HEADER BLOOD CLOTTING/INHIBITOR 10-MAR-22 7U9F TITLE INTEGRIN ALAPHIIBBETA3 COMPLEX WITH BMS COMPOUND 4 IN MN2+ COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GPALPHA IIB,GPIIB,PLATELET MEMBRANE GLYCOPROTEIN IIB; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: INTEGRIN BETA-3; COMPND 8 CHAIN: B, D; COMPND 9 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB HEAVY CHAIN; COMPND 13 CHAIN: E, H; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: FAB LIGHT CHAIN; COMPND 16 CHAIN: F, L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ITGA2B, GP2B, ITGAB; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: ITGB3, GP3A; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_COMMON: MOUSE; SOURCE 22 ORGANISM_TAXID: 10090 KEYWDS COMPLEX, INHIBITOR, BLOOD CLOTTING, BLOOD CLOTTING-INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR F.-Y.LIN,J.ZHU,J.ZHU,T.A.SPRINGER REVDAT 1 17-AUG-22 7U9F 0 JRNL AUTH J.ZHU,F.-Y.LIN,J.ZHU,T.A.SPRINGER JRNL TITL INTEGRIN ALPHA IIB BETA 3 HEADPIECE WITH FAB COMPLEX WITH JRNL TITL 2 BMS COMPOUND 4 IN MN2+. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.336 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 107262 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.863 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 46.0863 - 6.5017 0.98 7820 149 0.1854 0.2182 REMARK 3 2 6.5017 - 5.1628 0.99 7695 145 0.1966 0.1895 REMARK 3 3 5.1628 - 4.5109 0.99 7629 146 0.1744 0.2218 REMARK 3 4 4.5109 - 4.0987 0.99 7600 144 0.1836 0.1870 REMARK 3 5 4.0987 - 3.8051 0.99 7546 143 0.1998 0.2205 REMARK 3 6 3.8051 - 3.5808 1.00 7592 144 0.2108 0.2193 REMARK 3 7 3.5808 - 3.4016 1.00 7557 143 0.2204 0.2495 REMARK 3 8 3.4016 - 3.2535 1.00 7566 144 0.2424 0.2542 REMARK 3 9 3.2535 - 3.1283 1.00 7522 143 0.2575 0.2710 REMARK 3 10 3.1283 - 3.0204 1.00 7510 143 0.2801 0.3128 REMARK 3 11 3.0204 - 2.9260 1.00 7499 142 0.2984 0.3270 REMARK 3 12 2.9260 - 2.8423 0.99 7514 143 0.3090 0.3188 REMARK 3 13 2.8423 - 2.7675 0.97 7315 136 0.3202 0.3470 REMARK 3 14 2.7675 - 2.7000 0.92 6899 133 0.3389 0.3642 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.372 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.702 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 56.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.48 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 : 0.006 21731 REMARK 3 ANGLE : 0.532 29510 REMARK 3 CHIRALITY : 0.042 3280 REMARK 3 PLANARITY : 0.004 3818 REMARK 3 DIHEDRAL : 11.803 12957 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 43 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.9943 90.1432 38.9127 REMARK 3 T TENSOR REMARK 3 T11: 0.4522 T22: 0.3230 REMARK 3 T33: 0.4596 T12: 0.0489 REMARK 3 T13: 0.0855 T23: 0.0639 REMARK 3 L TENSOR REMARK 3 L11: 2.7571 L22: 1.6045 REMARK 3 L33: 1.5156 L12: -0.0920 REMARK 3 L13: 0.0481 L23: -0.0872 REMARK 3 S TENSOR REMARK 3 S11: 0.1484 S12: 0.2156 S13: 0.0460 REMARK 3 S21: -0.3815 S22: -0.1245 S23: 0.3414 REMARK 3 S31: -0.1247 S32: -0.3028 S33: -0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 304 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.6039 92.9075 62.0997 REMARK 3 T TENSOR REMARK 3 T11: 0.5085 T22: 0.2516 REMARK 3 T33: 0.4998 T12: -0.0372 REMARK 3 T13: 0.1607 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 1.2781 L22: 1.4654 REMARK 3 L33: 1.0894 L12: -0.0754 REMARK 3 L13: -0.3154 L23: 0.1926 REMARK 3 S TENSOR REMARK 3 S11: 0.1079 S12: -0.1203 S13: 0.0517 REMARK 3 S21: 0.3433 S22: -0.1576 S23: 0.3014 REMARK 3 S31: 0.1209 S32: -0.2432 S33: -0.0037 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 305 THROUGH 454 ) REMARK 3 ORIGIN FOR THE GROUP (A): 64.5387 83.4631 47.7747 REMARK 3 T TENSOR REMARK 3 T11: 0.4009 T22: 0.2028 REMARK 3 T33: 0.3915 T12: 0.0887 REMARK 3 T13: 0.0943 T23: 0.0447 REMARK 3 L TENSOR REMARK 3 L11: 1.5118 L22: 2.7069 REMARK 3 L33: 2.4858 L12: 0.4693 REMARK 3 L13: 0.1012 L23: 0.3977 REMARK 3 S TENSOR REMARK 3 S11: 0.0343 S12: 0.0014 S13: -0.1322 REMARK 3 S21: 0.1599 S22: -0.0020 S23: -0.1733 REMARK 3 S31: 0.2505 S32: 0.1587 S33: 0.0044 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 47 ) REMARK 3 ORIGIN FOR THE GROUP (A): 122.9364 86.0104 34.7866 REMARK 3 T TENSOR REMARK 3 T11: 0.9752 T22: 2.3407 REMARK 3 T33: 1.4643 T12: 0.6693 REMARK 3 T13: 0.1160 T23: -0.2574 REMARK 3 L TENSOR REMARK 3 L11: 0.0296 L22: 0.2933 REMARK 3 L33: 0.0634 L12: -0.0771 REMARK 3 L13: -0.0491 L23: 0.1197 REMARK 3 S TENSOR REMARK 3 S11: -0.3756 S12: 0.7367 S13: -0.7607 REMARK 3 S21: 0.3614 S22: 0.1983 S23: -0.8509 REMARK 3 S31: 0.4423 S32: 1.6711 S33: 0.0207 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 107.0885 110.2272 49.2892 REMARK 3 T TENSOR REMARK 3 T11: 0.6577 T22: 1.3533 REMARK 3 T33: 1.0755 T12: -0.0236 REMARK 3 T13: 0.0108 T23: -0.0748 REMARK 3 L TENSOR REMARK 3 L11: 1.0616 L22: 0.5744 REMARK 3 L33: 0.9833 L12: 0.3858 REMARK 3 L13: 0.4063 L23: -0.3248 REMARK 3 S TENSOR REMARK 3 S11: 0.1088 S12: 0.1845 S13: 0.4415 REMARK 3 S21: 0.0148 S22: 0.3398 S23: -0.5935 REMARK 3 S31: -0.1525 S32: 1.3350 S33: 0.0003 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 339 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.0577 117.4056 63.6368 REMARK 3 T TENSOR REMARK 3 T11: 0.5157 T22: 0.1838 REMARK 3 T33: 0.4418 T12: -0.0059 REMARK 3 T13: 0.0905 T23: 0.0167 REMARK 3 L TENSOR REMARK 3 L11: 1.5286 L22: 2.6266 REMARK 3 L33: 1.4096 L12: 0.7428 REMARK 3 L13: 0.0876 L23: 0.6716 REMARK 3 S TENSOR REMARK 3 S11: 0.1293 S12: -0.0986 S13: 0.2153 REMARK 3 S21: 0.2491 S22: -0.0938 S23: -0.0058 REMARK 3 S31: -0.2340 S32: 0.1169 S33: -0.0037 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 340 THROUGH 403 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.0949 106.4077 62.1288 REMARK 3 T TENSOR REMARK 3 T11: 0.7239 T22: 0.9210 REMARK 3 T33: 0.9257 T12: 0.1155 REMARK 3 T13: -0.1095 T23: -0.0853 REMARK 3 L TENSOR REMARK 3 L11: 0.7745 L22: 0.4804 REMARK 3 L33: 0.8396 L12: -0.4020 REMARK 3 L13: -0.7855 L23: -0.0883 REMARK 3 S TENSOR REMARK 3 S11: -0.1120 S12: 0.0260 S13: -0.2989 REMARK 3 S21: 0.2247 S22: 0.0287 S23: -0.1891 REMARK 3 S31: 0.6491 S32: 0.9076 S33: -0.0062 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 404 THROUGH 431 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.0391 103.9340 44.3812 REMARK 3 T TENSOR REMARK 3 T11: 0.6216 T22: 1.0240 REMARK 3 T33: 0.9934 T12: 0.1218 REMARK 3 T13: -0.0569 T23: -0.0852 REMARK 3 L TENSOR REMARK 3 L11: 0.2838 L22: 0.1440 REMARK 3 L33: 0.4356 L12: -0.0630 REMARK 3 L13: 0.2238 L23: -0.2495 REMARK 3 S TENSOR REMARK 3 S11: 0.3223 S12: 0.3475 S13: -0.0959 REMARK 3 S21: -0.3877 S22: -0.4560 S23: -0.1471 REMARK 3 S31: -0.0914 S32: 0.2894 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 432 THROUGH 466 ) REMARK 3 ORIGIN FOR THE GROUP (A): 115.5995 88.7682 19.3744 REMARK 3 T TENSOR REMARK 3 T11: 1.0482 T22: 2.2935 REMARK 3 T33: 1.2157 T12: 0.2763 REMARK 3 T13: 0.2249 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 0.1029 L22: 0.0631 REMARK 3 L33: 0.0594 L12: -0.0343 REMARK 3 L13: 0.0273 L23: -0.0191 REMARK 3 S TENSOR REMARK 3 S11: -0.0530 S12: 0.0841 S13: 0.3118 REMARK 3 S21: -0.2100 S22: 0.4377 S23: -0.6042 REMARK 3 S31: 0.0545 S32: 0.2687 S33: 0.0002 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 87.4296 94.0472 132.0078 REMARK 3 T TENSOR REMARK 3 T11: 0.4421 T22: 0.7000 REMARK 3 T33: 0.5095 T12: 0.0411 REMARK 3 T13: 0.0453 T23: 0.0643 REMARK 3 L TENSOR REMARK 3 L11: 2.2426 L22: 1.4574 REMARK 3 L33: 1.4152 L12: 0.0502 REMARK 3 L13: -0.4775 L23: 0.7169 REMARK 3 S TENSOR REMARK 3 S11: -0.2414 S12: -0.2171 S13: 0.0920 REMARK 3 S21: -0.1086 S22: -0.0392 S23: -0.2668 REMARK 3 S31: 0.2546 S32: 0.7477 S33: -0.0001 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 62 THROUGH 281 ) REMARK 3 ORIGIN FOR THE GROUP (A): 91.4134 89.3758 108.2887 REMARK 3 T TENSOR REMARK 3 T11: 0.6477 T22: 0.9272 REMARK 3 T33: 0.5541 T12: -0.0709 REMARK 3 T13: 0.2022 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 3.0193 L22: 0.9213 REMARK 3 L33: 1.5933 L12: 0.4051 REMARK 3 L13: -0.3330 L23: -0.9690 REMARK 3 S TENSOR REMARK 3 S11: -0.4331 S12: 0.8723 S13: -0.1320 REMARK 3 S21: -0.3567 S22: 0.1151 S23: -0.2930 REMARK 3 S31: 0.3999 S32: 0.5731 S33: 0.0140 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 282 THROUGH 453 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.5177 79.3035 126.0491 REMARK 3 T TENSOR REMARK 3 T11: 0.6377 T22: 0.4158 REMARK 3 T33: 0.5176 T12: -0.0050 REMARK 3 T13: 0.2525 T23: -0.0128 REMARK 3 L TENSOR REMARK 3 L11: 3.3218 L22: 2.3385 REMARK 3 L33: 3.1037 L12: 0.0831 REMARK 3 L13: 0.4443 L23: 