HEADER VIRUS 19-MAY-23 8JG5 TITLE CRYO-EM STRUCTURE OF THE GI.4 CHIBA VLP COMPLEXED WITH THE CV-1A1 FV- TITLE 2 CLASP COMPND MOL_ID: 1; COMPND 2 MOLECULE: VP1; COMPND 3 CHAIN: A, B, G; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: GENBANK ID AB042808; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VH,SARAH; COMPND 8 CHAIN: C, E; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: VH-SARAH CHIMERA OF LINKER (RESIDUES (-6)-0), VH COMPND 11 (RESIDUES 1-118), AND SARAH (RESIDUES 119-171); COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: VL,SARAH; COMPND 14 CHAIN: D, F; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: VL-SARAH CHIMERA OF LINKER (RESIDUES (-6)-0), VL COMPND 17 (RESIDUES 1-112), AND SARAH (RESIDUES 113-162) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOROVIRUS; SOURCE 3 ORGANISM_TAXID: 142786; SOURCE 4 GENE: ORF2; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NOROVIRUS, GI.4, VIRUS LIKE PARTICLE, HUMAN MONOCLONAL ANTIBODY, FV- KEYWDS 2 CLASP, VIRUS EXPDTA ELECTRON MICROSCOPY AUTHOR T.HOSAKA,K.KATSURA,T.KIMURA-SOMEYA,Y.SOMEYA,M.SHIROUZU REVDAT 1 17-APR-24 8JG5 0 JRNL AUTH T.KIMURA-SOMEYA,K.KATSURA,M.KATO-MURAYAMA,T.HOSAKA, JRNL AUTH 2 T.UCHIKUBO-KAMO,K.IHARA,K.HANADA,K.MURAYAMA,M.SHIROUZU, JRNL AUTH 3 Y.SOMEYA JRNL TITL STRUCTURAL ANALYSES OF THE GI.4 NOROVIRUS BY CRYO-ELECTRON JRNL TITL 2 MICROSCOPY AND X-RAY CRYSTALLOGRAPHY REVEAL BINDING SITES JRNL TITL 3 FOR HUMAN MONOCLONAL ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN 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 : 47125 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 8JG5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-23. REMARK 100 THE DEPOSITION ID IS D_1300037614. 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 : VIRAL PROTEIN 1 WITH ITS REMARK 245 ANTIBODY FRAGMENTS 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 : FEI TECNAI ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 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) : 5000.00 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) : 200 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: A, B, C, D, E, F, 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 BIOMT1 2 0.809011 0.500008 0.309020 -227.12922 REMARK 350 BIOMT2 2 -0.500008 0.309017 0.809012 140.37703 REMARK 350 BIOMT3 2 0.309020 -0.809012 0.500006 367.49508 REMARK 350 BIOMT1 3 0.499985 0.309022 0.809025 -227.12643 REMARK 350 BIOMT2 3 -0.309022 -0.809017 0.499997 594.63029 REMARK 350 BIOMT3 3 0.809025 -0.499997 -0.309002 367.49056 REMARK 350 BIOMT1 4 0.499985 -0.309022 0.809025 0.00452 REMARK 350 BIOMT2 4 0.309022 -0.809017 -0.499997 734.99722 REMARK 350 BIOMT3 4 0.809025 0.499997 -0.309002 -0.00731 REMARK 350 BIOMT1 5 0.809011 -0.500008 0.309020 140.37637 REMARK 350 BIOMT2 5 0.500008 0.309017 -0.809012 367.49549 REMARK 350 BIOMT3 5 0.309020 0.809012 0.500006 -227.12897 REMARK 350 BIOMT1 6 -0.500015 -0.309012 0.809009 367.50665 REMARK 350 BIOMT2 6 -0.309012 -0.809017 -0.500003 962.12684 REMARK 350 BIOMT3 6 0.809009 -0.500003 0.309032 140.37078 REMARK 350 BIOMT1 7 -0.000009 -1.000000 0.000000 735.00345 REMARK 350 BIOMT2 7 0.000009 0.000000 -1.000000 734.99655 REMARK 350 BIOMT3 7 1.000000 -0.000009 0.000009 0.00000 REMARK 350 BIOMT1 8 0.500000 -0.309022 -0.809015 594.62855 REMARK 350 BIOMT2 8 -0.309012 0.809017 -0.500003 367.49934 REMARK 350 BIOMT3 8 0.809019 0.499997 0.309017 -227.12708 REMARK 350 BIOMT1 9 0.309017 0.809014 -0.500005 140.37530 REMARK 350 BIOMT2 9 -0.809020 0.500000 0.309009 367.50386 REMARK 350 BIOMT3 9 0.499995 0.309025 0.809017 -227.12856 REMARK 350 BIOMT1 10 -0.309026 0.809020 0.499989 0.00624 REMARK 350 BIOMT2 10 -0.809020 -0.500000 0.309009 735.00387 REMARK 350 BIOMT3 10 0.499989 -0.309009 0.809026 -0.00238 REMARK 350 BIOMT1 11 0.309026 0.809020 -0.499989 140.36412 REMARK 350 BIOMT2 11 0.809020 -0.500000 -0.309009 367.49614 REMARK 350 BIOMT3 11 -0.499989 -0.309009 -0.809026 962.12429 REMARK 350 BIOMT1 12 -0.309017 0.809014 0.500005 -0.00067 REMARK 350 BIOMT2 12 0.809020 0.500000 -0.309009 -0.00386 REMARK 350 BIOMT3 12 -0.499995 0.309025 -0.809017 734.99548 REMARK 350 BIOMT1 13 -0.500000 -0.309022 0.809015 367.50238 REMARK 350 BIOMT2 13 0.309012 0.809017 0.500003 -227.12683 REMARK 350 BIOMT3 13 -0.809019 0.499997 -0.309017 594.62921 REMARK 350 BIOMT1 14 0.000009 -1.000000 0.000000 734.99655 REMARK 350 BIOMT2 14 -0.000009 0.000000 1.000000 0.00345 REMARK 350 BIOMT3 14 -1.000000 -0.000009 -0.000009 735.00690 REMARK 350 BIOMT1 15 0.500015 -0.309012 -0.809009 594.61738 REMARK 350 BIOMT2 15 0.309012 -0.809017 0.500003 367.50066 REMARK 350 BIOMT3 15 -0.809009 -0.500003 -0.309032 962.13135 REMARK 350 BIOMT1 16 -0.809011 -0.500008 -0.309020 962.12921 REMARK 350 BIOMT2 16 -0.500008 0.309017 0.809012 140.37703 REMARK 350 BIOMT3 16 -0.309020 0.809012 -0.500006 367.50492 REMARK 350 BIOMT1 17 -0.499985 -0.309022 -0.809025 962.12642 REMARK 350 BIOMT2 17 -0.309022 -0.809017 0.499997 594.63029 REMARK 350 BIOMT3 17 -0.809025 