HEADER VIRUS 29-JUL-22 7YMS TITLE CRYO-EM STRUCTURE OF COXSACKIEVIRUS A16 IN COMPLEX WITH A NEUTRALIZING TITLE 2 ANTIBODY 9B5 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 HEAVY CHAIN OF FAB 9B5; COMPND 23 CHAIN: F; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: THE LIGHT CHAIN OF FAB 9B5; COMPND 27 CHAIN: E; 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 9B5, CRYO-EM, STRUCTURAL PROTEIN, VIRUS EXPDTA ELECTRON MICROSCOPY AUTHOR Y.CONG,C.X.LIU REVDAT 1 24-AUG-22 7YMS 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. 2.90 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 3122 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 7YMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-AUG-22. REMARK 100 THE DEPOSITION ID IS D_1300031281. 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 IN COMPLEX REMARK 245 WITH A NEUTRALIZING ANTIBODY 9B5 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) : 3800.00 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, F, E 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 0.499998 0.808944 0.309210 -167.27914 REMARK 350 BIOMT2 2 -0.809092 0.309017 0.499878 291.99235 REMARK 350 BIOMT3 2 0.308823 -0.500118 0.809019 103.45345 REMARK 350 BIOMT1 3 -0.309021 0.499807 0.809135 17.27591 REMARK 350 BIOMT2 3 -0.500194 -0.809017 0.308703 569.28134 REMARK 350 BIOMT3 3 0.808895 -0.309329 0.500004 -10.54088 REMARK 350 BIOMT1 4 -0.309021 -0.500194 0.808895 298.61635 REMARK 350 BIOMT2 4 0.499807 -0.809017 -0.309329 448.66301 REMARK 350 BIOMT3 4 0.809135 0.308703 0.500004 -184.44671 REMARK 350 BIOMT1 5 0.499998 -0.809092 0.308823 287.93925 REMARK 350 BIOMT2 5 0.808944 0.309017 -0.500118 96.82779 REMARK 350 BIOMT3 5 0.309210 0.499878 0.809019 -177.93208 REMARK 350 BIOMT1 6 0.308917 -0.500252 0.808899 114.16406 REMARK 350 BIOMT2 6 -0.500252 -0.808810 -0.309152 747.09233 REMARK 350 BIOMT3 6 0.808899 -0.309152 -0.500107 277.29435 REMARK 350 BIOMT1 7 0.809014 -0.309235 0.499870 0.10238 REMARK 350 BIOMT2 7 0.308803 -0.500000 -0.809099 562.62502 REMARK 350 BIOMT3 7 0.500136 0.808934 -0.309014 -0.02533 REMARK 350 BIOMT1 8 0.809076 0.308895 0.499979 -173.80981 REMARK 350 BIOMT2 8 0.309079 0.499941 -0.809030 281.26845 REMARK 350 BIOMT3 8 -0.499865 0.809100 0.309017 120.54620 REMARK 350 BIOMT1 9 0.309017 0.499903 0.809077 -167.23177 REMARK 350 BIOMT2 9 -0.499806 0.809128 -0.309040 291.84784 REMARK 350 BIOMT3 9 -0.809137 -0.308882 0.499889 472.38319 REMARK 350 BIOMT1 10 -0.000099 -0.000177 1.000000 10.74586 REMARK 350 BIOMT2 10 -1.000000 0.000276 -0.000099 579.74283 REMARK 350 BIOMT3 10 -0.000276 -1.000000 -0.000177 569.25887 REMARK 350 BIOMT1 11 -0.809074 -0.308899 -0.499981 770.85247 REMARK 350 BIOMT2 11 -0.308899 -0.500232 0.808919 281.33403 REMARK 350 BIOMT3 11 -0.499981 0.808919 0.309305 120.54861 REMARK 350 BIOMT1 12 -0.309013 -0.499902 -0.809079 764.27265 