HEADER IMMUNE SYSTEM 17-APR-23 8SJ6 TITLE ARA H 2.01 38B7 8F3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 8F3 LIGHT CHAIN; COMPND 3 CHAIN: D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 8F3 HEAVY CHAIN; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 38B7 HEAVY CHAIN; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 38B7 LIGHT CHAIN; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ARA H 2 ALLERGEN; COMPND 19 CHAIN: Q; COMPND 20 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: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: OVARY; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: OVARY; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 26 ORGANISM_COMMON: HUMAN; SOURCE 27 ORGANISM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 29 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 31 EXPRESSION_SYSTEM_CELL_LINE: OVARY; SOURCE 32 MOL_ID: 5; SOURCE 33 ORGANISM_SCIENTIFIC: ARACHIS HYPOGAEA; SOURCE 34 ORGANISM_COMMON: PEANUT; SOURCE 35 ORGANISM_TAXID: 3818; SOURCE 36 GENE: ARA H 2; SOURCE 37 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 38 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 39 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 40 EXPRESSION_SYSTEM_CELL_LINE: OVARY KEYWDS ALLERGY, PEANUT, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR B.W.SPILLER,R.A.SHREM REVDAT 1 25-DEC-24 8SJ6 0 JRNL AUTH S.A.SMITH,R.A.SHREM,B.B.C.LANCA,J.ZHANG,J.J.W.WONG,D.CROOTE, JRNL AUTH 2 R.S.PEEBLES JR,B.W.SPILLER JRNL TITL ANTIGENIC DETERMINANTS OF PEANUT INDUCED ANAPHYLAXIS JRNL REF J CLIN IMMUNOL 2024 REMARK 2 REMARK 2 RESOLUTION. 3.97 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.97 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.09 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 3 NUMBER OF REFLECTIONS : 14113 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.254 REMARK 3 R VALUE (WORKING SET) : 0.252 REMARK 3 FREE R VALUE : 0.302 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760 REMARK 3 FREE R VALUE TEST SET COUNT : 672 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 97.0900 - 6.7900 0.95 2785 133 0.2153 0.2585 REMARK 3 2 6.7900 - 5.3900 0.98 2681 140 0.2762 0.3350 REMARK 3 3 5.3900 - 4.7100 0.98 2684 120 0.2454 0.3018 REMARK 3 4 4.7100 - 4.2800 0.98 2683 122 0.2645 0.3083 REMARK 3 5 4.2800 - 3.9700 0.99 2608 157 0.3211 0.3618 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.294 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 119.9 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.9 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 : 0.002 7672 REMARK 3 ANGLE : 0.445 10426 REMARK 3 CHIRALITY : 0.041 1149 REMARK 3 PLANARITY : 0.004 1357 REMARK 3 DIHEDRAL : 3.642 1054 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 33 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 13 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.9461 53.4698 106.3377 REMARK 3 T TENSOR REMARK 3 T11: 1.6359 T22: 1.7362 REMARK 3 T33: 1.6106 T12: -0.1648 REMARK 3 T13: 0.6151 T23: -0.0240 REMARK 3 L TENSOR REMARK 3 L11: 0.5729 L22: 4.8911 REMARK 3 L33: 3.5198 L12: -1.2486 REMARK 3 L13: 0.3077 L23: -0.2607 REMARK 3 S TENSOR REMARK 3 S11: 1.3743 S12: -0.6355 S13: 1.3548 REMARK 3 S21: -0.9028 S22: 0.2504 S23: -1.6656 REMARK 3 S31: -0.7805 S32: -0.4853 S33: -1.1145 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 14 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.9328 43.2801 105.7683 REMARK 3 T TENSOR REMARK 3 T11: 1.4270 T22: 1.5152 REMARK 3 T33: 1.2159 T12: 0.1788 REMARK 3 T13: 0.0299 T23: 0.0684 REMARK 3 L TENSOR REMARK 3 L11: 2.8647 L22: 7.0573 REMARK 3 L33: 3.3454 L12: -3.7546 REMARK 3 L13: 1.2304 L23: 0.8900 REMARK 3 S TENSOR REMARK 3 S11: 0.1491 S12: 0.4671 S13: -0.6489 REMARK 3 S21: -0.9821 S22: -0.5436 S23: -0.2856 REMARK 3 S31: -0.8705 S32: -1.4998 S33: -0.5910 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 62 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.6670 46.4264 98.7204 REMARK 3 T TENSOR REMARK 3 T11: 1.3851 T22: 1.4631 REMARK 3 T33: 1.9882 T12: 0.0647 REMARK 3 T13: 0.1679 T23: -0.0404 REMARK 3 L TENSOR