HEADER IMMUNE SYSTEM 29-JAN-24 8RTW TITLE CRYSTAL STRUCTURE OF THE ANTI-TESTOSTERONE FAB IN COMPLEX WITH TITLE 2 TESTOSTERONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-TESTOSTERONE FAB 220 LIGHT CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-TESTOSTERONE FAB 220 HEAVY CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS FAB, TESTOSTERONE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR V.ERONEN,T.PARKKINEN,N.HAKULINEN,J.ROUVINEN REVDAT 1 18-SEP-24 8RTW 0 JRNL AUTH V.ERONEN,K.TAKKINEN,A.TORNI,K.PENG,J.JANIS,T.PARKKINEN, JRNL AUTH 2 N.HAKULINEN,J.ROUVINEN JRNL TITL STRUCTURAL INSIGHTS INTO TERNARY IMMUNOCOMPLEX FORMATION AND JRNL TITL 2 CROSS-REACTIVITY: BINDING OF AN ANTI-IMMUNOCOMPLEX FABB12 TO JRNL TITL 3 FAB220-TESTOSTERONE COMPLEX. JRNL REF FEBS J. 2024 JRNL REFN ISSN 1742-464X JRNL PMID 39206623 JRNL DOI 10.1111/FEBS.17258 REMARK 2 REMARK 2 RESOLUTION. 1.99 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.02 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 NUMBER OF REFLECTIONS : 60674 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.290 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 48.0200 - 4.8100 0.91 4171 142 0.1604 0.1620 REMARK 3 2 4.8000 - 3.8100 0.94 4153 142 0.1451 0.1789 REMARK 3 3 3.8100 - 3.3300 0.94 4164 142 0.1685 0.2100 REMARK 3 4 3.3300 - 3.0300 0.95 4157 141 0.1951 0.2063 REMARK 3 5 3.0300 - 2.8100 0.96 4208 144 0.1970 0.2492 REMARK 3 6 2.8100 - 2.6500 0.96 4215 143 0.2158 0.2655 REMARK 3 7 2.6500 - 2.5100 0.97 4248 145 0.2213 0.2640 REMARK 3 8 2.5100 - 2.4000 0.96 4187 143 0.2293 0.2852 REMARK 3 9 2.4000 - 2.3100 0.98 4247 144 0.2347 0.3136 REMARK 3 10 2.3100 - 2.2300 0.97 4252 145 0.2449 0.3226 REMARK 3 11 2.2300 - 2.1600 0.97 4247 144 0.2581 0.3090 REMARK 3 12 2.1600 - 2.1000 0.98 4247 145 0.2936 0.3051 REMARK 3 13 2.1000 - 2.0400 0.95 4108 139 0.3173 0.3160 REMARK 3 14 2.0400 - 1.9900 0.93 4072 139 0.3430 0.3742 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.311 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.116 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.08 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 6858 REMARK 3 ANGLE : 1.100 9358 REMARK 3 CHIRALITY : 0.066 1044 REMARK 3 PLANARITY : 0.011 1186 REMARK 3 DIHEDRAL : 16.852 2432 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 8RTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1292136194. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-23 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 : ESRF REMARK 200 BEAMLINE : MASSIF-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9655 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60707 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990 REMARK 200 RESOLUTION RANGE LOW (A) : 48.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 200 DATA REDUNDANCY : 2.670 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 49.