HEADER IMMUNE SYSTEM 08-MAR-22 7U8C TITLE CRYSTAL STRUCTURE OF MESOTHELIN C-TERMINAL PEPTIDE-MORAB 15B6 FAB TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: MESOTHELIN, CLEAVED FORM; COMPND 3 CHAIN: BA2; COMPND 4 FRAGMENT: C-TERMINAL PEPTIDE (UNP RESIDUES 590-606); COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MORAB 15B6 FAB HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: MORAB 15B6 FAB LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: MOUSE; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_COMMON: MOUSE; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: MOUSE; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS MESOTHELIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.ZHAN,L.ESSER,D.XIA JRNL AUTH X.LIU,M.ONDA,N.WATSON,R.HASSAN,M.HO,T.K.BERA,J.WEI, JRNL AUTH 2 A.CHAKRABORTY,R.BEERS,Q.ZHOU,A.SHAJAHAN,P.AZADI,J.ZHAN, JRNL AUTH 3 D.XIA,I.PASTAN JRNL TITL HIGHLY ACTIVE CAR T CELLS THAT BIND TO A JUXTAMEMBRANE JRNL TITL 2 REGION OF MESOTHELIN AND ARE NOT BLOCKED BY SHED MESOTHELIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 119 39119 2022 JRNL REFN ESSN 1091-6490 JRNL PMID 35512094 JRNL DOI 10.1073/PNAS.2202439119 REMARK 2 REMARK 2 RESOLUTION. 1.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.01 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 NUMBER OF REFLECTIONS : 53531 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 2770 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 24.0100 - 4.7100 1.00 2942 165 0.1779 0.2075 REMARK 3 2 4.7100 - 3.7400 1.00 2768 162 0.1534 0.1928 REMARK 3 3 3.7400 - 3.2700 1.00 2725 127 0.1913 0.2372 REMARK 3 4 3.2700 - 2.9700 1.00 2723 119 0.2066 0.2209 REMARK 3 5 2.9700 - 2.7600 1.00 2697 142 0.2174 0.2388 REMARK 3 6 2.7600 - 2.6000 1.00 2651 148 0.2014 0.2388 REMARK 3 7 2.6000 - 2.4700 1.00 2658 149 0.1940 0.2311 REMARK 3 8 2.4700 - 2.3600 1.00 2659 144 0.2038 0.2495 REMARK 3 9 2.3600 - 2.2700 1.00 2627 150 0.2090 0.2464 REMARK 3 10 2.2700 - 2.1900 1.00 2609 152 0.2125 0.2638 REMARK 3 11 2.1900 - 2.1200 1.00 2653 140 0.2325 0.3024 REMARK 3 12 2.1200 - 2.0600 1.00 2630 148 0.2558 0.2911 REMARK 3 13 2.0600 - 2.0100 1.00 2617 134 0.2688 0.3215 REMARK 3 14 2.0100 - 1.9600 1.00 2578 151 0.2947 0.3016 REMARK 3 15 1.9600 - 1.9100 1.00 2615 125 0.3067 0.3542 REMARK 3 16 1.9100 - 1.8700 0.94 2483 153 0.3167 0.3337 REMARK 3 17 1.8700 - 1.8400 0.89 2282 125 0.3393 0.3268 REMARK 3 18 1.8400 - 1.8000 0.84 2188 116 0.3459 0.3840 REMARK 3 19 1.8000 - 1.7700 0.77 1995 132 0.3490 0.3723 REMARK 3 20 1.7700 - 1.7400 0.63 1661 88 0.3691 0.3716 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) : 0.222 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.311 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.07 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.17 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 3405 REMARK 3 ANGLE : 0.534 4651 REMARK 3 CHIRALITY : 0.044 539 REMARK 3 PLANARITY : 0.003 586 REMARK 3 DIHEDRAL : 11.837 1189 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'BA2' AND (RESID 584 THROUGH 590 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.1636 -8.7891 58.3587 REMARK 3 T TENSOR REMARK 3 T11: 0.5246 T22: 0.8286 REMARK 3 T33: 0.3124 T12: 0.1019 REMARK 3 T13: -0.0400 T23: 0.0654 REMARK 3 L TENSOR REMARK 3 L11: 2.2336 L22: 4.3751 REMARK 3 L33: 7.0180 L12: -0.8525 REMARK 3 L13: -2.7834 L23: 2.7138 REMARK 3 S TENSOR REMARK 3 S11: -0.4610 S12: -0.4796 S13: 0.1851 REMARK 3 S21: 1.3240 S22: 