HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-NOV-16 5TZ1
TITLE CRYSTAL STRUCTURE OF STEROL 14-ALPHA DEMETHYLASE (CYP51) FROM CANDIDA
TITLE 2 ALBICANS IN COMPLEX WITH THE TETRAZOLE-BASED ANTIFUNGAL DRUG
TITLE 3 CANDIDATE VT1161 (VT1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROL 14-ALPHA DEMETHYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYP51, CYTOCHROME P-450 LANOSTEROL 14-ALPHA-DEMETHYLASE;
COMPND 5 EC: 1.14.13.70;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ALBICANS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5476;
SOURCE 5 VARIANT: 1;
SOURCE 6 GENE: CYP51, ERG11;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: HMS-174;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS CYP51, CYTOCHROME P450, HEME, OXIDOREDUCTASE, MONOOXYGENASE, STEROL
KEYWDS 2 BIOSYNTHESIS, EUKARYOTIC MEMBRANES, CYTOCHROME P450 FOLD,
KEYWDS 3 ENDOPLASMIC RETICULUM MEMBRANE, OXIDOREDUCTASE-OXIDOREDUCTASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HARGROVE,Z.WAWRZAK,G.LEPESHEVA
REVDAT 5 04-OCT-23 5TZ1 1 LINK
REVDAT 4 22-NOV-17 5TZ1 1 REMARK
REVDAT 3 03-MAY-17 5TZ1 1 JRNL
REVDAT 2 22-MAR-17 5TZ1 1 JRNL
REVDAT 1 15-MAR-17 5TZ1 0
JRNL AUTH T.Y.HARGROVE,L.FRIGGERI,Z.WAWRZAK,A.QI,W.J.HOEKSTRA,
JRNL AUTH 2 R.J.SCHOTZINGER,J.D.YORK,F.P.GUENGERICH,G.I.LEPESHEVA
JRNL TITL STRUCTURAL ANALYSES OF CANDIDA ALBICANS STEROL 14
JRNL TITL 2 ALPHA-DEMETHYLASE COMPLEXED WITH AZOLE DRUGS ADDRESS THE
JRNL TITL 3 MOLECULAR BASIS OF AZOLE-MEDIATED INHIBITION OF FUNGAL
JRNL TITL 4 STEROL BIOSYNTHESIS.
JRNL REF J. BIOL. CHEM. V. 292 6728 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28258218
JRNL DOI 10.1074/JBC.M117.778308
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 62497
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3313
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4476
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 247
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7857
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 316
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.92000
REMARK 3 B22 (A**2) : -2.67000
REMARK 3 B33 (A**2) : -1.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.99000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.117
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8259 ; 0.002 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7669 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11233 ; 0.985 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17687 ; 0.759 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 966 ; 5.286 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 378 ;35.080 ;23.545
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1377 ;15.996 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;16.402 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1178 ; 0.050 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9214 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1976 ; 0.006 ; 0.020
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): 3870 ; 4.677 ; 3.932
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3869 ; 4.672 ; 3.932
