HEADER PROTEIN BINDING 25-MAR-24 9ERW TITLE MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 8C COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHAINS: E; COMPND 3 CHAIN: E; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: ANTI-CNPASE NANOBODY 8C; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: CNP,CNPASE; COMPND 10 EC: 3.1.4.37; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: MOUSE CNPASE CATALYTIC DOMAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 GENE: CNP, CNP1; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CNPASE, MYELIN, NANOBODY, SINGLE-DOMAIN ANTIBODY, COMPLEX, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA REVDAT 1 11-DEC-24 9ERW 0 JRNL AUTH S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA JRNL TITL MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 8C JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.73 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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) : 1.73 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.84 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 35389 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.650 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 44.8400 - 4.1700 0.98 2453 146 0.1548 0.1604 REMARK 3 2 4.1700 - 3.3100 0.99 2412 146 0.1686 0.1819 REMARK 3 3 3.3100 - 2.8900 0.98 2374 142 0.2024 0.2444 REMARK 3 4 2.8900 - 2.6300 0.99 2385 142 0.2189 0.2557 REMARK 3 5 2.6300 - 2.4400 1.00 2410 144 0.1971 0.2227 REMARK 3 6 2.4400 - 2.2900 1.00 2375 143 0.2000 0.2434 REMARK 3 7 2.2900 - 2.1800 1.00 2385 144 0.1893 0.2363 REMARK 3 8 2.1800 - 2.0800 0.96 2321 138 0.2237 0.2747 REMARK 3 9 2.0800 - 2.0000 0.99 2375 142 0.2165 0.2578 REMARK 3 10 2.0000 - 1.9400 1.00 2407 145 0.2187 0.2630 REMARK 3 11 1.9400 - 1.8700 1.00 2357 140 0.2429 0.3004 REMARK 3 12 1.8700 - 1.8200 1.00 2390 144 0.2889 0.3156 REMARK 3 13 1.8200 - 1.7700 1.00 2407 144 0.3331 0.3870 REMARK 3 14 1.7700 - 1.7300 0.99 2338 140 0.3965 0.4395 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) : 0.287 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.616 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.94 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 : 0.011 2660 REMARK 3 ANGLE : 1.050 3592 REMARK 3 CHIRALITY : 0.058 380 REMARK 3 PLANARITY : 0.009 460 REMARK 3 DIHEDRAL : 16.867 969 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 5 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.6481 24.2493 45.5796 REMARK 3 T TENSOR REMARK 3 T11: 0.5158 T22: 0.4406 REMARK 3 T33: 0.8113 T12: -0.0284 REMARK 3 T13: 0.1205 T23: 0.1681 REMARK 3 L TENSOR REMARK 3 L11: 8.6014 L22: 6.5459 REMARK 3 L33: 4.4251 L12: -1.7673 REMARK 3 L13: -2.2398 L23: 1.3861 REMARK 3 S TENSOR REMARK 3 S11: -0.1411 S12: -0.8023 S13: -1.3731 REMARK 3 S21: 0.2766 S22: 0.2183 S23: 1.1044 REMARK 3 S31: 1.8574 S32: -1.1598 S33: -0.0050 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 6 