HEADER VIRUS 22-JUN-22 7Y7M TITLE THE STRUCTURE OF COXSACKIEVIRUS A16 MATURE VIRION IN COMPLEX WITH FAB TITLE 2 8C4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAPSID PROTEIN VP1; COMPND 3 CHAIN: A; COMPND 4 EC: 3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAPSID PROTEIN VP2; COMPND 8 CHAIN: B; COMPND 9 EC: 3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: CAPSID PROTEIN VP3; COMPND 13 CHAIN: C; COMPND 14 SYNONYM: VP3; COMPND 15 EC: 3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: CAPSID PROTEIN VP4; COMPND 19 CHAIN: D; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: THE LIGHT CHAIN OF FAB 8C4; COMPND 23 CHAIN: G; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: THE HEAVY CHAIN OF FAB 8C4; COMPND 27 CHAIN: F; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 3 ORGANISM_TAXID: 31704; SOURCE 4 EXPRESSION_SYSTEM: MUS SP.; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 8 ORGANISM_TAXID: 31704; SOURCE 9 EXPRESSION_SYSTEM: MUS SP.; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 13 ORGANISM_TAXID: 31704; SOURCE 14 EXPRESSION_SYSTEM: MUS SP.; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 18 ORGANISM_TAXID: 31704; SOURCE 19 GENE: VP4; SOURCE 20 EXPRESSION_SYSTEM: MUS SP.; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 22 MOL_ID: 5; SOURCE 23 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 24 ORGANISM_TAXID: 31704; SOURCE 25 EXPRESSION_SYSTEM: CERCOPITHECUS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9533; SOURCE 27 MOL_ID: 6; SOURCE 28 ORGANISM_SCIENTIFIC: COXSACKIEVIRUS A16; SOURCE 29 ORGANISM_TAXID: 31704; SOURCE 30 EXPRESSION_SYSTEM: CERCOPITHECUS; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9533 KEYWDS COXSACKIEVIRUS A16, ANTIBODY, CRYO-EM, STRUCTURAL PROTEIN, VIRUS EXPDTA ELECTRON MICROSCOPY AUTHOR Y.CONG,C.X.LIU REVDAT 1 24-AUG-22 7Y7M 0 JRNL AUTH Y.CONG,C.X.LIU JRNL TITL MOLECULAR MECHANISM OF ANTIBODY NEUTRALIZATION OF JRNL TITL 2 COXSACKIEVIRUS A16 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.05 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) : 3.050 REMARK 3 NUMBER OF PARTICLES : 20196 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 7Y7M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-22. REMARK 100 THE DEPOSITION ID IS D_1300030388. 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 : CRYO-EM STRUCTURE OF REMARK 245 COXSACKIEVIRUS A16 MATURE VIRUS REMARK 245 IN COMPLEX WITH A NEUTRALIZING REMARK 245 ANTIBODY 8C4 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 : 7.50 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 TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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) : 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) : 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: A, B, C, D, G, F 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 0.500047 0.808974 0.309053 -167.25694 REMARK 350 BIOMT2 2 -0.808983 0.309017 0.500054 291.90919 REMARK 350 BIOMT3 2 0.309028 -0.500069 0.808970 103.39255 REMARK 350 BIOMT1 3 -0.308893 0.499964 0.809086 17.20740 REMARK 350 BIOMT2 3 -0.499988 -0.809017 0.309036 569.12407 REMARK 350 BIOMT3 3 0.809071 -0.309075 0.499876 -10.62804 REMARK 350 BIOMT1 4 -0.308893 -0.499988 0.809071 298.46957 REMARK 350 BIOMT2 4 0.499964 -0.809017 -0.309075 448.54310 REMARK 350 BIOMT3 4 0.809086 0.309036 0.499876 -184.48918 