REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.350 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.018 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.96 REMARK 3 NUMBER OF REFLECTIONS : 146559 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.1755 REMARK 3 R VALUE (WORKING SET) : 0.1753 REMARK 3 FREE R VALUE : 0.2037 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.7 REMARK 3 FREE R VALUE TEST SET COUNT : 1017 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 54.0320 - 4.4947 1.00 21443 140 0.1567 0.1813 REMARK 3 2 4.4947 - 3.5678 1.00 20864 176 0.1476 0.1745 REMARK 3 3 3.5678 - 3.1168 1.00 20746 137 0.1722 0.1834 REMARK 3 4 3.1168 - 2.8319 1.00 20686 146 0.1804 0.2380 REMARK 3 5 2.8319 - 2.6289 1.00 20663 152 0.2027 0.2479 REMARK 3 6 2.6289 - 2.4739 1.00 20600 132 0.2379 0.3057 REMARK 3 7 2.4739 - 2.3500 1.00 20540 134 0.2629 0.2697 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 : 0.333 REMARK 3 B_SOL : 46.232 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.30 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.12 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.4 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.7988 REMARK 3 B22 (A**2) : -0.6543 REMARK 3 B33 (A**2) : -0.3375 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : 0.0000 REMARK 3 B23 (A**2) : 0.0000 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 : 0.006 21086 REMARK 3 ANGLE : 0.676 28562 REMARK 3 CHIRALITY : 0.043 3186 REMARK 3 PLANARITY : 0.003 3700 REMARK 3 DIHEDRAL : 13.902 7674 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND (RESID 1:454 OR RESID 2004:2007) REMARK 3 ORIGIN FOR THE GROUP (A): 44.5823 84.4665 53.3158 REMARK 3 T TENSOR REMARK 3 T11: 0.1817 T22: 0.0810 REMARK 3 T33: 0.1277 T12: -0.0007 REMARK 3 T13: 0.0012 T23: 0.0387 REMARK 3 L TENSOR REMARK 3 L11: 0.9445 L22: 0.8007 REMARK 3 L33: 0.7587 L12: -0.0788 REMARK 3 L13: -0.3304 L23: 0.3767 REMARK 3 S TENSOR REMARK 3 S11: 0.0064 S12: 0.0030 S13: -0.0049 REMARK 3 S21: -0.0792 S22: -0.0423 S23: 0.0891 REMARK 3 S31: 0.0270 S32: -0.0378 S33: 0.0268 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN C AND (RESID 1:454 OR RESID 2004:2007) REMARK 3 ORIGIN FOR THE GROUP (A): 78.9097 82.1180 117.8466 REMARK 3 T TENSOR REMARK 3 T11: 0.2679 T22: 0.1888 REMARK 3 T33: 0.1273 T12: 0.0449 REMARK 3 T13: 0.0586 T23: 0.0142 REMARK 3 L TENSOR REMARK 3 L11: 1.3797 L22: 0.7833 REMARK 3 L33: 1.6570 L12: 0.0142 REMARK 3 L13: -0.2429 L23: -0.2802 REMARK 3 S TENSOR REMARK 3 S11: -0.0774 S12: -0.0038 S13: -0.0828 REMARK 3 S21: -0.0627 S22: -0.0183 S23: -0.1369 REMARK 3 S31: 0.3724 S32: 0.1725 S33: 0.0803 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN B AND RESID 1:56 REMARK 3 ORIGIN FOR THE GROUP (A): 117.3628 83.7845 35.0762 REMARK 3 T TENSOR REMARK 3 T11: 0.4939 T22: 1.1278 REMARK 3 T33: 0.7299 T12: 0.3152 REMARK 3 T13: -0.0711 T23: -0.1019 REMARK 3 L TENSOR REMARK 3 L11: 3.2159 L22: 0.9767 REMARK 3 L33: 2.4804 L12: -1.3378 REMARK 3 L13: -0.0799 L23: 0.5726 REMARK 3 S TENSOR REMARK 3 S11: -0.2614 S12: 0.0518 S13: -0.1054 REMARK 3 S21: 0.2217 S22: 0.1098 S23: -0.6032 REMARK 3 S31: 0.2866 S32: 0.7165 S33: 0.1648 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN B AND (RESID 