HEADER IMMUNE SYSTEM 02-SEP-24 9JE3 TITLE STRUCTURE OF #2-911 FAB IN COMPLEX WITH MEDI8852 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: #2-911 FAB HEAVY CHAIN; COMPND 3 CHAIN: E, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: #2-911 FAB LIGHT CHAIN; COMPND 7 CHAIN: F, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MEDI8852 FAB HEAVY CHAIN; COMPND 11 CHAIN: G, C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MEDI8852 FAB LIGHT CHAIN; COMPND 15 CHAIN: H, D; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 7 EXPRESSION_SYSTEM_CELL: EXPI 293; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 14 EXPRESSION_SYSTEM_CELL: EXPI 293; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 21 EXPRESSION_SYSTEM_CELL: EXPI 293; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 28 EXPRESSION_SYSTEM_CELL: EXPI 293 KEYWDS ANTIBODY, ANTI-IDIOTYPIC ANTIBODY, BROADLY-NEUTRALIZING ANTIBODY, KEYWDS 2 COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR H.ITOU,K.SANO,A.AINAI,T.SUZUKI REVDAT 1 03-SEP-25 9JE3 0 JRNL AUTH H.ITOU,K.SANO,A.AINAI,K.OTSUKI,T.INOUE,T.SUZUKI JRNL TITL FINDING AND MIMICKING A CONSERVED STRUCTURAL MOTIF HIDDEN IN JRNL TITL 2 INFLUENZA VIRUS HAEMAGGLUTININS USING ANTI-IDIOTYPIC JRNL TITL 3 ANTIBODIES: A NOVEL APPROACH FOR UNIVERSAL VACCINE ANTIGEN JRNL TITL 4 DESIGN. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.37 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC V5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.43 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 91583 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.137 REMARK 3 FREE R VALUE TEST SET COUNT : 4705 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13180 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 95 REMARK 3 SOLVENT ATOMS : 278 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.52 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.72600 REMARK 3 B22 (A**2) : 3.53200 REMARK 3 B33 (A**2) : 0.19500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.311 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.214 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.838 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9JE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300051094. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-MAY-24 REMARK 200 TEMPERATURE (KELVIN) : 273 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL45XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91583 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.374 REMARK 200 RESOLUTION RANGE LOW (A) : 48.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.8 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.03800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.7200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.46900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5JW3,2QHR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS (PH5.5), 13% PEG3350, REMARK 280 1% TACSIMATE, 10 MM TCEP, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 42.14150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.18400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.55550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.18400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.14150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.55550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H, X, I 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, J 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 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 F 213 