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4834 ; 6.872 ; 5.884
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4835 ; 6.872 ; 5.884
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4389 ; 4.809 ; 4.368
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4390 ; 4.808 ; 4.368
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6400 ; 7.017 ; 6.397
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10407 ;13.676 ;49.502
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10349 ;13.639 ;49.400
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5TZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000225027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97849
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65813
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.69100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 5FSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.4, 0.2 M SODIUM
REMARK 280 CHLORIDE, 10% PEG6000, 0.03 MM N-TRIDECYL-B-D-MALTOSIDE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.82000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.82000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.72000
REMARK 290 SMTRY3 4 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: 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 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 43
REMARK 465 ALA A 44
REMARK 465 HIS A 529
REMARK 465 HIS A 530
REMARK 465 HIS A 531
REMARK 465 HIS A 532
REMARK 465 MET B 43
REMARK 465 ALA B 44
REMARK 465 HIS B 529
REMARK 465 HIS B 530
REMARK 465 HIS B 531
REMARK 465 HIS B 532
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 436 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CD2 LEU A 263 NH2 ARG A 267 1.66
REMARK 500 NH1 ARG A 265 O HOH A 701 1.96
REMARK 500 O HOH B 810 O HOH B 842 2.07
REMARK 500 O ILE A 389 OG1 THR A 392 2.12
REMARK 500 O HOH A 827 O HOH A 829 2.16
REMARK 500 O PHE B 205 O HOH B 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 859 O HOH B 859 2656 2.06
REMARK 500 O HOH A 829 O HOH B 770 1564 2.11
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 TRP B 54 N - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 PRO B 56 C - N - CA ANGL. DEV. = 10.6 DEGREES
REMARK 500 PRO B 56 C - N - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU B 88 CA - CB - CG ANGL. DEV. = 22.6 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 131 -122.91 60.06
REMARK 500 ASP A 269 77.62 -165.69
REMARK 500 TYR B 53 73.28 -164.59
REMARK 500 PRO B 56 132.47 -35.82
REMARK 500 TRP B 57 4.11 57.88
REMARK 500 LEU B 88 -128.96 57.63
REMARK 500 ILE B 131 -123.84 57.63
REMARK 500 SER B 216 14.03 57.58
REMARK 500 PRO B 239 17.17 -69.15
REMARK 500 ASP B 275 -169.45 -161.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE B 233 0.06 SIDE CHAIN
REMARK 500 PHE B 319 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU B 150 19.25
REMARK 500 ASP B 347 10.71
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 470 SG
REMARK 620 2 HEM A 601 NA 94.1
REMARK 620 3 HEM A 601 NB 83.2 87.9
