HEADER VIRUS 07-MAR-21 7EAJ TITLE ECHOVIRUS3 EMPTY EXPANDED PARTICLE IN COMPLEX WITH 5G3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: VP1; COMPND 3 CHAIN: 1; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: VP0; COMPND 6 CHAIN: 2; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: VP3; COMPND 9 CHAIN: 3; COMPND 10 MOL_ID: 4; COMPND 11 MOLECULE: HEAVY CHAIN OF 5G3 FAB; COMPND 12 CHAIN: F; COMPND 13 MOL_ID: 5; COMPND 14 MOLECULE: LIGHT CHAIN OF 5G3 FAB; COMPND 15 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ECHOVIRUS E3; SOURCE 3 ORGANISM_TAXID: 47516; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: ECHOVIRUS E3; SOURCE 6 ORGANISM_TAXID: 47516; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: ECHOVIRUS E3; SOURCE 9 ORGANISM_TAXID: 47516; SOURCE 10 MOL_ID: 4; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 MOL_ID: 5; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090 KEYWDS ECHOVIRUS3, EMPTY EXPANDED PARTICLE, 5G3 FAB, VIRUS EXPDTA ELECTRON MICROSCOPY AUTHOR R.FENG JRNL AUTH R.FENG,L.WANG,D.SHI,B.ZHENG,L.ZHANG,H.HOU,D.XIA,L.CUI, JRNL AUTH 2 X.WANG,S.XU,K.WANG,L.ZHU JRNL TITL STRUCTURAL BASIS FOR NEUTRALIZATION OF AN ANICTERIC JRNL TITL 2 HEPATITIS ASSOCIATED ECHOVIRUS BY A POTENT NEUTRALIZING JRNL TITL 3 ANTIBODY. JRNL REF CELL DISCOV V. 7 35 2021 JRNL REFN ESSN 2056-5968 JRNL PMID 34035235 JRNL DOI 10.1038/S41421-021-00264-3 REMARK 2 REMARK 2 RESOLUTION. 4.10 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) : 4.100 REMARK 3 NUMBER OF PARTICLES : 41237 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 7EAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300021063. 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 : ECHOVIRUS E3 IN COMPLEX WITH REMARK 245 5G3 FAB; ECHOVIRUS E3; FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 QUANTUM (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : DARK FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 30.00 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: 1, 2, 3, F, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.670820 0.688191 0.276393 -182.99649 REMARK 350 BIOMT2 2 -0.162460 0.500000 -0.850651 435.77598 REMARK 350 BIOMT3 2 -0.723607 0.525731 0.447214 216.19075 REMARK 350 BIOMT1 3 0.138196 0.951057 -0.276394 53.89661 REMARK 350 BIOMT2 3 0.425325 -0.309017 -0.850651 499.49081 REMARK 350 BIOMT3 3 -0.894428 -0.000001 -0.447213 674.39260 REMARK 350 BIOMT1 4 0.138196 0.425325 -0.894428 383.30109 REMARK 350 BIOMT2 4 0.951057 -0.309017 -0.000000 103.09276 REMARK 350 BIOMT3 4 -0.276394 -0.850651 -0.447213 741.38616 REMARK 350 BIOMT1 5 0.670820 -0.162460 -0.723607 349.99115 REMARK 350 BIOMT2 5 0.688191 0.500000 0.525731 -205.60954 REMARK 350 BIOMT3 5 0.276393 -0.850651 0.447214 324.58862 REMARK 350 BIOMT1 6 -0.638197 0.262865 -0.723606 604.49423 REMARK 350 BIOMT2 6 0.262865 -0.809017 -0.525731 596.70229 REMARK 350 BIOMT3 6 -0.723606 -0.525731 0.447214 519.01145 REMARK 350 BIOMT1 7 0.052786 -0.688191 -0.723607 679.39551 REMARK 350 BIOMT2 7 0.688191 -0.500000 0.525731 82.39046 REMARK 350 BIOMT3 7 -0.723607 -0.525731 0.447214 519.01141 REMARK 350 BIOMT1 8 0.670820 -0.688191 0.276393 213.40166 REMARK 350 BIOMT2 8 0.162460 0.500000 0.850651 -147.77598 REMARK 350 BIOMT3 8 -0.723607 -0.525731 0.447214 519.01166 REMARK 350 BIOMT1 9 0.361804 0.262865 0.894427 -149.49965 REMARK 350 BIOMT2 9 -0.587785 0.809017 0.000000 224.28517 REMARK 350 BIOMT3 9 -0.723607 -0.525731 0.447213 519.01185 REMARK 350 BIOMT1 10 -0.447214 0.850651 0.276394 92.20885 REMARK 350 BIOMT2 10 -0.525732 0.000000 -0.850651 684.39804 REMARK 350 BIOMT3 10 -0.723606 -0.525732 0.447214 519.01172 REMARK 350 BIOMT1 11 -0.052786 0.688191 0.723607 -103.39551 REMARK 350 BIOMT2 11 0.688191 -0.500000 0.525731 82.39046 REMARK 350 BIOMT3 11 0.723607 0.525731 -0.447214 56.98859 REMARK 350 BIOMT1 12 -0.670820 0.688191 -0.276393 362.59834 REMARK 350 BIOMT2 12 0.162460 0.500000 0.850651 -147.77598 REMARK 350 BIOMT3 12 0.723607 0.525731 -0.447214 56.98834 REMARK 350 BIOMT1 13 -0.361804 -0.262865 -0.894427 725.49965 REMARK 350 BIOMT2 13 -0.587785 0.809017 0.000000 224.28517 REMARK 350 BIOMT3 13 0.723607 0.525731 -0.447213 56.98815 REMARK 350 BIOMT1 14 0.447214 -0.850651 -0.276394 483.79114 REMARK 350 BIOMT2 14 -0.525732 0.000000 -0.850651 684.39804 REMARK 350 BIOMT3 14 0.723606 0.525732 -0.447214 56.98827 REMARK 350 BIOMT1 15 0.638197 -0.262865 0.723606 -28.49424 REMARK 350 BIOMT2 15 0.262865 -0.809017 -0.525731 596.70229 REMARK 350 BIOMT3 15 0.723606 0.525731 -0.447214 56.98855 REMARK 350 BIOMT1 16 -0.309017 -0.951057 0.000000 650.90127 REMARK 350 BIOMT2 16 -0.951057 0.309017 0.000000 472.90723 REMARK 350 BIOMT3 16 0.000000 0.000000 -1.000000 575.99996 REMARK 350 BIOMT1 17 -0.052786 -0.688191 0.723607 293.00264 REMARK 350 BIOMT2 17 -0.688191 -0.500000 -0.525731 781.60953 REMARK 350 BIOMT3 17 0.723607 -0.525731 -0.447214 359.80949 REMARK 350 BIOMT1 18 -0.447213 0.000000 0.894428 159.20207 REMARK 350 BIOMT2 18 0.000000 -1.000000 0.000000 576.00000 REMARK 350 BIOMT3 18 0.894428 0.000000 0.447213 -98.39241 REMARK 350 BIOMT1 19 -0.947213 0.162460 0.276394 434.40741 REMARK 350 BIOMT2 19 0.162460 -0.500000 0.850651 140.22402 REMARK 350 BIOMT3 19 0.276394 0.850651 0.447213 -165.38629 REMARK 350 BIOMT1 20 -0.861804 -0.425325 -0.276393 738.29422 REMARK 350 BIOMT2 20 -0.425325 0.309017 0.850651 76.50919 REMARK 350 BIOMT3 20 -0.276393 0.850651 -0.447213 251.41111 REMARK 350 BIOMT1 21 -0.361803 0.587785 0.723607 14.51850 REMARK 350 BIOMT2 21 0.262865 0.809017 -0.525731 130.70851 REMARK 350 BIOMT3 21 -0.894427 0.000000 -0.447214 674.39262 REMARK 350 BIOMT1 22 -0.861804 0.425325 -0.276393 493.30705 REMARK 350 BIOMT2 22 0.425325 0.309017 -0.850651 321.49702 REMARK 350 BIOMT3 22 -0.276393 -0.850651 -0.447213 741.38611 REMARK 350 BIOMT1 23 -0.447214 -0.525732 -0.723606 776.60689 REMARK 350 BIOMT2 23 0.850651 0.000000 -0.525732 194.42334 REMARK 350 BIOMT3 23 0.276394 -0.850651 0.447214 324.58839 REMARK 350 BIOMT1 24 0.309017 -0.951057 0.000000 472.90727 REMARK 350 BIOMT2 24 0.951057 0.309017 -0.000000 -74.90103 REMARK 350 BIOMT3 24 0.000000 0.000001 1.000000 -0.00025 REMARK 350 BIOMT1 25 0.361803 -0.262865 0.894427 1.91075 REMARK 350 BIOMT2 25 0.587785 0.809017 0.000000 -114.27896 REMARK 350 BIOMT3 25 -0.723607 0.525731 0.447213 216.19066 REMARK 350 BIOMT1 26 -0.138196 -0.951057 0.276394 522.10338 REMARK 350 BIOMT2 26 0.425325 -0.309017 -0.850651 499.49081 REMARK 350 BIOMT3 26 0.894428 0.000001 0.447213 -98.39260 REMARK 350 BIOMT1 27 -0.138196 -0.425325 0.894428 192.69890 REMARK 350 BIOMT2 27 0.951057 -0.309017 -0.000000 103.09276 REMARK 350 BIOMT3 27 0.276394 0.850651 0.447213 -165.38616 REMARK 350 BIOMT1 28 -0.670820 0.162460 0.723607 226.00884 REMARK 350 