0.0429 REMARK 3 S TENSOR REMARK 3 S11: -0.4103 S12: 0.1848 S13: -0.5427 REMARK 3 S21: -0.1578 S22: 0.1740 S23: -0.1404 REMARK 3 S31: 0.6971 S32: 0.1554 S33: -0.0220 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.1659 81.6966 128.2129 REMARK 3 T TENSOR REMARK 3 T11: 0.8470 T22: 1.3848 REMARK 3 T33: 0.8751 T12: -0.4250 REMARK 3 T13: 0.0148 T23: 0.1073 REMARK 3 L TENSOR REMARK 3 L11: 1.3970 L22: 0.3669 REMARK 3 L33: 1.4263 L12: -0.1500 REMARK 3 L13: -0.2936 L23: 0.6582 REMARK 3 S TENSOR REMARK 3 S11: -0.3855 S12: 0.5932 S13: 0.0111 REMARK 3 S21: -0.0313 S22: 0.2928 S23: 0.3500 REMARK 3 S31: 0.5970 S32: -1.3281 S33: -0.0024 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 112 THROUGH 339 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.6036 102.9831 100.4177 REMARK 3 T TENSOR REMARK 3 T11: 0.6283 T22: 0.9513 REMARK 3 T33: 0.5410 T12: -0.2861 REMARK 3 T13: -0.0493 T23: 0.2633 REMARK 3 L TENSOR REMARK 3 L11: 2.5109 L22: 1.0747 REMARK 3 L33: 2.5771 L12: -0.3828 REMARK 3 L13: 0.8849 L23: -0.5845 REMARK 3 S TENSOR REMARK 3 S11: -0.2590 S12: 0.9146 S13: 0.5361 REMARK 3 S21: -0.3029 S22: 0.1554 S23: 0.0796 REMARK 3 S31: -0.1514 S32: -0.2222 S33: -0.0702 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 340 THROUGH 403 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.0410 85.7426 107.6148 REMARK 3 T TENSOR REMARK 3 T11: 1.0082 T22: 1.5271 REMARK 3 T33: 0.7019 T12: -0.5963 REMARK 3 T13: -0.0033 T23: 0.0940 REMARK 3 L TENSOR REMARK 3 L11: 0.3096 L22: 0.0408 REMARK 3 L33: 0.8251 L12: -0.1099 REMARK 3 L13: -0.6651 L23: 0.2641 REMARK 3 S TENSOR REMARK 3 S11: -0.6407 S12: 0.9167 S13: -0.3787 REMARK 3 S21: -0.1664 S22: 0.3484 S23: 0.0298 REMARK 3 S31: 1.0125 S32: -0.4441 S33: -0.0254 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 404 THROUGH 432 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.4648 88.8912 125.5194 REMARK 3 T TENSOR REMARK 3 T11: 0.7987 T22: 0.9834 REMARK 3 T33: 0.7020 T12: -0.1915 REMARK 3 T13: -0.0275 T23: 0.1327 REMARK 3 L TENSOR REMARK 3 L11: 0.5853 L22: 0.4309 REMARK 3 L33: 0.3267 L12: -0.2828 REMARK 3 L13: -0.1753 L23: 0.3270 REMARK 3 S TENSOR REMARK 3 S11: -0.3171 S12: 0.1481 S13: -0.0632 REMARK 3 S21: 0.1135 S22: 0.0414 S23: 0.0840 REMARK 3 S31: -0.2514 S32: 0.0235 S33: 0.0000 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 433 THROUGH 471 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.8867 78.5634 155.2615 REMARK 3 T TENSOR REMARK 3 T11: 1.1946 T22: 1.1600 REMARK 3 T33: 1.0600 T12: -0.2808 REMARK 3 T13: 0.2074 T23: -0.1181 REMARK 3 L TENSOR REMARK 3 L11: 0.3474 L22: 0.3257 REMARK 3 L33: 0.1445 L12: 0.3138 REMARK 3 L13: 0.0842 L23: 0.1667 REMARK 3 S TENSOR REMARK 3 S11: -0.4648 S12: -0.1249 S13: -0.0325 REMARK 3 S21: 0.4091 S22: -0.0247 S23: 0.1306 REMARK 3 S31: 0.0645 S32: -1.2361 S33: 0.0001 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 115.9929 89.1028 85.0697 REMARK 3 T TENSOR REMARK 3 T11: 1.0189 T22: 1.8635 REMARK 3 T33: 0.8275 T12: -0.1069 REMARK 3 T13: 0.2203 T23: 0.0728 REMARK 3 L TENSOR REMARK 3 L11: 1.0826 L22: 0.8616 REMARK 3 L33: 0.5054 L12: -0.6306 REMARK 3 L13: 0.1092 L23: 0.4490 REMARK 3 S TENSOR REMARK 3 S11: 0.1853 S12: 0.8252 S13: -0.0137 REMARK 3 S21: -0.3970 S22: -0.2392 S23: -0.0843 REMARK 3 S31: 0.5943 S32: -0.0523 S33: 0.0002 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 128 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): 157.5859 86.0935 78.9964 REMARK 3 T TENSOR REMARK 3 T11: 2.2000 T22: 3.1923 REMARK 3 T33: 1.5510 T12: 1.0196 REMARK 3 T13: -0.0618 T23: -0.2044 REMARK 3 L TENSOR REMARK 3 L11: 0.0037 L22: 0.0148 REMARK 3 L33: 0.0443 L12: 0.0080 REMARK 3 L13: 0.0268 L23: 0.0018 REMARK 3 S TENSOR REMARK 3 S11: 0.2234 S12: 0.5470 S13: 0.0920 REMARK 3 S21: 0.2781 S22: 0.3060 S23: -1.1116 REMARK 3 S31: -0.0419 S32: -0.2818 S33: 0.0003 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 150 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): 144.2072 78.2874 80.9780 REMARK 3 T TENSOR REMARK 3 T11: 1.8043 T22: 2.1180 REMARK 3 T33: 1.3915 T12: 0.3853 REMARK 3 T13: 0.0739 T23: 0.1889 REMARK 3 L TENSOR REMARK 3 L11: -0.0007 L22: 0.0265 REMARK 3 L33: 0.0113 L12: -0.0033 REMARK 3 L13: 0.0015 L23: 0.0256 REMARK 3 S TENSOR REMARK 3 S11: 0.1053 S12: 0.1903 S13: -0.4229 REMARK 3 S21: 0.0158 S22: -0.3483 S23: -0.7011 REMARK 3 S31: -0.1149 S32: 0.0177 S33: -0.0005 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 166 THROUGH 185 ) REMARK 3 ORIGIN FOR THE GROUP (A): 143.5840 87.4945 80.3584 REMARK 3 T TENSOR REMARK 3 T11: 1.2403 T22: 2.6747 REMARK 3 T33: 1.4366 T12: 0.3639 REMARK 3 T13: 0.1155 T23: 0.2809 REMARK 3 L TENSOR REMARK 3 L11: 0.0416 L22: 0.0442 REMARK 3 L33: 0.0046 L12: 0.0432 REMARK 3 L13: -0.0085 L23: -0.0071 REMARK 3 S TENSOR REMARK 3 S11: 0.6448 S12: 0.0866 S13: -0.1492 REMARK 3 S21: -0.3940 S22: -0.0236 S23: 0.3051 REMARK 3 S31: -0.2096 S32: -0.1448 S33: -0.0002 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 186 THROUGH 199 ) REMARK 3 ORIGIN FOR THE GROUP (A): 162.9831 79.6408 86.5750 REMARK 3 T TENSOR REMARK 3 T11: 1.8136 T22: 2.6035 REMARK 3 T33: 1.2888 T12: 1.5051 REMARK 3 T13: -0.1756 T23: 0.1371 REMARK 3 L TENSOR REMARK 3 L11: 0.2562 L22: 0.1920 REMARK 3 L33: 0.2005 L12: -0.0880 REMARK 3 L13: 0.0585 L23: -0.1140 REMARK 3 S TENSOR REMARK 3 S11: 0.4512 S12: 0.0483 S13: -0.1701 REMARK 3 S21: 0.0905 S22: 0.2618 S23: 0.1005 REMARK 3 S31: 0.3407 S32: -0.0875 S33: 0.0700 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 200 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 150.5552 76.2118 75.7136 REMARK 3 T TENSOR REMARK 3 T11: 1.6646 T22: 2.4148 REMARK 3 T33: 1.5732 T12: 0.9392 REMARK 3 T13: -0.4540 T23: -0.5417 REMARK 3 L TENSOR REMARK 3 L11: -0.0013 L22: 0.0226 REMARK 3 L33: 0.0160 L12: 0.0288 REMARK 3 L13: -0.0071 L23: -0.0236 REMARK 3 S TENSOR REMARK 3 S11: 0.0927 S12: -0.0318 S13: 0.1822 REMARK 3 S21: -0.1223 S22: 0.0786 S23: -0.7996 REMARK 3 S31: 0.0601 S32: 0.1717 S33: -0.0002 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 126.3900 99.4628 101.8424 REMARK 3 T TENSOR REMARK 3 T11: 0.6243 T22: 1.7866 REMARK 3 T33: 1.0167 T12: -0.1125 REMARK 3 T13: 0.1149 T23: 0.1436 REMARK 3 L TENSOR REMARK 3 L11: 0.4788 L22: 0.2746 REMARK 3 L33: 0.6624 L12: -0.1075 REMARK 3 L13: 0.2458 L23: 0.0350 REMARK 3 S TENSOR REMARK 3 S11: -0.1244 S12: 0.2787 S13: 0.4780 REMARK 3 S21: 0.0795 S22: -0.0544 S23: -0.3876 REMARK 3 S31: 0.0303 S32: 0.8205 S33: -0.0047 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 114 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 156.5951 88.9627 72.4857 REMARK 3 T TENSOR REMARK 3 T11: 1.7067 T22: 3.4636 REMARK 3 T33: 1.2299 T12: 0.9320 REMARK 3 T13: 0.6330 T23: 0.1931 REMARK 3 L TENSOR REMARK 3 L11: 0.1043 L22: 0.4482 REMARK 3 L33: 0.3536 L12: 0.0803 REMARK 3 L13: 0.1291 L23: -0.1745 REMARK 3 S TENSOR REMARK 3 S11: 0.1016 S12: 0.3068 S13: -0.0979 REMARK 3 S21: -0.6572 S22: 0.0178 S23: 0.0202 REMARK 3 S31: 0.1662 S32: -0.0259 S33: 0.1608 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 130 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): 150.9610 96.3442 87.1209 REMARK 3 T TENSOR REMARK 3 T11: 1.0899 T22: 2.8481 REMARK 3 T33: 1.2448 T12: 0.2025 REMARK 3 T13: 0.2334 T23: 0.3485 REMARK 3 L TENSOR REMARK 3 L11: 0.0447 L22: 0.0404 REMARK 3 L33: 0.0138 L12: -0.0140 REMARK 3 L13: 0.0122 L23: -0.0225 REMARK 3 S TENSOR REMARK 3 S11: 0.1951 S12: 0.6898 S13: -0.0536 REMARK 3 S21: -0.5070 S22: -0.4656 S23: -0.4295 REMARK 3 S31: 0.0514 S32: 0.5682 S33: -0.0003 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 145 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 151.9136 98.6405 77.9749 REMARK 3 T TENSOR REMARK 3 T11: 1.2528 T22: 2.4426 REMARK 3 T33: 1.4382 T12: 0.0811 REMARK 3 T13: 0.4462 T23: 0.4740 REMARK 3 L TENSOR REMARK 3 L11: -0.0120 L22: 0.0739 REMARK 3 L33: 0.1192 L12: 0.0091 REMARK 3 L13: 0.0556 L23: 0.1191 REMARK 3 S TENSOR REMARK 3 S11: 0.0966 S12: 0.5220 S13: 0.0106 REMARK 3 S21: -0.5350 S22: -0.1534 S23: -0.3974 REMARK 3 S31: -0.2634 S32: 0.3184 S33: 0.0000 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 198 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 161.4768 100.2686 81.3356 REMARK 3 T TENSOR REMARK 3 T11: 0.9863 T22: 2.4417 REMARK 3 T33: 1.6783 T12: 0.0542 REMARK 3 T13: 0.3091 T23: 0.1332 REMARK 3 L TENSOR REMARK 3 L11: -0.0209 L22: -0.0268 REMARK 3 L33: -0.0033 L12: -0.0371 REMARK 3 L13: -0.0039 L23: 0.0191 REMARK 3 S TENSOR REMARK 3 S11: 0.0534 S12: 0.8088 S13: -0.0013 REMARK 3 S21: -0.3110 S22: -0.1100 S23: -0.2548 REMARK 3 S31: 0.3623 S32: 0.4627 S33: 0.0002 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2037 