HEADER OXIDOREDUCTASE 14-DEC-05 2FDV
TITLE MICROSOMAL P450 2A6 WITH THE INHIBITOR N-METHYL(5-(PYRIDIN-3-YL)FURAN-
TITLE 2 2-YL)METHANAMINE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 2A6;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYPIIA6, COUMARIN 7-HYDROXYLASE, P450 IIA3, CYP2A3, P450I;
COMPND 5 EC: 1.14.14.1;
COMPND 6 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: CYP2A6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH-5 ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS CYP2A6, P450 2A6, P450, MONOOXYGENASE, DRUG METABOLIZING ENZYME,
KEYWDS 2 COUMARIN 7-HYDROXYLASE, NICOTINE OXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.YANO,C.D.STOUT,E.F.JOHNSON
REVDAT 4 30-AUG-23 2FDV 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2FDV 1 VERSN
REVDAT 2 12-DEC-06 2FDV 1 JRNL
REVDAT 1 28-NOV-06 2FDV 0
JRNL AUTH J.K.YANO,T.T.DENTON,M.A.CERNY,X.ZHANG,E.F.JOHNSON,
JRNL AUTH 2 J.R.CASHMAN
JRNL TITL SYNTHETIC INHIBITORS OF CYTOCHROME P-450 2A6: INHIBITORY
JRNL TITL 2 ACTIVITY, DIFFERENCE SPECTRA, MECHANISM OF INHIBITION, AND
JRNL TITL 3 PROTEIN COCRYSTALLIZATION.
JRNL REF J.MED.CHEM. V. 49 6987 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 17125252
JRNL DOI 10.1021/JM060519R
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 248540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 12294
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15029
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 281
REMARK 3 SOLVENT ATOMS : 1437
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.023
REMARK 3 BOND ANGLES (DEGREES) : 1.950
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
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 : SINGLE CRYSTAL SI(311) BENT
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING);
REMARK 200 SINGLE CRYSTAL SI(311) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 278644
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.66200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1Z10
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL2000, MONOMETHYL
REMARK 280 ETHER, TRIS, AMMONIUM SULFATE, ANAPOE-X-405 , PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 78.71500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 LYS A 26
REMARK 465 THR A 27
REMARK 465 SER A 28
REMARK 465 SER A 29
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 MET B 23
REMARK 465 ALA B 24
REMARK 465 LYS B 25
REMARK 465 LYS B 26
REMARK 465 THR B 27
REMARK 465 SER B 28
REMARK 465 SER B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 HIS B 497
REMARK 465 HIS B 498
REMARK 465 MET C 23
REMARK 465 ALA C 24
REMARK 465 LYS C 25
REMARK 465 LYS C 26
REMARK 465 THR C 27
REMARK 465 SER C 28
REMARK 465 SER C 29
REMARK 465 LYS C 30
REMARK 465 HIS C 495
REMARK 465 HIS C 496
REMARK 465 HIS C 497
REMARK 465 HIS C 498
REMARK 465 MET D 23
REMARK 465 ALA D 24
REMARK 465 LYS D 25
REMARK 465 LYS D 26
REMARK 465 THR D 27
REMARK 465 SER D 28
REMARK 465 SER D 29
REMARK 465 LYS D 30
REMARK 465 HIS D 495
REMARK 465 HIS D 496
REMARK 465 HIS D 497
REMARK 465 HIS D 498
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 103 CG GLU C 103 CD 0.114
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 269 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 MET B 352 CG - SD - CE ANGL. DEV. = -10.0 DEGREES
REMARK 500 GLN C 104 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG D 64 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 381 NE - CZ - NH1 ANGL. DEV. = 3.1 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 PHE A 42 -51.88 62.14