REMARK 350 BIOMT1 5 0.500047 -0.808983 0.309029 287.83482 REMARK 350 BIOMT2 5 0.808974 0.309017 -0.500069 96.80508 REMARK 350 BIOMT3 5 0.309053 0.500054 0.808970 -177.92069 REMARK 350 BIOMT1 6 0.309234 0.499954 0.808963 -167.27788 REMARK 350 BIOMT2 6 0.499954 -0.809084 0.308917 270.67327 REMARK 350 BIOMT3 6 0.808963 0.308917 -0.500150 103.44312 REMARK 350 BIOMT1 7 0.000169 0.000119 1.000000 10.58255 REMARK 350 BIOMT2 7 1.000000 -0.000050 -0.000169 -17.18679 REMARK 350 BIOMT3 7 0.000050 1.000000 -0.000119 6.60236 REMARK 350 BIOMT1 8 0.309017 -0.499896 0.809081 113.98147 REMARK 350 BIOMT2 8 0.500036 0.809043 0.308891 -184.47597 REMARK 350 BIOMT3 8 -0.808995 0.309117 0.499974 298.49082 REMARK 350 BIOMT1 9 0.808960 -0.309086 0.500050 0.02509 REMARK 350 BIOMT2 9 -0.309005 0.500057 0.808986 -0.00631 REMARK 350 BIOMT3 9 -0.500100 -0.808955 0.309017 575.72856 REMARK 350 BIOMT1 10 0.809094 0.308855 0.499976 -173.80275 REMARK 350 BIOMT2 10 -0.309055 -0.500000 0.809002 281.29139 REMARK 350 BIOMT3 10 0.499852 -0.809079 -0.309094 455.18245 REMARK 350 BIOMT1 11 -0.809036 0.308963 -0.500003 597.06076 REMARK 350 BIOMT2 11 0.308963 -0.500126 -0.808960 562.57302 REMARK 350 BIOMT3 11 -0.500003 -0.808960 0.309162 575.65903 REMARK 350 BIOMT1 12 -0.809017 -0.308979 -0.500024 770.87015 REMARK 350 BIOMT2 12 0.309098 0.499931 -0.809029 281.26510 REMARK 350 BIOMT3 12 0.499950 -0.809074 -0.308948 455.11015 REMARK 350 BIOMT1 13 -0.309110 -0.499907 -0.809039 764.29144 REMARK 350 BIOMT2 13 -0.499886 0.809110 -0.308959 291.85342 REMARK 350 BIOMT3 13 0.809052 0.308925 -0.500000 103.37092 REMARK 350 BIOMT1 14 -0.000169 0.000034 -1.000000 586.41618 REMARK 350 BIOMT2 14 -1.000000 0.000135 0.000169 579.70527 REMARK 350 BIOMT3 14 0.000135 1.000000 0.000034 6.53300 REMARK 350 BIOMT1 15 -0.309141 0.499943 -0.809005 483.06194 REMARK 350 BIOMT2 15 -0.500104 -0.809017 -0.308848 747.01919 REMARK 350 BIOMT3 15 -0.808905 0.309109 0.500124 298.42311 REMARK 350 BIOMT1 16 -0.500197 -0.808917 -0.308960 764.30070 REMARK 350 BIOMT2 16 -0.808917 0.309210 0.500043 291.83835 REMARK 350 BIOMT3 16 -0.308960 0.500043 -0.809012 472.31526 REMARK 350 BIOMT1 17 0.308800 -0.500114 -0.809029 579.88783 REMARK 350 BIOMT2 17 -0.500114 -0.808898 0.309143 569.09714 REMARK 350 BIOMT3 17 -0.809029 0.309143 -0.499902 586.31235 REMARK 350 BIOMT1 18 0.308986 0.499838 -0.809129 298.60327 REMARK 350 BIOMT2 18 0.499838 -0.809136 -0.308967 448.58312 REMARK 350 BIOMT3 18 -0.809129 -0.308967 -0.499850 760.18371 REMARK 350 BIOMT1 19 -0.499897 0.809041 -0.309121 309.17273 REMARK 350 BIOMT2 19 0.809041 0.308824 -0.500081 96.84258 REMARK 350 BIOMT3 19 -0.309121 -0.500081 -0.808927 753.64503 REMARK 350 BIOMT1 20 -1.000000 0.000186 0.000000 596.98957 REMARK 350 BIOMT2 20 0.000186 1.000000 -0.000085 -0.03102 REMARK 350 BIOMT3 20 0.000000 -0.000085 -1.000000 575.73254 REMARK 350 BIOMT1 21 -0.000016 -0.000034 1.000000 10.68101 REMARK 350 BIOMT2 21 -1.000000 0.000050 -0.000016 579.78255 REMARK 350 BIOMT3 21 -0.000050 -1.000000 -0.000034 569.15041 REMARK 350 BIOMT1 22 0.309048 -0.500093 0.808948 114.06631 REMARK 350 BIOMT2 22 -0.500093 -0.808950 -0.309041 747.05254 REMARK 350 BIOMT3 22 0.808948 -0.309041 -0.500098 277.24613 REMARK 350 BIOMT1 23 0.809094 -0.309055 0.499852 0.03325 REMARK 350 BIOMT2 23 0.308855 -0.500000 -0.809079 562.60404 REMARK 350 BIOMT3 23 0.499976 0.809002 -0.309094 0.02584 REMARK 350 BIOMT1 24 0.809074 