HEADER IMMUNE SYSTEM/VIRAL PROTEIN 02-MAY-24 9BLX TITLE RHESUS MACAQUE ITS111.01 FAB IN COMPLEX WITH SIV MPER PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ITS111.01 HEAVY; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ITS111.01 LIGHT; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 11 CHAIN: I, G; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 14 ORGANISM_TAXID: 11723 KEYWDS FAB, MPER, MEMBRANE-PROXIMAL EXTERNAL REGION, HIV-1, GP41, IMMUNE KEYWDS 2 SYSTEM, SIV, IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.GORMAN,M.AHMADI,P.D.KWONG REVDAT 1 15-JAN-25 9BLX 0 JRNL AUTH J.GORMAN,M.AHMADI,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. 1.96 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) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.9 REMARK 3 NUMBER OF REFLECTIONS : 76080 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.630 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 33.9400 - 4.7200 0.96 6062 164 0.1903 0.1942 REMARK 3 2 4.7200 - 3.7500 0.96 6038 163 0.1489 0.1609 REMARK 3 3 3.7500 - 3.2800 0.99 6169 166 0.1679 0.1892 REMARK 3 4 3.2800 - 2.9800 0.99 6172 167 0.1671 0.1856 REMARK 3 5 2.9800 - 2.7600 0.99 6183 166 0.1767 0.2222 REMARK 3 6 2.7600 - 2.6000 0.99 6222 169 0.1761 0.2094 REMARK 3 7 2.6000 - 2.4700 0.99 6156 166 0.1829 0.2299 REMARK 3 8 2.4700 - 2.3600 0.98 6103 165 0.1857 0.2490 REMARK 3 9 2.3600 - 2.2700 0.94 5806 157 0.1940 0.2486 REMARK 3 10 2.2700 - 2.1900 0.86 5382 145 0.2039 0.2592 REMARK 3 11 2.1900 - 2.1300 0.75 4637 125 0.2083 0.2168 REMARK 3 12 2.1300 - 2.0700 0.63 3897 105 0.2137 0.2729 REMARK 3 13 2.0600 - 2.0100 0.50 3073 83 0.2248 0.2532 REMARK 3 14 2.0100 - 1.9600 0.35 2180 59 0.2256 0.2964 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) : 0.215 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.413 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.17 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.013 7105 REMARK 3 ANGLE : 1.041 9665 REMARK 3 CHIRALITY : 0.067 1084 REMARK 3 PLANARITY : 0.009 1228 REMARK 3 DIHEDRAL : 14.734 2538 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 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.8921 26.0013 29.3226 REMARK 3 T TENSOR REMARK 3 T11: 0.1705 T22: 0.2590 REMARK 3 T33: 0.1855 T12: 0.0807 REMARK 3 T13: 0.0352 T23: 0.0287 REMARK 3 L TENSOR REMARK 3 L11: 0.9643 L22: 1.0577 REMARK 3 L33: 1.3108 L12: -0.2981 REMARK 3 L13: 0.0312 L23: -0.4157 REMARK 3 S TENSOR REMARK 3 S11: 0.0533 S12: 0.1125 S13: 0.0822 REMARK 3 S21: -0.0701 S22: 0.0124 S23: 0.1011 REMARK 3 S31: -0.2078 S32: -0.3437 S33: -0.0482 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 114 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.1217 30.0504 0.9357 REMARK 3 T TENSOR REMARK 3 T11: 0.2221 T22: 0.2687 REMARK 3 T33: 0.1634 T12: 0.0288 REMARK 3 T13: 0.0267 T23: 0.0374 REMARK 3 L TENSOR REMARK 3 L11: 1.7882 L22: 2.5567 REMARK 3 L33: 1.1003 L12: -0.8306 REMARK 3 L13: -0.2410 L23: 0.3868 REMARK 3 S TENSOR REMARK 3 S11: -0.0943 S12: 0.2102 S13: 0.0046 REMARK 3 S21: -0.1428 S22: 0.0954 S23: -0.0420 REMARK 3 S31: -0.0479 S32: -0.0173 S33: 0.0082 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.0782 18.6785 33.4525 REMARK 3 T TENSOR REMARK 3 T11: 0.1289 T22: 0.1203 REMARK 3 T33: 0.1362 T12: 0.0012 REMARK 3 T13: 0.0073 T23: -0.0199 REMARK 3 L TENSOR REMARK 3 L11: 1.4394 L22: 1.0566 REMARK 3 L33: 1.1172 L12: 0.0755 REMARK 3 L13: -0.2351 L23: -0.6032 REMARK 3 S TENSOR REMARK 3 S11: 0.0793 S12: -0.1051 S13: 0.1099 REMARK 3 S21: 0.1196 S22: -0.0164 S23: -0.0047 REMARK 3 S31: -0.1643 S32: 0.0307 S33: -0.0641 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.4623 37.6621 3.5036 REMARK 3 T TENSOR REMARK 3 T11: 0.2026 T22: 0.2210 REMARK 3 T33: 0.2643 T12: 0.0097 REMARK 3 T13: 0.0178 T23: 0.0717 REMARK 3 L