HEADER IMMUNE SYSTEM 03-MAY-24 9BNS TITLE RHESUS MACAQUE ITS114.01 FAB IN COMPLEX WITH SIV MPER PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: MPER PEPTIDE; COMPND 3 CHAIN: C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ITS114 HEAVY CHAIN; COMPND 7 CHAIN: H, A; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ITS114 LIGHT CHAIN; COMPND 11 CHAIN: L, B; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 4 ORGANISM_TAXID: 11723; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 7 ORGANISM_TAXID: 9544; SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 12 ORGANISM_TAXID: 9544; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, MPER, MEMBRANE-PROXIMAL EXTERNAL REGION, HIV-1, GP41, IMMUNE KEYWDS 2 SYSTEM, SIV EXPDTA X-RAY DIFFRACTION AUTHOR J.GORMAN,Y.-T.LAI,P.D.KWONG REVDAT 1 15-JAN-25 9BNS 0 JRNL AUTH J.GORMAN,P.D.KWONG JRNL TITL ISOLATION AND STRUCTURE OF BROAD SIV-NEUTRALIZING ANTIBODIES JRNL TITL 2 REVEAL A PROXIMAL HELICAL MPER EPITOPE RECOGNIZED BY A JRNL TITL 3 RHESUS MULTI-DONOR CLASS JRNL REF CELL REP 2025 JRNL REFN ESSN 2211-1247 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_5278 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6 REMARK 3 NUMBER OF REFLECTIONS : 36532 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1825 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 44.4400 - 7.0500 0.92 2793 145 0.2313 0.2528 REMARK 3 2 7.0400 - 5.6000 0.94 2694 142 0.2319 0.2885 REMARK 3 3 5.6000 - 4.8900 0.95 2673 141 0.1932 0.2283 REMARK 3 4 4.8900 - 4.4400 0.95 2660 139 0.1839 0.2208 REMARK 3 5 4.4400 - 4.1200 0.96 2672 142 0.1778 0.2407 REMARK 3 6 4.1200 - 3.8800 0.96 2653 139 0.2150 0.2468 REMARK 3 7 3.8800 - 3.6900 0.96 2650 139 0.2278 0.2860 REMARK 3 8 3.6900 - 3.5300 0.96 2643 139 0.2286 0.3037 REMARK 3 9 3.5300 - 3.3900 0.96 2651 140 0.2464 0.2944 REMARK 3 10 3.3900 - 3.2700 0.97 2672 140 0.2940 0.3394 REMARK 3 11 3.2700 - 3.1700 0.97 2646 140 0.3336 0.3726 REMARK 3 12 3.1700 - 3.0800 0.97 2638 139 0.3438 0.3899 REMARK 3 13 3.0800 - 3.0000 0.97 2662 140 0.3594 0.4139 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) : 0.485 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.527 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 89.84 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 112.1 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 5729 REMARK 3 ANGLE : 0.562 7798 REMARK 3 CHIRALITY : 0.044 868 REMARK 3 PLANARITY : 0.009 988 REMARK 3 DIHEDRAL : 13.662 2050 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.4748 -94.2434 -4.1882 REMARK 3 T TENSOR REMARK 3 T11: 0.8444 T22: 0.8003 REMARK 3 T33: 1.0445 T12: 0.0248 REMARK 3 T13: -0.3558 T23: -0.0262 REMARK 3 L TENSOR REMARK 3 L11: 2.8081 L22: 6.5369 REMARK 3 L33: 5.2923 L12: -0.2502 REMARK 3 L13: 0.2102 L23: -1.5432 REMARK 3 S TENSOR REMARK 3 S11: 0.4925 S12: -0.5505 S13: -0.8987 REMARK 3 S21: 0.1513 S22: 0.3087 S23: 0.5150 REMARK 3 S31: 1.3930 S32: 0.3881 S33: -0.8252 