HEADER CYTOKINE 30-APR-23 8SOZ TITLE STRUCTURE OF THE COMPLEX FORMED BY HUMAN INTERLEUKIN-2 AND SCFV 602 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 602 SINGLE CHAIN FRAGMENT VARIABLE; COMPND 3 CHAIN: C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: INTERLEUKIN-2; COMPND 7 CHAIN: A; COMPND 8 SYNONYM: IL-2,T-CELL GROWTH FACTOR,TCGF; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: IL2; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS COMPLEX, ANTIBODY, INTERLEUKIN, CYTOKINE EXPDTA X-RAY DIFFRACTION AUTHOR J.R.GOULD,E.K.LEONARD,S.D.CAO,J.B.SPANGLER REVDAT 1 04-SEP-24 8SOZ 0 JRNL AUTH E.K.LEONARD,J.TOMALA,J.R.GOULD,M.I.LEFF,J.X.LIN,P.LI, JRNL AUTH 2 M.J.PORTER,E.R.JOHANSEN,L.THOMPSON,S.D.CAO,S.HOU,T.HENCLOVA, JRNL AUTH 3 M.HULICIAK,P.R.SARGUNAS,C.S.FABILANE,O.VANEK,M.KOVAR, JRNL AUTH 4 B.SCHNEIDER,G.RAIMONDI,W.J.LEONARD,J.B.SPANGLER JRNL TITL ENGINEERED CYTOKINE/ANTIBODY FUSION PROTEINS IMPROVE IL-2 JRNL TITL 2 DELIVERY TO PRO-INFLAMMATORY CELLS AND PROMOTE ANTITUMOR JRNL TITL 3 ACTIVITY. JRNL REF JCI INSIGHT 2024 JRNL REFN ISSN 2379-3708 JRNL PMID 39115939 JRNL DOI 10.1172/JCI.INSIGHT.173469 REMARK 2 REMARK 2 RESOLUTION. 1.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.19.1_4122: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 37047 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930 REMARK 3 FREE R VALUE TEST SET COUNT : 1839 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 32.6000 - 3.5200 0.99 3656 193 0.1845 0.1900 REMARK 3 2 3.5200 - 2.8000 0.99 3603 163 0.2121 0.2625 REMARK 3 3 2.8000 - 2.4400 0.99 3558 184 0.2426 0.3025 REMARK 3 4 2.4400 - 2.2200 0.99 3555 174 0.2324 0.2925 REMARK 3 5 2.2200 - 2.0600 0.99 3563 195 0.2288 0.2615 REMARK 3 6 2.0600 - 1.9400 0.99 3505 188 0.2447 0.2664 REMARK 3 7 1.9400 - 1.8400 1.00 3555 189 0.2459 0.2997 REMARK 3 8 1.8400 - 1.7600 1.00 3500 197 0.2746 0.3171 REMARK 3 9 1.7600 - 1.6900 0.99 3559 178 0.3127 0.3391 REMARK 3 10 1.6900 - 1.6400 0.97 3418 178 0.3701 0.4010 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL 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) : NULL 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 : 0.009 2701 REMARK 3 ANGLE : 1.148 3659 REMARK 3 CHIRALITY : 0.067 423 REMARK 3 PLANARITY : 0.010 457 REMARK 3 DIHEDRAL : 6.319 359 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 8SOZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-23. REMARK 100 THE DEPOSITION ID IS D_1000274186. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JAN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.920 REMARK 200 MONOCHROMATOR : SI(111) DCM REMARK 200 OPTICS : KB BIMORPH MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37048 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640 REMARK 200 RESOLUTION RANGE LOW (A) : 61.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 1.50000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.010 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 (%): 31.