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 NZ LYS D 149 OE2 GLU D 195 2.18 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 E 80 CG - SD - CE ANGL. DEV. = -10.6 DEGREES REMARK 500 MET G 102 CG - SD - CE ANGL. DEV. = 11.5 DEGREES REMARK 500 MET A 80 CG - SD - CE ANGL. DEV. = -11.3 DEGREES REMARK 500 MET C 102 CG - SD - CE ANGL. DEV. = 9.7 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 LEU E 138 -165.17 -103.46 REMARK 500 ALA E 201 0.98 -69.34 REMARK 500 LYS E 208 115.90 -165.18 REMARK 500 THR F 51 -46.51 69.81 REMARK 500 ASN F 52 20.17 -140.15 REMARK 500 ALA F 84 -179.27 -174.49 REMARK 500 TYR F 92 74.26 -113.46 REMARK 500 SER F 93 -55.08 68.91 REMARK 500 ASN F 171 -0.11 79.96 REMARK 500 SER G 15 -9.76 79.75 REMARK 500 ARG G 52B 84.09 -151.20 REMARK 500 ASN G 76 67.48 62.52 REMARK 500 ASP G 144 60.41 64.33 REMARK 500 LEU H 29 75.27 -105.55 REMARK 500 ALA H 51 -40.49 71.26 REMARK 500 SER H 91 -121.42 60.65 REMARK 500 ASN H 138 61.70 61.30 REMARK 500 TYR H 140 131.19 -171.24 REMARK 500 PRO H 141 -167.44 -78.03 REMARK 500 LYS H 190 -57.86 -121.67 REMARK 500 HIS A 41 17.38 57.02 REMARK 500 SER A 82B 64.31 60.59 REMARK 500 ALA A 88 -179.61 179.55 REMARK 500 ASP A 173 -5.87 75.60 REMARK 500 THR A 187 -70.74 -75.00 REMARK 500 THR B 51 -49.38 70.11 REMARK 500 SER B 93 -49.53 68.73 REMARK 500 ASN B 171 -0.17 84.12 REMARK 500 SER C 15 -11.78 78.02 REMARK 500 ARG C 52B 76.41 -150.97 REMARK 500 ARG C 66 1.37 -150.43 REMARK 500 SER C 132 -56.65 -133.16 REMARK 500 LEU D 29 65.27 -100.82 REMARK 500 ALA D 51 -42.31 72.64 REMARK 500 SER D 67 110.30 -168.18 REMARK 500 SER D 91 -122.96 54.68 REMARK 500 ASN D 138 61.44 66.90 REMARK 500 LYS D 190 -57.98 -124.92 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 G 66 0.08 SIDE CHAIN REMARK 500 ARG H 54 0.08 SIDE CHAIN REMARK 500 ARG H 211 0.23 SIDE CHAIN REMARK 500 ARG D 54 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9JE3 E 1 212 PDB 9JE3 9JE3 1 212 DBREF 9JE3 F 1 213 PDB 9JE3 9JE3 1 213 DBREF 9JE3 G 1 213 PDB 9JE3 9JE3 1 213 DBREF 9JE3 H 1 214 PDB 9JE3 9JE3 1 214 DBREF 9JE3 A 1 212 PDB 9JE3 9JE3 1 212 DBREF 9JE3 B 1 213 PDB 9JE3 9JE3 1 213 DBREF 9JE3 C 1 213 PDB 9JE3 9JE3 1 213 DBREF 9JE3 D 1 214 PDB 9JE3 9JE3 1 214 SEQRES 1 E 217 GLU VAL GLN LEU GLN GLU SER GLY PRO GLU LEU MET LYS SEQRES 2 E 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 E 217 TYR SER PHE THR SER TYR ASN MET HIS TRP VAL LYS GLN SEQRES 4 E 217 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE ASP SEQRES 5 E 217 PRO PHE ASN ASP GLY THR THR TYR ASN GLN LYS PHE LYS SEQRES 6 E 217 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 E 217 ALA TYR MET HIS LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 E 217 ALA VAL TYR TYR CYS ALA LYS LEU GLY PRO TYR TRP TYR SEQRES 9 E 217 PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 E 217 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA SEQRES 11 E 217 PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU SEQRES 12 E 217 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 E 217 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 E 217 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 E 217 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER SEQRES 16 E 217 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 E 217 THR LYS VAL ASP LYS LYS ILE GLU PRO SEQRES 1 F 215 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 F 215 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 F 215 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 4 F 215 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY SEQRES 5 