HEADER VIRUS/IMMUNE SYSTEM 19-SEP-18 6MID TITLE CRYO-EM STRUCTURE OF THE ZIKV VIRION IN COMPLEX WITH FAB FRAGMENTS OF TITLE 2 THE POTENTLY NEUTRALIZING HUMAN MONOCLONAL ANTIBODY ZIKV-195 COMPND MOL_ID: 1; COMPND 2 MOLECULE: E PROTEIN; COMPND 3 CHAIN: A, C, E; COMPND 4 FRAGMENT: UNP RESIDUES 291-794; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: M PROTEIN; COMPND 7 CHAIN: B, D, F; COMPND 8 FRAGMENT: UNP RESIDUES 216-290; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MONOCLONAL ANTIBODY ZIKV-195 HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 FRAGMENT: FAB VARIABLE DOMAIN; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MONOCLONAL ANTIBODY ZIKV-195 LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 FRAGMENT: FAB VARIABLE DOMAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS (ISOLATE ZIKV/HUMAN/FRENCH SOURCE 3 POLYNESIA/10087PF/2013); SOURCE 4 ORGANISM_COMMON: ZIKV; SOURCE 5 ORGANISM_TAXID: 2043570; SOURCE 6 STRAIN: ISOLATE ZIKV/HUMAN/FRENCH POLYNESIA/10087PF/2013; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ZIKA VIRUS (ISOLATE ZIKV/HUMAN/FRENCH SOURCE 9 POLYNESIA/10087PF/2013); SOURCE 10 ORGANISM_COMMON: ZIKV; SOURCE 11 ORGANISM_TAXID: 2043570; SOURCE 12 STRAIN: ISOLATE ZIKV/HUMAN/FRENCH POLYNESIA/10087PF/2013; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606 KEYWDS VIRUS, MONOCLONAL ANTIBODY, COMPLEX, VIRUS-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR F.LONG,M.G.ROSSMANN REVDAT 1 16-JAN-19 6MID 0 JRNL AUTH F.LONG,M.DOYLE,E.FERNANDEZ,A.S.MILLER,T.KLOSE,M.SEVVANA, JRNL AUTH 2 A.BRYAN,E.DAVIDSON,B.J.DORANZ,R.J.KUHN,M.S.DIAMOND, JRNL AUTH 3 J.E.CROWE,M.G.ROSSMANN JRNL TITL STRUCTURAL BASIS OF A POTENT HUMAN MONOCLONAL ANTIBODY JRNL TITL 2 AGAINST ZIKA VIRUS TARGETING A QUATERNARY EPITOPE JRNL REF PROC.NATL.ACAD.SCI.USA 2019 JRNL REFN ESSN 1091-6490 JRNL DOI 10.1073/PNAS.1815432116 REMARK 2 REMARK 2 RESOLUTION. 4.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : FINDEM, CTFFIND, UCSF CHIMERA, EMFIT, REMARK 3 JSPR, JSPR, RELION, JSPR, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6CO8 REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : THE OCCUPANCY OF BOUND FABS WAS LOW. DUE TO REMARK 3 POOR DENSITY, ONLY THE VARIABLE DOMAIN OF FAB MOLECULE WAS REMARK 3 MODELED AND FIT INTO ONE OF THE THREE FAB BINDING SITES ON EACH REMARK 3 ICOSAHEDRAL ASYMMETRIC UNIT. 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) : 4.000 REMARK 3 NUMBER OF PARTICLES : 10687 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: THE MAP WAS MASKED BY REMOVING THE INTERNAL NUCLEIC REMARK 3 ACID REGION AND THE EXTERNAL BACKGROUND REGION. REMARK 4 REMARK 4 6MID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-18. REMARK 100 THE DEPOSITION ID IS D_1000236256. 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 : ZIKV VIRION IN COMPLEX WITH FAB REMARK 245 FRAGMENTS OF THE POTENTLY REMARK 245 NEUTRALIZING HUMAN MONOCLONAL REMARK 245 ANTIBODY ZIKV-195; ZIKA VIRUS; REMARK 245 MONOCLONAL ANTIBODY ZIKV-195 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : PURIFIED FROM INFECTED VERO REMARK 245 CELLS OVEREXPRESSING THE FURIN PROTEASE REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 1691 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (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 : BRIGHT 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) : 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, E, F, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.361803 0.587785 -0.723607 321.00079 REMARK 350 BIOMT2 2 -0.262865 0.809017 0.525731 -29.81122 REMARK 350 BIOMT3 2 0.894427 0.000000 0.447214 -141.68519 REMARK 350 BIOMT1 3 -0.670820 0.688191 -0.276393 522.14175 REMARK 350 BIOMT2 3 0.162460 0.500000 0.850651 -212.79734 REMARK 350 BIOMT3 3 0.723607 0.525731 -0.447214 82.06311 REMARK 350 BIOMT1 4 -0.670820 0.162460 0.723607 325.45291 REMARK 350 BIOMT2 4 0.688191 0.500000 0.525731 -296.07775 REMARK 350 BIOMT3 4 -0.276393 0.850651 -0.447214 362.03236 REMARK 350 BIOMT1 5 0.361803 -0.262865 0.894427 2.75156 REMARK 350 BIOMT2 5 0.587785 0.809017 0.000000 -164.56177 REMARK 350 BIOMT3 5 -0.723607 0.525731 0.447214 311.31457 REMARK 350 BIOMT1 6 -0.052786 0.688191 0.723607 -148.88937 REMARK 350 BIOMT2 6 0.688191 -0.500000 0.525731 118.64225 REMARK 350 BIOMT3 6 0.723607 0.525731 -0.447214 82.06329 REMARK 350 BIOMT1 7 0.447214 0.525731 0.723607 -288.87389 REMARK 350 BIOMT2 7 0.850651 0.000000 -0.525731 279.96945 REMARK 350 BIOMT3 7 -0.276393 0.850651 -0.447214 362.03253 REMARK 350 BIOMT1 8 0.670820 0.688191 0.276393 -263.51497 REMARK 350 BIOMT2 8 -0.162460 