TENSOR REMARK 3 L11: 2.1146 L22: 1.9326 REMARK 3 L33: 2.2314 L12: 0.4089 REMARK 3 L13: 0.2796 L23: 0.1804 REMARK 3 S TENSOR REMARK 3 S11: -0.0650 S12: 0.1960 S13: 0.3888 REMARK 3 S21: -0.0891 S22: -0.1051 S23: -0.2073 REMARK 3 S31: -0.3173 S32: 0.2455 S33: 0.1531 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.7633 52.4374 -5.1233 REMARK 3 T TENSOR REMARK 3 T11: 0.1748 T22: 0.2161 REMARK 3 T33: 0.1760 T12: 0.0727 REMARK 3 T13: -0.0201 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.7713 L22: 1.4320 REMARK 3 L33: 1.0762 L12: -0.2862 REMARK 3 L13: -0.0691 L23: 0.5331 REMARK 3 S TENSOR REMARK 3 S11: 0.0209 S12: -0.1319 S13: -0.0609 REMARK 3 S21: 0.0376 S22: 0.1016 S23: -0.2056 REMARK 3 S31: 0.1714 S32: 0.2838 S33: -0.0895 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.3275 47.0195 -37.2928 REMARK 3 T TENSOR REMARK 3 T11: 0.5463 T22: 0.4176 REMARK 3 T33: 0.2094 T12: 0.2666 REMARK 3 T13: 0.0149 T23: 0.0157 REMARK 3 L TENSOR REMARK 3 L11: 0.4506 L22: 0.9920 REMARK 3 L33: 1.0930 L12: -0.0140 REMARK 3 L13: 0.1414 L23: -0.7136 REMARK 3 S TENSOR REMARK 3 S11: 0.2282 S12: 0.4008 S13: 0.0674 REMARK 3 S21: -0.5981 S22: -0.2657 S23: -0.0581 REMARK 3 S31: -0.2934 S32: -0.1274 S33: 0.0057 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.0503 55.7003 -10.9265 REMARK 3 T TENSOR REMARK 3 T11: 0.1854 T22: 0.1910 REMARK 3 T33: 0.2155 T12: 0.0012 REMARK 3 T13: -0.0031 T23: 0.0561 REMARK 3 L TENSOR REMARK 3 L11: 0.8530 L22: 0.6797 REMARK 3 L33: 1.3045 L12: -0.1155 REMARK 3 L13: 0.5872 L23: 0.2136 REMARK 3 S TENSOR REMARK 3 S11: 0.0581 S12: -0.1451 S13: -0.1668 REMARK 3 S21: 0.0885 S22: 0.0762 S23: 0.0862 REMARK 3 S31: 0.1747 S32: -0.1728 S33: -0.1105 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -55.9489 37.2909 -41.4118 REMARK 3 T TENSOR REMARK 3 T11: 0.5272 T22: 0.5385 REMARK 3 T33: 0.6315 T12: 0.6125 REMARK 3 T13: -0.2802 T23: -0.5688 REMARK 3 L TENSOR REMARK 3 L11: 0.3470 L22: 0.3551 REMARK 3 L33: 0.3278 L12: -0.2181 REMARK 3 L13: -0.3375 L23: 0.1535 REMARK 3 S TENSOR REMARK 3 S11: 0.5041 S12: 0.6194 S13: -0.5526 REMARK 3 S21: -0.3878 S22: -0.1598 S23: 0.1227 REMARK 3 S31: 0.5605 S32: 0.4390 S33: 0.4191 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 661 THROUGH 674 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.2165 62.2561 10.6415 REMARK 3 T TENSOR REMARK 3 T11: 0.2648 T22: 0.3469 REMARK 3 T33: 0.2277 T12: 0.0702 REMARK 3 T13: -0.0080 T23: -0.0760 REMARK 3 L TENSOR REMARK 3 L11: 3.5936 L22: 6.5098 REMARK 3 L33: 3.6760 L12: 2.4476 REMARK 3 L13: -0.3290 L23: 0.3080 REMARK 3 S TENSOR REMARK 3 S11: 0.2262 S12: -0.3648 S13: -0.0219 REMARK 3 S21: 0.3285 S22: 0.0792 S23: -0.1995 REMARK 3 S31: -0.0353 S32: 0.1563 S33: -0.0579 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 661 THROUGH 674 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.4689 16.4726 45.2133 REMARK 3 T TENSOR REMARK 3 T11: 0.2091 T22: 0.3248 REMARK 3 T33: 0.2329 T12: 0.0382 REMARK 3 T13: 0.0651 T23: 0.0819 REMARK 3 L TENSOR REMARK 3 L11: 3.2486 L22: 4.5667 REMARK 3 L33: 4.2502 L12: 1.2310 REMARK 3 L13: -0.4990 L23: 0.3703 REMARK 3 S TENSOR REMARK 3 S11: 0.0998 S12: -0.0655 S13: 0.1813 REMARK 3 S21: 0.0538 S22: 0.0761 S23: 0.3593 REMARK 3 S31: -0.1744 S32: -0.2632 S33: 0.0513 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 9BLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000282972. 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85905 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.47700 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 (%): 60.