HEADER VIRUS 07-MAR-24 9AY1 TITLE CRYO-EM STRUCTURE OF SINV/EEEV IN COMPLEX WITH A POTENTLY NEUTRALIZING TITLE 2 HUMAN ANTIBODY IGG EEEV-373 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG EEEV-373 HEAVY CHAIN; COMPND 3 CHAIN: 1; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG EEEV-373 LIGHT CHAIN; COMPND 7 CHAIN: 2; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE GLYCOPROTEIN E1; COMPND 11 CHAIN: A, B, C, D; COMPND 12 SYNONYM: E1 ENVELOPE GLYCOPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: E2 GLYCOPROTEIN; COMPND 16 CHAIN: a, b, c, d; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: EASTERN EQUINE ENCEPHALITIS VIRUS; SOURCE 17 ORGANISM_TAXID: 11021; SOURCE 18 STRAIN: FL 93-939; SOURCE 19 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 10036; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: EASTERN EQUINE ENCEPHALITIS VIRUS; SOURCE 23 ORGANISM_TAXID: 11021; SOURCE 24 STRAIN: FL 93-939; SOURCE 25 GENE: E2; SOURCE 26 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 10036 KEYWDS CRYO-EM, SINGLE PARTICLE, VIRUS NEUTRALIZATION, INTRA-VIRION KEYWDS 2 CROSSLINK, VIRUS-IMMUNE SYSTEM COMPLEX, VIRUS EXPDTA ELECTRON MICROSCOPY AUTHOR A.BANDYOPADHYAY,T.KLOSE,R.J.KUHN REVDAT 1 11-JUN-25 9AY1 0 JRNL AUTH A.BANDYOPADHYAY,T.KLOSE,R.J.KUH JRNL TITL CRYO-EM STRUCTURE OF SINV/EEEV IN COMPLEX WITH A POTENTLY JRNL TITL 2 NEUTRALIZING HUMAN ANTIBODY IGG EEEV-373 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, LEGINON, CRYOSPARC, UCSF REMARK 3 CHIMERA, PHENIX, JSPR, JSPR, JSPR, JSPR REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6MX4 REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY 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) : 4.600 REMARK 3 NUMBER OF PARTICLES : 15932 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 9AY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000281077. 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 : EEEV IN COMPLEX WITH IGG EEEV REMARK 245 -373 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3549.00 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: 1, 2, A, B, C, D, a, b, c, d, REMARK 350 AND CHAINS: E, F, G, H 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 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT2 2 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 2 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT1 3 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT2 3 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 3 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT1 4 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT2 4 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT3 4 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT1 5 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT2 5 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT3 5 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 7 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 7 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT3 7 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT1 8 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 8 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT3 8 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT1 9 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 9 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 9 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT1 10 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 10 0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 10 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT1 11 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 11 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 12 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT2 12 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT3 12 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 13 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT2 13 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT3 13 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 14 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT2 14 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 14 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 15 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT2 15 0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 15 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 16 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 16 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 16 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 17 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 17 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 17 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 18 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 18 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 18 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 19 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 19 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT3 19 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 20 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 20 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT3 20 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 21 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 21 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT3 21 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 22 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT2 22 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 22 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT1 23 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT2 23 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 23 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT1 24 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 24 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 24 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT1 25 0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 25 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 25 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT1 26 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 26 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT3 26 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 27 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 27 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 27 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 28 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 28 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 28 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 29 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT2 29 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT3 29 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 30 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT2 30 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 30 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 31 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 31 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 31 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 32 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 32 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT3 32 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT1 33 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 33 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT3 33 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT1 34 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT2 34 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT3 34 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT1 35 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT2 35 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT3 35 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT1 36 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 36 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 36 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 37 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT2 37 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT3 37 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 38 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT2 38 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT3 38 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 