HEADER OXIDOREDUCTASE 11-OCT-09 2WUZ
TITLE X-RAY STRUCTURE OF CYP51 FROM TRYPANOSOMA CRUZI IN COMPLEX WITH
TITLE 2 FLUCONAZOLE IN ALTERNATIVE CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LANOSTEROL 14-ALPHA-DEMETHYLASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 22-481;
COMPND 5 SYNONYM: STEROL 14 ALPHA-DEMETHYLASE, CYP51;
COMPND 6 EC: 1.14.13.70;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS OXIDOREDUCTASE, METHYLTRANSFERASE, P450, IRON, CYP51, METAL-BINDING,
KEYWDS 2 ERGOSTEROL BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-K.CHEN,S.S.F.LEUNG,C.GUILBERT,M.JACOBSON,J.H.MCKERROW,L.M.PODUST
REVDAT 5 20-DEC-23 2WUZ 1 REMARK LINK
REVDAT 4 11-APR-12 2WUZ 1 JRNL REMARK VERSN HETSYN
REVDAT 3 07-APR-10 2WUZ 1 JRNL REMARK
REVDAT 2 02-FEB-10 2WUZ 1 TITLE JRNL REMARK
REVDAT 1 20-OCT-09 2WUZ 0
JRNL AUTH C.-K.CHEN,S.S.F.LEUNG,C.GUILBERT,M.JACOBSON,J.H.MCKERROW,
JRNL AUTH 2 L.M.PODUST
JRNL TITL STRUCTURAL CHARACTERIZATION OF CYP51 FROM TRYPANOSOMA CRUZI
JRNL TITL 2 AND TRYPANOSOMA BRUCEI BOUND TO THE ANTIFUNGAL DRUGS
JRNL TITL 3 POSACONAZOLE AND FLUCONAZOLE
JRNL REF PLOS NEGL TROP DIS V. 4 E651 2010
JRNL REFN ISSN 1935-2727
JRNL PMID 20386598
JRNL DOI 10.1371/JOURNAL.PNTD.0000651
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 38792
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2046
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1964
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 130
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -1.32000
REMARK 3 B33 (A**2) : 1.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.48000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.270
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.212
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.542
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7314 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9948 ; 1.891 ; 2.010
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 892 ; 7.399 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 311 ;36.515 ;23.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1226 ;17.932 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;19.171 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1078 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5564 ; 0.009 ; 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): 4472 ; 0.841 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7224 ; 1.450 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2842 ; 2.324 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2724 ; 3.523 ; 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): 7314 ; 1.534 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 179 ; 8.288 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 7124 ; 2.128 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 30 A 475 2
REMARK 3 1 B 30 B 475 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1684 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1684 ; 0.06 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1628 ; 0.10 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1628 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1684 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1684 ; 0.10 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1628 ; 0.10 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1628 ; 0.10 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 257 A 362
