HEADER OXIDOREDUCTASE 29-MAR-08 3COT
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER DELTA(4)-3-KETOSTEROID 5BETA-
TITLE 2 REDUCTASE (AKR1D1) IN COMPLEX WITH PROGESTERONE AND NADP. RESOLUTION:
TITLE 3 2.03 A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXO-5-BETA-STEROID 4-DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DELTA(4)-3-KETOSTEROID 5-BETA-REDUCTASE, ALDO-KETO REDUCTASE
COMPND 5 FAMILY 1 MEMBER D1;
COMPND 6 EC: 1.3.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AKR1D1, SRD5B1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28(A)
KEYWDS STEROID C-C DOUBLE BOND REDUCTION, 5BETA REDUCTASE, E120, BILE ACID
KEYWDS 2 CATABOLISM, CYTOPLASM, DISEASE MUTATION, LIPID METABOLISM, NADP,
KEYWDS 3 OXIDOREDUCTASE, STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.DI COSTANZO,J.DRURY,T.M.PENNING,D.W.CHRISTIANSON
REVDAT 4 30-AUG-23 3COT 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3COT 1 VERSN
REVDAT 2 24-JUN-08 3COT 1 JRNL
REVDAT 1 08-APR-08 3COT 0
JRNL AUTH L.DI COSTANZO,J.E.DRURY,T.M.PENNING,D.W.CHRISTIANSON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN LIVER {DELTA}4-3-KETOSTEROID
JRNL TITL 2 5{BETA}-REDUCTASE (AKR1D1) AND IMPLICATIONS FOR SUBSTRATE
JRNL TITL 3 BINDING AND CATALYSIS.
JRNL REF J.BIOL.CHEM. V. 283 16830 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18407998
JRNL DOI 10.1074/JBC.M801778200
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 71162.460
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 41289
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) : 0.194
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1866
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5156
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 237
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 142
REMARK 3 SOLVENT ATOMS : 497
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.11000
REMARK 3 B22 (A**2) : -8.56000
REMARK 3 B33 (A**2) : 9.67000
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) : 0.35
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
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) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 74.51
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.PARAM
REMARK 3 PARAMETER FILE 3 : NAP.PAR
REMARK 3 PARAMETER FILE 4 : STR.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NAP.TOP
REMARK 3 TOPOLOGY FILE 4 : STR.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3COT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-08
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 : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.008
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMETER
REMARK 200 AND VERTICAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44101
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
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: CNS
REMARK 200 STARTING MODEL: 3BUR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL 10%,PEG 4000, TRIS-HCL 100
REMARK 280 MM PH 7.5, VAPOR DIFFUSION, HANGING 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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.87150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.29150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.71700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.29150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.87150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.71700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 HIS A 8 36.57 -141.86
REMARK 500 ASN A 146 71.33 -154.86
REMARK 500 PHE A 200 77.79 -150.04
REMARK 500 THR A 224 171.23 75.84
REMARK 500 TRP A 230 -10.38 -144.53
REMARK 500 MET A 313 -7.80 -57.53
REMARK 500 HIS B 8 43.35 -144.29
REMARK 500 GLU B 28 106.92 -45.77
REMARK 500 THR B 224 171.99 77.95
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 B 3901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 3902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STR B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STR A 1501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CMF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH CORTISOEN AND NADP
DBREF 3COT A 1 326 UNP P51857 AK1D1_HUMAN 1 326
DBREF 3COT B 1 326 UNP P51857 AK1D1_HUMAN 1 326