0.500000 -0.850651 627.51733 REMARK 350 BIOMT3 8 -0.723607 0.525731 0.447214 311.31465 REMARK 350 BIOMT1 9 0.309017 0.951057 0.000000 -107.85776 REMARK 350 BIOMT2 9 -0.951057 0.309017 0.000000 680.98653 REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 0.00003 REMARK 350 BIOMT1 10 -0.138196 0.951057 0.276393 -37.01525 REMARK 350 BIOMT2 10 -0.425325 -0.309017 0.850651 366.48443 REMARK 350 BIOMT3 10 0.894427 0.000000 0.447213 -141.68509 REMARK 350 BIOMT1 11 -0.309017 -0.951057 0.000000 937.29777 REMARK 350 BIOMT2 11 -0.951057 0.309017 0.000000 680.98653 REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 829.43998 REMARK 350 BIOMT1 12 0.138196 -0.951057 -0.276393 866.45525 REMARK 350 BIOMT2 12 -0.425325 -0.309017 0.850651 366.48443 REMARK 350 BIOMT3 12 -0.894427 0.000000 -0.447213 971.12511 REMARK 350 BIOMT1 13 0.052786 -0.688191 -0.723607 978.32938 REMARK 350 BIOMT2 13 0.688191 -0.500000 0.525731 118.64225 REMARK 350 BIOMT3 13 -0.723607 -0.525731 0.447214 747.37672 REMARK 350 BIOMT1 14 -0.447214 -0.525731 -0.723607 1118.31390 REMARK 350 BIOMT2 14 0.850651 0.000000 -0.525731 279.96945 REMARK 350 BIOMT3 14 0.276393 -0.850651 0.447214 467.40748 REMARK 350 BIOMT1 15 -0.670820 -0.688191 -0.276393 1092.95497 REMARK 350 BIOMT2 15 -0.162460 0.500000 -0.850651 627.51733 REMARK 350 BIOMT3 15 0.723607 -0.525731 -0.447214 518.12537 REMARK 350 BIOMT1 16 -0.638197 0.262865 -0.723607 870.47161 REMARK 350 BIOMT2 16 0.262865 -0.809017 -0.525731 859.25122 REMARK 350 BIOMT3 16 -0.723607 -0.525731 0.447214 747.37675 REMARK 350 BIOMT1 17 -0.947213 -0.162460 0.276394 760.29786 REMARK 350 BIOMT2 17 -0.162460 -0.500000 -0.850651 1042.23733 REMARK 350 BIOMT3 17 0.276394 -0.850651 0.447213 467.40758 REMARK 350 BIOMT1 18 -0.052786 -0.688191 0.723607 421.92386 REMARK 350 BIOMT2 18 -0.688191 -0.500000 -0.525731 1125.51775 REMARK 350 BIOMT3 18 0.723607 -0.525731 -0.447214 518.12556 REMARK 350 BIOMT1 19 0.809017 -0.587785 0.000000 322.97097 REMARK 350 BIOMT2 19 -0.587785 -0.809017 0.000000 994.00176 REMARK 350 BIOMT3 19 -0.000000 0.000000 -1.000000 829.44015 REMARK 350 BIOMT1 20 0.447213 0.000000 -0.894427 600.18873 REMARK 350 BIOMT2 20 0.000000 -1.000000 0.000000 829.44000 REMARK 350 BIOMT3 20 -0.894427 0.000000 -0.447213 971.12518 REMARK 350 BIOMT1 21 -0.447214 0.525731 -0.723607 682.25130 REMARK 350 BIOMT2 21 -0.850651 0.000000 0.525731 549.47054 REMARK 350 BIOMT3 21 0.276393 0.850651 0.447214 -238.15620 REMARK 350 BIOMT1 22 -0.947213 0.162460 0.276394 625.54698 REMARK 350 BIOMT2 22 0.162460 -0.500000 0.850651 201.92267 REMARK 350 BIOMT3 22 0.276394 0.850651 0.447213 -238.15619 REMARK 350 BIOMT1 23 -0.138196 -0.425325 0.894427 277.48671 REMARK 350 BIOMT2 23 0.951057 -0.309017 0.000000 148.45347 REMARK 350 BIOMT3 23 0.276393 0.850651 0.447213 -238.15609 REMARK 350 BIOMT1 24 0.861804 -0.425325 0.276393 119.07794 REMARK 350 BIOMT2 24 0.425325 0.309017 -0.850651 462.95557 REMARK 350 BIOMT3 24 0.276393 0.850651 0.447213 -238.15605 REMARK 350 BIOMT1 25 0.670820 0.162460 -0.723607 369.23621 REMARK 350 BIOMT2 25 -0.688191 0.500000 -0.525731 710.79775 REMARK 350 BIOMT3 25 0.276393 0.850651 0.447214 -238.15612 REMARK 350 BIOMT1 26 -0.138196 -0.951057 0.276393 751.82907 REMARK 350 BIOMT2 26 0.425325 -0.309017 -0.850651 719.26663 REMARK 350 BIOMT3 26 0.894427 0.000000 0.447213 -141.68531 REMARK 350 BIOMT1 27 0.447214 -0.850651 -0.276393 696.65926 REMARK 350 BIOMT2 27 -0.525731 0.000000 -0.850651 985.53316 REMARK 350 BIOMT3 27 0.723607 0.525731 -0.447214 82.06307 REMARK 350 BIOMT1 28 0.138196 -0.425325 -0.894427 904.73501 REMARK 350 BIOMT2 28 -0.951057 -0.309017 0.000000 937.29758 REMARK 350 BIOMT3 28 -0.276393 0.850651 -0.447213 362.03221 REMARK 350 BIOMT1 29 -0.638197 -0.262865 -0.723607 1088.50270 REMARK 350 BIOMT2 29 -0.262865 -0.809017 0.525731 641.21983 REMARK 350 BIOMT3 29 -0.723607 0.525731 0.447214 311.31428 REMARK 350 BIOMT1 30 -0.809017 -0.587785 0.000000 994.00164 REMARK 350 BIOMT2 30 0.587785 -0.809017 0.000000 506.46929 REMARK 350 BIOMT3 30 0.000000 0.000000 1.000000 -0.00027 REMARK 350 BIOMT1 31 -0.361803 0.587785 0.723607 20.90662 REMARK 350 BIOMT2 31 0.262865 0.809017 -0.525731 188.22016 REMARK 350 BIOMT3 31 -0.894427 0.000000 -0.447214 971.12534 REMARK 350 BIOMT1 32 0.361803 0.262865 0.894427 -215.27953 REMARK 350 BIOMT2 32 -0.587785 0.809017 0.000000 322.97071 REMARK 350 BIOMT3 32 -0.723607 -0.525731 0.447214 747.37704 REMARK 350 BIOMT1 33 0.861804 0.425325 0.276393 -233.70377 REMARK 350 BIOMT2 33 -0.425325 0.309017 0.850651 110.17337 REMARK 350 BIOMT3 33 0.276393 -0.850651 0.447213 467.40785 REMARK 350 BIOMT1 34 0.447214 