HEADER OXIDOREDUCTASE, ELECTRON TRANSPORT 31-MAY-10 3N9Y
TITLE CRYSTAL STRUCTURE OF HUMAN CYP11A1 IN COMPLEX WITH CHOLESTEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 41-521;
COMPND 5 SYNONYM: CYTOCHROME P450 11A1, CYPXIA1, CYTOCHROME P450(SCC),
COMPND 6 CHOLESTEROL DESMOLASE;
COMPND 7 EC: 1.14.15.6;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ADRENODOXIN;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: UNP RESIDUES 62-175;
COMPND 13 SYNONYM: ADRENAL FERREDOXIN, FERREDOXIN-1, HEPATOREDOXIN;
COMPND 14 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: CYP11A, CYP11A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCW;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ADRENODOXIN, ADX, FDX1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS CYTOCHROME P450, CHOLESTEROL SIDE CHAIN CLEAVAGE, STRUCTURAL
KEYWDS 2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, OXIDOREDUCTASE,
KEYWDS 3 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR N.V.STRUSHKEVICH,F.MACKENZIE,W.TEMPEL,A.BOTCHKAREV,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,C.BOUNTRA,J.U.WEIGELT,H.PARK,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 5 21-FEB-24 3N9Y 1 REMARK SEQADV LINK
REVDAT 4 08-NOV-17 3N9Y 1 REMARK
REVDAT 3 13-JUL-11 3N9Y 1 JRNL
REVDAT 2 15-JUN-11 3N9Y 1 JRNL
REVDAT 1 08-JUN-11 3N9Y 0
JRNL AUTH N.STRUSHKEVICH,F.MACKENZIE,T.CHERKESOVA,I.GRABOVEC,S.USANOV,
JRNL AUTH 2 H.W.PARK
JRNL TITL STRUCTURAL BASIS FOR PREGNENOLONE BIOSYNTHESIS BY THE
JRNL TITL 2 MITOCHONDRIAL MONOOXYGENASE SYSTEM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 10139 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21636783
JRNL DOI 10.1073/PNAS.1019441108
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 91667
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4576
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6372
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 342
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 150
REMARK 3 SOLVENT ATOMS : 505
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : -2.09000
REMARK 3 B33 (A**2) : 0.83000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.74000
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): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9192 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12507 ; 1.243 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1073 ; 5.346 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;33.856 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1535 ;14.931 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;16.263 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1347 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7008 ; 0.005 ; 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): 5375 ; 0.666 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8709 ; 1.286 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3817 ; 1.830 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3794 ; 3.066 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3N9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-10
