HEADER VIRUS 11-MAR-25 9M7V TITLE CRYO-EM STRUCTURE OF ENTEROVIRUS A71 MATURE VIRION IN COMPLEX WITH FAB TITLE 2 CT11F9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: THE LIGHT CHAIN OF FAB CT11F9; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: THE HEAVY CHAIN OF FAB CT11F9; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CAPSID PROTEIN VP1; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: P1D,VIRION PROTEIN 1; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: CAPSID PROTEIN VP2; COMPND 15 CHAIN: B; COMPND 16 SYNONYM: P1B,VIRION PROTEIN 2; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: CAPSID PROTEIN VP3; COMPND 19 CHAIN: C; COMPND 20 SYNONYM: P1C,VIRION PROTEIN 3; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: CAPSID PROTEIN VP4; COMPND 23 CHAIN: D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: ENTEROVIRUS A71; SOURCE 13 ORGANISM_COMMON: EV71, EV-71; SOURCE 14 ORGANISM_TAXID: 39054; SOURCE 15 MOL_ID: 4; SOURCE 16 ORGANISM_SCIENTIFIC: ENTEROVIRUS A71; SOURCE 17 ORGANISM_COMMON: EV71, EV-71; SOURCE 18 ORGANISM_TAXID: 39054; SOURCE 19 MOL_ID: 5; SOURCE 20 ORGANISM_SCIENTIFIC: ENTEROVIRUS A71; SOURCE 21 ORGANISM_COMMON: EV71, EV-71; SOURCE 22 ORGANISM_TAXID: 39054; SOURCE 23 MOL_ID: 6; SOURCE 24 ORGANISM_SCIENTIFIC: ENTEROVIRUS A71; SOURCE 25 ORGANISM_COMMON: EV71, EV-71; SOURCE 26 ORGANISM_TAXID: 39054 KEYWDS VIRUS, ENTEROVIRUS A71 EXPDTA ELECTRON MICROSCOPY AUTHOR Y.JIANG,R.ZHU,Q.ZHENG,S.LI,N.XIA REVDAT 1 23-APR-25 9M7V 0 JRNL AUTH Y.JIANG,R.ZHU,Q.ZHENG,S.LI,N.XIA JRNL TITL DEVELOPMENT OF IN VITRO POTENCY METHODS TO REPLACE IN VIVO JRNL TITL 2 TESTS FOR ENTEROVIRUS 71 INACTIVATED VACCINE (HUMAN DIPLOID JRNL TITL 3 CELL-BASED/VERO CELL-BASED) JRNL REF VACCINES (BASEL) 2025 JRNL REFN ESSN 2076-393X REMARK 2 REMARK 2 RESOLUTION. 3.04 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.040 REMARK 3 NUMBER OF PARTICLES : 71798 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9M7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 14-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1300057289. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : ENTEROVIRUS A71 MATURE VIRION REMARK 245 IN COMPLEX WITH FAB CT11F9; REMARK 245 ENTEROVIRUS A71 MATURE VIRION; REMARK 245 FAB CT11F9 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TECNAI F30 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I). 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 APPLY THE FOLLOWING TO CHAINS: L, H, A, B, C, 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 350 BIOMT1 2 0.809017 -0.309017 0.500000 0.50000 REMARK 350 BIOMT2 2 -0.309017 0.500000 0.809017 0.80902 REMARK 350 BIOMT3 2 -0.500000 -0.809017 0.309017 575.30902 REMARK 350 BIOMT1 3 0.500000 -0.809017 0.309017 288.30902 REMARK 350 BIOMT2 3 -0.809017 -0.309017 0.500000 466.49379 REMARK 350 BIOMT3 3 -0.309017 -0.500000 -0.809017 752.18477 REMARK 350 BIOMT1 4 0.500000 -0.809017 -0.309017 465.68478 REMARK 350 BIOMT2 4 -0.809017 -0.309017 -0.500000 753.49379 REMARK 350 BIOMT3 4 0.309017 0.500000 -0.809017 286.19098 REMARK 350 BIOMT1 5 0.809017 -0.309017 -0.500000 287.50000 REMARK 350 BIOMT2 5 -0.309017 0.500000 -0.809017 465.18477 REMARK 350 BIOMT3 5 0.500000 0.809017 0.309017 -178.68478 REMARK 350 BIOMT1 6 -0.500000 -0.809017 0.309017 576.30902 REMARK 350 