HEADER IMMUNE SYSTEM 07-APR-25 9O3D TITLE CRYSTAL STRUCTURE OF BROADLY NEUTRALIZING ANTIBODY HEPC108 IN COMPLEX TITLE 2 WITH HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 ECTODOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEPC108 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, E, H, I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEPC108 FAB LIGHT CHAIN; COMPND 7 CHAIN: B, F, J, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN E2; COMPND 11 CHAIN: C, D, G, K; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTT5; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTT5; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS SUBTYPE 1B; SOURCE 23 ORGANISM_TAXID: 31647; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI; SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PCMV KEYWDS HCV GLYCOPROTEIN, BROADLY NEUTRALIZING ANTIBODIES, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.I.FLYAK,X.E.WILCOX REVDAT 1 21-JAN-26 9O3D 0 JRNL AUTH A.I.FLYAK,X.E.WILCOX JRNL TITL STRUCTURAL REPERTOIRE OF HCV BROADLY NEUTRALIZING ANTIBODIES JRNL TITL 2 TARGETING THE E2 FRLY SUPERSITE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 2.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 3 NUMBER OF REFLECTIONS : 112188 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) : 0.214 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 5691 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 52.3200 - 8.3200 0.94 3659 182 0.1885 0.2245 REMARK 3 2 8.3100 - 6.6000 0.93 3563 149 0.1882 0.2363 REMARK 3 3 6.6000 - 5.7700 0.98 3647 234 0.1970 0.2461 REMARK 3 4 5.7700 - 5.2400 0.98 3661 174 0.1667 0.2335 REMARK 3 5 5.2400 - 4.8700 0.91 3391 167 0.1507 0.2012 REMARK 3 6 4.8700 - 4.5800 0.97 3551 220 0.1511 0.2054 REMARK 3 7 4.5800 - 4.3500 0.98 3632 190 0.1501 0.1931 REMARK 3 8 4.3500 - 4.1600 0.98 3606 185 0.1700 0.2248 REMARK 3 9 4.1600 - 4.0000 0.97 3574 203 0.1903 0.2705 REMARK 3 10 4.0000 - 3.8600 0.97 3597 173 0.2036 0.2302 REMARK 3 11 3.8600 - 3.7400 0.91 3325 182 0.2047 0.2827 REMARK 3 12 3.7400 - 3.6400 0.93 3460 186 0.2171 0.2850 REMARK 3 13 3.6400 - 3.5400 0.97 3550 200 0.2220 0.3000 REMARK 3 14 3.5400 - 3.4500 0.97 3592 178 0.2302 0.3279 REMARK 3 15 3.4500 - 3.3800 0.97 3559 199 0.2412 0.3301 REMARK 3 16 3.3800 - 3.3000 0.97 3573 196 0.2736 0.3091 REMARK 3 17 3.3000 - 3.2400 0.97 3576 206 0.2662 0.3225 REMARK 3 18 3.2400 - 3.1800 0.97 3540 188 0.2687 0.3123 REMARK 3 19 3.1800 - 3.1200 0.98 3643 184 0.2618 0.3265 REMARK 3 20 3.1200 - 3.0700 0.94 3465 181 0.2729 0.3100 REMARK 3 21 3.0700 - 3.0200 0.91 3276 173 0.2828 0.3685 REMARK 3 22 3.0200 - 2.9700 0.97 3628 198 0.2996 0.3648 REMARK 3 23 2.9700 - 2.9300 0.97 3537 180 0.3073 0.3417 REMARK 3 24 2.9300 - 2.8900 0.97 3595 200 0.3105 0.3647 REMARK 3 25 2.8900 - 2.8500 0.96 3543 189 0.3186 0.3576 REMARK 3 26 2.8500 - 2.8100 0.97 3507 182 0.3279 0.3308 REMARK 3 27 2.8100 - 2.7700 0.98 3594 214 0.3515 0.4064 REMARK 3 28 2.7700 - 2.7400 0.97 3557 176 0.3728 0.4327 REMARK 3 29 2.7400 - 2.7100 0.97 3568 196 0.3803 0.3962 REMARK 3 30 2.7100 - 2.6800 0.97 3528 206 0.3886 0.4183 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.435 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.176 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.37 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 21743 REMARK 3 ANGLE : 1.212 29643 REMARK 3 CHIRALITY : 0.060 3438 REMARK 3 PLANARITY : 0.011 3736 REMARK 3 DIHEDRAL : 8.467 3803 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 48 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 2:111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.089 -55.271 58.780 REMARK 3 T TENSOR REMARK 3 T11: 0.5219 T22: 0.8338 REMARK 3 T33: 0.4001 T12: -0.0071 REMARK 3 T13: 0.0368 T23: 0.1136 REMARK 3 L TENSOR REMARK 3 L11: 2.6031 L22: 0.8799 REMARK 3 L33: 7.6956 L12: 0.0543 REMARK 3 L13: 1.3627 L23: -1.1607 REMARK 3 S TENSOR REMARK 3 S11: 0.0314 S12: -0.9749 S13: -0.1355 REMARK 3 S21: 0.2650 S22: -0.1754 S23: -0.0815 REMARK 3 S31: 0.2709 S32: -0.5070 S33: 0.1119 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 112:214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.064 -41.728 75.528 REMARK 3 T TENSOR REMARK 3 T11: 0.5548 T22: 1.0152 REMARK 3 T33: 0.7075 T12: 0.0454 REMARK 3 T13: 0.0932 T23: -0.1255 REMARK 3 L TENSOR REMARK 3 L11: 4.7905 L22: 9.3501 REMARK 3 L33: 6.5232 L12: 3.8776 REMARK 3 L13: -1.7475 L23: -2.6592 REMARK 3 S TENSOR REMARK 3 S11: 0.7469 S12: -1.0780 S13: 1.0020 REMARK 3 S21: 0.7040 S22: -0.6144 S23: 0.4067 REMARK 3 S31: -0.5144 S32: -0.0623 S33: -0.1495 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.903 -53.829 43.415 REMARK 3 T TENSOR REMARK 3 T11: 0.5422 T22: 0.7130 REMARK 3 T33: 0.4881 T12: 0.1725 REMARK 3 T13: 0.0854 T23: 0.1745 REMARK 3 L TENSOR REMARK 3 L11: 5.9615 L22: 2.1309 REMARK 3 L33: 7.1612 L12: 1.6967 REMARK 3 L13: 4.1506 L23: 1.8294 REMARK 3 S TENSOR REMARK 3 S11: -0.0302 S12: 0.9621 S13: -0.0288 REMARK 3 S21: -0.1521 S22: -0.0631 S23: -0.5138 REMARK 3 S31: 0.4540 S32: 1.4352 S33: 0.0726 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN B AND RESID 92:104 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.974 -60.858 48.119 REMARK 3 T TENSOR REMARK 3 T11: 0.8822 T22: -0.1900 REMARK 3 T33: 0.2975 T12: 0.1223 REMARK 3 T13: -0.2477 T23: 0.3272 REMARK 3 L TENSOR REMARK 3 L11: 0.5421 L22: 4.3499 REMARK 3 L33: 1.4085 L12: 0.9884 REMARK 3 L13: -0.7299 L23: -1.5649 REMARK 3 S TENSOR REMARK 3 S11: 0.3411 S12: -0.1524 S13: -0.4642 REMARK 3 S21: -0.3426 S22: 0.1328 S23: -0.2225 REMARK 3 S31: 0.1033 S32: -0.2572 S33: 0.0175 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN B AND RESID 105:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.452 -46.516 70.592 REMARK 3 T TENSOR REMARK 3 T11: 0.5797 T22: 0.7516 REMARK 3 T33: 0.7953 T12: -0.1633 REMARK 3 T13: -0.0842 T23: 0.0972 REMARK 3 L TENSOR REMARK 3 L11: 6.5356 L22: 3.1183 REMARK 3 L33: 1.8396 L12: -1.7774 REMARK 3 L13: -2.7043 L23: -0.6464 REMARK 3 S TENSOR REMARK 3 S11: 0.3098 S12: -0.2979 S13: 0.5719 REMARK 3 S21: 0.6648 S22: 0.1932 S23: -0.2104 REMARK 3 S31: 0.1717 S32: 0.3966 S33: -0.6036 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN B AND RESID 131:152 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.129 -51.535 70.364 REMARK 3 T TENSOR REMARK 3 T11: 0.4539 T22: 0.8820 REMARK 3 T33: 0.7467 T12: -0.0535 REMARK 3 T13: -0.1468 T23: 0.1662 REMARK 3 L TENSOR REMARK 3 L11: 4.3137 L22: 8.3132 REMARK 3 L33: 2.7100 L12: -0.8527 REMARK 3 L13: -1.1465 L23: 4.6530 REMARK 3 S TENSOR REMARK 3 S11: 0.2632 S12: -1.3892 S13: -0.4176 REMARK 3 S21: 1.0026 S22: -0.2182 S23: -0.1794 REMARK 3 S31: 0.9728 S32: -0.0953 S33: -0.0714 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN B AND RESID 153:190 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.288 -52.009 74.778 REMARK 3 T TENSOR REMARK 3 T11: 0.4395 T22: 1.0003 REMARK 3 T33: 0.7155 T12: -0.1503 REMARK 3 T13: -0.0242 T23: 0.1118 REMARK 3 L TENSOR REMARK 3 L11: 6.7739 L22: 6.5875 REMARK 3 L33: 5.0101 L12: -1.0299 REMARK 3 L13: 1.6325 L23: 1.0742 REMARK 3 S TENSOR REMARK 3 S11: 0.5571 S12: -1.3568 S13: -0.1608 REMARK 3 S21: 0.7244 S22: -0.6412 S23: -0.3508 REMARK 3 S31: 1.2557 S32: 0.9519 S33: 0.0964 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN B AND RESID 191:210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.100 -49.991 72.716 REMARK 3 T TENSOR REMARK 3 T11: 0.6551 T22: 1.6297 REMARK 3 T33: 1.2099 T12: -0.2355 REMARK 3 T13: -0.2692 T23: -0.1085 REMARK 3 L TENSOR REMARK 3 L11: 0.8807 L22: 2.8877 REMARK 3 L33: 4.2922 L12: -0.9935 REMARK 3 L13: 1.1875 L23: -3.3854 REMARK 3 S TENSOR REMARK 3 S11: -0.2570 S12: -1.6245 S13: 0.3379 REMARK 3 S21: 0.8194 S22: -1.4437 S23: -0.3459 REMARK 3 S31: -0.6553 S32: -0.0342 S33: 1.6567 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN C AND RESID 414:451 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.119 -55.969 0.517 REMARK 3 T TENSOR REMARK 3 T11: 0.7682 T22: 0.8149 REMARK 3 T33: 0.3830 T12: -0.3241 REMARK 3 T13: 0.2391 T23: -0.0393 REMARK 3 L TENSOR REMARK 3 L11: 5.8553 L22: 7.3077 REMARK 3 L33: 5.4126 L12: -6.1269 REMARK 3 L13: 0.9547 L23: 1.0320 REMARK 3 S TENSOR REMARK 3 S11: 0.2707 S12: 0.0886 S13: 0.0680 REMARK 3 S21: 0.2503 S22: -0.1413 S23: 0.0461 REMARK 3 S31: -0.3580 S32: -0.2997 S33: -0.1631 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN C AND RESID 452:538 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.977 -54.442 -14.078 REMARK 3 T TENSOR REMARK 3 T11: 0.7288 T22: 0.6893 REMARK 3 T33: 0.3607 T12: -0.1224 REMARK 3 T13: 0.0769 T23: -0.0503 REMARK 3 L TENSOR REMARK 3 L11: 6.8527 L22: 1.1126 REMARK 3 L33: 6.5042 L12: -1.6679 REMARK 3 L13: -5.6632 L23: 1.9171 REMARK 3 S TENSOR REMARK 3 S11: 0.0498 S12: 0.7861 S13: -0.1727 REMARK 3 S21: -0.2251 S22: -0.2009 S23: 0.2325 REMARK 3 S31: -0.1123 S32: -0.8568 S33: 0.1413 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: ( CHAIN C AND RESID 539:645 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.191 -54.701 -11.494 REMARK 3 T TENSOR REMARK 3 T11: 0.7078 T22: 0.7121 REMARK 3 T33: 0.3306 T12: -0.1388 REMARK 3 T13: 0.1097 T23: -0.0739 