HEADER IMMUNE SYSTEM 25-NOV-22 8FA6 TITLE CRYSTAL STRUCTURE OF KY15.10 FAB IN COMPLEX WITH CIRCUMSPOROZOITE TITLE 2 PROTEIN DND PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: KY15.10 ANTIBODY, HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: KY15.10 ANTIBODY, LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN DND PEPTIDE; COMPND 11 CHAIN: P, Q; COMPND 12 SYNONYM: CS; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 18 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM; SOURCE 19 ORGANISM_TAXID: 5833 KEYWDS MALARIA, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR E.THAI,K.PRIETO,J.P.JULIEN REVDAT 1 01-NOV-23 8FA6 0 JRNL AUTH E.THAI,R.MURUGAN,S.BINTER,C.BURN ASCHNER,K.PRIETO, JRNL AUTH 2 A.KASSARDJIAN,R.W.KANG,A.OBRAZTCOVA,G.COSTA,E.LEVASHINA, JRNL AUTH 3 P.KELLAM,H.WARDEMANN,J.P.JULIEN JRNL TITL MOLECULAR DETERMINANTS OF CROSS-REACTIVITY AND POTENCY BY JRNL TITL 2 VH3-33 ANTIBODIES AGAINST THE PLASMODIUM FALCIPARUM JRNL TITL 3 CIRCUMSPOROZOITE PROTEIN JRNL REF CELL REP 2023 JRNL REFN ESSN 2211-1247 JRNL DOI 10.1016/J.CELREP.2023.113330 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19_4080 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 29112 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1456 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 29.3800 - 5.5900 1.00 2865 151 0.1973 0.2302 REMARK 3 2 5.5900 - 4.4400 1.00 2792 147 0.1575 0.1913 REMARK 3 3 4.4400 - 3.8800 1.00 2767 146 0.1740 0.2134 REMARK 3 4 3.8800 - 3.5300 0.99 2777 146 0.1930 0.2190 REMARK 3 5 3.5300 - 3.2800 0.99 2726 144 0.2251 0.2599 REMARK 3 6 3.2700 - 3.0800 1.00 2755 145 0.2308 0.2978 REMARK 3 7 3.0800 - 2.9300 1.00 2765 145 0.2541 0.2858 REMARK 3 8 2.9300 - 2.8000 1.00 2740 144 0.2738 0.2868 REMARK 3 9 2.8000 - 2.6900 1.00 2741 145 0.2839 0.3446 REMARK 3 10 2.6900 - 2.6000 1.00 2728 143 0.2909 0.3409 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.345 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.682 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 56.77 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.78 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 : 0.003 7010 REMARK 3 ANGLE : 0.555 9528 REMARK 3 CHIRALITY : 0.042 1063 REMARK 3 PLANARITY : 0.004 1217 REMARK 3 DIHEDRAL : 11.015 2474 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 1:125 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.120 12.048 41.532 REMARK 3 T TENSOR REMARK 3 T11: 0.3565 T22: 0.4396 REMARK 3 T33: 0.3973 T12: -0.0547 REMARK 3 T13: 0.0495 T23: 0.0316 REMARK 3 L TENSOR REMARK 3 L11: 0.9531 L22: 1.9527 REMARK 3 L33: 4.3603 L12: -0.6761 REMARK 3 L13: -1.6167 L23: 2.0342 REMARK 3 S TENSOR REMARK 3 S11: -0.0607 S12: 0.1136 S13: -0.0855 REMARK 3 S21: 0.2193 S22: -0.0764 S23: 0.1217 REMARK 3 S31: -0.0310 S32: -0.1109 S33: 0.1350 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN H AND RESID 126:216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.948 1.238 12.149 REMARK 3 T TENSOR REMARK 3 T11: 0.4020 T22: 0.4011 REMARK 3 T33: 0.2911 T12: -0.0507 REMARK 3 T13: 0.0140 T23: 0.0177 REMARK 3 L TENSOR REMARK 3 L11: 6.4197 L22: 4.0427 REMARK 3 L33: 3.5277 L12: -2.2650 REMARK 3 L13: -0.9943 L23: 1.3508 REMARK 3 S TENSOR REMARK 3 S11: 0.0968 S12: 0.1618 S13: -0.4511 REMARK 3 S21: -0.2623 S22: 0.0301 S23: -0.0518 REMARK 3 S31: 0.3828 S32: 0.0304 S33: -0.0861 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.743 17.359 46.226 REMARK 3 T TENSOR REMARK 3 T11: 0.4486 T22: 0.3758 REMARK 3 T33: 0.3612 T12: 0.0180 REMARK 3 T13: -0.0794 T23: -0.0290 REMARK 3 L TENSOR REMARK 3 L11: 5.6210 L22: 1.7841 REMARK 3 L33: 3.2384 L12: -1.2301 REMARK 3 L13: -1.1646 L23: 0.3845 REMARK 3 S TENSOR REMARK 3 S11: -0.1797 S12: 0.0244 S13: 0.4137 REMARK 3 S21: 0.1225 S22: 0.1400 S23: -0.3286 REMARK 3 S31: 0.0497 S32: 0.2873 S33: 0.0244 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN L AND RESID 107:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 42.455 15.013 10.495 REMARK 3 T TENSOR REMARK 3 T11: 0.3291 T22: 0.3853 REMARK 3 T33: 0.3724 T12: -0.0126 REMARK 3 T13: 0.1007 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 3.2668 L22: 1.6865 REMARK 3 L33: 4.3815 L12: -0.6932 REMARK 3 L13: 1.9601 L23: -1.5998 REMARK 3 S TENSOR REMARK 3 S11: -0.0349 S12: 0.2337 S13: 0.0908 REMARK 3 S21: -0.1325 S22: -0.0235 S23: -0.1481 REMARK 3 S31: 0.0647 S32: 0.1553 S33: 0.1039 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN A AND RESID 1:125 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.221 8.366 -11.459 REMARK 3 T TENSOR REMARK 3 T11: 0.3862 T22: 0.7799 REMARK 3 T33: 0.6852 T12: -0.0074 REMARK 3 T13: -0.0274 T23: -0.1455 REMARK 3 L TENSOR REMARK 3 L11: 2.4820 L22: 2.3147 REMARK 3 L33: 3.4051 L12: -0.1520 REMARK 3 L13: -0.7734 L23: 1.8985 REMARK 3 S TENSOR REMARK 3 S11: -0.0391 S12: 0.3356 S13: -0.6539 REMARK 3 S21: -0.1914 S22: -0.5081 S23: 0.3120 REMARK 3 S31: 0.1558 S32: -1.0486 S33: 0.4577 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN A AND RESID 126:216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.826 37.035 8.959 REMARK 3 T TENSOR REMARK 3 T11: 0.5568 T22: 0.7465 REMARK 3 T33: 0.7132 T12: 0.1935 REMARK 3 T13: -0.1389 T23: -0.2148 REMARK 3 L TENSOR REMARK 3 L11: 3.0380 L22: 5.2930 REMARK 3 L33: 2.1167 L12: 0.8480 REMARK 3 L13: 0.5678 L23: 1.1029 REMARK 3 S TENSOR REMARK 3 S11: -0.1007 S12: -0.6746 S13: 0.8933 REMARK 3 S21: -0.1789 S22: -0.3352 S23: 0.9953 REMARK 3 S31: -0.5294 S32: -0.6569 S33: 0.4851 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.357 22.296 -26.060 REMARK 3 T TENSOR REMARK 3 T11: 0.6577 T22: 0.7559 REMARK 3 T33: 0.3880 T12: 0.2191 REMARK 3 T13: -0.0664 T23: -0.1150 REMARK 3 L TENSOR REMARK 3 L11: 4.4609 L22: 6.2258 REMARK 3 L33: 3.5791 L12: -0.3293 REMARK 3 L13: 0.6813 L23: 0.3367 REMARK 3 S TENSOR REMARK 3 S11: -0.0977 S12: 0.5541 S13: -0.0126 REMARK 3 S21: -0.6492 S22: -0.4490 S23: 0.5468 REMARK 3 S31: -0.8118 S32: -0.3795 S33: 0.5589 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN B AND RESID 107:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.705 38.548 4.217 REMARK 3 T TENSOR REMARK 3 T11: 0.6295 T22: 0.2781 REMARK 3 T33: 0.4365 T12: 0.0234 REMARK 3 T13: -0.0557 T23: -0.0416 REMARK 3 L TENSOR REMARK 3 L11: 3.2783 L22: 2.1463 REMARK 3 L33: 5.5424 L12: 0.3499 REMARK 3 L13: 3.0688 L23: 0.9540 REMARK 3 S TENSOR REMARK 3 S11: -0.2942 S12: -0.1244 S13: 0.5145 REMARK 3 S21: -0.4745 S22: -0.2957 S23: -0.0277 REMARK 3 S31: -0.8753 S32: -0.0366 S33: 0.5293 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN P AND RESID 2:10 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.881 19.175 57.563 REMARK 3 T TENSOR REMARK 3 T11: 0.5770 T22: 0.4997 REMARK 3 T33: 0.4416 T12: -0.0076 REMARK 3 T13: 0.1197 T23: -0.0326 REMARK 3 L TENSOR REMARK 3 L11: 4.9256 L22: 8.2812 REMARK 3 L33: 4.2368 L12: -4.1610 REMARK 3 L13: 1.9696 L23: -1.4821 REMARK 3 S TENSOR REMARK 3 S11: -0.6044 S12: -0.6429 S13: 0.2885 REMARK 3 S21: -0.2139 S22: 0.9043 S23: -0.1607 REMARK 3 S31: 0.0470 S32: -0.4970 S33: -0.3391 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN Q AND RESID 3:9 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.473 1.444 -26.931 REMARK 3 T TENSOR REMARK 3 T11: 0.4272 T22: 0.7816 REMARK 3 T33: 0.9894 T12: -0.0168 REMARK 3 T13: -0.0332 T23: -0.1809 REMARK 3 L TENSOR REMARK 3 L11: 4.4736 L22: 2.4682 REMARK 3 L33: 6.7099 L12: 0.1957 REMARK 3 L13: -4.0924 L23: 2.4397 REMARK 3 S TENSOR REMARK 3 S11: -0.3365 S12: -0.4257 S13: -1.5753 REMARK 3 S21: -1.6439 S22: -0.3268 S23: 0.2870 REMARK 3 S31: -0.2588 S32: -0.4670 S33: 0.5744 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 8FA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-22. REMARK 100 THE DEPOSITION ID IS D_1000270263. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-JUN-21 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 : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03319 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29115 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 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 (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.02 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES PH REMARK 280 7.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K 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 96.27450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.95250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 96.27450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.95250 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: 5580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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: 5060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19640 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Q 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 A 403 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 CYS B 214 REMARK 465 ASN P 1 REMARK 465 ASP P 11 REMARK 465 PRO P 12 REMARK 465 ASN Q 1 REMARK 465 VAL Q 2 REMARK 465 VAL Q 10 REMARK 465 ASP Q 11 REMARK 465 PRO Q 12 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 THR H 131 OG1 CG2 REMARK 470 LEU H 159 CG CD1 CD2 REMARK 470 ASN H 197 CG OD1 ND2 REMARK 470 LYS H 206 CG CD CE NZ REMARK 470 GLU L 143 CG CD OE1 OE2 REMARK 470 GLU L 161 CG CD OE1 OE2 REMARK 470 GLU L 213 CG CD OE1 OE2 REMARK 470 CYS L 214 SG REMARK 470 GLN A 1 CG CD OE1 NE2 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 ASP B 1 CG OD1 OD2 REMARK 470 GLU B 143 CG CD OE1 OE2 REMARK 470 GLU B 165 CG CD OE1 OE2 REMARK 470 ASP B 170 CG OD1 OD2 REMARK 470 ASP Q 3 CG OD1 OD2 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 ARG H 16 -168.92 -102.09 REMARK 500 GLU H 100 57.07 -90.91 REMARK 500 ASN H 100A 71.73 -68.12 REMARK 500 ASP H 101 -76.03 -118.66 REMARK 500 SER L 30 -125.01 57.37 REMARK 500 ALA L 51 -44.74 67.22 REMARK 500 ALA L 84 -163.86 -167.01 REMARK 500 TYR L 94 -151.88 62.87 REMARK 500 ASN L 138 73.20 55.46 REMARK 500 LYS A 43 -159.70 -153.61 REMARK 500 ASP A 101 -65.37 -132.93 REMARK 500 ASP A 144 62.43 66.25 REMARK 500 SER B 30 -118.64 52.89 REMARK 500 ALA B 51 -41.87 71.55 REMARK 500 PHE B 83 101.08 -59.37 REMARK 500 ALA B 84 -164.84 -163.38 REMARK 500 TYR B 94 -143.82 56.81 REMARK 500 ASN B 138 76.59 54.20 REMARK 500 ASN B 152 -0.17 63.28 REMARK 500 REMARK 500 REMARK: NULL DBREF 8FA6 H 1 216 PDB 8FA6 8FA6 1 216 DBREF 8FA6 L 1 214 PDB 8FA6 8FA6 1 214 DBREF 8FA6 A 1 216 PDB 8FA6 8FA6 1 216 DBREF 8FA6 B 1 214 PDB 8FA6 8FA6 1 214 DBREF 8FA6 P 1 12 UNP P08307 CSP_PLAFW 138 149 DBREF 8FA6 Q 1 12 UNP P08307 CSP_PLAFW 138 149 SEQRES 1 H 228 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 228 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 228 PHE THR PHE SER ASN SER GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 228 VAL PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 H 228 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 228 GLY ARG PHE SER VAL SER ARG ASP