HEADER OXIDOREDUCTASE 24-MAR-15 4UHI
TITLE HUMAN STEROL 14-ALPHA DEMETHYLASE (CYP51) IN COMPLEX WITH VFV IN C121
TITLE 2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROL 14-ALPHA DEMETHYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 61-503;
COMPND 5 SYNONYM: LDM, CYPLI, CYTOCHROME P450 51A1, CYTOCHROME P450-14DM,
COMPND 6 CYTOCHROME P45014DM, CYTOCHROME P450LI, LANOSTEROL 14-ALPHA
COMPND 7 DEMETHYLASE, STEROL 14ALPHA DEMETHYLASE;
COMPND 8 EC: 1.14.13.70;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS OXIDOREDUCTASE, MONOOXYGENASE, STEROL BIOSYNTHESIS, EUKARYOTIC
KEYWDS 2 MEMBRANES, CYTOCHROME P450 FOLD, ENDOPLASMIC RETICULUM
EXPDTA X-RAY DIFFRACTION
AUTHOR T.Y.HARGROVE,Z.WAWRZAK,G.I LEPESHEVA
REVDAT 4 20-JUN-18 4UHI 1 REMARK LINK
REVDAT 3 10-AUG-16 4UHI 1 JRNL
REVDAT 2 29-JUN-16 4UHI 1 JRNL
REVDAT 1 08-JUN-16 4UHI 0
JRNL AUTH T.Y.HARGROVE,L.FRIGGERI,Z.WAWRZAK,S.SIVAKUMARAN,
JRNL AUTH 2 E.M.YAZLOVITSKAYA,S.W.HIEBERT,F.P.GUENGERICH,M.R.WATERMAN,
JRNL AUTH 3 G.I.LEPESHEVA
JRNL TITL HUMAN STEROL 14ALPHA-DEMETHYLASE (CYP51) AS A TARGET FOR
JRNL TITL 2 ANTICANCER CHEMOTHERAPY: TOWARDS STRUCTURE-AIDED DRUG
JRNL TITL 3 DESIGN.
JRNL REF J.LIPID RES. V. 57 1552 2016
JRNL REFN ISSN 0022-2275
JRNL PMID 27313059
JRNL DOI 10.1194/JLR.M069229
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 133884
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7049
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) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9812
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 570
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 500
REMARK 3 SOLVENT ATOMS : 654
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.69000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : -0.92000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.207
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.417
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15208 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 14272 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20672 ; 0.981 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32820 ; 0.600 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1764 ; 5.594 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 680 ;35.975 ;23.471
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2536 ;13.117 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;17.515 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2160 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17032 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3684 ; 0.002 ; 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): 7068 ; 3.766 ; 3.793
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7067 ; 3.765 ; 3.792
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8828 ; 5.080 ; 5.679
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8139 ; 4.407 ; 4.163
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 4UHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-15
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) : 0.9787
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BE LENSES DIAMOND LAUE
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140942
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 98.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