F 215 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 F 215 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 F 215 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 F 215 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 F 215 LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SER SEQRES 10 F 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLU THR SEQRES 11 F 215 ASN LYS ALA THR LEU VAL CYS THR ILE THR ASP PHE TYR SEQRES 12 F 215 PRO GLY VAL VAL THR VAL ASP TRP LYS VAL ASP GLY THR SEQRES 13 F 215 PRO VAL THR GLN GLY MET GLU THR THR GLN PRO SER LYS SEQRES 14 F 215 GLN SER ASN ASN LYS TYR MET ALA SER SER TYR LEU THR SEQRES 15 F 215 LEU THR ALA ARG ALA TRP GLU ARG HIS SER SER TYR SER SEQRES 16 F 215 CYS GLN VAL THR HIS GLU GLY HIS THR VAL GLU LYS SER SEQRES 17 F 215 LEU SER ARG ALA ASP CYS SER SEQRES 1 G 228 GLN VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS SEQRES 2 G 228 PRO SER GLN THR LEU SER LEU THR CYS ALA ILE SER GLY SEQRES 3 G 228 ASP SER VAL SER SER TYR ASN ALA VAL TRP ASN TRP ILE SEQRES 4 G 228 ARG GLN SER PRO SER ARG GLY LEU GLU TRP LEU GLY ARG SEQRES 5 G 228 THR TYR TYR ARG SER GLY TRP TYR ASN ASP TYR ALA GLU SEQRES 6 G 228 SER VAL LYS SER ARG ILE THR ILE ASN PRO ASP THR SER SEQRES 7 G 228 LYS ASN GLN PHE SER LEU GLN LEU ASN SER VAL THR PRO SEQRES 8 G 228 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER GLY HIS SEQRES 9 G 228 ILE THR VAL PHE GLY VAL ASN VAL ASP ALA PHE ASP MET SEQRES 10 G 228 TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA SER SEQRES 11 G 228 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 G 228 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 G 228 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 G 228 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 G 228 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 G 228 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 G 228 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 G 228 VAL ASP LYS LYS VAL GLU PRO SEQRES 1 H 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 H 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER SEQRES 3 H 210 GLN SER LEU SER SER TYR THR HIS TRP TYR GLN GLN LYS SEQRES 4 H 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 H 210 SER ARG GLY SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 H 210 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 H 210 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 H 210 ARG THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 H 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 H 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 H 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 H 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 H 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 H 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 H 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 H 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 H 210 GLU CYS SEQRES 1 A 217 GLU VAL GLN LEU GLN GLU SER GLY PRO GLU LEU MET LYS SEQRES 2 A 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 217 TYR SER PHE THR SER TYR ASN MET HIS TRP VAL LYS GLN SEQRES 4 A 217 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE ASP SEQRES 5 A 217 PRO PHE ASN ASP GLY THR THR TYR ASN GLN LYS PHE LYS SEQRES 6 A 217 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 A 217 ALA TYR MET HIS LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 A 217 ALA VAL TYR TYR CYS ALA LYS LEU GLY PRO TYR TRP TYR SEQRES 9 A 217 PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 A 217 