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 : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92214
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CA ACETATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 57.34300
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 SER A 2
REMARK 465 THR A 3
REMARK 465 ARG A 4
REMARK 465 ASN A 476
REMARK 465 GLN A 477
REMARK 465 GLU A 478
REMARK 465 ALA A 479
REMARK 465 THR A 480
REMARK 465 GLN A 481
REMARK 465 GLN A 482
REMARK 465 HIS A 483
REMARK 465 HIS A 484
REMARK 465 HIS A 485
REMARK 465 HIS A 486
REMARK 465 HIS A 487
REMARK 465 HIS A 488
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 ARG B 4
REMARK 465 SER B 5
REMARK 465 ASN B 476
REMARK 465 GLN B 477
REMARK 465 GLU B 478
REMARK 465 ALA B 479
REMARK 465 THR B 480
REMARK 465 GLN B 481
REMARK 465 GLN B 482
REMARK 465 HIS B 483
REMARK 465 HIS B 484
REMARK 465 HIS B 485
REMARK 465 HIS B 486
REMARK 465 HIS B 487
REMARK 465 HIS B 488
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 GLU C 4
REMARK 465 ASP C 5
REMARK 465 LYS C 6
REMARK 465 ILE C 7
REMARK 465 THR C 8
REMARK 465 VAL C 9
REMARK 465 HIS C 10
REMARK 465 PHE C 11
REMARK 465 ILE C 12
REMARK 465 ASN C 13
REMARK 465 ARG C 14
REMARK 465 ASP C 15
REMARK 465 GLY C 16
REMARK 465 GLU C 17
REMARK 465 THR C 18
REMARK 465 LEU C 19
REMARK 465 THR C 20
REMARK 465 THR C 21
REMARK 465 LYS C 22
REMARK 465 GLY C 23
REMARK 465 LYS C 24
REMARK 465 VAL C 25
REMARK 465 GLY C 26
REMARK 465 ASP C 27
REMARK 465 LEU C 96
REMARK 465 THR C 97
REMARK 465 LYS C 98
REMARK 465 SER C 99
REMARK 465 MET C 100
REMARK 465 ASP C 101
REMARK 465 ASN C 102
REMARK 465 MET C 103
REMARK 465 THR C 104
REMARK 465 VAL C 105
REMARK 465 ARG C 106
REMARK 465 VAL C 107
REMARK 465 PRO C 108
REMARK 465 GLU C 109
REMARK 465 THR C 110
REMARK 465 VAL C 111
REMARK 465 ALA C 112
REMARK 465 ASP C 113
REMARK 465 ALA C 114
REMARK 465 ARG C 115
REMARK 465 SER D 2
REMARK 465 SER D 3
REMARK 465 GLU D 4
REMARK 465 ASP D 5
REMARK 465 LYS D 6
REMARK 465 ILE D 7
REMARK 465 THR D 8
REMARK 465 VAL D 9
REMARK 465 HIS D 10
REMARK 465 PHE D 11
REMARK 465 ILE D 12
REMARK 465 ASN D 13
REMARK 465 ARG D 14
REMARK 465 ASP D 15
REMARK 465 GLY D 16
REMARK 465 GLU D 17
REMARK 465 THR D 18
REMARK 465 LEU D 19
REMARK 465 THR D 20
REMARK 465 THR D 21
REMARK 465 LYS D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 VAL D 25
REMARK 465 GLY D 26
REMARK 465 ASP D 27
REMARK 465 LEU D 96
REMARK 465 THR D 97
REMARK 465 LYS D 98
REMARK 465 SER D 99
REMARK 465 MET D 100
REMARK 465 ASP D 101
REMARK 465 ASN D 102
REMARK 465 MET D 103
REMARK 465 THR D 104
REMARK 465 VAL D 105
REMARK 465 ARG D 106
REMARK 465 VAL D 107
REMARK 465 PRO D 108
REMARK 465 GLU D 109
REMARK 465 THR D 110
REMARK 465 VAL D 111
REMARK 465 ALA D 112
REMARK 465 ASP D 113
REMARK 465 ALA D 114
REMARK 465 ARG D 115
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 LEU A 460 CA - CB - CG ANGL. DEV. = -16.3 DEGREES