57:108 OR RESID 354:433) REMARK 3 ORIGIN FOR THE GROUP (A): 94.9303 102.1685 53.1640 REMARK 3 T TENSOR REMARK 3 T11: 0.2626 T22: 0.4293 REMARK 3 T33: 0.4457 T12: 0.0333 REMARK 3 T13: -0.0550 T23: -0.0764 REMARK 3 L TENSOR REMARK 3 L11: 1.5834 L22: 1.2067 REMARK 3 L33: 2.7810 L12: -0.3256 REMARK 3 L13: -0.6764 L23: 1.1158 REMARK 3 S TENSOR REMARK 3 S11: -0.0237 S12: -0.2778 S13: 0.2733 REMARK 3 S21: 0.1184 S22: 0.2052 S23: -0.2351 REMARK 3 S31: 0.1248 S32: 0.5371 S33: -0.1769 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN B AND (RESID 109:352 OR RESID 2001:2003) REMARK 3 ORIGIN FOR THE GROUP (A): 60.9882 112.2779 63.8442 REMARK 3 T TENSOR REMARK 3 T11: 0.2205 T22: 0.1241 REMARK 3 T33: 0.1653 T12: -0.0037 REMARK 3 T13: 0.0299 T23: -0.0101 REMARK 3 L TENSOR REMARK 3 L11: 1.4121 L22: 1.9466 REMARK 3 L33: 0.4898 L12: 0.2606 REMARK 3 L13: 0.0082 L23: 0.2384 REMARK 3 S TENSOR REMARK 3 S11: -0.0025 S12: -0.1312 S13: 0.2094 REMARK 3 S21: 0.0090 S22: 0.0403 S23: -0.0272 REMARK 3 S31: -0.1390 S32: 0.0353 S33: -0.0416 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN B AND RESID 434:471 REMARK 3 ORIGIN FOR THE GROUP (A): 109.9487 83.6738 19.2078 REMARK 3 T TENSOR REMARK 3 T11: 0.5623 T22: 0.9402 REMARK 3 T33: 0.5506 T12: 0.2446 REMARK 3 T13: 0.0124 T23: 0.1252 REMARK 3 L TENSOR REMARK 3 L11: 4.4859 L22: 1.6869 REMARK 3 L33: 4.4313 L12: 0.3221 REMARK 3 L13: 0.0168 L23: -0.0444 REMARK 3 S TENSOR REMARK 3 S11: -0.0138 S12: 0.0963 S13: -0.1398 REMARK 3 S21: 0.0507 S22: 0.3954 S23: -0.4773 REMARK 3 S31: 0.4502 S32: 0.1813 S33: -0.2196 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN D AND (RESID 109:352 OR RESID 2001:2003) REMARK 3 ORIGIN FOR THE GROUP (A): 54.6832 97.2554 99.6057 REMARK 3 T TENSOR REMARK 3 T11: 0.2455 T22: 0.4185 REMARK 3 T33: 0.0868 T12: -0.0475 REMARK 3 T13: 0.0272 T23: 0.0375 REMARK 3 L TENSOR REMARK 3 L11: 1.0868 L22: 0.7135 REMARK 3 L33: 1.9330 L12: -0.2137 REMARK 3 L13: 0.5605 L23: -0.2128 REMARK 3 S TENSOR REMARK 3 S11: -0.1267 S12: 0.1673 S13: 0.2417 REMARK 3 S21: -0.0746 S22: 0.0525 S23: 0.0701 REMARK 3 S31: -0.0036 S32: -0.5932 S33: 0.0333 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN D AND (RESID 57:108 OR RESID 353:433) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9148 95.7194 115.8250 REMARK 3 T TENSOR REMARK 3 T11: 0.7602 T22: 1.2791 REMARK 3 T33: 1.1286 T12: 0.1451 REMARK 3 T13: 0.1861 T23: 0.3192 REMARK 3 L TENSOR REMARK 3 L11: 1.0509 L22: 0.9505 REMARK 3 L33: 0.3319 L12: 0.1125 REMARK 3 L13: 0.0109 L23: -0.5572 REMARK 3 S TENSOR REMARK 3 S11: -0.3051 S12: -0.1019 S13: -0.2234 REMARK 3 S21: 0.2018 S22: -0.1310 S23: 0.1736 REMARK 3 S31: 0.4157 S32: 0.0548 S33: 0.3445 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN H AND RESID 1:119 REMARK 3 ORIGIN FOR THE GROUP (A): 110.5054 86.7539 87.0947 REMARK 3 T TENSOR REMARK 3 T11: 0.7396 T22: 1.0917 REMARK 3 T33: 0.6136 T12: 0.3161 REMARK 3 T13: 0.3249 T23: 0.2665 REMARK 3 L TENSOR REMARK 3 L11: 0.8651 L22: 0.0505 REMARK 3 L33: 1.2199 L12: -0.0930 REMARK 3 L13: -0.6644 L23: 0.2202 REMARK 3 S TENSOR REMARK 3 S11: 0.0339 S12: 0.4970 S13: -0.0376 REMARK 3 S21: -0.4988 S22: -0.3409 S23: -0.2886 REMARK 3 S31: 0.7782 S32: 0.5176 S33: 0.3840 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN H AND RESID 120:221 REMARK 3 ORIGIN FOR THE GROUP (A): 146.5635 80.0226 83.3810 REMARK 3 T TENSOR REMARK 3 T11: 0.4119 T22: 1.0673 REMARK 3 T33: 1.1558 T12: 0.2636 REMARK 3 T13: 0.1487 T23: 0.2074 REMARK 3 L TENSOR REMARK 3 L11: 0.6396 L22: 1.1726 REMARK 3 L33: 1.1599 L12: -0.5896 REMARK 3 L13: 0.4661 L23: 0.1951 REMARK 3 S TENSOR REMARK 3 S11: 0.4002 S12: 0.8650 S13: -0.1064 REMARK 3 S21: -0.2602 S22: -0.0664 S23: -0.7887 REMARK 3 S31: -0.3045 S32: 0.0562 S33: -0.1398 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN L AND RESID 1:108 REMARK 3 ORIGIN FOR THE GROUP (A): 119.7925 97.5928 103.2844 REMARK 3 T TENSOR REMARK 3 T11: 0.3163 T22: 1.1411 REMARK 3 T33: 0.9598 T12: 0.0078 REMARK 3 T13: 0.0573 T23: 0.3962 REMARK 3 L TENSOR REMARK 3 L11: 0.4038 L22: 0.2255 REMARK 3 L33: 0.3329 L12: -0.1335 REMARK 3 L13: -0.0884 L23: -0.1830 REMARK 3 S TENSOR REMARK 3 S11: -0.0847 S12: 0.0910 S13: 0.5058 REMARK 3 S21: 0.0168 S22: -0.2561 S23: -0.6528 REMARK 3 S31: -0.0210 S32: 0.8177 S33: -0.0417 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN L AND RESID 109:214 REMARK 3 ORIGIN FOR THE GROUP (A): 150.0809 95.3376 82.6679 REMARK 3 T TENSOR REMARK 3 T11: 1.1280 T22: 1.4278 REMARK 3 T33: 1.6964 T12: 0.2729 REMARK 3 T13: 0.6509 T23: 0.6103 REMARK 3 L TENSOR REMARK 3 L11: 0.0968 L22: 0.8049 REMARK 3 L33: 1.3891 L12: 0.1958 REMARK 3 L13: -0.1806 L23: 0.1231 REMARK 3 S TENSOR REMARK 3 S11: 0.4573 S12: 0.0979 S13: 0.0678 REMARK 3 S21: -0.8535 S22: -0.0582 S23: -0.6220 REMARK 3 S31: -0.5677 S32: 0.2103 S33: -0.1822 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN E AND RESID 1:119 REMARK 3 ORIGIN FOR THE GROUP (A): 9.5213 91.1187 80.7064 REMARK 3 T TENSOR REMARK 3 T11: 0.1775 T22: 0.2531 REMARK 3 T33: 0.3260 T12: -0.0149 REMARK 3 T13: 0.0301 T23: -0.0752 REMARK 3 L TENSOR REMARK 3 L11: 1.3409 L22: 0.8334 REMARK 3 L33: 1.1138 L12: 0.5521 REMARK 3 L13: -0.3135 L23: -0.1971 REMARK 3 S TENSOR REMARK 3 S11: 0.1379 S12: -0.1304 S13: 0.1636 REMARK 3 S21: 0.1728 S22: -0.1908 S23: 0.0605 REMARK 3 S31: -0.0341 S32: -0.1720 S33: 0.0469 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN E AND RESID 120:221 REMARK 3 ORIGIN FOR THE GROUP (A): -24.1378 78.0159 88.4692 REMARK 3 T TENSOR REMARK 3 T11: 0.3292 T22: 0.4070 REMARK 3 T33: 0.3587 T12: -0.0964 REMARK 3 T13: -0.1141 T23: -0.0929 REMARK 3 L TENSOR REMARK 3 L11: 1.5950 L22: 0.9909 REMARK 3 L33: 1.4651 L12: 0.8325 REMARK 3 L13: 0.6431 L23: 0.3623 REMARK 3 S TENSOR REMARK 3 S11: 0.4510 S12: -0.6521 S13: -0.1113 REMARK 3 S21: 0.4501 S22: -0.2937 S23: -0.1700 REMARK 3 S31: 0.3705 S32: -0.2128 S33: -0.1085 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN F AND RESID 1:108 REMARK 3 ORIGIN FOR THE GROUP (A): -0.5198 90.3747 61.5357 REMARK 3 T TENSOR REMARK 3 T11: 0.1713 T22: 0.4595 REMARK 3 T33: 0.4263 T12: -0.0075 REMARK 3 T13: -0.0386 T23: -0.0201 REMARK 3 L TENSOR REMARK 3 L11: 1.2886 L22: 0.0805 REMARK 3 L33: 0.5779 L12: 0.1319 REMARK 3 L13: -0.0937 L23: 0.0089 REMARK 3 S TENSOR REMARK 3 S11: 0.0465 S12: 0.3342 S13: 0.2221 REMARK 3 S21: -0.0929 S22: -0.0408 S23: 0.1575 REMARK 3 S31: 0.0252 S32: -0.3849 S33: -0.0328 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN F AND RESID 109:214 REMARK 3 ORIGIN