HEADER VIRUS 18-AUG-13 4C2I TITLE CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 1 TITLE 2 COMPLEXED WITH FAB FRAGMENTS OF HUMAN ANTIBODY 1F4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE PROTEIN; COMPND 3 CHAIN: A, C, E; COMPND 4 OTHER_DETAILS: STRAIN PVP159; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: POLYPROTEIN; COMPND 7 CHAIN: B, D, F; COMPND 8 FRAGMENT: MEMBRANE PROTEIN, RESIDUES 206-280; COMPND 9 OTHER_DETAILS: STRAIN PVP159; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: HEAVY CHAIN FAB FRAGMENT OF ANTIBODY 1F4; COMPND 12 CHAIN: H, M; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: LIGHT CHAIN FAB FRAGMENT OF ANTIBODY 1F4; COMPND 15 CHAIN: L, N SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11053; SOURCE 4 EXPRESSION_SYSTEM: AEDES ALBOPICTUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7160; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: C6/36; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: DENGUE VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11053; SOURCE 10 EXPRESSION_SYSTEM: AEDES ALBOPICTUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 7160; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: C6/36; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 CELL: B CELLS; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: 293F; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 CELL: B CELLS; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: 293F KEYWDS VIRUS, E PROTEINS, NEUTRALIZATION EXPDTA ELECTRON MICROSCOPY MDLTYP CA ATOMS ONLY, CHAIN A, C, E, B, D, F, H, M, L, N AUTHOR G.FIBRIANSAH,J.L.TAN,R.DE ALWIS,S.A.SMITH,T.-S.NG,V.A.KOSTYUCHENKO, AUTHOR 2 K.D.IBARRA,E.HARRIS,A.DE SILVA,J.E.CROWE JUNIOR,S.-M.LOK REVDAT 2 05-FEB-14 4C2I 1 SOURCE REMARK REVDAT 1 29-JAN-14 4C2I 0 JRNL AUTH G.FIBRIANSAH,J.L.TAN,S.A.SMITH,A.R.DE ALWIS,T.NG, JRNL AUTH 2 V.A.KOSTYUCHENKO,K.D.IBARRA,J.WANG,E.HARRIS,A.DE SILVA, JRNL AUTH 3 J.E.J.CROWE,S.LOK JRNL TITL A POTENT ANTI-DENGUE HUMAN ANTIBODY PREFERENTIALLY JRNL TITL 2 RECOGNIZES THE CONFORMATION OF E PROTEIN MONOMERS ASSEMBLED JRNL TITL 3 ON THE VIRUS SURFACE. JRNL REF EMBO MOL.MED. 2014 JRNL REFN ESSN 1757-4684 JRNL PMID 24421336 JRNL DOI 10.1002/EMMM.201303404 REMARK 2 REMARK 2 RESOLUTION. 6.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EMAN, MPSA REMARK 3 RECONSTRUCTION SCHEMA : CROSS-COMMON LINES REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 4AZX REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : CRYO-EM REMARK 3 REFINEMENT TARGET : CORRELATION REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : RIGID BODY REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1 REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 6 REMARK 3 NUMBER OF PARTICLES : 10270 REMARK 3 CTF CORRECTION METHOD : EACH PARTICLE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM REMARK 3 EMDB EMD-2442. (DEPOSITION ID: 11902). REMARK 4 REMARK 4 4C2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-13. REMARK 100 THE PDBE ID CODE IS EBI-58074. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : VITREOUS ICE REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : NULL REMARK 245 NAME OF SAMPLE : DENGUE VIRUS SEROTYPE 1 REMARK 245 WITH FAB FRAGMENTS OF REMARK 245 HUMAN MONOCLONAL ANTIBODY REMARK 245 1F4 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION 1 -- REMARK 245 CRYOGEN- ETHANE, HUMIDITY- REMARK 245 100, TEMPERATURE- 100, REMARK 245 INSTRUMENT- FEI VITROBOT REMARK 245 MARK IV, METHOD- BLOT REMARK 245 WITH FILTER PAPER FOR 2 S REMARK 245 BEFORE PLUNGING, REMARK 245 SAMPLE BUFFER : 12 MM TRIS-HCL PH 8.0, REMARK 245 120 MM NACL AND 1 REMARK 245 MM EDTA REMARK 245 PH : 8.0 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : 14-SEP-12 REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 254 REMARK 245 TEMPERATURE (KELVIN) : 100 REMARK 245 MICROSCOPE MODEL : OTHER REMARK 245 DETECTOR TYPE : DIRECT ELECTRON REMARK 245 DETECTOR (FALCON, FEI) REMARK 245 MINIMUM DEFOCUS (NM) : 1000 REMARK 245 MAXIMUM DEFOCUS (NM) : 4000 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.7 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 17.5 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : 47000 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 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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, M, N 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 -0.638197 0.262866 -0.723607 0.00000 REMARK 350 BIOMT2 2 0.262866 -0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 2 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 3 -0.447214 0.525731 -0.723607 0.00000 REMARK 350 BIOMT2 3 -0.850651 0.000000 0.525731 0.00000 REMARK 350 BIOMT3 3 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 4 -0.361803 0.262866 -0.894427 0.00000 REMARK 350 BIOMT2 4 0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 4 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 5 -0.670820 0.688191 -0.276393 0.00000 REMARK 350 BIOMT2 5 0.162460 0.500000 0.850651 0.00000 REMARK 350 BIOMT3 5 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 6 0.138197 0.425325 -0.894427 0.00000 REMARK 350 BIOMT2 