BIOMT2 6 -0.809017 0.309017 -0.500000 575.50000 REMARK 350 BIOMT3 6 0.309017 -0.500000 -0.809017 574.19098 REMARK 350 BIOMT1 7 -0.309017 -0.500000 -0.809017 753.18477 REMARK 350 BIOMT2 7 -0.500000 0.809017 -0.309017 287.69099 REMARK 350 BIOMT3 7 0.809017 0.309017 -0.500000 108.50621 REMARK 350 BIOMT1 8 0.309017 0.500000 -0.809017 287.19098 REMARK 350 BIOMT2 8 -0.500000 0.809017 0.309017 110.31523 REMARK 350 BIOMT3 8 0.809017 0.309017 0.500000 -178.49379 REMARK 350 BIOMT1 9 0.500000 0.809017 0.309017 -177.68477 REMARK 350 BIOMT2 9 -0.809017 0.309017 0.500000 288.50000 REMARK 350 BIOMT3 9 0.309017 -0.500000 0.809017 109.81523 REMARK 350 BIOMT1 10 0.000000 0.000000 1.000000 1.00000 REMARK 350 BIOMT2 10 -1.000000 0.000000 0.000000 576.00000 REMARK 350 BIOMT3 10 0.000000 -1.000000 0.000000 575.00000 REMARK 350 BIOMT1 11 0.309017 0.500000 -0.809017 287.19098 REMARK 350 BIOMT2 11 0.500000 -0.809017 -0.309017 465.68478 REMARK 350 BIOMT3 11 -0.809017 -0.309017 -0.500000 752.49379 REMARK 350 BIOMT1 12 0.500000 0.809017 0.309017 -177.68477 REMARK 350 BIOMT2 12 0.809017 -0.309017 -0.500000 287.50000 REMARK 350 BIOMT3 12 -0.309017 0.500000 -0.809017 464.18477 REMARK 350 BIOMT1 13 0.000000 0.000000 1.000000 1.00000 REMARK 350 BIOMT2 13 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 13 0.000000 1.000000 0.000000 -1.00000 REMARK 350 BIOMT1 14 -0.500000 -0.809017 0.309017 576.30902 REMARK 350 BIOMT2 14 0.809017 -0.309017 0.500000 0.50001 REMARK 350 BIOMT3 14 -0.309017 0.500000 0.809017 -0.19098 REMARK 350 BIOMT1 15 -0.309017 -0.500000 -0.809017 753.18477 REMARK 350 BIOMT2 15 0.500000 -0.809017 0.309017 288.30903 REMARK 350 BIOMT3 15 -0.809017 -0.309017 0.500000 465.49379 REMARK 350 BIOMT1 16 -0.809017 0.309017 0.500000 288.50000 REMARK 350 BIOMT2 16 0.309017 -0.500000 0.809017 110.81524 REMARK 350 BIOMT3 16 0.500000 0.809017 0.309017 -178.68478 REMARK 350 BIOMT1 17 -1.000000 0.000000 0.000000 576.00000 REMARK 350 BIOMT2 17 0.000000 -1.000000 0.000000 576.00001 REMARK 350 BIOMT3 17 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 18 -0.809017 0.309017 -0.500000 575.50000 REMARK 350 BIOMT2 18 0.309017 -0.500000 -0.809017 575.19099 REMARK 350 BIOMT3 18 -0.500000 -0.809017 0.309017 575.30902 REMARK 350 BIOMT1 19 -0.500000 0.809017 -0.309017 287.69098 REMARK 350 BIOMT2 19 0.809017 0.309017 -0.500000 109.50621 REMARK 350 BIOMT3 19 -0.309017 -0.500000 -0.809017 752.18477 REMARK 350 BIOMT1 20 -0.500000 0.809017 0.309017 110.31523 REMARK 350 BIOMT2 20 0.809017 0.309017 0.500000 -177.49379 REMARK 350 BIOMT3 20 0.309017 0.500000 -0.809017 286.19098 REMARK 350 BIOMT1 21 0.809017 0.309017 0.500000 -177.49379 REMARK 350 BIOMT2 21 -0.309017 -0.500000 0.809017 288.80902 REMARK 350 BIOMT3 21 0.500000 -0.809017 -0.309017 464.68477 REMARK 350 BIOMT1 22 0.309017 -0.500000 0.809017 110.81523 REMARK 350 BIOMT2 22 -0.500000 -0.809017 -0.309017 753.68478 REMARK 350 BIOMT3 22 0.809017 -0.309017 -0.500000 286.50000 REMARK 350 BIOMT1 23 0.000000 -1.000000 0.000000 576.00000 REMARK 350 BIOMT2 23 0.000000 0.000000 -1.000000 575.00000 REMARK 350 BIOMT3 23 1.000000 0.000000 0.000000 -1.00000 REMARK 350 BIOMT1 24 0.309017 -0.500000 -0.809017 575.19098 REMARK 350 BIOMT2 24 0.500000 0.809017 -0.309017 -0.30901 REMARK 350 BIOMT3 24 0.809017 -0.309017 0.500000 -0.50000 REMARK 350 BIOMT1 25 