HEADER OXIDOREDUCTASE 12-OCT-06 2IPG
TITLE CRYSTAL STRUCTURE OF 17ALPHA-HYDROXYSTEROID DEHYDROGENASE MUTANT K31A
TITLE 2 IN COMPLEX WITH NADP+ AND EPI-TESTOSTERONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3(17)ALPHA-HYDROXYSTEROID DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.-,1.1.1.209;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: AKR1C21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX1LT
KEYWDS 17A-HSD, AKR1C21, AKR, ALDO-KETO REDUCTASE, HSD, HYDROXYSTEROID
KEYWDS 2 DEHYDROGENASE, OPEN CONFORMATION, EPI-TESTOSTERONE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FAUCHER,L.CANTIN,K.PEREIRA DE JESUS-TRAN,M.LEMIEUX,V.LUU-THE,
AUTHOR 2 F.LABRIE,R.BRETON
REVDAT 6 30-AUG-23 2IPG 1 REMARK
REVDAT 5 06-FEB-19 2IPG 1 COMPND SOURCE DBREF SEQADV
REVDAT 5 2 1 HET HETNAM FORMUL
REVDAT 4 16-MAY-12 2IPG 1 MTRIX1 MTRIX2 MTRIX3 VERSN
REVDAT 3 12-MAY-09 2IPG 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 2 24-FEB-09 2IPG 1 VERSN
REVDAT 1 19-JUN-07 2IPG 0
JRNL AUTH F.FAUCHER,L.CANTIN,K.PEREIRA DE JESUS-TRAN,M.LEMIEUX,
JRNL AUTH 2 V.LUU-THE,F.LABRIE,R.BRETON
JRNL TITL MOUSE 17ALPHA-HYDROXYSTEROID DEHYDROGENASE (AKR1C21) BINDS
JRNL TITL 2 STEROIDS DIFFERENTLY FROM OTHER ALDO-KETO REDUCTASES:
JRNL TITL 3 IDENTIFICATION AND CHARACTERIZATION OF AMINO ACID RESIDUES
JRNL TITL 4 CRITICAL FOR SUBSTRATE BINDING.
JRNL REF J.MOL.BIOL. V. 369 525 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17442338
JRNL DOI 10.1016/J.JMB.2007.03.058
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1754729.910
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 49676
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) : 0.182
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2514
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7568
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE : 0.2320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 364
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 166
REMARK 3 SOLVENT ATOMS : 481
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.27000
REMARK 3 B22 (A**2) : -1.30000
REMARK 3 B33 (A**2) : -2.97000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.92000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.490 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 43.10
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : LIGANDS_.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : LIGANDS_.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-06; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; NULL
REMARK 200 RADIATION SOURCE : ROTATING ANODE; NULL
REMARK 200 BEAMLINE : NULL; NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : MIRRORS; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; NULL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43065
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : 0.17200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.19100
REMARK 200 R SYM FOR SHELL (I) : 0.26200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.930
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2IPF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-4000 24%, 0.1M MES, O.1M LI2SO4,
