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HEADER IMMUNE SYSTEM 26-JUN-01 1JGL TITLE CRYSTAL STRUCTURE OF IMMUNOGLOBULIN FAB FRAGMENT COMPLEXED TITLE 2 WITH 17-BETA-ESTRADIOL COMPND MOL_ID: 1; COMPND 2 MOLECULE: IG KAPPA-CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IG GAMMA-1-CHAIN; COMPND 7 CHAIN: H; COMPND 8 FRAGMENT: RESIDUES 1-215; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOMB3; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PCOMB3 KEYWDS ANTIBODY, FOUR-CENTER HYDROGEN BOND, STEROID EXPDTA X-RAY DIFFRACTION AUTHOR U.LAMMINMAKI,J.A.KANKARE REVDAT 2 25-DEC-02 1JGL 1 REMARK REVDAT 1 10-OCT-01 1JGL 0 JRNL AUTH U.LAMMINMAKI,J.A.KANKARE JRNL TITL CRYSTAL STRUCTURE OF A RECOMBINANT ANTI-ESTRADIOL JRNL TITL 2 FAB FRAGMENT IN COMPLEX WITH 17BETA -ESTRADIOL. JRNL REF J.BIOL.CHEM. V. 276 36687 2001 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH U.LAMMINMAKI,J.A.KANKARE REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF REMARK 1 TITL 2 A RECOMBINANT FAB FRAGMENT IN COMPLEX WITH REMARK 1 TITL 3 17-BETA-ESTRADIOL REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 56 1670 2000 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 2.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.28 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 450405.290 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.6 REMARK 3 NUMBER OF REFLECTIONS : 25614 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 SET) : 0.199 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2529 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2909 REMARK 3 BIN R VALUE (WORKING SET) : 0.2310 REMARK 3 BIN FREE R VALUE : 0.2980 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 310 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3225 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 20 REMARK 3 SOLVENT ATOMS : 340 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 11.60000 REMARK 3 B22 (A**2) : -3.62000 REMARK 3 B33 (A**2) : -7.98000 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24 REMARK 3 ESD FROM SIGMAA (A) : 0.18 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.93 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 49.54 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JGL COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB013746. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 9.10 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200HB REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25614 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25 REMARK 200 COMPLETENESS FOR SHELL (%) : 71.9 REMARK 200 DATA REDUNDANCY IN SHELL : 1.80 REMARK 200 R MERGE FOR SHELL (I) : 0.13500 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: CNS REMARK 200 STARTING MODEL: COMBINATION PDB ENTRIES 1TET (HEAVY CHAIN REMARK 200 VARIABLE DOMAIN)AND 1FDL (LIGHT CHAIN VARIABLE DOMAIN AND BOTH REMARK 200 CONSTANT_1 DOMAINS) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PEG8000, TRIS-HCL, PH 9.1, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 24.10350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.64250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.24800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.64250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.10350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.24800 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: L, H 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 CYS L 214 REMARK 465 SER H 28 REMARK 465 PHE H 29 REMARK 465 THR H 73 REMARK 465 SER H 74 REMARK 465 ALA H 75 REMARK 465 SER H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 GLN H 131 REMARK 465 THR H 132 REMARK 465 ASP H 214 REMARK 465 CYS H 215 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET H 34 SD MET H 34 CE -0.057 REMARK 500 PRO H 149 CG PRO H 149 CD 0.047 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLY L 99 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 THR L 114 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 ASN L 137 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 THR L 182 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 THR L 197 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 ILE L 205 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 VAL L 206 N - CA - C ANGL. DEV. = 9.9 DEGREES REMARK 500 LEU H 80 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LYS H 143 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLY H 144 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 LEU H 177 CA - CB - CG ANGL. DEV. = 9.9 