HEADER CELL ADHESION 16-DEC-24 9HQ5 TITLE CRYSTAL STRUCTURE OF TETRASPANIN CD63MUTANT LARGE EXTRACELLULAR LOOP TITLE 2 (LEL) IN COMPLEX WITH SYBODY SB3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CD63 ANTIGEN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GRANULOPHYSIN,LYSOSOMAL-ASSOCIATED MEMBRANE PROTEIN 3,LAMP- COMPND 5 3,LYSOSOME INTEGRAL MEMBRANE PROTEIN 1,LIMP1,MELANOMA-ASSOCIATED COMPND 6 ANTIGEN ME491,OMA81H,OCULAR MELANOMA-ASSOCIATED ANTIGEN,TETRASPANIN- COMPND 7 30,TSPAN-30; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: SYBODY SB3; COMPND 12 CHAIN: B; COMPND 13 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: CD63, MLA1, TSPAN30; SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2 (S2) CELLS; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630; SOURCE 12 EXPRESSION_SYSTEM: BACTERIA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 2; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: E.COLI MC1061 KEYWDS VIRUS ENTRY AND INFECTION MODULATOR, REGULATION OF CELL ADHESION AND KEYWDS 2 MIGRATION, REGULATION OF IMMUNE RESPONSE, CELL ADHESION EXPDTA X-RAY DIFFRACTION AUTHOR K.NAGARATHINAM,T.KREY REVDAT 1 19-NOV-25 9HQ5 0 JRNL AUTH K.NAGARATHINAM,D.KARAKULOVA,D.THIYAGARAJ,T.KREY JRNL TITL EVOLUTIONARY RELATIONSHIP OF TETRASPANINS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 9776 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.247 REMARK 3 R VALUE (WORKING SET) : 0.245 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 488 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 47.5000 - 3.7500 1.00 3229 170 0.2209 0.2578 REMARK 3 2 3.7500 - 2.9800 1.00 3039 159 0.2514 0.3084 REMARK 3 3 2.9800 - 2.6000 1.00 3020 159 0.2892 0.3448 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) : 0.299 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.043 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.43 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.77 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 1638 REMARK 3 ANGLE : 0.404 2225 REMARK 3 CHIRALITY : 0.040 234 REMARK 3 PLANARITY : 0.003 291 REMARK 3 DIHEDRAL : 18.960 556 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5121 27.8725 -19.1577 REMARK 3 T TENSOR REMARK 3 T11: 0.2612 T22: 0.2017 REMARK 3 T33: 0.3217 T12: 0.0480 REMARK 3 T13: 0.1362 T23: 0.1349 REMARK 3 L TENSOR REMARK 3 L11: 0.0055 L22: 0.0119 REMARK 3 L33: 0.0341 L12: 0.0080 REMARK 3 L13: -0.0140 L23: -0.0204 REMARK 3 S TENSOR REMARK 3 S11: -0.0230 S12: -0.0082 S13: -0.0270 REMARK 3 S21: 0.0136 S22: -0.0055 S23: -0.0525 REMARK 3 S31: 0.0517 S32: 0.0163 S33: 0.0232 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.1866 33.7970 -10.3833 REMARK 3 T TENSOR REMARK 3 T11: 0.0950 T22: 0.0832 REMARK 3 T33: 0.3415 T12: -0.0184 REMARK 3 T13: 0.0383 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.6191 L22: 0.6453 REMARK 3 L33: 0.2530 L12: -0.0890 REMARK 3 L13: 0.0042 L23: 0.2158 REMARK 3 S TENSOR REMARK 3 S11: -0.1577 S12: -0.0138 S13: 0.0909 REMARK 3 S21: -0.0353 S22: 0.0695 S23: -0.0999 REMARK 3 S31: 0.0106 S32: 0.1331 