0.499997 0.309002 367.50944 REMARK 350 BIOMT1 18 -0.499985 0.309022 -0.809025 734.99547 REMARK 350 BIOMT2 18 0.309022 -0.809017 -0.499997 734.99721 REMARK 350 BIOMT3 18 -0.809025 -0.499997 0.309002 735.00731 REMARK 350 BIOMT1 19 -0.809011 0.500008 -0.309020 594.62362 REMARK 350 BIOMT2 19 0.500008 0.309017 -0.809012 367.49548 REMARK 350 BIOMT3 19 -0.309020 -0.809012 -0.500006 962.12897 REMARK 350 BIOMT1 20 -1.000000 0.000000 0.000000 734.99999 REMARK 350 BIOMT2 20 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 20 0.000000 0.000000 -1.000000 735.00000 REMARK 350 BIOMT1 21 -0.000009 1.000000 0.000000 0.00345 REMARK 350 BIOMT2 21 -0.000009 0.000000 1.000000 0.00346 REMARK 350 BIOMT3 21 1.000000 0.000009 0.000009 -0.00690 REMARK 350 BIOMT1 22 -0.500015 0.309012 0.809009 140.38261 REMARK 350 BIOMT2 22 0.309012 -0.809017 0.500003 367.50067 REMARK 350 BIOMT3 22 0.809009 0.500003 0.309032 -227.13135 REMARK 350 BIOMT1 23 -0.309026 -0.809020 0.499989 594.63587 REMARK 350 BIOMT2 23 0.809020 -0.500000 -0.309009 367.49615 REMARK 350 BIOMT3 23 0.499989 0.309009 0.809026 -227.12429 REMARK 350 BIOMT1 24 0.309017 -0.809014 -0.500005 735.00066 REMARK 350 BIOMT2 24 0.809020 0.500000 -0.309009 -0.00386 REMARK 350 BIOMT3 24 0.499995 -0.309025 0.809017 0.00452 REMARK 350 BIOMT1 25 0.500000 0.309022 -0.809015 367.49761 REMARK 350 BIOMT2 25 0.309012 0.809017 0.500003 -227.12683 REMARK 350 BIOMT3 25 0.809019 -0.499997 0.309017 140.37079 REMARK 350 BIOMT1 26 -0.309008 -0.809014 -0.500011 962.12683 REMARK 350 BIOMT2 26 0.809014 -0.500000 0.309025 140.37079 REMARK 350 BIOMT3 26 -0.500011 -0.309025 0.809008 367.51011 REMARK 350 BIOMT1 27 0.000009 0.000009 -1.000000 734.99309 REMARK 350 BIOMT2 27 1.000000 0.000000 0.000009 -0.00345 REMARK 350 BIOMT3 27 0.000000 -1.000000 -0.000009 735.00346 REMARK 350 BIOMT1 28 -0.309017 0.809020 -0.499995 367.49720 REMARK 350 BIOMT2 28 0.809014 0.500000 0.309025 -227.12922 REMARK 350 BIOMT3 28 0.500005 -0.309009 -0.809017 594.62297 REMARK 350 BIOMT1 29 -0.809023 0.499992 0.309014 367.50599 REMARK 350 BIOMT2 29 0.499992 0.309017 0.809022 -227.12642 REMARK 350 BIOMT3 29 0.309014 0.809022 -0.499994 140.36971 REMARK 350 BIOMT1 30 -0.809017 -0.500008 0.309005 735.00731 REMARK 350 BIOMT2 30 0.499992 -0.309017 0.809022 0.00107 REMARK 350 BIOMT3 30 -0.309029 0.809012 0.500000 0.00624 REMARK 350 BIOMT1 31 0.809017 -0.500008 -0.309005 367.49827 REMARK 350 BIOMT2 31 -0.499992 -0.309017 -0.809022 962.12643 REMARK 350 BIOMT3 31 0.309029 0.809012 -0.500000 140.36971 REMARK 350 BIOMT1 32 0.809023 0.499992 -0.309014 -0.00041 REMARK 350 BIOMT2 32 -0.499992 0.309017 -0.809022 734.99894 REMARK 350 BIOMT3 32 -0.309014 0.809022 0.499994 -0.00066 REMARK 350 BIOMT1 33 0.309017 0.809020 0.499995 -227.12684 REMARK 350 BIOMT2 33 -0.809014 0.500000 -0.309025 594.62922 REMARK 350 BIOMT3 33 -0.500005 -0.309009 0.809017 367.49893 REMARK 350 BIOMT1 34 -0.000009 0.000009 1.000000 0.00000 REMARK 350 BIOMT2 34 -1.000000 0.000000 -0.000009 735.00345 REMARK 350 BIOMT3 34 0.000000 -1.000000 0.000009 734.99655 REMARK 350 BIOMT1 35 0.309008 -0.809014 0.500011 367.49852 REMARK 350 BIOMT2 35 -0.809014 -0.500000 -0.309025 962.12922 REMARK 350 BIOMT3 35 0.500011 -0.309025 -0.809008 594.62297 REMARK 350 BIOMT1 36 -0.500000 0.309022 0.809015 140.37144 REMARK 350 BIOMT2 36 -0.309012 0.809017 -0.500003 367.49934 REMARK 350 BIOMT3 36 -0.809019 -0.499997 -0.309017 962.12708 REMARK 350 BIOMT1 37 -0.309017 -0.809014 0.500005 594.62469 REMARK 350 BIOMT2 37 -0.809020 0.500000 0.309009 367.50386 REMARK 350 BIOMT3 37 -0.499995 -0.309025 -0.809017 962.12856 REMARK 350 BIOMT1 38 0.309026 -0.809020 -0.499989 734.99375 REMARK 350 BIOMT2 38 -0.809020 -0.500000 0.309009 735.00386 REMARK 350 BIOMT3 38 -0.499989 0.309009 -0.809026 735.00238 REMARK 350 BIOMT1 39 0.500015 0.309012 -0.809009 367.49334 REMARK 350 BIOMT2 39 -0.309012 -0.809017 -0.500003 962.12684 REMARK 350 BIOMT3 39 -0.809009 0.500003 -0.309032 594.62921 REMARK 350 BIOMT1 40 0.000009 1.000000 0.000000 -0.00346 REMARK 350 BIOMT2 40 0.000009 0.000000 -1.000000 734.99655 REMARK 350 BIOMT3 40 -1.000000 0.000009 -0.000009 735.00000 REMARK 350 BIOMT1 41 -0.000009 -0.000009 1.000000 0.00690 REMARK 350 BIOMT2 41 1.000000 0.000000 0.000009 -0.00345 REMARK 350 BIOMT3 41 0.000000 1.000000 0.000009 -0.00346 REMARK 350 BIOMT1 42 0.309017 -0.809020 0.499995 367.50279 REMARK 350 BIOMT2 42 0.809014 0.500000 0.309025 -227.12922 REMARK 350 BIOMT3 42 -0.500005 0.309009 0.809017 140.37703 REMARK 350 BIOMT1 43 0.809023 -0.499992 -0.309014 367.49401 REMARK 350 BIOMT2 43 0.499992 0.309017 0.809022 -227.12642 REMARK 350 BIOMT3 43 -0.309014 -0.809022 0.499994 594.63029 REMARK 350 BIOMT1 44 0.809017 0.500008 -0.309005 -0.00732 REMARK 350 BIOMT2 44 0.499992 -0.309017 0.809022 0.00107 REMARK 350 BIOMT3 44 0.309029 -0.809012 -0.500000 734.99376 REMARK 350 BIOMT1 45 0.309008 0.809014 0.500011 -227.12684 REMARK 350 BIOMT2 45 0.809014 -0.500000 0.309025 140.37079 REMARK 350 BIOMT3 45 0.500011 0.309025 -0.809008 367.48989 