HEADER ANTITOXIN 28-FEB-24 8S72 TITLE CRYSTAL STRUCTURE OF NEUTRALIZING FAB EQ4.DP46-3D FROM EQUINE TITLE 2 ANTIVENOM BOUND TO A CONSENSUS SHORT CHAIN THREE FINGER ALPHA- TITLE 3 NEUROTOXIN. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SHORT NEUROTOXIN 1; COMPND 3 CHAIN: N, A; COMPND 4 SYNONYM: NEUROTOXIN ALPHA,TOXIN ALPHA; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: N-TERMINAL GPGG LINKER SEQUENCE FROM TAG REMOVAL.; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HEAVY CHAIN OF FAB DOMAIN FROM ANTIVENOM NEUTRALIZING COMPND 9 ANTIBODY EQ4.DP46-3D.; COMPND 10 CHAIN: X, H; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: C-TERMINAL GLEVLFQ SEQUENCE REMNANT FROM HRV3C COMPND 13 CLEAVAGE.; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: LIGHT CHAIN OF FAB DOMAIN FROM ANTIVENOM NEUTRALIZING COMPND 16 ANTIBODY EQ4.DP46-3D.; COMPND 17 CHAIN: Y, L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 11 ORGANISM_TAXID: 9796; SOURCE 12 ORGAN: BLOOD; SOURCE 13 TISSUE: PBMC; SOURCE 14 CELL: MEMORY B CELL; SOURCE 15 GENE: IGHV4; SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 23 ORGANISM_TAXID: 9796; SOURCE 24 ORGAN: BLOOD; SOURCE 25 TISSUE: PBMC; SOURCE 26 CELL: MEMORY B CELL; SOURCE 27 GENE: IGLV; SOURCE 28 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 32 EXPRESSION_SYSTEM_PLASMID: PCDNA3.4 KEYWDS MONOCLONAL ANTIBODY, ANTIVENOM, COMPLEX, SHORT CHAIN ALPHA- KEYWDS 2 NEUROTOXIN, ANTITOXIN EXPDTA X-RAY DIFFRACTION AUTHOR F.AYRES,C.K.WIBMER REVDAT 1 10-SEP-25 8S72 0 JRNL AUTH F.AYRES,R.PATEL,N.CASEWELL,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. 2.78 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) : 2.78 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 63529 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.130 REMARK 3 FREE R VALUE TEST SET COUNT : 1986 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 20.6000 - 6.6300 1.00 4723 132 0.2326 0.2365 REMARK 3 2 6.6300 - 5.2900 1.00 4536 138 0.2415 0.2656 REMARK 3 3 5.2900 - 4.6300 1.00 4488 141 0.1943 0.2147 REMARK 3 4 4.6300 - 4.2100 1.00 4438 143 0.1800 0.2157 REMARK 3 5 4.2100 - 3.9100 1.00 4418 148 0.1999 0.2155 REMARK 3 6 3.9100 - 3.6800 1.00 4397 152 0.2095 0.2222 REMARK 3 7 3.6800 - 3.5000 1.00 4399 144 0.2198 0.2740 REMARK 3 8 3.5000 - 3.3500 1.00 4378 150 0.2299 0.2478 REMARK 3 9 3.3500 - 3.2200 1.00 4393 136 0.2464 0.2848 REMARK 3 10 3.2200 - 3.1100 1.00 4321 176 0.2691 0.2808 REMARK 3 11 3.1100 - 3.0100 1.00 4360 141 0.2765 0.2904 REMARK 3 12 3.0100 - 2.9300 1.00 4403 132 0.2924 0.3148 REMARK 3 13 2.9300 - 2.8500 1.00 4329 139 0.3138 0.3599 REMARK 3 14 2.8500 - 2.7800 0.91 3960 114 0.3209 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.120 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 59.12 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 : 0.004 NULL REMARK 3 ANGLE : 0.947 NULL REMARK 3 CHIRALITY : 0.096 1191 REMARK 3 PLANARITY : 0.005 1310 REMARK 3 DIHEDRAL : 6.150 1077 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN N AND RESID -3:60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -63.793 -62.563 -2.621 REMARK 3 T TENSOR REMARK 3 T11: 0.5372 T22: 0.5311 REMARK 3 T33: 0.5215 T12: 0.0411 REMARK 3 T13: -0.0076 T23: 0.0544 REMARK 3 L TENSOR REMARK 3 L11: 3.4785 L22: 1.3732 REMARK 3 L33: 3.0684 L12: 0.1401 REMARK 3 L13: -1.1848 L23: 0.7598 REMARK 3 S TENSOR REMARK 3 S11: -0.0472 S12: 0.1032 S13: -0.1846 