0.2124 S23: -0.2653 REMARK 3 S31: 0.4160 S32: 0.6737 S33: 0.2041 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'BA2' AND (RESID 591 THROUGH 598 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.8724 -18.1063 51.0458 REMARK 3 T TENSOR REMARK 3 T11: 0.3359 T22: 0.9732 REMARK 3 T33: 0.3359 T12: 0.0860 REMARK 3 T13: -0.0176 T23: 0.0218 REMARK 3 L TENSOR REMARK 3 L11: 5.1706 L22: 5.9371 REMARK 3 L33: 4.3968 L12: -4.6098 REMARK 3 L13: -1.3133 L23: 1.6022 REMARK 3 S TENSOR REMARK 3 S11: -0.6623 S12: -0.5050 S13: 0.1487 REMARK 3 S21: 1.1316 S22: 0.2704 S23: -0.5357 REMARK 3 S31: 0.2388 S32: 0.7792 S33: 0.1916 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.3413 -0.8128 37.4232 REMARK 3 T TENSOR REMARK 3 T11: 0.2102 T22: 0.5885 REMARK 3 T33: 0.3653 T12: -0.0385 REMARK 3 T13: -0.0538 T23: 0.0674 REMARK 3 L TENSOR REMARK 3 L11: 1.2743 L22: 1.5545 REMARK 3 L33: 3.9605 L12: 0.1940 REMARK 3 L13: 0.6746 L23: -0.3184 REMARK 3 S TENSOR REMARK 3 S11: -0.1378 S12: -0.1540 S13: 0.1329 REMARK 3 S21: -0.0462 S22: 0.0857 S23: 0.0398 REMARK 3 S31: -0.5885 S32: 0.2243 S33: 0.0747 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 121 THROUGH 135 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4768 -11.2929 -6.2247 REMARK 3 T TENSOR REMARK 3 T11: 0.8143 T22: 0.9784 REMARK 3 T33: 0.5961 T12: -0.1169 REMARK 3 T13: -0.0133 T23: 0.1091 REMARK 3 L TENSOR REMARK 3 L11: 1.8288 L22: 7.5830 REMARK 3 L33: 3.4995 L12: 0.9709 REMARK 3 L13: 0.7352 L23: -0.2388 REMARK 3 S TENSOR REMARK 3 S11: 0.0393 S12: 0.7955 S13: -0.1004 REMARK 3 S21: -1.6769 S22: 0.2034 S23: -1.1933 REMARK 3 S31: -0.1482 S32: 1.0589 S33: -0.2421 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 136 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.2731 -8.4723 3.0930 REMARK 3 T TENSOR REMARK 3 T11: 0.4994 T22: 0.6669 REMARK 3 T33: 0.4191 T12: -0.1658 REMARK 3 T13: -0.1364 T23: 0.2218 REMARK 3 L TENSOR REMARK 3 L11: 1.4536 L22: 2.2821 REMARK 3 L33: 4.4911 L12: -0.4773 REMARK 3 L13: 0.2324 L23: 0.9050 REMARK 3 S TENSOR REMARK 3 S11: -0.1595 S12: 0.2464 S13: -0.2091 REMARK 3 S21: -0.4580 S22: 0.0455 S23: 0.2020 REMARK 3 S31: -0.1317 S32: 0.0935 S33: 0.0340 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.1196 -20.2715 33.3181 REMARK 3 T TENSOR REMARK 3 T11: 0.1425 T22: 0.8429 REMARK 3 T33: 0.4276 T12: -0.0157 REMARK 3 T13: 0.0000 T23: 0.0890 REMARK 3 L TENSOR REMARK 3 L11: 1.7839 L22: 0.7335 REMARK 3 L33: 0.5415 L12: -0.4111 REMARK 3 L13: 0.0736 L23: 0.0784 REMARK 3 S TENSOR REMARK 3 S11: -0.0243 S12: -0.1880 S13: 0.1173 REMARK 3 S21: 0.0632 S22: 0.0423 S23: -0.3859 REMARK 3 S31: 0.0496 S32: 0.2528 S33: -0.1163 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 31 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.5467 -19.2508 37.8988 REMARK 3 T TENSOR REMARK 3 T11: 0.1134 T22: 0.8185 REMARK 3 T33: 0.3878 T12: 0.0177 REMARK 3 T13: -0.0189 T23: 0.1208 REMARK 3 L TENSOR REMARK 3 L11: 1.3011 L22: 0.9835 REMARK 3 L33: 1.1194 L12: -0.1143 REMARK 3 L13: 0.3327 L23: 0.2941 REMARK 3 S TENSOR REMARK 3 S11: -0.1995 S12: -0.3833 S13: -0.0824 REMARK 3 S21: 0.1231 S22: 0.1497 S23: -0.0771 REMARK 3 S31: 0.2271 S32: 0.2086 S33: -0.1344 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 104 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1788 -26.9372 18.5132 REMARK 3 T TENSOR REMARK 3 T11: 0.2196 T22: 0.6695 REMARK 3 T33: 0.3830 T12: -0.0512 REMARK 3 T13: 0.0330 T23: 0.0993 REMARK 3 L TENSOR REMARK 3 L11: 0.7625 L22: 0.4627 REMARK 3 L33: 