6 0.951057 -0.309017 0.000000 0.00000 REMARK 350 BIOMT3 6 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 7 -0.638197 -0.262866 -0.723607 0.00000 REMARK 350 BIOMT2 7 -0.262866 -0.809017 0.525731 0.00000 REMARK 350 BIOMT3 7 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 8 -0.809017 -0.587785 -0.000000 0.00000 REMARK 350 BIOMT2 8 0.587785 -0.809017 0.000000 0.00000 REMARK 350 BIOMT3 8 0.000000 -0.000000 1.000000 0.00000 REMARK 350 BIOMT1 9 -0.138197 0.951057 0.276393 0.00000 REMARK 350 BIOMT2 9 -0.425325 -0.309017 0.850651 0.00000 REMARK 350 BIOMT3 9 0.894427 -0.000000 0.447214 0.00000 REMARK 350 BIOMT1 10 0.670820 -0.162460 -0.723607 0.00000 REMARK 350 BIOMT2 10 0.688191 0.500000 0.525731 0.00000 REMARK 350 BIOMT3 10 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 11 0.447214 0.850651 -0.276393 0.00000 REMARK 350 BIOMT2 11 0.525731 -0.000000 0.850651 0.00000 REMARK 350 BIOMT3 11 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 12 0.052786 -0.688191 -0.723607 0.00000 REMARK 350 BIOMT2 12 0.688191 -0.500000 0.525731 0.00000 REMARK 350 BIOMT3 12 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 13 -0.947214 0.162460 0.276393 0.00000 REMARK 350 BIOMT2 13 0.162460 -0.500000 0.850651 0.00000 REMARK 350 BIOMT3 13 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 14 -0.138197 -0.425325 0.894427 0.00000 REMARK 350 BIOMT2 14 0.951057 -0.309017 -0.000000 0.00000 REMARK 350 BIOMT3 14 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 15 0.638197 0.262866 0.723607 0.00000 REMARK 350 BIOMT2 15 -0.262866 -0.809017 0.525731 0.00000 REMARK 350 BIOMT3 15 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 16 0.670820 -0.688191 0.276393 0.00000 REMARK 350 BIOMT2 16 0.162460 0.500000 0.850651 0.00000 REMARK 350 BIOMT3 16 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 17 0.947214 -0.162460 -0.276393 0.00000 REMARK 350 BIOMT2 17 0.162460 -0.500000 0.850651 0.00000 REMARK 350 BIOMT3 17 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 18 -0.447214 -0.850651 0.276393 0.00000 REMARK 350 BIOMT2 18 0.525731 0.000000 0.850651 0.00000 REMARK 350 BIOMT3 18 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 19 -0.052786 0.688191 0.723607 0.00000 REMARK 350 BIOMT2 19 0.688191 -0.500000 0.525731 0.00000 REMARK 350 BIOMT3 19 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 20 0.447214 0.525731 0.723607 0.00000 REMARK 350 BIOMT2 20 0.850651 -0.000000 -0.525731 0.00000 REMARK 350 BIOMT3 20 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 21 0.809017 -0.587785 -0.000000 0.00000 REMARK 350 BIOMT2 21 -0.587785 -0.809017 -0.000000 0.00000 REMARK 350 BIOMT3 21 -0.000000 -0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 22 -0.361803 -0.587785 0.723607 0.00000 REMARK 350 BIOMT2 22 -0.262866 0.809017 0.525731 0.00000 REMARK 350 BIOMT3 22 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 23 0.138197 -0.951057 -0.276393 0.00000 REMARK 350 BIOMT2 23 -0.425325 -0.309017 0.850651 0.00000 REMARK 350 BIOMT3 23 -0.894427 -0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 24 -0.670820 0.162460 0.723607 0.00000 REMARK 350 BIOMT2 24 0.688191 0.500000 0.525731 0.00000 REMARK 350 BIOMT3 24 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 25 0.809017 0.587785 0.000000 0.00000 REMARK 350 BIOMT2 25 0.587785 -0.809017 -0.000000 0.00000 REMARK 350 BIOMT3 25 0.000000 -0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 26 0.138197 0.951057 -0.276393 0.00000 REMARK 350 BIOMT2 26 0.425325 -0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 26 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 27 0.138197 -0.425325 -0.894427 0.00000 REMARK 350 BIOMT2 27 -0.951057 -0.309017 -0.000000 0.00000 REMARK 350 BIOMT3 27 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 28 -1.000000 -0.000000 -0.000000 0.00000 REMARK 350 BIOMT2 28 -0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 28 -0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 29 -0.861803 -0.425325 -0.276393 0.00000 REMARK 350 BIOMT2 29 -0.425325 0.309017 0.850651 0.00000 REMARK 350 BIOMT3 29 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 30 -0.309017 0.951057 0.000000 0.00000 REMARK 350 BIOMT2 30 0.951057 0.309017 -0.000000 0.00000 REMARK 350 BIOMT3 30 0.000000 -0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 31 0.447214 -0.000000 -0.894427 0.00000 REMARK 350 BIOMT2 31 -0.000000 -1.000000 -0.000000 0.00000 REMARK 350 BIOMT3 31 -0.894427 -0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 32 0.361803 0.587785 -0.723607 0.00000 REMARK 350 BIOMT2 32 -0.262866 0.809017 0.525731 0.00000 REMARK 350 BIOMT3 32 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 33 -0.447214 -0.525731 -0.723607 0.00000 REMARK 350 BIOMT2 33 0.850651 -0.000000 -0.525731 0.00000 REMARK 350 BIOMT3 33 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 34 -0.809017 0.587785 0.000000 0.00000 REMARK 350 BIOMT2 34 -0.587785 -0.809017 -0.000000 0.00000 REMARK 350 BIOMT3 34 -0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 35 -0.947214 -0.162460 0.276393 0.00000 REMARK 350 BIOMT2 35 -0.162460 -0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 35 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 