HEADER IMMUNE SYSTEM 04-JAN-23 8FPA TITLE STRUCTURE OF A CHIMERIC ANTIBODY (FAB) FRAGMENT BOUND TO DE-N-ACETYL TITLE 2 POLYSIALIC ACID (DPSA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERIC ANTIBODY FAB FRAGMENT, FD CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HUMANIZED ANTIBODY FAB FRAGMENT, LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, FAB, POLYSIALIC ACID, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.T.BEERNINK,J.AGIRRE,B.P.BEERNINK,G.R.MOE REVDAT 1 18-MAR-26 8FPA 0 JRNL AUTH P.T.BEERNINK,J.AGIRRE,B.P.BEERNINK,G.R.MOE JRNL TITL STRUCTURE OF DE-N-ACETYL POLYSIALIC ACID BOUND TO AN JRNL TITL 2 ANTIBODY FAB FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.83 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SERVALCAT 0.4.105 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.49 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 84628 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1458 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.83 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12061 REMARK 3 BIN R VALUE (WORKING SET) : 0.3013 REMARK 3 BIN FREE R VALUE : 0.3567 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 206 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6565 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 263 REMARK 3 SOLVENT ATOMS : 407 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.59 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.29 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.90317 REMARK 3 B22 (A**2) : -1.75152 REMARK 3 B33 (A**2) : -1.15165 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.27503 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8FPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-23. REMARK 100 THE DEPOSITION ID IS D_1000269548. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.3.1 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 PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84628 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830 REMARK 200 RESOLUTION RANGE LOW (A) : 74.490 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.08100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.19.2 REMARK 200 STARTING MODEL: 6PE7 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.23 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 24% POLYETHYLENE GLYCOL 1,500; 20% REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.71850 REMARK 290 SMTRY3 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F 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 LYS A 220 REMARK 465 SER A 221 REMARK 465 CYS A 222 REMARK 465 ASP A 223 REMARK 465 LYS A 224 REMARK 465 THR A 225 REMARK 465 HIS A 226 REMARK 465 GLY B 217 REMARK 465 GLU B 218 REMARK 465 CYS B 219 REMARK 465 LYS C 220 REMARK 465 SER C 221 REMARK 465 CYS C 222 REMARK 465 ASP C 223 REMARK 465 LYS C 224 REMARK 465 THR C 225 REMARK 465 HIS C 226 REMARK 465 LEU D 159 REMARK 465 GLN D 160 REMARK 465 SER D 161 REMARK 465 GLY D 162 REMARK 465 ASN D 163 REMARK 465 GLY D 217 REMARK 465 GLU D 218 REMARK 465 CYS D 219 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 LYS B 108 CG CD CE NZ REMARK 470 GLN D 152 CG CD OE1 NE2 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 TYR A 33 