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA SEQRES 11 A 217 PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU SEQRES 12 A 217 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 217 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 A 217 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 A 217 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER SEQRES 16 A 217 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 A 217 THR LYS VAL ASP LYS LYS ILE GLU PRO SEQRES 1 B 215 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 B 215 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 B 215 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 4 B 215 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY SEQRES 5 B 215 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 B 215 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 B 215 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 B 215 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 B 215 LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SER SEQRES 10 B 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLU THR SEQRES 11 B 215 ASN LYS ALA THR LEU VAL CYS THR ILE THR ASP PHE TYR SEQRES 12 B 215 PRO GLY VAL VAL THR VAL ASP TRP LYS VAL ASP GLY THR SEQRES 13 B 215 PRO VAL THR GLN GLY MET GLU THR THR GLN PRO SER LYS SEQRES 14 B 215 GLN SER ASN ASN LYS TYR MET ALA SER SER TYR LEU THR SEQRES 15 B 215 LEU THR ALA ARG ALA TRP GLU ARG HIS SER SER TYR SER SEQRES 16 B 215 CYS GLN VAL THR HIS GLU GLY HIS THR VAL GLU LYS SER SEQRES 17 B 215 LEU SER ARG ALA ASP CYS SER SEQRES 1 C 228 GLN VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 228 PRO SER GLN THR LEU SER LEU THR CYS ALA ILE SER GLY SEQRES 3 C 228 ASP SER VAL SER SER TYR ASN ALA VAL TRP ASN TRP ILE SEQRES 4 C 228 ARG GLN SER PRO SER ARG GLY LEU GLU TRP LEU GLY ARG SEQRES 5 C 228 THR TYR TYR ARG SER GLY TRP TYR ASN ASP TYR ALA GLU SEQRES 6 C 228 SER VAL LYS SER ARG ILE THR ILE ASN PRO ASP THR SER SEQRES 7 C 228 LYS ASN GLN PHE SER LEU GLN LEU ASN SER VAL THR PRO SEQRES 8 C 228 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER GLY HIS SEQRES 9 C 228 ILE THR VAL PHE GLY VAL ASN VAL ASP ALA PHE ASP MET SEQRES 10 C 228 TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA SER SEQRES 11 C 228 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 C 228 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 C 228 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 C 228 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 C 228 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 C 228 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 C 228 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 C 228 VAL ASP LYS LYS VAL GLU PRO SEQRES 1 D 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER SEQRES 3 D 210 GLN SER LEU SER SER TYR THR HIS TRP TYR GLN GLN LYS SEQRES 4 D 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 D 210 SER ARG GLY SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 210 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 210 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 D 210 ARG THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 D 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 D 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 D 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 D 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 D 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 D 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 D 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 D 