REMARK 500 LEU B 460 CA - CB - CG ANGL. DEV. = -15.4 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 SER A 105 -131.06 36.01
REMARK 500 LYS A 373 -5.50 81.45
REMARK 500 ASP A 405 94.31 -68.57
REMARK 500 LYS A 406 48.24 -86.79
REMARK 500 PHE A 411 47.59 36.06
REMARK 500 LEU A 460 -62.47 72.82
REMARK 500 SER B 105 -144.70 53.84
REMARK 500 LYS B 373 -4.75 80.10
REMARK 500 LYS B 406 36.57 -82.84
REMARK 500 PHE B 411 49.03 37.65
REMARK 500 LEU B 460 -61.16 72.15
REMARK 500 LEU C 38 -167.93 -73.35
REMARK 500 ASP C 39 -67.07 -90.49
REMARK 500 ILE C 40 120.15 -27.66
REMARK 500 GLU C 47 52.48 71.87
REMARK 500 CYS C 52 -157.12 -152.15
REMARK 500 SER C 53 28.31 -150.45
REMARK 500 CYS D 52 -158.95 -144.42
REMARK 500 SER D 53 26.92 -145.46
REMARK 500 GLU D 60 -108.37 -71.37
REMARK 500 ASP D 61 -51.81 -132.09
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 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 423 SG
REMARK 620 2 HEM A 601 NA 96.2
REMARK 620 3 HEM A 601 NB 86.3 89.3
REMARK 620 4 HEM A 601 NC 88.7 175.1 90.6
REMARK 620 5 HEM A 601 ND 98.2 90.5 175.4 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 423 SG
REMARK 620 2 HEM B 601 NA 97.0
REMARK 620 3 HEM B 601 NB 87.0 88.9
REMARK 620 4 HEM B 601 NC 87.8 175.1 90.9
REMARK 620 5 HEM B 601 ND 97.3 91.1 175.7 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 150 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 46 SG
REMARK 620 2 FES C 150 S1 123.1
REMARK 620 3 FES C 150 S2 115.9 93.3
REMARK 620 4 CYS C 52 SG 113.6 103.8 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 150 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 55 SG
REMARK 620 2 FES C 150 S1 105.5
REMARK 620 3 FES C 150 S2 114.1 93.4
REMARK 620 4 CYS C 92 SG 115.4 109.1 116.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 151 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 46 SG
REMARK 620 2 FES D 151 S1 126.2
REMARK 620 3 FES D 151 S2 115.5 91.9
REMARK 620 4 CYS D 52 SG 112.0 101.3 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 151 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 55 SG
REMARK 620 2 FES D 151 S1 118.3
REMARK 620 3 FES D 151 S2 121.9 92.1
REMARK 620 4 CYS D 92 SG 109.8 107.1 105.6
REMARK 620 N 1 2 3
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES D 151
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N9Z RELATED DB: PDB
REMARK 900 RELATED ID: 3NA0 RELATED DB: PDB
REMARK 900 RELATED ID: 3NA1 RELATED DB: PDB
DBREF 3N9Y A 2 482 UNP P05108 CP11A_HUMAN 41 521
DBREF 3N9Y B 2 482 UNP P05108 CP11A_HUMAN 41 521
DBREF 3N9Y C 2 115 UNP P10109 ADX_HUMAN 62 175
DBREF 3N9Y D 2 115 UNP P10109 ADX_HUMAN 62 175
SEQADV 3N9Y HIS A 483 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS A 484 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS A 485 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS A 486 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS A 487 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS A 488 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 483 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 484 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 485 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 486 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 487 UNP P05108 EXPRESSION TAG
