HEADER PROTEIN BINDING 17-APR-25 9O9A TITLE STRUCTURE OF THE IL-18 SURROGATE CYTOKINE AGONIST DR3087 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DR3087 IL-18 SURROGATE CYTOKINE AGONIST; COMPND 3 CHAIN: A, B; 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 9O9A 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. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.70 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 NUMBER OF REFLECTIONS : 32612 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) : 0.243 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1697 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) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2387 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.58 REMARK 3 BIN R VALUE (WORKING SET) : 0.4440 REMARK 3 BIN FREE R VALUE SET COUNT : 151 REMARK 3 BIN FREE R VALUE : 0.3810 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3486 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 47 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.86 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 9.55000 REMARK 3 B22 (A**2) : -5.08000 REMARK 3 B33 (A**2) : -4.47000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.14000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.262 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.743 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3545 ; 0.007 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3307 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4789 ; 1.718 ; 1.803 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7555 ; 0.584 ; 1.748 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 451 ; 8.656 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 32 ; 9.636 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 557 ;14.983 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 529 ; 0.071 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4325 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 895 ; 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): 1837 ; 7.702 ; 7.263 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1837 ; 7.702 ; 7.264 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2277 ;11.264 ;13.001 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2278 ;11.264 ;13.002 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1708 ; 7.542 ; 7.632 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1709 ; 7.540 ; 7.635 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2513 ;11.279 ;13.886 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3726 ;15.051 ;73.390 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3724 ;15.049 ;73.390 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 9O9A 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_1000295030. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-DEC-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 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 : 34359 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 37.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.78800 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 (%): 70.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0 1.6 M MAGNESIUM REMARK 280 SULFATE, VAPOR DIFFUSION, 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 45.90350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.32900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.90350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 86.32900 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: 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 350 REMARK 350 BIOMOLECULE: 2 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 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 GLU A 1 REMARK 465 GLY A 50 REMARK 465 ILE A 51 REMARK 465 ARG A 52 REMARK 465 ASP A 53 REMARK 465 LEU A 54 REMARK 465 GLY A 55 REMARK 465 SER A 56 REMARK 465 THR A 57 REMARK 465 ARG A 58 REMARK 465 TYR A 59 REMARK 465 LYS A 99 REMARK 465 SER A 100 