0.850651 -0.276393 -8.90442 REMARK 350 BIOMT2 34 0.525731 0.000000 0.850651 -156.09316 REMARK 350 BIOMT3 34 0.723607 -0.525731 -0.447214 518.12567 REMARK 350 BIOMT1 35 -0.309017 0.951057 0.000000 148.45345 REMARK 350 BIOMT2 35 0.951057 0.309017 0.000000 -107.85759 REMARK 350 BIOMT3 35 0.000000 0.000000 -1.000000 829.44020 REMARK 350 BIOMT1 36 0.947213 -0.162460 -0.276394 203.89303 REMARK 350 BIOMT2 36 0.162460 -0.500000 0.850651 201.92266 REMARK 350 BIOMT3 36 -0.276394 -0.850651 -0.447213 1067.59620 REMARK 350 BIOMT1 37 0.138196 0.425325 -0.894427 551.95330 REMARK 350 BIOMT2 37 0.951057 -0.309017 0.000000 148.45347 REMARK 350 BIOMT3 37 -0.276393 -0.850651 -0.447213 1067.59611 REMARK 350 BIOMT1 38 -0.861804 0.425325 -0.276393 710.36206 REMARK 350 BIOMT2 38 0.425325 0.309017 -0.850651 462.95557 REMARK 350 BIOMT3 38 -0.276393 -0.850651 -0.447213 1067.59606 REMARK 350 BIOMT1 39 -0.670820 -0.162460 0.723607 460.20379 REMARK 350 BIOMT2 39 -0.688191 0.500000 -0.525731 710.79775 REMARK 350 BIOMT3 39 -0.276393 -0.850651 -0.447214 1067.59613 REMARK 350 BIOMT1 40 0.447214 -0.525731 0.723607 147.18871 REMARK 350 BIOMT2 40 -0.850651 0.000000 0.525731 549.47054 REMARK 350 BIOMT3 40 -0.276393 -0.850651 -0.447214 1067.59622 REMARK 350 BIOMT1 41 -0.447214 -0.850651 0.276393 838.34444 REMARK 350 BIOMT2 41 0.525731 0.000000 0.850651 -156.09316 REMARK 350 BIOMT3 41 -0.723607 0.525731 0.447214 311.31434 REMARK 350 BIOMT1 42 0.309017 -0.951057 0.000000 680.98656 REMARK 350 BIOMT2 42 0.951057 0.309017 0.000000 -107.85759 REMARK 350 BIOMT3 42 0.000000 0.000000 1.000000 -0.00019 REMARK 350 BIOMT1 43 0.361803 -0.587785 -0.723607 808.53339 REMARK 350 BIOMT2 43 0.262865 0.809017 -0.525731 188.22017 REMARK 350 BIOMT3 43 0.894427 0.000000 0.447214 -141.68533 REMARK 350 BIOMT1 44 -0.361803 -0.262865 -0.894427 1044.71954 REMARK 350 BIOMT2 44 -0.587785 0.809017 0.000000 322.97071 REMARK 350 BIOMT3 44 0.723607 0.525731 -0.447214 82.06297 REMARK 350 BIOMT1 45 -0.861804 -0.425325 -0.276393 1063.14378 REMARK 350 BIOMT2 45 -0.425325 0.309017 0.850651 110.17337 REMARK 350 BIOMT3 45 -0.276393 0.850651 -0.447213 362.03216 REMARK 350 BIOMT1 46 -0.361803 0.262865 -0.894427 826.68845 REMARK 350 BIOMT2 46 0.587785 0.809017 0.000000 -164.56177 REMARK 350 BIOMT3 46 0.723607 -0.525731 -0.447214 518.12544 REMARK 350 BIOMT1 47 -1.000000 0.000000 0.000000 829.44001 REMARK 350 BIOMT2 47 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 47 0.000000 0.000000 -1.000000 829.44001 REMARK 350 BIOMT1 48 -0.361803 -0.587785 0.723607 508.43922 REMARK 350 BIOMT2 48 -0.262865 0.809017 0.525731 -29.81123 REMARK 350 BIOMT3 48 -0.894427 0.000000 -0.447214 971.12520 REMARK 350 BIOMT1 49 0.670820 -0.688191 0.276393 307.29827 REMARK 350 BIOMT2 49 0.162460 0.500000 0.850651 -212.79734 REMARK 350 BIOMT3 49 -0.723607 -0.525731 0.447214 747.37690 REMARK 350 BIOMT1 50 0.670820 -0.162460 -0.723607 503.98710 REMARK 350 BIOMT2 50 0.688191 0.500000 0.525731 -296.07775 REMARK 350 BIOMT3 50 0.276393 -0.850651 0.447214 467.40765 REMARK 350 BIOMT1 51 0.947213 0.162460 -0.276394 69.14214 REMARK 350 BIOMT2 51 -0.162460 -0.500000 -0.850651 1042.23733 REMARK 350 BIOMT3 51 -0.276394 0.850651 -0.447213 362.03244 REMARK 350 BIOMT1 52 0.052786 0.688191 -0.723607 407.51614 REMARK 350 BIOMT2 52 -0.688191 -0.500000 -0.525731 1125.51775 REMARK 350 BIOMT3 52 -0.723607 0.525731 0.447214 311.31447 REMARK 350 BIOMT1 53 -0.809017 0.587785 0.000000 506.46903 REMARK 350 BIOMT2 53 -0.587785 -0.809017 0.000000 994.00177 REMARK 350 BIOMT3 53 0.000000 0.000000 1.000000 -0.00013 REMARK 350 BIOMT1 54 -0.447213 0.000000 0.894427 229.25128 REMARK 350 BIOMT2 54 0.000000 -1.000000 0.000000 829.44000 REMARK 350 BIOMT3 54 0.894427 0.000000 0.447213 -141.68516 REMARK 350 BIOMT1 55 0.638197 -0.262865 0.723607 -41.03161 REMARK 350 BIOMT2 55 0.262865 -0.809017 -0.525731 859.25122 REMARK 350 BIOMT3 55 0.723607 0.525731 -0.447214 82.06327 REMARK 350 BIOMT1 56 -0.138196 0.425325 0.894427 -75.29501 REMARK 350 BIOMT2 56 -0.951057 -0.309017 0.000000 937.29758 REMARK 350 BIOMT3 56 0.276393 -0.850651 0.447213 467.40781 REMARK 350 BIOMT1 57 0.638197 0.262865 0.723607 -259.06270 REMARK 350 BIOMT2 57 -0.262865 -0.809017 0.525731 641.21983 REMARK 350 BIOMT3 57 0.723607 -0.525731 -0.447214 518.12574 REMARK 350 BIOMT1 58 0.809017 0.587785 0.000000 -164.56163 REMARK 350 BIOMT2 58 0.587785 -0.809017 0.000000 506.46929 REMARK 350 BIOMT3 58 0.000000 0.000000 -1.000000 829.44028 REMARK 350 BIOMT1 59 0.138196 0.951057 -0.276393 77.61093 REMARK 350 BIOMT2 59 0.425325 -0.309017 -0.850651 719.26662 REMARK 350 BIOMT3 59 -0.894427 0.000000 -0.447213 