FOR THE GROUP (A): -30.2430 90.9560 80.8720 REMARK 3 T TENSOR REMARK 3 T11: 0.2662 T22: 0.3919 REMARK 3 T33: 0.7221 T12: 0.0020 REMARK 3 T13: -0.0931 T23: -0.2851 REMARK 3 L TENSOR REMARK 3 L11: 1.3133 L22: 1.0709 REMARK 3 L33: 2.6326 L12: -0.0658 REMARK 3 L13: 0.2211 L23: 0.8404 REMARK 3 S TENSOR REMARK 3 S11: -0.1465 S12: -0.2729 S13: 0.9112 REMARK 3 S21: 0.0799 S22: -0.1429 S23: 0.3207 REMARK 3 S31: -0.3563 S32: -0.2941 S33: 0.2473 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN I REMARK 3 ORIGIN FOR THE GROUP (A): 46.3904 103.5836 74.0419 REMARK 3 T TENSOR REMARK 3 T11: 0.3614 T22: 0.3523 REMARK 3 T33: 0.1725 T12: -0.0463 REMARK 3 T13: -0.0002 T23: 0.0624 REMARK 3 L TENSOR REMARK 3 L11: 3.8167 L22: 1.3652 REMARK 3 L33: 6.0801 L12: -2.0311 REMARK 3 L13: -0.6067 L23: -0.7400 REMARK 3 S TENSOR REMARK 3 S11: 0.4060 S12: -0.5273 S13: -0.2410 REMARK 3 S21: 0.3738 S22: 0.0214 S23: 0.1399 REMARK 3 S31: 0.0839 S32: -0.2747 S33: -0.1531 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN J REMARK 3 ORIGIN FOR THE GROUP (A): 71.0147 90.5198 91.4768 REMARK 3 T TENSOR REMARK 3 T11: 0.5698 T22: 0.4156 REMARK 3 T33: 0.2324 T12: -0.0228 REMARK 3 T13: 0.0188 T23: 0.0116 REMARK 3 L TENSOR REMARK 3 L11: 3.5950 L22: 0.3928 REMARK 3 L33: 2.5984 L12: -0.4193 REMARK 3 L13: 1.8002 L23: -0.9739 REMARK 3 S TENSOR REMARK 3 S11: 0.2787 S12: 0.2197 S13: -0.4949 REMARK 3 S21: -0.2563 S22: -0.0551 S23: -0.1592 REMARK 3 S31: 0.5715 S32: 0.4495 S33: -0.1278 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3ZE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-12. REMARK 100 THE PDBE ID CODE IS EBI-54974. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.9 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23ID 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 : DOUBLE SI CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146644 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.35 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.4 REMARK 200 R MERGE (I) : 0.14 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.00 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.94 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.90 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 3T3P REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM REMARK 280 SULFATE, 0.1 M TRIS-HCL, PH 8.9 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 116.60500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.78000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 116.60500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.78000 REMARK 290 SMTRY3 4 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 11890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 67940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, I 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 61480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, J, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 A 455 REMARK 465 ALA A 456 REMARK 465 SER A 457 REMARK 465 GLY B 1 REMARK 465 PRO B 2 REMARK 465 GLU B 472 REMARK 465 VAL C 454 REMARK 465 LYS C 455 REMARK 465 ALA C 456 REMARK 465 SER C 457 REMARK 465 GLY D 1 REMARK 465 PRO D 2 REMARK 465 ASN D 3 REMARK 465 ILE D 4 REMARK 465 CYS