HEADER OXIDOREDUCTASE 18-SEP-02 1MRQ
TITLE CRYSTAL STRUCTURE OF HUMAN 20ALPHA-HSD IN TERNARY COMPLEX WITH NADP
TITLE 2 AND 20ALPHA-HYDROXY-PROGESTERONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER C1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 20ALPHA-HYDROXYSTEROID DEHYDROGENASE, TRANS-1,2-
COMPND 5 DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE, HIGH-AFFINITY HEPATIC BILE
COMPND 6 ACID-BINDING PROTEIN, HBAB, CHLORDECONE REDUCTASE HOMOLOG HAKRC,
COMPND 7 DIHYDRODIOL DEHYDROGENASE 2, DD2;
COMPND 8 EC: 1.1.1.149;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS 20ALPHA-HSD, HYDROXYSTEROID DEHYDROGENASE, PROGESTERONE, TERNARY
KEYWDS 2 COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.COUTURE,P.LEGRAND,L.CANTIN,V.LUU-THE,F.LABRIE,R.BRETON
REVDAT 5 14-FEB-24 1MRQ 1 REMARK SEQADV
REVDAT 4 11-OCT-17 1MRQ 1 REMARK
REVDAT 3 13-JUL-11 1MRQ 1 VERSN
REVDAT 2 24-FEB-09 1MRQ 1 VERSN
REVDAT 1 30-SEP-03 1MRQ 0
JRNL AUTH J.F.COUTURE,P.LEGRAND,L.CANTIN,V.LUU-THE,F.LABRIE,R.BRETON
JRNL TITL HUMAN 20ALPHA-HYDROXYSTEROID DEHYDROGENASE: CRYSTALLOGRAPHIC
JRNL TITL 2 AND SITE-DIRECTED MUTAGENESIS STUDIES LEAD TO THE
JRNL TITL 3 IDENTIFICATION OF AN ALTERNATIVE BINDING SITE FOR
JRNL TITL 4 C21-STEROIDS.
JRNL REF J.MOL.BIOL. V. 331 593 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12899831
JRNL DOI 10.1016/S0022-2836(03)00762-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.F.COUTURE,L.CANTIN,P.LEGRAND,V.LUU-THE,F.LABRIE,R.BRETON
REMARK 1 TITL EXPRESSION, CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS
REMARK 1 TITL 2 OF HUMAN AND RABBIT 20ALPHA-HYDROXYSTEROID DEHYDROGENASE IN
REMARK 1 TITL 3 COMPLEX WITH NADP(H) AND VARIOUS STEROID SUBSTRATES
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 135 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444901017346
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.07
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 41981
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) : 0.173
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2202
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2183
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.2040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 321
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.69
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): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.290
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2736 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3718 ; 1.250 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 322 ; 4.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 474 ;10.315 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 407 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2048 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1370 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 232 ; 0.108 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 19 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.096 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1619 ; 0.459 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2622 ; 0.871 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1117 ; 1.571 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1096 ; 2.596 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4120 39.4940 21.8710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0317 T22: 0.0453
REMARK 3 T33: 0.0760 T12: -0.0101
REMARK 3 T13: -0.0115 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.4103 L22: 1.1714
REMARK 3 L33: 0.7562 L12: -0.1639
REMARK 3 L13: 0.0771 L23: -0.2237
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: 0.0003 S13: -0.0201
REMARK 3 S21: -0.0707 S22: 0.0345 S23: 0.1287
REMARK 3 S31: 0.0131 S32: 0.0063 S33: -0.0155
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017132.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.17200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1J96
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, HEPES, AMMONIUM SULFATE,
REMARK 280 CALCIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 19.82500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.34000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.77000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.34000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.82500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.77000