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) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER MR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.4
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 84.33150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.93450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.33150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 72.93450
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 503
REMARK 465 LYS B 503
REMARK 465 LYS C 503
REMARK 465 LYS D 503
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 OE2 GLU A 83 C SER D 414 2555 1.83
REMARK 500 OE2 GLU A 83 N TRP D 415 2555 1.86
REMARK 500 OD2 ASP D 355 OD2 ASP D 355 2554 1.93
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 CYS A 402 O - C - N ANGL. DEV. = -14.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 70 -66.16 69.10
REMARK 500 ALA A 144 -117.93 57.00
REMARK 500 GLN A 313 -74.83 -89.64
REMARK 500 LEU A 349 71.99 50.33
REMARK 500 VAL A 440 45.44 -143.91
REMARK 500 PRO A 494 49.16 -82.41
REMARK 500 PHE B 70 -65.41 69.42
REMARK 500 SER B 80 75.94 -157.42
REMARK 500 ALA B 144 -120.02 58.38
REMARK 500 ASP B 292 -34.79 -39.59
REMARK 500 GLN B 313 -73.97 -87.20
REMARK 500 LEU B 349 72.83 40.18
REMARK 500 ARG B 374 59.85 -140.36
REMARK 500 VAL B 440 44.32 -141.01
REMARK 500 PHE C 70 -60.99 69.57
REMARK 500 SER C 80 80.75 -156.80
REMARK 500 ALA C 144 -121.49 56.49
REMARK 500 PRO C 494 44.20 -79.14
REMARK 500 PHE D 70 -62.63 70.32
REMARK 500 SER D 80 79.99 -153.13
REMARK 500 ALA D 144 -113.16 59.71
REMARK 500 GLN D 313 -74.93 -94.13
REMARK 500 ARG D 374 56.62 -140.17
REMARK 500 ALA D 391 28.34 45.50
REMARK 500 VAL D 440 47.25 -146.99
REMARK 500 PRO D 494 49.46 -86.55
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 CYS A 402 12.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2076 DISTANCE = 6.35 ANGSTROMS
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 540 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 449 SG
REMARK 620 2 HEM A 540 NA 93.7
REMARK 620 3 HEM A 540 NB 85.6 89.5
REMARK 620 4 HEM A 540 NC 84.4 176.4 87.2
REMARK 620 5 HEM A 540 ND 92.0 90.9 177.6 92.3
REMARK 620 6 VFV A 580 NAX 177.7 88.4 95.4 93.6 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 540 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 449 SG
REMARK 620 2 HEM B 540 NA 91.0
REMARK 620 3 HEM B 540 NB 83.1 89.2
REMARK 620 4 HEM B 540 NC 84.8 175.5 88.7
REMARK 620 5 HEM B 540 ND 93.6 91.2 176.6 90.7
REMARK 620 6 VFV B 580 NAX 170.3 94.0 88.7 89.9 94.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 540 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 449 SG
REMARK 620 2 HEM C 540 NA 98.3
REMARK 620 3 HEM C 540 NB 84.7 88.3
REMARK 620 4 HEM C 540 NC 83.1 176.0 88.2
REMARK 620 5 HEM C 540 ND 95.4 92.1 179.6 91.5
REMARK 620 6 VFV C 580 NAX 169.5 91.8 92.6 86.7 87.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 540 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 449 SG
REMARK 620 2 HEM D 540 NA 98.1
REMARK 620 3 HEM D 540 NB 82.3 89.5
REMARK 620 4 HEM D 540 NC 81.8 176.1 86.6
REMARK 620 5 HEM D 540 ND 95.7 92.2 177.6 91.7
REMARK 620 6 VFV D 580 NAX 168.5 91.1 90.9 88.6 90.7