SEQADV 3N9Y HIS B 488 UNP P05108 EXPRESSION TAG
SEQRES 1 A 487 SER THR ARG SER PRO ARG PRO PHE ASN GLU ILE PRO SER
SEQRES 2 A 487 PRO GLY ASP ASN GLY TRP LEU ASN LEU TYR HIS PHE TRP
SEQRES 3 A 487 ARG GLU THR GLY THR HIS LYS VAL HIS LEU HIS HIS VAL
SEQRES 4 A 487 GLN ASN PHE GLN LYS TYR GLY PRO ILE TYR ARG GLU LYS
SEQRES 5 A 487 LEU GLY ASN VAL GLU SER VAL TYR VAL ILE ASP PRO GLU
SEQRES 6 A 487 ASP VAL ALA LEU LEU PHE LYS SER GLU GLY PRO ASN PRO
SEQRES 7 A 487 GLU ARG PHE LEU ILE PRO PRO TRP VAL ALA TYR HIS GLN
SEQRES 8 A 487 TYR TYR GLN ARG PRO ILE GLY VAL LEU LEU LYS LYS SER
SEQRES 9 A 487 ALA ALA TRP LYS LYS ASP ARG VAL ALA LEU ASN GLN GLU
SEQRES 10 A 487 VAL MET ALA PRO GLU ALA THR LYS ASN PHE LEU PRO LEU
SEQRES 11 A 487 LEU ASP ALA VAL SER ARG ASP PHE VAL SER VAL LEU HIS
SEQRES 12 A 487 ARG ARG ILE LYS LYS ALA GLY SER GLY ASN TYR SER GLY
SEQRES 13 A 487 ASP ILE SER ASP ASP LEU PHE ARG PHE ALA PHE GLU SER
SEQRES 14 A 487 ILE THR ASN VAL ILE PHE GLY GLU ARG GLN GLY MET LEU
SEQRES 15 A 487 GLU GLU VAL VAL ASN PRO GLU ALA GLN ARG PHE ILE ASP
SEQRES 16 A 487 ALA ILE TYR GLN MET PHE HIS THR SER VAL PRO MET LEU
SEQRES 17 A 487 ASN LEU PRO PRO ASP LEU PHE ARG LEU PHE ARG THR LYS
SEQRES 18 A 487 THR TRP LYS ASP HIS VAL ALA ALA TRP ASP VAL ILE PHE
SEQRES 19 A 487 SER LYS ALA ASP ILE TYR THR GLN ASN PHE TYR TRP GLU
SEQRES 20 A 487 LEU ARG GLN LYS GLY SER VAL HIS HIS ASP TYR ARG GLY
SEQRES 21 A 487 ILE LEU TYR ARG LEU LEU GLY ASP SER LYS MET SER PHE
SEQRES 22 A 487 GLU ASP ILE LYS ALA ASN VAL THR GLU MET LEU ALA GLY
SEQRES 23 A 487 GLY VAL ASP THR THR SER MET THR LEU GLN TRP HIS LEU
SEQRES 24 A 487 TYR GLU MET ALA ARG ASN LEU LYS VAL GLN ASP MET LEU
SEQRES 25 A 487 ARG ALA GLU VAL LEU ALA ALA ARG HIS GLN ALA GLN GLY
SEQRES 26 A 487 ASP MET ALA THR MET LEU GLN LEU VAL PRO LEU LEU LYS
SEQRES 27 A 487 ALA SER ILE LYS GLU THR LEU ARG LEU HIS PRO ILE SER
SEQRES 28 A 487 VAL THR LEU GLN ARG TYR LEU VAL ASN ASP LEU VAL LEU
SEQRES 29 A 487 ARG ASP TYR MET ILE PRO ALA LYS THR LEU VAL GLN VAL
SEQRES 30 A 487 ALA ILE TYR ALA LEU GLY ARG GLU PRO THR PHE PHE PHE
SEQRES 31 A 487 ASP PRO GLU ASN PHE ASP PRO THR ARG TRP LEU SER LYS
SEQRES 32 A 487 ASP LYS ASN ILE THR TYR PHE ARG ASN LEU GLY PHE GLY
SEQRES 33 A 487 TRP GLY VAL ARG GLN CYS LEU GLY ARG ARG ILE ALA GLU
SEQRES 34 A 487 LEU GLU MET THR ILE PHE LEU ILE ASN MET LEU GLU ASN
SEQRES 35 A 487 PHE ARG VAL GLU ILE GLN HIS LEU SER ASP VAL GLY THR
SEQRES 36 A 487 THR PHE ASN LEU ILE LEU MET PRO GLU LYS PRO ILE SER
SEQRES 37 A 487 PHE THR PHE TRP PRO PHE ASN GLN GLU ALA THR GLN GLN
SEQRES 38 A 487 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 487 SER THR ARG SER PRO ARG PRO PHE ASN GLU ILE PRO SER
SEQRES 2 B 487 PRO GLY ASP ASN GLY TRP LEU ASN LEU TYR HIS PHE TRP
