HEADER PROTEIN BINDING 17-APR-25 9O9C TITLE STRUCTURE OF THE IL-18 SURROGATE CYTOKINE AGONIST DR3085 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IL-18 SURROGATE CYTOKINE AGONIST DR3085; COMPND 3 CHAIN: B, A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_COMMON: LLAMA; SOURCE 4 ORGANISM_TAXID: 9844; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SURROGATE CYTOKINE AGONIST, DUAL-VHH, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR R.TRENKER,S.VIVONA,P.J.LUPARDUS REVDAT 1 10-SEP-25 9O9C 0 JRNL AUTH R.TRENKER,D.ROKKAM,A.MORIN,P.BALASUBRAHMANYAM,V.PAREDES, JRNL AUTH 2 I.CHENG,R.DE WAAL MALEFYT,M.OFT,P.LUPARDUS,S.VIVONA JRNL TITL STRUCTURE-GUIDED STAPLING OF DIMERIC CONFORMATIONS AND JRNL TITL 2 LINKER ENGINEERING ENHANCE THERMOSTABILITY AND FINE-TUNE JRNL TITL 3 ACTIVITY OF BISPECIFIC VHH CYTOKINE AGONISTS JRNL REF ANTIBODIES V. 14 2025 JRNL REFN ISSN 2073-4468 JRNL DOI 10.3390/ANTIB14030074 REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0419 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.20 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 8208 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) : 0.238 REMARK 3 R VALUE (WORKING SET) : 0.235 REMARK 3 FREE R VALUE : 0.291 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 437 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.90 REMARK 3 REFLECTION IN BIN (WORKING SET) : 599 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.21 REMARK 3 BIN R VALUE (WORKING SET) : 0.3390 REMARK 3 BIN FREE R VALUE SET COUNT : 30 REMARK 3 BIN FREE R VALUE : 0.3590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3447 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.38000 REMARK 3 B22 (A**2) : 2.38000 REMARK 3 B33 (A**2) : -7.72000 REMARK 3 B12 (A**2) : 1.19000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.732 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.755 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 58.135 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.867 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.773 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3497 ; 0.004 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3314 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4736 ; 1.283 ; 1.804 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7575 ; 0.431 ; 1.753 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 452 ; 6.798 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 33 ; 4.473 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 568 ;14.150 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 545 ; 0.050 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4274 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 858 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1829 ; 5.766 ; 8.469 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1829 ; 5.765 ; 8.468 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2274 ; 9.637 ;15.200 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2275 ; 9.635 ;15.201 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1668 ; 5.807 ; 8.973 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1669 ; 5.806 ; 8.973 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2463 ; 9.851 ;16.360 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3715 ;14.202 ;86.610 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3716 ;14.203 ;86.620 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9O9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295042. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10210 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.590 REMARK 200 RESOLUTION RANGE LOW (A) : 39.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : 0.44900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.59 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.93 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 1.10900 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 71.