HEADER VIRUS 24-APR-25 9OCO TITLE SIPV3-2E1 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: VP1; COMPND 3 CHAIN: 1; COMPND 4 SYNONYM: GENOME POLYPROTEIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VP2; COMPND 7 CHAIN: 2; COMPND 8 SYNONYM: GENOME POLYPROTEIN; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: VP3; COMPND 11 CHAIN: 3; COMPND 12 SYNONYM: GENOME POLYPROTEIN; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: VP4; COMPND 15 CHAIN: 4; COMPND 16 SYNONYM: GENOME POLYPROTEIN; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: 2E1 HEAVY CHAIN; COMPND 19 CHAIN: H; COMPND 20 MOL_ID: 6; COMPND 21 MOLECULE: 2E1 LIGHT CHAIN; COMPND 22 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: POLIOVIRUS 3; SOURCE 3 ORGANISM_TAXID: 12086; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: POLIOVIRUS 3; SOURCE 6 ORGANISM_TAXID: 12086; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: POLIOVIRUS 3; SOURCE 9 ORGANISM_TAXID: 12086; SOURCE 10 MOL_ID: 4; SOURCE 11 ORGANISM_SCIENTIFIC: POLIOVIRUS 3; SOURCE 12 ORGANISM_TAXID: 12086; SOURCE 13 MOL_ID: 5; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 MOL_ID: 6; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606 KEYWDS VIRUS, ANTIBODY, COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.T.WADDEY,S.L.HAFENSTEIN REVDAT 1 17-DEC-25 9OCO 0 JRNL AUTH B.T.WADDEY,A.J.CHARNESKY,J.E.FAUST,N.M.DINUNNO,S.H.CHO, JRNL AUTH 2 C.M.BATOR,S.DONG,K.MAHMOOD,K.M.CHUMAKOV,S.K.DESSAIN, JRNL AUTH 3 S.L.HAFENSTEIN JRNL TITL NEUTRALIZING HUMAN MONOCLONAL ANTIBODIES TO POLIOVIRUS MAP JRNL TITL 2 TO THE RECEPTOR BINDING SITE JRNL REF NAT COMMUN 2025 JRNL REFN ESSN 2041-1723 REMARK 2 REMARK 2 RESOLUTION. 2.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.950 REMARK 3 NUMBER OF PARTICLES : 237897 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 9OCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295321. 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 : SIPV3-2E1 COMPLEX 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 : 8.00 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 5600.00 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: 1, 2, 3, 4, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT2 2 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT3 2 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT1 3 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT2 3 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT3 3 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT1 4 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 4 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT3 4 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT1 5 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 5 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT3 5 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT1 6 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 6 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT3 6 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 8 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 8 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 8 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT1 9 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 9 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 9 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT1 10 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 10 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT3 10 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT1 11 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT2 