D 5 REMARK 465 THR D 6 REMARK 465 THR D 7 REMARK 465 ARG D 8 REMARK 465 GLY D 9 REMARK 465 VAL D 10 REMARK 465 SER D 11 REMARK 465 SER D 12 REMARK 465 CYS D 13 REMARK 465 GLN D 14 REMARK 465 GLN D 15 REMARK 465 CYS D 16 REMARK 465 LEU D 17 REMARK 465 ALA D 18 REMARK 465 VAL D 19 REMARK 465 SER D 20 REMARK 465 PRO D 21 REMARK 465 MET D 22 REMARK 465 CYS D 23 REMARK 465 ALA D 24 REMARK 465 TRP D 25 REMARK 465 CYS D 26 REMARK 465 SER D 27 REMARK 465 ASP D 28 REMARK 465 GLU D 29 REMARK 465 ALA D 30 REMARK 465 LEU D 31 REMARK 465 PRO D 32 REMARK 465 LEU D 33 REMARK 465 GLY D 34 REMARK 465 SER D 35 REMARK 465 PRO D 36 REMARK 465 ARG D 37 REMARK 465 CYS D 38 REMARK 465 ASP D 39 REMARK 465 LEU D 40 REMARK 465 LYS D 41 REMARK 465 GLU D 42 REMARK 465 ASN D 43 REMARK 465 LEU D 44 REMARK 465 LEU D 45 REMARK 465 LYS D 46 REMARK 465 ASP D 47 REMARK 465 ASN D 48 REMARK 465 CYS D 49 REMARK 465 ALA D 50 REMARK 465 PRO D 51 REMARK 465 GLU D 52 REMARK 465 SER D 53 REMARK 465 ILE D 54 REMARK 465 GLU D 55 REMARK 465 PHE D 56 REMARK 465 PRO D 57 REMARK 465 VAL D 58 REMARK 465 LYS D 72 REMARK 465 GLY D 73 REMARK 465 SER D 74 REMARK 465 GLY D 75 REMARK 465 ASP D 76 REMARK 465 SER D 77 REMARK 465 SER D 78 REMARK 465 GLN D 79 REMARK 465 ASP D 434 REMARK 465 CYS D 435 REMARK 465 ALA D 436 REMARK 465 CYS D 437 REMARK 465 GLN D 438 REMARK 465 ALA D 439 REMARK 465 GLN D 440 REMARK 465 ALA D 441 REMARK 465 GLU D 442 REMARK 465 PRO D 443 REMARK 465 ASN D 444 REMARK 465 SER D 445 REMARK 465 HIS D 446 REMARK 465 ARG D 447 REMARK 465 CYS D 448 REMARK 465 ASN D 449 REMARK 465 ASN D 450 REMARK 465 GLY D 451 REMARK 465 ASN D 452 REMARK 465 GLY D 453 REMARK 465 THR D 454 REMARK 465 PHE D 455 REMARK 465 GLU D 456 REMARK 465 CYS D 457 REMARK 465 GLY D 458 REMARK 465 VAL D 459 REMARK 465 CYS D 460 REMARK 465 ARG D 461 REMARK 465 CYS D 462 REMARK 465 GLY D 463 REMARK 465 PRO D 464 REMARK 465 GLY D 465 REMARK 465 TRP D 466 REMARK 465 LEU D 467 REMARK 465 GLY D 468 REMARK 465 SER D 469 REMARK 465 GLN D 470 REMARK 465 CYS D 471 REMARK 465 GLU D 472 REMARK 465 GLY E 135 REMARK 465 ASP E 136 REMARK 465 THR E 137 REMARK 465 GLY E 220 REMARK 465 PRO E 221 REMARK 465 GLY H 135 REMARK 465 ASP H 136 REMARK 465 THR H 137 REMARK 465 GLY H 220 REMARK 465 PRO H 221 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 ARG A 90 CZ REMARK 480 GLN A 177 CD REMARK 480 GLU C 48 CD 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 OE1 GLN A 351 O HOH A 3394 2.19 REMARK 500 OG SER A 384 O HOH A 3430 2.06 REMARK 500 OD1 ASP B 126 O HOH B 3039 2.13 REMARK 500 HG A SER B 130 HG A SER B 337 1.32 REMARK 500 OG B SER B 130 OD2 ASP B 336 2.14 REMARK 500 OD1 ASN B 148 O HOH B 3048 2.10 REMARK 500 OE1B GLN B 319 O HOH B 3169 2.13 REMARK 500 O MET B 335 O HOH B 3040 2.10 REMARK 500 ND2 ASN B 371 C1 NAG B 3371 1.44 REMARK 500 ND2 ASN B 371 C2 NAG B 3371 2.12 REMARK 500 OD1B ASN C 2 O HOH C 3001 2.12 REMARK 500 OE1 GLN C 351 O HOH C 3221 2.13 REMARK 500 OG SER C 384 O HOH C 3243 2.05 REMARK 500 N B GLY I 492 O HOH A 3238 2.03 REMARK 500 NH2A ARG I 493 O HOH A 3222 2.17 REMARK 500 OG SER L 9 O HOH L 3004 2.19 REMARK 500 O3 SO4 A 1457 O HOH A 3482 2.09 REMARK 500 O HOH A 3052 O HOH A 3126 2.18 REMARK 500 O HOH A 3052 O HOH B 3055 1.98 REMARK 