REMARK 350 BIOMT2 12 0.500097 -0.809017 0.308861 270.62812 REMARK 350 BIOMT3 12 -0.808959 -0.309176 0.499996 472.38174 REMARK 350 BIOMT1 13 0.000099 0.000182 -1.000000 586.29452 REMARK 350 BIOMT2 13 1.000000 0.000084 0.000099 -17.30168 REMARK 350 BIOMT3 13 0.000084 -1.000000 -0.000182 569.15299 REMARK 350 BIOMT1 14 -0.308921 0.500254 -0.808897 482.87781 REMARK 350 BIOMT2 14 0.499961 0.808921 0.309331 -184.54618 REMARK 350 BIOMT3 14 0.809078 -0.308858 -0.500000 277.12779 REMARK 350 BIOMT1 15 -0.809017 0.309231 -0.499868 596.94090 REMARK 350 BIOMT2 15 -0.308983 0.499709 0.809210 0.02084 REMARK 350 BIOMT3 15 0.500021 0.809115 -0.308726 -0.12497 REMARK 350 BIOMT1 16 -0.499843 0.809152 -0.308919 309.06710 REMARK 350 BIOMT2 16 0.809152 0.309041 -0.499767 96.65828 REMARK 350 BIOMT3 16 -0.308919 -0.499767 -0.809198 753.57442 REMARK 350 BIOMT1 17 -1.000000 0.000192 0.000000 596.98774 REMARK 350 BIOMT2 17 0.000192 1.000000 0.000360 -0.16086 REMARK 350 BIOMT3 17 0.000000 0.000360 -1.000000 575.60752 REMARK 350 BIOMT1 18 -0.500154 -0.808885 -0.309114 764.32300 REMARK 350 BIOMT2 18 -0.808885 0.308993 0.500229 291.83652 REMARK 350 BIOMT3 18 -0.309114 0.500229 -0.808839 472.25907 REMARK 350 BIOMT1 19 0.308925 -0.499963 -0.809075 579.82123 REMARK 350 BIOMT2 19 -0.499963 -0.809032 0.309038 569.11997 REMARK 350 BIOMT3 19 -0.809075 0.309038 -0.499893 586.35311 REMARK 350 BIOMT1 20 0.309117 0.500039 -0.808955 298.45761 REMARK 350 BIOMT2 20 0.500039 -0.809002 -0.308994 448.49318 REMARK 350 BIOMT3 20 -0.808955 -0.308994 -0.500115 760.21555 REMARK 350 BIOMT1 21 -0.500000 0.808981 0.309111 131.25935 REMARK 350 BIOMT2 21 -0.808942 -0.308837 -0.500233 753.61835 REMARK 350 BIOMT3 21 -0.309214 -0.500169 0.808837 288.01702 REMARK 350 BIOMT1 22 -0.809079 -0.309075 0.499864 483.09381 REMARK 350 BIOMT2 22 -0.309075 -0.499650 -0.809211 747.00855 REMARK 350 BIOMT3 22 0.499864 -0.809211 0.308729 277.37344 REMARK 350 BIOMT1 23 -0.000099 -1.000000 -0.000276 579.90091 REMARK 350 BIOMT2 23 -0.000177 0.000276 -1.000000 569.10080 REMARK 350 BIOMT3 23 1.000000 -0.000099 -0.000177 -10.58780 REMARK 350 BIOMT1 24 0.808958 -0.308959 -0.500132 287.89653 REMARK 350 BIOMT2 24 -0.309135 0.500059 -0.808935 465.75757 REMARK 350 BIOMT3 24 0.500023 0.809003 0.309017 -177.91407 REMARK 350 BIOMT1 25 0.500002 0.809053 -0.308920 10.62080 REMARK 350 BIOMT2 25 -0.808979 0.309017 -0.500062 579.79568 REMARK 350 BIOMT3 25 -0.309115 0.499942 0.809015 6.63386 REMARK 350 BIOMT1 26 -0.309113 -0.499748 -0.809136 764.27562 REMARK 350 BIOMT2 26 -0.500037 0.809113 -0.308705 291.82469 REMARK 350 BIOMT3 26 0.808957 0.309173 -0.500000 103.32930 REMARK 350 BIOMT1 27 -0.000094 0.000177 -1.000000 586.35331 REMARK 350 BIOMT2 27 -1.000000 -0.000084 0.000094 579.78869 REMARK 350 BIOMT3 27 -0.000084 1.000000 0.000177 6.55715 REMARK 350 BIOMT1 28 -0.309013 0.500097 -0.808959 482.96727 REMARK 