971.12533 REMARK 350 BIOMT1 60 -0.447214 0.850651 0.276393 132.78074 REMARK 350 BIOMT2 60 -0.525731 0.000000 -0.850651 985.53315 REMARK 350 BIOMT3 60 -0.723607 -0.525731 0.447214 747.37695 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 VAL A 502 REMARK 465 SER A 503 REMARK 465 ALA A 504 REMARK 465 VAL C 502 REMARK 465 SER C 503 REMARK 465 ALA C 504 REMARK 465 VAL E 502 REMARK 465 SER E 503 REMARK 465 ALA E 504 REMARK 465 GLN H 1 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 LEU A 498 CG CD1 CD2 REMARK 470 ALA B 1 N REMARK 470 LEU C 498 CG CD1 CD2 REMARK 470 ASN H 104 CG OD1 ND2 REMARK 470 ASP H 116 CG OD1 OD2 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 O THR E 88 NZ LYS E 239 1.95 REMARK 500 OG1 THR E 321 OG1 THR E 325 2.07 REMARK 500 OE2 GLU C 62 OG SER C 122 2.08 REMARK 500 O HIS E 249 OH TYR H 111 2.12 REMARK 500 O GLY E 182 NH1 ARG E 299 2.13 REMARK 500 O ALA C 272 OG1 THR D 18 2.14 REMARK 500 OH TYR L 37 OH TYR L 99 2.16 REMARK 500 OD1 ASN C 154 OG SER L 95 2.17 REMARK 500 OH TYR C 203 O GLU C 276 2.18 REMARK 500 CD1 ILE C 130 CZ PHE C 198 2.18 REMARK 500 OG SER A 72 NH1 ARG A 99 2.18 REMARK 500 O VAL A 143 ND2 ASN A 163 2.19 REMARK 500 OG1 THR E 315 OE1 GLU E 329 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU C 141 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU E 141 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 LEU E 491 CA - CB - CG ANGL. DEV. = 15.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 CYS A 105 -167.10 -79.27 REMARK 500 SER A 122 -60.07 -94.82 REMARK 500 GLU A 162 -7.26 71.29 REMARK 500 THR A 194 59.15 -91.79 REMARK 500 ASP A 197 46.93 37.09 REMARK 500 TRP A 236 68.40 60.37 REMARK 500 ARG A 252 -50.42 -121.67 REMARK 500 LEU A 269 49.13 -91.71 REMARK 500 ALA A 311 64.02 64.84 REMARK 500 LYS A 316 70.92 59.73 REMARK 500 ILE A 317 133.25 -36.81 REMARK 500 LEU A 322 -0.87 58.31 REMARK 500 ASN A 362 70.98 31.94 REMARK 500 LYS A 394 33.72 -99.77 REMARK 500 ARG B 10 51.12 -119.21 REMARK 500 LYS B 11 127.13 -38.11 REMARK 500 THR B 18 -169.46 -76.45 REMARK 500 THR B 57 -2.77 62.92 REMARK 500 ARG C 2 -8.29 72.93 REMARK 500 VAL C 56 -162.35 -128.03 REMARK 500 ARG C 57 128.15 -30.78 REMARK 500 GLU C 162 -9.80 73.14 REMARK 500 ASP C 197 46.41 36.21 REMARK 500 ALA C 248 -77.32 -65.60 REMARK 500 HIS C 249 -41.02 -142.40 REMARK 500 LYS C 251 74.83 -69.34 REMARK 500 ARG C 252 118.70 -161.31 REMARK 500 LEU C 269 -75.75 -81.52 REMARK 500 ALA C 270 -0.34 57.03 REMARK 500 ASP C 278 41.93 -101.30 REMARK 500 ALA C 310 -173.43 -171.61 REMARK 500 ALA C 311 61.55 64.88 REMARK 500 THR C 321 52.28 -95.09 REMARK 500 LEU C 322 -5.48 63.56 REMARK 500 LEU C 352 66.09 61.21 REMARK 500 THR C 360 94.46 -69.70 REMARK 500 ASN C 362 67.17 30.57 REMARK 500 TRP C 462 -37.68 68.06 REMARK 500 SER C 483 48.57 -89.33 REMARK 500 SER D 16 -179.59 -67.34 REMARK 500 THR D 18 -167.07 -78.01 REMARK 500 ARG D 23 48.60 -96.88 REMARK 500 SER D 55 -62.01 -91.29 REMARK 500 ARG E 2 -1.96 75.30 REMARK 500 VAL E 56 -165.25 -126.11 REMARK 500 ARG E 57 127.57 -30.79 REMARK 500 ASP E 67 134.84 -33.39 REMARK 500 LYS E 84 36.68 -97.83 REMARK 500 ILE E 152 -60.56 -94.85 REMARK 500 GLU E 162 -10.59 72.23 REMARK 500 REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ALA E 490 -14.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 600 REMARK 610 NAG E 600 REMARK 610 NAG L 600 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 600 through NAG A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E REMARK 800 600 through NAG E 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG L REMARK 800 600 through NAG L 601 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-9131 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE ZIKV VIRION IN COMPLEX WITH FAB FRAGMENTS REMARK 900 OF THE POTENTLY NEUTRALIZING HUMAN MONOCLONAL ANTIBODY ZIKV-195 DBREF1 6MID A 1 504 UNP POLG_ZIKVF DBREF2 6MID A A0A024B7W1 291 794 DBREF1 6MID B 1 75 UNP POLG_ZIKVF DBREF2 6MID B A0A024B7W1 216 290 DBREF1 6MID C 1 504 UNP POLG_ZIKVF DBREF2 6MID C A0A024B7W1 291 794 DBREF1 6MID D 1 75 UNP POLG_ZIKVF DBREF2 6MID D A0A024B7W1 216 290 DBREF1 6MID E 1 504 UNP POLG_ZIKVF DBREF2 6MID E A0A024B7W1 291 794 DBREF1 6MID F 1 75 UNP POLG_ZIKVF DBREF2 6MID F A0A024B7W1 216 290 DBREF 6MID H 1 128 PDB 6MID 6MID 1 128 DBREF1 6MID L 1 96 UNP LV136_HUMAN DBREF2 6MID L A0A0B4J1U3 20 115 DBREF 6MID L 97 110 PDB 6MID 6MID 97 110 SEQRES 1 A 504 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 A 504 GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 A 504 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 A 504 