HEADER OXIDOREDUCTASE 03-JUN-04 1W0G
TITLE CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 3A4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN, RESIDUES 24-502;
COMPND 5 SYNONYM: QUININE 3-MONOOXYGENASE, CYPIIIA4, NIFEDIPINE OXIDASE, NF-
COMPND 6 25, P450-PCN1;
COMPND 7 EC: 1.14.13.67, 1.14.14.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI(+)
KEYWDS OXIDOREDUCTASE, NIFEDIPINE OXIDASE, CYTOCHROME P450, ELECTRON
KEYWDS 2 TRANSPORT, MONOOXYGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.WILLIAMS,J.COSME,D.M.VINKOVIC,A.WARD,H.C.ANGOVE,P.J.DAY,
AUTHOR 2 C.VONRHEIN,I.J.TICKLE,H.JHOTI
REVDAT 4 13-DEC-23 1W0G 1 LINK
REVDAT 3 24-FEB-09 1W0G 1 VERSN
REVDAT 2 05-AUG-04 1W0G 1 JRNL
REVDAT 1 22-JUL-04 1W0G 0
JRNL AUTH P.A.WILLIAMS,J.COSME,D.M.VINKOVIC,A.WARD,H.C.ANGOVE,P.J.DAY,
JRNL AUTH 2 C.VONRHEIN,I.J.TICKLE,H.JHOTI
JRNL TITL CRYSTAL STRUCTURES OF HUMAN CYTOCHROME P450 3A4 BOUND TO
JRNL TITL 2 METYRAPONE AND PROGESTERONE
JRNL REF SCIENCE V. 305 683 2004
JRNL REFN ISSN 0036-8075
JRNL PMID 15256616
JRNL DOI 10.1126/SCIENCE.1099736
REMARK 2
REMARK 2 RESOLUTION. 2.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003A
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) : 2.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 12577
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.318
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 689
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) : 2.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 939
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -0.27000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.493
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.418
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.287
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3810 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3545 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5170 ; 1.753 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8264 ; 1.050 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 452 ; 9.320 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 157 ;41.691 ;23.758
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 676 ;20.273 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.719 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 567 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4095 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 757 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1231 ; 0.270 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4344 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1895 ; 0.204 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2249 ; 0.092 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 51 ; 0.178 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 4 ; 0.123 ; 0.200
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): 4 ; 0.181 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 21 ; 0.171 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2892 ; 3.392 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 903 ; 0.913 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3727 ; 4.282 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1788 ; 3.315 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1441 ; 4.382 ; 7.500
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 : NULL
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1W0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1290015455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13241
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1W0E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 0.025M NACL, 7.5%
REMARK 280 (V/V) ISOPROPANOL, 10, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.97000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.45500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.50000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.97000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.45500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.50000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.97000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.45500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.50000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.97000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.45500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.50000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2009 LIES ON A SPECIAL POSITION.