500 O HOH A 3058 O HOH A 3096 2.08 REMARK 500 O HOH A 3077 O HOH A 3210 2.05 REMARK 500 O HOH A 3077 O HOH A 3220 2.06 REMARK 500 O HOH A 3111 O HOH A 3270 2.20 REMARK 500 O HOH A 3137 O HOH A 3138 2.19 REMARK 500 O HOH A 3137 O HOH A 3320 1.95 REMARK 500 O HOH A 3138 O HOH A 3319 2.03 REMARK 500 O HOH A 3140 O HOH A 3323 1.85 REMARK 500 O HOH A 3195 O HOH A 3445 1.80 REMARK 500 O HOH A 3195 O HOH A 3449 1.77 REMARK 500 O HOH A 3195 O HOH A 3446 1.90 REMARK 500 O HOH A 3199 O HOH A 3255 2.11 REMARK 500 O HOH A 3200 O HOH A 3255 2.18 REMARK 500 O HOH A 3216 O HOH A 3476 2.15 REMARK 500 O HOH A 3216 O HOH A 3217 2.15 REMARK 500 O HOH A 3217 O HOH A 3476 2.03 REMARK 500 O HOH A 3220 O HOH A 3223 2.09 REMARK 500 O HOH A 3237 O HOH A 3238 2.16 REMARK 500 O HOH A 3314 O HOH A 3319 2.14 REMARK 500 O HOH A 3316 O HOH A 3381 2.07 REMARK 500 O HOH A 3322 O HOH A 3323 2.07 REMARK 500 O HOH A 3323 O HOH A 3324 2.19 REMARK 500 O HOH A 3343 O HOH A 3360 2.05 REMARK 500 O HOH A 3358 O HOH A 3359 2.17 REMARK 500 O HOH A 3360 O HOH A 3425 2.02 REMARK 500 O HOH A 3381 O HOH A 3382 2.09 REMARK 500 O HOH A 3445 O HOH A 3449 1.81 REMARK 500 O HOH A 3446 O HOH A 3449 2.03 REMARK 500 O HOH B 3031 O HOH B 3164 2.15 REMARK 500 O HOH B 3040 O HOH B 3041 2.11 REMARK 500 O HOH C 3018 O HOH C 3036 2.08 REMARK 500 REMARK 500 THIS ENTRY HAS 59 CLOSE CONTACTS 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 O HOH C 3252 O HOH A 3480 1556 2.18 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 GLN A 47 -2.95 79.21 REMARK 500 SER A 101 -127.40 57.07 REMARK 500 LYS A 118 -116.99 60.04 REMARK 500 GLU A 123 133.98 98.52 REMARK 500 PHE A 191 12.67 83.63 REMARK 500 LEU A 212 -43.97 74.79 REMARK 500 TRP A 235 108.22 -57.36 REMARK 500 THR A 296 145.68 -171.36 REMARK 500 ARG B 8 -45.25 -141.42 REMARK 500 PHE B 56 77.30 -161.97 REMARK 500 ASP B 66 48.35 -152.83 REMARK 500 ILE B 131 30.27 -87.80 REMARK 500 VAL B 157 -85.27 -124.50 REMARK 500 PRO B 169 -178.56 -69.40 REMARK 500 LYS B 181 56.85 -92.75 REMARK 500 SER B 213 -151.70 -110.00 REMARK 500 ASP B 241 70.82 -107.68 REMARK 500 LEU B 258 -10.04 86.05 REMARK 500 SER B 334 82.81 -63.83 REMARK 500 MET B 335 -60.72 74.61 REMARK 500 CYS B 374 -82.84 -97.84 REMARK 500 SER C 101 -133.05 50.20 REMARK 500 LYS C 118 -118.91 64.65 REMARK 500 GLU C 123 138.81 96.22 REMARK 500 PHE C 191 14.16 80.14 REMARK 500 LEU C 212 -49.19 75.74 REMARK 500 THR C 296 143.89 -173.87 REMARK 500 VAL C 325 -31.11 -132.87 REMARK 500 PRO C 337 90.92 -66.66 REMARK 500 VAL D 107 -58.21 -133.11 REMARK 500 MET D 142 -40.64 -173.54 REMARK 500 ASN D 148 65.99 -104.58 REMARK 500 VAL D 157 -83.51 -127.72 REMARK 500 SER D 213 -147.01 -103.82 REMARK 500 ARG D 214 135.65 -170.79 REMARK 500 LEU D 258 -6.38 85.82 REMARK 500 SER D 334 -169.73 -163.56 REMARK 500 LYS D 410 -13.89 74.21 REMARK 500 LEU E 100 -67.27 -90.89 REMARK 500 VAL E 133 -73.28 -64.63 REMARK 500 SER E 162 29.69 41.68 REMARK 500 SER E 178 67.31 37.65 REMARK 500 ASP E 179 -13.81 78.23 REMARK 500 SER F 77 83.93 64.45 REMARK 500 ASN F 190 -68.23 -121.07 REMARK 500 ASN F 212 -66.76 67.92 REMARK 500 SER H 85 58.03 38.64 REMARK 500 ALA H 92 -179.14 -172.46 REMARK 500 TYR H 101 -58.11 -124.02 REMARK 500 THR H 122 97.13 -67.37 REMARK 500 REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B2001 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP I 495 OD1 REMARK 620 2 SER B 121 OG 92.8 REMARK 620 3 SER B 123 OG 86.3 91.5 REMARK 620 4 GLU B 220 OE2 92.4 88.8 178.7 REMARK 620 5 HOH B3035 O 162.7 79.0 78.8 102.6 REMARK 620 6 HOH B3038 O 96.3 169.3 94.6 85.3 93.