REMARK 3 L TENSOR REMARK 3 L11: 4.4380 L22: 1.9398 REMARK 3 L33: 4.8730 L12: -0.3399 REMARK 3 L13: -2.5218 L23: -0.1926 REMARK 3 S TENSOR REMARK 3 S11: 0.1964 S12: -0.1459 S13: -0.0485 REMARK 3 S21: 0.0491 S22: -0.2504 S23: -0.1697 REMARK 3 S31: -0.1369 S32: 0.8133 S33: 0.0494 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: ( CHAIN D AND RESID 413:521 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.679 -56.462 31.625 REMARK 3 T TENSOR REMARK 3 T11: 0.6537 T22: 0.8183 REMARK 3 T33: 0.3938 T12: -0.0511 REMARK 3 T13: 0.1345 T23: 0.0757 REMARK 3 L TENSOR REMARK 3 L11: 2.5363 L22: 0.1721 REMARK 3 L33: 4.3844 L12: -0.0368 REMARK 3 L13: 3.1957 L23: 0.1872 REMARK 3 S TENSOR REMARK 3 S11: 0.1406 S12: -0.3218 S13: -0.1311 REMARK 3 S21: -0.1058 S22: -0.1365 S23: 0.0414 REMARK 3 S31: 0.5222 S32: -0.5191 S33: -0.0026 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: ( CHAIN D AND RESID 522:645 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.168 -52.784 24.529 REMARK 3 T TENSOR REMARK 3 T11: 0.6294 T22: 0.8695 REMARK 3 T33: 0.2989 T12: -0.0253 REMARK 3 T13: 0.0883 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 3.6876 L22: 1.4347 REMARK 3 L33: 1.5368 L12: 0.4608 REMARK 3 L13: 2.3659 L23: -0.0003 REMARK 3 S TENSOR REMARK 3 S11: -0.1073 S12: 0.3042 S13: 0.0838 REMARK 3 S21: -0.2750 S22: -0.0950 S23: 0.0154 REMARK 3 S31: 0.3239 S32: -0.3489 S33: 0.2014 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: ( CHAIN E AND RESID 1:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.106 -15.800 104.828 REMARK 3 T TENSOR REMARK 3 T11: 0.5288 T22: 1.3735 REMARK 3 T33: 0.6470 T12: 0.2403 REMARK 3 T13: 0.1118 T23: 0.2077 REMARK 3 L TENSOR REMARK 3 L11: 7.8641 L22: 1.7595 REMARK 3 L33: 2.5269 L12: -0.6443 REMARK 3 L13: -3.7160 L23: 1.4517 REMARK 3 S TENSOR REMARK 3 S11: 0.3885 S12: -0.2184 S13: 0.3866 REMARK 3 S21: -0.2081 S22: -0.1004 S23: -0.6473 REMARK 3 S31: -0.1101 S32: 1.2584 S33: -0.3406 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: ( CHAIN E AND RESID 124:214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 81.551 -6.174 80.816 REMARK 3 T TENSOR REMARK 3 T11: 1.0207 T22: 1.3909 REMARK 3 T33: 1.1635 T12: 0.0221 REMARK 3 T13: 0.5063 T23: -0.0031 REMARK 3 L TENSOR REMARK 3 L11: 1.9315 L22: 1.3223 REMARK 3 L33: 1.0099 L12: -0.7993 REMARK 3 L13: 1.1122 L23: 0.1398 REMARK 3 S TENSOR REMARK 3 S11: 0.1135 S12: -0.4594 S13: 0.3939 REMARK 3 S21: -0.0819 S22: 0.2670 S23: -0.3314 REMARK 3 S31: -0.7431 S32: 0.6401 S33: -0.3876 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: ( CHAIN F AND RESID 1:25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.196 -17.575 83.511 REMARK 3 T TENSOR REMARK 3 T11: 0.8671 T22: 1.5764 REMARK 3 T33: 0.5311 T12: 0.3719 REMARK 3 T13: 0.2138 T23: 0.0602 REMARK 3 L TENSOR REMARK 3 L11: 3.3094 L22: 6.2455 REMARK 3 L33: 5.5147 L12: 4.5072 REMARK 3 L13: -3.9815 L23: -5.6569 REMARK 3 S TENSOR REMARK 3 S11: -0.1414 S12: 1.4344 S13: -0.3859 REMARK 3 S21: -0.7901 S22: 0.2693 S23: -0.4551 REMARK 3 S31: 0.2821 S32: -0.4360 S33: 0.1791 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: ( CHAIN F AND RESID 26:92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.681 -10.839 91.041 REMARK 3 T TENSOR REMARK 3 T11: 0.6673 T22: 1.5015 REMARK 3 T33: 0.6145 T12: 0.3854 REMARK 3 T13: 0.2988 T23: 0.2947 REMARK 3 L TENSOR REMARK 3 L11: 1.2406 L22: 0.7840 REMARK 3 L33: 3.2388 L12: 0.0797 REMARK 3 L13: -1.8564 L23: -0.5117 REMARK 3 S TENSOR REMARK 3 S11: 0.5068 S12: 1.3619 S13: 0.0165 REMARK 3 S21: -0.5288 S22: -0.4319 S23: -0.4236 REMARK 3 S31: -0.1063 S32: 0.1165 S33: 0.2501 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: ( CHAIN F AND RESID 93:115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.700 -14.820 85.725 REMARK 3 T TENSOR REMARK 3 T11: 0.7178 T22: 1.7277 REMARK 3 T33: 0.4019 T12: 0.6044 REMARK 3 T13: 0.7842 T23: 0.4980 REMARK 3 L TENSOR REMARK 3 L11: 0.6743 L22: 0.8970 REMARK 3 L33: 2.0316 L12: 0.3249 REMARK 3 L13: -0.5296 L23: -0.5692 REMARK 3 S TENSOR REMARK 3 S11: 0.7350 S12: 0.3657 S13: 0.1792 REMARK 3 S21: -0.7805 S22: 0.0108 S23: -0.3938 REMARK 3 S31: -0.4048 S32: -0.3585 S33: 0.3863 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: ( CHAIN F AND RESID 116:130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 87.548 -13.743 72.676 REMARK 3 T TENSOR REMARK 3 T11: 1.1863 T22: 1.9146 REMARK 3 T33: 1.5394 T12: 0.2169 REMARK 3 T13: 0.6346 T23: 0.5113 REMARK 3 L TENSOR REMARK 3 L11: 1.1502 L22: 1.7310 REMARK 3 L33: 3.6180 L12: -1.0499 REMARK 3 L13: 1.7373 L23: -0.7002 REMARK 3 S TENSOR REMARK 3 S11: -0.2842 S12: -0.5783 S13: -0.6614 REMARK 3 S21: -0.1436 S22: -0.2515 S23: -0.8500 REMARK 3 S31: -0.3429 S32: 1.1232 S33: 0.4517 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: ( CHAIN F AND RESID 131:215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.134 -17.716 68.717 REMARK 3 T TENSOR REMARK 3 T11: 1.1366 T22: 1.7089 REMARK 3 T33: 1.0380 T12: 0.3008 REMARK 3 T13: 0.5200 T23: 0.2074 REMARK 3 L TENSOR REMARK 3 L11: 2.2154 L22: 1.6485 REMARK 3 L33: 2.1085 L12: -0.3659 REMARK 3 L13: 1.0253 L23: -0.7725 REMARK 3 S TENSOR REMARK 3 S11: 0.8179 S12: 0.2828 S13: 0.0031 REMARK 3 S21: -0.1909 S22: -0.2904 S23: -0.1565 REMARK 3 S31: -0.1627 S32: 0.8469 S33: -0.5145 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: ( CHAIN G AND RESID 419:452 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.132 -17.105 115.980 REMARK 3 T TENSOR REMARK 3 T11: 0.3718 T22: 0.6486 REMARK 3 T33: 0.2858 T12: 0.1098 REMARK 3 T13: 0.0385 T23: 0.0416 REMARK 3 L TENSOR REMARK 3 L11: 7.6387 L22: 6.2704 REMARK 3 L33: 4.8266 L12: 1.5025 REMARK 3 L13: 0.1919 L23: -0.2354 REMARK 3 S TENSOR REMARK 3 S11: 0.0431 S12: -0.2659 S13: -0.4004 REMARK 3 S21: -0.0029 S22: -0.1877 S23: -0.3561 REMARK 3 S31: 0.4495 S32: 0.7220 S33: 0.1199 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: ( CHAIN G AND RESID 453:509 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.793 -18.896 132.642 REMARK 3 T TENSOR REMARK 3 T11: 0.5507 T22: 0.9046 REMARK 3 T33: 0.3779 T12: -0.0155 REMARK 3 T13: -0.0149 T23: 0.0995 REMARK 3 L TENSOR REMARK 3 L11: 6.7088 L22: 0.7785 REMARK 3 L33: 3.2195 L12: 0.9488 REMARK 3 L13: -4.6648 L23: -0.7174 REMARK 3 S TENSOR REMARK 3 S11: -0.3640 S12: -0.9177 S13: -0.2639 REMARK 3 S21: 0.2736 S22: -0.1480 S23: -0.2239 REMARK 3 S31: 0.4666 S32: 0.7697 S33: 0.5252 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: ( CHAIN G AND RESID 510:645 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.429 -11.069 126.566 REMARK 3 T TENSOR REMARK 3 T11: 0.3483 T22: 0.5920 REMARK 3 T33: 0.2535 T12: -0.0604 REMARK 3 T13: 0.0069 T23: 0.0144 REMARK 3 L TENSOR REMARK 3 L11: 3.3760 L22: 2.2778 REMARK 3 L33: 3.9363 L12: -0.0670 REMARK 3 L13: -2.1019 L23: 0.2141 REMARK 3 S TENSOR REMARK 3 S11: 0.3406 S12: -0.4360 S13: 0.1673 REMARK 3 S21: 0.0911 S22: -0.2590 S23: -0.0110 REMARK 3 S31: -0.2472 S32: 0.3086 S33: -0.0838 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: ( CHAIN H AND RESID 4:114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -59.387 -56.684 12.999 REMARK 3 T TENSOR REMARK 3 T11: 0.9315 T22: 1.2762 REMARK 3 T33: 0.7032 T12: -0.3696 REMARK 3 T13: 0.3063 T23: -0.2127 REMARK 3 L TENSOR REMARK 3 L11: 7.5334 L22: 1.4591 REMARK 3 L33: 4.6083 L12: 0.3632 REMARK 3 L13: -4.9205 L23: -0.9508 REMARK 3 S TENSOR REMARK 3 S11: 0.1090 S12: -0.0178 S13: 0.1291 REMARK 3 S21: 0.4662 S22: -0.2826 S23: 0.7209 REMARK 3 S31: 0.2496 S32: -0.8942 S33: 0.0841 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: ( CHAIN H AND RESID 115:134 ) REMARK 3 ORIGIN FOR THE GROUP (A): -79.839 -43.678 43.232 REMARK 3 T TENSOR REMARK 3 T11: 1.0719 T22: 1.8307 REMARK 3 T33: 1.1597 T12: 0.1453 REMARK 3 T13: 0.3683 T23: -0.3485 REMARK 3 L TENSOR REMARK 3 L11: 6.7681 L22: 5.3074 REMARK 3 L33: 2.0523 L12: 2.0603 REMARK 3 L13: -2.0841 L23: -3.2030 REMARK 3 S TENSOR REMARK 3 S11: -0.3389 S12: -1.5591 S13: 0.9312 REMARK 3 S21: 1.0830 S22: 0.2208 S23: 0.1915 REMARK 3 S31: 0.9727 S32: 0.9137 S33: 0.0299 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: ( CHAIN H AND RESID 135:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.025 -42.944 36.721 REMARK 3 T TENSOR REMARK 3 T11: 0.8914 T22: 1.5780 REMARK 3 T33: 0.7034 T12: 0.0977 REMARK 3 T13: 0.1817 T23: 0.0576 REMARK 3 L TENSOR REMARK 3 L11: 8.9788 L22: 6.0963 REMARK 3 L33: 0.8192 L12: 2.8412 REMARK 3 L13: -0.6753 L23: -2.1181 REMARK 3 S TENSOR REMARK 3 S11: -1.2364 S12: 0.9065 S13: 0.0561 REMARK 3 S21: -0.3384 S22: 0.8671 S23: 0.5333 REMARK 3 S31: 0.5541 S32: -0.6685 S33: 0.3700 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: ( CHAIN I AND RESID 1:32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.650 -10.618 49.699 REMARK 3 T TENSOR REMARK 3 T11: 0.5891 T22: 1.0712 REMARK 3 T33: 0.4508 T12: 0.3041 REMARK 3 T13: 0.0085 T23: 0.0158 REMARK 3 L TENSOR REMARK 3 L11: 7.2844 L22: 3.0404 REMARK 3 L33: 7.3813 L12: 4.1074 REMARK 3 L13: 5.6346 L23: 1.6355 REMARK 3 S TENSOR REMARK 3 S11: -0.4086 S12: 0.8984 S13: 0.9316 REMARK 3 S21: -0.7597 S22: 0.0391 S23: 0.2644 REMARK 3 S31: -0.9848 S32: 0.0866 S33: 0.3948 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: ( CHAIN I