HEADER OXIDOREDUCTASE 12-SEP-03 1QYW
TITLE CRYSTAL STRUCTURE OF HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID
TITLE 2 DEHYDROGENASE COMPLEX WITH ANDROSTANEDIONE AND NADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTRADIOL 17 BETA-DEHYDROGENASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 17-BETA-HSD 1, PLACENTAL 17-BETA-HYDROXYSTEROID
COMPND 5 DEHYDROGENASE, 20 ALPHA- HYDROXYSTEROID DEHYDROGENASE, 20-ALPHA-HSD,
COMPND 6 E2DH;
COMPND 7 EC: 1.1.1.62
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLACENTA
KEYWDS 17BHSD1, ANDROSTANEDIONE, C19-STEROID, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SHI,S.X.LIN
REVDAT 6 23-AUG-23 1QYW 1 REMARK
REVDAT 5 11-OCT-17 1QYW 1 REMARK
REVDAT 4 12-OCT-16 1QYW 1 TITLE
REVDAT 3 13-JUL-11 1QYW 1 VERSN
REVDAT 2 24-FEB-09 1QYW 1 VERSN
REVDAT 1 03-AUG-04 1QYW 0
JRNL AUTH R.SHI,S.X.LIN
JRNL TITL COFACTOR HYDROGEN BONDING ONTO THE PROTEIN MAIN CHAIN IS
JRNL TITL 2 CONSERVED IN THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY
JRNL TITL 3 AND CONTRIBUTES TO NICOTINAMIDE ORIENTATION.
JRNL REF J.BIOL.CHEM. V. 279 16778 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14966133
JRNL DOI 10.1074/JBC.M313156200
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 38107
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1867
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2116
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.90
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020237.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-01
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 : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38394
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.530
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.47
REMARK 200 R MERGE FOR SHELL (I) : 0.45400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: RIGID BODY REFINEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 1JTV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNISUM CHLORIDE, BETA
REMARK 280 -OCTYLGLUCOSIDE, HEPES, GLYCEROL, SOAKING WITH
REMARK 280 DIHYDROTESTOSTERONE AND NADP, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 300K
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 61.32300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.96300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.32300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.96300
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY
REMARK 300 THE TWO FOLD AXIS: -X, Y, -Z.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A 191
REMARK 465 PHE A 192
REMARK 465 MET A 193
REMARK 465 GLU A 194
REMARK 465 LYS A 195
REMARK 465 VAL A 196
REMARK 465 LEU A 197
REMARK 465 GLY A 198
REMARK 465 GLY A 285
REMARK 465 ASP A 286
REMARK 465 VAL A 287
REMARK 465 PRO A 288
REMARK 465 ALA A 289
REMARK 465 LYS A 290
REMARK 465 ALA A 291
REMARK 465 GLU A 292
REMARK 465 ALA A 293
REMARK 465 GLY A 294
REMARK 465 ALA A 295
REMARK 465 GLU A 296
REMARK 465 ALA A 297
REMARK 465 GLY A 298
REMARK 465 GLY A 299
REMARK 465 GLY A 300
REMARK 465 ALA A 301
REMARK 465 GLY A 302
REMARK 465 PRO A 303
REMARK 465 GLY A 304
REMARK 465 ALA A 305
REMARK 465 GLU A 306
REMARK 465 ASP A 307
REMARK 465 GLU A 308
REMARK 465 ALA A 309
REMARK 465 GLY A 310
REMARK 465 ARG A 311
REMARK 465 SER A 312
REMARK 465 ALA A 313
REMARK 465 VAL A 314
REMARK 465 GLY A 315
REMARK 465 ASP A 316
REMARK 465 PRO A 317
REMARK 465 GLU A 318
REMARK 465 LEU A 319
REMARK 465 GLY A 320
REMARK 465 ASP A 321
REMARK 465 PRO A 322
REMARK 465 PRO A 323
REMARK 465 ALA A 324
REMARK 465 ALA A 325
REMARK 465 PRO A 326
REMARK 465 GLN A 327
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 629 O HOH A 766 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 76 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 136 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 252 CG - CD - NE ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG A 266 NE - CZ - NH1 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 VAL A 115 -60.11 -102.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 SEVERAL ATOMS BELONGING TO NICOTINAMIDE PART OF HETNAM