REMARK 620 4 HEM A 601 NC 84.4 175.2 87.3
REMARK 620 5 HEM A 601 ND 92.9 91.5 176.0 93.2
REMARK 620 6 VT1 A 602 NAF 172.8 89.5 90.7 91.5 93.2
REMARK 620 N 1 2 3 4 5
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 470 SG
REMARK 620 2 HEM B 601 NA 92.3
REMARK 620 3 HEM B 601 NB 83.3 86.9
REMARK 620 4 HEM B 601 NC 84.7 174.2 87.9
REMARK 620 5 HEM B 601 ND 92.9 92.2 176.1 92.9
REMARK 620 6 VT1 B 602 NAF 172.6 90.7 90.1 91.7 93.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VT1 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 VT1 B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FSA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STEROL 14-ALPHA DEMETHYLASE (CYP51) FROM
REMARK 900 CANDIDA ALBICANS IN COMPLEX WITH POSACONAZOLE
DBREF 5TZ1 A 48 528 UNP Q9P4W0 Q9P4W0_CANAX 48 528
DBREF 5TZ1 B 48 528 UNP Q9P4W0 Q9P4W0_CANAX 48 528
SEQADV 5TZ1 MET A 43 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 ALA A 44 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 LYS A 45 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 LYS A 46 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 THR A 47 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 PRO A 48 UNP Q9P4W0 ALA 48 ENGINEERED MUTATION
SEQADV 5TZ1 LEU A 263 UNP Q9P4W0 SER 263 ENGINEERED MUTATION
SEQADV 5TZ1 HIS A 529 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS A 530 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS A 531 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS A 532 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 MET B 43 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 ALA B 44 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 LYS B 45 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 LYS B 46 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 THR B 47 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 PRO B 48 UNP Q9P4W0 ALA 48 ENGINEERED MUTATION
SEQADV 5TZ1 LEU B 263 UNP Q9P4W0 SER 263 ENGINEERED MUTATION
SEQADV 5TZ1 HIS B 529 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS B 530 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS B 531 UNP Q9P4W0 EXPRESSION TAG
SEQADV 5TZ1 HIS B 532 UNP Q9P4W0 EXPRESSION TAG
SEQRES 1 A 490 MET ALA LYS LYS THR PRO PRO LEU VAL PHE TYR TRP ILE
SEQRES 2 A 490 PRO TRP PHE GLY SER ALA ALA SER TYR GLY GLN GLN PRO
SEQRES 3 A 490 TYR GLU PHE PHE GLU SER CYS ARG GLN LYS TYR GLY ASP
SEQRES 4 A 490 VAL PHE SER PHE MET LEU LEU GLY LYS ILE MET THR VAL
SEQRES 5 A 490 TYR LEU GLY PRO LYS GLY HIS GLU PHE VAL PHE ASN ALA
SEQRES 6 A 490 LYS LEU SER ASP VAL SER ALA GLU GLU ALA TYR LYS HIS
SEQRES 7 A 490 LEU THR THR PRO VAL PHE GLY THR GLY VAL ILE TYR ASP
SEQRES 8 A 490 CYS PRO ASN SER ARG LEU MET GLU GLN LYS LYS PHE ALA
SEQRES 9 A 490 LYS PHE ALA LEU THR THR ASP SER PHE LYS ARG TYR VAL
SEQRES 10 A 490 PRO LYS ILE ARG GLU GLU ILE LEU ASN TYR PHE VAL THR
SEQRES 11 A 490 ASP GLU SER PHE LYS LEU LYS GLU LYS THR HIS GLY VAL
SEQRES 12 A 490 ALA ASN VAL MET LYS THR GLN PRO GLU ILE THR ILE PHE
SEQRES 13 A 490 THR ALA SER ARG SER LEU PHE GLY ASP GLU MET ARG ARG