BIOMT2 28 0.688191 0.500000 0.525731 -205.60953 REMARK 350 BIOMT3 28 -0.276393 0.850651 -0.447214 251.41139 REMARK 350 BIOMT1 29 -1.000000 0.000000 0.000000 575.99999 REMARK 350 BIOMT2 29 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 29 0.000000 0.000000 -1.000000 576.00000 REMARK 350 BIOMT1 30 -0.670820 -0.688191 -0.276393 758.99648 REMARK 350 BIOMT2 30 -0.162460 0.500000 -0.850651 435.77597 REMARK 350 BIOMT3 30 0.723607 -0.525731 -0.447214 359.80925 REMARK 350 BIOMT1 31 0.947213 -0.162460 -0.276394 141.59259 REMARK 350 BIOMT2 31 0.162460 -0.500000 0.850651 140.22402 REMARK 350 BIOMT3 31 -0.276394 -0.850651 -0.447213 741.38629 REMARK 350 BIOMT1 32 0.861804 0.425325 0.276393 -162.29423 REMARK 350 BIOMT2 32 -0.425325 0.309017 0.850651 76.50919 REMARK 350 BIOMT3 32 0.276393 -0.850651 0.447213 324.58889 REMARK 350 BIOMT1 33 0.309017 0.951057 0.000000 -74.90128 REMARK 350 BIOMT2 33 -0.951057 0.309017 0.000000 472.90724 REMARK 350 BIOMT3 33 0.000000 -0.000000 1.000000 0.00004 REMARK 350 BIOMT1 34 0.052786 0.688191 -0.723607 282.99736 REMARK 350 BIOMT2 34 -0.688191 -0.500000 -0.525731 781.60953 REMARK 350 BIOMT3 34 -0.723607 0.525731 0.447214 216.19050 REMARK 350 BIOMT1 35 0.447213 0.000000 -0.894428 416.79792 REMARK 350 BIOMT2 35 0.000000 -1.000000 0.000000 576.00000 REMARK 350 BIOMT3 35 -0.894428 0.000000 -0.447213 674.39241 REMARK 350 BIOMT1 36 -0.447214 0.525732 -0.723606 473.78552 REMARK 350 BIOMT2 36 -0.850651 0.000000 0.525732 381.57666 REMARK 350 BIOMT3 36 0.276394 0.850651 0.447214 -165.38631 REMARK 350 BIOMT1 37 0.138196 -0.425325 -0.894428 628.28826 REMARK 350 BIOMT2 37 -0.951057 -0.309017 0.000000 650.90102 REMARK 350 BIOMT3 37 -0.276394 0.850651 -0.447213 251.41117 REMARK 350 BIOMT1 38 0.809017 -0.587785 -0.000001 224.28553 REMARK 350 BIOMT2 38 -0.587785 -0.809017 0.000000 690.27895 REMARK 350 BIOMT3 38 -0.000001 0.000000 -1.000000 576.00019 REMARK 350 BIOMT1 39 0.638197 0.262865 0.723606 -179.90464 REMARK 350 BIOMT2 39 -0.262865 -0.809017 0.525731 445.29149 REMARK 350 BIOMT3 39 0.723606 -0.525731 -0.447214 359.80975 REMARK 350 BIOMT1 40 -0.138196 0.951057 0.276394 -25.70517 REMARK 350 BIOMT2 40 -0.425325 -0.309017 0.850651 254.50298 REMARK 350 BIOMT3 40 0.894428 -0.000000 0.447213 -98.39231 REMARK 350 BIOMT1 41 -0.361804 0.262865 -0.894427 574.08925 REMARK 350 BIOMT2 41 0.587785 0.809017 0.000000 -114.27896 REMARK 350 BIOMT3 41 0.723607 -0.525731 -0.447213 359.80935 REMARK 350 BIOMT1 42 0.361803 -0.587785 -0.723607 561.48149 REMARK 350 BIOMT2 42 0.262865 0.809017 -0.525731 130.70851 REMARK 350 BIOMT3 42 0.894427 0.000000 0.447214 -98.39262 REMARK 350 BIOMT1 43 0.861804 -0.425325 0.276393 82.69294 REMARK 350 BIOMT2 43 0.425325 0.309017 -0.850651 321.49702 REMARK 350 BIOMT3 43 0.276393 0.850651 0.447213 -165.38611 REMARK 350 BIOMT1 44 0.447214 0.525732 0.723606 -200.60690 REMARK 350 BIOMT2 44 0.850651 0.000000 -0.525732 194.42334 REMARK 350 BIOMT3 44 -0.276394 0.850651 -0.447214 251.41161 REMARK 350 BIOMT1 45 -0.309017 0.951057 0.000000 103.09272 REMARK 350 BIOMT2 45 0.951057 0.309017 -0.000000 -74.90103 REMARK 350 BIOMT3 45 0.000000 -0.000001 -1.000000 576.00025 REMARK 350 BIOMT1 46 0.947213 0.162460 -0.276394 48.01546 REMARK 350 BIOMT2 46 -0.162460 -0.500000 -0.850651 723.77597 REMARK 350 BIOMT3 46 -0.276394 0.850651 -0.447213 251.41148 REMARK 350 BIOMT1 47 0.809017 0.587785 -0.000001 -114.27877 REMARK 350 BIOMT2 47 0.587785 -0.809017 0.000000 351.71483 REMARK 350 BIOMT3 47 -0.000001 0.000000 -1.000000 576.00037 REMARK 350 BIOMT1 48 0.447214 0.850651 -0.276394 -6.18356 REMARK 350 BIOMT2 48 0.525732 0.000000 0.850651 -108.39805 REMARK 350 BIOMT3 48 0.723606 -0.525732 -0.447214 359.80966 REMARK 350 BIOMT1 49 0.361803 0.587785 -0.723607 222.91719 REMARK 350 BIOMT2 49 -0.262865 0.809017 0.525731 -20.70230 REMARK 350 BIOMT3 49 0.894427 0.000000 0.447214 -98.39244 REMARK 350 BIOMT1 50 0.670820 0.162460 -0.723607 256.41402 REMARK 350 BIOMT2 50 -0.688191 0.500000 -0.525731 493.60953 REMARK 350 BIOMT3 50 0.276393 0.850651 0.447214 -165.38620 REMARK 350 BIOMT1 51 -0.447214 -0.850651 0.276394 582.18355 REMARK 350 BIOMT2 51 0.525732 0.000000 0.850651 -108.39805 REMARK 350 BIOMT3 51 -0.723606 0.525732 0.447214 216.19035 REMARK 350 BIOMT1 52 -0.361803 -0.587785 0.723607 353.08281 REMARK 350 BIOMT2 52 -0.262865 0.809017 0.525731 -20.70230 REMARK 350 BIOMT3 52 -0.894427 0.000000 -0.447214 674.39244 REMARK 350 BIOMT1 53 -0.670820 -0.162460 0.723607 319.58597 REMARK 350 BIOMT2 53 -0.688191 0.500000 -0.525731 493.60953 REMARK 350 BIOMT3 53 -0.276393 -0.850651 -0.447214 741.38620 REMARK 350 BIOMT1 54 -0.947213 -0.162460 0.276394 527.98454 REMARK 350 BIOMT2 54 -0.162460 -0.500000 -0.850651 723.77597 REMARK 350 BIOMT3 54 0.276394 -0.850651 0.447213 324.58852 REMARK 350 BIOMT1 55 -0.809017 -0.587785 0.000001 690.27877 REMARK 350 BIOMT2 55 0.587785 -0.809017 0.000000 351.71483 REMARK 350 BIOMT3 55 0.000001 0.000000 1.000000 -0.00037 REMARK 350 BIOMT1 56 -0.138196 0.425325 0.894428 -52.28827 REMARK 350 BIOMT2 56 -0.951057 -0.309017 0.000000 650.90102 REMARK 350 BIOMT3 56 0.276394 -0.850651 0.447213 324.58883 REMARK 350 BIOMT1 57 -0.809017 0.587785 0.000001 351.71446 REMARK 350 BIOMT2 57 -0.587785 -0.809017 0.000000 690.27895 REMARK 350 BIOMT3 57 0.000001 0.000000 1.000000 -0.00019 REMARK 350 BIOMT1 58 -0.638197 -0.262865 -0.723606 755.90463 REMARK 350 BIOMT2 58 -0.262865 -0.809017 0.525731 445.29149 REMARK 350 BIOMT3 58 -0.723606 0.525731 0.447214 216.19025 REMARK 350 BIOMT1 59 0.138196 -0.951057 -0.276394 601.70516 REMARK 350 BIOMT2 59 -0.425325 -0.309017 0.850651 254.50298 REMARK 350 BIOMT3 59 -0.894428 0.000001 -0.447213 674.39231 REMARK 350 BIOMT1 60 0.447214 -0.525732 0.723606 102.21448 REMARK 350 BIOMT2 60 -0.850651 0.000000 0.525732 381.57666 REMARK 350 BIOMT3 60 -0.276394 -0.850651 -0.447214 741.38631 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY 1 1 REMARK 465 ASP 1 2 REMARK 465 VAL 1 3 REMARK 465 GLU 1 4 REMARK 465 GLU 1 5 REMARK 465 ALA 1 6 REMARK 465 ILE 1 7 REMARK 465 ASP 1 8 REMARK 465 ARG 1 9 REMARK 465 ALA 1 10 REMARK 465 VAL 1 11 REMARK 465 ALA 1 12 REMARK 465 ARG 1 13 REMARK 465 VAL 1 14 REMARK 465 ALA 1 15 REMARK 465 ASP 1 16 REMARK 465 THR 1 17 REMARK 465 MET 1 18 REMARK 465 PRO 1 19 REMARK 465 THR 1 20 REMARK 465 GLY 1 21 REMARK 465 PRO 1 22 REMARK 465 ARG 1 23 REMARK 465 ASN 1 24 REMARK 465 THR 1 25 REMARK 465 GLU 1 26 REMARK 465 SER 1 27 REMARK 465 VAL 1 28 REMARK 465 PRO 1 29 REMARK 465 ALA 1 30 REMARK 465 LEU 1 31 REMARK 465 THR 1 32 REMARK 465 ALA 1 33 REMARK 465 VAL 1 34 REMARK 465 GLU 1 35 REMARK 465 THR 1 36 REMARK 465 GLY 1 37 REMARK 465 HIS 1 38 REMARK 465 THR 1 39 REMARK 465 SER 1 40 REMARK 465 GLN 1 41 REMARK 465 VAL 1 42 REMARK 465 VAL 1 43 REMARK 465 PRO 1 44 REMARK 