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM SULFATE, TRIS, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K 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 79.18800 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.57950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.18800 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.57950 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 LEU A 0 REMARK 465 GLY B 219 REMARK 465 ALA B 220 REMARK 465 ALA B 221 REMARK 465 ALA B 222 REMARK 465 ALA B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS B 229 REMARK 465 GLU C -1 REMARK 465 LEU C 0 REMARK 465 GLY D 219 REMARK 465 ALA D 220 REMARK 465 ALA D 221 REMARK 465 ALA D 222 REMARK 465 ALA D 223 REMARK 465 HIS D 224 REMARK 465 HIS D 225 REMARK 465 HIS D 226 REMARK 465 HIS D 227 REMARK 465 HIS D 228 REMARK 465 HIS D 229 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 51 -24.16 66.43 REMARK 500 ASN A 212 -147.71 -81.93 REMARK 500 GLU A 213 75.24 71.76 REMARK 500 SER B 44 -168.85 -77.82 REMARK 500 SER B 131 89.78 -48.37 REMARK 500 ALA B 132 -46.11 -141.71 REMARK 500 ALA B 133 -163.14 56.77 REMARK 500 ALA C 51 -23.56 66.79 REMARK 500 ALA C 84 173.83 178.05 REMARK 500 GLN D 134 45.42 -142.84 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 B 59 0.08 SIDE CHAIN REMARK 500 ARG D 59 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8RTW A -1 214 PDB 8RTW 8RTW -1 214 DBREF 8RTW B 1 229 PDB 8RTW 8RTW 1 229 DBREF 8RTW C -1 214 PDB 8RTW 8RTW -1 214 DBREF 8RTW D 1 229 PDB 8RTW 8RTW 1 229 SEQRES 1 A 216 GLU LEU ASP ILE VAL MET THR GLN SER PRO LYS PHE MET SEQRES 2 A 216 SER SER SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS SEQRES 3 A 216 ALA SER GLN ASN VAL GLY ILE ASN VAL ALA TRP TYR GLN SEQRES 4 A 216 GLN LYS PRO GLY GLN SER PRO LYS ALA LEU ILE HIS SER SEQRES 5 A 216 ALA SER TYR ARG TYR SER GLY VAL PRO ASP ARG PHE THR SEQRES 6 A 216 GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 A 216 ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN SEQRES 8 A 216 GLN TYR ASN ILE TYR PRO TRP THR PHE GLY GLY ALA THR SEQRES 9 A 216 LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SEQRES 10 A 216 SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY SEQRES 11 A 216 GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO SEQRES 12 A 216 LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU SEQRES 13 A 216 ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SEQRES 14 A 216 SER LYS ASP SER THR TYR SER MET SER SER THR LEU THR SEQRES 15 A 216 LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR SEQRES 16 A 216 CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL SEQRES 17 A 216 LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 B 229 GLU VAL GLN LEU GLN GLN PRO GLY PRO GLU LEU VAL LYS SEQRES 2 B 229 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 229 TYR SER PHE THR ASP HIS ASN MET TYR TRP VAL LYS GLN SEQRES 4 B 229 SER HIS GLY LYS SER LEU GLU TRP ILE GLY SER ILE ASP SEQRES 5 B 229 PRO TYR ASN GLY GLY THR ARG TYR ASN GLN LYS PHE ARG SEQRES 6 B 229 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER GLY THR SEQRES 7 B 229 ALA PHE MET HIS LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 B 229 ALA VAL TYR TYR CYS TYR ILE GLY SER PHE TYR PHE VAL SEQRES 9 B 229 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 B 229 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 B 229 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 B 229 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 