AND RESID 33:111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.136 -17.124 55.957 REMARK 3 T TENSOR REMARK 3 T11: 0.4356 T22: 0.7962 REMARK 3 T33: 0.3823 T12: 0.1419 REMARK 3 T13: -0.0074 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 4.4240 L22: 2.3039 REMARK 3 L33: 5.7735 L12: 0.5874 REMARK 3 L13: 1.9477 L23: 2.2946 REMARK 3 S TENSOR REMARK 3 S11: 0.1852 S12: 0.7930 S13: 0.0566 REMARK 3 S21: -0.2881 S22: -0.1425 S23: 0.1382 REMARK 3 S31: 0.0072 S32: 0.2159 S33: -0.0477 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: ( CHAIN I AND RESID 112:188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.371 -9.023 34.147 REMARK 3 T TENSOR REMARK 3 T11: 0.8460 T22: 1.2288 REMARK 3 T33: 0.5914 T12: 0.2836 REMARK 3 T13: -0.0286 T23: 0.2207 REMARK 3 L TENSOR REMARK 3 L11: 6.8166 L22: 1.1842 REMARK 3 L33: 4.0897 L12: 0.6463 REMARK 3 L13: 0.7690 L23: 0.5283 REMARK 3 S TENSOR REMARK 3 S11: 0.4615 S12: 2.3961 S13: 0.8162 REMARK 3 S21: -0.6575 S22: -0.2093 S23: 0.1702 REMARK 3 S31: -0.5663 S32: 0.1394 S33: -0.2287 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: ( CHAIN I AND RESID 189:214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.391 -2.206 27.966 REMARK 3 T TENSOR REMARK 3 T11: 1.1928 T22: 1.7458 REMARK 3 T33: 0.7999 T12: 0.3678 REMARK 3 T13: 0.3161 T23: 0.3732 REMARK 3 L TENSOR REMARK 3 L11: 8.4427 L22: 4.0782 REMARK 3 L33: 5.3471 L12: -3.7454 REMARK 3 L13: 6.5893 L23: -2.5277 REMARK 3 S TENSOR REMARK 3 S11: 0.6179 S12: 2.4862 S13: 0.7677 REMARK 3 S21: -0.9433 S22: -0.4971 S23: -0.3658 REMARK 3 S31: -1.0415 S32: 0.0880 S33: -0.1218 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: ( CHAIN J AND RESID 1:25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.756 -17.239 68.529 REMARK 3 T TENSOR REMARK 3 T11: 0.4273 T22: 1.0824 REMARK 3 T33: 0.6406 T12: -0.0465 REMARK 3 T13: 0.0192 T23: 0.0096 REMARK 3 L TENSOR REMARK 3 L11: 7.9590 L22: 8.4812 REMARK 3 L33: 9.3706 L12: -6.6793 REMARK 3 L13: 5.8477 L23: -5.5279 REMARK 3 S TENSOR REMARK 3 S11: -0.3063 S12: -0.6805 S13: -0.6015 REMARK 3 S21: -0.1047 S22: 0.7309 S23: 1.1418 REMARK 3 S31: 0.0585 S32: -1.3199 S33: -0.5031 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: ( CHAIN J AND RESID 26:75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.982 -10.948 69.739 REMARK 3 T TENSOR REMARK 3 T11: 0.3998 T22: 0.9853 REMARK 3 T33: 0.4412 T12: 0.1771 REMARK 3 T13: -0.0287 T23: -0.1262 REMARK 3 L TENSOR REMARK 3 L11: 5.3836 L22: 6.7359 REMARK 3 L33: 2.5547 L12: -4.6920 REMARK 3 L13: 2.6341 L23: -1.2639 REMARK 3 S TENSOR REMARK 3 S11: -0.3279 S12: -0.8420 S13: 0.0988 REMARK 3 S21: 0.2990 S22: 0.2901 S23: 0.3946 REMARK 3 S31: -0.1654 S32: -1.2740 S33: -0.0157 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: ( CHAIN J AND RESID 76:104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.102 -14.113 64.894 REMARK 3 T TENSOR REMARK 3 T11: 0.4190 T22: 0.8526 REMARK 3 T33: 0.3645 T12: 0.0441 REMARK 3 T13: -0.0208 T23: -0.0720 REMARK 3 L TENSOR REMARK 3 L11: 4.4787 L22: 6.9025 REMARK 3 L33: 7.6704 L12: -2.9658 REMARK 3 L13: -0.7459 L23: 0.7560 REMARK 3 S TENSOR REMARK 3 S11: -0.2600 S12: -0.5779 S13: 0.0451 REMARK 3 S21: 0.4633 S22: 0.3615 S23: 0.4998 REMARK 3 S31: 0.1090 S32: -0.9868 S33: -0.0043 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: ( CHAIN J AND RESID 105:139 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.310 -12.656 38.783 REMARK 3 T TENSOR REMARK 3 T11: 0.6107 T22: 1.6476 REMARK 3 T33: 0.7881 T12: 0.2410 REMARK 3 T13: -0.1761 T23: -0.1645 REMARK 3 L TENSOR REMARK 3 L11: 0.9607 L22: 1.8747 REMARK 3 L33: 0.3460 L12: -0.6017 REMARK 3 L13: 0.4022 L23: -0.7951 REMARK 3 S TENSOR REMARK 3 S11: 0.3354 S12: 1.1084 S13: -0.8021 REMARK 3 S21: -0.5445 S22: -0.2085 S23: 0.4065 REMARK 3 S31: 0.1049 S32: 0.1587 S33: -0.1452 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: ( CHAIN J AND RESID 140:188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.348 -17.863 41.746 REMARK 3 T TENSOR REMARK 3 T11: 0.6554 T22: 0.9794 REMARK 3 T33: 0.7368 T12: 0.1235 REMARK 3 T13: -0.1855 T23: -0.0112 REMARK 3 L TENSOR REMARK 3 L11: 3.9134 L22: 5.7731 REMARK 3 L33: 3.3056 L12: -2.1786 REMARK 3 L13: -2.7665 L23: 1.3552 REMARK 3 S TENSOR REMARK 3 S11: 0.0083 S12: 0.7737 S13: -0.2952 REMARK 3 S21: -0.4152 S22: -0.1411 S23: 0.9031 REMARK 3 S31: 0.4345 S32: -0.1872 S33: 0.1093 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: ( CHAIN J AND RESID 189:214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -56.116 -19.192 36.821 REMARK 3 T TENSOR REMARK 3 T11: 0.8037 T22: 1.2642 REMARK 3 T33: 1.1508 T12: -0.0369 REMARK 3 T13: -0.3360 T23: -0.1962 REMARK 3 L TENSOR REMARK 3 L11: 2.7554 L22: 2.8448 REMARK 3 L33: 0.0038 L12: -2.0485 REMARK 3 L13: -0.1179 L23: 0.1275 REMARK 3 S TENSOR REMARK 3 S11: 0.0079 S12: 1.1729 S13: -1.1371 REMARK 3 S21: -1.0021 S22: -0.8001 S23: 1.3080 REMARK 3 S31: -0.0156 S32: -0.6461 S33: 0.7357 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: ( CHAIN K AND RESID 414:474 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.490 -18.899 83.959 REMARK 3 T TENSOR REMARK 3 T11: 0.3379 T22: 0.4750 REMARK 3 T33: 0.3815 T12: 0.1259 REMARK 3 T13: 0.0747 T23: -0.1027 REMARK 3 L TENSOR REMARK 3 L11: 4.6045 L22: 0.4367 REMARK 3 L33: 7.6055 L12: 0.0011 REMARK 3 L13: 4.5789 L23: -0.7966 REMARK 3 S TENSOR REMARK 3 S11: 0.2270 S12: 0.4987 S13: -0.4180 REMARK 3 S21: -0.0040 S22: 0.0517 S23: -0.0826 REMARK 3 S31: 0.4569 S32: 0.5239 S33: -0.3099 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: ( CHAIN K AND RESID 475:538 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.099 -9.790 78.681 REMARK 3 T TENSOR REMARK 3 T11: 0.3387 T22: 0.7190 REMARK 3 T33: 0.4478 T12: 0.0541 REMARK 3 T13: 0.0283 T23: 0.0635 REMARK 3 L TENSOR REMARK 3 L11: 2.6793 L22: 5.0378 REMARK 3 L33: 5.2879 L12: -0.3068 REMARK 3 L13: 0.2641 L23: -1.2985 REMARK 3 S TENSOR REMARK 3 S11: -0.1190 S12: 1.2060 S13: 0.0034 REMARK 3 S21: -0.5937 S22: -0.2301 S23: -0.6266 REMARK 3 S31: 0.2474 S32: 0.9432 S33: 0.3364 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: ( CHAIN K AND RESID 539:645 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.391 -13.730 93.401 REMARK 3 T TENSOR REMARK 3 T11: 0.3772 T22: 0.5513 REMARK 3 T33: 0.2487 T12: 0.0879 REMARK 3 T13: 0.0410 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 5.2874 L22: 1.4172 REMARK 3 L33: 3.7918 L12: 0.9365 REMARK 3 L13: 3.4721 L23: -0.0292 REMARK 3 S TENSOR REMARK 3 S11: 0.1532 S12: -0.3215 S13: -0.0070 REMARK 3 S21: 0.0851 S22: -0.1300 S23: -0.0049 REMARK 3 S31: 0.0165 S32: 0.1994 S33: -0.0325 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.546 -59.777 34.802 REMARK 3 T TENSOR REMARK 3 T11: 1.2097 T22: 1.3916 REMARK 3 T33: 0.6585 T12: -0.0217 REMARK 3 T13: 0.3622 T23: 0.1969 REMARK 3 L TENSOR REMARK 3 L11: 2.1283 L22: 2.3121 REMARK 3 L33: 8.3040 L12: -1.8280 REMARK 3 L13: -2.6920 L23: 4.2117 REMARK 3 S TENSOR REMARK 3 S11: -0.1781 S12: -1.0716 S13: -0.5799 REMARK 3 S21: 1.3097 S22: 0.1261 S23: 0.3453 REMARK 3 S31: 1.1603 S32: -0.6669 S33: 0.2709 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: ( CHAIN L AND RESID 19:69 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.962 -53.483 25.775 REMARK 3 T TENSOR REMARK 3 T11: 0.9773 T22: 1.3668 REMARK 3 T33: 0.6152 T12: -0.2724 REMARK 3 T13: 0.3424 T23: -0.0836 REMARK 3 L TENSOR REMARK 3 L11: 3.4950 L22: 2.7106 REMARK 3 L33: 6.3381 L12: -2.6869 REMARK 3 L13: -2.8075 L23: 3.6505 REMARK 3 S TENSOR REMARK 3 S11: -0.0040 S12: -1.5841 S13: -0.2854 REMARK 3 S21: 0.4343 S22: 0.1550 S23: 0.0670 REMARK 3 S31: 0.1884 S32: 0.7882 S33: -0.0080 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: ( CHAIN L AND RESID 70:92 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.598 -53.579 30.521 REMARK 3 T TENSOR REMARK 3 T11: 1.2343 T22: 1.5131 REMARK 3 T33: 0.6445 T12: -0.2966 REMARK 3 T13: 0.3820 T23: 0.0851 REMARK 3 L TENSOR REMARK 3 L11: 1.9534 L22: 2.4025 REMARK 3 L33: 8.2052 L12: -1.5013 REMARK 3 L13: -0.3798 L23: 3.4308 REMARK 3 S TENSOR REMARK 3 S11: -0.6008 S12: -0.9604 S13: 0.0677 REMARK 3 S21: -0.0602 S22: 0.3931 S23: -0.0569 REMARK 3 S31: -0.7496 S32: 0.2386 S33: 0.0807 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: ( CHAIN L AND RESID 93:109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.083 -59.235 25.974 REMARK 3 T TENSOR REMARK 3 T11: 1.0296 T22: 1.2467 REMARK 3 T33: 0.5936 T12: -0.1353 REMARK 3 T13: 0.5526 T23: 0.0961 REMARK 3 L TENSOR REMARK 3 L11: 1.2098 L22: 5.6422 REMARK 3 L33: 9.0746 L12: -0.7728 REMARK 3 L13: 1.3871 L23: 5.3003 REMARK 3 S TENSOR REMARK 3 S11: -1.0091 S12: -0.8424 S13: -0.6637 REMARK 3 S21: 0.4047 S22: 0.3130 S23: -0.2362 REMARK 3 S31: 0.9895 S32: 0.4631 S33: 0.5043 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: ( CHAIN L AND RESID 110:154 ) REMARK 3 ORIGIN FOR THE GROUP (A): -74.075 -50.207 50.381 REMARK 3 T TENSOR REMARK 3 T11: 1.1571 T22: 1.3629 REMARK 3 T33: 0.8690 T12: 0.1081 REMARK 3 T13: 0.4161 T23: 0.1045 REMARK 3 L TENSOR REMARK 3 L11: 2.4406 L22: 2.0731 REMARK 3 L33: 3.8101 L12: 0.2503 REMARK 3 L13: 1.8305 L23: 0.4943 REMARK 3 S TENSOR REMARK 3 S11: -0.8223 S12: -0.8694 S13: -0.8081 REMARK 3 S21: 0.4057 