REMARK 350 BIOMT1 46 0.809017 -0.499992 0.309029 140.36520 REMARK 350 BIOMT2 46 -0.500008 -0.309017 0.809012 367.50452 REMARK 350 BIOMT3 46 -0.309005 -0.809022 -0.500000 962.12470 REMARK 350 BIOMT1 47 1.000000 0.000000 0.000019 -0.00691 REMARK 350 BIOMT2 47 0.000000 -1.000000 0.000000 735.00001 REMARK 350 BIOMT3 47 0.000019 0.000000 -1.000000 734.99309 REMARK 350 BIOMT1 48 0.809017 0.499992 0.309029 -227.12922 REMARK 350 BIOMT2 48 0.500008 -0.309017 -0.809012 594.62298 REMARK 350 BIOMT3 48 -0.309005 0.809022 -0.500000 367.49375 REMARK 350 BIOMT1 49 0.500000 0.309012 0.809019 -227.12643 REMARK 350 BIOMT2 49 0.309022 0.809017 -0.499997 140.36972 REMARK 350 BIOMT3 49 -0.809015 0.500003 0.309017 367.49827 REMARK 350 BIOMT1 50 0.500000 -0.309012 0.809019 -0.00239 REMARK 350 BIOMT2 50 -0.309022 0.809017 0.499997 0.00279 REMARK 350 BIOMT3 50 -0.809015 -0.500003 0.309017 735.00041 REMARK 350 BIOMT1 51 -0.500000 -0.309012 -0.809019 962.12642 REMARK 350 BIOMT2 51 0.309022 0.809017 -0.499997 140.36971 REMARK 350 BIOMT3 51 0.809015 -0.500003 -0.309017 367.50173 REMARK 350 BIOMT1 52 -0.500000 0.309012 -0.809019 735.00238 REMARK 350 BIOMT2 52 -0.309022 0.809017 0.499997 0.00279 REMARK 350 BIOMT3 52 0.809015 0.500003 -0.309017 -0.00041 REMARK 350 BIOMT1 53 -0.809017 0.499992 -0.309029 594.63479 REMARK 350 BIOMT2 53 -0.500008 -0.309017 0.809012 367.50452 REMARK 350 BIOMT3 53 0.309005 0.809022 0.500000 -227.12470 REMARK 350 BIOMT1 54 -1.000000 0.000000 -0.000019 735.00690 REMARK 350 BIOMT2 54 0.000000 -1.000000 0.000000 735.00001 REMARK 350 BIOMT3 54 -0.000019 0.000000 1.000000 0.00690 REMARK 350 BIOMT1 55 -0.809017 -0.499992 -0.309029 962.12921 REMARK 350 BIOMT2 55 0.500008 -0.309017 -0.809012 594.62298 REMARK 350 BIOMT3 55 0.309005 -0.809022 0.500000 367.50625 REMARK 350 BIOMT1 56 -0.309008 0.809014 -0.500011 367.50146 REMARK 350 BIOMT2 56 -0.809014 -0.500000 -0.309025 962.12922 REMARK 350 BIOMT3 56 -0.500011 0.309025 0.809008 140.37702 REMARK 350 BIOMT1 57 -0.809017 0.500008 0.309005 367.50172 REMARK 350 BIOMT2 57 -0.499992 -0.309017 -0.809022 962.12643 REMARK 350 BIOMT3 57 -0.309029 -0.809012 0.500000 594.63028 REMARK 350 BIOMT1 58 -0.809023 -0.499992 0.309014 735.00040 REMARK 350 BIOMT2 58 -0.499992 0.309017 -0.809022 734.99893 REMARK 350 BIOMT3 58 0.309014 -0.809022 -0.499994 735.00066 REMARK 350 BIOMT1 59 -0.309017 -0.809020 -0.499995 962.12683 REMARK 350 BIOMT2 59 -0.809014 0.500000 -0.309025 594.62922 REMARK 350 BIOMT3 59 0.500005 0.309009 -0.809017 367.50106 REMARK 350 BIOMT1 60 0.000009 -0.000009 -1.000000 734.99999 REMARK 350 BIOMT2 60 -1.000000 0.000000 -0.000009 735.00346 REMARK 350 BIOMT3 60 0.000000 1.000000 -0.000009 0.00345 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 MET A 3 REMARK 465 ALA A 4 REMARK 465 SER A 5 REMARK 465 LYS A 6 REMARK 465 ASP A 7 REMARK 465 ALA A 8 REMARK 465 THR A 9 REMARK 465 PRO A 10 REMARK 465 SER A 11 REMARK 465 ALA A 12 REMARK 465 ASP A 13 REMARK 465 GLY A 14 REMARK 465 ALA A 15 REMARK 465 THR A 16 REMARK 465 GLY A 17 REMARK 465 ALA A 18 REMARK 465 GLY A 19 REMARK 465 GLN A 20 REMARK 465 LEU A 21 REMARK 465 VAL A 22 REMARK 465 PRO A 23 REMARK 465 GLU A 24 REMARK 465 VAL A 25 REMARK 465 ASN A 26 REMARK 465 THR A 27 REMARK 465 ALA A 28 REMARK 465 ASP A 29 REMARK 465 PRO A 30 REMARK 465 ILE A 31 REMARK 465 PRO A 32 REMARK 465 ILE A 33 REMARK 465 ASP A 34 REMARK 465 PRO A 35 REMARK 465 VAL A 36 REMARK 465 ALA A 37 REMARK 465 GLY A 38 REMARK 465 SER A 39 REMARK 465 SER A 40 REMARK 465 THR A 41 REMARK 465 ALA A 42 REMARK 465 ALA A 43 REMARK 465 PRO A 44 REMARK 465 VAL A 45 REMARK 465 ALA A 46 REMARK 465 GLY A 47 REMARK 465 GLN A 48 REMARK 465 VAL A 49 REMARK 465 LEU A 409 REMARK 465 ALA A 410 REMARK 465 GLU A 411 REMARK 465 GLY A 534 REMARK 465 PRO A 535 REMARK 465 ALA A 536 REMARK 465 ARG A 537 REMARK 465 GLY A 538 REMARK 465 ARG A 539 REMARK 465 LEU A 540 REMARK 465 GLY A 541 REMARK 465 VAL A 542 REMARK 465 ARG A 543 REMARK 465 ARG A 544 REMARK 465 MET B 3 REMARK 465 ALA B 4 REMARK 465 SER B 5 REMARK 465 LYS B 6 REMARK 465 ASP B 7 REMARK 465 ALA B 8 REMARK 465 THR B 9 REMARK 465 PRO B 10 REMARK 465 SER B 11 REMARK 465 ASP B 29 REMARK 465 PRO B 30 REMARK 465 ILE B 31 REMARK 465 PRO B 32 REMARK 465 ILE B 33 REMARK 465 ASP B 34 REMARK 465 PRO B 35 REMARK 465 VAL B 36 REMARK 465 ALA B 37 REMARK 465 GLY B 38 REMARK 465 SER B 39 REMARK 465 SER B 40 REMARK 465 THR B 41 REMARK 465 ALA B 42 REMARK 465 ALA B 43 REMARK 465 PRO B 44 REMARK 465 VAL B 45 REMARK 465 ALA B 46 REMARK 465 GLY B 47 REMARK 465 GLN B 48 REMARK 465 VAL B 49 REMARK 465 ALA B 533 REMARK 465 GLY B 534 REMARK 465 PRO B 535 REMARK 465 ALA B 536 REMARK 465 ARG B 537 REMARK 465 GLY B 538 REMARK 465 ARG B 539 REMARK 465 LEU B 540 REMARK 465 GLY B 541 REMARK 465 VAL B 542 REMARK 465 ARG B 543 REMARK 465 ARG B 544 REMARK 465 GLY C -6 REMARK 465 SER C -5 REMARK 465 SER C -4 REMARK 465 GLY C -3 REMARK 465 SER C -2 REMARK 465 SER C -1 REMARK 465 GLY C 0 REMARK 465 LYS C 171 REMARK 465 GLY D -6 REMARK 465 SER D -5 REMARK 