ASN SER GLU ASN THR SEQRES 7 H 228 LEU TYR LEU GLN MET SER ASN LEU ARG ALA GLU ASP THR SEQRES 8 H 228 ALA VAL TYR TYR CYS VAL ARG ALA TYR PHE ASP SER GLU SEQRES 9 H 228 ASN LEU TYR ASP TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 H 228 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER THR 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 SER ILE SER ARG TRP LEU ALA TRP PHE GLN LYS LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR THR ALA SER SEQRES 5 L 213 ASN LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 213 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 213 TYR ASN TYR TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 L 213 VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 A 228 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 228 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 228 PHE THR PHE SER ASN SER GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 228 VAL PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 A 228 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 228 GLY ARG PHE SER VAL SER ARG ASP ASN SER GLU ASN THR SEQRES 7 A 228 LEU TYR LEU GLN MET SER ASN LEU ARG ALA GLU ASP THR SEQRES 8 A 228 ALA VAL TYR TYR CYS VAL ARG ALA TYR PHE ASP SER GLU SEQRES 9 A 228 ASN LEU TYR ASP TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 A 228 GLY THR THR VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 213 ASP ILE GLN MET THR GLN SER PRO SER THR 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 SER ILE SER ARG TRP LEU ALA TRP PHE GLN LYS LYS SEQRES 4 B 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR THR ALA SER SEQRES 5 B 213 ASN LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 213 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 213 TYR ASN TYR TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 B 213 VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 B 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 B 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 B 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 B 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 B 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 B 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 B 213 ASN ARG GLY GLU CYS SEQRES 1 P 12 ASN VAL ASP PRO ASN ALA ASN PRO ASN VAL ASP PRO SEQRES 1 Q 12 ASN VAL ASP PRO ASN ALA ASN PRO ASN VAL ASP PRO HET EDO H 301 4 HET EDO H 302 4 HET EDO H 303 4 HET EDO L 301 4 HET EDO L 302 4 HET EDO A 301 4 HET EDO A 302 4 HET EDO B 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 7 EDO 8(C2 H6 O2) FORMUL 15 HOH *61(H2 O) HELIX 1 AA1 THR H 28 SER H 32 5 5 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 SER H 127 LYS H 129 5 3 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 GLN L 79 PHE L 83 5 5 HELIX 7 AA7 SER L 121 LYS L 126 1 6 HELIX 8 AA8 LYS L 183 HIS L 189 1 7 HELIX 9 AA9 THR A 28 SER A 32 5 5 HELIX 10 AB1 ASP A 61 LYS A 64 5 4 HELIX 11 AB2 ARG 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 GLN A 192 1 6 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 GLY B 128 1 8 HELIX 18 AB9 LYS B 183 GLU B 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 68 O GLN H 81 SHEET 1 AA2 6 VAL H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ALA H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 LYS H 57 TYR H 59 -1 O TYR H 58 N ILE H 50 SHEET 1 AA3 4 VAL H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ALA H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 MET H 100H TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 GLY H 162 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 