REMARK 500 PHE A 118 51.66 -97.02
REMARK 500 SER A 369 -160.55 56.33
REMARK 500 SER A 433 -168.31 63.58
REMARK 500 PHE B 42 -53.49 63.79
REMARK 500 PHE B 118 55.59 -93.73
REMARK 500 ASP B 195 112.83 -32.01
REMARK 500 ASP B 266 -169.99 -161.21
REMARK 500 SER B 369 -162.54 53.92
REMARK 500 ARG B 381 -130.64 52.58
REMARK 500 SER B 433 -166.34 66.32
REMARK 500 HIS B 495 -4.98 91.37
REMARK 500 LYS C 32 -103.76 110.95
REMARK 500 PHE C 42 -53.65 69.62
REMARK 500 SER C 369 -162.91 57.87
REMARK 500 ARG C 381 -132.94 49.72
REMARK 500 SER C 433 -168.94 60.78
REMARK 500 PHE D 42 -52.73 64.71
REMARK 500 ASN D 45 30.59 -96.66
REMARK 500 VAL D 140 110.57 63.18
REMARK 500 THR D 258 14.90 -159.13
REMARK 500 PRO D 261 -16.21 -41.17
REMARK 500 ASP D 266 -167.74 -164.07
REMARK 500 SER D 369 -159.87 52.15
REMARK 500 ARG D 381 -136.34 56.00
REMARK 500 SER D 433 -167.55 64.72
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 439 SG
REMARK 620 2 HEM A 500 NA 96.0
REMARK 620 3 HEM A 500 NB 90.1 89.6
REMARK 620 4 HEM A 500 NC 85.9 177.6 88.9
REMARK 620 5 HEM A 500 ND 94.2 89.7 175.7 91.6
REMARK 620 6 D2G A 501 N_2 175.2 88.3 87.8 89.7 87.9
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 439 SG
REMARK 620 2 HEM B 500 NA 96.7
REMARK 620 3 HEM B 500 NB 90.9 89.9
REMARK 620 4 HEM B 500 NC 86.8 176.4 90.9
REMARK 620 5 HEM B 500 ND 93.3 90.3 175.8 88.7
REMARK 620 6 D2G B 501 N_2 173.7 89.5 90.2 87.0 85.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 439 SG
REMARK 620 2 HEM C 500 NA 95.2
REMARK 620 3 HEM C 500 NB 90.4 90.0
REMARK 620 4 HEM C 500 NC 86.7 177.8 91.0
REMARK 620 5 HEM C 500 ND 91.8 89.4 177.8 89.5
REMARK 620 6 D2G C 501 N_2 175.0 89.8 89.1 88.3 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 439 SG
REMARK 620 2 HEM D 500 NA 97.0
REMARK 620 3 HEM D 500 NB 88.7 88.8
REMARK 620 4 HEM D 500 NC 85.4 177.4 90.2
REMARK 620 5 HEM D 500 ND 94.6 90.2 176.6 90.6
REMARK 620 6 D2G D 501 N_2 175.3 87.8 91.8 89.9 84.9
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 SO4 A 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D2G A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D2G B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D2G C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D2G D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MICROSOMAL P450 2A6 WITH COUMARIN
REMARK 900 RELATED ID: 1Z11 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN WITH METHOXSALEN
REMARK 900 RELATED ID: 2FDU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN WITH THE INHIBITOR N,N-
REMARK 900 DIMETHYL(5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE
REMARK 900 RELATED ID: 2FDW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN WITH THE INHIBITOR (5-
REMARK 900 (PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE
REMARK 900 RELATED ID: 2FDY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN WITH THE INHIBITOR ADRITHIOL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-28 WERE REPLACED WITH THE SEQUENCE MAKKTS
DBREF 2FDV A 29 494 UNP P11509 CP2A6_HUMAN 29 494
DBREF 2FDV B 29 494 UNP P11509 CP2A6_HUMAN 29 494
DBREF 2FDV C 29 494 UNP P11509 CP2A6_HUMAN 29 494
DBREF 2FDV D 29 494 UNP P11509 CP2A6_HUMAN 29 494