REMARK 3 S21: -0.1100 S22: 0.0798 S23: -0.0181 REMARK 3 S31: 0.1448 S32: -0.2021 S33: 0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID -3:60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.964 -62.718 16.630 REMARK 3 T TENSOR REMARK 3 T11: 0.6948 T22: 0.5376 REMARK 3 T33: 0.5735 T12: 0.0460 REMARK 3 T13: -0.0258 T23: 0.1054 REMARK 3 L TENSOR REMARK 3 L11: 3.2245 L22: 3.5970 REMARK 3 L33: 3.3600 L12: -1.4515 REMARK 3 L13: 1.7416 L23: 0.2608 REMARK 3 S TENSOR REMARK 3 S11: 0.1296 S12: -0.3095 S13: -0.4202 REMARK 3 S21: 0.7490 S22: -0.1757 S23: -0.5559 REMARK 3 S31: 0.2843 S32: 0.1714 S33: 0.0023 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN X AND RESID 2:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -85.515 -84.190 12.453 REMARK 3 T TENSOR REMARK 3 T11: 0.9128 T22: 0.4391 REMARK 3 T33: 0.7930 T12: -0.1092 REMARK 3 T13: 0.1577 T23: 0.0432 REMARK 3 L TENSOR REMARK 3 L11: 3.6499 L22: 2.8394 REMARK 3 L33: 3.2837 L12: 1.5877 REMARK 3 L13: -1.3507 L23: -0.7443 REMARK 3 S TENSOR REMARK 3 S11: -0.1580 S12: -0.1987 S13: -0.0872 REMARK 3 S21: 0.2903 S22: -0.0209 S23: 0.3232 REMARK 3 S31: 0.7513 S32: -0.0938 S33: 0.0008 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN X AND RESID 124:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -105.271 -107.691 5.254 REMARK 3 T TENSOR REMARK 3 T11: 1.0934 T22: 0.6861 REMARK 3 T33: 1.1740 T12: -0.2539 REMARK 3 T13: -0.0481 T23: -0.0072 REMARK 3 L TENSOR REMARK 3 L11: 1.8792 L22: 1.8963 REMARK 3 L33: 1.8782 L12: 1.8912 REMARK 3 L13: -1.4894 L23: -1.3861 REMARK 3 S TENSOR REMARK 3 S11: 0.0833 S12: 0.3600 S13: 0.1616 REMARK 3 S21: -0.4199 S22: 0.3122 S23: 0.0758 REMARK 3 S31: 0.1559 S32: -0.3411 S33: -0.0014 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN Y AND RESID 2:112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -83.840 -83.240 -8.543 REMARK 3 T TENSOR REMARK 3 T11: 0.9817 T22: 0.6817 REMARK 3 T33: 0.7401 T12: -0.1814 REMARK 3 T13: 0.0281 T23: -0.0265 REMARK 3 L TENSOR REMARK 3 L11: 2.0137 L22: 2.3375 REMARK 3 L33: 2.0001 L12: 0.9906 REMARK 3 L13: 0.0353 L23: 0.4470 REMARK 3 S TENSOR REMARK 3 S11: -0.3980 S12: 0.7930 S13: -0.0209 REMARK 3 S21: -0.8105 S22: 0.1767 S23: 0.2092 REMARK 3 S31: 0.6269 S32: -0.1239 S33: -0.0004 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN Y AND RESID 113:208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -114.713 -103.490 -6.985 REMARK 3 T TENSOR REMARK 3 T11: 1.2423 T22: 1.0533 REMARK 3 T33: 1.4012 T12: -0.3448 REMARK 3 T13: -0.1445 T23: 0.2789 REMARK 3 L TENSOR REMARK 3 L11: 1.2285 L22: 2.2987 REMARK 3 L33: 1.0592 L12: 0.8856 REMARK 3 L13: 0.5886 L23: 1.2741 REMARK 3 S TENSOR REMARK 3 S11: -0.0334 S12: 0.9894 S13: -0.1060 REMARK 3 S21: -0.6030 S22: 0.2702 S23: 0.8066 REMARK 3 S31: -0.3028 S32: -0.7114 S33: 0.0004 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN H AND RESID 2:123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.507 -32.422 2.373 REMARK 3 T TENSOR REMARK 3 T11: 0.5682 T22: 0.4286 REMARK 3 T33: 0.4362 T12: -0.0021 REMARK 3 T13: -0.0138 T23: 0.0627 REMARK 3 L TENSOR REMARK 3 L11: 2.1674 L22: 4.3617 REMARK 3 L33: 2.6808 L12: -1.9662 REMARK 3 L13: 0.8993 L23: -0.9011 REMARK 3 S TENSOR REMARK 3 S11: -0.0506 S12: 0.0394 S13: -0.0525 REMARK 3 S21: -0.2239 S22: -0.0635 S23: 0.0428 REMARK 3 S31: -0.2391 S32: 0.1441 S33: 0.0001 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN H AND RESID 