S22: 0.1084 S23: 0.6410 REMARK 3 S31: 0.6375 S32: -0.9831 S33: 0.6570 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: ( CHAIN L AND RESID 155:175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -67.410 -53.424 46.153 REMARK 3 T TENSOR REMARK 3 T11: 1.2724 T22: 1.1840 REMARK 3 T33: 0.6781 T12: 0.0479 REMARK 3 T13: 0.4387 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 4.5339 L22: 4.4439 REMARK 3 L33: 5.7097 L12: 2.6473 REMARK 3 L13: 0.3255 L23: -3.7252 REMARK 3 S TENSOR REMARK 3 S11: 0.4707 S12: 0.0232 S13: -0.2508 REMARK 3 S21: 1.0086 S22: -0.3386 S23: 0.2870 REMARK 3 S31: -0.3903 S32: -0.6951 S33: -0.1385 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: ( CHAIN L AND RESID 176:190 ) REMARK 3 ORIGIN FOR THE GROUP (A): -84.875 -53.824 48.322 REMARK 3 T TENSOR REMARK 3 T11: 1.4069 T22: 1.8026 REMARK 3 T33: 1.0695 T12: -0.1635 REMARK 3 T13: 0.4787 T23: 0.0850 REMARK 3 L TENSOR REMARK 3 L11: 0.9749 L22: 8.5322 REMARK 3 L33: 5.6496 L12: -0.1728 REMARK 3 L13: 2.2958 L23: 0.9922 REMARK 3 S TENSOR REMARK 3 S11: -1.3036 S12: -3.3285 S13: -1.4125 REMARK 3 S21: 0.4738 S22: -0.1573 S23: 1.9436 REMARK 3 S31: 1.8692 S32: -0.9221 S33: 1.3857 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: ( CHAIN L AND RESID 191:200 ) REMARK 3 ORIGIN FOR THE GROUP (A): -78.070 -52.895 57.188 REMARK 3 T TENSOR REMARK 3 T11: 1.0330 T22: 1.5186 REMARK 3 T33: 0.7560 T12: 0.0953 REMARK 3 T13: 0.3359 T23: 0.3165 REMARK 3 L TENSOR REMARK 3 L11: 4.5938 L22: 4.0473 REMARK 3 L33: 2.1399 L12: 2.6870 REMARK 3 L13: 3.0707 L23: 2.2722 REMARK 3 S TENSOR REMARK 3 S11: -0.7762 S12: -1.8499 S13: -0.4510 REMARK 3 S21: 0.7370 S22: 0.1411 S23: 1.4511 REMARK 3 S31: 1.6185 S32: -0.8553 S33: 0.5397 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: ( CHAIN L AND RESID 201:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -73.626 -49.260 59.397 REMARK 3 T TENSOR REMARK 3 T11: 1.2495 T22: 1.6121 REMARK 3 T33: 1.0671 T12: 0.1916 REMARK 3 T13: 0.4293 T23: 0.3139 REMARK 3 L TENSOR REMARK 3 L11: 1.0943 L22: 1.6291 REMARK 3 L33: 4.3476 L12: 0.0476 REMARK 3 L13: 1.9226 L23: -1.1725 REMARK 3 S TENSOR REMARK 3 S11: -0.4215 S12: -2.9574 S13: -0.8378 REMARK 3 S21: 0.2293 S22: 0.7127 S23: 0.4123 REMARK 3 S31: -0.2388 S32: -1.6495 S33: -0.3155 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 9O3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000291845. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.7 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112353 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680 REMARK 200 RESOLUTION RANGE LOW (A) : 82.210 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.14400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 1.77200 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 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM SODIUM TARTRATE REMARK 280 TETRAHYDRATE, 20% PEG3,350, PH 7.4, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 116.82000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.26500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.82000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.26500 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, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8920 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, P, Q, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L, M, N, O REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, S, T, U, V REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, W, X, Y 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 GLN A 1 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 THR A 219 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 REMARK 465 HIS A 223 REMARK 465 HIS A 224 REMARK 465 HIS A 225 REMARK 465 PHE B 211 REMARK 465 ASN B 212 REMARK 465 ARG B 213 REMARK 465 GLY B 214 REMARK 465 GLU B 215 REMARK 465 CYS B 216 REMARK 465 SER C 384 REMARK 465 THR C 385 REMARK 465 HIS C 386 REMARK 465 VAL C 387 REMARK 465 THR C 388 REMARK 465 GLY C 389 REMARK 465 GLY C 390 REMARK 465 THR C 391 REMARK 465 ALA C 392 REMARK 465 SER C 393 REMARK 465 HIS C 394 REMARK 465 THR C 395 REMARK 465 THR C 396 REMARK 465 ARG C 397 REMARK 465 HIS C 398 REMARK 465 PHE C 399 REMARK 465 ALA C 400 REMARK 465 SER C 401 REMARK 465 LEU C 402 REMARK 465 PHE C 403 REMARK 465 SER C 404 REMARK 465 SER C 405 REMARK 465 GLY C 406 REMARK 465 ALA C 407 REMARK 465 SER C 408 REMARK 465 GLN C 409 REMARK 465 ARG C 410 REMARK 465 VAL C 411 REMARK 465 GLN C 412 REMARK 465 LEU C 413 REMARK 465 SER D 384 REMARK 465 THR D 385 REMARK 465 HIS D 386 REMARK 465 VAL D 387 REMARK 465 THR D 388 REMARK 465 GLY D 389 REMARK 465 GLY D 390 REMARK 465 THR D 391 REMARK 465 ALA D 392 REMARK 465 SER D 393 REMARK 465 HIS D 394 REMARK 465 THR D 395 REMARK 465 THR D 396 REMARK 465 ARG D 397 REMARK 465 HIS D 398 REMARK 465 PHE D 399 REMARK 465 ALA D 400 REMARK 465 SER D 401 REMARK 465 LEU D 402 REMARK 465 PHE D 403 REMARK 465 SER D 404 REMARK 465 SER D 405 REMARK 465 GLY D 406 REMARK 465 ALA D 407 REMARK 465 SER D 408 REMARK 465 GLN D 409 REMARK 465 ARG D 410 REMARK 465 VAL D 411 REMARK 465 GLN D 412 REMARK 465 SER E 128 REMARK 465 LYS E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 SER E 215 REMARK 465 CYS E 216 REMARK 465 ASP E 217 REMARK 465 LYS E 218 REMARK 465 THR E 219 REMARK 465 HIS E 220 REMARK 465 HIS E 221 REMARK 465 HIS E 222 REMARK 465 HIS E 223 REMARK 465 HIS E 224 REMARK 465 HIS E 225 REMARK 465 CYS F 216 REMARK 465 SER G 384 REMARK 465 THR G 385 REMARK 465 HIS G 386 REMARK 465 VAL G 387 REMARK 465 THR G 388 REMARK 465 GLY G 389 REMARK 465 GLY G 390 REMARK 465 THR G 391 REMARK 465 ALA G 392 REMARK 465 SER G 393 REMARK 465 HIS G 394 REMARK 465 THR G 395 REMARK 465 THR G 396 REMARK 465 ARG G 397 REMARK 465 HIS G 398 REMARK 465 PHE G 399 REMARK 465 ALA G 400 REMARK 465 SER G 401 REMARK 465 LEU G 402 REMARK 465 PHE G 403 REMARK 465 SER G 404 REMARK 465 SER G 405 REMARK 465 GLY G 406 REMARK 465 ALA G 407 REMARK 465 SER G 408 REMARK 465 GLN G 409 REMARK 465 ARG G 410 REMARK 465 VAL G 411 REMARK 465 GLN G 412 REMARK 465 LEU G 413 REMARK 465 ILE G 414 REMARK 465 ASN G 415 REMARK 465 THR G 416 REMARK 465 ASN G 417 REMARK 465 GLY G 418 REMARK 465 GLN H 1 REMARK 465 VAL H 2 REMARK 465 GLN H 3 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 SER I 128 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 HIS I 223 REMARK 465 HIS I 224 REMARK 465 HIS I 225 REMARK 465 GLU J 215 REMARK 465 CYS J 216 REMARK 465 SER K 384 REMARK 465 THR K 385 REMARK 465 HIS K 386 REMARK 465 VAL K 387 REMARK 465 THR K 388 REMARK 465 GLY K 389 REMARK 465 GLY K 390 REMARK 465 THR K 391 REMARK 465 ALA K 392 REMARK 465 SER K 393 REMARK 465 HIS K 394 REMARK 465 THR K 395 REMARK 465 THR K 396 REMARK 465 ARG K 397 REMARK 465 HIS K 398 REMARK 465 PHE K 399 REMARK 465 ALA K 400 REMARK 465 SER K 401 REMARK 465 LEU K 402 REMARK 465 PHE K 403 REMARK 465 SER K 404 REMARK 465 SER K 405 REMARK 465 GLY K 406 REMARK 465 ALA K 407 REMARK 465 SER K 408 REMARK 465 GLN K 409 REMARK 465 ARG K 410 REMARK 465 VAL K 411 REMARK 465 GLN K 412 REMARK 465 LEU K 413 REMARK 465 GLY L 214 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE C 414 CG1 CG2 CD1 REMARK 470 LYS E 214 CG 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 HE22 GLN L 6 O TYR L 86 1.42 REMARK 500 HH22 ARG G 543 O PRO G 567 1.46 REMARK 500 O HIS G 445 H PHE G 447 1.46 REMARK 500 HH22 ARG C 543 O PRO C 567 1.53 REMARK 500 O THR K 473 H ASN K 570 1.57 REMARK 500 O ASP B 82 HH TYR B 86 1.57 REMARK 500 HH TYR D 474 O LYS D 596 1.58 REMARK 500 HH22 ARG I 100G OE1 GLU J 55 1.58 REMARK 500 HH21 ARG E 38 OH TYR E 90 1.58 REMARK 500 O THR C 473 H ASN C 570 1.60 REMARK 500 HG1 THR D 583 O TRP D 602 1.60 REMARK 500 OG1 THR H 116 OG SER H 203 1.82 REMARK 500 O HIS G 445 N PHE G 447 1.88 REMARK 500 NH2 ARG E 38 OH TYR E 90 1.89 REMARK 500 OE1 GLU J 189 NH1 ARG J 213 1.90 REMARK 500 ND2 ASN C 576 O5 NAG C 704 2.05 REMARK 500 O THR A 28 OG SER A 32 2.07 REMARK 500 OD1 ASN K 430 OG SER K 432 2.10 REMARK 500 CG ASN C 576 C1 NAG C 704 2.18 REMARK 500 O THR I 28 OG SER I 32 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 OE1 GLN I 192 NE2 GLN L 102 1565 2.