HEADER IMMUNE SYSTEM 25-NOV-24 9EHT TITLE CRYSTAL STRUCTURE OF PD-1/RETIFANLIMAB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN; COMPND 3 CHAIN: A, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN; COMPND 7 CHAIN: B, E; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PROGRAMMED CELL DEATH PROTEIN 1; COMPND 11 CHAIN: F, J; COMPND 12 SYNONYM: PROTEIN PD-1,HPD-1; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: PDCD1, PD1; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PD-1, IMMUNE CHECKPOINT, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.-S.HEO REVDAT 1 03-DEC-25 9EHT 0 JRNL AUTH Y.-S.HEO JRNL TITL CRYSTAL STRUCTURE OF PD-1/RETIFANLIMAB COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.13_2998: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 3 NUMBER OF REFLECTIONS : 175760 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 8786 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 29.2940 - 4.7894 0.99 5809 306 0.1800 0.2036 REMARK 3 2 4.7894 - 3.8041 0.99 5753 303 0.1471 0.1854 REMARK 3 3 3.8041 - 3.3240 0.98 5660 298 0.1570 0.1809 REMARK 3 4 3.3240 - 3.0205 0.98 5687 300 0.1676 0.1944 REMARK 3 5 3.0205 - 2.8041 0.98 5677 298 0.1768 0.1984 REMARK 3 6 2.8041 - 2.6389 0.98 5659 298 0.1765 0.2046 REMARK 3 7 2.6389 - 2.5068 0.98 5660 298 0.1805 0.1860 REMARK 3 8 2.5068 - 2.3978 0.98 5631 296 0.1822 0.2213 REMARK 3 9 2.3978 - 2.3055 0.97 5630 296 0.1844 0.1975 REMARK 3 10 2.3055 - 2.2260 0.97 5599 294 0.1799 0.1991 REMARK 3 11 2.2260 - 2.1564 0.97 5580 293 0.1769 0.2019 REMARK 3 12 2.1564 - 2.0948 0.97 5593 295 0.1781 0.1932 REMARK 3 13 2.0948 - 2.0396 0.97 5590 294 0.1820 0.2166 REMARK 3 14 2.0396 - 1.9899 0.97 5544 292 0.1838 0.2088 REMARK 3 15 1.9899 - 1.9447 0.97 5592 294 0.1908 0.2300 REMARK 3 16 1.9447 - 1.9033 0.97 5546 292 0.1958 0.2207 REMARK 3 17 1.9033 - 1.8652 0.96 5557 292 0.1956 0.2241 REMARK 3 18 1.8652 - 1.8300 0.96 5527 290 0.1992 0.2358 REMARK 3 19 1.8300 - 1.7974 0.96 5531 290 0.2059 0.2279 REMARK 3 20 1.7974 - 1.7669 0.96 5556 293 0.2167 0.2528 REMARK 3 21 1.7669 - 1.7384 0.96 5484 289 0.2201 0.2726 REMARK 3 22 1.7384 - 1.7116 0.96 5552 292 0.2148 0.2491 REMARK 3 23 1.7116 - 1.6865 0.96 5474 288 0.2177 0.2215 REMARK 3 24 1.6865 - 1.6627 0.96 5475 288 0.2314 0.2754 REMARK 3 25 1.6627 - 1.6403 0.96 5534 292 0.2377 0.2703 REMARK 3 26 1.6403 - 1.6190 0.96 5461 287 0.2360 0.2812 REMARK 3 27 1.6190 - 1.5987 0.95 5457 287 0.2403 0.2761 REMARK 3 28 1.5987 - 1.5795 0.95 5464 288 0.2553 0.3012 REMARK 3 29 1.5795 - 1.5611 0.95 5466 288 0.2634 0.3060 REMARK 3 30 1.5611 - 1.5440 0.91 5226 275 0.3062 0.3113 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) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.170 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.009 8587 REMARK 3 ANGLE : 1.427 11674 REMARK 3 CHIRALITY : 0.086 1306 REMARK 3 PLANARITY : 0.012 1498 REMARK 3 DIHEDRAL : 3.648 5139 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 1 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.2537 55.6920 51.8836 REMARK 3 T TENSOR REMARK 3 T11: 0.1776 T22: 0.0916 REMARK 3 T33: 0.1423 T12: 0.0418 REMARK 3 T13: 0.0029 T23: -0.0078 REMARK 3 L TENSOR REMARK 3 L11: 3.6698 L22: 1.5474 REMARK 3 L33: 1.5741 L12: 1.6599 REMARK 3 L13: 1.5576 L23: 0.6550 REMARK 3 S TENSOR REMARK 3 S11: -0.0662 S12: 0.0766 S13: -0.1640 REMARK 3 S21: 0.0792 S22: 0.1094 S23: -0.1055 REMARK 3 S31: 0.1311 S32: 0.1325 S33: -0.0710 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.9468 63.8710 52.5586 REMARK 3 T TENSOR REMARK 3 T11: 0.1614 T22: 0.0713 REMARK 3 T33: 0.1135 T12: 0.0048 REMARK 3 T13: 0.0133 T23: -0.0037 REMARK 3 L TENSOR REMARK 3 L11: 5.8450 L22: 5.9520 REMARK 3 L33: 6.9692 L12: -1.2912 REMARK 3 L13: 4.0627 L23: -2.6442 REMARK 3 S TENSOR REMARK 3 S11: -0.1944 S12: -0.0349 S13: 0.1258 REMARK 3 S21: 0.1119 S22: 0.2641 S23: 0.2834 REMARK 3 S31: -0.2321 S32: -0.2220 S33: -0.1222 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5491 56.1106 55.6815 REMARK 3 T TENSOR REMARK 3 T11: 0.1698 T22: 0.0832 REMARK 3 T33: 0.1432 T12: 0.0341 REMARK 3 T13: 0.0180 T23: -0.0081 REMARK 3 L TENSOR REMARK 3 L11: 3.3235 L22: 1.3416 REMARK 3 L33: 1.7017 L12: 1.8777 REMARK 3 L13: 0.8803 L23: 0.1470 REMARK 3 S TENSOR REMARK 3 S11: -0.0204 S12: -0.1254 S13: -0.0301 REMARK 3 S21: 0.1059 S22: 0.0370 S23: -0.0059 REMARK 3 S31: 0.0719 S32: -0.0566 S33: 0.0015 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9466 58.3390 44.4366 REMARK 3 T TENSOR REMARK 3 T11: 0.1659 T22: 0.0969 REMARK 3 T33: 0.1345 T12: 0.0026 REMARK 3 T13: -0.0041 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 2.8448 L22: 2.3362 REMARK 3 L33: 3.2594 L12: 2.3785 REMARK 3 L13: 3.0014 L23: 2.5550 REMARK 3 S TENSOR REMARK 3 S11: 0.0605 S12: -0.0483 S13: -0.0858 REMARK 3 S21: 0.0492 S22: 0.0108 S23: -0.0914 REMARK 3 S31: 0.1149 S32: -0.0172 S33: -0.0936 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.2923 68.6436 12.4848 REMARK 3 T TENSOR REMARK 3 T11: 0.2204 T22: 0.1317 REMARK 3 T33: 0.1411 T12: -0.0100 REMARK 3 T13: -0.0105 T23: -0.0040 REMARK 3 L TENSOR REMARK 3 L11: 3.2685 L22: 6.6542 REMARK 3 L33: 3.8925 L12: 2.3009 REMARK 3 L13: -0.3789 L23: -2.9982 REMARK 3 S TENSOR REMARK 3 S11: -0.0557 S12: 0.1849 S13: 0.2666 REMARK 3 S21: -0.5321 S22: 0.2197 S23: 0.5786 REMARK 3 S31: -0.1493 S32: -0.1423 S33: -0.1831 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 167 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.1953 60.2096 19.9316 REMARK 3 T TENSOR REMARK 3 T11: 0.1579 T22: 0.1409 REMARK 3 T33: 0.1520 T12: -0.0205 REMARK 3 T13: 0.0029 T23: -0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.7705 L22: 1.2722 REMARK 3 L33: 3.0276 L12: 0.6504 REMARK 3 L13: -0.7339 L23: -1.1039 REMARK 3 S TENSOR REMARK 3 S11: 0.0207 S12: -0.0110 S13: 0.0053 REMARK 3 S21: 0.0266 S22: -0.0393 S23: -0.0431 REMARK 3 S31: -0.1448 S32: 0.2389 S33: 0.0167 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.4365 62.4489 18.9006 REMARK 3 T TENSOR REMARK 3 T11: 0.1201 T22: 0.1062 REMARK 3 T33: 