HEADER CELL ADHESION 23-DEC-24 9HUR TITLE CRYSTAL STRUCTURE OF TETRASPANIN CD63MUTANT LARGE EXTRACELLULAR LOOP TITLE 2 (LEL) IN COMPLEX WITH SYBODY LA4 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 MOL_ID: 2; COMPND 10 MOLECULE: SYBODY LA4; COMPND 11 CHAIN: B; COMPND 12 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 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 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 9HUR 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. 1.65 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) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 30367 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1519 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 44.7500 - 3.6700 1.00 2895 153 0.1804 0.2029 REMARK 3 2 3.6700 - 2.9100 1.00 2687 141 0.2095 0.2289 REMARK 3 3 2.9100 - 2.5400 1.00 2643 139 0.2330 0.2620 REMARK 3 4 2.5400 - 2.3100 1.00 2618 138 0.2248 0.2766 REMARK 3 5 2.3100 - 2.1500 1.00 2610 137 0.2221 0.2583 REMARK 3 6 2.1500 - 2.0200 1.00 2588 137 0.2442 0.2624 REMARK 3 7 2.0200 - 1.9200 1.00 2572 135 0.2225 0.2472 REMARK 3 8 1.9200 - 1.8400 1.00 2560 135 0.2222 0.2746 REMARK 3 9 1.8300 - 1.7600 1.00 2564 135 0.2890 0.3187 REMARK 3 10 1.7600 - 1.7000 1.00 2546 134 0.3953 0.4247 REMARK 3 11 1.7000 - 1.6500 1.00 2565 135 0.5689 0.6900 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) : 0.317 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.831 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.65 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.26 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 : 0.013 1728 REMARK 3 ANGLE : 1.243 2348 REMARK 3 CHIRALITY : 0.078 259 REMARK 3 PLANARITY : 0.011 304 REMARK 3 DIHEDRAL : 14.482 589 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0024 -11.9369 38.7543 REMARK 3 T TENSOR REMARK 3 T11: 0.5499 T22: 0.3827 REMARK 3 T33: 0.4834 T12: -0.1080 REMARK 3 T13: -0.0579 T23: 0.1038 REMARK 3 L TENSOR REMARK 3 L11: 4.1782 L22: 1.4014 REMARK 3 L33: 2.9173 L12: 0.3813 REMARK 3 L13: 2.4483 L23: 0.0272 REMARK 3 S TENSOR REMARK 3 S11: 0.4216 S12: -0.1508 S13: -0.5866 REMARK 3 S21: 0.3036 S22: -0.1082 S23: 0.1550 REMARK 3 S31: 0.7589 S32: -0.4145 S33: 0.0148 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.8009 -6.2726 41.6570 REMARK 3 T TENSOR REMARK 3 T11: 0.5414 T22: 0.3379 REMARK 3 T33: 0.4011 T12: -0.0115 REMARK 3 T13: -0.0343 T23: 0.0764 REMARK 3 L TENSOR REMARK 3 L11: 2.3165 L22: 3.4010 REMARK 3 L33: 1.8916 L12: 0.7744 REMARK 3 L13: -1.5609 L23: 1.1107 REMARK 3 S TENSOR REMARK 3 S11: 0.3435 S12: -0.5198 S13: -0.2670 REMARK 3 S21: 0.5500 S22: -0.1090 S23: -0.0148 REMARK 3 S31: 0.3377 S32: -0.2759 S33: 0.0722 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.3170 -9.1389 10.8793 REMARK 3 T TENSOR REMARK 3 T11: 0.3069 T22: 0.3603 REMARK 3 T33: 0.3280 T12: -0.0180 REMARK 3 T13: -0.0591 T23: -0.0241 REMARK 3 L TENSOR REMARK 3 L11: 1.6691 L22: 2.3383 REMARK 3 L33: 1.2545 L12: 0.8124 REMARK 3 L13: -0.4616 L23: 1.2543 REMARK 3 S TENSOR REMARK 3 S11: -0.1474 S12: 0.3362 S13: -0.0493 REMARK 3 S21: 0.0478 S22: 0.3104 S23: -0.1511 REMARK 3 S31: -0.0773 S32: 0.2658 S33: 0.0029 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 56 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.4000 -2.9654 18.2897 REMARK 3 T TENSOR REMARK 3 T11: 0.4821 T22: 0.3122 REMARK 3 T33: 0.3650 T12: -0.0423 REMARK 3 T13: -0.0806 T23: -0.0017 REMARK 3 L TENSOR REMARK 3 L11: 2.1463 L22: 0.9400 REMARK 3 L33: 3.1732 L12: -1.4226 REMARK 3 L13: -0.0980 L23: 0.1303 REMARK 3 S TENSOR REMARK 3 S11: 0.0850 S12: -0.3675 S13: 0.2542 REMARK 3 S21: 0.4825 S22: -0.1565 S23: -0.3635 REMARK 3 S31: -0.6293 S32: 0.1987 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4891 -6.6908 11.6893 REMARK 3 T TENSOR REMARK 3 