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0170 -21.7210 16.2870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.1011
REMARK 3 T33: 0.0943 T12: -0.0044
REMARK 3 T13: -0.0493 T23: 0.0509
REMARK 3 L TENSOR
REMARK 3 L11: 0.7008 L22: 2.5695
REMARK 3 L33: 1.1814 L12: -0.3741
REMARK 3 L13: -0.2924 L23: -0.7000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0494 S12: -0.0864 S13: 0.0514
REMARK 3 S21: 0.5103 S22: -0.1049 S23: -0.2211
REMARK 3 S31: 0.0030 S32: 0.2142 S33: 0.0556
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 363 A 476
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4980 -28.1970 8.5550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0902 T22: 0.0631
REMARK 3 T33: 0.0956 T12: 0.0299
REMARK 3 T13: -0.0202 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 0.9391 L22: 2.0865
REMARK 3 L33: 1.6221 L12: -0.7014
REMARK 3 L13: 0.1841 L23: -0.3133
REMARK 3 S TENSOR
REMARK 3 S11: 0.1300 S12: -0.0112 S13: -0.2299
REMARK 3 S21: 0.0891 S22: -0.1327 S23: 0.0204
REMARK 3 S31: 0.1693 S32: 0.1135 S33: 0.0027
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 260 B 362
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3190 6.3680 16.4120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1112 T22: 0.1328
REMARK 3 T33: 0.1065 T12: 0.0323
REMARK 3 T13: 0.0534 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 0.4559 L22: 2.1016
REMARK 3 L33: 1.2999 L12: -0.1179
REMARK 3 L13: 0.3643 L23: 0.3578
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.0634 S13: 0.0287
REMARK 3 S21: 0.4076 S22: -0.0468 S23: 0.2513
REMARK 3 S31: -0.0688 S32: -0.3461 S33: 0.0434
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 363 B 480
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9620 12.4350 9.2240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0777 T22: 0.0633
REMARK 3 T33: 0.1334 T12: 0.0477
REMARK 3 T13: 0.0427 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.0693 L22: 1.8953
REMARK 3 L33: 2.3739 L12: -0.5062
REMARK 3 L13: 0.6049 L23: 0.1835
REMARK 3 S TENSOR
REMARK 3 S11: 0.1080 S12: 0.0428 S13: 0.2304
REMARK 3 S21: 0.1169 S22: -0.0475 S23: 0.0036
REMARK 3 S31: -0.1600 S32: -0.1828 S33: -0.0606
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 36.4990 -18.2830 -2.1650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.1391
REMARK 3 T33: 0.1041 T12: 0.0768
REMARK 3 T13: 0.0529 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 1.1423 L22: 2.9712
REMARK 3 L33: 1.9550 L12: -0.1939
REMARK 3 L13: 0.3133 L23: 0.4323
REMARK 3 S TENSOR
REMARK 3 S11: 0.1314 S12: 0.2882 S13: 0.0865
REMARK 3 S21: -0.4125 S22: -0.2628 S23: -0.1849
REMARK 3 S31: -0.0262 S32: 0.2737 S33: 0.1315
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3080 -7.6310 17.4930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.1248
REMARK 3 T33: 0.0909 T12: -0.0229
REMARK 3 T13: 0.0194 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.7663 L22: 1.7608
REMARK 3 L33: 1.0657 L12: -0.1797
REMARK 3 L13: 0.0350 L23: -0.2607
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: -0.1803 S13: 0.1477
REMARK 3 S21: 0.4001 S22: -0.1060 S23: 0.0446
REMARK 3 S31: -0.1044 S32: -0.0551 S33: 0.1071
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 28 B 150
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1870 2.5760 -2.0150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0685 T22: 0.1266
REMARK 3 T33: 0.0721 T12: 0.0597