B 229 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 B 229 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 B 229 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 B 229 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 B 229 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY ALA ALA SEQRES 18 B 229 ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 1 C 216 GLU LEU ASP ILE VAL MET THR GLN SER PRO LYS PHE MET SEQRES 2 C 216 SER SER SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS SEQRES 3 C 216 ALA SER GLN ASN VAL GLY ILE ASN VAL ALA TRP TYR GLN SEQRES 4 C 216 GLN LYS PRO GLY GLN SER PRO LYS ALA LEU ILE HIS SER SEQRES 5 C 216 ALA SER TYR ARG TYR SER GLY VAL PRO ASP ARG PHE THR SEQRES 6 C 216 GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 C 216 ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN SEQRES 8 C 216 GLN TYR ASN ILE TYR PRO TRP THR PHE GLY GLY ALA THR SEQRES 9 C 216 LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SEQRES 10 C 216 SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY SEQRES 11 C 216 GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO SEQRES 12 C 216 LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU SEQRES 13 C 216 ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SEQRES 14 C 216 SER LYS ASP SER THR TYR SER MET SER SER THR LEU THR SEQRES 15 C 216 LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR SEQRES 16 C 216 CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL SEQRES 17 C 216 LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 D 229 GLU VAL GLN LEU GLN GLN PRO GLY PRO GLU LEU VAL LYS SEQRES 2 D 229 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 229 TYR SER PHE THR ASP HIS ASN MET TYR TRP VAL LYS GLN SEQRES 4 D 229 SER HIS GLY LYS SER LEU GLU TRP ILE GLY SER ILE ASP SEQRES 5 D 229 PRO TYR ASN GLY GLY THR ARG TYR ASN GLN LYS PHE ARG SEQRES 6 D 229 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER GLY THR SEQRES 7 D 229 ALA PHE MET HIS LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 D 229 ALA VAL TYR TYR CYS TYR ILE GLY SER PHE TYR PHE VAL SEQRES 9 D 229 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 D 229 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 D 229 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 D 229 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 D 229 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 D 229 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 D 229 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 D 229 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 D 229 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY ALA ALA SEQRES 18 D 229 ALA ALA HIS HIS HIS HIS HIS HIS HET TES A 301 21 HET TES C 301 21 HETNAM TES TESTOSTERONE FORMUL 5 TES 2(C19 H28 O2) FORMUL 7 HOH *400(H2 O) HELIX 1 AA1 GLN A 79 LEU A 83 5 5 HELIX 2 AA2 SER A 121 SER A 127 1 7 HELIX 3 AA3 LYS A 183 ARG A 188 1 6 HELIX 4 AA4 SER B 28 HIS B 32 5 5 HELIX 5 AA5 GLN B 62 ARG B 65 5 4 HELIX 6 AA6 THR B 87 SER B 91 5 5 HELIX 7 AA7 SER B 159 SER B 161 5 3 HELIX 8 AA8 PRO B 203 SER B 206 5 4 HELIX 9 AA9 GLN C 79 LEU C 83 5 5 HELIX 10 AB1 SER C 121 SER C 127 1 7 HELIX 11 AB2 LYS C 