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 TYR A 33 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 TYR C 33 CB - CG - CD1 ANGL. DEV. = 3.9 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 ALA A 102 145.08 -170.83 REMARK 500 ASP A 150 61.36 64.71 REMARK 500 THR A 166 -43.98 -133.69 REMARK 500 TYR B 37 57.41 -95.19 REMARK 500 VAL B 56 -54.24 77.08 REMARK 500 ARG B 82 118.01 -161.79 REMARK 500 ASN B 157 10.70 56.57 REMARK 500 LYS C 43 -167.62 -123.21 REMARK 500 SER C 79 55.31 27.63 REMARK 500 ASP C 150 62.18 71.06 REMARK 500 TYR D 37 58.92 -95.58 REMARK 500 VAL D 56 -53.11 79.14 REMARK 500 ASN D 157 53.61 12.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 103 0.07 SIDE CHAIN REMARK 500 ARG C 103 0.07 SIDE CHAIN REMARK 500 ARG D 66 0.08 SIDE CHAIN REMARK 500 ARG D 216 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8FPA A 1 226 PDB 8FPA 8FPA 1 226 DBREF 8FPA B 1 219 PDB 8FPA 8FPA 1 219 DBREF 8FPA C 1 226 PDB 8FPA 8FPA 1 226 DBREF 8FPA D 1 219 PDB 8FPA 8FPA 1 219 SEQRES 1 A 226 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 226 PRO GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 226 PHE THR PHE THR PRO TYR TYR MET GLY TRP VAL ARG GLN SEQRES 4 A 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY TYR ILE ARG SEQRES 5 A 226 ASN LYS ALA ASN GLY TYR THR THR GLU TYR SER ALA SER SEQRES 6 A 226 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER GLN SEQRES 7 A 226 SER SER LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 A 226 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR ALA ARG GLY SEQRES 9 A 226 THR VAL ASP SER TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 A 226 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 A 226 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 A 226 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 A 226 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 A 226 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 A 226 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 A 226 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 A 226 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 A 226 CYS ASP LYS THR HIS SEQRES 1 B 219 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 B 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 B 219 GLN SER LEU LEU HIS SER ASN GLY LYS THR TYR LEU ASN SEQRES 4 B 219 TRP LEU LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 B 219 ILE TYR LEU VAL SER LYS LEU GLU SER GLY VAL PRO ASP SEQRES 6 B 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY LEU TYR SEQRES 8 B 219 TYR CYS LEU GLN ILE ILE HIS PHE PRO HIS THR PHE GLY SEQRES 9 B 219 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 B 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 B 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 226 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 226 PRO GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 226 PHE THR PHE THR PRO TYR TYR MET GLY TRP VAL ARG GLN SEQRES 4 C 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY TYR ILE ARG SEQRES 5 C 226 ASN LYS ALA ASN GLY TYR THR THR GLU TYR SER ALA SER SEQRES 6 C 226 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER GLN SEQRES 7 C 226 SER SER LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 C 226 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR ALA ARG GLY SEQRES 9 C 226 THR VAL ASP SER TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 C 226 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 C 226 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 C 226 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 C 226 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 C 226 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 C 226 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 C 226 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 C 226 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 C 226 CYS ASP LYS THR HIS SEQRES 1 D 219 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 D 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 D 219 GLN SER LEU LEU HIS SER ASN GLY LYS THR TYR LEU ASN SEQRES 4 D 219 TRP LEU LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 D 219 ILE TYR LEU VAL SER LYS LEU GLU SER GLY VAL PRO ASP SEQRES 6 D 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 D 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY LEU TYR SEQRES 8 D 219 TYR CYS LEU GLN ILE ILE HIS PHE PRO HIS THR PHE GLY SEQRES 9 D 219 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 D 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 D 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 D 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 D 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 D 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 D 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 D 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 D 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET Y8W E 1 37 HET 18D E 2 36 HET 18D E 3 36 HET Y98 E 4 26 HET Y8W F 1 37 HET 18D F 2 36 HET 18D F 3 36 HET Y98 F 4 26 HET ACY A 301 4 HET ACY A 302 4 HET GOL A 303 11 HET PEG A 304 15 HET PEG A 305 15 HET GOL B 301 11 HET GOL B 302 11 HET GOL B 303 11 HET GOL B 304 11 HET GOL B 305 11 HET GOL B 306 11 HET ACY B 307 4 HET GOL C 301 11 HET ACY C 302 4 HET GOL D 301 11 HET GOL D 302 11 HET PEG D 303 15 HET ACY D 304 4 HETNAM Y8W 3,5-DIDEOXY-5-PROPANAMIDO-D-GLYCERO-D-GALACTO-NON-2- HETNAM 2 Y8W ULOSONIC ACID HETNAM 18D 3,5-DIDEOXY-5-(PROPANOYLAMINO)-D-GLYCERO-ALPHA-D- HETNAM 2 18D GALACTO-NON-2-ULOPYRANOSONIC ACID HETNAM Y98 5-AMINO-3,5-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-NON-2- HETNAM 2 Y98 ULOPYRANOSONIC ACID HETNAM ACY ACETIC ACID HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN 18D 3,5-DIDEOXY-5-(PROPANOYLAMINO)-D-GLYCERO-ALPHA-D- HETSYN 2 18D GALACTO-NON-2-ULOSONIC ACID; 3,5-DIDEOXY-5- HETSYN 3 18D (PROPANOYLAMINO)-D-GLYCERO-D-GALACTO-NON-2-ULOSONIC HETSYN 4 18D ACID; 3,5-DIDEOXY-5-(PROPANOYLAMINO)-D-GLYCERO- HETSYN 5 18D GALACTO-NON-2-ULOSONIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 Y8W 2(C12 H21 N O9) FORMUL 5 18D 4(C12 H21 N O9) FORMUL 5 Y98 2(C9 H17 N O8) FORMUL 7 ACY 5(C2 H4 O2) FORMUL 9 GOL 10(C3 H8 O3) FORMUL 10 PEG 3(C4 H10 O3) FORMUL 25 HOH *407(H2 O) HELIX 1 AA1 ASN A 53 GLY A 57 5 5 HELIX 2 AA2 ASN A 76 GLN A 78 5 3 HELIX 3 AA3 LYS A 89 THR A 93 5 5 HELIX 4 AA4 SER A 133 LYS A 135 5 3 HELIX 5 AA5 SER A 162 ALA A 164 5 3 HELIX 6 AA6 SER A 193 LEU A 195 5 3 HELIX 7 AA7 LYS A 207 ASN A 210 5 4 HELIX 8 AA8 GLU B 84 LEU B 88 5 5 HELIX 9 AA9 SER B 