REMARK 3 T13: -0.0431 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.8978 L22: 2.4235
REMARK 3 L33: 1.8412 L12: -0.2737
REMARK 3 L13: 0.2051 L23: -0.6204
REMARK 3 S TENSOR
REMARK 3 S11: 0.1392 S12: 0.1475 S13: -0.0699
REMARK 3 S21: -0.2209 S22: -0.1533 S23: 0.1611
REMARK 3 S31: 0.0297 S32: -0.2834 S33: 0.0141
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 151 B 250
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4880 -7.7050 17.6800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1489 T22: 0.0814
REMARK 3 T33: 0.0723 T12: -0.0131
REMARK 3 T13: -0.0276 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.0030 L22: 1.8878
REMARK 3 L33: 1.4361 L12: 0.0986
REMARK 3 L13: -0.0999 L23: 0.3675
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0895 S13: -0.1319
REMARK 3 S21: 0.3922 S22: -0.1164 S23: -0.0344
REMARK 3 S31: 0.2471 S32: -0.1369 S33: 0.1397
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. SIDE
REMARK 3 CHAINS NOT VISIBLE IN THE DENSITY WAS MODELED AS ALANINE
REMARK 4
REMARK 4 2WUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.0
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) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40838
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 76.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2WV2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% POLYPROPYLENE GLYCOL 400, 0.1 TRIS
REMARK 280 -HCL, PH=6.0, PH 6.0
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 46.28700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 6230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 15
REMARK 465 ALA A 16
REMARK 465 LYS A 17
REMARK 465 LYS A 18
REMARK 465 LYS A 19
REMARK 465 LYS A 20
REMARK 465 LYS A 21
REMARK 465 LYS A 22
REMARK 465 SER A 23
REMARK 465 PHE A 24
REMARK 465 ASN A 25
REMARK 465 THR A 26
REMARK 465 GLU A 251
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 LYS A 477
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 15
REMARK 465 ALA B 16
REMARK 465 LYS B 17
REMARK 465 LYS B 18
REMARK 465 LYS B 19
REMARK 465 LYS B 20
REMARK 465 LYS B 21
REMARK 465 LYS B 22
REMARK 465 SER B 23
REMARK 465 PHE B 24
REMARK 465 ASN B 25
REMARK 465 THR B 26
REMARK 465 THR B 27
REMARK 465 GLU B 251
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 SER B 259
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 ARG A 28 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 37 CG1 CG2
REMARK 470 PHE A 41 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 134 CG CD1 CD2
REMARK 470 THR A 135 OG1 CG2
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 GLN A 140 CG CD OE1 NE2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 ASP A 161 CG OD1 OD2
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 GLU A 248 CG CD OE1 OE2
REMARK 470 GLU A 250 CD OE1 OE2
REMARK 470 ASN A 257 CG OD1 ND2
REMARK 470 THR A 258 OG1 CG2
REMARK 470 SER A 259 OG
REMARK 470 LYS A 267 CG CD CE NZ
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 GLN A 329 CG CD OE1 NE2
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 LYS A 476 CG CD CE NZ
REMARK 470 ARG B 28 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 93 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 120 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR B 135 OG1 CG2
REMARK 470 LYS B 138 CD CE NZ
REMARK 470 GLN B 140 CG CD OE1 NE2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 GLU B 160 CG CD OE1 OE2
REMARK 470 GLU B 248 CG CD OE1 OE2