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 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV A 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV B 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV C 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV D 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV D 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UHL RELATED DB: PDB
REMARK 900 HUMAN STEROL 14-ALPHA DEMETHYLASE (CYP51) IN COMPLEX WITH VFV IN P1
REMARK 900 SPACE GROUP
DBREF 4UHI A 61 503 UNP Q16850 CP51A_HUMAN 61 503
DBREF 4UHI B 61 503 UNP Q16850 CP51A_HUMAN 61 503
DBREF 4UHI C 61 503 UNP Q16850 CP51A_HUMAN 61 503
DBREF 4UHI D 61 503 UNP Q16850 CP51A_HUMAN 61 503
SEQRES 1 A 443 PRO PRO TYR ILE PHE SER PRO ILE PRO PHE LEU GLY HIS
SEQRES 2 A 443 ALA ILE ALA PHE GLY LYS SER PRO ILE GLU PHE LEU GLU
SEQRES 3 A 443 ASN ALA TYR GLU LYS TYR GLY PRO VAL PHE SER PHE THR
SEQRES 4 A 443 MET VAL GLY LYS THR PHE THR TYR LEU LEU GLY SER ASP
SEQRES 5 A 443 ALA ALA ALA LEU LEU PHE ASN SER LYS ASN GLU ASP LEU
SEQRES 6 A 443 ASN ALA GLU ASP VAL TYR SER ARG LEU THR THR PRO VAL
SEQRES 7 A 443 PHE GLY LYS GLY VAL ALA TYR ASP VAL PRO ASN PRO VAL
SEQRES 8 A 443 PHE LEU GLU GLN LYS LYS MET LEU LYS SER GLY LEU ASN
SEQRES 9 A 443 ILE ALA HIS PHE LYS GLN HIS VAL SER ILE ILE GLU LYS
SEQRES 10 A 443 GLU THR LYS GLU TYR PHE GLU SER TRP GLY GLU SER GLY
SEQRES 11 A 443 GLU LYS ASN VAL PHE GLU ALA LEU SER GLU LEU ILE ILE
SEQRES 12 A 443 LEU THR ALA SER HIS CYS LEU HIS GLY LYS GLU ILE ARG
SEQRES 13 A 443 SER GLN LEU ASN GLU LYS VAL ALA GLN LEU TYR ALA ASP
SEQRES 14 A 443 LEU ASP GLY GLY PHE SER HIS ALA ALA TRP LEU LEU PRO
SEQRES 15 A 443 GLY TRP LEU PRO LEU PRO SER PHE ARG ARG ARG ASP ARG
SEQRES 16 A 443 ALA HIS ARG GLU ILE LYS ASP ILE PHE TYR LYS ALA ILE
SEQRES 17 A 443 GLN LYS ARG ARG GLN SER GLN GLU LYS ILE ASP ASP ILE
SEQRES 18 A 443 LEU GLN THR LEU LEU ASP ALA THR TYR LYS ASP GLY ARG
SEQRES 19 A 443 PRO LEU THR ASP ASP GLU VAL ALA GLY MET LEU ILE GLY
SEQRES 20 A 443 LEU LEU LEU ALA GLY GLN HIS THR SER SER THR THR SER
SEQRES 21 A 443 ALA TRP MET GLY PHE PHE LEU ALA ARG ASP LYS THR LEU
SEQRES 22 A 443 GLN LYS LYS CYS TYR LEU GLU GLN LYS THR VAL CYS GLY
SEQRES 23 A 443 GLU ASN LEU PRO PRO LEU THR TYR ASP GLN LEU LYS ASP
SEQRES 24 A 443 LEU ASN LEU LEU ASP ARG CYS ILE LYS GLU THR LEU ARG
SEQRES 25 A 443 LEU ARG PRO PRO ILE MET ILE MET MET ARG MET ALA ARG
SEQRES 26 A 443 THR PRO GLN THR VAL ALA GLY TYR THR ILE PRO PRO GLY
SEQRES 27 A 443 HIS GLN VAL CYS VAL SER PRO THR VAL ASN GLN ARG LEU
SEQRES 28 A 443 LYS ASP SER TRP VAL GLU ARG LEU ASP PHE ASN PRO ASP
SEQRES 29 A 443 ARG TYR LEU GLN ASP ASN PRO ALA SER GLY GLU LYS PHE
SEQRES 30 A 443 ALA TYR VAL PRO PHE GLY ALA GLY ARG HIS ARG CYS ILE
SEQRES 31 A 443 GLY GLU ASN PHE ALA TYR VAL GLN ILE LYS THR ILE TRP
SEQRES 32 A 443 SER THR MET LEU ARG LEU TYR GLU PHE ASP LEU ILE ASP
SEQRES 33 A 443 GLY TYR PHE PRO THR VAL ASN TYR THR THR MET ILE HIS
SEQRES 34 A 443 THR PRO GLU ASN PRO VAL ILE ARG TYR LYS ARG ARG SER
SEQRES 35 A 443 LYS
SEQRES 1 B 443 PRO PRO TYR ILE PHE SER PRO ILE PRO PHE LEU GLY HIS
SEQRES 2 B 443 ALA ILE ALA PHE GLY LYS SER PRO ILE GLU PHE LEU GLU
SEQRES 3 B 443 ASN ALA TYR GLU LYS TYR GLY PRO VAL PHE SER PHE THR
SEQRES 4 B 443 MET VAL GLY LYS THR PHE THR TYR LEU LEU GLY SER ASP
