HEADER VIRUS/IMMUNE SYSTEM 29-JAN-24 8Y3I TITLE CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 N153Q TITLE 2 MUTANT IN COMPLEX WITH HUMAN ANTIBODY C10 FAB AT 37 DEG C COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE PROTEIN; COMPND 3 CHAIN: A, C, E; COMPND 4 SYNONYM: GENOME POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MEMBRANE PROTEIN; COMPND 9 CHAIN: B, D, F; COMPND 10 SYNONYM: GENOME POLYPROTEIN; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: HUMAN ANTIBODY C10 FAB (HEAVY CHAIN); COMPND 14 CHAIN: G, I, K; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: HUMAN ANTIBODY C10 FAB (LIGHT CHAIN); COMPND 18 CHAIN: H, J, L; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS TYPE 2; SOURCE 3 ORGANISM_TAXID: 11060; SOURCE 4 STRAIN: D2Y98P; SOURCE 5 GENE: E; SOURCE 6 EXPRESSION_SYSTEM: AEDES ALBOPICTUS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: ASIAN TIGER MOSQUITO; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7160; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: DENGUE VIRUS TYPE 2; SOURCE 11 ORGANISM_TAXID: 11060; SOURCE 12 STRAIN: D2Y98P; SOURCE 13 EXPRESSION_SYSTEM: AEDES ALBOPICTUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: ASIAN TIGER MOSQUITO; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7160; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 22 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 29 EXPRESSION_SYSTEM_CELL: EXPI293F KEYWDS DENGUE VIRUS, HUMAN ANTIBODY, DENGUE-ANTIBODY STRUCTURE, VIRUS, KEYWDS 2 VIRUS-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.FIBRIANSAH,T.S.NG,X.N.LIM,A.W.K.TAN,J.SHI,S.M.LOK REVDAT 1 29-JAN-25 8Y3I 0 JRNL AUTH G.FIBRIANSAH,T.S.NG,X.N.LIM,A.W.K.TAN,J.SHI,J.E.CROWE, JRNL AUTH 2 S.M.LOK JRNL TITL ROLE OF N-GLYCOSYLATION AT ASPARAGINE 153 OF DENGUE ENVELOPE JRNL TITL 2 PROTEIN IN IMMUNE RESPONSE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SERIALEM, COOT, RELION, RELION, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 4UIF 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 : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.900 REMARK 3 NUMBER OF PARTICLES : 102447 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8Y3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300043026. 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 : DENGUE VIRUS SEROTYPE 2 STRAIN REMARK 245 Y98P-PP1 N153Q MUTANT IN REMARK 245 COMPLEX WITH HUMAN ANTIBODY C10 REMARK 245 FAB AT 37 DEG C; DENGUE REMARK 245 SEROTYPE 2 STRAIN D2Y98P-PP1 REMARK 245 N153Q MUTANT; HUMAN ANTIBODY REMARK 245 C10 FAB (HEAVY AND LIGHT CHAINS) 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 : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4700.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2337.00 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, G, H, I, J, REMARK 350 AND CHAINS: K, 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 0.00000 REMARK 350 BIOMT2 2 -0.262866 0.809017 0.525731 0.00000 REMARK 350 BIOMT3 2 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 3 -0.670820 0.688191 -0.276393 0.00000 REMARK 350 BIOMT2 3 0.162460 0.500000 0.850651 0.00000 REMARK 350 BIOMT3 3 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 4 -0.670820 0.162460 0.723607 0.00000 REMARK 350 BIOMT2 4 0.688191 0.500000 0.525731 0.00000 REMARK 350 BIOMT3 4 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 5 0.361803 -0.262866 0.894427 0.00000 REMARK 350 BIOMT2 5 0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 5 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 6 -0.052787 0.688191 0.723607 0.00000 REMARK 350 BIOMT2 6 0.688191 -0.500000 0.525731 0.00000 REMARK 350 BIOMT3 6 0.723607 0.525731 -0.447213 0.00000 REMARK 350 BIOMT1 7 0.447214 0.525731 0.723607 0.00000 REMARK 350 BIOMT2 7 0.850651 0.000000 -0.525731 0.00000 REMARK 350 BIOMT3 7 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 8 0.670820 0.688191 0.276393 0.00000 REMARK 350 BIOMT2 8 -0.162460 0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 8 -0.723607 0.525731 0.447214 0.00000 REMARK 350 BIOMT1 9 0.309017 0.951057 0.000000 0.00000 REMARK 350 BIOMT2 9 -0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 10 -0.138197 0.951057 0.276393 0.00000 REMARK 350 BIOMT2 10 -0.425326 -0.309017 0.850651 0.00000 REMARK 350 BIOMT3 10 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 11 -0.309017 -0.951057 0.000000 0.00000 REMARK 350 BIOMT2 11 -0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 12 0.138197 -0.951057 -0.276393 0.00000 REMARK 350 BIOMT2 12 -0.425326 -0.309017 0.850651 0.00000 REMARK 350 BIOMT3 12 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 13 0.052787 -0.688191 -0.723607 0.00000 REMARK 350 BIOMT2 13 0.688191 -0.500000 0.525731 0.00000 REMARK 350 BIOMT3 13 -0.723607 -0.525731 0.447213 0.00000 REMARK 350 BIOMT1 14 -0.447214 -0.525731 -0.723607 0.00000 REMARK 350 BIOMT2 14 0.850651 0.000000 -0.525731 0.00000 REMARK 350 BIOMT3 14 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 15 -0.670820 -0.688191 -0.276393 0.00000 REMARK 350 BIOMT2 15 -0.162460 0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 15 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 16 -0.638196 0.262866 -0.723607 0.00000 