465 SER D -4 REMARK 465 GLY D -3 REMARK 465 SER D -2 REMARK 465 SER D -1 REMARK 465 GLY D 0 REMARK 465 GLN D 1 REMARK 465 LYS D 162 REMARK 465 GLY E -6 REMARK 465 SER E -5 REMARK 465 SER E -4 REMARK 465 GLY E -3 REMARK 465 SER E -2 REMARK 465 SER E -1 REMARK 465 GLY E 0 REMARK 465 GLU E 169 REMARK 465 ALA E 170 REMARK 465 LYS E 171 REMARK 465 GLY F -6 REMARK 465 SER F -5 REMARK 465 SER F -4 REMARK 465 GLY F -3 REMARK 465 SER F -2 REMARK 465 SER F -1 REMARK 465 GLY F 0 REMARK 465 GLN F 1 REMARK 465 LYS F 162 REMARK 465 MET G 3 REMARK 465 ALA G 4 REMARK 465 SER G 5 REMARK 465 LYS G 6 REMARK 465 ASP G 7 REMARK 465 ALA G 8 REMARK 465 THR G 9 REMARK 465 PRO G 10 REMARK 465 SER G 11 REMARK 465 ALA G 12 REMARK 465 ASP G 13 REMARK 465 GLY G 14 REMARK 465 ALA G 15 REMARK 465 THR G 16 REMARK 465 GLY G 17 REMARK 465 ALA G 18 REMARK 465 GLY G 19 REMARK 465 GLN G 20 REMARK 465 LEU G 21 REMARK 465 VAL G 22 REMARK 465 PRO G 23 REMARK 465 GLU G 24 REMARK 465 VAL G 25 REMARK 465 ASN G 26 REMARK 465 THR G 27 REMARK 465 ALA G 28 REMARK 465 ASP G 29 REMARK 465 PRO G 30 REMARK 465 ILE G 31 REMARK 465 PRO G 32 REMARK 465 ILE G 33 REMARK 465 ASP G 34 REMARK 465 PRO G 35 REMARK 465 VAL G 36 REMARK 465 ALA G 37 REMARK 465 GLY G 38 REMARK 465 SER G 39 REMARK 465 SER G 40 REMARK 465 THR G 41 REMARK 465 ALA G 42 REMARK 465 ALA G 43 REMARK 465 PRO G 44 REMARK 465 VAL G 45 REMARK 465 ALA G 46 REMARK 465 GLY G 47 REMARK 465 GLN G 48 REMARK 465 THR G 296 REMARK 465 SER G 297 REMARK 465 GLY G 298 REMARK 465 GLN G 299 REMARK 465 ILE G 338 REMARK 465 PRO G 339 REMARK 465 ASN G 340 REMARK 465 SER G 341 REMARK 465 SER G 342 REMARK 465 THR G 343 REMARK 465 GLN G 344 REMARK 465 ASN G 345 REMARK 465 ASN G 346 REMARK 465 PRO G 347 REMARK 465 GLU G 371 REMARK 465 ASN G 372 REMARK 465 VAL G 373 REMARK 465 SER G 374 REMARK 465 SER G 375 REMARK 465 GLY G 376 REMARK 465 GLY G 377 REMARK 465 ASP G 378 REMARK 465 ASP G 391 REMARK 465 SER G 392 REMARK 465 GLY G 393 REMARK 465 GLY G 394 REMARK 465 ALA G 395 REMARK 465 SER G 407 REMARK 465 SER G 408 REMARK 465 LEU G 409 REMARK 465 ALA G 410 REMARK 465 GLU G 411 REMARK 465 ALA G 412 REMARK 465 GLN G 440 REMARK 465 SER G 441 REMARK 465 GLY G 442 REMARK 465 SER G 443 REMARK 465 PRO G 444 REMARK 465 GLY G 534 REMARK 465 PRO G 535 REMARK 465 ALA G 536 REMARK 465 ARG G 537 REMARK 465 GLY G 538 REMARK 465 ARG G 539 REMARK 465 LEU G 540 REMARK 465 GLY G 541 REMARK 465 VAL G 542 REMARK 465 ARG G 543 REMARK 465 ARG G 544 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 CG2 THR G 280 O ALA G 319 2.09 REMARK 500 NZ LYS E 128 O PRO F 154 2.13 REMARK 500 OE1 GLN F 149 NH1 ARG F 152 2.13 REMARK 500 OG SER E 31 OE1 GLN E 102 2.17 REMARK 500 OG SER D 36 OG SER D 91 2.18 REMARK 500 N THR A 343 OE1 GLN E 105 2.19 REMARK 500 OG SER F 36 OG SER F 91 2.19 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 PRO F 154 CA - N - CD ANGL. DEV. = -18.1 DEGREES REMARK 500 PRO F 154 N - CD - CG ANGL. DEV. = -11.9 DEGREES REMARK 500 PRO G 417 CA - N - CD ANGL. DEV. = -11.9 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 LEU A 155 -5.06 69.20 REMARK 500 THR A 178 -169.47 -111.84 REMARK 500 THR A 191 53.36 -102.12 REMARK 500 THR A 280 52.13 -93.19 REMARK 500 TYR A 405 -3.74 69.83 REMARK 500 GLN B 65 31.06 -95.18 REMARK 500 LEU B 218 -60.95 -99.67 REMARK 500 GLN B 287 36.17 -99.06 REMARK 500 THR C 131 -118.16 50.64 REMARK 500 GLU C 133 -130.55 55.48 REMARK 500 ASN D 33 33.92 -98.76 REMARK 500 CYS D 150 17.07 -141.36 REMARK 500 CYS E 119 -50.51 -120.72 REMARK 500 SER E 120 -7.59 70.08 REMARK 500 VAL F 53 -56.13 68.46 REMARK 500 LEU G 218 -61.28 -94.08 REMARK 500 GLN G 260 -135.46 51.27 REMARK 500 CYS G 329 146.75 -171.34 REMARK 500 ASN G 425 -121.83 57.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36223 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE GI.4 CHIBA VLP COMPLEXED WITH THE CV-1A1 REMARK 900 FV-CLASP DBREF 8JG5 A 3 544 PDB 8JG5 8JG5 3 544 DBREF 8JG5 B 3 544 PDB 8JG5 8JG5 3 544 DBREF 8JG5 C -6 118 PDB 8JG5 8JG5 -6 118 DBREF 8JG5 C 119 171 PDB 8JG5 8JG5 119 171 DBREF 8JG5 D -6 112 PDB 8JG5 8JG5 -6 112 DBREF 8JG5 D 113 162 PDB 8JG5 8JG5 113 162 DBREF 8JG5 E -6 118 PDB 8JG5 8JG5 -6 118 DBREF 8JG5 E 119 171 PDB 8JG5 8JG5 119 171 DBREF 8JG5 F -6 112 PDB 8JG5 8JG5 -6 112 DBREF 8JG5 F 113 162 PDB 8JG5 8JG5 113 162 DBREF 8JG5 G 3 544 PDB 8JG5 8JG5 3 544 SEQRES 1 A 542 MET ALA SER LYS ASP ALA THR PRO SER ALA ASP GLY ALA SEQRES 2 A 542 THR GLY ALA GLY GLN LEU VAL PRO GLU VAL ASN THR ALA SEQRES 3 A 542 ASP PRO ILE PRO ILE ASP PRO VAL ALA GLY SER SER THR SEQRES 4 A 542 ALA ALA PRO VAL ALA GLY GLN VAL ASN LEU ILE ASP PRO SEQRES 5 A 542 TRP ILE ILE ASN ASN PHE VAL GLN ALA PRO GLN GLY GLU SEQRES 6 A 542 PHE THR ILE SER PRO ASN ASN THR PRO GLY ASP VAL LEU SEQRES 7 A 542 PHE ASP LEU GLN LEU GLY PRO HIS LEU ASN PRO PHE LEU SEQRES 8 A 542 SER HIS LEU SER GLN MET TYR ASN GLY TRP VAL GLY ASN SEQRES 9 A 542 MET ARG VAL ARG VAL VAL LEU ALA GLY ASN ALA PHE THR SEQRES 10 A 542 ALA GLY LYS VAL ILE ILE CYS CYS VAL PRO PRO GLY