SEQRES 5 B 443 ALA ALA ALA LEU LEU PHE ASN SER LYS ASN GLU ASP LEU
SEQRES 6 B 443 ASN ALA GLU ASP VAL TYR SER ARG LEU THR THR PRO VAL
SEQRES 7 B 443 PHE GLY LYS GLY VAL ALA TYR ASP VAL PRO ASN PRO VAL
SEQRES 8 B 443 PHE LEU GLU GLN LYS LYS MET LEU LYS SER GLY LEU ASN
SEQRES 9 B 443 ILE ALA HIS PHE LYS GLN HIS VAL SER ILE ILE GLU LYS
SEQRES 10 B 443 GLU THR LYS GLU TYR PHE GLU SER TRP GLY GLU SER GLY
SEQRES 11 B 443 GLU LYS ASN VAL PHE GLU ALA LEU SER GLU LEU ILE ILE
SEQRES 12 B 443 LEU THR ALA SER HIS CYS LEU HIS GLY LYS GLU ILE ARG
SEQRES 13 B 443 SER GLN LEU ASN GLU LYS VAL ALA GLN LEU TYR ALA ASP
SEQRES 14 B 443 LEU ASP GLY GLY PHE SER HIS ALA ALA TRP LEU LEU PRO
SEQRES 15 B 443 GLY TRP LEU PRO LEU PRO SER PHE ARG ARG ARG ASP ARG
SEQRES 16 B 443 ALA HIS ARG GLU ILE LYS ASP ILE PHE TYR LYS ALA ILE
SEQRES 17 B 443 GLN LYS ARG ARG GLN SER GLN GLU LYS ILE ASP ASP ILE
SEQRES 18 B 443 LEU GLN THR LEU LEU ASP ALA THR TYR LYS ASP GLY ARG
SEQRES 19 B 443 PRO LEU THR ASP ASP GLU VAL ALA GLY MET LEU ILE GLY
SEQRES 20 B 443 LEU LEU LEU ALA GLY GLN HIS THR SER SER THR THR SER
SEQRES 21 B 443 ALA TRP MET GLY PHE PHE LEU ALA ARG ASP LYS THR LEU
SEQRES 22 B 443 GLN LYS LYS CYS TYR LEU GLU GLN LYS THR VAL CYS GLY
SEQRES 23 B 443 GLU ASN LEU PRO PRO LEU THR TYR ASP GLN LEU LYS ASP
SEQRES 24 B 443 LEU ASN LEU LEU ASP ARG CYS ILE LYS GLU THR LEU ARG
SEQRES 25 B 443 LEU ARG PRO PRO ILE MET ILE MET MET ARG MET ALA ARG
SEQRES 26 B 443 THR PRO GLN THR VAL ALA GLY TYR THR ILE PRO PRO GLY
SEQRES 27 B 443 HIS GLN VAL CYS VAL SER PRO THR VAL ASN GLN ARG LEU
SEQRES 28 B 443 LYS ASP SER TRP VAL GLU ARG LEU ASP PHE ASN PRO ASP
SEQRES 29 B 443 ARG TYR LEU GLN ASP ASN PRO ALA SER GLY GLU LYS PHE
SEQRES 30 B 443 ALA TYR VAL PRO PHE GLY ALA GLY ARG HIS ARG CYS ILE
SEQRES 31 B 443 GLY GLU ASN PHE ALA TYR VAL GLN ILE LYS THR ILE TRP
SEQRES 32 B 443 SER THR MET LEU ARG LEU TYR GLU PHE ASP LEU ILE ASP
SEQRES 33 B 443 GLY TYR PHE PRO THR VAL ASN TYR THR THR MET ILE HIS
SEQRES 34 B 443 THR PRO GLU ASN PRO VAL ILE ARG TYR LYS ARG ARG SER
SEQRES 35 B 443 LYS
SEQRES 1 C 443 PRO PRO TYR ILE PHE SER PRO ILE PRO PHE LEU GLY HIS
SEQRES 2 C 443 ALA ILE ALA PHE GLY LYS SER PRO ILE GLU PHE LEU GLU
SEQRES 3 C 443 ASN ALA TYR GLU LYS TYR GLY PRO VAL PHE SER PHE THR
SEQRES 4 C 443 MET VAL GLY LYS THR PHE THR TYR LEU LEU GLY SER ASP
SEQRES 5 C 443 ALA ALA ALA LEU LEU PHE ASN SER LYS ASN GLU ASP LEU
SEQRES 6 C 443 ASN ALA GLU ASP VAL TYR SER ARG LEU THR THR PRO VAL
SEQRES 7 C 443 PHE GLY LYS GLY VAL ALA TYR ASP VAL PRO ASN PRO VAL
SEQRES 8 C 443 PHE LEU GLU GLN LYS LYS MET LEU LYS SER GLY LEU ASN
SEQRES 9 C 443 ILE ALA HIS PHE LYS GLN HIS VAL SER ILE ILE GLU LYS
SEQRES 10 C 443 GLU THR LYS GLU TYR PHE GLU SER TRP GLY GLU SER GLY
SEQRES 11 C 443 GLU LYS ASN VAL PHE GLU ALA LEU SER GLU LEU ILE ILE
SEQRES 12 C 443 LEU THR ALA SER HIS CYS LEU HIS GLY LYS GLU ILE ARG
SEQRES 13 C 443 SER GLN LEU ASN GLU LYS VAL ALA GLN LEU TYR ALA ASP
SEQRES 14 C 443 LEU ASP GLY GLY PHE SER HIS ALA ALA TRP LEU LEU PRO
SEQRES 15 C 443 GLY TRP LEU PRO LEU PRO SER PHE ARG ARG ARG ASP ARG
SEQRES 16 C 443 ALA HIS ARG GLU ILE LYS ASP ILE PHE TYR LYS ALA ILE
SEQRES 17 C 443 GLN LYS ARG ARG GLN SER GLN GLU LYS ILE ASP ASP ILE