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS A 92 CB CYS A 92 SG -0.139 REMARK 500 CYS K 644 CB CYS K 644 SG -0.124 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS K 607 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 7 -164.87 -75.44 REMARK 500 ALA A 9 -91.96 65.56 REMARK 500 GLU A 10 75.46 46.22 REMARK 500 SER A 16 -162.65 -77.59 REMARK 500 ASP A 27 161.05 64.83 REMARK 500 GLN A 64 129.06 -37.82 REMARK 500 ASP A 101 -146.79 -152.62 REMARK 500 SER A 113 -6.42 77.57 REMARK 500 SER A 130 -64.00 -95.46 REMARK 500 ASN A 199 114.32 -161.01 REMARK 500 SER B 30 -136.19 53.86 REMARK 500 VAL B 51 -46.45 82.32 REMARK 500 SER B 67 159.56 178.79 REMARK 500 ALA B 84 172.71 179.79 REMARK 500 GLN B 102 -37.58 -38.14 REMARK 500 PRO B 143 -161.88 -72.58 REMARK 500 ASN B 154 -7.76 75.03 REMARK 500 LYS B 192 -34.44 -131.76 REMARK 500 ASN C 415 -174.02 55.46 REMARK 500 ASN C 428 40.34 -96.23 REMARK 500 ASP C 431 57.87 -101.44 REMARK 500 ASN C 448 80.47 53.20 REMARK 500 ALA C 449 32.87 -94.31 REMARK 500 GLN C 467 140.52 -38.56 REMARK 500 SER C 480 150.13 -44.24 REMARK 500 PRO C 484 44.46 -85.66 REMARK 500 ASN C 540 127.07 -39.89 REMARK 500 ASN C 556 -86.08 -86.17 REMARK 500 SER C 557 -31.91 -152.39 REMARK 500 PRO C 590 -6.88 -56.95 REMARK 500 ALA C 592 57.53 -93.79 REMARK 500 SER C 599 28.44 -141.48 REMARK 500 PRO C 605 -2.40 -58.25 REMARK 500 ASN D 430 -73.95 -96.82 REMARK 500 SER D 450 94.07 -69.57 REMARK 500 TRP D 469 -168.18 -160.29 REMARK 500 THR D 510 -176.31 55.08 REMARK 500 ASN D 576 13.78 50.26 REMARK 500 SER D 599 20.47 -141.23 REMARK 500 THR E 28 115.20 -164.32 REMARK 500 PRO E 41 109.32 -57.79 REMARK 500 SER E 100A 58.03 38.09 REMARK 500 PRO E 147 -164.53 -78.51 REMARK 500 HIS E 164 58.80 -140.70 REMARK 500 ALA E 168 172.79 -59.64 REMARK 500 PRO E 185 155.20 -45.82 REMARK 500 SER E 187 59.57 -98.75 REMARK 500 THR E 191 60.57 -100.39 REMARK 500 SER F 30 -122.62 62.08 REMARK 500 VAL F 51 -52.95 70.42 REMARK 500 REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG G 460 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9O3D A 1 225 PDB 9O3D 9O3D 1 225 DBREF 9O3D B 1 216 PDB 9O3D 9O3D 1 216 DBREF 9O3D C 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 9O3D D 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 9O3D E 1 225 PDB 9O3D 9O3D 1 225 DBREF 9O3D F 1 216 PDB 9O3D 9O3D 1 216 DBREF 9O3D G 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 9O3D H 1 225 PDB 9O3D 9O3D 1 225 DBREF 9O3D I 1 225 PDB 9O3D 9O3D 1 225 DBREF 9O3D J 1 216 PDB 9O3D 9O3D 1 216 DBREF 9O3D K 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 9O3D L 1 216 PDB 9O3D 9O3D 1 216 SEQRES 1 A 237 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 237 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 237 ASP THR PHE SER SER SER ALA ILE SER TRP VAL ARG GLN SEQRES 4 A 237 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY SER ILE SEQRES 5 A 237 PRO ILE PHE GLY ALA THR LYS TYR ALA GLN LYS PHE GLN SEQRES 6 A 237 GLY ARG VAL THR ILE THR THR ASP LYS SER THR SER THR SEQRES 7 A 237 ALA TYR MET GLU LEU SER SER LEU ARG PHE GLU ASP THR SEQRES 8 A 237 ALA VAL TYR TYR CYS ALA ARG ALA SER ILE VAL ASN ILE SEQRES 9 A 237 SER GLY PHE VAL ARG PHE ARG PHE ASP SER TRP GLY GLN SEQRES 10 A 237 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 237 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 237 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 237 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 237 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 237 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 237 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 237 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 237 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS HIS SEQRES 19 A 237 HIS HIS HIS SEQRES 1 B 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 B 216 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP VAL SER SEQRES 5 B 216 ASN LEU GLU ILE GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 216 GLY SER GLY THR GLU PHE THR LEU THR ILE ASN SER LEU SEQRES 7 B 216 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN HIS TYR SEQRES 8 B 216 ASP ASP VAL PRO PRO VAL TYR THR PHE GLY GLN GLY THR SEQRES 9 B 216 SER LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 B 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 B 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 B 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 B 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 B 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 B 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 B 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 B 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 262 SER THR HIS VAL THR GLY GLY THR ALA SER HIS THR THR SEQRES 2 C 262 ARG HIS PHE ALA SER LEU PHE SER SER GLY ALA SER GLN SEQRES 3 C 262 ARG VAL GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE SEQRES 4 C 262 ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU HIS THR SEQRES 5 C 262 GLY PHE LEU ALA ALA LEU PHE TYR THR HIS LYS PHE ASN SEQRES 6 C 262 ALA SER GLY CYS PRO GLU ARG MET ALA HIS CYS ARG PRO SEQRES 7 C 262 ILE ASP GLU PHE ALA GLN GLY TRP GLY PRO ILE THR TYR SEQRES 8 C 262 ALA GLU GLY HIS GLY SER ASP GLN ARG PRO TYR CYS TRP SEQRES 9 C 262 HIS TYR ALA PRO ARG GLN CYS GLY THR ILE PRO ALA SER SEQRES 10 C 262 GLN VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SER PRO SEQRES 11 C 262 VAL VAL VAL GLY THR THR ASP ARG PHE GLY ALA PRO THR SEQRES 12 C 262 TYR THR TRP GLY GLU ASN GLU THR ASP VAL LEU ILE LEU SEQRES 13 C 262 ASN ASN THR ARG PRO PRO GLN GLY ASN TRP PHE GLY CYS SEQRES 14 C 262 THR TRP MET ASN SER THR GLY PHE THR LYS THR CYS GLY SEQRES 15 C 262 GLY PRO PRO CYS ASN ILE GLY GLY VAL GLY ASN ASN THR SEQRES 16 C 262 LEU THR CYS PRO THR ASP CYS PHE ARG LYS HIS PRO GLU SEQRES 17 C 262 ALA THR TYR THR LYS CYS GLY SER GLY PRO TRP LEU THR SEQRES 18 C 262 PRO ARG CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS SEQRES 19 C 262 TYR PRO CYS THR VAL ASN PHE THR ILE PHE LYS VAL ARG SEQRES 20 C 262 MET TYR VAL GLY GLY VAL GLU HIS ARG LEU ASN ALA ALA SEQRES 21 C 262 CYS ASN SEQRES 1 D 262 SER THR HIS VAL THR GLY GLY THR ALA SER HIS THR THR SEQRES 2 D 262 ARG HIS PHE ALA SER LEU PHE SER SER GLY ALA SER GLN SEQRES 3 D 262 ARG VAL GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE SEQRES 4 D 262 ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU HIS THR SEQRES 5 D 262 GLY PHE LEU ALA ALA LEU PHE TYR THR HIS LYS PHE ASN SEQRES 6 D 262 ALA SER GLY CYS PRO GLU ARG MET ALA HIS CYS ARG PRO SEQRES 7 D 262 ILE ASP GLU PHE ALA GLN GLY TRP GLY PRO ILE THR TYR SEQRES 8 D 262 ALA GLU GLY HIS GLY SER ASP GLN ARG PRO TYR CYS TRP SEQRES 9 D 262 HIS TYR ALA PRO ARG GLN CYS GLY THR ILE PRO ALA SER SEQRES 10 D 262 GLN VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SER PRO SEQRES 11 D 262 VAL VAL VAL GLY THR THR ASP ARG PHE GLY ALA PRO THR SEQRES 12 D 262 TYR THR TRP GLY GLU ASN GLU THR ASP VAL LEU ILE LEU SEQRES 13 D 262 ASN ASN THR ARG PRO PRO GLN GLY ASN TRP PHE GLY CYS SEQRES 14 D 262 THR TRP MET ASN SER THR GLY PHE THR LYS THR CYS GLY SEQRES 15 D 262 GLY PRO PRO CYS ASN ILE GLY GLY VAL GLY ASN ASN THR SEQRES 16 D 262 LEU THR CYS PRO THR ASP CYS PHE ARG LYS HIS PRO GLU SEQRES 17 D 262 ALA THR TYR THR LYS CYS GLY SER GLY PRO TRP LEU THR SEQRES 18 D 262 PRO ARG CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS SEQRES 19 D 262 TYR PRO CYS THR VAL ASN PHE THR ILE PHE LYS VAL ARG SEQRES 20 D 262 MET TYR VAL GLY GLY VAL GLU HIS ARG LEU ASN ALA ALA SEQRES 21 D 262 CYS ASN SEQRES 1 E 237 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 237 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 E 237 ASP THR PHE SER SER SER ALA ILE SER TRP VAL ARG GLN SEQRES 4 E 237 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY SER ILE SEQRES 5 E 237 PRO ILE PHE GLY ALA THR LYS TYR ALA GLN LYS PHE GLN SEQRES 6 E 237 GLY ARG VAL THR ILE THR THR ASP LYS SER THR SER THR SEQRES 7 E 237 ALA TYR MET GLU LEU SER SER LEU ARG PHE GLU ASP THR SEQRES 8 E 237 ALA VAL TYR TYR CYS ALA ARG ALA SER ILE VAL ASN ILE SEQRES 9 E 237 SER GLY PHE VAL ARG PHE ARG PHE ASP SER TRP GLY GLN SEQRES 10 E 237 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 E 237 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 E 237 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 E 237 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 E 237 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 E 237 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 E 237 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 E 237 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 E 237 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS HIS SEQRES 19 E 237 HIS HIS HIS SEQRES 1 F 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 F 216 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 F 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP VAL SER SEQRES 5 F 216 ASN LEU GLU ILE GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 216 GLY SER GLY THR GLU PHE THR LEU THR ILE ASN SER LEU SEQRES 7 F 216 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN HIS TYR SEQRES 8 F 216 ASP ASP VAL PRO PRO VAL TYR THR PHE GLY GLN GLY THR SEQRES 9 F 216 SER LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 F 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 F 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 F 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 F 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 F 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 F 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 F 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 F 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 262 SER THR HIS VAL THR GLY GLY THR ALA SER HIS THR THR SEQRES 2 G 262 ARG HIS PHE ALA SER LEU PHE SER SER GLY ALA SER GLN SEQRES 3 G 262 ARG VAL GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE SEQRES 4 G 262 ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU HIS THR SEQRES 5 G 262 GLY PHE LEU ALA ALA LEU PHE TYR THR HIS LYS PHE ASN