REMARK 3 L11: 7.1264 L22: 3.3983 REMARK 3 L33: 8.5129 L12: -0.2341 REMARK 3 L13: 5.3420 L23: 3.7535 REMARK 3 S TENSOR REMARK 3 S11: 0.7350 S12: -4.3178 S13: 3.1276 REMARK 3 S21: -0.8082 S22: -0.5002 S23: -1.0448 REMARK 3 S31: 0.0219 S32: -0.0376 S33: -0.0783 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.4225 45.3714 109.0353 REMARK 3 T TENSOR REMARK 3 T11: 1.0411 T22: 1.1795 REMARK 3 T33: 1.4570 T12: 0.1142 REMARK 3 T13: 0.2176 T23: 0.0395 REMARK 3 L TENSOR REMARK 3 L11: 4.8295 L22: 5.2591 REMARK 3 L33: 7.3960 L12: -1.3291 REMARK 3 L13: 2.9077 L23: 2.5054 REMARK 3 S TENSOR REMARK 3 S11: -0.7972 S12: 0.1657 S13: -0.3056 REMARK 3 S21: -0.4106 S22: 0.3769 S23: 0.5983 REMARK 3 S31: -1.1465 S32: -0.8224 S33: -0.0887 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.0511 63.0826 114.7637 REMARK 3 T TENSOR REMARK 3 T11: 1.6281 T22: 1.0984 REMARK 3 T33: 1.2500 T12: 0.7502 REMARK 3 T13: 0.0931 T23: 0.0186 REMARK 3 L TENSOR REMARK 3 L11: 8.5929 L22: 0.0704 REMARK 3 L33: 0.0854 L12: -0.8225 REMARK 3 L13: -0.8534 L23: 0.0775 REMARK 3 S TENSOR REMARK 3 S11: 0.8389 S12: 1.1806 S13: -2.3242 REMARK 3 S21: 0.4136 S22: 0.3634 S23: -0.1934 REMARK 3 S31: 0.7801 S32: 0.1070 S33: 3.8986 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.6451 69.6391 143.7911 REMARK 3 T TENSOR REMARK 3 T11: 1.9277 T22: 2.0105 REMARK 3 T33: 1.9493 T12: 0.2606 REMARK 3 T13: 0.3536 T23: -0.5564 REMARK 3 L TENSOR REMARK 3 L11: 6.8743 L22: 7.2448 REMARK 3 L33: 7.3557 L12: -2.3903 REMARK 3 L13: 2.4622 L23: -1.4371 REMARK 3 S TENSOR REMARK 3 S11: 0.7016 S12: -0.7122 S13: 0.2294 REMARK 3 S21: 0.0851 S22: 1.5218 S23: -0.5758 REMARK 3 S31: -0.2052 S32: 1.2318 S33: 0.0477 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 132 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5046 67.1971 123.8808 REMARK 3 T TENSOR REMARK 3 T11: 1.8269 T22: 1.6197 REMARK 3 T33: 1.8144 T12: 0.3925 REMARK 3 T13: 0.3662 T23: -0.1476 REMARK 3 L TENSOR REMARK 3 L11: 1.0067 L22: 2.9059 REMARK 3 L33: 0.2459 L12: 0.7005 REMARK 3 L13: -0.0882 L23: 0.7047 REMARK 3 S TENSOR REMARK 3 S11: 0.9660 S12: -0.6454 S13: 2.0481 REMARK 3 S21: -2.0601 S22: -0.6326 S23: -0.4013 REMARK 3 S31: -1.0664 S32: 1.4289 S33: 0.4672 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 145 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.7714 74.4319 130.4972 REMARK 3 T TENSOR REMARK 3 T11: 1.5434 T22: 1.5400 REMARK 3 T33: 1.8279 T12: -0.4807 REMARK 3 T13: 0.4638 T23: -0.5548 REMARK 3 L TENSOR REMARK 3 L11: 4.1725 L22: 3.1699 REMARK 3 L33: 4.6005 L12: -3.0988 REMARK 3 L13: -0.6493 L23: -1.5142 REMARK 3 S TENSOR REMARK 3 S11: -0.2252 S12: -0.7354 S13: -0.2266 REMARK 3 S21: -2.1936 S22: -0.2465 S23: 0.8820 REMARK 3 S31: 0.3004 S32: 1.4516 S33: 0.1497 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 164 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4116 67.9738 132.9291 REMARK 3 T TENSOR REMARK 3 T11: 1.3529 T22: 1.2304 REMARK 3 T33: 1.9898 T12: 0.0139 REMARK 3 T13: 0.8114 T23: -0.5822 REMARK 3 L TENSOR REMARK 3 L11: 1.3205 L22: 4.0942 REMARK 3 L33: 3.7808 L12: -2.0944 REMARK 3 L13: -0.2835 L23: -1.1381 REMARK 3 S TENSOR REMARK 3 S11: -0.0863 S12: -0.4089 S13: 0.6208 REMARK 3 S21: -0.2513 S22: -0.2401 S23: -1.9799 REMARK 3 S31: -1.1879 S32: 0.8308 S33: -6.3194 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 191 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.1197 78.5894 130.7804 REMARK 3 T TENSOR REMARK 3 T11: 2.1232 T22: 1.0830 REMARK 3 T33: 1.7855 T12: -0.0687 REMARK 3 T13: 0.4693 T23: -0.0445 REMARK 3 L TENSOR REMARK 3 L11: 3.4108 L22: 5.6675 REMARK 3 L33: 1.3030 L12: -2.0495 REMARK 3 L13: -0.7485 L23: -1.8206 REMARK 3 S TENSOR REMARK 3 S11: 1.2564 S12: 1.0265 S13: 0.1855 REMARK 3 S21: -0.0699 S22: 0.0498 S23: -2.3006 REMARK 3 S31: -1.4534 S32: 0.0242 S33: -1.0042 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1076 36.8860 130.5264 REMARK 3 T TENSOR REMARK 3 T11: 0.7565 T22: 1.8961 REMARK 3 T33: 0.8499 T12: 0.1208 REMARK 3 T13: 0.0770 T23: -0.2476 REMARK 3 L TENSOR REMARK 3 L11: 4.4249 L22: 8.0121 REMARK 3 L33: 7.0291 L12: 0.4314 REMARK 3 L13: 5.5627 L23: 0.8789 REMARK 3 S TENSOR REMARK 