HEADER OXIDOREDUCTASE 16-AUG-13 4C28
TITLE CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI CYP51 BOUND TO THE INHIBITOR
TITLE 2 (R)-N-(3-(1H-INDOL-3-YL)-1-OXO-1-(PYRIDIN-4-YLAMINO)PROPAN-2-YL)-4-
TITLE 3 (4-(4-CHLOROPHENYL)PIPERAZIN-1-YL)-2-FLUOROBENZAMIDE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROL 14-ALPHA DEMETHYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 29-481;
COMPND 5 SYNONYM: TC14DM, CYTOCHROME P450 51, LANOSTEROL 14-ALPHA DEMETHYLASE,
COMPND 6 CYP51;
COMPND 7 EC: 1.14.13.70;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: 32 N-TERMINUS RESIDUES ARE REPLACED WITH THE SEQUENCE
COMPND 10 MAKKTSSKGKL 6XHIS TAG ENGINEERED AT THE C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: HMS174(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS OXIDOREDUCTASE, STEROL BIOSYNTHESIS, CHAGAS DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.F.VIEIRA,C.M.CALVET,J.Y.CHOI,M.D.CAMERON,J.GUT,D.KELLAR,
AUTHOR 2 J.L.SIQUEIRA-NETO,J.H.MCKERROW,W.R.ROUSH,L.M.PODUST
REVDAT 4 20-DEC-23 4C28 1 REMARK
REVDAT 3 14-JAN-15 4C28 1 JRNL
REVDAT 2 26-NOV-14 4C28 1 JRNL
REVDAT 1 03-SEP-14 4C28 0
JRNL AUTH D.F.VIEIRA,J.Y.CHOI,C.M.CALVET,J.L.SIQUEIRA-NETO,
JRNL AUTH 2 J.B.JOHNSTON,D.KELLAR,J.GUT,M.D.CAMERON,J.H.MCKERROW,
JRNL AUTH 3 W.R.ROUSH,L.M.PODUST
JRNL TITL BINDING MODE AND POTENCY OF
JRNL TITL 2 N-INDOLYL-OXOPYRIDINYL-4-AMINO-PROPANYL-BASED INHIBITORS
JRNL TITL 3 TARGETING TRYPANOSOMA CRUZI CYP51
JRNL REF J.MED.CHEM. V. 57 10162 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25393646
JRNL DOI 10.1021/JM501568B
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.4
REMARK 3 NUMBER OF REFLECTIONS : 54178
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2904
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 40.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7033
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 177
REMARK 3 SOLVENT ATOMS : 410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 1.31000
REMARK 3 B33 (A**2) : -1.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.233
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.195
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.473
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7529 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7195 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10225 ; 1.911 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16530 ; 0.906 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 886 ; 6.371 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 329 ;36.689 ;23.252
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1273 ;16.471 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;21.349 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1080 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8439 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1792 ; 0.004 ; 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): 3547 ; 1.901 ; 2.307
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3546 ; 1.898 ; 2.306
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4436 ; 2.809 ; 3.446
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3982 ; 2.730 ; 2.596
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 4C28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1290058055.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESERCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56809
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 176.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4C0C
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 M AMMONIUM ACETATE, 0.1 M SODIUM
