HEADER IMMUNE SYSTEM 22-JUL-24 9IUT TITLE CRYSTAL STRUCTURE OF CANCER-SPECIFIC ANTI-HER2 ANTIBODY H2MAB-250 IN TITLE 2 COMPLEX WITH EPITOPE PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: H2MAB-250 VH(S112C)-SARAH; COMPND 3 CHAIN: A, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: H2MAB-250 VL-SARAH(S37C); COMPND 7 CHAIN: B, E; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: H2MAB-250 EPITOPE PEPTIDE; COMPND 11 CHAIN: C, F; COMPND 12 SYNONYM: METASTATIC LYMPH NODE GENE 19 PROTEIN,MLN 19,PROTO-ONCOGENE COMPND 13 NEU,PROTO-ONCOGENE C-ERBB-2,TYROSINE KINASE-TYPE CELL SURFACE COMPND 14 RECEPTOR HER2,P185ERBB2; COMPND 15 EC: 2.7.10.1; COMPND 16 ENGINEERED: YES; COMPND 17 OTHER_DETAILS: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS FV-CLASP, ANTIBODY, CANCER-SPECIFIC, HER2, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.ARIMORI,J.TAKAGI REVDAT 1 04-JUN-25 9IUT 0 JRNL AUTH M.P.HOSKING,S.SHIRINBAK,K.OMILUSIK,S.CHANDRA,M.K.KANEKO, JRNL AUTH 2 A.GENTILE,S.YAMAMOTO,B.SHRESTHA,J.GRANT,M.BOYETT,D.CARDENAS, JRNL AUTH 3 H.KEEGAN,S.IBITOKOU,C.PAVON,T.MIZOGUCHI,T.IHARA,D.NAKAYAMA, JRNL AUTH 4 R.ABUJAROUR,T.T.LEE,R.CLARKE,J.GOODRIDGE,E.PERALTA,T.MAEDA, JRNL AUTH 5 J.TAKAGI,T.ARIMORI,Y.KATO,B.VALAMEHR JRNL TITL PREFERENTIAL TUMOR TARGETING OF HER2 BY IPSC-DERIVED CAR-T JRNL TITL 2 CELLS ENGINEERED TO OVERCOME MULTIPLE BARRIERS TO SOLID JRNL TITL 3 TUMOR EFFICACY. JRNL REF CELL STEM CELL 2025 JRNL DOI 10.1016/J.STEM.2025.05.007 REMARK 2 REMARK 2 RESOLUTION. 2.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 2.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.07 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 41188 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2059 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 37.0700 - 5.1500 1.00 2756 145 0.1695 0.1867 REMARK 3 2 5.1500 - 4.0900 1.00 2658 140 0.1401 0.1615 REMARK 3 3 4.0900 - 3.5700 1.00 2636 138 0.1666 0.2085 REMARK 3 4 3.5700 - 3.2500 1.00 2604 137 0.1913 0.2559 REMARK 3 5 3.2500 - 3.0100 1.00 2623 138 0.2254 0.2429 REMARK 3 6 3.0100 - 2.8400 1.00 2590 137 0.2308 0.2689 REMARK 3 7 2.8400 - 2.6900 1.00 2616 138 0.2481 0.2940 REMARK 3 8 2.6900 - 2.5800 1.00 2583 135 0.2430 0.2792 REMARK 3 9 2.5800 - 2.4800 1.00 2597 137 0.2385 0.3000 REMARK 3 10 2.4800 - 2.3900 1.00 2610 137 0.2406 0.2798 REMARK 3 11 2.3900 - 2.3200 1.00 2584 136 0.2407 0.3031 REMARK 3 12 2.3200 - 2.2500 1.00 2570 136 0.2523 0.2655 REMARK 3 13 2.2500 - 2.1900 1.00 2586 136 0.2593 0.2837 REMARK 3 14 2.1900 - 2.1400 1.00 2588 136 0.2689 0.2730 REMARK 3 15 2.1400 - 2.0900 0.98 2528 133 0.2864 0.3174 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.224 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.793 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.02 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.60 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 5402 REMARK 3 ANGLE : 0.554 7302 REMARK 3 CHIRALITY : 0.039 800 REMARK 3 PLANARITY : 0.004 936 REMARK 3 DIHEDRAL : 15.557 729 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.4282 4.8763 -36.0513 REMARK 3 T TENSOR REMARK 3 T11: 0.2104 T22: 0.4021 REMARK 3 