11 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT3 11 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 12 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT2 12 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT3 12 0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 13 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 13 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 13 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT1 14 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT2 14 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 14 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 15 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT2 15 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 15 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 16 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT2 16 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 16 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 17 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 17 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 17 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 18 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 18 0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 18 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 19 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 19 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 19 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 20 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT2 20 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 20 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 21 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT2 21 0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 21 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT1 22 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 22 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 22 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 23 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 23 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 23 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT1 24 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 24 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 24 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT1 25 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT2 25 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 25 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT1 26 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 26 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT3 26 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 27 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT2 27 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 27 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 28 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT2 28 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 28 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 29 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT2 29 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 29 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT1 30 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT2 30 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 30 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT1 31 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 31 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT3 31 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 32 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 32 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT3 32 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT1 33 0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 33 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT3 33 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT1 34 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 34 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 34 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 35 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 35 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT3 35 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 36 0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT2 36 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT3 36 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 37 -0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT2 37 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT3 37 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 38 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 38 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 38 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 39 -0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 39 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT3 39 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 40 0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 40 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT3 40 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 41 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT2 41 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT3 41 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT1 42 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT2 42 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 42 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT1 43 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT2 43 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 43 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT1 44 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 44 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 44 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 45 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT2 45 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT3 45 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT1 46 -0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT2 46 0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT3 46 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 47 -0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT2 47 0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT3 47 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 48 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 48 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 48 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 49 0.809017 0.500000 0.309017 0.00000 REMARK 350 BIOMT2 49 -0.500000 0.309017 0.809017 0.00000 REMARK 350 BIOMT3 49 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT1 50 0.500000 -0.309017 0.809017 0.00000 REMARK 350 BIOMT2 50 -0.309017 0.809017 0.500000 0.00000 REMARK 350 BIOMT3 50 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT1 51 0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 51 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 51 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT1 52 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 52 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT3 52 