3 S11: 0.3027 S12: 0.2804 S13: 1.1382 REMARK 3 S21: -0.4670 S22: 0.3890 S23: 0.0325 REMARK 3 S31: 0.3145 S32: -2.1454 S33: 1.8301 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2948 26.7155 121.8373 REMARK 3 T TENSOR REMARK 3 T11: 0.5540 T22: 1.4983 REMARK 3 T33: 0.8638 T12: -0.0584 REMARK 3 T13: 0.0236 T23: -0.2148 REMARK 3 L TENSOR REMARK 3 L11: 2.4264 L22: 5.3091 REMARK 3 L33: 1.9972 L12: 2.8440 REMARK 3 L13: 4.9597 L23: 6.4528 REMARK 3 S TENSOR REMARK 3 S11: 1.1180 S12: -0.2779 S13: 0.0431 REMARK 3 S21: 0.5963 S22: -1.3969 S23: 0.0056 REMARK 3 S31: 1.3172 S32: -0.8192 S33: -1.2567 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.1149 35.2131 120.3519 REMARK 3 T TENSOR REMARK 3 T11: 0.9398 T22: 1.6946 REMARK 3 T33: 1.2528 T12: -0.0296 REMARK 3 T13: 0.2073 T23: -0.2919 REMARK 3 L TENSOR REMARK 3 L11: 3.4799 L22: 7.8624 REMARK 3 L33: 3.7365 L12: -2.2100 REMARK 3 L13: 1.5980 L23: -0.1726 REMARK 3 S TENSOR REMARK 3 S11: -0.4051 S12: -0.3256 S13: 0.2605 REMARK 3 S21: -0.1634 S22: 0.9393 S23: -0.5597 REMARK 3 S31: -0.1917 S32: 0.2886 S33: -0.3662 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 85 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.5235 41.4225 123.1016 REMARK 3 T TENSOR REMARK 3 T11: 0.4516 T22: 1.4546 REMARK 3 T33: 1.0084 T12: 0.1542 REMARK 3 T13: 0.1753 T23: -0.3668 REMARK 3 L TENSOR REMARK 3 L11: 3.6822 L22: 2.4869 REMARK 3 L33: 0.5800 L12: -1.2218 REMARK 3 L13: 0.0977 L23: -1.1287 REMARK 3 S TENSOR REMARK 3 S11: 0.1257 S12: -1.3852 S13: 0.8728 REMARK 3 S21: 0.8794 S22: -0.3914 S23: -0.4298 REMARK 3 S31: -0.3587 S32: -0.8601 S33: -1.8951 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 102 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5132 33.1725 110.6585 REMARK 3 T TENSOR REMARK 3 T11: 1.2318 T22: 1.2529 REMARK 3 T33: 1.1531 T12: -0.2726 REMARK 3 T13: 0.3281 T23: -0.0764 REMARK 3 L TENSOR REMARK 3 L11: 4.9851 L22: 8.9788 REMARK 3 L33: 7.4065 L12: -4.7313 REMARK 3 L13: 3.1666 L23: 1.9636 REMARK 3 S TENSOR REMARK 3 S11: 0.8247 S12: -0.1228 S13: -1.4785 REMARK 3 S21: -0.2196 S22: -0.1759 S23: -0.3900 REMARK 3 S31: -0.7648 S32: 2.3693 S33: -0.7647 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 116 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.1891 57.2299 139.7367 REMARK 3 T TENSOR REMARK 3 T11: 0.9800 T22: 1.1631 REMARK 3 T33: 1.2326 T12: 0.1305 REMARK 3 T13: -0.1673 T23: -0.4831 REMARK 3 L TENSOR REMARK 3 L11: 0.3002 L22: 2.3586 REMARK 3 L33: 2.3107 L12: 0.4331 REMARK 3 L13: -0.3731 L23: -1.9109 REMARK 3 S TENSOR REMARK 3 S11: -0.0370 S12: -0.8898 S13: -0.9422 REMARK 3 S21: 0.5680 S22: 0.6057 S23: -0.2219 REMARK 3 S31: -1.1280 S32: 0.3612 S33: -0.7141 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 155 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0749 53.6821 135.9115 REMARK 3 T TENSOR REMARK 3 T11: 1.5171 T22: 1.3058 REMARK 3 T33: 1.7949 T12: -0.0059 REMARK 3 T13: -0.1346 T23: -0.1849 REMARK 3 L TENSOR REMARK 3 L11: 3.3613 L22: 1.0592 REMARK 3 L33: 2.6044 L12: 0.6065 REMARK 3 L13: -1.3110 L23: 1.1818 REMARK 3 S TENSOR REMARK 3 S11: 0.7114 S12: 0.3344 S13: 0.0154 REMARK 3 S21: 0.4948 S22: -0.1314 S23: -0.7120 REMARK 3 S31: -0.2684 S32: -0.1215 S33: -0.6734 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 175 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.6540 58.4615 140.4845 REMARK 3 T TENSOR REMARK 3 T11: 0.8047 T22: 1.4375 REMARK 3 T33: 1.4811 T12: 0.1391 REMARK 3 T13: 0.0729 T23: -0.3927 REMARK 3 L TENSOR REMARK 3 L11: 0.2259 L22: 3.1992 REMARK 3 L33: 6.1570 L12: 0.7100 REMARK 3 L13: -0.2897 L23: 1.6727 REMARK 3 S TENSOR REMARK 3 S11: 1.1212 S12: 0.9003 S13: 0.4208 REMARK 3 S21: -0.1938 S22: -0.4033 S23: -0.3548 REMARK 3 S31: 0.2937 S32: 0.0442 S33: -0.2360 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.5646 0.4962 121.6896 REMARK 3 T TENSOR REMARK 3 T11: 0.9148 T22: 1.5469 REMARK 3 T33: 1.1575 T12: -0.2413 REMARK 3 T13: -0.1399 T23: -0.0223 REMARK 3 L TENSOR REMARK 3 L11: 2.7208 L22: 5.8058 REMARK 3 L33: 3.1621 L12: -1.9815 REMARK 3 L13: 1.9980 L23: 1.3392 REMARK 3 S TENSOR REMARK 3 S11: 0.0265 S12: -0.3777 S13: -0.3173 REMARK 3 S21: 0.8156 