HEADER PROTEIN BINDING 17-APR-25 9O99 TITLE STRUCTURE OF THE IL-2 SURROGATE CYTOKINE AGONIST DR638 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IL-2 SURROGATE CYTOKINE AGONIST DR638; COMPND 3 CHAIN: 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 9O99 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. 1.80 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.80 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 24498 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) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.211 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1296 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1784 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73 REMARK 3 BIN R VALUE (WORKING SET) : 0.2630 REMARK 3 BIN FREE R VALUE SET COUNT : 86 REMARK 3 BIN FREE R VALUE : 0.2760 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1820 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 268 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.10000 REMARK 3 B22 (A**2) : -0.88000 REMARK 3 B33 (A**2) : 2.98000 REMARK 3 B12 (A**2) : 0.00000 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): 0.119 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.519 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1852 ; 0.009 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 1680 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2505 ; 1.767 ; 1.795 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3866 ; 0.617 ; 1.739 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 245 ; 6.684 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 12 ;11.443 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 293 ;11.755 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 271 ; 0.090 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2278 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 446 ; 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): 983 ; 2.430 ; 2.425 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 983 ; 2.414 ; 2.426 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1227 ; 3.467 ; 4.338 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1228 ; 3.465 ; 4.344 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 869 ; 4.052 ; 2.798 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 870 ; 4.050 ; 2.804 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1279 ; 6.029 ; 4.942 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2089 ; 8.155 ;28.990 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1998 ; 8.008 ;28.110 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 9O99 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_1000295039. 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 : 7.5 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 : 25844 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 38.810 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.77400 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 (%): 51.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (V/V) GLYCEROL, 0.1 M HEPES PH REMARK 280 7.5, 30% (V/V) PEG 400 AND 5% (W/V) PEG 3000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 24.60250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.72550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.56750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.72550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.60250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.56750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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 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 247 REMARK 465 HIS A 248 REMARK 465 HIS A 249 REMARK 465 HIS A 250 REMARK 465 HIS A 251 REMARK 465 HIS A 252 REMARK 465 HIS A 253 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 O HOH A 520 O HOH A 546 1.79 REMARK 500 O HOH A 517 O HOH A 546 1.90 REMARK 500 OH TYR A 185 O HOH A 301 1.96 REMARK 500 O HOH A 435 O HOH A 448 2.05 REMARK 500 O HOH A 512 O HOH A 530 2.12 REMARK 500 O HOH A 427 O HOH A 508 2.13 REMARK 500 O HOH A 303 O HOH A 487 2.16 REMARK 500 O HOH A 493 O HOH A 500 2.16 REMARK 500 O HOH A 478 O HOH A 507 2.17 REMARK 500 O HOH A 487 O HOH A 529 2.17 REMARK 500 O HOH A 305 O HOH A 422 2.19 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 ARG A 174 CG - CD - NE ANGL. DEV. = -13.4 DEGREES REMARK 500 ARG A 223 NE - CZ - NH2 ANGL. DEV. = -3.0 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 92 163.31 177.97 REMARK 500 PRO A 162 129.20 -39.59 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 140 0.08 SIDE CHAIN REMARK 500 ARG A 174 0.17 SIDE CHAIN REMARK 500 ARG A 223 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9O99 A 1 253 PDB 9O99 9O99 1 253 SEQRES 1 A 253 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 253 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 A 253 PHE SER PHE SER SER TYR PRO MET THR TRP ALA ARG GLN SEQRES 4 A 253 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE ALA SEQRES 5 A 253 SER ASP GLY GLY SER THR ALA TYR ALA ALA SER VAL GLU SEQRES 6 A 253 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SER THR SEQRES 7 A 253 LEU TYR LEU GLN LEU ASN SER LEU LYS THR GLU ASP THR SEQRES 8 A 253 ALA MET TYR TYR CYS THR LYS GLY TYR GLY ASP GLY THR SEQRES 9 A 253 PRO ALA PRO GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 10 A 253 GLY GLY GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY SEQRES 11 A 253 GLY SER VAL GLN VAL GLY GLY SER LEU ARG LEU SER CYS SEQRES 12 A 253 ALA THR SER GLY ASP THR LYS SER ILE ARG CYS MET GLY SEQRES 13 A 253 TRP PHE ARG GLN THR PRO GLY LYS GLU ARG GLU GLY ILE SEQRES 14 A 253 ALA ALA ILE ASP ARG GLU GLY PHE ALA THR TYR ALA ASP SEQRES 15 A 253 SER VAL TYR ASP ARG PHE THR ILE ALA GLN ASP ASN ALA SEQRES 16 A 253 GLN ASN THR LEU TYR LEU GLU MET ASN ALA LEU LYS PRO SEQRES 17 A 253 GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLN ASN MET SEQRES 18 A 253 CYS ARG VAL VAL ARG GLY ALA MET THR GLY VAL ASP TYR SEQRES 19 A 253 TRP GLY LYS GLY THR GLN VAL THR VAL SER SER ALA SER SEQRES 20 A 253 HIS HIS HIS HIS HIS HIS FORMUL 2 HOH *268(H2 O) HELIX 1 AA1 SER A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 74 LYS A 76 5 3 HELIX 3 AA3 LYS A 87 THR A 91 5 5 HELIX 4 AA4 THR A 149 ILE A 152 5 4 HELIX 5 AA5 ASN A 194 GLN A 196 5 3 HELIX 6 AA6 LYS A 207 THR A 211 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 21 N SER A 7 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 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 GLY A 10 SHEET 3 AA2 6 ALA A 92 LYS A 98 -1 N TYR A 94 O THR A 111 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N THR A 35 O THR A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O ALA A 59 N THR A 50 SHEET 1 AA3 4 VAL A 123 SER A 128 0 SHEET 2 AA3 4 LEU A 139 GLY A 147 -1 O SER A 146 N GLN A 124 SHEET 3 AA3 4 THR A 198 MET A 203 -1 O MET A 203 N LEU A 139 SHEET 4 AA3 4 PHE A 188 ASP A 193 -1 N THR A 189 O GLU A 202 SHEET 1 AA4 6 SER A 132 GLN A 134 0 SHEET 2 AA4 6 THR A 239 SER A 244 1 O THR A 242 N VAL A 133 SHEET 3 AA4 6 ALA A 212 GLN A 219 -1 N TYR A 214 O THR A 239 SHEET 4 AA4 6 CYS A 154 GLN A 160 -1 N PHE A 158 O TYR A 215 SHEET 5 AA4 6 GLU A 167 ASP A 173 -1 O GLU A 167 N ARG A 159 SHEET 6 AA4 6 ALA A 178 TYR A 180 -1 O THR A 179 N ALA A 171 SHEET 1 AA5 4 SER A 132 GLN A 134 0 SHEET 2 AA5 4 THR A 239 SER A 244 1 O THR A 242 N VAL A 133 SHEET 3 AA5 4 ALA A 212 GLN A 219 -1 N TYR A 214 O THR A 239 SHEET 4 AA5 4 TYR A 234 TRP A 235 -1 O TYR A 234 N ALA A 218 SHEET 1 AA6 2 VAL A 224 VAL A 225 0 SHEET 2 AA6 2 ALA A 228 MET A 229 -1 O ALA A 228 N VAL A 225 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.46 SSBOND 2 CYS A 143 CYS A 216 1555 1555 2.37 SSBOND 3 CYS A 154 CYS A 222 1555 1555 2.24 CRYST1 49.205 63.135 87.451 90.00 90.00 90.00 P 21 21 21 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 0.020323 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015839 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011435 0.00000