HEADER DE NOVO PROTEIN 13-DEC-24 9MIN TITLE STRUCTURE OF A DESIGNED MINIBINDER TO NYESO1-A*02:01 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I ANTIGEN; COMPND 3 CHAIN: A, F; COMPND 4 SYNONYM: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN A ALPHA CHAIN,MHC COMPND 5 CLASS I ANTIGEN,MAJOR HISTOCOMPATIBILITY COMPLEX,CLASS I,A; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 10 CHAIN: B, G; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: CANCER/TESTIS ANTIGEN 1; COMPND 15 CHAIN: C, H; COMPND 16 SYNONYM: AUTOIMMUNOGENIC CANCER/TESTIS ANTIGEN NY-ESO-1,CANCER/TESTIS COMPND 17 ANTIGEN 6.1,CT6.1,L ANTIGEN FAMILY MEMBER 2,LAGE-2; COMPND 18 ENGINEERED: YES; COMPND 19 MUTATION: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: DESIGNED MINIBINDER KH46; COMPND 22 CHAIN: D, I; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: NANOBODY AD01; COMPND 26 CHAIN: E, J; COMPND 27 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HLA-A; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 22 ORGANISM_TAXID: 32630; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 27 ORGANISM_TAXID: 9844; SOURCE 28 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293 KEYWDS COMPLEX, IMMUNE SYSTEM, DE NOVO PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.M.JUDE,K.D.HOUSEHOLDER REVDAT 1 06-AUG-25 9MIN 0 JRNL AUTH K.D.HOUSEHOLDER,X.XIANG,K.M.JUDE,A.DENG,M.OBENAUS,Y.ZHAO, JRNL AUTH 2 S.C.WILSON,X.CHEN,N.WANG,K.C.GARCIA JRNL TITL DE NOVO DESIGN AND STRUCTURE OF A PEPTIDE-CENTRIC TCR MIMIC JRNL TITL 2 BINDING MODULE. JRNL REF SCIENCE V. 389 375 2025 JRNL REFN ESSN 1095-9203 JRNL PMID 40705894 JRNL DOI 10.1126/SCIENCE.ADV3813 REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.27 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 91895 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.255 REMARK 3 R VALUE (WORKING SET) : 0.255 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.510 REMARK 3 FREE R VALUE TEST SET COUNT : 1384 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 49.2700 - 4.4200 0.97 9203 135 0.2215 0.2168 REMARK 3 2 4.4200 - 3.5100 0.98 9043 141 0.2060 0.2385 REMARK 3 3 3.5100 - 3.0600 0.99 9042 142 0.2260 0.2313 REMARK 3 4 3.0600 - 2.7800 0.99 9066 142 0.2465 0.2803 REMARK 3 5 2.7800 - 2.5800 1.00 9059 138 0.2713 0.2708 REMARK 3 6 2.5800 - 2.4300 1.00 9066 138 0.2955 0.3017 REMARK 3 7 2.4300 - 2.3100 1.00 9004 134 0.3204 0.3861 REMARK 3 8 2.3100 - 2.2100 1.00 9008 138 0.3393 0.3536 REMARK 3 9 2.2100 - 2.1200 1.00 9026 143 0.3648 0.3613 REMARK 3 10 2.1200 - 2.0500 1.00 8994 133 0.3961 0.4129 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.316 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.493 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.16 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.86 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 : 0.003 10422 REMARK 3 ANGLE : 0.521 14062 REMARK 3 CHIRALITY : 0.038 1488 REMARK 3 PLANARITY : 0.005 1794 REMARK 3 DIHEDRAL : 13.915 3870 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 1:181) REMARK 3 ORIGIN FOR THE GROUP (A): -21.2692 -24.9045 12.0406 REMARK 3 T TENSOR REMARK 3 T11: 0.3194 T22: 0.2704 REMARK 3 T33: 0.3437 T12: 0.0390 REMARK 3 T13: 0.0356 T23: -0.0888 REMARK 3 L TENSOR REMARK 3 L11: 4.2440 L22: 3.5211 REMARK 3 L33: 2.1435 L12: 0.2635 REMARK 3 L13: 0.5384 L23: -0.6182 REMARK 3 S TENSOR REMARK 3 S11: -0.0584 S12: -0.2085 S13: 0.1592 REMARK 3 S21: 0.4859 S22: 0.0457 S23: 0.0428 REMARK 3 S31: -0.1455 S32: -0.1500 S33: 0.0037 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 182:275) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4806 -35.9471 -21.4915 REMARK 3 T TENSOR REMARK 3 T11: 0.8013 T22: 0.3019 REMARK 3 T33: 0.4861 T12: -0.0580 REMARK 3 T13: 0.1205 T23: -0.1052 REMARK 3 L TENSOR REMARK 3 L11: 2.1229 L22: 2.9958 REMARK 3 L33: 4.6449 L12: -1.1587 REMARK 3 L13: -0.1018 L23: 1.6051 REMARK 3 S TENSOR REMARK 3 S11: -0.1968 S12: 0.1696 S13: -0.4639 REMARK 3 S21: -1.0593 S22: 0.0760 S23: -0.1777 REMARK 3 S31: 1.0453 S32: -0.0582 S33: 0.0064 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN B AND RESID 