S22: -0.1726 S23: -0.4625 REMARK 3 S31: 0.0080 S32: 0.4794 S33: 0.3979 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 64 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.5556 9.0765 127.8355 REMARK 3 T TENSOR REMARK 3 T11: 1.8988 T22: 1.2900 REMARK 3 T33: 1.2375 T12: -0.1659 REMARK 3 T13: -0.3703 T23: -0.3669 REMARK 3 L TENSOR REMARK 3 L11: 4.4950 L22: 9.8335 REMARK 3 L33: 6.7767 L12: 0.3330 REMARK 3 L13: -0.5306 L23: -8.1584 REMARK 3 S TENSOR REMARK 3 S11: -0.2693 S12: -0.0387 S13: 0.5919 REMARK 3 S21: 0.4763 S22: -1.4605 S23: -1.0576 REMARK 3 S31: 0.1962 S32: 1.4226 S33: -0.6397 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.4608 2.3006 126.4339 REMARK 3 T TENSOR REMARK 3 T11: 0.9987 T22: 1.3432 REMARK 3 T33: 1.0768 T12: 0.0111 REMARK 3 T13: -0.0479 T23: 0.0384 REMARK 3 L TENSOR REMARK 3 L11: 2.1549 L22: 9.1706 REMARK 3 L33: 3.5301 L12: 0.6778 REMARK 3 L13: 2.6506 L23: -0.7786 REMARK 3 S TENSOR REMARK 3 S11: -0.2655 S12: -0.4094 S13: -0.4769 REMARK 3 S21: 1.8652 S22: 0.1615 S23: -2.1330 REMARK 3 S31: -1.1656 S32: -0.2455 S33: 0.6042 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.6244 2.1251 114.1079 REMARK 3 T TENSOR REMARK 3 T11: 0.9561 T22: 1.5189 REMARK 3 T33: 0.9967 T12: -0.3172 REMARK 3 T13: 0.1352 T23: 0.2102 REMARK 3 L TENSOR REMARK 3 L11: 0.9214 L22: 5.2693 REMARK 3 L33: 7.0430 L12: 2.2010 REMARK 3 L13: 2.5302 L23: 6.0885 REMARK 3 S TENSOR REMARK 3 S11: -0.7255 S12: -0.0202 S13: -0.9111 REMARK 3 S21: -0.7530 S22: -0.3619 S23: 0.6916 REMARK 3 S31: -1.0369 S32: -1.8920 S33: -1.5193 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.0528 -14.9627 131.1974 REMARK 3 T TENSOR REMARK 3 T11: 0.6019 T22: 1.7478 REMARK 3 T33: 1.3984 T12: -0.3537 REMARK 3 T13: -0.1112 T23: 0.6462 REMARK 3 L TENSOR REMARK 3 L11: 3.5471 L22: 0.8148 REMARK 3 L33: 2.1941 L12: -1.6219 REMARK 3 L13: -1.1553 L23: 0.8837 REMARK 3 S TENSOR REMARK 3 S11: 0.1251 S12: -2.3000 S13: -1.4839 REMARK 3 S21: 0.8615 S22: 0.1097 S23: -0.2559 REMARK 3 S31: 0.4622 S32: 0.7022 S33: 0.7841 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.5751 -35.9078 124.7447 REMARK 3 T TENSOR REMARK 3 T11: 0.5371 T22: 1.8921 REMARK 3 T33: 1.2845 T12: -0.0366 REMARK 3 T13: -0.5270 T23: 0.2762 REMARK 3 L TENSOR REMARK 3 L11: 0.0187 L22: 0.0906 REMARK 3 L33: 0.6549 L12: 0.0626 REMARK 3 L13: 0.1392 L23: 0.2128 REMARK 3 S TENSOR REMARK 3 S11: -0.3213 S12: -0.2379 S13: 0.5686 REMARK 3 S21: 0.1719 S22: -0.2706 S23: -0.8900 REMARK 3 S31: -0.4592 S32: 1.3235 S33: -5.8599 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 151 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.4007 -31.7599 119.6754 REMARK 3 T TENSOR REMARK 3 T11: 0.7771 T22: 1.6554 REMARK 3 T33: 1.2691 T12: -0.0953 REMARK 3 T13: 0.0074 T23: 0.1365 REMARK 3 L TENSOR REMARK 3 L11: 1.5204 L22: 2.6182 REMARK 3 L33: 1.6233 L12: -0.8309 REMARK 3 L13: 1.6241 L23: -0.7741 REMARK 3 S TENSOR REMARK 3 S11: -0.0106 S12: 0.7603 S13: -0.0917 REMARK 3 S21: -0.2478 S22: -0.5682 S23: -0.3114 REMARK 3 S31: 0.0351 S32: 0.0988 S33: -0.0438 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 74.1464 -33.0599 121.2310 REMARK 3 T TENSOR REMARK 3 T11: 0.9175 T22: 1.8096 REMARK 3 T33: 1.3830 T12: 0.0449 REMARK 3 T13: -0.0807 T23: 0.0979 REMARK 3 L TENSOR REMARK 3 L11: 1.4204 L22: 9.7789 REMARK 3 L33: 1.5477 L12: 1.5656 REMARK 3 L13: 1.2911 L23: 0.0542 REMARK 3 S TENSOR REMARK 3 S11: -0.3973 S12: 0.3505 S13: 0.4455 REMARK 3 S21: -2.2386 S22: -0.3253 S23: -0.3207 REMARK 3 S31: -0.0969 S32: 1.6764 S33: 0.1184 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.1617 -7.9902 114.2646 REMARK 3 T TENSOR REMARK 3 T11: 0.7671 T22: 1.6928 REMARK 3 T33: 1.2140 T12: -0.3124 REMARK 3 T13: -0.1945 T23: 0.0297 REMARK 3 L TENSOR REMARK 3 L11: 4.7520 L22: 5.6809 REMARK 3 L33: 0.7457 L12: -1.2677 REMARK 3 L13: 0.4229 L23: -2.1855 REMARK 3 S TENSOR REMARK 3 S11: 0.0306 S12: -0.3231 S13: 0.2310 REMARK 3 S21: -0.6025 S22: 0.3268 S23: 0.4368 REMARK 3 S31: -0.0365 S32: 0.0196 S33: -0.2010 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.2002 -38.0819 127.9399 REMARK 3 T TENSOR REMARK 3 T11: 0.7816 T22: 1.3383 REMARK 3 T33: 1.1962 T12: 0.0204 