39 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT2 39 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT3 39 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT1 40 0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 40 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT3 40 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 41 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 41 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 41 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT1 42 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT2 42 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 42 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT1 43 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT2 43 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 43 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT1 44 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT2 44 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 44 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 45 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT2 45 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 45 0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 46 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 46 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 46 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 47 0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT2 47 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT3 47 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 48 0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT2 48 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT3 48 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 49 0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT2 49 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT3 49 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT1 50 0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT2 50 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT3 50 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT1 51 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT2 51 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 51 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 52 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 52 -0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 52 0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT1 53 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 53 0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 53 0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 54 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 54 0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT3 54 -0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT1 55 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 55 -0.500000 -0.809017 -0.309017 0.00000 REMARK 350 BIOMT3 55 -0.809017 0.309017 0.500000 0.00000 REMARK 350 BIOMT1 56 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT2 56 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 56 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT1 57 -0.309017 -0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 57 0.500000 -0.809017 0.309017 0.00000 REMARK 350 BIOMT3 57 -0.809017 -0.309017 0.500000 0.00000 REMARK 350 BIOMT1 58 -0.809017 -0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 58 -0.309017 -0.500000 0.809017 0.00000 REMARK 350 BIOMT3 58 -0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT1 59 -0.809017 0.309017 -0.500000 0.00000 REMARK 350 BIOMT2 59 -0.309017 0.500000 0.809017 0.00000 REMARK 350 BIOMT3 59 0.500000 0.809017 -0.309017 0.00000 REMARK 350 BIOMT1 60 -0.309017 0.500000 -0.809017 0.00000 REMARK 350 BIOMT2 60 0.500000 0.809017 0.309017 0.00000 REMARK 350 BIOMT3 60 0.809017 -0.309017 -0.500000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN 1 1 CB CG CD OE1 NE2 REMARK 470 VAL 1 2 CB CG1 CG2 REMARK 470 GLN 1 3 CB CG CD OE1 NE2 REMARK 470 LEU 1 4 CB CG CD1 CD2 REMARK 470 VAL 1 5 CB CG1 CG2 REMARK 470 GLU 1 6 CB CG CD OE1 OE2 REMARK 470 SER 1 7 CB OG REMARK 470 VAL 1 11 CB CG1 CG2 REMARK 470 VAL 1 12 CB CG1 CG2 REMARK 470 GLN 1 13 CB CG CD OE1 NE2 REMARK 470 PRO 1 14 CB CG CD REMARK 470 ARG 1 16 CB CG CD NE CZ NH1 NH2 REMARK 470 SER 1 17 CB OG REMARK 470 LEU 1 18 CB CG CD1 CD2 REMARK 470 ARG 1 19 CB CG CD NE CZ NH1 NH2 REMARK 470 LEU 1 20 CB CG CD1 CD2 REMARK 470 SER 1 21 CB OG REMARK 470 CYS 1 22 CB SG REMARK 470 ALA 1 23 CB REMARK 470 ALA 1 24 CB REMARK 470 SER 1 25 CB OG REMARK 470 PHE 1 27 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR 1 28 CB OG1 CG2 REMARK 470 PHE 1 29 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER 1 30 CB OG REMARK 470 SER 1 31 CB OG REMARK 470 HIS 1 32 CB CG ND1 CD2 CE1 NE2 REMARK 470 VAL 1 33 CB CG1 CG2 REMARK 470 MET 1 34 CB CG SD CE REMARK 470 TYR 1 35 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 35 OH REMARK 470 TRP 1 36 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 1 36 CZ2 CZ3 CH2 REMARK 470 VAL 1 37 CB CG1 CG2 REMARK 470 ARG 1 38 CB CG CD NE CZ NH1 NH2 REMARK 470 GLN 1 39 CB CG CD OE1 NE2 REMARK 470 ALA 1 40 CB REMARK 470 PRO 1 41 CB CG CD REMARK 470 LYS 1 43 CB CG CD CE NZ REMARK 470 LEU 1 45 CB CG CD1 CD2 REMARK 470 GLU 1 46 CB CG CD OE1 OE2 REMARK 470 TRP 1 47 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 1 47 CZ2 CZ3 CH2 REMARK 470 VAL 1 48 CB CG1 CG2 REMARK 470 ALA 1 49 CB REMARK 470 VAL 1 50 CB CG1 CG2 REMARK 470 ILE 1 51 CB CG1 CG2 CD1 REMARK 470 THR 1 52 CB OG1 CG2 REMARK 470 TYR 1 53 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 53 OH REMARK 470 ASP 1 54 CB CG OD1 OD2 REMARK 470 ASN 1 57 CB CG OD1 ND2 REMARK 470 LYS 1 58 CB CG CD CE NZ REMARK 470 TYR 1 59 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 59 OH REMARK 470 TYR 1 60 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 60 OH REMARK 470 ALA 1 61 CB REMARK 470 ASP 1 62 CB CG OD1 OD2 REMARK 470 SER 1 63 CB OG REMARK 470 VAL 1 64 CB CG1 CG2 REMARK 470 ARG 1 65 CB CG CD NE CZ NH1 NH2 REMARK 470 ARG 1 67 CB CG CD NE CZ NH1 NH2 REMARK 470 LEU 1 68 CB CG CD1 CD2 REMARK 470 THR 1 69 CB OG1 CG2 REMARK 470 ILE 1 70 CB CG1 CG2 CD1 REMARK 470 SER 1 71 CB OG REMARK 470 ARG 1 72 CB CG CD NE CZ NH1 NH2 REMARK 470 ASP 1 73 CB CG OD1 OD2 REMARK 470 ASN 1 74 CB CG OD1 ND2 REMARK 470 SER 1 75 CB OG REMARK 470 LYS 1 76 CB CG CD CE NZ REMARK 470 ASN 1 77 CB CG OD1 ND2 REMARK 470 THR 1 78 CB OG1 CG2 REMARK 470 LEU 1 79 CB CG CD1 CD2 REMARK 470 TYR 1 80 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 80 OH REMARK 470 LEU 1 81 CB CG CD1 CD2 REMARK 470 GLN 1 82 CB CG CD OE1 NE2 REMARK 470 MET 1 83 CB CG SD CE REMARK 470 ASN 1 84 CB CG OD1 ND2 REMARK 470 SER 1 85 CB OG REMARK 470 LEU 1 86 CB CG CD1 CD2 REMARK 470 ARG 1 87 CB CG CD NE CZ NH1 NH2 REMARK 470 ALA 1 88 CB REMARK 470 GLU 1 89 CB CG CD OE1 OE2 REMARK 470 ASP 1 90 CB CG OD1 OD2 REMARK 470 THR 1 91 CB OG1 CG2 REMARK 470 ALA 1 92 CB REMARK 470 VAL 1 93 CB CG1 CG2 REMARK 470 TYR 1 94 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 94 OH REMARK 470 TYR 1 95 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 95 OH REMARK 470 CYS 1 96 CB SG REMARK 470 ALA 1 97 CB REMARK 470 SER 1 98 CB OG REMARK 470 PRO 1 99 CB CG CD REMARK 470 ARG 1 100 CB CG CD NE CZ NH1 NH2 REMARK 470 ASP 1 102 CB CG OD1 OD2 REMARK 470 SER 1 103 CB OG REMARK 470 SER 1 105 CB OG REMARK 470 TYR 1 106 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 106 OH REMARK 470 TYR 1 107 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 107 OH REMARK 470 ASP 1 108 CB CG OD1 OD2 REMARK 470 ILE 1 109 CB CG1 CG2 CD1 REMARK 470 ASP 1 110 CB CG OD1 OD2 REMARK 470 TYR 1 111 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 111 OH REMARK 470 PHE 1 112 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP 1 113 CB CG OD1 OD2 REMARK 470 TYR 1 114 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 114 OH REMARK 470 TRP 1 115 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 1 115 CZ2 CZ3 CH2 REMARK 470 GLN 1 117 CB CG CD OE1 NE2 REMARK 470 THR 1 119 CB OG1 CG2 REMARK 470 LEU 1 120 CB CG CD1 CD2 REMARK 470 VAL 1 121 CB CG1 CG2 REMARK 470 THR 1 122 CB OG1 CG2 REMARK 470 VAL 1 123 CB CG1 CG2 REMARK 470 SER 1 124 CB OG REMARK 470 SER 1 125 CB OG REMARK 470 ALA 1 126 CB REMARK 470 SER 1 127 CB OG REMARK 470 THR 1 128 CB OG1 CG2 REMARK 470 LYS 1 129 CB CG CD CE NZ REMARK 470 PRO 1 131 