0:99) REMARK 3 ORIGIN FOR THE GROUP (A): -18.9650 -15.9016 -13.1223 REMARK 3 T TENSOR REMARK 3 T11: 0.2306 T22: 0.2916 REMARK 3 T33: 0.2998 T12: -0.0021 REMARK 3 T13: 0.0758 T23: -0.1128 REMARK 3 L TENSOR REMARK 3 L11: 1.4709 L22: 3.2181 REMARK 3 L33: 2.9741 L12: -0.5379 REMARK 3 L13: 1.4677 L23: -1.6504 REMARK 3 S TENSOR REMARK 3 S11: -0.0700 S12: 0.0052 S13: 0.0354 REMARK 3 S21: -0.0943 S22: -0.1163 S23: -0.2762 REMARK 3 S31: 0.0818 S32: -0.0343 S33: 0.1938 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN D AND RESID 1:8) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9858 -0.6506 27.0430 REMARK 3 T TENSOR REMARK 3 T11: 2.2505 T22: 1.9849 REMARK 3 T33: 0.4431 T12: -0.7456 REMARK 3 T13: 0.0456 T23: -0.0244 REMARK 3 L TENSOR REMARK 3 L11: 1.2106 L22: 0.2897 REMARK 3 L33: 1.3364 L12: -0.4742 REMARK 3 L13: 0.8828 L23: -0.0810 REMARK 3 S TENSOR REMARK 3 S11: -0.1291 S12: -0.0087 S13: 0.1378 REMARK 3 S21: 0.4947 S22: -0.4382 S23: -0.0579 REMARK 3 S31: -0.9747 S32: 0.1112 S33: 0.2681 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN D AND RESID 9:48) REMARK 3 ORIGIN FOR THE GROUP (A): -33.2848 -18.0828 33.0154 REMARK 3 T TENSOR REMARK 3 T11: 2.1561 T22: 1.2140 REMARK 3 T33: 0.6955 T12: 0.0284 REMARK 3 T13: 0.7378 T23: -0.3255 REMARK 3 L TENSOR REMARK 3 L11: 1.4645 L22: 1.3348 REMARK 3 L33: 4.7819 L12: -0.8954 REMARK 3 L13: 0.8010 L23: 1.3865 REMARK 3 S TENSOR REMARK 3 S11: 0.1239 S12: -1.3405 S13: 0.5186 REMARK 3 S21: 0.4487 S22: 0.0415 S23: 0.6234 REMARK 3 S31: -0.6405 S32: 0.0192 S33: 0.4611 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN D AND RESID 49:74) REMARK 3 ORIGIN FOR THE GROUP (A): -12.3610 -14.3141 29.7928 REMARK 3 T TENSOR REMARK 3 T11: 1.9662 T22: 1.6655 REMARK 3 T33: 0.8965 T12: -0.8461 REMARK 3 T13: -0.1919 T23: 0.2286 REMARK 3 L TENSOR REMARK 3 L11: 6.6376 L22: 3.5222 REMARK 3 L33: 5.1223 L12: 0.9833 REMARK 3 L13: 2.5332 L23: 0.1908 REMARK 3 S TENSOR REMARK 3 S11: 0.1539 S12: -1.1049 S13: 0.7150 REMARK 3 S21: 1.0432 S22: -1.5136 S23: -0.6864 REMARK 3 S31: -1.4836 S32: 1.6089 S33: 1.1165 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN D AND RESID 75:119) REMARK 3 ORIGIN FOR THE GROUP (A): -26.5461 -28.5613 32.9604 REMARK 3 T TENSOR REMARK 3 T11: 1.4440 T22: 1.2221 REMARK 3 T33: 0.4074 T12: -0.2085 REMARK 3 T13: 0.0640 T23: 0.0863 REMARK 3 L TENSOR REMARK 3 L11: 3.1876 L22: 1.5949 REMARK 3 L33: 6.2335 L12: -0.6295 REMARK 3 L13: 2.0484 L23: 2.2435 REMARK 3 S TENSOR REMARK 3 S11: 0.5197 S12: -0.0651 S13: -0.4958 REMARK 3 S21: 1.6738 S22: -0.0092 S23: -0.2098 REMARK 3 S31: -0.8265 S32: 0.0847 S33: -0.3745 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN D AND RESID 120:128) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2895 -5.2245 37.3025 REMARK 3 T TENSOR REMARK 3 T11: 1.7526 T22: 1.4157 REMARK 3 T33: 1.0605 T12: -0.3084 REMARK 3 T13: 0.2835 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 0.9361 L22: 5.1668 REMARK 3 L33: 2.9148 L12: 2.1801 REMARK 3 L13: -1.6595 L23: -3.8663 REMARK 3 S TENSOR REMARK 3 S11: -0.1913 S12: 0.6869 S13: -0.1531 REMARK 3 S21: 0.2211 S22: -0.7175 S23: 0.3366 REMARK 3 S31: -1.1616 S32: 0.7323 S33: 0.7220 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN E AND RESID 3:26) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3591 6.1580 -16.3858 REMARK 3 T TENSOR REMARK 3 T11: 0.2601 T22: 0.3676 REMARK 3 T33: 0.6939 T12: -0.0345 REMARK 3 T13: -0.0095 T23: -0.1161 REMARK 3 L TENSOR REMARK 3 L11: 5.1209 L22: 3.2927 REMARK 3 L33: 4.9750 L12: 1.0709 REMARK 3 L13: 1.9375 L23: -0.7157 REMARK 3 S TENSOR REMARK 3 S11: -0.0256 S12: 0.2633 S13: 0.4451 REMARK 3 S21: -0.0198 S22: 0.1329 S23: -0.7605 REMARK 3 S31: -0.1420 S32: 0.8200 S33: -0.0708 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN E AND RESID 27:32) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5803 0.9174 -32.2681 REMARK 3 T TENSOR REMARK 3 T11: 0.6128 T22: 0.9471 REMARK 3 T33: 0.5623 T12: -0.0065 REMARK 3 T13: -0.1296 T23: -0.0956 REMARK 3 L TENSOR REMARK 3 L11: 1.0268 L22: 0.2929 REMARK 3 L33: 0.0209 L12: -0.4201 REMARK 3 L13: -0.0477 L23: -0.0308 REMARK 3 S TENSOR REMARK 3 S11: -0.2208 S12: 2.1179 S13: 0.8350 REMARK 3 S21: -1.6519 S22: -0.6937 S23: 0.2332 REMARK 3 S31: -0.5431 S32: -0.4670 S33: 0.4896 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN E AND RESID 33:118) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0734 1.4883 -14.0497 REMARK 3 T TENSOR REMARK 3 T11: 0.2838 T22: 0.2152 REMARK 3 T33: 0.3696 T12: -0.0376 REMARK 3 T13: 0.0013 T23: -0.0800 REMARK 3 L TENSOR REMARK 3 L11: 3.9905 L22: 2.4471 REMARK 3 L33: 1.2269 L12: -1.5344 REMARK 3 L13: -0.2072 L23: -0.8927 REMARK 3 S TENSOR REMARK 3 S11: -0.0877 S12: -0.1942 S13: -0.0713 REMARK 3 S21: 0.1409 S22: 0.0121 S23: -0.3162 REMARK 3 S31: -0.0694 S32: 0.1516 S33: 0.0649 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN F AND RESID 1:180) REMARK 3 ORIGIN FOR THE GROUP (A): -27.5689 24.8953 12.1301 REMARK 3 T TENSOR REMARK 3 T11: 0.2188 T22: 0.2949 REMARK 3 T33: 0.2947 T12: 0.0306 REMARK 3 T13: 0.0162 T23: -0.0787 REMARK 3 L TENSOR REMARK 3 L11: 4.4500 L22: 3.7497 REMARK 3 L33: 1.9840 L12: 0.3918 REMARK 3 L13: -0.3262 L23: 0.3889 REMARK 3 S TENSOR REMARK 3 S11: 0.0077 S12: -0.3840 S13: -0.0429 REMARK 3 S21: 0.2596 S22: -0.0473 S23: -0.0281 REMARK 3 S31: -0.0651 S32: 0.0416 S33: 0.0132 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN F AND RESID 181:276) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3629 35.8453 -21.3575 REMARK 3 T TENSOR REMARK 3 T11: 1.0060 T22: 0.2925 REMARK 3 T33: 0.5229 T12: -0.0496 REMARK 3 T13: 0.0428 T23: -0.0632 REMARK 3 L TENSOR REMARK 3 L11: 2.2379 L22: 4.2071 REMARK 3 L33: 3.4952 L12: 0.1553 REMARK 3 L13: 0.5085 L23: -0.8277 REMARK 3 S TENSOR REMARK 3 S11: -0.1674 S12: 0.2836 S13: 0.2725 REMARK 3 S21: -1.4869 S22: 0.1663 S23: 0.2385 REMARK 3 S31: -0.7560 S32: 0.1387 S33: 0.1308 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN G AND RESID 0:99) REMARK 3 ORIGIN FOR THE GROUP (A): -29.7199 15.8480 -13.1158 REMARK 3 T TENSOR REMARK 3 T11: 0.2852 T22: 0.1885 REMARK 3 T33: 0.3970 T12: -0.0046 REMARK 3 T13: -0.0276 T23: -0.0895 REMARK 3 L TENSOR REMARK 3 L11: 3.4853 L22: 1.5414 REMARK 3 L33: 2.9276 L12: -0.1511 REMARK 3 L13: -0.7986 L23: 0.6929 REMARK 3 S TENSOR REMARK 3 S11: 0.0141 S12: 0.0546 S13: 0.0701 REMARK 3 S21: -0.2888 S22: -0.0451 S23: 0.1193 REMARK 3 S31: -0.2561 S32: -0.0733 S33: 0.0455 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN I AND RESID 1:52) REMARK 3 ORIGIN FOR THE GROUP (A): -18.4520 15.4058 31.6532 REMARK 3 T TENSOR REMARK 3 T11: 1.6776 T22: 1.0262 REMARK 3 T33: 0.5481 T12: 0.0691 REMARK 3 T13: -0.4032 T23: 0.1062 REMARK 3 L TENSOR REMARK 3 L11: 0.9463 L22: 1.9549 REMARK 3 L33: 4.4797 L12: -0.7490 REMARK 3 L13: -1.1713 L23: -1.1765 REMARK 3 S TENSOR REMARK 3 S11: 0.4046 S12: -1.0531 S13: -0.6952 REMARK 3 S21: 0.5629 S22: -0.2937 S23: -0.9822 REMARK 3 S31: 1.4019 S32: -0.1856 S33: 0.0229 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN I AND RESID 53:75) REMARK 3 ORIGIN FOR THE GROUP (A): -37.5998 13.9854 30.2332 REMARK 3 T TENSOR REMARK 3 T11: 1.9138 T22: 1.1858 REMARK 3 T33: 0.9500 T12: -1.1388 REMARK 3 T13: 0.4230 T23: -0.2002 REMARK 3 L TENSOR REMARK 3 L11: 2.6305 L22: 0.9764 REMARK 3 L33: 1.7688 L12: 1.5154 REMARK 3 L13: -0.9315 L23: -0.9236 REMARK 3 S TENSOR REMARK 3 S11: -0.2339 S12: -0.3690 S13: -0.6470 REMARK 3 S21: 0.8945 S22: -0.9619 S23: 1.0922 REMARK 3 S31: 0.7120 S32: -0.7897 S33: 0.5188 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN I AND RESID 76:127) REMARK 3 ORIGIN FOR THE GROUP (A): -23.8775 25.4177 33.5851 REMARK 3 T TENSOR REMARK 3 T11: 0.9504 T22: 0.7734 REMARK 3 T33: 0.2678 T12: -0.2546 REMARK 3 T13: -0.0237 T23: -0.1430 REMARK 3 L TENSOR REMARK 3 L11: 1.9061 L22: 4.1299 REMARK 3 L33: 3.7275 L12: -1.7565 REMARK 3 L13: 1.1040 L23: 1.6287 REMARK 3 S TENSOR REMARK 3 S11: 0.5830 S12: -1.0551 S13: 0.4059 REMARK 3 S21: 1.5925 S22: -0.0857 S23: 0.4722 REMARK 3 S31: 0.0088 S32: 0.8379 S33: -0.2470 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN J AND RESID 3:28) REMARK 3 ORIGIN FOR THE GROUP (A): -50.8049 -5.7784 -17.4183 REMARK 3 T TENSOR REMARK 3 T11: 0.3571 T22: 0.2742 REMARK 3 T33: 0.4684 T12: -0.0450 REMARK 3 T13: -0.0093 T23: -0.1463 REMARK 3 L TENSOR REMARK 3 L11: 4.3813 L22: 5.0060 REMARK 3 L33: 5.4794 L12: 0.7448 REMARK 3 L13: -1.4665 L23: -0.8295 REMARK 3 S TENSOR REMARK 3 S11: -0.1359 S12: 0.3124 S13: -0.3525 REMARK 3 S21: -0.2802 S22: 0.2114 S23: 0.6589 REMARK 3 S31: 0.6317 S32: -0.6578 S33: -0.0525 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN J AND RESID 29:34) REMARK 3 ORIGIN FOR THE GROUP (A): -38.0372 -0.4297 -29.9849 REMARK 3 T TENSOR REMARK 3 T11: 0.6610 T22: 1.0138 REMARK 3 T33: -0.0328 T12: 0.0324 REMARK 3 T13: -0.0802 T23: -0.2049 REMARK 3 L TENSOR REMARK 3 L11: 2.5329 L22: 6.5184 REMARK 3 L33: 1.8618 L12: -0.4930 REMARK 3 L13: 1.2007 L23: 2.6389 REMARK 3 S TENSOR REMARK 3 S11: 0.2606 S12: 0.8866 S13: -0.4295 REMARK 3 S21: -1.6668 S22: -0.2341 S23: 0.4788 REMARK 3 S31: 0.3846 S32: -0.6159 S33: 0.0740 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN J AND RESID 35:118) REMARK 3 ORIGIN FOR THE GROUP (A): -43.8015 -1.5723 -13.7970 REMARK 3 T TENSOR REMARK 3 T11: 0.2639 T22: 0.3109 REMARK 3 T33: 0.2941 T12: 0.0197 REMARK 3 T13: -0.0070 T23: -0.1099 REMARK 3 L TENSOR REMARK 3 L11: 3.9240 L22: 3.3025 REMARK 3 L33: 1.5450 L12: 0.5602 REMARK 3 L13: -0.8713 L23: -0.5959 REMARK 3 S TENSOR REMARK 3 S11: -0.1406 S12: -0.0531 S13: -0.0089 REMARK 3 S21: -0.0612 S22: 0.0045 S23: 0.4821 REMARK 3 S31: -0.1767 S32: -0.0958 S33: 0.0971 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 5 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 275 or REMARK 3 resid 302)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 1 through 275 or REMARK 3 resid 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid -1 through 8 or REMARK 3 resid 10 through 99 or resid 101 through REMARK 3 104)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid -1 through 8 or REMARK 3 resid 10 through 99 or resid 101 through REMARK 3 103)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and resid 1 through 127) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "I" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_5 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "E" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "J" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9MIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000291052. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-NOV-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 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 EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92563 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050 REMARK 200 RESOLUTION RANGE LOW (A) : 49.270 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 23.30 REMARK 200 R MERGE (I) : 0.32520 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.4900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 24.00 REMARK 200 R MERGE FOR SHELL (I) : 3.47100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.450 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 (%): 50.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE 0.1 M BIS-TRIS REMARK 280 PH 5.5 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 47.72600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.87150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.26800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.87150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.72600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.26800 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I, 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 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 MET A -1 REMARK 465 GLY A 0 REMARK 465 PRO A 276 REMARK 465 MET D -1 REMARK 465 GLY D 0 REMARK 465 ALA D 129 REMARK 465 ALA D 130 REMARK 465 ALA D 131 REMARK 465 ALA D 132 REMARK 465 LEU D 133 REMARK 465 GLU D 134 REMARK 465 GLY E 119 REMARK 465 ALA E 120 REMARK 465 PRO E 121 REMARK 465 MET F -1 REMARK 465 GLY F 0 REMARK 465 MET I -1 REMARK 465 GLY I 0 REMARK 465 ALA I 128 REMARK 465 ALA I 129 REMARK 465 ALA I 130 REMARK 465 ALA I 131 REMARK 465 ALA I 132 REMARK 465 LEU I 133 REMARK 465 GLU I 134 REMARK 465 GLY J 119 REMARK 465 ALA J 