REMARK 280 PH 6.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 26.67000
REMARK 290 SMTRY3 2 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: 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 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 PRO A 119 31.71 -83.19
REMARK 500 THR A 221 159.80 73.51
REMARK 500 ARG A 250 -145.81 -121.73
REMARK 500 ARG A 301 22.57 -146.21
REMARK 500 PRO B 119 31.26 -83.05
REMARK 500 LEU B 197 75.40 -151.17
REMARK 500 THR B 221 160.84 76.06
REMARK 500 ARG B 250 -157.55 -128.44
REMARK 500 ARG B 301 20.37 -147.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FFA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FFA B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 327
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IPJ RELATED DB: PDB
REMARK 900 RELATED ID: 2IPF RELATED DB: PDB
DBREF 2IPG A 5 323 UNP Q91WR5 AK1CL_MOUSE 5 323
DBREF 2IPG B 5 323 UNP Q91WR5 AK1CL_MOUSE 5 323
SEQADV 2IPG ALA A 31 UNP Q91WR5 LYS 31 ENGINEERED MUTATION
SEQADV 2IPG ALA B 31 UNP Q91WR5 LYS 31 ENGINEERED MUTATION
SEQRES 1 A 319 CYS HIS CYS VAL ILE LEU ASN ASP GLY ASN PHE ILE PRO
SEQRES 2 A 319 VAL LEU GLY PHE GLY THR ALA LEU PRO LEU GLU CYS PRO
SEQRES 3 A 319 ALA SER LYS ALA LYS GLU LEU THR LYS ILE ALA ILE ASP
SEQRES 4 A 319 ALA GLY PHE HIS HIS PHE ASP SER ALA SER VAL TYR ASN
SEQRES 5 A 319 THR GLU ASP HIS VAL GLY GLU ALA ILE ARG SER LYS ILE
SEQRES 6 A 319 ALA ASP GLY THR VAL ARG ARG GLU ASP ILE PHE TYR THR
SEQRES 7 A 319 SER LYS VAL TRP CYS THR SER LEU HIS PRO GLU LEU VAL
SEQRES 8 A 319 ARG ALA SER LEU GLU ARG SER LEU GLN LYS LEU GLN PHE
SEQRES 9 A 319 ASP TYR VAL ASP LEU TYR LEU ILE HIS TYR PRO MET ALA
SEQRES 10 A 319 LEU LYS PRO GLY GLU GLU ASN PHE PRO VAL ASP GLU HIS
SEQRES 11 A 319 GLY LYS LEU ILE PHE ASP ARG VAL ASP LEU CYS ALA THR
SEQRES 12 A 319 TRP GLU ALA MET GLU LYS CYS LYS ASP ALA GLY LEU THR
SEQRES 13 A 319 LYS SER ILE GLY VAL SER ASN PHE ASN TYR ARG GLN LEU
SEQRES 14 A 319 GLU MET ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO
SEQRES 15 A 319 VAL CYS ASN GLN VAL GLU CYS HIS PRO TYR LEU ASN GLN
SEQRES 16 A 319 MET LYS LEU LEU ASP PHE CYS LYS SER LYS ASP ILE VAL
SEQRES 17 A 319 LEU VAL ALA TYR GLY VAL LEU GLY THR GLN ARG TYR GLY
SEQRES 18 A 319 GLY TRP VAL ASP GLN ASN SER PRO VAL LEU LEU ASP GLU
SEQRES 19 A 319 PRO VAL LEU GLY SER MET ALA LYS LYS TYR ASN ARG THR
SEQRES 20 A 319 PRO ALA LEU ILE ALA LEU ARG TYR GLN LEU GLN ARG GLY
SEQRES 21 A 319 ILE VAL VAL LEU ASN THR SER LEU LYS GLU GLU ARG ILE
SEQRES 22 A 319 LYS GLU ASN MET GLN VAL PHE GLU PHE GLN LEU SER SER
SEQRES 23 A 319 GLU ASP MET LYS VAL LEU ASP GLY LEU ASN ARG ASN MET
SEQRES 24 A 319 ARG TYR ILE PRO ALA ALA ILE PHE LYS GLY HIS PRO ASN
SEQRES 25 A 319 TRP PRO PHE LEU ASP GLU TYR
SEQRES 1 B 319 CYS HIS CYS VAL ILE LEU ASN ASP GLY ASN PHE ILE PRO
SEQRES 2 B 319 VAL LEU GLY PHE GLY THR ALA LEU PRO LEU GLU CYS PRO
SEQRES 3 B 319 ALA SER LYS ALA LYS GLU LEU THR LYS ILE ALA ILE ASP
SEQRES 4 B 319 ALA GLY PHE HIS HIS PHE ASP SER ALA SER VAL TYR ASN
SEQRES 5 B 319 THR GLU ASP HIS VAL GLY GLU ALA ILE ARG SER LYS ILE