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MGCL2 25% PEG 400 20% PEG 3350 REMARK 280 0.1M TRIS-HCL PH 8.5 (GLYCEROL FOR CRYOPROTECTANT), VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z 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 1.000000 0.000000 0.000000 83.43250 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.41700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.43250 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 59.41700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: 5850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, G 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: 6480 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I 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 392 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 421 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 427 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 490 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 ASP H 217 REMARK 465 LYS H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 GLY A 219 REMARK 465 LEU A 220 REMARK 465 GLU A 221 REMARK 465 VAL A 222 REMARK 465 ARG B 211 REMARK 465 GLY B 212 REMARK 465 GLU B 213 REMARK 465 LEU I 675 REMARK 465 ALA I 676 REMARK 465 SER I 677 REMARK 465 TRP I 678 REMARK 465 ILE I 679 REMARK 465 LYS I 680 REMARK 465 TYR I 681 REMARK 465 ILE I 682 REMARK 465 GLN I 683 REMARK 465 ARG I 684 REMARK 465 ARG I 685 REMARK 465 ARG I 686 REMARK 465 LEU G 675 REMARK 465 ALA G 676 REMARK 465 SER G 677 REMARK 465 TRP G 678 REMARK 465 ILE G 679 REMARK 465 LYS G 680 REMARK 465 TYR G 681 REMARK 465 ILE G 682 REMARK 465 GLN G 683 REMARK 465 ARG G 684 REMARK 465 ARG G 685 REMARK 465 ARG G 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 SG CYS H 22 HG CYS H 92 1.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 SER H 97 CB SER H 97 OG -0.089 REMARK 500 CYS H 196 CB CYS H 196 SG -0.098 REMARK 500 CYS L 194 CB CYS L 194 SG -0.102 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS L 23 CA - CB - SG ANGL. DEV. = 7.2 DEGREES 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 15 -8.39 80.86 REMARK 500 TYR H 100C -129.60 -92.11 REMARK 500 SER L 30 -128.88 51.56 REMARK 500 ALA L 51 -38.26 71.40 REMARK 500 SER L 77 63.08 36.15 REMARK 500 ALA L 84 171.89 175.85 REMARK 500 PRO L 95 31.08 -93.72 REMARK 500 ASN L 138 63.31 62.51 REMARK 500 LYS L 190 -62.09 -104.93 REMARK 500 SER A 15 -2.04 79.91 REMARK 500 TYR A 100C -135.20 -89.15 REMARK 500 ASP A 144 54.64 72.68 REMARK 500 SER B 30 -127.94 51.88 REMARK 500 ALA B 51 -36.85 71.28 REMARK 500 ALA B 84 169.35 176.67 REMARK 500 LYS B 190 -66.49 -107.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 504 DISTANCE = 6.72 ANGSTROMS DBREF 9BLX H 1 222 PDB 9BLX 9BLX 1 222 DBREF 9BLX L 1 213 PDB 9BLX 9BLX 1 213 DBREF 9BLX A 1 222 PDB 9BLX 9BLX 1 222 DBREF 9BLX B 1 213 PDB 9BLX 9BLX 1 213 DBREF1 9BLX I 660 686 UNP A0A4Y5TJX4_SIV DBREF2 9BLX I A0A4Y5TJX4 669 695 DBREF1 9BLX G 660 686 UNP A0A4Y5TJX4_SIV DBREF2 9BLX G A0A4Y5TJX4 669 695 SEQADV 9BLX ARG I 684 UNP A0A4Y5TJX TYR 693 CONFLICT SEQADV 9BLX ARG I 686 UNP A0A4Y5TJX VAL 695 CONFLICT SEQADV 9BLX ARG G 684 UNP A0A4Y5TJX TYR 693 CONFLICT SEQADV 9BLX ARG G 686 UNP A0A4Y5TJX VAL 695 CONFLICT SEQRES 1 H 232 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLU SEQRES 2 H 232 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 232 GLY SER ILE SER SER SER ASN TRP TRP THR TRP ILE ARG SEQRES 4 H 232 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN ILE SEQRES 5 H 232 GLY GLY ASN SER GLY LYS THR PHE TYR ASN PRO SER LEU SEQRES 6 H 232 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS LYS SEQRES 7 H 232 GLN PHE SER LEU ARG LEU SER SER VAL ALA ALA ALA ASP SEQRES 8 H 232 THR ALA VAL TYR TYR CYS ALA ARG HIS SER SER GLY TYR SEQRES 9 H 232 PHE THR LEU TYR ALA LEU ASP SER TRP GLY GLN GLY VAL SEQRES 10 H 232 VAL VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 232 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 232 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 232 