0.809017 0.309017 -0.500000 109.50621 REMARK 350 BIOMT2 25 0.309017 0.500000 0.809017 -177.18477 REMARK 350 BIOMT3 25 0.500000 -0.809017 0.309017 287.30902 REMARK 350 BIOMT1 26 -0.500000 -0.809017 -0.309017 753.68478 REMARK 350 BIOMT2 26 0.809017 -0.309017 -0.500000 287.50001 REMARK 350 BIOMT3 26 0.309017 -0.500000 0.809017 109.81523 REMARK 350 BIOMT1 27 0.000000 0.000000 -1.000000 575.00000 REMARK 350 BIOMT2 27 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 27 0.000000 -1.000000 0.000000 575.00000 REMARK 350 BIOMT1 28 0.500000 0.809017 -0.309017 -0.30902 REMARK 350 BIOMT2 28 0.809017 -0.309017 0.500000 0.50000 REMARK 350 BIOMT3 28 0.309017 -0.500000 -0.809017 574.19098 REMARK 350 BIOMT1 29 0.309017 0.500000 0.809017 -177.18477 REMARK 350 BIOMT2 29 0.500000 -0.809017 0.309017 288.30902 REMARK 350 BIOMT3 29 0.809017 0.309017 -0.500000 108.50621 REMARK 350 BIOMT1 30 -0.309017 -0.500000 0.809017 288.80902 REMARK 350 BIOMT2 30 0.500000 -0.809017 -0.309017 465.68478 REMARK 350 BIOMT3 30 0.809017 0.309017 0.500000 -178.49379 REMARK 350 BIOMT1 31 0.000000 0.000000 -1.000000 575.00000 REMARK 350 BIOMT2 31 -1.000000 0.000000 0.000000 576.00001 REMARK 350 BIOMT3 31 0.000000 1.000000 0.000000 -1.00001 REMARK 350 BIOMT1 32 0.500000 0.809017 -0.309017 -0.30902 REMARK 350 BIOMT2 32 -0.809017 0.309017 -0.500000 575.50000 REMARK 350 BIOMT3 32 -0.309017 0.500000 0.809017 -0.19099 REMARK 350 BIOMT1 33 0.309017 0.500000 0.809017 -177.18477 REMARK 350 BIOMT2 33 -0.500000 0.809017 -0.309017 287.69098 REMARK 350 BIOMT3 33 -0.809017 -0.309017 0.500000 465.49379 REMARK 350 BIOMT1 34 -0.309017 -0.500000 0.809017 288.80902 REMARK 350 BIOMT2 34 -0.500000 0.809017 0.309017 110.31523 REMARK 350 BIOMT3 34 -0.809017 -0.309017 -0.500000 752.49379 REMARK 350 BIOMT1 35 -0.500000 -0.809017 -0.309017 753.68478 REMARK 350 BIOMT2 35 -0.809017 0.309017 0.500000 288.50001 REMARK 350 BIOMT3 35 -0.309017 0.500000 -0.809017 464.18477 REMARK 350 BIOMT1 36 -0.309017 0.500000 0.809017 0.80902 REMARK 350 BIOMT2 36 0.500000 0.809017 -0.309017 -0.30902 REMARK 350 BIOMT3 36 -0.809017 0.309017 -0.500000 574.50000 REMARK 350 BIOMT1 37 -0.809017 -0.309017 0.500000 466.49379 REMARK 350 BIOMT2 37 0.309017 0.500000 0.809017 -177.18477 REMARK 350 BIOMT3 37 -0.500000 0.809017 -0.309017 286.69098 REMARK 350 BIOMT1 38 -0.809017 -0.309017 -0.500000 753.49379 REMARK 350 BIOMT2 38 -0.309017 -0.500000 0.809017 288.80903 REMARK 350 BIOMT3 38 -0.500000 0.809017 0.309017 109.31522 REMARK 350 BIOMT1 39 -0.309017 0.500000 -0.809017 465.18477 REMARK 350 BIOMT2 39 -0.500000 -0.809017 -0.309017 753.68478 REMARK 350 BIOMT3 39 -0.809017 0.309017 0.500000 287.50000 REMARK 350 BIOMT1 40 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 40 0.000000 0.000000 -1.000000 575.00000 REMARK 350 BIOMT3 40 -1.000000 0.000000 0.000000 575.00000 REMARK 350 BIOMT1 41 0.809017 -0.309017 0.500000 0.50000 REMARK 350 BIOMT2 41 0.309017 -0.500000 -0.809017 575.19099 REMARK 350 BIOMT3 41 0.500000 0.809017 -0.309017 -1.30902 REMARK 350 BIOMT1 42 0.500000 -0.809017 0.309017 288.30902 REMARK 350 BIOMT2 42 0.809017 0.309017 -0.500000 109.50621 REMARK 350 BIOMT3 42 0.309017 0.500000 0.809017 -178.18477 REMARK 350 BIOMT1 43 0.500000 -0.809017 -0.309017 465.68477 REMARK 350 BIOMT2 43 0.809017 0.309017 0.500000 -177.49378 REMARK 350 BIOMT3 