465 GLY 1 45 REMARK 465 ASP 1 46 REMARK 465 THR 1 47 REMARK 465 MET 1 48 REMARK 465 GLN 1 49 REMARK 465 THR 1 50 REMARK 465 ARG 1 51 REMARK 465 HIS 1 52 REMARK 465 VAL 1 53 REMARK 465 LYS 1 54 REMARK 465 ASN 1 55 REMARK 465 GLY 2 2 REMARK 465 ALA 2 3 REMARK 465 GLN 2 4 REMARK 465 VAL 2 5 REMARK 465 SER 2 6 REMARK 465 THR 2 7 REMARK 465 GLN 2 8 REMARK 465 LYS 2 9 REMARK 465 THR 2 10 REMARK 465 GLY 2 11 REMARK 465 ALA 2 12 REMARK 465 HIS 2 13 REMARK 465 GLU 2 14 REMARK 465 THR 2 15 REMARK 465 SER 2 16 REMARK 465 LEU 2 17 REMARK 465 THR 2 18 REMARK 465 ALA 2 19 REMARK 465 SER 2 20 REMARK 465 GLY 2 21 REMARK 465 ASN 2 22 REMARK 465 SER 2 23 REMARK 465 THR 2 24 REMARK 465 ILE 2 25 REMARK 465 HIS 2 26 REMARK 465 TYR 2 27 REMARK 465 THR 2 28 REMARK 465 ASN 2 29 REMARK 465 ILE 2 30 REMARK 465 ASN 2 31 REMARK 465 TYR 2 32 REMARK 465 TYR 2 33 REMARK 465 LYS 2 34 REMARK 465 ASP 2 35 REMARK 465 ALA 2 36 REMARK 465 ALA 2 37 REMARK 465 SER 2 38 REMARK 465 ASN 2 39 REMARK 465 SER 2 40 REMARK 465 ALA 2 41 REMARK 465 ASN 2 42 REMARK 465 ARG 2 43 REMARK 465 GLN 2 44 REMARK 465 ASP 2 45 REMARK 465 PHE 2 46 REMARK 465 THR 2 47 REMARK 465 GLN 2 48 REMARK 465 ASP 2 49 REMARK 465 PRO 2 50 REMARK 465 SER 2 51 REMARK 465 LYS 2 52 REMARK 465 PHE 2 53 REMARK 465 THR 2 54 REMARK 465 GLU 2 55 REMARK 465 PRO 2 56 REMARK 465 MET 2 57 REMARK 465 LYS 2 58 REMARK 465 ASP 2 59 REMARK 465 VAL 2 60 REMARK 465 MET 2 61 REMARK 465 ILE 2 62 REMARK 465 LYS 2 63 REMARK 465 SER 2 64 REMARK 465 LEU 2 65 REMARK 465 PRO 2 66 REMARK 465 ALA 2 67 REMARK 465 LEU 2 68 REMARK 465 ASN 2 69 REMARK 465 SER 2 70 REMARK 465 PRO 2 71 REMARK 465 THR 2 72 REMARK 465 VAL 2 73 REMARK 465 GLU 2 74 REMARK 465 GLU 2 75 REMARK 465 CYS 2 76 REMARK 465 GLY 2 77 REMARK 465 PHE 2 78 REMARK 465 SER 2 79 REMARK 465 ASP 2 80 REMARK 465 GLY 3 1 REMARK 465 LEU 3 2 REMARK 465 PRO 3 3 REMARK 465 THR 3 4 REMARK 465 MET 3 5 REMARK 465 LEU 3 6 REMARK 465 THR 3 7 REMARK 465 PRO 3 8 REMARK 465 GLY 3 9 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS 1 80 CG CD CE NZ REMARK 470 ARG 1 285 CG CD NE CZ NH1 NH2 REMARK 470 GLN 2 232 CG CD OE1 NE2 REMARK 470 TYR F 31 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN F 34 CG CD OE1 NE2 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 PRO 1 86 46.98 -85.27 REMARK 500 THR 1 97 52.17 -97.06 REMARK 500 GLN 1 135 -128.89 57.14 REMARK 500 VAL 1 139 140.77 -173.92 REMARK 500 SER 1 156 -166.65 -162.61 REMARK 500 CYS 1 176 -166.26 -126.17 REMARK 500 SER 1 228 -60.98 -90.95 REMARK 500 VAL 1 249 73.74 52.96 REMARK 500 SER 1 261 48.26 -93.17 REMARK 500 THR 1 290 -43.84 -138.56 REMARK 500 ASN 2 89 47.10 -91.30 REMARK 500 SER 2 90 -23.42 -141.74 REMARK 500 ASN 2 114 50.69 -92.55 REMARK 500 TYR 2 167 48.23 -90.97 REMARK 500 ASN 2 230 18.75 -140.46 REMARK 500 ASN 2 265 -31.07 -130.59 REMARK 500 MET 2 282 52.66 -91.68 REMARK 500 ASN 2 306 46.77 -90.98 REMARK 500 SER 3 16 64.91 -100.57 REMARK 500 LYS 3 59 -10.95 86.04 REMARK 500 ASN 3 63 34.51 -96.24 REMARK 500 ALA 3 67 31.06 -91.02 REMARK 500 LEU 3 78 -2.07 60.54 REMARK 500 SER 3 186 13.64 -148.08 REMARK 500 THR 3 234 -52.01 -125.02 REMARK 500 SER F 30 9.91 54.42 REMARK 500 GLN F 42 -127.85 -109.52 REMARK 500 LYS F 73 -64.37 -98.54 REMARK 500 PRO F 96 38.49 -95.58 REMARK 500 THR F 97 13.13 52.90 REMARK 500 ASP F 101 -126.19 52.01 REMARK 500 SER L 32 31.83 -95.23 REMARK 500 TRP L 56 15.51 58.21 REMARK 500 ALA L 57 10.77 57.59 REMARK 500 ALA L 90 -174.57 -171.30 REMARK 500 TYR L 98 -62.84 -90.