REMARK 3 T13: 0.1410 T23: 0.1743 REMARK 3 L TENSOR REMARK 3 L11: 4.0182 L22: 3.4441 REMARK 3 L33: 2.8013 L12: 1.9554 REMARK 3 L13: 0.7893 L23: -0.6613 REMARK 3 S TENSOR REMARK 3 S11: 0.1388 S12: 0.2855 S13: -1.2873 REMARK 3 S21: -0.1694 S22: -0.2096 S23: -0.5133 REMARK 3 S31: 0.9726 S32: 0.6638 S33: 0.1510 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 11 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.6708 21.5934 97.6588 REMARK 3 T TENSOR REMARK 3 T11: 0.7731 T22: 1.7396 REMARK 3 T33: 1.0779 T12: 0.0017 REMARK 3 T13: 0.2764 T23: 0.3591 REMARK 3 L TENSOR REMARK 3 L11: 4.9582 L22: 5.6531 REMARK 3 L33: 6.8372 L12: -4.4591 REMARK 3 L13: 0.5630 L23: -0.0714 REMARK 3 S TENSOR REMARK 3 S11: -0.6585 S12: -0.2640 S13: 1.1292 REMARK 3 S21: -0.4190 S22: -0.1470 S23: -0.6269 REMARK 3 S31: -1.3274 S32: -1.7181 S33: -1.6129 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 38 THROUGH 47 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.0891 17.5185 120.0717 REMARK 3 T TENSOR REMARK 3 T11: 1.5043 T22: 2.4329 REMARK 3 T33: 2.1054 T12: -0.1294 REMARK 3 T13: 0.3074 T23: -0.8826 REMARK 3 L TENSOR REMARK 3 L11: 0.1053 L22: 8.5488 REMARK 3 L33: 6.9987 L12: -0.9591 REMARK 3 L13: 0.8529 L23: -7.7320 REMARK 3 S TENSOR REMARK 3 S11: -0.8157 S12: -2.4405 S13: 1.1101 REMARK 3 S21: 3.8237 S22: -0.4130 S23: 1.1640 REMARK 3 S31: -1.7882 S32: -1.7562 S33: 0.2714 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 48 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.0565 23.3224 106.1736 REMARK 3 T TENSOR REMARK 3 T11: 1.6640 T22: 1.0065 REMARK 3 T33: 1.6092 T12: -0.8235 REMARK 3 T13: -0.2234 T23: -0.1499 REMARK 3 L TENSOR REMARK 3 L11: 2.9618 L22: 5.4505 REMARK 3 L33: 1.7161 L12: 1.9506 REMARK 3 L13: 0.6477 L23: 1.8145 REMARK 3 S TENSOR REMARK 3 S11: -0.5495 S12: 0.5492 S13: 0.5072 REMARK 3 S21: -1.2762 S22: 0.5054 S23: 0.1440 REMARK 3 S31: -0.2856 S32: -0.0302 S33: 1.1580 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 53 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.4403 31.9311 100.2122 REMARK 3 T TENSOR REMARK 3 T11: 1.3035 T22: 1.9891 REMARK 3 T33: 1.9184 T12: -0.4408 REMARK 3 T13: 0.3918 T23: 0.2906 REMARK 3 L TENSOR REMARK 3 L11: 4.6567 L22: 3.3251 REMARK 3 L33: 8.9202 L12: 0.4493 REMARK 3 L13: 4.3758 L23: 4.3933 REMARK 3 S TENSOR REMARK 3 S11: -1.2989 S12: 1.2970 S13: 1.8742 REMARK 3 S21: -0.1653 S22: -1.0656 S23: -1.0718 REMARK 3 S31: 0.1657 S32: -2.3628 S33: -2.8726 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 67 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.9057 16.6747 98.8508 REMARK 3 T TENSOR REMARK 3 T11: 1.2062 T22: 1.6404 REMARK 3 T33: 1.1558 T12: 0.1228 REMARK 3 T13: -0.0169 T23: -0.0572 REMARK 3 L TENSOR REMARK 3 L11: 5.8806 L22: 7.4263 REMARK 3 L33: 4.1122 L12: 0.1222 REMARK 3 L13: -2.3713 L23: -0.4861 REMARK 3 S TENSOR REMARK 3 S11: 0.1027 S12: 0.1178 S13: -0.6512 REMARK 3 S21: 0.0197 S22: 0.0076 S23: -0.9569 REMARK 3 S31: -0.0345 S32: 1.1431 S33: -0.0234 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 8SJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-23. REMARK 100 THE DEPOSITION ID IS D_1000273808. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-MAR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION FEB 5, 2021 REMARK 200 BUILT=20210205 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57338 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.970 REMARK 200 RESOLUTION RANGE LOW (A) : 97.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : 0.12300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.97 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.11 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.65200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 21% P8K, 200 MM NACL, 50 MM NAPI, 50 REMARK 280 MM CITRATE, PH 4.