43 -0.309017 -0.500000 0.809017 287.80902 REMARK 350 BIOMT1 44 0.809017 -0.309017 -0.500000 287.50000 REMARK 350 BIOMT2 44 0.309017 -0.500000 0.809017 110.81523 REMARK 350 BIOMT3 44 -0.500000 -0.809017 -0.309017 752.68477 REMARK 350 BIOMT1 45 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 45 0.000000 -1.000000 0.000000 576.00001 REMARK 350 BIOMT3 45 0.000000 0.000000 -1.000000 573.99999 REMARK 350 BIOMT1 46 0.000000 -1.000000 0.000000 576.00001 REMARK 350 BIOMT2 46 0.000000 0.000000 1.000000 1.00001 REMARK 350 BIOMT3 46 -1.000000 0.000000 0.000000 575.00000 REMARK 350 BIOMT1 47 0.309017 -0.500000 -0.809017 575.19099 REMARK 350 BIOMT2 47 -0.500000 -0.809017 0.309017 576.30902 REMARK 350 BIOMT3 47 -0.809017 0.309017 -0.500000 574.50000 REMARK 350 BIOMT1 48 0.809017 0.309017 -0.500000 109.50621 REMARK 350 BIOMT2 48 -0.309017 -0.500000 -0.809017 753.18478 REMARK 350 BIOMT3 48 -0.500000 0.809017 -0.309017 286.69098 REMARK 350 BIOMT1 49 0.809017 0.309017 0.500000 -177.49379 REMARK 350 BIOMT2 49 0.309017 0.500000 -0.809017 287.19098 REMARK 350 BIOMT3 49 -0.500000 0.809017 0.309017 109.31522 REMARK 350 BIOMT1 50 0.309017 -0.500000 0.809017 110.81523 REMARK 350 BIOMT2 50 0.500000 0.809017 0.309017 -177.68477 REMARK 350 BIOMT3 50 -0.809017 0.309017 0.500000 287.50000 REMARK 350 BIOMT1 51 -0.309017 0.500000 -0.809017 465.18477 REMARK 350 BIOMT2 51 0.500000 0.809017 0.309017 -177.68477 REMARK 350 BIOMT3 51 0.809017 -0.309017 -0.500000 286.50000 REMARK 350 BIOMT1 52 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 52 0.000000 0.000000 1.000000 1.00000 REMARK 350 BIOMT3 52 1.000000 0.000000 0.000000 -1.00000 REMARK 350 BIOMT1 53 -0.309017 0.500000 0.809017 0.80902 REMARK 350 BIOMT2 53 -0.500000 -0.809017 0.309017 576.30902 REMARK 350 BIOMT3 53 0.809017 -0.309017 0.500000 -0.50000 REMARK 350 BIOMT1 54 -0.809017 -0.309017 0.500000 466.49379 REMARK 350 BIOMT2 54 -0.309017 -0.500000 -0.809017 753.18478 REMARK 350 BIOMT3 54 0.500000 -0.809017 0.309017 287.30902 REMARK 350 BIOMT1 55 -0.809017 -0.309017 -0.500000 753.49379 REMARK 350 BIOMT2 55 0.309017 0.500000 -0.809017 287.19099 REMARK 350 BIOMT3 55 0.500000 -0.809017 -0.309017 464.68477 REMARK 350 BIOMT1 56 -0.500000 0.809017 0.309017 110.31523 REMARK 350 BIOMT2 56 -0.809017 -0.309017 -0.500000 753.49379 REMARK 350 BIOMT3 56 -0.309017 -0.500000 0.809017 287.80902 REMARK 350 BIOMT1 57 -0.809017 0.309017 0.500000 288.50000 REMARK 350 BIOMT2 57 -0.309017 0.500000 -0.809017 465.18477 REMARK 350 BIOMT3 57 -0.500000 -0.809017 -0.309017 752.68477 REMARK 350 BIOMT1 58 -1.000000 0.000000 0.000000 576.00000 REMARK 350 BIOMT2 58 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 58 0.000000 0.000000 -1.000000 574.00000 REMARK 350 BIOMT1 59 -0.809017 0.309017 -0.500000 575.50000 REMARK 350 BIOMT2 59 -0.309017 0.500000 0.809017 0.80902 REMARK 350 BIOMT3 59 0.500000 0.809017 -0.309017 -1.30902 REMARK 350 BIOMT1 60 -0.500000 0.809017 -0.309017 287.69098 REMARK 350 BIOMT2 60 -0.809017 -0.309017 0.500000 466.49380 REMARK 350 BIOMT3 60 0.309017 0.500000 0.809017 -178.18478 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 GLU L 104 REMARK 465 LEU L 105 REMARK 465 LYS L 106 REMARK 465 ASP H 1 REMARK 465 SER H 118 REMARK 465 SER H 119 REMARK 465 GLY A 1 REMARK 465 SER B 1 REMARK 465 PRO B 2 REMARK 465 SER B 3 REMARK 