CB CG CD REMARK 470 SER 1 132 CB OG REMARK 470 VAL 1 133 CB CG1 CG2 REMARK 470 PHE 1 134 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO 1 135 CB CG CD REMARK 470 LEU 1 136 CB CG CD1 CD2 REMARK 470 ALA 1 137 CB REMARK 470 PRO 1 138 CB CG CD REMARK 470 SER 1 139 CB OG REMARK 470 SER 1 140 CB OG REMARK 470 LYS 1 141 CB CG CD CE NZ REMARK 470 SER 1 142 CB OG REMARK 470 THR 1 143 CB OG1 CG2 REMARK 470 SER 1 144 CB OG REMARK 470 THR 1 147 CB OG1 CG2 REMARK 470 ALA 1 148 CB REMARK 470 ALA 1 149 CB REMARK 470 LEU 1 150 CB CG CD1 CD2 REMARK 470 CYS 1 152 CB SG REMARK 470 LEU 1 153 CB CG CD1 CD2 REMARK 470 VAL 1 154 CB CG1 CG2 REMARK 470 LYS 1 155 CB CG CD CE NZ REMARK 470 ASP 1 156 CB CG OD1 OD2 REMARK 470 TYR 1 157 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 157 OH REMARK 470 PHE 1 158 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO 1 159 CB CG CD REMARK 470 GLU 1 160 CB CG CD OE1 OE2 REMARK 470 PRO 1 161 CB CG CD REMARK 470 VAL 1 162 CB CG1 CG2 REMARK 470 THR 1 163 CB OG1 CG2 REMARK 470 VAL 1 164 CB CG1 CG2 REMARK 470 SER 1 165 CB OG REMARK 470 TRP 1 166 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 1 166 CZ2 CZ3 CH2 REMARK 470 ASN 1 167 CB CG OD1 ND2 REMARK 470 SER 1 168 CB OG REMARK 470 ALA 1 170 CB REMARK 470 LEU 1 171 CB CG CD1 CD2 REMARK 470 THR 1 172 CB OG1 CG2 REMARK 470 SER 1 173 CB OG REMARK 470 VAL 1 175 CB CG1 CG2 REMARK 470 HIS 1 176 CB CG ND1 CD2 CE1 NE2 REMARK 470 THR 1 177 CB OG1 CG2 REMARK 470 PHE 1 178 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO 1 179 CB CG CD REMARK 470 ALA 1 180 CB REMARK 470 VAL 1 181 CB CG1 CG2 REMARK 470 LEU 1 182 CB CG CD1 CD2 REMARK 470 GLN 1 183 CB CG CD OE1 NE2 REMARK 470 SER 1 184 CB OG REMARK 470 SER 1 185 CB OG REMARK 470 LEU 1 187 CB CG CD1 CD2 REMARK 470 TYR 1 188 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 188 OH REMARK 470 SER 1 189 CB OG REMARK 470 LEU 1 190 CB CG CD1 CD2 REMARK 470 SER 1 191 CB OG REMARK 470 SER 1 192 CB OG REMARK 470 VAL 1 193 CB CG1 CG2 REMARK 470 VAL 1 194 CB CG1 CG2 REMARK 470 THR 1 195 CB OG1 CG2 REMARK 470 VAL 1 196 CB CG1 CG2 REMARK 470 PRO 1 197 CB CG CD REMARK 470 SER 1 198 CB OG REMARK 470 SER 1 199 CB OG REMARK 470 SER 1 200 CB OG REMARK 470 LEU 1 201 CB CG CD1 CD2 REMARK 470 THR 1 203 CB OG1 CG2 REMARK 470 GLN 1 204 CB CG CD OE1 NE2 REMARK 470 THR 1 205 CB OG1 CG2 REMARK 470 TYR 1 206 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 1 206 OH REMARK 470 ILE 1 207 CB CG1 CG2 CD1 REMARK 470 CYS 1 208 CB SG REMARK 470 ASN 1 209 CB CG OD1 ND2 REMARK 470 VAL 1 210 CB CG1 CG2 REMARK 470 ASN 1 211 CB CG OD1 ND2 REMARK 470 HIS 1 212 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS 1 213 CB CG CD CE NZ REMARK 470 PRO 1 214 CB CG CD REMARK 470 SER 1 215 CB OG REMARK 470 ASN 1 216 CB CG OD1 ND2 REMARK 470 THR 1 217 CB OG1 CG2 REMARK 470 LYS 1 218 CB CG CD CE NZ REMARK 470 VAL 1 219 CB CG1 CG2 REMARK 470 ASP 1 220 CB CG OD1 OD2 REMARK 470 LYS 1 221 CB CG CD CE NZ REMARK 470 LYS 1 222 CB CG CD CE NZ REMARK 470 VAL 1 223 CB CG1 CG2 REMARK 470 GLU 1 224 CB CG CD OE1 OE2 REMARK 470 PRO 1 225 CB CG CD REMARK 470 LYS 1 226 CB CG CD CE NZ REMARK 470 SER 1 227 CB OG REMARK 470 CYS 1 228 CB SG REMARK 470 ASP 2 1 CB CG OD1 OD2 REMARK 470 ILE 2 2 CB CG1 CG2 CD1 REMARK 470 GLN 2 3 CB CG CD OE1 NE2 REMARK 470 MET 2 4 CB CG SD CE REMARK 470 THR 2 5 CB OG1 CG2 REMARK 470 GLN 2 6 CB CG CD OE1 NE2 REMARK 470 SER 2 7 CB OG REMARK 470 PRO 2 8 CB CG CD REMARK 470 SER 2 9 CB OG REMARK 470 ALA 2 10 CB REMARK 470 MET 2 11 CB CG SD CE REMARK 470 SER 2 12 CB OG REMARK 470 ALA 2 13 CB REMARK 470 SER 2 14 CB OG REMARK 470 VAL 2 15 CB CG1 CG2 REMARK 470 ASP 2 17 CB CG OD1 OD2 REMARK 470 ARG 2 18 CB CG CD NE CZ NH1 NH2 REMARK 470 VAL 2 19 CB CG1 CG2 REMARK 470 THR 2 20 CB OG1 CG2 REMARK 470 ILE 2 21 CB CG1 CG2 CD1 REMARK 470 THR 2 22 CB OG1 CG2 REMARK 470 CYS 2 23 CB SG REMARK 470 ARG 2 24 CB CG CD NE CZ NH1 NH2 REMARK 470 ALA 2 25 CB REMARK 470 SER 2 26 CB OG REMARK 470 GLN 2 27 CB CG CD OE1 NE2 REMARK 470 ILE 2 29 CB CG1 CG2 CD1 REMARK 470 SER 2 30 CB OG REMARK 470 ASN 2 31 CB CG OD1 ND2 REMARK 470 TYR 2 32 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 32 OH REMARK 470 LEU 2 33 CB CG CD1 CD2 REMARK 470 ALA 2 34 CB REMARK 470 TRP 2 35 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 2 35 CZ2 CZ3 CH2 REMARK 470 PHE 2 36 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN 2 37 CB CG CD OE1 NE2 REMARK 470 GLN 2 38 CB CG CD OE1 NE2 REMARK 470 LYS 2 39 CB CG CD CE NZ REMARK 470 PRO 2 40 CB CG CD REMARK 470 LYS 2 42 CB CG CD CE NZ REMARK 470 VAL 2 43 CB CG1 CG2 REMARK 470 PRO 2 44 CB CG CD REMARK 470 LYS 2 45 CB CG CD CE NZ REMARK 470 ARG 2 46 CB CG CD NE CZ NH1 NH2 REMARK 470 LEU 2 47 CB CG CD1 CD2 REMARK 470 ILE 2 48 CB CG1 CG2 CD1 REMARK 470 TYR 2 49 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 49 OH REMARK 470 ALA 2 50 CB REMARK 470 ALA 2 51 CB REMARK 470 SER 2 52 CB OG REMARK 470 SER 2 53 CB OG REMARK 470 LEU 2 54 CB CG CD1 CD2 REMARK 470 GLN 2 55 CB CG CD OE1 NE2 REMARK 470 SER 2 56 CB OG REMARK 470 VAL 2 58 CB CG1 CG2 REMARK 470 PRO 2 59 CB CG CD REMARK 470 SER 2 60 CB OG REMARK 470 ARG 2 61 CB CG CD NE CZ NH1 NH2 REMARK 470 PHE 2 62 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER 2 63 CB OG REMARK 470 SER 2 65 CB OG REMARK 470 SER 2 67 CB OG REMARK 470 THR 2 69 CB OG1 CG2 REMARK 470 GLU 2 70 CB CG CD OE1 OE2 REMARK 470 PHE 2 71 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR 2 72 CB OG1 CG2 REMARK 470 LEU 2 73 CB CG CD1 CD2 REMARK 470 THR 2 74 CB OG1 CG2 REMARK 470 ILE 2 75 CB CG1 CG2 CD1 REMARK 470 SER 2 76 CB OG REMARK 470 SER 2 77 CB OG REMARK 470 LEU 2 78 CB CG CD1 CD2 REMARK 470 GLN 2 79 CB CG CD OE1 NE2 REMARK 470 PRO 2 80 CB CG CD REMARK 470 GLU 2 81 CB CG CD OE1 OE2 REMARK 470 ASP 2 82 CB CG OD1 OD2 REMARK 470 PHE 2 83 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ALA 2 84 CB REMARK 470 THR 2 85 CB OG1 CG2 REMARK 470 TYR 2 86 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 86 OH REMARK 470 TYR 2 87 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 87 OH REMARK 470 CYS 2 88 CB SG REMARK 470 LEU 2 89 CB CG CD1 CD2 REMARK 470 GLN 2 90 CB CG CD OE1 NE2 REMARK 470 HIS 2 91 CB CG ND1 CD2 CE1 NE2 REMARK 470 ASN 2 92 CB CG OD1 ND2 REMARK 470 THR 2 93 CB OG1 CG2 REMARK 470 SER 2 94 CB OG REMARK 470 PRO 2 95 CB CG CD REMARK 470 SER 2 96 CB OG REMARK 470 PRO 2 97 CB CG CD REMARK 470 PHE 2 98 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN 2 100 CB CG CD OE1 NE2 REMARK 470 THR 2 102 CB OG1 CG2 REMARK 470 LYS 2 103 CB CG CD CE NZ REMARK 470 VAL 2 104 CB CG1 CG2 REMARK 470 GLU 2 105 CB CG CD OE1 OE2 REMARK 470 ILE 2 106 CB CG1 CG2 CD1 REMARK 470 LYS 2 107 CB CG CD CE NZ REMARK 470 ARG 2 108 CB CG CD NE CZ NH1 NH2 REMARK 470 THR 2 109 CB OG1 CG2 REMARK 470 VAL 2 110 CB CG1 CG2 REMARK 470 ALA 2 111 CB REMARK 470 ALA 2 112 CB REMARK 470 PRO 2 113 CB CG CD REMARK 470 SER 2 114 CB OG REMARK 470 VAL 2 115 CB CG1 CG2 REMARK 470 PHE 2 116 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE 2 117 CB CG1 CG2 CD1 REMARK 470 PHE 2 118 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO 2 119 CB CG CD REMARK 470 PRO 2 120 CB CG CD REMARK 470 SER 2 121 CB OG REMARK 470 ASP 2 122 CB CG OD1 OD2 REMARK 470 GLU 2 123 CB CG CD OE1 OE2 REMARK 470 GLN 2 124 CB CG CD OE1 NE2 REMARK 470 LEU 2 125 CB CG CD1 CD2 REMARK 470 LYS 2 126 CB CG CD CE NZ REMARK 470 SER 2 127 CB OG REMARK 470 THR 2 129 CB OG1 CG2 REMARK 470 ALA 2 130 CB REMARK 470 SER 2 131 CB OG REMARK 470 VAL 2 132 CB CG1 CG2 REMARK 470 VAL 2 133 CB CG1 CG2 REMARK 470 CYS 2 134 CB SG REMARK 470 LEU 2 135 CB CG CD1 CD2 REMARK 470 LEU 2 136 CB CG CD1 CD2 REMARK 470 ASN 2 137 CB CG OD1 ND2 REMARK 470 ASN 2 138 CB CG OD1 ND2 REMARK 470 PHE 2 139 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 140 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 140 OH REMARK 470 PRO 2 141 CB CG CD REMARK 470 ARG 2 142 CB CG CD NE CZ NH1 NH2 REMARK 470 GLU 2 143 CB CG CD OE1 OE2 REMARK 470 ALA 2 144 CB REMARK 470 LYS 2 145 CB CG CD CE NZ REMARK 470 VAL 2 146 CB CG1 CG2 REMARK 470 GLN 2 147 CB CG CD OE1 NE2 REMARK 470 TRP 2 148 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP 2 148 CZ2 CZ3 CH2 REMARK 470 LYS 2 149 CB CG CD CE NZ REMARK 470 VAL 2 150 CB CG1 CG2 REMARK 470 ASP 2 151 CB CG OD1 OD2 REMARK 470 ASN 2 152 CB CG OD1 ND2 REMARK 470 ALA 2 153 CB REMARK 470 LEU 2 154 CB CG CD1 CD2 REMARK 470 GLN 2 155 CB CG CD OE1 NE2 REMARK 470 