HEADER RNA 31-MAY-24 9C2K TITLE THE CRYSTAL STRUCTURE OF HIV-1 REV RESPONSE ELEMENT STEM-LOOP II IN TITLE 2 COMPLEX WITH A FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BL3-6 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BL3-6 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: REV RESPONSE ELEMENT; COMPND 11 CHAIN: R, C; COMPND 12 FRAGMENT: STEM-LOOP II; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 14 ORGANISM_TAXID: 11676 KEYWDS HIV-1, REPLICATION, FAB, CHAPERONE, REV RESPONSE ELEMENT, RNA EXPDTA X-RAY DIFFRACTION AUTHOR M.OJHA,D.KOIRALA REVDAT 1 28-MAY-25 9C2K 0 JRNL AUTH M.OJHA,D.KOIRALA JRNL TITL CRYSTAL STRUCTURE OF HIV-1 RRE SL2 IN COMPLEX WITH FAB BL3-6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.42 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.33 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.3 REMARK 3 NUMBER OF REFLECTIONS : 95959 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.550 REMARK 3 FREE R VALUE TEST SET COUNT : 3409 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.3300 - 6.9600 0.86 4008 150 0.1745 0.2035 REMARK 3 2 6.9600 - 5.5300 0.88 4040 155 0.1951 0.2447 REMARK 3 3 5.5300 - 4.8300 0.91 4193 149 0.1657 0.2570 REMARK 3 4 4.8300 - 4.3900 0.88 4104 149 0.1542 0.1940 REMARK 3 5 4.3900 - 4.0800 0.83 3851 139 0.1670 0.2535 REMARK 3 6 4.0800 - 3.8400 0.79 3642 133 0.1849 0.1940 REMARK 3 7 3.8400 - 3.6400 0.83 3849 137 0.1922 0.2738 REMARK 3 8 3.6400 - 3.4900 0.85 3921 143 0.1897 0.2745 REMARK 3 9 3.4900 - 3.3500 0.85 3977 147 0.1972 0.2988 REMARK 3 10 3.3500 - 3.2400 0.86 3997 145 0.2044 0.2502 REMARK 3 11 3.2400 - 3.1300 0.87 3982 146 0.2253 0.3001 REMARK 3 12 3.1300 - 3.0500 0.87 4029 149 0.2540 0.2969 REMARK 3 13 3.0500 - 2.9600 0.84 3910 143 0.2406 0.3002 REMARK 3 14 2.9600 - 2.8900 0.79 3648 142 0.2539 0.2652 REMARK 3 15 2.8900 - 2.8300 0.82 3826 146 0.2517 0.3006 REMARK 3 16 2.8300 - 2.7700 0.76 3507 132 0.2550 0.3639 REMARK 3 17 2.7700 - 2.7100 0.79 3626 137 0.2791 0.3348 REMARK 3 18 2.7100 - 2.6600 0.81 3761 136 0.2765 0.3766 REMARK 3 19 2.6600 - 2.6100 0.81 3729 136 0.2926 0.3869 REMARK 3 20 2.6100 - 2.5700 0.82 3822 131 0.2765 0.2911 REMARK 3 21 2.5700 - 2.5300 0.82 3842 144 0.2866 0.3258 REMARK 3 22 2.5300 - 2.4900 0.83 3813 140 0.2894 0.3657 REMARK 3 23 2.4900 - 2.4500 0.83 3819 142 0.2973 0.3758 REMARK 3 24 2.4500 - 2.4200 0.79 3654 138 0.3160 0.3406 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.398 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.393 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.12 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.72 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 10360 REMARK 3 ANGLE : 1.180 14740 REMARK 3 CHIRALITY : 0.055 1758 REMARK 3 PLANARITY : 0.008 1326 REMARK 3 DIHEDRAL : 16.343 4188 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 33 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1877 -15.5390 29.1105 REMARK 3 T TENSOR REMARK 3 T11: 0.3740 T22: 0.3710 REMARK 3 T33: 0.4626 T12: 0.0249 REMARK 3 T13: -0.0393 T23: 0.1940 REMARK 3 L TENSOR REMARK 3 L11: 7.7634 L22: 3.8529 REMARK 3 L33: 5.3479 L12: -1.6768 REMARK 3 L13: -2.3429 L23: -3.2799 REMARK 3 S TENSOR REMARK 3 S11: -0.1913 S12: 0.3825 S13: -0.2128 REMARK 3 S21: 0.3834 S22: 0.4272 S23: -1.2372 REMARK 3 S31: 1.0665 S32: 1.5953 S33: -0.1325 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 21 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.4676 -10.8431 23.4291 REMARK 3 T TENSOR REMARK 3 T11: 0.2740 T22: 0.2897 REMARK 3 T33: 0.3699 T12: 0.0176 REMARK 3 T13: -0.0196 T23: 0.0925 REMARK 3 L TENSOR REMARK 3 L11: 4.0242 L22: 2.9164 REMARK 3 L33: 4.2388 L12: 0.3623 REMARK 3 L13: 0.4357 L23: -0.4629 REMARK 3 S TENSOR REMARK 3 S11: 0.1569 S12: 0.0482 S13: 0.3618 REMARK 3 S21: 0.0560 S22: -0.2021 S23: -0.2214 REMARK 3 S31: -0.3530 S32: 0.2076 S33: 0.0540 