HEADER OXIDOREDUCTASE 09-JAN-10 3LC4
TITLE HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-DODECANOIC
TITLE 2 ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 2E1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 32-493;
COMPND 5 SYNONYM: CYPIIE1, 4-NITROPHENOL 2-HYDROXYLASE, P450-J;
COMPND 6 EC: 1.14.13.-;
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: CYP2E, CYP2E1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOPP3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK2E1DH
KEYWDS CYP2E1, P450 2E1, MONOOXYGENASE, ACETAMINOPHEN, HEME, ENDOPLASMIC
KEYWDS 2 RETICULUM, IRON, MEMBRANE, METAL-BINDING, MICROSOME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.E.SCOTT,P.R.PORUBSKY
REVDAT 3 06-SEP-23 3LC4 1 REMARK SEQADV LINK
REVDAT 2 28-JUL-10 3LC4 1 JRNL
REVDAT 1 12-MAY-10 3LC4 0
JRNL AUTH P.R.PORUBSKY,K.P.BATTAILE,E.E.SCOTT
JRNL TITL HUMAN CYTOCHROME P450 2E1 STRUCTURES WITH FATTY ACID ANALOGS
JRNL TITL 2 REVEAL A PREVIOUSLY UNOBSERVED BINDING MODE.
JRNL REF J.BIOL.CHEM. V. 285 22282 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20463018
JRNL DOI 10.1074/JBC.M110.109017
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 18847
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1018
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1313
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : 0.28000
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): 0.543
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.429
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.186
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7848 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10648 ; 1.504 ; 2.012
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 915 ; 6.345 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 370 ;35.617 ;23.135
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1335 ;23.341 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;21.775 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1125 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6014 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
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): 4609 ; 0.498 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7508 ; 0.975 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3239 ; 1.350 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3140 ; 2.421 ; 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 : 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 : 1.40
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 3LC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-09
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 : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SIDE-SCATTERING CUBEROOT I- BEAM
REMARK 200 BENT SINGLE CRYSTAL. ASYMMETRIC
REMARK 200 CUT 12.2 DEGS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19925
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 38.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.18900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3E6I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAHEPES PH 7.5, 5% ISO-PROPANOL, 22%
REMARK 280 PEG 2000 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 112.31450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 168.47175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.15725
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 22
REMARK 465 ALA A 23
REMARK 465 LYS A 24
REMARK 465 LYS A 25
REMARK 465 THR A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 LYS A 29
REMARK 465 GLY A 30
REMARK 465 GLY A 139
REMARK 465 LYS A 140
REMARK 465 GLN A 141
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 MET B 22
REMARK 465 ALA B 23
REMARK 465 LYS B 24
REMARK 465 LYS B 25
REMARK 465 THR B 26
REMARK 465 SER B 27
REMARK 465 SER B 28
REMARK 465 LYS B 29
REMARK 465 GLY B 30
REMARK 465 MET B 138
REMARK 465 GLY B 139
REMARK 465 LYS B 140
REMARK 465 GLN B 141
REMARK 465 HIS B 494
REMARK 465 HIS B 495
REMARK 465 HIS B 496
REMARK 465 HIS B 497
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 PRO A 104 C - N - CA ANGL. DEV. = 9.1 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 ILE A 41 -73.55 69.06
REMARK 500 PHE A 97 40.70 -103.71
REMARK 500 ALA A 108 -29.59 -39.22
REMARK 500 ILE A 114 -78.38 -134.89
REMARK 500 LEU A 171 -62.27 -101.08
REMARK 500 ARG A 186 38.59 39.19
REMARK 500 TYR A 191 11.53 -63.80
REMARK 500 CYS A 261 79.17 -106.67
REMARK 500 LYS A 275 -17.41 -42.88
REMARK 500 GLU A 276 37.94 -146.74