REMARK 280 ACETATE PH 4.5, 28% PEG 3350, 5% JEFFAMINE M-600 PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 36.47550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.41950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.50250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.41950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.47550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.50250
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 21
REMARK 465 ALA A 22
REMARK 465 LYS A 23
REMARK 465 LYS A 24
REMARK 465 THR A 25
REMARK 465 SER A 26
REMARK 465 SER A 27
REMARK 465 LYS A 28
REMARK 465 ALA A 252
REMARK 465 SER A 253
REMARK 465 LYS A 254
REMARK 465 ASP A 255
REMARK 465 ASN A 256
REMARK 465 ASN A 257
REMARK 465 LYS A 478
REMARK 465 LEU A 479
REMARK 465 PRO A 480
REMARK 465 SER A 481
REMARK 465 HIS 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 MET B 21
REMARK 465 ALA B 22
REMARK 465 LYS B 23
REMARK 465 LYS B 24
REMARK 465 THR B 25
REMARK 465 SER B 26
REMARK 465 SER B 27
REMARK 465 LYS B 28
REMARK 465 ALA B 252
REMARK 465 SER B 253
REMARK 465 LYS B 254
REMARK 465 ASP B 255
REMARK 465 ASN B 256
REMARK 465 ASN B 257
REMARK 465 THR B 258
REMARK 465 LYS B 477
REMARK 465 LYS B 478
REMARK 465 LEU B 479
REMARK 465 PRO B 480
REMARK 465 SER B 481
REMARK 465 HIS 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 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 PRO A 29 CG CD
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 470 THR A 258 OG1 CG2
REMARK 470 LYS A 477 CG CD CE NZ
REMARK 470 ILE B 136 CG1 CD1
REMARK 470 LYS B 138 CE NZ
REMARK 470 GLN B 140 CG CD OE1 NE2
REMARK 470 LYS B 190 CE NZ
REMARK 470 GLU B 250 CD OE1 OE2
REMARK 470 GLU B 251 CG CD OE1 OE2
REMARK 470 GLU B 325 CG CD OE1 OE2
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 OG SER A 277 O HOH A 2138 2.12
REMARK 500 O HOH B 2046 O HOH B 2047 2.14
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 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 456 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 347 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 351 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 449 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 456 CB - CG - OD1 ANGL. DEV. = 5.5 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 ASN A 51 83.13 -159.13
REMARK 500 ALA A 115 -115.07 60.16
REMARK 500 TRP A 158 57.40 -116.64
REMARK 500 LEU A 192 85.16 -154.20
REMARK 500 ALA B 115 -116.49 52.36
REMARK 500 TRP B 158 69.16 -106.28
REMARK 500 GLN B 293 -83.92 -31.47
REMARK 500 LEU B 448 48.91 -90.44
REMARK 500 LEU B 448 42.15 -90.44
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 A1450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 422 SG
REMARK 620 2 HEM A1450 NA 97.2
REMARK 620 3 HEM A1450 NB 87.0 88.6
REMARK 620 4 HEM A1450 NC 82.2 178.9 90.5
REMARK 620 5 HEM A1450 ND 93.3 92.0 179.3 88.9
REMARK 620 6 TW5 A1460 N2 174.5 88.3 93.0 92.3 86.6
REMARK 620 7 TW5 A1460 N2 174.2 88.6 92.4 92.0 87.2 0.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 422 SG
REMARK 620 2 HEM B1450 NA 96.2
REMARK 620 3 HEM B1450 NB 86.4 89.3
REMARK 620 4 HEM B1450 NC 84.7 178.4 89.5
REMARK 620 5 HEM B1450 ND 93.2 90.6 179.6 90.7
REMARK 620 6 TW5 B1460 N2 173.4 86.3 87.5 92.6 92.9
REMARK 620 7 TW5 B1460 N2 173.9 86.5 88.1 92.5 92.2 0.7
REMARK 620 N 1 2 3 4 5 6
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 1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TW5 A 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TW5 B 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1479
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C27 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI CYP51 BOUND TO THE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST 32 RESIDUES AT THE N-TERMINUS ARE REPLACED WITH THE
REMARK 999 MAKKTSSKGKL SEQUENCE, 6XHIS TAG ENGINEERED AT THE C-
REMARK 999 TERMINUS.