0.309071 0.499874 -173.82835 REMARK 350 BIOMT2 24 0.308905 0.499943 -0.809095 281.33862 REMARK 350 BIOMT3 24 -0.499976 0.809032 0.309017 120.59855 REMARK 350 BIOMT1 25 0.309017 0.500057 0.808982 -167.24768 REMARK 350 BIOMT2 25 -0.500012 0.808991 -0.309067 291.95552 REMARK 350 BIOMT3 25 -0.809010 -0.308993 0.500026 472.33688 REMARK 350 BIOMT1 26 0.808940 0.308936 -0.500174 114.11761 REMARK 350 BIOMT2 26 -0.309222 -0.500000 -0.808939 747.07241 REMARK 350 BIOMT3 26 -0.499997 0.809048 -0.308940 298.48204 REMARK 350 BIOMT1 27 0.000016 1.000000 -0.000135 17.28379 REMARK 350 BIOMT2 27 -0.000119 -0.000135 -1.000000 569.19903 REMARK 350 BIOMT3 27 -1.000000 0.000016 0.000119 586.33643 REMARK 350 BIOMT1 28 -0.809017 0.309098 0.499950 309.17628 REMARK 350 BIOMT2 28 -0.308979 0.499931 -0.809074 465.78692 REMARK 350 BIOMT3 28 -0.500024 -0.809029 -0.308948 753.61042 REMARK 350 BIOMT1 29 -0.500103 -0.808967 0.308981 586.40957 REMARK 350 BIOMT2 29 -0.808967 0.309125 -0.500014 579.74809 REMARK 350 BIOMT3 29 0.308981 -0.500014 -0.809022 569.13704 REMARK 350 BIOMT1 30 0.499850 -0.809067 -0.309129 465.85669 REMARK 350 BIOMT2 30 -0.809117 -0.308867 -0.499931 753.59208 REMARK 350 BIOMT3 30 0.308997 0.500012 -0.809017 287.85224 REMARK 350 BIOMT1 31 -0.500000 -0.808948 0.309198 586.31110 REMARK 350 BIOMT2 31 0.809060 -0.308975 0.499957 -17.25920 REMARK 350 BIOMT3 31 -0.308905 0.500138 0.808975 6.52760 REMARK 350 BIOMT1 32 0.499953 -0.809086 -0.308913 465.76900 REMARK 350 BIOMT2 32 0.809024 0.309017 0.499988 -191.08082 REMARK 350 BIOMT3 32 -0.309074 -0.499888 0.809064 287.83086 REMARK 350 BIOMT1 33 0.809074 0.308905 -0.499976 114.02952 REMARK 350 BIOMT2 33 0.309071 0.499943 0.809032 -184.49584 REMARK 350 BIOMT3 33 0.499874 -0.809095 0.309017 277.25490 REMARK 350 BIOMT1 34 0.000169 1.000000 0.000050 17.18466 REMARK 350 BIOMT2 34 0.000119 -0.000050 1.000000 -6.60449 REMARK 350 BIOMT3 34 1.000000 -0.000169 -0.000119 -10.58467 REMARK 350 BIOMT1 35 -0.808883 0.309129 0.500148 309.07073 REMARK 350 BIOMT2 35 0.309129 -0.499989 0.808981 96.75344 REMARK 350 BIOMT3 35 0.500148 0.808981 0.308872 -177.90334 REMARK 350 BIOMT1 36 -0.308924 0.500046 -0.809024 482.97386 REMARK 350 BIOMT2 36 0.500162 0.808924 0.308998 -184.51112 REMARK 350 BIOMT3 36 0.808952 -0.309186 -0.500000 277.25736 REMARK 350 BIOMT1 37 -0.809017 0.309179 -0.499900 596.96448 REMARK 350 BIOMT2 37 -0.308812 0.500069 0.809053 -0.08611 REMARK 350 BIOMT3 37 0.500126 0.808913 -0.309086 0.00399 REMARK 350 BIOMT1 38 -0.809151 -0.308948 -0.499826 770.84453 REMARK 350 BIOMT2 38 -0.308948 -0.499874 0.809121 281.18953 REMARK 350 BIOMT3 38 -0.499826 0.809121 0.309025 120.52626 REMARK 350 BIOMT1 39 -0.309141 -0.500104 -0.808905 764.31770 REMARK 350 BIOMT2 39 0.499943 -0.809017 0.309109 270.60243 REMARK 350 BIOMT3 39 -0.809005 -0.308848 0.500124 472.26649 REMARK 350 BIOMT1 40 0.000016 -0.000119 -1.000000 586.40383 REMARK 350 BIOMT2 40 1.000000 -0.000135 0.000016 -17.21640 REMARK 350 BIOMT3 40 -0.000135 -1.000000 0.000119 569.13163 REMARK 350 BIOMT1 41 -0.000016 -1.000000 -0.000050 579.81144 REMARK 350 BIOMT2 41 -0.000034 0.000050 -1.000000 569.12152 REMARK 350 BIOMT3 41 1.000000 -0.000016 -0.000034 -10.65212 REMARK 350 BIOMT1 42 0.808960 -0.309005 -0.500100 287.89976 REMARK 350 BIOMT2 42 -0.309086 0.500057 -0.808955 465.74942 REMARK 350 BIOMT3 42 0.500050 0.808986 0.309017 -177.91735 REMARK 350 BIOMT1 43 0.499953 