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 23
REMARK 465 ALA A 24
REMARK 465 ASP A 263
REMARK 465 THR A 264
REMARK 465 GLN A 265
REMARK 465 LYS A 266
REMARK 465 HIS A 267
REMARK 465 ARG A 268
REMARK 465 VAL A 269
REMARK 465 ASP A 277
REMARK 465 SER A 278
REMARK 465 GLN A 279
REMARK 465 ASN A 280
REMARK 465 SER A 281
REMARK 465 LYS A 282
REMARK 465 GLU A 283
REMARK 465 THR A 284
REMARK 465 GLU A 285
REMARK 465 SER A 286
REMARK 465 HIS A 287
REMARK 465 LYS A 288
REMARK 465 THR A 499
REMARK 465 VAL A 500
REMARK 465 SER A 501
REMARK 465 GLY A 502
REMARK 465 ALA A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 HIS A 506
REMARK 465 HIS A 507
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 ASP A 497 CG OD1 OD2
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 ND2 ASN A 104 OD1 ASP A 123 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE2 PHE A 226 CZ PHE A 226 2775 1.36
REMARK 500 CD1 ILE A 232 CD1 ILE A 232 4575 1.73
REMARK 500 CE2 PHE A 226 CE2 PHE A 226 2775 1.85
REMARK 500 CZ PHE A 226 CZ PHE A 226 2775 2.06
REMARK 500 CB PHE A 228 O PRO A 231 4575 2.10
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 ASP A 61 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 86 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 123 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 182 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 194 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 214 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 217 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 326 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 357 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 428 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU A 475 CA - CB - CG ANGL. DEV. = 17.1 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 THR A 27 70.09 -114.06
REMARK 500 PHE A 33 48.95 -98.48
REMARK 500 LYS A 34 -62.13 -122.60
REMARK 500 CYS A 58 -63.13 -29.05
REMARK 500 LYS A 67 -76.07 -60.69
REMARK 500 THR A 85 -54.50 -160.47
REMARK 500 LYS A 96 -72.75 -76.67
REMARK 500 CYS A 98 -39.71 5.65
REMARK 500 SER A 100 -75.37 -47.62
REMARK 500 PHE A 102 68.70 78.58
REMARK 500 PHE A 108 -157.48 -129.98
REMARK 500 MET A 114 -1.77 -58.41
REMARK 500 ASP A 123 -114.81 48.89
REMARK 500 ARG A 130 -71.74 -59.10
REMARK 500 LEU A 132 -50.94 167.22
REMARK 500 PRO A 169 158.47 -48.97
REMARK 500 LEU A 196 64.22 -46.92
REMARK 500 ASN A 197 -170.30 59.39
REMARK 500 ASN A 198 -160.10 67.77
REMARK 500 PRO A 199 73.58 -30.86
REMARK 500 ASP A 201 18.91 -142.99
REMARK 500 PHE A 203 -33.14 169.56
REMARK 500 LEU A 210 78.35 -66.37
REMARK 500 PHE A 215 5.79 -68.33
REMARK 500 PHE A 226 69.63 -116.46
REMARK 500 LEU A 236 23.05 -74.06
REMARK 500 ASN A 237 23.24 36.68
REMARK 500 LYS A 254 -75.67 -53.97
REMARK 500 ARG A 255 -31.47 -28.04
REMARK 500 THR A 323 40.16 26.32
REMARK 500 HIS A 324 57.86 -152.12
REMARK 500 PRO A 340 97.53 -22.02
REMARK 500 ASN A 341 106.65 18.84
REMARK 500 LYS A 342 109.31 45.71
REMARK 500 MET A 353 53.75 -153.26
REMARK 500 GLU A 354 30.37 -84.02
REMARK 500 LEU A 356 -70.78 -56.52
REMARK 500 ASP A 357 -30.81 -39.23
REMARK 500 PHE A 367 77.23 -119.76
REMARK 500 MET A 371 -10.49 -46.24
REMARK 500 LYS A 390 150.16 -46.04
REMARK 500 PRO A 397 79.57 -63.21
REMARK 500 ALA A 400 -77.53 -66.89
REMARK 500 LEU A 401 -64.98 -16.70
REMARK 500 HIS A 402 2.10 -55.24
REMARK 500 PRO A 405 -9.90 -45.90
REMARK 500 GLU A 410 53.78 35.81
REMARK 500 LEU A 415 96.10 -160.96
REMARK 500 GLU A 417 2.05 -57.47
REMARK 500 LYS A 422 -29.83 126.59
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 33 LYS A 34 142.74
REMARK 500 PRO A 202 PHE A 203 -129.02
REMARK 500 ALA A 322 THR A 323 -149.99
REMARK 500 THR A 323 HIS A 324 148.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A1501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 442 SG
REMARK 620 2 HEM A1501 NA 99.1
REMARK 620 3 HEM A1501 NB 82.9 96.6
REMARK 620 4 HEM A1501 NC 83.5 174.6 88.4
REMARK 620 5 HEM A1501 ND 99.7 83.8 177.2 91.1
REMARK 620 6 MYT A1499 N14 172.2 86.0 90.5 92.0 86.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYT A1499
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W0E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4
REMARK 900 RELATED ID: 1W0F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N TERMINUS TRUNCATED. THE CONFLICT SHOWN BELOW HAS
REMARK 999 HAS BEEN DESRCRIBED BY GONZALEZ ET AL., DNA VOL: 7,
REMARK 999 PAGES 79-86, 1998.