SEQRES 3 B 487 ARG GLU THR GLY THR HIS LYS VAL HIS LEU HIS HIS VAL
SEQRES 4 B 487 GLN ASN PHE GLN LYS TYR GLY PRO ILE TYR ARG GLU LYS
SEQRES 5 B 487 LEU GLY ASN VAL GLU SER VAL TYR VAL ILE ASP PRO GLU
SEQRES 6 B 487 ASP VAL ALA LEU LEU PHE LYS SER GLU GLY PRO ASN PRO
SEQRES 7 B 487 GLU ARG PHE LEU ILE PRO PRO TRP VAL ALA TYR HIS GLN
SEQRES 8 B 487 TYR TYR GLN ARG PRO ILE GLY VAL LEU LEU LYS LYS SER
SEQRES 9 B 487 ALA ALA TRP LYS LYS ASP ARG VAL ALA LEU ASN GLN GLU
SEQRES 10 B 487 VAL MET ALA PRO GLU ALA THR LYS ASN PHE LEU PRO LEU
SEQRES 11 B 487 LEU ASP ALA VAL SER ARG ASP PHE VAL SER VAL LEU HIS
SEQRES 12 B 487 ARG ARG ILE LYS LYS ALA GLY SER GLY ASN TYR SER GLY
SEQRES 13 B 487 ASP ILE SER ASP ASP LEU PHE ARG PHE ALA PHE GLU SER
SEQRES 14 B 487 ILE THR ASN VAL ILE PHE GLY GLU ARG GLN GLY MET LEU
SEQRES 15 B 487 GLU GLU VAL VAL ASN PRO GLU ALA GLN ARG PHE ILE ASP
SEQRES 16 B 487 ALA ILE TYR GLN MET PHE HIS THR SER VAL PRO MET LEU
SEQRES 17 B 487 ASN LEU PRO PRO ASP LEU PHE ARG LEU PHE ARG THR LYS
SEQRES 18 B 487 THR TRP LYS ASP HIS VAL ALA ALA TRP ASP VAL ILE PHE
SEQRES 19 B 487 SER LYS ALA ASP ILE TYR THR GLN ASN PHE TYR TRP GLU
SEQRES 20 B 487 LEU ARG GLN LYS GLY SER VAL HIS HIS ASP TYR ARG GLY
SEQRES 21 B 487 ILE LEU TYR ARG LEU LEU GLY ASP SER LYS MET SER PHE
SEQRES 22 B 487 GLU ASP ILE LYS ALA ASN VAL THR GLU MET LEU ALA GLY
SEQRES 23 B 487 GLY VAL ASP THR THR SER MET THR LEU GLN TRP HIS LEU
SEQRES 24 B 487 TYR GLU MET ALA ARG ASN LEU LYS VAL GLN ASP MET LEU
SEQRES 25 B 487 ARG ALA GLU VAL LEU ALA ALA ARG HIS GLN ALA GLN GLY
SEQRES 26 B 487 ASP MET ALA THR MET LEU GLN LEU VAL PRO LEU LEU LYS
SEQRES 27 B 487 ALA SER ILE LYS GLU THR LEU ARG LEU HIS PRO ILE SER
SEQRES 28 B 487 VAL THR LEU GLN ARG TYR LEU VAL ASN ASP LEU VAL LEU
SEQRES 29 B 487 ARG ASP TYR MET ILE PRO ALA LYS THR LEU VAL GLN VAL
SEQRES 30 B 487 ALA ILE TYR ALA LEU GLY ARG GLU PRO THR PHE PHE PHE
SEQRES 31 B 487 ASP PRO GLU ASN PHE ASP PRO THR ARG TRP LEU SER LYS
SEQRES 32 B 487 ASP LYS ASN ILE THR TYR PHE ARG ASN LEU GLY PHE GLY
SEQRES 33 B 487 TRP GLY VAL ARG GLN CYS LEU GLY ARG ARG ILE ALA GLU
SEQRES 34 B 487 LEU GLU MET THR ILE PHE LEU ILE ASN MET LEU GLU ASN
SEQRES 35 B 487 PHE ARG VAL GLU ILE GLN HIS LEU SER ASP VAL GLY THR
SEQRES 36 B 487 THR PHE ASN LEU ILE LEU MET PRO GLU LYS PRO ILE SER
SEQRES 37 B 487 PHE THR PHE TRP PRO PHE ASN GLN GLU ALA THR GLN GLN
SEQRES 38 B 487 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 114 SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE ASN ARG
SEQRES 2 C 114 ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL GLY ASP
SEQRES 3 C 114 SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU ASP ILE
SEQRES 4 C 114 ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA CYS SER
SEQRES 5 C 114 THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR GLU LYS
SEQRES 6 C 114 LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET LEU ASP
SEQRES 7 C 114 LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU GLY CYS
SEQRES 8 C 114 GLN ILE CYS LEU THR LYS SER MET ASP ASN MET THR VAL
