HEADER ANTITUMOR PROTEIN 12-APR-24 9BDO TITLE CRYSTAL STRUCTURE OF ANTI-ABTCR NANOBODY VHH COMPND MOL_ID: 1; COMPND 2 MOLECULE: TCE01 NANOBODY VHH; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922 KEYWDS NANOBODY, VHH, ANTIBODY, TCR, ANTITUMOR PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.QIU REVDAT 1 16-APR-25 9BDO 0 JRNL AUTH P.MEONI,A.P.VINTEM,V.CORTEZ-RETAMOZO,J.JACOBS, JRNL AUTH 2 E.DE TAVERNIER,P.FIORENTINI,D.VAN HOORICK,J.D.BATCHELOR, JRNL AUTH 3 E.SVIDRITSKIY,Y.QIU,E.DEJONCKHEERE,A.LI,L.I.PAO,M.A.BUYSE JRNL TITL IDENTIFICATION AND NON-CLINICAL CHARACTERIZATION OF JRNL TITL 2 SAR444200, A NOVEL ANTI-GPC3 NANOBODY T CELL ENGAGER, FOR JRNL TITL 3 THE TREATMENT OF GPC3+ SOLID TUMORS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.7 (19-MAR-2020) REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.06 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 26611 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870 REMARK 3 FREE R VALUE TEST SET COUNT : 1296 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 : 51 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.96 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.44 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 533 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2220 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 506 REMARK 3 BIN R VALUE (WORKING SET) : 0.2215 REMARK 3 BIN FREE R VALUE : 0.2330 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 2718 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 35 REMARK 3 SOLVENT ATOMS : 155 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.45 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.15690 REMARK 3 B22 (A**2) : -12.80680 REMARK 3 B33 (A**2) : 5.64990 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 9.42060 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.181 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.154 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.182 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.156 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 2812 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 3809 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 934 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 475 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 2812 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 344 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 2299 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.00 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.60 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.48 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 24.8865 8.9379 12.4403 REMARK 3 T TENSOR REMARK 3 T11: -0.0943 T22: 0.0029 REMARK 3 T33: -0.0525 T12: -0.0284 REMARK 3 T13: -0.0359 T23: 0.0461 REMARK 3 L TENSOR REMARK 3 L11: 4.5802 L22: 2.6279 REMARK 3 L33: 3.3214 L12: 1.6859 REMARK 3 L13: 1.6943 L23: 0.5463 REMARK 3 S TENSOR REMARK 3 S11: -0.0710 S12: -0.0601 S13: 0.2030 REMARK 3 S21: -0.1523 S22: 0.0816 S23: 0.2707 REMARK 3 S31: -0.0703 S32: -0.3032 S33: -0.0106 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): -4.3391 26.0919 13.3038 REMARK 3 T TENSOR REMARK 3 T11: -0.0376 T22: -0.0272 REMARK 3 T33: -0.1118 T12: 0.0349 REMARK 3 T13: -0.0789 T23: -0.0854 REMARK 3 L TENSOR REMARK 3 L11: 6.9407 L22: 2.2025 REMARK 3 L33: 7.2074 L12: -0.5076 REMARK 3 L13: 5.0383 L23: -0.3821 REMARK 3 S TENSOR REMARK 3 S11: 0.3444 S12: 0.7479 S13: -0.3826 REMARK 3 S21: -0.3426 S22: 0.0602 S23: 0.0245 REMARK 3 S31: 0.5391 S32: 0.7622 S33: -0.4046 