HEADER ANTITOXIN 14-NOV-23 8R4N TITLE CRYSTAL STRUCTURE OF NEUTRALIZING FAB EQ4.DP46-3A FROM EQUINE TITLE 2 ANTIVENOM BOUND TO SHORT CHAIN THREE FINGER ALPHA-NEUROTOXIN FROM TITLE 3 DENDROASPIS POLYLEPIS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: EQ4.DP46-3A HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: EQ4.DP46-3A LAMBDA CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SHORT NEUROTOXIN 1; COMPND 11 CHAIN: N; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 3 ORGANISM_TAXID: 9796; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: B CELL; SOURCE 6 GENE: IGHV; SOURCE 7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 14 ORGANISM_TAXID: 9796; SOURCE 15 TISSUE: BLOOD; SOURCE 16 CELL: B CELL; SOURCE 17 GENE: IGHV; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4; SOURCE 23 MOL_ID: 3; SOURCE 24 ORGANISM_SCIENTIFIC: DENDROASPIS POLYLEPIS; SOURCE 25 ORGANISM_TAXID: 8624; SOURCE 26 TISSUE: VENOM; SOURCE 27 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 29 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4 KEYWDS MONOCLONAL ANTIBODY, ANTIVENOM, COMPLEX, SHORT CHAIN ALPHA- KEYWDS 2 NEUROTOXIN, ANTITOXIN EXPDTA X-RAY DIFFRACTION AUTHOR C.K.WIBMER REVDAT 1 28-MAY-25 8R4N 0 JRNL AUTH C.K.WIBMER JRNL TITL A MONOCLONAL ANTIBODY FROM HORSES THAT NEUTRALIZES LONG AND JRNL TITL 2 SHORT CHAIN THREE FINGER NEUROTOXINS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.20 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 30760 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) : 0.206 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 2836 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 50.0000 - 5.9700 0.99 2776 148 0.2183 0.2220 REMARK 3 2 5.9600 - 4.7400 1.00 2777 142 0.1734 0.1809 REMARK 3 3 4.7400 - 4.1400 1.00 2785 140 0.1657 0.2075 REMARK 3 4 4.1400 - 3.7600 1.00 2772 149 0.1867 0.1697 REMARK 3 5 3.7600 - 3.4900 1.00 2789 140 0.1855 0.2098 REMARK 3 6 3.4900 - 3.2800 1.00 2738 138 0.2065 0.2689 REMARK 3 7 3.2800 - 3.1200 1.00 2792 148 0.2305 0.2933 REMARK 3 8 3.1200 - 2.9800 0.99 2731 148 0.2332 0.2568 REMARK 3 9 2.9800 - 2.8700 0.99 2771 146 0.2174 0.2450 REMARK 3 10 2.8700 - 2.7700 0.99 2740 147 0.2226 0.2795 REMARK 3 11 2.7700 - 2.6800 0.98 2702 140 0.2331 0.2948 REMARK 3 12 2.6800 - 2.6100 0.98 2742 143 0.2181 0.2543 REMARK 3 13 2.6100 - 2.5400 0.98 2732 139 0.2480 0.2738 REMARK 3 14 2.5400 - 2.4800 0.97 2681 141 0.2234 0.2356 REMARK 3 15 2.4800 - 2.4200 0.96 2686 143 0.2213 0.2556 REMARK 3 16 2.4200 - 2.3700 0.97 2659 140 0.2294 0.2482 REMARK 3 17 2.3700 - 2.3200 0.95 2618 143 0.2313 0.2668 REMARK 3 18 2.3200 - 2.2800 0.94 2612 135 0.2374 0.2342 REMARK 3 19 2.2800 - 2.2400 0.92 2564 138 0.2524 0.2550 REMARK 3 20 2.2400 - 2.2000 0.88 2436 128 0.2760 0.3424 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) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.56 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 NULL REMARK 3 ANGLE : 0.599 NULL REMARK 3 CHIRALITY : 0.046 573 REMARK 3 PLANARITY : 0.004 633 REMARK 3 DIHEDRAL : 5.073 518 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN H AND RESID 1:126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.386 -38.365 -39.827 REMARK 3 T TENSOR REMARK 3 T11: 