PHE SEQRES 11 A 542 GLN SER ARG THR LEU SER ILE ALA GLN ALA THR LEU PHE SEQRES 12 A 542 PRO HIS VAL ILE ALA ASP VAL ARG THR LEU ASP PRO VAL SEQRES 13 A 542 GLU VAL PRO LEU GLU ASP VAL ARG ASN VAL LEU TYR HIS SEQRES 14 A 542 ASN ASN ASP THR GLN PRO THR MET ARG LEU LEU CYS MET SEQRES 15 A 542 LEU TYR THR PRO LEU ARG THR GLY GLY ALA SER GLY GLY SEQRES 16 A 542 THR ASP SER PHE VAL VAL ALA GLY ARG VAL LEU THR CYS SEQRES 17 A 542 PRO GLY PRO ASP PHE ASN PHE LEU PHE LEU VAL PRO PRO SEQRES 18 A 542 THR VAL GLU GLN LYS THR ARG PRO PHE THR VAL PRO ASN SEQRES 19 A 542 ILE PRO LEU LYS TYR LEU SER ASN SER ARG ILE PRO ASN SEQRES 20 A 542 PRO ILE GLU GLY MET SER LEU SER PRO ASP GLN THR GLN SEQRES 21 A 542 ASN VAL GLN PHE GLN ASN GLY ARG CYS THR ILE ASP GLY SEQRES 22 A 542 GLN PRO LEU GLY THR THR PRO VAL SER VAL SER GLN LEU SEQRES 23 A 542 CYS LYS PHE ARG GLY ARG ILE THR SER GLY GLN ARG VAL SEQRES 24 A 542 LEU ASN LEU THR GLU LEU ASP GLY SER PRO PHE MET ALA SEQRES 25 A 542 PHE ALA ALA PRO ALA PRO ALA GLY PHE PRO ASP LEU GLY SEQRES 26 A 542 SER CYS ASP TRP HIS ILE GLU MET SER LYS ILE PRO ASN SEQRES 27 A 542 SER SER THR GLN ASN ASN PRO ILE VAL THR ASN SER VAL SEQRES 28 A 542 LYS PRO ASN SER GLN GLN PHE VAL PRO HIS LEU SER SER SEQRES 29 A 542 ILE THR LEU ASP GLU ASN VAL SER SER GLY GLY ASP TYR SEQRES 30 A 542 ILE GLY THR ILE GLN TRP THR SER PRO PRO SER ASP SER SEQRES 31 A 542 GLY GLY ALA ASN THR ASN PHE TRP LYS ILE PRO ASP TYR SEQRES 32 A 542 GLY SER SER LEU ALA GLU ALA SER GLN LEU ALA PRO ALA SEQRES 33 A 542 VAL TYR PRO PRO GLY PHE ASN GLU VAL ILE VAL TYR PHE SEQRES 34 A 542 MET ALA SER ILE PRO GLY PRO ASN GLN SER GLY SER PRO SEQRES 35 A 542 ASN LEU VAL PRO CYS LEU LEU PRO GLN GLU TYR ILE THR SEQRES 36 A 542 HIS PHE ILE SER GLU GLN ALA PRO ILE GLN GLY GLU ALA SEQRES 37 A 542 ALA LEU LEU HIS TYR VAL ASP PRO ASP THR ASN ARG ASN SEQRES 38 A 542 LEU GLY GLU PHE LYS LEU TYR PRO GLY GLY TYR LEU THR SEQRES 39 A 542 CYS VAL PRO ASN SER SER SER THR GLY PRO GLN GLN LEU SEQRES 40 A 542 PRO LEU ASP GLY VAL PHE VAL PHE ALA SER TRP VAL SER SEQRES 41 A 542 ARG PHE TYR GLN LEU LYS PRO VAL GLY THR ALA GLY PRO SEQRES 42 A 542 ALA ARG GLY ARG LEU GLY VAL ARG ARG SEQRES 1 B 542 MET ALA SER LYS ASP ALA THR PRO SER ALA ASP GLY ALA SEQRES 2 B 542 THR GLY ALA GLY GLN LEU VAL PRO GLU VAL ASN THR ALA SEQRES 3 B 542 ASP PRO ILE PRO ILE ASP PRO VAL ALA GLY SER SER THR SEQRES 4 B 542 ALA ALA PRO VAL ALA GLY GLN VAL ASN LEU ILE ASP PRO SEQRES 5 B 542 TRP ILE ILE ASN ASN PHE VAL GLN ALA PRO GLN GLY GLU SEQRES 6 B 542 PHE THR ILE SER PRO ASN ASN THR PRO GLY ASP VAL LEU SEQRES 7 B 542 PHE ASP LEU GLN LEU GLY PRO HIS LEU ASN PRO PHE LEU SEQRES 8 B 542 SER HIS LEU SER GLN MET TYR ASN GLY TRP VAL GLY ASN SEQRES 9 B 542 MET ARG VAL ARG VAL VAL LEU ALA GLY ASN ALA PHE THR SEQRES 10 B 542 ALA GLY LYS VAL ILE ILE CYS CYS VAL PRO PRO GLY PHE SEQRES 11 B 542 GLN SER ARG THR LEU SER ILE ALA GLN ALA THR LEU PHE SEQRES 12 B 542 PRO HIS VAL ILE ALA ASP VAL ARG THR LEU ASP PRO VAL SEQRES 13 B 542 GLU VAL PRO LEU GLU ASP VAL ARG ASN VAL LEU TYR HIS SEQRES 14 B 542 ASN ASN ASP THR GLN PRO THR MET ARG LEU LEU CYS MET SEQRES 15 B 542 LEU TYR THR PRO LEU ARG THR GLY GLY ALA SER GLY GLY SEQRES 16 B 542 THR ASP SER PHE VAL VAL ALA GLY ARG VAL LEU THR CYS SEQRES 17 B 542 PRO GLY PRO ASP PHE ASN PHE LEU PHE LEU VAL PRO PRO SEQRES 18 B 542 THR VAL GLU GLN LYS THR ARG PRO PHE THR VAL PRO ASN SEQRES 19 B 542 ILE PRO LEU LYS TYR LEU SER ASN SER ARG ILE PRO ASN SEQRES 20 B 542 PRO ILE GLU GLY MET SER LEU SER PRO ASP GLN THR GLN SEQRES 21 B 542 ASN VAL GLN PHE GLN ASN GLY ARG CYS THR ILE ASP GLY SEQRES 22 B 542 GLN PRO LEU GLY THR THR PRO VAL SER VAL SER GLN LEU SEQRES 23 B 542 CYS LYS PHE ARG GLY ARG ILE THR SER GLY GLN ARG VAL SEQRES 24 B 542 LEU ASN LEU THR GLU LEU ASP GLY SER PRO PHE MET ALA SEQRES 25 B 542 PHE ALA ALA PRO ALA PRO ALA GLY PHE PRO ASP LEU GLY SEQRES 26 B 542 SER CYS ASP TRP HIS ILE GLU MET SER LYS ILE PRO ASN SEQRES 27 B 542 SER SER THR GLN ASN ASN PRO ILE VAL THR ASN SER VAL SEQRES 28 B 542 LYS PRO ASN SER GLN GLN PHE VAL PRO HIS LEU SER SER SEQRES 29 B 542 ILE THR LEU ASP GLU ASN VAL SER SER GLY GLY ASP TYR SEQRES 30 B 542 ILE GLY THR ILE GLN TRP THR SER PRO PRO SER ASP SER SEQRES 31 B 542 GLY GLY ALA ASN THR ASN PHE TRP LYS ILE PRO ASP TYR SEQRES 32 B 542 GLY SER SER LEU ALA GLU ALA SER GLN LEU ALA PRO ALA SEQRES 33 B 542 VAL TYR PRO PRO GLY PHE ASN GLU VAL ILE VAL TYR PHE SEQRES 34 B 542 MET ALA SER ILE PRO GLY PRO ASN GLN SER GLY SER PRO SEQRES 35 B 542 ASN LEU VAL PRO CYS LEU LEU PRO GLN GLU TYR ILE THR SEQRES 36 B 542 HIS PHE ILE SER GLU GLN ALA PRO ILE GLN GLY GLU ALA SEQRES 37 B 542 ALA LEU LEU HIS TYR VAL ASP PRO ASP THR ASN ARG ASN SEQRES 38 B 542 LEU GLY GLU PHE LYS LEU TYR PRO GLY GLY TYR LEU THR SEQRES 39 B 542 CYS VAL PRO ASN SER SER SER THR GLY PRO GLN GLN LEU SEQRES 40 B 542 PRO LEU ASP GLY VAL PHE VAL PHE ALA SER TRP VAL SER SEQRES 41 B 542 ARG PHE TYR GLN LEU LYS PRO VAL GLY THR ALA GLY PRO SEQRES 42 B 542 ALA ARG GLY ARG LEU GLY VAL ARG ARG