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-31045 RELATED DB: EMDB REMARK 900 ECHOVIRUS3 EMPTY EXPANDED PARTICLE IN COMPLEX WITH 5G3 FAB DBREF1 7EAJ 1 1 292 UNP A0A6M4MJE3_9ENTO DBREF2 7EAJ 1 A0A6M4MJE3 569 860 DBREF1 7EAJ 2 2 330 UNP A0A6M4MJE3_9ENTO DBREF2 7EAJ 2 A0A6M4MJE3 2 330 DBREF1 7EAJ 3 1 238 UNP A0A6M4MJE3_9ENTO DBREF2 7EAJ 3 A0A6M4MJE3 331 568 DBREF 7EAJ F 4 112 PDB 7EAJ 7EAJ 4 112 DBREF 7EAJ L 1 115 PDB 7EAJ 7EAJ 1 115 SEQADV 7EAJ ASN 3 224 UNP A0A6M4MJE MET 554 CONFLICT SEQRES 1 1 292 GLY ASP VAL GLU GLU ALA ILE ASP ARG ALA VAL ALA ARG SEQRES 2 1 292 VAL ALA ASP THR MET PRO THR GLY PRO ARG ASN THR GLU SEQRES 3 1 292 SER VAL PRO ALA LEU THR ALA VAL GLU THR GLY HIS THR SEQRES 4 1 292 SER GLN VAL VAL PRO GLY ASP THR MET GLN THR ARG HIS SEQRES 5 1 292 VAL LYS ASN TYR HIS SER ARG THR GLU SER SER ILE GLU SEQRES 6 1 292 ASN PHE LEU CYS ARG ALA ALA CYS VAL TYR ILE ALA THR SEQRES 7 1 292 TYR LYS SER ALA GLY GLY THR PRO THR GLU ARG TYR ALA SEQRES 8 1 292 SER TRP ARG ILE ASN THR ARG GLN MET VAL GLN LEU ARG SEQRES 9 1 292 ARG LYS PHE GLU LEU PHE THR TYR LEU ARG PHE ASP MET SEQRES 10 1 292 GLU ILE THR PHE VAL ILE THR SER THR GLN ASP PRO GLY SEQRES 11 1 292 THR GLN LEU ALA GLN ASP MET PRO VAL LEU THR HIS GLN SEQRES 12 1 292 ILE MET TYR ILE PRO PRO GLY GLY PRO VAL PRO ASN SER SEQRES 13 1 292 ALA THR ASP PHE ALA TRP GLN SER SER THR ASN PRO SER SEQRES 14 1 292 ILE PHE TRP THR GLU GLY CYS ALA PRO ALA ARG MET SER SEQRES 15 1 292 VAL PRO PHE ILE SER ILE GLY ASN ALA TYR SER ASN PHE SEQRES 16 1 292 TYR ASP GLY TRP SER HIS PHE THR GLN GLU GLY VAL TYR SEQRES 17 1 292 GLY PHE ASN SER LEU ASN ASN MET GLY HIS ILE TYR VAL SEQRES 18 1 292 ARG HIS VAL ASN GLU GLN SER LEU GLY VAL SER THR SER SEQRES 19 1 292 THR LEU ARG VAL TYR PHE LYS PRO LYS HIS VAL ARG ALA SEQRES 20 1 292 TRP VAL PRO ARG PRO PRO ARG LEU SER PRO TYR VAL LYS SEQRES 21 1 292 SER SER ASN VAL ASN PHE LYS PRO THR ALA VAL THR THR SEQRES 22 1 292 GLU ARG LYS ASP ILE ASN ASP VAL GLY THR LEU ARG PRO SEQRES 23 1 292 VAL GLY TYR THR ASN HIS SEQRES 1 2 329 GLY ALA GLN VAL SER THR GLN LYS THR GLY ALA HIS GLU SEQRES 2 2 329 THR SER LEU THR ALA SER GLY ASN SER THR ILE HIS TYR SEQRES 3 2 329 THR ASN ILE ASN TYR TYR LYS ASP ALA ALA SER ASN SER SEQRES 4 2 329 ALA ASN ARG GLN ASP PHE THR GLN ASP PRO SER LYS PHE SEQRES 5 2 329 THR GLU PRO MET LYS ASP VAL MET ILE LYS SER LEU PRO SEQRES 6 2 329 ALA LEU ASN SER PRO THR VAL GLU GLU CYS GLY PHE SER SEQRES 7 2 329 ASP ARG VAL ARG SER ILE THR LEU GLY ASN SER THR ILE SEQRES 8 2 329 THR THR GLN GLU CYS ALA ASN VAL VAL VAL GLY TYR GLY SEQRES 9 2 329 VAL TRP PRO SER TYR LEU GLN ASP ASN GLU ALA THR ALA SEQRES 10 2 329 GLU ASP GLN PRO THR GLN PRO ASP VAL ALA THR CYS ARG SEQRES 11 2 329 PHE TYR THR LEU ASP SER ILE GLN TRP GLN LYS GLU SER SEQRES 12 2 329 ASP GLY TRP TRP TRP LYS PHE PRO GLU ALA LEU LYS ASN SEQRES 13 2 329 MET GLY LEU PHE GLY GLN ASN MET GLU TYR HIS TYR LEU SEQRES 14 2 329 GLY ARG SER GLY TYR THR ILE HIS VAL GLN CYS ASN ALA SEQRES 15 2 329 SER LYS PHE HIS GLN GLY CYS LEU LEU VAL VAL CYS VAL SEQRES 16 2 329 PRO GLU ALA GLU MET GLY CYS SER ASP VAL GLU ARG GLU SEQRES 17 2 329 VAL VAL ALA ALA SER LEU SER SER GLU ASP THR ALA LYS SEQRES 18 2 329 SER PHE SER ARG THR GLU SER ASN GLY GLN HIS THR VAL SEQRES 19 2 329 