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 87 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6661 -13.3426 32.2872 REMARK 3 T TENSOR REMARK 3 T11: 0.3942 T22: 0.3938 REMARK 3 T33: 0.3625 T12: 0.0015 REMARK 3 T13: -0.0340 T23: 0.1184 REMARK 3 L TENSOR REMARK 3 L11: 4.9817 L22: 6.1964 REMARK 3 L33: 8.5703 L12: 0.6930 REMARK 3 L13: 4.6490 L23: 4.7836 REMARK 3 S TENSOR REMARK 3 S11: -0.3183 S12: 0.0037 S13: 0.3427 REMARK 3 S21: 0.7315 S22: -0.2536 S23: 0.1814 REMARK 3 S31: -0.2919 S32: -0.0428 S33: 0.4848 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 103 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5509 -20.9474 13.4803 REMARK 3 T TENSOR REMARK 3 T11: 0.4714 T22: 0.4728 REMARK 3 T33: 0.3860 T12: 0.0561 REMARK 3 T13: 0.0626 T23: 0.1080 REMARK 3 L TENSOR REMARK 3 L11: 9.1641 L22: 8.0957 REMARK 3 L33: 9.1644 L12: -3.7921 REMARK 3 L13: 4.8993 L23: -2.3745 REMARK 3 S TENSOR REMARK 3 S11: 0.6352 S12: 0.7205 S13: -0.4579 REMARK 3 S21: -1.3907 S22: 0.0931 S23: -0.1089 REMARK 3 S31: 0.3380 S32: 0.1216 S33: -0.7133 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 116 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.5589 -30.2166 51.5025 REMARK 3 T TENSOR REMARK 3 T11: 0.4429 T22: 0.3583 REMARK 3 T33: 0.2868 T12: 0.0047 REMARK 3 T13: -0.0046 T23: 0.0766 REMARK 3 L TENSOR REMARK 3 L11: 1.7446 L22: 1.3565 REMARK 3 L33: 3.0672 L12: -1.0694 REMARK 3 L13: 0.8816 L23: -0.6718 REMARK 3 S TENSOR REMARK 3 S11: -0.1465 S12: -0.1803 S13: -0.0850 REMARK 3 S21: 0.1996 S22: 0.1194 S23: 0.0546 REMARK 3 S31: 0.0143 S32: 0.0599 S33: 0.0075 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 188 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9755 -37.1839 56.3539 REMARK 3 T TENSOR REMARK 3 T11: 0.4520 T22: 0.5704 REMARK 3 T33: 0.2836 T12: 0.1009 REMARK 3 T13: -0.0288 T23: 0.0919 REMARK 3 L TENSOR REMARK 3 L11: 2.1058 L22: 7.0362 REMARK 3 L33: 2.8883 L12: -1.1089 REMARK 3 L13: 0.2485 L23: -1.9962 REMARK 3 S TENSOR REMARK 3 S11: -0.3186 S12: -0.4204 S13: -0.1306 REMARK 3 S21: 0.0160 S22: 0.2646 S23: -0.5559 REMARK 3 S31: 0.4156 S32: 0.5695 S33: 0.1454 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8442 -29.8571 30.1785 REMARK 3 T TENSOR REMARK 3 T11: 0.3771 T22: 0.6444 REMARK 3 T33: 0.2624 T12: -0.1124 REMARK 3 T13: -0.0840 T23: 0.0831 REMARK 3 L TENSOR REMARK 3 L11: 9.3259 L22: 4.3075 REMARK 3 L33: 2.6677 L12: -6.2187 REMARK 3 L13: -2.2405 L23: 1.7709 REMARK 3 S TENSOR REMARK 3 S11: 0.2643 S12: -0.0976 S13: 0.1852 REMARK 3 S21: 0.3154 S22: -0.3140 S23: -0.1775 REMARK 3 S31: 0.2927 S32: -0.2860 S33: 0.0669 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 27 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.3788 -27.9469 22.9586 REMARK 3 T TENSOR REMARK 3 T11: 0.2669 T22: 0.3641 REMARK 3 T33: 0.3095 T12: -0.0126 REMARK 3 T13: -0.0322 T23: 0.0725 REMARK 3 L TENSOR REMARK 3 L11: 2.6102 L22: 5.0646 REMARK 3 L33: 4.6996 L12: 0.6949 REMARK 3 L13: 0.5192 L23: -0.2621 REMARK 3 S TENSOR REMARK 3 S11: 0.1573 S12: 0.2893 S13: -0.0864 REMARK 3 S21: -0.3126 S22: -0.0098 S23: 0.1944 REMARK 3 S31: 0.4806 S32: -0.0572 S33: -0.1629 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 104 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.6712 -43.2072 41.3092 REMARK 3 T TENSOR REMARK 3 T11: 0.8315 T22: 0.3214 REMARK 3 T33: 0.5120 T12: -0.1362 REMARK 3 T13: -0.1299 T23: 0.1005 REMARK 3 L TENSOR REMARK 3 L11: 0.0859 L22: 0.0804 REMARK 3 L33: 1.1203 L12: 0.0828 REMARK 3 L13: 0.3046 L23: 0.3024 REMARK 3 S TENSOR REMARK 3 S11: 0.1955 S12: -0.1746 S13: 0.2300 REMARK 3 S21: -0.5789 S22: -0.0249 S23: 0.5829 REMARK 3 S31: 1.6066 S32: -0.2216 S33: -0.2934 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.3683 -32.7765 64.8768 REMARK 3 T TENSOR REMARK 3 T11: 0.6499 T22: 0.9095 REMARK 3 T33: 0.3512 T12: -0.0551 REMARK 3 T13: 0.0097 T23: 0.1899 REMARK 3 L TENSOR REMARK 3 L11: 4.1735 L22: 