HEADER PROTEIN BINDING 17-APR-25 9O9B TITLE STRUCTURE OF THE IL-18 SURROGATE CYTOKINE AGONIST DR3097 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IL-18 SURROGATE CYTOKINE AGONIST DR3097; 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 9O9B 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. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 57.280 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 11206 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.246 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 547 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.3100 - 4.4400 0.90 2631 165 0.2291 0.2610 REMARK 3 2 4.4400 - 3.5300 0.91 2646 118 0.2175 0.3034 REMARK 3 3 3.5200 - 3.0800 0.92 2675 145 0.2766 0.3224 REMARK 3 4 3.0800 - 2.8000 0.94 2732 94 0.3153 0.4758 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.650 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 3313 REMARK 3 ANGLE : 1.331 4480 REMARK 3 CHIRALITY : 0.076 506 REMARK 3 PLANARITY : 0.011 580 REMARK 3 DIHEDRAL : 44.608 470 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9O9B 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_1000295038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-APR-24 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 : 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 : 11208 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 39.310 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.11200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : 0.67200 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 (%): 46.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.6 M SODIUM FORMATE 10% (V/V) REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,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 -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 0.00000 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 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 SER A 52 REMARK 465 LEU A 53 REMARK 465 GLY A 54 REMARK 465 SER A 102 REMARK 465 ARG A 103 REMARK 465 LEU A 104 REMARK 465 TYR A 105 REMARK 465 PRO A 106 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 127 REMARK 465 GLU A 128 REMARK 465 VAL A 129 REMARK 465 GLY A 228 REMARK 465 ARG A 229 REMARK 465 ASP A 230 REMARK 465 ALA A 243 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 465 SER B 27 REMARK 465 THR B 28 REMARK 465 ALA B 97 REMARK 465 ALA B 98 REMARK 465 ARG B 99 REMARK 465 SER B 100 REMARK 465 ASP B 101 REMARK 465 SER B 102 REMARK 465 ARG B 103 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 ALA B 150 REMARK 465 ALA B 151 REMARK 465 SER B 152 REMARK 465 THR B 153 REMARK 465 SER B 154 REMARK 465 THR B 155 REMARK 465 PHE B 156 REMARK 465 ARG B 157 REMARK 465 LEU B 158 REMARK 465 ASN B 159 REMARK 465 SER B 160 REMARK 465 ARG B 229 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 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 GLY A 35 REMARK 475 ARG A 45 REMARK 475 GLY A 50 REMARK 475 GLY B 35 REMARK 475 VAL B 48 REMARK 475 ALA B 49 REMARK 475 CYS B 149 REMARK 475 TYR B 186 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLN A 44 N CA C O REMARK 480 PRO A 60 N CA C O REMARK 480 ARG A 61 N CA C O REMARK 480 GLU B 1 N CA C O REMARK 480 THR B 183 N CA C O REMARK 480 THR B 184 N CA C O REMARK 480 ALA B 185 N CA C O 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 HG1 THR A 223 O ILE A 231 1.52 REMARK 500 O PRO A 57 HZ3 LYS B 64 1.58 REMARK 500 O GLY A 135 HG1 THR A 236 1.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HH12 ARG B 146 O ILE B 231 1556 1.53 REMARK 500 NH1 ARG B 146 O ILE B 231 1556 1.89 REMARK 500 O PRO A 41 NE2 GLN A 81 1556 2.10 REMARK 500 OG SER A 100 OG1 THR A 217 2445 2.10 REMARK 500 OG SER A 144 NH2 ARG A 232 1556 2.17 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 ILE A 34 CG1 - CB - CG2 ANGL. DEV. = -13.7 DEGREES REMARK 500 LEU A 131 CB - CG - CD2 ANGL. DEV. = -14.8 DEGREES REMARK 500 ARG A 146 CG - CD - NE ANGL. DEV. = 16.9 DEGREES REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG A 146 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES REMARK 500 GLN A 208 CA - CB - CG ANGL. DEV. = 19.5 DEGREES REMARK 500 ARG B 45 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES REMARK 500 LEU B 131 CB - CG - CD2 ANGL. DEV. = -12.5 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 LYS A 75 17.49 -141.06 REMARK 500 PRO A 87 1.63 -64.87 REMARK 500 CYS A 95 -61.71 -92.32 REMARK 500 ARG A 99 -78.84 -129.13 REMARK 500 SER A 100 88.16 -152.79 REMARK 500 SER A 152 72.36 32.84 REMARK 500 LEU A 158 29.33 -150.87 REMARK 500 ALA A 180 2.68 -66.49 REMARK 500 ALA A 224 -41.16 -139.16 REMARK 500 GLU B 43 -119.51 64.02 REMARK 500 LEU B 53 -131.23 55.89 REMARK 500 GLN B 109 56.27 -141.71 REMARK 500 ALA B 180 -147.20 56.31 REMARK 500 THR B 184 105.63 -161.