 PHE C 110 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 VAL C 131 REMARK 465 ALA C 132 REMARK 465 MET D -4 REMARK 465 ILE D -3 REMARK 465 VAL D -2 REMARK 465 LYS D -1 REMARK 465 ALA D 0 REMARK 465 GLY D 1 REMARK 465 ILE D 2 REMARK 465 THR D 3 REMARK 465 ILE D 4 REMARK 465 PRO D 5 REMARK 465 ARG D 6 REMARK 465 ASN D 7 REMARK 465 PRO D 8 REMARK 465 GLY D 9 REMARK 465 CYS D 10 REMARK 465 PRO D 11 REMARK 465 ASN D 12 REMARK 465 SER D 13 REMARK 465 GLU D 14 REMARK 465 ASP D 15 REMARK 465 LYS D 16 REMARK 465 ASN D 17 REMARK 465 PHE D 18 REMARK 465 PRO D 19 REMARK 465 ARG D 20 REMARK 465 THR D 21 REMARK 465 VAL D 22 REMARK 465 MET D 23 REMARK 465 VAL D 24 REMARK 465 ASN D 25 REMARK 465 LEU D 26 REMARK 465 ASN D 27 REMARK 465 ILE D 28 REMARK 465 HIS D 29 REMARK 465 ASN D 30 REMARK 465 ARG D 31 REMARK 465 ASN D 32 REMARK 465 THR D 33 REMARK 465 ASN D 34 REMARK 465 THR D 35 REMARK 465 LEU D 99 REMARK 465 ARG D 100 REMARK 465 ARG D 101 REMARK 465 GLU D 102 REMARK 465 PRO D 103 REMARK 465 PRO D 104 REMARK 465 HIS D 105 REMARK 465 CYS D 106 REMARK 465 PRO D 107 REMARK 465 ASN D 108 REMARK 465 SER D 109 REMARK 465 PHE D 110 REMARK 465 ARG D 111 REMARK 465 LEU D 112 REMARK 465 GLU D 113 REMARK 465 LYS D 114 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 VAL D 131 REMARK 465 ALA D 132 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 SER J 128 REMARK 465 LYS J 129 REMARK 465 SER J 130 REMARK 465 THR J 131 REMARK 465 SER J 132 REMARK 465 GLY J 133 REMARK 465 GLY J 134 REMARK 465 LYS J 214 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 ASP J 217 REMARK 465 LYS J 218 REMARK 465 THR J 219 REMARK 465 HIS J 220 REMARK 465 SER K 130 REMARK 465 THR K 131 REMARK 465 SER K 132 REMARK 465 CYS K 216 REMARK 465 ASP K 217 REMARK 465 LYS K 218 REMARK 465 THR K 219 REMARK 465 HIS K 220 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 SER M 213 REMARK 465 GLU N 211 REMARK 465 CYS N 212 REMARK 465 SER N 213 REMARK 465 ASN O 1 REMARK 465 SER O 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 GLU A 60 CG CD OE1 OE2 REMARK 470 SER A 109 OG REMARK 470 PHE A 110 CG CD1 CD2 CE1 CE2 CZ REMARK 470 HIS A 129 CG ND1 CD2 CE1 NE2 REMARK 470 ARG B 111 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 113 CG CD OE1 OE2 REMARK 470 ASN C 36 CG OD1 ND2 REMARK 470 GLU D 60 CG CD OE1 OE2 REMARK 470 GLU I 1 CG CD OE1 OE2 REMARK 470 LYS I 129 CG CD CE NZ REMARK 470 GLU K 1 CG CD OE1 OE2 REMARK 470 ASN L 1 CG OD1 ND2 REMARK 470 ASN M 1 CG OD1 ND2 REMARK 470 ASN N 1 CG OD1 ND2 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 OH TYR B 85 O3 SO4 B 1129 2.10 REMARK 500 OD2 ASP D 42 OH TYR K 32 2.19 REMARK 500 O ASP K 95 O VAL K 100 2.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG SER L 9 OD1 ASP M 67 1745 2.08 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 PRO C 37 C - N - CA ANGL. DEV. = 9.9 DEGREES REMARK 500 CYS I 140 CA - CB - SG ANGL. DEV. = -7.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 59 -82.04 -26.23 REMARK 500 VAL A 98 -162.92 -126.78 REMARK 500 PHE A 110 35.38 164.86 REMARK 500 SER B 49 63.66 -117.15 REMARK 500 ALA C 79 -3.11 -53.09 REMARK 500 VAL C 98 -155.82 -115.87 REMARK 500 LYS D 38 -26.88 -28.86 REMARK 500 SER D 49 65.73 -115.49 REMARK 500 VAL H 48 -57.36 -120.71 REMARK 500 SER H 82B 55.86 39.40 REMARK 500 ASP H 144 71.81 53.78 REMARK 500 THR H 160 43.69 -141.35 REMARK 500 THR H 191 -73.52 -92.03 REMARK 500 PRO H 213 -170.42 -68.30 REMARK 500 ALA I 88 166.27 177.84 REMARK 500 THR J 28 94.28 -65.28 REMARK 500 PRO J 41 116.92 -36.94 REMARK 500 ASP J 144 60.74 60.23 REMARK 500 SER J 156 22.29 41.68 REMARK 500 THR J 191 -66.25 -107.94 REMARK 500 LYS K 64 127.51 -38.11 REMARK 500 LEU K 96 -62.70 83.34 REMARK 500 THR K 191 -48.03 -130.81 REMARK 500 ASN L 51 -54.42 75.16 REMARK 500 ASN L 52 -0.09 -144.33 REMARK 500 ASP L 60 -38.81 -23.01 REMARK 500 ALA L 84 178.16 170.24 REMARK 500 THR L 90 -157.93 -144.90 REMARK 500 PRO L 142 -178.86 -67.56 REMARK 500 ASP L 152 -111.51 58.50 REMARK 500 ASN L 171 5.57 81.48 REMARK 500 ASN M 51 -51.33 71.87 REMARK 500 ASN M 52 2.04 -152.69 REMARK 500 LEU M 78 138.82 -39.16 REMARK 500 ALA M 84 173.60 174.38 REMARK 500 TYR M 94 -63.54 -122.18 REMARK 500 ASN M 129 35.91 73.95 REMARK 500 ASP M 152 -112.86 51.26 REMARK 500 ASN M 171 -12.46 75.84 REMARK 500 GLU M 211 42.38 -90.04 REMARK 500 ASN N 51 -55.45 73.35 REMARK 500 ASN N 52 7.69 -150.34 REMARK 500 ALA N 84 -173.88 177.85 REMARK 500 ASP N 152 -100.01 57.22 REMARK 500 ASN N 171 -12.61 100.43 REMARK 500 LYS N 172 -169.08 -79.76 REMARK 500 GLU N 199 -16.34 55.44 REMARK 500 PRO O 40 116.47 -37.41 REMARK 500 ASN O 51 -67.27 79.83 REMARK 500 ALA O 84 175.29 174.20 REMARK 500 REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS. 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 ASP K 95 23.7 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 O1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1129 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1130 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1129 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1130 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1129 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 N1211 REMARK 999 REMARK 999 SEQUENCE REMARK 999 SWISSPROT ACCESSION NUMBER Q16552. THE NUMBERING OF THE REMARK 999 FAB-FRAGMENT (CHAINS H,I,J,K AND L,M,N,O) ARE ACCORDING REMARK 999 TO THE NOMENCLATURE OF KABAT ET AL