S33: -0.0966 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.8747 35.1814 -0.4669 REMARK 3 T TENSOR REMARK 3 T11: 0.2920 T22: 0.1959 REMARK 3 T33: 0.1570 T12: 0.2657 REMARK 3 T13: 0.0469 T23: -0.1659 REMARK 3 L TENSOR REMARK 3 L11: 0.1212 L22: 0.0156 REMARK 3 L33: 0.0572 L12: 0.0392 REMARK 3 L13: 0.0677 L23: 0.0151 REMARK 3 S TENSOR REMARK 3 S11: -0.0352 S12: -0.0547 S13: 0.0617 REMARK 3 S21: 0.0138 S22: -0.0183 S23: 0.0564 REMARK 3 S31: 0.0094 S32: -0.0369 S33: 0.0645 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.7093 24.1074 -5.3176 REMARK 3 T TENSOR REMARK 3 T11: 0.1875 T22: 0.0017 REMARK 3 T33: 0.1290 T12: 0.0300 REMARK 3 T13: -0.0395 T23: -0.0686 REMARK 3 L TENSOR REMARK 3 L11: 0.0934 L22: 0.0283 REMARK 3 L33: 0.0281 L12: -0.0042 REMARK 3 L13: -0.0170 L23: -0.0208 REMARK 3 S TENSOR REMARK 3 S11: -0.0353 S12: -0.0011 S13: -0.0480 REMARK 3 S21: -0.0198 S22: -0.0343 S23: 0.0317 REMARK 3 S31: 0.0138 S32: -0.0043 S33: -0.3546 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.4486 24.8726 4.0827 REMARK 3 T TENSOR REMARK 3 T11: 0.2946 T22: 0.3414 REMARK 3 T33: 0.3232 T12: 0.2072 REMARK 3 T13: 0.0624 T23: 0.0045 REMARK 3 L TENSOR REMARK 3 L11: 0.2557 L22: 0.1933 REMARK 3 L33: 0.0809 L12: -0.0776 REMARK 3 L13: 0.1415 L23: -0.0569 REMARK 3 S TENSOR REMARK 3 S11: 0.0142 S12: -0.0254 S13: -0.1000 REMARK 3 S21: 0.0106 S22: 0.0346 S23: -0.0403 REMARK 3 S31: 0.0382 S32: 0.0915 S33: 0.0181 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 170 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.7420 24.7169 -6.4148 REMARK 3 T TENSOR REMARK 3 T11: 0.2337 T22: -0.0187 REMARK 3 T33: 0.1563 T12: -0.1671 REMARK 3 T13: 0.0657 T23: 0.0670 REMARK 3 L TENSOR REMARK 3 L11: 0.3269 L22: 0.1851 REMARK 3 L33: 0.0855 L12: -0.0210 REMARK 3 L13: 0.0038 L23: -0.1291 REMARK 3 S TENSOR REMARK 3 S11: 0.0168 S12: -0.1488 S13: -0.3024 REMARK 3 S21: 0.1007 S22: 0.0455 S23: 0.1443 REMARK 3 S31: 0.1077 S32: -0.0459 S33: 0.2299 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 11 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.1162 17.4528 -22.0073 REMARK 3 T TENSOR REMARK 3 T11: 0.1269 T22: 0.1234 REMARK 3 T33: 0.0646 T12: -0.0305 REMARK 3 T13: 0.0932 T23: -0.0214 REMARK 3 L TENSOR REMARK 3 L11: 0.0632 L22: 0.0327 REMARK 3 L33: 0.1480 L12: -0.0169 REMARK 3 L13: -0.0290 L23: -0.0308 REMARK 3 S TENSOR REMARK 3 S11: -0.0327 S12: 0.0219 S13: -0.0325 REMARK 3 S21: -0.0176 S22: -0.0179 S23: -0.0220 REMARK 3 S31: -0.0175 S32: 0.0733 S33: -0.2187 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0232 11.0340 -13.8153 REMARK 3 T TENSOR REMARK 3 T11: 0.2227 T22: 0.0564 REMARK 3 T33: 0.2018 T12: 0.0194 REMARK 3 T13: 0.0418 T23: 0.0852 REMARK 3 L TENSOR REMARK 3 L11: 0.1844 L22: 0.1103 REMARK 3 L33: 0.1784 L12: 0.1395 REMARK 3 L13: -0.0387 L23: 0.0127 REMARK 3 S TENSOR REMARK 3 S11: 0.0075 S12: 0.0250 S13: 0.2373 REMARK 3 S21: 0.1576 S22: -0.0452 S23: 0.1272 REMARK 3 S31: -0.1792 S32: 0.0092 S33: 0.3739 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 77 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4469 4.7367 -10.3097 REMARK 3 T TENSOR REMARK 3 T11: 0.1859 T22: -0.0078 REMARK 3 T33: -0.0306 T12: 0.2394 REMARK 3 T13: -0.0598 T23: 0.1739 REMARK 3 L TENSOR REMARK 3 L11: 0.1517 L22: 0.0323 REMARK 3 L33: 0.0125 L12: -0.0630 REMARK 3 L13: 0.0402 L23: -0.0171 REMARK 3 S TENSOR REMARK 3 S11: 0.0594 S12: -0.0369 S13: -0.0450 REMARK 3 S21: 0.0632 S22: 0.0165 S23: 0.0816 REMARK 3 S31: -0.0639 S32: 0.0056 S33: 0.4452 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.4564 16.6443 -9.9233 REMARK 3 T TENSOR REMARK 3 T11: 0.3432 T22: 0.2232 REMARK 3 T33: 0.0526 T12: 0.0642 REMARK 3 T13: -0.0498 T23: -0.2052 REMARK 3 L TENSOR REMARK 3 L11: 0.0597 L22: 0.0452 REMARK 3 L33: 0.1648 L12: 0.0139 REMARK 3 L13: -0.0102 L23: 0.0800 REMARK 3 S TENSOR REMARK 3 S11: 0.0561 S12: -0.0180 S13: -0.0160 REMARK 3 S21: 0.0231 S22: 0.0279 S23: -0.0279 REMARK 3 S31: -0.0260 S32: 0.0575 S33: 0.2920 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 88 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.7480 5.9210 -17.6125 REMARK 3 T TENSOR REMARK 3 T11: 0.2091 T22: 0.0372 REMARK 3 T33: 0.0708 T12: 0.1711 REMARK 3 T13: 0.0340 T23: -0.0476 REMARK 3 L TENSOR REMARK 3 L11: 0.0057 L22: 0.0039 REMARK 3 L33: 0.1469 L12: 0.0000 REMARK 3 L13: -0.0280 L23: -0.0046 REMARK 3 S TENSOR REMARK 3 S11: -0.0342 S12: -0.0355 S13: -0.0322 REMARK 3 S21: 0.0348 S22: 0.0347 S23: -0.0318 REMARK 3 S31: 0.0560 S32: 0.1186 S33: -0.0877 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.0154 6.0739 -18.0847 REMARK 3 T TENSOR REMARK 3 T11: 0.2271 T22: 0.2103 REMARK 3 T33: 0.2131 T12: 0.1450 REMARK 3 T13: -0.0042 T23: 0.1639 REMARK 3 L TENSOR REMARK 3 L11: 0.0510 L22: 0.1029 REMARK 3 L33: 0.0208 L12: -0.0045 REMARK 3 L13: 0.0090 L23: 0.0434 REMARK 3 S TENSOR REMARK 3 S11: 0.0385 S12: -0.0625 S13: -0.0919 REMARK 3 S21: 0.0981 S22: -0.0313 S23: -0.1347 REMARK 3 S31: 0.1268 S32: 0.1233 S33: -0.0554 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 9HQ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144011. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JUN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.984002 REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL 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 202440712 REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9778 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 47.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 10.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.9400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 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 : 4.880 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: TETRAGONAL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM SULFATE, 20.00 % W/V REMARK 280 POLYETHYLENE GLYCOL 3,350, PH 6.