SEQRES 1 C 178 GLY SER SER GLY SER SER GLY GLU VAL GLN LEU VAL GLU SEQRES 2 C 178 SER GLY ALA GLU VAL LYS LYS PRO GLY ALA SER VAL LYS SEQRES 3 C 178 VAL SER CYS LYS ALA SER GLY TYR THR PHE THR SER LEU SEQRES 4 C 178 TYR MET HIS TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 5 C 178 GLU TRP MET GLY MET ILE ASN PRO SER GLY GLY GLY THR SEQRES 6 C 178 TRP ASN ALA GLN LYS PHE GLN GLY ARG VAL THR MET THR SEQRES 7 C 178 ARG ASP THR SER THR SER THR VAL TYR MET GLU LEU ARG SEQRES 8 C 178 SER LEU ARG SER ASP ASP THR ALA MET TYR TYR CYS ALA SEQRES 9 C 178 ARG ASP SER ASP GLN TYR SER GLN GLY LEU GLY TYR TRP SEQRES 10 C 178 GLY GLN GLY THR LEU VAL THR VAL CYS SER GLY SER ASP SEQRES 11 C 178 TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU GLN SEQRES 12 C 178 LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN GLU SEQRES 13 C 178 ILE GLU GLU ILE ARG GLN LYS TYR GLN SER LYS ARG GLN SEQRES 14 C 178 PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 D 169 GLY SER SER GLY SER SER GLY GLN SER ALA LEU THR GLN SEQRES 2 D 169 PRO ALA SER VAL SER GLY SER PRO GLY GLN SER ILE THR SEQRES 3 D 169 ILE SER CYS THR GLY THR SER SER ASP VAL GLY GLY TYR SEQRES 4 D 169 ASN TYR VAL SER TRP TYR GLN GLN HIS PRO GLY LYS ALA SEQRES 5 D 169 PRO LYS LEU MET ILE TYR ASP VAL SER LYS ARG PRO SER SEQRES 6 D 169 GLY VAL SER ASN ARG PHE SER GLY SER LYS SER GLY ASN SEQRES 7 D 169 THR ALA SER LEU THR ILE SER GLY LEU GLN ALA LYS ASP SEQRES 8 D 169 GLU ALA ASP TYR TYR CYS SER SER TYR THR SER SER SER SEQRES 9 D 169 THR TRP VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU SEQRES 10 D 169 GLY GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL SEQRES 11 D 169 GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET SEQRES 12 D 169 MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SEQRES 13 D 169 CYS LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 E 178 GLY SER SER GLY SER SER GLY GLU VAL GLN LEU VAL GLU SEQRES 2 E 178 SER GLY ALA GLU VAL LYS LYS PRO GLY ALA SER VAL LYS SEQRES 3 E 178 VAL SER CYS LYS ALA SER GLY TYR THR PHE THR SER LEU SEQRES 4 E 178 TYR MET HIS TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 5 E 178 GLU TRP MET GLY MET ILE ASN PRO SER GLY GLY GLY THR SEQRES 6 E 178 TRP ASN ALA GLN LYS PHE GLN GLY ARG VAL THR MET THR SEQRES 7 E 178 ARG ASP THR SER THR SER THR VAL TYR MET GLU LEU ARG SEQRES 8 E 178 SER LEU ARG SER ASP ASP THR ALA MET TYR TYR CYS ALA SEQRES 9 E 178 ARG ASP SER ASP GLN TYR SER GLN GLY LEU GLY TYR TRP SEQRES 10 E 178 GLY GLN GLY THR LEU VAL THR VAL CYS SER GLY SER ASP SEQRES 11 E 178 TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU GLN SEQRES 12 E 178 LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN GLU SEQRES 13 E 178 ILE GLU GLU ILE ARG GLN LYS TYR GLN SER LYS ARG GLN SEQRES 14 E 178 PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 F 169 GLY SER SER GLY SER SER GLY GLN SER ALA LEU THR GLN SEQRES 2 F 169 PRO ALA SER VAL SER GLY SER PRO GLY GLN SER ILE THR SEQRES 3 F 169 ILE SER CYS THR GLY THR SER SER ASP VAL GLY GLY TYR SEQRES 4 F 169 ASN TYR VAL SER TRP TYR GLN GLN HIS PRO GLY LYS ALA SEQRES 5 F 169 PRO LYS LEU MET ILE TYR ASP VAL SER LYS ARG PRO SER SEQRES 6 F 169 GLY VAL SER ASN ARG PHE SER GLY SER LYS SER GLY ASN SEQRES 7 F 169 THR ALA SER LEU THR ILE SER GLY LEU GLN ALA LYS ASP SEQRES 8 F 169 GLU ALA ASP TYR TYR CYS SER SER TYR THR SER SER SER SEQRES 9 F 169 THR TRP VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU SEQRES 10 F 169 GLY GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL SEQRES 11 F 169 GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET SEQRES 12 F 169 MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SEQRES 13 F 169 CYS LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 G 542 MET ALA SER LYS ASP ALA THR PRO SER ALA ASP GLY ALA SEQRES 2 G 542 THR GLY ALA GLY GLN LEU VAL PRO GLU VAL ASN THR ALA SEQRES 3 G 542 ASP PRO ILE PRO ILE ASP PRO VAL ALA GLY SER SER THR SEQRES 4 G 542 ALA ALA PRO VAL ALA GLY GLN VAL ASN LEU ILE ASP PRO SEQRES 5 G 542 TRP ILE ILE ASN ASN PHE VAL GLN ALA PRO GLN GLY GLU SEQRES 6 G 542 PHE THR ILE SER PRO ASN ASN THR PRO GLY ASP VAL LEU SEQRES 7 G 542 PHE ASP LEU GLN LEU GLY PRO HIS LEU ASN PRO PHE LEU SEQRES 8 G 542 SER HIS LEU SER GLN MET TYR ASN GLY TRP VAL GLY ASN SEQRES 9 G 542 MET ARG VAL ARG VAL VAL LEU ALA GLY ASN ALA PHE THR SEQRES 10 G 542 ALA GLY LYS VAL ILE ILE CYS CYS VAL PRO PRO GLY PHE SEQRES 11 G 542 GLN SER ARG THR LEU SER ILE ALA GLN ALA THR LEU PHE SEQRES 12 G 542 PRO HIS VAL ILE ALA ASP VAL ARG THR LEU ASP PRO VAL SEQRES 13 G 542 GLU VAL PRO LEU GLU ASP VAL ARG ASN VAL LEU TYR HIS SEQRES 14 G 542 ASN ASN ASP THR GLN PRO THR MET ARG LEU LEU CYS MET SEQRES 15 G 542 LEU TYR THR PRO LEU ARG THR GLY GLY ALA SER GLY GLY SEQRES 16 G 542 THR ASP SER PHE VAL VAL ALA GLY ARG VAL LEU THR CYS SEQRES 17 G 542 PRO GLY PRO ASP PHE ASN PHE LEU PHE LEU VAL PRO PRO SEQRES 18 G 542 THR VAL GLU GLN LYS THR ARG PRO PHE THR VAL PRO ASN SEQRES 19 G 542 ILE PRO LEU LYS TYR LEU SER ASN SER ARG ILE