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA L 51 -37.20 68.43 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JHK RELATED DB: PDB REMARK 900 1JHK CONTAINS THE SAME PROTEIN(UNCOMPLEXED FORM). DBREF 1JGL L 1 214 UNP Q920E6 Q920E6_MOUSE 15 228 DBREF 1JGL H 1 215 GB 2072131 AAB53773 12 229 SEQADV 1JGL PHE L 118 UNP Q920E6 LEU 132 SEE REMARK 999 SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 L 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY THR TYR TYR CYS HIS HIS PHE SEQRES 8 L 214 TRP SER THR PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU VAL LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 H 218 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 H 218 PRO GLY GLU THR VAL ARG ILE SER CYS LYS ALA SER ASP SEQRES 3 H 218 TYR SER PHE MET THR SER GLY MET GLN TRP VAL GLN GLN SEQRES 4 H 218 MET PRO GLY LYS GLY LEU LYS TRP ILE GLY TRP LEU ASN SEQRES 5 H 218 THR GLN SER GLY VAL PRO GLU TYR ALA GLU ASP PHE LYS SEQRES 6 H 218 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA THR THR SEQRES 7 H 218 ALA TYR LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 H 218 ALA THR TYR PHE CYS ALA THR TRP GLY GLY ASN SER ALA SEQRES 9 H 218 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA SEQRES 10 H 218 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 H 218 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 H 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 H 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 218 SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR SEQRES 16 H 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS HET EST 911 20 HETNAM EST ESTRADIOL FORMUL 3 EST C18 H24 O2 FORMUL 4 HOH *340(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 ARG L 188 1 6 HELIX 4 4 GLU H 61 LYS H 64 5 4 HELIX 5 5 LYS H 83 THR H 87 5 5 HELIX 6 6 SER H 156 SER H 158 5 3 HELIX 7 7 PRO H 200 SER H 203 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 ALA L 25 -1 N THR L 22 O SER L 7 SHEET 3 A 4 GLN L 70 ILE L 75 -1 N TYR L 71 O CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 O SER L 63 N LYS L 74 SHEET 1 B 6 SER L 10 ALA L 13 0 SHEET 2 B 6 THR L 102 VAL L 106 1 O LYS L 103 N LEU L 11 SHEET 3 B 6 GLY L 84 HIS L 90 -1 O GLY L 84 N LEU L 104 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N ALA L 34 O HIS L 89 SHEET 5 B 6 GLN L 45 TYR L 49 -1 N GLN L 45 O GLN L 37 SHEET 6 B 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 C 4 THR L 114 PHE L 118 0 SHEET 2 C 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 C 4 TYR L 173 THR L 182 -1 N TYR L 173 O PHE L 139 SHEET 4 C 4 VAL L 159 TRP L 163 -1 O LEU L 160 N THR L 178 SHEET 1 D 4 SER L 153 ARG L 155 0 SHEET 2 D 4 ASN L 145 ILE L 150 -1 O TRP L 148 N ARG L 155 SHEET 3 D 4 SER L 191 THR L 197 -1 N THR L 193 O LYS L 149 SHEET 4 D 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 E 4 LEU H 4 GLN H 6 0 SHEET 2 E 4 VAL H 18 ALA H 24 -1 N LYS H 23 O VAL H 5 SHEET 3 E 4 THR H 77 ILE H 82 -1 N ALA H 78 O CYS H 22 SHEET 4 E 4 PHE H 67 LEU H 71 -1 O ALA H 68 N GLN H 81 SHEET 1 F 5 VAL H 56 TYR H 59 0 SHEET 2 F 5 LEU H 45 ASN H 52 -1 O TRP H 50 N GLU H 58 SHEET 3 F 5 MET H 34 GLN H 39 -1 O MET H 34 N LEU H 51 SHEET 4 F 5 ALA H 88 GLY H 96 -1 N THR H 89 O GLN H 39 SHEET 5 F 5 SER H 99 TRP H 103 -1 O SER H 99 N GLY H 96 SHEET 1 G 6 VAL H 56 TYR H 59 0 SHEET 2 G 6 LEU H 45 ASN H 52 -1 O TRP H 50 N GLU H 58 SHEET 3 G 6 MET H 34 GLN H 39 -1 O MET H 34 N LEU H 51 SHEET 4 G 6 ALA H 88 GLY H 96 -1 N THR H 89 O GLN H 39 SHEET 5 G 6 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 6 G 6 GLU H 10 LYS H 12 1 N GLU H 10 O THR H 108 SHEET 1 H 4 SER H 120 LEU H 124 0 SHEET 2 H 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 H 4 LEU H 174 PRO H 184 -1 N TYR H 175 O TYR H 145 SHEET 4 H 4 VAL H 163 THR H 165 -1 O HIS H 164 N SER H 180 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 I 4 LEU H 174 PRO H 184 -1 N TYR H 175 O TYR H 145 SHEET 4 I 4 VAL H 169 GLN H 171 -1 N VAL H 169 O THR H 176 SHEET 1 J 3 THR H 151 TRP H 154 0 SHEET 2 J 3 THR H 194 HIS H 199 -1 N ASN H 196 O THR H 153 SHEET 3 J 3 THR H 204 LYS H 209 -1 O THR H 204 N HIS H 199 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 195 CISPEP 1 SER L 7 PRO L 8 0 -0.11 CISPEP 2 THR L 94 PRO L 95 0 0.14 CISPEP 3 TYR L 140 PRO L 141 0 1.17 CISPEP 4 PHE H 146 PRO H 147 0 0.20 CISPEP 5 GLU H 148 PRO H 149 0 -0.17 CISPEP 6 TRP H 188 PRO H 189 0 1.51 CRYST1 48.207 64.496 165.285 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 0.020744 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015505 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006050 0.00000