0.3524 T22: 0.7236 REMARK 3 T33: 0.5933 T12: 0.1150 REMARK 3 T13: 0.0071 T23: -0.0169 REMARK 3 L TENSOR REMARK 3 L11: 2.9240 L22: 2.4157 REMARK 3 L33: 3.7541 L12: -0.5199 REMARK 3 L13: -1.0298 L23: 0.8384 REMARK 3 S TENSOR REMARK 3 S11: -0.2111 S12: -0.5731 S13: -0.0160 REMARK 3 S21: 0.1625 S22: 0.0261 S23: 0.4924 REMARK 3 S31: -0.0817 S32: -0.4023 S33: -0.0005 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN H AND RESID 127:211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.660 -27.231 -13.908 REMARK 3 T TENSOR REMARK 3 T11: 0.9875 T22: 1.2359 REMARK 3 T33: 0.8712 T12: 0.1934 REMARK 3 T13: 0.0398 T23: -0.1009 REMARK 3 L TENSOR REMARK 3 L11: 4.3426 L22: 2.0642 REMARK 3 L33: 3.0310 L12: -1.5618 REMARK 3 L13: -0.5385 L23: 0.5319 REMARK 3 S TENSOR REMARK 3 S11: -0.0607 S12: -0.6928 S13: 2.2011 REMARK 3 S21: 0.0529 S22: -0.0538 S23: 0.1445 REMARK 3 S31: -0.9789 S32: 0.0987 S33: -0.0355 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.784 -47.698 -42.451 REMARK 3 T TENSOR REMARK 3 T11: 0.3347 T22: 0.4208 REMARK 3 T33: 0.3380 T12: 0.0597 REMARK 3 T13: 0.0319 T23: 0.0626 REMARK 3 L TENSOR REMARK 3 L11: 3.2510 L22: 2.2447 REMARK 3 L33: 2.4652 L12: -0.8767 REMARK 3 L13: 0.4978 L23: 0.3970 REMARK 3 S TENSOR REMARK 3 S11: -0.1555 S12: -0.5203 S13: -0.2814 REMARK 3 S21: 0.2387 S22: 0.1961 S23: 0.1221 REMARK 3 S31: 0.1387 S32: 0.0491 S33: 0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN L AND RESID 114:210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.345 -39.235 -8.506 REMARK 3 T TENSOR REMARK 3 T11: 1.2863 T22: 1.7667 REMARK 3 T33: 0.5131 T12: 0.3618 REMARK 3 T13: -0.0756 T23: 0.1289 REMARK 3 L TENSOR REMARK 3 L11: 1.5735 L22: 2.4717 REMARK 3 L33: 2.6416 L12: 1.8761 REMARK 3 L13: 0.5596 L23: 1.1990 REMARK 3 S TENSOR REMARK 3 S11: -0.2122 S12: -1.9270 S13: -1.1917 REMARK 3 S21: 0.7774 S22: 0.1649 S23: -0.2379 REMARK 3 S31: 1.7158 S32: 0.2644 S33: -0.0902 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN N AND RESID 1:60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.446 -58.683 -66.085 REMARK 3 T TENSOR REMARK 3 T11: 0.7817 T22: 0.6677 REMARK 3 T33: 0.9394 T12: -0.1095 REMARK 3 T13: -0.1035 T23: -0.1348 REMARK 3 L TENSOR REMARK 3 L11: 1.6044 L22: 0.9720 REMARK 3 L33: 1.3878 L12: -0.1110 REMARK 3 L13: -1.3509 L23: 0.4154 REMARK 3 S TENSOR REMARK 3 S11: -0.2499 S12: 0.7104 S13: -0.8690 REMARK 3 S21: -0.8512 S22: -0.0499 S23: 0.2977 REMARK 3 S31: 0.4357 S32: -0.5662 S33: -0.0011 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 8R4N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-23. REMARK 100 THE DEPOSITION ID IS D_1292131778. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5-9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2.MULTIPLEX REMARK 200 DATA SCALING SOFTWARE : XIA2.MULTIPLEX REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30760 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 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 (%) : 98.7 REMARK 200 DATA REDUNDANCY : 20.00 REMARK 200 R MERGE (I) : 0.10520 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 30.8700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.08000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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 (%): 53.