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 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,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.44600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.08750 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.44600 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 97.08750 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C, A, B, Q 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 SER C 136 REMARK 465 SER C 137 REMARK 465 LYS C 138 REMARK 465 SER C 139 REMARK 465 THR C 140 REMARK 465 SER C 141 REMARK 465 GLY C 142 REMARK 465 SER C 224 REMARK 465 CYS C 225 REMARK 465 GLN A 1 REMARK 465 SER A 132 REMARK 465 SER A 133 REMARK 465 LYS A 134 REMARK 465 SER A 135 REMARK 465 THR A 136 REMARK 465 SER A 137 REMARK 465 GLY A 138 REMARK 465 CYS A 221 REMARK 465 GLU B 214 REMARK 465 CYS B 215 REMARK 465 GLU Q 5 REMARK 465 LEU Q 6 REMARK 465 GLN Q 7 REMARK 465 GLY Q 8 REMARK 465 ASP Q 9 REMARK 465 ARG Q 10 REMARK 465 SER Q 54 REMARK 465 PRO Q 55 REMARK 465 TYR Q 56 REMARK 465 ASP Q 57 REMARK 465 ARG Q 58 REMARK 465 ARG Q 59 REMARK 465 GLY Q 60 REMARK 465 VAL Q 131 REMARK 465 GLU Q 132 REMARK 465 SER Q 133 REMARK 465 GLY Q 134 REMARK 465 GLY Q 135 REMARK 465 ARG Q 136 REMARK 465 ASP Q 137 REMARK 465 ARG Q 138 REMARK 465 TYR Q 139 REMARK 465 GLY Q 140 REMARK 465 SER Q 141 REMARK 465 HIS Q 142 REMARK 465 HIS Q 143 REMARK 465 HIS Q 144 REMARK 465 HIS Q 145 REMARK 465 HIS Q 146 REMARK 465 HIS Q 147 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN D 42 58.78 38.86 REMARK 500 ALA D 43 82.75 -150.75 REMARK 500 ALA D 51 -4.79 67.80 REMARK 500 ARG D 91 15.48 -140.29 REMARK 500 PRO D 95 76.66 -67.35 REMARK 500 SER D 127 51.03 -94.13 REMARK 500 THR D 129 -173.07 57.99 REMARK 500 GLU D 165 51.56 -93.44 REMARK 500 PRO C 156 -159.03 -78.42 REMARK 500 GLU C 157 58.58 -117.45 REMARK 500 LYS A 65 -133.73 57.64 REMARK 500 ASP B 30 -136.02 57.99 REMARK 500 ALA B 51 -5.24 68.04 REMARK 500 GLN Q 33 -0.68 63.95 REMARK 500 ASP Q 35 73.83 44.14 REMARK 500 GLU Q 36 -37.82 -34.60 REMARK 500 TYR Q 39 -172.45 81.08 REMARK 500 GLN Q 48 174.30 63.38 REMARK 500 PHE Q 77 55.35 -93.69 REMARK 500 ARG Q 102 -4.27 67.69 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 GLU C 157 PRO C 158 148.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 8SJ6 D 1 214 PDB 8SJ6 8SJ6 1 214 DBREF 8SJ6 C 1 225 PDB 8SJ6 8SJ6 1 225 DBREF 8SJ6 A 1 221 PDB 8SJ6 8SJ6 1 221 DBREF 8SJ6 B 1 215 PDB 8SJ6 8SJ6 1 215 DBREF1 8SJ6 Q 5 139 UNP A0A445BYI5_ARAHY DBREF2 8SJ6 Q A0A445BYI5 26 160 SEQADV 8SJ6 GLY Q 140 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 SER Q 141 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 142 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 143 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 144 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 145 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 146 UNP A0A445BYI EXPRESSION TAG SEQADV 8SJ6 HIS Q 147 UNP A0A445BYI EXPRESSION TAG SEQRES 1 D 214 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 D 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 214 PRO SER ALA GLY ARG PHE LEU ALA TRP TYR GLN GLN ARG SEQRES 4 D 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 214 LYS ARG ALA THR ASP THR PRO ALA ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE ASN LEU THR ILE ALA SER LEU SEQRES 7 D 214 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS ARG SEQRES 8 D 214 SER ASN TRP PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 225 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 225 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER ASP SEQRES 3 C 225 ALA SER ILE ASP THR PRO SER TYR PHE TRP SER TRP ILE SEQRES 4 C 225 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY SER SEQRES 5 C 225 ILE TYR TYR THR GLY ASN LYS TYR SER ASN PRO SER LEU SEQRES 6 C 225 LYS SER ARG VAL THR MET SER VAL ASP THR PRO LYS ARG SEQRES 7 C 225 GLN PHE SER LEU ARG LEU SER SER VAL THR ALA ALA ASP SEQRES 8 C 225 THR ALA VAL TYR TYR CYS ALA ARG TYR VAL ASP TYR VAL SEQRES 9 C 225 TRP LEU ARG ALA PHE ASP ILE TRP GLY GLN GLY THR ARG SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 A 221 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 221 PRO GLY ARG SER LEU ARG LEU SER CYS VAL GLY SER GLY SEQRES 3 A 221 PHE THR PHE ARG ARG ASP ALA LYS TYR TRP VAL ARG GLN SEQRES 4 A 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 A 221 HIS ASP GLY GLY GLU