SEQADV 2FDV MET A 23 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV ALA A 24 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS A 25 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS A 26 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV THR A 27 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV SER A 28 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV HIS A 495 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS A 496 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS A 497 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS A 498 UNP P11509 EXPRESSION TAG
SEQADV 2FDV MET B 23 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV ALA B 24 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS B 25 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS B 26 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV THR B 27 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV SER B 28 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV HIS B 495 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS B 496 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS B 497 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS B 498 UNP P11509 EXPRESSION TAG
SEQADV 2FDV MET C 23 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV ALA C 24 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS C 25 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS C 26 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV THR C 27 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV SER C 28 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV HIS C 495 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS C 496 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS C 497 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS C 498 UNP P11509 EXPRESSION TAG
SEQADV 2FDV MET D 23 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV ALA D 24 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS D 25 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV LYS D 26 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV THR D 27 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV SER D 28 UNP P11509 CLONING ARTIFACT
SEQADV 2FDV HIS D 495 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS D 496 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS D 497 UNP P11509 EXPRESSION TAG
SEQADV 2FDV HIS D 498 UNP P11509 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 THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN
SEQRES 3 A 476 LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE
SEQRES 4 A 476 SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY
SEQRES 5 A 476 PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL
SEQRES 6 A 476 ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY
SEQRES 7 A 476 ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY
SEQRES 8 A 476 TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN
SEQRES 9 A 476 LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY
SEQRES 10 A 476 VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 A 476 ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY
SEQRES 12 A 476 ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL
SEQRES 13 A 476 SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE
SEQRES 14 A 476 ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET
SEQRES 15 A 476 MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY
SEQRES 16 A 476 GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU
SEQRES 17 A 476 PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY
SEQRES 18 A 476 LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN
SEQRES 19 A 476 ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP
SEQRES 20 A 476 SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO
SEQRES 21 A 476 ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR
SEQRES 22 A 476 LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR
SEQRES 23 A 476 THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO
SEQRES 24 A 476 GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL
SEQRES 25 A 476 ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA
SEQRES 26 A 476 LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN
SEQRES 27 A 476 ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG
SEQRES 28 A 476 VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO
SEQRES 29 A 476 LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU
SEQRES 30 A 476 ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN
SEQRES 31 A 476 PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS
SEQRES 32 A 476 SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN
SEQRES 33 A 476 CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU
SEQRES 34 A 476 PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER
SEQRES 35 A 476 SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS
SEQRES 36 A 476 VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER
SEQRES 37 A 476 PHE LEU PRO ARG 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 THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN
SEQRES 3 B 476 LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE
SEQRES 4 B 476 SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY
SEQRES 5 B 476 PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL
SEQRES 6 B 476 ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY
SEQRES 7 B 476 ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY
SEQRES 8 B 476 TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN
SEQRES 9 B 476 LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY
SEQRES 10 B 476 VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 B 476 ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY
SEQRES 12 B 476 ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL
SEQRES 13 B 476 SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE
SEQRES 14 B 476 ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET
SEQRES 15 B 476 MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY
SEQRES 16 B 476 GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU
SEQRES 17 B 476 PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY
SEQRES 18 B 476 LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN
SEQRES 19 B 476 ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP
SEQRES 20 B 476 SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO
SEQRES 21 B 476 ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR
SEQRES 22 B 476 LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR
SEQRES 23 B 476 THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO
SEQRES 24 B 476 GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL
SEQRES 25 B 476 ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA
SEQRES 26 B 476 LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN
SEQRES 27 B 476 ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG
SEQRES 28 B 476 VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO
SEQRES 29 B 476 LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU
SEQRES 30 B 476 ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN
SEQRES 31 B 476 PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS
SEQRES 32 B 476 SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN
SEQRES 33 B 476 CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU
SEQRES 34 B 476 PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER
SEQRES 35 B 476 SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS
SEQRES 36 B 476 VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER
SEQRES 37 B 476 PHE LEU PRO ARG HIS HIS HIS HIS
SEQRES 1 C 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 C 476 GLY PRO THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN
SEQRES 3 C 476 LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE
SEQRES 4 C 476 SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY
SEQRES 5 C 476 PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL
SEQRES 6 C 476 ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY
SEQRES 7 C 476 ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY
SEQRES 8 C 476 TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN
SEQRES 9 C 476 LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY
SEQRES 10 C 476 VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 C 476 ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY
SEQRES 12 C 476 ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL
SEQRES 13 C 476 SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE
SEQRES 14 C 476 ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET
SEQRES 15 C 476 MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY
SEQRES 16 C 476 GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU
SEQRES 17 C 476 PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY
SEQRES 18 C 476 LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN
SEQRES 19 C 476 ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP
SEQRES 20 C 476 SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO
SEQRES 21 C 476 ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR
SEQRES 22 C 476 LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR
SEQRES 23 C 476 THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO
SEQRES 24 C 476 GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL
SEQRES 25 C 476 ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA
SEQRES 26 C 476 LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN
SEQRES 27 C 476 ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG
SEQRES 28 C 476 VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO
SEQRES 29 C 476 LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU
SEQRES 30 C 476 ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN
SEQRES 31 C 476 PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS
SEQRES 32 C 476 SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN
SEQRES 33 C 476 CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU
SEQRES 34 C 476 PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER
SEQRES 35 C 476 SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS
SEQRES 36 C 476 VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER
SEQRES 37 C 476 PHE LEU PRO ARG HIS HIS HIS HIS
SEQRES 1 D 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 D 476 GLY PRO THR PRO LEU PRO PHE ILE GLY ASN TYR LEU GLN
SEQRES 3 D 476 LEU ASN THR GLU GLN MET TYR ASN SER LEU MET LYS ILE
SEQRES 4 D 476 SER GLU ARG TYR GLY PRO VAL PHE THR ILE HIS LEU GLY
SEQRES 5 D 476 PRO ARG ARG VAL VAL VAL LEU CYS GLY HIS ASP ALA VAL
SEQRES 6 D 476 ARG GLU ALA LEU VAL ASP GLN ALA GLU GLU PHE SER GLY
SEQRES 7 D 476 ARG GLY GLU GLN ALA THR PHE ASP TRP VAL PHE LYS GLY
SEQRES 8 D 476 TYR GLY VAL VAL PHE SER ASN GLY GLU ARG ALA LYS GLN
SEQRES 9 D 476 LEU ARG ARG PHE SER ILE ALA THR LEU ARG ASP PHE GLY