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU B 31 HIS B 32 -144.19 REMARK 500 TYR B 105 PRO B 106 -142.72 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 GLN A 81 0.09 SIDE CHAIN REMARK 500 GLN A 208 0.12 SIDE CHAIN REMARK 500 ARG B 61 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9O9B A 1 250 PDB 9O9B 9O9B 1 250 DBREF 9O9B B 1 250 PDB 9O9B 9O9B 1 250 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 ALA ALA SER GLY SEQRES 3 A 250 SER THR PHE SER LEU HIS VAL ILE GLY TRP TYR ARG GLN SEQRES 4 A 250 ALA PRO GLY GLU GLN ARG GLU MET VAL ALA GLY PHE SER SEQRES 5 A 250 LEU GLY GLY THR PRO TYR TYR PRO ARG SER VAL LYS GLY SEQRES 6 A 250 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP 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 ARG SER ASP SER 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 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 ALA ALA SER GLY SEQRES 3 B 250 SER THR PHE SER LEU HIS VAL ILE GLY TRP TYR ARG GLN SEQRES 4 B 250 ALA PRO GLY GLU GLN ARG GLU MET VAL ALA GLY PHE SER SEQRES 5 B 250 LEU GLY GLY THR PRO TYR TYR PRO ARG SER VAL LYS GLY SEQRES 6 B 250 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP 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 ARG SER ASP SER 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 HELIX 1 AA1 LYS A 213 THR A 217 5 5 HELIX 2 AA2 LYS B 86 THR B 90 5 5 HELIX 3 AA3 ASP B 188 LYS B 191 5 4 HELIX 4 AA4 LYS B 213 THR B 217 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 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 THR A 68 O GLN A 81 SHEET 1 AA2 5 LEU A 11 GLN A 13 0 SHEET 2 AA2 5 THR A 111 SER A 116 1 O SER A 116 N VAL A 12 SHEET 3 AA2 5 ALA A 91 TYR A 94 -1 N TYR A 93 O THR A 111 SHEET 4 AA2 5 TRP A 36 GLN A 39 -1 N TYR A 37 O TYR A 94 SHEET 5 AA2 5 GLU A 46 ALA A 49 -1 O ALA A 49 N TRP A 36 SHEET 1 AA3 4 GLU A 133 SER A 134 0 SHEET 2 AA3 4 LEU A 147 CYS A 149 -1 O SER A 148 N SER A 134 SHEET 3 AA3 4 VAL A 205 LEU A 207 -1 O LEU A 207 N LEU A 147 SHEET 4 AA3 4 ILE A 196 ARG A 198 -1 N SER A 197 O ASN A 206 SHEET 1 AA4 6 GLY A 137 LEU A 138 0 SHEET 2 AA4 6 THR A 236 THR A 239 1 O LEU A 237 N GLY A 137 SHEET 3 AA4 6 ALA A 218 TYR A 221 -1 N ALA A 218 O VAL A 238 SHEET 4 AA4 6 ILE A 161 GLN A 166 -1 N PHE A 164 O TYR A 221 SHEET 5 AA4 6 GLU A 173 ILE A 178 -1 O ILE A 178 N ILE A 161 SHEET 6 AA4 6 ALA A 185 TYR A 186 -1 O ALA A 185 N THR A 177 SHEET 1 AA5 4 GLN B 3 SER B 7 0 SHEET 2 AA5 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA5 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA5 4 ILE B 69 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA6 3 LEU B 11 VAL B 12 0 SHEET 2 AA6 3 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA6 3 ALA B 91 TYR B 93 -1 N TYR B 93 O THR B 111 SHEET 1 AA7 2 TRP B 36 ARG B 38 0 SHEET 2 AA7 2 GLU B 46 VAL B 48 -1 O GLU B 46 N ARG B 38 SHEET 1 AA8 6 LEU B 138 VAL B 139 0 SHEET 2 AA8 6 THR B 236 VAL B 240 1 O THR B 239 N VAL B 139 SHEET 3 AA8 6 ALA B 218 TYR B 221 -1 N TYR B 220 O THR B 236 SHEET 4 AA8 6 GLY B 162 GLN B 166 -1 N GLN B 166 O THR B 219 SHEET 5 AA8 6 GLU B 173 THR B 177 -1 O VAL B 175 N TRP B 163 SHEET 6 AA8 6 ALA B 185 TYR B 186 -1 O ALA B 185 N THR B 177 SHEET 1 AA9 3 LEU B 145 CYS B 149 0 SHEET 2 AA9 3 VAL B 205 MET B 209 -1 O MET B 209 N LEU B 145 SHEET 3 AA9 3 THR B 195 ARG B 198 -1 N SER B 197 O ASN B 206 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.03 SSBOND 2 CYS A 149 CYS A 222 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 4 CYS B 149 CYS B 222 1555 1555 2.04 CISPEP 1 GLN A 140 PRO A 141 0 -14.08 CRYST1 120.100 120.100 29.268 90.00 90.00 120.00 P 3 6 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 0.008326 0.004807 0.000000 0.00000 SCALE2 0.000000 0.009614 0.000000 0.00000 SCALE3 0.000000 0.000000 0.034167 0.00000