SEQRES 18 C 443 LEU GLN THR LEU LEU ASP ALA THR TYR LYS ASP GLY ARG
SEQRES 19 C 443 PRO LEU THR ASP ASP GLU VAL ALA GLY MET LEU ILE GLY
SEQRES 20 C 443 LEU LEU LEU ALA GLY GLN HIS THR SER SER THR THR SER
SEQRES 21 C 443 ALA TRP MET GLY PHE PHE LEU ALA ARG ASP LYS THR LEU
SEQRES 22 C 443 GLN LYS LYS CYS TYR LEU GLU GLN LYS THR VAL CYS GLY
SEQRES 23 C 443 GLU ASN LEU PRO PRO LEU THR TYR ASP GLN LEU LYS ASP
SEQRES 24 C 443 LEU ASN LEU LEU ASP ARG CYS ILE LYS GLU THR LEU ARG
SEQRES 25 C 443 LEU ARG PRO PRO ILE MET ILE MET MET ARG MET ALA ARG
SEQRES 26 C 443 THR PRO GLN THR VAL ALA GLY TYR THR ILE PRO PRO GLY
SEQRES 27 C 443 HIS GLN VAL CYS VAL SER PRO THR VAL ASN GLN ARG LEU
SEQRES 28 C 443 LYS ASP SER TRP VAL GLU ARG LEU ASP PHE ASN PRO ASP
SEQRES 29 C 443 ARG TYR LEU GLN ASP ASN PRO ALA SER GLY GLU LYS PHE
SEQRES 30 C 443 ALA TYR VAL PRO PHE GLY ALA GLY ARG HIS ARG CYS ILE
SEQRES 31 C 443 GLY GLU ASN PHE ALA TYR VAL GLN ILE LYS THR ILE TRP
SEQRES 32 C 443 SER THR MET LEU ARG LEU TYR GLU PHE ASP LEU ILE ASP
SEQRES 33 C 443 GLY TYR PHE PRO THR VAL ASN TYR THR THR MET ILE HIS
SEQRES 34 C 443 THR PRO GLU ASN PRO VAL ILE ARG TYR LYS ARG ARG SER
SEQRES 35 C 443 LYS
SEQRES 1 D 443 PRO PRO TYR ILE PHE SER PRO ILE PRO PHE LEU GLY HIS
SEQRES 2 D 443 ALA ILE ALA PHE GLY LYS SER PRO ILE GLU PHE LEU GLU
SEQRES 3 D 443 ASN ALA TYR GLU LYS TYR GLY PRO VAL PHE SER PHE THR
SEQRES 4 D 443 MET VAL GLY LYS THR PHE THR TYR LEU LEU GLY SER ASP
SEQRES 5 D 443 ALA ALA ALA LEU LEU PHE ASN SER LYS ASN GLU ASP LEU
SEQRES 6 D 443 ASN ALA GLU ASP VAL TYR SER ARG LEU THR THR PRO VAL
SEQRES 7 D 443 PHE GLY LYS GLY VAL ALA TYR ASP VAL PRO ASN PRO VAL
SEQRES 8 D 443 PHE LEU GLU GLN LYS LYS MET LEU LYS SER GLY LEU ASN
SEQRES 9 D 443 ILE ALA HIS PHE LYS GLN HIS VAL SER ILE ILE GLU LYS
SEQRES 10 D 443 GLU THR LYS GLU TYR PHE GLU SER TRP GLY GLU SER GLY
SEQRES 11 D 443 GLU LYS ASN VAL PHE GLU ALA LEU SER GLU LEU ILE ILE
SEQRES 12 D 443 LEU THR ALA SER HIS CYS LEU HIS GLY LYS GLU ILE ARG
SEQRES 13 D 443 SER GLN LEU ASN GLU LYS VAL ALA GLN LEU TYR ALA ASP
SEQRES 14 D 443 LEU ASP GLY GLY PHE SER HIS ALA ALA TRP LEU LEU PRO
SEQRES 15 D 443 GLY TRP LEU PRO LEU PRO SER PHE ARG ARG ARG ASP ARG
SEQRES 16 D 443 ALA HIS ARG GLU ILE LYS ASP ILE PHE TYR LYS ALA ILE
SEQRES 17 D 443 GLN LYS ARG ARG GLN SER GLN GLU LYS ILE ASP ASP ILE
SEQRES 18 D 443 LEU GLN THR LEU LEU ASP ALA THR TYR LYS ASP GLY ARG
SEQRES 19 D 443 PRO LEU THR ASP ASP GLU VAL ALA GLY MET LEU ILE GLY
SEQRES 20 D 443 LEU LEU LEU ALA GLY GLN HIS THR SER SER THR THR SER
SEQRES 21 D 443 ALA TRP MET GLY PHE PHE LEU ALA ARG ASP LYS THR LEU
SEQRES 22 D 443 GLN LYS LYS CYS TYR LEU GLU GLN LYS THR VAL CYS GLY
SEQRES 23 D 443 GLU ASN LEU PRO PRO LEU THR TYR ASP GLN LEU LYS ASP
SEQRES 24 D 443 LEU ASN LEU LEU ASP ARG CYS ILE LYS GLU THR LEU ARG
SEQRES 25 D 443 LEU ARG PRO PRO ILE MET ILE MET MET ARG MET ALA ARG
SEQRES 26 D 443 THR PRO GLN THR VAL ALA GLY TYR THR ILE PRO PRO GLY
SEQRES 27 D 443 HIS GLN VAL CYS VAL SER PRO THR VAL ASN GLN ARG LEU
SEQRES 28 D 443 LYS ASP SER TRP VAL GLU ARG LEU ASP PHE ASN PRO ASP
SEQRES 29 D 443 ARG TYR LEU GLN ASP ASN PRO ALA SER GLY GLU LYS PHE
SEQRES 30 D 443 ALA TYR VAL PRO PHE GLY ALA GLY ARG HIS ARG CYS ILE
SEQRES 31 D 443 GLY GLU ASN PHE ALA TYR VAL GLN ILE LYS THR ILE TRP