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 D 210 GLU CYS HET GLC X 1 11 HET GLC X 2 12 HET GLC I 1 11 HET GLC I 2 12 HET GLC J 1 11 HET GLC J 2 12 HET CIT H 301 13 HET CIT A 301 13 HETNAM GLC ALPHA-D-GLUCOPYRANOSE HETNAM CIT CITRIC ACID HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE FORMUL 9 GLC 6(C6 H12 O6) FORMUL 12 CIT 2(C6 H8 O7) FORMUL 14 HOH *278(H2 O) HELIX 1 AA1 GLN E 61 LYS E 64 5 4 HELIX 2 AA2 THR E 83 SER E 87 5 5 HELIX 3 AA3 VAL E 127 THR E 132 5 6 HELIX 4 AA4 SER E 156 SER E 158 5 3 HELIX 5 AA5 PRO E 200 SER E 203 5 4 HELIX 6 AA6 THR F 28 TYR F 32 5 5 HELIX 7 AA7 GLN F 79 GLU F 83 5 5 HELIX 8 AA8 SER F 122 GLU F 127 1 6 HELIX 9 AA9 ALA F 183 HIS F 189 1 7 HELIX 10 AB1 ALA F 210 CYS F 212 5 3 HELIX 11 AB2 THR G 83 THR G 87 5 5 HELIX 12 AB3 SER G 156 ALA G 158 5 3 HELIX 13 AB4 SER G 187 THR G 191 5 5 HELIX 14 AB5 LYS G 201 ASN G 204 5 4 HELIX 15 AB6 LEU H 29 SER H 31 5 3 HELIX 16 AB7 GLN H 79 PHE H 83 5 5 HELIX 17 AB8 SER H 121 SER H 127 1 7 HELIX 18 AB9 LYS H 183 LYS H 188 1 6 HELIX 19 AC1 GLN A 61 LYS A 64 5 4 HELIX 20 AC2 THR A 83 SER A 87 5 5 HELIX 21 AC3 SER A 156 SER A 158 5 3 HELIX 22 AC4 PRO A 200 SER A 203 5 4 HELIX 23 AC5 THR B 28 TYR B 32 5 5 HELIX 24 AC6 GLN B 79 GLU B 83 5 5 HELIX 25 AC7 SER B 122 GLU B 127 1 6 HELIX 26 AC8 ALA B 183 ARG B 188 1 6 HELIX 27 AC9 ALA B 210 CYS B 212 5 3 HELIX 28 AD1 GLU C 61 LYS C 64 5 4 HELIX 29 AD2 THR C 83 THR C 87 5 5 HELIX 30 AD3 SER C 156 ALA C 158 5 3 HELIX 31 AD4 SER C 187 THR C 191 5 5 HELIX 32 AD5 LYS C 201 ASN C 204 5 4 HELIX 33 AD6 LEU D 29 SER D 31 5 3 HELIX 34 AD7 GLN D 79 PHE D 83 5 5 HELIX 35 AD8 SER D 121 SER D 127 1 7 HELIX 36 AD9 LYS D 183 LYS D 188 1 6 SHEET 1 AA1 4 VAL E 2 GLU E 6 0 SHEET 2 AA1 4 VAL E 18 GLY E 26 -1 O SER E 25 N GLN E 3 SHEET 3 AA1 4 THR E 77 LEU E 82 -1 O ALA E 78 N CYS E 22 SHEET 4 AA1 4 ALA E 67 ASP E 72 -1 N THR E 70 O TYR E 79 SHEET 1 AA2 6 GLU E 10 MET E 12 0 SHEET 2 AA2 6 THR E 107 VAL E 111 1 O THR E 110 N MET E 12 SHEET 3 AA2 6 ALA E 88 LEU E 95 -1 N ALA E 88 O VAL E 109 SHEET 4 AA2 6 ASN E 33 SER E 40 -1 N VAL E 37 O TYR E 91 SHEET 5 AA2 6 SER E 44 ILE E 51 -1 O ILE E 51 N MET E 34 SHEET 6 AA2 6 THR E 57 TYR E 59 -1 O THR E 58 N TYR E 50 SHEET 1 AA3 4 GLU E 10 MET E 12 0 SHEET 2 AA3 4 THR E 107 VAL E 111 1 O THR E 110 N MET E 12 SHEET 3 AA3 4 ALA E 88 LEU E 95 -1 N ALA E 88 O VAL E 109 SHEET 4 AA3 4 PHE E 100A TRP E 103 -1 O VAL E 102 N LYS E 94 SHEET 1 AA4 4 SER E 120 LEU E 124 0 SHEET 2 AA4 4 SER E 135 TYR E 145 -1 O LEU E 141 N TYR E 122 SHEET 3 AA4 4 LEU E 174 THR E 184 -1 O TYR E 175 N TYR E 145 SHEET 4 AA4 4 VAL E 163 THR E 165 -1 N HIS E 164 O SER E 180 SHEET 1 AA5 4 SER E 120 LEU E 124 0 SHEET 2 AA5 4 SER E 135 TYR E 145 -1 O LEU E 141 N TYR E 122 SHEET 3 AA5 4 LEU E 174 THR E 184 -1 O TYR E 175 N TYR E 145 SHEET 4 AA5 4 VAL E 169 GLN E 171 -1 N GLN E 171 O LEU E 174 SHEET 1 AA6 3 THR E 151 TRP E 154 0 SHEET 2 AA6 3 THR E 194 HIS E 199 -1 O ALA E 198 N THR E 151 SHEET 3 AA6 3 THR E 204 LYS E 209 -1 O VAL E 206 N VAL E 197 SHEET 1 AA7 4 VAL F 4 THR F 5 0 SHEET 2 AA7 4 THR F 17 SER F 24 -1 O ARG F 23 N THR F 5 SHEET 3 AA7 4 LYS F 70 THR F 76 -1 O LEU F 73 N LEU F 20 SHEET 4 AA7 4 PHE F 62 ILE F 67 -1 N SER F 65 O ALA F 72 SHEET 1 AA8 6 ALA F 9 THR F 12 0 SHEET 2 AA8 6 THR F 102 VAL F 106 1 O THR F 105 N THR F 12 SHEET 3 AA8 6 ALA F 84 TRP F 91 -1 N ALA F 84 O LEU F 104 SHEET 4 AA8 6 ASN F 34 LYS F 39 -1 N GLU F 38 O ILE F 85 SHEET 5 AA8 6 LEU F 43 GLY F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AA8 6 ASN F 53 ARG F 54 -1 O ASN F 53 N GLY F 49 SHEET 1 AA9 4 ALA F 9 THR F 12 0 SHEET 2 AA9 