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 127 REMARK 465 TYR A 230 REMARK 465 SER A 231 REMARK 465 ALA A 255 REMARK 465 SER A 256 REMARK 465 HIS A 257 REMARK 465 HIS A 258 REMARK 465 HIS A 259 REMARK 465 HIS A 260 REMARK 465 HIS A 261 REMARK 465 HIS A 262 REMARK 465 GLU B 1 REMARK 465 SER B 27 REMARK 465 ILE B 51 REMARK 465 ARG B 52 REMARK 465 ASP B 53 REMARK 465 LEU B 54 REMARK 465 GLY B 55 REMARK 465 SER B 56 REMARK 465 THR B 57 REMARK 465 ARG B 58 REMARK 465 TYR B 59 REMARK 465 VAL B 60 REMARK 465 ASP B 61 REMARK 465 SER B 62 REMARK 465 VAL B 63 REMARK 465 LYS B 99 REMARK 465 SER B 100 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 TYR B 230 REMARK 465 ALA B 255 REMARK 465 SER B 256 REMARK 465 HIS B 257 REMARK 465 HIS B 258 REMARK 465 HIS B 259 REMARK 465 HIS B 260 REMARK 465 HIS B 261 REMARK 465 HIS B 262 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 OD2 ASP B 226 O HOH B 301 1.81 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 ASP A 61 -70.62 -84.04 REMARK 500 SER A 62 76.54 -68.83 REMARK 500 ARG A 66 -34.49 -150.28 REMARK 500 ALA A 91 168.81 168.57 REMARK 500 LEU A 104 76.48 61.86 REMARK 500 SER A 134 173.22 -58.16 REMARK 500 VAL A 175 -62.17 -109.25 REMARK 500 SER A 190 4.24 -64.02 REMARK 500 PHE B 29 77.20 59.87 REMARK 500 SER B 30 54.09 -117.43 REMARK 500 ARG B 45 153.99 -44.86 REMARK 500 ARG B 66 19.99 -152.14 REMARK 500 ALA B 91 167.97 171.78 REMARK 500 SER B 190 4.38 -62.89 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 239 0.08 SIDE CHAIN REMARK 500 ARG B 45 0.09 SIDE CHAIN REMARK 500 ARG B 146 0.10 SIDE CHAIN REMARK 500 ARG B 229 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 327 DISTANCE = 6.26 ANGSTROMS DBREF 9O9A A 1 262 PDB 9O9A 9O9A 1 262 DBREF 9O9A B 1 262 PDB 9O9A 9O9A 1 262 SEQRES 1 A 262 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 262 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 A 262 SER THR PHE SER ILE ASN ALA ILE GLY TRP TYR ARG GLN SEQRES 4 A 262 ALA PRO GLY GLU GLN ARG GLU LEU VAL VAL GLY ILE ARG SEQRES 5 A 262 ASP LEU GLY SER THR ARG TYR VAL ASP SER VAL LYS GLY SEQRES 6 A 262 ARG PHE THR LEU SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 A 262 TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR ALA SEQRES 8 A 262 VAL TYR TYR CYS ASN ALA ALA LYS SER GLY ASN ARG LEU SEQRES 9 A 262 TYR PRO TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 A 262 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL GLN SEQRES 11 A 262 LEU VAL GLU SER VAL GLY GLY LEU VAL GLN ALA GLY GLY SEQRES 12 A 262 SER LEU ARG LEU SER CYS ALA ALA SER GLY ARG THR PHE SEQRES 13 A 262 SER ASP TYR ALA VAL ALA TRP PHE ARG GLN ALA PRO GLY SEQRES 14 A 262 LYS GLU ARG GLU PHE VAL ALA VAL ILE THR ARG GLY GLY SEQRES 15 A 262 GLY SER THR VAL TYR THR ASP SER VAL LYS GLY ARG PHE SEQRES 16 A 262 THR ILE SER ARG ASP ASP ALA LYS ASN SER VAL TYR LEU SEQRES 17 A 262 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 18 A 262 TYR CYS ALA ALA ASP PHE MET ARG TYR SER SER THR LEU SEQRES 19 A 262 SER TYR ARG ALA ARG ALA TYR GLU HIS TRP GLY GLN GLY SEQRES 20 A 262 THR LEU VAL THR VAL SER SER ALA SER HIS HIS HIS HIS SEQRES 21 A 262 HIS HIS SEQRES 1 B 262 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 262 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 B 262 SER THR PHE SER ILE ASN ALA ILE GLY TRP TYR ARG GLN SEQRES 4 B 262 ALA PRO GLY GLU GLN ARG GLU LEU VAL VAL GLY ILE ARG SEQRES 5 B 262 ASP LEU GLY SER THR ARG TYR VAL ASP SER VAL LYS GLY SEQRES 6 B 262 ARG PHE THR LEU SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 B 262 TYR LEU GLN MET ASN SER LEU LYS PRO ASP ASP THR ALA SEQRES 8 B 262 VAL TYR TYR CYS ASN ALA ALA LYS SER GLY ASN ARG LEU SEQRES 9 B 262 TYR PRO TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 B 262 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU VAL GLN SEQRES 11 B 262 LEU VAL GLU SER VAL GLY GLY LEU VAL GLN ALA GLY GLY SEQRES 12 B 262 SER LEU ARG LEU SER CYS ALA ALA SER GLY ARG THR PHE SEQRES 13 B 262 SER ASP TYR ALA