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 232 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 232 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 232 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 232 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 232 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 213 GLN ASP ILE SER TYR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR GLN ALA SER SEQRES 5 L 213 THR LEU GLN GLY GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN TYR HIS SEQRES 8 L 213 ASN SER ASP PRO PHE THR PHE GLY PRO GLY THR LYS LEU SEQRES 9 L 213 ASP ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 213 PHE ASN ARG GLY GLU SEQRES 1 A 232 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLU SEQRES 2 A 232 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 232 GLY SER ILE SER SER SER ASN TRP TRP THR TRP ILE ARG SEQRES 4 A 232 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN ILE SEQRES 5 A 232 GLY GLY ASN SER GLY LYS THR PHE TYR ASN PRO SER LEU SEQRES 6 A 232 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS LYS SEQRES 7 A 232 GLN PHE SER LEU ARG LEU SER SER VAL ALA ALA ALA ASP SEQRES 8 A 232 THR ALA VAL TYR TYR CYS ALA ARG HIS SER SER GLY TYR SEQRES 9 A 232 PHE THR LEU TYR ALA LEU ASP SER TRP GLY GLN GLY VAL SEQRES 10 A 232 VAL VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 232 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 232 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 232 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 232 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 232 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 232 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 232 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 A 232 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL SEQRES 1 B 213 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 213 GLN ASP ILE SER TYR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 213 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR GLN ALA SER SEQRES 5 B 213 THR LEU GLN GLY GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 213 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN TYR HIS SEQRES 8 B 213 ASN SER ASP PRO PHE THR PHE GLY PRO GLY THR LYS LEU SEQRES 9 B 213 ASP ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 213 PHE ASN ARG GLY GLU SEQRES 1 I 27 LEU GLN LYS LEU ASN SER TRP ASP VAL PHE GLY ASN TRP SEQRES 2 I 27 PHE ASP LEU ALA SER TRP ILE LYS TYR ILE GLN ARG ARG SEQRES 3 I 27 ARG SEQRES 1 G 27 LEU GLN LYS LEU ASN SER TRP ASP VAL PHE GLY ASN TRP SEQRES 2 G 27 PHE ASP LEU ALA SER TRP ILE LYS TYR ILE GLN ARG ARG SEQRES 3 G 27 ARG HET PG4 H 301 31 HET PG4 A 301 31 HET PG4 A 302 31 HET GOL A 303 14 HET GOL B 301 14 HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 PG4 3(C8 H18 O5) FORMUL 10 GOL 2(C3 H8 O3) FORMUL 12 HOH *472(H2 O) HELIX 1 AA1 THR H 73 LYS H 75 5 3 HELIX 2 AA2 ALA H 83 THR H 87 5 5 HELIX 3 AA3 SER H 127 LYS H 129 5 3 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 SER L 127 1 7 HELIX 9 AA9 LYS L 183 GLU L 187 1 5 HELIX 10 AB1 LEU A 63 SER A 65 5 3 HELIX 11 AB2 ALA A 83 THR A 87 5 5 HELIX 12 AB3 SER A 127 LYS A 129 5 3 HELIX 13 AB4 SER A 156 ALA A 158 5 3 HELIX 14 AB5 SER A 187 THR A 191 5 5 HELIX 15 AB6 LYS A 201 ASN A 204 5 4 HELIX 16 AB7 GLN B 79 PHE B 83 5 5 HELIX 17 AB8 SER B 121 LYS B 126 1 6 HELIX 18 AB9 LYS B 183 GLU B 187 1 5 HELIX 19 AC1 ASN I 664 ASN I 671 1 8 HELIX 20 AC2 ASN G 664 ASN G 671 1 8 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 23 N GLN H 5 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 SER H 70 O SER H 79 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 SER H 97 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 TRP H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 GLY