89.6401 89.4491 REMARK 3 T TENSOR REMARK 3 T11: 1.1270 T22: 1.0636 REMARK 3 T33: 0.8649 T12: 0.0222 REMARK 3 T13: 0.3662 T23: 0.0839 REMARK 3 L TENSOR REMARK 3 L11: 0.3649 L22: 0.1333 REMARK 3 L33: 0.1845 L12: 0.0490 REMARK 3 L13: 0.1194 L23: -0.1413 REMARK 3 S TENSOR REMARK 3 S11: -0.3030 S12: -0.6447 S13: -0.2705 REMARK 3 S21: 0.7259 S22: 0.5341 S23: 0.0608 REMARK 3 S31: 0.0615 S32: -0.1961 S33: -0.0001 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 125 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0893 96.1857 83.6980 REMARK 3 T TENSOR REMARK 3 T11: 0.6819 T22: 0.8036 REMARK 3 T33: 0.7559 T12: 0.0552 REMARK 3 T13: 0.1766 T23: -0.0555 REMARK 3 L TENSOR REMARK 3 L11: 1.0317 L22: 1.4362 REMARK 3 L33: 1.3082 L12: 0.1852 REMARK 3 L13: 0.0249 L23: -0.8080 REMARK 3 S TENSOR REMARK 3 S11: -0.1158 S12: -0.4862 S13: -0.0772 REMARK 3 S21: 0.6466 S22: 0.1523 S23: 0.0207 REMARK 3 S31: 0.2417 S32: -0.0687 S33: 0.0000 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 126 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.3001 82.7521 93.2979 REMARK 3 T TENSOR REMARK 3 T11: 0.7751 T22: 1.1400 REMARK 3 T33: 2.0822 T12: 0.0391 REMARK 3 T13: 0.1925 T23: 0.4115 REMARK 3 L TENSOR REMARK 3 L11: 0.0793 L22: 0.1349 REMARK 3 L33: 0.1297 L12: -0.0688 REMARK 3 L13: -0.1005 L23: 0.0595 REMARK 3 S TENSOR REMARK 3 S11: -0.0921 S12: -0.2735 S13: -0.7262 REMARK 3 S21: -0.0399 S22: -0.4100 S23: 0.9691 REMARK 3 S31: 0.8817 S32: 0.2815 S33: -0.0054 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 152 THROUGH 168 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.3521 77.3995 91.4902 REMARK 3 T TENSOR REMARK 3 T11: 0.7823 T22: 1.0619 REMARK 3 T33: 2.3925 T12: 0.2313 REMARK 3 T13: 0.2813 T23: 0.1209 REMARK 3 L TENSOR REMARK 3 L11: 0.1630 L22: 0.7649 REMARK 3 L33: 1.5083 L12: 0.3488 REMARK 3 L13: -0.2222 L23: -0.5964 REMARK 3 S TENSOR REMARK 3 S11: -0.5627 S12: -0.4436 S13: -1.1755 REMARK 3 S21: -0.1609 S22: 0.0031 S23: 0.5925 REMARK 3 S31: 0.9701 S32: 0.0982 S33: -0.0848 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 169 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.7335 89.6587 90.2315 REMARK 3 T TENSOR REMARK 3 T11: 0.6689 T22: 1.1289 REMARK 3 T33: 1.4977 T12: 0.1244 REMARK 3 T13: 0.1142 T23: 0.0495 REMARK 3 L TENSOR REMARK 3 L11: 0.0394 L22: 0.1243 REMARK 3 L33: 0.2238 L12: -0.0438 REMARK 3 L13: 0.1054 L23: -0.0549 REMARK 3 S TENSOR REMARK 3 S11: -0.6488 S12: -0.4015 S13: -0.7608 REMARK 3 S21: 0.4995 S22: 0.3547 S23: 0.4796 REMARK 3 S31: -0.1763 S32: -0.3786 S33: -0.0009 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 180 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.8455 83.4618 90.0351 REMARK 3 T TENSOR REMARK 3 T11: 0.3006 T22: 1.2051 REMARK 3 T33: 2.0814 T12: -0.2442 REMARK 3 T13: 0.5421 T23: 0.4725 REMARK 3 L TENSOR REMARK 3 L11: 0.1708 L22: 0.1914 REMARK 3 L33: 0.3254 L12: -0.1000 REMARK 3 L13: 0.1886 L23: -0.2169 REMARK 3 S TENSOR REMARK 3 S11: -0.4260 S12: 0.2471 S13: -1.1307 REMARK 3 S21: -0.0737 S22: 0.2791 S23: 0.7229 REMARK 3 S31: 0.6411 S32: -0.3163 S33: -0.1899 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 191 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.1879 73.0413 93.0869 REMARK 3 T TENSOR REMARK 3 T11: 1.1109 T22: 1.2372 REMARK 3 T33: 2.5306 T12: -0.0617 REMARK 3 T13: 0.2389 T23: 0.3094 REMARK 3 L TENSOR REMARK 3 L11: 0.0159 L22: 0.0074 REMARK 3 L33: 0.0500 L12: 0.0055 REMARK 3 L13: -0.0226 L23: 0.0072 REMARK 3 S TENSOR REMARK 3 S11: -0.3223 S12: -0.0416 S13: -0.4808 REMARK 3 S21: 0.3084 S22: -0.0130 S23: 0.6139 REMARK 3 S31: 0.7725 S32: 0.2138 S33: 0.0002 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 206 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.7522 77.4481 100.2487 REMARK 3 T TENSOR REMARK 3 T11: 0.7839 T22: 1.0675 REMARK 3 T33: 1.7899 T12: -0.0096 REMARK 3 T13: 0.1462 T23: 0.6538 REMARK 3 L TENSOR REMARK 3 L11: 0.0075 L22: 0.0209 REMARK 3 L33: -0.0116 L12: -0.0155 REMARK 3 L13: 0.0000 L23: 0.0265 REMARK 3 S TENSOR REMARK 3 S11: 0.1867 S12: -0.1178 S13: 0.1829 REMARK 3 S21: 0.0575 S22: -0.1635 S23: -0.4296 REMARK 3 S31: 0.6708 S32: 0.2028 S33: 0.0001 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1878 95.7243 63.8683 REMARK 3 T TENSOR REMARK 3 T11: 0.4901 T22: 0.8941 REMARK 3 T33: 0.9678 T12: 0.0331 REMARK 3 T13: 0.0879 T23: -0.1910 REMARK 3 L TENSOR REMARK 3 L11: 1.1754 L22: 0.5134 REMARK 3 L33: 0.5679 L12: -0.0855 REMARK 3 L13: 0.1851 L23: 0.5396 REMARK 3 S TENSOR REMARK 3 S11: 0.0371 S12: 0.3210 S13: -0.1067 REMARK 3 S21: -0.1951 S22: -0.3205 S23: 0.6219 REMARK 3 S31: -0.1405 S32: -0.8162 S33: -0.0024 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.0451 95.4945 68.4127 REMARK 3 T TENSOR REMARK 3 T11: 0.4072 T22: 0.8427 REMARK 3 T33: 1.0126 T12: -0.0030 REMARK 3 T13: 0.1656 T23: -0.1569 REMARK 3 L TENSOR REMARK 3 L11: 0.2717 L22: 0.2666 REMARK 3 L33: 0.5252 L12: -0.0659 REMARK 3 L13: -0.2040 L23: 0.0151 REMARK 3 S TENSOR REMARK 3 S11: -0.1754 S12: 0.0744 S13: -0.5189 REMARK 3 S21: -0.6907 S22: -0.1643 S23: 0.4547 REMARK 3 S31: -0.1581 S32: -0.7642 S33: -0.0087 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.8491 88.2179 68.2935 REMARK 3 T TENSOR REMARK 3 T11: -0.3080 T22: 1.8134 REMARK 3 T33: 1.7853 T12: -0.2830 REMARK 3 T13: 0.2260 T23: -0.9082 REMARK 3 L TENSOR REMARK 3 L11: 0.0288 L22: 0.0718 REMARK 3 L33: 0.0551 L12: 0.0478 REMARK 3 L13: -0.0511 L23: -0.0529 REMARK 3 S TENSOR REMARK 3 S11: -0.0755 S12: 0.0914 S13: -0.0585 REMARK 3 S21: -0.1665 S22: 0.1099 S23: 0.2790 REMARK 3 S31: 0.1241 S32: -0.4717 S33: -0.0397 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.8360 87.5043 97.0774 REMARK 3 T TENSOR REMARK 3 T11: 0.7738 T22: 1.1228 REMARK 3 T33: 1.8701 T12: 0.0741 REMARK 3 T13: 0.4551 T23: 0.4840 REMARK 3 L TENSOR REMARK 3 L11: 0.4572 L22: 1.8022 REMARK 3 L33: 0.7053 L12: -0.6855 REMARK 3 L13: 0.0389 L23: 0.6912 REMARK 3 S TENSOR REMARK 3 S11: -0.3973 S12: -0.7217 S13: -1.2609 REMARK 3 S21: 1.0394 S22: 0.6658 S23: 0.2630 REMARK 3 S31: 0.3434 S32: 0.0510 S33: 0.0489 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 129 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.1992 90.4392 81.4416 REMARK 3 T TENSOR REMARK 3 T11: 0.3571 T22: 1.2292 REMARK 3 T33: 1.7142 T12: 0.0202 REMARK 3 T13: 0.2799 T23: -0.0715 REMARK 3 L TENSOR REMARK 3 L11: 0.1465 L22: 0.8115 REMARK 3 L33: 0.1512 L12: -0.0868 REMARK 3 L13: -0.1137 L23: -0.0286 REMARK 3 S TENSOR REMARK 3 S11: 0.0225 S12: 0.3257 S13: -1.3386 REMARK 3 S21: 0.1789 S22: 0.1102 S23: 0.3321 REMARK 3 S31: 0.2243 S32: 0.1945 S33: 0.3363 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 145 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.9715 94.9918 88.0071 REMARK 3 T TENSOR REMARK 3 T11: 0.3109 T22: 1.1166 REMARK 3 T33: 1.5200 T12: 0.0711 REMARK 3 T13: 0.3711 T23: 0.2479 REMARK 3 L TENSOR REMARK 3 L11: 0.4001 L22: 1.0440 REMARK 3 L33: 1.7561 L12: -0.0356 REMARK 3 L13: 0.6587 L23: -0.6308 REMARK 3 S TENSOR REMARK 3 S11: -0.4259 S12: -0.5550 S13: -1.2630 REMARK 3 S21: 0.4492 S22: 0.2827 S23: 0.1580 REMARK 3 S31: -0.8370 S32: 0.2096 S33: -0.2364 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 189 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.4591 94.2296 86.0770 REMARK 3 T TENSOR REMARK 3 T11: 0.6081 T22: 1.3558 REMARK 3 T33: 1.5297 T12: -0.0277 REMARK 3 T13: 0.2698 T23: -0.0887 REMARK 3 L TENSOR REMARK 3 L11: 0.1243 L22: 0.4234 REMARK 3 L33: 0.1686 L12: 0.0412 REMARK 3 L13: 0.0782 L23: 0.2535 REMARK 3 S TENSOR REMARK 3 S11: -0.0700 S12: 0.3250 S13: -1.5508 REMARK 3 S21: 0.2500 S22: -0.2995 S23: 0.8347 REMARK 3 S31: 0.1847 S32: -1.2992 S33: -0.0029 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 7U9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-22. REMARK 100 THE DEPOSITION ID IS D_1000262637. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97938 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107262 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.10000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.99500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: 3NIG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11-13% PEG 8000, 0.2 M AMMONIUM REMARK 280 SULFATE, 0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 297K 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 129.69850 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.14600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 129.69850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.14600 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, G, 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, J, K 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 LEU B 467 REMARK 465 GLY B 468 REMARK 465 SER B 469 REMARK 465 GLN B 470 REMARK 465 CYS B 471 REMARK 465 VAL C 454 REMARK 465 THR E 138 REMARK 465 GLY E 139 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 GLU B 174 CG CD OE1 OE2 REMARK 480 LYS D 350 CD CE NZ 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 O HOH A 786 O HOH A 966 2.15 REMARK 500 O HOH D 2116 O HOH D 2151 2.19 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 A 902 O HOH C 761 1554 2.19 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 SER A 101 -131.14 55.83 REMARK 500 LYS A 118 -120.25 60.54 REMARK 500 GLU A 123 132.68 87.35 REMARK 500 LEU A 212 -39.64 68.65 REMARK 500 PRO A 412 -177.81 -69.30 REMARK 500 ALA B 30 72.30 -69.88 REMARK 500 PHE B 56 83.55 -152.05 REMARK 500 ASP B 76 154.91 64.30 REMARK 500 SER B 77 48.91 -84.72 REMARK 500 GLN B 79 37.75 -87.96 REMARK 500 VAL B 157 -83.56 -132.12 REMARK 500 PRO B 160 76.16 -69.45 REMARK 500 MET B 180 -155.09 -105.66 REMARK 500 SER B 213 -161.73 -119.85 REMARK 500 ASP B 241 79.55 -111.34 REMARK 500 LEU B 258 -6.05 78.85 REMARK 500 LEU B 375 -124.82 59.75 REMARK 500 ASN C 2 -75.54 -88.73 REMARK 500 SER C 101 -137.79 52.44 REMARK 500 ASP C 102 34.17 -93.86 REMARK 500 LYS C 118 -125.49 58.73 REMARK 500 GLU C 123 142.71 81.33 REMARK 500 LEU C 212 -44.55 70.16 REMARK 500 THR C 263 14.15 59.89 REMARK 500 VAL C 325 -30.72 -136.83 REMARK 500 ALA D 30 42.26 -96.77 REMARK 500 PHE D 56 83.64 -150.86 REMARK 500 ASP D 66 53.96 -142.37 REMARK 500 SER D 74 -166.94 -77.33 REMARK 500 ASP D 109 61.25 60.68 REMARK 500 VAL D 157 -79.14 -133.42 REMARK 500 VAL D 193 -64.28 -103.18 REMARK 500 SER D 213 -162.90 -122.48 REMARK 500 ASP D 241 70.55 -108.70 REMARK 500 LEU D 258 -3.86 78.71 REMARK 500 CYS D 374 -112.91 -93.52 REMARK 500 ASN D 376 -135.30 52.89 REMARK 500 ASN D 450 -2.64 65.69 REMARK 500 ASN E 55 -34.50 -153.08 REMARK 500 PRO E 155 -169.11 -108.18 REMARK 500 SER E 192 32.46 -92.43 REMARK 500 PRO E 195 48.45 -90.62 REMARK 500 LYS E 211 58.49 -144.88 REMARK 500 SER F 43 -155.92 -88.42 REMARK 500 SER F 77 86.10 56.85 REMARK 500 ASN F 138 79.10 59.06 REMARK 500 GLU F 187 41.44 -76.70 REMARK 500 ASN F 190 -56.86 -121.43 REMARK 500 ASN F 212 77.54 54.48 REMARK 500 GLU F 213 -66.05 -90.82 REMARK 500 REMARK 500 THIS ENTRY HAS 55 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 CA A 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 243 OE1 REMARK 620 2 GLU A 243 OE2 54.4 REMARK 620 3 ASP A 245 OD1 119.0 64.9 REMARK 620 4 ASP A 247 O 73.3 76.4 88.5 REMARK 620 5 THR A 250 O 75.2 129.5 163.1 87.1 REMARK 620 6 THR A 250 OG1 141.5 139.2 83.9 77.3 79.2 REMARK 620 7 GLU A 252 OE1 96.3 74.8 71.8 150.0 118.0 121.2 REMARK 620 8 GLU A 252 OE2 134.0 128.7 87.9 149.1 87.5 71.8 55.1 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 297 OD1 REMARK 620 2 ASN A 299 OD1 75.4 REMARK 620 3 ASP A 301 OD1 65.2 74.4 REMARK 620 4 ARG A 303 O 75.5 150.8 91.2 REMARK 620 5 ASP A 305 OD1 135.9 109.5 158.8 93.2 REMARK 620 6 ASP A 305 OD2 84.9 82.8 145.9 97.1 53.8 REMARK 620 7 HOH A 635 O 150.5 90.0 86.4 114.7 73.0 119.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 505 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 365 OD1 REMARK 620 2 ASP A 367 OD1 89.0 REMARK 620 3 ASP A 369 OD1 75.7 85.9 REMARK 620 4 TYR A 371 O 74.0 163.0 89.4 REMARK 620 5 ASP A 373 OD1 138.0 109.8 140.4 84.0 REMARK 620 6 ASP A 373 OD2 92.8 86.3 166.2 94.9 53.3 REMARK 620 7 HOH A 644 O 140.6 96.8 66.0 96.1 76.0 126.4 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 506 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 426 OD1 REMARK 620 2 ASP A 428 OD1 73.6 REMARK 620 3 ASN A 430 OD1 82.3 85.0 REMARK 620 4 TYR A 432 O 82.6 155.3 85.3 REMARK 620 5 ASP A 434 OD1 142.0 116.4 133.0 86.5 REMARK 620 6 ASP A 434 OD2 91.1 86.1 170.1 101.2 55.5 REMARK 620 7 HOH A 622 O 139.6 72.1 73.9 126.3 74.3 107.3 REMARK 620 N 1 2 3 4 5 6 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 SER B 121 OG REMARK 620 2 GLU B 220 OE2 98.8 REMARK 620 3 I7R B2005 O2 106.1 93.8 REMARK 620 4 HOH B2115 O 100.4 160.8 82.8 REMARK 620 5 HOH B2138 O 75.3 107.0 158.8 76.2 REMARK 620 6 HOH B2179 O 161.7 83.1 91.9 78.1 86.7 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 SER B 123 O REMARK 620 2 ASP B 126 OD1 83.7 REMARK 620 3 ASP B 126 OD2 138.7 60.5 REMARK 620 4 ASP B 127 OD1 107.9 98.0 97.5 REMARK 620 5 MET B 335 O 147.6 127.2 67.4 80.2 REMARK 620 6 HOH B2156 O 80.7 163.6 135.8 82.3 69.2 REMARK 620 7 HOH B2190 O 80.5 98.2 84.7 162.5 84.8 84.0 REMARK 620 N 1 2 3 4 5 6 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 158 OD2 REMARK 620 2 ASN B 215 OD1 102.0 REMARK 620 3 ASP B 217 O 162.5 88.6 REMARK 620 4 ASP B 217 OD1 92.5 89.2 73.6 REMARK 620 5 PRO B 219 O 84.1 163.8 89.5 105.7 REMARK 620 6 GLU B 220 OE1 97.8 80.1 97.7 166.5 84.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 505 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 243 OE1 REMARK 620 2 GLU C 243 OE2 54.4 REMARK 620 3 ASP C 245 OD1 120.8 66.5 REMARK 620 4 ASP C 247 O 82.3 74.1 85.4 REMARK 620 5 THR C 250 O 74.8 126.3 159.5 83.9 REMARK 620 6 THR C 250 OG1 146.9 135.0 80.3 73.8 80.0 REMARK 620 7 GLU C 252 OE1 90.9 80.4 75.5 152.6 120.0 120.6 REMARK 620 8 GLU C 252 OE2 139.8 124.8 72.8 138.0 104.4 67.4 53.9 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 506 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 297 OD1 REMARK 620 2 ASN C 299 OD1 76.4 REMARK 620 3 ASP C 301 OD1 69.5 68.6 REMARK 620 4 ARG C 303 O 85.3 160.0 97.5 REMARK 620 5 ASP C 305 OD1 142.7 120.0 146.0 79.7 REMARK 620 6 ASP C 305 OD2 95.6 87.8 154.2 102.3 55.5 REMARK 620 7 HOH C 620 O 152.9 85.3 85.4 108.7 64.1 103.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 507 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 365 OD1 REMARK 620 2 ASP C 367 OD1 85.1 REMARK 620 3 ASP C 369 OD1 73.8 74.1 REMARK 620 4 TYR C 371 O 74.6 157.4 90.6 REMARK 620 5 ASP C 373 OD1 137.3 124.3 138.9 78.1 REMARK 620 6 ASP C 373 OD2 98.4 96.0 167.6 96.6 53.0 REMARK 620 7 HOH C 626 O 139.8 96.8 68.4 92.5 72.7 121.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 508 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 426 OD1 REMARK 620 2 ASP C 428 OD1 73.6 REMARK 620 3 ASN C 430 OD1 84.6 86.3 REMARK 620 4 TYR C 432 O 83.8 157.4 90.4 REMARK 620 5 ASP C 434 OD1 142.3 112.2 131.9 86.4 REMARK 620 6 ASP C 434 OD2 92.3 78.0 164.3 104.6 55.3 REMARK 620 7 HOH C 602 O 128.4 57.6 77.0 143.0 77.3 93.1 REMARK 620 N 1 2 3 4 5 6 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 SER D 121 OG REMARK 620 2 GLU D 220 OE2 91.3 REMARK 620 3 I7R D2006 O2 104.4 103.3 REMARK 620 4 HOH D2116 O 108.4 148.0 96.0 REMARK 620 5 HOH D2151 O 82.8 98.8 156.4 60.6 REMARK 620 6 HOH D2175 O 163.5 86.8 91.9 67.0 81.3 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 SER D 123 O REMARK 620 2 ASP D 126 OD1 93.3 REMARK 620 3 ASP D 127 OD1 102.4 77.4 REMARK 620 4 MET D 335 O 164.0 102.5 79.1 REMARK 620 5 HOH D2117 O 84.9 169.4 113.2 80.0 REMARK 620 6 HOH D2204 O 95.0 103.1 162.5 83.8 66.7 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 ASP D 158 OD2 REMARK 620 2 ASN D 215 OD1 99.3 REMARK 620 3 ASP D 217 O 168.8 87.5 REMARK 620 4 ASP D 217 OD1 93.3 84.8 78.5 REMARK 620 5 PRO D 219 O 76.8 170.3 97.8 104.2 REMARK 620 6 GLU D 220 OE1 104.5 96.1 83.4 161.8 76.6 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7TCT RELATED DB: PDB REMARK 900 RELATED ID: 7THO RELATED DB: PDB REMARK 900 RELATED ID: 7U60 RELATED DB: PDB REMARK 900 RELATED ID: 7TMZ RELATED DB: PDB REMARK 900 RELATED ID: 7TPD RELATED DB: PDB REMARK 900 RELATED ID: 7TD8 RELATED DB: PDB DBREF 7U9F A 1 454 UNP P08514 ITA2B_HUMAN 32 485 DBREF 7U9F B 1 471 UNP P05106 ITB3_HUMAN 27 497 DBREF 7U9F C 1 454 UNP P08514 ITA2B_HUMAN 32 485 DBREF 7U9F D 1 471 UNP P05106 ITB3_HUMAN 27 497 DBREF 7U9F E 1 219 PDB 7U9F 7U9F 1 219 DBREF 7U9F F 1 214 PDB 7U9F 7U9F 1 214 DBREF 7U9F H 1 219 PDB 7U9F 7U9F 1 219 DBREF 7U9F L 1 214 PDB 7U9F 7U9F 1 214 SEQRES 1 A 454 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY SEQRES 2 A 454 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS SEQRES 3 A 454 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA SEQRES 4 A 454 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY SEQRES 5 A 454 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS SEQRES 6 A 454 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN SEQRES 7 A 454 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN SEQRES 8 A 454 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE SEQRES 9 A 454 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU SEQRES 10 A 454 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS SEQRES 11 A 454 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR SEQRES 12 A 454 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL SEQRES 13 A 454 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA SEQRES 14 A 454 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL SEQRES 15 A 454 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU SEQRES 16 A 454 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG SEQRES 17 A 454 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU SEQRES 18 A 454 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR SEQRES 19 A 454 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP SEQRES 20 A 454 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP SEQRES 21 A 454 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR SEQRES 22 A 454 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA SEQRES 23 A 454 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN SEQRES 24 A 454 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU SEQRES 25 A 454 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL SEQRES 26 A 454 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS SEQRES 27 A 454 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN SEQRES 28 A 454 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY SEQRES 29 A 454 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA SEQRES 30 A 454 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU SEQRES 31 A 454 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO SEQRES 32 A 454 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA SEQRES 33 A 454 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP SEQRES 34 A 454 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA SEQRES 35 A 454 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL SEQRES 1 B 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS SEQRES 2 B 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SEQRES 3 B 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP SEQRES 4 B 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SEQRES 5 B 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU SEQRES 6 B 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER SEQRES 7 B 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG SEQRES 8 B 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL SEQRES 9 B 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU SEQRES 10 B 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER SEQRES 11 B 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG SEQRES 12 B 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE SEQRES 13 B 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO SEQRES 14 B 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR SEQRES 15 B 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR SEQRES 16 B 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS SEQRES 17 B 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY SEQRES 18 B 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU SEQRES 19 B 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL SEQRES 20 B 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY SEQRES 21 B 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS SEQRES 22 B 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR SEQRES 23 B 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SEQRES 24 B 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU SEQRES 25 B 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE SEQRES 26 B 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER SEQRES 27 B 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE SEQRES 28 B 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU SEQRES 29 B 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN SEQRES 30 B 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS SEQRES 31 B 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL SEQRES 32 B 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE SEQRES 33 B 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL SEQRES 34 B 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU SEQRES 35 B 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE SEQRES 36 B 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SEQRES 37 B 471 SER GLN CYS SEQRES 1 C 454 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY SEQRES 2 C 454 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS SEQRES 3 C 454 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA SEQRES 4 C 454 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY SEQRES 5 C 454 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS SEQRES 6 C 454 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN SEQRES 7 C 454 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN SEQRES 8 C 454 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE SEQRES 9 C 454 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU SEQRES 10 C 454 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS SEQRES 11 C 454 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR SEQRES 12 C 454 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL SEQRES 13 C 454 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA SEQRES 14 C 454 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL SEQRES 15 C 454 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU SEQRES 16 C 454 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG SEQRES 17 C 454 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU SEQRES 18 C 454 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR SEQRES 19 C 454 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP SEQRES 20 C 454 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP SEQRES 21 C 454 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR SEQRES 22 C 454 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA SEQRES 23 C 454 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN SEQRES 24 C 454 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU SEQRES 25 C 454 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL SEQRES 26 C 454 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS SEQRES 27 C 454 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN SEQRES 28 C 454 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY SEQRES 29 C 454 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA SEQRES 30 C 454 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU SEQRES 31 C 454 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO SEQRES 32 C 454 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA SEQRES 33 C 454 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP SEQRES 34 C 454 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA SEQRES 35 C 454 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL SEQRES 1 D 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS SEQRES 2 D 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SEQRES 3 D 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP SEQRES 4 D 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SEQRES 5 D 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU SEQRES 6 D 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER SEQRES 7 D 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG SEQRES 8 D 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL SEQRES 9 D 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU SEQRES 10 D 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER SEQRES 11 D 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG SEQRES 12 D 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE SEQRES 13 D 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO SEQRES 14 D 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR SEQRES 15 D 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR SEQRES 16 D 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS SEQRES 17 D 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY SEQRES 18 D 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU SEQRES 19 D 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL SEQRES 20 D 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY SEQRES 21 D 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS SEQRES 22 D 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR SEQRES 23 D 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SEQRES 24 D 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU SEQRES 25 D 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE SEQRES 26 D 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER SEQRES 27 D 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE SEQRES 