3.2940 L12: -0.3579 REMARK 3 L13: 0.6821 L23: 0.5720 REMARK 3 S TENSOR REMARK 3 S11: -0.0605 S12: 0.1582 S13: 0.0773 REMARK 3 S21: -0.1524 S22: 0.0340 S23: 0.0239 REMARK 3 S31: -0.0455 S32: 0.3176 S33: -0.0185 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 117 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.9076 -7.0861 0.5269 REMARK 3 T TENSOR REMARK 3 T11: 0.5472 T22: 0.9030 REMARK 3 T33: 0.4186 T12: -0.1996 REMARK 3 T13: -0.0752 T23: 0.2761 REMARK 3 L TENSOR REMARK 3 L11: 1.2115 L22: 4.8634 REMARK 3 L33: 1.1795 L12: -0.5993 REMARK 3 L13: 0.1701 L23: -0.9962 REMARK 3 S TENSOR REMARK 3 S11: -0.0132 S12: 0.5040 S13: 0.2736 REMARK 3 S21: -0.7206 S22: -0.1300 S23: -0.0986 REMARK 3 S31: -0.4434 S32: 0.5151 S33: 0.1733 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 143 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.8759 -9.9688 8.1459 REMARK 3 T TENSOR REMARK 3 T11: 0.4451 T22: 0.8893 REMARK 3 T33: 0.4620 T12: -0.2416 REMARK 3 T13: -0.0530 T23: 0.2453 REMARK 3 L TENSOR REMARK 3 L11: 1.3183 L22: 2.4477 REMARK 3 L33: 0.5719 L12: -0.1962 REMARK 3 L13: -0.2308 L23: 0.0180 REMARK 3 S TENSOR REMARK 3 S11: -0.0972 S12: 0.3852 S13: 0.2097 REMARK 3 S21: -0.2936 S22: -0.0007 S23: -0.3064 REMARK 3 S31: -0.4166 S32: 0.4421 S33: 0.0550 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 191 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.2945 -13.9889 0.8560 REMARK 3 T TENSOR REMARK 3 T11: 0.5826 T22: 1.0828 REMARK 3 T33: 0.4861 T12: -0.1239 REMARK 3 T13: 0.0722 T23: 0.2008 REMARK 3 L TENSOR REMARK 3 L11: 0.3900 L22: 1.2510 REMARK 3 L33: 0.7253 L12: -0.3586 REMARK 3 L13: 0.0790 L23: 0.4969 REMARK 3 S TENSOR REMARK 3 S11: 0.1128 S12: 0.2613 S13: 0.2225 REMARK 3 S21: -0.8907 S22: -0.0683 S23: -0.2809 REMARK 3 S31: -0.2053 S32: 0.3561 S33: 0.0957 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 7U8C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000263383. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03317 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53658 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 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 (%) : 95.3 REMARK 200 DATA REDUNDANCY : 27.40 REMARK 200 R MERGE (I) : 0.09200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 35.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.49700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: BALBES REMARK 200 STARTING MODEL: PDB ENTRY 3RIF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.5, 26% REMARK 280 PEG550 MME, 6% 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 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 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 125.06700 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.41600 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.41600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 187.60050 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.41600 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.41600 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.53350 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.41600 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.41600 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 187.60050 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.41600 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.41600 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 62.53350 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 