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 LYS B 267 CE NZ
REMARK 470 ARG B 271 NE CZ NH1 NH2
REMARK 470 GLU B 325 CG CD OE1 OE2
REMARK 470 GLN B 329 CG CD OE1 NE2
REMARK 470 ARG B 475 NE CZ NH1 NH2
REMARK 470 LYS B 477 CE NZ
REMARK 470 LEU B 479 CG CD1 CD2
REMARK 470 PRO B 480 CG CD
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 O VAL B 369 O SER B 371 1.99
REMARK 500 O VAL A 369 O SER A 371 2.01
REMARK 500 OE2 GLU B 242 O HOH B 2036 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 382 CB CYS B 382 SG -0.097
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 31 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 GLU A 112 CA - C - N ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 GLU A 348 OE1 - CD - OE2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 351 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 404 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 LEU B 53 CB - CG - CD1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG B 230 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU B 348 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG B 351 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 404 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 29 0.41 -65.53
REMARK 500 VAL A 39 76.05 47.60
REMARK 500 LEU A 53 -70.35 -53.03
REMARK 500 GLU A 112 -94.17 -34.57
REMARK 500 ALA A 115 -119.64 61.11
REMARK 500 LEU A 134 52.52 -119.86
REMARK 500 THR A 135 108.31 173.73
REMARK 500 ILE A 136 6.14 -151.64
REMARK 500 GLU A 160 172.56 -57.60
REMARK 500 THR A 258 -95.33 -48.57
REMARK 500 ASP A 272 -165.86 -73.27
REMARK 500 TYR A 372 151.20 65.34
REMARK 500 ILE A 413 36.13 -141.08
REMARK 500 LEU A 448 37.31 -92.10
REMARK 500 ARG A 449 26.99 -147.73
REMARK 500 ASP A 450 -62.96 55.73
REMARK 500 ASN A 467 -39.01 -30.03
REMARK 500 VAL B 39 77.03 50.28
REMARK 500 LEU B 53 -74.18 -54.93
REMARK 500 VAL B 109 -61.56 -103.72
REMARK 500 GLU B 112 152.90 -48.75
REMARK 500 ALA B 115 -116.56 55.67
REMARK 500 GLU B 132 12.13 -68.61
REMARK 500 THR B 135 111.19 -177.93
REMARK 500 TRP B 158 53.18 -116.59
REMARK 500 ASP B 272 -169.38 -71.24
REMARK 500 TYR B 372 151.57 67.87
REMARK 500 LEU B 448 32.24 -91.14
REMARK 500 ASN B 467 -39.35 -32.40
REMARK 500 LYS B 478 -79.33 -105.20
REMARK 500 LEU B 479 -173.45 -68.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 42 GLY A 43 -72.29
REMARK 500 LEU B 42 GLY B 43 -142.04
REMARK 500 LYS B 478 LEU B 479 -143.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PROTOPORPHYRIN IX CONTAINING FE (HEM): THIOLATE BOND
REMARK 600 BETWEEN THE HEME FE AND CYS422
REMARK 600 FLUCONAZOLE (TPF): COORDINATION BOND BETWEEN THE HEME FE
REMARK 600 AND FLUCONAZOLE
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 96.6
REMARK 620 3 HEM A1450 NB 88.8 88.1
REMARK 620 4 HEM A1450 NC 84.7 175.2 96.6
REMARK 620 5 HEM A1450 ND 91.8 88.1 176.2 87.2
REMARK 620 6 TPF A1460 N5 177.8 82.1 89.4 96.8 89.9
REMARK 620 N 1 2 3 4 5
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 98.6
REMARK 620 3 HEM B1450 NB 93.5 88.7
REMARK 620 4 HEM B1450 NC 85.2 174.0 95.8
REMARK 620 5 HEM B1450 ND 88.5 93.1 177.2 82.2
REMARK 620 6 TPF B1460 N2 175.1 82.9 91.3 92.9 86.7
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 1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPF 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 TPF B 1460