SEQRES 6 G 262 ALA SER GLY CYS PRO GLU ARG MET ALA HIS CYS ARG PRO SEQRES 7 G 262 ILE ASP GLU PHE ALA GLN GLY TRP GLY PRO ILE THR TYR SEQRES 8 G 262 ALA GLU GLY HIS GLY SER ASP GLN ARG PRO TYR CYS TRP SEQRES 9 G 262 HIS TYR ALA PRO ARG GLN CYS GLY THR ILE PRO ALA SER SEQRES 10 G 262 GLN VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SER PRO SEQRES 11 G 262 VAL VAL VAL GLY THR THR ASP ARG PHE GLY ALA PRO THR SEQRES 12 G 262 TYR THR TRP GLY GLU ASN GLU THR ASP VAL LEU ILE LEU SEQRES 13 G 262 ASN ASN THR ARG PRO PRO GLN GLY ASN TRP PHE GLY CYS SEQRES 14 G 262 THR TRP MET ASN SER THR GLY PHE THR LYS THR CYS GLY SEQRES 15 G 262 GLY PRO PRO CYS ASN ILE GLY GLY VAL GLY ASN ASN THR SEQRES 16 G 262 LEU THR CYS PRO THR ASP CYS PHE ARG LYS HIS PRO GLU SEQRES 17 G 262 ALA THR TYR THR LYS CYS GLY SER GLY PRO TRP LEU THR SEQRES 18 G 262 PRO ARG CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS SEQRES 19 G 262 TYR PRO CYS THR VAL ASN PHE THR ILE PHE LYS VAL ARG SEQRES 20 G 262 MET TYR VAL GLY GLY VAL GLU HIS ARG LEU ASN ALA ALA SEQRES 21 G 262 CYS ASN SEQRES 1 H 237 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 237 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 237 ASP THR PHE SER SER SER ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 237 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY SER ILE SEQRES 5 H 237 PRO ILE PHE GLY ALA THR LYS TYR ALA GLN LYS PHE GLN SEQRES 6 H 237 GLY ARG VAL THR ILE THR THR ASP LYS SER THR SER THR SEQRES 7 H 237 ALA TYR MET GLU LEU SER SER LEU ARG PHE GLU ASP THR SEQRES 8 H 237 ALA VAL TYR TYR CYS ALA ARG ALA SER ILE VAL ASN ILE SEQRES 9 H 237 SER GLY PHE VAL ARG PHE ARG PHE ASP SER TRP GLY GLN SEQRES 10 H 237 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 237 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 237 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 237 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 237 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 237 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 237 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 237 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 237 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS HIS SEQRES 19 H 237 HIS HIS HIS SEQRES 1 I 237 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 237 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 237 ASP THR PHE SER SER SER ALA ILE SER TRP VAL ARG GLN SEQRES 4 I 237 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY SER ILE SEQRES 5 I 237 PRO ILE PHE GLY ALA THR LYS TYR ALA GLN LYS PHE GLN SEQRES 6 I 237 GLY ARG VAL THR ILE THR THR ASP LYS SER THR SER THR SEQRES 7 I 237 ALA TYR MET GLU LEU SER SER LEU ARG PHE GLU ASP THR SEQRES 8 I 237 ALA VAL TYR TYR CYS ALA ARG ALA SER ILE VAL ASN ILE SEQRES 9 I 237 SER GLY PHE VAL ARG PHE ARG PHE ASP SER TRP GLY GLN SEQRES 10 I 237 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 I 237 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 I 237 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 I 237 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 I 237 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 I 237 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 I 237 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 I 237 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 I 237 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS HIS SEQRES 19 I 237 HIS HIS HIS SEQRES 1 J 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 J 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 J 216 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 J 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP VAL SER SEQRES 5 J 216 ASN LEU GLU ILE GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 J 216 GLY SER GLY THR GLU PHE THR LEU THR ILE ASN SER LEU SEQRES 7 J 216 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN HIS TYR SEQRES 8 J 216 ASP ASP VAL PRO PRO VAL TYR THR PHE GLY GLN GLY THR SEQRES 9 J 216 SER LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 J 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 J 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 J 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 J 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 J 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 J 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 J 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 J 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 262 SER THR HIS VAL THR GLY GLY THR ALA SER HIS THR THR SEQRES 2 K 262 ARG HIS PHE ALA SER LEU PHE SER SER GLY ALA SER GLN SEQRES 3 K 262 ARG VAL GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE SEQRES 4 K 262 ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU HIS THR SEQRES 5 K 262 GLY PHE LEU ALA ALA LEU PHE TYR THR HIS LYS PHE ASN SEQRES 6 K 262 ALA SER GLY CYS PRO GLU ARG MET ALA HIS CYS ARG PRO SEQRES 7 K 262 ILE ASP GLU PHE ALA GLN GLY TRP GLY PRO ILE THR TYR SEQRES 8 K 262 ALA GLU GLY HIS GLY SER ASP GLN ARG PRO TYR CYS TRP SEQRES 9 K 262 HIS TYR ALA PRO ARG GLN CYS GLY THR ILE PRO ALA SER SEQRES 10 K 262 GLN VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SER PRO SEQRES 11 K 262 VAL VAL VAL GLY THR THR ASP ARG PHE GLY ALA PRO THR SEQRES 12 K 262 TYR THR TRP GLY GLU ASN GLU THR ASP VAL LEU ILE LEU SEQRES 13 K 262 ASN ASN THR ARG PRO PRO GLN GLY ASN TRP PHE GLY CYS SEQRES 14 K 262 THR TRP MET ASN SER THR GLY PHE THR LYS THR CYS GLY SEQRES 15 K 262 GLY PRO PRO CYS ASN ILE GLY GLY VAL GLY ASN ASN THR SEQRES 16 K 262 LEU THR CYS PRO THR ASP CYS PHE ARG LYS HIS PRO GLU SEQRES 17 K 262 ALA THR TYR THR LYS CYS GLY SER GLY PRO TRP LEU THR SEQRES 18 K 262 PRO ARG CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS SEQRES 19 K 262 TYR PRO CYS THR VAL ASN PHE THR ILE PHE LYS VAL ARG SEQRES 20 K 262 MET TYR VAL GLY GLY VAL GLU HIS ARG LEU ASN ALA ALA SEQRES 21 K 262 CYS ASN SEQRES 1 L 216 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 216 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP VAL SER SEQRES 5 L 216 ASN LEU GLU ILE GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 216 GLY SER GLY THR GLU PHE THR LEU THR ILE ASN SER LEU SEQRES 7 L 216 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN HIS TYR SEQRES 8 L 216 ASP ASP VAL PRO PRO VAL TYR THR PHE GLY GLN GLY THR SEQRES 9 L 216 SER LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 L 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 216 LYS SER PHE ASN ARG GLY GLU CYS HET NAG M 1 26 HET NAG M 2 27 HET NAG N 1 26 HET NAG N 2 26 HET BMA N 3 11 HET NAG O 1 26 HET NAG O 2 26 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET MAN O 6 11 HET NAG P 1 26 HET NAG P 2 27 HET NAG Q 1 26 HET NAG Q 2 26 HET BMA Q 3 11 HET MAN Q 4 11 HET NAG R 1 26 HET NAG R 2 26 HET BMA R 3 11 HET NAG S 1 26 HET NAG S 2 27 HET NAG T 1 26 HET NAG T 2 26 HET BMA T 3 19 HET MAN T 4 21 HET NAG U 1 26 HET NAG U 2 26 HET BMA U 3 21 HET NAG V 1 26 HET NAG V 2 26 HET NAG W 1 26 HET NAG W 2 27 HET NAG X 1 26 HET NAG X 2 27 HET NAG Y 1 26 HET NAG Y 2 26 HET BMA Y 3 19 HET MAN Y 4 20 HET MAN Y 5 21 HET MAN Y 6 21 HET GOL C 701 14 HET NAG C 702 27 HET NAG C 703 27 HET NAG C 704 27 HET NAG C 705 27 HET GOL D 701 14 HET NAG D 702 27 HET NAG D 703 27 HET NAG D 704 14 HET NAG D 705 14 HET NAG D 706 27 HET GOL G 701 14 HET NAG G 702 27 HET NAG G 703 27 HET GOL K 701 14 HET GOL K 702 14 HET NAG K 703 27 HET NAG K 704 27 HET NAG K 705 27 HET NAG K 706 27 HET NAG K 707 27 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GOL GLYCEROL 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 HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 13 NAG 42(C8 H15 N O6) FORMUL 14 BMA 7(C6 H12 O6) FORMUL 15 MAN 8(C6 H12 O6) FORMUL 26 GOL 5(C3 H8 O3) FORMUL 47 HOH *39(H2 O) HELIX 1 AA1 ARG A 83 THR A 87 5 5 HELIX 2 AA2 SER A 156 ALA A 158 5 3 HELIX 3 AA3 SER A 187 LEU A 189 5 3 HELIX 4 AA4 LYS A 201 ASN A 204 5 4 HELIX 5 AA5 GLN B 79 LEU B 83 5 5 HELIX 6 AA6 SER B 123 SER B 129 1 7 HELIX 7 AA7 LYS B 185 HIS B 191 1 7 HELIX 8 AA8 HIS C 421 THR C 425 5 5 HELIX 9 AA9 GLY C 436 TYR C 443 1 8 HELIX 10 AB1 THR C 444 PHE C 447 5 4 HELIX 11 AB2 GLY C 451 MET C 456 1 6 HELIX 12 AB3 PRO C 461 PHE C 465 5 5 HELIX 13 AB4 SER C 500 VAL C 502 5 3 HELIX 14 AB5 THR C 593 GLY C 598 1 6 HELIX 15 AB6 TYR C 613 TYR C 618 1 6 HELIX 16 AB7 PRO C 619 VAL C 622 5 4 HELIX 17 AB8 HIS D 421 THR D 425 5 5 HELIX 18 AB9 GLY D 436 TYR D 443 1 8 HELIX 19 AC1 THR D 444 PHE D 447 5 4 HELIX 20 AC2 GLY D 451 HIS D 458 1 8 HELIX 21 AC3 PRO D 461 PHE D 465 5 5 HELIX 22 AC4 THR D 593 GLY D 598 1 6 HELIX 23 AC5 TYR D 613 TYR D 618 1 6 HELIX 24 AC6 PRO D 619 VAL D 622 5 4 HELIX 25 AC7 ARG E 83 THR E 87 5 5 HELIX 26 AC8 SER E 156 ALA E 158 5 3 HELIX 27 AC9 PRO E 185 LEU E 189 5 5 HELIX 28 AD1 GLN F 79 LEU F 83 5 5 HELIX 29 AD2 SER F 123 GLY F 130 1 8 HELIX 30 AD3 LYS F 185 HIS F 191 1 7 HELIX 31 AD4 HIS G 421 THR G 425 5 5 HELIX 32 AD5 GLY G 436 TYR G 443 1 8 HELIX 33 AD6 CYS G 452 HIS G 458 1 7 HELIX 34 AD7 PRO G 461 PHE G 465 5 5 HELIX 35 AD8 THR G 593 GLY G 598 1 6 HELIX 36 AD9 TYR G 613 TYR G 618 1 6 HELIX 37 AE1 PRO G 619 VAL G 622 5 4 