5.2348 REMARK 3 L33: 4.1602 L12: 0.2978 REMARK 3 L13: -0.6002 L23: 1.6832 REMARK 3 S TENSOR REMARK 3 S11: 0.0226 S12: -1.3348 S13: -0.0712 REMARK 3 S21: 0.5590 S22: 0.0816 S23: -0.8408 REMARK 3 S31: 0.1175 S32: 1.1871 S33: -0.0165 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.8691 -32.6301 57.1331 REMARK 3 T TENSOR REMARK 3 T11: 0.5414 T22: 0.5252 REMARK 3 T33: 0.4703 T12: 0.0604 REMARK 3 T13: 0.0195 T23: 0.1992 REMARK 3 L TENSOR REMARK 3 L11: 1.7768 L22: 4.0226 REMARK 3 L33: 6.6758 L12: 0.4252 REMARK 3 L13: 0.2131 L23: 3.4872 REMARK 3 S TENSOR REMARK 3 S11: 0.0230 S12: 0.2036 S13: 0.2084 REMARK 3 S21: -0.0882 S22: -0.1645 S23: 0.6226 REMARK 3 S31: -0.8705 S32: -0.9557 S33: 0.1170 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2421 -33.1344 55.2828 REMARK 3 T TENSOR REMARK 3 T11: 0.5272 T22: 0.5034 REMARK 3 T33: 0.3997 T12: -0.0134 REMARK 3 T13: 0.0874 T23: 0.1901 REMARK 3 L TENSOR REMARK 3 L11: 1.3499 L22: 4.4868 REMARK 3 L33: 8.7030 L12: 0.9538 REMARK 3 L13: 1.2738 L23: 4.5268 REMARK 3 S TENSOR REMARK 3 S11: -0.0332 S12: 0.0608 S13: 0.1129 REMARK 3 S21: -0.3197 S22: 0.2481 S23: 0.0344 REMARK 3 S31: -0.7659 S32: 0.3971 S33: -0.2481 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 190 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.7860 -37.8853 65.0232 REMARK 3 T TENSOR REMARK 3 T11: 0.7735 T22: 0.5869 REMARK 3 T33: 0.4883 T12: -0.0360 REMARK 3 T13: 0.1948 T23: 0.1706 REMARK 3 L TENSOR REMARK 3 L11: 4.9362 L22: 6.1522 REMARK 3 L33: 3.9644 L12: 2.7130 REMARK 3 L13: 2.9827 L23: 4.5440 REMARK 3 S TENSOR REMARK 3 S11: 0.2442 S12: -0.8619 S13: -0.1960 REMARK 3 S21: 1.1001 S22: -0.1724 S23: 0.3556 REMARK 3 S31: 1.0047 S32: -1.2556 S33: -0.2731 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 20 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.3409 -35.0182 35.6482 REMARK 3 T TENSOR REMARK 3 T11: 0.4511 T22: 0.3292 REMARK 3 T33: 0.3147 T12: 0.1672 REMARK 3 T13: 0.0030 T23: 0.0456 REMARK 3 L TENSOR REMARK 3 L11: 6.6775 L22: 9.3202 REMARK 3 L33: 3.8608 L12: 7.5961 REMARK 3 L13: -0.8051 L23: -0.5940 REMARK 3 S TENSOR REMARK 3 S11: 0.3828 S12: -0.5462 S13: 1.0743 REMARK 3 S21: 0.1230 S22: -0.1771 S23: 0.6977 REMARK 3 S31: -0.2204 S32: -0.4053 S33: -0.2382 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.7852 -43.9807 43.1388 REMARK 3 T TENSOR REMARK 3 T11: 0.5633 T22: 0.5949 REMARK 3 T33: 0.2830 T12: 0.1088 REMARK 3 T13: -0.0387 T23: 0.0403 REMARK 3 L TENSOR REMARK 3 L11: 3.4596 L22: 1.0352 REMARK 3 L33: 1.3026 L12: 0.0752 REMARK 3 L13: -0.6035 L23: -0.5473 REMARK 3 S TENSOR REMARK 3 S11: -0.1689 S12: -0.5230 S13: -0.3253 REMARK 3 S21: 0.5030 S22: 0.1964 S23: -0.0797 REMARK 3 S31: 0.1610 S32: 0.1618 S33: 0.1006 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.4629 -47.1641 34.0798 REMARK 3 T TENSOR REMARK 3 T11: 0.4566 T22: 0.3733 REMARK 3 T33: 0.3050 T12: 0.1027 REMARK 3 T13: 0.0185 T23: 0.0710 REMARK 3 L TENSOR REMARK 3 L11: 3.6918 L22: 3.1690 REMARK 3 L33: 1.6552 L12: 0.2114 REMARK 3 L13: 0.2869 L23: -0.0678 REMARK 3 S TENSOR REMARK 3 S11: -0.1358 S12: -0.1815 S13: -0.1284 REMARK 3 S21: -0.0938 S22: 0.0668 S23: -0.2944 REMARK 3 S31: 0.2035 S32: 0.2004 S33: 0.1146 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.3052 -41.9946 40.6040 REMARK 3 T TENSOR REMARK 3 T11: 0.4434 T22: 0.6536 REMARK 3 T33: 0.3362 T12: 0.1460 REMARK 3 T13: -0.0041 T23: 0.1360 REMARK 3 L TENSOR REMARK 3 L11: 3.0774 L22: 2.0347 REMARK 3 L33: 1.9647 L12: 0.3717 REMARK 3 L13: -0.4035 L23: -0.6826 REMARK 3 S TENSOR REMARK 3 S11: 0.1377 S12: -1.1892 S13: -0.0524 REMARK 3 S21: 0.2996 S22: -0.0055 S23: -0.4938 REMARK 3 S31: -0.5156 S32: 0.9382 S33: 0.2822 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.1602 -39.5076 31.2024 REMARK 3 T TENSOR REMARK 3 T11: 0.5241 T22: 0.5409 REMARK 3 T33: 0.3475 T12: 0.0803 REMARK 3 T13: 0.0006 T23: 0.0831 REMARK 3 L TENSOR REMARK 3 L11: 