SEQRES 9 C 114 ARG VAL PRO GLU THR VAL ALA ASP ALA ARG
SEQRES 1 D 114 SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE ASN ARG
SEQRES 2 D 114 ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL GLY ASP
SEQRES 3 D 114 SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU ASP ILE
SEQRES 4 D 114 ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA CYS SER
SEQRES 5 D 114 THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR GLU LYS
SEQRES 6 D 114 LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET LEU ASP
SEQRES 7 D 114 LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU GLY CYS
SEQRES 8 D 114 GLN ILE CYS LEU THR LYS SER MET ASP ASN MET THR VAL
SEQRES 9 D 114 ARG VAL PRO GLU THR VAL ALA ASP ALA ARG
HET HEM A 601 43
HET CLR A 602 28
HET HEM B 601 43
HET CLR B 602 28
HET FES C 150 4
HET FES D 151 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CLR CHOLESTEROL
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETSYN HEM HEME
FORMUL 5 HEM 2(C34 H32 FE N4 O4)
FORMUL 6 CLR 2(C27 H46 O)
FORMUL 9 FES 2(FE2 S2)
FORMUL 11 HOH *505(H2 O)
HELIX 1 1 PRO A 8 ILE A 12 5 5
HELIX 2 2 ASN A 18 THR A 30 1 13
HELIX 3 3 GLY A 31 HIS A 33 5 3
HELIX 4 4 LYS A 34 GLY A 47 1 14
HELIX 5 5 ASP A 64 SER A 74 1 11
HELIX 6 6 ILE A 84 TYR A 94 1 11
HELIX 7 7 GLY A 99 LYS A 103 5 5
HELIX 8 8 LYS A 104 MET A 120 1 17
HELIX 9 9 ALA A 121 LYS A 126 1 6
HELIX 10 10 ASN A 127 GLY A 151 1 25
HELIX 11 11 ILE A 159 GLY A 177 1 19
HELIX 12 12 ASN A 188 VAL A 206 1 19
HELIX 13 13 PRO A 207 LEU A 209 5 3
HELIX 14 14 PRO A 212 ARG A 220 1 9
HELIX 15 15 ARG A 220 GLY A 253 1 34
HELIX 16 16 GLY A 261 ASP A 269 1 9
HELIX 17 17 SER A 273 ASP A 290 1 18
HELIX 18 18 ASP A 290 ASN A 306 1 17
HELIX 19 19 ASN A 306 ALA A 324 1 19
HELIX 20 20 ASP A 327 LEU A 332 1 6
HELIX 21 21 VAL A 335 HIS A 349 1 15
HELIX 22 22 ILE A 380 ARG A 385 1 6
HELIX 23 23 ASP A 397 LEU A 402 5 6
HELIX 24 24 TRP A 418 GLN A 422 5 5
HELIX 25 25 GLY A 425 ASN A 443 1 19
HELIX 26 26 PRO B 8 ILE B 12 5 5
HELIX 27 27 ASN B 18 THR B 30 1 13
HELIX 28 28 GLY B 31 HIS B 33 5 3
HELIX 29 29 LYS B 34 GLY B 47 1 14
HELIX 30 30 ASP B 64 SER B 74 1 11
HELIX 31 31 ILE B 84 TYR B 94 1 11
HELIX 32 32 GLY B 99 LYS B 103 5 5
HELIX 33 33 LYS B 104 MET B 120 1 17
HELIX 34 34 ALA B 121 LYS B 126 1 6
HELIX 35 35 ASN B 127 GLY B 151 1 25
HELIX 36 36 ILE B 159 GLY B 177 1 19
HELIX 37 37 ASN B 188 VAL B 206 1 19
HELIX 38 38 PRO B 207 LEU B 209 5 3
HELIX 39 39 PRO B 212 ARG B 220 1 9
HELIX 40 40 ARG B 220 GLY B 253 1 34
HELIX 41 41 GLY B 261 ASP B 269 1 9
HELIX 42 42 SER B 273 ASN B 306 1 34
HELIX 43 43 ASN B 306 ALA B 324 1 19
HELIX 44 44 ASP B 327 LEU B 332 1 6
HELIX 45 45 VAL B 335 HIS B 349 1 15
HELIX 46 46 ALA B 379 ARG B 385 1 7
HELIX 47 47 ASP B 397 SER B 403 5 7
HELIX 48 48 TRP B 418 GLN B 422 5 5
HELIX 49 49 GLY B 425 ASN B 443 1 19
HELIX 50 50 SER C 28 ASN C 37 1 10
HELIX 51 51 GLU C 60 GLU C 65 1 6
HELIX 52 52 THR C 71 LEU C 80 1 10
HELIX 53 53 CYS C 92 ILE C 94 5 3
HELIX 54 54 SER D 28 ASN D 37 1 10
HELIX 55 55 ASP D 61 LYS D 66 1 6