T11: 0.3152 T22: 0.2950 REMARK 3 T33: 0.3448 T12: 0.0028 REMARK 3 T13: -0.0798 T23: 0.0199 REMARK 3 L TENSOR REMARK 3 L11: 3.7663 L22: 3.0312 REMARK 3 L33: 4.0791 L12: 0.6846 REMARK 3 L13: 0.8947 L23: -0.9447 REMARK 3 S TENSOR REMARK 3 S11: 0.0046 S12: 0.1561 S13: -0.0985 REMARK 3 S21: 0.0323 S22: 0.1929 S23: 0.2399 REMARK 3 S31: 0.0002 S32: -0.0627 S33: -0.0006 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 104 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.1980 -5.8697 20.7917 REMARK 3 T TENSOR REMARK 3 T11: 0.3639 T22: 0.2587 REMARK 3 T33: 0.3239 T12: 0.0042 REMARK 3 T13: -0.0324 T23: 0.0109 REMARK 3 L TENSOR REMARK 3 L11: 1.0124 L22: 0.5317 REMARK 3 L33: 1.9665 L12: 0.5284 REMARK 3 L13: 0.6095 L23: 0.9420 REMARK 3 S TENSOR REMARK 3 S11: -0.0445 S12: -0.0939 S13: 0.1566 REMARK 3 S21: 0.2937 S22: 0.1038 S23: -0.1981 REMARK 3 S31: -0.1313 S32: 0.1617 S33: -0.0003 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 9HUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144269. 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 20240712 REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30367 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 44.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4 REMARK 200 DATA REDUNDANCY : 15.30 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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 : 1.420 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 (%): 40.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM FORMATE;0.2M AMMONIUM REMARK 280 ACETATE; 0.2M SODIUM CITRATE TRIBASIC DIHYDRATE; 0.2M POTASSIUM REMARK 280 SODIUM TARTRATE TETRAHYDRATE: 0.2M SODIUM OXAMATE; 25% V/V MPD; REMARK 280 25% PEG 1000; 25% W/V PEG 3350, PH 6.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 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 114.22000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 22.81500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 22.81500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.11000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 22.81500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 22.81500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 171.33000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 22.81500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 22.81500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.11000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 22.81500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 22.81500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 171.33000 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 114.22000 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 SER A 103 REMARK 465 GLY A 104 REMARK 465 TYR A 105 REMARK 465 VAL A 106 REMARK 465 PHE A 107 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 GLY B 130 REMARK 465 ARG B 131 REMARK 465 ALA B 132 REMARK 465 GLY B 133 REMARK 465 GLU B 134 REMARK 465 GLN B 135 REMARK 465 LYS B 136 REMARK 465 LEU B 137 REMARK 465 ILE B 138 REMARK 465 SER B 139 REMARK 465 GLU B 140 REMARK 465 GLU B 141 REMARK 465 ASP B 142 REMARK 465 LEU B 143 REMARK 465 ASN B 144 REMARK 465 SER B 145 REMARK 465 ALA B 146 REMARK 465 VAL B 147 REMARK 465 ASP B 148 REMARK 465 HIS B 149 REMARK 465 HIS B 150 REMARK 465 HIS B 151 REMARK 465 HIS B 152 REMARK 465 HIS B 153 REMARK 465 HIS B 154 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 ARG A 108 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 110 CG CD CE NZ REMARK 470 VAL A 111 CG1 CG2 REMARK 470 SER A 150 OG REMARK 470 GLU A 155 CG CD OE1 OE2 REMARK 470 LYS A 156 CG CD CE NZ REMARK 470 SER A 159 OG REMARK 470 LYS A 162 CG CD CE NZ REMARK 470 ASN A 163 CG OD1 ND2 REMARK 470 GLU A 183 CG CD OE1 OE2 REMARK 470 LYS A 184 