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1 M TRIS PH REMARK 280 8.5 AND 1.26 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 121.23067 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.61533 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.92300 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 30.30767 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 151.53833 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: MONOMERIC 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 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 B 27 REMARK 465 THR B 28 REMARK 465 PHE B 29 REMARK 465 GLY B 118 REMARK 465 GLY B 119 REMARK 465 GLY B 120 REMARK 465 GLY B 121 REMARK 465 SER B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 GLY B 126 REMARK 465 SER B 127 REMARK 465 ALA B 243 REMARK 465 SER B 244 REMARK 465 HIS B 245 REMARK 465 HIS B 246 REMARK 465 HIS B 247 REMARK 465 HIS B 248 REMARK 465 HIS B 249 REMARK 465 HIS B 250 REMARK 465 GLU A 1 REMARK 465 ASN A 102 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 SER A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 SER A 154 REMARK 465 THR A 155 REMARK 465 SER A 244 REMARK 465 HIS A 245 REMARK 465 HIS A 246 REMARK 465 HIS A 247 REMARK 465 HIS A 248 REMARK 465 HIS A 249 REMARK 465 HIS A 250 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 ARG B 157 CG CD NE CZ NH1 NH2 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 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ARG B 66 -52.68 -130.18 REMARK 500 ALA B 91 179.92 174.25 REMARK 500 TYR B 94 -167.14 -111.30 REMARK 500 CYS B 95 13.17 -150.66 REMARK 500 ALA B 98 9.08 -156.96 REMARK 500 SER B 152 38.30 74.60 REMARK 500 ASN B 159 -163.50 77.54 REMARK 500 GLN B 166 113.57 -164.39 REMARK 500 ASP B 182 30.75 71.92 REMARK 500 ASP B 199 75.93 56.17 REMARK 500 ALA B 224 -28.49 -142.53 REMARK 500 ARG B 225 75.35 58.97 REMARK 500 THR A 28 56.20 72.84 REMARK 500 LEU A 54 -1.31 85.19 REMARK 500 ALA A 98 57.27 -151.30 REMARK 500 LEU A 158 150.30 -44.11 REMARK 500 ASN A 159 -81.01 -121.65 REMARK 500 VAL A 175 -51.21 -128.00 REMARK 500 ASP A 182 43.89 70.40 REMARK 500 ARG A 193 -62.44 -93.57 REMARK 500 PHE A 227 73.47 44.28 REMARK 500 REMARK 500 REMARK: NULL DBREF 9O9C B 1 250 PDB 9O9C 9O9C 1 250 DBREF 9O9C A 1 250 PDB 9O9C 9O9C 1 250 SEQRES 1 B 250 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 250 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 B 250 SER THR PHE SER ILE ASN ALA ILE GLY TRP TYR ARG GLN SEQRES 4 B 250 ALA PRO GLY GLU GLN ARG GLU LEU VAL VAL GLY ILE ARG SEQRES 5 B 250 ASP LEU GLY SER THR ARG TYR VAL ASP SER VAL LYS GLY SEQRES 6 B 250 ARG PHE THR LEU SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 B 250 TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR ALA SEQRES 8 B 250 VAL TYR TYR CYS ASN ALA ALA LYS SER GLY ASN ARG LEU SEQRES 9 B 250 TYR PRO TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 B 250 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL GLN SEQRES 11 B 250 LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 12 B 250 SER LEU ARG LEU SER CYS ALA ALA SER THR SER THR PHE SEQRES 13 B 250 ARG LEU ASN SER ILE GLY TRP PHE ARG GLN ALA PRO GLY SEQRES 14 B 250 LYS GLN ARG GLU LEU VAL ALA THR ILE THR ALA ASP ASP SEQRES 15 B 250 THR THR ALA TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 16 B 250 ILE SER ARG ASP ASN ALA VAL ASN THR VAL ASN LEU GLN SEQRES 17 B 250 MET ASN SER LEU LYS PRO GLU ASP THR ALA THR TYR TYR SEQRES 18 B 250 CYS THR ALA ARG VAL PHE GLY ARG ASP ILE ARG GLY GLN SEQRES 19 B 250 GLY THR LEU VAL THR VAL SER SER ALA SER HIS HIS HIS SEQRES 20 B 250 HIS HIS HIS SEQRES 1 A 250 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 250 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 A 250 SER THR PHE SER ILE ASN ALA ILE GLY TRP TYR ARG GLN SEQRES 4 A 250 ALA PRO GLY GLU GLN ARG GLU LEU VAL VAL GLY ILE ARG SEQRES 5 A 250 ASP LEU GLY SER THR ARG TYR VAL ASP SER VAL LYS GLY SEQRES 6 A 250 ARG PHE THR LEU SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 A 250 TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR ALA SEQRES 8 A 250 VAL TYR TYR CYS ASN ALA ALA LYS SER GLY ASN ARG LEU SEQRES 9 A 250 TYR PRO TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 A 250 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL GLN SEQRES 11 A 250 LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 12 A 250 SER LEU ARG LEU SER CYS ALA ALA SER THR SER THR PHE SEQRES 13 A 250 ARG LEU ASN SER ILE GLY TRP PHE ARG GLN ALA PRO GLY SEQRES 14 A 250 LYS GLN ARG GLU LEU VAL ALA THR ILE THR ALA ASP ASP SEQRES 15 A 250 THR THR ALA TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 16 A 250 ILE SER ARG ASP ASN ALA VAL ASN THR VAL ASN LEU GLN SEQRES 17 A 250 MET ASN SER LEU LYS PRO GLU ASP THR ALA THR TYR TYR SEQRES 18 A 250 CYS THR ALA ARG VAL PHE GLY ARG ASP ILE ARG GLY GLN SEQRES 19 A 250 GLY THR LEU VAL THR VAL SER SER ALA SER HIS HIS HIS SEQRES 20 A 250 HIS HIS HIS HELIX 1 AA1 SER B 30 ILE B 34 5 5 HELIX 2 AA2 ASN B 73 LYS B 75 5 3 HELIX 3 AA3 LYS B 86 THR B 90 5 5 HELIX 4 AA4 ASP B 199 VAL B 202 5 4 HELIX 5 AA5 LYS B 213 THR B 217 5 5 HELIX 6 AA6 SER A 30 ASN A 32 5 3 HELIX 7 AA7 ASP A 61 LYS A 64 5 4 HELIX 8 AA8 LYS A 86 THR A 90 5 5 HELIX 9 AA9 LYS A 213 THR A 217 5 5 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 GLY B 15 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 77 LEU B 85 -1 O LEU B 85 N GLY B 15 SHEET 4 AA1 4 PHE B 67 THR B 68 -1 N THR B 68 O GLN B 81 SHEET 1 AA2 4 GLN B 3 SER B 7 0 SHEET 2 AA2 4 GLY B 15 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA2 4 THR B 77 LEU B 85 -1 O LEU B 85 N GLY B 15 SHEET 4 AA2 4 ARG B 71 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 AA3 5 LEU B 11 VAL B 12 0 SHEET 2 AA3 5 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA3 5 ALA B 91 TYR B 93 -1 N TYR B 93 O THR B 111 SHEET 4 AA3 5 TYR B 37 ALA B 40 -1 N GLN B 39 O VAL B 92 SHEET 5 AA3 5 GLU B 43 LEU B 47 -1 O GLU B 46 N ARG B 38 SHEET 1 AA4 2 VAL B 49 ILE B 51 0 SHEET 2 AA4 2 THR B 57 TYR B 59 -1 O ARG B 58 N GLY B 50 SHEET 1 AA5 4 VAL B 132 SER B 134 0 SHEET 2 AA5 4 SER B 144 ALA B 150 -1 O ALA B 150 N VAL B 132 SHEET 3 AA5 4 THR B 204 ASN B 210 -1 O LEU B 207 N LEU B 147 SHEET 4 AA5 4 PHE B 194 SER B 197 -1 N THR B 195 O GLN B 208 SHEET 1 AA6 5 THR B 184 TYR B 186 0 SHEET 2 AA6 5 GLU B 173 ILE B 178 -1 N THR B 177 O ALA B 185 SHEET 3 AA6 5 ILE B 161 GLN B 166 -1 N TRP B 163 O ALA B 176 SHEET 4 AA6 5 ALA B 218 THR B 223 -1 O TYR B 221 N PHE B 164 SHEET 5 AA6 5 THR B 236 VAL B 238 -1 O THR B 236 N TYR B 220 SHEET 1 AA7 4 GLN A 3 SER A 7 0 SHEET 2 AA7 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA7 4 THR A 77 MET A 82 -1 O LEU A 80 N LEU A 20 SHEET 4 AA7 4 ARG A 71 ASP A 72 -1 N ASP A 72 O THR A 77 SHEET 1 AA8 6 GLY A 10 GLN A 13 0 SHEET 2 AA8 6 THR A 111 SER A 116 1 O THR A 114 N VAL A 12 SHEET 3 AA8 6 ALA A 91 TYR A 93 -1 N TYR A 93 O THR A 111 SHEET 4 AA8 6 ILE A 34 GLN A 39 -1 N GLN A 39 O VAL A 92 SHEET 5 AA8 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA8 6 THR A 57 TYR A 59 -1 O ARG A 58 N GLY A 50 SHEET 1 AA9 5 GLY A 10 GLN A 13 0 SHEET 2 AA9 5 THR A 111 SER A 116 1 O THR A 114 N VAL A 12 SHEET 3 AA9 5 ALA A 91 TYR A 93 -1 N TYR A 93 O THR A 111 SHEET 4 AA9 5 ILE A 34 GLN A 39 -1 N GLN A 39 O VAL A 92 SHEET 5 AA9 5 ASN A 96 ALA A 97 -1 O ASN A 96 N GLY A 35 SHEET 1 AB1 4 LEU A 131 SER A 134 0 SHEET 2 AB1 4 LEU A 145 ALA A 151 -1 O SER A 148 N SER A 134 SHEET 3 AB1 4 THR A 204 MET A 209 -1 O MET A 209 N LEU A 145 SHEET 4 AB1 4 THR A 195 ASP A 199 -1 N THR A 195 O GLN A 208 SHEET 1 AB2 4 ARG A 172 ILE A 178 0 SHEET 2 AB2 4 ILE A 161 GLN A 166 -1 N TRP A 163 O ALA A 176 SHEET 3 AB2 4 ALA A 218 VAL A 226 -1 O TYR A 221 N PHE A 164 SHEET 4 AB2 4 ARG A 229 ARG A 232 -1 O ARG A 229 N VAL A 226 SHEET 1 AB3 4 ARG A 172 ILE A 178 0 SHEET 2 AB3 4 ILE A 161 GLN A 166 -1 N TRP A 163 O ALA A 176 SHEET 3 AB3 4 ALA A 218 VAL A 226 -1 O TYR A 221 N PHE A 164 SHEET 4 AB3 4 THR A 236 VAL A 238 -1 O THR A 236 N TYR A 220 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 2 CYS B 149 CYS B 222 1555 1555 2.03 SSBOND 3 CYS A 22 CYS A 95 1555 1555 2.05 SSBOND 4 CYS A 149 CYS A 222 1555 1555 2.04 CRYST1 92.640 92.640 181.846 90.00 90.00 120.00 P 65 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 0.010794 0.006232 0.000000 0.00000 SCALE2 0.000000 0.012464 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005499 0.00000