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 79.4441 -80.5999 0.1245 REMARK 3 T TENSOR REMARK 3 T11: 0.5711 T22: 1.5371 REMARK 3 T33: 0.9479 T12: 0.1014 REMARK 3 T13: -0.0848 T23: -0.3877 REMARK 3 L TENSOR REMARK 3 L11: 4.9693 L22: 2.7105 REMARK 3 L33: 4.9347 L12: 1.0649 REMARK 3 L13: 3.7899 L23: -0.7081 REMARK 3 S TENSOR REMARK 3 S11: 0.3868 S12: 0.2960 S13: 0.0835 REMARK 3 S21: 0.1318 S22: 0.1189 S23: -0.2257 REMARK 3 S31: 0.2030 S32: 1.5869 S33: -0.4905 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.5067 -59.4897 3.8422 REMARK 3 T TENSOR REMARK 3 T11: 0.3796 T22: 0.7211 REMARK 3 T33: 0.7719 T12: -0.1197 REMARK 3 T13: 0.0389 T23: 0.0676 REMARK 3 L TENSOR REMARK 3 L11: 2.4417 L22: 4.8718 REMARK 3 L33: 7.2856 L12: -0.7872 REMARK 3 L13: -2.7083 L23: 2.8279 REMARK 3 S TENSOR REMARK 3 S11: 0.1871 S12: -0.1793 S13: -0.0917 REMARK 3 S21: -0.0309 S22: 0.0625 S23: -0.3464 REMARK 3 S31: -0.4437 S32: -0.1770 S33: -0.2361 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 115 THROUGH 212) REMARK 3 ORIGIN FOR THE GROUP (A): 20.8659 -58.5290 32.3192 REMARK 3 T TENSOR REMARK 3 T11: 0.6073 T22: 1.0321 REMARK 3 T33: 0.4973 T12: -0.0299 REMARK 3 T13: -0.0056 T23: -0.0589 REMARK 3 L TENSOR REMARK 3 L11: 5.7742 L22: 4.8931 REMARK 3 L33: 9.1535 L12: 0.7401 REMARK 3 L13: -0.1206 L23: -2.2002 REMARK 3 S TENSOR REMARK 3 S11: -0.1708 S12: 0.2256 S13: -0.5872 REMARK 3 S21: 0.2235 S22: 0.1532 S23: 0.0376 REMARK 3 S31: -0.2298 S32: -1.1213 S33: -0.1025 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.4047 -72.7112 1.3299 REMARK 3 T TENSOR REMARK 3 T11: 0.5756 T22: 1.3289 REMARK 3 T33: 0.7162 T12: -0.2812 REMARK 3 T13: 0.0488 T23: -0.0348 REMARK 3 L TENSOR REMARK 3 L11: 7.5752 L22: 2.0734 REMARK 3 L33: 4.6601 L12: 2.5443 REMARK 3 L13: -3.4643 L23: 0.5011 REMARK 3 S TENSOR REMARK 3 S11: -0.1002 S12: 0.0009 S13: -0.2022 REMARK 3 S21: 0.1285 S22: -0.2563 S23: 0.2130 REMARK 3 S31: 0.6743 S32: -1.7177 S33: 0.3136 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.9929 -55.5700 32.2361 REMARK 3 T TENSOR REMARK 3 T11: 0.6726 T22: 1.7673 REMARK 3 T33: 0.9620 T12: 0.1217 REMARK 3 T13: 0.0301 T23: -0.1738 REMARK 3 L TENSOR REMARK 3 L11: 2.8094 L22: 5.7495 REMARK 3 L33: 3.4413 L12: 1.4280 REMARK 3 L13: -0.1650 L23: 1.4801 REMARK 3 S TENSOR REMARK 3 S11: -0.2579 S12: 0.0528 S13: -0.1397 REMARK 3 S21: 0.1546 S22: -0.3987 S23: 1.2292 REMARK 3 S31: -0.4246 S32: -1.7327 S33: 0.6282 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 660 THROUGH 672 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.8508 -79.9716 -16.2168 REMARK 3 T TENSOR REMARK 3 T11: 0.4436 T22: 0.7302 REMARK 3 T33: 0.8307 T12: -0.0243 REMARK 3 T13: -0.0935 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 7.6999 L22: 2.3201 REMARK 3 L33: 7.3949 L12: -0.5377 REMARK 3 L13: 5.6014 L23: -1.7404 REMARK 3 S TENSOR REMARK 3 S11: 0.4909 S12: 0.2430 S13: -1.1049 REMARK 3 S21: -0.4229 S22: -0.8021 S23: 0.5224 REMARK 3 S31: 0.5926 S32: 0.9469 