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WX2 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF CYP51 FROM THE HUMAN PATHOGEN TRYPANOSOMA CRUZI
REMARK 900 IN COMPLEX WITH FLUCONAZOLE
REMARK 900 RELATED ID: 2WV2 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF CYP51 FROM THE HUMAN PATHOGEN TRYPANOSOMA BRUCEI
REMARK 900 IN COMPLEX WITH FLUCONAZOLE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 21 RESIDUES UPSTREAM OF K22 WERE REPLACED WITH
REMARK 999 THE FRAGMENT MAKKKKK AT THE N-TERMINUS. HIS6-TAG WAS
REMARK 999 INTRODUCED AT THE C-TERMINUS
DBREF 2WUZ A 15 21 PDB 2WUZ 2WUZ 15 21
DBREF 2WUZ A 22 481 UNP Q5I4E1 Q5I4E1_TRYCR 22 481
DBREF 2WUZ A 482 487 PDB 2WUZ 2WUZ 482 487
DBREF 2WUZ B 15 21 PDB 2WUZ 2WUZ 15 21
DBREF 2WUZ B 22 481 UNP Q5I4E1 Q5I4E1_TRYCR 22 481
DBREF 2WUZ B 482 487 PDB 2WUZ 2WUZ 482 487
SEQRES 1 A 473 MET ALA LYS LYS LYS LYS LYS LYS SER PHE ASN THR THR
SEQRES 2 A 473 ARG PRO THR ASP PRO PRO VAL TYR PRO VAL THR VAL PRO
SEQRES 3 A 473 PHE LEU GLY HIS ILE VAL GLN PHE GLY LYS ASN PRO LEU
SEQRES 4 A 473 GLU PHE MET GLN ARG CYS LYS ARG ASP LEU LYS SER GLY
SEQRES 5 A 473 VAL PHE THR ILE SER ILE GLY GLY GLN ARG VAL THR ILE
SEQRES 6 A 473 VAL GLY ASP PRO HIS GLU HIS SER ARG PHE PHE SER PRO
SEQRES 7 A 473 ARG ASN GLU ILE LEU SER PRO ARG GLU VAL TYR THR ILE
SEQRES 8 A 473 MET THR PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA
SEQRES 9 A 473 PRO TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA
SEQRES 10 A 473 GLU GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO
SEQRES 11 A 473 ALA ILE GLN HIS GLU VAL ARG LYS PHE MET ALA GLU ASN
SEQRES 12 A 473 TRP LYS GLU ASP GLU GLY VAL ILE ASN LEU LEU GLU ASP
SEQRES 13 A 473 CYS GLY ALA MET ILE ILE ASN THR ALA CYS GLN CYS LEU
SEQRES 14 A 473 PHE GLY GLU ASP LEU ARG LYS ARG LEU ASN ALA ARG HIS
SEQRES 15 A 473 PHE ALA GLN LEU LEU SER LYS MET GLU SER SER LEU ILE
SEQRES 16 A 473 PRO ALA ALA VAL PHE MET PRO TRP LEU LEU ARG LEU PRO
SEQRES 17 A 473 LEU PRO GLN SER ALA ARG CYS ARG GLU ALA ARG ALA GLU
SEQRES 18 A 473 LEU GLN LYS ILE LEU GLY GLU ILE ILE VAL ALA ARG GLU
SEQRES 19 A 473 LYS GLU GLU ALA SER LYS ASP ASN ASN THR SER ASP LEU
SEQRES 20 A 473 LEU GLY GLY LEU LEU LYS ALA VAL TYR ARG ASP GLY THR
SEQRES 21 A 473 ARG MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA
SEQRES 22 A 473 ALA MET PHE ALA GLY GLN HIS THR SER THR ILE THR THR
SEQRES 23 A 473 SER TRP SER MET LEU HIS LEU MET HIS PRO LYS ASN LYS
SEQRES 24 A 473 LYS TRP LEU ASP LYS LEU HIS LYS GLU ILE ASP GLU PHE
SEQRES 25 A 473 PRO ALA GLN LEU ASN TYR ASP ASN VAL MET ASP GLU MET
SEQRES 26 A 473 PRO PHE ALA GLU ARG CYS VAL ARG GLU SER ILE ARG ARG
SEQRES 27 A 473 ASP PRO PRO LEU LEU MET VAL MET ARG MET VAL LYS ALA
SEQRES 28 A 473 GLU VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP
SEQRES 29 A 473 ILE ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU
SEQRES 30 A 473 GLU ALA PHE PRO ASN PRO ARG LEU TRP ASP PRO GLU ARG
SEQRES 31 A 473 ASP GLU LYS VAL ASP GLY ALA PHE ILE GLY PHE GLY ALA
SEQRES 32 A 473 GLY VAL HIS LYS CYS ILE GLY GLN LYS PHE ALA LEU LEU
SEQRES 33 A 473 GLN VAL LYS THR ILE LEU ALA THR ALA PHE ARG GLU TYR
SEQRES 34 A 473 ASP PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP
SEQRES 35 A 473 TYR HIS THR MET VAL VAL GLY PRO THR LEU ASN GLN CYS
SEQRES 36 A 473 LEU VAL LYS TYR THR ARG LYS LYS LYS LEU PRO SER HIS
SEQRES 37 A 473 HIS HIS HIS HIS HIS
SEQRES 1 B 473 MET ALA LYS LYS LYS LYS LYS LYS SER PHE ASN THR THR