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B2002 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 251 OD2 REMARK 620 2 HOH B3117 O 90.7 REMARK 620 3 SER B 123 O 80.4 105.3 REMARK 620 4 HOH B3041 O 97.8 146.6 107.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B2003 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 217 OD1 REMARK 620 2 ASP B 217 O 76.2 REMARK 620 3 ASP B 158 OD2 100.3 169.4 REMARK 620 4 ASN B 215 OD1 87.5 90.5 99.5 REMARK 620 5 PRO B 219 O 105.1 87.8 83.4 166.5 REMARK 620 6 GLU B 220 OE1 166.6 93.2 91.6 84.5 82.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN D2001 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH D3011 O REMARK 620 2 SER D 121 OG 172.2 REMARK 620 3 SER D 123 OG 96.4 90.2 REMARK 620 4 GLU D 220 OE2 86.0 87.9 173.0 REMARK 620 5 ASP J 495 OD1 93.6 91.2 84.1 89.2 REMARK 620 6 HOH D3009 O 102.2 74.9 79.4 106.5 158.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN D2002 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH D3014 O REMARK 620 2 ASP D 127 OD2 78.1 REMARK 620 3 ASP D 251 OD2 102.6 90.0 REMARK 620 4 HOH D3010 O 90.3 167.5 87.9 REMARK 620 5 SER D 123 O 171.9 94.2 80.0 97.5 REMARK 620 6 ASP D 126 OD1 96.7 82.0 157.1 104.3 79.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN D2003 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO D 219 O REMARK 620 2 ASP D 158 OD2 78.5 REMARK 620 3 GLU D 220 OE1 86.8 97.0 REMARK 620 4 ASP D 217 O 93.5 166.1 93.8 REMARK 620 5 ASN D 215 OD1 174.4 97.0 90.5 91.6 REMARK 620 6 ASP D 217 OD1 96.8 93.5 169.3 76.0 86.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 243 OE1 REMARK 620 2 GLU A 243 OE2 54.6 REMARK 620 3 ASP A 245 OD1 122.1 67.4 REMARK 620 4 ASP A 247 O 79.8 79.1 91.3 REMARK 620 5 THR A 250 O 70.7 125.0 166.5 86.7 REMARK 620 6 THR A 250 OG1 139.6 145.3 90.1 75.2 76.5 REMARK 620 7 GLU A 252 OE1 85.0 80.3 84.5 159.0 102.0 125.2 REMARK 620 8 GLU A 252 OE2 124.7 131.0 91.3 147.8 83.4 72.7 53.1 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 301 OD1 REMARK 620 2 ASP A 297 OD1 77.7 REMARK 620 3 ASN A 299 OD1 82.4 77.6 REMARK 620 4 ARG A 303 O 90.5 82.7 160.1 REMARK 620 5 ASP A 305 OD1 148.9 130.6 113.1 82.2 REMARK 620 6 ASP A 305 OD2 157.8 81.8 84.9 95.4 53.3 REMARK 620 7 HOH A3348 O 81.4 156.5 89.1 108.2 72.4 116.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2006 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 365 OD1 REMARK 620 2 TYR A 371 O 75.8 REMARK 620 3 ASP A 373 OD2 88.7 93.3 REMARK 620 4 ASP A 369 OD1 75.2 89.0 162.7 REMARK 620 5 ASP A 367 OD1 81.5 157.2 84.6 86.6 REMARK 620 6 ASP A 373 OD1 134.4 82.4 52.9 144.3 113.5 REMARK 620 7 HOH A3413 O 149.5 100.1 121.8 74.5 100.2 73.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2007 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 426 OD1 REMARK 620 2 ASN A 430 OD1 85.0 REMARK 620 3 TYR A 432 O 79.2 87.4 REMARK 620 4 ASP A 428 OD1 77.0 86.0 155.7 REMARK 620 5 ASP A 434 OD1 134.4 134.4 81.0 119.7 REMARK 620 6 ASP A 434 OD2 87.5 171.0 96.1 87.4 54.5 REMARK 620 7 HOH A3470 O 147.7 79.5 127.8 73.8 73.7 104.