HELIX 38 AE2 PRO H 52A GLY H 55 5 4 HELIX 39 AE3 ARG H 83 THR H 87 5 5 HELIX 40 AE4 SER H 187 LEU H 189 5 3 HELIX 41 AE5 PRO I 52A GLY I 55 5 4 HELIX 42 AE6 SER I 187 GLN I 192 5 6 HELIX 43 AE7 HIS I 200 ASN I 204 5 5 HELIX 44 AE8 GLN J 79 LEU J 83 5 5 HELIX 45 AE9 SER J 123 SER J 129 1 7 HELIX 46 AF1 SER J 184 GLU J 189 1 6 HELIX 47 AF2 HIS K 421 THR K 425 5 5 HELIX 48 AF3 GLY K 436 TYR K 443 1 8 HELIX 49 AF4 THR K 444 PHE K 447 5 4 HELIX 50 AF5 GLY K 451 HIS K 458 1 8 HELIX 51 AF6 PRO K 461 PHE K 465 5 5 HELIX 52 AF7 SER K 500 VAL K 502 5 3 HELIX 53 AF8 THR K 593 GLY K 598 1 6 HELIX 54 AF9 TYR K 613 TYR K 618 1 6 HELIX 55 AG1 PRO K 619 VAL K 622 5 4 HELIX 56 AG2 GLN L 79 LEU L 83 5 5 HELIX 57 AG3 SER L 123 LYS L 128 1 6 HELIX 58 AG4 LYS L 185 HIS L 191 1 7 SHEET 1 AA1 4 LEU A 4 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 ALA A 24 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 77 LEU A 82 -1 O ALA A 78 N CYS A 22 SHEET 4 AA1 4 VAL A 67 ASP A 72 -1 N THR A 70 O TYR A 79 SHEET 1 AA2 6 VAL A 11 LYS A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N LYS A 12 SHEET 3 AA2 6 ALA A 88 ILE A 100 -1 N ALA A 88 O VAL A 109 SHEET 4 AA2 6 ALA A 33 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AA2 6 LEU A 45 ILE A 52 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 ALA A 56 TYR A 59 -1 O LYS A 58 N GLY A 50 SHEET 1 AA3 4 VAL A 11 LYS A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N LYS A 12 SHEET 3 AA3 4 ALA A 88 ILE A 100 -1 N ALA A 88 O VAL A 109 SHEET 4 AA3 4 PHE A 100C TRP A 103 -1 O SER A 102 N ARG A 94 SHEET 1 AA4 4 PHE A 122 LEU A 124 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 PHE A 122 LEU A 124 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 CYS A 196 HIS A 200 -1 O ASN A 199 N THR A 151 SHEET 3 AA6 3 THR A 205 VAL A 207 -1 O VAL A 207 N VAL A 198 SHEET 1 AA7 4 MET B 4 GLN B 6 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O GLN B 24 N THR B 5 SHEET 3 AA7 4 GLU B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 65 O THR B 72 SHEET 1 AA8 6 SER B 10 ALA B 13 0 SHEET 2 AA8 6 THR B 104 ILE B 108 1 O GLU B 107 N LEU B 11 SHEET 3 AA8 6 ALA B 84 TYR B 91 -1 N ALA B 84 O LEU B 106 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA9 4 SER B 10 ALA B 13 0 SHEET 2 AA9 4 THR B 104 ILE B 108 1 O GLU B 107 N LEU B 11 SHEET 3 AA9 4 ALA B 84 TYR B 91 -1 N ALA B 84 O LEU B 106 SHEET 4 AA9 4 TYR B 98 PHE B 100 -1 O THR B 99 N HIS B 90 SHEET 1 AB1 4 SER B 116 ILE B 119 0 SHEET 2 AB1 4 THR B 131 PHE B 141 -1 O ASN B 139 N SER B 116 SHEET 3 AB1 4 TYR B 175 SER B 184 -1 O LEU B 181 N VAL B 134 SHEET 4 AB1 4 SER B 161 VAL B 165 -1 N GLN B 162 O THR B 180 SHEET 1 AB2 4 ALA B 155 LEU B 156 0 SHEET 2 AB2 4 ALA B 146 VAL B 152 -1 N VAL B 152 O ALA B 155 SHEET 3 AB2 4 TYR B 194 HIS B 200 -1 O ALA B 195 N LYS B 151 SHEET 4 AB2 4 VAL B 207 LYS B 209 -1 O LYS B 209 N CYS B 196 SHEET 1 AB3 3 GLY C 468 TYR C 474 0 SHEET 2 AB3 3 CYS C 569 GLY C 573 -1 O ASN C 570 N THR C 473 SHEET 3 AB3 3 THR C 578 CYS C 581 -1 O CYS C 581 N CYS C 569 SHEET 1 AB4 2 THR C 496 PRO C 498 0 SHEET 2 AB4 2 VAL C 536 ILE C 538 -1 O LEU C 537 N ILE C 497 SHEET 1 AB5 4 PRO C 513 VAL C 516 0 SHEET 2 AB5 4 VAL C 506 PHE C 509 -1 N CYS C 508 O VAL C 514 SHEET 3 AB5 4 GLY C 551 MET C 555 -1 O THR C 553 N TYR C 507 SHEET 4 AB5 4 THR C 561 GLY C 565 -1 O LYS C 562 N TRP C 554 SHEET 1 AB6 4 TRP C 602 THR C 604 0 SHEET 2 AB6 4 CYS C 607 VAL C 609 -1 O CYS C 607 N LEU C 603 SHEET 3 AB6 4 GLU C 637 CYS C 644 -1 O ALA C 643 N LEU C 608 SHEET 4 AB6 4 THR C 625 TYR C 632 -1 N VAL C 629 O LEU C 640 SHEET 1 AB7 5 ILE D 414 ASN D 415 0 SHEET 2 AB7 5 VAL D 514 VAL D 516 -1 O VAL D 515 N ASN D 415 SHEET 3 AB7 5 VAL D 502 CYS D 508 -1 N CYS D 508 O VAL D 514 SHEET 4 AB7 5 GLY D 551 ASN D 556 -1 O THR D 553 N TYR D 507 SHEET 5 AB7 5 THR D 561 GLY D 565 -1 O LYS D 562 N TRP D 554 SHEET 1 AB8 3 GLY D 468 TYR D 474 0 SHEET 2 AB8 3 CYS D 569 GLY D 573 -1 O ASN D 570 N THR D 473 SHEET 3 AB8 3 THR D 578 CYS D 581 -1 O CYS D 581 N CYS D 569 SHEET 1 AB9 2 THR D 496 PRO D 498 0 SHEET 2 AB9 2 VAL D 536 ILE D 538 -1 O LEU D 537 N ILE D 497 SHEET 1 AC1 4 TRP D 602 THR D 604 0 SHEET 2 AC1 4 CYS D 607 VAL D 609 -1 O CYS D 607 N THR D 604 SHEET 3 AC1 4 VAL D 636 CYS D 644 -1 O ALA D 643 N LEU D 608 SHEET 4 AC1 4 THR D 625 VAL D 633 -1 N MET D 631 O HIS D 638 SHEET 1 AC2 4 LEU E 4 GLN E 6 0 SHEET 2 AC2 4 VAL E 18 ALA E 24 -1 O LYS E 23 N VAL E 5 SHEET 3 AC2 4 THR E 77 LEU E 82 -1 O ALA E 78 N CYS E 22 SHEET 4 AC2 4 VAL E 67 ASP E 72 -1 N THR E 70 O TYR E 79 SHEET 1 AC3 6 GLU E 10 LYS E 12 0 SHEET 2 AC3 6 THR E 107 VAL E 111 1 O THR E 110 N LYS E 12 SHEET 3 AC3 6 ALA E 88 ILE E 100 -1 N ALA E 88 O VAL E 109 SHEET 4 AC3 6 ALA E 33 GLN E 39 -1 N GLN E 39 O VAL E 89 SHEET 5 AC3 6 LEU E 45 ILE E 52 -1 O GLU E 46 N ARG E 38 SHEET 6 AC3 6 ALA E 56 TYR E 59 -1 O LYS E 58 N GLY E 50 SHEET 1 AC4 4 GLU E 10 LYS E 12 0 SHEET 2 AC4 4 THR E 107 VAL E 111 1 O THR E 110 N LYS E 12 SHEET 3 AC4 4 ALA E 88 ILE E 100 -1 N ALA E 88 O VAL E 109 SHEET 4 AC4 4 PHE E 100C TRP E 103 -1 O ARG E 100E N VAL E 98 SHEET 1 AC5 4 SER E 120 LEU E 124 0 SHEET 2 AC5 4 ALA E 136 TYR E 145 -1 O LYS E 143 N SER E 120 SHEET 3 AC5 4 TYR E 176 VAL E 184 -1 O TYR E 176 N TYR E 145 SHEET 4 AC5 4 VAL E 169 LEU E 170 -1 N VAL E 169 O SER E 177 SHEET 1 AC6 3 THR E 151 TRP E 154 0 SHEET 2 AC6 3 TYR E 194 ASN E 199 -1 O ASN E 199 N THR E 151 SHEET 3 AC6 3 VAL E 207 VAL E 211 -1 O VAL E 207 N VAL E 198 SHEET 1 AC7 4 MET F 4 GLN F 6 0 SHEET 2 AC7 4 VAL F 19 ALA F 25 -1 O GLN F 24 N THR F 5 SHEET 3 AC7 4 GLU F 70 ILE F 75 -1 O ILE F 75 N VAL F 19 SHEET 4 AC7 4 PHE F 62 SER F 67 -1 N SER F 65 O THR F 72 SHEET 1 AC8 6 SER F 10 SER F 14 0 SHEET 2 AC8 6 THR F 104 LYS F 109 1 O LYS F 109 N ALA F 13 SHEET 3 AC8 6 THR F 85 ASP F 92 -1 N TYR F 86 O THR F 104 SHEET 4 AC8 6 LEU F 33 GLN F 38 -1 N TYR F 36 O PHE F 87 SHEET 5 AC8 6 LYS F 45 TYR F 49 -1 O LYS F 45 N GLN F 37 SHEET 6 AC8 6 ASN F 53 LEU F 54 -1 O ASN F 53 N TYR F 49 SHEET 1 AC9 4 SER F 10 SER F 14 0 SHEET 2 AC9 4 THR F 104 LYS F 109 1 O LYS F 109 N ALA F 13 SHEET 3 AC9 4 THR F 85 ASP F 92 -1 N TYR F 86 O THR F 104 SHEET 4 AC9 4 VAL F 97 PHE F 100 -1 O THR F 99 N HIS F 90 SHEET 1 AD1 4 SER F 116 PHE F 120 0 SHEET 2 AD1 4 THR F 131 PHE F 141 -1 O VAL F 135 N PHE F 120 SHEET 3 AD1 4 TYR F 175 SER F 184 -1 O LEU F 181 N VAL F 134 SHEET 4 AD1 4 SER F 161 VAL F 165 -1 N GLN F 162 O THR F 180 SHEET 1 AD2 4 ALA F 155 LEU F 156 0 SHEET 2 AD2 4 LYS F 147 VAL F 152 -1 N VAL F 152 O ALA F 155 SHEET 3 AD2 4 VAL F 193 THR F 199 -1 O GLU F 197 N GLN F 149 SHEET 4 AD2 4 VAL F 207 ASN F 212 -1 O VAL F 207 N VAL F 198 SHEET 1 AD3 3 ALA G 426 LEU G 427 0 SHEET 2 AD3 3 CYS G 503 PHE G 509 -1 O GLY G 504 N ALA G 426 SHEET 3 AD3 3 PRO G 513 VAL G 516 -1 O VAL G 514 N CYS G 508 SHEET 1 AD4 4 ALA G 426 LEU G 427 0 SHEET 2 AD4 4 CYS G 503 PHE G 509 -1 O GLY G 504 N ALA G 426 SHEET 3 AD4 4 GLY G 551 MET G 555 -1 O MET G 555 N CYS G 503 SHEET 4 AD4 4 THR G 561 GLY G 565 -1 O LYS G 562 N TRP G 554 SHEET 1 AD5 3 THR G 473 TYR G 474 0 SHEET 2 AD5 3 CYS G 569 GLY G 572 -1 O ASN G 570 N THR G 473 SHEET 3 AD5 3 THR G 578 CYS G 581 -1 O CYS G 581 N CYS G 569 SHEET 1 AD6 2 THR G 496 PRO G 498 0 SHEET 2 AD6 2 VAL G 536 ILE G 538 -1 O LEU G 537 N ILE G 497 SHEET 1 AD7 4 TRP G 602 THR G 604 0 SHEET 2 AD7 4 CYS G 607 VAL G 609 -1 O CYS G 607 N LEU G 603 SHEET 3 AD7 4 VAL G 636 CYS G 644 -1 O ALA G 643 N LEU G 608 SHEET 4 AD7 4 THR G 625 VAL G 633 -1 N PHE G 627 O ALA G 642 SHEET 1 AD8 6 GLU H 10 LYS H 12 0 SHEET 2 AD8 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AD8 6 ALA H 88 ILE H 100 -1 N ALA H 88 O VAL H 109 SHEET 4 AD8 6 SER H 32 GLN H 39 -1 N ALA H 33 O ALA H 95 SHEET 5 AD8 6 LEU H 45 ILE H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AD8 6 ALA H 56 TYR H 59 -1 O LYS H 58 N GLY H 50 SHEET 1 AD9 4 GLU H 10 LYS H 12 0 SHEET 2 AD9 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AD9 4 ALA H 88 ILE H 100 -1 N ALA H 88 O VAL H 109 SHEET 4 AD9 4 PHE H 100C TRP H 103 -1 O ARG H 100E N VAL H 98 SHEET 1 AE1 3 VAL H 18 LYS H 23 0 SHEET 2 AE1 3 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 3 AE1 3 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AE2 4 SER H 120 VAL H 121 0 SHEET 2 AE2 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AE2 4 TYR H 176 PRO H 185 -1 O SER H 180 N CYS H 140 SHEET 4 AE2 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AE3 4 SER H 120 VAL H 121 0 SHEET 2 AE3 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AE3 4 TYR H 176 PRO H 185 -1 O SER H 180 N CYS H 140 SHEET 4 AE3 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AE4 3 THR H 151 TRP H 154 0 SHEET 2 AE4 3 ILE H 195 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AE4 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AE5 4 LEU I 4 GLN I 6 0 SHEET 2 AE5 4 VAL I 18 ALA I 24 -1 O LYS I 23 N VAL I 5 SHEET 3 AE5 4 THR I 77 LEU I 82 -1 O ALA I 78 N CYS I 22 SHEET 4 AE5 4 VAL I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AE6 6 GLU I 10 LYS I 12 0 SHEET 2 AE6 6 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AE6 6 ALA I 88 ILE I 100 -1 N ALA I 88 O VAL I 109 SHEET 4 AE6 6 ALA