REMARK 350 BIOMT2 16 0.262866 -0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 16 -0.723607 -0.525731 0.447213 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 -0.052787 -0.688191 0.723607 0.00000 REMARK 350 BIOMT2 18 -0.688191 -0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 18 0.723607 -0.525731 -0.447213 0.00000 REMARK 350 BIOMT1 19 0.809017 -0.587785 0.000000 0.00000 REMARK 350 BIOMT2 19 -0.587785 -0.809017 0.000000 0.00000 REMARK 350 BIOMT3 19 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 20 0.447214 0.000000 -0.894427 0.00000 REMARK 350 BIOMT2 20 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 20 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 21 -0.447214 0.525731 -0.723607 0.00000 REMARK 350 BIOMT2 21 -0.850651 0.000000 0.525731 0.00000 REMARK 350 BIOMT3 21 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 22 -0.947214 0.162460 0.276393 0.00000 REMARK 350 BIOMT2 22 0.162460 -0.500000 0.850651 0.00000 REMARK 350 BIOMT3 22 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 23 -0.138197 -0.425326 0.894427 0.00000 REMARK 350 BIOMT2 23 0.951057 -0.309017 0.000000 0.00000 REMARK 350 BIOMT3 23 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 24 0.861803 -0.425326 0.276393 0.00000 REMARK 350 BIOMT2 24 0.425326 0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 24 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 25 0.670820 0.162460 -0.723607 0.00000 REMARK 350 BIOMT2 25 -0.688191 0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 25 0.276393 0.850651 0.447214 0.00000 REMARK 350 BIOMT1 26 -0.138197 -0.951057 0.276393 0.00000 REMARK 350 BIOMT2 26 0.425326 -0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 26 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 27 0.447214 -0.850651 -0.276393 0.00000 REMARK 350 BIOMT2 27 -0.525731 0.000000 -0.850651 0.00000 REMARK 350 BIOMT3 27 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 28 0.138197 -0.425326 -0.894427 0.00000 REMARK 350 BIOMT2 28 -0.951057 -0.309017 0.000000 0.00000 REMARK 350 BIOMT3 28 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 29 -0.638196 -0.262866 -0.723607 0.00000 REMARK 350 BIOMT2 29 -0.262866 -0.809017 0.525731 0.00000 REMARK 350 BIOMT3 29 -0.723607 0.525731 0.447213 0.00000 REMARK 350 BIOMT1 30 -0.809017 -0.587785 0.000000 0.00000 REMARK 350 BIOMT2 30 0.587785 -0.809017 0.000000 0.00000 REMARK 350 BIOMT3 30 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 31 -0.361803 0.587785 0.723607 0.00000 REMARK 350 BIOMT2 31 0.262866 0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 31 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 32 0.361803 0.262866 0.894427 0.00000 REMARK 350 BIOMT2 32 -0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 32 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 33 0.861803 0.425326 0.276393 0.00000 REMARK 350 BIOMT2 33 -0.425326 0.309017 0.850651 0.00000 REMARK 350 BIOMT3 33 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 34 0.447214 0.850651 -0.276393 0.00000 REMARK 350 BIOMT2 34 0.525731 0.000000 0.850651 0.00000 REMARK 350 BIOMT3 34 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 35 -0.309017 0.951057 0.000000 0.00000 REMARK 350 BIOMT2 35 0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 35 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 36 0.947214 -0.162460 -0.276393 0.00000 REMARK 350 BIOMT2 36 0.162460 -0.500000 0.850651 0.00000 REMARK 350 BIOMT3 36 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 37 0.138197 0.425326 -0.894427 0.00000 REMARK 350 BIOMT2 37 0.951057 -0.309017 0.000000 0.00000 REMARK 350 BIOMT3 37 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 38 -0.861803 0.425326 -0.276393 0.00000 REMARK 350 BIOMT2 38 0.425326 0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 38 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 39 -0.670820 -0.162460 0.723607 0.00000 REMARK 350 BIOMT2 39 -0.688191 0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 39 -0.276393 -0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 40 0.447214 -0.525731 0.723607 0.00000 REMARK 350 BIOMT2 40 -0.850651 0.000000 0.525731 0.00000 REMARK 350 BIOMT3 40 -0.276393 -0.850651 -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 0.309017 -0.951057 0.000000 0.00000 REMARK 350 BIOMT2 42 0.951057 0.309017 0.000000 0.00000 REMARK 350 BIOMT3 42 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 43 0.361803 -0.587785 -0.723607 0.00000 REMARK 350 BIOMT2 43 0.262866 0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 43 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 44 -0.361803 -0.262866 -0.894427 0.00000 REMARK 350 BIOMT2 44 -0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 44 0.723607 0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 45 -0.861803 -0.425326 -0.276393 0.00000 REMARK 350 BIOMT2 45 -0.425326 0.309017 0.850651 0.00000 REMARK 350 BIOMT3 45 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 46 -0.361803 0.262866 -0.894427 0.00000 REMARK 350 BIOMT2 46 0.587785 0.809017 0.000000 0.00000 REMARK 350 BIOMT3 46 0.723607 -0.525731 -0.447214 0.00000 REMARK 350 BIOMT1 47 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 47 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 