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SPG BUFFER (PH9.0), 50% PEG1500, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 52.31150 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 108.21350 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 52.31150 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 108.21350 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 52.31150 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 108.21350 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 52.31150 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 108.21350 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 52.31150 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 108.21350 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 52.31150 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 108.21350 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 52.31150 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 108.21350 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 52.31150 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 52.31150 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 108.21350 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 APPLY THE FOLLOWING TO CHAINS: H, L, N 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 L 318 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 376 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 382 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 389 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 408 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 409 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 SER H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 VAL H 212 REMARK 465 ILE H 213 REMARK 465 LYS H 214 REMARK 465 GLU H 215 REMARK 465 CYS H 216 REMARK 465 GLY H 217 REMARK 465 LEU H 218 REMARK 465 GLU H 219 REMARK 465 VAL H 220 REMARK 465 LEU H 221 REMARK 465 PHE H 222 REMARK 465 GLN H 223 REMARK 465 ALA L 153 REMARK 465 VAL L 154 REMARK 465 THR L 155 REMARK 465 ASN L 156 REMARK 465 ASP L 157 REMARK 465 ARG L 158 REMARK 465 VAL L 159 REMARK 465 CYS L 211 REMARK 465 PRO L 212 REMARK 465 LEU N 61 REMARK 465 GLU N 62 REMARK 465 VAL N 63 REMARK 465 LEU N 64 REMARK 465 PHE N 65 REMARK 465 GLN N 66 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 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 120 CG CD CE NZ REMARK 470 HIS H 127 CG ND1 CD2 CE1 NE2 REMARK 470 LEU H 189 CG CD1 CD2 REMARK 470 LYS H 190 CG CD CE NZ REMARK 470 GLN H 192 CG CD OE1 NE2 REMARK 470 ILE H 195 CG1 CG2 CD1 REMARK 470 LYS H 206 CG CD CE NZ REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 210 CG CD CE NZ REMARK 470 GLN L 1 CG CD OE1 NE2 REMARK 470 LEU L 125 CG CD1 CD2 REMARK 470 ASN L 128 CG OD1 ND2 REMARK 470 LYS L 129 CG CD CE NZ REMARK 470 GLU L 145 CG CD OE1 OE2 REMARK 470 ILE L 147 CG1 CG2 CD1 REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 ASN L 151 CG OD1 ND2 REMARK 470 LEU L 178 CG CD1 CD2 REMARK 470 GLU L 184 CG CD OE1 OE2 REMARK 470 VAL L 191 CG1 CG2 REMARK 470 GLN L 194 CG CD OE1 NE2 REMARK 470 LYS L 200 CG CD CE NZ REMARK 470 GLU L 203 CG CD OE1 OE2 REMARK 470 LYS L 205 CG CD CE NZ REMARK 470 SER L 209 OG REMARK 