0.1378 T12: -0.0144 REMARK 3 T13: -0.0113 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 0.5618 L22: 3.2387 REMARK 3 L33: 5.9357 L12: 0.4349 REMARK 3 L13: -1.1159 L23: -2.5772 REMARK 3 S TENSOR REMARK 3 S11: 0.1103 S12: 0.0543 S13: 0.0351 REMARK 3 S21: -0.0603 S22: -0.0798 S23: -0.0378 REMARK 3 S31: -0.3039 S32: 0.1081 S33: -0.0162 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.9512 53.3148 14.4939 REMARK 3 T TENSOR REMARK 3 T11: 0.1084 T22: 0.1129 REMARK 3 T33: 0.1465 T12: -0.0331 REMARK 3 T13: 0.0050 T23: -0.0219 REMARK 3 L TENSOR REMARK 3 L11: 2.1153 L22: 5.5361 REMARK 3 L33: 9.6809 L12: -0.7426 REMARK 3 L13: 0.2371 L23: -4.3000 REMARK 3 S TENSOR REMARK 3 S11: -0.0460 S12: 0.0733 S13: 0.0217 REMARK 3 S21: -0.2891 S22: -0.0391 S23: 0.0368 REMARK 3 S31: 0.2740 S32: -0.1685 S33: 0.0313 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.0216 83.7124 46.9927 REMARK 3 T TENSOR REMARK 3 T11: 0.1645 T22: 0.0464 REMARK 3 T33: 0.1297 T12: 0.0008 REMARK 3 T13: -0.0247 T23: -0.0238 REMARK 3 L TENSOR REMARK 3 L11: 2.2238 L22: 1.6104 REMARK 3 L33: 6.4206 L12: -1.3430 REMARK 3 L13: -0.0925 L23: -0.7485 REMARK 3 S TENSOR REMARK 3 S11: -0.0133 S12: 0.0846 S13: 0.0472 REMARK 3 S21: 0.0396 S22: 0.1519 S23: 0.1729 REMARK 3 S31: -0.2543 S32: -0.3574 S33: -0.2471 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.7202 78.3383 54.4267 REMARK 3 T TENSOR REMARK 3 T11: 0.2104 T22: 0.0855 REMARK 3 T33: 0.1420 T12: 0.0039 REMARK 3 T13: -0.0282 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 2.2320 L22: 2.5119 REMARK 3 L33: 1.1465 L12: -0.7305 REMARK 3 L13: 0.1360 L23: -1.5410 REMARK 3 S TENSOR REMARK 3 S11: -0.0852 S12: -0.0196 S13: -0.0271 REMARK 3 S21: 0.0558 S22: 0.0325 S23: 0.0055 REMARK 3 S31: -0.0003 S32: 0.0167 S33: 0.0429 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.7565 81.5265 53.0022 REMARK 3 T TENSOR REMARK 3 T11: 0.1799 T22: 0.1263 REMARK 3 T33: 0.2236 T12: -0.0233 REMARK 3 T13: -0.0382 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 4.3203 L22: 3.3333 REMARK 3 L33: 6.4320 L12: -0.8532 REMARK 3 L13: 1.8569 L23: 0.4857 REMARK 3 S TENSOR REMARK 3 S11: -0.2199 S12: 0.1979 S13: 0.1658 REMARK 3 S21: 0.1641 S22: -0.0827 S23: -0.3645 REMARK 3 S31: 0.1647 S32: 0.6490 S33: 0.2269 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.9980 85.9076 49.1929 REMARK 3 T TENSOR REMARK 3 T11: 0.2180 T22: 0.0634 REMARK 3 T33: 0.1796 T12: 0.0014 REMARK 3 T13: -0.0254 T23: 0.0082 REMARK 3 L TENSOR REMARK 3 L11: 1.2822 L22: 1.2698 REMARK 3 L33: 5.1958 L12: 0.2779 REMARK 3 L13: 0.7068 L23: 0.5377 REMARK 3 S TENSOR REMARK 3 S11: -0.0913 S12: -0.0324 S13: 0.1291 REMARK 3 S21: 0.0405 S22: 0.1101 S23: -0.1630 REMARK 3 S31: -0.3253 S32: 0.2795 S33: -0.0311 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.8515 72.9834 39.1036 REMARK 3 T TENSOR REMARK 3 T11: 0.1914 T22: 0.0644 REMARK 3 T33: 0.1369 T12: -0.0078 REMARK 3 T13: 0.0028 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 0.9406 L22: 0.1978 REMARK 3 L33: 2.3120 L12: -0.2772 REMARK 3 L13: 0.7198 L23: -0.5217 REMARK 3 S TENSOR REMARK 3 S11: -0.0148 S12: 0.0639 S13: -0.0624 REMARK 3 S21: -0.0091 S22: 0.0209 S23: -0.0130 REMARK 3 S31: 0.1194 S32: -0.0125 S33: 0.0210 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 181 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.1927 71.6008 26.4182 REMARK 3 T TENSOR REMARK 3 T11: 0.1785 T22: 0.0917 REMARK 3 T33: 0.1309 T12: -0.0055 REMARK 3 T13: -0.0010 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 3.5123 L22: 2.9151 REMARK 3 L33: 1.3291 L12: 2.1210 REMARK 3 L13: -0.3602 L23: -0.3513 REMARK 3 S TENSOR REMARK 3 S11: -0.0169 S12: -0.0068 S13: -0.0774 REMARK 3 S21: 0.1097 S22: -0.0391 S23: 0.0020 REMARK 3 S31: -0.0838 S32: -0.0026 S33: 0.0476 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 182 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.0885 69.8106 23.4207 REMARK 3 T TENSOR REMARK 3 T11: 0.1403 T22: 0.1349 REMARK 3 T33: 0.1105 T12: -0.0011 REMARK 3 T13: 0.0125 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 6.3543 L22: 7.0675 REMARK 3 L33: 2.1765 L12: 4.6073 REMARK 3 L13: 0.9368 L23: 0.4226 REMARK 3 S TENSOR REMARK 3 S11: -0.1065 S12: 0.2270 S13: 0.0699 REMARK 3 S21: -0.1214 S22: 0.0626 S23: 0.4501 REMARK 3 S31: -0.0476 S32: -0.2178 S33: 0.0634 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 210 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.2385 74.9467 18.0560 REMARK 3 T TENSOR REMARK 3 T11: 0.2966 T22: 0.2106 REMARK 3 T33: 0.2343 T12: -0.0089 REMARK 3 T13: -0.0657 T23: 0.0875 REMARK 3 L TENSOR REMARK 3 L11: 6.5036 L22: 6.3298 REMARK 3 L33: 6.4621 L12: 3.4560 REMARK 3 L13: 1.9864 L23: 4.7324 REMARK 3 S TENSOR REMARK 3 S11: -0.1740 S12: 0.4580 S13: 0.3480 REMARK 3 S21: -0.9716 S22: -0.1464 S23: 0.6409 REMARK 3 S31: -0.8299 S32: -0.5051 S33: 0.2221 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.8555 46.0702 1.3761 REMARK 3 T TENSOR REMARK 3 T11: 0.1103 T22: 0.1718 REMARK 3 T33: 0.1270 T12: -0.0226 REMARK 3 T13: 0.0451 T23: -0.0170 REMARK 3 L TENSOR REMARK 3 L11: 1.1737 L22: 1.8388 REMARK 3 L33: 7.3187 L12: -0.9649 REMARK 3 L13: 1.7168 L23: -2.6772 REMARK 3 S TENSOR REMARK 3 S11: -0.0072 S12: 0.0047 S13: -0.0569 REMARK 3 S21: 0.0747 S22: 0.1004 S23: 0.1289 REMARK 3 S31: 0.1071 S32: -0.3905 S33: -0.1052 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 37 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.4799 40.6922 -0.4045 REMARK 3 T TENSOR REMARK 3 T11: 0.1671 T22: 0.1598 REMARK 3 T33: 0.1427 T12: 0.0152 REMARK 3 T13: 0.0324 T23: -0.0016 REMARK 3 L TENSOR REMARK 3 L11: 2.2719 L22: 3.1925 REMARK 3 L33: 6.3962 L12: 1.4553 REMARK 3 L13: 3.0038 L23: -0.2849 REMARK 3 S TENSOR REMARK 3 S11: 0.0467 S12: -0.0468 S13: -0.3756 REMARK 3 S21: 0.0943 S22: 0.0674 S23: -0.2166 REMARK 3 S31: 0.2627 S32: 0.2132 S33: -0.0807 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 53 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.8358 40.3265 3.1560 REMARK 3 T TENSOR REMARK 3 T11: 0.1718 T22: 0.1426 REMARK 3 T33: 0.1468 T12: -0.0100 