DBREF 4C28 A 29 481 UNP Q7Z1V1 CP51_TRYCC 29 481
DBREF 4C28 B 29 481 UNP Q7Z1V1 CP51_TRYCC 29 481
SEQADV 4C28 MET A 21 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 ALA A 22 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS A 23 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS A 24 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 THR A 25 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 SER A 26 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 SER A 27 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS A 28 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 482 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 483 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 484 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 485 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 486 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS A 487 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 MET B 21 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 ALA B 22 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS B 23 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS B 24 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 THR B 25 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 SER B 26 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 SER B 27 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 LYS B 28 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 482 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 483 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 484 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 485 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 486 UNP Q7Z1V1 EXPRESSION TAG
SEQADV 4C28 HIS B 487 UNP Q7Z1V1 EXPRESSION TAG
SEQRES 1 A 467 MET ALA LYS LYS THR SER SER LYS PRO THR ASP PRO PRO
SEQRES 2 A 467 VAL TYR PRO VAL THR VAL PRO PHE LEU GLY HIS ILE VAL
SEQRES 3 A 467 GLN PHE GLY LYS ASN PRO LEU GLU PHE MET GLN ARG CYS
SEQRES 4 A 467 LYS ARG ASP LEU LYS SER GLY VAL PHE THR ILE SER ILE
SEQRES 5 A 467 GLY GLY GLN ARG VAL THR ILE VAL GLY ASP PRO HIS GLU
SEQRES 6 A 467 HIS SER ARG PHE PHE SER PRO ARG ASN GLU ILE LEU SER
SEQRES 7 A 467 PRO ARG GLU VAL TYR THR ILE MET THR PRO VAL PHE GLY
SEQRES 8 A 467 GLU GLY VAL ALA TYR ALA ALA PRO TYR PRO ARG MET ARG
SEQRES 9 A 467 GLU GLN LEU ASN PHE LEU ALA GLU GLU LEU THR ILE ALA
SEQRES 10 A 467 LYS PHE GLN ASN PHE VAL PRO ALA ILE GLN HIS GLU VAL
SEQRES 11 A 467 ARG LYS PHE MET ALA GLU ASN TRP LYS GLU ASP GLU GLY
SEQRES 12 A 467 VAL ILE ASN LEU LEU GLU ASP CYS GLY ALA MET ILE ILE
SEQRES 13 A 467 ASN THR ALA CYS GLN CYS LEU PHE GLY GLU ASP LEU ARG
SEQRES 14 A 467 LYS ARG LEU ASN ALA ARG HIS PHE ALA GLN LEU LEU SER
SEQRES 15 A 467 LYS MET GLU SER SER LEU ILE PRO ALA ALA VAL PHE MET
SEQRES 16 A 467 PRO TRP LEU LEU ARG LEU PRO LEU PRO GLN SER ALA ARG
SEQRES 17 A 467 CYS ARG GLU ALA ARG ALA GLU LEU GLN LYS ILE LEU GLY