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 A 504 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 A 504 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 504 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 A 504 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 504 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 A 504 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 A 504 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 A 504 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 A 504 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 A 504 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 A 504 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 A 504 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 A 504 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 A 504 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 A 504 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 A 504 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 A 504 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 A 504 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 A 504 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 A 504 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 A 504 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 A 504 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 A 504 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 A 504 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 A 504 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 A 504 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 A 504 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 A 504 GLY SER THR ILE GLY LYS ALA PHE GLU ALA THR VAL ARG SEQRES 33 A 504 GLY ALA LYS ARG MET ALA VAL LEU GLY ASP THR ALA TRP SEQRES 34 A 504 ASP PHE GLY SER VAL GLY GLY ALA LEU ASN SER LEU GLY SEQRES 35 A 504 LYS GLY ILE HIS GLN ILE PHE GLY ALA ALA PHE LYS SER SEQRES 36 A 504 LEU PHE GLY GLY MET SER TRP PHE SER GLN ILE LEU ILE SEQRES 37 A 504 GLY THR LEU LEU MET TRP LEU GLY LEU ASN THR LYS ASN SEQRES 38 A 504 GLY SER ILE SER LEU MET CYS LEU ALA LEU GLY GLY VAL SEQRES 39 A 504 LEU ILE PHE LEU SER THR ALA VAL SER ALA SEQRES 1 B 75 ALA VAL THR LEU PRO SER HIS SER THR ARG LYS LEU GLN SEQRES 2 B 75 THR ARG SER GLN THR TRP LEU GLU SER ARG GLU TYR THR SEQRES 3 B 75 LYS HIS LEU ILE ARG VAL GLU ASN TRP ILE PHE ARG ASN SEQRES 4 B 75 PRO GLY PHE ALA LEU ALA ALA ALA ALA ILE ALA TRP LEU SEQRES 5 B 75 LEU GLY SER SER THR SER GLN LYS VAL ILE TYR LEU VAL SEQRES 6 B 75 MET ILE LEU LEU ILE ALA PRO ALA TYR SER SEQRES 1 C 504 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 C 504 GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 C 504 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 C 504 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 C 504 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 C 504 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 C 504 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 C 504 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 C 504 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 C 504 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 C 504 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 C 504 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 C 504 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 C 504 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 C 504 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 C 504 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 C 504 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 C 504 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 C 504 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 C 504 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 C 504 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 C 504 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 C 504 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 C 504 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 C 504 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 C 504 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 C 504 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 C 504 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 C 504 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 C 504 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 C 504 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 C 504 GLY SER THR ILE GLY LYS ALA PHE GLU ALA THR VAL ARG SEQRES 33 C 504 GLY ALA LYS ARG MET ALA VAL LEU GLY ASP THR ALA TRP SEQRES 34 C 504 ASP PHE GLY SER VAL GLY