SEQADV 3COT MET A -19 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY A -18 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER A -17 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER A -16 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -15 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -14 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -13 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -12 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -11 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A -10 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER A -9 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER A -8 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY A -7 UNP P51857 EXPRESSION TAG
SEQADV 3COT LEU A -6 UNP P51857 EXPRESSION TAG
SEQADV 3COT VAL A -5 UNP P51857 EXPRESSION TAG
SEQADV 3COT PRO A -4 UNP P51857 EXPRESSION TAG
SEQADV 3COT ARG A -3 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY A -2 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER A -1 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS A 0 UNP P51857 EXPRESSION TAG
SEQADV 3COT MET B -19 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY B -18 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER B -17 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER B -16 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -15 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -14 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -13 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -12 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -11 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B -10 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER B -9 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER B -8 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY B -7 UNP P51857 EXPRESSION TAG
SEQADV 3COT LEU B -6 UNP P51857 EXPRESSION TAG
SEQADV 3COT VAL B -5 UNP P51857 EXPRESSION TAG
SEQADV 3COT PRO B -4 UNP P51857 EXPRESSION TAG
SEQADV 3COT ARG B -3 UNP P51857 EXPRESSION TAG
SEQADV 3COT GLY B -2 UNP P51857 EXPRESSION TAG
SEQADV 3COT SER B -1 UNP P51857 EXPRESSION TAG
SEQADV 3COT HIS B 0 UNP P51857 EXPRESSION TAG
SEQRES 1 A 346 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 346 LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA
SEQRES 3 A 346 SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO
SEQRES 4 A 346 ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR
SEQRES 5 A 346 PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE
SEQRES 6 A 346 ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR
SEQRES 7 A 346 GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS
SEQRES 8 A 346 ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR
SEQRES 9 A 346 CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET
SEQRES 10 A 346 VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN
SEQRES 11 A 346 LEU ASP TYR VAL ASP LEU TYR ILE ILE GLU VAL PRO MET
SEQRES 12 A 346 ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU
SEQRES 13 A 346 ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA
SEQRES 14 A 346 THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU
SEQRES 15 A 346 VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN
SEQRES 16 A 346 LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS
SEQRES 17 A 346 PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR
SEQRES 18 A 346 GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE
SEQRES 19 A 346 VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN
SEQRES 20 A 346 PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS
SEQRES 21 A 346 ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS
SEQRES 22 A 346 THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG
SEQRES 23 A 346 GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG
SEQRES 24 A 346 ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR
SEQRES 25 A 346 GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN
SEQRES 26 A 346 VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO
SEQRES 27 A 346 GLU TYR PRO PHE HIS ASP GLU TYR
SEQRES 1 B 346 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 346 LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA
SEQRES 3 B 346 SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO
SEQRES 4 B 346 ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR
SEQRES 5 B 346 PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE
SEQRES 6 B 346 ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR
SEQRES 7 B 346 GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS
SEQRES 8 B 346 ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR
SEQRES 9 B 346 CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET
SEQRES 10 B 346 VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN
SEQRES 11 B 346 LEU ASP TYR VAL ASP LEU TYR ILE ILE GLU VAL PRO MET
SEQRES 12 B 346 ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU
SEQRES 13 B 346 ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA
SEQRES 14 B 346 THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU
SEQRES 15 B 346 VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN
SEQRES 16 B 346 LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS
SEQRES 17 B 346 PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR
SEQRES 18 B 346 GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE
SEQRES 19 B 346 VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN
SEQRES 20 B 346 PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS
SEQRES 21 B 346 ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS
SEQRES 22 B 346 THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG
SEQRES 23 B 346 GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG
SEQRES 24 B 346 ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR
SEQRES 25 B 346 GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN
SEQRES 26 B 346 VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO
SEQRES 27 B 346 GLU TYR PRO PHE HIS ASP GLU TYR
HET NAP A3902 48
HET STR A1501 23
HET NAP B3901 48
HET STR B1500 23
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM STR PROGESTERONE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 STR 2(C21 H30 O2)
FORMUL 7 HOH *497(H2 O)
HELIX 1 1 GLY A 35 GLY A 48 1 14
HELIX 2 2 ALA A 55 GLN A 59 5 5
HELIX 3 3 ASN A 60 GLU A 74 1 15
HELIX 4 4 ARG A 78 ILE A 82 5 5
HELIX 5 5 TRP A 89 HIS A 93 5 5
HELIX 6 6 VAL A 94 GLU A 96 5 3
HELIX 7 7 MET A 97 GLN A 110 1 14
HELIX 8 8 ASN A 146 ALA A 160 1 15
HELIX 9 9 ASN A 172 ASN A 181 1 10
HELIX 10 10 GLN A 202 HIS A 212 1 11
HELIX 11 11 PRO A 237 LYS A 240 5 4
HELIX 12 12 ASP A 241 ASN A 252 1 12
HELIX 13 13 THR A 254 ARG A 266 1 13
HELIX 14 14 ASN A 276 GLN A 285 1 10
HELIX 15 15 THR A 292 ALA A 301 1 10
HELIX 16 16 LEU A 311 ARG A 315 5 5
HELIX 17 17 GLU B 28 THR B 32 5 5
HELIX 18 18 GLY B 35 GLY B 48 1 14
HELIX 19 19 ALA B 55 GLN B 59 5 5
HELIX 20 20 ASN B 60 GLU B 74 1 15
HELIX 21 21 ARG B 78 ILE B 82 5 5
HELIX 22 22 TRP B 89 HIS B 93 5 5
HELIX 23 23 VAL B 94 GLN B 110 1 17
HELIX 24 24 ASN B 146 ALA B 160 1 15
HELIX 25 25 ASN B 172 ASN B 181 1 10
HELIX 26 26 GLN B 202 HIS B 212 1 11
HELIX 27 27 PRO B 237 LYS B 240 5 4
HELIX 28 28 ASP B 241 LYS B 249 1 9
HELIX 29 29 THR B 254 ARG B 266 1 13
HELIX 30 30 ASN B 276 GLN B 285 1 10
HELIX 31 31 THR B 292 ALA B 301 1 10
HELIX 32 32 LEU B 311 ARG B 315 5 5
SHEET 1 A 2 ARG A 9 PRO A 11 0
SHEET 2 A 2 SER A 17 PRO A 19 -1 O ILE A 18 N ILE A 10
SHEET 1 B 8 LEU A 23 GLY A 24 0
SHEET 2 B 8 HIS A 51 ASP A 53 1 O ASP A 53 N LEU A 23
SHEET 3 B 8 PHE A 83 LEU A 88 1 O PHE A 83 N ILE A 52
SHEET 4 B 8 VAL A 114 ILE A 119 1 O ILE A 118 N LEU A 88
SHEET 5 B 8 VAL A 163 SER A 169 1 O SER A 165 N TYR A 117
SHEET 6 B 8 SER A 191 GLU A 195 1 O SER A 191 N VAL A 168
SHEET 7 B 8 VAL A 215 TYR A 219 1 O THR A 217 N VAL A 194
SHEET 8 B 8 VAL A 269 VAL A 270 1 O VAL A 269 N ALA A 218
SHEET 1 C 2 ALA A 124 PHE A 125 0
SHEET 2 C 2 TYR A 142 HIS A 143 -1 O HIS A 143 N ALA A 124
SHEET 1 D 2 ARG B 9 PRO B 11 0
SHEET 2 D 2 SER B 17 PRO B 19 -1 O ILE B 18 N ILE B 10
SHEET 1 E 8 LEU B 23 GLY B 24 0
SHEET 2 E 8 HIS B 51 ASP B 53 1 O ASP B 53 N LEU B 23
SHEET 3 E 8 PHE B 83 LEU B 88 1 O PHE B 83 N ILE B 52
SHEET 4 E 8 VAL B 114 ILE B 119 1 O LEU B 116 N GLY B 86
SHEET 5 E 8 VAL B 163 SER B 169 1 O SER B 165 N TYR B 117
SHEET 6 E 8 SER B 191 GLU B 195 1 O SER B 191 N VAL B 168
SHEET 7 E 8 VAL B 215 TYR B 219 1 O TYR B 219 N VAL B 194
SHEET 8 E 8 VAL B 269 VAL B 270 1 O VAL B 269 N ALA B 218
SITE 1 AC1 26 GLY B 24 THR B 25 TYR B 26 ASP B 53
SITE 2 AC1 26 TYR B 58 LYS B 87 SER B 169 ASN B 170
SITE 3 AC1 26 GLN B 193 TYR B 219 SER B 220 PRO B 221
SITE 4 AC1 26 LEU B 222 GLY B 223 THR B 224 SER B 225
SITE 5 AC1 26 LEU B 239 ALA B 256 ILE B 271 PRO B 272
SITE 6 AC1 26 LYS B 273 SER B 274 PHE B 275 ARG B 279
SITE 7 AC1 26 GLU B 282 ASN B 283
SITE 1 AC2 26 GLY A 24 THR A 25 TYR A 26 ASP A 53
SITE 2 AC2 26 TYR A 58 LYS A 87 SER A 169 ASN A 170
SITE 3 AC2 26 GLN A 193 TYR A 219 SER A 220 PRO A 221
SITE 4 AC2 26 LEU A 222 GLY A 223 THR A 224 SER A 225
SITE 5 AC2 26 LEU A 239 ALA A 256 ILE A 271 PRO A 272
SITE 6 AC2 26 LYS A 273 SER A 274 PHE A 275 ARG A 279
SITE 7 AC2 26 GLU A 282 ASN A 283
SITE 1 AC3 5 TYR B 26 TYR B 58 GLU B 120 TRP B 230
SITE 2 AC3 5 TRP B 314
SITE 1 AC4 5 TYR A 26 TYR A 58 GLU A 120 TYR A 132
SITE 2 AC4 5 TRP A 230
CRYST1 49.743 109.434 128.583 90.00 90.00 90.00 P 21 21 21 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 0.020103 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007777 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