SEQRES 18 A 467 GLU ILE ILE VAL ALA ARG GLU LYS GLU GLU ALA SER LYS
SEQRES 19 A 467 ASP ASN ASN THR SER ASP LEU LEU GLY GLY LEU LEU LYS
SEQRES 20 A 467 ALA VAL TYR ARG ASP GLY THR ARG MET SER LEU HIS GLU
SEQRES 21 A 467 VAL CYS GLY MET ILE VAL ALA ALA MET PHE ALA GLY GLN
SEQRES 22 A 467 HIS THR SER THR ILE THR THR SER TRP SER MET LEU HIS
SEQRES 23 A 467 LEU MET HIS PRO LYS ASN LYS LYS TRP LEU ASP LYS LEU
SEQRES 24 A 467 HIS LYS GLU ILE ASP GLU PHE PRO ALA GLN LEU ASN TYR
SEQRES 25 A 467 ASP ASN VAL MET ASP GLU MET PRO PHE ALA GLU ARG CYS
SEQRES 26 A 467 VAL ARG GLU SER ILE ARG ARG ASP PRO PRO LEU LEU MET
SEQRES 27 A 467 VAL MET ARG MET VAL LYS ALA GLU VAL LYS VAL GLY SER
SEQRES 28 A 467 TYR VAL VAL PRO LYS GLY ASP ILE ILE ALA CYS SER PRO
SEQRES 29 A 467 LEU LEU SER HIS HIS ASP GLU GLU ALA PHE PRO ASN PRO
SEQRES 30 A 467 ARG LEU TRP ASP PRO GLU ARG ASP GLU LYS VAL ASP GLY
SEQRES 31 A 467 ALA PHE ILE GLY PHE GLY ALA GLY VAL HIS LYS CYS ILE
SEQRES 32 A 467 GLY GLN LYS PHE ALA LEU LEU GLN VAL LYS THR ILE LEU
SEQRES 33 A 467 ALA THR ALA PHE ARG GLU TYR ASP PHE GLN LEU LEU ARG
SEQRES 34 A 467 ASP GLU VAL PRO ASP PRO ASP TYR HIS THR MET VAL VAL
SEQRES 35 A 467 GLY PRO THR LEU ASN GLN CYS LEU VAL LYS TYR THR ARG
SEQRES 36 A 467 LYS LYS LYS LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 467 MET ALA LYS LYS THR SER SER LYS PRO THR ASP PRO PRO
SEQRES 2 B 467 VAL TYR PRO VAL THR VAL PRO PHE LEU GLY HIS ILE VAL
SEQRES 3 B 467 GLN PHE GLY LYS ASN PRO LEU GLU PHE MET GLN ARG CYS
SEQRES 4 B 467 LYS ARG ASP LEU LYS SER GLY VAL PHE THR ILE SER ILE
SEQRES 5 B 467 GLY GLY GLN ARG VAL THR ILE VAL GLY ASP PRO HIS GLU
SEQRES 6 B 467 HIS SER ARG PHE PHE SER PRO ARG ASN GLU ILE LEU SER
SEQRES 7 B 467 PRO ARG GLU VAL TYR THR ILE MET THR PRO VAL PHE GLY
SEQRES 8 B 467 GLU GLY VAL ALA TYR ALA ALA PRO TYR PRO ARG MET ARG
SEQRES 9 B 467 GLU GLN LEU ASN PHE LEU ALA GLU GLU LEU THR ILE ALA
SEQRES 10 B 467 LYS PHE GLN ASN PHE VAL PRO ALA ILE GLN HIS GLU VAL
SEQRES 11 B 467 ARG LYS PHE MET ALA GLU ASN TRP LYS GLU ASP GLU GLY
SEQRES 12 B 467 VAL ILE ASN LEU LEU GLU ASP CYS GLY ALA MET ILE ILE
SEQRES 13 B 467 ASN THR ALA CYS GLN CYS LEU PHE GLY GLU ASP LEU ARG
SEQRES 14 B 467 LYS ARG LEU ASN ALA ARG HIS PHE ALA GLN LEU LEU SER
SEQRES 15 B 467 LYS MET GLU SER SER LEU ILE PRO ALA ALA VAL PHE MET
SEQRES 16 B 467 PRO TRP LEU LEU ARG LEU PRO LEU PRO GLN SER ALA ARG
SEQRES 17 B 467 CYS ARG GLU ALA ARG ALA GLU LEU GLN LYS ILE LEU GLY
SEQRES 18 B 467 GLU ILE ILE VAL ALA ARG GLU LYS GLU GLU ALA SER LYS
SEQRES 19 B 467 ASP ASN ASN THR SER ASP LEU LEU GLY GLY LEU LEU LYS
SEQRES 20 B 467 ALA VAL TYR ARG ASP GLY THR ARG MET SER LEU HIS GLU
SEQRES 21 B 467 VAL CYS GLY MET ILE VAL ALA ALA MET PHE ALA GLY GLN
SEQRES 22 B 467 HIS THR SER THR ILE THR THR SER TRP SER MET LEU HIS
SEQRES 23 B 467 LEU MET HIS PRO LYS ASN LYS LYS TRP LEU ASP LYS LEU
SEQRES 24 B 467 HIS LYS GLU ILE ASP GLU PHE PRO ALA GLN LEU ASN TYR
SEQRES 25 B 467 ASP ASN VAL MET ASP GLU MET PRO PHE ALA GLU ARG CYS