REMARK 3 T13: 0.0155 T23: -0.0070 REMARK 3 L TENSOR REMARK 3 L11: 0.3696 L22: 0.3020 REMARK 3 L33: 4.7896 L12: -0.0036 REMARK 3 L13: 0.4728 L23: -0.5277 REMARK 3 S TENSOR REMARK 3 S11: 0.0537 S12: -0.0182 S13: -0.0914 REMARK 3 S21: -0.0667 S22: 0.0221 S23: 0.0485 REMARK 3 S31: 0.5363 S32: -0.1891 S33: -0.0834 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 118 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.7813 52.0288 33.9216 REMARK 3 T TENSOR REMARK 3 T11: 0.2051 T22: 0.4798 REMARK 3 T33: 0.2684 T12: 0.0046 REMARK 3 T13: 0.0230 T23: -0.1221 REMARK 3 L TENSOR REMARK 3 L11: 3.1128 L22: 9.2804 REMARK 3 L33: 3.5421 L12: 5.3734 REMARK 3 L13: -1.4801 L23: -1.8409 REMARK 3 S TENSOR REMARK 3 S11: -0.1849 S12: -0.1675 S13: -0.1712 REMARK 3 S21: -0.1105 S22: 0.2676 S23: -0.7770 REMARK 3 S31: -0.1706 S32: 0.9346 S33: -0.0488 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 133 THROUGH 178 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.5490 49.0416 27.2588 REMARK 3 T TENSOR REMARK 3 T11: 0.1755 T22: 0.2032 REMARK 3 T33: 0.1316 T12: 0.0267 REMARK 3 T13: 0.0043 T23: -0.0004 REMARK 3 L TENSOR REMARK 3 L11: 1.1154 L22: 4.2591 REMARK 3 L33: 2.8748 L12: 1.6986 REMARK 3 L13: 1.2574 L23: 2.6425 REMARK 3 S TENSOR REMARK 3 S11: -0.0659 S12: 0.1411 S13: -0.0720 REMARK 3 S21: -0.1986 S22: 0.1492 S23: -0.1230 REMARK 3 S31: -0.0764 S32: 0.2261 S33: -0.0711 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 179 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.3680 55.5356 35.9448 REMARK 3 T TENSOR REMARK 3 T11: 0.1391 T22: 0.1455 REMARK 3 T33: 0.1489 T12: 0.0489 REMARK 3 T13: -0.0007 T23: -0.0203 REMARK 3 L TENSOR REMARK 3 L11: 5.8310 L22: 4.4237 REMARK 3 L33: 3.7550 L12: 4.1473 REMARK 3 L13: 1.7321 L23: 2.0317 REMARK 3 S TENSOR REMARK 3 S11: 0.1131 S12: -0.2717 S13: 0.2717 REMARK 3 S21: 0.1008 S22: -0.1439 S23: 0.0907 REMARK 3 S31: -0.0376 S32: 0.2357 S33: 0.0192 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.8387 49.4747 -4.7252 REMARK 3 T TENSOR REMARK 3 T11: 0.1358 T22: 0.2148 REMARK 3 T33: 0.1140 T12: 0.0034 REMARK 3 T13: 0.0265 T23: -0.0055 REMARK 3 L TENSOR REMARK 3 L11: 2.0461 L22: 3.7837 REMARK 3 L33: 4.9969 L12: 1.2342 REMARK 3 L13: 0.9793 L23: 2.7526 REMARK 3 S TENSOR REMARK 3 S11: -0.0053 S12: -0.0828 S13: -0.0385 REMARK 3 S21: 0.0370 S22: 0.1544 S23: -0.1972 REMARK 3 S31: 0.0025 S32: 0.4429 S33: -0.2462 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 18 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.3896 47.6337 -10.4057 REMARK 3 T TENSOR REMARK 3 T11: 0.1342 T22: 0.1448 REMARK 3 T33: 0.0930 T12: -0.0140 REMARK 3 T13: 0.0174 T23: -0.0009 REMARK 3 L TENSOR REMARK 3 L11: 2.8383 L22: 1.8516 REMARK 3 L33: 1.6991 L12: 0.5546 REMARK 3 L13: 0.1889 L23: 0.0358 REMARK 3 S TENSOR REMARK 3 S11: 0.0552 S12: -0.3248 S13: -0.0060 REMARK 3 S21: 0.1646 S22: -0.0990 S23: -0.0197 REMARK 3 S31: -0.0069 S32: 0.0963 S33: 0.0064 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 45 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.7964 54.2508 -15.0054 REMARK 3 T TENSOR REMARK 3 T11: 0.1359 T22: 0.1194 REMARK 3 T33: 0.1552 T12: -0.0141 REMARK 3 T13: 0.0116 T23: -0.0083 REMARK 3 L TENSOR REMARK 3 L11: 3.0714 L22: 1.9012 REMARK 3 L33: 6.0785 L12: -0.5039 REMARK 3 L13: -1.9855 L23: -0.5865 REMARK 3 S TENSOR REMARK 3 S11: 0.1022 S12: 0.0159 S13: 0.2569 REMARK 3 S21: -0.0453 S22: -0.0082 S23: 0.0540 REMARK 3 S31: -0.2128 S32: -0.0948 S33: -0.0919 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.0965 56.0702 -12.7905 REMARK 3 T TENSOR REMARK 3 T11: 0.1747 T22: 0.1452 REMARK 3 T33: 0.1255 T12: -0.0298 REMARK 3 T13: 0.0095 T23: 0.0070 REMARK 3 L TENSOR REMARK 3 L11: 3.3667 L22: 6.3826 REMARK 3 L33: 7.5896 L12: -0.9599 REMARK 3 L13: -2.8537 L23: 4.6945 REMARK 3 S TENSOR REMARK 3 S11: 0.0799 S12: -0.1356 S13: 0.2766 REMARK 3 S21: -0.1091 S22: 0.0138 S23: 0.0249 REMARK 3 S31: -0.3943 S32: 0.1702 S33: -0.1633 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 84 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.5963 55.2431 -2.1461 REMARK 3 T TENSOR REMARK 3 T11: 0.1554 T22: 0.1913 REMARK 3 T33: 0.1168 T12: -0.0090 REMARK 3 T13: 0.0174 T23: -0.0278 REMARK 3 L TENSOR REMARK 3 L11: 4.0712 L22: 2.2059 REMARK 3 L33: 6.2373 L12: 2.8896 REMARK 3 L13: 2.9061 L23: 1.8877 REMARK 3 S TENSOR REMARK 3 S11: 0.0105 S12: -0.2864 S13: 0.2280 REMARK 3 S21: -0.0408 S22: -0.1270 S23: -0.0127 REMARK 3 S31: -0.4201 S32: 0.0321 S33: 0.1847 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 99 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.4072 46.9964 10.1574 REMARK 3 T TENSOR REMARK 3 T11: 0.1687 T22: 0.2130 REMARK 3 T33: 0.1141 T12: 0.0035 REMARK 3 T13: 0.0117 T23: -0.0093 REMARK 3 L TENSOR REMARK 3 L11: 1.2630 L22: 0.5493 REMARK 3 L33: 2.1215 L12: 0.0791 REMARK 3 L13: 1.2604 L23: 0.5016 REMARK 3 S TENSOR REMARK 3 S11: 0.0192 S12: -0.2283 S13: -0.0310 REMARK 3 S21: 0.1217 S22: 0.0460 S23: -0.0552 REMARK 3 S31: 0.1338 S32: 0.0029 S33: -0.0588 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 141 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.3579 44.3110 23.0948 REMARK 3 T TENSOR REMARK 3 T11: 0.1954 T22: 0.3250 REMARK 3 T33: 0.1737 T12: 0.0309 REMARK 3 T13: 0.0237 T23: -0.0186 REMARK 3 L TENSOR REMARK 3 L11: 0.8789 L22: 3.2374 REMARK 3 L33: 2.9181 L12: 1.2042 REMARK 3 L13: 0.0445 L23: -2.0172 REMARK 3 S TENSOR REMARK 3 S11: -0.0299 S12: 0.0721 S13: -0.0623 REMARK 3 S21: -0.0221 S22: 0.0361 S23: -0.0982 REMARK 3 S31: 0.0783 S32: 0.0325 S33: -0.0004 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 195 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.9398 39.8271 25.0123 REMARK 3 T TENSOR REMARK 3 T11: 0.1466 T22: 0.3754 REMARK 3 T33: 0.2159 T12: 0.0790 REMARK 3 T13: 0.0241 T23: -0.0081 REMARK 3 L TENSOR REMARK 3 L11: 1.8791 L22: 6.8896 REMARK 3 L33: 4.7204 L12: 2.1546 REMARK 3 L13: -2.0953 L23: -1.5803 REMARK 3 S TENSOR REMARK 3 S11: -0.0852 S12: -0.0853 S13: -0.1357 REMARK 3 S21: 0.0881 S22: -0.1373 S23: -0.2862 REMARK 3 S31: 0.4103 S32: 0.3812 