47 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 48 -0.361803 -0.587785 0.723607 0.00000 REMARK 350 BIOMT2 48 -0.262866 0.809017 0.525731 0.00000 REMARK 350 BIOMT3 48 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 49 0.670820 -0.688191 0.276393 0.00000 REMARK 350 BIOMT2 49 0.162460 0.500000 0.850651 0.00000 REMARK 350 BIOMT3 49 -0.723607 -0.525731 0.447214 0.00000 REMARK 350 BIOMT1 50 0.670820 -0.162460 -0.723607 0.00000 REMARK 350 BIOMT2 50 0.688191 0.500000 0.525731 0.00000 REMARK 350 BIOMT3 50 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 51 0.947214 0.162460 -0.276393 0.00000 REMARK 350 BIOMT2 51 -0.162460 -0.500000 -0.850651 0.00000 REMARK 350 BIOMT3 51 -0.276393 0.850651 -0.447214 0.00000 REMARK 350 BIOMT1 52 0.052787 0.688191 -0.723607 0.00000 REMARK 350 BIOMT2 52 -0.688191 -0.500000 -0.525731 0.00000 REMARK 350 BIOMT3 52 -0.723607 0.525731 0.447213 0.00000 REMARK 350 BIOMT1 53 -0.809017 0.587785 0.000000 0.00000 REMARK 350 BIOMT2 53 -0.587785 -0.809017 0.000000 0.00000 REMARK 350 BIOMT3 53 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 54 -0.447214 0.000000 0.894427 0.00000 REMARK 350 BIOMT2 54 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 54 0.894427 0.000000 0.447214 0.00000 REMARK 350 BIOMT1 55 0.638196 -0.262866 0.723607 0.00000 REMARK 350 BIOMT2 55 0.262866 -0.809017 -0.525731 0.00000 REMARK 350 BIOMT3 55 0.723607 0.525731 -0.447213 0.00000 REMARK 350 BIOMT1 56 -0.138197 0.425326 0.894427 0.00000 REMARK 350 BIOMT2 56 -0.951057 -0.309017 0.000000 0.00000 REMARK 350 BIOMT3 56 0.276393 -0.850651 0.447214 0.00000 REMARK 350 BIOMT1 57 0.638196 0.262866 0.723607 0.00000 REMARK 350 BIOMT2 57 -0.262866 -0.809017 0.525731 0.00000 REMARK 350 BIOMT3 57 0.723607 -0.525731 -0.447213 0.00000 REMARK 350 BIOMT1 58 0.809017 0.587785 0.000000 0.00000 REMARK 350 BIOMT2 58 0.587785 -0.809017 0.000000 0.00000 REMARK 350 BIOMT3 58 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 59 0.138197 0.951057 -0.276393 0.00000 REMARK 350 BIOMT2 59 0.425326 -0.309017 -0.850651 0.00000 REMARK 350 BIOMT3 59 -0.894427 0.000000 -0.447214 0.00000 REMARK 350 BIOMT1 60 -0.447214 0.850651 0.276393 0.00000 REMARK 350 BIOMT2 60 -0.525731 0.000000 -0.850651 0.00000 REMARK 350 BIOMT3 60 -0.723607 -0.525731 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 G 127 REMARK 465 SER I 127 REMARK 465 GLU K 1 REMARK 465 SER K 127 REMARK 465 SER L 0 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 NH2 ARG G 67 OD2 ASP G 90 1.81 REMARK 500 OG SER A 470 OG SER A 476 1.94 REMARK 500 OD2 ASP E 10 NH2 ARG E 411 2.01 REMARK 500 OD2 ASP I 99 OH TYR I 107 2.01 REMARK 500 O GLY A 445 OG SER A 449 2.02 REMARK 500 OD2 ASP A 10 NH2 ARG A 411 2.04 REMARK 500 OG SER K 17 OE2 GLU K 82 2.04 REMARK 500 N ALA C 495 OE2 GLU D 13 2.04 REMARK 500 O GLY C 445 OG SER C 449 2.07 REMARK 500 O ASP L 28 OG SER L 92 2.07 REMARK 500 OG1 THR A 319 OE2 GLU A 368 2.09 REMARK 500 NZ LYS C 246 OD2 ASP K 106 2.14 REMARK 500 OE1 GLU C 184 NH2 ARG C 288 2.16 REMARK 500 NE2 GLN A 167 OE2 GLU E 311 2.17 REMARK 500 OD1 ASP I 99 OG1 THR I 111 2.18 REMARK 500 OG1 THR E 280 OG1 THR F 14 2.19 REMARK 500 NZ LYS E 123 OE2 GLU E 202 2.19 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 THR A 76 -0.87 79.97 REMARK 500 THR A 226 -9.99 68.35 REMARK 500 GLN A 233 65.96 -100.40 REMARK 500 MET A 289 57.11 -95.52 REMARK 500 THR A 303 67.82 -100.45 REMARK 500 GLN A 494 137.71 85.13 REMARK 500 VAL B 8 -67.49 -90.22 REMARK 500 THR B 14 -167.84 -101.62 REMARK 500 THR B 55 -2.14 83.33 REMARK 500 ASN C 194 2.86 83.76 REMARK 500 GLU C 202 -120.48 65.08 REMARK 500 GLN C 233 38.18 70.58 REMARK 500 LEU C 253 36.38 71.15 REMARK 500 GLN C 494 42.18 72.15 REMARK 500 HIS D 7 30.45 -95.88 REMARK 500 HIS D 39 66.35 -116.63 REMARK 500 ASN E 203 -3.29 82.22 REMARK 500 SER E 298 54.60 -96.66 REMARK 500 ASP E 362 58.85 -92.38 REMARK 500 ASP E 417 -2.47 65.86 REMARK 500 GLN E 494 62.47 62.43 REMARK 500 THR G 28 99.58 -69.26 REMARK 500 PRO G 41 78.22 -64.61 REMARK 500 GLU G 89 -8.43 -58.78 REMARK 500 TRP G 113 54.20 -94.12 REMARK 500 GLN H 1 -132.16 50.92 REMARK 500 ASP H 28 -68.33 -104.59 REMARK 500 VAL H 53 -65.16 76.10 REMARK 500 MET I 48 -60.38 -91.23 REMARK 500 TRP I 113 59.09 -96.05 REMARK 500 TRP K 113 51.66 -93.29 REMARK 500 TYR L 34 49.05 -85.11 REMARK 500 VAL L 53 -59.09 74.48 REMARK 500 VAL L 109 -51.66 67.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 188 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38881 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 REMARK 900 N153Q MUTANT AT 4 DEG C REMARK 900 RELATED ID: EMD-38882 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 REMARK 900 N153Q MUTANT IN COMPLEX WITH HUMAN ANTIBODY 2D22 FAB AT 37 DEG C REMARK 900 RELATED ID: EMD-38884 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 AT 4 REMARK 900 DEG C REMARK 900 RELATED ID: EMD-38885 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 IN REMARK 900 COMPLEX WITH HUMAN ANTIBODY 2D22 FAB AT 37 DEG C REMARK 900 RELATED ID: EMD-38886 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 IN REMARK 900 COMPLEX WITH HUMAN ANTIBODY C10 FAB AT 37 DEG C REMARK 900 RELATED ID: EMD-38883 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DENGUE