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 GLU A 193 CG CD OE1 OE2 REMARK 470 GLU A 204 CG CD OE1 OE2 REMARK 470 ASN A 205 CG OD1 ND2 REMARK 470 TYR A 207 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE A 208 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 3 OG REMARK 470 SER B 4 OG REMARK 470 GLN B 5 CG CD OE1 NE2 REMARK 470 GLU B 48 CG CD OE1 OE2 REMARK 470 LYS B 108 CG CD CE NZ REMARK 470 GLN B 121 CG CD OE1 NE2 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 ALA A 148 -65.65 -93.03 REMARK 500 SER A 159 -14.85 65.12 REMARK 500 TYR A 207 -13.75 -143.01 REMARK 500 ALA B 96 164.81 179.20 REMARK 500 LYS B 108 68.22 -111.43 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HUR A 104 203 UNP P08962 CD63_HUMAN 104 203 DBREF 9HUR B 1 154 PDB 9HUR 9HUR 1 154 SEQADV 9HUR ARG A 102 UNP P08962 EXPRESSION TAG SEQADV 9HUR SER A 103 UNP P08962 EXPRESSION TAG SEQADV 9HUR SER A 130 UNP P08962 ASN 130 ENGINEERED MUTATION SEQADV 9HUR SER A 150 UNP P08962 ASN 150 ENGINEERED MUTATION SEQADV 9HUR SER A 172 UNP P08962 ASN 172 ENGINEERED MUTATION SEQADV 9HUR GLU A 204 UNP P08962 EXPRESSION TAG SEQADV 9HUR ASN A 205 UNP P08962 EXPRESSION TAG SEQADV 9HUR LEU A 206 UNP P08962 EXPRESSION TAG SEQADV 9HUR TYR A 207 UNP P08962 EXPRESSION TAG SEQADV 9HUR PHE A 208 UNP P08962 EXPRESSION TAG SEQADV 9HUR 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 154 GLY SER SER SER GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 B 154 GLY SER VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS SEQRES 3 B 154 ALA ALA SER GLY SER ILE SER SER ILE THR TYR LEU GLY SEQRES 4 B 154 TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 B 154 ALA ALA LEU MET THR THR ASP GLY SER THR TYR TYR ALA SEQRES 6 B 154 ASN SER VAL LYS GLY ARG PHE THR VAL SER LEU ASP ASN SEQRES 7 B 154 ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS SEQRES 8 B 154 PRO GLU ASP THR ALA LEU TYR TYR CYS ALA ALA ALA GLU SEQRES 9 B 154 ASN GLY PHE LYS ILE PRO LEU TRP GLU TYR ILE TYR THR SEQRES 10 B 154 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER ALA GLY SEQRES 11 B 154 ARG ALA GLY GLU GLN LYS LEU ILE SER GLU GLU ASP LEU SEQRES 12 B 154 ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS HET SO4 A 301 5 HET NA B 201 1 HETNAM SO4 SULFATE ION HETNAM NA SODIUM ION FORMUL 3 SO4 O4 S 2- FORMUL 4 NA NA 1+ FORMUL 5 HOH *78(H2 O) HELIX 1 AA1 ARG A 108 TYR A 126 1 19 HELIX 2 AA2 ASN A 129 LYS A 144 1 16 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 GLY A 190 ASN A 202 1 13 HELIX 7 AA7 VAL A 203 LEU A 206 5 4 HELIX 8 AA8 ASN B 78 LYS B 80 5 3 HELIX 9 AA9 LYS B 91 THR B 95 5 5 HELIX 10 AB1 TRP B 112 TYR B 116 5 5 SHEET 1 AA1 4 VAL B 6 SER B 11 0 SHEET 2 AA1 4 LEU B 22 GLY B 30 -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 ASP B 77 O THR B 82 SHEET 1 AA2 6 GLY B 14 GLN B 17 0 SHEET 2 AA2 6 THR B 123 SER B 128 1 O THR B 126 N GLY B 14 SHEET 3 AA2 6 ALA B 96 GLU B 104 -1 N TYR B 98 O THR B 123 SHEET 4 AA2 6 ILE B 35 GLN B 43 -1 N THR B 36 O ALA B 103 SHEET 5 AA2 6 GLU B 50 MET B 56 -1 O ALA B 53 N TRP B 40 SHEET 6 AA2 6 THR B 62 TYR B 64 -1 O TYR B 63 N ALA B 54 SHEET 1 AA3 4 GLY B 14 GLN B 17 0 SHEET 2 AA3 4 THR B 123 SER B 128 1 O THR B 126 N GLY B 14 SHEET 3 AA3 4 ALA B 96 GLU B 104 -1 N TYR B 98 O THR B 123 SHEET 4 AA3 4 TYR B 118 TRP B 119 -1 O TYR B 118 N ALA B 102 SSBOND 1 CYS A 145 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 146 CYS A 169 1555 1555 2.02 SSBOND 3 CYS A 170 CYS A 177 1555 1555 2.05 SSBOND 4 CYS B 26 CYS B 100 1555 1555 1.98 LINK O ILE B 115 NA NA B 201 1555 1555 2.85 CRYST1 45.630 45.630 228.440 90.00 90.00 90.00 P 41 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 0.021915 0.000000 0.000000 0.00000 SCALE2 0.000000 0.021915 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004378 0.00000