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 VAL H 211 -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 ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 VAL L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 LYS L 38 -1 N PHE L 36 O TYR L 87 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 VAL L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 4 GLN A 3 SER A 7 0 SHEET 2 AB3 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AB3 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AB3 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AB4 6 VAL A 11 VAL A 12 0 SHEET 2 AB4 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB4 6 ALA A 88 ALA A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB4 6 MET A 34 GLN A 39 -1 N HIS A 35 O VAL A 93 SHEET 5 AB4 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AB4 6 LYS A 57 TYR A 59 -1 O TYR A 58 N ILE A 50 SHEET 1 AB5 4 VAL A 11 VAL A 12 0 SHEET 2 AB5 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB5 4 ALA A 88 ALA A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB5 4 MET A 100H TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AB6 4 SER A 120 LEU A 124 0 SHEET 2 AB6 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AB6 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB6 4 HIS A 164 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB7 4 THR A 131 SER A 132 0 SHEET 2 AB7 4 THR A 135 TYR A 145 -1 O THR A 135 N SER A 132 SHEET 3 AB7 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB7 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB8 3 THR A 151 TRP A 154 0 SHEET 2 AB8 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB8 3 THR A 205 LYS A 210 -1 O LYS A 209 N CYS A 196 SHEET 1 AB9 4 MET B 4 SER B 7 0 SHEET 2 AB9 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 AB9 4 GLU B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB9 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AC1 6 THR B 10 ALA B 13 0 SHEET 2 AC1 6 THR B 102 VAL B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AC1 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AC1 6 LEU B 33 LYS B 38 -1 N PHE B 36 O TYR B 87 SHEET 5 AC1 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AC1 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AC2 4 THR B 10 ALA B 13 0 SHEET 2 AC2 4 THR B 102 VAL B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AC2 4 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AC2 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AC3 4 SER B 114 PHE B 118 0 SHEET 2 AC3 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AC3 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AC3 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AC4 4 ALA B 153 LEU B 154 0 SHEET 2 AC4 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AC4 4 VAL B 191 THR B 197 -1 O ALA B 193 N LYS B 149 SHEET 4 AC4 4 VAL B 205 ASN B 210 -1 O LYS B 207 N CYS B 194 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 5 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 6 CYS A 140 CYS A 196 1555 1555 2.04 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.05 SSBOND 8 CYS B 134 CYS B 194 1555 1555 2.03 CISPEP 1 PHE H 146 PRO H 147 0 -2.28 CISPEP 2 GLU H 148 PRO H 149 0 -0.04 CISPEP 3 SER L 7 PRO L 8 0 -3.03 CISPEP 4 TYR L 140 PRO L 141 0 2.03 CISPEP 5 PHE A 146 PRO A 147 0 -1.33 CISPEP 6 GLU A 148 PRO A 149 0 2.15 CISPEP 7 SER B 7 PRO B 8 0 -2.92 CISPEP 8 TYR B 140 PRO B 141 0 5.24 CRYST1 192.549 61.905 82.540 90.00 104.49 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 0.005193 0.000000 0.001342 0.00000 SCALE2 0.000000 0.016154 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012513 0.00000