350 BIOMT2 28 -0.499902 -0.809017 -0.309176 747.05306 REMARK 350 BIOMT3 28 -0.809079 0.308861 0.499996 298.58183 REMARK 350 BIOMT1 29 -0.808955 0.309139 -0.500025 596.99349 REMARK 350 BIOMT2 29 0.309139 -0.499768 -0.809114 562.46413 REMARK 350 BIOMT3 29 -0.500025 -0.809114 0.308724 575.83516 REMARK 350 BIOMT1 30 -0.809017 -0.308799 -0.500135 770.85161 REMARK 350 BIOMT2 30 0.309055 0.500291 -0.808823 281.11752 REMARK 350 BIOMT3 30 0.499977 -0.808920 -0.309308 455.16246 REMARK 350 BIOMT1 31 0.000094 -0.000182 1.000000 10.68993 REMARK 350 BIOMT2 31 1.000000 -0.000276 -0.000094 -17.14520 REMARK 350 BIOMT3 31 0.000276 1.000000 0.000182 6.44836 REMARK 350 BIOMT1 32 0.309017 -0.500098 0.808956 114.07448 REMARK 350 BIOMT2 32 0.500193 0.808906 0.308996 -184.51457 REMARK 350 BIOMT3 32 -0.808898 0.309149 0.500111 298.41341 REMARK 350 BIOMT1 33 0.808958 -0.309135 0.500023 0.04686 REMARK 350 BIOMT2 33 -0.308959 0.500059 0.809003 -0.02535 REMARK 350 BIOMT3 33 -0.500132 -0.808935 0.309017 575.73252 REMARK 350 BIOMT1 34 0.809014 0.308803 0.500136 -173.81065 REMARK 350 BIOMT2 34 -0.309235 -0.500000 0.808934 281.36464 REMARK 350 BIOMT3 34 0.499870 -0.809099 -0.309014 455.16011 REMARK 350 BIOMT1 35 0.309109 0.499746 0.809139 -167.23287 REMARK 350 BIOMT2 35 0.499746 -0.809224 0.308885 270.78399 REMARK 350 BIOMT3 35 0.809139 0.308885 -0.499885 103.32315 REMARK 350 BIOMT1 36 0.809020 -0.309051 -0.499975 287.85873 REMARK 350 BIOMT2 36 0.308979 -0.500000 0.809031 96.78680 REMARK 350 BIOMT3 36 -0.500019 -0.809004 -0.309020 753.62270 REMARK 350 BIOMT1 37 0.500155 0.808996 -0.308820 10.56202 REMARK 350 BIOMT2 37 0.808882 -0.309172 0.500122 -17.19803 REMARK 350 BIOMT3 37 0.309118 -0.499938 -0.809017 569.07338 REMARK 350 BIOMT1 38 -0.499846 0.809038 0.309211 131.16858 REMARK 350 BIOMT2 38 0.809038 0.308682 0.500173 -191.04388 REMARK 350 BIOMT3 38 0.309211 0.500173 -0.808836 287.69083 REMARK 350 BIOMT1 39 -0.809017 -0.308983 0.500021 483.00425 REMARK 350 BIOMT2 39 0.309231 0.499709 0.809115 -184.50169 REMARK 350 BIOMT3 39 -0.499868 0.809210 -0.308726 298.33618 REMARK 350 BIOMT1 40 -0.000094 -1.000000 -0.000084 579.84409 REMARK 350 BIOMT2 40 0.000177 -0.000084 1.000000 -6.61255 REMARK 350 BIOMT3 40 -1.000000 0.000094 0.000177 586.29791 REMARK 350 BIOMT1 41 -0.500000 -0.808942 -0.309214 764.32189 REMARK 350 BIOMT2 41 0.808981 -0.308837 -0.500169 270.61628 REMARK 350 BIOMT3 41 0.309111 -0.500233 0.808837 103.45197 REMARK 350 BIOMT1 42 0.309017 -0.499806 -0.809137 579.76742 REMARK 350 BIOMT2 42 0.499903 0.809128 -0.308882 -6.63170 REMARK 350 BIOMT3 42 0.809077 -0.309040 0.499889 -10.64300 REMARK 350 BIOMT1 43 0.309017 0.500193 -0.808898 298.42786 REMARK 350 BIOMT2 43 -0.500098 0.808906 0.309149 114.04915 REMARK 350 BIOMT3 43 0.808956 0.308996 0.500111 -184.50687 REMARK 350 BIOMT1 44 -0.500000 0.809090 -0.308827 309.10492 REMARK 350 BIOMT2 44 -0.809055 -0.309197 0.499827 465.88201 REMARK 350 BIOMT3 44 0.308916 0.499771 0.809197 -177.86568 REMARK 350 BIOMT1 45 -1.000000 0.000000 -0.000005 597.04327 REMARK 350 BIOMT2 45 0.000000 -1.000000 -0.000360 562.64581 REMARK 350 BIOMT3 45 -0.000005 -0.000360 1.000000 0.10267 REMARK 350 BIOMT1 46 0.000094 1.000000 0.000276 17.14242 REMARK 350 BIOMT2 46 -0.000182 -0.000276 1.000000 -6.45114 REMARK 350 BIOMT3 46 1.000000 -0.000094 0.000182 -10.69271 REMARK 350 BIOMT1 47 -0.808960 0.308955 0.500130 309.14765 REMARK 350 BIOMT2 47 0.308955 -0.500350 0.808824 96.95225 REMARK 350 BIOMT3 47 0.500130 0.808824 0.309310 -177.98032 REMARK 350 BIOMT1 48 -0.500000 -0.809055 0.308916 586.42244 REMARK 350 BIOMT2 48 0.809090 -0.309197 0.499771 -17.15222 REMARK 350 BIOMT3 48 -0.308827 0.499827 0.809197 6.52800 REMARK 350 BIOMT1 49 0.500002 -0.808979 -0.309115 465.78246 REMARK 350 BIOMT2 49 0.809053 0.309017 0.499942 -191.07606 REMARK 350 BIOMT3 49 -0.308920 -0.500062 0.809015 287.84802 REMARK 350 BIOMT1 50 0.809076 0.309079 -0.499865 113.94806 REMARK 350 BIOMT2 50 0.308895 0.499941 0.809100 -184.46243 REMARK 350 BIOMT3 50 0.499979 -0.809030 0.309017 277.20504 REMARK 350 BIOMT1 51 0.809020 0.308979 -0.500019 114.03751 REMARK 350 BIOMT2 51 -0.309051 -0.500000 -0.809004 747.04021 REMARK 350 BIOMT3 51 -0.499975 0.809031 -0.309020 298.50272 REMARK 350 BIOMT1 52 0.000099 1.000000 0.000084 17.19621 REMARK 350 BIOMT2 52 0.000182 0.000084 -1.000000 569.04753 REMARK 350 BIOMT3 52 -1.000000 0.000099 -0.000182 586.39998 REMARK 350 BIOMT1 53 -0.809017 0.309055 0.499977 309.18072 REMARK 350 BIOMT2 53 -0.308799 0.500291 -0.808920 465.58802 REMARK 350 BIOMT3 53 -0.500135 -0.808823 -0.309308 753.68906 REMARK 350 BIOMT1 54 -0.500157 -0.808994 0.308824 586.47837 REMARK 350 BIOMT2 54 -0.808994 0.309352 -0.499831 579.63920 REMARK 350 BIOMT3 54 0.308824 -0.499831 -0.809195 569.18214 REMARK 350 BIOMT1 55 0.499845 -0.809040 -0.309207 465.87323 REMARK 350 BIOMT2 55 -0.809149 -0.308862 -0.499882 753.58622 REMARK 350 BIOMT3 55 0.308923 0.500058 -0.809017 287.86151 REMARK 350 BIOMT1 56 -0.309113 -0.500037 0.808957 298.58180 REMARK 350 BIOMT2 56 -0.499748 0.809113 0.309173 113.87929 REMARK 350 BIOMT3 56 -0.809136 -0.308705 -0.500000 760.15540 REMARK 350 BIOMT1 57 0.499845 -0.809149 0.308923 287.97235 REMARK 350 BIOMT2 57 -0.809040 -0.308862 0.500058 465.71655 REMARK 350 BIOMT3 57 -0.309207 -0.499882 -0.809017 753.64072 REMARK 350 BIOMT1 58 1.000000 -0.000192 0.000005 0.05261 REMARK 350 BIOMT2 58 -0.000192 -1.000000 0.000000 562.59968 REMARK 350 BIOMT3 58 0.000005 0.000000 -1.000000 575.70719 REMARK 350 BIOMT1 59 0.500155 0.808882 0.309118 -167.28213 REMARK 350 BIOMT2 59 0.808996 -0.309172 -0.499938 270.63949 REMARK 350 BIOMT3 59 -0.308820 0.500122 -0.809017 472.25289 REMARK 350 BIOMT1 60 -0.308921 0.499961 0.809078 17.21906 REMARK 350 BIOMT2 60 0.500254 0.808921 -0.308858 -6.68497 REMARK 350 BIOMT3 60 -0.808897 0.309331 -0.500000 586.24816 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 ARG A 18 REMARK 465 SER A 19 REMARK 465 LEU A 20 REMARK 465 THR A 21 REMARK 465 ALA A 22 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 E 214 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 GLN A 101 -60.69 -93.85 REMARK 500 ILE A 262 78.15 54.22 REMARK 500 VAL B 60 -52.30 -123.88 REMARK 500 PRO B 83 45.02 -93.32 REMARK 500 ASN C 56 30.43 -91.77 REMARK 500 ASN C 61 31.17 -96.57 REMARK 500 THR C 238 -67.91 -93.56 REMARK 500 PRO D 56 53.70 -91.53 REMARK 500 LYS F 54 -64.57 -100.40 REMARK 500 ASN F 55 -56.64 -120.42 REMARK 500 ASP F 57 115.47 -160.63 REMARK 500 TYR F 106 72.49 58.79 REMARK 500 ALA E 51 10.72 59.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-33941 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF COXSACKIEVIRUS A16 IN COMPLEX WITH A REMARK 900 NEUTRALIZING ANTIBODY 9B5 DBREF 7YMS A 1 297 UNP M4TAU2 M4TAU2_9ENTO 566 862 DBREF 7YMS B 1 254 UNP A9LXZ4 A9LXZ4_9ENTO 70 323 DBREF 7YMS C 1 242 UNP A9LXZ4 A9LXZ4_9ENTO 324 565 DBREF 7YMS D 1 69 UNP A8TSC7 A8TSC7_9ENTO 1 69 DBREF 7YMS F 1 218 PDB 7YMS 7YMS 1 218 DBREF 7YMS E 1 214 PDB 7YMS 7YMS 1 214 SEQADV 7YMS 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 F 218 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 F 218 PRO GLY ALA SER VAL LYS MET SER CYS LYS THR SER GLY SEQRES 3 F 218 TYR THR PHE THR GLU ASN THR MET HIS TRP VAL ARG GLN SEQRES 4 F 218 SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE TYR SEQRES 5 F 218 PRO LYS ASN ASP ASP THR LYS TYR ASN GLN LYS PHE LYS SEQRES 6 F 218 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 F 218 ALA CYS MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 F 218 ALA VAL TYR TYR CYS ALA ARG GLY ASP TYR GLU ASN TYR SEQRES 9 F 218 PHE TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 F 218 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR SEQRES 11 F 218 PRO LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER SEQRES 12 F 218 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 F 218 SER VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 F 218 SER VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU SEQRES 15 F 218 TYR THR MET SER SER SER VAL THR VAL PRO SER SER THR SEQRES 16 F 218 TRP PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO SEQRES 17 F 218 ALA SER SER THR THR VAL ASP LYS LYS LEU SEQRES 1 E 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER VAL SEQRES 2 E 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 E 214 GLU ASN ILE TYR SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 E 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ALA ALA THR SEQRES 5 E 214 ASN LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 E 214 GLN SER GLU ASP PHE GLY THR TYR TYR CYS GLN GLN PHE SEQRES 8 E 214 TRP ASP