I 33 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 AE6 6 GLU I 46 ILE I 52 -1 O MET I 48 N TRP I 36 SHEET 6 AE6 6 ALA I 56 TYR I 59 -1 O LYS I 58 N GLY I 50 SHEET 1 AE7 4 GLU I 10 LYS I 12 0 SHEET 2 AE7 4 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AE7 4 ALA I 88 ILE I 100 -1 N ALA I 88 O VAL I 109 SHEET 4 AE7 4 PHE I 100C TRP I 103 -1 O ARG I 100E N VAL I 98 SHEET 1 AE8 4 SER I 120 LEU I 124 0 SHEET 2 AE8 4 THR I 135 TYR I 145 -1 O LYS I 143 N SER I 120 SHEET 3 AE8 4 TYR I 176 PRO I 185 -1 O TYR I 176 N TYR I 145 SHEET 4 AE8 4 HIS I 164 THR I 165 -1 N HIS I 164 O VAL I 181 SHEET 1 AE9 4 SER I 120 LEU I 124 0 SHEET 2 AE9 4 THR I 135 TYR I 145 -1 O LYS I 143 N SER I 120 SHEET 3 AE9 4 TYR I 176 PRO I 185 -1 O TYR I 176 N TYR I 145 SHEET 4 AE9 4 VAL I 169 LEU I 170 -1 N VAL I 169 O SER I 177 SHEET 1 AF1 3 SER I 153 TRP I 154 0 SHEET 2 AF1 3 ILE I 195 ASN I 197 -1 O ASN I 197 N SER I 153 SHEET 3 AF1 3 ASP I 208 ARG I 210 -1 O LYS I 209 N CYS I 196 SHEET 1 AF2 4 MET J 4 SER J 7 0 SHEET 2 AF2 4 VAL J 19 ALA J 25 -1 O THR J 22 N SER J 7 SHEET 3 AF2 4 GLU J 70 ILE J 75 -1 O PHE J 71 N CYS J 23 SHEET 4 AF2 4 PHE J 62 SER J 67 -1 N SER J 65 O THR J 72 SHEET 1 AF3 6 SER J 10 SER J 14 0 SHEET 2 AF3 6 THR J 104 LYS J 109 1 O GLU J 107 N LEU J 11 SHEET 3 AF3 6 ALA J 84 ASP J 92 -1 N TYR J 86 O THR J 104 SHEET 4 AF3 6 LEU J 33 GLN J 38 -1 N TYR J 36 O PHE J 87 SHEET 5 AF3 6 LYS J 45 TYR J 49 -1 O LEU J 47 N TRP J 35 SHEET 6 AF3 6 ASN J 53 LEU J 54 -1 O ASN J 53 N TYR J 49 SHEET 1 AF4 4 SER J 10 SER J 14 0 SHEET 2 AF4 4 THR J 104 LYS J 109 1 O GLU J 107 N LEU J 11 SHEET 3 AF4 4 ALA J 84 ASP J 92 -1 N TYR J 86 O THR J 104 SHEET 4 AF4 4 VAL J 97 PHE J 100 -1 O VAL J 97 N ASP J 92 SHEET 1 AF5 4 SER J 116 PHE J 120 0 SHEET 2 AF5 4 SER J 133 PHE J 141 -1 O ASN J 139 N SER J 116 SHEET 3 AF5 4 TYR J 175 THR J 182 -1 O TYR J 175 N PHE J 141 SHEET 4 AF5 4 SER J 161 VAL J 165 -1 N SER J 164 O SER J 178 SHEET 1 AF6 4 ALA J 155 LEU J 156 0 SHEET 2 AF6 4 LYS J 147 VAL J 152 -1 N VAL J 152 O ALA J 155 SHEET 3 AF6 4 VAL J 193 THR J 199 -1 O GLU J 197 N GLN J 149 SHEET 4 AF6 4 VAL J 207 ASN J 212 -1 O VAL J 207 N VAL J 198 SHEET 1 AF7 3 THR K 473 TYR K 474 0 SHEET 2 AF7 3 CYS K 569 ASN K 570 -1 O ASN K 570 N THR K 473 SHEET 3 AF7 3 THR K 580 CYS K 581 -1 O CYS K 581 N CYS K 569 SHEET 1 AF8 2 THR K 496 PRO K 498 0 SHEET 2 AF8 2 VAL K 536 ILE K 538 -1 O LEU K 537 N ILE K 497 SHEET 1 AF9 4 PRO K 513 VAL K 516 0 SHEET 2 AF9 4 CYS K 503 PHE K 509 -1 N CYS K 508 O VAL K 514 SHEET 3 AF9 4 GLY K 551 MET K 555 -1 O MET K 555 N CYS K 503 SHEET 4 AF9 4 THR K 561 GLY K 565 -1 O LYS K 562 N TRP K 554 SHEET 1 AG1 3 CYS K 607 VAL K 609 0 SHEET 2 AG1 3 VAL K 636 CYS K 644 -1 O ALA K 643 N LEU K 608 SHEET 3 AG1 3 THR K 625 VAL K 633 -1 N MET K 631 O HIS K 638 SHEET 1 AG2 4 MET L 4 SER L 7 0 SHEET 2 AG2 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AG2 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AG2 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AG3 6 SER L 10 SER L 14 0 SHEET 2 AG3 6 THR L 104 LYS L 109 1 O LYS L 109 N ALA L 13 SHEET 3 AG3 6 THR L 85 ASP L 92 -1 N TYR L 86 O THR L 104 SHEET 4 AG3 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AG3 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AG3 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AG4 4 SER L 10 SER L 14 0 SHEET 2 AG4 4 THR L 104 LYS L 109 1 O LYS L 109 N ALA L 13 SHEET 3 AG4 4 THR L 85 ASP L 92 -1 N TYR L 86 O THR L 104 SHEET 4 AG4 4 VAL L 97 PHE L 100 -1 O THR L 99 N HIS L 90 SHEET 1 AG5 4 SER L 116 PHE L 120 0 SHEET 2 AG5 4 THR L 131 PHE L 141 -1 O ASN L 139 N SER L 116 SHEET 3 AG5 4 TYR L 175 SER L 184 -1 O LEU L 181 N VAL L 134 SHEET 4 AG5 4 SER L 161 THR L 166 -1 N SER L 164 O SER L 178 SHEET 1 AG6 4 ALA L 155 LEU L 156 0 SHEET 2 AG6 4 ALA L 146 VAL L 152 -1 N VAL L 152 O ALA L 155 SHEET 3 AG6 4 ALA L 195 HIS L 200 -1 O GLU L 197 N GLN L 149 SHEET 4 AG6 4 VAL L 207 SER L 210 -1 O LYS L 209 N CYS L 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.00 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.09 SSBOND 4 CYS B 136 CYS B 196 1555 1555 2.05 SSBOND 5 CYS C 429 CYS C 503 1555 1555 2.00 SSBOND 6 CYS C 452 CYS C 620 1555 1555 2.06 SSBOND 7 CYS C 459 CYS C 486 1555 1555 2.04 SSBOND 8 CYS C 494 CYS C 564 1555 1555 2.06 SSBOND 9 CYS C 508 CYS C 552 1555 1555 2.07 SSBOND 10 CYS C 569 CYS C 597 1555 1555 2.05 SSBOND 11 CYS C 581 CYS C 585 1555 1555 2.07 SSBOND 12 CYS C 607 CYS C 644 1555 1555 2.10 SSBOND 13 CYS D 429 CYS D 503 1555 1555 2.03 SSBOND 14 CYS D 452 CYS D 620 1555 1555 2.04 SSBOND 15 CYS D 459 CYS D 486 1555 1555 2.02 SSBOND 16 CYS D 494 CYS D 564 1555 1555 2.06 SSBOND 17 CYS D 508 CYS D 552 1555 1555 2.03 SSBOND 18 CYS D 569 CYS D 597 1555 1555 2.05 SSBOND 19 CYS D 581 CYS D 585 1555 1555 2.06 SSBOND 20 CYS D 607 CYS D 644 1555 1555 2.08 SSBOND 21 CYS E 22 CYS E 92 1555 1555 2.05 SSBOND 22 CYS E 140 CYS E 196 1555 1555 2.02 SSBOND 23 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 24 CYS F 136 CYS F 196 1555 1555 2.04 SSBOND 25 CYS G 429 CYS G 503 1555 1555 2.03 SSBOND 26 CYS G 452 CYS G 620 1555 1555 2.05 SSBOND 27 CYS G 459 CYS G 486 1555 1555 2.03 SSBOND 28 CYS G 494 CYS G 564 1555 1555 2.06 SSBOND 29 CYS G 508 CYS G 552 1555 1555 2.06 SSBOND 30 CYS G 569 CYS G 597 1555 1555 2.07 SSBOND 31 CYS G 581 CYS G 585 1555 1555 2.09 SSBOND 32 CYS G 607 CYS G 644 1555 1555 2.09 SSBOND 33 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 34 CYS H 140 CYS H 196 1555 1555 2.02 SSBOND 35 CYS I 22 CYS I 92 1555 1555 2.06 SSBOND 36 CYS I 140 CYS I 196 1555 1555 2.04 SSBOND 37 CYS J 23 CYS J 88 1555 1555 2.10 SSBOND 38 CYS J 136 CYS J 196 1555 1555 2.04 SSBOND 39 CYS K 429 CYS K 503 1555 1555 2.04 SSBOND 40 CYS K 452 CYS K 620 1555 1555 2.06 SSBOND 41 CYS K 459 CYS K 486 1555 1555 2.04 SSBOND 42 CYS K 494 CYS K 564 1555 1555 2.07 SSBOND 43 CYS K 508 CYS K 552 1555 1555 2.06 SSBOND 44 CYS K 569 CYS K 597 1555 1555 2.08 SSBOND 45 CYS K 581 CYS K 585 1555 1555 2.08 SSBOND 46 CYS K 607 CYS K 644 1555 1555 2.03 SSBOND 47 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 48 CYS L 136 CYS L 196 1555 1555 2.05 LINK ND2 ASN C 423 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN C 430 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 703 1555 1555 1.46 LINK ND2 ASN C 540 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C 556 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN C 576 C1 NAG C 704 1555 1555 1.43 LINK ND2 ASN C 623 C1 NAG C 705 1555 1555 1.44 LINK ND2 ASN D 423 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN D 430 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN D 448 C1 NAG D 703 1555 1555 1.43 LINK ND2 ASN D 532 C1 NAG D 704 1555 1555 1.43 LINK ND2 ASN D 540 C1 NAG Q 1 1555 1555 1.43 LINK ND2 ASN D 556 C1 NAG R 1 1555 1555 1.45 LINK ND2 ASN D 576 C1 NAG D 705 1555 1555 1.46 LINK ND2 ASN D 623 C1 NAG D 706 1555 1555 1.44 LINK ND2 ASN G 423 C1 NAG S 1 1555 1555 1.45 LINK ND2 ASN G 430 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN G 540 C1 NAG U 1 1555 1555 1.45 LINK ND2 ASN G 556 C1 NAG V 1 1555 1555 1.46 LINK ND2 ASN G 576 C1 NAG G 702 1555 1555 1.44 LINK ND2 ASN G 623 C1 NAG G 703 1555 1555 1.43 LINK ND2 ASN K 423 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN K 430 C1 NAG K 703 1555 1555 1.43 LINK ND2 ASN K 448 C1 NAG K 704 1555 1555 1.44 LINK ND2 ASN K 532 C1 NAG K 705 1555 1555 1.46 LINK ND2 ASN K 540 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN K 556 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN K 576 C1 NAG K 706 1555 1555 1.44 LINK ND2 ASN K 623 C1 NAG K 707 1555 1555 1.46 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.47 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O6 BMA O 3 C1 MAN O 4 1555 1555 1.45 LINK O3 BMA O 3 C1 MAN O 6 1555 1555 1.45 LINK O6 MAN O 4 C1 MAN O 5 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.46 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.46 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.48 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.46 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.47 LINK O3 BMA Y 3 C1 MAN Y 4 1555 1555 1.46 LINK O6 BMA Y 3 C1 MAN Y 6 1555 1555 1.45 LINK O2 MAN Y 4 C1 MAN Y 5 1555 1555 1.46 CISPEP 1 TYR B 142 PRO B 143 0 -1.08 CISPEP 2 THR C 510 PRO C 511 0 -12.40 CISPEP 3 PRO D 544 PRO D 545 0 12.32 CISPEP 4 GLY D 566 PRO D 567 0 0.09 CISPEP 5 PHE E 146 PRO E 147 0 -7.88 CISPEP 6 TYR F 142 PRO F 143 0 0.57 CISPEP 7 THR G 510 PRO G 511 0 17.34 CISPEP 8 PHE H 146 PRO H 147 0 -11.04 CISPEP 9 GLU H 148 PRO H 149 0 6.99 CISPEP 10 PHE I 146 PRO I 147 0 -2.73 CISPEP 11 GLU I 148 PRO I 149 0 -4.39 CISPEP 12 SER J 7 PRO J 8 0 -1.64 CISPEP 13 TYR J 142 PRO J 143 0 7.26 CISPEP 14 THR K 510 PRO K 511 0 -15.02 CISPEP 15 PRO K 544 PRO K 545 0 14.19 CISPEP 16 GLY K 566 PRO K 567 0 2.62 CISPEP 17 SER L 7 PRO L 8 0 -11.84 CISPEP 18 TYR L 142 PRO L 143 0 -3.16 CRYST1 233.640 78.530 227.781 90.00 90.94 90.00 C 1 2 1 16 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 0.004280 0.000000 0.000070 0.00000 SCALE2 0.000000 0.012734 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004391 0.00000