GLN THR VAL VAL TYR ASN ALA GLY MET GLY VAL GLY VAL SEQRES 20 2 329 GLY ASN LEU THR ILE PHE PRO HIS GLN TRP ILE ASN LEU SEQRES 21 2 329 ARG THR ASN ASN SER ALA THR ILE VAL MET PRO TYR ILE SEQRES 22 2 329 ASN SER VAL PRO MET ASP ASN MET PHE ARG HIS TYR ASN SEQRES 23 2 329 PHE THR LEU MET ILE ILE PRO PHE ALA LYS LEU GLU TYR SEQRES 24 2 329 THR GLU GLN ALA SER ASN TYR VAL PRO ILE THR VAL THR SEQRES 25 2 329 VAL ALA PRO MET CYS ALA GLU TYR ASN GLY LEU ARG LEU SEQRES 26 2 329 ALA SER HIS GLN SEQRES 1 3 238 GLY LEU PRO THR MET LEU THR PRO GLY SER ASN GLN PHE SEQRES 2 3 238 LEU THR SER ASP ASP PHE GLN SER PRO SER ALA MET PRO SEQRES 3 3 238 GLN PHE ASP VAL THR PRO GLU MET LYS ILE PRO GLY GLU SEQRES 4 3 238 VAL HIS ASN LEU MET GLU ILE ALA GLU VAL ASP SER VAL SEQRES 5 3 238 VAL PRO VAL ASN ASN THR LYS GLU ASN ILE ASN SER MET SEQRES 6 3 238 GLU ALA TYR ARG ILE PRO VAL THR GLY GLY ASP GLN LEU SEQRES 7 3 238 HIS THR GLN VAL PHE GLY PHE GLN MET GLN PRO GLY LEU SEQRES 8 3 238 ASN SER VAL PHE LYS ARG THR LEU LEU GLY GLU ILE LEU SEQRES 9 3 238 ASN TYR TYR ALA HIS TRP SER GLY SER VAL LYS LEU THR SEQRES 10 3 238 PHE VAL PHE CYS GLY SER ALA MET ALA THR GLY LYS PHE SEQRES 11 3 238 LEU LEU ALA TYR SER PRO PRO GLY ALA SER PRO PRO GLN SEQRES 12 3 238 ASN ARG LYS GLN ALA MET LEU GLY THR HIS VAL ILE TRP SEQRES 13 3 238 ASP VAL GLY LEU GLN SER SER CYS VAL LEU CYS ILE PRO SEQRES 14 3 238 TRP ILE SER GLN THR HIS TYR ARG LEU VAL GLN GLN ASP SEQRES 15 3 238 GLU TYR THR SER ALA GLY TYR VAL THR CYS TRP TYR GLN SEQRES 16 3 238 THR GLY LEU ILE VAL PRO PRO GLY ALA PRO PRO SER CYS SEQRES 17 3 238 THR ILE LEU CYS PHE ALA SER ALA CYS ASN ASP PHE SER SEQRES 18 3 238 VAL ARG ASN LEU ARG ASP THR PRO PHE ILE GLU GLN THR SEQRES 19 3 238 GLN LEU LEU GLN SEQRES 1 F 112 LEU GLN GLN SER GLY ALA GLU LEU ALA ARG PRO TRP ALA SEQRES 2 F 112 SER VAL LYS ILE SER CYS GLN ALA PHE TYR THR PHE ASN SEQRES 3 F 112 SER TYR GLY MET GLN TRP VAL LYS GLN ARG PRO GLY GLN SEQRES 4 F 112 GLY LEU GLU TRP ILE GLY THR ILE TYR PRO GLY ASN GLY SEQRES 5 F 112 GLN THR SER TYR ASN GLN ARG PHE LYS GLY LYS ALA THR SEQRES 6 F 112 LEU THR ALA ASP LYS SER PRO SER THR ALA TYR MET GLN SEQRES 7 F 112 LEU ILE SER LEU THR SER GLU ASP SER ALA GLY CYS PHE SEQRES 8 F 112 CYS ALA VAL VAL PRO THR VAL ASP PHE ASP TYR TRP GLY SEQRES 9 F 112 GLN GLY THR LEU VAL THR VAL SER SEQRES 1 L 115 ASP ILE VAL MET SER GLN SER PRO SER SER LEU ALA VAL SEQRES 2 L 115 SER VAL TRP GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 L 115 GLN SER LEU LEU TYR SER ASN THR GLN LYS ASN TYR LEU SEQRES 4 L 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 L 115 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 115 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 115 LEU THR ILE SER SER VAL LYS ALA GLU ASP LEU ALA VAL SEQRES 8 L 115 TYR TYR CYS GLN GLN TYR TYR SER TYR PRO LEU THR PHE SEQRES 9 L 115 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA HELIX 1 AA1 ARG 1 59 SER 1 62 5 4 HELIX 2 AA2 SER 1 63 CYS 1 69 1 7 HELIX 3 AA3 MET 1 100 GLU 1 108 1 9 HELIX 4 AA4 ASP 1 159 SER 1 164 5 6 HELIX 5 AA5 GLN 2 112 ALA 2 116 5 5 HELIX 6 AA6 PRO 2 125 CYS 2 130 1 6 HELIX 7 AA7 PRO 2 152 LYS 2 156 5 5 HELIX 8 AA8 MET 2 158 TYR 2 167 1 10 HELIX 9 AA9 VAL 2 211 SER 2 216 1 6 HELIX 10 AB1 GLY 2 247 PHE 2 254 5 8 HELIX 11 AB2 LEU 3 43 GLU 3 48 1 6 HELIX 12 AB3 SER 3 64 TYR 3 68 5 5 HELIX 13 AB4 LEU 3 99 LEU 3 