GLY ALA LEU ASN SER LEU GLY SEQRES 35 C 504 LYS GLY ILE HIS GLN ILE PHE GLY ALA ALA PHE LYS SER SEQRES 36 C 504 LEU PHE GLY GLY MET SER TRP PHE SER GLN ILE LEU ILE SEQRES 37 C 504 GLY THR LEU LEU MET TRP LEU GLY LEU ASN THR LYS ASN SEQRES 38 C 504 GLY SER ILE SER LEU MET CYS LEU ALA LEU GLY GLY VAL SEQRES 39 C 504 LEU ILE PHE LEU SER THR ALA VAL SER ALA SEQRES 1 D 75 ALA VAL THR LEU PRO SER HIS SER THR ARG LYS LEU GLN SEQRES 2 D 75 THR ARG SER GLN THR TRP LEU GLU SER ARG GLU TYR THR SEQRES 3 D 75 LYS HIS LEU ILE ARG VAL GLU ASN TRP ILE PHE ARG ASN SEQRES 4 D 75 PRO GLY PHE ALA LEU ALA ALA ALA ALA ILE ALA TRP LEU SEQRES 5 D 75 LEU GLY SER SER THR SER GLN LYS VAL ILE TYR LEU VAL SEQRES 6 D 75 MET ILE LEU LEU ILE ALA PRO ALA TYR SER SEQRES 1 E 504 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 E 504 GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 E 504 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 E 504 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 E 504 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 E 504 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 E 504 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 E 504 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 E 504 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 E 504 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 E 504 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 E 504 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 E 504 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 E 504 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 E 504 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 E 504 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 E 504 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 E 504 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 E 504 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 E 504 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 E 504 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 E 504 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 E 504 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 E 504 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 E 504 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 E 504 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 E 504 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 E 504 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 E 504 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 E 504 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 E 504 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 E 504 GLY SER THR ILE GLY LYS ALA PHE GLU ALA THR VAL ARG SEQRES 33 E 504 GLY ALA LYS ARG MET ALA VAL LEU GLY ASP THR ALA TRP SEQRES 34 E 504 ASP PHE GLY SER VAL GLY GLY ALA LEU ASN SER LEU GLY SEQRES 35 E 504 LYS GLY ILE HIS GLN ILE PHE GLY ALA ALA PHE LYS SER SEQRES 36 E 504 LEU PHE GLY GLY MET SER TRP PHE SER GLN ILE LEU ILE SEQRES 37 E 504 GLY THR LEU LEU MET TRP LEU GLY LEU ASN THR LYS ASN SEQRES 38 E 504 GLY SER ILE SER LEU MET CYS LEU ALA LEU GLY GLY VAL SEQRES 39 E 504 LEU ILE PHE LEU SER THR ALA VAL SER ALA SEQRES 1 F 75 ALA VAL THR LEU PRO SER HIS SER THR ARG LYS LEU GLN SEQRES 2 F 75 THR ARG SER GLN THR TRP LEU GLU SER ARG GLU TYR THR SEQRES 3 F 75 LYS HIS LEU ILE ARG VAL GLU ASN TRP ILE PHE ARG ASN SEQRES 4 F 75 PRO GLY PHE ALA LEU ALA ALA ALA ALA ILE ALA TRP LEU SEQRES 5 F 75 LEU GLY SER SER THR SER GLN LYS VAL ILE TYR LEU VAL SEQRES 6 F 75 MET ILE LEU LEU ILE ALA PRO ALA TYR SER SEQRES 1 H 128 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL HIS SEQRES 2 H 128 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 128 PHE THR PHE SER SER SER ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 H 128 TYR ASP GLY SER ASN LYS TYR TYR GLY ASP SER VAL LYS SEQRES 6 H 128 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 128 LEU TYR LEU GLN MET HIS SER LEU ARG ALA GLU ASP THR SEQRES 8 H 128 ALA VAL TYR TYR CYS ALA LYS ASP ARG ASP ALA TYR ASN SEQRES 9 H 128 THR VAL GLY TYR PHE ALA TYR TYR TYR GLY MET ASP VAL SEQRES 10 H 128 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 L 110 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLU ALA SEQRES 2 L 110 PRO ARG GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 L 110 SER ASN ILE GLY ASN ASN ALA VAL ASN TRP TYR GLN GLN SEQRES 4 L 110 LEU PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR ASP SEQRES 5 L 110 ASP LEU LEU PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 L 110 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 L 110 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8 