465 ALA B 4 REMARK 465 GLU B 5 REMARK 465 ALA B 6 REMARK 465 CYS B 7 REMARK 465 GLY B 8 REMARK 465 TYR B 9 REMARK 465 MET D 1 REMARK 465 GLY D 2 REMARK 465 SER D 3 REMARK 465 GLN D 4 REMARK 465 VAL D 5 REMARK 465 SER D 6 REMARK 465 THR D 7 REMARK 465 GLN D 8 REMARK 465 ARG D 9 REMARK 465 SER D 10 REMARK 465 GLY D 11 REMARK 465 SER D 12 REMARK 465 HIS D 13 REMARK 465 GLY D 22 REMARK 465 SER D 23 REMARK 465 THR D 24 REMARK 465 ILE D 25 REMARK 465 LYS D 69 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN L 1 CG CD OE1 NE2 REMARK 470 GLU L 17 CG CD OE1 OE2 REMARK 470 LYS L 44 CG CD CE NZ REMARK 470 GLU L 80 CG CD OE1 OE2 REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 GLN H 5 CG CD OE1 NE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 GLN H 16 CG CD OE1 NE2 REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 LYS H 82 CG CD CE NZ REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 ARG A 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 98 CG CD CE NZ REMARK 470 ASP B 11 CG OD1 OD2 REMARK 470 LYS B 149 CG CD CE NZ REMARK 470 GLN B 161 CG CD OE1 NE2 REMARK 470 GLN C 242 CG CD OE1 NE2 REMARK 470 GLU D 14 CG CD OE1 OE2 REMARK 470 GLU D 21 CG CD OE1 OE2 REMARK 470 ILE D 60 CG1 CG2 CD1 REMARK 470 PHE D 61 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU D 63 CG CD OE1 OE2 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 ASN D 15 OG SER D 36 2.13 REMARK 500 OD1 ASP A 81 NE2 GLN D 44 2.19 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 THR L 50 -9.21 70.80 REMARK 500 SER L 51 -36.49 -131.04 REMARK 500 ALA L 83 -168.77 -160.45 REMARK 500 TYR H 33 170.32 68.77 REMARK 500 ASP H 90 52.34 -90.87 REMARK 500 ALA A 26 75.24 -155.53 REMARK 500 THR A 173 50.86 38.55 REMARK 500 ILE A 262 77.80 53.58 REMARK 500 PRO A 277 47.55 -85.16 REMARK 500 ASN B 30 -177.11 67.47 REMARK 500 TYR B 35 15.07 59.08 REMARK 500 ASP B 57 -114.64 65.21 REMARK 500 PRO B 83 31.88 -92.62 REMARK 500 CYS B 112 116.43 -162.02 REMARK 500 ASP B 167 19.94 58.78 REMARK 500 ALA B 168 10.65 -140.53 REMARK 500 GLN C 76 -169.14 -126.43 REMARK 500 ASN C 201 172.77 178.05 REMARK 500 ALA C 219 -167.95 -161.28 REMARK 500 ASN D 55 70.77 -152.40 REMARK 500 PRO D 56 56.69 -95.81 REMARK 500 GLU D 63 39.76 -91.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63694 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF ENTEROVIRUS A71 MATURE VIRION IN COMPLEX WITH REMARK 900 FAB CT11F9 DBREF 9M7V L 1 106 PDB 9M7V 9M7V 1 106 DBREF 9M7V H 1 119 PDB 9M7V 9M7V 1 119 DBREF 9M7V A 1 297 UNP B9VUU3 POLG_HE71 566 862 DBREF 9M7V B 1 254 UNP B9VUU3 POLG_HE71 70 323 DBREF 9M7V C 1 242 UNP B9VUU3 POLG_HE71 324 565 DBREF 9M7V D 1 69 UNP B9VUU3 POLG_HE71 1 69 SEQADV 9M7V HIS A 22 UNP B9VUU3 GLN 587 CONFLICT SEQADV 9M7V ASP A 31 UNP B9VUU3 ASN 596 CONFLICT SEQADV 9M7V LYS A 98 UNP B9VUU3 GLU 663 CONFLICT SEQRES 1 L 106 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 L 106 SER PRO GLY GLU LYS VAL THR ILE SER CYS SER ALA SER SEQRES 3 L 106 SER SER VAL ARG TYR MET TYR TRP TYR GLN GLN LYS PRO SEQRES 4 L 106 GLY SER ALA PRO LYS PRO TRP ILE TYR ARG THR SER ASN SEQRES 5 L 106 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 106 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 106 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TYR HIS SEQRES 8 L 106 SER TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 L 106 LEU LYS SEQRES 1 H 119 ASP VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 119 PRO SER GLN SER LEU SER LEU THR CYS SER VAL THR GLY SEQRES 3 H 119 TYR SER ILE THR SER GLY TYR TYR TRP ASN TRP ILE ARG SEQRES 4 H 119 GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE SEQRES 5 H 119 ASN TYR GLY GLY SER ASN PHE TYR ASN PRO SER LEU LYS SEQRES 6 H 119 ASN ARG ILE SER ILE THR ARG ASP THR SER ARG ASN GLN SEQRES 7 H 119 PHE PHE LEU LYS LEU ASN SER VAL THR THR GLU ASP THR SEQRES 8 H 119 ALA THR TYR TYR CYS ALA ARG GLY GLY TYR TYR ASP TYR SEQRES 9 H 119 ASP GLY ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 119 SER SER SEQRES 1 A 297 GLY ASP ARG VAL ALA ASP VAL ILE GLU SER SER ILE GLY SEQRES 2 A 297 ASP SER VAL SER ARG ALA LEU THR HIS ALA LEU PRO ALA SEQRES 3 A 297 PRO THR GLY GLN ASP THR GLN VAL SER SER HIS ARG LEU SEQRES 4 A 297 ASP THR GLY LYS VAL PRO ALA LEU GLN ALA ALA GLU ILE SEQRES 5 A 297 GLY ALA SER SER ASN ALA SER ASP GLU SER MET ILE GLU SEQRES 6 A 297 THR ARG CYS VAL LEU ASN SER HIS SER THR ALA GLU THR SEQRES 7 A 297 THR LEU ASP SER PHE PHE SER ARG ALA GLY LEU VAL GLY SEQRES 8 A 297 GLU ILE ASP LEU PRO LEU LYS GLY THR THR ASN PRO ASN SEQRES 9 A 297 GLY TYR ALA ASN TRP ASP ILE ASP ILE THR GLY TYR ALA SEQRES 10 A 297 GLN MET ARG ARG LYS VAL GLU LEU PHE THR TYR MET ARG SEQRES 11 A 297 PHE ASP ALA GLU PHE THR PHE VAL ALA CYS THR PRO THR SEQRES 12 A 297 GLY GLU VAL VAL PRO GLN LEU LEU GLN TYR MET PHE VAL SEQRES 13 A 297 PRO PRO GLY ALA PRO LYS PRO ASP SER ARG GLU SER LEU SEQRES 14 A 297 ALA TRP GLN THR ALA THR ASN PRO SER VAL PHE VAL LYS SEQRES 15 A 297 LEU SER ASP PRO PRO ALA GLN VAL SER VAL PRO PHE MET SEQRES 16 A 297 SER PRO ALA SER ALA TYR GLN TRP PHE TYR ASP GLY TYR SEQRES 17 A 297 PRO THR PHE GLY GLU HIS LYS GLN GLU LYS ASP LEU GLU SEQRES 18 A 297 TYR GLY ALA CYS PRO ASN ASN MET MET GLY THR PHE SER SEQRES 19 A 297 VAL ARG THR VAL GLY THR SER LYS SER LYS TYR PRO LEU SEQRES 20 A 297 VAL VAL ARG ILE TYR MET ARG MET LYS HIS VAL ARG ALA SEQRES 21 A 297 TRP ILE PRO ARG PRO MET ARG ASN GLN ASN TYR LEU PHE SEQRES 22 A 297 LYS ALA ASN PRO ASN TYR ALA GLY ASN SER ILE LYS PRO SEQRES 23 A 297 THR GLY THR SER ARG THR ALA ILE THR THR LEU SEQRES 1 B 254 SER PRO SER ALA GLU ALA CYS GLY TYR SER ASP ARG VAL SEQRES 2 B 254 ALA GLN LEU THR ILE GLY ASN SER THR ILE THR THR GLN SEQRES 3 B 254 GLU ALA ALA ASN ILE ILE VAL GLY TYR GLY GLU TRP PRO SEQRES 4 B 254 SER TYR CYS SER ASP SER ASP ALA THR ALA VAL ASP LYS SEQRES 5 B 254 PRO THR ARG PRO ASP VAL SER VAL ASN ARG PHE TYR THR SEQRES 6 B 254 LEU ASP THR LYS LEU TRP GLU LYS SER SER LYS GLY TRP SEQRES 7 B 254 TYR TRP LYS PHE PRO ASP VAL LEU THR GLU THR GLY VAL SEQRES 8 B 254 PHE GLY GLN ASN ALA GLN PHE HIS TYR LEU TYR ARG SER SEQRES 9 B 254 GLY PHE CYS ILE HIS VAL GLN CYS ASN ALA SER LYS PHE SEQRES 10 B 254 HIS GLN GLY ALA LEU LEU VAL ALA VAL LEU PRO GLU TYR SEQRES 11 B 254 VAL ILE GLY THR VAL ALA GLY GLY THR GLY THR GLU ASP SEQRES 12 B 254 SER HIS PRO PRO TYR LYS GLN THR GLN PRO GLY ALA ASP SEQRES 13 B 254 GLY PHE GLU LEU GLN HIS PRO TYR VAL LEU ASP ALA GLY SEQRES 14 B 254 ILE PRO ILE SER GLN LEU THR VAL CYS PRO HIS GLN TRP SEQRES 15 B 254 ILE ASN LEU ARG THR ASN ASN CYS ALA THR ILE ILE VAL SEQRES 16 B 254 PRO TYR ILE ASN ALA LEU PRO PHE ASP SER ALA LEU ASN