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15-30% PEG 3350, 0.1-0.35 AMMONIUM REMARK 280 FLUORIDE, PH 7.4, VAPOR DIFFUSION, HANGING 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 68.59600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.20950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.59600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.20950 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 ALA C 114 REMARK 465 GLY C 115 REMARK 465 ILE C 116 REMARK 465 LEU C 117 REMARK 465 GLY C 118 REMARK 465 SER C 119 REMARK 465 GLY C 120 REMARK 465 GLY C 121 REMARK 465 GLY C 122 REMARK 465 GLY C 123 REMARK 465 SER C 124 REMARK 465 GLY C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 GLY C 128 REMARK 465 SER C 129 REMARK 465 GLY C 130 REMARK 465 GLY C 131 REMARK 465 GLY C 132 REMARK 465 GLY C 133 REMARK 465 SER C 134 REMARK 465 ALA A -2 REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 ALA A 1 REMARK 465 PRO A 2 REMARK 465 THR A 3 REMARK 465 SER A 4 REMARK 465 TYR A 31 REMARK 465 LYS A 32 REMARK 465 ASN A 33 REMARK 465 PRO A 34 REMARK 465 GLN A 74 REMARK 465 SER A 75 REMARK 465 LYS A 76 REMARK 465 ASN A 77 REMARK 465 PHE A 78 REMARK 465 HIS A 79 REMARK 465 LEU A 80 REMARK 465 GLU A 100 REMARK 465 THR A 101 REMARK 465 THR A 102 REMARK 465 THR A 133 REMARK 465 ALA A 134 REMARK 465 ALA A 135 REMARK 465 ALA A 136 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 SER C 187 O HOH C 301 2.06 REMARK 500 O HOH C 397 O HOH C 417 2.15 REMARK 500 O HOH C 314 O HOH C 400 2.16 REMARK 500 O HOH C 389 O HOH A 230 2.16 REMARK 500 O HOH A 202 O HOH A 208 2.16 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 OG SER C 15 OD1 ASN A 29 4545 1.62 REMARK 500 O GLY C 107 NZ LYS C 241 4556 1.87 REMARK 500 O HOH C 304 O HOH C 306 4556 1.97 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 PHE A 103 O - C - N ANGL. DEV. = 9.7 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 GLN C 98 63.53 -103.65 REMARK 500 SER C 141 -132.38 -41.18 REMARK 500 ASP C 151 152.82 66.80 REMARK 500 ALA C 185 -35.94 73.24 REMARK 500 SER C 211 68.59 33.69 REMARK 500 PHE C 225 37.56 -140.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8SOW RELATED DB: PDB REMARK 900 8SOW DESCRIBES A COMPLEX BETWEEN A HIGHLY SIMILAR SCFV AND THE SAME REMARK 900 CYTOKINE DBREF 8SOZ C 1 241 PDB 8SOZ 8SOZ 1 241 DBREF 8SOZ A 0 133 UNP P60568 IL2_HUMAN 20 153 SEQADV 8SOZ ALA A -2 UNP P60568 EXPRESSION TAG SEQADV 8SOZ GLY A -1 UNP P60568 EXPRESSION TAG SEQADV 8SOZ ALA A 134 UNP P60568 EXPRESSION TAG SEQADV 8SOZ ALA A 135 UNP P60568 EXPRESSION TAG SEQADV 8SOZ ALA A 136 UNP P60568 EXPRESSION TAG SEQRES 1 C 241 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 C 241 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 C 241 PHE SER LEU THR ASN TYR ASP ILE SER TRP ILE ARG GLN SEQRES 4 C 241 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 C 241 THR GLY GLY GLY THR ASN TYR ASN SER GLY PHE MET SER SEQRES 6 C 241 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 C 241 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA SEQRES 8 C 241 ILE TYR TYR CYS VAL ARG GLN GLY ARG THR PRO TYR TRP SEQRES 9 C 241 GLY GLN GLY THR LEU VAL THR VAL SER ALA GLY ILE LEU SEQRES 10 C 241 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 11 C 241 GLY GLY GLY SER ASP ILE GLN VAL THR GLN SER PRO SER SEQRES 12 C 241 SER LEU SER VAL SER LEU GLY ASP ARG VAL THR ILE THR SEQRES 13 C 241 CYS LYS ALA SER LYS ASP ILE TYR ASN ARG