S33: 0.2188 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 210 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.1741 43.7753 29.1588 REMARK 3 T TENSOR REMARK 3 T11: 0.2791 T22: 0.4841 REMARK 3 T33: 0.2730 T12: 0.0306 REMARK 3 T13: -0.0887 T23: 0.0578 REMARK 3 L TENSOR REMARK 3 L11: 5.0520 L22: 3.6414 REMARK 3 L33: 8.4290 L12: 1.2624 REMARK 3 L13: -0.3789 L23: -2.1871 REMARK 3 S TENSOR REMARK 3 S11: 0.1771 S12: -0.4791 S13: -0.0462 REMARK 3 S21: 0.4556 S22: -0.2462 S23: -0.3383 REMARK 3 S31: 0.1085 S32: 0.2883 S33: 0.2342 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 32 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.5924 43.4379 -33.3082 REMARK 3 T TENSOR REMARK 3 T11: 0.3446 T22: 0.4341 REMARK 3 T33: 0.1802 T12: -0.1157 REMARK 3 T13: 0.0554 T23: -0.0013 REMARK 3 L TENSOR REMARK 3 L11: 6.3400 L22: 6.4754 REMARK 3 L33: 9.0968 L12: 0.4251 REMARK 3 L13: 6.6557 L23: 4.1210 REMARK 3 S TENSOR REMARK 3 S11: -0.1939 S12: 1.1142 S13: 0.0649 REMARK 3 S21: -0.5504 S22: 0.3532 S23: -0.5256 REMARK 3 S31: -0.3065 S32: -0.0625 S33: -0.0241 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 41 THROUGH 55 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2658 32.3510 -32.7569 REMARK 3 T TENSOR REMARK 3 T11: 0.4516 T22: 0.7757 REMARK 3 T33: 0.3393 T12: -0.3087 REMARK 3 T13: -0.0171 T23: -0.0645 REMARK 3 L TENSOR REMARK 3 L11: 0.7086 L22: 3.8744 REMARK 3 L33: 0.3168 L12: 1.3607 REMARK 3 L13: 0.3839 L23: 1.1050 REMARK 3 S TENSOR REMARK 3 S11: 0.1240 S12: 0.2234 S13: -0.5597 REMARK 3 S21: 0.3253 S22: -0.0773 S23: 0.2347 REMARK 3 S31: 0.7539 S32: -0.6490 S33: -0.2069 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 56 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0337 39.9865 -24.9031 REMARK 3 T TENSOR REMARK 3 T11: 0.3141 T22: 0.4033 REMARK 3 T33: 0.2746 T12: -0.0356 REMARK 3 T13: 0.0082 T23: -0.0992 REMARK 3 L TENSOR REMARK 3 L11: 6.5121 L22: 2.3662 REMARK 3 L33: 9.8938 L12: -0.1266 REMARK 3 L13: 4.7810 L23: -1.7091 REMARK 3 S TENSOR REMARK 3 S11: -0.2743 S12: 1.4253 S13: -0.4440 REMARK 3 S21: -0.2153 S22: -0.2669 S23: -0.0529 REMARK 3 S31: 0.3264 S32: 0.7100 S33: 0.3025 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 64 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.9635 40.9335 -21.8596 REMARK 3 T TENSOR REMARK 3 T11: 0.2617 T22: 0.3371 REMARK 3 T33: 0.1875 T12: -0.0835 REMARK 3 T13: -0.0281 T23: -0.0059 REMARK 3 L TENSOR REMARK 3 L11: 2.1578 L22: 3.9157 REMARK 3 L33: 7.9898 L12: -0.0342 REMARK 3 L13: 4.0102 L23: -1.3153 REMARK 3 S TENSOR REMARK 3 S11: -0.0481 S12: -0.2321 S13: -0.1204 REMARK 3 S21: 0.0748 S22: 0.1018 S23: 0.3029 REMARK 3 S31: -0.0671 S32: -0.7958 S33: -0.0223 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 83 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.8577 30.9320 -13.2026 REMARK 3 T TENSOR REMARK 3 T11: 0.6204 T22: 0.5653 REMARK 3 T33: 0.4041 T12: -0.2696 REMARK 3 T13: 0.0194 T23: 0.0977 REMARK 3 L TENSOR REMARK 3 L11: 4.8898 L22: 1.7685 REMARK 3 L33: 0.9580 L12: -2.9783 REMARK 3 L13: 2.1962 L23: -1.3309 REMARK 3 S TENSOR REMARK 3 S11: 0.0930 S12: -0.6103 S13: -0.7609 REMARK 3 S21: 0.6091 S22: 0.1984 S23: 0.7301 REMARK 3 S31: 0.6867 S32: -1.1718 S33: -0.2596 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 95 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.7215 31.6057 -27.4025 REMARK 3 T TENSOR REMARK 3 T11: 0.4796 T22: 0.3305 REMARK 3 T33: 0.2423 T12: -0.1070 REMARK 3 T13: -0.0474 T23: -0.0615 REMARK 3 L TENSOR REMARK 3 L11: 6.4603 L22: 7.8980 REMARK 3 L33: 5.8939 L12: -3.2550 REMARK 3 L13: -3.4910 L23: 0.7971 REMARK 3 S TENSOR REMARK 3 S11: -0.1920 S12: 0.2292 S13: -0.5746 REMARK 3 S21: 0.1296 S22: 0.2630 S23: 0.0156 REMARK 3 S31: 1.2989 S32: -0.1648 S33: 0.0003 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 111 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.7205 32.5689 -26.1232 REMARK 3 T TENSOR REMARK 3 T11: 0.2270 T22: 1.2458 REMARK 3 T33: 0.4465 T12: -0.8229 REMARK 3 T13: -0.1857 T23: 0.1141 REMARK 3 L TENSOR REMARK 3 L11: 1.2450 L22: 6.9727 REMARK 3 L33: 1.6613 L12: 0.9697 REMARK 3 L13: -1.4269 L23: -1.5372 REMARK 3 S TENSOR REMARK 3 S11: 0.2091 S12: -0.4051 S13: -0.3021 REMARK 3 S21: 0.1444 S22: 0.0078 S23: 0.7586 REMARK 3 S31: 0.3551 S32: -0.5734 S33: -0.2045 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 119 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.0957 47.1622 -23.2451 REMARK 3 T TENSOR REMARK 3 T11: 0.1563 T22: 0.2607 REMARK 3 T33: 0.1395 T12: -0.0367 REMARK 3 T13: -0.0045 T23: 0.0218 REMARK 3 L TENSOR REMARK 3 L11: 8.1398 L22: 2.7874 REMARK 3 L33: 8.1420 L12: 4.4480 REMARK 3 L13: 7.9492 L23: 4.3939 REMARK 3 S TENSOR REMARK 3 S11: -0.0984 S12: 0.1427 S13: 0.0833 REMARK 3 S21: -0.1232 S22: 0.0931 S23: 0.0588 REMARK 3 S31: -0.0787 S32: -0.2408 S33: 0.0855 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 137 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.5770 36.6736 -33.8934 REMARK 3 T TENSOR REMARK 3 T11: 0.3669 T22: 1.0351 REMARK 3 T33: 0.3636 T12: -0.3707 REMARK 3 T13: -0.0231 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 3.8162 L22: 7.2892 REMARK 3 L33: 0.1631 L12: 4.6875 REMARK 3 L13: 0.6744 L23: 0.5538 REMARK 3 S TENSOR REMARK 3 S11: -0.1852 S12: 0.4364 S13: 0.6488 REMARK 3 S21: -0.2077 S22: 0.0699 S23: 1.0919 REMARK 3 S31: 0.1426 S32: -1.2061 S33: 0.1408 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 34 THROUGH 55 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9350 59.5552 88.7040 REMARK 3 T TENSOR REMARK 3 T11: 0.3288 T22: 0.2596 REMARK 3 T33: 0.1529 T12: 0.0043 REMARK 3 T13: -0.0686 T23: -0.0257 REMARK 3 L TENSOR REMARK 3 L11: 2.8269 L22: 3.4696 REMARK 3 L33: 5.8399 L12: 1.2628 REMARK 3 L13: -0.3247 L23: -2.4859 REMARK 3 S TENSOR REMARK 3 S11: -0.2518 S12: -0.1101 S13: 0.0535 REMARK 3 S21: 0.1968 S22: 0.1669 S23: -0.0145 REMARK 3 S31: -0.4664 S32: -0.1820 S33: 0.1015 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 56 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8089 73.2252 73.9618 REMARK 3 T TENSOR