HEADER OXIDOREDUCTASE 17-APR-08 3CV6
TITLE THE CRYSTAL STRUCTURE OF MOUSE 17-ALPHA HYDROXYSTEROID DEHYDROGENASE
TITLE 2 GG225.226PP MUTANT IN COMPLEX WITH INHIBITOR AND COFACTOR NADP+.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER C21;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 17-ALPHA-HYDROXYSTEROID DEHYDROGENASE, 17-ALPHA-HSD, 3-
COMPND 5 ALPHA-HYDROXYSTEROID DEHYDROGENASE, DIHYDRODIOL DEHYDROGENASE TYPE 1,
COMPND 6 DD1, DIHYDRODIOL DEHYDROGENASE TYPE 3, DD3;
COMPND 7 EC: 1.1.1.209;
COMPND 8 ENGINEERED: YES;
COMPND 9 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK223-3
KEYWDS ALDO-KETO REDUCTASE, HYDROXYSTEROID DEHYDROGENASE, TERNARY COMPLEX,
KEYWDS 2 HEXESTROL, LIPID METABOLISM, NADP, OXIDOREDUCTASE, PHOSPHOPROTEIN,
KEYWDS 3 STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR U.DHAGAT,O.EL-KABBANI
REVDAT 5 01-NOV-23 3CV6 1 REMARK
REVDAT 4 10-NOV-21 3CV6 1 REMARK SEQADV
REVDAT 3 13-NOV-19 3CV6 1 REMARK
REVDAT 2 18-APR-12 3CV6 1 JRNL VERSN
REVDAT 1 03-MAR-09 3CV6 0
JRNL AUTH U.DHAGAT,S.ENDO,H.MAMIYA,A.HARA,O.EL-KABBANI
JRNL TITL STRUCTURE OF THE G225P/G226P MUTANT OF MOUSE
JRNL TITL 2 3(17)ALPHA-HYDROXYSTEROID DEHYDROGENASE (AKR1C21) TERNARY
JRNL TITL 3 COMPLEX: IMPLICATIONS FOR THE BINDING OF INHIBITOR AND
JRNL TITL 4 SUBSTRATE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 65 257 2009
JRNL REFN ISSN 0907-4449
JRNL PMID 19237748
JRNL DOI 10.1107/S0907444908044028
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 46635
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2487
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3451
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5196
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 664
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : -0.41000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.221
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.418
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5600 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7616 ; 1.713 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 678 ;11.949 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;37.927 ;24.263
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 987 ;14.598 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.939 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 830 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4200 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2566 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3728 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 456 ; 0.196 ; 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): 38 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.179 ; 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): 3432 ; 0.778 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5360 ; 1.245 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2532 ; 1.992 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2241 ; 2.931 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 323 4
REMARK 3 1 B 1 B 323 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2619 ; 0.23 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2619 ; 0.41 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JAN-07
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.010
REMARK 200 R MERGE (I) : 0.03920
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.44
REMARK 200 R MERGE FOR SHELL (I) : 0.36720
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2P5N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 10% PEG L6000, 5% 2-METHYL
REMARK 280 -2,4-PENTANEDIOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.18267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.09133
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU B 261 CA CB CG CD1 CD2
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 THR A 221 163.46 75.05
REMARK 500 THR B 221 158.69 68.69
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 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXS A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXS B 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 353
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE DIFFERENCES BETWEEN THE SEQRES AND THE SEQUENCE DATABASE.
REMARK 999 THIS IS A VARIANT AT THESE POSITIONS. THR221 IN MOLECULES A AND B
REMARK 999 MAKES CLOSE CONTACTS WITH THE COENZYME RESULTING IN A DEVIATION IN
REMARK 999 CHIRALITY.