SEQRES 10 D 476 VAL GLY LYS ARG GLY ILE GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 D 476 ALA GLY PHE LEU ILE ASP ALA LEU ARG GLY THR GLY GLY
SEQRES 12 D 476 ALA ASN ILE ASP PRO THR PHE PHE LEU SER ARG THR VAL
SEQRES 13 D 476 SER ASN VAL ILE SER SER ILE VAL PHE GLY ASP ARG PHE
SEQRES 14 D 476 ASP TYR LYS ASP LYS GLU PHE LEU SER LEU LEU ARG MET
SEQRES 15 D 476 MET LEU GLY ILE PHE GLN PHE THR SER THR SER THR GLY
SEQRES 16 D 476 GLN LEU TYR GLU MET PHE SER SER VAL MET LYS HIS LEU
SEQRES 17 D 476 PRO GLY PRO GLN GLN GLN ALA PHE GLN LEU LEU GLN GLY
SEQRES 18 D 476 LEU GLU ASP PHE ILE ALA LYS LYS VAL GLU HIS ASN GLN
SEQRES 19 D 476 ARG THR LEU ASP PRO ASN SER PRO ARG ASP PHE ILE ASP
SEQRES 20 D 476 SER PHE LEU ILE ARG MET GLN GLU GLU GLU LYS ASN PRO
SEQRES 21 D 476 ASN THR GLU PHE TYR LEU LYS ASN LEU VAL MET THR THR
SEQRES 22 D 476 LEU ASN LEU PHE ILE GLY GLY THR GLU THR VAL SER THR
SEQRES 23 D 476 THR LEU ARG TYR GLY PHE LEU LEU LEU MET LYS HIS PRO
SEQRES 24 D 476 GLU VAL GLU ALA LYS VAL HIS GLU GLU ILE ASP ARG VAL
SEQRES 25 D 476 ILE GLY LYS ASN ARG GLN PRO LYS PHE GLU ASP ARG ALA
SEQRES 26 D 476 LYS MET PRO TYR MET GLU ALA VAL ILE HIS GLU ILE GLN
SEQRES 27 D 476 ARG PHE GLY ASP VAL ILE PRO MET SER LEU ALA ARG ARG
SEQRES 28 D 476 VAL LYS LYS ASP THR LYS PHE ARG ASP PHE PHE LEU PRO
SEQRES 29 D 476 LYS GLY THR GLU VAL TYR PRO MET LEU GLY SER VAL LEU
SEQRES 30 D 476 ARG ASP PRO SER PHE PHE SER ASN PRO GLN ASP PHE ASN
SEQRES 31 D 476 PRO GLN HIS PHE LEU ASN GLU LYS GLY GLN PHE LYS LYS
SEQRES 32 D 476 SER ASP ALA PHE VAL PRO PHE SER ILE GLY LYS ARG ASN
SEQRES 33 D 476 CYS PHE GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU
SEQRES 34 D 476 PHE PHE THR THR VAL MET GLN ASN PHE ARG LEU LYS SER
SEQRES 35 D 476 SER GLN SER PRO LYS ASP ILE ASP VAL SER PRO LYS HIS
SEQRES 36 D 476 VAL GLY PHE ALA THR ILE PRO ARG ASN TYR THR MET SER
SEQRES 37 D 476 PHE LEU PRO ARG HIS HIS HIS HIS
HET SO4 A2502 5
HET SO4 A2503 5
HET SO4 A2504 5
HET HEM A 500 43
HET D2G A 501 14
HET EDO A2003 4
HET SO4 B2506 5
HET HEM B 500 43
HET D2G B 501 14
HET SO4 C2508 5
HET HEM C 500 43
HET D2G C 501 14
HET EDO C2001 4
HET EDO C2002 4
HET EDO C2004 4
HET EDO C2005 4
HET EDO C2006 4
HET HEM D 500 43
HET D2G D 501 14
HET EDO D2007 4
HETNAM SO4 SULFATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM D2G N-METHYL(5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HEM HEME
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 8 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 D2G 4(C11 H12 N2 O)
FORMUL 10 EDO 7(C2 H6 O2)
FORMUL 25 HOH *1437(H2 O)
HELIX 1 1 ASN A 45 LEU A 49 5 5
HELIX 2 2 ASN A 50 GLU A 52 5 3
HELIX 3 3 GLN A 53 GLY A 66 1 14
HELIX 4 4 GLY A 83 VAL A 92 1 10
HELIX 5 5 GLN A 104 LYS A 112 1 9
HELIX 6 6 ASN A 120 PHE A 138 1 19
HELIX 7 7 LYS A 142 THR A 163 1 22
HELIX 8 8 PRO A 170 GLY A 188 1 19
HELIX 9 9 ASP A 195 SER A 213 1 19
HELIX 10 10 THR A 214 LYS A 228 1 15
HELIX 11 11 GLY A 232 ARG A 257 1 26
HELIX 12 12 ASP A 266 GLU A 278 1 13
HELIX 13 13 TYR A 287 HIS A 320 1 34
HELIX 14 14 HIS A 320 ILE A 335 1 16
HELIX 15 15 LYS A 342 LYS A 348 5 7
HELIX 16 16 MET A 349 ASP A 364 1 16
HELIX 17 17 MET A 394 ARG A 400 1 7
HELIX 18 18 ASN A 412 LEU A 417 5 6
HELIX 19 19 GLY A 441 ASN A 459 1 19
HELIX 20 20 SER A 467 ILE A 471 5 5
HELIX 21 21 ASN B 45 LEU B 49 5 5
HELIX 22 22 ASN B 50 GLU B 52 5 3
HELIX 23 23 GLN B 53 GLY B 66 1 14
HELIX 24 24 CYS B 82 VAL B 92 1 11
HELIX 25 25 GLN B 104 LYS B 112 1 9
HELIX 26 26 ASN B 120 PHE B 138 1 19
HELIX 27 27 LYS B 142 THR B 163 1 22
HELIX 28 28 PRO B 170 GLY B 188 1 19