L 110 TRP ASP ASP SER LEU THR ARG TYR VAL PHE GLY THR GLY SEQRES 9 L 110 THR LYS VAL THR VAL LEU HET NAG A 600 14 HET NAG A 601 14 HET NAG E 600 14 HET NAG E 601 14 HET NAG L 600 14 HET NAG L 601 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 9 NAG 6(C8 H15 N O6) HELIX 1 AA1 LEU A 82 SER A 86 5 5 HELIX 2 AA2 GLY A 100 GLY A 104 5 5 HELIX 3 AA3 GLN A 131 LEU A 135 5 5 HELIX 4 AA4 HIS A 148 ILE A 152 5 5 HELIX 5 AA5 ASP A 197 SER A 199 5 3 HELIX 6 AA6 LYS A 215 HIS A 219 1 5 HELIX 7 AA7 ASN A 238 ALA A 241 5 4 HELIX 8 AA8 GLU A 262 THR A 267 1 6 HELIX 9 AA9 SER A 405 GLY A 425 1 21 HELIX 10 AB1 ASP A 426 PHE A 431 5 6 HELIX 11 AB2 SER A 440 SER A 455 1 16 HELIX 12 AB3 SER A 461 LEU A 475 1 15 HELIX 13 AB4 ILE A 484 THR A 500 1 17 HELIX 14 AB5 SER B 6 LYS B 11 5 6 HELIX 15 AB6 LYS B 27 ASN B 39 1 13 HELIX 16 AB7 PRO B 40 ALA B 50 1 11 HELIX 17 AB8 SER B 58 ALA B 71 1 14 HELIX 18 AB9 GLN C 131 GLU C 133 5 3 HELIX 19 AC1 HIS C 148 ILE C 152 5 5 HELIX 20 AC2 ASP C 197 SER C 199 5 3 HELIX 21 AC3 LYS C 215 HIS C 219 1 5 HELIX 22 AC4 ASN C 238 ALA C 241 5 4 HELIX 23 AC5 GLN C 261 ALA C 270 1 10 HELIX 24 AC6 ASP C 296 LEU C 298 5 3 HELIX 25 AC7 SER C 405 LEU C 424 1 20 HELIX 26 AC8 ASP C 426 PHE C 431 5 6 HELIX 27 AC9 SER C 440 SER C 455 1 16 HELIX 28 AD1 TRP C 462 LEU C 475 1 14 HELIX 29 AD2 ASN C 481 SER C 485 5 5 HELIX 30 AD3 CYS C 488 THR C 500 1 13 HELIX 31 AD4 THR D 26 ASN D 39 1 14 HELIX 32 AD5 PRO D 40 GLY D 54 1 15 HELIX 33 AD6 SER D 56 ALA D 71 1 16 HELIX 34 AD7 GLN E 131 GLU E 133 5 3 HELIX 35 AD8 HIS E 148 ILE E 152 5 5 HELIX 36 AD9 ASP E 197 SER E 199 5 3 HELIX 37 AE1 LYS E 215 HIS E 219 1 5 HELIX 38 AE2 ASN E 238 LEU E 242 5 5 HELIX 39 AE3 GLN E 261 THR E 267 1 7 HELIX 40 AE4 SER E 405 LEU E 424 1 20 HELIX 41 AE5 GLY E 425 PHE E 431 5 7 HELIX 42 AE6 SER E 440 SER E 455 1 16 HELIX 43 AE7 SER E 461 LEU E 477 1 17 HELIX 44 AE8 CYS E 488 THR E 500 1 13 HELIX 45 AE9 SER F 6 LYS F 11 5 6 HELIX 46 AF1 LYS F 27 ASN F 39 1 13 HELIX 47 AF2 PRO F 40 GLY F 54 1 15 HELIX 48 AF3 SER F 56 ALA F 71 1 16 HELIX 49 AF4 ASP H 73 ASN H 77 5 5 SHEET 1 AA1 5 ARG A 9 GLU A 13 0 SHEET 2 AA1 5 CYS A 30 MET A 34 1 O THR A 32 N ASP A 10 SHEET 3 AA1 5 VAL A 41 VAL A 50 -1 O ILE A 43 N VAL A 31 SHEET 4 AA1 5 TYR A 137 VAL A 143 -1 O MET A 140 N GLU A 44 SHEET 5 AA1 5 ARG A 164 ILE A 169 -1 O VAL A 167 N ILE A 139 SHEET 1 AA2 4 ARG A 9 GLU A 13 0 SHEET 2 AA2 4 CYS A 30 MET A 34 1 O THR A 32 N ASP A 10 SHEET 3 AA2 4 VAL A 41 VAL A 50 -1 O ILE A 43 N VAL A 31 SHEET 4 AA2 4 GLY A 282 LEU A 284 -1 O LEU A 284 N THR A 48 SHEET 1 AA3 4 TRP A 20 VAL A 24 0 SHEET 2 AA3 4 LYS A 290 LYS A 294 -1 O CYS A 291 N VAL A 23 SHEET 3 AA3 4 GLY A 187 GLU A 191 -1 N GLY A 187 O LYS A 294 SHEET 4 AA3 4 ARG A 175 GLU A 177 -1 N ALA A 176 O LEU A 188 SHEET 1 AA4 5 ALA A 54 GLU A 55 0 SHEET 2 AA4 5 THR A 126 SER A 129 -1 O SER A 129 N ALA A 54 SHEET 3 AA4 5 LEU A 201 MET A 206 -1 O TYR A 203 N LYS A 128 SHEET 4 AA4 5 LYS A 209 HIS A 214 -1 O LYS A 209 N MET A 206 SHEET 5 AA4 5 LEU A 273 ALA A 275 -1 O LEU A 273 N LEU A 212 SHEET 1 AA5 3 LYS A 123 LYS A 124 0 SHEET 2 AA5 3 SER A 58 GLU A 62 -1 N TYR A 61 O LYS A 123 SHEET 3 AA5 3 TRP A 225 HIS A 226 -1 O HIS A 226 N SER A 58 SHEET 1 AA6 3 ILE A 65 ARG A 73 0 SHEET 2 AA6 3 GLY A 109 PHE A 119 -1 O VAL A 114 N ASP A 71 SHEET 3 AA6 3 TYR A 90 ARG A 99 -1 N VAL A 97 O GLY A 111 SHEET 1 AA7 2 VAL A 243 GLU A 244 0 SHEET 2 AA7 2 VAL A 256 VAL A 257 -1 O VAL A 256 N GLU A 244 SHEET 1 AA8 2 ALA A 319 GLU A 320 0 SHEET 2 AA8 2 VAL A 326 THR A 327 -1 O THR A 327 N ALA A 319 SHEET 1 AA9 2 GLU A 329 ALA A 333 0 SHEET 2 AA9 2 ASN A 371 MET A 375 -1 O MET A 374 N VAL A 330 SHEET 1 AB1 2 CYS A 339 LYS A 340 0 SHEET 2 AB1 2 VAL A 364 ILE A 365 -1 O ILE A 365 N CYS A 339 SHEET 1 AB2 3 ALA A 343 ALA A 346 0 SHEET 2 AB2 3 GLY A 383 ILE A 389 -1 O TYR A 386 N ALA A 346 SHEET 3 AB2 3 ILE A 396 ARG A 402 -1 O HIS A 398 N ILE A 387 SHEET 1 AB3 2 ARG A 357 LEU A 358 0 SHEET 2 AB3 2 LEU A 378 ASP A 379 -1 O ASP A 379 N ARG A 357 SHEET 1 AB4 5 ASP C 10 VAL C 12 0 SHEET 2 AB4 5 VAL C 31 VAL C 33 1 O THR C 32 N ASP C 10 SHEET 3 AB4 5 VAL C 41 VAL C 50 -1 O ILE C 43 N VAL C 31 SHEET 4 AB4 5 LEU C 135 VAL C 143 -1 O MET C 140 N GLU C 44 SHEET 5 AB4 5 ARG C 164 ILE C 169 -1 O ALA C 165 N LEU C 141 SHEET 1 AB5 4 ASP C 10 VAL C 12 0 SHEET 2 AB5 4 VAL C 31 VAL C 33 1 O THR C 32 N ASP C 10 SHEET 3 AB5 4 VAL C 41 VAL C 50 -1 O ILE C 43 N VAL C 31 SHEET 4 AB5 4 GLY C 282 LEU C 284 -1 O GLY C 282 N VAL C 50 SHEET 1 AB6 4 TRP C 20 GLU C 26 0 SHEET 2 AB6 4 HIS C 288 LYS C 294 -1 O LEU C 293 N VAL C 21 SHEET 3 AB6 4 GLY C 184 