REMARK 3 T11: 0.8737 T22: 0.4005 REMARK 3 T33: 0.3647 T12: 0.0993 REMARK 3 T13: -0.0521 T23: -0.0179 REMARK 3 L TENSOR REMARK 3 L11: 4.3352 L22: 5.0558 REMARK 3 L33: 7.2527 L12: -4.2567 REMARK 3 L13: 5.6003 L23: -5.3479 REMARK 3 S TENSOR REMARK 3 S11: -0.7433 S12: -0.7009 S13: 1.0511 REMARK 3 S21: 0.6766 S22: 0.3063 S23: 0.5282 REMARK 3 S31: -0.8585 S32: -0.1313 S33: 0.3489 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 64 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.0477 58.2990 75.9023 REMARK 3 T TENSOR REMARK 3 T11: 0.2885 T22: 0.2881 REMARK 3 T33: 0.1494 T12: -0.0009 REMARK 3 T13: -0.0194 T23: -0.0187 REMARK 3 L TENSOR REMARK 3 L11: 4.3447 L22: 8.5005 REMARK 3 L33: 4.6721 L12: -4.0958 REMARK 3 L13: 4.4980 L23: -4.7330 REMARK 3 S TENSOR REMARK 3 S11: -0.0098 S12: 0.3098 S13: 0.0355 REMARK 3 S21: -0.3642 S22: -0.0419 S23: -0.4285 REMARK 3 S31: 0.2211 S32: 0.5329 S33: 0.0587 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 83 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.5847 51.3974 73.4632 REMARK 3 T TENSOR REMARK 3 T11: 0.4288 T22: 0.2530 REMARK 3 T33: 0.2529 T12: -0.0469 REMARK 3 T13: -0.0422 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 7.4130 L22: 0.3552 REMARK 3 L33: 6.9990 L12: -1.7363 REMARK 3 L13: 7.2901 L23: -1.6579 REMARK 3 S TENSOR REMARK 3 S11: 0.5794 S12: -0.3916 S13: -0.8367 REMARK 3 S21: -0.2582 S22: 0.1323 S23: 0.2511 REMARK 3 S31: 1.2794 S32: -0.4315 S33: -0.5251 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 95 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.6495 63.7243 83.3233 REMARK 3 T TENSOR REMARK 3 T11: 0.2828 T22: 0.3570 REMARK 3 T33: 0.1969 T12: 0.0435 REMARK 3 T13: -0.0573 T23: -0.0723 REMARK 3 L TENSOR REMARK 3 L11: 5.0933 L22: 8.4265 REMARK 3 L33: 7.6309 L12: -5.3907 REMARK 3 L13: -1.2098 L23: 0.2124 REMARK 3 S TENSOR REMARK 3 S11: 0.1488 S12: -0.4306 S13: 0.2006 REMARK 3 S21: 0.3538 S22: -0.3694 S23: 0.2469 REMARK 3 S31: -0.7613 S32: -0.5522 S33: 0.1644 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 111 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.2797 46.8695 86.6486 REMARK 3 T TENSOR REMARK 3 T11: 0.3310 T22: 0.2421 REMARK 3 T33: 0.2779 T12: 0.0137 REMARK 3 T13: 0.0021 T23: 0.0138 REMARK 3 L TENSOR REMARK 3 L11: 3.9367 L22: 2.0643 REMARK 3 L33: 8.9513 L12: -0.9237 REMARK 3 L13: -5.9285 L23: 1.5764 REMARK 3 S TENSOR REMARK 3 S11: -0.0897 S12: 0.1709 S13: -0.7078 REMARK 3 S21: -0.2209 S22: -0.0655 S23: -0.0190 REMARK 3 S31: 0.6372 S32: -0.1285 S33: 0.0860 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 119 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.8440 63.3569 75.9983 REMARK 3 T TENSOR REMARK 3 T11: 0.3075 T22: 0.2029 REMARK 3 T33: 0.2168 T12: 0.0128 REMARK 3 T13: -0.0631 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 2.1325 L22: 5.5536 REMARK 3 L33: 8.6284 L12: -3.3346 REMARK 3 L13: 4.3195 L23: -6.8410 REMARK 3 S TENSOR REMARK 3 S11: -0.3824 S12: -0.1322 S13: 0.1580 REMARK 3 S21: 0.3153 S22: 0.0013 S23: -0.3174 REMARK 3 S31: -0.6478 S32: -0.1975 S33: 0.3871 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 129 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.6483 60.7438 80.7903 REMARK 3 T TENSOR REMARK 3 T11: 0.3117 T22: 0.1991 REMARK 3 T33: 0.2093 T12: 0.0200 REMARK 3 T13: -0.0590 T23: -0.0181 REMARK 3 L TENSOR REMARK 3 L11: 2.6021 L22: 4.6298 REMARK 3 L33: 7.6039 L12: -1.5879 REMARK 3 L13: 2.3140 L23: -4.6221 REMARK 3 S TENSOR REMARK 3 S11: -0.0640 S12: -0.0500 S13: -0.0730 REMARK 3 S21: 0.6041 S22: -0.4023 S23: -0.1390 REMARK 3 S31: -0.5723 S32: 0.7865 S33: 0.5921 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 9EHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000290504. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-OCT-24 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 : PAL/PLS REMARK 200 BEAMLINE : 5C (4A) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 175789 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 35.00 % (W/V) 2,4-METHYL PENTANEDIOL, REMARK 280 200 MM SODIUM CHLORIDE, AND 100 MM TRIS AT PH 7.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.58000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5510 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24500 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J 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: 5620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 217 REMARK 465 CYS A 218 REMARK 465 CYS B 222 REMARK 465 ASP B 223 REMARK 465 LYS B 224 REMARK 465 THR B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS B 229 REMARK 465 HIS B 230 REMARK 465 HIS B 231 REMARK 465 GLU D 217 REMARK 465 CYS D 218 REMARK 465 CYS E 222 REMARK 465 ASP E 223 REMARK 465 LYS E 224 REMARK 465 THR E 225 REMARK 465 HIS E 226 REMARK 465 HIS E 227 REMARK 465 HIS E 228 REMARK 465 HIS E 229 REMARK 465 HIS E 230 REMARK 465 HIS E 231 REMARK 465 ASP F 26 REMARK 465 SER F 27 REMARK 465 PRO F 28 REMARK 465 ASP F 29 REMARK 465 ARG F 30 REMARK 465 PRO F 31 REMARK 465 PRO F 72 REMARK 465 SER F 73 REMARK 465 ASN F 74 REMARK 465 GLN F 75 REMARK 465 GLY F 90 REMARK 465 GLN F 91 REMARK 465 ALA F 149 REMARK 465 GLU F 150 REMARK 465 ASP J 26 REMARK 465 SER J 27 REMARK 465 PRO J 28 REMARK 465 ASP J 29 REMARK 465 ARG J 30 REMARK 465 PRO J 31 REMARK 465 TRP J 32 REMARK 465 ASN J 33 REMARK 465 PRO J 72 REMARK 465 SER J 73 REMARK 465 ASN J 74 REMARK 465 GLN J 75 REMARK 465 ARG J 148 REMARK 465 ALA J 149 REMARK 465 GLU J 150 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 GLN J 88 CG CD OE1 NE2 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 307 O HOH A 539 1.69 REMARK 500 O HOH F 216 O HOH F 273 1.80 REMARK 500 OE1 GLU J 141 O HOH J 201 1.81 REMARK 500 OE1 GLU D 191 O HOH D 301 1.84 REMARK 500 O HOH D 471 O HOH D 491 1.85 REMARK 500 O HOH F 207 O HOH F 243 1.85 REMARK 500 O HOH A 453 O HOH A 512 1.85 REMARK 500 OE1 GLU E 154 O HOH E 301 1.86 REMARK 500 O HOH A 301 O HOH A 545 1.86 REMARK 500 O HOH A 346 O HOH A 387 1.86 REMARK 500 O HOH A 353 O HOH A 594 