HELIX 56 56 THR D 71 LEU D 80 1 10
HELIX 57 57 CYS D 92 ILE D 94 5 3
SHEET 1 A 4 ILE A 49 LEU A 54 0
SHEET 2 A 4 VAL A 57 VAL A 62 -1 O TYR A 61 N TYR A 50
SHEET 3 A 4 LEU A 375 ALA A 379 1 O GLN A 377 N VAL A 60
SHEET 4 A 4 THR A 354 TYR A 358 -1 N LEU A 355 O VAL A 378
SHEET 1 B 3 TYR A 155 GLY A 157 0
SHEET 2 B 3 PHE A 470 PRO A 474 -1 O PHE A 472 N TYR A 155
SHEET 3 B 3 PHE A 444 GLU A 447 -1 N GLU A 447 O THR A 471
SHEET 1 C 2 LEU A 363 LEU A 365 0
SHEET 2 C 2 TYR A 368 ILE A 370 -1 O ILE A 370 N LEU A 363
SHEET 1 D 2 THR A 456 PHE A 458 0
SHEET 2 D 2 LEU A 462 PRO A 464 -1 O MET A 463 N THR A 457
SHEET 1 E 4 ILE B 49 LEU B 54 0
SHEET 2 E 4 VAL B 57 VAL B 62 -1 O TYR B 61 N TYR B 50
SHEET 3 E 4 LEU B 375 VAL B 378 1 O GLN B 377 N VAL B 60
SHEET 4 E 4 LEU B 355 TYR B 358 -1 N LEU B 355 O VAL B 378
SHEET 1 F 3 TYR B 155 GLY B 157 0
SHEET 2 F 3 PHE B 470 PRO B 474 -1 O PHE B 472 N TYR B 155
SHEET 3 F 3 PHE B 444 ILE B 448 -1 N ARG B 445 O TRP B 473
SHEET 1 G 2 LEU B 363 LEU B 365 0
SHEET 2 G 2 TYR B 368 ILE B 370 -1 O ILE B 370 N LEU B 363
SHEET 1 H 2 THR B 456 PHE B 458 0
SHEET 2 H 2 LEU B 462 PRO B 464 -1 O MET B 463 N THR B 457
SHEET 1 I 2 HIS C 56 ILE C 58 0
SHEET 2 I 2 SER C 88 LEU C 90 -1 O ARG C 89 N LEU C 57
SHEET 1 J 2 HIS D 56 ILE D 58 0
SHEET 2 J 2 SER D 88 LEU D 90 -1 O ARG D 89 N LEU D 57
LINK SG CYS A 423 FE HEM A 601 1555 1555 2.50
LINK SG CYS B 423 FE HEM B 601 1555 1555 2.47
LINK SG CYS C 46 FE1 FES C 150 1555 1555 2.06
LINK SG CYS C 52 FE1 FES C 150 1555 1555 2.44
LINK SG CYS C 55 FE2 FES C 150 1555 1555 2.18
LINK SG CYS C 92 FE2 FES C 150 1555 1555 2.25
LINK SG CYS D 46 FE1 FES D 151 1555 1555 2.01
LINK SG CYS D 52 FE1 FES D 151 1555 1555 2.50
LINK SG CYS D 55 FE2 FES D 151 1555 1555 2.08
LINK SG CYS D 92 FE2 FES D 151 1555 1555 2.38
SITE 1 AC1 21 ARG A 81 VAL A 100 TRP A 108 ARG A 112
SITE 2 AC1 21 MET A 284 GLY A 287 GLY A 288 THR A 291
SITE 3 AC1 21 THR A 295 ILE A 351 SER A 352 ARG A 357
SITE 4 AC1 21 GLY A 415 PHE A 416 GLY A 417 TRP A 418
SITE 5 AC1 21 ARG A 421 GLN A 422 CYS A 423 GLY A 425
SITE 6 AC1 21 HOH A 499
SITE 1 AC2 6 PHE A 82 SER A 352 THR A 354 GLN A 356
SITE 2 AC2 6 HOH A 538 HOH A 573
SITE 1 AC3 23 ARG B 81 VAL B 100 TRP B 108 ARG B 112
SITE 2 AC3 23 MET B 284 GLY B 287 GLY B 288 THR B 291
SITE 3 AC3 23 THR B 295 LEU B 346 ILE B 351 SER B 352
SITE 4 AC3 23 LEU B 355 ARG B 357 GLY B 415 PHE B 416
SITE 5 AC3 23 GLY B 417 TRP B 418 ARG B 421 GLN B 422
SITE 6 AC3 23 CYS B 423 GLY B 425 HOH B 499
SITE 1 AC4 8 PHE B 82 MET B 201 GLU B 283 SER B 352
SITE 2 AC4 8 THR B 354 GLN B 356 HOH B 559 HOH B 590
SITE 1 AC5 6 GLY C 44 CYS C 46 GLY C 48 CYS C 52
SITE 2 AC5 6 CYS C 55 CYS C 92
SITE 1 AC6 8 LEU D 30 GLY D 44 CYS D 46 GLY D 48
SITE 2 AC6 8 LEU D 50 CYS D 52 CYS D 55 CYS D 92
CRYST1 82.999 114.686 86.019 90.00 101.96 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012048 0.000000 0.002552 0.00000
SCALE2 0.000000 0.008719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011883 0.00000
(ATOM LINES ARE NOT SHOWN.)
END