28 D 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU SEQRES 29 D 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN SEQRES 30 D 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS SEQRES 31 D 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL SEQRES 32 D 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE SEQRES 33 D 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL SEQRES 34 D 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU SEQRES 35 D 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE SEQRES 36 D 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SEQRES 37 D 471 SER GLN CYS SEQRES 1 E 216 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 E 216 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 E 216 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN SEQRES 4 E 216 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 E 216 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN SEQRES 6 E 216 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 E 216 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 E 216 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR SEQRES 9 E 216 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 E 216 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 E 216 ALA PRO VAL CYS THR GLY SER SER VAL THR LEU GLY CYS SEQRES 12 E 216 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR SEQRES 13 E 216 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 E 216 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 E 216 SER VAL THR VAL THR SER SER THR TRP PRO SER GLN SER SEQRES 16 E 216 ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 E 216 VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 1 F 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL SEQRES 2 F 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER SEQRES 3 F 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS SEQRES 4 F 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR SEQRES 5 F 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 F 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR SEQRES 8 F 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 F 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 F 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 F 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 F 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 F 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 F 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 F 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 F 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 F 214 PHE ASN ARG ASN GLU CYS SEQRES 1 H 216 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 216 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 216 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN SEQRES 4 H 216 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 216 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN SEQRES 6 H 216 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 H 216 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 H 216 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR SEQRES 9 H 216 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 H 216 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 216 ALA PRO VAL CYS THR GLY SER SER VAL THR LEU GLY CYS SEQRES 12 H 216 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR SEQRES 13 H 216 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 216 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 216 SER VAL THR VAL THR SER SER THR TRP PRO SER GLN SER SEQRES 16 H 216 ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 216 VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 1 L 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL SEQRES 2 L 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER SEQRES 3 L 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR SEQRES 5 L 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 L 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR SEQRES 8 L 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET MAN G 5 11 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET NAG K 1 14 HET NAG K 2 14 HET SO4 A 501 5 HET SO4 A 502 5 HET CA A 503 1 HET CA A 504 1 HET CA A 505 1 HET CA A 506 1 HET SO4 A 507 5 HET SO4 A 508 5 HET MN B2001 1 HET MN B2002 1 HET MN B2003 1 HET NAG B2004 14 HET I7R B2005 31 HET SO4 C 501 5 HET SO4 C 502 5 HET SO4 C 503 5 HET CL C 504 1 HET CA C 505 1 HET CA C 506 1 HET CA C 507 1 HET CA C 508 1 HET SO4 C 509 5 HET MN D2001 1 HET MN D2002 1 HET MN D2003 1 HET NAG D2004 14 HET CL D2005 1 HET I7R D2006 31 HET SO4 L 301 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM SO4 SULFATE ION HETNAM CA CALCIUM ION HETNAM MN MANGANESE (II) ION HETNAM I7R (4-{[(5S)-3-{4-[(E)-IMINO(4-METHYLPIPERAZIN-1-YL) HETNAM 2 I7R METHYL]PHENYL}-4,5-DIHYDRO-1,2-OXAZOL-5- HETNAM 3 I7R YL]METHYL}PIPERAZIN-1-YL)ACETIC ACID HETNAM CL CHLORIDE ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 9 NAG 10(C8 H15 N O6) FORMUL 9 BMA 2(C6 H12 O6) FORMUL 9 MAN 3(C6 H12 O6) FORMUL 13 SO4 9(O4 S 2-) FORMUL 15 CA 8(CA 2+) FORMUL 21 MN 6(MN 2+) FORMUL 25 I7R 2(C22 H32 N6 O3) FORMUL 29 CL 2(CL 1-) FORMUL 42 HOH *1104(H2 O) HELIX 1 AA1 LEU A 151 ASN A 158 1 8 HELIX 2 AA2 GLY A 187 LEU A 192 1 6 HELIX 3 AA3 VAL A 200 TYR A 207 1 8 HELIX 4 AA4 ASN A 227 PHE A 231 5 5 HELIX 5 AA5 THR A 259 LEU A 264 1 6 HELIX 6 AA6 TYR A 440 ALA A 442 5 3 HELIX 7 AA7 ASN B 3 ARG B 8 1 6 HELIX 8 AA8 SER B 12 ALA B 18 1 7 HELIX 9 AA9 LEU B 40 ASP B 47 1 8 HELIX 10 AB1 ALA B 50 GLU B 52 5 3 HELIX 11 AB2 SER B 121 SER B 123 5 3 HELIX 12 AB3 MET B 124 ILE B 131 1 8 HELIX 13 AB4 ASN B 133 ARG B 143 1 11 HELIX 14 AB5 PRO B 169 ASN B 175 1 7 HELIX 15 AB6 VAL B 200 LYS B 209 1 10 HELIX 16 AB7 GLY B 221 CYS B 232 1 12 HELIX 17 AB8 CYS B 232 GLY B 237 1 6 HELIX 18 AB9 LEU B 258 GLY B 264 5 7 HELIX 19 AC1 SER B 291 LYS B 302 1 12 HELIX 20 AC2 VAL B 314 ILE B 325 1 12 HELIX 21 AC3 ASN B 339 ARG B 352 1 14 HELIX 22 AC4 CYS B 435 ALA B 441 5 7 HELIX 23 AC5 LEU C 151 ASN C 158 1 8 HELIX 24 AC6 GLY C 187 LEU C 192 1 6 HELIX 25 AC7 VAL C 200 TYR C 207 1 8 HELIX 26 AC8 ASN C 227 PHE C 231 5 5 HELIX 27 AC9 THR C 259 LEU C 264 1 6 HELIX 28 AD1 ASN D 3 ARG D 8 1 6 HELIX 29 AD2 SER D 12 ALA D 18 1 7 HELIX 30 AD3 LEU D 40 ASP D 47 1 8 HELIX 31 AD4 ALA D 50 GLU D 52 5 3 HELIX 32 AD5 SER D 121 SER D 123 5 3 HELIX 33 AD6 MET D 124 TRP D 129 1 6 HELIX 34 AD7 SER D 130 GLN D 132 5 3 HELIX 35 AD8 ASN D 133 THR D 146 1 14 HELIX 36 AD9 PRO D 169 ASN D 175 1 7 HELIX 37 AE1 VAL D 200 LYS D 208 1 9 HELIX 38 AE2 GLY D 221 CYS D 232 1 12 HELIX 39 AE3 CYS D 232 GLY D 237 1 6 HELIX 40 AE4 LEU D 258 GLY D 264 5 7 HELIX 41 AE5 SER D 291 LYS D 302 1 12 HELIX 42 AE6 VAL D 314 GLU D 323 1 10 HELIX 43 AE7 ASN D 339 ARG D 352 1 14 HELIX 44 AE8 CYS D 435 ALA D 439 5 5 HELIX 45 AE9 ASN E 28 THR E 32 5 5 HELIX 46 AF1 PRO E 62 GLN E 65 5 4 HELIX 47 AF2 THR E 87 THR E 91 5 5 HELIX 48 AF3 ASP F 79 PHE F 83 5 5 HELIX 49 AF4 SER F 121 THR F 126 1 6 HELIX 50 AF5 LYS F 183 GLU F 187 1 5 HELIX 51 AF6 ASN H 28 THR H 32 5 5 HELIX 52 AF7 PRO H 62 GLN H 65 5 4 HELIX 53 AF8 THR H 87 THR H 91 5 5 HELIX 54 AF9 SER L 121 THR L 126 1 6 HELIX 55 AG1 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 THR A 9 ALA A 12 0 SHEET 2 AA1 4 GLN A 444 TYR A 448 -1 O VAL A 445 N TYR A 11 SHEET 3 AA1 4 ASP A 434 ALA A 439 -1 N LEU A 435 O TYR A 448 SHEET 4 AA1 4 SER A 420 VAL A 425 -1 N ARG A 422 O ILE A 436 SHEET 1 AA2 3 LEU A 23 LYS A 27 0 SHEET 2 AA2 3 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26 SHEET 3 AA2 3 GLY A 52 PRO A 57 -1 O CYS A 56 N ILE A 35 SHEET 1 AA3 4 THR A 76 VAL A 79 0 SHEET 2 AA3 4 GLN A 82 PHE A 87 -1 O LEU A 84 N ARG A 77 SHEET 3 AA3 4 HIS A 112 GLU A 117 -1 O LEU A 116 N THR A 83 SHEET 4 AA3 4 GLU A 120 GLU A 121 -1 O GLU A 120 N GLU A 117 SHEET 1 AA4 4 VAL A 97 TRP A 100 0 SHEET 2 AA4 4 VAL A 103 ALA A 108 -1 O VAL A 105 N VAL A 98 SHEET 3 AA4 4 SER A 129 ALA A 133 -1 O PHE A 131 N ALA A 106 SHEET 4 AA4 4 ARG A 140 TYR A 143 -1 O ALA A 141 N LEU A 132 SHEET 1 AA5 4 SER A 172 VAL A 175 0 SHEET 2 AA5 4 GLU A 180 ALA A 185 -1 O VAL A 182 N VAL A 174 SHEET 3 AA5 4 LEU A 194 PRO A 199 -1 O ALA A 196 N LEU A 183 SHEET 4 AA5 4 SER A 220 LEU A 221 -1 O SER A 220 N GLN A 197 SHEET 1 AA6 4 VAL A 239 GLY A 242 0 SHEET 2 AA6 4 GLU A 252 ALA A 257 -1 O VAL A 254 N ALA A 240 SHEET 3 AA6 4 ALA A 266 LEU A 270 -1 O ALA A 266 N ALA A 257 SHEET 4 AA6 4 ARG A 276 ARG A 281 -1 O LEU A 280 N VAL A 267 SHEET 1 AA7 4 VAL A 293 THR A 296 0 SHEET 2 AA7 4 ASP A 305 ALA A 310 -1 O LEU A 307 N ALA A 294 