VIRUS SEROTYPE 2 STRAIN D2Y98P-PP1 REMARK 900 N153Q MUTANT IN COMPLEX WITH HUMAN ANTIBODY C10 FAB AT 37 DEG C DBREF1 8Y3I A 1 495 UNP A0A678XB23_9FLAV DBREF2 8Y3I A A0A678XB23 1 495 DBREF 8Y3I B 1 75 UNP A4GVG9 A4GVG9_9FLAV 206 280 DBREF1 8Y3I C 1 495 UNP A0A678XB23_9FLAV DBREF2 8Y3I C A0A678XB23 1 495 DBREF 8Y3I D 1 75 UNP A4GVG9 A4GVG9_9FLAV 206 280 DBREF1 8Y3I E 1 495 UNP A0A678XB23_9FLAV DBREF2 8Y3I E A0A678XB23 1 495 DBREF 8Y3I F 1 75 UNP A4GVG9 A4GVG9_9FLAV 206 280 DBREF 8Y3I G 1 127 PDB 8Y3I 8Y3I 1 127 DBREF 8Y3I H 0 110 PDB 8Y3I 8Y3I 0 110 DBREF 8Y3I I 1 127 PDB 8Y3I 8Y3I 1 127 DBREF 8Y3I J 0 110 PDB 8Y3I 8Y3I 0 110 DBREF 8Y3I K 1 127 PDB 8Y3I 8Y3I 1 127 DBREF 8Y3I L 0 110 PDB 8Y3I 8Y3I 0 110 SEQADV 8Y3I GLN A 153 UNP A0A678XB2 ASN 153 ENGINEERED MUTATION SEQADV 8Y3I GLN C 153 UNP A0A678XB2 ASN 153 ENGINEERED MUTATION SEQADV 8Y3I GLN E 153 UNP A0A678XB2 ASN 153 ENGINEERED MUTATION SEQRES 1 A 495 MET ARG CYS ILE GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 A 495 GLY VAL SER GLY GLY SER TRP VAL ASP ILE VAL LEU GLU SEQRES 3 A 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASN LYS PRO SEQRES 4 A 495 THR LEU ASP PHE GLU LEU ILE LYS THR GLU ALA LYS HIS SEQRES 5 A 495 PRO ALA THR LEU ARG LYS TYR CYS ILE GLU ALA LYS LEU SEQRES 6 A 495 THR ASN THR THR THR ALA SER ARG CYS PRO THR GLN GLY SEQRES 7 A 495 GLU PRO SER LEU ASN GLU GLU GLN ASP LYS ARG PHE VAL SEQRES 8 A 495 CYS LYS HIS SER MET VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 495 CYS GLY LEU PHE GLY LYS GLY GLY ILE VAL THR CYS ALA SEQRES 10 A 495 MET PHE THR CYS LYS LYS ASN MET GLU GLY LYS ILE VAL SEQRES 11 A 495 GLN PRO GLU ASN LEU GLU TYR THR ILE VAL ILE THR PRO SEQRES 12 A 495 HIS SER GLY GLU GLU ASN ALA VAL GLY GLN ASP THR GLY SEQRES 13 A 495 LYS HIS GLY LYS GLU ILE LYS VAL THR PRO GLN SER SER SEQRES 14 A 495 ILE THR GLU ALA GLU LEU THR GLY TYR GLY THR VAL THR SEQRES 15 A 495 MET GLU CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 A 495 MET VAL LEU LEU GLN MET GLU ASN LYS ALA TRP LEU VAL SEQRES 17 A 495 HIS ARG GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP LEU SEQRES 18 A 495 PRO GLY ALA ASP THR GLN GLY SER ASN TRP ILE GLN LYS SEQRES 19 A 495 GLU THR LEU VAL THR PHE LYS ASN PRO HIS ALA LYS LYS SEQRES 20 A 495 GLN ASP 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 MET SER SEQRES 22 A 495 SER GLY ASN LEU LEU PHE THR GLY HIS LEU LYS CYS ARG SEQRES 23 A 495 LEU ARG MET ASP LYS LEU GLN LEU LYS GLY MET SER TYR SEQRES 24 A 495 SER MET CYS THR GLY LYS PHE LYS VAL VAL LYS GLU ILE SEQRES 25 A 495 ALA GLU THR GLN HIS GLY THR ILE VAL ILE ARG VAL GLN SEQRES 26 A 495 TYR GLU GLY ASP GLY SER PRO CYS LYS ILE PRO PHE GLU SEQRES 27 A 495 ILE MET ASP LEU GLU LYS ARG HIS VAL LEU GLY ARG LEU SEQRES 28 A 495 ILE THR VAL ASN PRO ILE VAL THR GLU LYS ASP SER PRO SEQRES 29 A 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY ASP SER TYR SEQRES 30 A 495 ILE ILE ILE GLY VAL GLU PRO GLY GLN LEU LYS LEU SER SEQRES 31 A 495 TRP PHE LYS LYS GLY SER SER ILE GLY GLN MET PHE GLU SEQRES 32 A 495 THR THR MET ARG GLY ALA LYS ARG MET ALA ILE LEU GLY SEQRES 33 A 495 ASP THR ALA TRP ASP PHE GLY SER LEU GLY GLY VAL PHE SEQRES 34 A 495 THR SER ILE GLY LYS ALA LEU HIS GLN VAL PHE GLY ALA SEQRES 35 A 495 ILE TYR GLY ALA ALA PHE SER GLY VAL SER TRP THR MET SEQRES 36 A 495 LYS ILE LEU ILE GLY VAL VAL ILE THR TRP ILE GLY MET SEQRES 37 A 495 ASN SER ARG SER THR SER LEU SER VAL SER LEU VAL LEU SEQRES 38 A 495 VAL GLY VAL VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 A 495 ALA SEQRES 1 B 75 SER VAL ALA LEU VAL PRO HIS VAL GLY MET 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 HIS ALA GLN ARG ILE GLU THR TRP VAL LEU ARG HIS SEQRES 4 B 75 PRO GLY PHE THR ILE MET ALA ALA ILE LEU ALA TYR THR SEQRES 5 B 75 ILE GLY THR THR TYR PHE GLN ARG VAL LEU ILE PHE ILE SEQRES 6 B 75 LEU LEU THR ALA VAL ALA PRO SER MET THR SEQRES 1 C 495 MET ARG CYS ILE GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 C 495 GLY VAL SER GLY GLY SER TRP VAL ASP ILE VAL LEU GLU SEQRES 3 C 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASN LYS PRO SEQRES 4 C 495 THR LEU ASP PHE GLU LEU ILE LYS THR GLU ALA LYS HIS SEQRES 5 C 495 PRO ALA THR LEU ARG LYS TYR CYS ILE GLU ALA LYS LEU SEQRES 6 C 495 THR ASN THR THR THR ALA SER ARG CYS PRO THR GLN GLY SEQRES 7 C 495 GLU PRO SER LEU ASN GLU GLU GLN ASP LYS ARG PHE VAL SEQRES 8 C 495 CYS LYS HIS SER MET VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 C 495 CYS GLY LEU PHE GLY LYS GLY GLY ILE VAL THR CYS ALA SEQRES 10 C 495 MET PHE THR CYS LYS LYS ASN MET GLU GLY LYS ILE VAL SEQRES 11 C 495 GLN PRO GLU ASN LEU GLU TYR THR ILE VAL ILE THR PRO SEQRES 12 C 495 HIS SER GLY GLU GLU ASN ALA VAL GLY GLN ASP THR GLY SEQRES 13 C 495 LYS HIS GLY LYS GLU ILE LYS VAL THR PRO GLN SER SER SEQRES 14 C 495 ILE THR GLU ALA GLU LEU THR GLY TYR GLY THR VAL THR SEQRES 15 C 495 MET GLU CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 C 495 MET VAL LEU LEU GLN MET GLU ASN LYS ALA TRP LEU VAL SEQRES 17 C 495 HIS ARG GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP LEU SEQRES 18 C 495 PRO GLY ALA ASP THR GLN GLY SER ASN TRP ILE GLN LYS SEQRES 19 C 495 GLU THR LEU VAL THR PHE LYS ASN PRO HIS ALA LYS LYS