120 REMARK 465 PRO J 121 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 LYS E 5 CG CD CE NZ REMARK 470 PHE E 31 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN E 110 CG CD OE1 NE2 REMARK 470 SER E 118 OG REMARK 470 LYS J 5 CG CD CE NZ REMARK 470 PHE J 31 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN J 110 CG CD OE1 NE2 REMARK 470 SER J 118 OG 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 ASP A 29 -130.28 59.70 REMARK 500 TYR A 123 -71.73 -104.23 REMARK 500 PRO A 210 -174.24 -69.54 REMARK 500 LYS A 243 142.19 -170.37 REMARK 500 ILE B 1 -0.79 -58.10 REMARK 500 SER B 57 -168.39 -100.56 REMARK 500 ASP B 98 42.87 -109.89 REMARK 500 ASN E 34 -93.59 -93.35 REMARK 500 ASP F 29 -124.46 59.74 REMARK 500 LEU F 110 -72.82 -104.46 REMARK 500 TYR F 123 -70.68 -111.64 REMARK 500 GLN F 180 32.27 -87.09 REMARK 500 ASP G 98 40.58 -107.74 REMARK 500 PHE J 31 12.46 -140.54 REMARK 500 ASN J 34 -92.77 -93.75 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MIN A 0 276 UNP Q53Z42 Q53Z42_HUMAN 24 300 DBREF 9MIN B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 9MIN C 1 9 UNP P78358 CTG1B_HUMAN 157 165 DBREF 9MIN D -1 134 PDB 9MIN 9MIN -1 134 DBREF 9MIN E 3 121 PDB 9MIN 9MIN 3 121 DBREF 9MIN F 0 276 UNP Q53Z42 Q53Z42_HUMAN 24 300 DBREF 9MIN G 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 9MIN H 1 9 UNP P78358 CTG1B_HUMAN 157 165 DBREF 9MIN I -1 134 PDB 9MIN 9MIN -1 134 DBREF 9MIN J 3 121 PDB 9MIN 9MIN 3 121 SEQADV 9MIN MET A -1 UNP Q53Z42 INITIATING METHIONINE SEQADV 9MIN GLY A 0 UNP Q53Z42 ALA 24 CONFLICT SEQADV 9MIN MET B -1 UNP P61769 INITIATING METHIONINE SEQADV 9MIN GLY B 0 UNP P61769 EXPRESSION TAG SEQADV 9MIN VAL C 9 UNP P78358 CYS 165 ENGINEERED MUTATION SEQADV 9MIN MET F -1 UNP Q53Z42 INITIATING METHIONINE SEQADV 9MIN GLY F 0 UNP Q53Z42 ALA 24 CONFLICT SEQADV 9MIN MET G -1 UNP P61769 INITIATING METHIONINE SEQADV 9MIN GLY G 0 UNP P61769 EXPRESSION TAG SEQADV 9MIN VAL H 9 UNP P78358 CYS 165 ENGINEERED MUTATION SEQRES 1 A 278 MET GLY GLY SER HIS SER MET ARG TYR PHE PHE THR SER SEQRES 2 A 278 VAL SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA SEQRES 3 A 278 VAL GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SEQRES 4 A 278 SER ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO SEQRES 5 A 278 TRP ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU SEQRES 6 A 278 THR ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL SEQRES 7 A 278 ASP LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU SEQRES 8 A 278 ALA GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP SEQRES 9 A 278 VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN SEQRES 10 A 278 TYR ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU SEQRES 11 A 278 ASP LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN SEQRES 12 A 278 THR THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU SEQRES 13 A 278 GLN LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP SEQRES 14 A 278 LEU ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN SEQRES 15 A 278 ARG THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA SEQRES 16 A 278 VAL SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SEQRES 17 A 278 SER PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG SEQRES 18 A 278 ASP GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU SEQRES 19 A 278 THR ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SEQRES 20 A 278 ALA VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR SEQRES 21 A 278 CYS HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR SEQRES 22 A 278 LEU ARG TRP GLU PRO SEQRES 1 B 101 MET GLY ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER SEQRES 2 B 101 ARG HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN SEQRES 3 B 101 CYS TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL SEQRES 4 B 101 ASP LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU SEQRES 5 B 101 HIS SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR SEQRES 6 B 101 LEU LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP SEQRES 7 B 101 GLU TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN SEQRES 8 B 101 PRO LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 C 9 SER LEU LEU MET TRP ILE THR GLN VAL SEQRES 1 D 136 MET GLY ALA ALA GLU ARG LEU GLN LYS MET LEU GLU GLU SEQRES 2 D 136 ALA LYS GLU LEU LEU LYS LYS SER LYS GLU TYR LEU GLU SEQRES 3 D 136 LYS ALA LYS LYS LEU LEU LYS GLU GLY LYS VAL ASP GLU SEQRES 4 D 136 ALA LEU LYS GLU LEU GLU LYS ALA LEU LEU TYR LEU VAL SEQRES 5 D 136 GLU ALA VAL ASN LEU LEU ARG VAL VAL SER ALA GLU LEU SEQRES 6 D 136 GLY ASP ALA GLU LEU LYS ALA LEU VAL GLU GLU ALA GLU SEQRES 7 D 136 LYS TYR LEU ASN LYS ALA VAL THR TYR TYR TYR LYS ALA SEQRES 8 D 136 LYS LEU THR LYS ASP PRO GLU GLU LYS LYS LYS TYR VAL SEQRES 9 D 136 GLU LYS SER ILE GLU TYR ALA GLU LYS ALA LEU LYS ILE SEQRES 10 D 136 ALA GLU GLU ALA VAL LYS LEU ALA GLU LYS VAL VAL ALA SEQRES 11 D 136 ALA ALA ALA ALA LEU GLU SEQRES 1 E 119 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 119 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 119 SER ILE PHE SER ILE ASN THR MET GLY TRP TYR ARG GLN SEQRES 4 E 119 THR PRO GLY LYS GLN ARG ASP LEU VAL ALA ASP ILE SER SEQRES 5 E 119 SER GLY GLY SER THR LYS TYR GLY ASP SER VAL LYS GLY SEQRES 6 E 119 ARG PHE THR ILE SER ARG ASP ASN THR LYS ASN THR VAL SEQRES 7 E 119 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 E 119 VAL TYR TYR CYS TYR GLY LEU SER TYR SER ASN ASP ASP SEQRES 9 E 119 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY SEQRES 10 E 119 ALA PRO SEQRES 1 F 278 MET GLY GLY SER HIS SER MET ARG TYR PHE PHE THR SER SEQRES 2 F 278 VAL SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA SEQRES 3 F 278 VAL GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SEQRES 4 F 278 SER ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO SEQRES 5 F 278 TRP ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU SEQRES 6 F 278 THR ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL SEQRES 7 F 278 ASP LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU SEQRES 8 F 278 ALA GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP SEQRES 9 F 278 VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN SEQRES 10 F 278 TYR ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU SEQRES 11 F 278 ASP LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN SEQRES 12 F 278 THR THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU SEQRES 13 F 278 GLN LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP SEQRES 14 F 278 LEU ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN SEQRES 15 F 278 ARG THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA SEQRES 16 F 278 VAL SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SEQRES 17 F 278 SER PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG SEQRES 18 F 278 ASP GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU SEQRES 19 F 278 THR ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SEQRES 20 F 278 ALA VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR SEQRES 21 F 278 CYS HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR SEQRES 22 F 278 LEU ARG TRP GLU PRO SEQRES 1 G 101 MET GLY ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER SEQRES 2 G 101 ARG HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN SEQRES 3 G 101 CYS TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL SEQRES 4 G 101 ASP LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU SEQRES 5 G 101 HIS SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR SEQRES 6 G 101 LEU LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP SEQRES 7 G 101 GLU TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN SEQRES 8 G 101 PRO LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 H 9 SER LEU LEU MET TRP ILE THR GLN VAL SEQRES 1 I 136 MET GLY ALA ALA GLU ARG LEU GLN LYS MET LEU GLU GLU SEQRES 2 I 136 ALA LYS GLU LEU LEU LYS LYS SER LYS GLU TYR LEU GLU SEQRES 3 I 136 LYS ALA LYS LYS LEU LEU LYS GLU GLY LYS VAL ASP GLU SEQRES 4 I 136 ALA LEU LYS GLU LEU GLU LYS ALA LEU LEU TYR LEU VAL SEQRES 5 I 136 GLU ALA VAL ASN LEU LEU ARG VAL VAL SER ALA GLU LEU SEQRES 6 I 136 GLY ASP ALA GLU LEU LYS ALA LEU VAL GLU GLU ALA GLU SEQRES 7 I 136 LYS TYR LEU ASN LYS