T33: 0.2175 T12: -0.0151 REMARK 3 T13: -0.0142 T23: -0.0417 REMARK 3 L TENSOR REMARK 3 L11: 1.3323 L22: 2.9348 REMARK 3 L33: 2.1290 L12: 0.6146 REMARK 3 L13: -0.5852 L23: -1.1353 REMARK 3 S TENSOR REMARK 3 S11: -0.0159 S12: -0.0029 S13: 0.0035 REMARK 3 S21: 0.0429 S22: -0.0485 S23: -0.0433 REMARK 3 S31: -0.0305 S32: -0.1317 S33: 0.0059 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.2129 8.8974 -38.9066 REMARK 3 T TENSOR REMARK 3 T11: 0.2102 T22: 0.3749 REMARK 3 T33: 0.2552 T12: 0.0206 REMARK 3 T13: -0.0208 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 1.2638 L22: 2.0141 REMARK 3 L33: 1.7628 L12: 0.2023 REMARK 3 L13: -0.7882 L23: -0.7261 REMARK 3 S TENSOR REMARK 3 S11: 0.0465 S12: -0.0625 S13: 0.1951 REMARK 3 S21: -0.0696 S22: -0.0677 S23: -0.0264 REMARK 3 S31: -0.1091 S32: -0.1808 S33: 0.0293 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.9549 26.6309 -63.4037 REMARK 3 T TENSOR REMARK 3 T11: 0.6575 T22: 0.3900 REMARK 3 T33: 0.5069 T12: -0.0079 REMARK 3 T13: -0.0028 T23: 0.0554 REMARK 3 L TENSOR REMARK 3 L11: 2.2289 L22: 2.2257 REMARK 3 L33: 5.8804 L12: -0.1947 REMARK 3 L13: -1.6706 L23: 0.6208 REMARK 3 S TENSOR REMARK 3 S11: 0.1635 S12: 0.4071 S13: 0.6881 REMARK 3 S21: 0.1317 S22: 0.0438 S23: 0.3883 REMARK 3 S31: -1.0511 S32: -0.6327 S33: -0.4059 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.7571 5.8544 -46.2226 REMARK 3 T TENSOR REMARK 3 T11: 0.3706 T22: 0.4850 REMARK 3 T33: 0.3264 T12: -0.0453 REMARK 3 T13: 0.0273 T23: 0.0278 REMARK 3 L TENSOR REMARK 3 L11: -0.1856 L22: 4.7345 REMARK 3 L33: 5.3368 L12: -1.8439 REMARK 3 L13: 2.2986 L23: -6.5641 REMARK 3 S TENSOR REMARK 3 S11: 0.1147 S12: 0.1393 S13: -0.0774 REMARK 3 S21: -0.0709 S22: -0.1315 S23: -0.0118 REMARK 3 S31: 0.0580 S32: 0.4837 S33: 0.1227 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.3172 4.2921 -16.9178 REMARK 3 T TENSOR REMARK 3 T11: 0.2230 T22: 0.3935 REMARK 3 T33: 0.2267 T12: -0.0396 REMARK 3 T13: -0.0131 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 2.6345 L22: 1.9205 REMARK 3 L33: 3.5090 L12: 0.2289 REMARK 3 L13: 0.4399 L23: 0.0639 REMARK 3 S TENSOR REMARK 3 S11: 0.0590 S12: -0.3041 S13: -0.0147 REMARK 3 S21: 0.1342 S22: -0.0548 S23: -0.1290 REMARK 3 S31: -0.0261 S32: -0.0265 S33: 0.0024 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0849 4.5353 -40.9179 REMARK 3 T TENSOR REMARK 3 T11: 0.2249 T22: 0.3549 REMARK 3 T33: 0.2664 T12: 0.0074 REMARK 3 T13: 0.0267 T23: 0.0324 REMARK 3 L TENSOR REMARK 3 L11: 0.3158 L22: 0.4761 REMARK 3 L33: 1.0895 L12: 0.0869 REMARK 3 L13: 0.4339 L23: -0.0712 REMARK 3 S TENSOR REMARK 3 S11: -0.0652 S12: -0.0674 S13: 0.0587 REMARK 3 S21: -0.0346 S22: 0.0519 S23: -0.0629 REMARK 3 S31: 0.1657 S32: -0.2543 S33: 0.0198 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 611 THROUGH 618 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.5635 2.8848 -23.2310 REMARK 3 T TENSOR REMARK 3 T11: 0.3197 T22: 0.5627 REMARK 3 T33: 0.2777 T12: -0.0967 REMARK 3 T13: 0.0531 T23: -0.0793 REMARK 3 L TENSOR REMARK 3 L11: 6.1249 L22: 5.0405 REMARK 3 L33: 4.8958 L12: -0.0929 REMARK 3 L13: 0.3991 L23: -1.8988 REMARK 3 S TENSOR REMARK 3 S11: 0.3997 S12: -0.4854 S13: -0.1498 