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 243 OE2 REMARK 620 2 ASP C 245 OD1 59.9 REMARK 620 3 GLU C 252 OE1 81.1 87.6 REMARK 620 4 GLU C 252 OE2 128.1 90.5 54.1 REMARK 620 5 ASP C 247 O 68.4 82.4 148.9 154.6 REMARK 620 6 THR C 250 O 127.3 167.2 103.6 91.1 90.7 REMARK 620 7 THR C 250 OG1 138.8 90.7 129.2 75.2 80.5 77.5 REMARK 620 8 GLU C 243 OE1 54.9 114.8 84.1 130.8 73.7 73.1 140.2 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 299 OD1 REMARK 620 2 ASP C 305 OD1 116.2 REMARK 620 3 HOH C3201 O 98.1 76.3 REMARK 620 4 ASP C 297 OD1 74.9 130.5 153.0 REMARK 620 5 ASP C 301 OD1 80.1 153.3 80.7 72.4 REMARK 620 6 ARG C 303 O 154.7 81.1 104.1 79.9 91.7 REMARK 620 7 ASP C 305 OD2 83.3 53.6 122.8 82.9 153.0 94.4 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2006 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 369 OD1 REMARK 620 2 ASP C 373 OD1 144.6 REMARK 620 3 ASP C 367 OD1 81.4 114.5 REMARK 620 4 ASP C 373 OD2 162.6 52.9 88.8 REMARK 620 5 HOH C3236 O 72.5 73.9 98.0 123.4 REMARK 620 6 TYR C 371 O 92.2 81.9 159.4 92.0 98.7 REMARK 620 7 ASP C 365 OD1 74.7 136.2 82.3 89.8 146.8 77.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2007 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 434 OD1 REMARK 620 2 HOH C3274 O 73.1 REMARK 620 3 ASP C 426 OD1 136.3 147.4 REMARK 620 4 ASN C 430 OD1 134.7 79.3 83.0 REMARK 620 5 TYR C 432 O 86.1 129.2 75.3 84.3 REMARK 620 6 ASP C 428 OD1 115.7 76.4 76.7 91.0 152.0 REMARK 620 7 ASP C 434 OD2 54.1 104.9 89.6 171.2 98.4 82.6 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1455 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1454 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1456 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1455 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1456 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J1498 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1457 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1457 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1458 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG B3320 THROUGH MAN B3325 BOUND TO ASN B 320 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE REMARK 800 NAG C2015 BOUND TO ASN C 15 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG D3320 THROUGH MAN D3323 BOUND TO ASN D 320 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-SACCHARIDE REMARK 800 NAG B3371 AND NAG B3372 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ZDX RELATED DB: PDB REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE REMARK 900 COMPLEX REMARK 900 RELATED ID: 3ZDY RELATED DB: PDB REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE REMARK 900 COMPLEX REMARK 900 RELATED ID: 3ZDZ RELATED DB: PDB REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE REMARK 900 COMPLEX REMARK 900 RELATED ID: 3ZE0 RELATED DB: PDB REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE REMARK 900 COMPLEX REMARK 900 RELATED ID: 3ZE1 RELATED DB: PDB REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE REMARK 900 COMPLEX