DBREF 3CV6 A 1 323 UNP Q91WR5 AK1CL_MOUSE 1 323
DBREF 3CV6 B 1 323 UNP Q91WR5 AK1CL_MOUSE 1 323
SEQADV 3CV6 LEU A 27 UNP Q91WR5 VAL 27 SEE REMARK 999
SEQADV 3CV6 HIS A 60 UNP Q91WR5 ARG 60 SEE REMARK 999
SEQADV 3CV6 HIS A 91 UNP Q91WR5 ARG 91 SEE REMARK 999
SEQADV 3CV6 GLU A 100 UNP Q91WR5 VAL 100 SEE REMARK 999
SEQADV 3CV6 TYR A 170 UNP Q91WR5 SER 170 SEE REMARK 999
SEQADV 3CV6 PRO A 225 UNP Q91WR5 GLY 225 ENGINEERED MUTATION
SEQADV 3CV6 PRO A 226 UNP Q91WR5 GLY 226 ENGINEERED MUTATION
SEQADV 3CV6 LEU B 27 UNP Q91WR5 VAL 27 SEE REMARK 999
SEQADV 3CV6 HIS B 60 UNP Q91WR5 ARG 60 SEE REMARK 999
SEQADV 3CV6 HIS B 91 UNP Q91WR5 ARG 91 SEE REMARK 999
SEQADV 3CV6 GLU B 100 UNP Q91WR5 VAL 100 SEE REMARK 999
SEQADV 3CV6 TYR B 170 UNP Q91WR5 SER 170 SEE REMARK 999
SEQADV 3CV6 PRO B 225 UNP Q91WR5 GLY 225 ENGINEERED MUTATION
SEQADV 3CV6 PRO B 226 UNP Q91WR5 GLY 226 ENGINEERED MUTATION
SEQRES 1 A 323 MET ASN SER LYS CYS HIS CYS VAL ILE LEU ASN ASP GLY
SEQRES 2 A 323 ASN PHE ILE PRO VAL LEU GLY PHE GLY THR ALA LEU PRO
SEQRES 3 A 323 LEU GLU CYS PRO LYS SER LYS ALA LYS GLU LEU THR LYS
SEQRES 4 A 323 ILE ALA ILE ASP ALA GLY PHE HIS HIS PHE ASP SER ALA
SEQRES 5 A 323 SER VAL TYR ASN THR GLU ASP HIS VAL GLY GLU ALA ILE
SEQRES 6 A 323 ARG SER LYS ILE ALA ASP GLY THR VAL ARG ARG GLU ASP
SEQRES 7 A 323 ILE PHE TYR THR SER LYS VAL TRP CYS THR SER LEU HIS
SEQRES 8 A 323 PRO GLU LEU VAL ARG ALA SER LEU GLU ARG SER LEU GLN
SEQRES 9 A 323 LYS LEU GLN PHE ASP TYR VAL ASP LEU TYR LEU ILE HIS
SEQRES 10 A 323 TYR PRO MET ALA LEU LYS PRO GLY GLU GLU ASN PHE PRO
SEQRES 11 A 323 VAL ASP GLU HIS GLY LYS LEU ILE PHE ASP ARG VAL ASP
SEQRES 12 A 323 LEU CYS ALA THR TRP GLU ALA MET GLU LYS CYS LYS ASP
SEQRES 13 A 323 ALA GLY LEU THR LYS SER ILE GLY VAL SER ASN PHE ASN
SEQRES 14 A 323 TYR 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 LEU ASN GLN MET LYS LEU LEU ASP PHE CYS LYS SER
SEQRES 17 A 323 LYS ASP ILE VAL LEU VAL ALA TYR GLY VAL LEU GLY THR
SEQRES 18 A 323 GLN ARG TYR PRO PRO TRP VAL ASP GLN ASN SER PRO VAL
SEQRES 19 A 323 LEU LEU ASP GLU PRO VAL LEU GLY SER MET ALA LYS LYS
SEQRES 20 A 323 TYR ASN ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN
SEQRES 21 A 323 LEU GLN ARG GLY ILE VAL VAL LEU ASN THR SER LEU LYS
SEQRES 22 A 323 GLU GLU ARG ILE LYS GLU ASN MET GLN VAL PHE GLU PHE
SEQRES 23 A 323 GLN LEU SER SER GLU ASP MET LYS VAL LEU ASP GLY LEU
SEQRES 24 A 323 ASN ARG ASN MET ARG TYR ILE PRO ALA ALA ILE PHE LYS