SHEET 3 AA7 4 ARG A 327 PHE A 331 -1 O ARG A 327 N ALA A 310 SHEET 4 AA7 4 LEU A 345 THR A 348 -1 O LEU A 347 N VAL A 328 SHEET 1 AA8 2 MET A 314 ARG A 317 0 SHEET 2 AA8 2 LYS A 321 GLU A 324 -1 O ALA A 323 N GLU A 315 SHEET 1 AA9 4 ILE A 360 GLY A 364 0 SHEET 2 AA9 4 ASP A 373 ALA A 378 -1 O ASP A 373 N GLY A 364 SHEET 3 AA9 4 GLN A 388 PHE A 392 -1 O GLN A 388 N ALA A 378 SHEET 4 AA9 4 GLN A 405 ASP A 408 -1 O LEU A 407 N VAL A 389 SHEET 1 AB1 2 GLY A 394 GLN A 395 0 SHEET 2 AB1 2 GLY A 398 LEU A 399 -1 O GLY A 398 N GLN A 395 SHEET 1 AB2 3 CYS B 38 ASP B 39 0 SHEET 2 AB2 3 ALA B 24 CYS B 26 -1 N ALA B 24 O ASP B 39 SHEET 3 AB2 3 ILE B 54 GLU B 55 -1 O GLU B 55 N TRP B 25 SHEET 1 AB3 6 GLU B 60 GLU B 65 0 SHEET 2 AB3 6 ARG B 87 LEU B 92 -1 O ALA B 89 N ARG B 62 SHEET 3 AB3 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90 SHEET 4 AB3 6 GLU B 411 PRO B 418 -1 N ILE B 416 O LEU B 425 SHEET 5 AB3 6 VAL B 355 ARG B 360 -1 N GLU B 358 O LYS B 417 SHEET 6 AB3 6 SER B 385 CYS B 386 -1 O CYS B 386 N VAL B 355 SHEET 1 AB4 5 VAL B 83 SER B 84 0 SHEET 2 AB4 5 SER B 97 ARG B 105 -1 O GLN B 103 N SER B 84 SHEET 3 AB4 5 THR B 394 VAL B 403 -1 O ILE B 399 N PHE B 100 SHEET 4 AB4 5 LEU B 366 CYS B 374 -1 N SER B 367 O LYS B 402 SHEET 5 AB4 5 GLU B 378 PRO B 381 -1 O ILE B 380 N ALA B 372 SHEET 1 AB5 6 TYR B 190 THR B 197 0 SHEET 2 AB5 6 LEU B 149 PHE B 156 -1 N ALA B 155 O LYS B 191 SHEET 3 AB5 6 VAL B 112 ASP B 119 1 N TYR B 116 O GLY B 154 SHEET 4 AB5 6 SER B 243 THR B 250 1 O SER B 243 N ASP B 113 SHEET 5 AB5 6 ILE B 304 THR B 311 1 O ILE B 307 N PHE B 248 SHEET 6 AB5 6 THR B 329 LEU B 333 1 O LEU B 333 N VAL B 310 SHEET 1 AB6 2 GLY B 453 GLU B 456 0 SHEET 2 AB6 2 VAL B 459 CYS B 462 -1 O ARG B 461 N THR B 454 SHEET 1 AB7 4 THR C 9 ALA C 12 0 SHEET 2 AB7 4 GLN C 444 TYR C 448 -1 O VAL C 445 N TYR C 11 SHEET 3 AB7 4 ASP C 434 ALA C 439 -1 N LEU C 435 O TYR C 448 SHEET 4 AB7 4 SER C 420 VAL C 425 -1 N VAL C 425 O ASP C 434 SHEET 1 AB8 3 LEU C 23 LYS C 27 0 SHEET 2 AB8 3 VAL C 33 ALA C 39 -1 O ALA C 34 N HIS C 26 SHEET 3 AB8 3 GLY C 52 PRO C 57 -1 O CYS C 56 N ILE C 35 SHEET 1 AB9 4 THR C 76 VAL C 79 0 SHEET 2 AB9 4 GLN C 82 PHE C 87 -1 O LEU C 84 N ARG C 77 SHEET 3 AB9 4 HIS C 112 GLU C 117 -1 O HIS C 112 N PHE C 87 SHEET 4 AB9 4 GLU C 120 GLU C 121 -1 O GLU C 120 N GLU C 117 SHEET 1 AC1 4 VAL C 97 TRP C 100 0 SHEET 2 AC1 4 VAL C 103 ALA C 108 -1 O VAL C 105 N VAL C 98 SHEET 3 AC1 4 SER C 129 ALA C 133 -1 O PHE C 131 N ALA C 106 SHEET 4 AC1 4 ARG C 140 TYR C 143 -1 O ALA C 141 N LEU C 132 SHEET 1 AC2 4 SER C 172 VAL C 175 0 SHEET 2 AC2 4 GLU C 180 ALA C 185 -1 O GLY C 184 N SER C 172 SHEET 3 AC2 4 LEU C 194 PRO C 199 -1 O ALA C 196 N LEU C 183 SHEET 4 AC2 4 SER C 220 LEU C 221 -1 O SER C 220 N GLN C 197 SHEET 1 AC3 4 VAL C 239 GLY C 242 0 SHEET 2 AC3 4 GLU C 252 ALA C 257 -1 O VAL C 254 N ALA C 240 SHEET 3 AC3 4 ALA C 266 LEU C 270 -1 O ALA C 266 N ALA C 257 SHEET 4 AC3 4 ARG C 276 ARG C 281 -1 O LEU C 277 N ILE C 269 SHEET 1 AC4 4 VAL C 293 THR C 296 0 SHEET 2 AC4 4 ASP C 305 ALA C 310 -1 O LEU C 307 N ALA C 294 SHEET 3 AC4 4 ARG C 327 PHE C 331 -1 O TYR C 329 N VAL C 308 SHEET 4 AC4 4 LEU C 345 THR C 348 -1 O LEU C 347 N VAL C 328 SHEET 1 AC5 2 MET C 314 ARG C 317 0 SHEET 2 AC5 2 LYS C 321 GLU C 324 -1 O ALA C 323 N GLU C 315 SHEET 1 AC6 4 ILE C 360 PRO C 362 0 SHEET 2 AC6 4 ILE C 374 ALA C 378 -1 O ALA C 375 N ALA C 361 SHEET 3 AC6 4 GLN C 388 PHE C 392 -1 O LEU C 390 N VAL C 376 SHEET 4 AC6 4 GLN C 405 ASP C 408 -1 O LEU C 407 N VAL C 389 SHEET 1 AC7 2 GLY C 394 GLN C 395 0 SHEET 2 AC7 2 GLY C 398 LEU C 399 -1 O GLY C 398 N GLN C 395 SHEET 1 AC8 3 CYS D 38 ASP D 39 0 SHEET 2 AC8 3 ALA D 24 CYS D 26 -1 N ALA D 24 O ASP D 39 SHEET 3 AC8 3 ILE D 54 GLU D 55 -1 O GLU D 55 N TRP D 25 SHEET 1 AC9 6 ALA D 61 GLU D 65 0 SHEET 2 AC9 6 ARG D 87 LEU D 92 -1 O ALA D 89 N ARG D 62 SHEET 3 AC9 6 LEU D 425 PHE D 431 1 O GLN D 428 N LEU D 90 SHEET 4 AC9 6 GLU D 411 PRO D 418 -1 N ILE D 416 O LEU D 425 SHEET 5 AC9 6 VAL D 355 ARG D 360 -1 N ARG D 360 O THR D 415 SHEET 6 AC9 6 SER D 385 CYS D 386 -1 O CYS D 386 N VAL D 355 SHEET 1 AD1 5 VAL D 83 SER D 84 0 SHEET 2 AD1 5 SER D 97 ARG D 105 -1 O GLN D 103 N SER D 84 SHEET 3 AD1 5 THR D 394 VAL D 403 -1 O ILE D 399 N PHE D 100 SHEET 4 AD1 5 LEU D 366 THR D 373 -1 N THR D 373 O SER D 396 SHEET 5 AD1 5 VAL D 379 PRO D 381 -1 O ILE D 380 N ALA D 372 SHEET 1 AD2 6 TYR D 190 THR D 197 0 SHEET 2 AD2 6 LEU D 149 PHE D 156 -1 N ALA D 155 O LYS D 191 SHEET 3 AD2 6 VAL D 112 ASP D 119 1 N TYR D 116 O GLY D 152 SHEET 4 AD2 6 SER D 243 THR D 250 1 O SER D 243 N ASP D 113 SHEET 5 AD2 6 ASN D 305 THR D 311 1 O ILE D 307 N LEU D 246 SHEET 6 AD2 6 THR D 329 LEU D 333 1 O LEU D 333 N VAL D 310 SHEET 1 AD3 2 GLY D 453 GLU D 456 0 SHEET 2 AD3 2 VAL D 459 CYS D 462 -1 O ARG D 461 N THR D 454 SHEET 1 AD4 4 GLN E 3 GLN E 6 0 SHEET 2 AD4 4 VAL E 18 SER E 25 -1 O THR E 23 N GLN E 5 SHEET 3 AD4 4 THR E 78 LEU E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AD4 4 ALA E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AD5 6 GLU E 10 VAL E 12 0 SHEET 2 AD5 6 THR E 113 VAL E 117 1 O THR E 116 N GLU E 10 SHEET 3 AD5 6 ALA E 92 ARG E 98 -1 N ALA E 92 O VAL E 115 SHEET 4 AD5 6 VAL E 34 ARG E 40 -1 N HIS E 35 O VAL E 97 SHEET 5 AD5 6 GLY E 44 ILE E 51 -1 O GLU E 46 N LYS E 38 SHEET 6 AD5 6 THR E 58 TYR E 60 -1 O LYS E 59 N ARG E 50 SHEET 1 AD6 4 GLU E 10 VAL E 12 0 SHEET 2 AD6 4 THR E 113 VAL E 117 1 O THR E 116 N GLU E 10 SHEET 3 AD6 4 ALA E 92 ARG E 98 -1 N ALA E 92 O VAL E 115 SHEET 4 AD6 4 TYR E 108 TRP E 109 -1 O TYR E 108 N ARG E 98 SHEET 1 AD7 4 SER E 126 LEU E 130 0 SHEET 2 AD7 4 SER E 141 LYS E 149 -1 O LEU E 147 N TYR E 128 SHEET 3 AD7 4 TYR E 181 THR E 190 -1 O VAL E 189 N VAL E 142 SHEET 4 AD7 4 VAL E 175 LEU E 176 -1 N VAL E 175 O THR E 182 SHEET 1 AD8 3 THR E 157 THR E 159 0 SHEET 2 AD8 3 THR E 200 ALA E 204 -1 O ALA E 204 N THR E 157 SHEET 3 AD8 3 ASP E 213 LYS E 215 -1 O LYS E 214 N CYS E 201 SHEET 1 AD9 4 MET F 4 SER F 7 0 SHEET 2 AD9 4 VAL F 19 ALA F 25 -1 O HIS F 24 N THR F 5 SHEET 3 AD9 4 ASP F 70 ILE F 75 -1 O LEU F 73 N ILE F 21 SHEET 4 AD9 4 PHE F 62 SER F 67 -1 N SER F 65 O SER F 72 SHEET 1 AE1 6 SER F 10 VAL F 13 0 SHEET 2 AE1 6 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13 SHEET 3 AE1 6 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AE1 6 ILE F 33 GLN F 38 -1 N GLY F 34 O VAL F 89 SHEET 5 AE1 6 PHE F 44 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AE1 6 ASN F 53 LEU F 54 -1 O ASN F 53 N TYR F 49 SHEET 1 AE2 4 SER F 10 VAL F 13 0 SHEET 2 AE2 4 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13 SHEET 3 AE2 4 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AE2 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90 SHEET 1 AE3 4 THR F 114 PHE F 118 0 SHEET 2 AE3 4 GLY F 129 PHE F 139 -1 O VAL F 133 N PHE F 118 SHEET 3 AE3 4 TYR F 173 THR F 182 -1 O TYR F 173 N PHE F 139 SHEET 4 AE3 4 VAL F 159 TRP F 163 -1 N SER F 162 O SER F 176 SHEET 1 AE4 4 SER F 153 ARG F 155 0 SHEET 2 AE4 4 ASN F 145 ILE F 150 -1 N TRP F 148 O ARG F 155 SHEET 3 AE4 4 TYR F 192 HIS F 198 -1 O GLU F 195 N LYS F 147 SHEET 4 AE4 4 SER F 201 LYS F 207 -1 O ILE F 205 N ALA F 196 SHEET 1 AE5 4 GLN H 3 GLN H 6 0 SHEET 2 AE5 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AE5 4 THR H 78 LEU H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AE5 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AE6 6 GLU H 10 VAL H 12 0 SHEET 2 AE6 6 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10 SHEET 3 AE6 6 VAL H 93 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AE6 6 VAL H 34 ARG H 40 -1 N HIS H 35 O VAL H 97 SHEET 5 AE6 6 GLY H 44 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AE6 6 THR H 58 TYR H 60 -1 O LYS H 59 N ARG H 50 SHEET 1 AE7 4 GLU H 10 VAL H 12 0 SHEET 2 AE7 4 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10 SHEET 3 AE7 4 VAL H 93 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AE7 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AE8 4 SER H 126 LEU H 130 0 SHEET 2 AE8 4 SER H 141 TYR H 151 -1 O LEU H 147 N TYR H 128 SHEET 3 AE8 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148 SHEET 4 AE8 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186 SHEET 1 AE9 4 SER H 126 LEU H 130 0 SHEET 2 AE9 4 SER H 141 TYR H 151 -1 O LEU H 147 N TYR H 128 SHEET 3 AE9 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148 SHEET 4 AE9 4 VAL H 175 GLN H 177 -1 N GLN H 177 O LEU H 180 SHEET 1 AF1 3 THR H 157 TRP H 160 0 SHEET 2 AF1 3 THR H 200 HIS H 205 -1 O ALA H 204 N THR H 157 SHEET 3 AF1 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205 