SEQRES 6 B 319 ALA ASP GLY THR VAL ARG ARG GLU ASP ILE PHE TYR THR
SEQRES 7 B 319 SER LYS VAL TRP CYS THR SER LEU HIS PRO GLU LEU VAL
SEQRES 8 B 319 ARG ALA SER LEU GLU ARG SER LEU GLN LYS LEU GLN PHE
SEQRES 9 B 319 ASP TYR VAL ASP LEU TYR LEU ILE HIS TYR PRO MET ALA
SEQRES 10 B 319 LEU LYS PRO GLY GLU GLU ASN PHE PRO VAL ASP GLU HIS
SEQRES 11 B 319 GLY LYS LEU ILE PHE ASP ARG VAL ASP LEU CYS ALA THR
SEQRES 12 B 319 TRP GLU ALA MET GLU LYS CYS LYS ASP ALA GLY LEU THR
SEQRES 13 B 319 LYS SER ILE GLY VAL SER ASN PHE ASN TYR ARG GLN LEU
SEQRES 14 B 319 GLU MET ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO
SEQRES 15 B 319 VAL CYS ASN GLN VAL GLU CYS HIS PRO TYR LEU ASN GLN
SEQRES 16 B 319 MET LYS LEU LEU ASP PHE CYS LYS SER LYS ASP ILE VAL
SEQRES 17 B 319 LEU VAL ALA TYR GLY VAL LEU GLY THR GLN ARG TYR GLY
SEQRES 18 B 319 GLY TRP VAL ASP GLN ASN SER PRO VAL LEU LEU ASP GLU
SEQRES 19 B 319 PRO VAL LEU GLY SER MET ALA LYS LYS TYR ASN ARG THR
SEQRES 20 B 319 PRO ALA LEU ILE ALA LEU ARG TYR GLN LEU GLN ARG GLY
SEQRES 21 B 319 ILE VAL VAL LEU ASN THR SER LEU LYS GLU GLU ARG ILE
SEQRES 22 B 319 LYS GLU ASN MET GLN VAL PHE GLU PHE GLN LEU SER SER
SEQRES 23 B 319 GLU ASP MET LYS VAL LEU ASP GLY LEU ASN ARG ASN MET
SEQRES 24 B 319 ARG TYR ILE PRO ALA ALA ILE PHE LYS GLY HIS PRO ASN
SEQRES 25 B 319 TRP PRO PHE LEU ASP GLU TYR
HET NAP A 1 48
HET FFA A 3 21
HET BME A 324 4
HET BME A 325 4
HET EDO A 326 4
HET EDO A 327 4
HET NAP B 2 48
HET FFA B 4 21
HET BME B 324 4
HET BME B 325 4
HET EDO B 326 4
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM FFA (10ALPHA,13ALPHA,14BETA,17ALPHA)-17-HYDROXYANDROST-4-
HETNAM 2 FFA EN-3-ONE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN FFA EPI-TESTOSTERONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 FFA 2(C19 H28 O2)
FORMUL 5 BME 4(C2 H6 O S)
FORMUL 7 EDO 3(C2 H6 O2)
FORMUL 14 HOH *481(H2 O)
HELIX 1 1 SER A 32 GLY A 45 1 14
HELIX 2 2 ALA A 52 ASN A 56 5 5
HELIX 3 3 THR A 57 ASP A 71 1 15
HELIX 4 4 ARG A 75 ILE A 79 5 5
HELIX 5 5 TRP A 86 LEU A 90 5 5
HELIX 6 6 LEU A 94 GLN A 107 1 14
HELIX 7 7 ASP A 143 ALA A 157 1 15
HELIX 8 8 ASN A 169 ASN A 178 1 10
HELIX 9 9 GLN A 199 LYS A 209 1 11
HELIX 10 10 VAL A 234 ASP A 237 5 4
HELIX 11 11 GLU A 238 ASN A 249 1 12
HELIX 12 12 THR A 251 GLN A 262 1 12
HELIX 13 13 LYS A 273 MET A 281 1 9
HELIX 14 14 GLN A 282 PHE A 286 5 5
HELIX 15 15 SER A 289 GLY A 298 1 10
HELIX 16 16 ALA A 308 LYS A 312 5 5
HELIX 17 17 SER B 32 GLY B 45 1 14
HELIX 18 18 ALA B 52 ASN B 56 5 5
HELIX 19 19 THR B 57 ASP B 71 1 15
HELIX 20 20 ARG B 75 ILE B 79 5 5
HELIX 21 21 TRP B 86 LEU B 90 5 5
HELIX 22 22 HIS B 91 GLU B 93 5 3
HELIX 23 23 LEU B 94 GLN B 107 1 14
HELIX 24 24 ASP B 143 ALA B 157 1 15
HELIX 25 25 ASN B 169 ASN B 178 1 10
HELIX 26 26 GLN B 199 LYS B 209 1 11
HELIX 27 27 VAL B 234 ASP B 237 5 4
HELIX 28 28 GLU B 238 ASN B 249 1 12
HELIX 29 29 THR B 251 GLN B 262 1 12
HELIX 30 30 LYS B 273 MET B 281 1 9
HELIX 31 31 GLN B 282 PHE B 286 5 5
HELIX 32 32 SER B 289 GLY B 298 1 10
HELIX 33 33 ALA B 308 LYS B 312 5 5
SHEET 1 A 2 CYS A 7 ILE A 9 0
SHEET 2 A 2 PHE A 15 PRO A 17 -1 O ILE A 16 N VAL A 8