HELIX 29 29 ASP B 195 THR B 212 1 18
HELIX 30 30 THR B 214 LYS B 228 1 15
HELIX 31 31 GLY B 232 THR B 258 1 27
HELIX 32 32 ASP B 266 GLU B 279 1 14
HELIX 33 33 TYR B 287 HIS B 320 1 34
HELIX 34 34 HIS B 320 ILE B 335 1 16
HELIX 35 35 LYS B 342 LYS B 348 5 7
HELIX 36 36 MET B 349 ASP B 364 1 16
HELIX 37 37 MET B 394 ARG B 400 1 7
HELIX 38 38 ASN B 412 LEU B 417 5 6
HELIX 39 39 GLY B 441 ASN B 459 1 19
HELIX 40 40 SER B 467 ILE B 471 5 5
HELIX 41 41 ASN C 45 LEU C 49 5 5
HELIX 42 42 ASN C 50 GLU C 52 5 3
HELIX 43 43 GLN C 53 GLY C 66 1 14
HELIX 44 44 GLY C 83 VAL C 92 1 10
HELIX 45 45 GLN C 104 LYS C 112 1 9
HELIX 46 46 ASN C 120 PHE C 138 1 19
HELIX 47 47 LYS C 142 GLY C 162 1 21
HELIX 48 48 PRO C 170 GLY C 188 1 19
HELIX 49 49 ASP C 195 THR C 212 1 18
HELIX 50 50 THR C 214 LYS C 228 1 15
HELIX 51 51 GLY C 232 LEU C 259 1 28
HELIX 52 52 ASP C 266 GLU C 278 1 13
HELIX 53 53 TYR C 287 HIS C 320 1 34
HELIX 54 54 HIS C 320 ILE C 335 1 16
HELIX 55 55 LYS C 342 LYS C 348 5 7
HELIX 56 56 MET C 349 ASP C 364 1 16
HELIX 57 57 MET C 394 ARG C 400 1 7
HELIX 58 58 ASN C 412 LEU C 417 5 6
HELIX 59 59 GLY C 441 ASN C 459 1 19
HELIX 60 60 SER C 467 ILE C 471 5 5
HELIX 61 61 ASN D 45 LEU D 49 5 5
HELIX 62 62 ASN D 50 GLU D 52 5 3
HELIX 63 63 GLN D 53 GLY D 66 1 14
HELIX 64 64 CYS D 82 VAL D 92 1 11
HELIX 65 65 GLN D 104 LYS D 112 1 9
HELIX 66 66 ASN D 120 PHE D 138 1 19
HELIX 67 67 LYS D 142 THR D 163 1 22
HELIX 68 68 PRO D 170 GLY D 188 1 19
HELIX 69 69 ASP D 195 SER D 213 1 19
HELIX 70 70 THR D 214 LYS D 228 1 15
HELIX 71 71 GLY D 232 ARG D 257 1 26
HELIX 72 72 ASP D 266 GLU D 278 1 13
HELIX 73 73 TYR D 287 HIS D 320 1 34
HELIX 74 74 HIS D 320 ILE D 335 1 16
HELIX 75 75 LYS D 342 LYS D 348 5 7
HELIX 76 76 MET D 349 ASP D 364 1 16
HELIX 77 77 MET D 394 ARG D 400 1 7
HELIX 78 78 ASN D 412 LEU D 417 5 6
HELIX 79 79 GLY D 441 ASN D 459 1 19
HELIX 80 80 SER D 467 ILE D 471 5 5
SHEET 1 A 5 VAL A 68 LEU A 73 0
SHEET 2 A 5 ARG A 76 LEU A 81 -1 O VAL A 78 N ILE A 71
SHEET 3 A 5 GLU A 390 PRO A 393 1 O GLU A 390 N VAL A 79
SHEET 4 A 5 ARG A 372 ARG A 373 -1 N ARG A 372 O VAL A 391
SHEET 5 A 5 GLY A 100 ARG A 101 -1 N GLY A 100 O ARG A 373
SHEET 1 B 2 THR A 378 PHE A 380 0
SHEET 2 B 2 PHE A 383 LEU A 385 -1 O LEU A 385 N THR A 378
SHEET 1 C 2 PHE A 460 SER A 464 0
SHEET 2 C 2 MET A 489 PRO A 493 -1 O LEU A 492 N ARG A 461
SHEET 1 D 2 HIS A 477 VAL A 478 0
SHEET 2 D 2 THR A 482 ILE A 483 -1 O ILE A 483 N HIS A 477
SHEET 1 E 5 VAL B 68 LEU B 73 0
SHEET 2 E 5 ARG B 76 LEU B 81 -1 O VAL B 78 N ILE B 71
SHEET 3 E 5 GLU B 390 PRO B 393 1 O TYR B 392 N LEU B 81
SHEET 4 E 5 ARG B 372 ARG B 373 -1 N ARG B 372 O VAL B 391
SHEET 5 E 5 GLY B 100 ARG B 101 -1 N GLY B 100 O ARG B 373
SHEET 1 F 2 THR B 378 PHE B 380 0
SHEET 2 F 2 PHE B 383 LEU B 385 -1 O LEU B 385 N THR B 378
SHEET 1 G 2 PHE B 460 SER B 464 0
SHEET 2 G 2 MET B 489 PRO B 493 -1 O SER B 490 N LYS B 463
SHEET 1 H 2 PRO B 475 VAL B 478 0
SHEET 2 H 2 THR B 482 PRO B 484 -1 O ILE B 483 N LYS B 476
SHEET 1 I 5 VAL C 68 LEU C 73 0
SHEET 2 I 5 ARG C 76 LEU C 81 -1 O VAL C 78 N ILE C 71
SHEET 3 I 5 GLU C 390 PRO C 393 1 O TYR C 392 N LEU C 81
SHEET 4 I 5 ARG C 372 ARG C 373 -1 N ARG C 372 O VAL C 391
SHEET 5 I 5 GLY C 100 ARG C 101 -1 N GLY C 100 O ARG C 373
SHEET 1 J 2 THR C 378 PHE C 380 0
SHEET 2 J 2 PHE C 383 LEU C 385 -1 O LEU C 385 N THR C 378
SHEET 1 K 2 PHE C 460 SER C 464 0
SHEET 2 K 2 MET C 489 PRO C 493 -1 O LEU C 492 N ARG C 461
SHEET 1 L 2 PRO C 475 VAL C 478 0
SHEET 2 L 2 THR C 482 PRO C 484 -1 O ILE C 483 N HIS C 477