SEQRES 20 C 495 GLN ASP 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 MET SER SEQRES 22 C 495 SER GLY ASN LEU LEU PHE THR GLY HIS LEU LYS CYS ARG SEQRES 23 C 495 LEU ARG MET ASP LYS LEU GLN LEU LYS GLY MET SER TYR SEQRES 24 C 495 SER MET CYS THR GLY LYS PHE LYS VAL VAL LYS GLU ILE SEQRES 25 C 495 ALA GLU THR GLN HIS GLY THR ILE VAL ILE ARG VAL GLN SEQRES 26 C 495 TYR GLU GLY ASP GLY SER PRO CYS LYS ILE PRO PHE GLU SEQRES 27 C 495 ILE MET ASP LEU GLU LYS ARG HIS VAL LEU GLY ARG LEU SEQRES 28 C 495 ILE THR VAL ASN PRO ILE VAL THR GLU LYS ASP SER PRO SEQRES 29 C 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY ASP SER TYR SEQRES 30 C 495 ILE ILE ILE GLY VAL GLU PRO GLY GLN LEU LYS LEU SER SEQRES 31 C 495 TRP PHE LYS LYS GLY SER SER ILE GLY GLN MET PHE GLU SEQRES 32 C 495 THR THR MET ARG GLY ALA LYS ARG MET ALA ILE LEU GLY SEQRES 33 C 495 ASP THR ALA TRP ASP PHE GLY SER LEU GLY GLY VAL PHE SEQRES 34 C 495 THR SER ILE GLY LYS ALA LEU HIS GLN VAL PHE GLY ALA SEQRES 35 C 495 ILE TYR GLY ALA ALA PHE SER GLY VAL SER TRP THR MET SEQRES 36 C 495 LYS ILE LEU ILE GLY VAL VAL ILE THR TRP ILE GLY MET SEQRES 37 C 495 ASN SER ARG SER THR SER LEU SER VAL SER LEU VAL LEU SEQRES 38 C 495 VAL GLY VAL VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 C 495 ALA SEQRES 1 D 75 SER VAL ALA LEU VAL PRO HIS VAL GLY MET 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 HIS ALA GLN ARG ILE GLU THR TRP VAL LEU ARG HIS SEQRES 4 D 75 PRO GLY PHE THR ILE MET ALA ALA ILE LEU ALA TYR THR SEQRES 5 D 75 ILE GLY THR THR TYR PHE GLN ARG VAL LEU ILE PHE ILE SEQRES 6 D 75 LEU LEU THR ALA VAL ALA PRO SER MET THR SEQRES 1 E 495 MET ARG CYS ILE GLY ILE SER ASN ARG ASP PHE VAL GLU SEQRES 2 E 495 GLY VAL SER GLY GLY SER TRP VAL ASP ILE VAL LEU GLU SEQRES 3 E 495 HIS GLY SER CYS VAL THR THR MET ALA LYS ASN LYS PRO SEQRES 4 E 495 THR LEU ASP PHE GLU LEU ILE LYS THR GLU ALA LYS HIS SEQRES 5 E 495 PRO ALA THR LEU ARG LYS TYR CYS ILE GLU ALA LYS LEU SEQRES 6 E 495 THR ASN THR THR THR ALA SER ARG CYS PRO THR GLN GLY SEQRES 7 E 495 GLU PRO SER LEU ASN GLU GLU GLN ASP LYS ARG PHE VAL SEQRES 8 E 495 CYS LYS HIS SER MET VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 E 495 CYS GLY LEU PHE GLY LYS GLY GLY ILE VAL THR CYS ALA SEQRES 10 E 495 MET PHE THR CYS LYS LYS ASN MET GLU GLY LYS ILE VAL SEQRES 11 E 495 GLN PRO GLU ASN LEU GLU TYR THR ILE VAL ILE THR PRO SEQRES 12 E 495 HIS SER GLY GLU GLU ASN ALA VAL GLY GLN ASP THR GLY SEQRES 13 E 495 LYS HIS GLY LYS GLU ILE LYS VAL THR PRO GLN SER SER SEQRES 14 E 495 ILE THR GLU ALA GLU LEU THR GLY TYR GLY THR VAL THR SEQRES 15 E 495 MET GLU CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU SEQRES 16 E 495 MET VAL LEU LEU GLN MET GLU ASN LYS ALA TRP LEU VAL SEQRES 17 E 495 HIS ARG GLN TRP PHE LEU ASP LEU PRO LEU PRO TRP LEU SEQRES 18 E 495 PRO GLY ALA ASP THR GLN GLY SER ASN TRP ILE GLN LYS SEQRES 19 E 495 GLU THR LEU VAL THR PHE LYS ASN PRO HIS ALA LYS LYS SEQRES 20 E 495 GLN ASP 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 MET SER SEQRES 22 E 495 SER GLY ASN LEU LEU PHE THR GLY HIS LEU LYS CYS ARG SEQRES 23 E 495 LEU ARG MET ASP LYS LEU GLN LEU LYS GLY MET SER TYR SEQRES 24 E 495 SER MET CYS THR GLY LYS PHE LYS VAL VAL LYS GLU ILE SEQRES 25 E 495 ALA GLU THR GLN HIS GLY THR ILE VAL ILE ARG VAL GLN SEQRES 26 E 495 TYR GLU GLY ASP GLY SER PRO CYS LYS ILE PRO PHE GLU SEQRES 27 E 495 ILE MET ASP LEU GLU LYS ARG HIS VAL LEU GLY ARG LEU SEQRES 28 E 495 ILE THR VAL ASN PRO ILE VAL THR GLU LYS ASP SER PRO SEQRES 29 E 495 VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY ASP SER TYR SEQRES 30 E 495 ILE ILE ILE GLY VAL GLU PRO GLY GLN LEU LYS LEU SER SEQRES 31 E 495 TRP PHE LYS LYS GLY SER SER ILE GLY GLN MET PHE GLU SEQRES 32 E 495 THR THR MET ARG GLY ALA LYS ARG MET ALA ILE LEU GLY SEQRES 33 E 495 ASP THR ALA TRP ASP PHE GLY SER LEU GLY GLY VAL PHE SEQRES 34 E 495 THR SER ILE GLY LYS ALA LEU HIS GLN VAL PHE GLY ALA SEQRES 35 E 495 ILE TYR GLY ALA ALA PHE SER GLY VAL SER TRP THR MET SEQRES 36 E 495 LYS ILE LEU ILE GLY VAL VAL ILE THR TRP ILE GLY MET SEQRES 37 E 495 ASN SER ARG SER THR SER LEU SER VAL SER LEU VAL LEU SEQRES 38 E 495 VAL GLY VAL VAL THR LEU TYR LEU GLY VAL MET VAL GLN SEQRES 39 E 495 ALA SEQRES 1 F 75 SER VAL ALA LEU VAL PRO HIS VAL GLY MET 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 HIS ALA GLN ARG ILE GLU THR TRP VAL LEU ARG HIS SEQRES 4 F 75 PRO GLY PHE THR ILE MET ALA ALA ILE LEU ALA TYR THR SEQRES 5 F 75 ILE GLY THR THR TYR PHE GLN ARG VAL LEU ILE PHE ILE SEQRES 6 F 75 LEU LEU THR ALA VAL ALA PRO SER MET THR SEQRES 1 G 127 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 127 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 G 127 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 G 127 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 G 127 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 G 127 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 G 127 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 G 127 ALA ILE TYR TYR CYS ALA ARG ASP LYS VAL ASP ASP TYR SEQRES 9 G 127 GLY ASP TYR TRP PHE PRO THR LEU TRP TYR PHE ASP TYR SEQRES 10 G 127 TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 H 111 SER GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SEQRES 2 H 111 SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SEQRES 3 H 111 SER SER ASP VAL GLY GLY PHE ASN TYR VAL SER TRP PHE SEQRES 4 H 111 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET LEU TYR SEQRES 5 H 111 ASP VAL THR SER ARG PRO SER GLY VAL SER SER ARG PHE SEQRES 6 H 111 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 H 111 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 H 111 SER SER HIS THR SER ARG GLY THR TRP VAL PHE GLY GLY SEQRES 9 H 111 GLY THR LYS LEU THR VAL LEU SEQRES 1 I 127 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 127 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 127 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 I 127 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 I 127 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 I 127 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 I 127 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 I 127 ALA ILE TYR TYR CYS ALA ARG ASP LYS VAL ASP ASP TYR SEQRES 9 I 127 GLY ASP TYR TRP PHE PRO THR LEU TRP TYR PHE ASP TYR SEQRES 10 I 127 TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 J 111 SER GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SEQRES 2 J 111 SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SEQRES 3 J 111 SER SER ASP VAL GLY GLY PHE ASN TYR VAL SER TRP PHE SEQRES 4 J 111 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET LEU TYR SEQRES 5 J 111 ASP VAL THR SER ARG PRO SER GLY VAL SER SER ARG PHE SEQRES 6 J 111 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 J 111 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 J 111 SER SER HIS THR SER ARG GLY THR TRP VAL PHE GLY GLY SEQRES 9 J 111 GLY THR LYS LEU THR VAL LEU SEQRES 1 K 127 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 127 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 K 127 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 K 127 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 K 127 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 K 127 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 K 127 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 K 127 ALA ILE TYR TYR CYS ALA ARG ASP LYS VAL ASP ASP TYR SEQRES 9 K 127 GLY ASP TYR TRP PHE PRO THR LEU TRP TYR PHE ASP TYR SEQRES 10 K 127 TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 L 111 SER GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SEQRES 2 L 111 SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SEQRES 3 L 111 SER SER ASP VAL GLY GLY PHE ASN TYR VAL SER TRP PHE SEQRES 4 L 111 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET LEU TYR SEQRES 5 L 111 ASP VAL THR SER ARG PRO SER GLY VAL SER SER ARG PHE SEQRES 6 L 111 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 L 111 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 L 111 SER SER HIS THR SER ARG GLY THR TRP VAL PHE GLY GLY SEQRES 9 L 111 GLY THR LYS LEU THR VAL LEU HET NAG A 501 14 HET NAG C 501 14 HET NAG E 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 13 NAG 3(C8 H15 N O6) HELIX 1 AA1 LEU A 82 ASP A 87 5 6 HELIX 2 AA2 GLN A 131 GLU A 133 5 3 HELIX 3 AA3 SER A 186 LEU A 191 1 6 HELIX 4 AA4 ASP A 192 ASN A 194 5 3 HELIX 5 AA5 ARG A 210 ASP A 215 1 6 HELIX 6 AA6 GLN A 233 THR A 236 5 4 HELIX 7 AA7 GLY A 258 LEU A 264 1 7 HELIX 8 AA8 SER A 396 GLY A 416 1 21 HELIX 9 AA9 ASP A 417 PHE A 422 5 6 HELIX 10 AB1 GLY A 427 PHE A 448 1 22 HELIX 11 AB2 SER A 452 ASN A 469 1 18 HELIX 12 AB3 SER A 472 VAL A 493 1 22 HELIX 13 AB4 MET B 20 ALA B 25 1 6 HELIX 14 AB5 TRP B 26 HIS B 39 1 14 HELIX 15 AB6 HIS B 39 ILE B 53 1 15 HELIX 16 AB7 THR B 56 MET B 74 1 19 HELIX 17 AB8 MET C 1 GLY C 5 5 5 HELIX 18 AB9 LEU C 82 GLN C 86 5 5 HELIX 19 AC1 GLN C 131 GLU C 133 5 3 HELIX 20 AC2 SER C 186 GLY C 190 5 5 HELIX 21 AC3 ARG C 210 ASP C 215 1 6 HELIX 22 AC4 GLN C 233 VAL C 238 5 6 HELIX 23 AC5 GLN C 256 LEU C 264 1 9 HELIX 24 AC6 SER C 396 LEU C 415 1 20 HELIX 25 AC7 GLY C 416 PHE C 422 5 7 HELIX 26 AC8 GLY C 427 SER C 449 1 23 HELIX 27 AC9 SER C 452 SER C 470 1 19 HELIX 28 AD1 SER C 472 VAL C 493 1 22 HELIX 29 AD2 SER D 1 VAL D 5 5 5 HELIX 30 AD3 MET D 20 ALA D 25 1 6 HELIX 31 AD4 TRP D 26 HIS D 39 1 14 HELIX 32 AD5 HIS D 39 GLY D 54 1 16 HELIX 33 AD6 THR D 56 THR D 75 1 20 HELIX 34 AD7 LEU E 82 ASP E 87 5 6 HELIX 35 AD8 GLN E 131 GLU E 133 5 3 HELIX 36 AD9 SER E 186 LEU E 191 1 6 HELIX 37 AE1 ARG E 210 ASP E 215 1 6 HELIX 38 AE2 GLN E 233 THR E 236 5 4 HELIX 39 AE3 ASN E 242 LYS E 246 5 5 HELIX 40 AE4 GLN E 256 LEU E 264 1 9 HELIX 41 AE5 SER E 396 LEU E 415 1 20 HELIX 42 AE6 THR E 418 PHE E 422 5 5 HELIX 43 AE7 GLY E 427 PHE E 448 1 22 HELIX 44 AE8 SER E 452 ASN E 469 1 18 HELIX 45 AE9 SER E 472 VAL E 493 1 22 HELIX 46 AF1 SER F 1 VAL F 5 5 5 HELIX 47 AF2 MET F 20 TRP F 26 1 7 HELIX 48 AF3 TRP F 26 HIS F 39 1 14 HELIX 49 AF4 HIS F 39 ILE F 53 1 15 HELIX 50 AF5 THR F 56 MET F 74 1 19 HELIX 51 AF6 THR G 28 THR G 30 5 3 HELIX 52 AF7 PHE G 64 ASP G 66 5 3 HELIX 53 AF8 ARG G 87 THR G 91 5 5 HELIX 54 AF9 ARG I 87 THR I 91 5 5 HELIX 55 AG1 THR K 28 THR K 30 5 3 HELIX 56 AG2 GLN K 62 GLN K 65 5 4 HELIX 57 AG3 ARG K 87 THR K 91 5 5 HELIX 58 AG4 GLN L 81 GLU L 85 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 