SHEET 1 B 9 LEU A 19 GLY A 22 0
SHEET 2 B 9 HIS A 48 ASP A 50 1 O HIS A 48 N PHE A 21
SHEET 3 B 9 PHE A 80 VAL A 85 1 O PHE A 80 N PHE A 49
SHEET 4 B 9 VAL A 111 ILE A 116 1 O LEU A 115 N VAL A 85
SHEET 5 B 9 THR A 160 SER A 166 1 O GLY A 164 N TYR A 114
SHEET 6 B 9 CYS A 188 GLU A 192 1 O CYS A 188 N VAL A 165
SHEET 7 B 9 VAL A 212 TYR A 216 1 O VAL A 212 N ASN A 189
SHEET 8 B 9 VAL A 266 ASN A 269 1 O VAL A 266 N ALA A 215
SHEET 9 B 9 LEU A 19 GLY A 22 1 N GLY A 20 O VAL A 267
SHEET 1 C 2 CYS B 7 ILE B 9 0
SHEET 2 C 2 PHE B 15 PRO B 17 -1 O ILE B 16 N VAL B 8
SHEET 1 D 9 LEU B 19 GLY B 22 0
SHEET 2 D 9 HIS B 48 ASP B 50 1 O HIS B 48 N PHE B 21
SHEET 3 D 9 PHE B 80 VAL B 85 1 O PHE B 80 N PHE B 49
SHEET 4 D 9 VAL B 111 ILE B 116 1 O LEU B 115 N VAL B 85
SHEET 5 D 9 THR B 160 SER B 166 1 O GLY B 164 N TYR B 114
SHEET 6 D 9 CYS B 188 GLU B 192 1 O CYS B 188 N VAL B 165
SHEET 7 D 9 VAL B 212 TYR B 216 1 O VAL B 214 N VAL B 191
SHEET 8 D 9 VAL B 266 ASN B 269 1 O VAL B 266 N ALA B 215
SHEET 9 D 9 LEU B 19 GLY B 22 1 N GLY B 20 O VAL B 267
SSBOND 1 CYS A 5 CYS A 7 1555 1555 2.04
SSBOND 2 CYS B 5 CYS B 7 1555 1555 2.03
SITE 1 AC1 37 FFA A 3 GLY A 22 THR A 23 ALA A 24
SITE 2 AC1 37 ASP A 50 TYR A 55 LYS A 84 HIS A 117
SITE 3 AC1 37 SER A 166 ASN A 167 GLN A 190 TYR A 216
SITE 4 AC1 37 GLY A 217 VAL A 218 LEU A 219 GLY A 220
SITE 5 AC1 37 THR A 221 GLN A 222 TYR A 224 LEU A 236
SITE 6 AC1 37 ALA A 253 ASN A 269 THR A 270 SER A 271
SITE 7 AC1 37 LEU A 272 LYS A 273 ARG A 276 GLU A 279
SITE 8 AC1 37 ASN A 280 ILE A 306 EDO A 326 HOH A 330
SITE 9 AC1 37 HOH A 352 HOH A 354 HOH A 364 HOH A 405
SITE 10 AC1 37 HOH A 407
SITE 1 AC2 36 FFA B 4 GLY B 22 THR B 23 ALA B 24
SITE 2 AC2 36 ASP B 50 TYR B 55 LYS B 84 HIS B 117
SITE 3 AC2 36 SER B 166 ASN B 167 GLN B 190 TYR B 216
SITE 4 AC2 36 GLY B 217 VAL B 218 LEU B 219 GLY B 220
SITE 5 AC2 36 THR B 221 GLN B 222 TYR B 224 LEU B 236
SITE 6 AC2 36 ALA B 253 ASN B 269 THR B 270 SER B 271
SITE 7 AC2 36 LEU B 272 LYS B 273 ARG B 276 GLU B 279
SITE 8 AC2 36 ASN B 280 HOH B 327 HOH B 331 HOH B 370
SITE 9 AC2 36 HOH B 381 HOH B 389 HOH B 422 HOH B 461
SITE 1 AC3 8 NAP A 1 LEU A 25 LEU A 27 TYR A 55
SITE 2 AC3 8 HIS A 117 TYR A 118 PHE A 129 TRP A 227
SITE 1 AC4 8 NAP B 2 LEU B 25 LEU B 27 TYR B 55
SITE 2 AC4 8 HIS B 117 TYR B 118 TYR B 224 TRP B 227
SITE 1 AC5 1 CYS A 29
SITE 1 AC6 4 ASP A 143 LEU A 144 CYS A 145 MET A 175
SITE 1 AC7 2 GLU B 28 CYS B 29
SITE 1 AC8 1 CYS B 145
SITE 1 AC9 5 NAP A 1 LYS A 273 ARG A 276 HOH A 352
SITE 2 AC9 5 HOH A 364
SITE 1 BC1 5 ASP B 12 TYR B 184 LYS B 185 HOH B 366
SITE 2 BC1 5 HOH B 491
SITE 1 BC2 6 ASP A 12 TYR A 184 LYS A 185 HOH A 379
SITE 2 BC2 6 HOH A 520 HOH A 552
CRYST1 74.030 53.340 85.120 90.00 93.46 90.00 P 1 21 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 0.013508 0.000000 0.000817 0.00000
SCALE2 0.000000 0.018748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011770 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.867700 -0.484600 0.110600 -9.91370 1
MTRIX2 2 -0.484000 -0.874400 -0.034200 -12.63780 1
MTRIX3 2 0.113200 -0.023900 -0.993300 106.07110 1
(ATOM LINES ARE NOT SHOWN.)
END