470 ARG N 11 CG CD NE CZ NH1 NH2 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 15 -16.93 76.03 REMARK 500 PHE H 146 134.29 -176.05 REMARK 500 SER H 191 -50.26 -130.13 REMARK 500 ASN L 27B -87.32 -128.39 REMARK 500 ALA L 84 -179.85 175.98 REMARK 500 PRO L 141 -179.00 -63.77 REMARK 500 SER L 190 113.19 -169.75 REMARK 500 SER L 209 -169.56 -75.96 REMARK 500 SER N 8 -120.85 42.22 REMARK 500 ASN N 59 55.33 -119.86 REMARK 500 REMARK 500 REMARK: NULL DBREF 8R4N H 1 223 PDB 8R4N 8R4N 1 223 DBREF 8R4N L 1 212 PDB 8R4N 8R4N 1 212 DBREF 8R4N N 1 60 UNP P01416 3S11_DENPO 1 60 SEQADV 8R4N GLY N 60A UNP P01416 EXPRESSION TAG SEQADV 8R4N LEU N 61 UNP P01416 EXPRESSION TAG SEQADV 8R4N GLU N 62 UNP P01416 EXPRESSION TAG SEQADV 8R4N VAL N 63 UNP P01416 EXPRESSION TAG SEQADV 8R4N LEU N 64 UNP P01416 EXPRESSION TAG SEQADV 8R4N PHE N 65 UNP P01416 EXPRESSION TAG SEQADV 8R4N GLN N 66 UNP P01416 EXPRESSION TAG SEQRES 1 H 236 GLN VAL GLN LEU THR GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 236 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 236 LEU SER LEU SER ARG ASN THR ALA GLY TRP VAL ARG GLN SEQRES 4 H 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ASP ILE SER SEQRES 5 H 236 GLY ASP GLY ILE PRO GLY GLY GLU SER GLU TYR TYR ASN SEQRES 6 H 236 PRO VAL LEU LYS PRO ARG VAL SER ILE THR LYS ASP THR SEQRES 7 H 236 SER LYS SER GLN LEU TYR LEU THR LEU ASN SER LEU THR SEQRES 8 H 236 SER GLU ASP THR ALA VAL TYR TYR CYS THR GLY SER GLY SEQRES 9 H 236 ASP THR TYR TYR TRP ARG ASP GLY ASP ARG TYR TRP GLY SEQRES 10 H 236 GLN GLY ILE LEU VAL THR VAL SER SER ALA SER THR THR SEQRES 11 H 236 ALA PRO LYS VAL PHE PRO LEU ALA SER HIS SER ALA ALA SEQRES 12 H 236 THR SER GLY SER THR VAL ALA LEU GLY CYS LEU VAL SER SEQRES 13 H 236 SER TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 236 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SER VAL SEQRES 15 H 236 LEU GLN SER SER GLY LEU TYR SER LEU SER SER MET VAL SEQRES 16 H 236 THR VAL PRO ALA SER SER LEU LYS SER GLN THR TYR ILE SEQRES 17 H 236 CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP SEQRES 18 H 236 LYS LYS ILE VAL ILE LYS GLU CYS GLY LEU GLU VAL LEU SEQRES 19 H 236 PHE GLN SEQRES 1 L 217 GLN SER VAL THR GLN PRO ALA SER VAL SER GLY THR LEU SEQRES 2 L 217 GLY GLN THR VAL THR ILE SER CYS SER GLY SER LYS SER SEQRES 3 L 217 ASN ILE GLY ASP THR PRO THR TYR VAL GLY TRP PHE GLN SEQRES 4 L 217 GLN ILE PRO GLY THR ALA PRO LYS THR LEU ILE TYR GLY SEQRES 5 L 217 ASP ASN ARG ARG ALA SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER VAL SER GLY ASN THR ALA THR LEU THR ILE SER SEQRES 7 L 217 GLY VAL GLN ALA GLU ASP GLU ALA VAL TYR TRP CYS GLY SEQRES 8 L 217 SER TRP ASP VAL ASN SER ASP SER GLU LEU PHE GLY GLY SEQRES 9 L 217 GLY THR HIS LEU THR ILE ALA GLY GLY PRO THR SER ALA SEQRES 10 L 217 PRO SER VAL SER LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 SER ALA ASN LYS ALA THR VAL VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE SER PRO SER GLY LEU GLU VAL ILE TRP LYS VAL ASN SEQRES 13 L 217 ASP ALA VAL THR ASN ASP ARG VAL GLN THR THR ARG PRO SEQRES 14 L 217 SER LYS GLN SER ASN GLY LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU THR ARG THR SER THR GLU TRP LYS SER TYR SER SER SEQRES 16 L 217 VAL SER CYS GLN VAL