PRO ASN SEQRES 20 G 542 PRO ILE GLU GLY MET SER LEU SER PRO ASP GLN THR GLN SEQRES 21 G 542 ASN VAL GLN PHE GLN ASN GLY ARG CYS THR ILE ASP GLY SEQRES 22 G 542 GLN PRO LEU GLY THR THR PRO VAL SER VAL SER GLN LEU SEQRES 23 G 542 CYS LYS PHE ARG GLY ARG ILE THR SER GLY GLN ARG VAL SEQRES 24 G 542 LEU ASN LEU THR GLU LEU ASP GLY SER PRO PHE MET ALA SEQRES 25 G 542 PHE ALA ALA PRO ALA PRO ALA GLY PHE PRO ASP LEU GLY SEQRES 26 G 542 SER CYS ASP TRP HIS ILE GLU MET SER LYS ILE PRO ASN SEQRES 27 G 542 SER SER THR GLN ASN ASN PRO ILE VAL THR ASN SER VAL SEQRES 28 G 542 LYS PRO ASN SER GLN GLN PHE VAL PRO HIS LEU SER SER SEQRES 29 G 542 ILE THR LEU ASP GLU ASN VAL SER SER GLY GLY ASP TYR SEQRES 30 G 542 ILE GLY THR ILE GLN TRP THR SER PRO PRO SER ASP SER SEQRES 31 G 542 GLY GLY ALA ASN THR ASN PHE TRP LYS ILE PRO ASP TYR SEQRES 32 G 542 GLY SER SER LEU ALA GLU ALA SER GLN LEU ALA PRO ALA SEQRES 33 G 542 VAL TYR PRO PRO GLY PHE ASN GLU VAL ILE VAL TYR PHE SEQRES 34 G 542 MET ALA SER ILE PRO GLY PRO ASN GLN SER GLY SER PRO SEQRES 35 G 542 ASN LEU VAL PRO CYS LEU LEU PRO GLN GLU TYR ILE THR SEQRES 36 G 542 HIS PHE ILE SER GLU GLN ALA PRO ILE GLN GLY GLU ALA SEQRES 37 G 542 ALA LEU LEU HIS TYR VAL ASP PRO ASP THR ASN ARG ASN SEQRES 38 G 542 LEU GLY GLU PHE LYS LEU TYR PRO GLY GLY TYR LEU THR SEQRES 39 G 542 CYS VAL PRO ASN SER SER SER THR GLY PRO GLN GLN LEU SEQRES 40 G 542 PRO LEU ASP GLY VAL PHE VAL PHE ALA SER TRP VAL SER SEQRES 41 G 542 ARG PHE TYR GLN LEU LYS PRO VAL GLY THR ALA GLY PRO SEQRES 42 G 542 ALA ARG GLY ARG LEU GLY VAL ARG ARG HELIX 1 AA1 ASP A 53 ASN A 59 1 7 HELIX 2 AA2 GLY A 86 LEU A 89 5 4 HELIX 3 AA3 ASN A 90 MET A 99 1 10 HELIX 4 AA4 SER A 138 THR A 143 1 6 HELIX 5 AA5 GLY A 196 PHE A 201 1 6 HELIX 6 AA6 SER A 284 LEU A 288 5 5 HELIX 7 AA7 VAL A 361 SER A 365 5 5 HELIX 8 AA8 PRO A 452 GLU A 462 1 11 HELIX 9 AA9 GLY A 505 LEU A 509 5 5 HELIX 10 AB1 GLY B 14 GLY B 19 1 6 HELIX 11 AB2 ASP B 53 ASN B 59 1 7 HELIX 12 AB3 GLY B 86 LEU B 89 5 4 HELIX 13 AB4 ASN B 90 GLN B 98 1 9 HELIX 14 AB5 SER B 138 THR B 143 1 6 HELIX 15 AB6 THR B 198 VAL B 202 5 5 HELIX 16 AB7 SER B 284 LEU B 288 5 5 HELIX 17 AB8 MET B 313 ALA B 317 5 5 HELIX 18 AB9 VAL B 361 SER B 365 5 5 HELIX 19 AC1 PRO B 452 GLU B 462 1 11 HELIX 20 AC2 THR B 504 LEU B 509 5 6 HELIX 21 AC3 GLN C 62 GLN C 65 5 4 HELIX 22 AC4 ASP C 123 SER C 129 1 7 HELIX 23 AC5 ASP C 134 LEU C 139 1 6 HELIX 24 AC6 ALA C 141 LYS C 160 1 20 HELIX 25 AC7 ARG C 161 GLU C 169 1 9 HELIX 26 AC8 GLN D 81 GLU D 85 5 5 HELIX 27 AC9 TYR D 115 TRP D 121 1 7 HELIX 28 AD1 THR D 122 ARG D 152 1 31 HELIX 29 AD2 ARG D 152 ALA D 161 1 10 HELIX 30 AD3 THR E 28 LEU E 32 5 5 HELIX 31 AD4 ALA E 61 GLN E 65 5 5 HELIX 32 AD5 ARG E 87 THR E 91 5 5 HELIX 33 AD6 TYR E 124 THR E 131 1 8 HELIX 34 AD7 THR E 131 ILE E 168 1 38 HELIX 35 AD8 GLN F 81 GLU F 85 5 5 HELIX 36 AD9 THR F 122 LEU F 131 1 10 HELIX 37 AE1 ASP F 134 ALA F 161 1 28 HELIX 38 AE2 ASP G 53 ASN G 59 1 7 HELIX 39 AE3 GLY G 86 LEU G 89 5 4 HELIX 40 AE4 ASN G 90 TYR G 100 1 11 HELIX 41 AE5 SER G 138 THR G 143 1 6 HELIX 42 AE6 GLU G 226 ARG G 230 5 5 HELIX 43 AE7 PRO G 238 LEU G 242 5 5 HELIX 44 AE8 PRO G 452 GLU G 462 1 11 HELIX 45 AE9 GLY G 505 LEU G 509 5 5 SHEET 1 AA1 4 VAL A 61 ILE A 70 0 SHEET 2 AA1 4 VAL A 203 PRO A 211 -1 O VAL A 203 N ILE A 70 SHEET 3 AA1 4 MET A 107 ALA A 114 -1 N ARG A 110 O LEU A 208 SHEET 4 AA1 4 VAL A 158 LEU A 162 -1 O VAL A 160 N VAL A 109 SHEET 1 AA2 4 VAL A 79 GLN A 84 0 SHEET 2 AA2 4 ARG A 180 ARG A 190 -1 O LEU A 181 N LEU A 83 SHEET 3 AA2 4 ALA A 120 VAL A 128 -1 N CYS A 126 O LEU A 182 SHEET 4 AA2 4 HIS A 147 ASP A 151 -1 O ALA A 150 N VAL A 123 SHEET 1 AA3 3 HIS A 171 ASN A 172 0 SHEET 2 AA3 3 GLY A 102 VAL A 104 -1 N TRP A 103 O HIS A 171 SHEET 3 AA3 3 ASN A 216 PHE A 217 -1 O ASN A 216 N VAL A 104 SHEET 1 AA4 3 GLY A 253 SER A 255 0 SHEET 2 AA4 3 VAL A 427 SER A 434 -1 O TYR A 430 N SER A 255 SHEET 3 AA4 3 LEU A 446 VAL A 447 -1 O VAL A 447 N ALA A 433 SHEET 1 AA5 6 GLY A 253 SER A 255 0 SHEET 2 AA5 6 VAL A 427 SER A 434 -1 O TYR A 430 N SER A 255 SHEET 3 AA5 6 LEU A 495 CYS A 497 -1 O LEU A 495 N VAL A 429 SHEET 4 AA5 6 ARG A 482 LEU A 489 -1 N LYS A 488 O THR A 496 SHEET 5 AA5 6 ALA A 470 ASP A 477 -1 N ALA A 471 O LEU A 489 SHEET 6 AA5 6 VAL A 514 VAL A 521 -1 O VAL A 521 N ALA A 470 SHEET 1 AA6 6 VAL A 349 VAL A 353 0 SHEET 2 AA6 6 ASP A 330 LYS A 337 -1 N TRP A 331 O VAL A 353 SHEET 3 AA6 6 GLY A 377 SER A 387 -1 O SER A 387 N ASP A 330 SHEET 4 AA6 6 LYS A 290 ILE A 295 -1 N GLY A 293 O TYR A 379 SHEET 5 AA6 6 VAL A 301 THR A 305 -1 O THR A 305 N ARG A 292 SHEET 6 AA6 6 ILE A 367 THR A 368 -1 O ILE A 367 N LEU A 302 SHEET 1 AA7 4 VAL B 61 ILE B 70 0 SHEET 2 AA7 4 VAL B 203 PRO B 211 -1 O GLY B 205 N PHE B 68 SHEET 3 AA7 4 MET B 107 VAL B 112 -1 N ARG B 110 O LEU B 208 SHEET 4 AA7 4 VAL B 158 LEU B 162 -1 O LEU B 162 N MET B 107 SHEET 1 AA8 4 VAL B 79 GLN B 84 0 SHEET 2 AA8 4 ARG B 180 THR B 187 -1 O LEU B 181 N LEU B 83 SHEET 3 AA8 4 LYS B 122 VAL B 128 -1 N CYS B 126 O LEU B 182 