SEQRES 32 D 443 SER THR MET LEU ARG LEU TYR GLU PHE ASP LEU ILE ASP
SEQRES 33 D 443 GLY TYR PHE PRO THR VAL ASN TYR THR THR MET ILE HIS
SEQRES 34 D 443 THR PRO GLU ASN PRO VAL ILE ARG TYR LYS ARG ARG SER
SEQRES 35 D 443 LYS
HET HEM A 540 43
HET VFV A 580 41
HET VFV A 600 41
HET HEM B 540 43
HET VFV B 580 41
HET VFV B 600 41
HET HEM C 540 43
HET VFV C 580 41
HET VFV C 600 41
HET HEM D 540 43
HET VFV D 580 41
HET VFV D 600 41
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM VFV N-[(1R)-1-(3,4'-DIFLUOROBIPHENYL-4-YL)-2-(1H-IMIDAZOL-
HETNAM 2 VFV 1-YL)ETHYL]-4-(5-PHENYL-1,3,4-OXADIAZOL-2-YL)BENZAMIDE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 VFV 8(C32 H23 F2 N5 O2)
FORMUL 17 HOH *654(H2 O)
HELIX 1 1 HIS A 73 SER A 80 1 8
HELIX 2 2 SER A 80 GLY A 93 1 14
HELIX 3 3 GLY A 110 SER A 120 1 11
HELIX 4 4 ALA A 127 GLY A 140 1 14
HELIX 5 5 VAL A 143 VAL A 147 5 5
HELIX 6 6 PRO A 148 LEU A 163 1 16
HELIX 7 7 ASN A 164 SER A 185 1 22
HELIX 8 8 VAL A 194 GLY A 212 1 19
HELIX 9 9 GLY A 212 GLN A 218 1 7
HELIX 10 10 ASN A 220 GLY A 232 1 13
HELIX 11 11 SER A 235 LEU A 241 1 7
HELIX 12 12 LEU A 247 SER A 274 1 28
HELIX 13 13 ASP A 280 ALA A 288 1 9
HELIX 14 14 THR A 297 GLY A 346 1 50
HELIX 15 15 THR A 353 LYS A 358 1 6
HELIX 16 16 LEU A 360 ARG A 374 1 15
HELIX 17 17 SER A 404 GLN A 409 1 6
HELIX 18 18 ASN A 422 GLN A 428 5 7
HELIX 19 19 ASN A 430 GLU A 435 1 6
HELIX 20 20 ALA A 444 ARG A 448 5 5
HELIX 21 21 GLY A 451 LEU A 469 1 19
HELIX 22 22 HIS B 73 SER B 80 1 8
HELIX 23 23 SER B 80 GLY B 93 1 14
HELIX 24 24 GLY B 110 SER B 120 1 11
HELIX 25 25 ALA B 127 GLY B 140 1 14
HELIX 26 26 VAL B 143 VAL B 147 5 5
HELIX 27 27 PRO B 148 LEU B 163 1 16
HELIX 28 28 ASN B 164 GLU B 184 1 21
HELIX 29 29 SER B 185 GLY B 187 5 3
HELIX 30 30 VAL B 194 GLY B 212 1 19
HELIX 31 31 GLY B 212 GLN B 218 1 7
HELIX 32 32 ASN B 220 GLY B 232 1 13
HELIX 33 33 SER B 235 LEU B 241 1 7
HELIX 34 34 LEU B 247 GLN B 273 1 27
HELIX 35 35 ASP B 280 ASP B 287 1 8
HELIX 36 36 THR B 297 GLY B 346 1 50
HELIX 37 37 THR B 353 LEU B 360 1 8
HELIX 38 38 LEU B 360 ARG B 374 1 15
HELIX 39 39 SER B 404 GLN B 409 1 6
HELIX 40 40 ASN B 422 GLN B 428 5 7
HELIX 41 41 ASN B 430 GLU B 435 1 6
HELIX 42 42 ALA B 444 ARG B 448 5 5
HELIX 43 43 GLY B 451 LEU B 469 1 19
HELIX 44 44 HIS C 73 SER C 80 1 8
HELIX 45 45 SER C 80 GLY C 93 1 14
HELIX 46 46 GLY C 110 SER C 120 1 11
HELIX 47 47 ALA C 127 GLY C 140 1 14
HELIX 48 48 VAL C 143 VAL C 147 5 5
HELIX 49 49 PRO C 148 LEU C 163 1 16
HELIX 50 50 ASN C 164 GLU C 184 1 21
HELIX 51 51 SER C 185 GLY C 187 5 3
HELIX 52 52 VAL C 194 HIS C 211 1 18
HELIX 53 53 GLY C 212 GLN C 218 1 7
HELIX 54 54 ASN C 220 GLY C 232 1 13
HELIX 55 55 SER C 235 LEU C 241 1 7
HELIX 56 56 LEU C 247 SER C 274 1 28
HELIX 57 57 ASP C 280 ASP C 287 1 8
HELIX 58 58 THR C 297 ASP C 330 1 34
HELIX 59 59 ASP C 330 GLY C 346 1 17
HELIX 60 60 THR C 353 ASP C 359 1 7
HELIX 61 61 LEU C 360 ARG C 374 1 15
HELIX 62 62 SER C 404 GLN C 409 1 6
HELIX 63 63 ASN C 422 GLN C 428 5 7
HELIX 64 64 ASN C 430 GLU C 435 1 6
HELIX 65 65 ALA C 444 ARG C 448 5 5
HELIX 66 66 GLY C 451 LEU C 469 1 19
HELIX 67 67 HIS D 73 SER D 80 1 8
HELIX 68 68 SER D 80 GLY D 93 1 14
HELIX 69 69 GLY D 110 SER D 120 1 11
HELIX 70 70 ALA D 127 GLY D 140 1 14
HELIX 71 71 VAL D 143 VAL D 147 5 5