SEQRES 14 A 490 ILE PHE ASP ARG SER PHE ALA GLN LEU TYR SER ASP LEU
SEQRES 15 A 490 ASP LYS GLY PHE THR PRO ILE ASN PHE VAL PHE PRO ASN
SEQRES 16 A 490 LEU PRO LEU PRO HIS TYR TRP ARG ARG ASP ALA ALA GLN
SEQRES 17 A 490 LYS LYS ILE SER ALA THR TYR MET LYS GLU ILE LYS LEU
SEQRES 18 A 490 ARG ARG GLU ARG GLY ASP ILE ASP PRO ASN ARG ASP LEU
SEQRES 19 A 490 ILE ASP SER LEU LEU ILE HIS SER THR TYR LYS ASP GLY
SEQRES 20 A 490 VAL LYS MET THR ASP GLN GLU ILE ALA ASN LEU LEU ILE
SEQRES 21 A 490 GLY ILE LEU MET GLY GLY GLN HIS THR SER ALA SER THR
SEQRES 22 A 490 SER ALA TRP PHE LEU LEU HIS LEU GLY GLU LYS PRO HIS
SEQRES 23 A 490 LEU GLN ASP VAL ILE TYR GLN GLU VAL VAL GLU LEU LEU
SEQRES 24 A 490 LYS GLU LYS GLY GLY ASP LEU ASN ASP LEU THR TYR GLU
SEQRES 25 A 490 ASP LEU GLN LYS LEU PRO SER VAL ASN ASN THR ILE LYS
SEQRES 26 A 490 GLU THR LEU ARG MET HIS MET PRO LEU HIS SER ILE PHE
SEQRES 27 A 490 ARG LYS VAL THR ASN PRO LEU ARG ILE PRO GLU THR ASN
SEQRES 28 A 490 TYR ILE VAL PRO LYS GLY HIS TYR VAL LEU VAL SER PRO
SEQRES 29 A 490 GLY TYR ALA HIS THR SER GLU ARG TYR PHE ASP ASN PRO
SEQRES 30 A 490 GLU ASP PHE ASP PRO THR ARG TRP ASP THR ALA ALA ALA
SEQRES 31 A 490 LYS ALA ASN SER VAL SER PHE ASN SER SER ASP GLU VAL
SEQRES 32 A 490 ASP TYR GLY PHE GLY LYS VAL SER LYS GLY VAL SER SER
SEQRES 33 A 490 PRO TYR LEU PRO PHE GLY GLY GLY ARG HIS ARG CYS ILE
SEQRES 34 A 490 GLY GLU GLN PHE ALA TYR VAL GLN LEU GLY THR ILE LEU
SEQRES 35 A 490 THR THR PHE VAL TYR ASN LEU ARG TRP THR ILE ASP GLY
SEQRES 36 A 490 TYR LYS VAL PRO ASP PRO ASP TYR SER SER MET VAL VAL
SEQRES 37 A 490 LEU PRO THR GLU PRO ALA GLU ILE ILE TRP GLU LYS ARG
SEQRES 38 A 490 GLU THR CYS MET PHE HIS HIS HIS HIS
SEQRES 1 B 490 MET ALA LYS LYS THR PRO PRO LEU VAL PHE TYR TRP ILE
SEQRES 2 B 490 PRO TRP PHE GLY SER ALA ALA SER TYR GLY GLN GLN PRO
SEQRES 3 B 490 TYR GLU PHE PHE GLU SER CYS ARG GLN LYS TYR GLY ASP
SEQRES 4 B 490 VAL PHE SER PHE MET LEU LEU GLY LYS ILE MET THR VAL
SEQRES 5 B 490 TYR LEU GLY PRO LYS GLY HIS GLU PHE VAL PHE ASN ALA
SEQRES 6 B 490 LYS LEU SER ASP VAL SER ALA GLU GLU ALA TYR LYS HIS
SEQRES 7 B 490 LEU THR THR PRO VAL PHE GLY THR GLY VAL ILE TYR ASP
SEQRES 8 B 490 CYS PRO ASN SER ARG LEU MET GLU GLN LYS LYS PHE ALA
SEQRES 9 B 490 LYS PHE ALA LEU THR THR ASP SER PHE LYS ARG TYR VAL
SEQRES 10 B 490 PRO LYS ILE ARG GLU GLU ILE LEU ASN TYR PHE VAL THR
SEQRES 11 B 490 ASP GLU SER PHE LYS LEU LYS GLU LYS THR HIS GLY VAL
SEQRES 12 B 490 ALA ASN VAL MET LYS THR GLN PRO GLU ILE THR ILE PHE
SEQRES 13 B 490 THR ALA SER ARG SER LEU PHE GLY ASP GLU MET ARG ARG
SEQRES 14 B 490 ILE PHE ASP ARG SER PHE ALA GLN LEU TYR SER ASP LEU
SEQRES 15 B 490 ASP LYS GLY PHE THR PRO ILE ASN PHE VAL PHE PRO ASN
SEQRES 16 B 490 LEU PRO LEU PRO HIS TYR TRP ARG ARG ASP ALA ALA GLN
SEQRES 17 B 490 LYS LYS ILE SER ALA THR TYR MET LYS GLU ILE LYS LEU
SEQRES 18 B 490 ARG ARG GLU ARG GLY ASP ILE ASP PRO ASN ARG ASP LEU
SEQRES 19 B 490 ILE ASP SER LEU LEU ILE HIS SER THR TYR LYS ASP GLY
SEQRES 20 B 490 VAL LYS MET THR ASP GLN GLU ILE ALA ASN LEU LEU ILE
SEQRES 21 B 490 GLY ILE LEU MET GLY GLY GLN HIS THR SER ALA SER THR