ASP C 189 -1 N GLY C 187 O LYS C 294 SHEET 4 AB6 4 ARG C 175 LEU C 180 -1 N ALA C 178 O LEU C 186 SHEET 1 AB7 5 ALA C 54 GLU C 55 0 SHEET 2 AB7 5 LYS C 128 SER C 129 -1 O SER C 129 N ALA C 54 SHEET 3 AB7 5 LEU C 201 THR C 205 -1 O TYR C 203 N LYS C 128 SHEET 4 AB7 5 HIS C 210 HIS C 214 -1 O VAL C 213 N TYR C 202 SHEET 5 AB7 5 LEU C 273 ALA C 275 -1 O ALA C 275 N HIS C 210 SHEET 1 AB8 4 TYR C 90 THR C 95 0 SHEET 2 AB8 4 SER C 112 LYS C 124 -1 O LEU C 113 N THR C 95 SHEET 3 AB8 4 SER C 58 ARG C 73 -1 N ASP C 71 O VAL C 114 SHEET 4 AB8 4 TRP C 225 HIS C 226 -1 O HIS C 226 N SER C 58 SHEET 1 AB9 2 ASP C 98 ARG C 99 0 SHEET 2 AB9 2 GLY C 109 LYS C 110 -1 O GLY C 109 N ARG C 99 SHEET 1 AC1 2 VAL C 243 ASP C 247 0 SHEET 2 AC1 2 GLN C 253 VAL C 257 -1 O THR C 254 N LYS C 246 SHEET 1 AC2 3 PHE C 312 GLU C 320 0 SHEET 2 AC2 3 VAL C 326 ALA C 333 -1 O THR C 327 N ALA C 319 SHEET 3 AC2 3 ASN C 371 LEU C 378 -1 O MET C 374 N VAL C 330 SHEET 1 AC3 2 CYS C 339 LYS C 340 0 SHEET 2 AC3 2 VAL C 364 ILE C 365 -1 O ILE C 365 N CYS C 339 SHEET 1 AC4 4 THR C 353 PRO C 354 0 SHEET 2 AC4 4 GLN C 344 VAL C 347 -1 N VAL C 347 O THR C 353 SHEET 3 AC4 4 ASP C 384 VAL C 388 -1 O TYR C 386 N ALA C 346 SHEET 4 AC4 4 HIS C 399 HIS C 401 -1 O TRP C 400 N SER C 385 SHEET 1 AC5 9 ARG E 9 GLU E 13 0 SHEET 2 AC5 9 CYS E 30 MET E 34 1 O THR E 32 N ASP E 10 SHEET 3 AC5 9 VAL E 41 VAL E 50 -1 O ILE E 43 N VAL E 31 SHEET 4 AC5 9 GLY E 282 LEU E 284 -1 O LEU E 284 N THR E 48 SHEET 5 AC5 9 GLU E 274 MET E 277 -1 N GLU E 276 O ARG E 283 SHEET 6 AC5 9 LYS E 209 HIS E 214 -1 N HIS E 210 O ALA E 275 SHEET 7 AC5 9 LEU E 201 MET E 206 -1 N MET E 206 O LYS E 209 SHEET 8 AC5 9 THR E 126 SER E 129 -1 N LYS E 128 O TYR E 203 SHEET 9 AC5 9 ALA E 54 VAL E 56 -1 N ALA E 54 O SER E 129 SHEET 1 AC6 5 ARG E 9 GLU E 13 0 SHEET 2 AC6 5 CYS E 30 MET E 34 1 O THR E 32 N ASP E 10 SHEET 3 AC6 5 VAL E 41 VAL E 50 -1 O ILE E 43 N VAL E 31 SHEET 4 AC6 5 LEU E 135 VAL E 143 -1 O SER E 142 N ASP E 42 SHEET 5 AC6 5 ARG E 164 ILE E 169 -1 O ALA E 165 N LEU E 141 SHEET 1 AC7 4 TRP E 20 VAL E 24 0 SHEET 2 AC7 4 LYS E 290 LYS E 294 -1 O CYS E 291 N VAL E 23 SHEET 3 AC7 4 GLY E 184 LEU E 188 -1 N GLY E 187 O LYS E 294 SHEET 4 AC7 4 ALA E 176 LEU E 180 -1 N ALA E 178 O LEU E 186 SHEET 1 AC8 2 SER E 58 TYR E 59 0 SHEET 2 AC8 2 TRP E 225 HIS E 226 -1 O HIS E 226 N SER E 58 SHEET 1 AC9 3 ALA E 63 ARG E 73 0 SHEET 2 AC9 3 SER E 112 CYS E 121 -1 O CYS E 116 N ALA E 69 SHEET 3 AC9 3 TYR E 90 THR E 95 -1 N VAL E 91 O ALA E 117 SHEET 1 AD1 2 ASP E 98 ARG E 99 0 SHEET 2 AD1 2 GLY E 109 LYS E 110 -1 O GLY E 109 N ARG E 99 SHEET 1 AD2 2 ALA E 319 GLU E 320 0 SHEET 2 AD2 2 VAL E 326 THR E 327 -1 O THR E 327 N ALA E 319 SHEET 1 AD3 2 GLU E 329 ALA E 333 0 SHEET 2 AD3 2 ASN E 371 MET E 375 -1 O MET E 374 N VAL E 330 SHEET 1 AD4 3 GLN E 344 ALA E 346 0 SHEET 2 AD4 3 GLY E 383 VAL E 388 -1 O TYR E 386 N ALA E 346 SHEET 3 AD4 3 HIS E 399 ARG E 402 -1 O ARG E 402 N GLY E 383 SHEET 1 AD5 4 VAL H 5 SER H 7 0 SHEET 2 AD5 4 LEU H 18 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AD5 4 LEU H 79 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AD5 4 PHE H 68 SER H 71 -1 N THR H 69 O GLN H 82 SHEET 1 AD6 2 GLY H 10 VAL H 11 0 SHEET 2 AD6 2 VAL H 124 THR H 125 1 O THR H 125 N GLY H 10 SHEET 1 AD7 4 LYS H 58 TYR H 60 0 SHEET 2 AD7 4 GLU H 46 ILE H 51 -1 N VAL H 50 O TYR H 59 SHEET 3 AD7 4 MET H 34 GLN H 39 -1 N MET H 34 O ILE H 51 SHEET 4 AD7 4 VAL H 93 TYR H 95 -1 O VAL H 93 N GLN H 39 SHEET 1 AD8 5 SER L 9 GLU L 12 0 SHEET 2 AD8 5 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AD8 5 ASP L 86 ASP L 93 -1 N TYR L 87 O THR L 105 SHEET 4 AD8 5 ASN L 35 GLN L 39 -1 N ASN L 35 O ALA L 90 SHEET 5 AD8 5 LYS L 46 LEU L 47 -1 O LYS L 46 N GLN L 38 SHEET 1 AD9 4 SER L 9 GLU L 12 0 SHEET 2 AD9 4 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AD9 4 ASP L 86 ASP L 93 -1 N TYR L 87 O THR L 105 SHEET 4 AD9 4 ARG L 98 PHE L 101 -1 O ARG L 98 N ASP L 93 SHEET 1 AE1 2 ARG L 17 SER L 23 0 SHEET 2 AE1 2 SER L 71 SER L 77 -1 O ALA L 72 N CYS L 22 SSBOND 1 CYS A 60 CYS A 121 1555 1555 2.03 SSBOND 2 CYS A 190 CYS A 291 1555 1555 2.03 SSBOND 3 CYS C 60 CYS C 121 1555 1555 2.03 SSBOND 4 CYS E 60 CYS E 121 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.03 LINK O4 NAG A 600 C1 NAG A 601 1555 1555 1.44 LINK O4 NAG E 600 C1 NAG E 601 1555 1555 1.44 LINK O4 NAG L 600 C1 NAG L 601 1555 1555 1.44 SITE 1 AC1 3 GLY A 150 ASN A 154 THR A 156 SITE 1 AC2 3 MET E 151 ASN E 154 THR E 156 SITE 1 AC3 6 GLY C 150 MET C 151 ASN C 154 ASP L 94 SITE 2 AC3 6 SER L 95 LEU L 96 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