126 SER B 132 1 7 HELIX 10 AB1 LYS B 188 HIS B 194 1 7 HELIX 11 AB2 ASN C 53 GLY C 57 5 5 HELIX 12 AB3 ASN C 76 GLN C 78 5 3 HELIX 13 AB4 LYS C 89 THR C 93 5 5 HELIX 14 AB5 SER C 133 LYS C 135 5 3 HELIX 15 AB6 SER C 162 ALA C 164 5 3 HELIX 16 AB7 SER C 193 THR C 197 5 5 HELIX 17 AB8 LYS C 207 ASN C 210 5 4 HELIX 18 AB9 GLU D 84 LEU D 88 5 5 HELIX 19 AC1 SER D 126 SER D 132 1 7 HELIX 20 AC2 LYS D 188 LYS D 193 1 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 SER A 80 MET A 85 -1 O MET A 85 N LEU A 18 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N THR A 71 O GLN A 84 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 113 VAL A 117 1 O THR A 116 N VAL A 12 SHEET 3 AA2 6 ALA A 94 ALA A 102 -1 N TYR A 96 O THR A 113 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 97 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O GLU A 61 N TYR A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 113 VAL A 117 1 O THR A 116 N VAL A 12 SHEET 3 AA3 4 ALA A 94 ALA A 102 -1 N TYR A 96 O THR A 113 SHEET 4 AA3 4 THR A 105 TRP A 109 -1 O THR A 105 N ALA A 102 SHEET 1 AA4 4 SER A 126 LEU A 130 0 SHEET 2 AA4 4 THR A 141 TYR A 151 -1 O LEU A 147 N PHE A 128 SHEET 3 AA4 4 TYR A 182 PRO A 191 -1 O LEU A 184 N VAL A 148 SHEET 4 AA4 4 VAL A 169 THR A 171 -1 N HIS A 170 O VAL A 187 SHEET 1 AA5 4 THR A 137 SER A 138 0 SHEET 2 AA5 4 THR A 141 TYR A 151 -1 O THR A 141 N SER A 138 SHEET 3 AA5 4 TYR A 182 PRO A 191 -1 O LEU A 184 N VAL A 148 SHEET 4 AA5 4 VAL A 175 LEU A 176 -1 N VAL A 175 O SER A 183 SHEET 1 AA6 3 THR A 157 TRP A 160 0 SHEET 2 AA6 3 ILE A 201 HIS A 206 -1 O ASN A 203 N SER A 159 SHEET 3 AA6 3 THR A 211 LYS A 216 -1 O VAL A 213 N VAL A 204 SHEET 1 AA7 4 MET B 4 THR B 7 0 SHEET 2 AA7 4 ALA B 19 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA7 4 ASP B 75 ILE B 80 -1 O LEU B 78 N ILE B 21 SHEET 4 AA7 4 PHE B 67 SER B 72 -1 N SER B 68 O LYS B 79 SHEET 1 AA8 6 SER B 10 VAL B 13 0 SHEET 2 AA8 6 THR B 107 ILE B 111 1 O LYS B 108 N LEU B 11 SHEET 3 AA8 6 GLY B 89 GLN B 95 -1 N GLY B 89 O VAL B 109 SHEET 4 AA8 6 LEU B 38 GLN B 43 -1 N GLN B 43 O LEU B 90 SHEET 5 AA8 6 GLN B 50 TYR B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA8 6 LYS B 58 LEU B 59 -1 O LYS B 58 N TYR B 54 SHEET 1 AA9 4 SER B 10 VAL B 13 0 SHEET 2 AA9 4 THR B 107 ILE B 111 1 O LYS B 108 N LEU B 11 SHEET 3 AA9 4 GLY B 89 GLN B 95 -1 N GLY B 89 O VAL B 109 SHEET 4 AA9 4 THR B 102 PHE B 103 -1 O THR B 102 N GLN B 95 SHEET 1 AB1 4 SER B 119 PHE B 123 0 SHEET 2 AB1 4 THR B 134 PHE B 144 -1 O ASN B 142 N SER B 119 SHEET 3 AB1 4 TYR B 178 SER B 187 -1 O TYR B 178 N PHE B 144 SHEET 4 AB1 4 SER B 164 VAL B 168 -1 N GLN B 165 O THR B 183 SHEET 1 AB2 4 ALA B 158 LEU B 159 0 SHEET 2 AB2 4 LYS B 150 VAL B 155 -1 N VAL B 155 O ALA B 158 SHEET 3 AB2 4 VAL B 196 THR B 202 -1 O GLU B 200 N GLN B 152 SHEET 4 AB2 4 VAL B 210 ASN B 215 -1 O VAL B 210 N VAL B 201 SHEET 1 AB3 4 GLN C 3 SER C 7 0 SHEET 2 AB3 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AB3 4 SER C 80 MET C 85 -1 O MET C 85 N LEU C 18 SHEET 4 AB3 4 PHE C 70 ASP C 75 -1 N THR C 71 O GLN C 84 SHEET 1 AB4 6 LEU C 11 VAL C 12 0 SHEET 2 AB4 6 THR C 113 VAL C 117 1 O THR C 116 N VAL C 12 SHEET 3 AB4 6 ALA C 94 ALA C 102 -1 N TYR C 96 O THR C 113 SHEET 4 AB4 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 