VAL ALA TRP PHE ARG GLN ALA PRO GLY SEQRES 14 B 262 LYS GLU ARG GLU PHE VAL ALA VAL ILE THR ARG GLY GLY SEQRES 15 B 262 GLY SER THR VAL TYR THR ASP SER VAL LYS GLY ARG PHE SEQRES 16 B 262 THR ILE SER ARG ASP ASP ALA LYS ASN SER VAL TYR LEU SEQRES 17 B 262 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 18 B 262 TYR CYS ALA ALA ASP PHE MET ARG TYR SER SER THR LEU SEQRES 19 B 262 SER TYR ARG ALA ARG ALA TYR GLU HIS TRP GLY GLN GLY SEQRES 20 B 262 THR LEU VAL THR VAL SER SER ALA SER HIS HIS HIS HIS SEQRES 21 B 262 HIS HIS FORMUL 3 HOH *47(H2 O) HELIX 1 AA1 LYS A 86 THR A 90 5 5 HELIX 2 AA2 THR A 155 SER A 157 5 3 HELIX 3 AA3 ARG A 180 GLY A 183 5 4 HELIX 4 AA4 ASP A 189 LYS A 192 5 4 HELIX 5 AA5 ASP A 201 LYS A 203 5 3 HELIX 6 AA6 LYS A 214 THR A 218 5 5 HELIX 7 AA7 ARG A 237 TYR A 241 5 5 HELIX 8 AA8 LYS B 86 THR B 90 5 5 HELIX 9 AA9 THR B 155 SER B 157 5 3 HELIX 10 AB1 ARG B 180 GLY B 183 5 4 HELIX 11 AB2 ASP B 189 LYS B 192 5 4 HELIX 12 AB3 ASP B 201 LYS B 203 5 3 HELIX 13 AB4 LYS B 214 THR B 218 5 5 HELIX 14 AB5 ARG B 237 TYR B 241 5 5 SHEET 1 AA1 4 GLU A 6 SER A 7 0 SHEET 2 AA1 4 LEU A 18 CYS A 22 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 VAL A 78 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ARG A 71 -1 N SER A 70 O TYR A 79 SHEET 1 AA2 5 GLY A 10 GLN A 13 0 SHEET 2 AA2 5 THR A 111 SER A 116 1 O THR A 114 N GLY A 10 SHEET 3 AA2 5 ALA A 91 ALA A 97 -1 N TYR A 93 O THR A 111 SHEET 4 AA2 5 ILE A 34 GLN A 39 -1 N TYR A 37 O TYR A 94 SHEET 5 AA2 5 GLU A 46 VAL A 49 -1 O VAL A 49 N TRP A 36 SHEET 1 AA3 4 LEU A 131 GLU A 133 0 SHEET 2 AA3 4 LEU A 145 ALA A 151 -1 O ALA A 150 N VAL A 132 SHEET 3 AA3 4 SER A 205 MET A 210 -1 O MET A 210 N LEU A 145 SHEET 4 AA3 4 PHE A 195 ASP A 200 -1 N THR A 196 O GLN A 209 SHEET 1 AA4 6 GLY A 137 GLN A 140 0 SHEET 2 AA4 6 THR A 248 SER A 253 1 O THR A 251 N VAL A 139 SHEET 3 AA4 6 ALA A 219 PHE A 227 -1 N TYR A 221 O THR A 248 SHEET 4 AA4 6 TYR A 159 GLN A 166 -1 N ALA A 162 O ALA A 224 SHEET 5 AA4 6 GLU A 173 ILE A 178 -1 O GLU A 173 N ARG A 165 SHEET 6 AA4 6 THR A 185 TYR A 187 -1 O VAL A 186 N VAL A 177 SHEET 1 AA5 4 GLY A 137 GLN A 140 0 SHEET 2 AA5 4 THR A 248 SER A 253 1 O THR A 251 N VAL A 139 SHEET 3 AA5 4 ALA A 219 PHE A 227 -1 N TYR A 221 O THR A 248 SHEET 4 AA5 4 HIS A 243 TRP A 244 -1 O HIS A 243 N ALA A 225 SHEET 1 AA6 4 GLU B 6 SER B 7 0 SHEET 2 AA6 4 LEU B 18 THR B 23 -1 O SER B 21 N SER B 7 SHEET 3 AA6 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA6 4 PHE B 67 ARG B 71 -1 N SER B 70 O TYR B 79 SHEET 1 AA7 5 GLY B 10 GLN B 13 0 SHEET 2 AA7 5 THR B 111 SER B 116 1 O THR B 114 N GLY B 10 SHEET 3 AA7 5 ALA B 91 ALA B 97 -1 N TYR B 93 O THR B 111 SHEET 4 AA7 5 ILE B 34 GLN B 39 -1 N TYR B 37 O TYR B 94 SHEET 5 AA7 5 GLU B 46 VAL B 49 -1 O VAL B 49 N TRP B 36 SHEET 1 AA8 4 LEU B 131 GLU B 133 0 SHEET 2 AA8 4 LEU B 145 ALA B 151 -1 O ALA B 150 N VAL B 132 SHEET 3 AA8 4 SER B 205 MET B 210 -1 O MET B 210 N LEU B 145 SHEET 4 AA8 4 PHE B 195 ASP B 200 -1 N THR B 196 O GLN B 209 SHEET 1 AA9 6 GLY B 137 GLN B 140 0 SHEET 2 AA9 6 THR B 248 SER B 253 1 O SER B 253 N VAL B 139 SHEET 3 AA9 6 ALA B 219 PHE B 227 -1 N TYR B 221 O THR B 248 SHEET 4 AA9 6 TYR B 159 GLN B 166 -1 N ALA B 162 O ALA B 224 SHEET 5 AA9 6 GLU B 173 ILE B 178 -1 O ALA B 176 N TRP B 163 SHEET 6 AA9 6 THR B 185 TYR B 187 -1 O VAL B 186 N VAL B 177 SHEET 1 AB1 4 GLY B 137 GLN B 140 0 SHEET 2 AB1 4 THR B 248 SER B 253 1 O SER B 253 N VAL B 139 SHEET 3 AB1 4 ALA B 219 PHE B 227 -1 N TYR B 221 O THR B 248 SHEET 4 AB1 4 HIS B 243 TRP B 244 -1 O HIS B 243 N ALA B 225 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.03 SSBOND 2 CYS A 149 CYS A 223 1555 1555 2.05 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.06 SSBOND 4 CYS B 149 CYS B 223 1555 1555 2.05 CRYST1 91.807 172.658 59.292 90.00 90.01 90.00 C 1 2 1 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 0.010892 0.000000 0.000002 0.00000 SCALE2 0.000000 0.005792 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016866 0.00000