LYS HIS GLN GLY LYS THR VAL GLU SEQRES 17 L 217 LYS LYS VAL SER PRO SER GLU CYS PRO SEQRES 1 N 67 ARG ILE CYS TYR ASN HIS GLN SER THR THR ARG ALA THR SEQRES 2 N 67 THR LYS SER CYS GLU GLU ASN SER CYS TYR LYS LYS TYR SEQRES 3 N 67 TRP ARG ASP HIS ARG GLY THR ILE ILE GLU ARG GLY CYS SEQRES 4 N 67 GLY CYS PRO LYS VAL LYS PRO GLY VAL GLY ILE HIS CYS SEQRES 5 N 67 CYS GLN SER ASP LYS CYS ASN TYR GLY LEU GLU VAL LEU SEQRES 6 N 67 PHE GLN FORMUL 4 HOH *201(H2 O) HELIX 1 AA1 THR H 83 THR H 87 5 5 HELIX 2 AA2 SER H 187 SER H 191 5 5 HELIX 3 AA3 PRO H 201 SER H 204 5 4 HELIX 4 AA4 GLN L 79 GLU L 83 5 5 HELIX 5 AA5 SER L 121 ALA L 127 1 7 HELIX 6 AA6 THR L 181 SER L 187 1 7 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 ILE H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 SER H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 AA2 6 ALA H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 GLU H 57 TYR H 59 -1 O TYR H 58 N ASP H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 ILE H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 SER H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 AA3 4 ARG H 101 TRP H 103 -1 O TYR H 102 N GLY H 94 SHEET 1 AA4 4 LYS H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N VAL H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O MET H 181 SHEET 1 AA5 4 LYS H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N VAL H 136 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA7 6 SER L 9 THR L 14 0 SHEET 2 AA7 6 THR L 102 ALA L 107 1 O HIS L 103 N VAL L 11 SHEET 3 AA7 6 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA7 6 VAL L 33 GLN L 38 -1 N GLY L 34 O GLY L 89 SHEET 5 AA7 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA7 6 ARG L 53 ARG L 54 -1 O ARG L 53 N TYR L 49 SHEET 1 AA8 4 SER L 9 THR L 14 0 SHEET 2 AA8 4 THR L 102 ALA L 107 1 O HIS L 103 N VAL L 11 SHEET 3 AA8 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 4 SER L 95B PHE L 98 -1 O SER L 95B N ASP L 92 SHEET 1 AA9 3 THR L 18 SER L 24 0 SHEET 2 AA9 3 THR L 70 SER L 76 -1 O ALA L 71 N CYS L 23 SHEET 3 AA9 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AB1 4 TYR L 172 ARG L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB1 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AB2 3 GLU L 145 LYS L 149 0 SHEET 2 AB2 3 VAL L 191 HIS L 197 -1 O LYS L 196 N GLU L 145 SHEET 3 AB2 3 LYS L 200 VAL L 206 -1 O LYS L 204 N CYS L 193 SHEET 1 AB3 2 ILE N 2 TYR N 4 0 SHEET 2 AB3 2 THR N 14 SER N 16 -1 O LYS N 15 N CYS N 3 SHEET 1 AB4 3 THR N 33 CYS N 39 0 SHEET 2 AB4 3 CYS N 22 ARG N 28 -1 N LYS N 25 O GLU N 36 SHEET 3 AB4 3 GLY N 49 CYS N 53 -1 O GLY N 49 N TYR N 26 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 193 1555 1555 2.03 SSBOND 5 CYS N 3 CYS N 22 1555 1555 2.03 SSBOND 6 CYS N 17 CYS N 39 1555 1555 2.03 SSBOND 7 CYS N 41 CYS N 52 1555 1555 2.03 SSBOND 8 CYS N 53 CYS N 58 1555 1555 2.03 CISPEP 1 PHE H 146 PRO H 147 0 -1.00 CISPEP 2 THR L 29 PRO L 30 0 1.73 CISPEP 3 SER L 140 PRO L 141 0 0.77 CRYST1 104.623 104.623 216.427 90.00 90.00 90.00 I 4 2 2 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 0.009558 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009558 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004620 0.00000