97 SHEET 5 AB4 6 GLU C 46 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 6 AB4 6 THR C 60 TYR C 62 -1 O GLU C 61 N TYR C 50 SHEET 1 AB5 4 LEU C 11 VAL C 12 0 SHEET 2 AB5 4 THR C 113 VAL C 117 1 O THR C 116 N VAL C 12 SHEET 3 AB5 4 ALA C 94 ALA C 102 -1 N TYR C 96 O THR C 113 SHEET 4 AB5 4 THR C 105 TRP C 109 -1 O THR C 105 N ALA C 102 SHEET 1 AB6 4 SER C 126 LEU C 130 0 SHEET 2 AB6 4 THR C 141 TYR C 151 -1 O GLY C 145 N LEU C 130 SHEET 3 AB6 4 TYR C 182 PRO C 191 -1 O TYR C 182 N TYR C 151 SHEET 4 AB6 4 VAL C 169 THR C 171 -1 N HIS C 170 O VAL C 187 SHEET 1 AB7 4 THR C 137 SER C 138 0 SHEET 2 AB7 4 THR C 141 TYR C 151 -1 O THR C 141 N SER C 138 SHEET 3 AB7 4 TYR C 182 PRO C 191 -1 O TYR C 182 N TYR C 151 SHEET 4 AB7 4 VAL C 175 LEU C 176 -1 N VAL C 175 O SER C 183 SHEET 1 AB8 3 THR C 157 TRP C 160 0 SHEET 2 AB8 3 ILE C 201 HIS C 206 -1 O ASN C 203 N SER C 159 SHEET 3 AB8 3 THR C 211 LYS C 216 -1 O VAL C 213 N VAL C 204 SHEET 1 AB9 4 MET D 4 THR D 7 0 SHEET 2 AB9 4 ALA D 19 SER D 25 -1 O LYS D 24 N THR D 5 SHEET 3 AB9 4 ASP D 75 ILE D 80 -1 O LEU D 78 N ILE D 21 SHEET 4 AB9 4 PHE D 67 SER D 72 -1 N SER D 68 O LYS D 79 SHEET 1 AC1 6 SER D 10 VAL D 13 0 SHEET 2 AC1 6 THR D 107 ILE D 111 1 O GLU D 110 N VAL D 13 SHEET 3 AC1 6 GLY D 89 GLN D 95 -1 N GLY D 89 O VAL D 109 SHEET 4 AC1 6 LEU D 38 GLN D 43 -1 N GLN D 43 O LEU D 90 SHEET 5 AC1 6 GLN D 50 TYR D 54 -1 O LEU D 52 N TRP D 40 SHEET 6 AC1 6 LYS D 58 LEU D 59 -1 O LYS D 58 N TYR D 54 SHEET 1 AC2 4 SER D 10 VAL D 13 0 SHEET 2 AC2 4 THR D 107 ILE D 111 1 O GLU D 110 N VAL D 13 SHEET 3 AC2 4 GLY D 89 GLN D 95 -1 N GLY D 89 O VAL D 109 SHEET 4 AC2 4 THR D 102 PHE D 103 -1 O THR D 102 N GLN D 95 SHEET 1 AC3 4 SER D 119 PHE D 123 0 SHEET 2 AC3 4 THR D 134 PHE D 144 -1 O ASN D 142 N SER D 119 SHEET 3 AC3 4 TYR D 178 SER D 187 -1 O SER D 182 N CYS D 139 SHEET 4 AC3 4 GLN D 165 VAL D 168 -1 N GLN D 165 O THR D 183 SHEET 1 AC4 3 LYS D 150 VAL D 155 0 SHEET 2 AC4 3 VAL D 196 THR D 202 -1 O GLU D 200 N GLN D 152 SHEET 3 AC4 3 VAL D 210 ASN D 215 -1 O VAL D 210 N VAL D 201 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.22 SSBOND 2 CYS A 146 CYS A 202 1555 1555 2.10 SSBOND 3 CYS B 23 CYS B 93 1555 1555 2.17 SSBOND 4 CYS B 139 CYS B 199 1555 1555 1.93 SSBOND 5 CYS C 22 CYS C 98 1555 1555 2.20 SSBOND 6 CYS C 146 CYS C 202 1555 1555 2.11 SSBOND 7 CYS D 23 CYS D 93 1555 1555 2.12 SSBOND 8 CYS D 139 CYS D 199 1555 1555 1.99 LINK O9 Y8W E 1 C2 18D E 2 1555 1555 1.43 LINK O8 18D E 2 C2 18D E 3 1555 1555 1.43 LINK O8 18D E 3 C2 Y98 E 4 1555 1555 1.45 LINK O9 Y8W F 1 C2 18D F 2 1555 1555 1.41 LINK O8 18D F 2 C2 18D F 3 1555 1555 1.41 LINK O8 18D F 3 C2 Y98 F 4 1555 1555 1.48 CISPEP 1 PHE A 152 PRO A 153 0 -10.75 CISPEP 2 GLU A 154 PRO A 155 0 -6.12 CISPEP 3 THR B 7 PRO B 8 0 -13.60 CISPEP 4 PHE B 99 PRO B 100 0 -10.56 CISPEP 5 TYR B 145 PRO B 146 0 4.42 CISPEP 6 PHE C 152 PRO C 153 0 -8.90 CISPEP 7 GLU C 154 PRO C 155 0 -2.91 CISPEP 8 THR D 7 PRO D 8 0 -18.33 CISPEP 9 PHE D 99 PRO D 100 0 -12.69 CISPEP 10 TYR D 145 PRO D 146 0 5.71 CRYST1 74.585 71.437 91.495 90.00 92.95 90.00 P 1 21 1 4 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 0.013408 0.000000 0.000692 0.00000 SCALE2 0.000000 0.013998 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010944 0.00000