LEU ALA TRP SEQRES 14 C 241 TYR GLN GLN LYS PRO GLY ASN ALA PRO ARG LEU LEU ILE SEQRES 15 C 241 SER GLY ALA THR SER LEU GLU THR GLY VAL PRO SER ARG SEQRES 16 C 241 PHE SER GLY SER GLY SER GLY LYS ASP TYR THR LEU THR SEQRES 17 C 241 ILE THR SER LEU GLN THR GLU ASP VAL ALA THR TYR TYR SEQRES 18 C 241 CYS GLN GLN PHE TRP GLY THR PRO TYR THR PHE GLY GLY SEQRES 19 C 241 GLY THR LYS LEU GLU ILE LYS SEQRES 1 A 139 ALA GLY SER ALA PRO THR SER SER SER THR LYS LYS THR SEQRES 2 A 139 GLN LEU GLN LEU GLU HIS LEU LEU LEU ASP LEU GLN MET SEQRES 3 A 139 ILE LEU ASN GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU SEQRES 4 A 139 THR ARG MET LEU THR PHE LYS PHE TYR MET PRO LYS LYS SEQRES 5 A 139 ALA THR GLU LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU SEQRES 6 A 139 LEU LYS PRO LEU GLU GLU VAL LEU ASN LEU ALA GLN SER SEQRES 7 A 139 LYS ASN PHE HIS LEU ARG PRO ARG ASP LEU ILE SER ASN SEQRES 8 A 139 ILE ASN VAL ILE VAL LEU GLU LEU LYS GLY SER GLU THR SEQRES 9 A 139 THR PHE MET CYS GLU TYR ALA ASP GLU THR ALA THR ILE SEQRES 10 A 139 VAL GLU PHE LEU ASN ARG TRP ILE THR PHE CYS GLN SER SEQRES 11 A 139 ILE ILE SER THR LEU THR ALA ALA ALA FORMUL 3 HOH *155(H2 O) HELIX 1 AA1 PHE C 63 SER C 65 5 3 HELIX 2 AA2 GLN C 86 THR C 90 5 5 HELIX 3 AA3 GLN C 213 VAL C 217 5 5 HELIX 4 AA4 SER A 6 ASN A 29 1 24 HELIX 5 AA5 LEU A 36 LEU A 40 1 5 HELIX 6 AA6 GLU A 52 HIS A 55 5 4 HELIX 7 AA7 LEU A 56 GLU A 62 1 7 HELIX 8 AA8 GLU A 62 ASN A 71 1 10 HELIX 9 AA9 PRO A 82 GLY A 98 1 17 HELIX 10 AB1 THR A 113 LEU A 132 1 20 SHEET 1 AA1 4 GLN C 3 SER C 7 0 SHEET 2 AA1 4 LEU C 18 SER C 25 -1 O THR C 21 N SER C 7 SHEET 3 AA1 4 GLN C 77 MET C 82 -1 O VAL C 78 N CYS C 22 SHEET 4 AA1 4 LEU C 67 ASP C 72 -1 N THR C 70 O PHE C 79 SHEET 1 AA2 6 LEU C 11 VAL C 12 0 SHEET 2 AA2 6 THR C 108 VAL C 112 1 O THR C 111 N VAL C 12 SHEET 3 AA2 6 ALA C 91 ARG C 97 -1 N TYR C 93 O THR C 108 SHEET 4 AA2 6 ILE C 34 GLN C 39 -1 N ILE C 37 O TYR C 94 SHEET 5 AA2 6 GLU C 46 ILE C 51 -1 O GLY C 49 N TRP C 36 SHEET 6 AA2 6 THR C 57 TYR C 59 -1 O ASN C 58 N VAL C 50 SHEET 1 AA3 4 LEU C 11 VAL C 12 0 SHEET 2 AA3 4 THR C 108 VAL C 112 1 O THR C 111 N VAL C 12 SHEET 3 AA3 4 ALA C 91 ARG C 97 -1 N TYR C 93 O THR C 108 SHEET 4 AA3 4 TYR C 103 TRP C 104 -1 O TYR C 103 N ARG C 97 SHEET 1 AA4 4 VAL C 138 GLN C 140 0 SHEET 2 AA4 4 VAL C 153 ALA C 159 -1 O LYS C 158 N THR C 139 SHEET 3 AA4 4 ASP C 204 ILE C 209 -1 O LEU C 207 N ILE C 155 SHEET 4 AA4 4 PHE C 196 SER C 201 -1 N SER C 197 O THR C 208 SHEET 1 AA5 6 SER C 144 VAL C 147 0 SHEET 2 AA5 6 THR C 236 ILE C 240 1 O GLU C 239 N LEU C 145 SHEET 3 AA5 6 ALA C 218 GLN C 224 -1 N TYR C 220 O THR C 236 SHEET 4 AA5 6 LEU C 167 GLN C 172 -1 N TYR C 170 O TYR C 221 SHEET 5 AA5 6 ARG C 179 SER C 183 -1 O ARG C 179 N GLN C 171 SHEET 6 AA5 6 SER C 187 LEU C 188 -1 O SER C 187 N SER C 183 SSBOND 1 CYS C 22 CYS C 95 1555 1555 2.08 SSBOND 2 CYS C 157 CYS C 222 1555 1555 2.06 SSBOND 3 CYS A 58 CYS A 105 1555 1555 2.04 CISPEP 1 THR C 228 PRO C 229 0 0.94 CRYST1 137.192 36.419 64.189 90.00 108.12 90.00 C 1 2 1 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 0.007289 0.000000 0.002385 0.00000 SCALE2 0.000000 0.027458 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016392 0.00000