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8222 28.1554 25.4061 REMARK 3 T TENSOR REMARK 3 T11: 0.4383 T22: 0.2759 REMARK 3 T33: 0.3738 T12: -0.0929 REMARK 3 T13: -0.0883 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 5.2711 L22: 5.5768 REMARK 3 L33: 2.0080 L12: 0.3280 REMARK 3 L13: -2.0164 L23: -2.1237 REMARK 3 S TENSOR REMARK 3 S11: -0.2752 S12: 0.6448 S13: -0.1312 REMARK 3 S21: -0.6979 S22: -0.2281 S23: -0.0052 REMARK 3 S31: -0.5872 S32: -0.2122 S33: 0.6132 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 16 THROUGH 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.3845 32.5146 29.9785 REMARK 3 T TENSOR REMARK 3 T11: 0.4396 T22: 0.2886 REMARK 3 T33: 0.3770 T12: -0.0250 REMARK 3 T13: -0.0240 T23: -0.0433 REMARK 3 L TENSOR REMARK 3 L11: 6.6215 L22: 4.9306 REMARK 3 L33: 3.7063 L12: 1.8471 REMARK 3 L13: -4.5433 L23: -2.8478 REMARK 3 S TENSOR REMARK 3 S11: 0.1405 S12: 0.0076 S13: 0.2574 REMARK 3 S21: -0.3721 S22: -0.0683 S23: 0.3037 REMARK 3 S31: -0.0119 S32: -0.2158 S33: 0.0513 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.8729 50.9156 58.1059 REMARK 3 T TENSOR REMARK 3 T11: 0.3186 T22: 0.2336 REMARK 3 T33: 0.2572 T12: -0.0046 REMARK 3 T13: -0.0852 T23: 0.0090 REMARK 3 L TENSOR REMARK 3 L11: 3.8329 L22: 9.3340 REMARK 3 L33: 4.9217 L12: 0.2686 REMARK 3 L13: 1.1632 L23: 0.0807 REMARK 3 S TENSOR REMARK 3 S11: -0.4088 S12: -0.0862 S13: 0.5445 REMARK 3 S21: -0.2818 S22: 0.0720 S23: -0.6241 REMARK 3 S31: -0.6357 S32: 0.4953 S33: 0.2830 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.6118 36.4743 71.8286 REMARK 3 T TENSOR REMARK 3 T11: 0.3771 T22: 0.9665 REMARK 3 T33: 0.3618 T12: 0.0763 REMARK 3 T13: 0.0611 T23: 0.0605 REMARK 3 L TENSOR REMARK 3 L11: 0.4818 L22: 0.6727 REMARK 3 L33: 3.1387 L12: 0.5037 REMARK 3 L13: -1.1173 L23: -1.0677 REMARK 3 S TENSOR REMARK 3 S11: -0.1854 S12: -1.2252 S13: -0.1746 REMARK 3 S21: 0.2666 S22: 0.3404 S23: 0.2390 REMARK 3 S31: -0.7396 S32: -1.8050 S33: -0.1270 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 194 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8104 35.7410 89.0983 REMARK 3 T TENSOR REMARK 3 T11: 0.8045 T22: 2.2017 REMARK 3 T33: -0.0229 T12: 0.4185 REMARK 3 T13: 0.1641 T23: 0.2993 REMARK 3 L TENSOR REMARK 3 L11: 0.0206 L22: 0.8533 REMARK 3 L33: 1.4211 L12: 0.0938 REMARK 3 L13: -0.0329 L23: -0.8592 REMARK 3 S TENSOR REMARK 3 S11: -0.3530 S12: -0.9674 S13: -0.3149 REMARK 3 S21: 0.4564 S22: -0.0725 S23: 0.0205 REMARK 3 S31: 0.6498 S32: 0.4313 S33: -0.1234 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 221 THROUGH 236 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.4905 47.1012 68.2364 REMARK 3 T TENSOR REMARK 3 T11: 0.4923 T22: 0.5961 REMARK 3 T33: 0.3074 T12: 0.1411 REMARK 3 T13: -0.0283 T23: -0.0285 REMARK 3 L TENSOR REMARK 3 L11: 0.0718 L22: 1.8851 REMARK 3 L33: 6.9001 L12: 0.1151 REMARK 3 L13: -0.4300 L23: -3.3354 REMARK 3 S TENSOR REMARK 3 S11: 0.0917 S12: -1.1876 S13: 0.0852 REMARK 3 S21: 0.7598 S22: 0.0970 S23: 