0.809024 -0.309074 10.68763 REMARK 350 BIOMT2 43 -0.809086 0.309017 -0.499888 579.77769 REMARK 350 BIOMT3 43 -0.308913 0.499988 0.809064 6.54637 REMARK 350 BIOMT1 44 -0.500000 0.809010 0.309036 131.27278 REMARK 350 BIOMT2 44 -0.809051 -0.309059 -0.499919 753.62314 REMARK 350 BIOMT3 44 -0.308929 -0.499986 0.809059 287.81644 REMARK 350 BIOMT1 45 -0.808998 -0.309029 0.500024 483.01064 REMARK 350 BIOMT2 45 -0.309029 -0.500011 -0.809005 747.03727 REMARK 350 BIOMT3 45 0.500024 -0.809005 0.309009 277.18719 REMARK 350 BIOMT1 46 -0.500000 0.809060 -0.308905 309.13567 REMARK 350 BIOMT2 46 -0.808948 -0.308975 0.500138 465.69777 REMARK 350 BIOMT3 46 0.309198 0.499957 0.808975 -177.93795 REMARK 350 BIOMT1 47 -1.000000 0.000000 0.000153 596.99772 REMARK 350 BIOMT2 47 0.000000 -1.000000 0.000085 562.51793 REMARK 350 BIOMT3 47 0.000153 0.000085 1.000000 -0.06952 REMARK 350 BIOMT1 48 -0.500000 -0.809051 -0.308929 764.27049 REMARK 350 BIOMT2 48 0.809010 -0.309059 -0.499986 270.61750 REMARK 350 BIOMT3 48 0.309036 -0.499919 0.809059 103.32215 REMARK 350 BIOMT1 49 0.309017 -0.500012 -0.809010 579.78870 REMARK 350 BIOMT2 49 0.500057 0.808991 -0.308993 -6.60704 REMARK 350 BIOMT3 49 0.808982 -0.309067 0.500026 -10.64671 REMARK 350 BIOMT1 50 0.309017 0.500036 -0.808995 298.49992 REMARK 350 BIOMT2 50 -0.499896 0.809043 0.309117 113.95920 REMARK 350 BIOMT3 50 0.809081 0.308891 0.499974 -184.47501 REMARK 350 BIOMT1 51 -0.308924 0.500162 0.808952 17.19965 REMARK 350 BIOMT2 51 0.500046 0.808924 -0.309186 -6.52952 REMARK 350 BIOMT3 51 -0.809024 0.308998 -0.500000 586.37980 REMARK 350 BIOMT1 52 -0.309110 -0.499886 0.809052 298.51082 REMARK 350 BIOMT2 52 -0.499907 0.809110 0.308925 113.99923 REMARK 350 BIOMT3 52 -0.809039 -0.308959 -0.500000 760.19789 REMARK 350 BIOMT1 53 0.499850 -0.809117 0.308998 287.94035 REMARK 350 BIOMT2 53 -0.809067 -0.308867 0.500012 465.73921 REMARK 350 BIOMT3 53 -0.309129 -0.499931 -0.809017 753.63103 REMARK 350 BIOMT1 54 1.000000 -0.000186 -0.000153 0.09628 REMARK 350 BIOMT2 54 -0.000186 -1.000000 0.000000 562.59773 REMARK 350 BIOMT3 54 -0.000153 0.000000 -1.000000 575.75439 REMARK 350 BIOMT1 55 0.500150 0.808993 0.308836 -167.23067 REMARK 350 BIOMT2 55 0.808891 -0.309167 -0.500112 270.71960 REMARK 350 BIOMT3 55 -0.309105 0.499946 -0.809017 472.38746 REMARK 350 BIOMT1 56 0.808940 -0.309222 -0.499997 287.93681 REMARK 350 BIOMT2 56 0.308936 -0.500000 0.809048 96.79487 REMARK 350 BIOMT3 56 -0.500174 -0.808939 -0.308940 753.62768 REMARK 350 BIOMT1 57 0.500150 0.808891 -0.309105 10.67528 REMARK 350 BIOMT2 57 0.808993 -0.309167 0.499946 -17.18193 REMARK 350 BIOMT3 57 0.308836 -0.500112 -0.809017 569.20640 REMARK 350 BIOMT1 58 -0.499802 0.809143 0.309005 131.18511 REMARK 350 BIOMT2 58 0.809143 0.308909 0.499862 -191.04976 REMARK 350 BIOMT3 58 0.309005 0.499862 -0.809107 287.91787 REMARK 350 BIOMT1 59 -0.809017 -0.308812 0.500126 482.92581 REMARK 350 BIOMT2 59 0.309179 0.500069 0.808913 -184.52919 REMARK 350 BIOMT3 59 -0.499900 0.809053 -0.309086 298.49328 REMARK 350 BIOMT1 60 -0.000169 -1.000000 0.000135 579.80369 REMARK 350 BIOMT2 60 0.000034 0.000135 1.000000 -6.63142 REMARK 350 BIOMT3 60 -1.000000 0.000169 0.000034 586.31777 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 A 1 REMARK 465 ASP A 9 REMARK 465 GLN A 10 REMARK 465 THR A 11 REMARK 465 VAL A 12 REMARK 465 ASN A 13 REMARK 465 ASN A 14 REMARK 465 GLN A 15 REMARK 465 VAL A 