124:216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -74.647 -1.044 11.862 REMARK 3 T TENSOR REMARK 3 T11: 0.6314 T22: 0.4072 REMARK 3 T33: 0.4078 T12: 0.0322 REMARK 3 T13: 0.0133 T23: 0.0337 REMARK 3 L TENSOR REMARK 3 L11: 4.4254 L22: 3.7430 REMARK 3 L33: 4.7028 L12: 0.0037 REMARK 3 L13: 0.3653 L23: 0.9301 REMARK 3 S TENSOR REMARK 3 S11: 0.0154 S12: -0.2760 S13: 0.3367 REMARK 3 S21: 0.2630 S22: 0.1384 S23: -0.2036 REMARK 3 S31: -0.1279 S32: 0.2507 S33: -0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN L AND RESID 2:112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -68.635 -34.689 23.209 REMARK 3 T TENSOR REMARK 3 T11: 0.5555 T22: 0.5057 REMARK 3 T33: 0.4729 T12: 0.0392 REMARK 3 T13: -0.0061 T23: 0.0690 REMARK 3 L TENSOR REMARK 3 L11: 1.4199 L22: 2.2250 REMARK 3 L33: 4.0507 L12: -0.0758 REMARK 3 L13: 0.2780 L23: 1.4575 REMARK 3 S TENSOR REMARK 3 S11: -0.0868 S12: -0.2820 S13: -0.0554 REMARK 3 S21: 0.2263 S22: 0.0330 S23: 0.0451 REMARK 3 S31: -0.2432 S32: -0.0410 S33: 0.0001 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN L AND RESID 113:211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -85.109 -0.733 23.275 REMARK 3 T TENSOR REMARK 3 T11: 0.7370 T22: 0.3805 REMARK 3 T33: 0.4615 T12: -0.0990 REMARK 3 T13: 0.0398 T23: -0.0055 REMARK 3 L TENSOR REMARK 3 L11: 4.9500 L22: 4.7004 REMARK 3 L33: 3.9641 L12: -2.4466 REMARK 3 L13: 0.7207 L23: 0.1448 REMARK 3 S TENSOR REMARK 3 S11: -0.0437 S12: -0.0581 S13: -0.1582 REMARK 3 S21: 0.1999 S22: -0.0302 S23: 0.3240 REMARK 3 S31: 0.3607 S32: -0.1347 S33: -0.0005 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 8S72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292136932. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-DEC-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7-9 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6199 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X CDTE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64005 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780 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 (%) : 99.7 REMARK 200 DATA REDUNDANCY : 78.50 REMARK 200 R MERGE (I) : 0.54100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 54.9 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 : 0.900 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HCL (PH 8,0) 60% MPD REMARK 280 CRYOPROTECTED WITH 10% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+1/3 REMARK 290 6555 X-Y,X,Z+2/3 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+1/3 REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.17500 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.35000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.17500 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.35000 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.17500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 66.35000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 33.17500 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 66.35000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 11970 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 41820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, A, X, Y, 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 346 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 365 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 HIS X 127 REMARK 465 SER X 128 REMARK 465 ALA X 129 REMARK 465 ALA X 130 