3.4699 L22: 2.9796 REMARK 3 L33: 1.2158 L12: 0.8018 REMARK 3 L13: 0.4774 L23: -0.5619 REMARK 3 S TENSOR REMARK 3 S11: -0.0092 S12: 0.0215 S13: 0.2548 REMARK 3 S21: -0.2285 S22: -0.2852 S23: -0.1342 REMARK 3 S31: 0.1492 S32: 0.5339 S33: 0.1838 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -51.1868 -55.6473 35.5057 REMARK 3 T TENSOR REMARK 3 T11: 0.7179 T22: 0.6197 REMARK 3 T33: 0.2937 T12: 0.0704 REMARK 3 T13: -0.0508 T23: 0.0810 REMARK 3 L TENSOR REMARK 3 L11: 5.5191 L22: 6.3516 REMARK 3 L33: 5.6120 L12: -1.9629 REMARK 3 L13: 1.4519 L23: 0.5904 REMARK 3 S TENSOR REMARK 3 S11: 0.4224 S12: -0.5311 S13: -0.4409 REMARK 3 S21: 0.2263 S22: 0.2139 S23: 0.4484 REMARK 3 S31: 0.4510 S32: -1.2218 S33: -0.5511 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.6377 -23.3559 21.6354 REMARK 3 T TENSOR REMARK 3 T11: 0.3712 T22: 0.4950 REMARK 3 T33: 0.3432 T12: 0.1147 REMARK 3 T13: 0.0179 T23: 0.0145 REMARK 3 L TENSOR REMARK 3 L11: 1.9616 L22: 3.9267 REMARK 3 L33: 3.8031 L12: 0.3227 REMARK 3 L13: 0.4918 L23: -2.3178 REMARK 3 S TENSOR REMARK 3 S11: 0.0733 S12: 0.0622 S13: 0.1495 REMARK 3 S21: 0.4254 S22: -0.4662 S23: -0.5202 REMARK 3 S31: -0.0576 S32: 0.6897 S33: 0.3087 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.9064 -19.4076 0.9827 REMARK 3 T TENSOR REMARK 3 T11: 0.5976 T22: 0.6043 REMARK 3 T33: 0.3956 T12: 0.2508 REMARK 3 T13: 0.0817 T23: 0.1685 REMARK 3 L TENSOR REMARK 3 L11: 2.1447 L22: 3.6302 REMARK 3 L33: 2.9024 L12: 0.7029 REMARK 3 L13: -0.6976 L23: -1.8671 REMARK 3 S TENSOR REMARK 3 S11: 0.2373 S12: 0.9765 S13: 0.3084 REMARK 3 S21: -0.9725 S22: -0.1359 S23: -0.1067 REMARK 3 S31: 0.2629 S32: 0.8863 S33: 0.0548 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.6224 -22.2328 10.6465 REMARK 3 T TENSOR REMARK 3 T11: 0.4191 T22: 0.5870 REMARK 3 T33: 0.3176 T12: 0.1075 REMARK 3 T13: -0.0112 T23: 0.1459 REMARK 3 L TENSOR REMARK 3 L11: 0.8739 L22: 2.3700 REMARK 3 L33: 0.3304 L12: 0.2372 REMARK 3 L13: -0.2622 L23: 0.3360 REMARK 3 S TENSOR REMARK 3 S11: 0.1393 S12: 0.4397 S13: 0.1398 REMARK 3 S21: -0.1113 S22: -0.2170 S23: -0.0193 REMARK 3 S31: 0.2406 S32: 0.4016 S33: 0.0711 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): -50.7017 -12.1687 9.0083 REMARK 3 T TENSOR REMARK 3 T11: 0.4076 T22: 0.5406 REMARK 3 T33: 0.4589 T12: 0.0382 REMARK 3 T13: 0.0343 T23: 0.2282 REMARK 3 L TENSOR REMARK 3 L11: 4.3153 L22: 4.0581 REMARK 3 L33: 4.2587 L12: -1.3194 REMARK 3 L13: 4.0385 L23: 0.2611 REMARK 3 S TENSOR REMARK 3 S11: -0.1193 S12: -0.1923 S13: 0.6967 REMARK 3 S21: -0.2706 S22: 0.2233 S23: 0.1201 REMARK 3 S31: -1.0503 S32: -0.4059 S33: -0.2248 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -45.1977 -55.2585 13.8686 REMARK 3 T TENSOR REMARK 3 T11: 1.0121 T22: 0.4082 REMARK 3 T33: 0.3591 T12: 0.0898 REMARK 3 T13: 0.1280 T23: 0.0199 REMARK 3 L TENSOR REMARK 3 L11: 4.9229 L22: 5.8131 REMARK 3 L33: 7.1131 L12: -0.8909 REMARK 3 L13: 3.2947 L23: -1.7514 REMARK 3 S TENSOR REMARK 3 S11: 0.0648 S12: 0.6566 S13: -0.1874 REMARK 3 S21: -0.9175 S22: -0.6046 S23: -0.3752 REMARK 3 S31: 0.8827 S32: 0.7403 S33: 0.4902 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -51.2192 -55.3896 21.2931 REMARK 3 T TENSOR REMARK 3 T11: 0.7232 T22: 0.3424 REMARK 3 T33: 0.3408 T12: 0.0381 REMARK 3 T13: -0.0074 T23: 0.0017 REMARK 3 L TENSOR REMARK 3 L11: 3.5431 L22: 2.7976 REMARK 3 L33: 4.2460 L12: 0.6566 REMARK 3 L13: 0.7804 L23: -0.8972 REMARK 3 S TENSOR REMARK 3 S11: 0.1394 S12: -0.0121 S13: -0.3686 REMARK 3 S21: -0.2791 S22: -0.0952 S23: 0.1657 REMARK 3 S31: 0.5473 S32: -0.3179 S33: -0.0898 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.2362 -33.5980 7.2972 REMARK 3 T TENSOR REMARK 3 T11: 0.5628 T22: 0.4877 REMARK 3 T33: 0.3013 T12: 0.0896 REMARK 3 T13: 0.0217 T23: 0.0303 REMARK 3 L TENSOR REMARK 3 L11: 0.7949 L22: 2.2344 REMARK 3 L33: 2.5458 L12: 0.5574 REMARK 3 L13: -0.7968 L23: -1.5948 REMARK 3 S