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 2.6119 -8.2586 13.4234 REMARK 3 T TENSOR REMARK 3 T11: -0.0805 T22: -0.0151 REMARK 3 T33: -0.1226 T12: -0.0385 REMARK 3 T13: -0.0123 T23: 0.0228 REMARK 3 L TENSOR REMARK 3 L11: 7.8649 L22: 2.2288 REMARK 3 L33: 3.6289 L12: 1.3329 REMARK 3 L13: 2.0323 L23: 0.0936 REMARK 3 S TENSOR REMARK 3 S11: -0.0443 S12: -0.0758 S13: 0.1708 REMARK 3 S21: 0.0708 S22: -0.1103 S23: -0.0297 REMARK 3 S31: -0.1640 S32: 0.1059 S33: 0.1547 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9BDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-24. REMARK 100 THE DEPOSITION ID IS D_1000283141. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-DEC-19 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 : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0334 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26641 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.948 REMARK 200 RESOLUTION RANGE LOW (A) : 57.120 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.10000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.73100 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M LI2SO4, 10 MM TRIMETHYLTMAMINE, REMARK 280 90 MM NAAC (PH 4.4), AND 27% (W/V) PEG8000., VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 48.47450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.36250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.47450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.36250 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, 3 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 ASP A 61 REMARK 465 GLY B 54 REMARK 465 ASP B 55 REMARK 465 ASP B 61 REMARK 465 SER B 62 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 B 56 CG CD OE1 NE2 REMARK 470 ASP B 58 CG OD1 OD2 REMARK 470 LYS B 64 CG CD CE NZ 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 ASP A 55 64.58 73.46 REMARK 500 LYS A 64 88.74 -64.38 REMARK 500 TYR A 104 -32.95 66.47 REMARK 500 TYR B 104 -37.88 67.09 REMARK 500 ILE C 53 104.01 -59.43 REMARK 500 TYR C 104 -37.25 63.28 REMARK 500 REMARK 500 REMARK: NULL DBREF 9BDO A 1 117 PDB 9BDO 9BDO 1 117 DBREF 9BDO B 1 117 PDB 9BDO 9BDO 1 117 DBREF 9BDO C 1 117 PDB 9BDO 9BDO 1 117 SEQRES 1 A 117 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 117 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 A 117 TYR VAL HIS LYS ILE ASN PHE TYR GLY TRP TYR ARG GLN SEQRES 4 A 117 ALA PRO GLY LYS GLU ARG GLU LYS VAL ALA HIS ILE SER SEQRES 5 A 117 ILE GLY ASP GLN THR ASP TYR ALA ASP SER ALA LYS GLY SEQRES 6 A 117 ARG PHE THR ILE SER ARG ASP GLU SER LYS ASN THR VAL SEQRES 7 A 117 TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP THR ALA SEQRES 8 A 117 ALA TYR TYR CYS ARG ALA LEU SER ARG ILE TRP PRO TYR SEQRES 9 A 117 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 B 117 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 B 117 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 B 117 TYR VAL HIS LYS ILE ASN PHE TYR GLY TRP TYR ARG GLN SEQRES 4 B 117 ALA PRO GLY LYS GLU ARG GLU LYS VAL ALA HIS ILE SER SEQRES 5 B 117 ILE GLY ASP GLN THR ASP TYR ALA ASP SER ALA LYS GLY SEQRES 6 B 117 ARG PHE THR ILE SER ARG ASP GLU SER LYS ASN THR VAL SEQRES 7 B 117 TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP THR ALA SEQRES 8 B 117 ALA TYR TYR CYS ARG ALA LEU SER ARG ILE TRP PRO TYR SEQRES 9 B 117 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 C 117 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 117 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 C 117 TYR VAL HIS LYS ILE ASN PHE TYR GLY TRP TYR ARG GLN SEQRES 4 C 