REMARK 465 THR X 131 REMARK 465 LYS X 214 REMARK 465 GLU X 215 REMARK 465 CYS X 216 REMARK 465 GLY X 217 REMARK 465 LEU X 218 REMARK 465 GLU X 219 REMARK 465 VAL X 220 REMARK 465 LEU X 221 REMARK 465 PHE X 222 REMARK 465 GLN X 223 REMARK 465 SER Y 209 REMARK 465 GLU Y 210 REMARK 465 CYS Y 211 REMARK 465 PRO Y 212 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 PRO L 212 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 N 28 CG CD NE CZ NH1 NH2 REMARK 470 LYS X 13 CG CD CE NZ REMARK 470 LYS X 120 CG CD CE NZ REMARK 470 SER X 132 OG REMARK 470 LYS X 190 CG CD CE NZ REMARK 470 LYS Y 45 CG CD CE NZ REMARK 470 ASN Y 128 CG OD1 ND2 REMARK 470 LYS Y 129 CG CD CE NZ REMARK 470 GLU Y 145 CG CD OE1 OE2 REMARK 470 ILE Y 147 CG1 CG2 CD1 REMARK 470 LYS Y 149 CG CD CE NZ REMARK 470 VAL Y 150 CG1 CG2 REMARK 470 ASN Y 151 CG OD1 ND2 REMARK 470 VAL Y 154 CG1 CG2 REMARK 470 THR Y 155 OG1 CG2 REMARK 470 ASN Y 156 CG OD1 ND2 REMARK 470 ASP Y 157 CG OD1 OD2 REMARK 470 ARG Y 158 CG CD NE CZ NH1 NH2 REMARK 470 VAL Y 159 CG1 CG2 REMARK 470 ARG Y 163 CG CD NE CZ NH1 NH2 REMARK 470 LYS Y 166 CG CD CE NZ REMARK 470 LYS Y 171 CG CD CE NZ REMARK 470 LEU Y 178 CG CD1 CD2 REMARK 470 ARG Y 180 CG CD NE CZ NH1 NH2 REMARK 470 GLU Y 184 CG CD OE1 OE2 REMARK 470 LYS Y 186 CG CD CE NZ REMARK 470 SER Y 190 OG REMARK 470 VAL Y 191 CG1 CG2 REMARK 470 GLN Y 194 CG CD OE1 NE2 REMARK 470 LYS Y 196 CG CD CE NZ REMARK 470 GLN Y 198 CG CD OE1 NE2 REMARK 470 LYS Y 200 CG CD CE NZ REMARK 470 GLU Y 203 CG CD OE1 OE2 REMARK 470 LYS Y 205 CG CD CE NZ REMARK 470 LEU Y 206 CG CD1 CD2 REMARK 470 LYS H 190 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ 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 N 8 -123.34 56.41 REMARK 500 ASN N 59 42.24 -91.71 REMARK 500 SER A 8 -122.25 55.21 REMARK 500 ASN A 59 42.75 -90.97 REMARK 500 GLN X 16 -160.26 -117.80 REMARK 500 LEU X 29 32.64 -98.20 REMARK 500 VAL X 98 -63.90 -125.68 REMARK 500 SER X 144 68.02 61.71 REMARK 500 PRO X 147 -166.80 -73.53 REMARK 500 SER X 188 39.41 -97.31 REMARK 500 ASN Y 27B -88.64 -122.26 REMARK 500 GLU Y 68 -119.93 53.07 REMARK 500 ALA Y 84 177.03 179.66 REMARK 500 ASP Y 95A 58.48 39.86 REMARK 500 ASN Y 151 -118.51 60.04 REMARK 500 GLN H 16 -164.82 -118.47 REMARK 500 LEU H 29 34.86 -96.34 REMARK 500 ILE H 48 -60.29 -91.77 REMARK 500 VAL H 98 -63.82 -124.66 REMARK 500 SER H 144 69.23 60.74 REMARK 500 PRO H 147 -168.62 -73.15 REMARK 500 ASN L 27B -88.09 -122.44 REMARK 500 GLU L 68 -120.11 53.87 REMARK 500 ASP L 95A 57.69 38.83 REMARK 500 ASN L 151 -120.58 59.12 REMARK 500 GLU L 210 51.72 -104.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8R4N RELATED DB: PDB REMARK 900 SOMATICALLY RELATED ANTIBODY BOUND TO SIMILAR TOXIN DBREF 8S72 N 1 60 UNP P01426 3S11_NAJPA 1 61 DBREF 8S72 A 1 60 UNP P01426 3S11_NAJPA 1 61 DBREF 8S72 X 1 223 PDB 8S72 8S72 1 223 DBREF 8S72 Y 1 212 PDB 8S72 8S72 1 212 DBREF 8S72 H 1 223 PDB 8S72 8S72 1 223 DBREF 8S72 L 1 212 PDB 8S72 8S72 1 212 SEQADV 8S72 GLY N -3 UNP P01426 EXPRESSION TAG SEQADV 8S72 PRO N -2 UNP P01426 EXPRESSION TAG SEQADV 8S72 GLY N -1 UNP P01426 LINKER SEQADV 8S72 GLY N 0 UNP P01426 LINKER SEQADV 8S72 MET N 1 UNP P01426 LEU 1 CONFLICT SEQADV 8S72 ILE N 2 UNP P01426 GLU 2 CONFLICT SEQADV 8S72 TYR N 4 UNP P01426 HIS 4 ENGINEERED MUTATION SEQADV 8S72 N UNP P01426 PRO 18 DELETION SEQADV 8S72 SER N 18 UNP P01426 GLY 19 ENGINEERED MUTATION SEQADV 8S72 SER N 21 UNP P01426 ASN 22 ENGINEERED