S33: 0.2103 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 673 THROUGH 684 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.1974 -84.0847 -11.9727 REMARK 3 T TENSOR REMARK 3 T11: 0.7185 T22: 1.6606 REMARK 3 T33: 1.1785 T12: -0.7282 REMARK 3 T13: -0.0182 T23: 0.2258 REMARK 3 L TENSOR REMARK 3 L11: 2.9659 L22: 2.0515 REMARK 3 L33: 0.0601 L12: 2.4688 REMARK 3 L13: -0.4338 L23: -0.3555 REMARK 3 S TENSOR REMARK 3 S11: 0.4347 S12: 0.0138 S13: -0.6445 REMARK 3 S21: 0.0495 S22: -0.1681 S23: 0.6532 REMARK 3 S31: 1.6678 S32: -3.0475 S33: 0.2207 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 660 THROUGH 672 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.2560 -67.1325 -12.4180 REMARK 3 T TENSOR REMARK 3 T11: 0.5424 T22: 0.6255 REMARK 3 T33: 0.7727 T12: -0.1606 REMARK 3 T13: 0.0825 T23: -0.0581 REMARK 3 L TENSOR REMARK 3 L11: 7.2821 L22: 5.9305 REMARK 3 L33: 6.9496 L12: -4.4953 REMARK 3 L13: -2.6406 L23: 0.5913 REMARK 3 S TENSOR REMARK 3 S11: 0.0383 S12: 0.3583 S13: 0.0757 REMARK 3 S21: -0.0062 S22: 0.0026 S23: 0.2765 REMARK 3 S31: -0.8114 S32: -0.1819 S33: 0.0265 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 673 THROUGH 685 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.6497 -64.2354 -12.5807 REMARK 3 T TENSOR REMARK 3 T11: 0.5567 T22: 0.9951 REMARK 3 T33: 1.0012 T12: -0.1759 REMARK 3 T13: 0.1514 T23: -0.1080 REMARK 3 L TENSOR REMARK 3 L11: 5.6792 L22: 7.1317 REMARK 3 L33: 4.7858 L12: -4.9765 REMARK 3 L13: -5.1758 L23: 4.1691 REMARK 3 S TENSOR REMARK 3 S11: 0.0732 S12: 0.3328 S13: 1.2341 REMARK 3 S21: 0.3459 S22: 1.1796 S23: -0.4363 REMARK 3 S31: -0.8794 S32: 1.7834 S33: -1.2102 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 9BNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000282974. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-AUG-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36532 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 44.440 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07 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 : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 137.32667 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 68.66333 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 102.99500 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 34.33167 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 171.65833 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 137.32667 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 68.66333 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 34.33167 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 102.99500 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 171.65833 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 12820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D 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 C 653 REMARK 465 ARG C 654 REMARK 465 ARG C 655 REMARK 465 ASN C 656 REMARK 465 MET C 657 REMARK 