SHEET 1 AF2 4 MET L 4 SER L 7 0 SHEET 2 AF2 4 VAL L 19 ALA L 25 -1 O HIS L 24 N THR L 5 SHEET 3 AF2 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AF2 4 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AF3 6 SER L 10 VAL L 13 0 SHEET 2 AF3 6 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11 SHEET 3 AF3 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AF3 6 ILE L 33 GLN L 38 -1 N GLY L 34 O VAL L 89 SHEET 5 AF3 6 PHE L 44 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AF3 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AF4 4 SER L 10 VAL L 13 0 SHEET 2 AF4 4 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11 SHEET 3 AF4 4 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AF4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AF5 4 THR L 114 PHE L 118 0 SHEET 2 AF5 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AF5 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AF5 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AF6 4 SER L 153 ARG L 155 0 SHEET 2 AF6 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AF6 4 SER L 191 HIS L 198 -1 O GLU L 195 N LYS L 147 SHEET 4 AF6 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.03 SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.03 SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.02 SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.03 SSBOND 5 CYS B 13 CYS B 435 1555 1555 2.03 SSBOND 6 CYS B 16 CYS B 38 1555 1555 2.03 SSBOND 7 CYS B 26 CYS B 49 1555 1555 2.03 SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.04 SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.03 SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.03 SSBOND 11 CYS B 406 CYS B 433 1555 1555 2.03 SSBOND 12 CYS B 437 CYS B 457 1555 1555 2.03 SSBOND 13 CYS B 448 CYS B 460 1555 1555 2.03 SSBOND 14 CYS C 56 CYS C 65 1555 1555 2.03 SSBOND 15 CYS C 107 CYS C 130 1555 1555 2.04 SSBOND 16 CYS C 146 CYS C 167 1555 1555 2.03 SSBOND 17 CYS D 5 CYS D 23 1555 1555 2.03 SSBOND 18 CYS D 13 CYS D 435 1555 1555 2.03 SSBOND 19 CYS D 16 CYS D 38 1555 1555 2.03 SSBOND 20 CYS D 26 CYS D 49 1555 1555 2.03 SSBOND 21 CYS D 177 CYS D 184 1555 1555 2.03 SSBOND 22 CYS D 232 CYS D 273 1555 1555 2.03 SSBOND 23 CYS D 374 CYS D 386 1555 1555 2.03 SSBOND 24 CYS D 406 CYS D 433 1555 1555 2.03 SSBOND 25 CYS D 437 CYS D 457 1555 1555 2.03 SSBOND 26 CYS D 448 CYS D 460 1555 1555 2.03 SSBOND 27 CYS D 462 CYS D 471 1555 1555 2.04 SSBOND 28 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 29 CYS E 134 CYS F 214 1555 1555 2.04 SSBOND 30 CYS E 146 CYS E 201 1555 1555 2.02 SSBOND 31 CYS F 23 CYS F 88 1555 1555 2.03 SSBOND 32 CYS F 134 CYS F 194 1555 1555 2.04 SSBOND 33 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 34 CYS H 134 CYS L 214 1555 1555 2.03 SSBOND 35 CYS H 146 CYS H 201 1555 1555 2.03 SSBOND 36 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 37 CYS L 134 CYS L 194 1555 1555 2.04 LINK ND2 ASN B 99 C1 NAG B2004 1555 1555 1.44 LINK ND2 ASN B 320 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN B 371 C1 NAG I 1 1555 1555 1.43 LINK ND2 ASN D 99 C1 NAG D2004 1555 1555 1.44 LINK ND2 ASN D 320 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN D 371 C1 NAG K 1 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45 LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.45 LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK OE1 GLU A 243 CA CA A 503 1555 1555 2.40 LINK OE2 GLU A 243 CA CA A 503 1555 1555 2.40 LINK OD1 ASP A 245 CA CA A 503 1555 1555 2.32 LINK O ASP A 247 CA CA A 503 1555 1555 2.34 LINK O THR A 250 CA CA A 503 1555 1555 2.32 LINK OG1 THR A 250 CA CA A 503 1555 1555 2.42 LINK OE1 GLU A 252 CA CA A 503 1555 1555 2.37 LINK OE2 GLU A 252 CA CA A 503 1555 1555 2.38 LINK OD1 ASP A 297 CA CA A 504 1555 1555 2.37 LINK OD1 ASN A 299 CA CA A 504 1555 1555 2.30 LINK OD1 ASP A 301 CA CA A 504 1555 1555 2.45 LINK O ARG A 303 CA CA A 504 1555 1555 2.34 LINK OD1 ASP A 305 CA CA A 504 1555 1555 2.42 LINK OD2 ASP A 305 CA CA A 504 1555 1555 2.42 LINK OD1 ASP A 365 CA CA A 505 1555 1555 2.38 LINK OD1 ASP A 367 CA CA A 505 1555 1555 2.36 LINK OD1 ASP A 369 CA CA A 505 1555 1555 2.44 LINK O TYR A 371 CA CA A 505 1555 1555 2.27 LINK OD1 ASP A 373 CA CA A 505 1555 1555 2.42 LINK OD2 ASP A 373 CA CA A 505 1555 1555 2.46 LINK OD1 ASP A 426 CA CA A 506 1555 1555 2.33 LINK OD1 ASP A 428 CA CA A 506 1555 1555 2.35 LINK OD1 ASN A 430 CA CA A 506 1555 1555 2.35 LINK O TYR A 432 CA CA A 506 1555 1555 2.29 LINK OD1 ASP A 434 CA CA A 506 1555 1555 2.34 LINK OD2 ASP A 434 CA CA A 506 1555 1555 2.37 LINK CA CA A 504 O HOH A 635 1555 1555 2.35 LINK CA CA A 505 O HOH A 644 1555 1555 2.39 LINK CA CA A 506 O HOH A 622 1555 1555 2.39 LINK OG SER B 121 MN MN B2001 1555 1555 2.26 LINK O SER B 123 MN MN B2002 1555 1555 2.21 LINK OD1AASP B 126 MN MN B2002 1555 1555 2.16 LINK OD2AASP B 126 MN MN B2002 1555 1555 2.19 LINK OD1 ASP B 127 MN MN B2002 1555 1555 2.17 LINK OD2 ASP B 158 MN MN B2003 1555 1555 2.19 LINK OD1 ASN B 215 MN MN B2003 1555 1555 2.17 LINK O ASP B 217 MN MN B2003 1555 1555 2.21 LINK OD1 ASP B 217 MN MN B2003 1555 1555 2.15 LINK O PRO B 219 MN MN B2003 1555 1555 2.08 LINK OE2 GLU B 220 MN MN B2001 1555 1555 2.14 LINK OE1 GLU B 220 MN MN B2003 1555 1555 2.17 LINK O MET B 335 MN MN B2002 1555 1555 2.79 LINK MN MN B2001 O2 I7R B2005 1555 1555 2.19 LINK MN MN B2001 O HOH B2115 1555 1555 2.17 LINK MN MN B2001 O HOH B2138 1555 1555 2.17 LINK MN MN B2001 O HOH B2179 1555 1555 2.20 LINK MN MN B2002 O HOH B2156 1555 1555 2.28 LINK MN MN B2002 O HOH B2190 1555 1555 2.27 LINK OE1 GLU C 243 CA CA C 505 1555 1555 2.39 LINK OE2 GLU C 243 CA CA C 505 1555 1555 2.41 LINK OD1 ASP C 245 CA CA C 505 1555 1555 2.31 LINK O ASP C 247 CA CA C 505 1555 1555 2.39 LINK O THR C 250 CA CA C 505 1555 1555 2.38 LINK OG1 THR C 250 CA CA C 505 1555 1555 2.43 LINK OE1 GLU C 252 CA CA C 505 1555 1555 2.42 LINK OE2 GLU C 252 CA CA C 505 1555 1555 2.42 LINK OD1 ASP C 297 CA CA C 506 1555 1555 2.34 LINK OD1 ASN C 299 CA CA C 506 1555 1555 2.37 LINK OD1 ASP C 301 CA CA C 506 1555 1555 2.32 LINK O ARG C 303 CA CA C 506 1555 1555 2.34 LINK OD1 ASP C 305 CA CA C 506 1555 1555 2.37 LINK OD2 ASP C 305 CA CA C 506 1555 1555 2.35 LINK OD1 ASP C 365 CA CA C 507 1555 1555 2.40 LINK OD1 ASP C 367 CA CA C 507 1555 1555 2.41 LINK OD1 ASP C 369 CA CA C 507 1555 1555 2.45 LINK O TYR C 371 CA CA C 507 1555 1555 2.30 LINK OD1 ASP C 373 CA CA C 507 1555 1555 2.46 LINK OD2 ASP C 373 CA CA C 507 1555 1555 2.44 LINK OD1 ASP C 426 CA CA C 508 1555 1555 2.32 LINK OD1 ASP C 428 CA CA C 508 1555 1555 2.38 LINK OD1 ASN C 430 CA CA C 508 1555 1555 2.37 LINK O TYR C 432 CA CA C 508 1555 1555 2.31 LINK OD1 ASP C 434 CA CA C 508 1555 1555 2.35 LINK OD2 ASP C 434 CA CA C 508 1555 1555 2.37 LINK CA CA C 506 O HOH C 620 1555 1555 2.39 LINK CA CA C 507 O HOH C 626 1555 1555 2.44 LINK CA CA C 508 O HOH C 602 1555 1555 2.41 LINK OG SER D 121 MN MN D2001 1555 1555 2.20 LINK O SER D 123 MN MN D2002 1555 1555 2.20 LINK OD1 ASP D 126 MN MN D2002 1555 1555 2.16 LINK OD1 ASP D 127 MN MN D2002 1555 1555 2.17 LINK OD2 ASP D 158 MN MN D2003 1555 1555 2.18 LINK OD1 ASN D 215 MN MN D2003 1555 1555 2.17 LINK O ASP D 217 MN MN D2003 1555 1555 2.19 LINK OD1 ASP D 217 MN MN D2003 1555 1555 2.14 LINK O PRO D 219 MN MN D2003 1555 1555 2.20 LINK OE2 GLU D 220 MN MN D2001 1555 1555 2.15 LINK OE1 GLU D 220 MN MN D2003 1555 1555 2.16 LINK O MET D 335 MN MN D2002 1555 1555 2.49 LINK MN MN D2001 O2 I7R D2006 1555 1555 2.17 LINK MN MN D2001 O HOH D2116 1555 1555 2.19 LINK MN MN D2001 O HOH D2151 1555 1555 2.16 LINK MN MN D2001 O HOH D2175 1555 1555 2.18 LINK MN MN D2002 O HOH D2117 1555 1555 2.28 LINK MN MN D2002 O HOH D2204 1555 1555 2.31 CISPEP 1 SER B 84 PRO B 85 0 -1.95 CISPEP 2 SER B 162 PRO B 163 0 4.57 CISPEP 3 SER B 168 PRO B 169 0 -5.60 CISPEP 4 SER D 84 PRO D 85 0 -1.35 CISPEP 5 SER D 162 PRO D 163 0 3.13 CISPEP 6 SER D 168 PRO D 169 0 -7.03 CISPEP 7 PHE E 152 PRO E 153 0 -0.99 CISPEP 8 GLU E 154 PRO E 155 0 -2.80 CISPEP 9 TRP E 194 PRO E 195 0 2.02 CISPEP 10 SER F 7 PRO F 8 0 -1.20 CISPEP 11 LEU F 94 PRO F 95 0 2.20 CISPEP 12 TYR F 140 PRO F 141 0 -0.87 CISPEP 13 PHE H 152 PRO H 153 0 -3.42 CISPEP 14 GLU H 154 PRO H 155 0 -4.25 CISPEP 15 TRP H 194 PRO H 195 0 -1.32 CISPEP 16 SER L 7 PRO L 8 0 -1.54 CISPEP 17 LEU L 94 PRO L 95 0 3.60 CISPEP 18 TYR L 140 PRO L 141 0 0.44 CRYST1 259.397 144.292 104.923 90.00 90.00 90.00 P 21 21 2 8 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 0.003855 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006930 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009531 0.00000