REMARK 3 S21: 0.4830 S22: 0.0444 S23: 0.3935 REMARK 3 S31: -0.2921 S32: -0.4682 S33: -0.5312 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.9793 20.2521 -12.3464 REMARK 3 T TENSOR REMARK 3 T11: 0.2928 T22: 0.4569 REMARK 3 T33: 0.2661 T12: 0.0057 REMARK 3 T13: -0.0320 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 3.0903 L22: 1.7736 REMARK 3 L33: 1.3073 L12: -0.8166 REMARK 3 L13: 1.2262 L23: -1.1453 REMARK 3 S TENSOR REMARK 3 S11: 0.0376 S12: 0.4480 S13: 0.1405 REMARK 3 S21: -0.2948 S22: -0.0591 S23: 0.0869 REMARK 3 S31: 0.0209 S32: 0.0172 S33: 0.0167 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 118 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.2886 38.2835 -36.1984 REMARK 3 T TENSOR REMARK 3 T11: 0.3748 T22: 0.5612 REMARK 3 T33: 0.4634 T12: -0.1016 REMARK 3 T13: -0.0110 T23: 0.0156 REMARK 3 L TENSOR REMARK 3 L11: 6.0552 L22: 3.3143 REMARK 3 L33: 6.6071 L12: 1.4849 REMARK 3 L13: 5.1296 L23: 1.5577 REMARK 3 S TENSOR REMARK 3 S11: 0.0647 S12: -0.2461 S13: -0.2640 REMARK 3 S21: 0.0766 S22: -0.2654 S23: 0.5693 REMARK 3 S31: 0.7468 S32: -0.8892 S33: -0.0480 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 125 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.6295 48.6715 -21.4393 REMARK 3 T TENSOR REMARK 3 T11: 0.2070 T22: 0.2854 REMARK 3 T33: 0.2067 T12: 0.0370 REMARK 3 T13: 0.0346 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 6.5767 L22: 1.7505 REMARK 3 L33: 7.7373 L12: 2.4990 REMARK 3 L13: 6.7078 L23: 2.6201 REMARK 3 S TENSOR REMARK 3 S11: -0.1859 S12: 0.2365 S13: 0.1526 REMARK 3 S21: -0.0654 S22: 0.1156 S23: 0.1024 REMARK 3 S31: -0.1483 S32: 0.1861 S33: 0.0645 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.3640 27.1829 7.6954 REMARK 3 T TENSOR REMARK 3 T11: 0.2228 T22: 0.3383 REMARK 3 T33: 0.2273 T12: 0.0230 REMARK 3 T13: 0.0040 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 1.8836 L22: 4.9161 REMARK 3 L33: 2.6729 L12: 0.5600 REMARK 3 L13: 0.2799 L23: -0.7270 REMARK 3 S TENSOR REMARK 3 S11: -0.0397 S12: -0.1282 S13: 0.1125 REMARK 3 S21: 0.1589 S22: -0.0292 S23: -0.0440 REMARK 3 S31: -0.0814 S32: -0.1172 S33: 0.0690 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 102 THROUGH 159 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.7280 41.5829 -13.8620 REMARK 3 T TENSOR REMARK 3 T11: 0.2814 T22: 0.3141 REMARK 3 T33: 0.2794 T12: 0.0375 REMARK 3 T13: 0.0160 T23: 0.0343 REMARK 3 L TENSOR REMARK 3 L11: 3.6426 L22: 0.3294 REMARK 3 L33: 4.1742 L12: 0.5519 REMARK 3 L13: 3.1000 L23: 0.2746 REMARK 3 S TENSOR REMARK 3 S11: 0.0943 S12: -0.1634 S13: -0.0904 REMARK 3 S21: 0.1002 S22: 0.0379 S23: 0.0036 REMARK 3 S31: 0.1889 S32: 0.0703 S33: -0.0872 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 611 THROUGH 618 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.6225 10.4170 2.0314 REMARK 3 T TENSOR REMARK 3 T11: 0.3644 T22: 0.2340 REMARK 3 T33: 0.4140 T12: 0.0449 REMARK 3 T13: 0.0373 T23: 0.0308 REMARK 3 L TENSOR REMARK 3 L11: 4.2635 L22: 5.7922 REMARK 3 L33: 5.5029 L12: 0.3782 REMARK 3 L13: -0.5673 L23: 1.8230 REMARK 3 S TENSOR REMARK 3 S11: -0.2260 S12: -0.4015 S13: -0.8058 REMARK 3 S21: 0.2445 S22: 0.1421 S23: 0.0448 REMARK 3 S31: 0.9781 S32: 0.0806 S33: 0.0013 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 9IUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049667. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-MAY-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 : SPRING-8 REMARK 200 BEAMLINE : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41195 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090 REMARK 200 RESOLUTION RANGE LOW (A) : 42.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.12400 REMARK 200 FOR THE DATA SET : 10.6600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.83000 REMARK 200 FOR SHELL : 2.080 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 (%): 44.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M BIS-TRIS PH 5.7, REMARK 280 25% W/V PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.04150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.04150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.27250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.59950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.27250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.59950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.04150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.27250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.59950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.04150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.27250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.59950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16270 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 227 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 247 LIES ON A SPECIAL POSITION. 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 ALA A 163 REMARK 465 LYS A 164 REMARK 465 GLY B -1 REMARK 465 ARG B 108 REMARK 465 GLY B 109 REMARK 465 SER B 110 REMARK 465 ASP B 111 REMARK 465 TYR B 112 REMARK 465 GLU B 113 REMARK 465 GLY D -1 REMARK 465 ALA D 163 REMARK 465 LYS D 164 REMARK 465 GLY E -1 REMARK 465 ARG E 0 REMARK 465 LYS E 107 REMARK 465 ARG E 108 REMARK 465 GLY E 109 REMARK 465 SER E 110 REMARK 465 ASP E 111 REMARK 465 GLY E 160 REMARK 465 THR E 161 REMARK 465 LEU E 162 REMARK 465 LEU E 163 REMARK 465 GLY E 164 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 VAL B 51 -50.40 72.06 REMARK 500 ARG D 43 -11.58 77.83 REMARK 500 VAL E 51 -50.38 69.38 REMARK 500 REMARK 500 REMARK: NULL DBREF 9IUT A -1 164 PDB 9IUT 9IUT -1 164 DBREF 9IUT B -1 164 PDB 9IUT 9IUT -1 164 DBREF 9IUT C 611 618 UNP P04626 ERBB2_HUMAN 611 618 DBREF 9IUT D -1 164 PDB 9IUT 9IUT -1 164 DBREF 9IUT E -1 164 PDB 9IUT 9IUT -1 164 DBREF 9IUT F 611 618 UNP P04626 ERBB2_HUMAN 611 618 SEQRES 1 A 169 GLY ARG GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 A 169 VAL GLN PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SEQRES 3 A 169 SER GLY PHE THR PHE SER ASN TYR GLY MET SER TRP VAL SEQRES 4 A 169 ARG GLN THR PRO ASP ARG ARG LEU GLU LEU VAL ALA THR SEQRES 5 A 169 ILE ASN ASN ASN GLY GLY GLY THR TYR TYR PRO ASP SER SEQRES 6 A 169 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 A 169 ASN THR LEU TYR LEU GLN MET SER SER LEU