0.0398 REMARK 3 S31: -1.0806 S32: -0.6980 S33: -0.2902 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 237 THROUGH 279 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.7054 43.4686 61.7969 REMARK 3 T TENSOR REMARK 3 T11: 0.1831 T22: 0.3871 REMARK 3 T33: 0.3369 T12: 0.0627 REMARK 3 T13: -0.0538 T23: 0.0344 REMARK 3 L TENSOR REMARK 3 L11: 2.2319 L22: 3.4744 REMARK 3 L33: 4.4534 L12: 0.3788 REMARK 3 L13: 0.1502 L23: -0.5848 REMARK 3 S TENSOR REMARK 3 S11: -0.1995 S12: -0.5285 S13: 0.0481 REMARK 3 S21: 0.0745 S22: -0.1213 S23: -0.4588 REMARK 3 S31: -0.3023 S32: 0.4077 S33: 0.2982 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 291 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.0286 36.2493 59.3151 REMARK 3 T TENSOR REMARK 3 T11: 0.3337 T22: 0.3856 REMARK 3 T33: 0.4288 T12: 0.0747 REMARK 3 T13: 0.0191 T23: 0.0553 REMARK 3 L TENSOR REMARK 3 L11: 2.4353 L22: 3.4292 REMARK 3 L33: 4.1868 L12: 1.3054 REMARK 3 L13: -2.2875 L23: -3.5865 REMARK 3 S TENSOR REMARK 3 S11: -0.2339 S12: 0.0554 S13: -0.8906 REMARK 3 S21: -0.1074 S22: -0.1485 S23: -0.8580 REMARK 3 S31: 0.8788 S32: 0.7702 S33: 0.2700 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 295 THROUGH 303 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.6150 37.9380 73.1405 REMARK 3 T TENSOR REMARK 3 T11: 0.6755 T22: 1.3250 REMARK 3 T33: 0.6455 T12: 0.2391 REMARK 3 T13: 0.1616 T23: 0.1321 REMARK 3 L TENSOR REMARK 3 L11: 1.6677 L22: 6.7110 REMARK 3 L33: 1.1005 L12: 3.0756 REMARK 3 L13: -0.3243 L23: -1.3226 REMARK 3 S TENSOR REMARK 3 S11: 0.3200 S12: -0.5610 S13: 0.6036 REMARK 3 S21: 0.5505 S22: -0.0194 S23: 0.0338 REMARK 3 S31: -0.7212 S32: 0.8128 S33: -0.2551 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 304 THROUGH 336 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.5306 40.2964 75.4967 REMARK 3 T TENSOR REMARK 3 T11: 0.4301 T22: 0.8409 REMARK 3 T33: 0.3325 T12: 0.1139 REMARK 3 T13: -0.0643 T23: 0.0361 REMARK 3 L TENSOR REMARK 3 L11: 2.9095 L22: 2.2103 REMARK 3 L33: 3.9205 L12: 1.7701 REMARK 3 L13: 1.5923 L23: -0.9188 REMARK 3 S TENSOR REMARK 3 S11: -0.1954 S12: -1.2824 S13: 0.2798 REMARK 3 S21: 0.2311 S22: -0.0840 S23: -0.4222 REMARK 3 S31: -0.4240 S32: 0.4508 S33: 0.3689 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 337 THROUGH 348 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.0541 23.1728 81.0328 REMARK 3 T TENSOR REMARK 3 T11: 0.6602 T22: 1.4893 REMARK 3 T33: 0.7498 T12: 0.0309 REMARK 3 T13: 0.0796 T23: 0.3746 REMARK 3 L TENSOR REMARK 3 L11: 4.5084 L22: 3.1170 REMARK 3 L33: 2.0149 L12: -1.7770 REMARK 3 L13: 6.1464 L23: -0.4860 REMARK 3 S TENSOR REMARK 3 S11: -0.2261 S12: 0.4340 S13: 0.3763 REMARK 3 S21: 0.1859 S22: -0.1790 S23: 0.1392 REMARK 3 S31: 0.6047 S32: -0.3936 S33: 0.4549 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 349 THROUGH 378 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.2822 34.3061 70.9054 REMARK 3 T TENSOR REMARK 3 T11: 0.3736 T22: 0.7208 REMARK 3 T33: 0.3787 T12: 