4 THR F 102 VAL F 106 1 O THR F 105 N THR F 12 SHEET 3 AA9 4 ALA F 84 TRP F 91 -1 N ALA F 84 O LEU F 104 SHEET 4 AA9 4 TRP F 96 PHE F 98 -1 O VAL F 97 N LEU F 90 SHEET 1 AB1 4 SER F 115 LEU F 118 0 SHEET 2 AB1 4 LYS F 130 PHE F 140 -1 O THR F 138 N SER F 115 SHEET 3 AB1 4 TYR F 173 THR F 182 -1 O LEU F 181 N ALA F 131 SHEET 4 AB1 4 MET F 160 THR F 162 -1 N GLU F 161 O TYR F 178 SHEET 1 AB2 4 SER F 115 LEU F 118 0 SHEET 2 AB2 4 LYS F 130 PHE F 140 -1 O THR F 138 N SER F 115 SHEET 3 AB2 4 TYR F 173 THR F 182 -1 O LEU F 181 N ALA F 131 SHEET 4 AB2 4 SER F 166 LYS F 167 -1 N SER F 166 O MET F 174 SHEET 1 AB3 4 THR F 154 PRO F 155 0 SHEET 2 AB3 4 THR F 146 VAL F 151 -1 N VAL F 151 O THR F 154 SHEET 3 AB3 4 SER F 191 HIS F 198 -1 O GLN F 195 N ASP F 148 SHEET 4 AB3 4 HIS F 201 SER F 208 -1 O LEU F 207 N TYR F 192 SHEET 1 AB4 4 GLN G 3 SER G 7 0 SHEET 2 AB4 4 LEU G 18 SER G 25 -1 O ALA G 23 N GLN G 5 SHEET 3 AB4 4 GLN G 77 LEU G 82 -1 O LEU G 82 N LEU G 18 SHEET 4 AB4 4 ILE G 67 ASP G 72 -1 N ASP G 72 O GLN G 77 SHEET 1 AB5 6 LEU G 11 VAL G 12 0 SHEET 2 AB5 6 THR G 107 VAL G 111 1 O THR G 110 N VAL G 12 SHEET 3 AB5 6 ALA G 88 SER G 95 -1 N ALA G 88 O VAL G 109 SHEET 4 AB5 6 VAL G 35 SER G 40 -1 N ILE G 37 O TYR G 91 SHEET 5 AB5 6 GLY G 44 TYR G 52A-1 O GLU G 46 N ARG G 38 SHEET 6 AB5 6 TRP G 55 TYR G 59 -1 O TYR G 56 N TYR G 52 SHEET 1 AB6 4 LEU G 11 VAL G 12 0 SHEET 2 AB6 4 THR G 107 VAL G 111 1 O THR G 110 N VAL G 12 SHEET 3 AB6 4 ALA G 88 SER G 95 -1 N ALA G 88 O VAL G 109 SHEET 4 AB6 4 PHE G 100H TRP G 103 -1 O MET G 102 N ARG G 94 SHEET 1 AB7 2 THR G 99 VAL G 100 0 SHEET 2 AB7 2 VAL G 100C ASN G 100D-1 O VAL G 100C N VAL G 100 SHEET 1 AB8 4 SER G 120 LEU G 124 0 SHEET 2 AB8 4 THR G 135 TYR G 145 -1 O LEU G 141 N PHE G 122 SHEET 3 AB8 4 TYR G 176 PRO G 185 -1 O LEU G 178 N VAL G 142 SHEET 4 AB8 4 VAL G 163 THR G 165 -1 N HIS G 164 O VAL G 181 SHEET 1 AB9 4 SER G 120 LEU G 124 0 SHEET 2 AB9 4 THR G 135 TYR G 145 -1 O LEU G 141 N PHE G 122 SHEET 3 AB9 4 TYR G 176 PRO G 185 -1 O LEU G 178 N VAL G 142 SHEET 4 AB9 4 VAL G 169 LEU G 170 -1 N VAL G 169 O SER G 177 SHEET 1 AC1 3 THR G 151 TRP G 154 0 SHEET 2 AC1 3 ILE G 195 HIS G 200 -1 O ASN G 197 N SER G 153 SHEET 3 AC1 3 THR G 205 LYS G 210 -1 O VAL G 207 N VAL G 198 SHEET 1 AC2 4 THR H 5 SER H 7 0 SHEET 2 AC2 4 VAL H 19 ARG H 24 -1 O THR H 22 N SER H 7 SHEET 3 AC2 4 ASP H 70 ILE H 75 -1 O PHE H 71 N CYS H 23 SHEET 4 AC2 4 PHE H 62 SER H 67 -1 N SER H 65 O THR H 72 SHEET 1 AC3 6 SER H 10 SER H 14 0 SHEET 2 AC3 6 THR H 102 LYS H 107 1 O GLU H 105 N LEU H 11 SHEET 3 AC3 6 ALA H 84 GLN H 90 -1 N ALA H 84 O VAL H 104 SHEET 4 AC3 6 THR H 33 GLN H 38 -1 N TYR H 36 O TYR H 87 SHEET 5 AC3 6 LYS H 45 TYR H 49 -1 O LYS H 45 N GLN H 37 SHEET 6 AC3 6 SER H 53 ARG H 54 -1 O SER H 53 N TYR H 49 SHEET 1 AC4 4 SER H 10 SER H 14 0 SHEET 2 AC4 4 THR H 102 LYS H 107 1 O GLU H 105 N LEU H 11 SHEET 3 AC4 4 ALA H 84 GLN H 90 -1 N ALA H 84 O VAL H 104 SHEET 4 AC4 4 THR H 97 PHE H 98 -1 O THR H 97 N GLN H 90 SHEET 1 AC5 4 SER H 114 PHE H 118 0 SHEET 2 AC5 4 THR H 129 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 AC5 4 TYR H 173 SER H 182 -1 O LEU H 181 N ALA H 130 SHEET 4 AC5 4 SER H 159 VAL H 163 -1 N GLN H 160 O THR H 178 SHEET 1 AC6 4 ALA H 153 LEU H 154 0 SHEET 2 AC6 4 LYS H 145 VAL H 150 -1 N VAL H 150 O ALA H 153 SHEET 3 AC6 4 VAL H 191 THR H 197 -1 O THR H 197 N LYS H 145 SHEET 4 AC6 4 VAL H 205 ASN H 210 -1 O VAL H 205 N VAL H 196 SHEET 1 AC7 4 VAL A 2 GLU A 6 0 SHEET 2 AC7 4 VAL A 18 GLY A 26 -1 O LYS A 23 N GLN A 5 SHEET 3 AC7 4 THR A 77 LEU A 82 -1 O ALA A 78 N CYS A 22 SHEET 4 