SEQRES 17 B 254 HIS CYS ASN PHE GLY LEU LEU VAL VAL PRO ILE SER PRO SEQRES 18 B 254 LEU ASP TYR ASP GLN GLY ALA THR PRO VAL ILE PRO ILE SEQRES 19 B 254 THR ILE THR LEU ALA PRO MET CYS SER GLU PHE ALA GLY SEQRES 20 B 254 LEU ARG GLN ALA VAL THR GLN SEQRES 1 C 242 GLY PHE PRO THR GLU LEU LYS PRO GLY THR ASN GLN PHE SEQRES 2 C 242 LEU THR THR ASP ASP GLY VAL SER ALA PRO ILE LEU PRO SEQRES 3 C 242 ASN PHE HIS PRO THR PRO CYS ILE HIS ILE PRO GLY GLU SEQRES 4 C 242 VAL ARG ASN LEU LEU GLU LEU CYS GLN VAL GLU THR ILE SEQRES 5 C 242 LEU GLU VAL ASN ASN VAL PRO THR ASN ALA THR SER LEU SEQRES 6 C 242 MET GLU ARG LEU ARG PHE PRO VAL SER ALA GLN ALA GLY SEQRES 7 C 242 LYS GLY GLU LEU CYS ALA VAL PHE ARG ALA ASP PRO GLY SEQRES 8 C 242 ARG ASN GLY PRO TRP GLN SER THR LEU LEU GLY GLN LEU SEQRES 9 C 242 CYS GLY TYR TYR THR GLN TRP SER GLY SER LEU GLU VAL SEQRES 10 C 242 THR PHE MET PHE THR GLY SER PHE MET ALA THR GLY LYS SEQRES 11 C 242 MET LEU ILE ALA TYR THR PRO PRO GLY GLY PRO LEU PRO SEQRES 12 C 242 LYS ASP ARG ALA THR ALA MET LEU GLY THR HIS VAL ILE SEQRES 13 C 242 TRP ASP PHE GLY LEU GLN SER SER VAL THR LEU VAL ILE SEQRES 14 C 242 PRO TRP ILE SER ASN THR HIS TYR ARG ALA HIS ALA ARG SEQRES 15 C 242 ASP GLY VAL PHE ASP TYR TYR THR THR GLY LEU VAL SER SEQRES 16 C 242 ILE TRP TYR GLN THR ASN TYR VAL VAL PRO ILE GLY ALA SEQRES 17 C 242 PRO ASN THR ALA TYR ILE ILE ALA LEU ALA ALA ALA GLN SEQRES 18 C 242 LYS ASN PHE THR MET LYS LEU CYS LYS ASP ALA SER ASP SEQRES 19 C 242 ILE LEU GLN THR GLY THR ILE GLN SEQRES 1 D 69 MET GLY SER GLN VAL SER THR GLN ARG SER GLY SER HIS SEQRES 2 D 69 GLU ASN SER ASN SER ALA THR GLU GLY SER THR ILE ASN SEQRES 3 D 69 TYR THR THR ILE ASN TYR TYR LYS ASP SER TYR ALA ALA SEQRES 4 D 69 THR ALA GLY LYS GLN SER LEU LYS GLN ASP PRO ASP LYS SEQRES 5 D 69 PHE ALA ASN PRO VAL LYS ASP ILE PHE THR GLU MET ALA SEQRES 6 D 69 ALA PRO LEU LYS HET SPH A 301 21 HETNAM SPH SPHINGOSINE FORMUL 7 SPH C18 H37 N O2 HELIX 1 AA1 PRO H 62 LYS H 65 5 4 HELIX 2 AA2 VAL A 4 GLU A 9 1 6 HELIX 3 AA3 ALA A 49 GLY A 53 5 5 HELIX 4 AA4 THR A 75 THR A 78 5 4 HELIX 5 AA5 THR A 79 SER A 85 1 7 HELIX 6 AA6 TYR A 116 GLU A 124 1 9 HELIX 7 AA7 SER A 168 THR A 173 5 6 HELIX 8 AA8 LYS A 215 TYR A 222 5 8 HELIX 9 AA9 CYS A 225 MET A 229 5 5 HELIX 10 AB1 TYR B 35 GLU B 37 5 3 HELIX 11 AB2 PRO B 56 VAL B 60 5 5 HELIX 12 AB3 PRO B 83 THR B 87 5 5 HELIX 13 AB4 THR B 89 PHE B 98 1 10 HELIX 14 AB5 PRO B 147 GLN B 152 1 6 HELIX 15 AB6 PRO B 153 GLY B 157 5 5 HELIX 16 AB7 HIS B 162 LEU B 166 5 5 HELIX 17 AB8 PRO B 171 CYS B 178 5 8 HELIX 18 AB9 ASN C 42 VAL C 49 5 8 HELIX 19 AC1 ASN C 61 ARG C 70 5 10 HELIX 20 AC2 GLY C 94 SER C 98 5 5 HELIX 21 AC3 THR C 99 GLY C 106 1 8 HELIX 22 AC4 ASP C 145 MET C 150 1 6 HELIX 23 AC5 GLY C 184 THR C 190 5 7 HELIX 24 AC6 ASP D 35 ALA D 39 5 5 HELIX 25 AC7 PRO D 50 ASN D 55 1 6 SHEET 1 AA1 4 LEU L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O SER L 24 N THR L 5 SHEET 3 AA1 4 SER L 69 ILE L 74 -1 O LEU L 72 N ILE L 21 SHEET 4 AA1 4 PHE L 61 SER L 66 -1 N SER L 64 O SER L 71 SHEET 1 AA2 5 ASN L 52 LEU L 53 0 SHEET 2 AA2 5 LYS L 44 TYR L 48 -1 N TYR L 48 O ASN L 52 SHEET 3 AA2 5 TYR L 33 GLN L 37 -1 N TRP L 34 O ILE L 47 SHEET 4 AA2 5 THR L 84 GLN L 88 -1 O GLN L 88 N TYR L 33 SHEET 5 AA2 5 THR L 101 LYS L 102 -1 O THR L 101 N TYR L 85 SHEET 1 AA3 4 