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K 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 69.32000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.61500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.61500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.98000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.61500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.61500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.66000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.61500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.61500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.98000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.61500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.61500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.66000 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 69.32000 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: A, 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 ARG A 102 REMARK 465 ASN A 202 REMARK 465 VAL A 203 REMARK 465 GLU A 204 REMARK 465 ASN A 205 REMARK 465 LEU A 206 REMARK 465 TYR A 207 REMARK 465 PHE A 208 REMARK 465 GLN A 209 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 SER B 3 REMARK 465 SER B 4 REMARK 465 GLY B 120 REMARK 465 ARG B 121 REMARK 465 ALA B 122 REMARK 465 GLY B 123 REMARK 465 GLU B 124 REMARK 465 GLN B 125 REMARK 465 LYS B 126 REMARK 465 LEU B 127 REMARK 465 ILE B 128 REMARK 465 SER B 129 REMARK 465 GLU B 130 REMARK 465 GLU B 131 REMARK 465 ASP B 132 REMARK 465 LEU B 133 REMARK 465 ASN B 134 REMARK 465 SER B 135 REMARK 465 ALA B 136 REMARK 465 VAL B 137 REMARK 465 ASP B 138 REMARK 465 HIS B 139 REMARK 465 HIS B 140 REMARK 465 HIS B 141 REMARK 465 HIS B 142 REMARK 465 HIS B 143 REMARK 465 HIS B 144 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 TYR A 105 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 108 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 110 CG CD CE NZ REMARK 470 ASN A 125 CG OD1 ND2 REMARK 470 LYS A 128 CG CD CE NZ REMARK 470 LYS A 156 CG CD CE NZ REMARK 470 SER A 159 OG REMARK 470 SER A 161 OG REMARK 470 LYS A 162 CG CD CE NZ REMARK 470 LYS A 184 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 LYS A 201 CG CD CE NZ REMARK 470 LYS B 47 CG CD CE NZ REMARK 470 SER B 75 OG REMARK 470 SER B 89 OG REMARK 470 LYS B 91 CG CD CE NZ REMARK 470 GLU B 93 CG CD OE1 OE2 REMARK 470 VAL B 102 CG1 CG2 REMARK 470 VAL B 104 CG1 CG2 REMARK 470 TRP B 106 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 106 CZ3 CH2 REMARK 470 VAL B 117 CG1 CG2 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 HIS B 58 -130.89 59.62 REMARK 500 TRP B 106 -168.56 -111.42 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HQ5 A 104 203 UNP P08962 CD63_HUMAN 104 203 DBREF 9HQ5 B 1 144 PDB 9HQ5 9HQ5 1 144 SEQADV 9HQ5 ARG A 102 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 SER A 103 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 SER A 130 UNP P08962 ASN 130 ENGINEERED MUTATION SEQADV 9HQ5 SER A 150 UNP P08962 ASN 150 ENGINEERED MUTATION SEQADV 9HQ5 SER A 172 UNP P08962 ASN 172 ENGINEERED MUTATION SEQADV 9HQ5 GLU A 204 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 ASN A 205 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 LEU A 206 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 TYR A 207 