1.86 REMARK 500 O HOH J 214 O HOH J 261 1.87 REMARK 500 O VAL F 43 O HOH F 201 1.89 REMARK 500 O HOH B 645 O HOH B 647 1.89 REMARK 500 OG1 THR B 141 O HOH B 301 1.89 REMARK 500 O HOH A 576 O HOH A 621 1.90 REMARK 500 O HOH E 388 O HOH E 543 1.91 REMARK 500 O HOH A 350 O HOH B 372 1.91 REMARK 500 O HOH A 528 O HOH A 538 1.92 REMARK 500 OE1 GLN A 203 O HOH A 301 1.92 REMARK 500 O HOH B 468 O HOH B 549 1.92 REMARK 500 O HOH A 327 O HOH A 427 1.93 REMARK 500 O HOH A 400 O HOH B 340 1.93 REMARK 500 O HOH A 431 O HOH A 517 1.94 REMARK 500 O HOH B 560 O HOH B 569 1.95 REMARK 500 O HOH J 260 O HOH J 280 1.95 REMARK 500 O HOH E 312 O HOH E 350 1.96 REMARK 500 O HOH A 580 O HOH A 603 1.96 REMARK 500 NZ LYS D 43 O HOH D 302 1.96 REMARK 500 O HOH D 533 O HOH D 563 1.97 REMARK 500 O HOH A 319 O HOH A 578 1.98 REMARK 500 O HOH A 355 O HOH A 517 1.99 REMARK 500 NE2 GLN F 88 O HOH F 202 2.00 REMARK 500 OE1 GLU A 169 O HOH A 302 2.00 REMARK 500 O HOH A 515 O HOH A 554 2.01 REMARK 500 NH1 ARG E 87 O HOH E 302 2.02 REMARK 500 O HOH E 349 O HOH E 499 2.03 REMARK 500 O HOH J 213 O HOH J 288 2.04 REMARK 500 O HOH D 320 O HOH D 439 2.05 REMARK 500 O HOH A 303 O HOH A 419 2.05 REMARK 500 O HOH B 636 O HOH B 650 2.06 REMARK 500 O HOH B 551 O HOH B 572 2.06 REMARK 500 O HOH J 222 O HOH J 229 2.06 REMARK 500 O HOH F 268 O HOH F 270 2.07 REMARK 500 O HOH B 330 O HOH B 543 2.07 REMARK 500 O SER F 71 O HOH F 203 2.07 REMARK 500 O HOH A 397 O HOH A 613 2.07 REMARK 500 O HOH A 433 O HOH A 583 2.07 REMARK 500 O HOH A 546 O HOH B 555 2.07 REMARK 500 O HOH A 481 O HOH A 498 2.07 REMARK 500 REMARK 500 THIS ENTRY HAS 91 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 569 O HOH D 534 2556 1.82 REMARK 500 O HOH B 525 O HOH E 437 2555 1.95 REMARK 500 O HOH E 522 O HOH J 274 1554 2.05 REMARK 500 O HOH B 316 O HOH E 425 2555 2.06 REMARK 500 O HOH B 628 O HOH J 325 2657 2.07 REMARK 500 O HOH B 302 O HOH F 223 2555 2.08 REMARK 500 O HOH B 575 O HOH E 403 2555 2.18 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 ALA A 55 C - N - CA ANGL. DEV. = 26.8 DEGREES REMARK 500 ALA A 55 CA - C - N ANGL. DEV. = 14.3 DEGREES REMARK 500 ALA A 55 O - C - N ANGL. DEV. = -17.1 DEGREES REMARK 500 SER A 56 C - N - CA ANGL. DEV. = 16.1 DEGREES REMARK 500 GLY B 102 C - N - CA ANGL. DEV. = 13.6 DEGREES REMARK 500 ALA D 55 C - N - CA ANGL. DEV. = 21.6 DEGREES REMARK 500 ALA D 55 CA - C - N ANGL. DEV. = 13.9 DEGREES REMARK 500 ALA D 55 O - C - N ANGL. DEV. = -14.2 DEGREES REMARK 500 SER D 56 C - N - CA ANGL. DEV. = 16.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ALA A 55 SER A 56 123.18 REMARK 500 ALA D 55 SER D 56 119.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 VAL A 29 12.34 REMARK 500 PHE A 36 17.03 REMARK 500 ALA A 55 -24.06 REMARK 500 ASN A 156 -10.20 REMARK 500 PHE B 106 14.87 REMARK 500 VAL D 29 12.28 REMARK 500 PHE D 36 -14.65 REMARK 500 ALA D 55 -20.54 REMARK 500 ASN D 156 -10.76 REMARK 500 PHE E 106 13.41 REMARK 500 SER F 62 -10.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 644 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH B 648 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH B 649 DISTANCE = 6.51 ANGSTROMS REMARK 525 HOH B 650 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH B 651 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH D 584 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH E 586 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH E 587 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH J 327 DISTANCE = 6.24 ANGSTROMS REMARK 525 HOH J 328 DISTANCE = 7.02 ANGSTROMS DBREF 9EHT A 1 218 PDB 9EHT 9EHT 1 218 DBREF 9EHT B 1 231 PDB 9EHT 9EHT 1 231 DBREF 9EHT D 1 218 PDB 9EHT 9EHT 1 218 DBREF 9EHT E 1 231 PDB 9EHT 9EHT 1 231 DBREF 9EHT F 26 150 UNP Q15116 PDCD1_HUMAN 26 150 DBREF 9EHT J 26 150 UNP Q15116 PDCD1_HUMAN 26 150 SEQADV 9EHT SER F 93 UNP Q15116 CYS 93 CONFLICT SEQADV 9EHT SER J 93 UNP Q15116 CYS 93 CONFLICT SEQRES 1 A 218 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 A 218 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 A 218 GLU SER VAL ASP ASN TYR GLY MET SER PHE MET ASN TRP SEQRES 4 A 218 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 A 218 HIS ALA ALA SER ASN GLN GLY SER GLY VAL PRO SER ARG SEQRES 6 A 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 7 A 218 ILE SER SER LEU GLU PRO GLU ASP PHE ALA VAL TYR PHE SEQRES 8 A 218 CYS GLN GLN SER LYS GLU VAL PRO TYR THR PHE GLY GLY SEQRES 9 A 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 A 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 A 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 A 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 A 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 A 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 A 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 A 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 A 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 B 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 231 TYR SER PHE THR SER TYR TRP MET ASN TRP VAL ARG GLN SEQRES 4 B 231 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY VAL ILE HIS SEQRES 5 B 231 PRO SER ASP SER GLU THR TRP LEU ASP GLN LYS PHE LYS SEQRES 6 B 231 ASP ARG VAL THR ILE THR VAL ASP LYS SER THR SER THR SEQRES 7 B 231 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 B 231 ALA VAL TYR TYR CYS ALA ARG GLU HIS TYR GLY THR SER SEQRES 9 B 231 PRO PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 B 231 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 B 231 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 B 231 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 B 231 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 B 231 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 B 231 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 B 231 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 B 231 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 B 231 CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 