MUTATION SEQADV 8S72 THR N 26 UNP P01426 VAL 27 ENGINEERED MUTATION SEQADV 8S72 LYS N 43 UNP P01426 THR 44 ENGINEERED MUTATION SEQADV 8S72 HIS N 51 UNP P01426 ASN 52 ENGINEERED MUTATION SEQADV 8S72 ARG N 54 UNP P01426 THR 55 ENGINEERED MUTATION SEQADV 8S72 GLY A -3 UNP P01426 EXPRESSION TAG SEQADV 8S72 PRO A -2 UNP P01426 EXPRESSION TAG SEQADV 8S72 GLY A -1 UNP P01426 LINKER SEQADV 8S72 GLY A 0 UNP P01426 LINKER SEQADV 8S72 MET A 1 UNP P01426 LEU 1 CONFLICT SEQADV 8S72 ILE A 2 UNP P01426 GLU 2 CONFLICT SEQADV 8S72 TYR A 4 UNP P01426 HIS 4 ENGINEERED MUTATION SEQADV 8S72 A UNP P01426 PRO 18 DELETION SEQADV 8S72 SER A 18 UNP P01426 GLY 19 ENGINEERED MUTATION SEQADV 8S72 SER A 21 UNP P01426 ASN 22 ENGINEERED MUTATION SEQADV 8S72 THR A 26 UNP P01426 VAL 27 ENGINEERED MUTATION SEQADV 8S72 LYS A 43 UNP P01426 THR 44 ENGINEERED MUTATION SEQADV 8S72 HIS A 51 UNP P01426 ASN 52 ENGINEERED MUTATION SEQADV 8S72 ARG A 54 UNP P01426 THR 55 ENGINEERED MUTATION SEQRES 1 N 64 GLY PRO GLY GLY MET ILE CYS TYR ASN GLN GLN SER SER SEQRES 2 N 64 GLN PRO PRO THR THR LYS THR CYS SER GLU THR SER CYS SEQRES 3 N 64 TYR LYS LYS THR TRP ARG ASP HIS ARG GLY THR ILE ILE SEQRES 4 N 64 GLU ARG GLY CYS GLY CYS PRO LYS VAL LYS PRO GLY ILE SEQRES 5 N 64 LYS LEU HIS CYS CYS ARG THR ASP LYS CYS ASN ASN SEQRES 1 A 64 GLY PRO GLY GLY MET ILE CYS TYR ASN GLN GLN SER SER SEQRES 2 A 64 GLN PRO PRO THR THR LYS THR CYS SER GLU THR SER CYS SEQRES 3 A 64 TYR LYS LYS THR TRP ARG ASP HIS ARG GLY THR ILE ILE SEQRES 4 A 64 GLU ARG GLY CYS GLY CYS PRO LYS VAL LYS PRO GLY ILE SEQRES 5 A 64 LYS LEU HIS CYS CYS ARG THR ASP LYS CYS ASN ASN SEQRES 1 X 233 PCA VAL GLN LEU THR GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 X 233 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 X 233 LEU SER LEU THR ASN ASN VAL ALA GLY SER GLY TRP VAL SEQRES 4 X 233 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY ASP SEQRES 5 X 233 ILE SER GLY ASP GLY VAL THR TYR TYR ASN PRO ALA LEU SEQRES 6 X 233 LYS PRO ARG VAL SER ILE THR LYS ASP THR SER LYS SER SEQRES 7 X 233 GLN VAL TYR LEU ALA LEU ASN ARG LEU THR GLY GLU ASP SEQRES 8 X 233 THR ALA VAL TYR TYR CYS VAL GLY ASN ALA ASP VAL TYR SEQRES 9 X 233 TYR TRP ARG ASP GLY GLU LYS TYR TRP GLY GLN GLY ILE SEQRES 10 X 233 LEU VAL THR VAL SER SER ALA SER THR THR ALA PRO LYS SEQRES 11 X 233 VAL PHE PRO LEU ALA SER HIS SER ALA ALA THR SER GLY SEQRES 12 X 233 SER THR VAL ALA LEU GLY CYS LEU VAL SER SER TYR PHE SEQRES 13 X 233 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 X 233 THR SER GLY VAL HIS THR PHE PRO SER VAL LEU GLN SER SEQRES 15 X 233 SER GLY LEU TYR SER LEU SER SER MET VAL THR VAL PRO SEQRES 16 X 233 ALA SER SER LEU LYS SER GLN THR TYR ILE CYS ASN VAL SEQRES 17 X 233 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 X 233 VAL ILE LYS GLU CYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 Y 217 PCA SER VAL THR GLN PRO ALA SER VAL SER GLY THR LEU SEQRES 2 Y 217 GLY GLN THR VAL THR ILE SER CYS SER GLY SER LYS SER SEQRES 3 Y 217 ASN ILE GLY ASP THR PRO SER TYR VAL GLY TRP PHE GLN SEQRES 4 Y 217 GLN ILE PRO GLY THR ALA PRO LYS THR LEU ILE TYR GLY SEQRES 5 Y 217 ASP GLY LYS ARG ALA SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 Y 217 GLY SER VAL SER GLU ASN THR ALA THR LEU THR ILE SER SEQRES 7 Y 217 GLY VAL GLN ALA GLU ASP GLU ALA ASP TYR TRP CYS ALA SEQRES 8 Y 217 SER TRP ASP VAL ASN SER ASP SER GLU VAL PHE GLY GLY SEQRES 9 Y 217 GLY THR HIS