DBREF 1W0G A 23 24 PDB 1W0G 1W0G 23 24
DBREF 1W0G A 25 503 UNP P08684 CP34_HUMAN 24 502
DBREF 1W0G A 504 507 PDB 1W0G 1W0G 504 507
SEQADV 1W0G VAL A 392 UNP P08684 TRP 391 CONFLICT
SEQRES 1 A 485 MET ALA TYR GLY THR HIS SER HIS GLY LEU PHE LYS LYS
SEQRES 2 A 485 LEU GLY ILE PRO GLY PRO THR PRO LEU PRO PHE LEU GLY
SEQRES 3 A 485 ASN ILE LEU SER TYR HIS LYS GLY PHE CYS MET PHE ASP
SEQRES 4 A 485 MET GLU CYS HIS LYS LYS TYR GLY LYS VAL TRP GLY PHE
SEQRES 5 A 485 TYR ASP GLY GLN GLN PRO VAL LEU ALA ILE THR ASP PRO
SEQRES 6 A 485 ASP MET ILE LYS THR VAL LEU VAL LYS GLU CYS TYR SER
SEQRES 7 A 485 VAL PHE THR ASN ARG ARG PRO PHE GLY PRO VAL GLY PHE
SEQRES 8 A 485 MET LYS SER ALA ILE SER ILE ALA GLU ASP GLU GLU TRP
SEQRES 9 A 485 LYS ARG LEU ARG SER LEU LEU SER PRO THR PHE THR SER
SEQRES 10 A 485 GLY LYS LEU LYS GLU MET VAL PRO ILE ILE ALA GLN TYR
SEQRES 11 A 485 GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA GLU
SEQRES 12 A 485 THR GLY LYS PRO VAL THR LEU LYS ASP VAL PHE GLY ALA
SEQRES 13 A 485 TYR SER MET ASP VAL ILE THR SER THR SER PHE GLY VAL
SEQRES 14 A 485 ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE VAL
SEQRES 15 A 485 GLU ASN THR LYS LYS LEU LEU ARG PHE ASP PHE LEU ASP
SEQRES 16 A 485 PRO PHE PHE LEU SER ILE THR VAL PHE PRO PHE LEU ILE
SEQRES 17 A 485 PRO ILE LEU GLU VAL LEU ASN ILE CYS VAL PHE PRO ARG
SEQRES 18 A 485 GLU VAL THR ASN PHE LEU ARG LYS SER VAL LYS ARG MET
SEQRES 19 A 485 LYS GLU SER ARG LEU GLU ASP THR GLN LYS HIS ARG VAL
SEQRES 20 A 485 ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER LYS
SEQRES 21 A 485 GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU LEU
SEQRES 22 A 485 VAL ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR GLU
SEQRES 23 A 485 THR THR SER SER VAL LEU SER PHE ILE MET TYR GLU LEU
SEQRES 24 A 485 ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN GLU GLU
SEQRES 25 A 485 ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR TYR
SEQRES 26 A 485 ASP THR VAL LEU GLN MET GLU TYR LEU ASP MET VAL VAL
SEQRES 27 A 485 ASN GLU THR LEU ARG LEU PHE PRO ILE ALA MET ARG LEU
SEQRES 28 A 485 GLU ARG VAL CYS LYS LYS ASP VAL GLU ILE ASN GLY MET
SEQRES 29 A 485 PHE ILE PRO LYS GLY VAL VAL VAL MET ILE PRO SER TYR
SEQRES 30 A 485 ALA LEU HIS ARG ASP PRO LYS TYR TRP THR GLU PRO GLU
SEQRES 31 A 485 LYS PHE LEU PRO GLU ARG PHE SER LYS LYS ASN LYS ASP
SEQRES 32 A 485 ASN ILE ASP PRO TYR ILE TYR THR PRO PHE GLY SER GLY