SEQRES 22 B 490 SER ALA TRP PHE LEU LEU HIS LEU GLY GLU LYS PRO HIS
SEQRES 23 B 490 LEU GLN ASP VAL ILE TYR GLN GLU VAL VAL GLU LEU LEU
SEQRES 24 B 490 LYS GLU LYS GLY GLY ASP LEU ASN ASP LEU THR TYR GLU
SEQRES 25 B 490 ASP LEU GLN LYS LEU PRO SER VAL ASN ASN THR ILE LYS
SEQRES 26 B 490 GLU THR LEU ARG MET HIS MET PRO LEU HIS SER ILE PHE
SEQRES 27 B 490 ARG LYS VAL THR ASN PRO LEU ARG ILE PRO GLU THR ASN
SEQRES 28 B 490 TYR ILE VAL PRO LYS GLY HIS TYR VAL LEU VAL SER PRO
SEQRES 29 B 490 GLY TYR ALA HIS THR SER GLU ARG TYR PHE ASP ASN PRO
SEQRES 30 B 490 GLU ASP PHE ASP PRO THR ARG TRP ASP THR ALA ALA ALA
SEQRES 31 B 490 LYS ALA ASN SER VAL SER PHE ASN SER SER ASP GLU VAL
SEQRES 32 B 490 ASP TYR GLY PHE GLY LYS VAL SER LYS GLY VAL SER SER
SEQRES 33 B 490 PRO TYR LEU PRO PHE GLY GLY GLY ARG HIS ARG CYS ILE
SEQRES 34 B 490 GLY GLU GLN PHE ALA TYR VAL GLN LEU GLY THR ILE LEU
SEQRES 35 B 490 THR THR PHE VAL TYR ASN LEU ARG TRP THR ILE ASP GLY
SEQRES 36 B 490 TYR LYS VAL PRO ASP PRO ASP TYR SER SER MET VAL VAL
SEQRES 37 B 490 LEU PRO THR GLU PRO ALA GLU ILE ILE TRP GLU LYS ARG
SEQRES 38 B 490 GLU THR CYS MET PHE HIS HIS HIS HIS
HET HEM A 601 43
HET VT1 A 602 37
HET HEM B 601 43
HET VT1 B 602 37
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM VT1 (R)-2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-3-(1H-TETRAZOL-
HETNAM 2 VT1 1-YL)-1-(5-(4-(2,2,2-TRIFLUOROETHOXY)PHENYL)PYRIDIN-2-
HETNAM 3 VT1 YL)PROPAN-2-OL
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 VT1 2(C23 H16 F7 N5 O2)
FORMUL 7 HOH *316(H2 O)
HELIX 1 AA1 SER A 60 GLN A 67 1 8
HELIX 2 AA2 GLN A 67 GLY A 80 1 14
HELIX 3 AA3 GLY A 97 ASN A 106 1 10
HELIX 4 AA4 ALA A 114 GLY A 127 1 14
HELIX 5 AA5 PRO A 135 PHE A 148 1 14
HELIX 6 AA6 THR A 151 ASP A 173 1 23
HELIX 7 AA7 VAL A 188 GLY A 206 1 19
HELIX 8 AA8 GLY A 206 PHE A 213 1 8
HELIX 9 AA9 ASP A 214 LYS A 226 1 13
HELIX 10 AB1 GLY A 227 THR A 229 5 3
HELIX 11 AB2 PRO A 230 PHE A 235 1 6
HELIX 12 AB3 LEU A 240 ARG A 267 1 28
HELIX 13 AB4 ASP A 275 HIS A 283 1 9
HELIX 14 AB5 THR A 293 LYS A 326 1 34
HELIX 15 AB6 LYS A 326 GLY A 345 1 20
HELIX 16 AB7 ASP A 347 LEU A 351 5 5
HELIX 17 AB8 THR A 352 GLN A 357 1 6
HELIX 18 AB9 LEU A 359 HIS A 373 1 15
HELIX 19 AC1 SER A 405 THR A 411 1 7
HELIX 20 AC2 ASP A 423 ASP A 428 5 6
HELIX 21 AC3 THR A 429 ASN A 435 1 7
HELIX 22 AC4 GLY A 465 ARG A 469 5 5
HELIX 23 AC5 GLY A 472 ASN A 490 1 19
HELIX 24 AC6 SER B 60 GLY B 65 1 6
HELIX 25 AC7 GLN B 67 GLY B 80 1 14
HELIX 26 AC8 LEU B 96 ASN B 106 1 11
HELIX 27 AC9 ALA B 114 GLY B 127 1 14
HELIX 28 AD1 VAL B 130 CYS B 134 5 5
HELIX 29 AD2 PRO B 135 PHE B 148 1 14
HELIX 30 AD3 THR B 151 ASP B 173 1 23
HELIX 31 AD4 VAL B 188 GLY B 206 1 19
HELIX 32 AD5 GLY B 206 ILE B 212 1 7
HELIX 33 AD6 SER B 216 GLY B 227 1 12
HELIX 34 AD7 PHE B 228 VAL B 234 5 7
HELIX 35 AD8 LEU B 240 GLU B 266 1 27
HELIX 36 AD9 ASP B 275 HIS B 283 1 9
HELIX 37 AE1 THR B 293 LYS B 326 1 34
HELIX 38 AE2 LYS B 326 GLY B 345 1 20
HELIX 39 AE3 ASP B 347 LEU B 351 5 5
HELIX 40 AE4 THR B 352 GLN B 357 1 6
HELIX 41 AE5 LEU B 359 HIS B 373 1 15
HELIX 42 AE6 SER B 405 THR B 411 1 7