SEQRES 26 B 467 VAL ARG GLU SER ILE ARG ARG ASP PRO PRO LEU LEU MET
SEQRES 27 B 467 VAL MET ARG MET VAL LYS ALA GLU VAL LYS VAL GLY SER
SEQRES 28 B 467 TYR VAL VAL PRO LYS GLY ASP ILE ILE ALA CYS SER PRO
SEQRES 29 B 467 LEU LEU SER HIS HIS ASP GLU GLU ALA PHE PRO ASN PRO
SEQRES 30 B 467 ARG LEU TRP ASP PRO GLU ARG ASP GLU LYS VAL ASP GLY
SEQRES 31 B 467 ALA PHE ILE GLY PHE GLY ALA GLY VAL HIS LYS CYS ILE
SEQRES 32 B 467 GLY GLN LYS PHE ALA LEU LEU GLN VAL LYS THR ILE LEU
SEQRES 33 B 467 ALA THR ALA PHE ARG GLU TYR ASP PHE GLN LEU LEU ARG
SEQRES 34 B 467 ASP GLU VAL PRO ASP PRO ASP TYR HIS THR MET VAL VAL
SEQRES 35 B 467 GLY PRO THR LEU ASN GLN CYS LEU VAL LYS TYR THR ARG
SEQRES 36 B 467 LYS LYS LYS LEU PRO SER HIS HIS HIS HIS HIS HIS
HET HEM A1450 43
HET TW5 A1460 86
HET EDO A1478 4
HET CL A1479 1
HET HEM B1450 43
HET TW5 B1460 86
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM TW5 (R)-N-(3-(1H-INDOL-3-YL)-1-OXO-1-(PYRIDIN-4-YLAMINO)
HETNAM 2 TW5 PROPAN-2-YL)-4-(4-(4-CHLOROPHENYL)PIPERAZIN-1-YL)-2-
HETNAM 3 TW5 FLUOROBENZAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN HEM HEME
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 TW5 2(C33 H30 CL F N6 O2)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 CL CL 1-
FORMUL 9 HOH *410(H2 O)
HELIX 1 1 HIS A 44 ASN A 51 1 8
HELIX 2 2 ASN A 51 LEU A 63 1 13
HELIX 3 3 ASP A 82 GLU A 85 5 4
HELIX 4 4 HIS A 86 SER A 91 1 6
HELIX 5 5 TYR A 103 ILE A 105 5 3
HELIX 6 6 MET A 106 GLY A 111 1 6
HELIX 7 7 VAL A 114 ALA A 118 5 5
HELIX 8 8 PRO A 119 GLU A 133 1 15
HELIX 9 9 LEU A 134 PHE A 139 5 6
HELIX 10 10 ASN A 141 TRP A 158 1 18
HELIX 11 11 LEU A 167 PHE A 184 1 18
HELIX 12 12 GLY A 185 LEU A 192 1 8
HELIX 13 13 ASN A 193 SER A 207 1 15
HELIX 14 14 ILE A 209 PHE A 214 5 6
HELIX 15 15 MET A 215 LEU A 221 5 7
HELIX 16 16 ARG A 228 GLU A 251 1 24
HELIX 17 17 ASP A 260 LEU A 266 1 7
HELIX 18 18 SER A 277 HIS A 309 1 33
HELIX 19 19 ASN A 312 ASP A 324 1 13
HELIX 20 20 ASN A 331 GLU A 338 1 8
HELIX 21 21 MET A 339 ASP A 353 1 15
HELIX 22 22 SER A 383 HIS A 388 1 6
HELIX 23 23 ALA A 417 LYS A 421 5 5
HELIX 24 24 GLY A 424 GLU A 442 1 19
HELIX 25 25 LEU A 466 GLN A 468 5 3
HELIX 26 26 HIS B 44 ASN B 51 1 8
HELIX 27 27 ASN B 51 LEU B 63 1 13
HELIX 28 28 ASP B 82 GLU B 85 5 4
HELIX 29 29 HIS B 86 SER B 91 1 6
HELIX 30 30 TYR B 103 ILE B 105 5 3
HELIX 31 31 MET B 106 GLY B 111 1 6
HELIX 32 32 VAL B 114 ALA B 118 5 5
HELIX 33 33 PRO B 119 GLU B 133 1 15
HELIX 34 34 LEU B 134 PHE B 139 5 6
HELIX 35 35 ASN B 141 TRP B 158 1 18
HELIX 36 36 LEU B 167 PHE B 184 1 18
HELIX 37 37 GLY B 185 LEU B 192 1 8
HELIX 38 38 ASN B 193 SER B 206 1 14
HELIX 39 39 ILE B 209 PHE B 214 5 6
HELIX 40 40 MET B 215 LEU B 221 5 7
HELIX 41 41 ARG B 228 GLU B 251 1 24
HELIX 42 42 ASP B 260 LYS B 267 1 8
HELIX 43 43 SER B 277 HIS B 309 1 33
HELIX 44 44 ASN B 312 ASP B 324 1 13
HELIX 45 45 ASN B 331 GLU B 338 1 8
HELIX 46 46 MET B 339 ASP B 353 1 15