36 0.309017 0.951057 0.000000 0.00000 REMARK 350 BIOMT2 36 -0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 36 -0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 37 0.361803 -0.587785 -0.723607 0.00000 REMARK 350 BIOMT2 37 0.262866 0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 37 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 38 -0.361803 -0.262866 -0.894427 0.00000 REMARK 350 BIOMT2 38 -0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 38 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 39 -0.861803 0.425325 -0.276393 0.00000 REMARK 350 BIOMT2 39 0.425325 0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 39 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 40 0.052786 0.688191 -0.723607 0.00000 REMARK 350 BIOMT2 40 -0.688191 -0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 40 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 41 -0.447214 0.850651 0.276393 0.00000 REMARK 350 BIOMT2 41 -0.525731 -0.000000 -0.850651 0.00000 REMARK 350 BIOMT3 41 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 42 0.670820 0.162460 -0.723607 0.00000 REMARK 350 BIOMT2 42 -0.688191 0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 42 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 43 -0.670820 -0.688191 -0.276393 0.00000 REMARK 350 BIOMT2 43 -0.162460 0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 43 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 44 -0.309017 -0.951057 -0.000000 0.00000 REMARK 350 BIOMT2 44 -0.951057 0.309017 -0.000000 0.00000 REMARK 350 BIOMT3 44 -0.000000 -0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 45 -0.361803 0.587785 0.723607 0.00000 REMARK 350 BIOMT2 45 0.262866 0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 45 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 46 0.947214 0.162460 -0.276393 0.00000 REMARK 350 BIOMT2 46 -0.162460 -0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 46 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 47 0.670820 0.688191 0.276393 0.00000 REMARK 350 BIOMT2 47 -0.162460 0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 47 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 48 0.447214 -0.850651 -0.276393 0.00000 REMARK 350 BIOMT2 48 -0.525731 0.000000 -0.850651 0.00000 REMARK 350 BIOMT3 48 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 49 -0.670820 -0.162460 0.723607 0.00000 REMARK 350 BIOMT2 49 -0.688191 0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 49 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 50 0.447214 -0.525731 0.723607 0.00000 REMARK 350 BIOMT2 50 -0.850651 0.000000 0.525731 0.00000 REMARK 350 BIOMT3 50 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 51 0.361803 -0.262866 0.894427 0.00000 REMARK 350 BIOMT2 51 0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 51 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 52 0.638197 -0.262866 0.723607 0.00000 REMARK 350 BIOMT2 52 0.262866 -0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 52 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 53 0.861803 -0.425325 0.276393 0.00000 REMARK 350 BIOMT2 53 0.425325 0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 53 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 54 -0.052786 -0.688191 0.723607 0.00000 REMARK 350 BIOMT2 54 -0.688191 -0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 54 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 55 0.361803 0.262866 0.894427 0.00000 REMARK 350 BIOMT2 55 -0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 55 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 56 0.861803 0.425325 0.276393 0.00000 REMARK 350 BIOMT2 56 -0.425325 0.309017 0.850651 0.00000 REMARK 350 BIOMT3 56 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 57 0.309017 -0.951057 -0.000000 0.00000 REMARK 350 BIOMT2 57 0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 57 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 58 -0.447214 0.000000 0.894427 0.00000 REMARK 350 BIOMT2 58 0.000000 -1.000000 -0.000000 0.00000 REMARK 350 BIOMT3 58 0.894427 -0.000000 0.447214 0.00000 REMARK 350 BIOMT1 59 -0.138197 -0.951057 0.276393 0.00000 REMARK 350 BIOMT2 59 0.425325 -0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 59 0.894427 -0.000000 0.447214 0.00000 REMARK 350 BIOMT1 60 -0.138197 0.425325 0.894427 0.00000 REMARK 350 BIOMT2 60 -0.951057 -0.309017 -0.000000 0.00000 REMARK 350 BIOMT3 60 0.276393 -0.850651 0.447214 0.00000 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 SER B 73 REMARK 465 MET B 74 REMARK 465 ALA B 75 REMARK 465 SER D 73 REMARK 465 MET D 74 REMARK 465 ALA D 75 REMARK 465 SER F 73 REMARK 465 MET F 74 REMARK 465 ALA F 75 REMARK 465 GLY H 1 REMARK 465 SER H 2 REMARK 465 TRP H 3 REMARK 465 ALA H 4 REMARK 465 LEU L 1 REMARK 465 ALA L 2 REMARK 465 THR L 3 REMARK 465 MET L 4 REMARK 465 ALA L 5 REMARK 465 TRP L 6 REMARK 465 MET L 7 REMARK 465 MET L 8 REMARK 465 LEU L 9 REMARK 465 LEU L 10 REMARK 465 LEU L 11 REMARK 465 LEU L 12 REMARK 465 THR L 13 REMARK 465 LEU L 14 REMARK 465 ILE L 15 REMARK 465 THR L 16 REMARK 465 HIS L 17 REMARK 465 CYS L 18 REMARK 465 ALA L 19 REMARK 465 GLY L 20 REMARK 465 SER L 21 REMARK 465 TRP L 22 REMARK 