THR PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 E 214 ALA ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 E 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 E 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 E 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 E 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 E 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 E 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 E 214 PHE ASN ARG ASN GLU CYS HELIX 1 AA1 ALA A 49 GLY A 53 5 5 HELIX 2 AA2 ALA A 79 SER A 85 1 7 HELIX 3 AA3 TYR A 116 GLU A 124 1 9 HELIX 4 AA4 SER A 168 THR A 173 5 6 HELIX 5 AA5 ASN A 218 TYR A 222 5 5 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 ARG C 68 5 5 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 PHE C 186 THR C 190 5 5 HELIX 19 AC1 PRO D 50 ASP D 55 1 6 HELIX 20 AC2 THR F 28 THR F 30 5 3 HELIX 21 AC3 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 5 LEU A 47 GLN A 48 0 SHEET 2 AA2 5 SER C 164 VAL C 169 -1 O SER C 164 N GLN A 48 SHEET 3 AA2 5 LEU C 115 PHE C 121 -1 N LEU C 115 O VAL C 169 SHEET 4 AA2 5 THR C 211 ALA C 220 -1 O LEU C 217 N THR C 118 SHEET 5 AA2 5 THR C 51 LEU C 53 -1 N LEU C 53 O ALA C 216 SHEET 1 AA3 5 LEU A 47 GLN A 48 0 SHEET 2 AA3 5 SER C 164 VAL C 169 -1 O SER C 164 N GLN A 48 SHEET 3 AA3 5 LEU C 115 PHE C 121 -1 N LEU C 115 O VAL C 169 SHEET 4 AA3 5 THR C 211 ALA C 220 -1 O LEU C 217 N THR C 118 SHEET 5 AA3 5 CYS C 70 SER C 74 -1 N VAL C 73 O ALA C 212 SHEET 1 AA4 5 GLY A 88 MET A 95 0 SHEET 2 AA4 5 ILE A 247 PRO A 263 -1 O LEU A 249 N ILE A 93 SHEET 3 AA4 5 PHE A 126 ALA A 140 -1 N ARG A 130 O ARG A 259 SHEET 4 AA4 5 ALA A 188 VAL A 192 -1 O VAL A 192 N ALA A 133 SHEET 5 AA4 5 ALA C 22 PRO C 23 1 O ALA C 22 N SER A 191 SHEET 1 AA5 4 TYR A 201 GLN A 202 0 SHEET 2 AA5 4 PHE A 126 ALA A 140 -1 N MET A 129 O TYR A 201 SHEET 3 AA5 4 ILE A 247 PRO A 263 -1 O ARG A 259 N ARG A 130 SHEET 4 AA5 4 GLU C 39 VAL C 40 -1 O VAL C 40 N ALA A 260 SHEET 1 AA6 4 TYR A 106 ASP A 110 0 SHEET 2 AA6 4 THR A 232 THR A 237 -1 O PHE A 233 N TRP A 109 SHEET 3 AA6 4 LEU A 150 VAL A 156 -1 N VAL A 156 O THR A 232 SHEET 4 AA6 4 PHE A 180 LYS A 182 -1 O VAL A 181 N LEU A 151 SHEET 1 AA7 2 ALA B 14 ILE B 18 0 SHEET 2 AA7 2 SER B 21 THR B 25 -1 O ILE B 23 N LEU B 16 SHEET 1 AA8 5 VAL B 32 ILE B 33 0 SHEET 2 AA8 5 CYS B 190 VAL B 195 1 O ILE B 194 N VAL B 32 SHEET 3 AA8 5 HIS B 99 GLN B 111 -1 N PHE B 106 O VAL B 195 SHEET 4 AA8 5 ILE B 232 LEU B 248 -1 O MET B 241 N GLY B 105 SHEET 5 AA8 5 PHE B 64 TRP B 71 -1 N PHE B 64 O ILE B 238 SHEET 1 AA9 5 ALA B 158 VAL B 159 0 SHEET 2 AA9 5 TRP B 78 PHE B 82 -1 N TYR B 79 O ALA B 158 SHEET 3 AA9 5 PHE B 212 ASP B 223 -1 O LEU B 214 N TRP B 80 SHEET 4 AA9 5 GLN B 119 PRO B 128 -1 N ALA B 125 O LEU B 215 SHEET 5 AA9 5 HIS B 180 ASN B 184 -1 O ILE B 183 N LEU B 122 SHEET 1 AB1 4 LEU C 82 ARG C 87 0 