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 53 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT2 53 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT3 53 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT1 54 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 54 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 54 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT1 55 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 55 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 55 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 56 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT2 56 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 56 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT1 57 0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 57 0.309017 -0.809017 0.500000 0.00000 REMARK 350 BIOMT3 57 -0.809017 -0.500000 -0.309017 0.00000 REMARK 350 BIOMT1 58 0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 58 -0.809017 -0.500000 0.309017 0.00000 REMARK 350 BIOMT3 58 -0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 59 -0.309017 -0.809017 -0.500000 0.00000 REMARK 350 BIOMT2 59 -0.809017 0.500000 -0.309017 0.00000 REMARK 350 BIOMT3 59 0.500000 0.309017 -0.809017 0.00000 REMARK 350 BIOMT1 60 -0.500000 -0.309017 -0.809017 0.00000 REMARK 350 BIOMT2 60 0.309017 0.809017 -0.500000 0.00000 REMARK 350 BIOMT3 60 0.809017 -0.500000 -0.309017 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY 1 3 REMARK 465 ILE 1 4 REMARK 465 GLU 1 5 REMARK 465 ASP 1 6 REMARK 465 LEU 1 7 REMARK 465 ILE 1 8 REMARK 465 SER 1 9 REMARK 465 GLU 1 10 REMARK 465 VAL 1 11 REMARK 465 ALA 1 12 REMARK 465 GLN 1 13 REMARK 465 GLY 1 14 REMARK 465 ALA 1 15 REMARK 465 LEU 1 16 REMARK 465 THR 1 17 REMARK 465 LEU 1 18 REMARK 465 SER 1 19 REMARK 465 LEU 1 20 REMARK 465 PRO 1 21 REMARK 465 LYS 1 22 REMARK 465 GLN 1 23 REMARK 465 GLN 1 24 REMARK 465 SER 2 1 REMARK 465 PRO 2 2 REMARK 465 ASN 2 3 REMARK 465 VAL 2 4 REMARK 465 GLU 2 5 REMARK 465 ALA 2 6 REMARK 465 CYS 2 7 REMARK 465 GLY 2 8 REMARK 465 GLN 2 271 REMARK 465 LEU 3 236 REMARK 465 PRO 3 237 REMARK 465 GLN 3 238 REMARK 465 SER 4 16 REMARK 465 ASN 4 17 REMARK 465 ARG 4 18 REMARK 465 ALA 4 19 REMARK 465 TYR 4 20 REMARK 465 GLY 4 21 REMARK 465 GLY 4 22 REMARK 465 SER 4 23 REMARK 465 ASN 4 69 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 OE1 GLN L 40 HH TYR L 42 1.59 REMARK 500 NH1 ARG 1 109 OD1 ASP 1 236 2.17 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 1 98 33.28 -141.77 REMARK 500 THR 1 111 148.27 -171.31 REMARK 500 ALA 1 204 144.53 -170.04 REMARK 500 ASP 1 248 -179.81 -69.10 REMARK 500 CYS 1 271 75.45 53.40 REMARK 500 ARG 1 288 -52.68 -122.49 REMARK 500 ASN 1 290 -64.10 -95.09 REMARK 500 TYR 2 35 18.73 56.87 REMARK 500 ASP 2 57 -102.81 61.12 REMARK 500 SER 2 104 149.02 -174.04 REMARK 500 CYS 2 112 118.22 -160.59 REMARK 500 ALA 2 239 45.43 -143.29 REMARK 500 PRO 3 137 -179.25 -67.13 REMARK 500 THR 3 196 -127.85 66.89 REMARK 500 ARG H 98 141.83 -171.07 REMARK 500 GLU L 56 -2.45 68.87 REMARK 500 ASP L 57 -14.47 75.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70320 RELATED DB: EMDB REMARK 900 SIPV3-2E1 COMPLEX DBREF 9OCO 1 3 302 UNP P03302 POLG_POL3L 579 878 DBREF 9OCO 2 1 271 UNP P03302 POLG_POL3L 70 340 DBREF 9OCO 3 1 238 UNP P03302 POLG_POL3L 341 578 DBREF 9OCO 4 2 69 UNP P03302 POLG_POL3L 2 69 DBREF 9OCO H 1 127 PDB 9OCO 9OCO 1 127 DBREF 9OCO L 1 127 PDB 9OCO 9OCO 1 127 SEQADV 9OCO ARG 1 288 UNP P03302 LYS 864 VARIANT SEQADV 9OCO PHE 3 91 UNP P03302 SER 431 VARIANT SEQRES 1 1 300 GLY ILE GLU ASP LEU ILE SER GLU VAL ALA GLN GLY ALA SEQRES 