465 ALA L 23 REMARK 465 GLN L 24 REMARK 465 THR L 236 REMARK 465 GLU L 237 REMARK 465 CYS L 238 REMARK 465 SER L 239 REMARK 465 GLY M 1 REMARK 465 SER M 2 REMARK 465 TRP M 3 REMARK 465 ALA M 4 REMARK 465 LEU N 1 REMARK 465 ALA N 2 REMARK 465 THR N 3 REMARK 465 MET N 4 REMARK 465 ALA N 5 REMARK 465 TRP N 6 REMARK 465 MET N 7 REMARK 465 MET N 8 REMARK 465 LEU N 9 REMARK 465 LEU N 10 REMARK 465 LEU N 11 REMARK 465 LEU N 12 REMARK 465 THR N 13 REMARK 465 LEU N 14 REMARK 465 ILE N 15 REMARK 465 THR N 16 REMARK 465 HIS N 17 REMARK 465 CYS N 18 REMARK 465 ALA N 19 REMARK 465 GLY N 20 REMARK 465 SER N 21 REMARK 465 TRP N 22 REMARK 465 ALA N 23 REMARK 465 GLN N 24 REMARK 465 THR N 236 REMARK 465 GLU N 237 REMARK 465 CYS N 238 REMARK 465 SER N 239 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 1501 REMARK 610 NAG A 1601 REMARK 610 NAG C 1501 REMARK 610 NAG C 1601 REMARK 610 NAG E 1496 REMARK 610 NAG E 1601 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG A1601 THROUGH NAG A1602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG E1496 THROUGH NAG E1498 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG E1601 THROUGH NAG E1602 REMARK 900 REMARK 900 VIRUS SEROTYPE 1 REMARK 900 RELATED ID: EMD-2442 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 1 COMPLEXED WITH REMARK 900 FAB FRAGMENTS OF HUMAN ANTIBODY 1F4 REMARK 999 REMARK 999 SEQUENCE REMARK 999 DENGUE VIRUS SEROTYPE 1 STRAIN PVP159 USED IN THIS STRUCTURAL STUDY REMARK 999 IS A LABORATORY STRAIN. IT HAS SEVERAL MUTATIONS COMPARED TO THAT REMARK 999 DESCRIBED IN Q7TGE4. IT HAS BEEN SEQUENCED AS A PART OF POLYPROTEIN REMARK 999 ENCODED BY THE VIRAL GENOME. DBREF 4C2I A 1 495 UNP Q7TGE4 Q7TGE4_9FLAV 1 495 DBREF 4C2I C 1 495 UNP Q7TGE4 Q7TGE4_9FLAV 1 495 DBREF 4C2I E 1 495 UNP Q7TGE4 Q7TGE4_9FLAV 1 495 DBREF 4C2I B 1 75 UNP G3F5K5 G3F5K5_9FLAV 206 280 DBREF 4C2I D 1 75 UNP G3F5K5 G3F5K5_9FLAV 206 280 DBREF 4C2I F 1 75 UNP G3F5K5 G3F5K5_9FLAV 206 280 DBREF 4C2I H 5 232 PDB 4C2I 4C2I 5 232 DBREF 4C2I M 5 232 PDB 4C2I 4C2I 5 232 DBREF 4C2I L 25 235 PDB 4C2I 4C2I 25 235 DBREF 4C2I N 25 235 PDB 4C2I 4C2I 25 235 SEQADV 4C2I SER A 7 UNP Q7TGE4 GLY 7 CONFLICT SEQADV 4C2I ASN A 8 UNP Q7TGE4 SER 8 CONFLICT SEQADV 4C2I ALA A 17 UNP Q7TGE4 GLY 17 CONFLICT SEQADV 4C2I THR A 18 UNP Q7TGE4 ALA 18 CONFLICT SEQADV 4C2I GLY A 19 UNP Q7TGE4 THR 19 CONFLICT SEQADV 4C2I SER C 7 UNP Q7TGE4 GLY 7 CONFLICT SEQADV 4C2I ASN C 8 UNP Q7TGE4 SER 8 CONFLICT SEQADV 4C2I ALA C 17 UNP Q7TGE4 GLY 17 CONFLICT SEQADV 4C2I THR C 18 UNP Q7TGE4 ALA 18 CONFLICT SEQADV 4C2I GLY C 19 UNP Q7TGE4 THR 19 CONFLICT SEQADV 4C2I SER E 7 UNP Q7TGE4 GLY 7 CONFLICT SEQADV 4C2I ASN E 8 UNP Q7TGE4 SER 8 CONFLICT SEQADV 4C2I ALA E 17 UNP Q7TGE4 GLY 17 CONFLICT SEQADV 4C2I THR E 18 UNP Q7TGE4 ALA 18 CONFLICT SEQADV 4C2I GLY E 19 UNP Q7TGE4 THR 19 CONFLICT SEQRES 1 A 495 MET ARG CYS VAL GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 A 495 GLY LEU SER ALA THR GLY TRP VAL ASP VAL VAL LEU GLU SEQRES 3 A 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASP LYS PRO SEQRES 4 A 495 THR LEU ASP ILE GLU LEU LEU LYS THR GLU VAL THR ASN SEQRES 5 A 495 PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU ALA LYS ILE SEQRES 6 A 495 SER ASN THR THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 495 GLU ALA THR LEU VAL GLU GLU GLN ASP ALA ASN PHE VAL SEQRES 8 A 495 CYS ARG ARG THR PHE VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 495 CYS GLY LEU PHE GLY LYS GLY SER LEU ILE THR CYS ALA SEQRES 10 A 495 LYS PHE LYS CYS VAL THR LYS LEU GLU GLY LYS ILE VAL SEQRES 11 A 495 GLN TYR GLU ASN LEU LYS TYR SER VAL ILE VAL THR VAL SEQRES 12 A 495 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU SER THR SEQRES 13 A 495 GLU HIS GLY THR THR ALA THR ILE THR PRO GLN ALA PRO SEQRES 14 A 495 THR THR GLU ILE GLN LEU THR ASP TYR GLY ALA LEU THR SEQRES 15 A 495 LEU ASP CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 A 495 MET VAL LEU LEU THR MET LYS GLU LYS SER TRP LEU VAL SEQRES 17 A 495 HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP THR SEQRES 18 A 495 SER GLY ALA SER THR SER GLN GLU THR TRP ASN ARG GLN SEQRES 19 A 495 ASP LEU LEU VAL THR PHE LYS THR ALA HIS ALA LYS LYS SEQRES 20 A 495 GLN GLU VAL VAL VAL LEU GLY SER GLN GLU GLY ALA MET SEQRES 21 A 495 HIS THR ALA LEU THR GLY ALA THR GLU ILE GLN THR SER SEQRES 22 A 495 GLY THR THR THR ILE PHE ALA GLY HIS LEU LYS CYS ARG SEQRES 23 A 495 LEU LYS MET ASP LYS LEU THR LEU LYS GLY MET SER TYR SEQRES 24 A 495 VAL MET CYS THR GLY SER PHE LYS LEU GLU LYS GLU VAL SEQRES 25 A 495 ALA GLU THR GLN HIS GLY THR VAL LEU VAL GLN ILE LYS SEQRES 26 A 495 TYR GLU GLY THR ASP ALA PRO CYS LYS ILE PRO PHE SER SEQRES 27 A 495 THR GLN ASP GLU LYS GLY VAL THR GLN ASN GLY ARG LEU SEQRES 28 A 495 ILE THR ALA ASN PRO ILE VAL THR ASP LYS GLU LYS PRO SEQRES 29 A 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY GLU SER TYR SEQRES 30 A 495 ILE VAL ILE GLY ALA GLY GLU LYS ALA LEU LYS LEU SER SEQRES 31 A 495 TRP PHE LYS LYS GLY SER SER ILE GLY LYS MET PHE GLU SEQRES 32 A 495 ALA THR ALA ARG GLY ALA ARG ARG MET ALA ILE LEU GLY SEQRES 33 A 495 ASP THR ALA TRP ASP PHE GLY SER ILE GLY GLY VAL PHE SEQRES 34 A 495 THR SER VAL GLY LYS LEU VAL