SER 2 156 CB OG REMARK 470 ASN 2 158 CB CG OD1 ND2 REMARK 470 SER 2 159 CB OG REMARK 470 GLN 2 160 CB CG CD OE1 NE2 REMARK 470 GLU 2 161 CB CG CD OE1 OE2 REMARK 470 SER 2 162 CB OG REMARK 470 VAL 2 163 CB CG1 CG2 REMARK 470 THR 2 164 CB OG1 CG2 REMARK 470 GLU 2 165 CB CG CD OE1 OE2 REMARK 470 GLN 2 166 CB CG CD OE1 NE2 REMARK 470 ASP 2 167 CB CG OD1 OD2 REMARK 470 SER 2 168 CB OG REMARK 470 LYS 2 169 CB CG CD CE NZ REMARK 470 ASP 2 170 CB CG OD1 OD2 REMARK 470 SER 2 171 CB OG REMARK 470 THR 2 172 CB OG1 CG2 REMARK 470 TYR 2 173 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 173 OH REMARK 470 SER 2 174 CB OG REMARK 470 LEU 2 175 CB CG CD1 CD2 REMARK 470 SER 2 176 CB OG REMARK 470 SER 2 177 CB OG REMARK 470 THR 2 178 CB OG1 CG2 REMARK 470 LEU 2 179 CB CG CD1 CD2 REMARK 470 THR 2 180 CB OG1 CG2 REMARK 470 LEU 2 181 CB CG CD1 CD2 REMARK 470 SER 2 182 CB OG REMARK 470 LYS 2 183 CB CG CD CE NZ REMARK 470 ALA 2 184 CB REMARK 470 ASP 2 185 CB CG OD1 OD2 REMARK 470 TYR 2 186 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 186 OH REMARK 470 GLU 2 187 CB CG CD OE1 OE2 REMARK 470 LYS 2 188 CB CG CD CE NZ REMARK 470 HIS 2 189 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS 2 190 CB CG CD CE NZ REMARK 470 LEU 2 191 CB CG CD1 CD2 REMARK 470 TYR 2 192 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR 2 192 OH REMARK 470 ALA 2 193 CB REMARK 470 CYS 2 194 CB SG REMARK 470 GLU 2 195 CB CG CD OE1 OE2 REMARK 470 VAL 2 196 CB CG1 CG2 REMARK 470 THR 2 197 CB OG1 CG2 REMARK 470 HIS 2 198 CB CG ND1 CD2 CE1 NE2 REMARK 470 GLN 2 199 CB CG CD OE1 NE2 REMARK 470 LEU 2 201 CB CG CD1 CD2 REMARK 470 SER 2 202 CB OG REMARK 470 SER 2 203 CB OG REMARK 470 PRO 2 204 CB CG CD REMARK 470 VAL 2 205 CB CG1 CG2 REMARK 470 THR 2 206 CB OG1 CG2 REMARK 470 LYS 2 207 CB CG CD CE NZ REMARK 470 SER 2 208 CB OG REMARK 470 PHE 2 209 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN 2 210 CB CG OD1 ND2 REMARK 470 ARG 2 211 CB CG CD NE CZ NH1 NH2 REMARK 470 GLU 2 213 CB CG CD OE1 OE2 REMARK 470 CYS 2 214 CB SG 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 OH TYR B 76 OE1 GLU B 105 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET a 65 CA - CB - CG ANGL. DEV. = 10.9 DEGREES REMARK 500 LEU c 291 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO 1 99 -178.57 -68.63 REMARK 500 PHE 1 112 76.79 69.43 REMARK 500 SER 2 30 -100.97 51.44 REMARK 500 ALA 2 51 2.90 59.53 REMARK 500 SER 2 52 -14.65 -160.46 REMARK 500 ASN 2 152 -1.89 67.36 REMARK 500 TYR A 15 57.46 -102.53 REMARK 500 GLN A 30 78.04 -151.56 REMARK 500 ILE A 39 76.98 39.28 REMARK 500 GLU A 45 -60.29 -92.09 REMARK 500 TRP A 89 -106.62 51.82 REMARK 500 SER A 144 26.41 -146.15 REMARK 500 GLU A 192 176.06 179.68 REMARK 500 ALA A 227 17.25 57.09 REMARK 500 TRP A 244 -9.26 71.23 REMARK 500 LEU A 267 104.18 60.30 REMARK 500 THR A 305 -149.95 -95.76 REMARK 500 TYR A 309 43.52 -101.45 REMARK 500 LYS A 322 52.23 -113.26 REMARK 500 ALA A 360 13.94 -143.17 REMARK 500 CYS A 371 109.64 -52.62 REMARK 500 CYS A 377 47.90 -88.45 REMARK 500 ALA A 393 15.48 -142.19 REMARK 500 GLN A 394 -30.04 -139.06 REMARK 500 HIS A 395 68.16 27.11 REMARK 500 GLN B 30 117.23 -163.02 REMARK 500 SER B 141 19.43 57.99 REMARK 500 GLU B 192 173.01 178.69 REMARK 500 TRP B 244 -9.23 71.84 REMARK 500 ASP B 247 29.54 -141.07 REMARK 500 PRO B 266 3.77 -56.30 REMARK 500 LEU B 267 37.16 75.80 REMARK 500 SER B 292 2.31 -68.19 REMARK 500 GLU B 306 116.41 -161.35 REMARK 500 CYS B 371 64.32 38.91 REMARK 500 ILE C 39 71.17 53.19 REMARK 500 TYR C 85 70.62 -155.26 REMARK 500 MET C 88 82.70 -152.91 REMARK 500 TRP C 89 -28.70 47.42 REMARK 500 HIS C 183 -1.89 -141.00 REMARK 500 TRP C 244 -11.22 71.67 REMARK 500 PRO C 266 3.23 -55.97 REMARK 500 LEU C 267 37.80 75.45 REMARK 500 ASP C 299 23.91 49.28 REMARK 500 THR C 372 42.65 71.22 REMARK 500 HIS C 387 -79.73 -59.44 REMARK 500 VAL C 389 -114.02 -141.10 REMARK 500 HIS C 395 60.13 32.36 REMARK 500 THR C 396 27.21 -146.49 REMARK 500 ILE D 39 70.37 54.77 REMARK 500 REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS. 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 D 21 0.25 SIDE CHAIN REMARK 500 ARG a 242 0.10 SIDE CHAIN REMARK 500 ARG a 334 0.08 SIDE CHAIN REMARK 500 ARG c 37 0.15 SIDE CHAIN REMARK 500 ARG c 224 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG E 1 REMARK 610 NAG F 1 REMARK 610 NAG G 1 REMARK 610 NAG H 1 REMARK 610 BMA D 501 REMARK 610 NAG a 401 REMARK 610 NAG b 401 REMARK 610 NAG c 401 REMARK 610 NAG d 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43980 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SINV/EEEV IN COMPLEX WITH A POTENTLY REMARK 900 NEUTRALIZING HUMAN ANTIBODY IGG EEEV-373 DBREF 9AY1 1 1 228 PDB 9AY1 9AY1 1 228 DBREF 9AY1 2 1 214 PDB 9AY1 9AY1 1 214 DBREF 9AY1 A 1 400 UNP Q4QXJ7 POLS_EEEVF 802 1201 DBREF 9AY1 B 1 400 UNP Q4QXJ7 POLS_EEEVF 802 1201 DBREF 9AY1 C 1 400 UNP Q4QXJ7 POLS_EEEVF 802 1201 DBREF 9AY1 D 1 400 UNP Q4QXJ7 POLS_EEEVF 802 1201 DBREF 9AY1 a 1 338 UNP A9XR09 A9XR09_EEEV 1 338 DBREF 9AY1 b 1 338 UNP A9XR09 A9XR09_EEEV 1 338 DBREF 9AY1 c 1 338 UNP A9XR09 A9XR09_EEEV 1 338 DBREF 9AY1 d 1 338 UNP A9XR09 A9XR09_EEEV 1 338 SEQRES 1 1 228 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 1 228 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 1 228 PHE THR PHE SER SER HIS VAL MET TYR TRP VAL ARG GLN SEQRES 4 1 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE THR SEQRES 5 1 228 TYR ASP GLY GLY ASN LYS TYR TYR ALA ASP SER VAL ARG SEQRES 6 1 228 GLY ARG LEU THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 1 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 1 228 ALA VAL TYR TYR CYS ALA SER PRO ARG GLY ASP SER GLY SEQRES 9 1 228 SER TYR TYR ASP ILE ASP TYR PHE ASP TYR TRP GLY GLN SEQRES 10 1 228 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 1 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 1 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 1 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 1 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 1 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 1 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 1 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 1 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 2 214 ASP ILE GLN MET THR GLN SER PRO SER ALA MET SER ALA SEQRES 2 2 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 2 214 GLN GLY ILE SER ASN TYR LEU ALA TRP PHE GLN GLN LYS SEQRES 4 2 214 PRO GLY LYS VAL PRO LYS ARG LEU ILE TYR ALA ALA SER SEQRES 5 2 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 2 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 2 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLN HIS SEQRES 8 2 214 ASN THR SER PRO SER PRO PHE GLY GLN GLY THR LYS VAL SEQRES 9 2 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 2 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 2 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 2 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 2 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 2 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 2 214 LYS ALA ASP TYR GLU LYS HIS LYS LEU TYR ALA CYS GLU SEQRES 16 2 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 2 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 400 TYR GLU HIS THR ALA VAL MET PRO ASN LYS VAL GLY ILE SEQRES 2 A 400 PRO TYR LYS ALA LEU VAL GLU ARG PRO GLY TYR ALA PRO SEQRES 3 A 400 VAL HIS LEU GLN ILE GLN LEU VAL ASN THR ARG ILE ILE SEQRES 4 A 400 PRO SER THR ASN LEU GLU TYR ILE THR CYS LYS TYR LYS SEQRES 5 A 400 THR LYS VAL PRO SER PRO VAL VAL LYS CYS CYS GLY ALA SEQRES 6 A 400 THR GLN CYS THR SER LYS PRO HIS PRO ASP TYR GLN CYS SEQRES 7 A 400 GLN VAL PHE THR GLY VAL TYR PRO PHE MET TRP GLY GLY SEQRES 8 A 400 ALA TYR CYS PHE CYS ASP THR GLU ASN THR GLN MET SER SEQRES 9 A 400 GLU ALA TYR VAL GLU ARG SER GLU GLU CYS SER ILE ASP SEQRES 10 A 400 HIS ALA LYS ALA TYR LYS VAL HIS THR GLY THR VAL GLN SEQRES 11 A 400 ALA MET VAL ASN ILE THR TYR GLY SER VAL SER TRP ARG SEQRES 12 A 400 SER ALA ASP VAL TYR VAL ASN GLY GLU THR PRO ALA LYS SEQRES 13 A 400 ILE GLY ASP ALA LYS LEU ILE ILE GLY PRO LEU SER SER SEQRES 14 A 400 ALA TRP SER PRO PHE ASP ASN LYS VAL VAL VAL TYR GLY SEQRES 15 A 400 HIS GLU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY THR SEQRES 16 A 400 GLY LYS ALA GLY SER PHE GLY ASP LEU GLN SER ARG THR SEQRES 17 A 400 SER THR SER ASN ASP LEU TYR