TENSOR REMARK 3 S11: 0.1672 S12: 0.3024 S13: 0.2005 REMARK 3 S21: -0.2627 S22: -0.2363 S23: 0.0060 REMARK 3 S31: 0.2437 S32: 0.2659 S33: -0.0453 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.7062 -28.4856 -1.8205 REMARK 3 T TENSOR REMARK 3 T11: 0.6253 T22: 0.6111 REMARK 3 T33: 0.3289 T12: 0.2399 REMARK 3 T13: 0.0512 T23: 0.1052 REMARK 3 L TENSOR REMARK 3 L11: 5.6824 L22: 4.6053 REMARK 3 L33: 3.0821 L12: 3.4156 REMARK 3 L13: -0.1570 L23: -0.3548 REMARK 3 S TENSOR REMARK 3 S11: -0.0980 S12: 0.3838 S13: -0.2147 REMARK 3 S21: -0.4872 S22: 0.0497 S23: -0.3913 REMARK 3 S31: 0.3038 S32: 0.3803 S33: 0.0358 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.4426 10.4590 8.0105 REMARK 3 T TENSOR REMARK 3 T11: 1.4083 T22: 0.8375 REMARK 3 T33: 1.1789 T12: 0.3816 REMARK 3 T13: 0.2006 T23: 0.1344 REMARK 3 L TENSOR REMARK 3 L11: 6.8776 L22: 2.2766 REMARK 3 L33: 7.0205 L12: 3.1164 REMARK 3 L13: -1.4419 L23: -3.1001 REMARK 3 S TENSOR REMARK 3 S11: -0.7292 S12: 0.3395 S13: 1.3221 REMARK 3 S21: 1.0101 S22: 1.7899 S23: 1.4913 REMARK 3 S31: -0.8570 S32: -0.7621 S33: -0.6276 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 16 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.8944 20.6601 12.6946 REMARK 3 T TENSOR REMARK 3 T11: 1.6124 T22: 1.9729 REMARK 3 T33: 2.3422 T12: 0.0667 REMARK 3 T13: -0.1661 T23: -0.3964 REMARK 3 L TENSOR REMARK 3 L11: 0.5835 L22: 1.8242 REMARK 3 L33: 1.5188 L12: 0.8224 REMARK 3 L13: -0.8433 L23: -1.6276 REMARK 3 S TENSOR REMARK 3 S11: -0.7681 S12: 0.8388 S13: -1.0341 REMARK 3 S21: -0.3269 S22: -0.5088 S23: -0.5976 REMARK 3 S31: 0.1504 S32: 2.0315 S33: 0.5126 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 31 THROUGH 45 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.2115 14.3635 -1.1611 REMARK 3 T TENSOR REMARK 3 T11: 1.5375 T22: 0.8029 REMARK 3 T33: 1.9221 T12: 0.2498 REMARK 3 T13: -0.3907 T23: 0.0035 REMARK 3 L TENSOR REMARK 3 L11: 4.6014 L22: 5.5268 REMARK 3 L33: 5.6469 L12: -5.0606 REMARK 3 L13: -3.2392 L23: 3.6414 REMARK 3 S TENSOR REMARK 3 S11: 0.4508 S12: -0.0634 S13: 1.7751 REMARK 3 S21: -1.6587 S22: -0.4180 S23: -0.9078 REMARK 3 S31: -1.0774 S32: 0.2839 S33: -0.3511 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 46 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.7622 -2.5562 7.1655 REMARK 3 T TENSOR REMARK 3 T11: 0.6650 T22: 0.7206 REMARK 3 T33: 0.7239 T12: 0.1455 REMARK 3 T13: -0.0466 T23: 0.2074 REMARK 3 L TENSOR REMARK 3 L11: 0.8525 L22: 0.4269 REMARK 3 L33: 1.2795 L12: 0.6112 REMARK 3 L13: -0.9313 L23: -0.8230 REMARK 3 S TENSOR REMARK 3 S11: 0.4789 S12: 0.7022 S13: 0.4011 REMARK 3 S21: 0.0467 S22: -0.1616 S23: 0.4800 REMARK 3 S31: -0.5397 S32: -0.4161 S33: -0.2447 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.6115 -72.1628 54.3257 REMARK 3 T TENSOR REMARK 3 T11: 1.7781 T22: 2.1835 REMARK 3 T33: 2.3274 T12: 0.1477 REMARK 3 T13: -0.5360 T23: -0.1845 REMARK 3 L TENSOR REMARK 3 L11: 4.3053 L22: 4.9023 REMARK 3 L33: 4.7338 L12: 2.9575 REMARK 3 L13: -0.7312 L23: 2.9997 REMARK 3 S TENSOR REMARK 3 S11: 0.6478 S12: -1.9893 S13: 0.8054 REMARK 3 S21: 0.9048 S22: 0.0327 S23: -1.5710 REMARK 3 S31: -0.3178 S32: 1.8698 S33: -0.6482 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 31 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.5375 -76.9435 47.4988 REMARK 3 T TENSOR REMARK 3 T11: 1.2518 T22: 0.9166 REMARK 3 T33: 1.0603 T12: 0.4520 REMARK 3 T13: -0.1849 T23: 0.1450 REMARK 3 L TENSOR REMARK 3 L11: 2.4482 L22: 3.9553 REMARK 3 L33: 2.3497 L12: 0.7054 REMARK 3 L13: -0.5817 L23: -0.1889 REMARK 3 S TENSOR REMARK 3 S11: 0.1034 S12: -0.1708 S13: -1.1288 REMARK 3 S21: 0.2547 S22: -0.0219 S23: -0.9707 REMARK 3 S31: 1.1501 S32: 1.1278 S33: -0.2099 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "R" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9C2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284544. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5-7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102736 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420 REMARK 200 RESOLUTION RANGE LOW (A) : 45.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 1.800 REMARK 200 R MERGE (I) : 0.08400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4 REMARK 200 DATA REDUNDANCY IN SHELL : 1.80 REMARK 200 R MERGE FOR SHELL (I) : 0.39200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE TRIHYDRATE PH REMARK 280 7.0, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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 APPLY THE FOLLOWING TO CHAINS: H, L, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLU H 1 REMARK 465 ILE H 2 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 THR H 233 REMARK 465 GLU A 1 REMARK 465 ILE A 2 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 THR A 231 REMARK 465 HIS A 232 REMARK 465 THR A 233 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 A R 51 O4' - C1' - N9 ANGL. DEV. = -5.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR H 57 -23.72 68.47 REMARK 500 SER H 88 62.81 36.75 REMARK 500 SER H 108 32.18 -145.31 REMARK 500 SER H 139 -179.57 -172.93 REMARK 500 LYS H 141 -1.11 84.77 REMARK 500 SER L 31 -126.11 50.55 REMARK 500 ALA L 52 -21.51 72.01 REMARK 500 ALA L 145 113.12 -161.56 REMARK 500 ASN L 153 -3.61 70.57 REMARK 500 GLU A 4 -159.15 -83.56 REMARK 500 TYR A 57 -23.23 67.60 REMARK 500 ARG A 70 -32.41 -130.15 REMARK 500 SER A 108 33.08 -143.68 REMARK 500 THR A 143 -64.14 -104.45 REMARK 500 SER A 144 72.59 54.90 REMARK 500 THR A 172 -33.23 -131.57 REMARK 500 SER B 31 -126.22 51.52 REMARK 500 SER B 51 -99.72 54.84 REMARK 500 ALA B 52 -15.62 -143.22 REMARK 500 ALA B 145 115.47 -161.24 REMARK 500 ASN B 153 -4.31 69.99 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C2K H 1 233 PDB 9C2K 9C2K 1 233 DBREF 9C2K L 1 215 PDB 9C2K 9C2K 1 215 DBREF 9C2K A 1 233 PDB 9C2K 9C2K 1 233 DBREF 9C2K B 1 215 PDB 9C2K 9C2K 1 215 DBREF 9C2K R 2 71 GB 902798 U26942.1 7175 7240 DBREF 9C2K C 2 71 GB 902798 U26942.1 7175 7240 SEQADV 9C2K G R 1 GB 902798 INSERTION SEQADV 9C2K G R 49 GB 902798 U 7222 CONFLICT SEQADV 9C2K A R 50 GB 902798 U 7223 CONFLICT SEQADV 9C2K A R 52 GB 902798 INSERTION SEQADV 9C2K C R 53 GB 902798 INSERTION SEQADV 9C2K A R 54 GB 902798 INSERTION SEQADV 9C2K C R 55 GB 902798 INSERTION SEQADV 9C2K C R 72 GB 902798 INSERTION SEQADV 9C2K G C 1 GB 902798 INSERTION SEQADV 9C2K G C 49 GB 902798 U 7222 CONFLICT SEQADV 9C2K A C 50 GB 902798 U 7223 CONFLICT SEQADV 9C2K A C 52 GB 902798 INSERTION SEQADV 9C2K C C 53 GB 902798 INSERTION SEQADV 9C2K A C 54 GB 902798 INSERTION SEQADV 9C2K C C 55 GB 902798 INSERTION SEQADV 9C2K C C 72 GB 902798 INSERTION SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE TYR ILE SER TYR SER SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE SER PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR SEQRES 9 H 233 ARG ARG ARG SER GLY ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 10 H 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER TYR SER PHE PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 A 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 A 233 ALA SER GLY PHE TYR ILE SER TYR SER SER ILE HIS TRP SEQRES 4 A 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 A 233 SER ILE SER PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 A 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 A 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 A 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN GLY TYR SEQRES 9 A 233 ARG ARG ARG SER GLY ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 10 A 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 B 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 B 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 B 