HIS GLN ILE PHE GLY THR SEQRES 35 A 495 ALA TYR GLY VAL LEU PHE SER GLY VAL SER TRP THR MET SEQRES 36 A 495 LYS ILE GLY ILE GLY VAL LEU LEU THR TRP LEU GLY LEU SEQRES 37 A 495 ASN SER ARG SER THR SER LEU SER MET THR CYS ILE ALA SEQRES 38 A 495 VAL GLY LEU VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 A 495 ALA SEQRES 1 C 495 MET ARG CYS VAL GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 C 495 GLY LEU SER ALA THR GLY TRP VAL ASP VAL VAL LEU GLU SEQRES 3 C 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASP LYS PRO SEQRES 4 C 495 THR LEU ASP ILE GLU LEU LEU LYS THR GLU VAL THR ASN SEQRES 5 C 495 PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU ALA LYS ILE SEQRES 6 C 495 SER ASN THR THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 C 495 GLU ALA THR LEU VAL GLU GLU GLN ASP ALA ASN PHE VAL SEQRES 8 C 495 CYS ARG ARG THR PHE VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 C 495 CYS GLY LEU PHE GLY LYS GLY SER LEU ILE THR CYS ALA SEQRES 10 C 495 LYS PHE LYS CYS VAL THR LYS LEU GLU GLY LYS ILE VAL SEQRES 11 C 495 GLN TYR GLU ASN LEU LYS TYR SER VAL ILE VAL THR VAL SEQRES 12 C 495 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU SER THR SEQRES 13 C 495 GLU HIS GLY THR THR ALA THR ILE THR PRO GLN ALA PRO SEQRES 14 C 495 THR THR GLU ILE GLN LEU THR ASP TYR GLY ALA LEU THR SEQRES 15 C 495 LEU ASP CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 C 495 MET VAL LEU LEU THR MET LYS GLU LYS SER TRP LEU VAL SEQRES 17 C 495 HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP THR SEQRES 18 C 495 SER GLY ALA SER THR SER GLN GLU THR TRP ASN ARG GLN SEQRES 19 C 495 ASP LEU LEU VAL THR PHE LYS THR ALA HIS ALA LYS LYS SEQRES 20 C 495 GLN GLU VAL VAL VAL LEU GLY SER GLN GLU GLY ALA MET SEQRES 21 C 495 HIS THR ALA LEU THR GLY ALA THR GLU ILE GLN THR SER SEQRES 22 C 495 GLY THR THR THR ILE PHE ALA GLY HIS LEU LYS CYS ARG SEQRES 23 C 495 LEU LYS MET ASP LYS LEU THR LEU LYS GLY MET SER TYR SEQRES 24 C 495 VAL MET CYS THR GLY SER PHE LYS LEU GLU LYS GLU VAL SEQRES 25 C 495 ALA GLU THR GLN HIS GLY THR VAL LEU VAL GLN ILE LYS SEQRES 26 C 495 TYR GLU GLY THR ASP ALA PRO CYS LYS ILE PRO PHE SER SEQRES 27 C 495 THR GLN ASP GLU LYS GLY VAL THR GLN ASN GLY ARG LEU SEQRES 28 C 495 ILE THR ALA ASN PRO ILE VAL THR ASP LYS GLU LYS PRO SEQRES 29 C 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY GLU SER TYR SEQRES 30 C 495 ILE VAL ILE GLY ALA GLY GLU LYS ALA LEU LYS LEU SER SEQRES 31 C 495 TRP PHE LYS LYS GLY SER SER ILE GLY LYS MET PHE GLU SEQRES 32 C 495 ALA THR ALA ARG GLY ALA ARG ARG MET ALA ILE LEU GLY SEQRES 33 C 495 ASP THR ALA TRP ASP PHE GLY SER ILE GLY GLY VAL PHE SEQRES 34 C 495 THR SER VAL GLY LYS LEU VAL HIS GLN ILE PHE GLY THR SEQRES 35 C 495 ALA TYR GLY VAL LEU PHE SER GLY VAL SER TRP THR MET SEQRES 36 C 495 LYS ILE GLY ILE GLY VAL LEU LEU THR TRP LEU GLY LEU SEQRES 37 C 495 ASN SER ARG SER THR SER LEU SER MET THR CYS ILE ALA SEQRES 38 C 495 VAL GLY LEU VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 C 495 ALA SEQRES 1 E 495 MET ARG CYS VAL GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 E 495 GLY LEU SER ALA THR GLY TRP VAL ASP VAL VAL LEU GLU SEQRES 3 E 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASP LYS PRO SEQRES 4 E 495 THR LEU ASP ILE GLU LEU LEU LYS THR GLU VAL THR ASN SEQRES 5 E 495 PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU ALA LYS ILE SEQRES 6 E 495 SER ASN THR THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 E 495 GLU ALA THR LEU VAL GLU GLU GLN ASP ALA ASN PHE VAL SEQRES 8 E 495 CYS ARG ARG THR PHE VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 E 495 CYS GLY LEU PHE GLY LYS GLY SER LEU ILE THR CYS ALA SEQRES 10 E 495 LYS PHE LYS CYS VAL THR LYS LEU GLU GLY LYS ILE VAL SEQRES 11 E 495 GLN TYR GLU ASN LEU LYS TYR SER VAL ILE VAL THR VAL SEQRES 12 E 495 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU SER THR SEQRES 13 E 495 GLU HIS GLY THR THR ALA THR ILE THR PRO GLN ALA PRO SEQRES 14 E 495 THR THR GLU ILE GLN LEU THR ASP TYR GLY ALA LEU THR SEQRES 15 E 495 LEU ASP CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 E 495 MET VAL LEU LEU THR MET LYS GLU LYS SER TRP LEU VAL SEQRES 17 E 495 HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP THR SEQRES 18 E 495 SER GLY ALA SER THR SER GLN GLU THR TRP ASN ARG GLN SEQRES 19 E 495 ASP LEU LEU VAL THR PHE LYS THR ALA HIS ALA LYS LYS SEQRES 20 E 495 GLN GLU VAL VAL VAL LEU GLY SER GLN GLU GLY ALA MET SEQRES 21 E 495 HIS THR ALA LEU THR GLY ALA THR GLU ILE GLN THR SER SEQRES 22 E 495 GLY THR THR THR ILE PHE ALA GLY HIS LEU LYS CYS ARG SEQRES 23 E 495 LEU LYS MET ASP LYS LEU THR LEU LYS GLY MET SER TYR SEQRES 24 E 495 VAL MET CYS THR GLY SER PHE LYS LEU GLU LYS GLU VAL SEQRES 25 E 495 ALA GLU THR GLN HIS GLY THR VAL LEU VAL GLN ILE LYS SEQRES 26 E 495 TYR GLU GLY THR ASP ALA PRO CYS LYS ILE PRO PHE SER SEQRES 27 E 495 THR GLN ASP GLU LYS GLY VAL THR GLN ASN GLY ARG LEU SEQRES 28 E 495 ILE THR ALA ASN PRO ILE VAL THR ASP LYS GLU LYS PRO SEQRES 29 E 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY GLU SER TYR SEQRES 30 E 495 ILE VAL ILE GLY ALA GLY GLU LYS ALA LEU LYS LEU SER SEQRES 31 E 495 TRP PHE LYS LYS GLY SER SER ILE GLY