183 GLU C 187 1 5 HELIX 12 AB3 SER D 28 HIS D 32 5 5 HELIX 13 AB4 GLN D 62 ARG D 65 5 4 HELIX 14 AB5 LYS D 74 SER D 76 5 3 HELIX 15 AB6 THR D 87 SER D 91 5 5 HELIX 16 AB7 SER D 159 SER D 161 5 3 HELIX 17 AB8 PRO D 203 SER D 206 5 4 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O LYS A 24 N THR A 5 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O ILE A 75 N VAL A 19 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N THR A 63 O THR A 74 SHEET 1 AA2 6 PHE A 10 SER A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O GLU A 105 N MET A 11 SHEET 3 AA2 6 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA2 6 VAL A 33 GLN A 38 -1 N TYR A 36 O PHE A 87 SHEET 5 AA2 6 LYS A 45 HIS A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 TYR A 53 ARG A 54 -1 O TYR A 53 N HIS A 49 SHEET 1 AA3 4 PHE A 10 SER A 13 0 SHEET 2 AA3 4 THR A 102 ILE A 106 1 O GLU A 105 N MET A 11 SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 THR A 114 PHE A 118 0 SHEET 2 AA4 4 GLY A 129 PHE A 139 -1 O ASN A 137 N THR A 114 SHEET 3 AA4 4 TYR A 173 THR A 182 -1 O LEU A 179 N VAL A 132 SHEET 4 AA4 4 VAL A 159 TRP A 163 -1 N LEU A 160 O THR A 178 SHEET 1 AA5 4 SER A 153 ARG A 155 0 SHEET 2 AA5 4 ASN A 145 ILE A 150 -1 N ILE A 150 O SER A 153 SHEET 3 AA5 4 SER A 191 THR A 197 -1 O THR A 197 N ASN A 145 SHEET 4 AA5 4 ILE A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SHEET 1 AA6 4 GLN B 3 GLN B 5 0 SHEET 2 AA6 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA6 4 THR B 78 LEU B 83 -1 O MET B 81 N VAL B 20 SHEET 4 AA6 4 ALA B 68 ASP B 73 -1 N THR B 71 O PHE B 80 SHEET 1 AA7 6 GLU B 10 VAL B 12 0 SHEET 2 AA7 6 THR B 110 VAL B 114 1 O THR B 113 N GLU B 10 SHEET 3 AA7 6 ALA B 92 GLY B 99 -1 N ALA B 92 O VAL B 112 SHEET 4 AA7 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA7 6 LEU B 45 ILE B 51 -1 O ILE B 48 N TRP B 36 SHEET 6 AA7 6 THR B 58 TYR B 60 -1 O ARG B 59 N SER B 50 SHEET 1 AA8 4 GLU B 10 VAL B 12 0 SHEET 2 AA8 4 THR B 110 VAL B 114 1 O THR B 113 N GLU B 10 SHEET 3 AA8 4 ALA B 92 GLY B 99 -1 N ALA B 92 O VAL B 112 SHEET 4 AA8 4 VAL B 104 TRP B 106 -1 O TYR B 105 N ILE B 98 SHEET 1 AA9 4 SER B 123 LEU B 127 0 SHEET 2 AA9 4 MET B 138 TYR B 148 -1 O LYS B 146 N SER B 123 SHEET 3 AA9 4 LEU B 177 PRO B 187 -1 O TYR B 178 N TYR B 148 SHEET 4 AA9 4 HIS B 167 THR B 168 -1 N HIS B 167 O SER B 183 SHEET 1 AB1 4 SER B 123 LEU B 127 0 SHEET 2 AB1 4 MET B 138 TYR B 148 -1 O LYS B 146 N SER B 123 SHEET 3 AB1 4 LEU B 177 PRO B 187 -1 O TYR B 178 N TYR B 148 SHEET 4 AB1 4 VAL B 172 GLN B 174 -1 N GLN B 174 O LEU B 177 SHEET 1 AB2 3 THR B 154 TRP B 157 0 SHEET 2 AB2 3 THR B 197 HIS B 202 -1 O ASN B 199 N THR B 156 SHEET 3 AB2 3 THR B 207 LYS B 212 -1 O VAL B 209 N VAL B 200 SHEET 1 AB3 4 MET C 4 SER C 7 0 SHEET 2 AB3 4 VAL C 19 ALA C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AB3 4 ASP C 70 ILE C 75 -1 O LEU C 73 N VAL C 21 SHEET 4 AB3 4 PHE C 62 SER C 67 -1 N SER C 65 O THR C 72 SHEET 1 AB4 6 PHE C 10 SER C 13 0 SHEET 2 AB4 6 THR C 102 ILE C 106 1 O GLU C 105 N MET C 11 SHEET 3 AB4 6 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB4 6 VAL C 33 GLN C 38 -1 N TYR C 36 O PHE C 87 SHEET 5 AB4 6 LYS C 45 HIS