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 B 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 B 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 B 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 B 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 B 215 SER TYR SER PHE PRO SER THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 R 72 G G C A C U A U G G G C G SEQRES 2 R 72 C A G C G U C A A U G A C SEQRES 3 R 72 G C U G A C G G U A C A G SEQRES 4 R 72 G C C A G A C A A G A A A SEQRES 5 R 72 C A C U U G U C U G A U A SEQRES 6 R 72 U A G U G C C SEQRES 1 C 72 G G C A C U A U G G G C G SEQRES 2 C 72 C A G C G U C A A U G A C SEQRES 3 C 72 G C U G A C G G U A C A G SEQRES 4 C 72 G C C A G A C A A G A A A SEQRES 5 C 72 C A C U U G U C U G A U A SEQRES 6 C 72 U A G U G C C HET GOL H 301 6 HET GOL H 302 6 HET GOL H 303 6 HET GOL H 304 6 HET PO4 L 301 5 HET GOL L 302 6 HET GOL L 303 6 HET GOL L 304 6 HET GOL L 305 6 HET GOL A 301 6 HET GOL A 302 6 HET PO4 B 301 5 HET PO4 B 302 5 HET GOL B 303 6 HET GOL B 304 6 HET GOL B 305 6 HET GOL B 306 6 HET GOL B 307 6 HET PO4 R 101 5 HET MG R 102 1 HET GOL R 103 6 HET PO4 C 101 5 HETNAM GOL GLYCEROL HETNAM PO4 PHOSPHATE ION HETNAM MG MAGNESIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 GOL 16(C3 H8 O3) FORMUL 11 PO4 5(O4 P 3-) FORMUL 26 MG MG 2+ FORMUL 29 HOH *409(H2 O) HELIX 1 AA1 TYR H 31 SER H 35 5 5 HELIX 2 AA2 ASP H 65 LYS H 68 5 4 HELIX 3 AA3 ARG H 90 THR H 94 5 5 HELIX 4 AA4 TYR H 104 GLY H 109 1 6 HELIX 5 AA5 SER H 168 ALA H 170 5 3 HELIX 6 AA6 SER H 199 LEU H 201 5 3 HELIX 7 AA7 GLN L 80 PHE L 84 5 5 HELIX 8 AA8 SER L 122 SER L 128 1 7 HELIX 9 AA9 LYS L 184 GLU L 188 1 5 HELIX 10 AB1 TYR A 31 SER A 35 5 5 HELIX 11 AB2 ARG A 90 THR A 94 5 5 HELIX 12 AB3 TYR A 104 GLY A 109 1 6 HELIX 13 AB4 SER A 139 THR A 143 5 5 HELIX 14 AB5 SER A 168 ALA A 170 5 3 HELIX 15 AB6 SER A 199 LEU A 201 5 3 HELIX 16 AB7 LYS A 213 ASN A 216 5 4 HELIX 17 AB8 GLN B 80 PHE B 84 5 5 HELIX 18 AB9 SER B 122 SER B 128 1 7 HELIX 19 AC1 LYS B 184 LYS B 189 1 6 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O SER H 24 N SER H 10 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N SER H 74 O TYR H 83 SHEET 1 AA2 6 GLY H 13 VAL H 15 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 SHEET 3 AA2 6 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AA2 6 ILE H 37 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA2 6 LEU H 48 ILE H 54 -1 O GLU H 49 N ARG H 41 SHEET 6 AA2 6 THR H 61 TYR H 63 -1 O TYR H 62 N SER H 53 SHEET 1 AA3 4 GLY H 13 VAL H 15 0 SHEET 2 AA3 4 THR H 119 VAL H 123 1 O THR H 122 N GLY H 13 SHEET 3 AA3 4 ALA H 95 GLN H 102 -1 N TYR H 97 O THR H 119 SHEET 4 AA3 4 PHE H 112 TRP H 115 -1 O TYR H 114 N ARG H 101 SHEET 1 AA4 4 SER H 132 LEU H 136 0 SHEET 2 AA4 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA4 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA5 4 THR H 143 SER H 144 0 SHEET 2 AA5 4 THR H 147 TYR H 157 -1 O THR H 147 N SER H 144 SHEET 3 AA5 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA5 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AA6 3 THR H 163 TRP H 166 0 SHEET 2 AA6 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AA6 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O LEU L 74 N ILE L 22 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 SER L 11 ALA L 14 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 12 SHEET 3 AA8 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 VAL L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA8 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AA8 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 SER L 11 ALA L 14 0 SHEET 2 AA9 4 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 12 SHEET 3 AA9 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O ASN L 138 N SER L 115 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB3 4 GLN