16 REMARK 465 ASN A 17 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 CYS G 214 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 CZ PHE A 233 C15 SPH A 301 2.14 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 63 -36.41 -131.44 REMARK 500 ASN A 218 54.98 -93.83 REMARK 500 LEU A 220 45.56 -89.18 REMARK 500 ILE A 262 78.98 58.13 REMARK 500 PRO B 83 32.77 -92.18 REMARK 500 GLU C 54 75.90 -102.73 REMARK 500 ASN C 56 56.10 -92.73 REMARK 500 SER C 163 52.00 -93.38 REMARK 500 ARG C 178 113.43 -160.75 REMARK 500 LEU C 228 75.20 61.36 REMARK 500 THR C 238 -62.70 -93.70 REMARK 500 ASN C 240 149.57 -172.03 REMARK 500 PRO D 56 55.05 -90.60 REMARK 500 ASN G 31 19.14 57.06 REMARK 500 THR G 52 -39.66 -131.89 REMARK 500 ASN G 138 73.58 58.89 REMARK 500 ASN G 190 -31.63 -130.02 REMARK 500 PHE F 64 27.84 -140.16 REMARK 500 ASP F 90 31.01 -92.44 REMARK 500 PRO F 193 35.08 -91.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-33670 RELATED DB: EMDB REMARK 900 THE STRUCTURE OF COXSACKIEVIRUS A16 MATURE VIRION IN COMPLEX WITH REMARK 900 FAB 8C4 DBREF 7Y7M A 1 297 UNP M4TAU2 M4TAU2_9ENTO 566 862 DBREF 7Y7M B 1 254 UNP A9LXZ4 A9LXZ4_9ENTO 70 323 DBREF 7Y7M C 1 242 UNP A9LXZ4 A9LXZ4_9ENTO 324 565 DBREF 7Y7M D 1 69 UNP A8TSC7 A8TSC7_9ENTO 1 69 DBREF 7Y7M G 1 214 PDB 7Y7M 7Y7M 1 214 DBREF 7Y7M F 1 214 PDB 7Y7M 7Y7M 1 214 SEQADV 7Y7M ARG D 52 UNP A8TSC7 LYS 52 CONFLICT SEQRES 1 A 297 GLY ASP PRO ILE ALA ASP MET ILE ASP GLN THR VAL ASN SEQRES 2 A 297 ASN GLN VAL ASN ARG SER LEU THR ALA LEU GLN VAL LEU SEQRES 3 A 297 PRO THR ALA ALA ASN THR GLU ALA SER SER HIS ARG LEU SEQRES 4 A 297 GLY THR GLY VAL VAL PRO ALA LEU GLN ALA ALA GLU THR SEQRES 5 A 297 GLY ALA SER SER ASN ALA SER ASP LYS ASN LEU ILE GLU SEQRES 6 A 297 THR ARG CYS VAL LEU ASN HIS HIS SER THR GLN GLU THR SEQRES 7 A 297 ALA ILE GLY ASN PHE PHE SER ARG ALA GLY LEU VAL SER SEQRES 8 A 297 ILE ILE THR MET PRO THR MET GLY THR GLN ASN THR ASP SEQRES 9 A 297 GLY TYR ALA ASN TRP ASP ILE ASP LEU MET GLY TYR ALA SEQRES 10 A 297 GLN LEU ARG ARG LYS CYS GLU LEU PHE THR TYR MET ARG SEQRES 11 A 297 PHE ASP ALA GLU PHE THR PHE VAL VAL ALA LYS PRO ASN SEQRES 12 A 297 GLY GLU LEU VAL PRO GLN LEU LEU GLN TYR MET TYR VAL SEQRES 13 A 297 PRO PRO GLY ALA PRO LYS PRO THR SER ARG ASP SER PHE SEQRES 14 A 297 ALA TRP GLN THR ALA THR ASN PRO SER VAL PHE VAL LYS SEQRES 15 A 297 MET THR 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 LEU GLN ALA ASN ASP LEU ASP SEQRES 18 A 297 TYR GLY GLN CYS PRO ASN ASN MET MET GLY THR PHE SER SEQRES 19 A 297 ILE ARG THR VAL GLY THR LYS LYS SER PRO HIS SER ILE SEQRES 20 A 297 THR LEU ARG VAL TYR MET ARG ILE LYS HIS VAL ARG ALA SEQRES 21 A 297 TRP ILE PRO ARG PRO LEU ARG ASN GLN PRO TYR LEU PHE SEQRES 22 A 297 LYS THR ASN PRO ASN TYR LYS GLY ASN ASP ILE LYS CYS SEQRES 23 A 297 THR SER THR SER ARG ASP LYS 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 VAL ILE ALA TYR GLY GLU TRP PRO SEQRES 4 B 254 GLU TYR CYS PRO ASP THR ASP ALA THR ALA VAL ASP LYS SEQRES 5 B 254 PRO THR ARG PRO ASP VAL SER VAL ASN ARG PHE PHE THR SEQRES 6 B 254 LEU ASP THR LYS SER TRP ALA LYS ASP SER LYS GLY TRP SEQRES 7 B 254 TYR TRP LYS PHE PRO ASP VAL LEU THR GLU VAL 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 VAL 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 LEU GLY THR ILE ALA GLY GLY THR GLY ASN GLU ASN SEQRES 12 B 254 SER HIS PRO PRO TYR ALA THR THR GLN PRO GLY GLN VAL