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 PHE A 208 UNP P08962 EXPRESSION TAG SEQADV 9HQ5 GLN A 209 UNP P08962 EXPRESSION TAG SEQRES 1 A 108 ARG SER GLY TYR VAL PHE ARG ASP LYS VAL MET SER GLU SEQRES 2 A 108 PHE ASN ASN ASN PHE ARG GLN GLN MET GLU ASN TYR PRO SEQRES 3 A 108 LYS ASN SER HIS THR ALA SER ILE LEU ASP ARG MET GLN SEQRES 4 A 108 ALA ASP PHE LYS CYS CYS GLY ALA ALA SER TYR THR ASP SEQRES 5 A 108 TRP GLU LYS ILE PRO SER MET SER LYS ASN ARG VAL PRO SEQRES 6 A 108 ASP SER CYS CYS ILE SER VAL THR VAL GLY CYS GLY ILE SEQRES 7 A 108 ASN PHE ASN GLU LYS ALA ILE HIS LYS GLU GLY CYS VAL SEQRES 8 A 108 GLU LYS ILE GLY GLY TRP LEU ARG LYS ASN VAL GLU ASN SEQRES 9 A 108 LEU TYR PHE GLN SEQRES 1 B 144 GLY SER SER SER GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 B 144 GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS SEQRES 3 B 144 ALA ALA SER GLY PHE PRO VAL ALA SER GLY ASN MET ALA SEQRES 4 B 144 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL SEQRES 5 B 144 ALA ALA ILE LYS SER HIS GLY TYR GLY THR LYS TYR ALA SEQRES 6 B 144 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 B 144 ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS SEQRES 8 B 144 PRO GLU ASP THR ALA VAL TYR TYR CYS TYR VAL TYR VAL SEQRES 9 B 144 GLY TRP LEU TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 10 B 144 SER ALA GLY ARG ALA GLY GLU GLN LYS LEU ILE SER GLU SEQRES 11 B 144 GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS SEQRES 12 B 144 HIS HET SO4 A 301 5 HET SO4 A 302 5 HET SO4 B 201 5 HETNAM SO4 SULFATE ION FORMUL 3 SO4 3(O4 S 2-) HELIX 1 AA1 ASP A 109 ASN A 125 1 17 HELIX 2 AA2 ASN A 129 PHE A 143 1 15 HELIX 3 AA3 SER A 150 ILE A 157 5 8 HELIX 4 AA4 PRO A 166 CYS A 170 5 5 HELIX 5 AA5 ASN A 182 ILE A 186 5 5 HELIX 6 AA6 CYS A 191 GLY A 197 1 7 HELIX 7 AA7 TRP A 198 ARG A 200 5 3 HELIX 8 AA8 PRO B 32 GLY B 36 5 5 HELIX 9 AA9 ASP B 66 LYS B 69 5 4 HELIX 10 AB1 LYS B 91 THR B 95 5 5 SHEET 1 AA1 4 GLN B 7 SER B 11 0 SHEET 2 AA1 4 LEU B 22 SER B 29 -1 O SER B 25 N SER B 11 SHEET 3 AA1 4 THR B 82 MET B 87 -1 O MET B 87 N LEU B 22 SHEET 4 AA1 4 PHE B 72 ASP B 77 -1 N THR B 73 O GLN B 86 SHEET 1 AA2 6 LEU B 15 VAL B 16 0 SHEET 2 AA2 6 THR B 113 VAL B 117 1 O THR B 116 N VAL B 16 SHEET 3 AA2 6 ALA B 96 TYR B 103 -1 N TYR B 98 O THR B 113 SHEET 4 AA2 6 ASN B 37 GLN B 43 -1 N TYR B 41 O TYR B 99 SHEET 5 AA2 6 GLU B 50 ILE B 55 -1 O ILE B 55 N MET B 38 SHEET 6 AA2 6 THR B 62 TYR B 64 -1 O LYS B 63 N ALA B 54 SHEET 1 AA3 4 LEU B 15 VAL B 16 0 SHEET 2 AA3 4 THR B 113 VAL B 117 1 O THR B 116 N VAL B 16 SHEET 3 AA3 4 ALA B 96 TYR B 103 -1 N TYR B 98 O THR B 113 SHEET 4 AA3 4 LEU B 107 TRP B 109 -1 O TYR B 108 N VAL B 102 SSBOND 1 CYS A 145 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 146 CYS A 169 1555 1555 2.03 SSBOND 3 CYS A 170 CYS A 177 1555 1555 2.03 SSBOND 4 CYS B 26 CYS B 100 1555 1555 2.03 CRYST1 65.230 65.230 138.640 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 0.015330 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015330 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007213 0.00000