AC7 4 ALA A 67 ASP A 72 -1 N THR A 70 O TYR A 79 SHEET 1 AC8 6 GLU A 10 MET A 12 0 SHEET 2 AC8 6 THR A 107 VAL A 111 1 O THR A 110 N MET A 12 SHEET 3 AC8 6 ALA A 88 LEU A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AC8 6 ASN A 33 SER A 40 -1 N GLN A 39 O VAL A 89 SHEET 5 AC8 6 SER A 44 ILE A 51 -1 O SER A 44 N SER A 40 SHEET 6 AC8 6 THR A 57 TYR A 59 -1 O THR A 58 N TYR A 50 SHEET 1 AC9 4 GLU A 10 MET A 12 0 SHEET 2 AC9 4 THR A 107 VAL A 111 1 O THR A 110 N MET A 12 SHEET 3 AC9 4 ALA A 88 LEU A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AC9 4 PHE A 100A TRP A 103 -1 O VAL A 102 N LYS A 94 SHEET 1 AD1 4 SER A 120 LEU A 124 0 SHEET 2 AD1 4 SER A 135 TYR A 145 -1 O LEU A 141 N TYR A 122 SHEET 3 AD1 4 LEU A 174 THR A 184 -1 O LEU A 177 N VAL A 142 SHEET 4 AD1 4 VAL A 163 THR A 165 -1 N HIS A 164 O SER A 180 SHEET 1 AD2 4 SER A 120 LEU A 124 0 SHEET 2 AD2 4 SER A 135 TYR A 145 -1 O LEU A 141 N TYR A 122 SHEET 3 AD2 4 LEU A 174 THR A 184 -1 O LEU A 177 N VAL A 142 SHEET 4 AD2 4 VAL A 169 GLN A 171 -1 N GLN A 171 O LEU A 174 SHEET 1 AD3 3 THR A 151 TRP A 154 0 SHEET 2 AD3 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AD3 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AD4 4 VAL B 4 THR B 5 0 SHEET 2 AD4 4 VAL B 18 SER B 24 -1 O ARG B 23 N THR B 5 SHEET 3 AD4 4 LYS B 70 ILE B 75 -1 O LEU B 73 N LEU B 20 SHEET 4 AD4 4 PHE B 62 ILE B 67 -1 N SER B 63 O THR B 74 SHEET 1 AD5 6 ALA B 9 THR B 12 0 SHEET 2 AD5 6 THR B 102 VAL B 106 1 O THR B 105 N LEU B 10 SHEET 3 AD5 6 ALA B 84 TRP B 91 -1 N ALA B 84 O LEU B 104 SHEET 4 AD5 6 ASN B 34 LYS B 39 -1 N GLU B 38 O ILE B 85 SHEET 5 AD5 6 LEU B 43 GLY B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AD5 6 ASN B 53 ARG B 54 -1 O ASN B 53 N GLY B 49 SHEET 1 AD6 4 ALA B 9 THR B 12 0 SHEET 2 AD6 4 THR B 102 VAL B 106 1 O THR B 105 N LEU B 10 SHEET 3 AD6 4 ALA B 84 TRP B 91 -1 N ALA B 84 O LEU B 104 SHEET 4 AD6 4 TRP B 96 PHE B 98 -1 O VAL B 97 N LEU B 90 SHEET 1 AD7 4 SER B 115 PHE B 119 0 SHEET 2 AD7 4 LYS B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AD7 4 TYR B 173 THR B 182 -1 O SER B 177 N CYS B 135 SHEET 4 AD7 4 MET B 160 THR B 162 -1 N GLU B 161 O TYR B 178 SHEET 1 AD8 4 SER B 115 PHE B 119 0 SHEET 2 AD8 4 LYS B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AD8 4 TYR B 173 THR B 182 -1 O SER B 177 N CYS B 135 SHEET 4 AD8 4 SER B 166 LYS B 167 -1 N SER B 166 O MET B 174 SHEET 1 AD9 4 THR B 154 PRO B 155 0 SHEET 2 AD9 4 THR B 146 VAL B 151 -1 N VAL B 151 O THR B 154 SHEET 3 AD9 4 SER B 191 HIS B 198 -1 O THR B 197 N THR B 146 SHEET 4 AD9 4 HIS B 201 SER B 208 -1 O VAL B 203 N VAL B 196 SHEET 1 AE1 4 GLN C 3 SER C 7 0 SHEET 2 AE1 4 LEU C 18 SER C 25 -1 O ALA C 23 N GLN C 5 SHEET 3 AE1 4 GLN C 77 LEU C 82 -1 O PHE C 78 N CYS C 22 SHEET 4 AE1 4 ILE C 67 THR C 68 -1 N THR C 68 O GLN C 81 SHEET 1 AE2 4 GLN C 3 SER C 7 0 SHEET 2 AE2 4 LEU C 18 SER C 25 -1 O ALA C 23 N GLN C 5 SHEET 3 AE2 4 GLN C 77 LEU C 82 -1 O PHE C 78 N CYS C 22 SHEET 4 AE2 4 PRO C 71 ASP C 72 -1 N ASP C 72 O GLN C 77 SHEET 1 AE3 6 LEU C 11 VAL C 12 0 SHEET 2 AE3 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AE3 6 ALA C 88 SER C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AE3 6 VAL C 35 SER C 40 -1 N ILE C 37 O TYR C 91 SHEET 5 AE3 6 GLY C 44 TYR C 52A-1 O GLU C 46 N ARG C 38 SHEET 6 AE3 6 TRP C 55 TYR C 59 -1 O TYR C 56 N TYR C 52 SHEET 1 AE4 4 LEU C 11 VAL C 12 0 SHEET 2 AE4 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AE4 4 ALA C 88 SER C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AE4 4 MET C 102 TRP C 103 -1 O MET C 102 N ARG C 94 SHEET 1 