LYS SER GLU SEQRES 8 A 169 ASP THR ALA MET TYR TYR CYS THR SER PRO GLY LEU LEU SEQRES 9 A 169 TRP ASP ALA TRP GLY ALA GLY THR THR VAL THR VAL CYS SEQRES 10 A 169 SER GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL SEQRES 11 A 169 GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET SEQRES 12 A 169 MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SEQRES 13 A 169 SER LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 B 171 GLY ARG ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SEQRES 2 B 171 SER VAL SER ILE GLY GLN PRO ALA SER ILE SER CYS LYS SEQRES 3 B 171 SER SER GLN SER LEU LEU ASP SER ASP GLY ARG THR TYR SEQRES 4 B 171 LEU ASN TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS SEQRES 5 B 171 ARG LEU ILE TYR LEU VAL SER LYS LEU ASP SER GLY ALA SEQRES 6 B 171 PRO ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE SEQRES 7 B 171 THR LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY SEQRES 8 B 171 VAL TYR TYR CYS TRP GLN GLY THR HIS PHE PRO GLN THR SEQRES 9 B 171 PHE GLY GLY GLY THR LYS LEU GLU ILE LYS ARG GLY SER SEQRES 10 B 171 ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU SEQRES 11 B 171 GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN SEQRES 12 B 171 GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS ARG SEQRES 13 B 171 GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS GLY THR LEU SEQRES 14 B 171 LEU GLY SEQRES 1 C 8 MET PRO ILE TRP LYS PHE PRO ASP SEQRES 1 D 169 GLY ARG GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 D 169 VAL GLN PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SEQRES 3 D 169 SER GLY PHE THR PHE SER ASN TYR GLY MET SER TRP VAL SEQRES 4 D 169 ARG GLN THR PRO ASP ARG ARG LEU GLU LEU VAL ALA THR SEQRES 5 D 169 ILE ASN ASN ASN GLY GLY GLY THR TYR TYR PRO ASP SER SEQRES 6 D 169 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 D 169 ASN THR LEU TYR LEU GLN MET SER SER LEU LYS SER GLU SEQRES 8 D 169 ASP THR ALA MET TYR TYR CYS THR SER PRO GLY LEU LEU SEQRES 9 D 169 TRP ASP ALA TRP GLY ALA GLY THR THR VAL THR VAL CYS SEQRES 10 D 169 SER GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL SEQRES 11 D 169 GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET SEQRES 12 D 169 MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SEQRES 13 D 169 SER LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 E 171 GLY ARG ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SEQRES 2 E 171 SER VAL SER ILE GLY GLN PRO ALA SER ILE SER CYS LYS SEQRES 3 E 171 SER SER GLN SER LEU LEU ASP SER ASP GLY ARG THR TYR SEQRES 4 E 171 LEU ASN TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS SEQRES 5 E 171 ARG LEU ILE TYR LEU VAL SER LYS LEU ASP SER GLY ALA SEQRES 6 E 171 PRO ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE SEQRES 7 E 171 THR LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY SEQRES 8 E 171 VAL TYR TYR CYS TRP GLN GLY THR HIS PHE PRO GLN THR SEQRES 9 E 171 PHE GLY GLY GLY THR LYS LEU GLU ILE LYS ARG GLY SER SEQRES 10 E 171 ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU SEQRES 11 E 171 GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN SEQRES 12 E 171 GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS ARG SEQRES 13 E 171 GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS GLY THR LEU SEQRES 14 E 171 LEU GLY SEQRES 1 F 8 MET PRO ILE TRP LYS PHE PRO ASP FORMUL 7 HOH *374(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 LYS A 83 THR A 87 5 5 HELIX 3 AA3 TYR A 117 TRP A 123 5 7 HELIX 4 AA4 THR A 124 GLU A 162 1 39 HELIX 5 AA5 GLU B 79 LEU B 83 5 5 HELIX 6 AA6 PHE B 114 TRP B 118 5 5 HELIX 7 AA7 THR B 119 ALA B 158 1 40 HELIX 8 AA8 THR D 28 TYR D 32 5 5 HELIX 9 AA9 ASN D 73 LYS D 75 5 3 HELIX 10 AB1 LYS D 83 THR D 87 5 5 HELIX 11 AB2 TYR D 117 TRP D 123 5 7 HELIX 12 AB3 THR D 124 GLU D 162 1 39 HELIX 13 AB4 GLU E 79 LEU E 83 5 5 HELIX 14 AB5 TYR E 112 TRP E 118 5 7 HELIX 15 AB6 THR E 119 ALA E 129 1 11 HELIX 16 AB7 ALA E 129 LYS E 159 1 31 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 THR A 93 -1 N ALA A 88 O VAL A 109 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 57 TYR A 58 -1 O TYR A 58 N THR A 50 SHEET 1 AA3 4 MET B 4 THR B 7 0 SHEET 2 AA3 4 ALA B 19 SER B 25 -1 O SER B 22 N THR B 7 SHEET 3 AA3 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA3 4 PHE B 62 SER B 67 -1 N SER B 65 O THR B 72 SHEET 1 AA4 6 THR B 10 VAL B 13 0 SHEET 2 AA4 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AA4 6 GLY B 84 GLN B 90 -1 N GLY B 84 O LEU B 104 SHEET 4 AA4 6 LEU B 33 GLN B 38 -1 N ASN B 34 O TRP B 89 SHEET 5 AA4 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA4 6 LYS B 53 LEU B 54 -1 O LYS B 53 N TYR B 49 SHEET 1 AA5 4 GLN D 3 SER D 7 0 SHEET 2 AA5 4 SER D 17 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AA5 4 THR D 77 SER D 82A-1 O MET D 82 N LEU D 18 SHEET 4 AA5 4 PHE D 67 ASP D 72 -1 N SER D 70 O TYR D 79 SHEET 1 AA6 6 LEU D 11 VAL D 12 0 SHEET 2 AA6 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AA6 6 ALA D 88 THR D 93 -1 N TYR D 90 O THR D 107 SHEET 4 AA6 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 91 SHEET 5 AA6 6 LEU D 45 ILE D 51 -1 O VAL D 48 N TRP D 36 SHEET 6 AA6 6 THR D 57 TYR D 58 -1 O TYR D 58 N THR D 50 SHEET 1 AA7 4 MET E 4 THR E 7 0 SHEET 2 AA7 4 ALA E 19 SER E 25 -1 O LYS E 24 N THR E 5 SHEET 3 AA7 4 ASP E 70 ILE E 75 -1 O ILE E 75 N ALA E 19 SHEET 4 AA7 4 PHE E 62 SER E 67 -1 N THR E 63 O LYS E 74 SHEET 1 AA8 6 THR E 10 SER E 12 0 SHEET 2 AA8 6 THR E 102 GLU E 105 1 O LYS E 103 N LEU E 11 SHEET 3 AA8 6 GLY E 84 GLN E 90 -1 N GLY E 84 O LEU E 104 SHEET 4 AA8 6 LEU E 33 GLN E 38 -1 N LEU E 36 O TYR E 87 SHEET 5 AA8 6 PRO E 44 TYR E 49 -1 O LEU E 47 N TRP E 35 SHEET 6 AA8 6 LYS E 53 LEU E 54 -1 O LYS E 53 N TYR E 49 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 2 CYS A 112 CYS B 147 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 5 CYS D 112 CYS E 147 1555 1555 2.03 SSBOND 6 CYS E 23 CYS E 88 1555 1555 2.03 CISPEP 1 THR B 7 PRO B 8 0 -2.70 CISPEP 2 PHE B 94 PRO B 95 0 5.14 CISPEP 3 THR E 7 PRO E 8 0 -4.01 CISPEP 4 PHE E 94 PRO E 95 0 3.05 CRYST1 116.545 123.199 96.083 90.00 90.00 90.00 C 2 2 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008580 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008117 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010408 0.00000