ALA VAL THR TYR TYR TYR LYS ALA SEQRES 8 I 136 LYS LEU THR LYS ASP PRO GLU GLU LYS LYS LYS TYR VAL SEQRES 9 I 136 GLU LYS SER ILE GLU TYR ALA GLU LYS ALA LEU LYS ILE SEQRES 10 I 136 ALA GLU GLU ALA VAL LYS LEU ALA GLU LYS VAL VAL ALA SEQRES 11 I 136 ALA ALA ALA ALA LEU GLU SEQRES 1 J 119 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 119 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 J 119 SER ILE PHE SER ILE ASN THR MET GLY TRP TYR ARG GLN SEQRES 4 J 119 THR PRO GLY LYS GLN ARG ASP LEU VAL ALA ASP ILE SER SEQRES 5 J 119 SER GLY GLY SER THR LYS TYR GLY ASP SER VAL LYS GLY SEQRES 6 J 119 ARG PHE THR ILE SER ARG ASP ASN THR LYS ASN THR VAL SEQRES 7 J 119 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 J 119 VAL TYR TYR CYS TYR GLY LEU SER TYR SER ASN ASP ASP SEQRES 9 J 119 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY SEQRES 10 J 119 ALA PRO HET GOL A 301 6 HET GOL A 302 6 HET GOL A 303 6 HET GOL A 304 6 HET GOL A 305 6 HET GOL B 101 6 HET GOL B 102 6 HET GOL B 103 6 HET GOL B 104 6 HET GOL E 201 6 HET GOL F 301 6 HET GOL F 302 6 HET GOL F 303 6 HET GOL G 201 6 HET GOL G 202 6 HET GOL J 201 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 11 GOL 16(C3 H8 O3) FORMUL 27 HOH *270(H2 O) HELIX 1 AA1 PRO A 50 GLU A 55 5 6 HELIX 2 AA2 GLY A 56 TYR A 85 1 30 HELIX 3 AA3 ASP A 137 ALA A 150 1 14 HELIX 4 AA4 HIS A 151 GLY A 162 1 12 HELIX 5 AA5 GLY A 162 GLY A 175 1 14 HELIX 6 AA6 GLY A 175 GLN A 180 1 6 HELIX 7 AA7 GLN A 253 GLN A 255 5 3 HELIX 8 AA8 ALA D 2 GLU D 32 1 31 HELIX 9 AA9 LYS D 34 LEU D 63 1 30 HELIX 10 AB1 ASP D 65 THR D 92 1 28 HELIX 11 AB2 ASP D 94 ALA D 128 1 35 HELIX 12 AB3 ASN E 75 LYS E 77 5 3 HELIX 13 AB4 LYS E 88 THR E 92 5 5 HELIX 14 AB5 TRP F 51 GLU F 55 5 5 HELIX 15 AB6 GLY F 56 TYR F 85 1 30 HELIX 16 AB7 ASP F 137 ALA F 150 1 14 HELIX 17 AB8 HIS F 151 GLY F 162 1 12 HELIX 18 AB9 GLY F 162 GLY F 175 1 14 HELIX 19 AC1 GLY F 175 GLN F 180 1 6 HELIX 20 AC2 GLN F 253 GLN F 255 5 3 HELIX 21 AC3 ALA I 2 GLY I 33 1 32 HELIX 22 AC4 LYS I 34 LEU I 63 1 30 HELIX 23 AC5 ASP I 65 THR I 92 1 28 HELIX 24 AC6 ASP I 94 VAL I 127 1 34 HELIX 25 AC7 ASP J 63 LYS J 66 5 4 HELIX 26 AC8 ASN J 75 LYS J 77 5 3 HELIX 27 AC9 LYS J 88 THR J 92 5 5 SHEET 1 AA1 8 GLU A 46 PRO A 47 0 SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31 SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N PHE A 8 O VAL A 25 SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O ARG A 97 N PHE A 9 SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O GLN A 115 N MET A 98 SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114 SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125 SHEET 1 AA2 4 LYS A 186 HIS A 192 0 SHEET 2 AA2 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192 SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 AA2 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 AA3 4 LYS A 186 HIS A 192 0 SHEET 2 AA3 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192 SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 AA4 4 GLU A 222 ASP A 223 0 SHEET 2 AA4 4 ILE A 213 ARG A 219 -1 N ARG A 219 O GLU A 222 SHEET 3 AA4 4 TYR A 257 HIS A 263 -1 O HIS A 260 N THR A 216 SHEET 4 AA4 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259 SHEET 1 AA5 4 LYS B 6 SER B 11 0 SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23 SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AA6 4 LYS B 6 SER B 11 0 SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23 SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AA7 4 GLU B 44 ARG B 45 0 SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40 SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80 SHEET 1 AA8 4 LYS E 5 SER E 9 0 SHEET 2 AA8 4 LEU E 20 SER E 27 -1 O SER E 27 N LYS E 5 SHEET 3 AA8 4 THR E 79 MET E 84 -1 O MET E 84 N LEU E 20 SHEET 4 AA8 4 PHE E 69 ASP E 74 -1 N THR E 70 O GLN E 83 SHEET 1 AA9 6 GLY E 12 VAL E 14 0 SHEET 2 AA9 6 THR E 112 VAL E 116 1 O THR E 115 N GLY E 12 SHEET 3 AA9 6 ALA E 93 SER E 101 -1 N TYR E 95 O THR E 112 SHEET 4 AA9 6 ILE E 33 GLN E 41 -1 N ASN E 34 O LEU E 100 SHEET 5 AA9 6 ASP E 48 ILE E 53 -1 O ALA E 51 