GLN H 3 SER H 7 0 SHEET 2 AA3 4 LEU H 18 THR H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA3 4 GLN H 78 LEU H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AA3 4 ILE H 68 ASP H 73 -1 N ASP H 73 O GLN H 78 SHEET 1 AA4 5 ASN H 58 TYR H 60 0 SHEET 2 AA4 5 LEU H 46 ILE H 52 -1 N TYR H 51 O PHE H 59 SHEET 3 AA4 5 TYR H 34 GLN H 40 -1 N TRP H 37 O MET H 49 SHEET 4 AA4 5 THR H 93 GLY H 99 -1 O TYR H 95 N ILE H 38 SHEET 5 AA4 5 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AA5 5 ASN H 58 TYR H 60 0 SHEET 2 AA5 5 LEU H 46 ILE H 52 -1 N TYR H 51 O PHE H 59 SHEET 3 AA5 5 TYR H 34 GLN H 40 -1 N TRP H 37 O MET H 49 SHEET 4 AA5 5 THR H 93 GLY H 99 -1 O TYR H 95 N ILE H 38 SHEET 5 AA5 5 THR H 113 THR H 114 -1 O THR H 113 N TYR H 94 SHEET 1 AA6 2 LEU A 24 PRO A 25 0 SHEET 2 AA6 2 LYS D 47 GLN D 48 -1 O GLN D 48 N LEU A 24 SHEET 1 AA7 5 LEU A 47 GLN A 48 0 SHEET 2 AA7 5 SER C 164 ILE C 169 -1 O SER C 164 N GLN A 48 SHEET 3 AA7 5 LEU C 115 PHE C 121 -1 N VAL C 117 O LEU C 167 SHEET 4 AA7 5 THR C 211 ALA C 220 -1 O LEU C 217 N THR C 118 SHEET 5 AA7 5 THR C 51 ILE C 52 -1 N THR C 51 O ALA C 218 SHEET 1 AA8 5 LEU A 47 GLN A 48 0 SHEET 2 AA8 5 SER C 164 ILE C 169 -1 O SER C 164 N GLN A 48 SHEET 3 AA8 5 LEU C 115 PHE C 121 -1 N VAL C 117 O LEU C 167 SHEET 4 AA8 5 THR C 211 ALA C 220 -1 O LEU C 217 N THR C 118 SHEET 5 AA8 5 PHE C 71 SER C 74 -1 N VAL C 73 O ALA C 212 SHEET 1 AA9 5 GLY A 88 LEU A 95 0 SHEET 2 AA9 5 LEU A 247 PRO A 263 -1 O VAL A 249 N ILE A 93 SHEET 3 AA9 5 PHE A 126 CYS A 140 -1 N ASP A 132 O LYS A 256 SHEET 4 AA9 5 ALA A 188 VAL A 192 -1 O VAL A 192 N ALA A 133 SHEET 5 AA9 5 ALA C 22 PRO C 23 1 O ALA C 22 N SER A 191 SHEET 1 AB1 4 TYR A 201 GLN A 202 0 SHEET 2 AB1 4 PHE A 126 CYS A 140 -1 N MET A 129 O TYR A 201 SHEET 3 AB1 4 LEU A 247 PRO A 263 -1 O LYS A 256 N ASP A 132 SHEET 4 AB1 4 GLU C 39 VAL C 40 -1 O VAL C 40 N ALA A 260 SHEET 1 AB2 4 TYR A 106 ASP A 110 0 SHEET 2 AB2 4 THR A 232 THR A 237 -1 O PHE A 233 N TRP A 109 SHEET 3 AB2 4 LEU A 150 VAL A 156 -1 N VAL A 156 O THR A 232 SHEET 4 AB2 4 SER A 178 LYS A 182 -1 O VAL A 181 N LEU A 151 SHEET 1 AB3 2 ALA B 14 ILE B 18 0 SHEET 2 AB3 2 SER B 21 THR B 25 -1 O ILE B 23 N LEU B 16 SHEET 1 AB4 5 ILE B 32 VAL B 33 0 SHEET 2 AB4 5 CYS B 190 VAL B 195 1 O ILE B 194 N ILE B 32 SHEET 3 AB4 5 HIS B 99 GLN B 111 -1 N ILE B 108 O ILE B 193 SHEET 4 AB4 5 ILE B 232 LEU B 248 -1 O MET B 241 N GLY B 105 SHEET 5 AB4 5 TYR B 64 TRP B 71 -1 N TYR B 64 O LEU B 238 SHEET 1 AB5 5 PHE B 158 GLU B 159 0 SHEET 2 AB5 5 TRP B 78 PHE B 82 -1 N TYR B 79 O PHE B 158 SHEET 3 AB5 5 PHE B 212 ASP B 223 -1 O PHE B 212 N PHE B 82 SHEET 4 AB5 5 GLN B 119 PRO B 128 -1 N ALA B 125 O LEU B 215 SHEET 5 AB5 5 HIS B 180 ASN B 184 -1 O GLN B 181 N VAL B 124 SHEET 1 AB6 4 LEU C 82 ARG C 87 0 SHEET 2 AB6 4 LEU C 193 VAL C 203 -1 O ILE C 196 N CYS C 83 SHEET 3 AB6 4 THR C 128 THR C 136 -1 N LEU C 132 O TRP C 197 SHEET 4 AB6 4 THR C 153 ASP C 158 -1 O THR C 153 N TYR C 135 SHEET 1 AB7 3 ARG C 178 ALA C 179 0 SHEET 2 AB7 3 TYR C 108 SER C 112 -1 N TRP C 111 O ARG C 178 SHEET 3 AB7 3 THR C 225 CYS C 229 -1 O THR C 225 N SER C 112 SSBOND 1 CYS L 23 CYS L 87 1555 1555 2.04 CISPEP 1 SER L 7 PRO L 8 0 -2.42 CISPEP 2 TYR L 93 PRO L 94 0 1.12 CISPEP 3 PHE B 82 PRO B 83 0 -1.16 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000