ALA ASN THR ASN LEU LYS SEQRES 18 A 400 LEU GLN ARG PRO GLN ALA GLY ILE VAL HIS THR PRO PHE SEQRES 19 A 400 THR GLN ALA PRO SER GLY PHE GLU ARG TRP LYS ARG ASP SEQRES 20 A 400 LYS GLY ALA PRO LEU ASN ASP VAL ALA PRO PHE GLY CYS SEQRES 21 A 400 SER ILE ALA LEU GLU PRO LEU ARG ALA GLU ASN CYS ALA SEQRES 22 A 400 VAL GLY SER ILE PRO ILE SER ILE ASP ILE PRO ASP ALA SEQRES 23 A 400 ALA PHE THR ARG ILE SER GLU THR PRO THR VAL SER ASP SEQRES 24 A 400 LEU GLU CYS LYS ILE THR GLU CYS THR TYR ALA SER ASP SEQRES 25 A 400 PHE GLY GLY ILE ALA THR VAL ALA TYR LYS SER SER LYS SEQRES 26 A 400 ALA GLY ASN CYS PRO ILE HIS SER PRO SER GLY VAL ALA SEQRES 27 A 400 VAL ILE LYS GLU ASN ASP VAL THR LEU ALA GLU SER GLY SEQRES 28 A 400 SER PHE THR PHE HIS PHE SER THR ALA ASN ILE HIS PRO SEQRES 29 A 400 ALA PHE LYS LEU GLN VAL CYS THR SER ALA VAL THR CYS SEQRES 30 A 400 LYS GLY ASP CYS LYS PRO PRO LYS ASP HIS ILE VAL ASP SEQRES 31 A 400 TYR PRO ALA GLN HIS THR GLU SER PHE THR SEQRES 1 B 400 TYR GLU HIS THR ALA VAL MET PRO ASN LYS VAL GLY ILE SEQRES 2 B 400 PRO TYR LYS ALA LEU VAL GLU ARG PRO GLY TYR ALA PRO SEQRES 3 B 400 VAL HIS LEU GLN ILE GLN LEU VAL ASN THR ARG ILE ILE SEQRES 4 B 400 PRO SER THR ASN LEU GLU TYR ILE THR CYS LYS TYR LYS SEQRES 5 B 400 THR LYS VAL PRO SER PRO VAL VAL LYS CYS CYS GLY ALA SEQRES 6 B 400 THR GLN CYS THR SER LYS PRO HIS PRO ASP TYR GLN CYS SEQRES 7 B 400 GLN VAL PHE THR GLY VAL TYR PRO PHE MET TRP GLY GLY SEQRES 8 B 400 ALA TYR CYS PHE CYS ASP THR GLU ASN THR GLN MET SER SEQRES 9 B 400 GLU ALA TYR VAL GLU ARG SER GLU GLU CYS SER ILE ASP SEQRES 10 B 400 HIS ALA LYS ALA TYR LYS VAL HIS THR GLY THR VAL GLN SEQRES 11 B 400 ALA MET VAL ASN ILE THR TYR GLY SER VAL SER TRP ARG SEQRES 12 B 400 SER ALA ASP VAL TYR VAL ASN GLY GLU THR PRO ALA LYS SEQRES 13 B 400 ILE GLY ASP ALA LYS LEU ILE ILE GLY PRO LEU SER SER SEQRES 14 B 400 ALA TRP SER PRO PHE ASP ASN LYS VAL VAL VAL TYR GLY SEQRES 15 B 400 HIS GLU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY THR SEQRES 16 B 400 GLY LYS ALA GLY SER PHE GLY ASP LEU GLN SER ARG THR SEQRES 17 B 400 SER THR SER ASN ASP LEU TYR ALA ASN THR ASN LEU LYS SEQRES 18 B 400 LEU GLN ARG PRO GLN ALA GLY ILE VAL HIS THR PRO PHE SEQRES 19 B 400 THR GLN ALA PRO SER GLY PHE GLU ARG TRP LYS ARG ASP SEQRES 20 B 400 LYS GLY ALA PRO LEU ASN ASP VAL ALA PRO PHE GLY CYS SEQRES 21 B 400 SER ILE ALA LEU GLU PRO LEU ARG ALA GLU ASN CYS ALA SEQRES 22 B 400 VAL GLY SER ILE PRO ILE SER ILE ASP ILE PRO ASP ALA SEQRES 23 B 400 ALA PHE THR ARG ILE SER GLU THR PRO THR VAL SER ASP SEQRES 24 B 400 LEU GLU CYS LYS ILE THR GLU CYS THR TYR ALA SER ASP SEQRES 25 B 400 PHE GLY GLY ILE ALA THR VAL ALA TYR LYS SER SER LYS SEQRES 26 B 400 ALA GLY ASN CYS PRO ILE HIS SER PRO SER GLY VAL ALA SEQRES 27 B 400 VAL ILE LYS GLU ASN ASP VAL THR LEU ALA GLU SER GLY SEQRES 28 B 400 SER PHE THR PHE HIS PHE SER THR ALA ASN ILE HIS PRO SEQRES 29 B 400 ALA PHE LYS LEU GLN VAL CYS THR SER ALA VAL THR CYS SEQRES 30 B 400 LYS GLY ASP CYS LYS PRO PRO LYS ASP HIS ILE VAL ASP SEQRES 31 B 400 TYR PRO ALA GLN HIS THR GLU SER PHE THR SEQRES 1 C 400 TYR GLU HIS THR ALA VAL MET PRO ASN LYS VAL GLY ILE SEQRES 2 C 400 PRO TYR LYS ALA LEU VAL GLU ARG PRO GLY TYR ALA PRO SEQRES 3 C 400 VAL HIS LEU GLN ILE GLN LEU VAL ASN THR ARG ILE ILE SEQRES 4 C 400 PRO SER THR ASN LEU GLU TYR ILE THR CYS LYS TYR LYS SEQRES 5 C 400 THR LYS VAL PRO SER PRO VAL VAL LYS CYS CYS GLY ALA SEQRES 6 C 400 THR GLN CYS THR SER LYS PRO HIS PRO ASP TYR GLN CYS SEQRES 7 C 400 GLN VAL PHE THR GLY VAL TYR PRO PHE MET TRP GLY GLY SEQRES 8 C 400 ALA TYR CYS PHE CYS ASP THR GLU ASN THR GLN MET SER SEQRES 9 C 400 GLU ALA TYR VAL GLU ARG SER GLU GLU CYS SER ILE ASP SEQRES 10 C 400 HIS ALA LYS ALA TYR LYS VAL HIS THR GLY THR VAL GLN SEQRES 11 C 400 ALA MET VAL ASN ILE THR TYR GLY SER VAL SER TRP ARG SEQRES 12 C 400 SER ALA ASP VAL TYR VAL ASN GLY GLU THR PRO ALA LYS SEQRES 13 C 400 ILE GLY ASP ALA LYS LEU ILE ILE GLY PRO LEU SER SER SEQRES 14 C 400 ALA TRP SER PRO PHE ASP ASN LYS VAL VAL VAL TYR GLY SEQRES 15 C 400 HIS GLU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY THR SEQRES 16 C 400 GLY LYS ALA GLY SER PHE GLY ASP LEU GLN SER ARG THR SEQRES 17 C 400 SER THR SER ASN ASP LEU TYR ALA ASN THR ASN LEU LYS SEQRES 18 C 400 LEU GLN ARG PRO GLN ALA GLY ILE VAL HIS THR PRO PHE SEQRES 19 C 400 THR GLN ALA PRO SER GLY PHE GLU ARG TRP LYS ARG ASP SEQRES 20 C 400 LYS GLY ALA PRO LEU ASN ASP VAL ALA PRO PHE GLY CYS SEQRES 21 C 400 SER ILE ALA LEU GLU PRO LEU ARG ALA GLU ASN CYS ALA SEQRES 22 C 400 VAL GLY SER ILE PRO ILE SER ILE ASP ILE PRO ASP ALA SEQRES 23 C 400 ALA PHE THR ARG ILE SER GLU THR PRO THR VAL SER ASP SEQRES 24 C 400 LEU GLU CYS LYS ILE THR GLU CYS THR TYR ALA SER ASP SEQRES 25 C 400 PHE GLY GLY ILE ALA THR VAL ALA TYR LYS SER SER LYS SEQRES 26 C 400 ALA GLY ASN CYS PRO ILE HIS SER PRO SER GLY VAL ALA SEQRES 27 C 400 VAL ILE LYS GLU ASN ASP VAL THR LEU ALA GLU SER GLY SEQRES 28 C 400 SER PHE THR PHE HIS PHE SER THR ALA ASN ILE HIS PRO SEQRES 29 C 400 ALA PHE LYS LEU GLN VAL CYS THR SER ALA VAL THR CYS SEQRES 30 C 400 LYS GLY ASP CYS LYS PRO PRO LYS ASP HIS ILE VAL ASP SEQRES 31 C 400 TYR PRO ALA GLN HIS THR GLU SER PHE THR SEQRES 1 D 400 TYR GLU HIS THR ALA VAL MET PRO ASN LYS VAL GLY ILE SEQRES 2 D 400 PRO TYR LYS ALA LEU VAL GLU ARG PRO GLY TYR ALA PRO SEQRES 3 D 400 VAL HIS LEU GLN ILE GLN LEU VAL ASN THR ARG ILE ILE SEQRES 4 D 400 PRO SER THR ASN LEU GLU TYR ILE THR CYS LYS TYR LYS SEQRES 5 D 400 THR LYS VAL PRO SER PRO VAL VAL LYS CYS CYS GLY ALA SEQRES 6 D 400 THR GLN CYS THR SER LYS PRO HIS PRO ASP TYR GLN CYS SEQRES 7 D 400 GLN VAL PHE THR GLY VAL TYR PRO PHE MET TRP GLY GLY SEQRES 8 D 400 ALA TYR CYS PHE CYS ASP THR GLU ASN THR GLN MET SER SEQRES 9 D 400 GLU ALA TYR VAL GLU ARG SER GLU GLU CYS SER ILE ASP SEQRES 10 D 400 HIS ALA LYS ALA TYR LYS VAL HIS THR GLY THR VAL GLN SEQRES 11 D 400 ALA MET VAL ASN ILE THR TYR GLY SER VAL SER TRP ARG SEQRES 12 D 400 SER ALA ASP VAL TYR VAL ASN GLY GLU THR PRO ALA LYS SEQRES 13 D 400 ILE GLY ASP ALA LYS LEU ILE ILE GLY PRO LEU SER SER SEQRES 14 D 400 ALA TRP SER PRO PHE ASP ASN LYS VAL VAL VAL TYR GLY SEQRES 15 D 400 HIS GLU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY THR SEQRES 16 D 400 GLY LYS ALA GLY SER PHE GLY ASP LEU GLN SER ARG THR SEQRES 17 D 400 SER THR SER ASN ASP LEU TYR ALA ASN THR ASN LEU LYS SEQRES 18 D 400 LEU GLN ARG PRO GLN ALA GLY ILE VAL HIS THR PRO PHE SEQRES 19 D 400 THR GLN ALA PRO SER GLY PHE GLU ARG TRP LYS ARG ASP SEQRES 20 D 400 LYS GLY ALA PRO LEU ASN ASP VAL ALA PRO PHE GLY CYS SEQRES 21 D 400 SER ILE ALA LEU GLU PRO LEU ARG ALA GLU ASN CYS ALA SEQRES 22 D 400 VAL GLY SER ILE PRO ILE SER ILE ASP ILE PRO ASP ALA SEQRES 23 D 400 ALA PHE THR ARG ILE SER GLU THR PRO THR VAL SER ASP SEQRES 24 D 400 LEU GLU CYS LYS ILE THR GLU CYS THR TYR ALA SER ASP SEQRES 25 D 400 PHE GLY GLY ILE ALA THR VAL ALA TYR LYS SER SER LYS SEQRES 26 D 400 ALA GLY ASN CYS PRO ILE HIS SER PRO SER GLY VAL ALA SEQRES 27 D 400 VAL ILE LYS GLU ASN ASP VAL THR LEU ALA GLU SER GLY SEQRES 28 D 400 SER PHE THR PHE HIS PHE SER THR ALA ASN ILE HIS PRO SEQRES 29 D 400 ALA PHE LYS LEU GLN VAL CYS THR SER ALA VAL THR CYS SEQRES 30 D 400 LYS GLY ASP CYS LYS PRO PRO LYS ASP HIS ILE VAL ASP SEQRES 31 D 400 TYR PRO ALA GLN HIS THR GLU SER PHE THR SEQRES 1 a 338 ASP LEU ASP THR HIS PHE THR GLN TYR LYS LEU ALA ARG SEQRES 2 a 338 PRO TYR ILE ALA ASP CYS PRO ASN CYS GLY HIS SER ARG SEQRES 3 a 338 CYS ASP SER PRO ILE ALA ILE GLU GLU VAL ARG GLY ASP SEQRES 4 a 338 ALA HIS ALA GLY VAL ILE ARG ILE GLN THR SER ALA MET SEQRES 5 a 338 PHE GLY LEU LYS THR ASP GLY VAL ASP LEU ALA TYR MET SEQRES 6 a 338 SER PHE MET ASN GLY LYS THR GLN LYS SER ILE LYS ILE SEQRES 7 a 338 ASP ASN LEU HIS VAL ARG THR SER ALA PRO CYS SER LEU SEQRES 8 a 338 VAL SER HIS HIS GLY TYR TYR ILE LEU ALA GLN CYS PRO SEQRES 9 a 338 PRO GLY ASP THR VAL THR VAL GLY PHE HIS ASP GLY PRO SEQRES 10 a 338 ASN ARG HIS THR CYS THR VAL ALA HIS LYS VAL GLU PHE SEQRES 11 a 338 ARG PRO VAL GLY ARG GLU LYS TYR ARG HIS PRO PRO GLU SEQRES 12 a 338 HIS GLY VAL GLU LEU PRO CYS ASN ARG TYR THR HIS LYS SEQRES 13 a 338 ARG ALA ASP GLN GLY HIS TYR VAL GLU MET HIS GLN PRO SEQRES 14 a 338 GLY LEU VAL ALA ASP HIS SER LEU LEU SER ILE HIS SER SEQRES 15 a 338 ALA LYS VAL LYS ILE THR VAL PRO SER GLY ALA GLN VAL SEQRES 16 a 338 LYS TYR TYR CYS LYS CYS PRO ASP VAL ARG GLU GLY ILE SEQRES 17 a 338 THR SER SER ASP HIS THR