HEADER OXIDOREDUCTASE 08-MAY-09 2WI9
TITLE SELECTIVE OXIDATION OF CARBOLIDE C-H BONDS BY ENGINEERED MACROLIDE
TITLE 2 P450 MONOOXYGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 HYDROXYLASE PIKC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PIKC;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_TAXID: 54571;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ANTIBIOTIC BIOSYNTHESIS, CYP107L1, CYTOCHROME P450, HEME, IRON,
KEYWDS 2 MACROLIDE MONOOXYGENASE, METAL-BINDING, MONOOXYGENASE,
KEYWDS 3 OXIDOREDUCTASE, OXIDOREDUCTASE ANTIBIOTIC BIOSYNTHESIS, PIKC
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LI,M.R.CHAULAGAIN,A.R.KNAUFF,L.M.PODUST,J.MONTGOMERY,D.H.SHERMAN
REVDAT 3 13-DEC-23 2WI9 1 REMARK LINK
REVDAT 2 24-NOV-09 2WI9 1 JRNL REMARK
REVDAT 1 27-OCT-09 2WI9 0
JRNL AUTH S.LI,M.R.CHAULAGAIN,A.R.KNAUFF,L.M.PODUST,J.MONTGOMERY,
JRNL AUTH 2 D.H.SHERMAN
JRNL TITL SELECTIVE OXIDATION OF CARBOLIDE C-H BONDS BY AN ENGINEERED
JRNL TITL 2 MACROLIDE P450 MONO-OXYGENASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 18463 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19833867
JRNL DOI 10.1073/PNAS.0907203106
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 88.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 60321
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6789
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3744
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 400
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 576
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.32000
REMARK 3 B22 (A**2) : 1.65000
REMARK 3 B33 (A**2) : -1.34000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.931
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6578 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9018 ; 1.983 ; 2.031
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 817 ; 5.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 288 ;30.970 ;22.153
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1002 ;15.112 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;19.521 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 999 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5079 ; 0.011 ; 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): 4051 ; 1.213 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6523 ; 2.061 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2527 ; 3.222 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2493 ; 4.973 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2WI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1290039763.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
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) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68456
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 87.70
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 2C6H
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.1 M TRIS-HCL, PH 7.5;
REMARK 280 200 MM MGCL2
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 30.12700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.62200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.54700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.62200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.12700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.54700
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASP 50 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASP 50 TO ASN
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ALA A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 GLN A 5
REMARK 465 GLN A 6
REMARK 465 GLY A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 GLY A 408
REMARK 465 ARG A 409