LEU THR VAL ALA GLY GLY PRO THR SER ALA SEQRES 10 Y 217 PRO SER VAL SER LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 Y 217 SER ALA ASN LYS ALA THR VAL VAL CYS LEU ILE SER ASP SEQRES 12 Y 217 PHE SER PRO SER GLY LEU GLU VAL ILE TRP LYS VAL ASN SEQRES 13 Y 217 ASP ALA VAL THR ASN ASP ARG VAL GLN THR THR ARG PRO SEQRES 14 Y 217 SER LYS GLN SER ASN GLY LYS TYR ALA ALA SER SER TYR SEQRES 15 Y 217 LEU THR ARG THR SER THR GLU TRP LYS SER TYR SER SER SEQRES 16 Y 217 VAL SER CYS GLN VAL LYS HIS GLN GLY LYS THR VAL GLU SEQRES 17 Y 217 LYS LYS LEU SER PRO SER GLU CYS PRO SEQRES 1 H 233 PCA VAL GLN LEU THR GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 233 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 233 LEU SER LEU THR ASN ASN VAL ALA GLY SER GLY TRP VAL SEQRES 4 H 233 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY ASP SEQRES 5 H 233 ILE SER GLY ASP GLY VAL THR TYR TYR ASN PRO ALA LEU SEQRES 6 H 233 LYS PRO ARG VAL SER ILE THR LYS ASP THR SER LYS SER SEQRES 7 H 233 GLN VAL TYR LEU ALA LEU ASN ARG LEU THR GLY GLU ASP SEQRES 8 H 233 THR ALA VAL TYR TYR CYS VAL GLY ASN ALA ASP VAL TYR SEQRES 9 H 233 TYR TRP ARG ASP GLY GLU LYS TYR TRP GLY GLN GLY ILE SEQRES 10 H 233 LEU VAL THR VAL SER SER ALA SER THR THR ALA PRO LYS SEQRES 11 H 233 VAL PHE PRO LEU ALA SER HIS SER ALA ALA THR SER GLY SEQRES 12 H 233 SER THR VAL ALA LEU GLY CYS LEU VAL SER SER TYR PHE SEQRES 13 H 233 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 233 THR SER GLY VAL HIS THR PHE PRO SER VAL LEU GLN SER SEQRES 15 H 233 SER GLY LEU TYR SER LEU SER SER MET VAL THR VAL PRO SEQRES 16 H 233 ALA SER SER LEU LYS SER GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 233 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 H 233 VAL ILE LYS GLU CYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 217 PCA 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 SER 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 GLY LYS ARG ALA SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER VAL SER GLU ASN THR ALA THR LEU THR ILE SER SEQRES 7 L 217 GLY VAL GLN ALA GLU ASP GLU ALA ASP TYR TRP CYS ALA SEQRES 8 L 217 SER TRP ASP VAL ASN SER ASP SER GLU VAL PHE GLY GLY SEQRES 9 L 217 GLY THR HIS LEU THR VAL 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 LEU SER PRO SER GLU CYS PRO HET PCA X 1 14 HET PCA Y 1 14 HET PCA H 1 14 HET PCA L 1 14 HETNAM PCA PYROGLUTAMIC ACID FORMUL 3 PCA 4(C5 H7 N O3) FORMUL 7 HOH *204(H2 O) HELIX 1 AA1 LEU X 63 PRO X 65 5 3 HELIX 2 AA2 THR X 83 THR X 87 5 5 HELIX 3 AA3 SER X 156 ALA X 158 5 3 HELIX 4 AA4 SER X 187 LEU X 189 5 3 HELIX 5 AA5 GLN Y 79 GLU Y 83 5 5 HELIX 6 AA6 SER Y 121 SER Y 126 1 6 HELIX 7 AA7 THR Y 181 TYR Y 188 1 8 HELIX 8 AA8 PRO H 61 PRO H 65 5 5 HELIX 9 AA9 THR H 83 THR H 87 5 5 HELIX 10 AB1 SER H 126 ALA H 130 5 5 HELIX 11 AB2 SER H 156 ALA H 158 5 3 HELIX 12 AB3 SER H 187 SER H 191 5 5 HELIX 13 AB4 GLN L 79 GLU L 83 5 5 HELIX 14 AB5 SER L 121 SER L 126 1 6 HELIX 15 AB6 THR L 181 TYR L 188 1 8 SHEET 1 AA1 2 MET N 1 TYR N 4 0 SHEET 2 AA1 2 THR N 14 CYS N 17 -1 O LYS N 15 N CYS N 3 SHEET 1 AA2 6 GLY N 32 CYS N 39 0 SHEET 2 AA2 6 CYS N 22 ASP N 29 -1 N TRP N 27 O ILE N 34 SHEET 3 AA2 6 LYS N 49 CYS N 53 -1 O LYS N 49 N THR N 26 SHEET 4 AA2 6 LYS A 49 CYS A 53 -1 O CYS A 52 N LEU N 50 SHEET 5 AA2 6 CYS A 22 ASP A 29 -1 N THR A 26 O LYS A 49 SHEET 6 AA2 6 GLY A 32 CYS A 39 -1 O GLU A 36 N LYS A 25 SHEET 1 AA3 2 MET A 1 