0.0662 REMARK 3 T13: 0.0254 T23: 0.1878 REMARK 3 L TENSOR REMARK 3 L11: 1.3202 L22: 1.3953 REMARK 3 L33: 5.8398 L12: -0.1451 REMARK 3 L13: 0.6163 L23: -2.7974 REMARK 3 S TENSOR REMARK 3 S11: -0.1049 S12: -1.0542 S13: -0.2844 REMARK 3 S21: 0.2076 S22: 0.0855 S23: -0.1114 REMARK 3 S31: 0.2088 S32: -0.2146 S33: 0.0677 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 23 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.0317 32.2674 45.0132 REMARK 3 T TENSOR REMARK 3 T11: 0.3028 T22: 0.2548 REMARK 3 T33: 0.3089 T12: 0.0165 REMARK 3 T13: 0.0174 T23: -0.0478 REMARK 3 L TENSOR REMARK 3 L11: 5.4404 L22: 4.5233 REMARK 3 L33: 5.3608 L12: 0.4640 REMARK 3 L13: -0.4526 L23: 0.8602 REMARK 3 S TENSOR REMARK 3 S11: -0.0199 S12: -0.3015 S13: -0.0807 REMARK 3 S21: 0.4293 S22: -0.2102 S23: 0.6774 REMARK 3 S31: 0.0101 S32: -0.7298 S33: 0.2637 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 40 THROUGH 57 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2573 35.1242 41.8813 REMARK 3 T TENSOR REMARK 3 T11: 0.3406 T22: 0.2226 REMARK 3 T33: 0.3583 T12: -0.0089 REMARK 3 T13: -0.0288 T23: 0.0093 REMARK 3 L TENSOR REMARK 3 L11: 4.4106 L22: 9.0979 REMARK 3 L33: 4.7717 L12: -3.2980 REMARK 3 L13: -2.9096 L23: 3.6284 REMARK 3 S TENSOR REMARK 3 S11: -0.1269 S12: -0.2702 S13: -0.0452 REMARK 3 S21: -0.1162 S22: 0.2658 S23: 0.2019 REMARK 3 S31: -0.0745 S32: 0.1915 S33: -0.1234 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 58 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8178 40.5178 35.7185 REMARK 3 T TENSOR REMARK 3 T11: 0.3974 T22: 0.1554 REMARK 3 T33: 0.3751 T12: -0.0289 REMARK 3 T13: 0.0030 T23: 0.0253 REMARK 3 L TENSOR REMARK 3 L11: 4.3691 L22: 4.9208 REMARK 3 L33: 5.7676 L12: -1.1874 REMARK 3 L13: 0.4169 L23: 0.4314 REMARK 3 S TENSOR REMARK 3 S11: -0.0059 S12: 0.0678 S13: 0.6545 REMARK 3 S21: -0.7355 S22: 0.0902 S23: -0.2451 REMARK 3 S31: -0.7310 S32: 0.1121 S33: -0.0407 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 74 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2872 35.9770 37.1941 REMARK 3 T TENSOR REMARK 3 T11: 0.3287 T22: 0.4378 REMARK 3 T33: 0.4154 T12: -0.0119 REMARK 3 T13: -0.0812 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 4.2781 L22: 7.1179 REMARK 3 L33: 6.6035 L12: -0.4398 REMARK 3 L13: -5.3195 L23: 0.4593 REMARK 3 S TENSOR REMARK 3 S11: 0.1475 S12: 0.2108 S13: 0.1979 REMARK 3 S21: -0.0045 S22: -0.1999 S23: 0.7108 REMARK 3 S31: -0.7380 S32: -0.7734 S33: 0.0633 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 84 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4590 34.5673 25.8169 REMARK 3 T TENSOR REMARK 3 T11: 0.4759 T22: 0.3420 REMARK 3 T33: 0.4041 T12: -0.0778 REMARK 3 T13: 0.0477 T23: 0.0543 REMARK 3 L TENSOR REMARK 3 L11: 3.0956 L22: 4.8104 REMARK 3 L33: 5.0018 L12: 0.0582 REMARK 3 L13: 1.7215 L23: -4.3075 REMARK 3 S TENSOR REMARK 3 S11: -0.1104 S12: 0.5462 S13: 0.9906 REMARK 3 S21: 0.2196 S22: -0.4624 S23: -1.4831 REMARK 3 S31: -0.8083 S32: 0.5758 S33: 