125.06700 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: BA2, H, L 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 H 301 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 431 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 ILE B 582 REMARK 465 PRO B 583 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 H 420 O HOH H 421 2.10 REMARK 500 O HOH H 406 O HOH H 422 2.13 REMARK 500 O HOH L 437 O HOH L 448 2.14 REMARK 500 O HOH L 416 O HOH L 435 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG SER L 96 OD1 ASP L 213 4555 2.07 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 SER H 44 -134.90 61.36 REMARK 500 SER H 161 -35.67 -150.77 REMARK 500 TYR L 34 61.65 38.66 REMARK 500 ASP L 43 35.67 82.82 REMARK 500 THR L 53 -53.86 77.40 REMARK 500 ASN L 54 19.20 -152.36 REMARK 500 SER L 95 -53.11 69.10 REMARK 500 SER L 96 11.79 -144.59 REMARK 500 LEU L 109 107.16 -53.61 REMARK 500 SER L 192 -65.09 -98.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 466 DISTANCE = 6.05 ANGSTROMS REMARK 525 HOH L 467 DISTANCE = 6.48 ANGSTROMS DBREF 7U8CA2 582 598 UNP Q13421 MSLN_HUMAN 590 606 DBREF 7U8C H 1 214 PDB 7U8C 7U8C 1 214 DBREF 7U8C L 1 213 PDB 7U8C 7U8C 1 213 SEQRES 1A2 17 ILE PRO ASN GLY TYR LEU VAL LEU ASP LEU SER MET GLN SEQRES 2A2 17 GLU ALA LEU SER SEQRES 1 H 214 GLU VAL GLN LEU GLN GLN SER GLY PRO VAL LEU VAL LYS SEQRES 2 H 214 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 214 TYR SER PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 214 SER ASN GLY LYS SER LEU GLU TRP ILE GLY ARG ILE ASN SEQRES 5 H 214 PRO TYR THR GLY VAL PRO SER TYR LYS HIS ASN PHE LYS SEQRES 6 H 214 ASP LYS ALA SER LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 H 214 ALA TYR MET GLU LEU HIS SER LEU THR SER GLU ASP SER SEQRES 8 H 214 ALA VAL TYR TYR CYS ALA ARG GLU LEU GLY GLY TYR TRP SEQRES 9 H 214 GLY GLN GLY THR THR LEU THR VAL SER SER ALA LYS THR SEQRES 10 H 214 THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY CYS GLY SEQRES 11 H 214 ASP THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL SEQRES 12 H 214 LYS GLY TYR PHE PRO GLU SER VAL THR VAL THR TRP ASN SEQRES 13 H 214 SER GLY SER LEU SER SER SER VAL HIS THR PHE PRO ALA SEQRES 14 H 214 LEU LEU GLN SER GLY LEU TYR THR MET SER SER SER VAL SEQRES 15 H 214 THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR SEQRES 16 H 214 CYS SER VAL ALA HIS PRO ALA SER SER THR THR VAL ASP SEQRES 17 H 214 LYS LYS LEU GLU PRO SER SEQRES 1 L 213 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 L 213 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 L 213 GLY ALA VAL THR THR GLY ASN TYR PRO ASN TRP VAL GLN SEQRES 4 L 213 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE ALA GLY SEQRES 5 L 213 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 L 213 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 L 213 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 L 213 LEU TRP PHE SER SER HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 L 213 LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SER SEQRES 10 L 213 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLU THR SEQRES 11 L 213 ASN LYS ALA THR LEU VAL CYS THR ILE THR ASP PHE TYR SEQRES 12 L 213 PRO GLY VAL VAL THR VAL ASP TRP LYS VAL ASP GLY THR SEQRES 13 L 213 PRO VAL THR GLN GLY MET GLU THR THR GLN PRO SER LYS SEQRES 14 L 213 GLN SER ASN ASN LYS TYR MET ALA SER SER TYR LEU THR SEQRES 15 L 213 LEU THR ALA ARG ALA TRP GLU ARG HIS SER SER PHE SER SEQRES 