D 218 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 D 218 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 218 GLU SER VAL ASP ASN TYR GLY MET SER PHE MET ASN TRP SEQRES 4 D 218 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 D 218 HIS ALA ALA SER ASN GLN GLY SER GLY VAL PRO SER ARG SEQRES 6 D 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 7 D 218 ILE SER SER LEU GLU PRO GLU ASP PHE ALA VAL TYR PHE SEQRES 8 D 218 CYS GLN GLN SER LYS GLU VAL PRO TYR THR PHE GLY GLY SEQRES 9 D 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 D 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 D 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 D 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 D 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 D 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 D 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 D 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 D 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 E 231 TYR SER PHE THR SER TYR TRP MET ASN TRP VAL ARG GLN SEQRES 4 E 231 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY VAL ILE HIS SEQRES 5 E 231 PRO SER ASP SER GLU THR TRP LEU ASP GLN LYS PHE LYS SEQRES 6 E 231 ASP ARG VAL THR ILE THR VAL ASP LYS SER THR SER THR SEQRES 7 E 231 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 E 231 ALA VAL TYR TYR CYS ALA ARG GLU HIS TYR GLY THR SER SEQRES 9 E 231 PRO PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 E 231 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 E 231 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 E 231 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 E 231 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 E 231 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 E 231 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 E 231 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 E 231 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 E 231 CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 F 125 ASP SER PRO ASP ARG PRO TRP ASN PRO PRO THR PHE SER SEQRES 2 F 125 PRO ALA LEU LEU VAL VAL THR GLU GLY ASP ASN ALA THR SEQRES 3 F 125 PHE THR CYS SER PHE SER ASN THR SER GLU SER PHE VAL SEQRES 4 F 125 LEU ASN TRP TYR ARG MET SER PRO SER ASN GLN THR ASP SEQRES 5 F 125 LYS LEU ALA ALA PHE PRO GLU ASP ARG SER GLN PRO GLY SEQRES 6 F 125 GLN ASP SER ARG PHE ARG VAL THR GLN LEU PRO ASN GLY SEQRES 7 F 125 ARG ASP PHE HIS MET SER VAL VAL ARG ALA ARG ARG ASN SEQRES 8 F 125 ASP SER GLY THR TYR LEU CYS GLY ALA ILE SER LEU ALA SEQRES 9 F 125 PRO LYS ALA GLN ILE LYS GLU SER LEU ARG ALA GLU LEU SEQRES 10 F 125 ARG VAL THR GLU ARG ARG ALA GLU SEQRES 1 J 125 ASP SER PRO ASP ARG PRO TRP ASN PRO PRO THR PHE SER SEQRES 2 J 125 PRO ALA LEU LEU VAL VAL THR GLU GLY ASP ASN ALA THR SEQRES 3 J 125 PHE THR CYS SER PHE SER ASN THR SER GLU SER PHE VAL SEQRES 4 J 125 LEU ASN TRP TYR ARG MET SER PRO SER ASN GLN THR ASP SEQRES 5 J 125 LYS LEU ALA ALA PHE PRO GLU ASP ARG SER GLN PRO GLY SEQRES 6 J 125 GLN ASP SER ARG PHE ARG VAL THR GLN LEU PRO ASN GLY SEQRES 7 J 125 ARG ASP PHE HIS MET SER VAL VAL ARG ALA ARG ARG ASN SEQRES 8 J 125 ASP SER GLY THR TYR LEU CYS GLY ALA ILE SER LEU ALA SEQRES 9 J 125 PRO LYS ALA GLN ILE LYS GLU SER LEU ARG ALA GLU LEU SEQRES 10 J 125 ARG VAL THR GLU ARG ARG ALA GLU FORMUL 7 HOH *1488(H2 O) HELIX 1 AA1 GLU A 83 PHE A 87 5 5 HELIX 2 AA2 SER A 125 SER A 131 1 7 HELIX 3 AA3 LYS A 187 GLU A 191 1 5 HELIX 4 AA4 SER B 28 TYR B 32 5 5 HELIX 5 AA5 GLN B 62 LYS B 65 5 4 HELIX 6 AA6 LYS B 74 THR B 76 5 3 HELIX 7 AA7 ARG B 87 THR B 91 5 5 HELIX 8 AA8 SER B 162 ALA B 164 5 3 HELIX 9 AA9 SER B 193 LEU B 195 5 3 HELIX 10 AB1 LYS B 207 ASN B 210 5 4 HELIX 11 AB2 GLU D 83 PHE D 87 5 5 HELIX 12 AB3 SER D 125 SER D 131 1 7 HELIX 13 AB4 LYS D 187 GLU D 191 1 5 HELIX 14 AB5 SER E 28 TYR E 32 5 5 HELIX 15 AB6 GLN E 62 LYS E 65 5 4 HELIX 16 AB7 ARG E 87 THR E 91 5 5 HELIX 17 AB8 SER E 162 ALA E 164 5 3 HELIX 18 AB9 SER E 193 LEU E 195 5 3 HELIX 19 AC1 LYS E 207 ASN E 210 5 4 HELIX 20 AC2 ARG F 114 SER F 118 5 5 HELIX 21 AC3 ARG J 114 SER J 118 5 5 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 ALA A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 ASP A 74 ILE A 79 -1 O LEU A 77 N LEU A 21 SHEET 4 AA1 4 PHE A 66 SER A 71 -1 N SER A 67 O THR A 78 SHEET 1 AA2 6 THR A 10 LEU A 13 0 SHEET 2 AA2 6 THR A 106 ILE A 110 1 O GLU A 109 N LEU A 11 SHEET 3 AA2 6 VAL A 89 GLN A 94 -1 N TYR A 90 O THR A 106 SHEET 4 AA2 6 MET A 37 GLN A 42 -1 N GLN A 42 O VAL A 89 SHEET 5 AA2 6 LYS A 49 HIS A 53 -1 O LEU A 51 N TRP A 39 SHEET 6 AA2 6 ASN A 57 GLN A 58 -1 O ASN A 57 N HIS A 53 SHEET 1 AA3 4 THR A 10 LEU A 13 0 SHEET 2 AA3 4 THR A 106 ILE A 110 1 O GLU A 109 N LEU A 11 SHEET 3 AA3 4 VAL A 89 GLN A 94 -1 N TYR A 90 O THR A 106 SHEET 4 AA3 4 THR A 101 PHE A 102 -1 O THR A 101 N GLN A 94 SHEET 1 AA4 2 ASP A 30 ASN A 31 0 SHEET 2 AA4 2 MET A 34 SER A 35 -1 O MET A 34 N ASN A 31 SHEET 1 AA5 4 SER A 118 PHE A 122 0 SHEET 2 AA5 4 THR A 133 PHE A 143 -1 O LEU A 139 N PHE A 120 SHEET 3 AA5 4 TYR A 177 SER A 186 -1 O LEU A 183 N VAL A 136 SHEET 4 AA5 4 SER A 163 VAL A 167 -1 N SER A 166 O SER A 180 SHEET 1 AA6 4 ALA A 157 LEU A 158 0 SHEET 2 AA6 4 LYS A 149 VAL A 154 -1 N VAL A 154 O ALA A 157 SHEET 3 AA6 4 VAL A 195 THR A 201 -1 O GLU A 199 N GLN A 151 SHEET 4 AA6 4 VAL A 209 ASN A 214 -1 O VAL A 209 N VAL A 200 SHEET 1 AA7 4 GLN B 3 GLN B 6 0 SHEET 2 AA7 4 VAL B 18 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 AA7 4 THR B 78 LEU B 83 -1 O MET B 81 N VAL B 20 SHEET 4 AA7 4 VAL B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AA8 6 GLU B 10 LYS B 12 0 SHEET 2 AA8 6 THR B 113 VAL B 117 1 O THR B 116 N LYS B 12 SHEET 3 AA8 6 ALA B 92 HIS B 100 -1 N TYR B 94 O THR B 113 SHEET 4 AA8 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA8 6 LEU B 45 HIS B 52 -1 O ILE B 48 N TRP B 36 SHEET 6 AA8 6 GLU B 57 LEU B 60 -1 O TRP B 59 N VAL B 50 SHEET 1 AA9 4 GLU B 10 LYS B 12 0 SHEET 2 AA9 4 THR B 113 VAL B 117 1 O THR