HELIX 72 72 PRO D 148 LEU D 163 1 16
HELIX 73 73 ASN D 164 PHE D 183 1 20
HELIX 74 74 GLU D 184 GLY D 187 5 4
HELIX 75 75 VAL D 194 HIS D 211 1 18
HELIX 76 76 GLY D 212 GLN D 218 1 7
HELIX 77 77 ASN D 220 GLY D 232 1 13
HELIX 78 78 SER D 235 LEU D 241 1 7
HELIX 79 79 LEU D 247 SER D 274 1 28
HELIX 80 80 ASP D 280 ALA D 288 1 9
HELIX 81 81 THR D 297 GLY D 346 1 50
HELIX 82 82 THR D 353 ASP D 359 1 7
HELIX 83 83 LEU D 360 ARG D 374 1 15
HELIX 84 84 SER D 404 GLN D 409 1 6
HELIX 85 85 ASN D 422 GLN D 428 5 7
HELIX 86 86 ASN D 430 GLU D 435 1 6
HELIX 87 87 ALA D 444 ARG D 448 5 5
HELIX 88 88 GLY D 451 LEU D 469 1 19
SHEET 1 AA 5 VAL A 95 MET A 100 0
SHEET 2 AA 5 LYS A 103 LEU A 108 -1 O LYS A 103 N MET A 100
SHEET 3 AA 5 GLN A 400 VAL A 403 1 O GLN A 400 N THR A 106
SHEET 4 AA 5 MET A 380 ALA A 384 -1 O MET A 380 N VAL A 403
SHEET 5 AA 5 LEU A 125 ASN A 126 -1 O ASN A 126 N MET A 383
SHEET 1 AB 3 SER A 189 ASN A 193 0
SHEET 2 AB 3 VAL A 495 ARG A 500 -1 O ILE A 496 N LYS A 192
SHEET 3 AB 3 TYR A 470 ASP A 473 -1 O GLU A 471 N LYS A 499
SHEET 1 AC 2 GLN A 388 VAL A 390 0
SHEET 2 AC 2 TYR A 393 ILE A 395 -1 O TYR A 393 N VAL A 390
SHEET 1 AD 2 VAL A 482 ASN A 483 0
SHEET 2 AD 2 THR A 490 PRO A 491 -1 O THR A 490 N ASN A 483
SHEET 1 BA 6 TYR B 63 ILE B 64 0
SHEET 2 BA 6 VAL B 95 MET B 100 1 O SER B 97 N ILE B 64
SHEET 3 BA 6 LYS B 103 LEU B 108 -1 O LYS B 103 N MET B 100
SHEET 4 BA 6 GLN B 400 VAL B 403 1 O GLN B 400 N THR B 106
SHEET 5 BA 6 MET B 380 ALA B 384 -1 O MET B 380 N VAL B 403
SHEET 6 BA 6 LEU B 125 ASN B 126 -1 O ASN B 126 N MET B 383
SHEET 1 BB 3 SER B 189 ASN B 193 0
SHEET 2 BB 3 VAL B 495 ARG B 500 -1 O ILE B 496 N LYS B 192
SHEET 3 BB 3 TYR B 470 ASP B 473 -1 O GLU B 471 N LYS B 499
SHEET 1 BC 2 GLN B 388 VAL B 390 0
SHEET 2 BC 2 TYR B 393 ILE B 395 -1 O TYR B 393 N VAL B 390
SHEET 1 BD 2 VAL B 482 ASN B 483 0
SHEET 2 BD 2 THR B 490 PRO B 491 -1 O THR B 490 N ASN B 483
SHEET 1 CA 5 VAL C 95 MET C 100 0
SHEET 2 CA 5 LYS C 103 LEU C 108 -1 O LYS C 103 N MET C 100
SHEET 3 CA 5 GLN C 400 VAL C 403 1 O GLN C 400 N THR C 106
SHEET 4 CA 5 MET C 380 ALA C 384 -1 O MET C 380 N VAL C 403
SHEET 5 CA 5 LEU C 125 ASN C 126 -1 O ASN C 126 N MET C 383
SHEET 1 CB 3 SER C 189 ASN C 193 0
SHEET 2 CB 3 VAL C 495 ARG C 500 -1 O ILE C 496 N LYS C 192
SHEET 3 CB 3 TYR C 470 ASP C 473 -1 O GLU C 471 N LYS C 499
SHEET 1 CC 2 GLN C 388 VAL C 390 0
SHEET 2 CC 2 TYR C 393 ILE C 395 -1 O TYR C 393 N VAL C 390
SHEET 1 CD 2 VAL C 482 ASN C 483 0
SHEET 2 CD 2 THR C 490 PRO C 491 -1 O THR C 490 N ASN C 483
SHEET 1 DA 5 VAL D 95 MET D 100 0
SHEET 2 DA 5 LYS D 103 LEU D 108 -1 O LYS D 103 N MET D 100
SHEET 3 DA 5 GLN D 400 VAL D 403 1 O GLN D 400 N THR D 106
SHEET 4 DA 5 MET D 380 ALA D 384 -1 O MET D 380 N VAL D 403
SHEET 5 DA 5 LEU D 125 ASN D 126 -1 O ASN D 126 N MET D 383
SHEET 1 DB 3 SER D 189 ASN D 193 0
SHEET 2 DB 3 VAL D 495 ARG D 500 -1 O ILE D 496 N LYS D 192
SHEET 3 DB 3 TYR D 470 ASP D 473 -1 O GLU D 471 N LYS D 499
SHEET 1 DC 2 GLN D 388 VAL D 390 0
SHEET 2 DC 2 TYR D 393 ILE D 395 -1 O TYR D 393 N VAL D 390
SHEET 1 DD 2 VAL D 482 ASN D 483 0
SHEET 2 DD 2 THR D 490 PRO D 491 -1 O THR D 490 N ASN D 483
LINK SG CYS A 449 FE HEM A 540 1555 1555 2.31
LINK SG CYS B 449 FE HEM B 540 1555 1555 2.27