HELIX 43 AE7 ASP B 423 ASP B 428 5 6
HELIX 44 AE8 THR B 429 SER B 436 1 8
HELIX 45 AE9 GLY B 465 ARG B 469 5 5
HELIX 46 AF1 GLY B 472 ASN B 490 1 19
SHEET 1 AA1 5 VAL A 82 LEU A 87 0
SHEET 2 AA1 5 LYS A 90 TYR A 95 -1 O VAL A 94 N PHE A 83
SHEET 3 AA1 5 TYR A 401 VAL A 404 1 O TYR A 401 N THR A 93
SHEET 4 AA1 5 ILE A 379 VAL A 383 -1 N ILE A 379 O VAL A 404
SHEET 5 AA1 5 VAL A 112 SER A 113 -1 N SER A 113 O LYS A 382
SHEET 1 AA2 3 HIS A 183 ASN A 187 0
SHEET 2 AA2 3 GLU A 517 LYS A 522 -1 O ILE A 518 N ALA A 186
SHEET 3 AA2 3 LEU A 491 THR A 494 -1 N ARG A 492 O GLU A 521
SHEET 1 AA3 2 LEU A 387 ARG A 388 0
SHEET 2 AA3 2 ILE A 395 VAL A 396 -1 O VAL A 396 N LEU A 387
SHEET 1 AA4 2 GLU A 444 ASP A 446 0
SHEET 2 AA4 2 LYS A 451 SER A 453 -1 O VAL A 452 N VAL A 445
SHEET 1 AA5 2 PRO A 503 ASP A 504 0
SHEET 2 AA5 2 LEU A 511 PRO A 512 -1 O LEU A 511 N ASP A 504
SHEET 1 AA6 6 LEU B 50 PHE B 52 0
SHEET 2 AA6 6 VAL B 82 LEU B 87 1 O MET B 86 N PHE B 52
SHEET 3 AA6 6 LYS B 90 TYR B 95 -1 O LYS B 90 N LEU B 87
SHEET 4 AA6 6 TYR B 401 VAL B 404 1 O TYR B 401 N THR B 93
SHEET 5 AA6 6 ILE B 379 VAL B 383 -1 N ILE B 379 O VAL B 404
SHEET 6 AA6 6 VAL B 112 SER B 113 -1 N SER B 113 O LYS B 382
SHEET 1 AA7 3 HIS B 183 ASN B 187 0
SHEET 2 AA7 3 GLU B 517 LYS B 522 -1 O ILE B 518 N ALA B 186
SHEET 3 AA7 3 LEU B 491 THR B 494 -1 N ARG B 492 O GLU B 521
SHEET 1 AA8 2 LEU B 387 ARG B 388 0
SHEET 2 AA8 2 ILE B 395 VAL B 396 -1 O VAL B 396 N LEU B 387
SHEET 1 AA9 2 GLU B 444 ASP B 446 0
SHEET 2 AA9 2 LYS B 451 SER B 453 -1 O VAL B 452 N VAL B 445
SHEET 1 AB1 2 PRO B 503 ASP B 504 0
SHEET 2 AB1 2 LEU B 511 PRO B 512 -1 O LEU B 511 N ASP B 504
LINK SG CYS A 470 FE HEM A 601 1555 1555 2.35
LINK FE HEM A 601 NAF VT1 A 602 1555 1555 2.25
LINK SG CYS B 470 FE HEM B 601 1555 1555 2.39
LINK FE HEM B 601 NAF VT1 B 602 1555 1555 2.20
SITE 1 AC1 21 TYR A 118 TYR A 132 LEU A 139 LYS A 143
SITE 2 AC1 21 ILE A 304 GLY A 308 THR A 311 THR A 315
SITE 3 AC1 21 MET A 374 PRO A 375 ILE A 379 ARG A 381
SITE 4 AC1 21 PRO A 462 PHE A 463 GLY A 464 HIS A 468
SITE 5 AC1 21 CYS A 470 ILE A 471 GLY A 472 VT1 A 602
SITE 6 AC1 21 HOH A 738
SITE 1 AC2 14 TYR A 64 PHE A 126 TYR A 132 PHE A 228
SITE 2 AC2 14 GLY A 303 GLY A 307 THR A 311 LEU A 376
SITE 3 AC2 14 HIS A 377 SER A 378 PHE A 380 MET A 508
SITE 4 AC2 14 HEM A 601 HOH A 738
SITE 1 AC3 19 TYR B 118 TYR B 132 LEU B 139 LYS B 143
SITE 2 AC3 19 GLY B 308 THR B 311 ILE B 379 ARG B 381
SITE 3 AC3 19 PRO B 462 PHE B 463 GLY B 464 HIS B 468
SITE 4 AC3 19 CYS B 470 ILE B 471 GLY B 472 ALA B 476
SITE 5 AC3 19 VT1 B 602 HOH B 761 HOH B 767
SITE 1 AC4 15 TYR B 64 TYR B 118 ILE B 131 TYR B 132
SITE 2 AC4 15 PHE B 228 PRO B 230 GLY B 303 GLY B 307
SITE 3 AC4 15 THR B 311 HIS B 377 SER B 378 PHE B 380
SITE 4 AC4 15 MET B 508 HEM B 601 HOH B 761
CRYST1 177.640 71.440 79.190 90.00 96.63 90.00 C 1 2 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 0.005629 0.000000 0.000654 0.00000
SCALE2 0.000000 0.013998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012713 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