SEQRES 13 B 254 GLY ALA VAL LEU THR HIS PRO TYR VAL LEU ASP ALA GLY SEQRES 14 B 254 ILE PRO LEU 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 MET ASN THR VAL PRO PHE ASP SER ALA LEU ASN SEQRES 17 B 254 HIS CYS ASN PHE GLY LEU LEU VAL ILE PRO VAL VAL PRO SEQRES 18 B 254 LEU ASP PHE ASN ALA GLY ALA THR SER GLU ILE PRO ILE SEQRES 19 B 254 THR VAL THR ILE ALA PRO MET CYS ALA GLU PHE ALA GLY SEQRES 20 B 254 LEU ARG GLN ALA VAL LYS GLN SEQRES 1 C 242 GLY ILE 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 GLY PHE HIS PRO THR PRO PRO ILE HIS ILE PRO GLY GLU SEQRES 4 C 242 VAL ARG ASN LEU LEU GLU ILE CYS ARG VAL GLU THR ILE SEQRES 5 C 242 LEU GLU VAL ASN ASN LEU LYS THR ASN GLU THR THR PRO SEQRES 6 C 242 MET GLN ARG LEU CYS PHE PRO VAL SER VAL GLN SER LYS SEQRES 7 C 242 THR GLY GLU LEU CYS ALA ALA PHE ARG ALA ASP PRO GLY SEQRES 8 C 242 ARG ASP GLY PRO TRP GLN SER THR ILE LEU GLY GLN LEU SEQRES 9 C 242 CYS ARG TYR TYR THR GLN TRP SER GLY SER LEU GLU VAL SEQRES 10 C 242 THR PHE MET PHE ALA GLY SER PHE MET ALA THR GLY LYS SEQRES 11 C 242 MET LEU ILE ALA TYR THR PRO PRO GLY GLY SER VAL PRO SEQRES 12 C 242 ALA ASP ARG ILE 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 VAL SEQRES 14 C 242 PRO TRP ILE SER ASN THR HIS TYR ARG ALA HIS ALA ARG SEQRES 15 C 242 ALA GLY TYR PHE ASP TYR TYR THR THR GLY ILE ILE THR SEQRES 16 C 242 ILE TRP TYR GLN THR ASN TYR VAL VAL PRO ILE GLY ALA SEQRES 17 C 242 PRO THR THR ALA TYR ILE VAL ALA LEU ALA ALA ALA GLN SEQRES 18 C 242 ASP ASN PHE THR MET LYS LEU CYS LYS ASP THR GLU ASP SEQRES 19 C 242 ILE GLU GLN THR ALA ASN 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 SER GLU GLY SER THR ILE ASN SEQRES 3 D 69 TYR THR THR ILE ASN TYR TYR LYS ASP ALA TYR ALA ALA SEQRES 4 D 69 SER ALA GLY ARG GLN ASP MET SER GLN ASP PRO LYS ARG SEQRES 5 D 69 PHE THR ASP PRO VAL MET ASP VAL ILE HIS GLU MET ALA SEQRES 6 D 69 PRO PRO LEU LYS SEQRES 1 G 214 ASP ILE GLN MET THR GLN SER SER SER TYR LEU SER VAL SEQRES 2 G 214 SER LEU GLY GLY ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 G 214 ASP HIS ILE ASN ASN TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 G 214 PRO GLY ASN ALA PRO ARG LEU LEU ILE SER GLY ALA THR SEQRES 5 G 214 SER LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 G 214 GLY SER GLY LYS ASP TYR THR LEU SER ILE THR SER LEU SEQRES 7 G 214 GLN THR GLU ASP VAL ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 G 214 TRP ASN SER PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 G 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 G 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 G 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 G 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 G 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 G 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 G 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 G 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 G 214 PHE ASN ARG ASN GLU CYS SEQRES 1 F 214 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 F 214 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 F 214 TYR ALA PHE SER THR SER TRP MET ASN TRP VAL ILE GLN SEQRES 4 F 214 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE TYR SEQRES 5 F 214 PRO GLY ASP GLY ASP THR ASN TYR ASN GLY LYS PHE LYS SEQRES 6 F 214 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 F 214 ALA TYR MET GLN LEU SER SER LEU THR