GLU ASP TYR ALA GLU SER VAL LYS SEQRES 6 A 221 GLY ARG PHE THR ILE SER ARG ASP ASN SER ARG GLU THR SEQRES 7 A 221 VAL TYR LEU GLU MET ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 A 221 ALA VAL TYR TYR CYS ALA THR THR ARG SER GLY TRP TYR SEQRES 9 A 221 PHE ASP TYR TRP GLY GLN GLY ALA LEU VAL THR VAL SER SEQRES 10 A 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 A 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 A 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 A 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 A 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 A 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 A 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 215 SER PRO GLY ALA ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 215 GLN SER VAL ASP THR TYR LEU ALA TRP TYR GLN GLN ARG SEQRES 4 B 215 ARG GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 215 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 B 215 ASN ASN TRP ARG THR TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE ASN ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 Q 143 GLU LEU GLN GLY ASP ARG ARG CYS GLN SER GLN LEU GLU SEQRES 2 Q 143 ARG ALA ASN LEU ARG PRO CYS GLU GLN HIS LEU MET GLN SEQRES 3 Q 143 LYS ILE GLN ARG ASP GLU ASP SER TYR GLU ARG ASP PRO SEQRES 4 Q 143 TYR SER PRO SER GLN ASP PRO TYR SER PRO SER PRO TYR SEQRES 5 Q 143 ASP ARG ARG GLY ALA GLY SER SER GLN HIS GLN GLU ARG SEQRES 6 Q 143 CYS CYS ASN GLU LEU ASN GLU PHE GLU ASN ASN GLN ARG SEQRES 7 Q 143 CYS MET CYS GLU ALA LEU GLN GLN ILE MET GLU ASN GLN SEQRES 8 Q 143 SER ASP ARG LEU GLN GLY ARG GLN GLN GLU GLN GLN PHE SEQRES 9 Q 143 LYS ARG GLU LEU ARG ASN LEU PRO GLN GLN CYS GLY LEU SEQRES 10 Q 143 ARG ALA PRO GLN ARG CYS ASP LEU ASP VAL GLU SER GLY SEQRES 11 Q 143 GLY ARG ASP ARG TYR GLY SER HIS HIS HIS HIS HIS HIS HELIX 1 AA1 GLU D 79 PHE D 83 5 5 HELIX 2 AA2 SER D 121 SER D 127 1 7 HELIX 3 AA3 SER D 182 HIS D 189 1 8 HELIX 4 AA4 THR C 88 THR C 92 5 5 HELIX 5 AA5 SER C 165 ALA C 167 5 3 HELIX 6 AA6 SER C 196 LEU C 198 5 3 HELIX 7 AA7 VAL A 64 GLY A 66 5 3 HELIX 8 AA8 ARG A 87 THR A 91 5 5 HELIX 9 AA9 SER A 192 THR A 196 5 5 HELIX 10 AB1 LYS A 206 ASN A 209 5 4 HELIX 11 AB2 GLU B 79 PHE B 83 5 5 HELIX 12 AB3 SER B 122 LYS B 127 1 6 HELIX 13 AB4 LYS B 184 HIS B 190 1 7 HELIX 14 AB5 CYS Q 12 ALA Q 19 1 8 HELIX 15 AB6 LEU Q 21 GLN Q 33 1 13 HELIX 16 AB7 HIS Q 66 GLU Q 76 1 11 HELIX 17 AB8 ASN Q 80 GLN Q 95 1 16 HELIX 18 AB9 GLN Q 103 ASN Q 114 1 12 HELIX 19 AC1 ASN Q 114 CYS Q 119 1 6 SHEET 1 AA1 4 LEU D 4 GLN D 6 0 SHEET 2 AA1 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AA1 4 ASP D 70 ILE D 75 -1 O LEU D 73 N LEU D 21 SHEET 4 AA1 4 PHE D 62 GLY D 66 -1 N SER D 63 O THR D 74 SHEET 1 AA2 6 THR D 10 LEU D 13 0 SHEET 2 AA2 6 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AA2 6 VAL D 85 GLN D 89 -1 N TYR D 86 O THR D 102 SHEET 4 AA2 6 ALA D 34 GLN D 38 -1 N GLN D 38 O VAL D 85 SHEET 5 AA2 6 ARG D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AA2 6 LYS D 53 ARG D 54 -1 O LYS D 53 N TYR D 49 SHEET 1 AA3 4 VAL D 115 PHE D 118 0 SHEET 2 AA3 4 VAL D 132 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AA3 4 TYR D 173 LEU D 179 -1 O LEU D 179 N VAL D 132 SHEET 4 AA3 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AA4 3 LYS D 145 VAL D 150 0 SHEET 2 AA4 3 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 3 AA4 3 VAL D 205 ASN D 210 -1 O LYS D 207 N CYS D 194 SHEET 1 AA5 4 LEU C 4 SER C 7 0 SHEET 2 AA5 4 LEU C 18 VAL C 24 -1 O THR C 23 N GLN C 5 SHEET 3 AA5 4 GLN C 79 LEU C 84 -1 O LEU C 82 N LEU C 20 SHEET 4 AA5 4 VAL C 69 ASP C 74 -1 N ASP C 74 O GLN C 79 SHEET 1 AA6 6 LEU C 11 VAL C 12 0 SHEET 2 AA6 6 THR C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AA6 6 ALA C 93 VAL C 101 -1 N TYR C 95 O THR C 116 SHEET 4 AA6 6 TYR C 34 GLN C 41 -1 N ILE C 39 O TYR C 96 SHEET 5 AA6 6 GLU C 48 ILE C 53 -1 O ILE C 53 N TRP C 36 SHEET 6 AA6 6 LYS C 59 SER C 61 -1 O TYR C 60 N SER C 52 SHEET 1 AA7 4 LEU C 11 VAL C 12 0 SHEET 2 AA7 4 THR C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AA7 4 ALA C 93 VAL C 101 -1 N TYR C 95 O THR