0.5280 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 92 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.7517 30.2207 43.6818 REMARK 3 T TENSOR REMARK 3 T11: 0.3241 T22: 0.1786 REMARK 3 T33: 0.3273 T12: 0.0215 REMARK 3 T13: -0.0015 T23: 0.0162 REMARK 3 L TENSOR REMARK 3 L11: 1.2880 L22: 1.8230 REMARK 3 L33: 7.3457 L12: -0.2491 REMARK 3 L13: -0.8980 L23: 2.9476 REMARK 3 S TENSOR REMARK 3 S11: -0.0463 S12: -0.0207 S13: -0.1737 REMARK 3 S21: 0.0738 S22: 0.0372 S23: -0.0101 REMARK 3 S31: 0.3676 S32: 0.0749 S33: 0.0009 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 9ERW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292137547. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, DESY REMARK 200 BEAMLINE : P11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35411 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 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 : 1.000 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 (%): 45.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB PH 8.0, 25% PEG1500, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 27.08500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, B 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 E 128 REMARK 465 GLY B 159 REMARK 465 LEU B 160 REMARK 465 ILE B 206 REMARK 465 SER B 207 REMARK 465 GLY B 208 REMARK 465 ASP B 209 REMARK 465 GLU B 210 REMARK 465 PRO B 211 REMARK 465 LYS B 212 REMARK 465 GLU B 213 REMARK 465 ASP B 292 REMARK 465 LEU B 293 REMARK 465 ASP B 294 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 E 224 O HOH E 265 1.83 REMARK 500 O HOH E 287 O HOH E 290 2.11 REMARK 500 O HOH E 254 O HOH E 276 2.13 REMARK 500 O HOH B 437 O HOH B 464 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PHE B 221 31.14 -96.72 REMARK 500 PRO B 225 103.29 -56.64 REMARK 500 THR B 233 -62.53 -101.59 REMARK 500 PRO B 296 -92.36 -100.02 REMARK 500 SER B 297 29.66 -157.80 REMARK 500 ALA B 316 -82.46 -13.61 REMARK 500 THR B 374 -162.81 -161.69 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ERW E 1 128 PDB 9ERW 9ERW 1 128 DBREF 9ERW B 159 378 UNP P16330 CN37_MOUSE 179 398 SEQRES 1 E 128 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 128 ALA GLY GLY SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 E 128 PHE THR PHE ASP ASP TYR ALA MET GLY TRP TYR ARG GLN SEQRES 4 E 128 ALA PRO GLY LYS GLU ARG VAL GLY VAL SER CYS ILE SER SEQRES 5 E 128 ARG THR ASP GLY TYR THR TYR TYR LEU ASP SER VAL LYS SEQRES 6 E 128 GLY ARG PHE THR ILE SER THR ASP HIS ALA LYS HIS THR SEQRES 7 E 128 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO ASP ASP THR SEQRES 8 E 128 GLY LEU TYR TYR CYS ALA ALA ASP ALA ASP PRO GLU TYR SEQRES 9 E 128 GLY SER ARG CYS PRO ASP PRO TYR TYR GLY MET ASP TYR SEQRES 10 E 128 TRP GLY LYS GLY ILE LEU VAL THR VAL SER SER SEQRES 1 B 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 B 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 B 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 