SEQRES 2 B 473 ARG PRO THR ASP PRO PRO VAL TYR PRO VAL THR VAL PRO
SEQRES 3 B 473 PHE LEU GLY HIS ILE VAL GLN PHE GLY LYS ASN PRO LEU
SEQRES 4 B 473 GLU PHE MET GLN ARG CYS LYS ARG ASP LEU LYS SER GLY
SEQRES 5 B 473 VAL PHE THR ILE SER ILE GLY GLY GLN ARG VAL THR ILE
SEQRES 6 B 473 VAL GLY ASP PRO HIS GLU HIS SER ARG PHE PHE SER PRO
SEQRES 7 B 473 ARG ASN GLU ILE LEU SER PRO ARG GLU VAL TYR THR ILE
SEQRES 8 B 473 MET THR PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA
SEQRES 9 B 473 PRO TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA
SEQRES 10 B 473 GLU GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO
SEQRES 11 B 473 ALA ILE GLN HIS GLU VAL ARG LYS PHE MET ALA GLU ASN
SEQRES 12 B 473 TRP LYS GLU ASP GLU GLY VAL ILE ASN LEU LEU GLU ASP
SEQRES 13 B 473 CYS GLY ALA MET ILE ILE ASN THR ALA CYS GLN CYS LEU
SEQRES 14 B 473 PHE GLY GLU ASP LEU ARG LYS ARG LEU ASN ALA ARG HIS
SEQRES 15 B 473 PHE ALA GLN LEU LEU SER LYS MET GLU SER SER LEU ILE
SEQRES 16 B 473 PRO ALA ALA VAL PHE MET PRO TRP LEU LEU ARG LEU PRO
SEQRES 17 B 473 LEU PRO GLN SER ALA ARG CYS ARG GLU ALA ARG ALA GLU
SEQRES 18 B 473 LEU GLN LYS ILE LEU GLY GLU ILE ILE VAL ALA ARG GLU
SEQRES 19 B 473 LYS GLU GLU ALA SER LYS ASP ASN ASN THR SER ASP LEU
SEQRES 20 B 473 LEU GLY GLY LEU LEU LYS ALA VAL TYR ARG ASP GLY THR
SEQRES 21 B 473 ARG MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA
SEQRES 22 B 473 ALA MET PHE ALA GLY GLN HIS THR SER THR ILE THR THR
SEQRES 23 B 473 SER TRP SER MET LEU HIS LEU MET HIS PRO LYS ASN LYS
SEQRES 24 B 473 LYS TRP LEU ASP LYS LEU HIS LYS GLU ILE ASP GLU PHE
SEQRES 25 B 473 PRO ALA GLN LEU ASN TYR ASP ASN VAL MET ASP GLU MET
SEQRES 26 B 473 PRO PHE ALA GLU ARG CYS VAL ARG GLU SER ILE ARG ARG
SEQRES 27 B 473 ASP PRO PRO LEU LEU MET VAL MET ARG MET VAL LYS ALA
SEQRES 28 B 473 GLU VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP
SEQRES 29 B 473 ILE ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU
SEQRES 30 B 473 GLU ALA PHE PRO ASN PRO ARG LEU TRP ASP PRO GLU ARG
SEQRES 31 B 473 ASP GLU LYS VAL ASP GLY ALA PHE ILE GLY PHE GLY ALA
SEQRES 32 B 473 GLY VAL HIS LYS CYS ILE GLY GLN LYS PHE ALA LEU LEU
SEQRES 33 B 473 GLN VAL LYS THR ILE LEU ALA THR ALA PHE ARG GLU TYR
SEQRES 34 B 473 ASP PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP
SEQRES 35 B 473 TYR HIS THR MET VAL VAL GLY PRO THR LEU ASN GLN CYS
SEQRES 36 B 473 LEU VAL LYS TYR THR ARG LYS LYS LYS LEU PRO SER HIS
SEQRES 37 B 473 HIS HIS HIS HIS HIS
HET HEM A1450 43
HET TPF A1460 22
HET HEM B1450 43
HET TPF B1460 22
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM TPF 2-(2,4-DIFLUOROPHENYL)-1,3-DI(1H-1,2,4-TRIAZOL-1-YL)
HETNAM 2 TPF PROPAN-2-OL
HETSYN HEM HEME
HETSYN TPF FLUCONAZOLE; ALPHA-(2,4-DIFLUOROPHENYL)-ALPHA-(1H-1,2,
HETSYN 2 TPF 4-TRIAZOLE-1-YLMETHYL)-1H-1,2,4-TRIAZOLE-1-ETHANOL;
HETSYN 3 TPF ELAZOR; TRIFLUCAN; BIOZOLENE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 TPF 2(C13 H12 F2 N6 O)
FORMUL 7 HOH *176(H2 O)
HELIX 1 1 ASN A 51 LEU A 63 1 13
HELIX 2 2 ASP A 82 GLU A 85 5 4
HELIX 3 3 HIS A 86 SER A 91 1 6
HELIX 4 4 TYR A 103 THR A 107 5 5
HELIX 5 5 VAL A 114 ALA A 118 5 5
HELIX 6 6 PRO A 119 GLU A 132 1 14
HELIX 7 7 ALA A 137 GLN A 140 5 4
HELIX 8 8 ASN A 141 TRP A 158 1 18
HELIX 9 9 LEU A 167 CYS A 171 1 5
HELIX 10 10 ALA A 173 PHE A 184 1 12
HELIX 11 11 GLU A 186 LEU A 192 1 7
HELIX 12 12 ASN A 193 SER A 207 1 15
HELIX 13 13 PRO A 210 MET A 215 1 6
HELIX 14 14 PRO A 216 LEU A 221 5 6