104 1 6 HELIX 14 AB5 ASN 3 144 GLY 3 151 1 8 HELIX 15 AB6 GLN F 61 LYS F 64 5 4 HELIX 16 AB7 THR F 83 SER F 87 5 5 SHEET 1 AA1 8 ALA 1 72 CYS 1 73 0 SHEET 2 AA1 8 ALA 1 77 TYR 1 79 0 SHEET 3 AA1 8 PHE 1 110 GLN 1 127 0 SHEET 4 AA1 8 ALA 1 179 VAL 1 183 -1 O VAL 1 183 N MET 1 117 SHEET 5 AA1 8 TYR 1 192 SER 1 193 -1 O TYR 1 192 N LEU 1 113 SHEET 6 AA1 8 SER 1 232 PHE 1 240 -1 O TYR 1 239 N THR 1 120 SHEET 7 AA1 8 PRO 1 242 PRO 1 250 -1 O LYS 1 243 N ASP 1 116 SHEET 8 AA1 8 GLU 3 39 VAL 3 40 -1 O VAL 3 40 N ALA 1 247 SHEET 1 AA2 4 TYR 1 90 ARG 1 94 0 SHEET 2 AA2 4 HIS 1 218 HIS 1 223 -1 O VAL 1 221 N ALA 1 91 SHEET 3 AA2 4 THR 1 141 ILE 1 147 -1 N MET 1 145 O TYR 1 220 SHEET 4 AA2 4 SER 1 169 THR 1 173 -1 O TRP 1 172 N HIS 1 142 SHEET 1 AA3 2 SER 2 84 THR 2 86 0 SHEET 2 AA3 2 ILE 2 92 THR 2 94 -1 O THR 2 93 N ILE 2 85 SHEET 1 AA4 7 VAL 2 101 VAL 2 102 0 SHEET 2 AA4 7 TYR 2 133 THR 2 134 0 SHEET 3 AA4 7 ILE 2 138 TRP 2 140 0 SHEET 4 AA4 7 LEU 2 170 CYS 2 181 0 SHEET 5 AA4 7 SER 2 266 MET 2 271 -1 O ALA 2 267 N VAL 2 179 SHEET 6 AA4 7 VAL 2 308 VAL 2 314 -1 O THR 2 311 N GLN 2 180 SHEET 7 AA4 7 PRO 2 316 ASN 2 322 -1 O MET 2 317 N GLY 2 174 SHEET 1 AA5 5 LYS 2 222 SER 2 223 0 SHEET 2 AA5 5 TRP 2 147 PHE 2 151 -1 N TRP 2 148 O LYS 2 222 SHEET 3 AA5 5 PHE 2 288 GLU 2 299 -1 O PHE 2 288 N PHE 2 151 SHEET 4 AA5 5 GLN 2 188 PRO 2 197 -1 N VAL 2 196 O THR 2 289 SHEET 5 AA5 5 HIS 2 256 ASN 2 260 -1 O ILE 2 259 N LEU 2 191 SHEET 1 AA6 5 SER 3 51 VAL 3 52 0 SHEET 2 AA6 5 ILE 3 70 VAL 3 72 0 SHEET 3 AA6 5 VAL 3 114 PHE 3 120 0 SHEET 4 AA6 5 SER 3 163 ILE 3 168 -1 O LEU 3 166 N LEU 3 116 SHEET 5 AA6 5 CYS 3 208 ALA 3 216 -1 O LEU 3 211 N VAL 3 119 SHEET 1 AA7 4 GLN 3 81 GLN 3 86 0 SHEET 2 AA7 4 TYR 3 189 ILE 3 199 -1 O CYS 3 192 N VAL 3 82 SHEET 3 AA7 4 THR 3 127 SER 3 135 -1 N THR 3 127 O ILE 3 199 SHEET 4 AA7 4 THR 3 152 ASP 3 157 -1 O THR 3 152 N TYR 3 134 SHEET 1 AA8 3 ARG 3 177 LEU 3 178 0 SHEET 2 AA8 3 TYR 3 107 SER 3 111 -1 N TRP 3 110 O ARG 3 177 SHEET 3 AA8 3 SER 3 221 LEU 3 225 -1 O SER 3 221 N SER 3 111 SHEET 1 AA9 4 GLN F 5 GLN F 6 0 SHEET 2 AA9 4 VAL F 18 GLN F 23 -1 O GLN F 23 N GLN F 5 SHEET 3 AA9 4 THR F 77 LEU F 82 -1 O MET F 80 N ILE F 20 SHEET 4 AA9 4 ALA F 67 ALA F 71 -1 N THR F 68 O GLN F 81 SHEET 1 AB1 6 LEU F 11 ALA F 12 0 SHEET 2 AB1 6 LEU F 108 VAL F 111 1 O THR F 110 N ALA F 12 SHEET 3 AB1 6 ALA F 88 VAL F 94 -1 N ALA F 88 O VAL F 109 SHEET 4 AB1 6 MET F 33 GLN F 38 -1 N GLN F 34 O ALA F 93 SHEET 5 AB1 6 LEU F 44 TYR F 51 -1 O GLU F 45 N LYS F 37 SHEET 6 AB1 6 GLN F 56 TYR F 59 -1 O SER F 58 N THR F 49 SHEET 1 AB2 4 MET L 4 SER L 7 0 SHEET 2 AB2 4 SER L 22 SER L 25 -1 O LYS L 24 N SER L 5 SHEET 3 AB2 4 ASP L 76 THR L 80 -1 O PHE L 77 N CYS L 23 SHEET 4 AB2 4 THR L 69 SER L 73 -1 N SER L 71 O THR L 78 SHEET 1 AB3 6 SER L 10 VAL L 13 0 SHEET 2 AB3 6 THR L 108 LEU L 112 1 O GLU L 111 N LEU L 11 SHEET 3 AB3 6 ALA L 90 GLN L 96 -1 N TYR L 92 O THR L 108 SHEET 4 AB3 6 LEU L 39 GLN L 44 -1 N ALA L 40 O GLN L 95 SHEET 5 AB3 6 LYS L 51 TYR L 55 -1 O LEU L 53 N TRP L 41 SHEET 6 AB3 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SSBOND 1 CYS F 22 CYS F 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 94 1555 1555 2.04 CISPEP 1 PHE 2 151 PRO 2 152 0 6.90 CISPEP 2 SER L 7 PRO L 8 0 0.75 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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