A 6 SER A 10 0 SHEET 2 AB3 4 LEU A 21 SER A 28 -1 O SER A 24 N SER A 10 SHEET 3 AB3 4 THR A 81 MET A 86 -1 O LEU A 84 N LEU A 23 SHEET 4 AB3 4 PHE A 71 ASP A 76 -1 N SER A 74 O TYR A 83 SHEET 1 AB4 6 GLY A 13 VAL A 15 0 SHEET 2 AB4 6 THR A 119 VAL A 123 1 O THR A 122 N GLY A 13 SHEET 3 AB4 6 ALA A 95 GLN A 102 -1 N TYR A 97 O THR A 119 SHEET 4 AB4 6 ILE A 37 GLN A 42 -1 N VAL A 40 O TYR A 98 SHEET 5 AB4 6 GLU A 49 ILE A 54 -1 O GLU A 49 N ARG A 41 SHEET 6 AB4 6 THR A 61 TYR A 63 -1 O TYR A 62 N SER A 53 SHEET 1 AB5 4 GLY A 13 VAL A 15 0 SHEET 2 AB5 4 THR A 119 VAL A 123 1 O THR A 122 N GLY A 13 SHEET 3 AB5 4 ALA A 95 GLN A 102 -1 N TYR A 97 O THR A 119 SHEET 4 AB5 4 PHE A 112 TRP A 115 -1 O TYR A 114 N ARG A 101 SHEET 1 AB6 4 SER A 132 LEU A 136 0 SHEET 2 AB6 4 THR A 147 TYR A 157 -1 O LYS A 155 N SER A 132 SHEET 3 AB6 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB6 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AB7 4 SER A 132 LEU A 136 0 SHEET 2 AB7 4 THR A 147 TYR A 157 -1 O LYS A 155 N SER A 132 SHEET 3 AB7 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AB7 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AB8 3 THR A 163 TRP A 166 0 SHEET 2 AB8 3 ILE A 207 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AB8 3 THR A 217 LYS A 222 -1 O THR A 217 N HIS A 212 SHEET 1 AB9 4 MET B 5 SER B 8 0 SHEET 2 AB9 4 VAL B 20 ALA B 26 -1 O THR B 23 N SER B 8 SHEET 3 AB9 4 ASP B 71 ILE B 76 -1 O PHE B 72 N CYS B 24 SHEET 4 AB9 4 PHE B 63 SER B 68 -1 N SER B 68 O ASP B 71 SHEET 1 AC1 6 SER B 11 ALA B 14 0 SHEET 2 AC1 6 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC1 6 THR B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC1 6 VAL B 34 GLN B 39 -1 N GLN B 39 O THR B 86 SHEET 5 AC1 6 LYS B 46 TYR B 50 -1 O LEU B 48 N TRP B 36 SHEET 6 AC1 6 SER B 54 LEU B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AC2 4 SER B 11 ALA B 14 0 SHEET 2 AC2 4 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 12 SHEET 3 AC2 4 THR B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC2 4 THR B 98 PHE B 99 -1 O THR B 98 N GLN B 91 SHEET 1 AC3 4 SER B 115 PHE B 119 0 SHEET 2 AC3 4 THR B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AC3 4 TYR B 174 SER B 183 -1 O LEU B 180 N VAL B 133 SHEET 4 AC3 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AC4 4 ALA B 154 LEU B 155 0 SHEET 2 AC4 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AC4 4 VAL B 192 THR B 198 -1 O ALA B 194 N LYS B 150 SHEET 4 AC4 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.04 SSBOND 2 CYS H 152 CYS H 208 1555 1555 2.05 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.09 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.06 SSBOND 5 CYS A 25 CYS A 99 1555 1555 2.06 SSBOND 6 CYS A 152 CYS A 208 1555 1555 2.05 SSBOND 7 CYS B 24 CYS B 89 1555 1555 2.08 SSBOND 8 CYS B 135 CYS B 195 1555 1555 2.04 CISPEP 1 PHE H 158 PRO H 159 0 -0.18 CISPEP 2 GLU H 160 PRO H 161 0 -2.28 CISPEP 3 SER L 8 PRO L 9 0 -4.59 CISPEP 4 PHE L 95 PRO L 96 0 -1.03 CISPEP 5 TYR L 141 PRO L 142 0 -0.41 CISPEP 6 PHE A 158 PRO A 159 0 -1.11 CISPEP 7 GLU A 160 PRO A 161 0 -3.63 CISPEP 8 SER B 8 PRO B 9 0 -3.73 CISPEP 9 PHE B 95 PRO B 96 0 0.45 CISPEP 10 TYR B 141 PRO B 142 0 2.64 CRYST1 72.359 76.238 82.599 116.56 94.91 102.75 P 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013820 0.003127 0.003062 0.00000 SCALE2 0.000000 0.013448 0.007350 0.00000 SCALE3 0.000000 0.000000 0.013848 0.00000 MTRIX1 1 -0.395785 0.784067 0.478114 -0.01415 1 MTRIX2 1 0.784185 0.017608 0.620277 -1.91188 1 MTRIX3 1 0.477920 0.620426 -0.621823 94.45963 1 MTRIX1 2 -0.405704 0.781748 0.473577 -0.64759 1 MTRIX2 2 0.774793 0.019281 0.631922 -2.51502 1 MTRIX3 2 0.484872 0.623297 -0.613515 94.77967 1 MTRIX1 3 -0.436027 0.761934 0.478892 -5.11000 1 MTRIX2 3 0.695566 -0.052323 0.716554 -15.52024 1 MTRIX3 3 0.571024 0.645538 -0.507161 93.73821 1