N TRP E 38 SHEET 6 AA9 6 THR E 59 TYR E 61 -1 O LYS E 60 N ASP E 52 SHEET 1 AB1 4 GLY E 12 VAL E 14 0 SHEET 2 AB1 4 THR E 112 VAL E 116 1 O THR E 115 N GLY E 12 SHEET 3 AB1 4 ALA E 93 SER E 101 -1 N TYR E 95 O THR E 112 SHEET 4 AB1 4 ASP E 106 TRP E 108 -1 O TYR E 107 N GLY E 99 SHEET 1 AB2 8 GLU F 46 PRO F 47 0 SHEET 2 AB2 8 THR F 31 ASP F 37 -1 N ARG F 35 O GLU F 46 SHEET 3 AB2 8 ARG F 21 VAL F 28 -1 N VAL F 28 O THR F 31 SHEET 4 AB2 8 HIS F 3 VAL F 12 -1 N ARG F 6 O TYR F 27 SHEET 5 AB2 8 THR F 94 VAL F 103 -1 O ARG F 97 N PHE F 9 SHEET 6 AB2 8 PHE F 109 TYR F 118 -1 O GLN F 115 N MET F 98 SHEET 7 AB2 8 LYS F 121 LEU F 126 -1 O TYR F 123 N TYR F 116 SHEET 8 AB2 8 TRP F 133 ALA F 135 -1 O THR F 134 N ALA F 125 SHEET 1 AB3 4 LYS F 186 HIS F 192 0 SHEET 2 AB3 4 GLU F 198 PHE F 208 -1 O TRP F 204 N HIS F 188 SHEET 3 AB3 4 PHE F 241 PRO F 250 -1 O ALA F 245 N CYS F 203 SHEET 4 AB3 4 THR F 228 LEU F 230 -1 N GLU F 229 O ALA F 246 SHEET 1 AB4 4 LYS F 186 HIS F 192 0 SHEET 2 AB4 4 GLU F 198 PHE F 208 -1 O TRP F 204 N HIS F 188 SHEET 3 AB4 4 PHE F 241 PRO F 250 -1 O ALA F 245 N CYS F 203 SHEET 4 AB4 4 ARG F 234 PRO F 235 -1 N ARG F 234 O GLN F 242 SHEET 1 AB5 4 GLU F 222 GLN F 224 0 SHEET 2 AB5 4 THR F 214 ARG F 219 -1 N ARG F 219 O GLU F 222 SHEET 3 AB5 4 TYR F 257 GLN F 262 -1 O THR F 258 N GLN F 218 SHEET 4 AB5 4 LEU F 270 ARG F 273 -1 O LEU F 272 N CYS F 259 SHEET 1 AB6 4 LYS G 6 SER G 11 0 SHEET 2 AB6 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10 SHEET 3 AB6 4 PHE G 62 PHE G 70 -1 O THR G 68 N LEU G 23 SHEET 4 AB6 4 GLU G 50 HIS G 51 -1 N GLU G 50 O TYR G 67 SHEET 1 AB7 4 LYS G 6 SER G 11 0 SHEET 2 AB7 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10 SHEET 3 AB7 4 PHE G 62 PHE G 70 -1 O THR G 68 N LEU G 23 SHEET 4 AB7 4 SER G 55 PHE G 56 -1 N SER G 55 O TYR G 63 SHEET 1 AB8 4 GLU G 44 ARG G 45 0 SHEET 2 AB8 4 GLU G 36 LYS G 41 -1 N LYS G 41 O GLU G 44 SHEET 3 AB8 4 TYR G 78 ASN G 83 -1 O ALA G 79 N LEU G 40 SHEET 4 AB8 4 LYS G 91 LYS G 94 -1 O LYS G 91 N VAL G 82 SHEET 1 AB9 4 LYS J 5 SER J 9 0 SHEET 2 AB9 4 LEU J 20 SER J 27 -1 O SER J 27 N LYS J 5 SHEET 3 AB9 4 THR J 79 MET J 84 -1 O MET J 84 N LEU J 20 SHEET 4 AB9 4 PHE J 69 ASP J 74 -1 N THR J 70 O GLN J 83 SHEET 1 AC1 6 GLY J 12 VAL J 14 0 SHEET 2 AC1 6 THR J 112 VAL J 116 1 O THR J 115 N GLY J 12 SHEET 3 AC1 6 ALA J 93 SER J 101 -1 N TYR J 95 O THR J 112 SHEET 4 AC1 6 ILE J 33 GLN J 41 -1 N ASN J 34 O LEU J 100 SHEET 5 AC1 6 ASP J 48 ILE J 53 -1 O ALA J 51 N TRP J 38 SHEET 6 AC1 6 THR J 59 TYR J 61 -1 O LYS J 60 N ASP J 52 SHEET 1 AC2 4 GLY J 12 VAL J 14 0 SHEET 2 AC2 4 THR J 112 VAL J 116 1 O THR J 115 N GLY J 12 SHEET 3 AC2 4 ALA J 93 SER J 101 -1 N TYR J 95 O THR J 112 SHEET 4 AC2 4 ASP J 106 TRP J 108 -1 O TYR J 107 N GLY J 99 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04 SSBOND 4 CYS E 24 CYS E 97 1555 1555 2.03 SSBOND 5 CYS F 101 CYS F 164 1555 1555 2.04 SSBOND 6 CYS F 203 CYS F 259 1555 1555 2.03 SSBOND 7 CYS G 25 CYS G 80 1555 1555 2.04 SSBOND 8 CYS J 24 CYS J 97 1555 1555 2.03 CISPEP 1 TYR A 209 PRO A 210 0 2.22 CISPEP 2 HIS B 31 PRO B 32 0 1.10 CISPEP 3 TYR F 209 PRO F 210 0 -0.36 CISPEP 4 HIS G 31 PRO G 32 0 0.08 CRYST1 95.452 98.536 155.743 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010476 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010149 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006421 0.00000 MTRIX1 1 -0.999970 0.001712 0.007499 -48.78024 1 MTRIX2 1 -0.001701 -0.999998 0.001397 -0.03736 1 MTRIX3 1 0.007501 0.001384 0.999971 0.24960 1 MTRIX1 2 -0.999979 0.005149 0.004004 -48.27006 1 MTRIX2 2 -0.005176 -0.999962 -0.006952 -0.04271 1 MTRIX3 2 0.003968 -0.006972 0.999968 -0.11311 1 MTRIX1 3 -0.999987 -0.004521 0.002379 -48.88841 1 MTRIX2 3 0.004514 -0.999986 -0.002824 0.20138 1 MTRIX3 3 0.002392 -0.002813 0.999993 0.00042 1 MTRIX1 4 -0.999603 0.028032 -0.002951 -47.72070 1 MTRIX2 4 -0.028046 -0.999595 0.004753 -0.81190 1 MTRIX3 4 -0.002817 0.004833 0.999984 -0.00415 1 MTRIX1 5 -0.999959 0.007969 -0.004337 -48.73154 1 MTRIX2 5 -0.007983 -0.999963 0.003235 0.07025 1 MTRIX3 5 -0.004311 0.003269 0.999985 -0.02459 1