THR THR CYS THR ASP VAL LYS SEQRES 18 a 338 GLN CYS ARG ALA TYR LEU ILE ASP ASN LYS LYS TRP VAL SEQRES 19 a 338 TYR ASN SER GLY ARG LEU PRO ARG GLY GLU GLY ASP THR SEQRES 20 a 338 PHE LYS GLY LYS LEU HIS VAL PRO PHE VAL PRO VAL LYS SEQRES 21 a 338 ALA LYS CYS ILE ALA THR LEU ALA PRO GLU PRO LEU VAL SEQRES 22 a 338 GLU HIS LYS HIS ARG THR LEU ILE LEU HIS LEU HIS PRO SEQRES 23 a 338 ASP HIS PRO THR LEU LEU THR THR ARG SER LEU GLY SER SEQRES 24 a 338 ASP ALA ASN PRO THR ARG GLN TRP ILE GLU ARG PRO THR SEQRES 25 a 338 THR VAL ASN PHE THR VAL THR GLY GLU GLY LEU GLU TYR SEQRES 26 a 338 THR TRP GLY ASN HIS PRO PRO LYS ARG VAL TRP ALA GLN SEQRES 1 b 338 ASP LEU ASP THR HIS PHE THR GLN TYR LYS LEU ALA ARG SEQRES 2 b 338 PRO TYR ILE ALA ASP CYS PRO ASN CYS GLY HIS SER ARG SEQRES 3 b 338 CYS ASP SER PRO ILE ALA ILE GLU GLU VAL ARG GLY ASP SEQRES 4 b 338 ALA HIS ALA GLY VAL ILE ARG ILE GLN THR SER ALA MET SEQRES 5 b 338 PHE GLY LEU LYS THR ASP GLY VAL ASP LEU ALA TYR MET SEQRES 6 b 338 SER PHE MET ASN GLY LYS THR GLN LYS SER ILE LYS ILE SEQRES 7 b 338 ASP ASN LEU HIS VAL ARG THR SER ALA PRO CYS SER LEU SEQRES 8 b 338 VAL SER HIS HIS GLY TYR TYR ILE LEU ALA GLN CYS PRO SEQRES 9 b 338 PRO GLY ASP THR VAL THR VAL GLY PHE HIS ASP GLY PRO SEQRES 10 b 338 ASN ARG HIS THR CYS THR VAL ALA HIS LYS VAL GLU PHE SEQRES 11 b 338 ARG PRO VAL GLY ARG GLU LYS TYR ARG HIS PRO PRO GLU SEQRES 12 b 338 HIS GLY VAL GLU LEU PRO CYS ASN ARG TYR THR HIS LYS SEQRES 13 b 338 ARG ALA ASP GLN GLY HIS TYR VAL GLU MET HIS GLN PRO SEQRES 14 b 338 GLY LEU VAL ALA ASP HIS SER LEU LEU SER ILE HIS SER SEQRES 15 b 338 ALA LYS VAL LYS ILE THR VAL PRO SER GLY ALA GLN VAL SEQRES 16 b 338 LYS TYR TYR CYS LYS CYS PRO ASP VAL ARG GLU GLY ILE SEQRES 17 b 338 THR SER SER ASP HIS THR THR THR CYS THR ASP VAL LYS SEQRES 18 b 338 GLN CYS ARG ALA TYR LEU ILE ASP ASN LYS LYS TRP VAL SEQRES 19 b 338 TYR ASN SER GLY ARG LEU PRO ARG GLY GLU GLY ASP THR SEQRES 20 b 338 PHE LYS GLY LYS LEU HIS VAL PRO PHE VAL PRO VAL LYS SEQRES 21 b 338 ALA LYS CYS ILE ALA THR LEU ALA PRO GLU PRO LEU VAL SEQRES 22 b 338 GLU HIS LYS HIS ARG THR LEU ILE LEU HIS LEU HIS PRO SEQRES 23 b 338 ASP HIS PRO THR LEU LEU THR THR ARG SER LEU GLY SER SEQRES 24 b 338 ASP ALA ASN PRO THR ARG GLN TRP ILE GLU ARG PRO THR SEQRES 25 b 338 THR VAL ASN PHE THR VAL THR GLY GLU GLY LEU GLU TYR SEQRES 26 b 338 THR TRP GLY ASN HIS PRO PRO LYS ARG VAL TRP ALA GLN SEQRES 1 c 338 ASP LEU ASP THR HIS PHE THR GLN TYR LYS LEU ALA ARG SEQRES 2 c 338 PRO TYR ILE ALA ASP CYS PRO ASN CYS GLY HIS SER ARG SEQRES 3 c 338 CYS ASP SER PRO ILE ALA ILE GLU GLU VAL ARG GLY ASP SEQRES 4 c 338 ALA HIS ALA GLY VAL ILE ARG ILE GLN THR SER ALA MET SEQRES 5 c 338 PHE GLY LEU LYS THR ASP GLY VAL ASP LEU ALA TYR MET SEQRES 6 c 338 SER PHE MET ASN GLY LYS THR GLN LYS SER ILE LYS ILE SEQRES 7 c 338 ASP ASN LEU HIS VAL ARG THR SER ALA PRO CYS SER LEU SEQRES 8 c 338 VAL SER HIS HIS GLY TYR TYR ILE LEU ALA GLN CYS PRO SEQRES 9 c 338 PRO GLY ASP THR VAL THR VAL GLY PHE HIS ASP GLY PRO SEQRES 10 c 338 ASN ARG HIS THR CYS THR VAL ALA HIS LYS VAL GLU PHE SEQRES 11 c 338 ARG PRO VAL GLY ARG GLU LYS TYR ARG HIS PRO PRO GLU SEQRES 12 c 338 HIS GLY VAL GLU LEU PRO CYS ASN ARG TYR THR HIS LYS SEQRES 13 c 338 ARG ALA ASP GLN GLY HIS TYR VAL GLU MET HIS GLN PRO SEQRES 14 c 338 GLY LEU VAL ALA ASP HIS SER LEU LEU SER ILE HIS SER SEQRES 15 c 338 ALA LYS VAL LYS ILE THR VAL PRO SER GLY ALA GLN VAL SEQRES 16 c 338 LYS TYR TYR CYS LYS CYS PRO ASP VAL ARG GLU GLY ILE SEQRES 17 c 338 THR SER SER ASP HIS THR THR THR CYS THR ASP VAL LYS SEQRES 18 c 338 GLN CYS ARG ALA TYR LEU ILE ASP ASN LYS LYS TRP VAL SEQRES 19 c 338 TYR ASN SER GLY ARG LEU PRO ARG GLY GLU GLY ASP THR SEQRES 20 c 338 PHE LYS GLY LYS LEU HIS VAL PRO PHE VAL PRO VAL LYS SEQRES 21 c 338 ALA LYS CYS ILE ALA THR LEU ALA PRO GLU PRO LEU VAL SEQRES 22 c 338 GLU HIS LYS HIS ARG THR LEU ILE LEU HIS LEU HIS PRO SEQRES 23 c 338 ASP HIS PRO THR LEU LEU THR THR ARG SER LEU GLY SER SEQRES 24 c 338 ASP ALA ASN PRO THR ARG GLN TRP ILE GLU ARG PRO THR SEQRES 25 c 338 THR VAL ASN PHE THR VAL THR GLY GLU GLY LEU GLU TYR SEQRES 26 c 338 THR TRP GLY ASN HIS PRO PRO LYS ARG VAL TRP ALA GLN SEQRES 1 d 338 ASP LEU ASP THR HIS PHE THR GLN TYR LYS LEU ALA ARG SEQRES 2 d 338 PRO TYR ILE ALA ASP CYS PRO ASN CYS GLY HIS SER ARG SEQRES 3 d 338 CYS ASP SER PRO ILE ALA ILE GLU GLU VAL ARG GLY ASP SEQRES 4 d 338 ALA HIS ALA GLY VAL ILE ARG ILE GLN THR SER ALA MET SEQRES 5 d 338 PHE GLY LEU LYS THR ASP GLY VAL ASP LEU ALA TYR MET SEQRES 6 d 338 SER PHE MET ASN GLY LYS THR GLN LYS SER ILE LYS ILE SEQRES 7 d 338 ASP ASN LEU HIS VAL ARG THR SER ALA PRO CYS SER LEU SEQRES 8 d 338 VAL SER HIS HIS GLY TYR TYR ILE LEU ALA GLN CYS PRO SEQRES 9 d 338 PRO GLY ASP THR VAL THR VAL GLY PHE HIS ASP GLY PRO SEQRES 10 d 338 ASN ARG HIS THR CYS THR VAL ALA HIS LYS VAL GLU PHE SEQRES 11 d 338 ARG PRO VAL GLY ARG GLU LYS TYR ARG HIS PRO PRO GLU SEQRES 12 d 338 HIS GLY VAL GLU LEU PRO CYS ASN ARG TYR THR HIS LYS SEQRES 13 d 338 ARG ALA ASP GLN GLY HIS TYR VAL GLU MET HIS GLN PRO SEQRES 14 d 338 GLY LEU VAL ALA ASP HIS SER LEU LEU SER ILE HIS SER SEQRES 15 d 338 ALA LYS VAL LYS ILE THR VAL PRO SER GLY ALA GLN VAL SEQRES 16 d 338 LYS TYR TYR CYS LYS CYS PRO ASP VAL ARG GLU GLY ILE SEQRES 17 d 338 THR SER SER ASP HIS THR THR THR CYS THR ASP VAL LYS SEQRES 18 d 338 GLN CYS ARG ALA TYR LEU ILE ASP ASN LYS LYS TRP VAL SEQRES 19 d 338 TYR ASN SER GLY ARG LEU PRO ARG GLY GLU GLY ASP THR SEQRES 20 d 338 PHE LYS GLY LYS LEU HIS VAL PRO PHE VAL PRO VAL LYS SEQRES 21 d 338 ALA LYS CYS ILE ALA THR LEU ALA PRO GLU PRO LEU VAL SEQRES 22 d 338 GLU HIS LYS HIS ARG THR LEU ILE LEU HIS LEU HIS PRO SEQRES 23 d 338 ASP HIS PRO THR LEU LEU THR THR ARG SER LEU GLY SER SEQRES 24 d 338 ASP ALA ASN PRO THR ARG GLN TRP ILE GLU ARG PRO THR SEQRES 25 d 338 THR VAL ASN PHE THR VAL THR GLY GLU GLY LEU GLU TYR SEQRES 26 d 338 THR TRP GLY ASN HIS PRO PRO LYS ARG VAL TRP ALA GLN HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG H 1 14 HET NAG H 2 14 HET BMA D 501 11 HET NAG a 401 14 HET NAG b 401 14 HET NAG c 401 14 HET NAG d 401 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 11 NAG 12(C8 H15 N O6) FORMUL 11 BMA 4(C6 H12 O6) HELIX 1 AA1 THR 1 28 HIS 1 32 5 5 HELIX 2 AA2 ASN 1 74 LYS 1 76 5 3 HELIX 3 AA3 ARG 1 87 THR 1 91 5 5 HELIX 4 AA4 SER 1 139 LYS 1 141 5 3 HELIX 5 AA5 SER 1 168 ALA 1 170 5 3 HELIX 6 AA6 SER 1 199 LEU 1 201 5 3 HELIX 7 AA7 LYS 1 213 ASN 1 216 5 4 HELIX 8 AA8 GLN 2 79 PHE 2 83 5 5 HELIX 9 AA9 SER 2 121 SER 2 127 1 7 HELIX 10 AB1 LYS 2 183 HIS 2 189 1 7 HELIX 11 AB2 GLU A 112 ILE A 116 5 5 HELIX 12 AB3 PRO A 251 ALA A 256 1 6 HELIX 13 AB4 PRO A 257 CYS A 260 5 4 HELIX 14 AB5 PRO A 284 PHE A 288 5 5 HELIX 15 AB6 GLU B 112 ILE B 116 5 5 HELIX 16 AB7 PRO B 251 VAL B 255 5 5 HELIX 17 AB8 ARG B 290 THR B 294 5 5 HELIX 18 AB9 GLU C 112 ILE C 116 5 5 HELIX 19 AC1 PRO C 225 ILE C 229 5 5 HELIX 20 AC2 PRO C 251 ALA C 256 1 6 HELIX 21 AC3 PRO C 257 CYS C 260 5 4 HELIX 22 AC4 PRO C 284 PHE C 288 5 5 HELIX 23 AC5 GLU D 112 ILE D 116 5 5 HELIX 24 AC6 PRO D 251 VAL D 255 5 5 HELIX 25 AC7 HIS a 5 ALA a 12 1 8 HELIX 26 AC8 HIS a 175 LEU a 178 5 4 HELIX 27 AC9 ASP a 219 LYS a 221 5 3 HELIX 28 AD1 HIS b 5 LYS b 10 1 6 HELIX 29 AD2 ASP b 219 CYS b 223 5 5 HELIX 30 AD3 HIS c 5 LYS c 10 1 6 HELIX 31 AD4 ASP c 219 LYS c 221 5 3 HELIX 32 AD5 ASP d 1 THR d 4 5 4 HELIX 33 AD6 HIS d 5 ALA d 12 1 8 HELIX 34 AD7 HIS d 175 LEU d 178 5 4 HELIX 35 AD8 ASP d 219 CYS d 223 5 5 SHEET 1 AA1 4 GLN 1 3 SER 1 7 0 SHEET 2 AA1 4 LEU 1 18 SER 1 25 -1 O SER 1 21 N SER 1 7 SHEET 3 AA1 4 THR 1 78 MET 1 83 -1 O MET 1 83 N LEU 1 18 SHEET 4 AA1 4 LEU 1 68 ASP 1 73 -1 N SER 1 71 O TYR 1 80 SHEET 1 AA2 6 GLY 1 10 VAL 1 12 0 SHEET 2 AA2 6 THR 1 119 VAL 1 123 1 O THR 1 122 N VAL 1 12 SHEET 3 AA2 6 ALA 1 92 SER 1 98 -1 N TYR 1 94 O THR 1 119 SHEET 4 AA2 6 MET 1 34 GLN 1 39 -1 N VAL 1 37 O TYR 1 95 SHEET 5 AA2 6 LEU 1 45 ILE 1 51 -1 O GLU 1 46 N ARG 1 38 SHEET 6 AA2 6 LYS 1 58 TYR 1 60 -1 O TYR 1 59 N VAL 1 50 SHEET 1 AA3 4 GLY 1 10 VAL 1 12 0 SHEET 2 AA3 4 THR 1 119 VAL 1 123 1 O THR 1 122 N VAL 1 12 SHEET 3 AA3 4 ALA 1 92 SER 1 98 -1 N TYR 1 94 O THR 1 119 SHEET 4 AA3 4 TYR 1 114 TRP 1 115 -1 O TYR 1 114 N SER 1 98 SHEET 1 AA4 4 SER 1 132 LEU 1 136 0 SHEET 2 AA4 4 THR 1 147 TYR 1 157 -1 O GLY 1 151 N LEU 1 136 SHEET 3 AA4 4 TYR 1 188 PRO 1 197 -1 O TYR 1 188 N TYR 1 157 SHEET 4 AA4 4 VAL 1 175 THR 1 177 -1 N HIS 1 176 