B 116 N LYS B 12 SHEET 3 AA9 4 ALA B 92 HIS B 100 -1 N TYR B 94 O THR B 113 SHEET 4 AA9 4 SER B 104 TRP B 109 -1 O TYR B 108 N ARG B 98 SHEET 1 AB1 4 SER B 126 LEU B 130 0 SHEET 2 AB1 4 THR B 141 TYR B 151 -1 O LEU B 147 N PHE B 128 SHEET 3 AB1 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148 SHEET 4 AB1 4 VAL B 169 THR B 171 -1 N HIS B 170 O VAL B 187 SHEET 1 AB2 4 THR B 137 SER B 138 0 SHEET 2 AB2 4 THR B 141 TYR B 151 -1 O THR B 141 N SER B 138 SHEET 3 AB2 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148 SHEET 4 AB2 4 VAL B 175 LEU B 176 -1 N VAL B 175 O SER B 183 SHEET 1 AB3 3 THR B 157 TRP B 160 0 SHEET 2 AB3 3 ILE B 201 HIS B 206 -1 O ASN B 203 N SER B 159 SHEET 3 AB3 3 THR B 211 LYS B 216 -1 O VAL B 213 N VAL B 204 SHEET 1 AB4 4 LEU D 4 SER D 7 0 SHEET 2 AB4 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB4 4 ASP D 74 ILE D 79 -1 O LEU D 77 N LEU D 21 SHEET 4 AB4 4 PHE D 66 SER D 71 -1 N SER D 67 O THR D 78 SHEET 1 AB5 6 THR D 10 LEU D 13 0 SHEET 2 AB5 6 THR D 106 ILE D 110 1 O GLU D 109 N LEU D 11 SHEET 3 AB5 6 VAL D 89 GLN D 94 -1 N TYR D 90 O THR D 106 SHEET 4 AB5 6 MET D 37 GLN D 42 -1 N GLN D 42 O VAL D 89 SHEET 5 AB5 6 LYS D 49 HIS D 53 -1 O LEU D 51 N TRP D 39 SHEET 6 AB5 6 ASN D 57 GLN D 58 -1 O ASN D 57 N HIS D 53 SHEET 1 AB6 4 THR D 10 LEU D 13 0 SHEET 2 AB6 4 THR D 106 ILE D 110 1 O GLU D 109 N LEU D 11 SHEET 3 AB6 4 VAL D 89 GLN D 94 -1 N TYR D 90 O THR D 106 SHEET 4 AB6 4 THR D 101 PHE D 102 -1 O THR D 101 N GLN D 94 SHEET 1 AB7 2 ASP D 30 ASN D 31 0 SHEET 2 AB7 2 MET D 34 SER D 35 -1 O MET D 34 N ASN D 31 SHEET 1 AB8 4 SER D 118 PHE D 122 0 SHEET 2 AB8 4 THR D 133 PHE D 143 -1 O LEU D 139 N PHE D 120 SHEET 3 AB8 4 TYR D 177 SER D 186 -1 O TYR D 177 N PHE D 143 SHEET 4 AB8 4 SER D 163 VAL D 167 -1 N GLN D 164 O THR D 182 SHEET 1 AB9 4 ALA D 157 LEU D 158 0 SHEET 2 AB9 4 LYS D 149 VAL D 154 -1 N VAL D 154 O ALA D 157 SHEET 3 AB9 4 VAL D 195 THR D 201 -1 O GLU D 199 N GLN D 151 SHEET 4 AB9 4 VAL D 209 ASN D 214 -1 O LYS D 211 N CYS D 198 SHEET 1 AC1 4 GLN E 3 GLN E 6 0 SHEET 2 AC1 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AC1 4 THR E 78 LEU E 83 -1 O ALA E 79 N CYS E 22 SHEET 4 AC1 4 VAL E 68 ASP E 73 -1 N THR E 69 O GLU E 82 SHEET 1 AC2 6 GLU E 10 LYS E 12 0 SHEET 2 AC2 6 THR E 113 VAL E 117 1 O THR E 116 N LYS E 12 SHEET 3 AC2 6 ALA E 92 HIS E 100 -1 N TYR E 94 O THR E 113 SHEET 4 AC2 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AC2 6 LEU E 45 HIS E 52 -1 O ILE E 48 N TRP E 36 SHEET 6 AC2 6 GLU E 57 LEU E 60 -1 O TRP E 59 N VAL E 50 SHEET 1 AC3 4 GLU E 10 LYS E 12 0 SHEET 2 AC3 4 THR E 113 VAL E 117 1 O THR E 116 N LYS E 12 SHEET 3 AC3 4 ALA E 92 HIS E 100 -1 N TYR E 94 O THR E 113 SHEET 4 AC3 4 SER E 104 TRP E 109 -1 O TYR E 108 N ARG E 98 SHEET 1 AC4 4 SER E 126 LEU E 130 0 SHEET 2 AC4 4 THR E 141 TYR E 151 -1 O LEU E 147 N PHE E 128 SHEET 3 AC4 4 TYR E 182 PRO E 191 -1 O LEU E 184 N VAL E 148 SHEET 4 AC4 4 VAL E 169 THR E 171 -1 N HIS E 170 O VAL E 187 SHEET 1 AC5 4 THR E 137 SER E 138 0 SHEET 2 AC5 4 THR E 141 TYR E 151 -1 O THR E 141 N SER E 138 SHEET 3 AC5 4 TYR E 182 PRO E 191 -1 O LEU E 184 N VAL E 148 SHEET 4 AC5 4 VAL E 175 LEU E 176 -1 N VAL E 175 O SER E 183 SHEET 1 AC6 3 THR E 157 TRP E 160 0 SHEET 2 AC6 3 ILE E 201 HIS E 206 -1 O ASN E 203 N SER E 159 SHEET 3 AC6 3 THR E 211 LYS E 216 -1 O VAL E 213 N VAL E 204 SHEET 1 AC7 4 THR F 36 SER F 38 0 SHEET 2 AC7 4 ALA F 50 SER F 55 -1 O THR F 53 N SER F 38 SHEET 3 AC7 4 ASP F 105 VAL F 110 -1 O VAL F 110 N ALA F 50 SHEET 4 AC7 4 PHE F 95 GLN F 99 -1 N THR F 98 O HIS F 107 SHEET 1 AC8 5 LEU F 41 THR F 45 0 SHEET 2 AC8 5 ALA F 140 THR F 145 1 O ARG F 143 N LEU F 42 SHEET 3 AC8 5 GLY F 119 LEU F 128 -1 N TYR F 121 O ALA F 140 SHEET 4 AC8 5 VAL F 64 MET F 70 -1 N VAL F 64 O ILE F 126 SHEET 5 AC8 5 ASP F 77 PHE F 82 -1 O LEU F 79 N TRP F 67 SHEET 1 AC9 4 LEU F 41 THR F 45 0 SHEET 2 AC9 4 ALA F 140 THR F 145 1 O ARG F 143 N LEU F 42 SHEET 3 AC9 4 GLY F 119 LEU F 128 -1 N TYR F 121 O ALA F 140 SHEET 4 AC9 4 ALA F 132 GLU F 136 -1 O LYS F 135 N ALA F 125 SHEET 1 AD1 4 THR J 36 SER J 38 0 SHEET 2 AD1 4 ALA J 50 SER J 55 -1 O THR J 53 N SER J 38 SHEET 3 AD1 4 ASP J 105 VAL J 110 -1 O MET J 108 N PHE J 52 SHEET 4 AD1 4 PHE J 95 GLN J 99 -1 N ARG J 96 O SER J 109 SHEET 1 AD2 5 LEU J 41 THR J 45 0 SHEET 2 AD2 5 ALA J 140 THR J 145 1 O ARG J 143 N VAL J 44 SHEET 3 AD2 5 GLY J 119 LEU J 128 -1 N TYR J 121 O ALA J 140 SHEET 4 AD2 5 VAL J 64 ARG J 69 -1 N VAL J 64 O ILE J 126 SHEET 5 AD2 5 ASP J 77 PHE J 82 -1 O LEU J 79 N TRP J 67 SHEET 1 AD3 4 LEU J 41 THR J 45 0 SHEET 2 AD3 4 ALA J 140 THR J 145 1 O ARG J 143 N VAL J 44 SHEET 3 AD3 4 GLY J 119 LEU J 128 -1 N TYR J 121 O ALA J 140 SHEET 4 AD3 4 ALA J 132 GLU J 136 -1 O GLN J 133 N SER J 127 SSBOND 1 CYS A 23 CYS A 92 1555 1555 2.12 SSBOND 2 CYS A 138 CYS A 198 1555 1555 2.02 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.06 SSBOND 4 CYS B 146 CYS B 202 1555 1555 2.05 SSBOND 5 CYS D 23 CYS D 92 1555 1555 2.12 SSBOND 6 CYS D 138 CYS D 198 1555 1555 2.02 SSBOND 7 CYS E 22 CYS E 96 1555 1555 2.07 SSBOND 8 CYS E 146 CYS E 202 1555 1555 2.03 SSBOND 9 CYS F 54 CYS F 123 1555 1555 2.06 SSBOND 10 CYS J 54 CYS J 123 1555 1555 2.06 CISPEP 1 SER A 7 PRO A 8 0 -3.75 CISPEP 2 VAL A 98 PRO A 99 0 2.22 CISPEP 3 TYR A 144 PRO A 145 0 -3.81 CISPEP 4 PHE B 152 PRO B 153 0 -9.93 CISPEP 5 GLU B 154 PRO B 155 0 -4.98 CISPEP 6 SER D 7 PRO D 8 0 -3.34 CISPEP 7 VAL D 98 PRO D 99 0 1.80 CISPEP 8 TYR D 144 PRO D 145 0 -4.70 CISPEP 9 PHE E 152 PRO E 153 0 -9.54 CISPEP 10 GLU E 154 PRO E 155 0 -4.79 CISPEP 11 SER F 38 PRO F 39 0 -0.42 CISPEP 12 PHE F 82 PRO F 83 0 -3.15 CISPEP 13 ALA F 129 PRO F 130 0 24.46 CISPEP 14 SER J 38 PRO J 39 0 -3.03 CISPEP 15 PHE J 82 PRO J 83 0 -2.23 CISPEP 16 ALA J 129 PRO J 130 0 26.30 CRYST1 81.500 93.160 89.910 90.00 112.39 90.00 P 1 21 1 4 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 0.012270 0.000000 0.005055 0.00000 SCALE2 0.000000 0.010734 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012029 0.00000