465 TYR C 658 REMARK 465 GLU C 659 REMARK 465 ARG C 685 REMARK 465 ARG C 686 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 GLU H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 ALA H 132 REMARK 465 ALA H 133 REMARK 465 LEU H 134 REMARK 465 GLY H 135 REMARK 465 CYS H 136 REMARK 465 LEU H 137 REMARK 465 VAL H 138 REMARK 465 LYS H 139 REMARK 465 ASP H 140 REMARK 465 TYR H 141 REMARK 465 PHE H 142 REMARK 465 PRO H 143 REMARK 465 GLU H 144 REMARK 465 PRO H 145 REMARK 465 VAL H 146 REMARK 465 THR H 147 REMARK 465 VAL H 148 REMARK 465 SER H 149 REMARK 465 TRP H 150 REMARK 465 ASN H 151 REMARK 465 SER H 152 REMARK 465 GLY H 153 REMARK 465 SER H 154 REMARK 465 LEU H 155 REMARK 465 THR H 156 REMARK 465 SER H 157 REMARK 465 GLY H 158 REMARK 465 VAL H 159 REMARK 465 HIS H 160 REMARK 465 THR H 161 REMARK 465 PHE H 162 REMARK 465 PRO H 163 REMARK 465 ALA H 164 REMARK 465 VAL H 165 REMARK 465 LEU H 166 REMARK 465 GLN H 167 REMARK 465 SER H 168 REMARK 465 SER H 169 REMARK 465 GLY H 170 REMARK 465 LEU H 171 REMARK 465 TYR H 172 REMARK 465 SER H 173 REMARK 465 LEU H 174 REMARK 465 SER H 175 REMARK 465 SER H 176 REMARK 465 VAL H 177 REMARK 465 VAL H 178 REMARK 465 THR H 179 REMARK 465 VAL H 180 REMARK 465 PRO H 181 REMARK 465 SER H 182 REMARK 465 SER H 183 REMARK 465 SER H 184 REMARK 465 LEU H 185 REMARK 465 GLY H 186 REMARK 465 THR H 187 REMARK 465 GLN H 188 REMARK 465 THR H 189 REMARK 465 TYR H 190 REMARK 465 VAL H 191 REMARK 465 CYS H 192 REMARK 465 ASN H 193 REMARK 465 VAL H 194 REMARK 465 ASN H 195 REMARK 465 HIS H 196 REMARK 465 LYS H 197 REMARK 465 PRO H 198 REMARK 465 SER H 199 REMARK 465 ASN H 200 REMARK 465 THR H 201 REMARK 465 LYS H 202 REMARK 465 VAL H 203 REMARK 465 ASP H 204 REMARK 465 LYS H 205 REMARK 465 ARG H 206 REMARK 465 VAL H 207 REMARK 465 GLU H 208 REMARK 465 ILE H 209 REMARK 465 LYS H 210 REMARK 465 ALA H 211 REMARK 465 ALA H 212 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 ARG D 653 REMARK 465 ARG D 654 REMARK 465 ARG D 655 REMARK 465 ASN D 656 REMARK 465 MET D 657 REMARK 465 TYR D 658 REMARK 465 GLU D 659 REMARK 465 ARG D 686 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O SER A 28 OG SER A 31 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 7 -155.33 -145.67 REMARK 500 SER H 15 74.45 40.95 REMARK 500 GLU H 16 -138.06 -151.83 REMARK 500 ARG H 66 37.30 -147.52 REMARK 500 ALA H 88 -177.85 -170.88 REMARK 500 LEU L 11 134.77 -171.63 REMARK 500 ILE L 29 31.07 -95.77 REMARK 500 SER L 30 -130.12 46.22 REMARK 500 ALA L 51 -38.24 75.80 REMARK 500 SER L 67 70.56 -157.28 REMARK 500 SER L 77 108.94 -166.04 REMARK 500 ILE L 106 -160.98 -103.87 REMARK 500 ARG L 108 74.29 49.77 REMARK 500 SER A 15 9.17 85.30 REMARK 500 GLU A 16 -147.93 -93.14 REMARK 500 LYS A 43 -152.50 -143.58 REMARK 500 ARG A 66 42.52 -143.03 REMARK 500 GLU A 96 -171.02 -66.08 REMARK 500 SER A 127 -111.05 -111.75 REMARK 500 SER A 128 33.80 -165.09 REMARK 500 GLU A 129 -152.50 -116.02 REMARK 500 ASP A 