2 1 300 LEU THR LEU SER LEU PRO LYS GLN GLN ASP SER LEU PRO SEQRES 3 1 300 ASP THR LYS ALA SER GLY PRO ALA HIS SER LYS GLU VAL SEQRES 4 1 300 PRO ALA LEU THR ALA VAL GLU THR GLY ALA THR ASN PRO SEQRES 5 1 300 LEU ALA PRO SER ASP THR VAL GLN THR ARG HIS VAL VAL SEQRES 6 1 300 GLN ARG ARG SER ARG SER GLU SER THR ILE GLU SER PHE SEQRES 7 1 300 PHE ALA ARG GLY ALA CYS VAL ALA ILE ILE GLU VAL ASP SEQRES 8 1 300 ASN GLU GLN PRO THR THR ARG ALA GLN LYS LEU PHE ALA SEQRES 9 1 300 MET TRP ARG ILE THR TYR LYS ASP THR VAL GLN LEU ARG SEQRES 10 1 300 ARG LYS LEU GLU PHE PHE THR TYR SER ARG PHE ASP MET SEQRES 11 1 300 GLU PHE THR PHE VAL VAL THR ALA ASN PHE THR ASN ALA SEQRES 12 1 300 ASN ASN GLY HIS ALA LEU ASN GLN VAL TYR GLN ILE MET SEQRES 13 1 300 TYR ILE PRO PRO GLY ALA PRO THR PRO LYS SER TRP ASP SEQRES 14 1 300 ASP TYR THR TRP GLN THR SER SER ASN PRO SER ILE PHE SEQRES 15 1 300 TYR THR TYR GLY ALA ALA PRO ALA ARG ILE SER VAL PRO SEQRES 16 1 300 TYR VAL GLY LEU ALA ASN ALA TYR SER HIS PHE TYR ASP SEQRES 17 1 300 GLY PHE ALA LYS VAL PRO LEU LYS THR ASP ALA ASN ASP SEQRES 18 1 300 GLN ILE GLY ASP SER LEU TYR SER ALA MET THR VAL ASP SEQRES 19 1 300 ASP PHE GLY VAL LEU ALA VAL ARG VAL VAL ASN ASP HIS SEQRES 20 1 300 ASN PRO THR LYS VAL THR SER LYS VAL ARG ILE TYR MET SEQRES 21 1 300 LYS PRO LYS HIS VAL ARG VAL TRP CYS PRO ARG PRO PRO SEQRES 22 1 300 ARG ALA VAL PRO TYR TYR GLY PRO GLY VAL ASP TYR ARG SEQRES 23 1 300 ASN ASN LEU ASP PRO LEU SER GLU LYS GLY LEU THR THR SEQRES 24 1 300 TYR SEQRES 1 2 271 SER PRO ASN VAL GLU ALA CYS GLY TYR SER ASP ARG VAL SEQRES 2 2 271 LEU GLN LEU THR LEU GLY ASN SER THR ILE THR THR GLN SEQRES 3 2 271 GLU ALA ALA ASN SER VAL VAL ALA TYR GLY ARG TRP PRO SEQRES 4 2 271 GLU PHE ILE ARG ASP ASP GLU ALA ASN PRO VAL ASP GLN SEQRES 5 2 271 PRO THR GLU PRO ASP VAL ALA THR CYS ARG PHE TYR THR SEQRES 6 2 271 LEU ASP THR VAL MET TRP GLY LYS GLU SER LYS GLY TRP SEQRES 7 2 271 TRP TRP LYS LEU PRO ASP ALA LEU ARG ASP MET GLY LEU SEQRES 8 2 271 PHE GLY GLN ASN MET TYR TYR HIS TYR LEU GLY ARG SER SEQRES 9 2 271 GLY TYR THR VAL HIS VAL GLN CYS ASN ALA SER LYS PHE SEQRES 10 2 271 HIS GLN GLY ALA LEU GLY VAL PHE ALA ILE PRO GLU TYR SEQRES 11 2 271 CYS LEU ALA GLY ASP SER ASP LYS GLN ARG TYR THR SER SEQRES 12 2 271 TYR ALA ASN ALA ASN PRO GLY GLU ARG GLY GLY LYS PHE SEQRES 13 2 271 TYR SER GLN PHE ASN LYS ASP ASN ALA VAL THR SER PRO SEQRES 14 2 271 LYS ARG GLU PHE CYS PRO VAL ASP TYR LEU LEU GLY CYS SEQRES 15 2 271 GLY VAL LEU LEU GLY ASN ALA PHE VAL TYR PRO HIS GLN SEQRES 16 2 271 ILE ILE ASN LEU ARG THR ASN ASN SER ALA THR ILE VAL SEQRES 17 2 271 LEU PRO TYR VAL ASN ALA LEU ALA ILE ASP SER MET VAL SEQRES 18 2 271 LYS HIS ASN ASN TRP GLY ILE ALA ILE LEU PRO LEU SER SEQRES 19 2 271 PRO LEU ASP PHE ALA GLN ASP SER SER VAL GLU ILE PRO SEQRES 20 2 271 ILE THR VAL THR ILE ALA PRO MET CYS SER GLU PHE ASN SEQRES 21 2 271 GLY LEU ARG ASN VAL THR ALA PRO LYS PHE GLN SEQRES 1 3 238 GLY LEU PRO VAL LEU ASN THR PRO GLY SER ASN GLN TYR SEQRES 2 3 238 LEU THR SER ASP ASN HIS GLN SER PRO CYS ALA ILE PRO SEQRES 3 3 238 GLU PHE ASP VAL THR PRO PRO ILE ASP ILE PRO GLY GLU SEQRES 4 3 238 VAL LYS ASN MET MET GLU LEU ALA GLU ILE ASP THR MET SEQRES 5 3 238 ILE PRO LEU ASN LEU GLU SER THR LYS ARG ASN THR MET SEQRES 6 3 238 ASP MET TYR ARG VAL THR LEU SER ASP SER ALA ASP LEU SEQRES 7 3 238 SER GLN PRO ILE LEU CYS LEU SER LEU SER PRO ALA PHE SEQRES 8 3 238 ASP PRO ARG LEU SER HIS THR MET LEU GLY GLU VAL LEU SEQRES 9 3 238 ASN TYR TYR THR HIS TRP ALA GLY SER LEU LYS PHE THR SEQRES 10 3 238 PHE LEU PHE CYS GLY SER MET MET ALA THR GLY LYS ILE SEQRES 11 3 238 