16 L 213 CYS GLN VAL THR HIS GLU GLY HIS THR VAL GLU LYS SER SEQRES 17 L 213 SER SER ARG ALA ASP FORMUL 4 HOH *311(H2 O) HELIX 1 AA1 ASPA2 590 GLNA2 594 5 5 HELIX 2 AA2 SER H 28 TYR H 32 5 5 HELIX 3 AA3 HIS H 62 LYS H 65 5 4 HELIX 4 AA4 THR H 87 SER H 91 5 5 HELIX 5 AA5 SER H 157 SER H 159 5 3 HELIX 6 AA6 PRO H 201 SER H 204 5 4 HELIX 7 AA7 THR L 30 TYR L 34 5 5 HELIX 8 AA8 GLN L 81 GLU L 85 5 5 HELIX 9 AA9 SER L 124 GLU L 129 1 6 HELIX 10 AB1 ALA L 185 ARG L 190 1 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N ILE H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA2 6 VAL H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O THR H 111 N VAL H 10 SHEET 3 AA2 6 ALA H 92 ALA H 97 -1 N ALA H 92 O LEU H 110 SHEET 4 AA2 6 MET H 34 SER H 40 -1 N HIS H 35 O ALA H 97 SHEET 5 AA2 6 SER H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 PRO H 58 TYR H 60 -1 O SER H 59 N ARG H 50 SHEET 1 AA3 4 SER H 121 LEU H 125 0 SHEET 2 AA3 4 SER H 136 TYR H 146 -1 O LEU H 142 N TYR H 123 SHEET 3 AA3 4 LEU H 175 PRO H 185 -1 O VAL H 182 N LEU H 139 SHEET 4 AA3 4 VAL H 164 THR H 166 -1 N HIS H 165 O SER H 181 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 SER H 136 TYR H 146 -1 O LEU H 142 N TYR H 123 SHEET 3 AA4 4 LEU H 175 PRO H 185 -1 O VAL H 182 N LEU H 139 SHEET 4 AA4 4 LEU H 170 GLN H 172 -1 N GLN H 172 O LEU H 175 SHEET 1 AA5 3 THR H 152 TRP H 155 0 SHEET 2 AA5 3 THR H 195 HIS H 200 -1 O SER H 197 N THR H 154 SHEET 3 AA5 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA6 4 VAL L 4 GLN L 6 0 SHEET 2 AA6 4 THR L 17 SER L 24 -1 O ARG L 23 N THR L 5 SHEET 3 AA6 4 LYS L 72 THR L 78 -1 O LEU L 75 N LEU L 20 SHEET 4 AA6 4 PHE L 64 ILE L 69 -1 N SER L 65 O THR L 76 SHEET 1 AA7 6 ALA L 9 THR L 12 0 SHEET 2 AA7 6 THR L 104 VAL L 108 1 O THR L 107 N LEU L 10 SHEET 3 AA7 6 ALA L 86 TRP L 93 -1 N ALA L 86 O LEU L 106 SHEET 4 AA7 6 ASN L 36 LYS L 41 -1 N GLU L 40 O ILE L 87 SHEET 5 AA7 6 LEU L 45 ALA L 51 -1 O THR L 47 N GLN L 39 SHEET 6 AA7 6 ASN L 55 ARG L 56 -1 O ASN L 55 N ALA L 51 SHEET 1 AA8 4 ALA L 9 THR L 12 0 SHEET 2 AA8 4 THR L 104 VAL L 108 1 O THR L 107 N LEU L 10 SHEET 3 AA8 4 ALA L 86 TRP L 93 -1 N ALA L 86 O LEU L 106 SHEET 4 AA8 4 TRP L 98 PHE L 100 -1 O VAL L 99 N LEU L 92 SHEET 1 AA9 4 SER L 117 PHE L 121 0 SHEET 2 AA9 4 LYS L 132 PHE L 142 -1 O VAL L 136 N PHE L 121 SHEET 3 AA9 4 TYR L 175 THR L 184 -1 O LEU L 183 N ALA L 133 SHEET 4 AA9 4 MET L 162 THR L 164 -1 N GLU L 163 O TYR L 180 SHEET 1 AB1 4 SER L 117 PHE L 121 0 SHEET 2 AB1 4 LYS L 132 PHE L 142 -1 O VAL L 136 N PHE L 121 SHEET 3 AB1 4 TYR L 175 THR L 184 -1 O LEU L 183 N ALA L 133 SHEET 4 AB1 4 SER L 168 LYS L 169 -1 N SER L 168 O MET L 176 SHEET 1 AB2 4 THR L 156 PRO L 157 0 SHEET 2 AB2 4 THR L 148 VAL L 153 -1 N VAL L 153 O THR L 156 SHEET 3 AB2 4 SER L 193 HIS L 200 -1 O GLN L 197 N ASP L 150 SHEET 4 AB2 4 HIS L 203 SER L 210 -1 O HIS L 203 N HIS L 200 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 2 CYS H 141 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 22 CYS L 90 1555 1555 2.06 SSBOND 4 CYS L 137 CYS L 196 1555 1555 2.04 CISPEP 1 PHE H 147 PRO H 148 0 -4.43 CISPEP 2 GLU H 149 SER H 150 0 2.93 CISPEP 3 TRP H 189 PRO H 190 0 4.65 CISPEP 4 TYR L 143 PRO L 144 0 0.32 CRYST1 64.832 64.832 250.134 90.00 90.00 90.00 P 43 21 2 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 0.015424 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015424 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003998 0.00000