SHEET 4 AA8 4 HIS B 147 ASP B 151 -1 O ALA B 150 N VAL B 123 SHEET 1 AA9 3 HIS B 171 ASN B 172 0 SHEET 2 AA9 3 GLY B 102 VAL B 104 -1 N TRP B 103 O HIS B 171 SHEET 3 AA9 3 ASN B 216 PHE B 217 -1 O ASN B 216 N VAL B 104 SHEET 1 AB1 3 GLY B 253 SER B 255 0 SHEET 2 AB1 3 VAL B 427 SER B 434 -1 O MET B 432 N GLY B 253 SHEET 3 AB1 3 LEU B 446 CYS B 449 -1 O VAL B 447 N ALA B 433 SHEET 1 AB2 6 GLY B 253 SER B 255 0 SHEET 2 AB2 6 VAL B 427 SER B 434 -1 O MET B 432 N GLY B 253 SHEET 3 AB2 6 LEU B 495 CYS B 497 -1 O LEU B 495 N VAL B 429 SHEET 4 AB2 6 ASN B 483 LEU B 489 -1 N LYS B 488 O THR B 496 SHEET 5 AB2 6 ALA B 470 VAL B 476 -1 N ALA B 471 O LEU B 489 SHEET 6 AB2 6 VAL B 514 VAL B 521 -1 O SER B 519 N LEU B 472 SHEET 1 AB3 6 VAL B 349 VAL B 353 0 SHEET 2 AB3 6 ASP B 330 LYS B 337 -1 N MET B 335 O VAL B 349 SHEET 3 AB3 6 GLY B 377 SER B 387 -1 O ILE B 380 N SER B 336 SHEET 4 AB3 6 PHE B 291 ILE B 295 -1 N GLY B 293 O TYR B 379 SHEET 5 AB3 6 GLN B 299 THR B 305 -1 O THR B 305 N ARG B 292 SHEET 6 AB3 6 ILE B 367 VAL B 373 -1 O ILE B 367 N LEU B 302 SHEET 1 AB4 4 GLN C 3 GLU C 6 0 SHEET 2 AB4 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AB4 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AB4 4 VAL C 68 ASP C 73 -1 N THR C 71 O TYR C 80 SHEET 1 AB5 5 TRP C 59 ASN C 60 0 SHEET 2 AB5 5 GLY C 44 ILE C 51 -1 N MET C 50 O TRP C 59 SHEET 3 AB5 5 MET C 34 ALA C 40 -1 N ARG C 38 O GLU C 46 SHEET 4 AB5 5 ALA C 92 ASP C 99 -1 O ALA C 97 N HIS C 35 SHEET 5 AB5 5 LEU C 107 TRP C 110 -1 O TYR C 109 N ARG C 98 SHEET 1 AB6 5 TRP C 59 ASN C 60 0 SHEET 2 AB6 5 GLY C 44 ILE C 51 -1 N MET C 50 O TRP C 59 SHEET 3 AB6 5 MET C 34 ALA C 40 -1 N ARG C 38 O GLU C 46 SHEET 4 AB6 5 ALA C 92 ASP C 99 -1 O ALA C 97 N HIS C 35 SHEET 5 AB6 5 THR C 114 VAL C 116 -1 O THR C 114 N TYR C 94 SHEET 1 AB7 5 SER D 9 SER D 11 0 SHEET 2 AB7 5 THR D 105 THR D 108 1 O THR D 108 N VAL D 10 SHEET 3 AB7 5 ASP D 87 TYR D 93 -1 N TYR D 88 O THR D 105 SHEET 4 AB7 5 VAL D 35 GLN D 40 -1 N TYR D 38 O TYR D 89 SHEET 5 AB7 5 LYS D 47 ILE D 50 -1 O ILE D 50 N TRP D 37 SHEET 1 AB8 4 SER D 9 SER D 11 0 SHEET 2 AB8 4 THR D 105 THR D 108 1 O THR D 108 N VAL D 10 SHEET 3 AB8 4 ASP D 87 TYR D 93 -1 N TYR D 88 O THR D 105 SHEET 4 AB8 4 TRP D 99 PHE D 101 -1 O VAL D 100 N SER D 92 SHEET 1 AB9 3 ILE D 18 THR D 23 0 SHEET 2 AB9 3 THR D 72 ILE D 77 -1 O LEU D 75 N ILE D 20 SHEET 3 AB9 3 PHE D 64 SER D 69 -1 N SER D 67 O SER D 74 SHEET 1 AC1 4 GLN E 3 GLU E 6 0 SHEET 2 AC1 4 SER E 17 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AC1 4 THR E 78 ARG E 84 -1 O MET E 81 N VAL E 20 SHEET 4 AC1 4 VAL E 68 ASP E 73 -1 N THR E 71 O TYR E 80 SHEET 1 AC2 6 GLU E 10 VAL E 11 0 SHEET 2 AC2 6 THR E 114 THR E 117 1 O THR E 117 N GLU E 10 SHEET 3 AC2 6 ALA E 92 ASP E 99 -1 N TYR E 94 O THR E 114 SHEET 4 AC2 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AC2 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AC2 6 THR E 58 TRP E 59 -1 O TRP E 59 N MET E 50 SHEET 1 AC3 4 GLU E 10 VAL E 11 0 SHEET 2 AC3 4 THR E 114 THR E 117 1 O THR E 117 N GLU E 10 SHEET 3 AC3 4 ALA E 92 ASP E 99 -1 N TYR E 94 O THR E 114 SHEET 4 AC3 4 LEU E 107 TRP E 110 -1 O TYR E 109 N ARG E 98 SHEET 1 AC4 3 ILE F 18 THR F 23 0 SHEET 2 AC4 3 THR F 72 ILE F 77 -1 O ALA F 73 N CYS F 22 SHEET 3 AC4 3 SER F 65 SER F 69 -1 N SER F 69 O THR F 72 SHEET 1 AC5 4 LYS F 47 ILE F 50 0 SHEET 2 AC5 4 VAL F 35 GLN F 40 -1 N TRP F 37 O ILE F 50 SHEET 3 AC5 4 ASP F 87 TYR F 93 -1 O SER F 91 N SER F 36 SHEET 4 AC5 4 TRP F 99 PHE F 101 -1 O VAL F 100 N SER F 92 SHEET 1 AC6 4 VAL G 61 ILE G 70 0 SHEET 2 AC6 4 VAL G 203 PRO G 211 -1 O GLY G 205 N PHE G 68 SHEET 3 AC6 4 MET G 107 LEU G 113 -1 N ARG G 110 O LEU G 208 SHEET 4 AC6 4 VAL G 158 LEU G 162 -1 O VAL G 160 N VAL G 109 SHEET 1 AC7 4 VAL G 79 GLN G 84 0 SHEET 2 AC7 4 ARG G 180 THR G 191 -1 O LEU G 181 N LEU G 83 SHEET 3 AC7 4 THR G 119 VAL G 128 -1 N ILE G 124 O MET G 184 SHEET 4 AC7 4 HIS G 147 ASP G 151 -1 O ALA G 150 N VAL G 123 SHEET 1 AC8 3 HIS G 171 ASN G 172 0 SHEET 2 AC8 3 GLY G 102 VAL G 104 -1 N TRP G 103 O HIS G 171 SHEET 3 AC8 3 ASN G 216 PHE G 217 -1 O ASN G 216 N VAL G 104 SHEET 1 AC9 2 GLY G 253 SER G 255 0 SHEET 2 AC9 2 TYR G 430 MET G 432 -1 O TYR G 430 N SER G 255 SHEET 1 AD1 4 LYS G 290 ARG G 292 0 SHEET 2 AD1 4 ILE G 380 SER G 387 -1 O GLY G 381 N PHE G 291 SHEET 3 AD1 4 ASP G 330 GLU G 334 -1 N GLU G 334 O THR G 382 SHEET 4 AD1 4 THR G 350 VAL G 353 -1 O VAL G 353 N TRP G 331 SHEET 1 AD2 5 VAL G 427 ILE G 428 0 SHEET 2 AD2 5 TYR G 494 CYS G 497 -1 O CYS G 497 N VAL G 427 SHEET 3 AD2 5 ASN G 483 TYR G 490 -1 N LYS G 488 O THR G 496 SHEET 4 AD2 5 ALA G 470 VAL G 476 -1 N ALA G 471 O LEU G 489 SHEET 5 AD2 5 VAL G 514 VAL G 521 -1 O VAL G 521 N ALA G 470 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 2 CYS C 119 CYS D 150 1555 1555 2.03 SSBOND 3 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 4 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 5 CYS F 22 CYS F 90 1555 1555 2.03 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