H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O PHE H 58 N ASN H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 SER H 97 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 LEU H 100B TRP H 103 -1 O TYR H 100C N SER H 96 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA 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 199 N THR H 151 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 102 ARG L 107 1 O ARG L 107 N ALA L 13 SHEET 3 AA8 6 ALA L 84 TYR L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 ASN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O SER L 177 N CYS L 134 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB2 4 GLN A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O THR A 23 N GLN A 5 SHEET 3 AB2 4 GLN A 77 LEU A 82 -1 O PHE A 78 N CYS A 22 SHEET 4 AB2 4 VAL A 67 ASP A 72 -1 N ASP A 72 O GLN A 77 SHEET 1 AB3 6 LEU A 11 VAL A 12 0 SHEET 2 AB3 6 VAL A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB3 6 ALA A 88 SER A 97 -1 N TYR A 90 O VAL A 107 SHEET 4 AB3 6 TRP A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AB3 6 GLU A 46 GLY A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AB3 6 THR A 57 TYR A 59 -1 O PHE A 58 N ASN A 50 SHEET 1 AB4 4 LEU A 11 VAL A 12 0 SHEET 2 AB4 4 VAL A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB4 4 ALA A 88 SER A 97 -1 N TYR A 90 O VAL A 107 SHEET 4 AB4 4 LEU A 100B TRP A 103 -1 O TYR A 100C N SER A 96 SHEET 1 AB5 4 SER A 120 LEU A 124 0 SHEET 2 AB5 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB5 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB5 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB6 4 THR A 131 SER A 132 0 SHEET 2 AB6 4 THR A 135 TYR A 145 -1 O THR A 135 N SER A 132 SHEET 3 AB6 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB6 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB7 3 THR A 151 TRP A 154 0 SHEET 2 AB7 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB7 3 THR A 205 ARG A 210 -1 O VAL A 207 N VAL A 198 SHEET 1 AB8 4 MET B 4 SER B 7 0 SHEET 2 AB8 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB9 6 SER B 10 SER B 14 0 SHEET 2 AB9 6 THR B 102 ARG B 107 1 O ARG B 107 N ALA B 13 SHEET 3 AB9 6 ALA B 84 TYR B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AB9 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AB9 6 ASN B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB9 6 THR B 53 LEU B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AC1 4 SER B 114 PHE B 118 0 SHEET 2 AC1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AC1 4 TYR B 173 SER B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 AC1 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AC2 3 LYS B 145 VAL B 150 0 SHEET 2 AC2 3 TYR B 192 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 3 AC2 3 VAL B 205 PHE B 209 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.32 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.07 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.19 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 SSBOND 5 CYS A 22 CYS A 92 1555 1555 2.27 SSBOND 6 CYS A 140 CYS A 196 1555 1555 2.05 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.17 SSBOND 8 CYS B 134 CYS B 194 1555 1555 2.07 CISPEP 1 PHE H 146 PRO H 147 0 -4.34 CISPEP 2 GLU H 148 PRO H 149 0 -1.24 CISPEP 3 SER L 7 PRO L 8 0 -4.95 CISPEP 4 ASP L 94 PRO L 95 0 5.55 CISPEP 5 TYR L 140 PRO L 141 0 1.68 CISPEP 6 PHE A 146 PRO A 147 0 -7.26 CISPEP 7 GLU A 148 PRO A 149 0 -1.02 CISPEP 8 SER B 7 PRO B 8 0 -5.27 CISPEP 9 ASP B 94 PRO B 95 0 7.27 CISPEP 10 TYR B 140 PRO B 141 0 0.37 CRYST1 166.865 118.834 66.541 90.00 104.71 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.005993 0.000000 0.001573 0.00000 SCALE2 0.000000 0.008415 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015537 0.00000