SEQRES 25 A 323 GLY HIS PRO ASN TRP PRO PHE LEU ASP GLU TYR
SEQRES 1 B 323 MET ASN SER LYS CYS HIS CYS VAL ILE LEU ASN ASP GLY
SEQRES 2 B 323 ASN PHE ILE PRO VAL LEU GLY PHE GLY THR ALA LEU PRO
SEQRES 3 B 323 LEU GLU CYS PRO LYS SER LYS ALA LYS GLU LEU THR LYS
SEQRES 4 B 323 ILE ALA ILE ASP ALA GLY PHE HIS HIS PHE ASP SER ALA
SEQRES 5 B 323 SER VAL TYR ASN THR GLU ASP HIS VAL GLY GLU ALA ILE
SEQRES 6 B 323 ARG SER LYS ILE ALA ASP GLY THR VAL ARG ARG GLU ASP
SEQRES 7 B 323 ILE PHE TYR THR SER LYS VAL TRP CYS THR SER LEU HIS
SEQRES 8 B 323 PRO GLU LEU VAL ARG ALA SER LEU GLU ARG SER LEU GLN
SEQRES 9 B 323 LYS LEU GLN PHE ASP TYR VAL ASP LEU TYR LEU ILE HIS
SEQRES 10 B 323 TYR PRO MET ALA LEU LYS PRO GLY GLU GLU ASN PHE PRO
SEQRES 11 B 323 VAL ASP GLU HIS GLY LYS LEU ILE PHE ASP ARG VAL ASP
SEQRES 12 B 323 LEU CYS ALA THR TRP GLU ALA MET GLU LYS CYS LYS ASP
SEQRES 13 B 323 ALA GLY LEU THR LYS SER ILE GLY VAL SER ASN PHE ASN
SEQRES 14 B 323 TYR ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU
SEQRES 15 B 323 LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO
SEQRES 16 B 323 TYR LEU ASN GLN MET LYS LEU LEU ASP PHE CYS LYS SER
SEQRES 17 B 323 LYS ASP ILE VAL LEU VAL ALA TYR GLY VAL LEU GLY THR
SEQRES 18 B 323 GLN ARG TYR PRO PRO TRP VAL ASP GLN ASN SER PRO VAL
SEQRES 19 B 323 LEU LEU ASP GLU PRO VAL LEU GLY SER MET ALA LYS LYS
SEQRES 20 B 323 TYR ASN ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN
SEQRES 21 B 323 LEU GLN ARG GLY ILE VAL VAL LEU ASN THR SER LEU LYS
SEQRES 22 B 323 GLU GLU ARG ILE LYS GLU ASN MET GLN VAL PHE GLU PHE
SEQRES 23 B 323 GLN LEU SER SER GLU ASP MET LYS VAL LEU ASP GLY LEU
SEQRES 24 B 323 ASN ARG ASN MET ARG TYR ILE PRO ALA ALA ILE PHE LYS
SEQRES 25 B 323 GLY HIS PRO ASN TRP PRO PHE LEU ASP GLU TYR
HET NAP A 350 48
HET HXS A 351 20
HET BME A 352 4
HET BME A 353 4
HET NAP B 350 48
HET HXS B 351 20
HET BME B 352 4
HET BME B 354 4
HET BME B 355 4
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM HXS 4-[(1R,2S)-1-ETHYL-2-(4-HYDROXYPHENYL)BUTYL]PHENOL
HETNAM BME BETA-MERCAPTOETHANOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 HXS 2(C18 H22 O2)
FORMUL 5 BME 5(C2 H6 O S)
FORMUL 12 HOH *664(H2 O)
HELIX 1 1 SER A 32 GLY A 45 1 14
HELIX 2 2 THR A 57 ASP A 71 1 15
HELIX 3 3 ARG A 75 ILE A 79 5 5
HELIX 4 4 HIS A 91 GLN A 107 1 17
HELIX 5 5 ASP A 143 ALA A 157 1 15
HELIX 6 6 ASN A 169 ASN A 178 1 10
HELIX 7 7 GLN A 199 LYS A 209 1 11