117 ALA PRO GLY LYS GLU ARG GLU LYS VAL ALA HIS ILE SER SEQRES 5 C 117 ILE GLY ASP GLN THR ASP TYR ALA ASP SER ALA LYS GLY SEQRES 6 C 117 ARG PHE THR ILE SER ARG ASP GLU SER LYS ASN THR VAL SEQRES 7 C 117 TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP THR ALA SEQRES 8 C 117 ALA TYR TYR CYS ARG ALA LEU SER ARG ILE TRP PRO TYR SEQRES 9 C 117 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER HET SO4 A 201 5 HET SO4 A 202 5 HET GOL C 201 6 HET ACT C 202 4 HET GOL C 203 6 HET ACT C 204 4 HET SO4 C 205 5 HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL HETNAM ACT ACETATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 SO4 3(O4 S 2-) FORMUL 6 GOL 2(C3 H8 O3) FORMUL 7 ACT 2(C2 H3 O2 1-) FORMUL 11 HOH *155(H2 O) HELIX 1 AA1 ALA A 63 ARG A 66 1 4 HELIX 2 AA2 GLU A 73 LYS A 75 5 3 HELIX 3 AA3 ARG A 86 THR A 90 5 5 HELIX 4 AA4 GLU B 73 LYS B 75 5 3 HELIX 5 AA5 ARG B 86 THR B 90 5 5 HELIX 6 AA6 ASP C 61 LYS C 64 5 4 HELIX 7 AA7 GLU C 73 LYS C 75 5 3 HELIX 8 AA8 ARG C 86 THR C 90 5 5 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 LEU A 18 ALA A 24 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 111 VAL A 115 1 O THR A 114 N VAL A 12 SHEET 3 AA2 6 ALA A 91 SER A 99 -1 N TYR A 93 O THR A 111 SHEET 4 AA2 6 ILE A 31 GLN A 39 -1 N TYR A 37 O TYR A 94 SHEET 5 AA2 6 GLU A 46 SER A 52 -1 O ALA A 49 N TRP A 36 SHEET 6 AA2 6 GLN A 56 TYR A 59 -1 O ASP A 58 N HIS A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 111 VAL A 115 1 O THR A 114 N VAL A 12 SHEET 3 AA3 4 ALA A 91 SER A 99 -1 N TYR A 93 O THR A 111 SHEET 4 AA3 4 ASP A 105 TRP A 107 -1 O TYR A 106 N ALA A 97 SHEET 1 AA4 4 LEU B 4 SER B 7 0 SHEET 2 AA4 4 LEU B 18 ALA B 24 -1 O VAL B 23 N VAL B 5 SHEET 3 AA4 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA4 4 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA5 6 VAL B 11 VAL B 12 0 SHEET 2 AA5 6 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA5 6 ALA B 91 SER B 99 -1 N TYR B 93 O THR B 111 SHEET 4 AA5 6 ILE B 31 GLN B 39 -1 N TYR B 37 O TYR B 94 SHEET 5 AA5 6 GLU B 46 SER B 52 -1 O ALA B 49 N TRP B 36 SHEET 6 AA5 6 THR B 57 TYR B 59 -1 O ASP B 58 N HIS B 50 SHEET 1 AA6 4 VAL B 11 VAL B 12 0 SHEET 2 AA6 4 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA6 4 ALA B 91 SER B 99 -1 N TYR B 93 O THR B 111 SHEET 4 AA6 4 ASP B 105 TRP B 107 -1 O TYR B 106 N ALA B 97 SHEET 1 AA7 4 LEU C 4 SER C 7 0 SHEET 2 AA7 4 LEU C 18 ALA C 24 -1 O VAL C 23 N VAL C 5 SHEET 3 AA7 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA7 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AA8 6 GLY C 10 VAL C 12 0 SHEET 2 AA8 6 THR C 111 VAL C 115 1 O THR C 114 N VAL C 12 SHEET 3 AA8 6 ALA C 91 SER C 99 -1 N TYR C 93 O THR C 111 SHEET 4 AA8 6 ILE C 31 GLN C 39 -1 N TYR C 37 O TYR C 94 SHEET 5 AA8 6 GLU C 46 SER C 52 -1 O GLU C 46 N ARG C 38 SHEET 6 AA8 6 GLN C 56 TYR C 59 -1 O GLN C 56 N SER C 52 SHEET 1 AA9 4 GLY C 10 VAL C 12 0 SHEET 2 AA9 4 THR C 111 VAL C 115 1 O THR C 114 N VAL C 12 SHEET 3 AA9 4 ALA C 91 SER C 99 -1 N TYR C 93 O THR C 111 SHEET 4 AA9 4 ASP C 105 TRP C 107 -1 O TYR C 106 N ALA C 97 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.04 SSBOND 2 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 3 CYS C 22 CYS C 95 1555 1555 2.05 CISPEP 1 TRP A 102 PRO A 103 0 8.63 CISPEP 2 TRP B 102 PRO B 103 0 9.69 CISPEP 3 TRP C 102 PRO C 103 0 13.60 CRYST1 96.949 70.725 54.403 90.00 94.86 90.00 C 1 2 1 12 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 0.010315 0.000000 0.000877 0.00000 SCALE2 0.000000 0.014139 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018448 0.00000