C 116 SHEET 4 AA7 4 PHE C 109 TRP C 112 -1 O ILE C 111 N ARG C 99 SHEET 1 AA8 4 SER C 129 LEU C 133 0 SHEET 2 AA8 4 THR C 144 TYR C 154 -1 O LYS C 152 N SER C 129 SHEET 3 AA8 4 TYR C 185 PRO C 194 -1 O VAL C 191 N LEU C 147 SHEET 4 AA8 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AA9 4 SER C 129 LEU C 133 0 SHEET 2 AA9 4 THR C 144 TYR C 154 -1 O LYS C 152 N SER C 129 SHEET 3 AA9 4 TYR C 185 PRO C 194 -1 O VAL C 191 N LEU C 147 SHEET 4 AA9 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB1 3 THR C 160 TRP C 163 0 SHEET 2 AB1 3 TYR C 203 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB1 3 THR C 214 VAL C 220 -1 O LYS C 218 N CYS C 205 SHEET 1 AB2 4 GLN A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O VAL A 23 N VAL A 5 SHEET 3 AB2 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AB2 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AB3 6 GLY A 10 VAL A 12 0 SHEET 2 AB3 6 ALA A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AB3 6 ALA A 92 THR A 99 -1 N TYR A 94 O ALA A 112 SHEET 4 AB3 6 ALA A 33 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AB3 6 LEU A 45 ILE A 51 -1 O ILE A 51 N LYS A 34 SHEET 6 AB3 6 GLU A 58 TYR A 60 -1 O ASP A 59 N ALA A 50 SHEET 1 AB4 4 GLY A 10 VAL A 12 0 SHEET 2 AB4 4 ALA A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AB4 4 ALA A 92 THR A 99 -1 N TYR A 94 O ALA A 112 SHEET 4 AB4 4 TYR A 107 TRP A 108 -1 N TYR A 107 O THR A 98 SHEET 1 AB5 4 SER A 125 LEU A 129 0 SHEET 2 AB5 4 ALA A 141 TYR A 150 -1 O LEU A 146 N PHE A 127 SHEET 3 AB5 4 TYR A 181 VAL A 189 -1 O LEU A 183 N VAL A 147 SHEET 4 AB5 4 VAL A 168 THR A 170 -1 N HIS A 169 O VAL A 186 SHEET 1 AB6 4 SER A 125 LEU A 129 0 SHEET 2 AB6 4 ALA A 141 TYR A 150 -1 O LEU A 146 N PHE A 127 SHEET 3 AB6 4 TYR A 181 VAL A 189 -1 O LEU A 183 N VAL A 147 SHEET 4 AB6 4 VAL A 174 LEU A 175 -1 N VAL A 174 O SER A 182 SHEET 1 AB7 3 THR A 156 TRP A 159 0 SHEET 2 AB7 3 TYR A 199 HIS A 205 -1 O ASN A 202 N SER A 158 SHEET 3 AB7 3 THR A 210 VAL A 216 -1 O THR A 210 N HIS A 205 SHEET 1 AB8 4 LEU B 4 SER B 7 0 SHEET 2 AB8 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N SER B 65 O THR B 72 SHEET 1 AB9 6 THR B 10 LEU B 13 0 SHEET 2 AB9 6 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 11 SHEET 3 AB9 6 VAL B 85 ASN B 92 -1 N TYR B 86 O THR B 103 SHEET 4 AB9 6 ALA B 34 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AB9 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB9 6 LYS B 53 ARG B 54 -1 O LYS B 53 N TYR B 49 SHEET 1 AC1 4 THR B 10 LEU B 13 0 SHEET 2 AC1 4 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 11 SHEET 3 AC1 4 VAL B 85 ASN B 92 -1 N TYR B 86 O THR B 103 SHEET 4 AC1 4 THR B 96 PHE B 99 -1 O THR B 96 N ASN B 92 SHEET 1 AC2 4 SER B 115 PHE B 119 0 SHEET 2 AC2 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AC2 4 TYR B 174 SER B 183 -1 O LEU B 176 N LEU B 137 SHEET 4 AC2 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AC3 4 ALA B 154 LEU B 155 0 SHEET 2 AC3 4 ALA B 145 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AC3 4 TYR B 193 HIS B 199 -1 O GLU B 196 N GLN B 148 SHEET 4 AC3 4 VAL B 206 PHE B 210 -1 O LYS B 208 N CYS B 195 SSBOND 1 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 2 CYS D 134 CYS D 194 1555 1555 2.03 SSBOND 3 CYS C 149 CYS C 205 1555 1555 2.03 SSBOND 4 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 5 CYS A 145 CYS A 201 1555 1555 2.03 SSBOND 6 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 7 CYS B 135 CYS B 195 1555 1555 2.03 SSBOND 8 CYS Q 12 CYS Q 83 1555 1555 2.03 SSBOND 9 CYS Q 24 CYS Q 70 1555 1555 2.03 SSBOND 10 CYS Q 71 CYS Q 119 1555 1555 2.03 SSBOND 11 CYS Q 85 CYS Q 127 1555 1555 2.03 CISPEP 1 TYR D 140 PRO D 141 0 4.99 CISPEP 2 PHE C 155 PRO C 156 0 -1.35 CISPEP 3 PHE A 151 PRO A 152 0 -2.64 CISPEP 4 GLU A 153 PRO A 154 0 -4.69 CISPEP 5 SER B 7 PRO B 8 0 -1.70 CISPEP 6 TYR B 141 PRO B 142 0 1.89 CRYST1 44.400 182.892 194.175 90.00 90.00 90.00 P 2 21 21 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 0.022523 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005468 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005150 0.00000