REMARK 465 GLU A 410
REMARK 465 ALA A 411
REMARK 465 GLY A 412
REMARK 465 ARG A 413
REMARK 465 ARG A 414
REMARK 465 THR A 415
REMARK 465 GLY A 416
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ALA B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ARG B 3
REMARK 465 THR B 4
REMARK 465 GLN B 5
REMARK 465 GLN B 6
REMARK 465 GLY B 7
REMARK 465 THR B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 PRO B 12
REMARK 465 PRO B 13
REMARK 465 GLY B 408
REMARK 465 ARG B 409
REMARK 465 GLU B 410
REMARK 465 ALA B 411
REMARK 465 GLY B 412
REMARK 465 ARG B 413
REMARK 465 ARG B 414
REMARK 465 THR B 415
REMARK 465 GLY B 416
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 12 CG CD
REMARK 470 LEU A 15 CG CD1 CD2
REMARK 470 GLN A 22 CG CD OE1 NE2
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ASP A 182 CG OD1 OD2
REMARK 470 GLU A 246 CG CD OE1 OE2
REMARK 470 ARG A 406 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 407 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 20 CG CD1 CD2
REMARK 470 GLN B 22 CG CD OE1 NE2
REMARK 470 ASP B 305 CG OD1 OD2
REMARK 470 GLU B 386 CG CD OE1 OE2
REMARK 470 ARG B 404 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 407 CG CD NE CZ NH1 NH2
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 ARG A 34 O HOH A 2011 1.77
REMARK 500 O HOH B 2039 O HOH B 2256 1.85
REMARK 500 NH2 ARG B 200 O HOH B 2150 1.91
REMARK 500 NH1 ARG A 324 O HOH A 2251 1.93
REMARK 500 O2 1D2 B 1409 O HOH B 2277 1.95
REMARK 500 NE ARG B 200 O HOH B 2150 1.96
REMARK 500 O HOH B 2130 O HOH B 2264 1.99
REMARK 500 O HOH B 2021 O HOH B 2082 2.05
REMARK 500 O HOH A 2286 O HOH A 2287 2.05
REMARK 500 O HOH B 2021 O HOH B 2083 2.05
REMARK 500 OD1 ASP A 203 O HOH A 2171 2.09
REMARK 500 O HOH B 2182 O HOH B 2183 2.13
REMARK 500 ND1 HIS B 238 O HOH B 2197 2.14
REMARK 500 NH1 ARG A 115 O HOH A 2117 2.16
REMARK 500 O ASP A 27 O HOH A 2005 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2035 O HOH A 2209 4456 2.09
REMARK 500 O HOH A 2202 O HOH A 2266 4556 2.11
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 GLU A 211 CG GLU A 211 CD 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 67 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG B 99 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 99 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 285 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 285 NE - CZ - NH2 ANGL. DEV. = -7.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 13 -174.89 -55.13
REMARK 500 GLN A 22 -85.29 -159.33
REMARK 500 ASP A 23 -62.74 85.37
REMARK 500 GLU A 94 42.35 -109.52
REMARK 500 GLU A 94 47.92 -109.52
REMARK 500 LEU A 148 -51.58 -145.24
REMARK 500 ALA A 170 -37.14 -36.71
REMARK 500 ASP A 176 18.95 -58.24
REMARK 500 ALA A 177 -58.46 -137.66
REMARK 500 PHE A 178 -76.50 -54.77
REMARK 500 PHE A 178 -80.45 -51.07
REMARK 500 PRO A 181 -144.03 -66.05
REMARK 500 ASP A 182 5.13 173.17
REMARK 500 ASP A 183 122.01 170.63
REMARK 500 ASP A 272 87.66 -150.56
REMARK 500 GLU A 287 55.81 -145.48
REMARK 500 HIS A 349 132.44 -173.43
REMARK 500 GLU B 94 40.74 -105.22
REMARK 500 LEU B 148 -56.39 -139.15
REMARK 500 HIS B 349 136.70 -173.12
REMARK 500 CYS B 354 116.57 -36.88
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 A1408 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 354 SG
REMARK 620 2 HEM A1408 NA 103.4
REMARK 620 3 HEM A1408 NB 90.8 92.5
REMARK 620 4 HEM A1408 NC 92.4 164.2 87.1
REMARK 620 5 HEM A1408 ND 103.5 86.5 165.5 89.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1408 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 354 SG
REMARK 620 2 HEM B1408 NA 103.1
REMARK 620 3 HEM B1408 NB 92.5 90.5
REMARK 620 4 HEM B1408 NC 93.9 163.0 88.4
REMARK 620 5 HEM B1408 ND 105.7 86.0 161.8 89.8