LEU VAL ALA TYR ALA PRO PRO GLY ALA GLN PRO PRO THR SEQRES 12 3 238 SER ARG LYS GLU ALA MET LEU GLY THR HIS VAL ILE TRP SEQRES 13 3 238 ASP LEU GLY LEU GLN SER SER CYS THR MET VAL VAL PRO SEQRES 14 3 238 TRP ILE SER ASN VAL THR TYR ARG GLN THR THR GLN ASP SEQRES 15 3 238 SER PHE THR GLU GLY GLY TYR ILE SER MET PHE TYR GLN SEQRES 16 3 238 THR ARG ILE VAL VAL PRO LEU SER THR PRO LYS SER MET SEQRES 17 3 238 SER MET LEU GLY PHE VAL SER ALA CYS ASN ASP PHE SER SEQRES 18 3 238 VAL ARG LEU LEU ARG ASP THR THR HIS ILE SER GLN SER SEQRES 19 3 238 ALA LEU PRO GLN SEQRES 1 4 68 GLY ALA GLN VAL SER SER GLN LYS VAL GLY ALA HIS GLU SEQRES 2 4 68 ASN SER ASN ARG ALA TYR GLY GLY SER THR ILE ASN TYR SEQRES 3 4 68 THR THR ILE ASN TYR TYR LYS ASP SER ALA SER ASN ALA SEQRES 4 4 68 ALA SER LYS GLN ASP TYR SER GLN ASP PRO SER LYS PHE SEQRES 5 4 68 THR GLU PRO LEU LYS ASP VAL LEU ILE LYS THR ALA PRO SEQRES 6 4 68 ALA LEU ASN SEQRES 1 H 127 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 127 SER GLY GLU SER LEU LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 127 TYR HIS PHE THR SER TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 H 127 MET PRO GLY LYS GLY LEU GLU TRP MET GLY PHE ILE TYR SEQRES 5 H 127 PRO GLY ASP SER ASP THR ARG TYR GLY PRO SER PHE GLN SEQRES 6 H 127 GLY GLN VAL SER ILE SER ALA ASP LYS SER SER SER THR SEQRES 7 H 127 ALA TYR LEU GLN TRP SER ARG LEU LYS ALA SER ASP THR SEQRES 8 H 127 ALA MET TYR PHE CYS ALA ARG HIS GLY GLY PHE ALA SER SEQRES 9 H 127 SER LEU TYR SER SER SER PHE ARG PRO PRO ASP TYR TRP SEQRES 10 H 127 GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 L 110 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 L 110 PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER SEQRES 3 L 110 GLY SER ILE ALA SER SER TYR VAL GLN TRP TYR GLN GLN SEQRES 4 L 110 ARG PRO GLY SER SER PRO THR THR VAL ILE TYR GLU ASP SEQRES 5 L 110 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 L 110 SER ILE ASP SER SER SER ASN SER ALA SER LEU ILE ILE SEQRES 7 L 110 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 L 110 GLN SER TYR ASP SER SER ASN GLN VAL PHE GLY GLY GLY SEQRES 9 L 110 THR LYS LEU THR VAL LEU HET PLM 12000 49 HETNAM PLM PALMITIC ACID FORMUL 7 PLM C16 H32 O2 HELIX 1 AA1 ALA 1 46 GLY 1 50 5 5 HELIX 2 AA2 ALA 1 56 THR 1 60 5 5 HELIX 3 AA3 ARG 1 72 SER 1 75 5 4 HELIX 4 AA4 THR 1 76 ALA 1 82 1 7 HELIX 5 AA5 VAL 1 116 GLU 1 123 1 8 HELIX 6 AA6 ASP 1 172 THR 1 177 5 6 HELIX 7 AA7 ASN 1 222 GLY 1 226 5 5 HELIX 8 AA8 TYR 2 35 ARG 2 37 5 3 HELIX 9 AA9 ARG 2 43 ALA 2 47 5 5 HELIX 10 AB1 PRO 2 56 THR 2 60 5 5 HELIX 11 AB2 PRO 2 83 ARG 2 87 5 5 HELIX 12 AB3 MET 2 89 HIS 2 99 1 11 HELIX 13 AB4 SER 2 143 ASN 2 148 1 6 HELIX 14 AB5 PRO 2 149 GLY 2 153 5 5 HELIX 15 AB6 VAL 2 176 LEU 2 180 5 5 HELIX 16 AB7 LEU 2 185 TYR 2 192 5 8 HELIX 17 AB8 MET 3 43 GLU 3 48 1 6 HELIX 18 AB9 THR 3 64 MET 3 67 5 4 HELIX 19 AC1 ASP 3 92 HIS 3 97 1 6 HELIX 20 AC2 THR 3 98 ASN 3 105 1 8 HELIX 21 AC3 SER 3 144 MET 3 149 1 6 HELIX 22 AC4 ASP 3 182 GLU 3 186 5 5 HELIX 23 AC5 ASP 4 35 ASN 4 39 5 5 HELIX 24 AC6 PRO 4 50 GLU 4 55 1 6 HELIX 25 AC7 HIS H 28 TYR H 32 5 5 HELIX 26 AC8 LYS H 87 THR H 91 5 5 HELIX 27 AC9 TYR H 107 PHE H 111 5 5 HELIX 28 AD1 LYS L 95 GLU L 99 5 5 SHEET 1 AA1 5 LEU 1 44 THR 1 45 0 SHEET 2 AA1 5 SER 3 163 VAL 3 168 -1 O SER 3 163 N THR 1 45 SHEET 3 AA1 5 LEU 3 114 PHE 3 120 -1 N LEU 3 114 O VAL 3 168 SHEET 4 AA1 5 SER 3 207 ALA 3 216 -1 O LEU 3 211 N LEU 3 119 SHEET 5 AA1 5 THR 3 51 MET 3 52 -1 N THR 3 51 O VAL 3 214 SHEET 1 AA2 5 LEU 1 44 THR 1 45 0 SHEET 2 AA2 5 SER 3 163 VAL 3 168 -1 O SER 3 163 N THR 1 45 SHEET 3 AA2 5 