TYR A 4 0 SHEET 2 AA3 2 THR A 14 CYS A 17 -1 O LYS A 15 N CYS A 3 SHEET 1 AA4 4 GLN X 3 SER X 7 0 SHEET 2 AA4 4 LEU X 18 SER X 25 -1 O THR X 21 N SER X 7 SHEET 3 AA4 4 GLN X 77 LEU X 82 -1 O LEU X 80 N LEU X 20 SHEET 4 AA4 4 VAL X 67 ASP X 72 -1 N ASP X 72 O GLN X 77 SHEET 1 AA5 6 LEU X 11 VAL X 12 0 SHEET 2 AA5 6 ILE X 107 VAL X 111 1 O THR X 110 N VAL X 12 SHEET 3 AA5 6 ALA X 88 ALA X 96 -1 N ALA X 88 O VAL X 109 SHEET 4 AA5 6 GLY X 35 GLN X 39 -1 N GLY X 35 O ASN X 95 SHEET 5 AA5 6 LEU X 45 SER X 52 -1 O GLU X 46 N ARG X 38 SHEET 6 AA5 6 THR X 57 TYR X 59 -1 O TYR X 58 N ASP X 50 SHEET 1 AA6 4 LEU X 11 VAL X 12 0 SHEET 2 AA6 4 ILE X 107 VAL X 111 1 O THR X 110 N VAL X 12 SHEET 3 AA6 4 ALA X 88 ALA X 96 -1 N ALA X 88 O VAL X 109 SHEET 4 AA6 4 GLU X 100E TRP X 103 -1 O TYR X 102 N GLY X 94 SHEET 1 AA7 4 LYS X 120 LEU X 124 0 SHEET 2 AA7 4 THR X 135 TYR X 145 -1 O LEU X 141 N PHE X 122 SHEET 3 AA7 4 TYR X 176 PRO X 185 -1 O TYR X 176 N TYR X 145 SHEET 4 AA7 4 VAL X 163 THR X 165 -1 N HIS X 164 O MET X 181 SHEET 1 AA8 4 LYS X 120 LEU X 124 0 SHEET 2 AA8 4 THR X 135 TYR X 145 -1 O LEU X 141 N PHE X 122 SHEET 3 AA8 4 TYR X 176 PRO X 185 -1 O TYR X 176 N TYR X 145 SHEET 4 AA8 4 VAL X 169 LEU X 170 -1 N VAL X 169 O SER X 177 SHEET 1 AA9 3 THR X 151 TRP X 154 0 SHEET 2 AA9 3 ILE X 195 HIS X 200 -1 O ALA X 199 N THR X 151 SHEET 3 AA9 3 THR X 205 LYS X 210 -1 O THR X 205 N HIS X 200 SHEET 1 AB1 6 SER Y 9 THR Y 14 0 SHEET 2 AB1 6 THR Y 102 ALA Y 106A 1 O HIS Y 103 N VAL Y 11 SHEET 3 AB1 6 ALA Y 84 ASP Y 92 -1 N ALA Y 84 O LEU Y 104 SHEET 4 AB1 6 VAL Y 33 GLN Y 38 -1 N GLN Y 38 O ASP Y 85 SHEET 5 AB1 6 LYS Y 45 TYR Y 49 -1 O LYS Y 45 N GLN Y 37 SHEET 6 AB1 6 LYS Y 53 ARG Y 54 -1 O LYS Y 53 N TYR Y 49 SHEET 1 AB2 4 SER Y 9 THR Y 14 0 SHEET 2 AB2 4 THR Y 102 ALA Y 106A 1 O HIS Y 103 N VAL Y 11 SHEET 3 AB2 4 ALA Y 84 ASP Y 92 -1 N ALA Y 84 O LEU Y 104 SHEET 4 AB2 4 SER Y 95B PHE Y 98 -1 O SER Y 95B N ASP Y 92 SHEET 1 AB3 3 THR Y 18 SER Y 24 0 SHEET 2 AB3 3 THR Y 70 SER Y 76 -1 O ALA Y 71 N CYS Y 23 SHEET 3 AB3 3 PHE Y 62 SER Y 67 -1 N SER Y 67 O THR Y 70 SHEET 1 AB4 4 SER Y 114 PHE Y 118 0 SHEET 2 AB4 4 ALA Y 130 PHE Y 139 -1 O VAL Y 133 N PHE Y 118 SHEET 3 AB4 4 TYR Y 172 ARG Y 180 -1 O ALA Y 174 N ILE Y 136 SHEET 4 AB4 4 VAL Y 159 THR Y 161 -1 N GLN Y 160 O TYR Y 177 SHEET 1 AB5 4 SER Y 114 PHE Y 118 0 SHEET 2 AB5 4 ALA Y 130 PHE Y 139 -1 O VAL Y 133 N PHE Y 118 SHEET 3 AB5 4 TYR Y 172 ARG Y 180 -1 O ALA Y 174 N ILE Y 136 SHEET 4 AB5 4 SER Y 165 LYS Y 166 -1 N SER Y 165 O ALA Y 173 SHEET 1 AB6 4 ALA Y 153 VAL Y 154 0 SHEET 2 AB6 4 GLU Y 145 VAL Y 150 -1 N VAL Y 150 O ALA Y 153 SHEET 3 AB6 4 VAL Y 191 HIS Y 197 -1 O GLN Y 194 N ILE Y 147 SHEET 4 AB6 4 LYS Y 200 LEU Y 206 -1 O LYS Y 204 N CYS Y 193 SHEET 1 AB7 4 GLN H 3 SER H 7 0 SHEET 2 AB7 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AB7 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AB7 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AB8 6 LEU H 11 VAL H 12 0 SHEET 2 AB8 6 ILE H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB8 6 ALA H 88 ALA H 96 -1 N TYR H 90 O ILE H 107 SHEET 4 AB8 6 GLY H 35 GLN H 39 -1 N GLY H 35 O ASN H 95 SHEET 5 AB8 6 LEU H 45 SER H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AB8 6 THR H 57 TYR H 59 -1 O TYR H 58 N ASP H 50 SHEET 1 AB9 4 LEU H 11 VAL H 12 0 SHEET 2 AB9 4 ILE H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB9 4 ALA H 88 ALA H 96 -1 N TYR