O VAL 1 193 SHEET 1 AA5 4 THR 1 143 SER 1 144 0 SHEET 2 AA5 4 THR 1 147 TYR 1 157 -1 O THR 1 147 N SER 1 144 SHEET 3 AA5 4 TYR 1 188 PRO 1 197 -1 O TYR 1 188 N TYR 1 157 SHEET 4 AA5 4 VAL 1 181 LEU 1 182 -1 N VAL 1 181 O SER 1 189 SHEET 1 AA6 3 THR 1 163 TRP 1 166 0 SHEET 2 AA6 3 TYR 1 206 HIS 1 212 -1 O ASN 1 209 N SER 1 165 SHEET 3 AA6 3 THR 1 217 VAL 1 223 -1 O VAL 1 219 N VAL 1 210 SHEET 1 AA7 4 MET 2 4 SER 2 7 0 SHEET 2 AA7 4 VAL 2 19 ALA 2 25 -1 O ARG 2 24 N THR 2 5 SHEET 3 AA7 4 GLU 2 70 ILE 2 75 -1 O PHE 2 71 N CYS 2 23 SHEET 4 AA7 4 PHE 2 62 SER 2 67 -1 N SER 2 63 O THR 2 74 SHEET 1 AA8 6 ALA 2 10 ALA 2 13 0 SHEET 2 AA8 6 THR 2 102 ILE 2 106 1 O GLU 2 105 N MET 2 11 SHEET 3 AA8 6 THR 2 85 GLN 2 90 -1 N TYR 2 86 O THR 2 102 SHEET 4 AA8 6 LEU 2 33 GLN 2 38 -1 N GLN 2 38 O THR 2 85 SHEET 5 AA8 6 LYS 2 45 TYR 2 49 -1 O LEU 2 47 N TRP 2 35 SHEET 6 AA8 6 SER 2 53 LEU 2 54 -1 O SER 2 53 N TYR 2 49 SHEET 1 AA9 4 SER 2 114 PHE 2 118 0 SHEET 2 AA9 4 THR 2 129 PHE 2 139 -1 O VAL 2 133 N PHE 2 118 SHEET 3 AA9 4 TYR 2 173 SER 2 182 -1 O LEU 2 175 N LEU 2 136 SHEET 4 AA9 4 SER 2 159 VAL 2 163 -1 N SER 2 162 O SER 2 176 SHEET 1 AB1 4 ALA 2 153 LEU 2 154 0 SHEET 2 AB1 4 ALA 2 144 VAL 2 150 -1 N VAL 2 150 O ALA 2 153 SHEET 3 AB1 4 LEU 2 191 HIS 2 198 -1 O ALA 2 193 N LYS 2 149 SHEET 4 AB1 4 VAL 2 205 ASN 2 210 -1 O LYS 2 207 N CYS 2 194 SHEET 1 AB2 3 GLU A 2 PRO A 8 0 SHEET 2 AB2 3 SER A 276 ASP A 282 -1 O ILE A 279 N ALA A 5 SHEET 3 AB2 3 LYS A 161 ILE A 164 -1 N ILE A 163 O SER A 280 SHEET 1 AB3 2 LEU A 18 VAL A 19 0 SHEET 2 AB3 2 VAL A 27 HIS A 28 -1 O VAL A 27 N VAL A 19 SHEET 1 AB4 3 ILE A 31 ARG A 37 0 SHEET 2 AB4 3 GLN A 130 ILE A 135 -1 O ASN A 134 N GLN A 32 SHEET 3 AB4 3 ALA A 145 TYR A 148 -1 O VAL A 147 N ALA A 131 SHEET 1 AB5 6 GLU A 184 TYR A 186 0 SHEET 2 AB5 6 LYS A 177 TYR A 181 -1 N TYR A 181 O GLU A 184 SHEET 3 AB5 6 ALA A 119 LYS A 123 -1 N LYS A 120 O VAL A 180 SHEET 4 AB5 6 ASN A 43 THR A 48 -1 N TYR A 46 O ALA A 121 SHEET 5 AB5 6 LEU A 204 SER A 206 -1 O SER A 206 N ILE A 47 SHEET 6 AB5 6 TYR A 215 ALA A 216 -1 O TYR A 215 N GLN A 205 SHEET 1 AB6 3 TYR A 51 LYS A 54 0 SHEET 2 AB6 3 THR A 101 ARG A 110 -1 O GLU A 109 N LYS A 52 SHEET 3 AB6 3 VAL A 59 LYS A 61 -1 N VAL A 59 O MET A 103 SHEET 1 AB7 3 TYR A 51 LYS A 54 0 SHEET 2 AB7 3 THR A 101 ARG A 110 -1 O GLU A 109 N LYS A 52 SHEET 3 AB7 3 GLN A 77 THR A 82 -1 N PHE A 81 O GLN A 102 SHEET 1 AB8 2 LYS A 221 LEU A 222 0 SHEET 2 AB8 2 PHE A 234 THR A 235 -1 O THR A 235 N LYS A 221 SHEET 1 AB9 2 SER A 261 ALA A 263 0 SHEET 2 AB9 2 ARG A 268 GLU A 270 -1 O ARG A 268 N ALA A 263 SHEET 1 AC1 4 GLU A 301 ILE A 304 0 SHEET 2 AC1 4 GLY A 315 ALA A 320 -1 O ALA A 320 N GLU A 301 SHEET 3 AC1 4 SER A 352 THR A 359 -1 O PHE A 357 N GLY A 315 SHEET 4 AC1 4 ALA A 338 ILE A 340 -1 N VAL A 339 O SER A 358 SHEET 1 AC2 2 CYS A 307 THR A 308 0 SHEET 2 AC2 2 CYS A 381 LYS A 382 1 O LYS A 382 N CYS A 307 SHEET 1 AC3 2 GLY A 327 ASN A 328 0 SHEET 2 AC3 2 THR A 346 LEU A 347 -1 O LEU A 347 N GLY A 327 SHEET 1 AC4 3 ILE A 331 HIS A 332 0 SHEET 2 AC4 3 LYS A 367 VAL A 370 -1 O GLN A 369 N HIS A 332 SHEET 3 AC4 3 SER A 373 THR A 376 -1 O SER A 373 N VAL A 370 SHEET 1 AC5 3 GLU B 2 PRO B 8 0 SHEET 2 AC5 3 SER B 276 ASP B 282 -1 O ILE B 279 N ALA B 5 SHEET 3 AC5 3 LYS B 161 ILE B 163 -1 N ILE B 163 O SER B 280 SHEET 1 AC6 2 LEU B 18 VAL B 19 0 SHEET 2 AC6 2 VAL B 27 HIS B 28 -1 O VAL B 27 N VAL B 19 SHEET 1 AC7 3 ILE B 31 ASN B 35 0 SHEET 2 AC7 3 GLN B 130 ILE B 135 -1 O MET B 132 N VAL B 34 SHEET 3 AC7 3 ALA B 145 TYR B 148 -1 O VAL B 147 N ALA B 131 SHEET 1 AC8 4 THR B 42 THR B 48 0 SHEET 2 AC8 4 ALA B 119 VAL B 124 -1 O ALA B 121 N TYR B 46 SHEET 3 AC8 4 LYS B 177 TYR B 181 -1 O VAL B 178 N TYR B 122 SHEET 4 AC8 4 GLU B 184 TYR B 186 -1 O TYR B 186 N VAL B 179 SHEET 1 AC9 3 TYR B 51 LYS B 54 0 SHEET 2 AC9 3 THR B 101 ARG B 110 -1 O GLU B 109 N LYS B 52 SHEET 3 AC9 3 VAL B 59 LYS B 61 -1 N VAL B 59 O MET B 103 SHEET 1 AD1 3 TYR B 51 LYS B 54 0 SHEET 2 AD1 3 THR B 101 ARG B 110 -1 O GLU B 109 N LYS B 52 SHEET 3 AD1 3 GLN B 77 THR B 82 -1 N GLN B 77 O ALA B 106 SHEET 1 AD2 2 PHE B 87 MET B 88 0 SHEET 2 AD2 2 GLY B 91 ALA B 92 -1 O GLY B 91 N MET B 88 SHEET 1 AD3 2 LEU B 204 SER B 206 0 SHEET 2 AD3 2 LEU B 214 ALA B 216 -1 O TYR B 215 N GLN B 205 SHEET 1 AD4 2 LYS B 221 LEU B 222 0 SHEET 2 AD4 2 PHE B 234 THR B 235 -1 O THR B 235 N LYS B 221 SHEET 1 AD5 5 ALA B 338 ILE B 340 0 SHEET 2 AD5 5 SER B 352 THR B 359 -1 O SER B 358 N VAL B 339 SHEET 3 AD5 5 GLY B 315 ALA B 320 -1 N GLY B 315 O PHE B 357 SHEET 4 AD5 5 GLU B 301 THR B 308 -1 N LYS B 303 O THR B 318 SHEET 5 AD5 5 CYS B 381 LYS B 382 1 O LYS B 382 N CYS B 307 SHEET 1 AD6 4 ASP B 344 LEU B 347 0 SHEET 2 AD6 4 GLY B 327 HIS B 332 -1 N GLY B 327 O LEU B 347 SHEET 3 AD6 4 ALA B 365 VAL B 370 -1 O GLN B 369 N HIS B 332 SHEET 4 AD6 4 ALA B 374 LYS B 378 -1 O VAL B 375 N LEU B 368 SHEET 1 AD7 4 GLU C 2 PRO C 8 0 SHEET 2 AD7 4 SER C 276 ASP C 282 -1 O ILE C 277 N MET C 7 SHEET 3 AD7 4 LYS C 161 ILE C 163 -1 N LYS C 161 O ASP C 282 SHEET 4 AD7 4 ALA C 155 LYS C 156 -1 N ALA C 155 O LEU C 162 SHEET 1 AD8 4 LEU C 18 VAL C 19 0 SHEET 2 AD8 4 VAL C 27 ASN C 35 -1 O VAL C 27 N VAL C 19 SHEET 3 AD8 4 GLN C 130 TYR C 137 -1 O ASN C 134 N GLN C 32 SHEET 4 AD8 4 SER C 144 TYR C 148 -1 O VAL C 147 N ALA C 131 SHEET 1 AD9 6 GLU C 184 TYR C 186 0 SHEET 2 AD9 6 LYS C 177 TYR C 181 -1 N VAL C 179 O TYR C 186 SHEET 3 AD9 6 ALA C 119 VAL C 124 -1 N LYS C 120 O VAL C 180 SHEET 4 AD9 6 THR C 42 THR C 48 -1 N THR C 48 O ALA C 119 SHEET 5 AD9 6 LEU C 204 SER C 206 -1 O SER C 206 N ILE C 47 SHEET 6 AD9 6 LEU C 214 ALA C 216 -1 O TYR C 215 N GLN C 205 SHEET 1 AE1 3 TYR C 51 LYS C 54 0 SHEET 2 AE1 3 THR C 101 ARG C 110 -1 O GLU C 109 N LYS C 52 SHEET 3 AE1 3 VAL C 59 LYS C 61 -1 N VAL C 59 O MET C 103 SHEET 1 AE2 3 TYR C 51 LYS C 54 0 SHEET 2 AE2 3 THR C 101 ARG C 110 -1 O GLU C 109 N LYS C 52 SHEET 3 AE2 3 GLN C 77 THR C 82 -1 N PHE C 81 O GLN C 102 SHEET 1 AE3 2 LYS C 221 LEU C 222 0 SHEET 2 AE3 2 PHE C 234 THR C 235 -1 O THR C 235 N LYS C 221 SHEET 1 AE4 5 ALA C 338 ILE C 340 0 SHEET 2 AE4 5 SER C 352 THR C 359 -1 O SER C 358 N VAL C 339 SHEET 3 AE4 5 GLY C 315 SER C 323 -1 N GLY C 315 O PHE C 357 SHEET 4 AE4 5 VAL C 297 THR C 308 -1 N THR C 305 O ILE C 316 SHEET 5 AE4 5 CYS C 381 LYS C 382 1 O LYS C 382 N CYS C 307 SHEET 1 AE5 3 ASP C 344 LEU C 347 0 SHEET 2 AE5 3 GLY C 327 HIS C 332 -1 N GLY C 327 O LEU C 347 SHEET 3 AE5 3 GLN C 369 VAL C 370 -1 O GLN C 369 N HIS C 332 SHEET 1 AE6 2 PHE C 366 LYS C 367 0 SHEET 2 AE6 2 THR C 376 CYS C 377 -1 O CYS C 377 N PHE C 366 SHEET 1 AE7 4 GLU D 2 PRO D 8 0 SHEET 2 AE7 4 SER D 276 ASP D 282 -1 O ILE D 279 N ALA D 5 SHEET 3 AE7 4 ALA D 160 ILE D 163 -1 N ILE D 163 O SER D 280 SHEET 4 AE7 4 PRO D 154 ILE D 157 -1 O ALA D 155 N LEU D 162 SHEET 1 AE8 2 ALA D 17 VAL D 19 0 SHEET 2 AE8 2 VAL D 27 LEU D 29 -1 O VAL D 27 N VAL D 19 SHEET 1 AE9 3 ILE D 31 LEU D 33 0 SHEET 2 AE9 3 GLN D 130 ILE D 135 -1 O ASN D 134 N GLN D 32 SHEET 3 AE9 3 SER D 144 TYR D 148 -1 O ALA D 145 N VAL D 133 SHEET 1 AF1 4 THR D 42 THR D 48 0 SHEET 2 AF1 4 ALA D 119 VAL D 124 -1 O ALA D 121 N GLU D 45 SHEET 3 AF1 4 LYS D 177 TYR D 181 -1 O VAL D 180 N LYS D 120 SHEET 4 AF1 4 GLU D 184 TYR D 186 -1 O TYR D 186 N VAL D 179 SHEET 1 AF2 3 TYR D 51 LYS D 54 0 SHEET 2 AF2 3 THR D 101 ARG D 110 -1 O GLU D 109 N LYS D 52 SHEET 3 AF2 3 VAL D 59 LYS D 61 -1 N VAL D 59 O MET D 103 SHEET 1 AF3 3 TYR D 51 LYS D 54 0 SHEET 2 AF3 3 THR D 101 ARG D 110 -1 O GLU D 109 N LYS D 52 SHEET 3 AF3 3 GLN D 77 PHE D 81 -1 N PHE D 81 O GLN D 102 SHEET 1 AF4 2 LEU D 204 SER D 206 0 SHEET 2 AF4 2 LEU D 214 ALA D 216 -1 O TYR D 215 N GLN D 205 SHEET 1 AF5 2 LYS D 221 LEU D 222 0 SHEET 2 AF5 2 PHE D 234 THR D 235 -1 O THR D 235 N LYS D 221 SHEET 1 AF6 4 GLU D 301 GLU D 306 0 SHEET 2 AF6 4 GLY D 315 ALA D 320 -1 O ALA D 320 N GLU D 301 SHEET 3 AF6 4 SER D 352 THR D 359 -1 O PHE D 357 N GLY D 315 SHEET 4 AF6 4 ALA D 338 ILE D 340 -1 N VAL D 339 O SER D 358 SHEET 1 AF7 4 ASP D 344 LEU D 347 0 SHEET 2 AF7 4 GLY D 327 HIS D 332 -1 N GLY D 327 O LEU D 347 SHEET 3 AF7 4 LYS D 367 VAL D 370 -1 O GLN D 369 N HIS D 332 SHEET 4 AF7 4 ALA D 374 THR D 376 -1 O VAL D 375 N LEU D 368 SHEET 1 AF8 4 GLU a 34 ARG a 37 0 SHEET 2 AF8 4 VAL a 44 GLY a 54 -1 O ARG a 46 N ARG a 37 SHEET 3 AF8 4 TYR a 64 SER a 66 -1 O SER a 66 N MET a 52 SHEET 4 AF8 4 ILE a 76 LYS a 77 -1 O ILE a 76 N MET a 65 SHEET 1 AF9 3 GLU