REMARK 500 ALA A 280 -72.84 -54.95
REMARK 500 TYR A 318 76.02 -117.44
REMARK 500 SER A 336 -64.70 -126.36
REMARK 500 THR A 362 61.09 38.65
REMARK 500 VAL A 364 79.34 -102.92
REMARK 500 ASN A 367 -178.43 60.32
REMARK 500 ARG A 379 -126.07 54.87
REMARK 500 ASP A 405 70.07 43.94
REMARK 500 SER A 431 -168.30 82.32
REMARK 500 CYS A 437 126.58 -36.73
REMARK 500 PRO A 466 -9.18 -44.43
REMARK 500 PRO A 491 166.94 -38.33
REMARK 500 PRO B 34 179.17 -57.13
REMARK 500 ILE B 41 -46.71 69.06
REMARK 500 ASP B 111 21.71 47.60
REMARK 500 ILE B 114 -71.37 -134.01
REMARK 500 ARG B 186 12.18 53.35
REMARK 500 TYR B 191 16.46 -66.72
REMARK 500 ASN B 192 -9.12 -144.11
REMARK 500 SER B 231 -7.29 -54.43
REMARK 500 SER B 279 120.91 -36.06
REMARK 500 TYR B 318 76.18 -119.98
REMARK 500 SER B 336 -62.84 -109.91
REMARK 500 THR B 362 57.34 37.72
REMARK 500 VAL B 364 75.14 -108.64
REMARK 500 ASN B 367 172.96 61.04
REMARK 500 ASP B 375 126.97 -37.57
REMARK 500 ARG B 379 -115.68 55.03
REMARK 500 ASN B 416 139.75 82.84
REMARK 500 SER B 431 -167.73 78.61
REMARK 500 PRO B 466 -18.67 -44.84
REMARK 500 PRO B 491 164.58 -47.26
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 A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 437 SG
REMARK 620 2 HEM A 500 NA 97.2
REMARK 620 3 HEM A 500 NB 83.3 87.4
REMARK 620 4 HEM A 500 NC 83.2 179.2 92.0
REMARK 620 5 HEM A 500 ND 96.3 93.4 179.2 87.2
REMARK 620 6 LC4 A 501 N15 167.0 71.9 89.1 107.6 91.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 437 SG
REMARK 620 2 HEM B 500 NA 96.8
REMARK 620 3 HEM B 500 NB 82.9 87.3
REMARK 620 4 HEM B 500 NC 83.0 178.7 91.4
REMARK 620 5 HEM B 500 ND 94.9 95.0 177.0 86.3
REMARK 620 6 LC4 B 501 N15 164.0 67.3 94.5 112.9 88.2
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 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC4 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GPH RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-DECANOIC
REMARK 900 ACID
REMARK 900 RELATED ID: 3KOH RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-OCTANOIC
REMARK 900 ACID
REMARK 900 RELATED ID: 3E6I RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH INDAZOLE
REMARK 900 RELATED ID: 3E4E RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH 4-METHYLPYRAZOLE
DBREF 3LC4 A 32 493 UNP P05181 CP2E1_HUMAN 32 493
DBREF 3LC4 B 32 493 UNP P05181 CP2E1_HUMAN 32 493
SEQADV 3LC4 MET A 22 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 ALA A 23 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS A 24 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS A 25 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 THR A 26 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 SER A 27 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 SER A 28 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS A 29 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 GLY A 30 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS A 31 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS A 494 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS A 495 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS A 496 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS A 497 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 MET B 22 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 ALA B 23 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS B 24 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS B 25 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 THR B 26 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 SER B 27 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 SER B 28 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS B 29 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 GLY B 30 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 LYS B 31 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS B 494 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS B 495 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS B 496 UNP P05181 EXPRESSION TAG
SEQADV 3LC4 HIS B 497 UNP P05181 EXPRESSION TAG
SEQRES 1 A 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 A 476 GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN
SEQRES 3 A 476 LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU
SEQRES 4 A 476 ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY
SEQRES 5 A 476 SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL
SEQRES 6 A 476 LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY
SEQRES 7 A 476 ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG
SEQRES 8 A 476 GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE
SEQRES 9 A 476 ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET
SEQRES 10 A 476 GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA
SEQRES 11 A 476 HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN
SEQRES 12 A 476 PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS
SEQRES 13 A 476 ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP
SEQRES 14 A 476 TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE
SEQRES 15 A 476 ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN
SEQRES 16 A 476 LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO
SEQRES 17 A 476 GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL
SEQRES 18 A 476 LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN
SEQRES 19 A 476 SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS
SEQRES 20 A 476 LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU
SEQRES 21 A 476 ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA
SEQRES 22 A 476 ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR
SEQRES 23 A 476 LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU
SEQRES 24 A 476 ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE
SEQRES 25 A 476 GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU
SEQRES 26 A 476 MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG
SEQRES 27 A 476 PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA
SEQRES 28 A 476 THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS
SEQRES 29 A 476 GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR
SEQRES 30 A 476 ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO
SEQRES 31 A 476 GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER
SEQRES 32 A 476 ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS
SEQRES 33 A 476 ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU
SEQRES 34 A 476 LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU
SEQRES 35 A 476 VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE
SEQRES 36 A 476 GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL
SEQRES 37 A 476 ILE PRO ARG SER HIS HIS HIS HIS
SEQRES 1 B 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 B 476 GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN
SEQRES 3 B 476 LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU
SEQRES 4 B 476 ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY
SEQRES 5 B 476 SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL
SEQRES 6 B 476 LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY
SEQRES 7 B 476 ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG
SEQRES 8 B 476 GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE
SEQRES 9 B 476 ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET
SEQRES 10 B 476 GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA
SEQRES 11 B 476 HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN
SEQRES 12 B 476 PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS
SEQRES 13 B 476 ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP
SEQRES 14 B 476 TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE
SEQRES 15 B 476 ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN
SEQRES 16 B 476 LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO
SEQRES 17 B 476 GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL
SEQRES 18 B 476 LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN
SEQRES 19 B 476 SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS
SEQRES 20 B 476 LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU
SEQRES 21 B 476 ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA
SEQRES 22 B 476 ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR
SEQRES 23 B 476 LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU
SEQRES 24 B 476 ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE
SEQRES 25 B 476 GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU
SEQRES 26 B 476 MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG
SEQRES 27 B 476 PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA
SEQRES 28 B 476 THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS
SEQRES 29 B 476 GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR
SEQRES 30 B 476 ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO
SEQRES 31 B 476 GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER
SEQRES 32 B 476 ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS
SEQRES 33 B 476 ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU
SEQRES 34 B 476 LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU
SEQRES 35 B 476 VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE
SEQRES 36 B 476 GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL
SEQRES 37 B 476 ILE PRO ARG SER HIS HIS HIS HIS
HET HEM A 500 43
HET LC4 A 501 19
HET HEM B 500 43
HET LC4 B 501 19
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM LC4 12-(1H-IMIDAZOL-1-YL)DODECANOIC ACID
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 LC4 2(C15 H26 N2 O2)
FORMUL 7 HOH *5(H2 O)
HELIX 1 1 ASN A 44 LEU A 48 5 5
HELIX 2 2 GLU A 49 LYS A 51 5 3
HELIX 3 3 ASN A 52 GLY A 65 1 14
HELIX 4 4 GLY A 82 ASP A 92 1 11
HELIX 5 5 LEU A 103 ARG A 110 5 8
HELIX 6 6 THR A 121 TYR A 136 1 16
HELIX 7 7 GLY A 142 LYS A 160 1 19
HELIX 8 8 PRO A 168 GLY A 173 1 6
HELIX 9 9 GLY A 173 ARG A 186 1 14
HELIX 10 10 ASP A 193 SER A 211 1 19
HELIX 11 11 THR A 212 PHE A 221 1 10
HELIX 12 12 PHE A 221 HIS A 226 1 6
HELIX 13 13 SER A 231 LEU A 257 1 27
HELIX 14 14 ASP A 264 LYS A 275 1 12
HELIX 15 15 THR A 285 TYR A 318 1 34
HELIX 16 16 TYR A 318 ILE A 333 1 16
HELIX 17 17 ALA A 340 GLU A 346 5 7
HELIX 18 18 MET A 347 THR A 362 1 16
HELIX 19 19 LEU A 393 TYR A 398 1 6
HELIX 20 20 LYS A 410 LEU A 415 5 6
HELIX 21 21 THR A 432 VAL A 436 5 5
HELIX 22 22 GLY A 439 HIS A 457 1 19
HELIX 23 23 ASN B 44 LEU B 48 5 5
HELIX 24 24 GLU B 49 LYS B 51 5 3
HELIX 25 25 ASN B 52 GLY B 65 1 14
HELIX 26 26 GLY B 82 TYR B 93 1 12
HELIX 27 27 LYS B 94 SER B 98 5 5
HELIX 28 28 LEU B 103 ARG B 110 5 8
HELIX 29 29 THR B 121 TYR B 136 1 16
HELIX 30 30 GLY B 142 LYS B 160 1 19
HELIX 31 31 ASP B 167 ILE B 172 5 6
HELIX 32 32 GLY B 173 ARG B 186 1 14
HELIX 33 33 ASP B 193 SER B 211 1 19
HELIX 34 34 THR B 212 PHE B 221 1 10
HELIX 35 35 PHE B 221 HIS B 226 1 6
HELIX 36 36 SER B 231 GLN B 255 1 25
HELIX 37 37 ASP B 264 LYS B 275 1 12
HELIX 38 38 THR B 285 TYR B 318 1 34
HELIX 39 39 TYR B 318 GLY B 334 1 17
HELIX 40 40 ALA B 340 GLU B 346 5 7
HELIX 41 41 MET B 347 THR B 362 1 16
HELIX 42 42 THR B 392 TYR B 398 1 7
HELIX 43 43 LYS B 410 LEU B 415 5 6
HELIX 44 44 GLY B 439 HIS B 457 1 19
SHEET 1 A 5 VAL A 67 VAL A 72 0
SHEET 2 A 5 GLN A 75 HIS A 81 -1 O MET A 77 N LEU A 70
SHEET 3 A 5 VAL A 388 THR A 392 1 O VAL A 390 N VAL A 78
SHEET 4 A 5 HIS A 370 GLU A 371 -1 N HIS A 370 O VAL A 389
SHEET 5 A 5 GLY A 99 ARG A 100 -1 N GLY A 99 O GLU A 371
SHEET 1 B 3 PRO A 165 PHE A 166 0
SHEET 2 B 3 LEU A 487 PRO A 491 -1 O LEU A 487 N PHE A 166
SHEET 3 B 3 PHE A 458 PRO A 462 -1 N LYS A 461 O CYS A 488
SHEET 1 C 2 THR A 376 PHE A 378 0
SHEET 2 C 2 TYR A 381 ILE A 383 -1 O TYR A 381 N PHE A 378
SHEET 1 D 2 HIS A 475 ILE A 476 0
SHEET 2 D 2 CYS A 480 ILE A 481 -1 O ILE A 481 N HIS A 475
SHEET 1 E 5 VAL B 67 VAL B 72 0
SHEET 2 E 5 GLN B 75 MET B 80 -1 O MET B 77 N LEU B 70
SHEET 3 E 5 VAL B 388 PRO B 391 1 O VAL B 390 N VAL B 78
SHEET 4 E 5 HIS B 370 GLU B 371 -1 N HIS B 370 O VAL B 389
SHEET 5 E 5 GLY B 99 ARG B 100 -1 N GLY B 99 O GLU B 371
SHEET 1 F 2 THR B 376 PHE B 378 0
SHEET 2 F 2 TYR B 381 ILE B 383 -1 O ILE B 383 N THR B 376
SHEET 1 G 2 PHE B 458 PRO B 462 0
SHEET 2 G 2 LEU B 487 PRO B 491 -1 O CYS B 488 N LYS B 461
SHEET 1 H 2 HIS B 475 ILE B 476 0
SHEET 2 H 2 CYS B 480 ILE B 481 -1 O ILE B 481 N HIS B 475
LINK SG CYS A 437 FE HEM A 500 1555 1555 2.53
LINK FE HEM A 500 N15 LC4 A 501 1555 1555 2.47
LINK SG CYS B 437 FE HEM B 500 1555 1555 2.42
LINK FE HEM B 500 N15 LC4 B 501 1555 1555 2.63
SITE 1 AC1 20 ARG A 100 ILE A 114 ILE A 115 TRP A 122
SITE 2 AC1 20 ARG A 126 ALA A 299 GLY A 300 THR A 303
SITE 3 AC1 20 THR A 307 ASN A 367 LEU A 368 HIS A 370
SITE 4 AC1 20 LEU A 393 PRO A 429 PHE A 430 SER A 431
SITE 5 AC1 20 ARG A 435 CYS A 437 GLY A 439 LC4 A 501
SITE 1 AC2 9 HIS A 109 ASN A 206 PHE A 207 VAL A 239
SITE 2 AC2 9 VAL A 242 LYS A 243 PHE A 298 THR A 303
SITE 3 AC2 9 HEM A 500
SITE 1 AC3 20 ARG B 100 ILE B 114 ILE B 115 TRP B 122
SITE 2 AC3 20 ARG B 126 ALA B 299 GLY B 300 THR B 303
SITE 3 AC3 20 ASN B 367 LEU B 368 HIS B 370 LEU B 393
SITE 4 AC3 20 PRO B 429 SER B 431 ARG B 435 CYS B 437
SITE 5 AC3 20 ALA B 438 GLY B 439 ALA B 443 LC4 B 501
SITE 1 AC4 10 HIS B 109 ASN B 206 PHE B 207 VAL B 239
SITE 2 AC4 10 VAL B 242 LYS B 243 PHE B 298 THR B 303
SITE 3 AC4 10 LEU B 368 HEM B 500
CRYST1 70.779 70.779 224.629 90.00 90.00 90.00 P 43 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 0.014129 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004452 0.00000
(ATOM LINES ARE NOT SHOWN.)
END