REMARK 620 N 1 2 3 4
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 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1D2 A 1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1D2 B 1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CD8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2CA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2BVJ RELATED DB: PDB
REMARK 900 LIGAND-FREE STRUCTURE OF CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2C7X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC
REMARK 900 (CYP107L1)
REMARK 900 RELATED ID: 2VZM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NARBOMYCIN-BOUND PIKC D50N MUTANT
REMARK 900 RELATED ID: 2C6H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2VZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YC-17-BOUND PIKC D50N MUTANT
REMARK 900 RELATED ID: 2WHW RELATED DB: PDB
REMARK 900 SELECTIVE OXIDATION OF CARBOLIDE C-H BONDS BY ENGINEERED MACROLIDE
REMARK 900 P450 MONOOXYGENASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 20 N-TERMINAL RESIDUES INCLUDING 6XHIS TAG ARE ENGINEERED
DBREF 2WI9 A -19 0 PDB 2WI9 2WI9 -19 0
DBREF 2WI9 A 1 416 UNP O87605 O87605_9ACTO 1 416
DBREF 2WI9 B -19 0 PDB 2WI9 2WI9 -19 0
DBREF 2WI9 B 1 416 UNP O87605 O87605_9ACTO 1 416
SEQADV 2WI9 ASN A 50 UNP O87605 ASP 50 ENGINEERED MUTATION
SEQADV 2WI9 ASN B 50 UNP O87605 ASP 50 ENGINEERED MUTATION
SEQRES 1 A 436 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 436 LEU VAL PRO ALA GLY SER HIS MET ARG ARG THR GLN GLN
SEQRES 3 A 436 GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA
SEQRES 4 A 436 LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR
SEQRES 5 A 436 ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG
SEQRES 6 A 436 THR PRO GLU GLY ASN GLU VAL TRP LEU VAL VAL GLY TYR
SEQRES 7 A 436 ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER
SEQRES 8 A 436 LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA
SEQRES 9 A 436 GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO
SEQRES 10 A 436 PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU
SEQRES 11 A 436 PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL
SEQRES 12 A 436 GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA
SEQRES 13 A 436 ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA
SEQRES 14 A 436 TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY
SEQRES 15 A 436 VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR
SEQRES 16 A 436 ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN
SEQRES 17 A 436 THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU
SEQRES 18 A 436 ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU
SEQRES 19 A 436 SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG
SEQRES 20 A 436 LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU
SEQRES 21 A 436 LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA
SEQRES 22 A 436 ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU
SEQRES 23 A 436 ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA
SEQRES 24 A 436 VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER
SEQRES 25 A 436 ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP
SEQRES 26 A 436 GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL
SEQRES 27 A 436 LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP
SEQRES 28 A 436 PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS
SEQRES 29 A 436 LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA
SEQRES 30 A 436 PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA
SEQRES 31 A 436 LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER
SEQRES 32 A 436 PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG
SEQRES 33 A 436 GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG
SEQRES 34 A 436 GLU ALA GLY ARG ARG THR GLY
SEQRES 1 B 436 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 436 LEU VAL PRO ALA GLY SER HIS MET ARG ARG THR GLN GLN
SEQRES 3 B 436 GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA
SEQRES 4 B 436 LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR
SEQRES 5 B 436 ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG
SEQRES 6 B 436 THR PRO GLU GLY ASN GLU VAL TRP LEU VAL VAL GLY TYR
SEQRES 7 B 436 ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER
SEQRES 8 B 436 LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA
SEQRES 9 B 436 GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO
SEQRES 10 B 436 PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU
SEQRES 11 B 436 PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL
SEQRES 12 B 436 GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA
SEQRES 13 B 436 ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA
SEQRES 14 B 436 TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY
SEQRES 15 B 436 VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR
SEQRES 16 B 436 ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN
SEQRES 17 B 436 THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU
SEQRES 18 B 436 ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU
SEQRES 19 B 436 SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG
SEQRES 20 B 436 LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU
SEQRES 21 B 436 LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA
SEQRES 22 B 436 ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU
SEQRES 23 B 436 ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA
SEQRES 24 B 436 VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER
SEQRES 25 B 436 ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP
SEQRES 26 B 436 GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL
SEQRES 27 B 436 LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP
SEQRES 28 B 436 PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS
SEQRES 29 B 436 LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA
SEQRES 30 B 436 PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA
SEQRES 31 B 436 LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER
SEQRES 32 B 436 PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG
SEQRES 33 B 436 GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG
SEQRES 34 B 436 GLU ALA GLY ARG ARG THR GLY
HET HEM A1408 43
HET 1D2 A1409 24
HET HEM B1408 43
HET 1D2 B1409 48
HET SO4 B1410 5
HET SO4 B1411 5
HET SO4 B1412 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 1D2 CYCLODODECYL 3,4,6-TRIDEOXY-3-(DIMETHYLAMINO)-BETA-D-
HETNAM 2 1D2 XYLO-HEXOPYRANOSIDE
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 1D2 2(C20 H39 N O3)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 10 HOH *576(H2 O)
HELIX 1 1 PRO A 28 GLY A 39 1 12
HELIX 2 2 GLY A 57 ALA A 66 1 10
HELIX 3 3 ASP A 73 SER A 77 5 5
HELIX 4 4 THR A 82 ASN A 89 1 8
HELIX 5 5 ASN A 91 SER A 95 5 5
HELIX 6 6 PRO A 98 LEU A 106 1 9
HELIX 7 7 VAL A 107 PHE A 111 5 5
HELIX 8 8 THR A 112 LEU A 118 1 7
HELIX 9 9 LEU A 119 ALA A 136 1 18
HELIX 10 10 LEU A 144 LEU A 148 1 5
HELIX 11 11 TRP A 150 GLY A 162 1 13
HELIX 12 12 PRO A 164 ASP A 167 5 4
HELIX 13 13 ARG A 168 ASP A 176 1 9
HELIX 14 14 ASP A 183 ARG A 206 1 24
HELIX 15 15 ASP A 212 ASP A 224 1 13
HELIX 16 16 THR A 229 THR A 247 1 19
HELIX 17 17 THR A 247 SER A 261 1 15
HELIX 18 18 HIS A 262 ASP A 272 1 11
HELIX 19 19 LEU A 275 GLY A 288 1 14
HELIX 20 20 VAL A 318 HIS A 323 1 6
HELIX 21 21 GLY A 356 CYS A 375 1 20
HELIX 22 22 SER A 383 LEU A 387 5 5
HELIX 23 23 GLY B 21 ASP B 27 1 7
HELIX 24 24 PRO B 28 GLY B 39 1 12