REMARK 600 'NAP' COULD NOT BE MODELED AND ARE MISSING FROM THE
REMARK 600 COORDINATES
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAP A 361
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5SD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IOL RELATED DB: PDB
REMARK 900 17BHSD1-ESTRADIOL COMPLEX
REMARK 900 RELATED ID: 1JTV RELATED DB: PDB
REMARK 900 17BHSD1-TESTOSTERONE COMPLEX
REMARK 900 RELATED ID: 1QYV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID
REMARK 900 DEHYDROGENASE COMPLEX WITH NADP
REMARK 900 RELATED ID: 1QYX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID
REMARK 900 DEHYDROGENASE COMPLEX WITH ANDROSTENEDIONE AND NADP
DBREF 1QYW A 1 327 UNP P14061 DHB1_HUMAN 1 327
SEQRES 1 A 327 ALA ARG THR VAL VAL LEU ILE THR GLY CYS SER SER GLY
SEQRES 2 A 327 ILE GLY LEU HIS LEU ALA VAL ARG LEU ALA SER ASP PRO
SEQRES 3 A 327 SER GLN SER PHE LYS VAL TYR ALA THR LEU ARG ASP LEU
SEQRES 4 A 327 LYS THR GLN GLY ARG LEU TRP GLU ALA ALA ARG ALA LEU
SEQRES 5 A 327 ALA CYS PRO PRO GLY SER LEU GLU THR LEU GLN LEU ASP
SEQRES 6 A 327 VAL ARG ASP SER LYS SER VAL ALA ALA ALA ARG GLU ARG
SEQRES 7 A 327 VAL THR GLU GLY ARG VAL ASP VAL LEU VAL CYS ASN ALA
SEQRES 8 A 327 GLY LEU GLY LEU LEU GLY PRO LEU GLU ALA LEU GLY GLU
SEQRES 9 A 327 ASP ALA VAL ALA SER VAL LEU ASP VAL ASN VAL VAL GLY
SEQRES 10 A 327 THR VAL ARG MET LEU GLN ALA PHE LEU PRO ASP MET LYS
SEQRES 11 A 327 ARG ARG GLY SER GLY ARG VAL LEU VAL THR GLY SER VAL
SEQRES 12 A 327 GLY GLY LEU MET GLY LEU PRO PHE ASN ASP VAL TYR CYS
SEQRES 13 A 327 ALA SER LYS PHE ALA LEU GLU GLY LEU CYS GLU SER LEU
SEQRES 14 A 327 ALA VAL LEU LEU LEU PRO PHE GLY VAL HIS LEU SER LEU
SEQRES 15 A 327 ILE GLU CYS GLY PRO VAL HIS THR ALA PHE MET GLU LYS
SEQRES 16 A 327 VAL LEU GLY SER PRO GLU GLU VAL LEU ASP ARG THR ASP
SEQRES 17 A 327 ILE HIS THR PHE HIS ARG PHE TYR GLN TYR LEU ALA HIS
SEQRES 18 A 327 SER LYS GLN VAL PHE ARG GLU ALA ALA GLN ASN PRO GLU
SEQRES 19 A 327 GLU VAL ALA GLU VAL PHE LEU THR ALA LEU ARG ALA PRO
SEQRES 20 A 327 LYS PRO THR LEU ARG TYR PHE THR THR GLU ARG PHE LEU
SEQRES 21 A 327 PRO LEU LEU ARG MET ARG LEU ASP ASP PRO SER GLY SER
SEQRES 22 A 327 ASN TYR VAL THR ALA MET HIS ARG GLU VAL PHE GLY ASP
SEQRES 23 A 327 VAL PRO ALA LYS ALA GLU ALA GLY ALA GLU ALA GLY GLY
SEQRES 24 A 327 GLY ALA GLY PRO GLY ALA GLU ASP GLU ALA GLY ARG SER
SEQRES 25 A 327 ALA VAL GLY ASP PRO GLU LEU GLY ASP PRO PRO ALA ALA
SEQRES 26 A 327 PRO GLN
HET 5SD A 500 21
HET NAP A 361 27
HET GOL A 600 6
HETNAM 5SD 5ALPHA-ANDROSTAN-3,17-DIONE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 5SD C19 H28 O2
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *218(H2 O)
HELIX 1 1 SER A 12 SER A 24 1 13
HELIX 2 2 ASP A 38 THR A 41 5 4
HELIX 3 3 GLN A 42 LEU A 52 1 11
HELIX 4 4 ASP A 68 ARG A 78 1 11
HELIX 5 5 PRO A 98 LEU A 102 5 5
HELIX 6 6 GLY A 103 VAL A 115 1 13
HELIX 7 7 VAL A 115 GLY A 133 1 19
HELIX 8 8 GLY A 144 LEU A 146 5 3
HELIX 9 9 ASN A 152 LEU A 174 1 23
HELIX 10 10 SER A 199 ARG A 206 1 8
HELIX 11 11 ASP A 208 ALA A 230 1 23
HELIX 12 12 ASN A 232 ALA A 246 1 15
HELIX 13 13 PHE A 259 ASP A 269 1 11
HELIX 14 14 GLY A 272 PHE A 284 1 13
SHEET 1 A 7 LEU A 59 GLN A 63 0
SHEET 2 A 7 PHE A 30 LEU A 36 1 N ALA A 34 O GLU A 60
SHEET 3 A 7 THR A 3 ILE A 7 1 N VAL A 5 O TYR A 33
SHEET 4 A 7 VAL A 86 CYS A 89 1 O VAL A 88 N LEU A 6
SHEET 5 A 7 GLY A 135 SER A 142 1 O ARG A 136 N LEU A 87
SHEET 6 A 7 VAL A 178 CYS A 185 1 O HIS A 179 N VAL A 137
SHEET 7 A 7 ARG A 252 PHE A 254 1 O TYR A 253 N GLU A 184
SITE 1 AC1 4 VAL A 143 HIS A 221 SER A 222 HOH A 651
SITE 1 AC2 20 GLY A 9 SER A 11 SER A 12 ARG A 37
SITE 2 AC2 20 LEU A 64 ASP A 65 VAL A 66 ARG A 67
SITE 3 AC2 20 ALA A 91 GLY A 92 LEU A 93 VAL A 113
SITE 4 AC2 20 HOH A 601 HOH A 605 HOH A 617 HOH A 671
SITE 5 AC2 20 HOH A 687 HOH A 787 HOH A 792 HOH A 811
SITE 1 AC3 7 ARG A 252 ARG A 266 ASP A 269 PRO A 270
SITE 2 AC3 7 HOH A 627 HOH A 636 HOH A 642
CRYST1 122.646 43.926 60.793 90.00 99.76 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 0.008154 0.000000 0.001402 0.00000
SCALE2 0.000000 0.022766 -0.000001 0.00000
SCALE3 0.000000 0.000000 0.016691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