C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AB4 6 TYR C 53 ARG C 54 -1 O TYR C 53 N HIS C 49 SHEET 1 AB5 4 PHE C 10 SER C 13 0 SHEET 2 AB5 4 THR C 102 ILE C 106 1 O GLU C 105 N MET C 11 SHEET 3 AB5 4 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB5 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AB6 4 THR C 114 PHE C 118 0 SHEET 2 AB6 4 GLY C 129 PHE C 139 -1 O ASN C 137 N THR C 114 SHEET 3 AB6 4 TYR C 173 THR C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 AB6 4 VAL C 159 TRP C 163 -1 N SER C 162 O SER C 176 SHEET 1 AB7 4 SER C 153 ARG C 155 0 SHEET 2 AB7 4 ASN C 145 ILE C 150 -1 N ILE C 150 O SER C 153 SHEET 3 AB7 4 SER C 191 THR C 197 -1 O THR C 197 N ASN C 145 SHEET 4 AB7 4 ILE C 205 ASN C 210 -1 O LYS C 207 N CYS C 194 SHEET 1 AB8 4 GLN D 3 GLN D 5 0 SHEET 2 AB8 4 VAL D 18 SER D 25 -1 O LYS D 23 N GLN D 5 SHEET 3 AB8 4 THR D 78 LEU D 83 -1 O MET D 81 N VAL D 20 SHEET 4 AB8 4 ALA D 68 ASP D 73 -1 N THR D 71 O PHE D 80 SHEET 1 AB9 6 GLU D 10 VAL D 12 0 SHEET 2 AB9 6 THR D 110 VAL D 114 1 O THR D 113 N VAL D 12 SHEET 3 AB9 6 ALA D 92 GLY D 99 -1 N ALA D 92 O VAL D 112 SHEET 4 AB9 6 MET D 34 GLN D 39 -1 N TYR D 35 O TYR D 97 SHEET 5 AB9 6 LEU D 45 ILE D 51 -1 O ILE D 51 N MET D 34 SHEET 6 AB9 6 THR D 58 TYR D 60 -1 O ARG D 59 N SER D 50 SHEET 1 AC1 4 GLU D 10 VAL D 12 0 SHEET 2 AC1 4 THR D 110 VAL D 114 1 O THR D 113 N VAL D 12 SHEET 3 AC1 4 ALA D 92 GLY D 99 -1 N ALA D 92 O VAL D 112 SHEET 4 AC1 4 VAL D 104 TRP D 106 -1 O TYR D 105 N ILE D 98 SHEET 1 AC2 4 SER D 123 LEU D 127 0 SHEET 2 AC2 4 MET D 138 TYR D 148 -1 O GLY D 142 N LEU D 127 SHEET 3 AC2 4 LEU D 177 PRO D 187 -1 O LEU D 180 N VAL D 145 SHEET 4 AC2 4 VAL D 166 THR D 168 -1 N HIS D 167 O SER D 183 SHEET 1 AC3 4 SER D 123 LEU D 127 0 SHEET 2 AC3 4 MET D 138 TYR D 148 -1 O GLY D 142 N LEU D 127 SHEET 3 AC3 4 LEU D 177 PRO D 187 -1 O LEU D 180 N VAL D 145 SHEET 4 AC3 4 VAL D 172 GLN D 174 -1 N GLN D 174 O LEU D 177 SHEET 1 AC4 3 THR D 154 TRP D 157 0 SHEET 2 AC4 3 THR D 197 HIS D 202 -1 O ASN D 199 N THR D 156 SHEET 3 AC4 3 THR D 207 LYS D 212 -1 O VAL D 209 N VAL D 200 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.08 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.03 SSBOND 3 CYS A 214 CYS B 218 1555 1555 2.03 SSBOND 4 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 5 CYS B 143 CYS B 198 1555 1555 2.03 SSBOND 6 CYS C 23 CYS C 88 1555 1555 2.05 SSBOND 7 CYS C 134 CYS C 194 1555 1555 2.01 SSBOND 8 CYS C 214 CYS D 218 1555 1555 2.04 SSBOND 9 CYS D 22 CYS D 96 1555 1555 2.05 SSBOND 10 CYS D 143 CYS D 198 1555 1555 2.03 CISPEP 1 SER A 7 PRO A 8 0 -1.67 CISPEP 2 TYR A 94 PRO A 95 0 -12.66 CISPEP 3 TYR A 140 PRO A 141 0 -1.87 CISPEP 4 PHE B 149 PRO B 150 0 -8.52 CISPEP 5 GLU B 151 PRO B 152 0 0.22 CISPEP 6 TRP B 191 PRO B 192 0 5.44 CISPEP 7 SER C 7 PRO C 8 0 -0.93 CISPEP 8 TYR C 94 PRO C 95 0 -9.06 CISPEP 9 TYR C 140 PRO C 141 0 2.37 CISPEP 10 PHE D 149 PRO D 150 0 -9.32 CISPEP 11 GLU D 151 PRO D 152 0 2.83 CISPEP 12 TRP D 191 PRO D 192 0 -0.97 CRYST1 158.376 53.159 111.947 90.00 96.40 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 0.006314 0.000000 0.000708 0.00000 SCALE2 0.000000 0.018811 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008989 0.00000