140 74.93 55.73 REMARK 500 SER B 30 -129.82 42.29 REMARK 500 ALA B 51 -33.56 76.45 REMARK 500 SER B 52 50.15 -152.18 REMARK 500 SER B 76 -79.45 -91.35 REMARK 500 GLU B 105 -158.83 -92.68 REMARK 500 TYR B 140 134.69 -176.35 REMARK 500 ALA B 144 144.14 -171.78 REMARK 500 ASN B 152 -9.38 72.04 REMARK 500 SER B 156 59.83 -105.28 REMARK 500 ASN B 158 54.93 -155.39 REMARK 500 THR B 164 -154.27 -90.22 REMARK 500 THR B 172 -158.55 -87.88 REMARK 500 SER B 174 138.21 -179.27 REMARK 500 GLU B 187 50.13 -94.07 REMARK 500 ARG B 211 108.32 -54.72 REMARK 500 LYS D 662 -36.73 -138.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG D 684 0.14 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9BLX RELATED DB: PDB REMARK 900 SAME ANTIBODY CLASS DBREF 9BNS C 653 686 PDB 9BNS 9BNS 653 686 DBREF 9BNS H 1 212 PDB 9BNS 9BNS 1 212 DBREF 9BNS L 1 214 PDB 9BNS 9BNS 1 214 DBREF 9BNS A 1 212 PDB 9BNS 9BNS 1 212 DBREF 9BNS B 1 214 PDB 9BNS 9BNS 1 214 DBREF 9BNS D 653 686 PDB 9BNS 9BNS 653 686 SEQRES 1 C 34 ARG ARG ARG ASN MET TYR GLU LEU GLN LYS LEU ASN SER SEQRES 2 C 34 TRP ASP VAL PHE GLY ASN TRP PHE ASP LEU ALA SER TRP SEQRES 3 C 34 ILE LYS TYR ILE GLN ARG ARG ARG SEQRES 1 H 222 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU LEU LYS SEQRES 2 H 222 PRO SER GLU THR LEU SER LEU THR CYS GLU VAL SER GLY SEQRES 3 H 222 ALA SER ILE SER SER SER ASN TRP TRP ASN TRP ILE ARG SEQRES 4 H 222 GLN SER PRO GLY LYS GLY LEU GLU TRP ILE GLY THR ILE SEQRES 5 H 222 GLY GLY ASN SER GLY LYS ILE ALA SER SER PRO SER LEU SEQRES 6 H 222 GLU SER ARG VAL ILE MET SER LYS ASP PRO SER LYS ASN SEQRES 7 H 222 ARG PHE SER LEU LYS MET THR SER VAL THR ALA ALA ASP SEQRES 8 H 222 THR ALA ILE TYR TYR CYS THR ARG GLN GLU GLN THR LEU SEQRES 9 H 222 PHE TRP VAL LYS ARG PHE ASP VAL TRP GLY PRO GLY ILE SEQRES 10 H 222 LEU VAL SER VAL THR SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 222 VAL PHE PRO LEU ALA PRO SER SER GLU SER THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS ALA SEQRES 18 H 222 ALA SEQRES 1 L 214 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN ARG SEQRES 4 L 214 PRO GLY LYS ALA PRO ARG PRO LEU ILE ASP SER ALA SER SEQRES 5 L 214 THR LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA ILE TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 TYR SER ASP PRO PHE THR PHE GLY PRO GLY THR GLU LEU SEQRES 9 L 214 GLU ILE TYR ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 222 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU LEU LYS SEQRES 2 A 222 PRO SER GLU THR LEU SER LEU THR CYS GLU VAL SER GLY SEQRES 3 A 222 ALA SER ILE SER SER SER ASN TRP TRP ASN TRP ILE ARG SEQRES 4 A 222 GLN SER PRO GLY LYS GLY LEU GLU TRP ILE GLY THR ILE SEQRES 5 A 222 GLY GLY ASN SER GLY LYS ILE ALA SER SER PRO SER LEU SEQRES 6 A 222 GLU SER ARG VAL ILE MET SER LYS ASP PRO SER LYS ASN SEQRES 7 A 222 ARG PHE SER LEU LYS MET THR SER VAL THR ALA ALA ASP SEQRES 8 A 222 THR ALA ILE TYR TYR CYS THR ARG GLN GLU GLN THR LEU SEQRES 9 