VAL A 12 SHEET 3 AA1 5 LEU A 41 ALA A 50 -1 O PHE A 43 N VAL A 31 SHEET 4 AA1 5 LEU A 135 PRO A 143 -1 O THR A 138 N LYS A 47 SHEET 5 AA1 5 LYS A 160 VAL A 164 -1 O LYS A 160 N ILE A 141 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 VAL A 12 SHEET 3 AA2 4 LEU A 41 ALA A 50 -1 O PHE A 43 N VAL A 31 SHEET 4 AA2 4 ASN A 276 LEU A 278 -1 O LEU A 278 N THR A 48 SHEET 1 AA3 4 TRP A 20 GLU A 26 0 SHEET 2 AA3 4 HIS A 282 ARG A 288 -1 O LEU A 287 N VAL A 21 SHEET 3 AA3 4 THR A 180 CYS A 185 -1 N GLU A 184 O ARG A 286 SHEET 4 AA3 4 ILE A 170 GLU A 174 -1 N ALA A 173 O VAL A 181 SHEET 1 AA4 4 PHE A 90 ARG A 99 0 SHEET 2 AA4 4 GLY A 109 ILE A 129 -1 O GLY A 111 N VAL A 97 SHEET 3 AA4 4 ALA A 54 SER A 72 -1 N THR A 66 O MET A 118 SHEET 4 AA4 4 TRP A 220 PRO A 222 -1 O LEU A 221 N LYS A 58 SHEET 1 AA5 5 PHE A 90 ARG A 99 0 SHEET 2 AA5 5 GLY A 109 ILE A 129 -1 O GLY A 111 N VAL A 97 SHEET 3 AA5 5 MET A 196 GLN A 200 -1 O LEU A 198 N LYS A 128 SHEET 4 AA5 5 ALA A 205 HIS A 209 -1 O TRP A 206 N LEU A 199 SHEET 5 AA5 5 THR A 268 ILE A 270 -1 O ILE A 270 N ALA A 205 SHEET 1 AA6 4 GLY A 146 GLU A 147 0 SHEET 2 AA6 4 VAL A 365 GLU A 370 -1 O ASN A 366 N GLY A 146 SHEET 3 AA6 4 ILE A 320 TYR A 326 -1 N ILE A 322 O ILE A 367 SHEET 4 AA6 4 PHE A 306 GLU A 314 -1 N LYS A 307 O GLN A 325 SHEET 1 AA7 6 GLY A 146 GLU A 147 0 SHEET 2 AA7 6 VAL A 365 GLU A 370 -1 O ASN A 366 N GLY A 146 SHEET 3 AA7 6 VAL A 347 LEU A 351 -1 N ARG A 350 O GLU A 370 SHEET 4 AA7 6 PHE A 337 MET A 340 -1 N ILE A 339 O GLY A 349 SHEET 5 AA7 6 ASP A 375 ILE A 380 -1 O ILE A 379 N GLU A 338 SHEET 6 AA7 6 LEU A 387 PHE A 392 -1 O LEU A 389 N ILE A 378 SHEET 1 AA8 2 VAL A 238 LYS A 241 0 SHEET 2 AA8 2 ASP A 249 VAL A 252 -1 O VAL A 251 N THR A 239 SHEET 1 AA9 2 CYS A 333 LYS A 334 0 SHEET 2 AA9 2 ILE A 357 VAL A 358 -1 O VAL A 358 N CYS A 333 SHEET 1 AB1 5 ARG C 9 GLU C 13 0 SHEET 2 AB1 5 CYS C 30 MET C 34 1 O THR C 32 N ASP C 10 SHEET 3 AB1 5 LEU C 41 ALA C 50 -1 O PHE C 43 N VAL C 31 SHEET 4 AB1 5 LEU C 135 PRO C 143 -1 O GLU C 136 N GLU C 49 SHEET 5 AB1 5 LYS C 160 VAL C 164 -1 O LYS C 160 N ILE C 141 SHEET 1 AB2 4 ARG C 9 GLU C 13 0 SHEET 2 AB2 4 CYS C 30 MET C 34 1 O THR C 32 N ASP C 10 SHEET 3 AB2 4 LEU C 41 ALA C 50 -1 O PHE C 43 N VAL C 31 SHEET 4 AB2 4 LEU C 277 LEU C 278 -1 O LEU C 278 N THR C 48 SHEET 1 AB3 4 TRP C 20 VAL C 24 0 SHEET 2 AB3 4 LYS C 284 ARG C 288 -1 O LEU C 287 N VAL C 21 SHEET 3 AB3 4 GLY C 179 GLU C 184 -1 N GLU C 184 O ARG C 286 SHEET 4 AB3 4 ILE C 170 LEU C 175 -1 N ALA C 173 O VAL C 181 SHEET 1 AB4 4 PHE C 90 ARG C 99 0 SHEET 2 AB4 4 GLY C 109 ILE C 129 -1 O ILE C 113 N SER C 95 SHEET 3 AB4 4 ALA C 54 SER C 72 -1 N THR C 66 O MET C 118 SHEET 4 AB4 4 TRP C 220 LEU C 221 -1 O LEU C 221 N LYS C 58 SHEET 1 AB5 5 PHE C 90 ARG C 99 0 SHEET 2 AB5 5 GLY C 109 ILE C 129 -1 O ILE C 113 N SER C 95 SHEET 3 AB5 5 MET C 196 MET C 201 -1 O LEU C 198 N LYS C 128 SHEET 4 AB5 5 LYS C 204 HIS C 209 -1 O TRP C 206 N LEU C 199 SHEET 5 AB5 5 THR C 268 ILE C 270 -1 O ILE C 270 N ALA C 205 SHEET 1 AB6 2 THR C 239 LYS C 241 0 SHEET 2 AB6 2 ASP C 249 VAL C 251 -1 O ASP C 249 N LYS C 241 SHEET 1 AB7 4 LYS C 305 GLU C 314 0 SHEET 2 AB7 4 ILE C 320 GLU C 327 -1 O GLN C 325 N LYS C 307 SHEET 3 AB7 4 ASN C 366 GLU C 370 -1 O ILE C 367 N ILE C 322 SHEET 4 AB7 4 ARG C 350 LEU C 351 -1 N ARG C 350 O GLU C 370 SHEET 1 AB8 2 CYS C 333 LYS C 334 0 SHEET 2 AB8 2 ILE C 357 VAL C 358 -1 O VAL C 358 N CYS C 333 SHEET 1 AB9 3 PHE C 337 MET C 340 0 SHEET 2 AB9 3 GLY C 374 ILE C 380 -1 O ILE C 379 N GLU C 338 SHEET 3 AB9 3 LEU C 387 LYS C 393 -1 O LEU C 389 N ILE C 378 SHEET 1 AC1 5 ARG E 9 GLU E 13 0 SHEET 2 AC1 5 CYS E 30 MET E 34 1 O THR E 32 N ASP E 10 SHEET 3 AC1 5 LEU E 41 ALA E 50 -1 O PHE E 43 N VAL E 31 SHEET 4 AC1 5 LEU E 135 PRO E 143 -1 O THR E 138 N LYS E 47 SHEET 5 AC1 5 LYS E 160 VAL E 164 -1 O LYS E 160 N ILE E 141 SHEET 1 AC2 4 ARG E 9 GLU E 13 0 SHEET 2 AC2 4 CYS E 30 MET E 34 1 O THR E 32 N ASP E 10 SHEET 3 AC2 4 LEU E 41 ALA E 50 -1 O PHE E 43 N VAL E 31 SHEET 4 AC2 4 ASN E 276 LEU E 278 -1 O LEU E 278 N THR E 48 SHEET 1 AC3 4 TRP E 20 GLU E 26 0 SHEET 2 AC3 4 HIS E 282 ARG E 288 -1 O LEU E 283 N LEU E 25 SHEET 3 AC3 4 THR E 180 CYS E 185 -1 N THR E 182 O ARG E 288 SHEET 4 AC3 4 ILE E 170 GLU E 174 -1 N THR E 171 O MET E 183 SHEET 1 AC4 4 THR E 69 SER E 72 0 SHEET 2 AC4 4 GLY E 109 ILE E 129 -1 O CYS E 116 N THR E 69 SHEET 3 AC4 4 ALA E 54 LEU E 65 -1 N ALA E 54 O ILE E 129 SHEET 4 AC4 4 TRP E 220 LEU E 221 -1 O LEU E 221 N LYS E 58 SHEET 1 AC5 5 PHE E 90 ARG E 99 0 SHEET 2 AC5 5 GLY E 109 ILE E 129 -1 O ILE E 113 N SER E 95 SHEET 3 AC5 5 MET E 196 GLN E 200 -1 O LEU E 198 N LYS E 128 SHEET 4 AC5 5 ALA E 205 HIS E 209 -1 O VAL E 208 N VAL E 197 SHEET 5 AC5 5 THR E 268 GLU E 269 -1 O THR E 268 N LEU E 207 SHEET 1 AC6 2 VAL E 238 LYS E 241 0 SHEET 2 AC6 2 ASP E 249 VAL E 252 -1 O ASP E 249 N LYS E 241 SHEET 1 AC7 7 LYS E 305 GLU E 314 0 SHEET 2 AC7 7 ILE E 320 GLU E 327 -1 O VAL E 321 N ALA E 313 SHEET 3 AC7 7 VAL E 365 GLU E 370 -1 O ALA E 369 N ILE E 320 SHEET 4 AC7 7 VAL E 347 LEU E 351 -1 N ARG E 350 O GLU E 370 SHEET 5 AC7 7 PHE E 337 MET E 340 -1 N ILE E 339 O LEU E 348 SHEET 6 AC7 7 GLY E 374 ILE E 380 -1 O ILE E 379 N GLU E 338 SHEET 7 AC7 7 