HELIX 8 8 VAL A 234 ASP A 237 5 4
HELIX 9 9 GLU A 238 ASN A 249 1 12
HELIX 10 10 THR A 251 GLN A 262 1 12
HELIX 11 11 LYS A 273 MET A 281 1 9
HELIX 12 12 GLN A 282 GLU A 285 5 4
HELIX 13 13 SER A 289 GLY A 298 1 10
HELIX 14 14 ALA A 308 LYS A 312 5 5
HELIX 15 15 SER B 32 ALA B 44 1 13
HELIX 16 16 ALA B 52 ASN B 56 5 5
HELIX 17 17 THR B 57 ASP B 71 1 15
HELIX 18 18 ARG B 75 ILE B 79 5 5
HELIX 19 19 TRP B 86 LEU B 90 5 5
HELIX 20 20 HIS B 91 GLN B 107 1 17
HELIX 21 21 ASP B 143 ALA B 157 1 15
HELIX 22 22 ASN B 169 ASN B 178 1 10
HELIX 23 23 GLN B 199 LYS B 209 1 11
HELIX 24 24 VAL B 234 ASP B 237 5 4
HELIX 25 25 GLU B 238 TYR B 248 1 11
HELIX 26 26 THR B 251 GLN B 262 1 12
HELIX 27 27 LYS B 273 MET B 281 1 9
HELIX 28 28 GLN B 282 GLU B 285 5 4
HELIX 29 29 SER B 289 GLY B 298 1 10
HELIX 30 30 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 214 N VAL A 191
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 THR B 82 N PHE B 49
SHEET 4 D 9 VAL B 111 ILE B 116 1 O LEU B 113 N SER B 83
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 GLN B 190 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
SHEET 1 E 2 ALA B 121 LEU B 122 0
SHEET 2 E 2 PHE B 139 ASP B 140 -1 O ASP B 140 N ALA B 121
SSBOND 1 CYS A 5 CYS A 7 1555 1555 2.02
SSBOND 2 CYS B 5 CYS B 7 1555 1555 2.30
SITE 1 AC1 26 GLY A 22 THR A 23 ALA A 24 ASP A 50
SITE 2 AC1 26 TYR A 55 HIS A 117 SER A 166 ASN A 167
SITE 3 AC1 26 GLN A 190 TYR A 216 GLY A 217 LEU A 219
SITE 4 AC1 26 GLY A 220 THR A 221 GLN A 222 TYR A 224
SITE 5 AC1 26 LEU A 236 ALA A 253 ASN A 269 THR A 270
SITE 6 AC1 26 SER A 271 LEU A 272 LYS A 273 ARG A 276
SITE 7 AC1 26 GLU A 279 ASN A 280
SITE 1 AC2 25 GLY B 22 THR B 23 ALA B 24 ASP B 50
SITE 2 AC2 25 TYR B 55 HIS B 117 SER B 166 ASN B 167
SITE 3 AC2 25 GLN B 190 TYR B 216 GLY B 217 LEU B 219
SITE 4 AC2 25 GLY B 220 THR B 221 GLN B 222 TYR B 224
SITE 5 AC2 25 ALA B 253 ASN B 269 THR B 270 SER B 271
SITE 6 AC2 25 LEU B 272 LYS B 273 ARG B 276 GLU B 279
SITE 7 AC2 25 ASN B 280
SITE 1 AC3 9 ALA A 24 LEU A 25 LEU A 27 LYS A 31
SITE 2 AC3 9 TYR A 55 HIS A 117 TYR A 118 TYR A 224
SITE 3 AC3 9 TRP A 227
SITE 1 AC4 8 ALA B 24 LEU B 25 LYS B 31 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 1 HIS A 6
CRYST1 102.108 102.108 72.274 90.00 90.00 120.00 P 32 6
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 0.009794 0.005654 0.000000 0.00000
SCALE2 0.000000 0.011309 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