LYS MET PHE GLU SEQRES 32 E 495 ALA THR ALA ARG GLY ALA ARG ARG MET ALA ILE LEU GLY SEQRES 33 E 495 ASP THR ALA TRP ASP PHE GLY SER ILE GLY GLY VAL PHE SEQRES 34 E 495 THR SER VAL GLY LYS LEU VAL HIS GLN ILE PHE GLY THR SEQRES 35 E 495 ALA TYR GLY VAL LEU PHE SER GLY VAL SER TRP THR MET SEQRES 36 E 495 LYS ILE GLY ILE GLY VAL LEU LEU THR TRP LEU GLY LEU SEQRES 37 E 495 ASN SER ARG SER THR SER LEU SER MET THR CYS ILE ALA SEQRES 38 E 495 VAL GLY LEU VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 E 495 ALA SEQRES 1 B 75 SER VAL ALA LEU ALA PRO HIS VAL GLY LEU GLY LEU GLU SEQRES 2 B 75 THR ARG THR GLU THR TRP MET SER SER GLU GLY ALA TRP SEQRES 3 B 75 LYS GLN ILE GLN LYS VAL GLU THR TRP ALA LEU GLY HIS SEQRES 4 B 75 PRO GLY PHE THR VAL ILE ALA LEU PHE LEU ALA HIS ALA SEQRES 5 B 75 ILE GLY THR SER ILE THR GLN LYS GLY ILE ILE PHE ILE SEQRES 6 B 75 LEU LEU MET LEU VAL THR PRO SER MET ALA SEQRES 1 D 75 SER VAL ALA LEU ALA PRO HIS VAL GLY LEU GLY LEU GLU SEQRES 2 D 75 THR ARG THR GLU THR TRP MET SER SER GLU GLY ALA TRP SEQRES 3 D 75 LYS GLN ILE GLN LYS VAL GLU THR TRP ALA LEU GLY HIS SEQRES 4 D 75 PRO GLY PHE THR VAL ILE ALA LEU PHE LEU ALA HIS ALA SEQRES 5 D 75 ILE GLY THR SER ILE THR GLN LYS GLY ILE ILE PHE ILE SEQRES 6 D 75 LEU LEU MET LEU VAL THR PRO SER MET ALA SEQRES 1 F 75 SER VAL ALA LEU ALA PRO HIS VAL GLY LEU GLY LEU GLU SEQRES 2 F 75 THR ARG THR GLU THR TRP MET SER SER GLU GLY ALA TRP SEQRES 3 F 75 LYS GLN ILE GLN LYS VAL GLU THR TRP ALA LEU GLY HIS SEQRES 4 F 75 PRO GLY PHE THR VAL ILE ALA LEU PHE LEU ALA HIS ALA SEQRES 5 F 75 ILE GLY THR SER ILE THR GLN LYS GLY ILE ILE PHE ILE SEQRES 6 F 75 LEU LEU MET LEU VAL THR PRO SER MET ALA SEQRES 1 H 232 GLY SER TRP ALA GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 H 232 GLY VAL VAL GLN PRO GLY ARG SER LEU ARG LEU SER CYS SEQRES 3 H 232 ALA ALA SER GLY PHE THR PHE SER ALA TYR GLY MET HIS SEQRES 4 H 232 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5 H 232 ALA ILE ILE TRP TYR ASP GLY SER ASN LYS TYR TYR ALA SEQRES 6 H 232 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 H 232 SER LYS ASN THR LEU HIS LEU GLN MET ASN SER LEU ARG SEQRES 8 H 232 ALA GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP LYS SEQRES 9 H 232 ASN PRO GLY THR LYS PRO TYR TYR HIS TYR GLY MET ASP SEQRES 10 H 232 VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 11 H 232 GLY THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 232 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 232 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 232 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 232 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 232 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 232 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 232 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 M 232 GLY SER TRP ALA GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 M 232 GLY VAL VAL GLN PRO GLY ARG SER LEU ARG LEU SER CYS SEQRES 3 M 232 ALA ALA SER GLY PHE THR PHE SER ALA TYR GLY MET HIS SEQRES 4 M 232 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5 M 232 ALA ILE ILE TRP TYR ASP GLY SER ASN LYS TYR TYR ALA SEQRES 6 M 232 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 M 232 SER LYS ASN THR LEU HIS LEU GLN MET ASN SER LEU ARG SEQRES 8 M 232 ALA GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP LYS SEQRES 9 M 232 ASN PRO GLY THR LYS PRO TYR TYR HIS TYR GLY MET ASP SEQRES 10 M 232 VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 11 M 232 GLY THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 M 232 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 M 232 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 M 232 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 M 232 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 M 232 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 M 232 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 M 232 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 239 LEU ALA THR MET ALA TRP MET MET LEU LEU LEU LEU THR SEQRES 2 L 239 LEU ILE THR HIS CYS ALA GLY SER TRP ALA GLN SER VAL SEQRES 3 L 239 LEU THR GLN PRO PRO SER VAL SER GLU ALA PRO ARG GLN SEQRES 4 L 239 ARG VAL THR ILE SER CYS SER GLY SER SER SER ASN ILE SEQRES 5 L 239 GLY ASN ASN ALA VAL ASN TRP TYR GLN GLN PHE PRO GLY SEQRES 6 L 239 LYS ALA PRO LYS LEU LEU ILE TYR TYR ASP ASP LEU LEU SEQRES 7 L 239 PRO SER GLY VAL SER ASP ARG PHE SER GLY SER LYS SER SEQRES 8 L 239 GLY THR SER ALA SER LEU ALA ILE SER GLY LEU GLN SER SEQRES 9 L 239 GLU ASP GLU ALA TYR TYR TYR CYS ALA ALA TRP ASP ASP SEQRES 10 L 239 SER LEU ILE GLY VAL VAL PHE GLY GLY GLY THR LYS LEU SEQRES 11 L 239 THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR SEQRES 12 L 239 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 13 L 239 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 14 L 239 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 15 L 239 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 16 L 239 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 17 L 239 PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN SEQRES 18 L 239 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 