a 34 ARG a 37 0 SHEET 2 AF9 3 VAL a 44 GLY a 54 -1 O ARG a 46 N ARG a 37 SHEET 3 AF9 3 SER a 90 GLN a 102 -1 O ALA a 101 N ILE a 45 SHEET 1 AG1 3 HIS a 82 ARG a 84 0 SHEET 2 AG1 3 GLY a 106 GLY a 112 -1 O THR a 110 N ARG a 84 SHEET 3 AG1 3 CYS a 122 VAL a 128 -1 O CYS a 122 N VAL a 111 SHEET 1 AG2 2 GLU a 147 LEU a 148 0 SHEET 2 AG2 2 CYS a 263 ILE a 264 -1 O CYS a 263 N LEU a 148 SHEET 1 AG3 2 ARG a 152 TYR a 153 0 SHEET 2 AG3 2 PRO a 258 VAL a 259 -1 O VAL a 259 N ARG a 152 SHEET 1 AG4 2 TYR a 163 VAL a 164 0 SHEET 2 AG4 2 LEU a 252 HIS a 253 -1 O LEU a 252 N VAL a 164 SHEET 1 AG5 2 MET a 166 HIS a 167 0 SHEET 2 AG5 2 VAL a 234 TYR a 235 -1 O VAL a 234 N HIS a 167 SHEET 1 AG6 3 VAL a 172 ALA a 173 0 SHEET 2 AG6 3 CYS a 223 LEU a 227 -1 O LEU a 227 N VAL a 172 SHEET 3 AG6 3 LYS a 196 CYS a 199 -1 N TYR a 198 O ARG a 224 SHEET 1 AG7 2 SER a 179 ILE a 180 0 SHEET 2 AG7 2 VAL a 185 LYS a 186 -1 O LYS a 186 N SER a 179 SHEET 1 AG8 3 LEU a 272 LYS a 276 0 SHEET 2 AG8 3 THR a 279 HIS a 283 -1 O HIS a 283 N LEU a 272 SHEET 3 AG8 3 THR a 313 PHE a 316 -1 O PHE a 316 N LEU a 280 SHEET 1 AG9 4 THR a 304 ILE a 308 0 SHEET 2 AG9 4 THR a 290 SER a 296 -1 N THR a 294 O THR a 304 SHEET 3 AG9 4 LEU a 323 TRP a 327 -1 O THR a 326 N THR a 293 SHEET 4 AG9 4 LYS a 333 VAL a 335 -1 O VAL a 335 N LEU a 323 SHEET 1 AH1 3 ILE b 33 ARG b 37 0 SHEET 2 AH1 3 VAL b 44 PHE b 53 -1 O ARG b 46 N ARG b 37 SHEET 3 AH1 3 SER b 90 GLN b 102 -1 O ALA b 101 N ILE b 45 SHEET 1 AH2 2 TYR b 64 ASN b 69 0 SHEET 2 AH2 2 THR b 72 LYS b 77 -1 O LYS b 74 N PHE b 67 SHEET 1 AH3 3 HIS b 82 ARG b 84 0 SHEET 2 AH3 3 GLY b 106 GLY b 112 -1 O GLY b 112 N HIS b 82 SHEET 3 AH3 3 THR b 121 VAL b 128 -1 O CYS b 122 N VAL b 111 SHEET 1 AH4 2 VAL b 146 LEU b 148 0 SHEET 2 AH4 2 CYS b 263 ALA b 265 -1 O ALA b 265 N VAL b 146 SHEET 1 AH5 2 ARG b 152 TYR b 153 0 SHEET 2 AH5 2 PRO b 258 VAL b 259 -1 O VAL b 259 N ARG b 152 SHEET 1 AH6 2 TYR b 163 VAL b 164 0 SHEET 2 AH6 2 LEU b 252 HIS b 253 -1 O LEU b 252 N VAL b 164 SHEET 1 AH7 2 VAL b 172 ALA b 173 0 SHEET 2 AH7 2 TYR b 226 LEU b 227 -1 O LEU b 227 N VAL b 172 SHEET 1 AH8 2 LEU b 178 ILE b 180 0 SHEET 2 AH8 2 VAL b 185 ILE b 187 -1 O LYS b 186 N SER b 179 SHEET 1 AH9 3 LEU b 272 LYS b 276 0 SHEET 2 AH9 3 THR b 279 LEU b 284 -1 O HIS b 283 N LEU b 272 SHEET 3 AH9 3 THR b 312 PHE b 316 -1 O PHE b 316 N LEU b 280 SHEET 1 AI1 4 THR b 304 ILE b 308 0 SHEET 2 AI1 4 THR b 290 SER b 296 -1 N THR b 290 O ILE b 308 SHEET 3 AI1 4 LEU b 323 TRP b 327 -1 O THR b 326 N THR b 293 SHEET 4 AI1 4 LYS b 333 VAL b 335 -1 O LYS b 333 N TYR b 325 SHEET 1 AI2 4 ILE c 33 ARG c 37 0 SHEET 2 AI2 4 VAL c 44 GLY c 54 -1 O ARG c 46 N ARG c 37 SHEET 3 AI2 4 TYR c 64 ASN c 69 -1 O SER c 66 N MET c 52 SHEET 4 AI2 4 THR c 72 LYS c 77 -1 O ILE c 76 N MET c 65 SHEET 1 AI3 3 ILE c 33 ARG c 37 0 SHEET 2 AI3 3 VAL c 44 GLY c 54 -1 O ARG c 46 N ARG c 37 SHEET 3 AI3 3 SER c 90 GLN c 102 -1 O GLY c 96 N PHE c 53 SHEET 1 AI4 3 HIS c 82 ARG c 84 0 SHEET 2 AI4 3 GLY c 106 GLY c 112 -1 O THR c 110 N ARG c 84 SHEET 3 AI4 3 THR c 121 VAL c 128 -1 O VAL c 128 N GLY c 106 SHEET 1 AI5 2 GLU c 147 LEU c 148 0 SHEET 2 AI5 2 CYS c 263 ILE c 264 -1 O CYS c 263 N LEU c 148 SHEET 1 AI6 2 ARG c 152 TYR c 153 0 SHEET 2 AI6 2 PRO c 258 VAL c 259 -1 O VAL c 259 N ARG c 152 SHEET 1 AI7 2 TYR c 163 VAL c 164 0 SHEET 2 AI7 2 LEU c 252 HIS c 253 -1 O LEU c 252 N VAL c 164 SHEET 1 AI8 3 VAL c 172 ALA c 173 0 SHEET 2 AI8 3 CYS c 223 LEU c 227 -1 O LEU c 227 N VAL c 172 SHEET 3 AI8 3 TYR c 197 CYS c 199 -1 N TYR c 198 O ARG c 224 SHEET 1 AI9 2 LEU c 178 ILE c 180 0 SHEET 2 AI9 2 VAL c 185 ILE c 187 -1 O LYS c 186 N SER c 179 SHEET 1 AJ1 3 LEU c 272 LYS c 276 0 SHEET 2 AJ1 3 THR c 279 LEU c 284 -1 O ILE c 281 N GLU c 274 SHEET 3 AJ1 3 THR c 312 THR c 317 -1 O VAL c 314 N LEU c 282 SHEET 1 AJ2 4 THR c 304 ILE c 308 0 SHEET 2 AJ2 4 THR c 290 SER c 296 -1 N THR c 294 O THR c 304 SHEET 3 AJ2 4 LEU c 323 TRP c 327 -1 O GLU c 324 N ARG c 295 SHEET 4 AJ2 4 LYS c 333 VAL c 335 -1 O LYS c 333 N TYR c 325 SHEET 1 AJ3 4 ILE d 33 ARG d 37 0 SHEET 2 AJ3 4 VAL d 44 THR d 49 -1 O ARG d 46 N ARG d 37 SHEET 3 AJ3 4 TYR d 98 GLN d 102 -1 O ALA d 101 N ILE d 45 SHEET 4 AJ3 4 SER d 90 HIS d 95 -1 N SER d 93 O LEU d 100 SHEET 1 AJ4 3 MET d 52 GLY d 54 0 SHEET 2 AJ4 3 TYR d 64 ASN d 69 -1 O SER d 66 N MET d 52 SHEET 3 AJ4 3 THR d 72 LYS d 77 -1 O ILE d 76 N MET d 65 SHEET 1 AJ5 3 HIS d 82 ARG d 84 0 SHEET 2 AJ5 3 GLY d 106 GLY d 112 -1 O THR d 110 N ARG d 84 SHEET 3 AJ5 3 THR d 121 VAL d 128 -1 O CYS d 122 N VAL d 111 SHEET 1 AJ6 2 GLU d 147 PRO d 149 0 SHEET 2 AJ6 2 LYS d 262 ILE d 264 -1 N CYS d 263 O LEU d 148 SHEET 1 AJ7 2 ARG d 152 TYR d 153 0 SHEET 2 AJ7 2 PRO d 258 VAL d 259 -1 O VAL d 259 N ARG d 152 SHEET 1 AJ8 2 TYR d 163 VAL d 164 0 SHEET 2 AJ8 2 LEU d 252 HIS d 253 -1 O LEU d 252 N VAL d 164 SHEET 1 AJ9 2 VAL d 172 ALA d 173 0 SHEET 2 AJ9 2 TYR d 226 LEU d 227 -1 O LEU d 227 N VAL d 172 SHEET 1 AK1 2 SER d 179 ILE d 180 0 SHEET 2 AK1 2 VAL d 185 LYS d 186 -1 O LYS d 186 N SER d 179 SHEET 1 AK2 3 LEU d 272 HIS d 275 0 SHEET 2 AK2 3 THR d 279 LEU d 284 -1 O HIS d 283 N LEU d 272 SHEET 3 AK2 3 THR d 312 THR d 317 -1 O PHE d 316 N LEU d 280 SHEET 1 AK3 4 THR d 304 ILE d 308 0 SHEET 2 AK3 4 THR d 290 SER d 296 -1 N THR d 290 O ILE d 308 SHEET 3 AK3 4 LEU d 323 TRP d 327 -1 O THR d 326 N THR d 293 SHEET 4 AK3 4 LYS d 333 VAL d 335 -1 O LYS d 333 N TYR d 325 SSBOND 1 CYS A 49 CYS A 114 1555 1555 2.03 SSBOND 2 CYS A 62 CYS A 94 1555 1555 2.04 SSBOND 3 CYS A 63 CYS A 96 1555 1555 2.04 SSBOND 4 CYS A 68 CYS A 78 1555 1555 2.03 SSBOND 5 CYS A 260 CYS A 272 1555 1555 2.04 SSBOND 6 CYS A 302 CYS A 377 1555 1555 2.03 SSBOND 7 CYS A 307 CYS A 381 1555 1555 2.04 SSBOND 8 CYS A 329 CYS A 371 1555 1555 2.04 SSBOND 9 CYS B 49 CYS B 114 1555 1555 2.03 SSBOND 10 CYS B 62 CYS B 94 1555 1555 2.04 SSBOND 11 CYS B 63 CYS B 96 1555 1555 2.03 SSBOND 12 CYS B 68 CYS B 78 1555 1555 2.03 SSBOND 13 CYS B 260 CYS B 272 1555 1555 2.04 SSBOND 14 CYS B 302 CYS B 377 1555 1555 2.03 SSBOND 15 CYS B 307 CYS B 381 1555 1555 2.03 SSBOND 16 CYS B 329 CYS B 371 1555 1555 2.03 SSBOND 17 CYS C 49 CYS C 114 1555 1555 2.02 SSBOND 18 CYS C 62 CYS C 94 1555 1555 2.04 SSBOND 19 CYS C 63 CYS C 96 1555 1555 2.03 SSBOND 20 CYS C 68 CYS C 78 1555 1555 2.03 SSBOND 21 CYS C 260 CYS C 272 1555 1555 2.04 SSBOND 22 CYS C 302 CYS C 377 1555 1555 2.03 SSBOND 23 CYS C 307 CYS C 381 1555 1555 2.03 SSBOND 24 CYS C 329 CYS C 371 1555 1555 2.04 SSBOND 25 CYS D 49 CYS D 114 1555 1555 2.03 SSBOND 26 CYS D 62 CYS D 94 1555 1555 2.04 SSBOND 27 CYS D 63 CYS D 96 1555 1555 2.04 SSBOND 28 CYS D 68 CYS D 78 1555 1555 2.03 SSBOND 29 CYS D 260 CYS D 272 1555 1555 2.04 SSBOND 30 CYS D 302 CYS D 377 1555 1555 2.03 SSBOND 31 CYS D 307 CYS D 381 1555 1555 2.04 SSBOND 32 CYS D 329 CYS D 371 1555 1555 2.03 SSBOND 33 CYS a 19 CYS a 122 1555 1555 2.03 SSBOND 34 CYS a 22 CYS a 27 1555 1555 2.03 SSBOND 35 CYS a 89 CYS a 103 1555 1555 2.03 SSBOND 36 CYS a 150 CYS a 263 1555 1555 2.03 SSBOND 37 CYS a 199 CYS a 223 1555 1555 2.04 SSBOND 38 CYS a 201 CYS a 217 1555 1555 2.03 SSBOND 39 CYS b 19 CYS b 122 1555 1555 2.03 SSBOND 40 CYS b 22 CYS b 27 1555 1555 2.03 SSBOND 41 CYS b 89 CYS b 103 1555 1555 2.03 SSBOND 42 CYS b 150 CYS b 263 1555 1555 2.03 SSBOND 43 CYS b 199 CYS b 223 1555 1555 2.04 SSBOND 44 CYS b 201 CYS b 217 1555 1555 2.04 SSBOND 45 CYS c 19 CYS c 122 1555 1555 2.03 SSBOND 46 CYS c 22 CYS c 27 1555 1555 2.03 SSBOND 47 CYS c 89 CYS c 103 1555 1555 2.03 SSBOND 48 CYS c 150 CYS c 263 1555 1555 2.04 SSBOND 49 CYS c 199 CYS c 223 1555 1555 2.04 SSBOND 50 CYS c 201 CYS c 217 1555 1555 2.03 SSBOND 51 CYS d 19 CYS d 122 1555 1555 2.03 SSBOND 52 CYS d 22 CYS d 27 1555 1555 2.03 SSBOND 53 CYS d 89 CYS d 103 1555 1555 2.03 SSBOND 54 CYS d 150 CYS d 263 1555 1555 2.03 SSBOND 55 CYS d 199 CYS d 223 1555 1555 2.04 SSBOND 56 CYS d 201 CYS d 217 1555 1555 2.04 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.42 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.47 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.41 CISPEP 1 PHE 1 158 PRO 1 159 0 -11.76 CISPEP 2 GLU 1 160 PRO 1 161 0 -2.47 CISPEP 3 SER 2 7 PRO 2 8 0 -5.40 CISPEP 4 SER 2 94 PRO 2 95 0 0.00 CISPEP 5 TYR 2 140 PRO 2 141 0 2.53 CISPEP 6 GLY A 165 PRO A 166 0 4.48 CISPEP 7 GLY B 165 PRO B 166 0 2.61 CISPEP 8 GLY C 165 PRO C 166 0 1.21 CISPEP 9 GLY D 165 PRO D 166 0 2.58 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