H 90 O ILE H 107 SHEET 4 AB9 4 GLU H 100E TRP H 103 -1 O TYR H 102 N GLY H 94 SHEET 1 AC1 4 LYS H 120 LEU H 124 0 SHEET 2 AC1 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AC1 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AC1 4 VAL H 163 THR H 165 -1 N HIS H 164 O MET H 181 SHEET 1 AC2 4 LYS H 120 LEU H 124 0 SHEET 2 AC2 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AC2 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AC2 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AC3 3 THR H 151 TRP H 154 0 SHEET 2 AC3 3 ILE H 195 HIS H 200 -1 O ALA H 199 N THR H 151 SHEET 3 AC3 3 THR H 205 LYS H 210 -1 O LYS H 209 N CYS H 196 SHEET 1 AC4 6 SER L 9 THR L 14 0 SHEET 2 AC4 6 THR L 102 ALA L 106A 1 O ALA L 106A N GLY L 13 SHEET 3 AC4 6 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AC4 6 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AC4 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC4 6 LYS L 53 ARG L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 AC5 4 SER L 9 THR L 14 0 SHEET 2 AC5 4 THR L 102 ALA L 106A 1 O ALA L 106A N GLY L 13 SHEET 3 AC5 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AC5 4 SER L 95B PHE L 98 -1 O SER L 95B N ASP L 92 SHEET 1 AC6 3 VAL L 19 SER L 24 0 SHEET 2 AC6 3 THR L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AC6 3 PHE L 62 SER L 67 -1 N SER L 67 O THR L 70 SHEET 1 AC7 4 SER L 114 PHE L 118 0 SHEET 2 AC7 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AC7 4 TYR L 172 ARG L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AC7 4 VAL L 159 THR L 161 -1 N GLN L 160 O TYR L 177 SHEET 1 AC8 4 SER L 114 PHE L 118 0 SHEET 2 AC8 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AC8 4 TYR L 172 ARG L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AC8 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AC9 4 ALA L 153 THR L 155 0 SHEET 2 AC9 4 GLU L 145 VAL L 150 -1 N TRP L 148 O THR L 155 SHEET 3 AC9 4 VAL L 191 HIS L 197 -1 O GLN L 194 N ILE L 147 SHEET 4 AC9 4 LYS L 200 LEU L 206 -1 O LYS L 204 N CYS L 193 SSBOND 1 CYS N 3 CYS N 22 1555 1555 2.00 SSBOND 2 CYS N 17 CYS N 39 1555 1555 2.03 SSBOND 3 CYS N 41 CYS N 52 1555 1555 2.03 SSBOND 4 CYS N 53 CYS N 58 1555 1555 2.03 SSBOND 5 CYS A 3 CYS A 22 1555 1555 2.00 SSBOND 6 CYS A 17 CYS A 39 1555 1555 2.02 SSBOND 7 CYS A 41 CYS A 52 1555 1555 2.04 SSBOND 8 CYS A 53 CYS A 58 1555 1555 2.03 SSBOND 9 CYS X 22 CYS X 92 1555 1555 2.03 SSBOND 10 CYS X 140 CYS X 196 1555 1555 2.04 SSBOND 11 CYS Y 23 CYS Y 88 1555 1555 2.03 SSBOND 12 CYS Y 134 CYS Y 193 1555 1555 2.03 SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 14 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 15 CYS H 216 CYS L 211 1555 1555 2.03 SSBOND 16 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 17 CYS L 134 CYS L 193 1555 1555 2.03 LINK C PCA X 1 N VAL X 2 1555 1555 1.33 LINK C PCA Y 1 N SER Y 2 1555 1555 1.33 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA L 1 N SER L 2 1555 1555 1.33 CISPEP 1 PHE X 146 PRO X 147 0 1.64 CISPEP 2 THR Y 29 PRO Y 30 0 -3.38 CISPEP 3 SER Y 140 PRO Y 141 0 11.59 CISPEP 4 PHE H 146 PRO H 147 0 -1.32 CISPEP 5 THR L 29 PRO L 30 0 -3.29 CISPEP 6 SER L 140 PRO L 141 0 7.49 CRYST1 294.846 294.846 99.525 90.00 90.00 120.00 P 64 2 2 24 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 0.003392 0.001958 0.000000 0.00000 SCALE2 0.000000 0.003916 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010048 0.00000