19 L 239 PRO THR GLU CYS SER SEQRES 1 N 239 LEU ALA THR MET ALA TRP MET MET LEU LEU LEU LEU THR SEQRES 2 N 239 LEU ILE THR HIS CYS ALA GLY SER TRP ALA GLN SER VAL SEQRES 3 N 239 LEU THR GLN PRO PRO SER VAL SER GLU ALA PRO ARG GLN SEQRES 4 N 239 ARG VAL THR ILE SER CYS SER GLY SER SER SER ASN ILE SEQRES 5 N 239 GLY ASN ASN ALA VAL ASN TRP TYR GLN GLN PHE PRO GLY SEQRES 6 N 239 LYS ALA PRO LYS LEU LEU ILE TYR TYR ASP ASP LEU LEU SEQRES 7 N 239 PRO SER GLY VAL SER ASP ARG PHE SER GLY SER LYS SER SEQRES 8 N 239 GLY THR SER ALA SER LEU ALA ILE SER GLY LEU GLN SER SEQRES 9 N 239 GLU ASP GLU ALA TYR TYR TYR CYS ALA ALA TRP ASP ASP SEQRES 10 N 239 SER LEU ILE GLY VAL VAL PHE GLY GLY GLY THR LYS LEU SEQRES 11 N 239 THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR SEQRES 12 N 239 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 13 N 239 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 14 N 239 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 15 N 239 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 16 N 239 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 17 N 239 PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN SEQRES 18 N 239 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 19 N 239 PRO THR GLU CYS SER HET NAG A1501 14 HET NAG A1502 14 HET NAG A1503 14 HET NAG A1601 14 HET NAG A1602 14 HET NAG C1501 14 HET NAG C1601 14 HET NAG C1602 14 HET NAG E1496 14 HET NAG E1497 14 HET NAG E1498 14 HET NAG E1601 14 HET NAG E1602 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 11 NAG 13(C8 H15 N O6) LINK O4 NAG A1501 C1 NAG A1502 1555 1555 1.39 LINK O4 NAG A1502 C1 NAG A1503 1555 1555 1.54 LINK O4 NAG A1601 C1 NAG A1602 1555 1555 1.42 LINK O4 NAG C1601 C1 NAG C1602 1555 1555 1.31 LINK O4 NAG E1496 C1 NAG E1497 1555 1555 1.40 LINK O4 NAG E1497 C1 NAG E1498 1555 1555 1.33 LINK O4 NAG E1601 C1 NAG E1602 1555 1555 1.34 SITE 1 AC1 1 NAG A1501 SITE 1 AC2 1 ASN E 67 SITE 1 AC3 2 ASN E 153 NAG E1496 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 MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1 MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1 MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1 MTRIX1 2 -0.638197 0.262866 -0.723607 0.00000 MTRIX2 2 0.262866 -0.809017 -0.525731 0.00000 MTRIX3 2 -0.723607 -0.525731 0.447214 0.00000 MTRIX1 3 -0.447214 0.525731 -0.723607 0.00000 MTRIX2 3 -0.850651 0.000000 0.525731 0.00000 MTRIX3 3 0.276393 0.850651 0.447214 0.00000 MTRIX1 4 -0.361803 0.262866 -0.894427 0.00000 MTRIX2 4 0.587785 0.809017 0.000000 0.00000 MTRIX3 4 0.723607 -0.525731 -0.447214 0.00000 MTRIX1 5 -0.670820 0.688191 -0.276393 0.00000 MTRIX2 5 0.162460 0.500000 0.850651 0.00000 MTRIX3 5 0.723607 0.525731 -0.447214 0.00000 MTRIX1 6 0.138197 0.425325 -0.894427 0.00000 MTRIX2 6 0.951057 -0.309017 0.000000 0.00000 MTRIX3 6 -0.276393 -0.850651 -0.447214 0.00000 MTRIX1 7 -0.638197 -0.262866 -0.723607 0.00000 MTRIX2 7 -0.262866 -0.809017 0.525731 0.00000 MTRIX3 7 -0.723607 0.525731 0.447214 0.00000 MTRIX1 8 -0.809017 -0.587785 0.000000 0.00000 MTRIX2 8 0.587785 -0.809017 0.000000 0.00000 MTRIX3 8 0.000000 0.000000 1.000000 0.00000 MTRIX1 9 -0.138197 0.951057 0.276393 0.00000 MTRIX2 9 -0.425325 -0.309017 0.850651 0.00000 MTRIX3 9 0.894427 0.000000 0.447214 0.00000 MTRIX1 10 0.670820 -0.162460 -0.723607 0.00000 MTRIX2 10 0.688191 0.500000 0.525731 0.00000 MTRIX3 10 0.276393 -0.850651 0.447214 0.00000 MTRIX1 11 0.447214 0.850651 -0.276393 0.00000 MTRIX2 11 0.525731 0.000000 0.850651 0.00000 MTRIX3 11 0.723607 -0.525731 -0.447214 0.00000 MTRIX1 12 0.052786 -0.688191 -0.723607 0.00000 MTRIX2 12 0.688191 -0.500000 0.525731 0.00000 MTRIX3 12 -0.723607 -0.525731 0.447214 0.00000 MTRIX1 13 -0.947214 0.162460 0.276393 0.00000 MTRIX2 13 0.162460 -0.500000 0.850651 0.00000 MTRIX3 13 0.276393 0.850651 0.447214 0.00000 MTRIX1 14 -0.138197 -0.425325 0.894427 0.00000 MTRIX2 14 0.951057 -0.309017 0.000000 0.00000 MTRIX3 14 0.276393 0.850651 0.447214 0.00000 MTRIX1 15 0.638197 0.262866 0.723607 0.00000 MTRIX2 15 -0.262866 -0.809017 0.525731 0.00000 MTRIX3 15 0.723607 -0.525731 -0.447214 0.00000 MTRIX1 16 0.670820 -0.688191 0.276393 0.00000 MTRIX2 16 0.162460 0.500000 0.850651 0.00000 MTRIX3 16 -0.723607 -0.525731 0.447214 0.00000 MTRIX1 17 0.947214 -0.162460 -0.276393 0.00000 MTRIX2 17 0.162460 -0.500000 0.850651 0.00000 MTRIX3 17 -0.276393 -0.850651 -0.447214 0.00000 MTRIX1 18 -0.447214 -0.850651 0.276393 0.00000 MTRIX2 18 0.525731 0.000000 0.850651 0.00000 MTRIX3 18 -0.723607 0.525731 0.447214 0.00000 MTRIX1 19 -0.052786 0.688191 0.723607 0.00000 MTRIX2 19 0.688191 -0.500000 0.525731 0.00000 MTRIX3 19 0.723607 0.525731 -0.447214 0.00000 MTRIX1 20 0.447214 0.525731 0.723607 0.00000 MTRIX2 20 0.850651 0.000000 -0.525731 0.00000 MTRIX3 20 -0.276393 0.850651 -0.447214 0.00000 MTRIX1 21 0.809017 -0.587785 0.000000 0.00000 MTRIX2 21 -0.587785 -0.809017 0.000000 0.00000 MTRIX3 21 0.000000 0.000000 -1.000000 0.00000 MTRIX1 22 -0.361803 -0.587785 0.723607 0.00000 MTRIX2 22 -0.262866 0.809017 0.525731 0.00000 MTRIX3 22 -0.894427 0.000000 -0.447214 0.00000 MTRIX1 23 0.138197 -0.951057 -0.276393 0.00000 MTRIX2 23 -0.425325 -0.309017 0.850651 0.00000 MTRIX3 23 -0.894427 0.000000 -0.447214 0.00000 MTRIX1 24 -0.670820 0.162460 0.723607 0.00000 MTRIX2 24 0.688191 0.500000 0.525731 0.00000 MTRIX3 24 -0.276393 0.850651 -0.447214 0.00000 MTRIX1 25 0.809017 0.587785 0.000000 0.00000 MTRIX2 25 0.587785 -0.809017 0.000000 0.00000 MTRIX3 25 0.000000 0.000000 -1.000000 0.00000 MTRIX1 26 0.138197 0.951057 -0.276393 0.00000 MTRIX2 26 0.425325 -0.309017 -0.850651 0.00000 MTRIX3 26 -0.894427 0.000000 -0.447214 0.00000 MTRIX1 27 0.138197 -0.425325 -0.894427 0.00000 MTRIX2 27 -0.951057 -0.309017 0.000000 0.00000 MTRIX3 27 -0.276393 0.850651 -0.447214 0.00000 MTRIX1 28 -1.000000 0.000000 0.000000 0.00000 MTRIX2 28 0.000000 1.000000 0.000000 0.00000 MTRIX3 28 0.000000 0.000000 -1.000000 0.00000 MTRIX1 29 -0.861803 -0.425325 -0.276393 0.00000 MTRIX2 29 -0.425325 0.309017 0.850651 0.00000 MTRIX3 29 -0.276393 0.850651 -0.447214 0.00000 MTRIX1 30 -0.309017 0.951057 0.000000 0.00000 MTRIX2 30 0.951057 0.309017 0.000000 0.00000 MTRIX3 30 0.000000 0.000000 -1.000000 0.00000 MTRIX1 31 0.447214 0.000000 -0.894427 0.00000 MTRIX2 31 0.000000 -1.000000 0.000000 0.00000 MTRIX3 31 -0.894427 0.000000 -0.447214 0.00000 MTRIX1 32 0.361803 0.587785 -0.723607 0.00000 MTRIX2 32 -0.262866 0.809017 0.525731 0.00000 MTRIX3 32 0.894427 0.000000 0.447214 0.00000 MTRIX1 33 -0.447214 -0.525731 -0.723607 0.00000 MTRIX2 33 0.850651 0.000000 -0.525731 0.00000 MTRIX3 33 0.276393 -0.850651 0.447214 0.00000 MTRIX1 34 -0.809017 0.587785 0.000000 0.00000 MTRIX2 34 -0.587785 -0.809017 0.000000 0.00000 MTRIX3 34 0.000000 0.000000 1.000000 0.00000 MTRIX1 35 -0.947214 -0.162460 0.276393 0.00000 MTRIX2 35 -0.162460 -0.500000 -0.850651 0.00000 MTRIX3 35 0.276393 -0.850651 0.447214 0.00000 MTRIX1 36 0.309017 0.951057 0.000000 0.00000 MTRIX2 36 -0.951057 0.309017 0.000000 0.00000 MTRIX3 36 0.000000 0.000000 1.000000 0.00000 MTRIX1 37 0.361803 -0.587785 -0.723607 0.00000 MTRIX2 37 0.262866 0.809017 -0.525731 0.00000 MTRIX3 37 0.894427 0.000000 0.447214 0.00000 MTRIX1 38 -0.361803 -0.262866 -0.894427 0.00000 MTRIX2 38 -0.587785 0.809017 0.000000 0.00000 MTRIX3 38 0.723607 0.525731 -0.447214 0.00000 MTRIX1 39 -0.861803 0.425325 -0.276393 0.00000 MTRIX2 39 0.425325 0.309017 -0.850651 0.00000 MTRIX3 39 -0.276393 -0.850651 -0.447214 0.00000 MTRIX1 40 0.052786 0.688191 -0.723607 0.00000 MTRIX2 40 -0.688191 -0.500000 -0.525731 0.00000 MTRIX3 40 -0.723607 0.525731 0.447214 0.00000 MTRIX1 41 -0.447214 0.850651 0.276393 0.00000 MTRIX2 41 -0.525731 0.000000 -0.850651 0.00000 MTRIX3 41 -0.723607 -0.525731 0.447214 0.00000 MTRIX1 42 0.670820 0.162460 -0.723607 0.00000 MTRIX2 42 -0.688191 0.500000 -0.525731 0.00000 MTRIX3 42 0.276393 0.850651 0.447214 0.00000 MTRIX1 43 -0.670820 -0.688191 -0.276393 0.00000 MTRIX2 43 -0.162460 0.500000 -0.850651 0.00000 MTRIX3 43 0.723607 -0.525731 -0.447214 0.00000 MTRIX1 44 -0.309017 -0.951057 0.000000 0.00000 MTRIX2 44 -0.951057 0.309017 0.000000 0.00000 MTRIX3 44 0.000000 0.000000 -1.000000 0.00000 MTRIX1 45 -0.361803 0.587785 0.723607 0.00000 MTRIX2 45 0.262866 0.809017 -0.525731 0.00000 MTRIX3 45 -0.894427 0.000000 -0.447214 0.00000 MTRIX1 46 0.947214 0.162460 -0.276393 0.00000 MTRIX2 46 -0.162460 -0.500000 -0.850651 0.00000 MTRIX3 46 -0.276393 0.850651 -0.447214 0.00000 MTRIX1 47 0.670820 0.688191 0.276393 0.00000 MTRIX2 47 -0.162460 0.500000 -0.850651 0.00000 MTRIX3 47 -0.723607 0.525731 0.447214 0.00000 MTRIX1 48 0.447214 -0.850651 -0.276393 0.00000 MTRIX2 48 -0.525731 0.000000 -0.850651 0.00000 MTRIX3 48 0.723607 0.525731 -0.447214 0.00000 MTRIX1 49 -0.670820 -0.162460 0.723607 0.00000 MTRIX2 49 -0.688191 0.500000 -0.525731 0.00000 MTRIX3 49 -0.276393 -0.850651 -0.447214 0.00000 MTRIX1 50 0.447214 -0.525731 0.723607 0.00000 MTRIX2 50 -0.850651 0.000000 0.525731 0.00000 MTRIX3 50 -0.276393 -0.850651 -0.447214 0.00000 MTRIX1 51 0.361803 -0.262866 0.894427 0.00000 MTRIX2 51 0.587785 0.809017 0.000000 0.00000 MTRIX3 51 -0.723607 0.525731 0.447214 0.00000 MTRIX1 52 0.638197 -0.262866 0.723607 0.00000 MTRIX2 52 0.262866 -0.809017 -0.525731 0.00000 MTRIX3 52 0.723607 0.525731 -0.447214 0.00000 MTRIX1 53 0.861803 -0.425325 0.276393 0.00000 MTRIX2 53 0.425325 0.309017 -0.850651 0.00000 MTRIX3 53 0.276393 0.850651 0.447214 0.00000 MTRIX1 54 -0.052786 -0.688191 0.723607 0.00000 MTRIX2 54 -0.688191 -0.500000 -0.525731 0.00000 MTRIX3 54 0.723607 -0.525731 -0.447214 0.00000 MTRIX1 55 0.361803 0.262866 0.894427 0.00000 MTRIX2 55 -0.587785 0.809017 0.000000 0.00000 MTRIX3 55 -0.723607 -0.525731 0.447214 0.00000 MTRIX1 56 0.861803 0.425325 0.276393 0.00000 MTRIX2 56 -0.425325 0.309017 0.850651 0.00000 MTRIX3 56 0.276393 -0.850651 0.447214 0.00000 MTRIX1 57 0.309017 -0.951057 0.000000 0.00000 MTRIX2 57 0.951057 0.309017 0.000000 0.00000 MTRIX3 57 0.000000 0.000000 1.000000 0.00000 MTRIX1 58 -0.447214 0.000000 0.894427 0.00000 MTRIX2 58 0.000000 -1.000000 0.000000 0.00000 MTRIX3 58 0.894427 0.000000 0.447214 0.00000 MTRIX1 59 -0.138197 -0.951057 0.276393 0.00000 MTRIX2 59 0.425325 -0.309017 -0.850651 0.00000 MTRIX3 59 0.894427 0.000000 0.447214 0.00000 MTRIX1 60 -0.138197 0.425325 0.894427 0.00000 MTRIX2 60 -0.951057 -0.309017 0.000000 0.00000 MTRIX3 60 0.276393 -0.850651 0.447214 0.00000