HELIX 15 15 LEU A 223 LEU A 240 1 18
HELIX 16 16 GLU A 242 GLU A 248 1 7
HELIX 17 17 SER A 277 CYS A 282 1 6
HELIX 18 18 MET A 284 ALA A 291 1 8
HELIX 19 19 GLN A 293 HIS A 309 1 17
HELIX 20 20 ASN A 312 ASP A 324 1 13
HELIX 21 21 ASN A 331 GLU A 338 1 8
HELIX 22 22 MET A 339 ASP A 353 1 15
HELIX 23 23 SER A 383 HIS A 388 1 6
HELIX 24 24 GLN A 425 GLU A 442 1 18
HELIX 25 25 THR A 465 GLN A 468 5 4
HELIX 26 26 ASN B 51 LEU B 63 1 13
HELIX 27 27 ASP B 82 GLU B 85 5 4
HELIX 28 28 HIS B 86 SER B 91 1 6
HELIX 29 29 TYR B 103 THR B 107 5 5
HELIX 30 30 VAL B 114 ALA B 118 5 5
HELIX 31 31 PRO B 119 GLU B 132 1 14
HELIX 32 32 ALA B 137 GLN B 140 5 4
HELIX 33 33 ASN B 141 TRP B 158 1 18
HELIX 34 34 LEU B 167 CYS B 171 1 5
HELIX 35 35 ALA B 173 PHE B 184 1 12
HELIX 36 36 GLU B 186 LEU B 192 1 7
HELIX 37 37 ASN B 193 SER B 206 1 14
HELIX 38 38 ILE B 209 PHE B 214 5 6
HELIX 39 39 MET B 215 LEU B 221 5 7
HELIX 40 40 LEU B 223 LEU B 240 1 18
HELIX 41 41 GLU B 242 GLU B 248 1 7
HELIX 42 42 SER B 277 CYS B 282 1 6
HELIX 43 43 MET B 284 ALA B 291 1 8
HELIX 44 44 GLN B 293 HIS B 309 1 17
HELIX 45 45 ASN B 312 ASP B 324 1 13
HELIX 46 46 ASN B 331 GLU B 338 1 8
HELIX 47 47 MET B 339 ASP B 353 1 15
HELIX 48 48 SER B 383 HIS B 388 1 6
HELIX 49 49 GLN B 425 GLU B 442 1 18
HELIX 50 50 THR B 465 GLN B 468 5 4
SHEET 1 AA 5 PHE A 68 SER A 71 0
SHEET 2 AA 5 ARG A 76 ILE A 79 -1 O VAL A 77 N ILE A 70
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 ILE A 165 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 LYS A 368 0
SHEET 2 AC 2 VAL A 373 VAL A 374 -1 O VAL A 374 N VAL A 367
SHEET 1 BA 5 PHE B 68 SER B 71 0
SHEET 2 BA 5 ARG B 76 ILE B 79 -1 O VAL B 77 N ILE B 70
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 ILE B 165 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 LYS B 368 0
SHEET 2 BC 2 VAL B 373 VAL B 374 -1 O VAL B 374 N VAL B 367
LINK SG CYS A 422 FE HEM A1450 1555 1555 2.20
LINK FE HEM A1450 N5 TPF A1460 1555 1555 2.20
LINK SG CYS B 422 FE HEM B1450 1555 1555 2.19
LINK FE HEM B1450 N2 TPF B1460 1555 1555 2.18
CISPEP 1 THR A 135 ILE A 136 0 -16.85
CISPEP 2 THR B 135 ILE B 136 0 -18.66
SITE 1 AC1 23 TYR A 103 TYR A 116 ARG A 124 LEU A 127
SITE 2 AC1 23 ALA A 288 ALA A 291 GLY A 292 THR A 295
SITE 3 AC1 23 THR A 299 PRO A 355 LEU A 356 VAL A 359
SITE 4 AC1 23 ARG A 361 GLY A 414 PHE A 415 GLY A 416
SITE 5 AC1 23 VAL A 419 HIS A 420 CYS A 422 ILE A 423
SITE 6 AC1 23 GLY A 424 TPF A1460 HOH A2066
SITE 1 AC2 9 TYR A 103 PHE A 110 ALA A 287 ALA A 291
SITE 2 AC2 9 THR A 295 LEU A 356 MET A 460 VAL A 461
SITE 3 AC2 9 HEM A1450
SITE 1 AC3 23 TYR B 103 TYR B 116 ARG B 124 LEU B 127
SITE 2 AC3 23 LEU B 130 LEU B 134 ALA B 288 ALA B 291
SITE 3 AC3 23 GLY B 292 THR B 295 THR B 299 PRO B 355
SITE 4 AC3 23 LEU B 356 VAL B 359 ARG B 361 GLY B 414
SITE 5 AC3 23 PHE B 415 GLY B 416 HIS B 420 CYS B 422
SITE 6 AC3 23 ILE B 423 GLY B 424 TPF B1460
SITE 1 AC4 10 TYR B 103 MET B 106 PHE B 110 ALA B 287
SITE 2 AC4 10 ALA B 291 THR B 295 LEU B 356 MET B 460
SITE 3 AC4 10 VAL B 461 HEM B1450
CRYST1 74.858 92.574 78.277 90.00 102.14 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 0.013359 0.000000 0.002874 0.00000
SCALE2 0.000000 0.010802 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013067 0.00000
MTRIX1 1 -0.999860 0.001180 0.016780 37.33375 1
MTRIX2 1 -0.001030 -0.999960 0.008960 -15.76784 1
MTRIX3 1 0.016790 0.008940 0.999820 -0.36569 1
(ATOM LINES ARE NOT SHOWN.)
END