B 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 B 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 B 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 B 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 B 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 B 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 B 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 B 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 B 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 B 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 B 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 B 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 B 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 B 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY FORMUL 3 HOH *156(H2 O) HELIX 1 AA1 ASP E 62 LYS E 65 5 4 HELIX 2 AA2 LYS E 87 THR E 91 5 5 HELIX 3 AA3 ASP E 101 SER E 106 1 6 HELIX 4 AA4 GLU B 161 LEU B 165 5 5 HELIX 5 AA5 THR B 174 ASN B 194 1 21 HELIX 6 AA6 HIS B 195 GLU B 201 1 7 HELIX 7 AA7 GLU B 216 PHE B 221 1 6 HELIX 8 AA8 ASP B 237 LYS B 240 5 4 HELIX 9 AA9 GLY B 243 GLN B 250 1 8 HELIX 10 AB1 GLN B 250 TYR B 257 1 8 HELIX 11 AB2 THR B 282 GLN B 287 1 6 HELIX 12 AB3 PRO B 320 LYS B 335 1 16 SHEET 1 AA1 4 GLN E 3 SER E 7 0 SHEET 2 AA1 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AA1 4 THR E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AA1 4 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AA2 6 GLY E 10 GLN E 13 0 SHEET 2 AA2 6 ILE E 122 SER E 127 1 O THR E 125 N GLY E 10 SHEET 3 AA2 6 GLY E 92 ASP E 99 -1 N TYR E 94 O ILE E 122 SHEET 4 AA2 6 ALA E 33 GLN E 39 -1 N TYR E 37 O TYR E 95 SHEET 5 AA2 6 VAL E 46 SER E 52 -1 O VAL E 48 N TRP E 36 SHEET 6 AA2 6 THR E 58 TYR E 60 -1 O TYR E 59 N CYS E 50 SHEET 1 AA3 4 GLY E 10 GLN E 13 0 SHEET 2 AA3 4 ILE E 122 SER E 127 1 O THR E 125 N GLY E 10 SHEET 3 AA3 4 GLY E 92 ASP E 99 -1 N TYR E 94 O ILE E 122 SHEET 4 AA3 4 TYR E 117 TRP E 118 -1 O TYR E 117 N ALA E 98 SHEET 1 AA4 6 HIS B 230 PHE B 235 0 SHEET 2 AA4 6 TYR B 168 LEU B 173 -1 N TRP B 171 O CYS B 231 SHEET 3 AA4 6 ARG B 358 TYR B 376 -1 O ILE B 372 N PHE B 172 SHEET 4 AA4 6 ALA B 260 VAL B 270 -1 N ILE B 265 O MET B 367 SHEET 5 AA4 6 THR B 274 VAL B 279 -1 O GLN B 278 N ALA B 267 SHEET 6 AA4 6 HIS B 309 CYS B 314 -1 O LEU B 312 N ALA B 275 SHEET 1 AA5 5 HIS B 230 PHE B 235 0 SHEET 2 AA5 5 TYR B 168 LEU B 173 -1 N TRP B 171 O CYS B 231 SHEET 3 AA5 5 ARG B 358 TYR B 376 -1 O ILE B 372 N PHE B 172 SHEET 4 AA5 5 GLY B 349 GLY B 355 -1 N TYR B 352 O MET B 360 SHEET 5 AA5 5 GLY B 344 LEU B 346 -1 N GLY B 344 O LEU B 351 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.07 SSBOND 2 CYS E 50 CYS E 108 1555 1555 2.12 CRYST1 39.860 54.170 80.400 90.00 96.36 90.00 P 1 21 1 2 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 0.025088 0.000000 0.002794 0.00000 SCALE2 0.000000 0.018460 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012515 0.00000