A 222 PHE TRP VAL LYS ARG PHE ASP VAL TRP GLY PRO GLY ILE SEQRES 10 A 222 LEU VAL SER VAL THR SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 222 VAL PHE PRO LEU ALA PRO SER SER GLU SER THR ALA ALA SEQRES 12 A 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 A 222 THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY VAL SEQRES 14 A 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 A 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 A 222 GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS PRO SEQRES 17 A 222 SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS ALA SEQRES 18 A 222 ALA SEQRES 1 B 214 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN ARG SEQRES 4 B 214 PRO GLY LYS ALA PRO ARG PRO LEU ILE ASP SER ALA SER SEQRES 5 B 214 THR LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA ILE TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 TYR SER ASP PRO PHE THR PHE GLY PRO GLY THR GLU LEU SEQRES 9 B 214 GLU ILE TYR ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 D 34 ARG ARG ARG ASN MET TYR GLU LEU GLN LYS LEU ASN SER SEQRES 2 D 34 TRP ASP VAL PHE GLY ASN TRP PHE ASP LEU ALA SER TRP SEQRES 3 D 34 ILE LYS TYR ILE GLN ARG ARG ARG HELIX 1 AA1 ASN C 664 ASN C 671 1 8 HELIX 2 AA2 ASP C 674 ARG C 684 1 11 HELIX 3 AA3 LEU H 63 SER H 65 5 3 HELIX 4 AA4 THR H 83 THR H 87 5 5 HELIX 5 AA5 LEU A 63 SER A 65 5 3 HELIX 6 AA6 PRO A 73 LYS A 75 5 3 HELIX 7 AA7 SER A 152 SER A 154 5 3 HELIX 8 AA8 SER A 183 GLN A 188 5 6 HELIX 9 AA9 PRO A 198 ASN A 200 5 3 HELIX 10 AB1 GLN B 79 PHE B 83 5 5 HELIX 11 AB2 SER B 121 GLY B 128 1 8 HELIX 12 AB3 SER B 182 GLU B 187 1 6 HELIX 13 AB4 ASN D 664 ASN D 671 1 8 HELIX 14 AB5 ASP D 674 ARG D 684 1 11 SHEET 1 AA1 4 LEU H 4 GLU H 6 0 SHEET 2 AA1 4 THR H 17 VAL H 24 -1 O GLU H 23 N GLN H 5 SHEET 3 AA1 4 ARG H 77 THR H 82A-1 O PHE H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O ARG H 77 SHEET 1 AA2 6 LEU H 11 LEU H 12 0 SHEET 2 AA2 6 ILE H 107 VAL H 111 1 O SER H 110 N LEU H 12 SHEET 3 AA2 6 ALA H 88 GLN H 97 -1 N TYR H 90 O ILE H 107 SHEET 4 AA2 6 TRP H 34 SER H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLY H 44 GLY H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 ILE H 57 SER H 59 -1 O ALA H 58 N THR H 50 SHEET 1 AA3 4 LEU H 11 LEU H 12 0 SHEET 2 AA3 4 ILE H 107 VAL H 111 1 O SER H 110 N LEU H 12 SHEET 3 AA3 4 ALA H 88 GLN H 97 -1 N TYR H 90 O ILE H 107 SHEET 4 AA3 4 VAL H 100B TRP H 103 -1 O LYS H 100C N GLU H 96 SHEET 1 AA4 4 MET L 4 SER L 7 0 SHEET 2 AA4 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA4 4 PHE L 62 SER L 65 -1 N SER L 63 O THR L 74 SHEET 1 AA5 5 THR L 53 LEU L 54 0 SHEET 2 AA5 5 ARG L 45 ASP L 49 -1 N ASP L 49 O THR L 53 SHEET 3 AA5 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA5 5 ILE L 85 GLN L 90 -1 O ILE L 85 N GLN L 38 SHEET 5 AA5 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA6 4 GLN A 3 SER A 7 0 SHEET 2 AA6 4 THR A 17 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA6 