LEU 3 114 PHE 3 120 -1 N LEU 3 114 O VAL 3 168 SHEET 4 AA2 5 SER 3 207 ALA 3 216 -1 O LEU 3 211 N LEU 3 119 SHEET 5 AA2 5 ARG 3 69 SER 3 73 -1 N LEU 3 72 O MET 3 208 SHEET 1 AA3 4 ALA 1 85 ASN 1 94 0 SHEET 2 AA3 4 VAL 1 254 PRO 1 272 -1 O VAL 1 258 N ILE 1 90 SHEET 3 AA3 4 PHE 1 125 PHE 1 142 -1 N ASP 1 131 O LYS 1 265 SHEET 4 AA3 4 TYR 1 205 SER 1 206 -1 O TYR 1 205 N SER 1 128 SHEET 1 AA4 4 ALA 1 192 VAL 1 196 0 SHEET 2 AA4 4 PHE 1 125 PHE 1 142 -1 N MET 1 132 O VAL 1 196 SHEET 3 AA4 4 VAL 1 254 PRO 1 272 -1 O LYS 1 265 N ASP 1 131 SHEET 4 AA4 4 GLU 3 39 VAL 3 40 -1 O VAL 3 40 N VAL 1 269 SHEET 1 AA5 4 PHE 1 105 ARG 1 109 0 SHEET 2 AA5 4 VAL 1 240 VAL 1 245 -1 O LEU 1 241 N TRP 1 108 SHEET 3 AA5 4 VAL 1 154 ILE 1 160 -1 N MET 1 158 O ALA 1 242 SHEET 4 AA5 4 SER 1 182 THR 1 186 -1 O TYR 1 185 N TYR 1 155 SHEET 1 AA6 2 LEU 2 14 LEU 2 18 0 SHEET 2 AA6 2 SER 2 21 THR 2 25 -1 O ILE 2 23 N LEU 2 16 SHEET 1 AA7 5 ALA 2 28 VAL 2 33 0 SHEET 2 AA7 5 SER 2 204 LEU 2 209 1 O VAL 2 208 N VAL 2 32 SHEET 3 AA7 5 GLY 2 102 GLN 2 111 -1 N TYR 2 106 O LEU 2 209 SHEET 4 AA7 5 GLU 2 245 PHE 2 259 -1 O MET 2 255 N GLY 2 105 SHEET 5 AA7 5 TYR 2 64 THR 2 65 -1 N TYR 2 64 O ILE 2 252 SHEET 1 AA8 5 ALA 2 28 VAL 2 33 0 SHEET 2 AA8 5 SER 2 204 LEU 2 209 1 O VAL 2 208 N VAL 2 32 SHEET 3 AA8 5 GLY 2 102 GLN 2 111 -1 N TYR 2 106 O LEU 2 209 SHEET 4 AA8 5 GLU 2 245 PHE 2 259 -1 O MET 2 255 N GLY 2 105 SHEET 5 AA8 5 VAL 2 69 GLY 2 72 -1 N TRP 2 71 O ILE 2 246 SHEET 1 AA9 5 GLY 2 154 LYS 2 155 0 SHEET 2 AA9 5 TRP 2 78 LEU 2 82 -1 N TRP 2 79 O GLY 2 154 SHEET 3 AA9 5 TRP 2 226 ASP 2 237 -1 O ILE 2 228 N TRP 2 80 SHEET 4 AA9 5 GLN 2 119 PRO 2 128 -1 N GLY 2 123 O LEU 2 231 SHEET 5 AA9 5 HIS 2 194 ASN 2 198 -1 O GLN 2 195 N VAL 2 124 SHEET 1 AB1 4 LEU 3 83 SER 3 86 0 SHEET 2 AB1 4 TYR 3 189 VAL 3 199 -1 O ILE 3 190 N LEU 3 85 SHEET 3 AB1 4 THR 3 127 ALA 3 135 -1 N LEU 3 131 O PHE 3 193 SHEET 4 AB1 4 THR 3 152 ASP 3 157 -1 O THR 3 152 N TYR 3 134 SHEET 1 AB2 3 ARG 3 177 GLN 3 178 0 SHEET 2 AB2 3 HIS 3 109 ALA 3 111 -1 N TRP 3 110 O ARG 3 177 SHEET 3 AB2 3 SER 3 221 VAL 3 222 -1 O SER 3 221 N ALA 3 111 SHEET 1 AB3 2 GLN 4 4 SER 4 7 0 SHEET 2 AB3 2 ASN 4 26 THR 4 29 -1 O THR 4 29 N GLN 4 4 SHEET 1 AB4 4 GLN H 3 GLN H 6 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB4 4 THR H 78 TRP H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AB4 4 VAL H 68 ASP H 73 -1 N SER H 69 O GLN H 82 SHEET 1 AB5 5 GLU H 10 VAL H 11 0 SHEET 2 AB5 5 THR H 121 THR H 124 1 O LEU H 122 N GLU H 10 SHEET 3 AB5 5 MET H 93 ARG H 98 -1 N TYR H 94 O THR H 121 SHEET 4 AB5 5 ILE H 34 GLN H 39 -1 N VAL H 37 O PHE H 95 SHEET 5 AB5 5 GLU H 46 ILE H 51 -1 O ILE H 51 N ILE H 34 SHEET 1 AB6 4 GLU H 10 VAL H 11 0 SHEET 2 AB6 4 THR H 121 THR H 124 1 O LEU H 122 N GLU H 10 SHEET 3 AB6 4 MET H 93 ARG H 98 -1 N TYR H 94 O THR H 121 SHEET 4 AB6 4 TYR H 116 TRP H 117 -1 N TYR H 116 O ARG H 98 SHEET 1 AB7 4 LEU L 4 THR L 5 0 SHEET 2 AB7 4 THR L 18 ARG L 25 -1 O THR L 24 N THR L 5 SHEET 3 AB7 4 SER L 86 SER L 92 -1 O LEU L 89 N ILE L 21 SHEET 4 AB7 4 PHE L 76 ASP L 81 -1 N SER L 79 O SER L 88 SHEET 1 AB8 5 SER L 9 GLU L 13 0 SHEET 2 AB8 5 THR L 122 VAL L 126 1 O THR L 125 N GLU L 13 SHEET 3 AB8 5 ALA L 100 TYR L 103 -1 N TYR L 102 O THR L 122 SHEET 4 AB8 5 TRP L 41 GLN L 44 -1 N GLN L 44 O ASP L 101 SHEET 5 AB8 5 THR L 51 ILE L 54 -1 O ILE L 54 N TRP L 41 SHEET 1 AB9 2 GLN L 105 TYR L 107 0 SHEET 2 AB9 2 GLN L 116 PHE L 118 -1 O VAL L 117 N SER L 106 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 104 1555 1555 2.03 CISPEP 1 LEU 2 82 PRO 2 83 0 -0.92 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