LINK SG CYS C 449 FE HEM C 540 1555 1555 2.22
LINK SG CYS D 449 FE HEM D 540 1555 1555 2.30
LINK FE HEM A 540 NAX VFV A 580 1555 1555 2.04
LINK FE HEM B 540 NAX VFV B 580 1555 1555 2.05
LINK FE HEM C 540 NAX VFV C 580 1555 1555 2.07
LINK FE HEM D 540 NAX VFV D 580 1555 1555 2.06
SITE 1 AC1 19 TYR A 145 PHE A 152 LYS A 156 ALA A 311
SITE 2 AC1 19 THR A 315 PRO A 376 ILE A 377 MET A 380
SITE 3 AC1 19 ARG A 382 PRO A 441 PHE A 442 GLY A 443
SITE 4 AC1 19 HIS A 447 CYS A 449 ILE A 450 GLY A 451
SITE 5 AC1 19 ALA A 455 VFV A 580 HOH A2203
SITE 1 AC2 17 TYR A 131 LEU A 134 THR A 135 PHE A 139
SITE 2 AC2 17 PHE A 152 LEU A 159 PHE A 234 TRP A 239
SITE 3 AC2 17 MET A 304 GLY A 307 LEU A 308 LEU A 310
SITE 4 AC2 17 ALA A 311 ILE A 377 MET A 487 HEM A 540
SITE 5 AC2 17 VFV A 600
SITE 1 AC3 15 PHE A 77 MET A 100 VAL A 101 PHE A 105
SITE 2 AC3 15 TYR A 107 HIS A 236 TRP A 239 ILE A 379
SITE 3 AC3 15 MET A 381 VFV A 580 HOH A2117 HOH A2222
SITE 4 AC3 15 LEU B 245 PRO B 246 LEU B 247
SITE 1 AC4 17 TYR B 145 PHE B 152 LYS B 156 ALA B 311
SITE 2 AC4 17 THR B 315 PRO B 376 ILE B 377 MET B 380
SITE 3 AC4 17 ARG B 382 PRO B 441 PHE B 442 GLY B 443
SITE 4 AC4 17 HIS B 447 CYS B 449 GLY B 451 VFV B 580
SITE 5 AC4 17 HOH B2047
SITE 1 AC5 18 TYR B 131 LEU B 134 PHE B 139 ALA B 144
SITE 2 AC5 18 LEU B 159 PHE B 234 SER B 235 HIS B 236
SITE 3 AC5 18 TRP B 239 MET B 304 GLY B 307 LEU B 308
SITE 4 AC5 18 ALA B 311 THR B 315 ILE B 377 HEM B 540
SITE 5 AC5 18 VFV B 600 HOH B2040
SITE 1 AC6 16 LEU A 245 PRO A 246 LEU A 247 PHE B 77
SITE 2 AC6 16 MET B 100 VAL B 101 PHE B 105 TYR B 107
SITE 3 AC6 16 HIS B 236 TRP B 239 ILE B 379 MET B 381
SITE 4 AC6 16 VFV B 580 HOH B2092 HOH B2179 HOH B2180
SITE 1 AC7 20 TYR C 145 PHE C 152 LYS C 156 ALA C 311
SITE 2 AC7 20 THR C 315 PRO C 376 ILE C 377 MET C 380
SITE 3 AC7 20 ARG C 382 PRO C 441 PHE C 442 GLY C 443
SITE 4 AC7 20 HIS C 447 CYS C 449 ILE C 450 GLY C 451
SITE 5 AC7 20 ALA C 455 VFV C 580 HOH C2028 HOH C2115
SITE 1 AC8 16 TYR C 131 LEU C 134 PHE C 139 ALA C 144
SITE 2 AC8 16 PHE C 152 LEU C 159 PHE C 234 TRP C 239
SITE 3 AC8 16 MET C 304 GLY C 307 LEU C 310 ALA C 311
SITE 4 AC8 16 THR C 315 ILE C 377 HEM C 540 VFV C 600
SITE 1 AC9 14 PHE C 77 MET C 100 VAL C 101 PHE C 105
SITE 2 AC9 14 TYR C 107 HIS C 236 TRP C 239 ILE C 379
SITE 3 AC9 14 MET C 381 ILE C 488 VFV C 580 HOH C2131
SITE 4 AC9 14 PRO D 246 LEU D 247
SITE 1 BC1 19 TYR D 145 PHE D 152 LYS D 156 ALA D 311
SITE 2 BC1 19 GLY D 312 THR D 315 PRO D 376 ILE D 377
SITE 3 BC1 19 MET D 380 ARG D 382 PRO D 441 PHE D 442
SITE 4 BC1 19 GLY D 443 HIS D 447 CYS D 449 ILE D 450
SITE 5 BC1 19 GLY D 451 ALA D 455 VFV D 580
SITE 1 BC2 14 LEU D 134 PHE D 139 LEU D 159 PHE D 234
SITE 2 BC2 14 TRP D 239 MET D 304 GLY D 307 LEU D 308
SITE 3 BC2 14 LEU D 310 ALA D 311 ILE D 377 HEM D 540
SITE 4 BC2 14 VFV D 600 HOH D2120
SITE 1 BC3 16 LEU C 245 PRO C 246 LEU C 247 PHE D 77
SITE 2 BC3 16 MET D 100 VAL D 101 PHE D 105 TYR D 107
SITE 3 BC3 16 HIS D 236 TRP D 239 LEU D 240 ILE D 379
SITE 4 BC3 16 MET D 381 ILE D 488 VFV D 580 HOH D2121
CRYST1 168.663 145.869 115.987 90.00 127.15 90.00 C 1 2 1 16
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 0.005929 0.000000 0.004492 0.00000
SCALE2 0.000000 0.006855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