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: BIOLOGICAL ASSEMBLY IS A MONOMER
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 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 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 26 152.55 -49.30
REMARK 500 ASN A 134 -12.11 99.60
REMARK 500 PHE A 197 77.26 -150.61
REMARK 500 SER A 221 163.23 81.05
REMARK 500 ARG A 250 -145.06 -123.10
REMARK 500 ARG A 301 19.55 -145.73
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 502
DBREF 1MRQ A 2 323 UNP Q04828 AK1C1_HUMAN 2 323
SEQADV 1MRQ GLN A 1 UNP Q04828 CLONING ARTIFACT
SEQRES 1 A 323 GLN ASP SER LYS TYR GLN CYS VAL LYS LEU ASN ASP GLY
SEQRES 2 A 323 HIS PHE MET PRO VAL LEU GLY PHE GLY THR TYR ALA PRO
SEQRES 3 A 323 ALA GLU VAL PRO LYS SER LYS ALA LEU GLU ALA THR LYS
SEQRES 4 A 323 LEU ALA ILE GLU ALA GLY PHE ARG HIS ILE ASP SER ALA
SEQRES 5 A 323 HIS LEU TYR ASN ASN GLU GLU GLN VAL GLY LEU ALA ILE
SEQRES 6 A 323 ARG SER LYS ILE ALA ASP GLY SER VAL LYS ARG GLU ASP
SEQRES 7 A 323 ILE PHE TYR THR SER LYS LEU TRP CYS ASN SER HIS ARG
SEQRES 8 A 323 PRO GLU LEU VAL ARG PRO ALA LEU GLU ARG SER LEU LYS
SEQRES 9 A 323 ASN LEU GLN LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS
SEQRES 10 A 323 PHE PRO VAL SER VAL LYS PRO GLY GLU GLU VAL ILE PRO
SEQRES 11 A 323 LYS ASP GLU ASN GLY LYS ILE LEU PHE ASP THR VAL ASP
SEQRES 12 A 323 LEU CYS ALA THR TRP GLU ALA VAL GLU LYS CYS LYS ASP
SEQRES 13 A 323 ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN
SEQRES 14 A 323 ARG ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU
SEQRES 15 A 323 LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO
SEQRES 16 A 323 TYR PHE ASN GLN ARG LYS LEU LEU ASP PHE CYS LYS SER
SEQRES 17 A 323 LYS ASP ILE VAL LEU VAL ALA TYR SER ALA LEU GLY SER
SEQRES 18 A 323 HIS ARG GLU GLU PRO TRP VAL ASP PRO ASN SER PRO VAL
SEQRES 19 A 323 LEU LEU GLU ASP PRO VAL LEU CYS ALA LEU ALA LYS LYS
SEQRES 20 A 323 HIS LYS ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN
SEQRES 21 A 323 LEU GLN ARG GLY VAL VAL VAL LEU ALA LYS SER TYR ASN
SEQRES 22 A 323 GLU GLN ARG ILE ARG GLN ASN VAL GLN VAL PHE GLU PHE
SEQRES 23 A 323 GLN LEU THR SER GLU GLU MET LYS ALA ILE ASP GLY LEU
SEQRES 24 A 323 ASN ARG ASN VAL ARG TYR LEU THR LEU ASP ILE PHE ALA
SEQRES 25 A 323 GLY PRO PRO ASN TYR PRO PHE SER ASP GLU TYR
HET NAP A 500 48
HET STR A 501 23
HET BME A 502 4
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM STR PROGESTERONE
HETNAM BME BETA-MERCAPTOETHANOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 STR C21 H30 O2
FORMUL 4 BME C2 H6 O S
FORMUL 5 HOH *321(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 ASN A 57 ASP A 71 1 15
HELIX 4 4 LYS A 75 ILE A 79 5 5
HELIX 5 5 TRP A 86 HIS A 90 5 5
HELIX 6 6 ARG A 91 GLN A 107 1 17
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 GLU A 237 5 4
HELIX 11 11 ASP A 238 LYS A 249 1 12
HELIX 12 12 THR A 251 ARG A 263 1 13
HELIX 13 13 ASN A 273 VAL A 281 1 9
HELIX 14 14 GLN A 282 PHE A 286 5 5
HELIX 15 15 THR A 289 GLY A 298 1 10
HELIX 16 16 LEU A 308 ALA A 312 5 5
SHEET 1 A 2 CYS A 7 LYS A 9 0
SHEET 2 A 2 PHE A 15 PRO A 17 -1 O MET 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 ASP A 50 N PHE A 21
SHEET 3 B 9 PHE A 80 LEU A 85 1 O PHE A 80 N ILE A 49
SHEET 4 B 9 VAL A 111 ILE A 116 1 O LEU A 115 N LEU A 85
SHEET 5 B 9 ALA A 160 SER A 166 1 O LYS A 161 N VAL A 111
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 214 N VAL A 191
SHEET 8 B 9 VAL A 266 LYS A 270 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
CISPEP 1 GLU A 225 PRO A 226 0 -2.02
SITE 1 AC1 37 GLY A 22 THR A 23 TYR A 24 ASP A 50
SITE 2 AC1 37 TYR A 55 HIS A 117 SER A 166 ASN A 167
SITE 3 AC1 37 GLN A 190 TYR A 216 SER A 217 ALA A 218
SITE 4 AC1 37 LEU A 219 GLY A 220 SER A 221 HIS A 222
SITE 5 AC1 37 LEU A 236 ALA A 253 LEU A 268 ALA A 269
SITE 6 AC1 37 LYS A 270 SER A 271 TYR A 272 ARG A 276
SITE 7 AC1 37 GLN A 279 ASN A 280 LEU A 306 STR A 501
SITE 8 AC1 37 HOH A 510 HOH A 516 HOH A 529 HOH A 544
SITE 9 AC1 37 HOH A 562 HOH A 629 HOH A 672 HOH A 789
SITE 10 AC1 37 HOH A 822
SITE 1 AC2 12 TYR A 24 LEU A 54 TYR A 55 GLU A 127
SITE 2 AC2 12 VAL A 128 ILE A 129 HIS A 222 TRP A 227
SITE 3 AC2 12 LEU A 306 LEU A 308 NAP A 500 HOH A 822
SITE 1 AC3 6 HIS A 14 PHE A 15 ARG A 301 HOH A 532
SITE 2 AC3 6 HOH A 658 HOH A 708
CRYST1 39.650 83.540 100.680 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 0.025221 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011970 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