HELIX 25 25 GLY B 57 ASP B 67 1 11
HELIX 26 26 ASP B 73 SER B 77 5 5
HELIX 27 27 THR B 82 ALA B 87 1 6
HELIX 28 28 ASN B 91 SER B 95 5 5
HELIX 29 29 PRO B 98 LEU B 106 1 9
HELIX 30 30 VAL B 107 PHE B 111 5 5
HELIX 31 31 THR B 112 LEU B 118 1 7
HELIX 32 32 LEU B 119 ALA B 136 1 18
HELIX 33 33 LEU B 144 LEU B 148 1 5
HELIX 34 34 TRP B 150 LEU B 161 1 12
HELIX 35 35 PRO B 164 ASP B 167 5 4
HELIX 36 36 ARG B 168 PHE B 180 1 13
HELIX 37 37 ASP B 183 ARG B 206 1 24
HELIX 38 38 ASP B 212 ASP B 224 1 13
HELIX 39 39 THR B 229 THR B 247 1 19
HELIX 40 40 THR B 247 SER B 261 1 15
HELIX 41 41 HIS B 262 ASP B 272 1 11
HELIX 42 42 LEU B 275 GLY B 288 1 14
HELIX 43 43 VAL B 318 HIS B 323 1 6
HELIX 44 44 GLY B 356 CYS B 375 1 20
HELIX 45 45 SER B 383 LEU B 387 5 5
SHEET 1 AA 4 LEU A 15 ASP A 16 0
SHEET 2 AA 4 ALA A 41 ARG A 45 1 O ARG A 43 N LEU A 15
SHEET 3 AA 4 GLU A 51 VAL A 55 -1 O VAL A 52 N VAL A 44
SHEET 4 AA 4 VAL A 315 VAL A 317 1 O LEU A 316 N VAL A 55
SHEET 1 AB 2 PHE A 70 SER A 71 0
SHEET 2 AB 2 PHE A 297 PRO A 298 -1 O PHE A 297 N SER A 71
SHEET 1 AC 3 ARG A 141 ASP A 143 0
SHEET 2 AC 3 PRO A 402 ARG A 404 -1 O ILE A 403 N ALA A 142
SHEET 3 AC 3 ALA A 379 LEU A 380 -1 O ALA A 379 N ARG A 404
SHEET 1 AD 2 VAL A 302 LEU A 304 0
SHEET 2 AD 2 THR A 307 ILE A 309 -1 O THR A 307 N LEU A 304
SHEET 1 BA 4 LEU B 15 ASP B 16 0
SHEET 2 BA 4 ALA B 41 ARG B 45 1 O ARG B 43 N LEU B 15
SHEET 3 BA 4 GLU B 51 VAL B 55 -1 O VAL B 52 N VAL B 44
SHEET 4 BA 4 VAL B 315 VAL B 317 1 O LEU B 316 N VAL B 55
SHEET 1 BB 2 PHE B 70 SER B 71 0
SHEET 2 BB 2 PHE B 297 PRO B 298 -1 O PHE B 297 N SER B 71
SHEET 1 BC 3 ARG B 141 ASP B 143 0
SHEET 2 BC 3 PRO B 402 ARG B 404 -1 O ILE B 403 N ALA B 142
SHEET 3 BC 3 ALA B 379 LEU B 380 -1 O ALA B 379 N ARG B 404
SHEET 1 BD 2 VAL B 302 LEU B 304 0
SHEET 2 BD 2 THR B 307 ILE B 309 -1 O THR B 307 N LEU B 304
LINK SG CYS A 354 FE HEM A1408 1555 1555 2.29
LINK SG CYS B 354 FE HEM B1408 1555 1555 2.27
CISPEP 1 LEU A 20 GLY A 21 0 -17.69
CISPEP 2 GLY A 21 GLN A 22 0 -11.13
CISPEP 3 GLN A 22 ASP A 23 0 -5.92
CISPEP 4 PRO A 97 PRO A 98 0 6.50
CISPEP 5 PRO B 97 PRO B 98 0 6.56
SITE 1 AC1 25 LYS A 72 MET A 92 LEU A 93 HIS A 100
SITE 2 AC1 25 ARG A 104 PHE A 111 ALA A 243 THR A 247
SITE 3 AC1 25 THR A 248 LEU A 251 PRO A 289 ALA A 293
SITE 4 AC1 25 THR A 294 ARG A 296 ALA A 346 PHE A 347
SITE 5 AC1 25 GLY A 348 ILE A 351 HIS A 352 CYS A 354
SITE 6 AC1 25 ILE A 355 ALA A 360 1D2 A1409 HOH A2294
SITE 7 AC1 25 HOH A2295
SITE 1 AC2 11 LEU A 93 GLU A 94 PHE A 178 VAL A 242
SITE 2 AC2 11 ALA A 243 GLU A 246 ILE A 395 HEM A1408
SITE 3 AC2 11 HOH A2086 HOH A2294 HOH A2296
SITE 1 AC3 24 LYS B 72 MET B 92 LEU B 93 HIS B 100
SITE 2 AC3 24 ARG B 104 PHE B 111 LEU B 240 ALA B 243
SITE 3 AC3 24 THR B 247 THR B 248 LEU B 251 ALA B 293
SITE 4 AC3 24 THR B 294 ARG B 296 ALA B 346 PHE B 347
SITE 5 AC3 24 GLY B 348 ILE B 351 HIS B 352 CYS B 354
SITE 6 AC3 24 ILE B 355 ALA B 360 1D2 B1409 HOH B2276
SITE 1 AC4 18 GLU B 85 LEU B 88 ASN B 91 LEU B 93
SITE 2 AC4 18 GLU B 94 PHE B 178 HIS B 238 ILE B 239
SITE 3 AC4 18 ALA B 243 GLU B 246 THR B 247 THR B 294
SITE 4 AC4 18 MET B 394 ILE B 395 HEM B1408 HOH B2072
SITE 5 AC4 18 HOH B2277 HOH B2278
SITE 1 AC5 7 ARG B 62 LEU B 106 ARG B 109 THR B 220
SITE 2 AC5 7 ARG B 227 HOH B2279 HOH B2280
SITE 1 AC6 4 ARG B 60 ASP B 303 LEU B 304 ASP B 305
SITE 1 AC7 3 ASP B 167 TYR B 197 SER B 204
CRYST1 60.254 109.094 153.244 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 0.016596 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006526 0.00000
MTRIX1 1 -0.999930 -0.012150 0.000560 74.86146 1
MTRIX2 1 -0.011970 0.991200 0.131820 -9.10812 1
MTRIX3 1 -0.002160 0.131810 -0.991270 72.46054 1
(ATOM LINES ARE NOT SHOWN.)
END