SER VAL ASP SER SEQRES 8 F 214 ALA VAL TYR PHE CYS ALA ARG ARG ASP TYR GLY TYR PHE SEQRES 9 F 214 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 F 214 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11 F 214 GLY CYS GLY ASP THR THR GLY SER SER VAL THR LEU GLY SEQRES 12 F 214 CYS LEU VAL LYS GLY TYR PHE PRO GLU SER VAL THR VAL SEQRES 13 F 214 THR TRP ASN SER GLY SER LEU SER SER SER VAL HIS THR SEQRES 14 F 214 PHE PRO ALA LEU LEU GLN SER GLY LEU TYR THR MET SER SEQRES 15 F 214 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLN SEQRES 16 F 214 THR VAL THR CYS SER VAL ALA HIS PRO ALA SER SER THR SEQRES 17 F 214 THR VAL ASP LYS LYS LEU HET SPH A 301 21 HETNAM SPH SPHINGOSINE FORMUL 7 SPH C18 H37 N O2 HELIX 1 AA1 ALA A 49 GLY A 53 5 5 HELIX 2 AA2 SER A 59 LEU A 63 5 5 HELIX 3 AA3 ALA A 79 PHE A 84 1 6 HELIX 4 AA4 TYR A 116 GLU A 124 1 9 HELIX 5 AA5 SER A 168 THR A 173 5 6 HELIX 6 AA6 CYS A 225 MET A 229 5 5 HELIX 7 AA7 TYR B 35 GLU B 37 5 3 HELIX 8 AA8 PRO B 83 THR B 87 5 5 HELIX 9 AA9 VAL B 89 PHE B 98 1 10 HELIX 10 AB1 ILE B 135 THR B 139 5 5 HELIX 11 AB2 PRO B 147 GLN B 152 1 6 HELIX 12 AB3 GLN B 174 CYS B 178 5 5 HELIX 13 AB4 LEU C 43 ARG C 48 1 6 HELIX 14 AB5 THR C 64 CYS C 70 5 7 HELIX 15 AB6 GLY C 94 SER C 98 5 5 HELIX 16 AB7 THR C 99 ARG C 106 1 8 HELIX 17 AB8 ASP C 145 MET C 150 1 6 HELIX 18 AB9 GLY C 184 THR C 190 5 7 HELIX 19 AC1 ASP D 35 ALA D 39 5 5 HELIX 20 AC2 PRO D 50 ASP D 55 1 6 HELIX 21 AC3 GLN G 124 SER G 127 5 4 HELIX 22 AC4 ASP G 184 ARG G 188 5 5 HELIX 23 AC5 ALA F 28 SER F 32 5 5 HELIX 24 AC6 GLY F 62 LYS F 65 5 4 HELIX 25 AC7 THR F 87 SER F 91 5 5 SHEET 1 AA1 2 GLN A 24 VAL A 25 0 SHEET 2 AA1 2 SER D 47 GLN D 48 -1 O GLN D 48 N GLN A 24 SHEET 1 AA2 4 GLY A 88 MET A 95 0 SHEET 2 AA2 4 ILE A 247 MET A 253 -1 O ILE A 247 N MET A 95 SHEET 3 AA2 4 PHE A 126 ALA A 140 -1 N ALA A 140 O THR A 248 SHEET 4 AA2 4 LYS A 256 PRO A 263 -1 O LYS A 256 N ASP A 132 SHEET 1 AA3 4 TYR A 201 GLN A 202 0 SHEET 2 AA3 4 PHE A 126 ALA A 140 -1 N MET A 129 O TYR A 201 SHEET 3 AA3 4 ALA A 188 VAL A 192 -1 O VAL A 192 N ALA A 133 SHEET 4 AA3 4 ALA C 22 PRO C 23 1 O ALA C 22 N SER A 191 SHEET 1 AA4 4 TYR A 106 ASP A 110 0 SHEET 2 AA4 4 THR A 232 THR A 237 -1 O ILE A 235 N ALA A 107 SHEET 3 AA4 4 LEU A 151 VAL A 156 -1 N VAL A 156 O THR A 232 SHEET 4 AA4 4 SER A 178 VAL A 181 -1 O VAL A 181 N LEU A 151 SHEET 1 AA5 2 ALA B 14 ILE B 18 0 SHEET 2 AA5 2 SER B 21 THR B 25 -1 O THR B 25 N ALA B 14 SHEET 1 AA6 5 ILE B 31 ILE B 33 0 SHEET 2 AA6 5 CYS B 190 VAL B 195 1 O ILE B 194 N VAL B 32 SHEET 3 AA6 5 HIS B 99 GLN B 111 -1 N PHE B 106 O VAL B 195 SHEET 4 AA6 5 ILE B 232 LEU B 248 -1 O MET B 241 N GLY B 105 SHEET 5 AA6 5 PHE B 64 THR B 65 -1 N PHE B 64 O ILE B 238 SHEET 1 AA7 5 ILE B 31 ILE B 33 0 SHEET 2 AA7 5 CYS B 190 VAL B 195 1 O ILE B 194 N VAL B 32 SHEET 3 AA7 5 HIS B 99 GLN B 111 -1 N PHE B 106 O VAL B 195 SHEET 4 AA7 5 ILE B 232 LEU B 248 -1 O MET B 241 N GLY B 105 SHEET 5 AA7 5 LYS B 69 TRP B 71 -1 N LYS B 69 O ILE B 234 SHEET 1 AA8 5 ALA B 158 VAL B 159 0 SHEET 2 AA8 5 TRP B 78 PHE B 82 -1 N TYR B 79 O ALA B 158 SHEET 3 AA8 5 PHE B 212 ASP B 223 -1 O VAL B 216 N TRP B 78 SHEET 4 AA8 5 GLN B 119 PRO B 128 -1 N LEU B 127 O GLY B 213 SHEET 5 AA8 5 HIS B 180 ASN B 184 -1 O GLN B 181 N VAL B 124 SHEET 1 AA9 3 THR C 51 LEU C 53 0 SHEET 2 AA9 3 THR C 211 ALA C 220 -1 O ALA C 216 N LEU C 53 SHEET 3 AA9 3 PHE C 71 SER C 74 -1 