SHEET 1 M 5 VAL D 68 LEU D 73 0
SHEET 2 M 5 ARG D 76 LEU D 81 -1 O VAL D 80 N PHE D 69
SHEET 3 M 5 GLU D 390 PRO D 393 1 O TYR D 392 N LEU D 81
SHEET 4 M 5 ARG D 372 ARG D 373 -1 N ARG D 372 O VAL D 391
SHEET 5 M 5 GLY D 100 ARG D 101 -1 N GLY D 100 O ARG D 373
SHEET 1 N 2 THR D 378 PHE D 380 0
SHEET 2 N 2 PHE D 383 LEU D 385 -1 O LEU D 385 N THR D 378
SHEET 1 O 2 PHE D 460 SER D 464 0
SHEET 2 O 2 MET D 489 PRO D 493 -1 O LEU D 492 N ARG D 461
SHEET 1 P 2 PRO D 475 VAL D 478 0
SHEET 2 P 2 THR D 482 PRO D 484 -1 O ILE D 483 N HIS D 477
LINK SG CYS A 439 FE HEM A 500 1555 1555 2.31
LINK FE HEM A 500 N_2 D2G A 501 1555 1555 2.18
LINK SG CYS B 439 FE HEM B 500 1555 1555 2.36
LINK FE HEM B 500 N_2 D2G B 501 1555 1555 2.25
LINK SG CYS C 439 FE HEM C 500 1555 1555 2.30
LINK FE HEM C 500 N_2 D2G C 501 1555 1555 2.16
LINK SG CYS D 439 FE HEM D 500 1555 1555 2.27
LINK FE HEM D 500 N_2 D2G D 501 1555 1555 2.14
SITE 1 AC1 5 ARG A 136 GLY A 141 HOH A2673 HOH A2815
SITE 2 AC1 5 HOH A2820
SITE 1 AC2 5 ARG A 129 HOH A2553 HOH A2704 HOH A2816
SITE 2 AC2 5 HOH A2871
SITE 1 AC3 8 THR A 214 SER A 215 THR A 216 HOH A2529
SITE 2 AC3 8 HOH A2530 HOH A2767 THR B 216 PRO B 233
SITE 1 AC4 5 ARG B 136 GLY B 141 HOH B2597 HOH B2628
SITE 2 AC4 5 HOH B2746
SITE 1 AC5 3 ARG C 136 HOH C2706 HOH C2858
SITE 1 AC6 21 ARG A 101 VAL A 116 VAL A 117 ARG A 128
SITE 2 AC6 21 GLY A 301 GLY A 302 THR A 305 THR A 309
SITE 3 AC6 21 SER A 369 ARG A 372 LEU A 395 PRO A 431
SITE 4 AC6 21 PHE A 432 SER A 433 ARG A 437 CYS A 439
SITE 5 AC6 21 PHE A 440 GLY A 441 D2G A 501 HOH A2508
SITE 6 AC6 21 HOH A2509
SITE 1 AC7 9 PHE A 107 PHE A 111 PHE A 209 ASN A 297
SITE 2 AC7 9 ILE A 300 GLY A 301 THR A 305 PHE A 480
SITE 3 AC7 9 HEM A 500
SITE 1 AC8 19 ARG B 101 VAL B 116 VAL B 117 ARG B 128
SITE 2 AC8 19 THR B 305 THR B 309 SER B 369 ARG B 372
SITE 3 AC8 19 PRO B 431 PHE B 432 SER B 433 ARG B 437
SITE 4 AC8 19 ASN B 438 CYS B 439 PHE B 440 GLY B 441
SITE 5 AC8 19 D2G B 501 HOH B2510 HOH B2517
SITE 1 AC9 8 PHE B 107 PHE B 111 PHE B 209 ASN B 297
SITE 2 AC9 8 GLY B 301 THR B 305 PHE B 480 HEM B 500
SITE 1 BC1 19 ARG C 101 VAL C 117 ARG C 128 GLY C 302
SITE 2 BC1 19 THR C 305 THR C 309 GLN C 360 ARG C 372
SITE 3 BC1 19 LEU C 395 PRO C 431 PHE C 432 SER C 433
SITE 4 BC1 19 ARG C 437 CYS C 439 PHE C 440 GLY C 441
SITE 5 BC1 19 D2G C 501 HOH C2514 HOH C2559
SITE 1 BC2 8 PHE C 107 PHE C 111 PHE C 209 ASN C 297
SITE 2 BC2 8 GLY C 301 THR C 305 PHE C 480 HEM C 500
SITE 1 BC3 21 ARG D 101 VAL D 117 ARG D 128 GLY D 302
SITE 2 BC3 21 THR D 305 THR D 309 GLN D 360 SER D 369
SITE 3 BC3 21 ARG D 372 LEU D 395 PRO D 431 PHE D 432
SITE 4 BC3 21 SER D 433 ARG D 437 CYS D 439 PHE D 440
SITE 5 BC3 21 GLY D 441 LEU D 444 D2G D 501 HOH D2010
SITE 6 BC3 21 HOH D2076
SITE 1 BC4 8 PHE D 107 PHE D 111 PHE D 209 ASN D 297
SITE 2 BC4 8 GLY D 301 THR D 305 PHE D 480 HEM D 500
SITE 1 BC5 3 THR C 38 PRO C 39 LEU C 40
SITE 1 BC6 3 PRO C 37 ARG C 64 TYR C 65
SITE 1 BC7 2 ASP A 85 PHE A 404
SITE 1 BC8 7 GLU C 103 GLN C 104 ASP C 108 LYS C 112
SITE 2 BC8 7 GLY C 113 PHE C 118 HOH C2808
SITE 1 BC9 3 ARG C 88 ASP C 427 HOH C2565
SITE 1 CC1 4 GLN C 210 LYS C 476 ASN C 486 HOH C2606
SITE 1 CC2 5 LYS D 319 HIS D 320 ASP D 410 PHE D 411
SITE 2 CC2 5 VAL D 473
CRYST1 69.927 157.430 103.897 90.00 92.21 90.00 P 1 21 1 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 0.014301 0.000000 0.000552 0.00000
SCALE2 0.000000 0.006352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009632 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