HELIX 47 47 SER B 383 HIS B 388 1 6
HELIX 48 48 ALA B 417 LYS B 421 5 5
HELIX 49 49 GLY B 424 GLU B 442 1 19
HELIX 50 50 LEU B 466 GLN B 468 5 3
SHEET 1 AA 5 VAL A 67 ILE A 72 0
SHEET 2 AA 5 GLN A 75 VAL A 80 -1 O GLN A 75 N ILE A 72
SHEET 3 AA 5 ILE A 379 CYS A 382 1 O ILE A 379 N THR A 78
SHEET 4 AA 5 VAL A 359 VAL A 363 -1 O VAL A 359 N CYS A 382
SHEET 5 AA 5 LEU A 97 SER A 98 -1 O SER A 98 N MET A 362
SHEET 1 AB 3 GLU A 162 ASN A 166 0
SHEET 2 AB 3 LEU A 470 ARG A 475 -1 O VAL A 471 N ILE A 165
SHEET 3 AB 3 TYR A 443 LEU A 447 -1 O ASP A 444 N THR A 474
SHEET 1 AC 2 VAL A 367 VAL A 369 0
SHEET 2 AC 2 TYR A 372 VAL A 374 -1 O TYR A 372 N VAL A 369
SHEET 1 AD 2 PRO A 455 ASP A 456 0
SHEET 2 AD 2 GLY A 463 PRO A 464 -1 O GLY A 463 N ASP A 456
SHEET 1 BA 5 VAL B 67 ILE B 72 0
SHEET 2 BA 5 GLN B 75 VAL B 80 -1 O GLN B 75 N ILE B 72
SHEET 3 BA 5 ILE B 379 CYS B 382 1 O ILE B 379 N THR B 78
SHEET 4 BA 5 VAL B 359 VAL B 363 -1 O VAL B 359 N CYS B 382
SHEET 5 BA 5 LEU B 97 SER B 98 -1 O SER B 98 N MET B 362
SHEET 1 BB 3 GLU B 162 ASN B 166 0
SHEET 2 BB 3 LEU B 470 ARG B 475 -1 O VAL B 471 N ILE B 165
SHEET 3 BB 3 TYR B 443 LEU B 447 -1 O ASP B 444 N THR B 474
SHEET 1 BC 2 VAL B 367 VAL B 369 0
SHEET 2 BC 2 TYR B 372 VAL B 374 -1 O TYR B 372 N VAL B 369
SHEET 1 BD 2 PRO B 455 ASP B 456 0
SHEET 2 BD 2 GLY B 463 PRO B 464 -1 O GLY B 463 N ASP B 456
LINK SG CYS A 422 FE HEM A1450 1555 1555 2.27
LINK FE HEM A1450 N2 BTW5 A1460 1555 1555 2.19
LINK FE HEM A1450 N2 ATW5 A1460 1555 1555 2.18
LINK SG CYS B 422 FE HEM B1450 1555 1555 2.23
LINK FE HEM B1450 N2 BTW5 B1460 1555 1555 2.14
LINK FE HEM B1450 N2 ATW5 B1460 1555 1555 2.12
SITE 1 AC1 23 TYR A 116 ARG A 124 LEU A 127 LEU A 134
SITE 2 AC1 23 ALA A 288 ALA A 291 GLY A 292 THR A 295
SITE 3 AC1 23 THR A 299 LEU A 356 ARG A 361 GLY A 414
SITE 4 AC1 23 PHE A 415 GLY A 416 VAL A 419 HIS A 420
SITE 5 AC1 23 LYS A 421 CYS A 422 ILE A 423 GLY A 424
SITE 6 AC1 23 TW5 A1460 HOH A2052 HOH A2201
SITE 1 AC2 16 ILE A 45 PHE A 48 GLY A 49 PHE A 110
SITE 2 AC2 16 TYR A 116 PRO A 210 PHE A 214 PHE A 290
SITE 3 AC2 16 ALA A 291 LEU A 356 MET A 460 VAL A 461
SITE 4 AC2 16 HEM A1450 HOH A2050 HOH A2101 PRO B 222
SITE 1 AC3 21 MET B 123 ARG B 124 LEU B 134 ALA B 288
SITE 2 AC3 21 ALA B 291 GLY B 292 THR B 295 SER B 296
SITE 3 AC3 21 LEU B 356 VAL B 359 ARG B 361 GLY B 414
SITE 4 AC3 21 PHE B 415 GLY B 416 HIS B 420 CYS B 422
SITE 5 AC3 21 ILE B 423 GLY B 424 ALA B 428 TW5 B1460
SITE 6 AC3 21 HOH B2154
SITE 1 AC4 13 PRO A 222 ILE B 45 PHE B 48 MET B 106
SITE 2 AC4 13 PHE B 110 TYR B 116 PRO B 210 PHE B 214
SITE 3 AC4 13 ALA B 291 MET B 460 VAL B 461 HEM B1450
SITE 4 AC4 13 HOH B2073
SITE 1 AC5 6 ILE A 175 ALA A 179 ALA A 288 MET A 289
SITE 2 AC5 6 GLY A 292 GLN A 293
SITE 1 AC6 2 GLY A 111 GLU A 112
CRYST1 72.951 79.005 176.839 90.00 90.00 90.00 P 21 21 21 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 0.013708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