SHEET 2 AB1 4 ILE C 193 VAL C 203 -1 O ILE C 194 N PHE C 86 SHEET 3 AB1 4 THR C 128 THR C 136 -1 N LEU C 132 O TRP C 197 SHEET 4 AB1 4 THR C 153 ASP C 158 -1 O THR C 153 N TYR C 135 SHEET 1 AB2 2 TYR C 108 SER C 112 0 SHEET 2 AB2 2 THR C 225 CYS C 229 -1 O THR C 225 N SER C 112 SHEET 1 AB3 4 GLN F 3 GLN F 6 0 SHEET 2 AB3 4 CYS F 22 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AB3 4 THR F 78 LEU F 83 -1 O ALA F 79 N CYS F 22 SHEET 4 AB3 4 VAL F 18 LYS F 19 -1 N VAL F 18 O LEU F 83 SHEET 1 AB4 4 GLN F 3 GLN F 6 0 SHEET 2 AB4 4 CYS F 22 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AB4 4 THR F 78 LEU F 83 -1 O ALA F 79 N CYS F 22 SHEET 4 AB4 4 ALA F 68 ASP F 73 -1 N THR F 71 O CYS F 80 SHEET 1 AB5 6 LEU F 11 VAL F 12 0 SHEET 2 AB5 6 THR F 115 VAL F 119 1 O THR F 118 N VAL F 12 SHEET 3 AB5 6 ALA F 92 TYR F 101 -1 N TYR F 94 O THR F 115 SHEET 4 AB5 6 ASN F 32 SER F 40 -1 N THR F 33 O GLY F 99 SHEET 5 AB5 6 SER F 44 ILE F 51 -1 O ILE F 48 N TRP F 36 SHEET 6 AB5 6 THR F 58 TYR F 60 -1 O LYS F 59 N GLY F 50 SHEET 1 AB6 3 SER F 128 TYR F 130 0 SHEET 2 AB6 3 LEU F 149 LYS F 151 -1 O LYS F 151 N SER F 128 SHEET 3 AB6 3 THR F 184 MET F 185 -1 O MET F 185 N VAL F 150 SHEET 1 AB7 3 THR F 159 THR F 161 0 SHEET 2 AB7 3 THR F 202 HIS F 207 -1 O ALA F 206 N THR F 159 SHEET 3 AB7 3 THR F 212 LYS F 217 -1 O THR F 212 N HIS F 207 SHEET 1 AB8 4 MET E 4 SER E 7 0 SHEET 2 AB8 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AB8 4 TYR E 71 ILE E 75 -1 O ILE E 75 N VAL E 19 SHEET 4 AB8 4 PHE E 62 GLY E 66 -1 N SER E 63 O LYS E 74 SHEET 1 AB9 5 SER E 10 SER E 12 0 SHEET 2 AB9 5 THR E 102 ALA E 105 1 O LYS E 103 N LEU E 11 SHEET 3 AB9 5 GLY E 84 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB9 5 LEU E 33 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AB9 5 GLN E 45 LEU E 46 -1 O GLN E 45 N GLN E 37 SHEET 1 AC1 2 VAL E 48 TYR E 49 0 SHEET 2 AC1 2 ASN E 53 LEU E 54 -1 O ASN E 53 N TYR E 49 SHEET 1 AC2 2 THR E 114 ILE E 117 0 SHEET 2 AC2 2 CYS E 134 ASN E 137 -1 O ASN E 137 N THR E 114 SHEET 1 AC3 3 VAL E 146 LYS E 149 0 SHEET 2 AC3 3 TYR E 192 ALA E 196 -1 O GLU E 195 N LYS E 147 SHEET 3 AC3 3 SER E 208 PHE E 209 -1 O PHE E 209 N TYR E 192 SSBOND 1 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 2 CYS F 148 CYS F 203 1555 1555 2.03 SSBOND 3 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 4 CYS E 134 CYS E 194 1555 1555 2.03 CISPEP 1 PHE B 82 PRO B 83 0 0.06 CISPEP 2 HIS F 41 GLY F 42 0 -0.84 CISPEP 3 PRO F 134 GLY F 135 0 0.71 CISPEP 4 THR F 140 GLY F 141 0 -1.86 CISPEP 5 PHE F 154 PRO F 155 0 -4.05 CISPEP 6 GLU F 156 SER F 157 0 0.84 CISPEP 7 TRP F 196 PRO F 197 0 -2.34 CISPEP 8 SER E 7 PRO E 8 0 -1.54 CISPEP 9 ASN E 76 SER E 77 0 -0.51 CISPEP 10 THR E 94 PRO E 95 0 2.66 CISPEP 11 TYR E 140 PRO E 141 0 0.95 CISPEP 12 GLN E 156 ASN E 157 0 -2.36 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