AE5 2 THR C 99 VAL C 100 0 SHEET 2 AE5 2 VAL C 100C ASN C 100D-1 O VAL C 100C N VAL C 100 SHEET 1 AE6 4 SER C 120 LEU C 124 0 SHEET 2 AE6 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124 SHEET 3 AE6 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AE6 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AE7 4 SER C 120 LEU C 124 0 SHEET 2 AE7 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124 SHEET 3 AE7 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AE7 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AE8 3 THR C 151 TRP C 154 0 SHEET 2 AE8 3 ILE C 195 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AE8 3 THR C 205 LYS C 210 -1 O VAL C 207 N VAL C 198 SHEET 1 AE9 4 THR D 5 SER D 7 0 SHEET 2 AE9 4 VAL D 19 ARG D 24 -1 O ARG D 24 N THR D 5 SHEET 3 AE9 4 ASP D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AE9 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AF1 6 SER D 10 SER D 14 0 SHEET 2 AF1 6 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AF1 6 ALA D 84 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AF1 6 THR D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AF1 6 LYS D 45 TYR D 49 -1 O ILE D 48 N TRP D 35 SHEET 6 AF1 6 SER D 53 ARG D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AF2 4 SER D 10 SER D 14 0 SHEET 2 AF2 4 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AF2 4 ALA D 84 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AF2 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AF3 4 SER D 114 PHE D 118 0 SHEET 2 AF3 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AF3 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AF3 4 SER D 159 VAL D 163 -1 N SER D 162 O SER D 176 SHEET 1 AF4 4 ALA D 153 LEU D 154 0 SHEET 2 AF4 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AF4 4 VAL D 191 THR D 197 -1 O THR D 197 N LYS D 145 SHEET 4 AF4 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SSBOND 1 CYS E 22 CYS E 92 1555 1555 2.12 SSBOND 2 CYS E 140 CYS E 195 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 88 1555 1555 2.07 SSBOND 4 CYS F 135 CYS F 194 1555 1555 2.04 SSBOND 5 CYS G 22 CYS G 92 1555 1555 2.20 SSBOND 6 CYS G 140 CYS G 196 1555 1555 2.04 SSBOND 7 CYS H 23 CYS H 88 1555 1555 2.04 SSBOND 8 CYS H 134 CYS H 194 1555 1555 2.06 SSBOND 9 CYS A 22 CYS A 92 1555 1555 2.07 SSBOND 10 CYS A 140 CYS A 195 1555 1555 2.06 SSBOND 11 CYS B 22 CYS B 88 1555 1555 2.03 SSBOND 12 CYS B 135 CYS B 194 1555 1555 2.06 SSBOND 13 CYS C 22 CYS C 92 1555 1555 2.19 SSBOND 14 CYS C 140 CYS C 196 1555 1555 2.02 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 16 CYS D 134 CYS D 194 1555 1555 2.07 LINK C1 GLC X 1 O1 GLC X 2 1555 1555 1.40 LINK C1 GLC I 1 O1 GLC I 2 1555 1555 1.41 LINK C1 GLC J 1 O1 GLC J 2 1555 1555 1.40 CISPEP 1 PHE E 146 PRO E 147 0 -2.58 CISPEP 2 GLU E 148 PRO E 149 0 6.63 CISPEP 3 TRP E 188 PRO E 189 0 9.72 CISPEP 4 TYR F 141 PRO F 142 0 -1.63 CISPEP 5 PHE G 146 PRO G 147 0 -8.78 CISPEP 6 GLU G 148 PRO G 149 0 -6.34 CISPEP 7 SER H 7 PRO H 8 0 -0.15 CISPEP 8 TYR H 140 PRO H 141 0 0.13 CISPEP 9 PHE A 146 PRO A 147 0 -9.54 CISPEP 10 GLU A 148 PRO A 149 0 8.37 CISPEP 11 TRP A 188 PRO A 189 0 4.98 CISPEP 12 TYR B 141 PRO B 142 0 2.47 CISPEP 13 PHE C 146 PRO C 147 0 -5.99 CISPEP 14 GLU C 148 PRO C 149 0 -6.93 CISPEP 15 SER D 7 PRO D 8 0 -4.52 CISPEP 16 TYR D 140 PRO D 141 0 -2.45 CRYST1 84.283 151.111 176.368 90.00 90.00 90.00 P 21 21 21 8 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 0.011865 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006618 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005670 0.00000