4 ARG A 77 THR A 82A-1 O MET A 82 N LEU A 18 SHEET 4 AA6 4 VAL A 67 ASP A 72 -1 N ILE A 68 O LYS A 81 SHEET 1 AA7 6 LEU A 11 LEU A 12 0 SHEET 2 AA7 6 ILE A 107 VAL A 111 1 O SER A 110 N LEU A 12 SHEET 3 AA7 6 ALA A 88 GLN A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AA7 6 TRP A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AA7 6 LEU A 45 GLY A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AA7 6 ILE A 57 SER A 59 -1 O ALA A 58 N THR A 50 SHEET 1 AA8 4 LEU A 11 LEU A 12 0 SHEET 2 AA8 4 ILE A 107 VAL A 111 1 O SER A 110 N LEU A 12 SHEET 3 AA8 4 ALA A 88 GLN A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AA8 4 VAL A 102 TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AA9 4 SER A 120 LEU A 124 0 SHEET 2 AA9 4 THR A 131 TYR A 141 -1 O GLY A 135 N LEU A 124 SHEET 3 AA9 4 TYR A 172 PRO A 181 -1 O TYR A 172 N TYR A 141 SHEET 4 AA9 4 VAL A 159 THR A 161 -1 N HIS A 160 O VAL A 177 SHEET 1 AB1 3 VAL A 146 TRP A 150 0 SHEET 2 AB1 3 TYR A 190 HIS A 196 -1 O ASN A 193 N SER A 149 SHEET 3 AB1 3 THR A 201 VAL A 207 -1 O THR A 201 N HIS A 196 SHEET 1 AB2 4 MET B 4 SER B 7 0 SHEET 2 AB2 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB2 4 GLU B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB2 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB3 6 SER B 10 LEU B 11 0 SHEET 2 AB3 6 THR B 102 LEU B 104 1 O GLU B 103 N LEU B 11 SHEET 3 AB3 6 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AB3 6 LEU B 33 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AB3 6 ARG B 45 ASP B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB3 6 THR B 53 LEU B 54 -1 O THR B 53 N ASP B 49 SHEET 1 AB4 4 SER B 10 LEU B 11 0 SHEET 2 AB4 4 THR B 102 LEU B 104 1 O GLU B 103 N LEU B 11 SHEET 3 AB4 4 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AB4 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB5 4 VAL B 115 PHE B 118 0 SHEET 2 AB5 4 VAL B 132 LEU B 136 -1 O LEU B 135 N PHE B 116 SHEET 3 AB5 4 LEU B 175 LEU B 179 -1 O SER B 177 N CYS B 134 SHEET 4 AB5 4 SER B 159 GLN B 160 -1 N GLN B 160 O THR B 178 SHEET 1 AB6 4 ALA B 153 LEU B 154 0 SHEET 2 AB6 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB6 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AB6 4 LYS B 207 ASN B 210 -1 O LYS B 207 N CYS B 194 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 4 CYS A 136 CYS A 192 1555 1555 2.04 SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 6 CYS B 134 CYS B 194 1555 1555 2.03 CISPEP 1 SER L 7 PRO L 8 0 -8.35 CISPEP 2 ASP L 94 PRO L 95 0 2.20 CISPEP 3 PHE A 142 PRO A 143 0 -5.85 CISPEP 4 GLU A 144 PRO A 145 0 1.88 CISPEP 5 SER B 7 PRO B 8 0 -3.27 CISPEP 6 ASP B 94 PRO B 95 0 2.01 CISPEP 7 TYR B 140 PRO B 141 0 5.94 CRYST1 175.900 175.900 205.990 90.00 90.00 120.00 P 65 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 0.005685 0.003282 0.000000 0.00000 SCALE2 0.000000 0.006565 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004855 0.00000