SEQRES 33 A 485 PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN
SEQRES 34 A 485 MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER
SEQRES 35 A 485 PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU
SEQRES 36 A 485 SER LEU GLY GLY LEU LEU GLN PRO GLU LYS PRO VAL VAL
SEQRES 37 A 485 LEU LYS VAL GLU SER ARG ASP GLY THR VAL SER GLY ALA
SEQRES 38 A 485 HIS HIS HIS HIS
HET MYT A1499 17
HET HEM A1501 43
HETNAM MYT METYRAPONE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 MYT C14 H14 N2 O
FORMUL 3 HEM C34 H32 FE N4 O4
FORMUL 4 HOH *29(H2 O)
HELIX 1 1 ASN A 49 LYS A 55 5 7
HELIX 2 2 GLY A 56 GLY A 69 1 14
HELIX 3 3 ASP A 86 VAL A 95 1 10
HELIX 4 4 VAL A 111 ALA A 117 5 7
HELIX 5 5 GLU A 122 SER A 131 1 10
HELIX 6 6 LEU A 133 THR A 138 1 6
HELIX 7 7 MET A 145 ASN A 159 1 15
HELIX 8 8 LEU A 160 GLU A 165 1 6
HELIX 9 9 LEU A 172 PHE A 189 1 18
HELIX 10 10 PHE A 203 LYS A 208 1 6
HELIX 11 11 ASP A 217 PHE A 226 1 10
HELIX 12 12 PHE A 228 LEU A 236 1 9
HELIX 13 13 PRO A 242 LEU A 261 1 20
HELIX 14 14 ASP A 270 MET A 275 1 6
HELIX 15 15 SER A 291 LEU A 321 1 31
HELIX 16 16 ASP A 326 LEU A 339 1 14
HELIX 17 17 THR A 346 GLN A 352 1 7
HELIX 18 18 TYR A 355 PHE A 367 1 13
HELIX 19 19 SER A 398 HIS A 402 1 5
HELIX 20 20 LEU A 415 SER A 420 5 6
HELIX 21 21 GLY A 444 GLN A 461 1 18
SHEET 1 AA 4 TRP A 72 ASP A 76 0
SHEET 2 AA 4 GLN A 79 ALA A 83 -1 O GLN A 79 N ASP A 76
SHEET 3 AA 4 VAL A 393 PRO A 397 1 O VAL A 393 N LEU A 82
SHEET 4 AA 4 ARG A 372 VAL A 376 -1 O LEU A 373 N ILE A 396
SHEET 1 AB 3 VAL A 170 THR A 171 0
SHEET 2 AB 3 VAL A 490 SER A 495 -1 O LEU A 491 N VAL A 170
SHEET 3 AB 3 PHE A 463 LYS A 466 -1 O SER A 464 N GLU A 494
SHEET 1 AC 2 VAL A 381 ILE A 383 0
SHEET 2 AC 2 MET A 386 ILE A 388 -1 O MET A 386 N ILE A 383
LINK SG CYS A 442 FE HEM A1501 1555 1555 2.22
LINK N14 MYT A1499 FE HEM A1501 1555 1555 2.27
SITE 1 AC1 19 ARG A 105 ILE A 118 TRP A 126 ARG A 130
SITE 2 AC1 19 PHE A 137 PHE A 302 ALA A 305 THR A 309
SITE 3 AC1 19 ARG A 375 PRO A 434 PHE A 435 GLY A 436
SITE 4 AC1 19 SER A 437 ARG A 440 ASN A 441 CYS A 442
SITE 5 AC1 19 ILE A 443 ALA A 448 MYT A1499
SITE 1 AC2 5 SER A 119 ALA A 305 THR A 309 ALA A 370
SITE 2 AC2 5 HEM A1501
CRYST1 77.940 100.910 131.000 90.00 90.00 90.00 I 2 2 2 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 0.012830 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