N VAL C 73 O ALA C 212 SHEET 1 AB1 4 THR C 51 LEU C 53 0 SHEET 2 AB1 4 THR C 211 ALA C 220 -1 O ALA C 216 N LEU C 53 SHEET 3 AB1 4 LEU C 115 PHE C 121 -1 N THR C 118 O LEU C 217 SHEET 4 AB1 4 SER C 164 VAL C 169 -1 O VAL C 169 N LEU C 115 SHEET 1 AB2 4 LEU C 82 ARG C 87 0 SHEET 2 AB2 4 ILE C 193 VAL C 203 -1 O ILE C 196 N CYS C 83 SHEET 3 AB2 4 THR C 128 THR C 136 -1 N THR C 128 O VAL C 203 SHEET 4 AB2 4 THR C 153 ASP C 158 -1 O TRP C 157 N MET C 131 SHEET 1 AB3 3 ARG C 178 ALA C 179 0 SHEET 2 AB3 3 TYR C 108 SER C 112 -1 N TRP C 111 O ARG C 178 SHEET 3 AB3 3 THR C 225 CYS C 229 -1 O THR C 225 N SER C 112 SHEET 1 AB4 6 TYR G 10 SER G 12 0 SHEET 2 AB4 6 THR G 102 GLU G 105 1 O LYS G 103 N LEU G 11 SHEET 3 AB4 6 THR G 85 GLN G 90 -1 N TYR G 86 O THR G 102 SHEET 4 AB4 6 LEU G 33 GLN G 38 -1 N TYR G 36 O TYR G 87 SHEET 5 AB4 6 ARG G 45 SER G 49 -1 O LEU G 47 N TRP G 35 SHEET 6 AB4 6 SER G 53 LEU G 54 -1 O SER G 53 N SER G 49 SHEET 1 AB5 3 ARG G 18 LYS G 24 0 SHEET 2 AB5 3 ASP G 70 THR G 76 -1 O LEU G 73 N ILE G 21 SHEET 3 AB5 3 PHE G 62 GLY G 66 -1 N SER G 65 O THR G 72 SHEET 1 AB6 4 THR G 114 PHE G 118 0 SHEET 2 AB6 4 GLY G 129 PHE G 139 -1 O PHE G 135 N SER G 116 SHEET 3 AB6 4 TYR G 173 THR G 182 -1 O LEU G 181 N ALA G 130 SHEET 4 AB6 4 LEU G 160 TRP G 163 -1 N SER G 162 O SER G 176 SHEET 1 AB7 4 SER G 153 GLU G 154 0 SHEET 2 AB7 4 ASN G 145 ILE G 150 -1 N ILE G 150 O SER G 153 SHEET 3 AB7 4 SER G 191 THR G 197 -1 O GLU G 195 N LYS G 147 SHEET 4 AB7 4 ILE G 205 ASN G 210 -1 O PHE G 209 N TYR G 192 SHEET 1 AB8 4 GLN F 3 GLN F 6 0 SHEET 2 AB8 4 VAL F 18 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AB8 4 THR F 78 LEU F 83 -1 O MET F 81 N ILE F 20 SHEET 4 AB8 4 ALA F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AB9 6 GLU F 10 VAL F 12 0 SHEET 2 AB9 6 THR F 111 VAL F 115 1 O THR F 112 N GLU F 10 SHEET 3 AB9 6 ALA F 92 ARG F 99 -1 N TYR F 94 O THR F 111 SHEET 4 AB9 6 MET F 34 GLN F 39 -1 N ASN F 35 O ALA F 97 SHEET 5 AB9 6 GLU F 46 ILE F 51 -1 O GLU F 46 N ILE F 38 SHEET 6 AB9 6 THR F 58 TYR F 60 -1 O ASN F 59 N ARG F 50 SHEET 1 AC1 4 GLU F 10 VAL F 12 0 SHEET 2 AC1 4 THR F 111 VAL F 115 1 O THR F 112 N GLU F 10 SHEET 3 AC1 4 ALA F 92 ARG F 99 -1 N TYR F 94 O THR F 111 SHEET 4 AC1 4 PHE F 104 TRP F 107 -1 O TYR F 106 N ARG F 98 SHEET 1 AC2 3 SER F 124 LEU F 128 0 SHEET 2 AC2 3 SER F 139 TYR F 149 -1 O LEU F 145 N TYR F 126 SHEET 3 AC2 3 TYR F 179 SER F 182 -1 O MET F 181 N VAL F 146 SHEET 1 AC3 3 SER F 124 LEU F 128 0 SHEET 2 AC3 3 SER F 139 TYR F 149 -1 O LEU F 145 N TYR F 126 SHEET 3 AC3 3 VAL F 185 PRO F 188 -1 O VAL F 185 N LEU F 142 SHEET 1 AC4 3 THR F 157 TRP F 158 0 SHEET 2 AC4 3 THR F 198 SER F 200 -1 O SER F 200 N THR F 157 SHEET 3 AC4 3 ASP F 211 LYS F 213 -1 O LYS F 212 N CYS F 199 SSBOND 1 CYS G 23 CYS G 88 1555 1555 2.04 SSBOND 2 CYS G 134 CYS G 194 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 4 CYS F 144 CYS F 199 1555 1555 2.04 CISPEP 1 PHE B 82 PRO B 83 0 3.21 CISPEP 2 SER G 7 SER G 8 0 3.34 CISPEP 3 THR G 76 SER G 77 0 -2.23 CISPEP 4 SER G 94 PRO G 95 0 0.35 CISPEP 5 TYR G 140 PRO G 141 0 -5.97 CISPEP 6 GLN G 156 ASN G 157 0 13.88 CISPEP 7 PRO F 41 GLY F 42 0 -2.17 CISPEP 8 PRO F 130 GLY F 131 0 1.95 CISPEP 9 THR F 136 GLY F 137 0 5.17 CISPEP 10 PHE F 150 PRO F 151 0 0.56 CISPEP 11 GLU F 152 SER F 153 0 -2.79 CISPEP 12 TRP F 192 PRO F 193 0 2.09 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