LEU E 387 LYS E 393 -1 O LEU E 389 N ILE E 378 SHEET 1 AC8 2 CYS E 333 LYS E 334 0 SHEET 2 AC8 2 ILE E 357 VAL E 358 -1 O VAL E 358 N CYS E 333 SHEET 1 AC9 4 GLN G 3 GLU G 6 0 SHEET 2 AC9 4 VAL G 18 SER G 25 -1 O LYS G 23 N VAL G 5 SHEET 3 AC9 4 THR G 78 LEU G 83 -1 O ALA G 79 N CYS G 22 SHEET 4 AC9 4 VAL G 68 ASP G 73 -1 N THR G 71 O TYR G 80 SHEET 1 AD1 6 GLU G 10 VAL G 11 0 SHEET 2 AD1 6 THR G 122 THR G 125 1 O THR G 125 N GLU G 10 SHEET 3 AD1 6 ALA G 92 TYR G 95 -1 N ALA G 92 O VAL G 124 SHEET 4 AD1 6 TYR G 32 GLN G 39 -1 N GLN G 39 O ILE G 93 SHEET 5 AD1 6 GLU G 46 ASN G 52 -1 O GLU G 46 N ARG G 38 SHEET 6 AD1 6 THR G 58 TYR G 60 -1 O LYS G 59 N TRP G 50 SHEET 1 AD2 5 GLU G 10 VAL G 11 0 SHEET 2 AD2 5 THR G 122 THR G 125 1 O THR G 125 N GLU G 10 SHEET 3 AD2 5 ALA G 92 TYR G 95 -1 N ALA G 92 O VAL G 124 SHEET 4 AD2 5 TYR G 32 GLN G 39 -1 N GLN G 39 O ILE G 93 SHEET 5 AD2 5 ARG G 98 LYS G 100 -1 O ASP G 99 N ALA G 33 SHEET 1 AD3 5 SER H 9 GLY H 12 0 SHEET 2 AD3 5 THR H 105 VAL H 109 1 O THR H 108 N VAL H 10 SHEET 3 AD3 5 ASP H 87 HIS H 93 -1 N TYR H 88 O THR H 105 SHEET 4 AD3 5 VAL H 35 GLN H 40 -1 N SER H 36 O SER H 91 SHEET 5 AD3 5 LYS H 47 LEU H 50 -1 O LYS H 47 N GLN H 39 SHEET 1 AD4 4 SER H 9 GLY H 12 0 SHEET 2 AD4 4 THR H 105 VAL H 109 1 O THR H 108 N VAL H 10 SHEET 3 AD4 4 ASP H 87 HIS H 93 -1 N TYR H 88 O THR H 105 SHEET 4 AD4 4 TRP H 99 PHE H 101 -1 O VAL H 100 N SER H 92 SHEET 1 AD5 3 ILE H 18 THR H 23 0 SHEET 2 AD5 3 THR H 72 ILE H 77 -1 O ALA H 73 N CYS H 22 SHEET 3 AD5 3 PHE H 64 SER H 69 -1 N SER H 69 O THR H 72 SHEET 1 AD6 4 GLN I 3 GLU I 6 0 SHEET 2 AD6 4 VAL I 20 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AD6 4 THR I 78 LEU I 83 -1 O MET I 81 N VAL I 20 SHEET 4 AD6 4 VAL I 68 ASP I 73 -1 N THR I 71 O TYR I 80 SHEET 1 AD7 6 GLU I 10 VAL I 11 0 SHEET 2 AD7 6 THR I 122 THR I 125 1 O LEU I 123 N GLU I 10 SHEET 3 AD7 6 ALA I 92 LYS I 100 -1 N TYR I 94 O THR I 122 SHEET 4 AD7 6 TYR I 32 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AD7 6 LEU I 45 ASN I 52 -1 O GLU I 46 N ARG I 38 SHEET 6 AD7 6 THR I 58 TYR I 60 -1 O LYS I 59 N TRP I 50 SHEET 1 AD8 5 SER J 9 GLY J 12 0 SHEET 2 AD8 5 THR J 105 VAL J 109 1 O LYS J 106 N VAL J 10 SHEET 3 AD8 5 ASP J 87 HIS J 93 -1 N TYR J 88 O THR J 105 SHEET 4 AD8 5 SER J 36 GLN J 40 -1 N PHE J 38 O TYR J 89 SHEET 5 AD8 5 LYS J 47 LEU J 50 -1 O MET J 49 N TRP J 37 SHEET 1 AD9 4 SER J 9 GLY J 12 0 SHEET 2 AD9 4 THR J 105 VAL J 109 1 O LYS J 106 N VAL J 10 SHEET 3 AD9 4 ASP J 87 HIS J 93 -1 N TYR J 88 O THR J 105 SHEET 4 AD9 4 TRP J 99 PHE J 101 -1 O VAL J 100 N SER J 92 SHEET 1 AE1 3 ILE J 18 THR J 23 0 SHEET 2 AE1 3 THR J 72 ILE J 77 -1 O ALA J 73 N CYS J 22 SHEET 3 AE1 3 PHE J 64 SER J 69 -1 N SER J 67 O SER J 74 SHEET 1 AE2 4 GLN K 3 GLU K 6 0 SHEET 2 AE2 4 VAL K 18 SER K 25 -1 O LYS K 23 N VAL K 5 SHEET 3 AE2 4 THR K 78 LEU K 83 -1 O MET K 81 N VAL K 20 SHEET 4 AE2 4 VAL K 68 ASP K 73 -1 N THR K 71 O TYR K 80 SHEET 1 AE3 6 GLU K 10 VAL K 11 0 SHEET 2 AE3 6 THR K 122 THR K 125 1 O LEU K 123 N GLU K 10 SHEET 3 AE3 6 ALA K 92 LYS K 100 -1 N TYR K 94 O THR K 122 SHEET 4 AE3 6 TYR K 32 GLN K 39 -1 N HIS K 35 O ALA K 97 SHEET 5 AE3 6 LEU K 45 ASN K 52 -1 O MET K 48 N TRP K 36 SHEET 6 AE3 6 THR K 58 TYR K 60 -1 O LYS K 59 N TRP K 50 SHEET 1 AE4 5 SER L 9 VAL L 10 0 SHEET 2 AE4 5 THR L 105 LEU L 107 1 O LYS L 106 N VAL L 10 SHEET 3 AE4 5 ASP L 87 HIS L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AE4 5 VAL L 35 GLN L 40 -1 N PHE L 38 O TYR L 89 SHEET 5 AE4 5 LYS L 47 LEU L 50 -1 O LYS L 47 N GLN L 39 SHEET 1 AE5 4 SER L 9 VAL L 10 0 SHEET 2 AE5 4 THR L 105 LEU L 107 1 O LYS L 106 N VAL L 10 SHEET 3 AE5 4 ASP L 87 HIS L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AE5 4 TRP L 99 PHE L 101 -1 O VAL L 100 N SER L 92 SHEET 1 AE6 3 ILE L 18 THR L 23 0 SHEET 2 AE6 3 THR L 72 ILE L 77 -1 O ALA L 73 N CYS L 22 SHEET 3 AE6 3 PHE L 64 SER L 69 -1 N SER L 67 O SER L 74 SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.02 SSBOND 2 CYS A 60 CYS A 121 1555 1555 2.03 SSBOND 3 CYS A 74 CYS A 105 1555 1555 2.03 SSBOND 4 CYS A 92 CYS A 116 1555 1555 2.03 SSBOND 5 CYS A 185 CYS A 285 1555 1555 2.03 SSBOND 6 CYS A 302 CYS A 333 1555 1555 2.03 SSBOND 7 CYS C 3 CYS C 30 1555 1555 2.03 SSBOND 8 CYS C 60 CYS C 121 1555 1555 2.04 SSBOND 9 CYS C 74 CYS C 105 1555 1555 2.03 SSBOND 10 CYS C 92 CYS C 116 1555 1555 2.03 SSBOND 11 CYS C 185 CYS C 285 1555 1555 2.03 SSBOND 12 CYS C 302 CYS C 333 1555 1555 2.03 SSBOND 13 CYS E 3 CYS E 30 1555 1555 2.03 SSBOND 14 CYS E 60 CYS E 121 1555 1555 2.03 SSBOND 15 CYS E 74 CYS E 105 1555 1555 2.04 SSBOND 16 CYS E 92 CYS E 116 1555 1555 2.03 SSBOND 17 CYS E 185 CYS E 285 1555 1555 2.03 SSBOND 18 CYS E 302 CYS E 333 1555 1555 2.03 SSBOND 19 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 20 CYS H 22 CYS H 90 1555 1555 2.03 SSBOND 21 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 22 CYS J 22 CYS J 90 1555 1555 2.03 SSBOND 23 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 24 CYS L 22 CYS L 90 1555 1555 2.03 LINK ND2 ASN A 67 C1 NAG A 501 1555 1555 1.43 LINK ND2 ASN C 67 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN E 67 C1 NAG E 501 1555 1555 1.44 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