HEADER OXIDOREDUCTASE 23-MAR-10 2X9P
TITLE X-RAY STRUCTURE OF THE SUBSTRATE-FREE CYTOCHROME P450 PIMD - A POLYENE
TITLE 2 MACROLIDE ANTIBIOTIC PIMARICIN EPOXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PIMD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIMD;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES NATALENSIS;
SOURCE 3 ORGANISM_TAXID: 68242;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE-30
KEYWDS EPOXIDATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.KELLS,H.OUELLET,J.SANTOS-ABERTURAS,J.F.APARICIO,L.M.PODUST
REVDAT 5 20-DEC-23 2X9P 1 REMARK
REVDAT 4 08-MAY-19 2X9P 1 REMARK
REVDAT 3 05-OCT-11 2X9P 1 JRNL REMARK VERSN
REVDAT 2 08-SEP-10 2X9P 1 JRNL
REVDAT 1 04-AUG-10 2X9P 0
JRNL AUTH P.M.KELLS,H.OUELLET,J.SANTOS-ABERTURAS,J.F.APARICIO,
JRNL AUTH 2 L.M.PODUST
JRNL TITL STRUCTURE OF CYTOCHROME P450 PIMD SUGGESTS EPOXIDATION OF
JRNL TITL 2 THE POLYENE MACROLIDE PIMARICIN OCCURS VIA A
JRNL TITL 3 HYDROPEROXOFERRIC INTERMEDIATE.
JRNL REF CHEM.BIOL. V. 17 841 2010
JRNL REFN ISSN 1074-5521
JRNL PMID 20797613
JRNL DOI 10.1016/J.CHEMBIOL.2010.05.026
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 32420
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1725
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2365
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2927
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : 0.14000
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): 0.368
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.629
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3086 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4228 ; 1.974 ; 2.034
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 389 ; 6.127 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;33.470 ;23.233
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 473 ;17.416 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;21.195 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 473 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2385 ; 0.011 ; 0.022
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): 1945 ; 1.597 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3126 ; 2.579 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1141 ; 3.899 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1102 ; 5.853 ; 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): 3086 ; 2.473 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 177 ;11.306 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3013 ; 5.524 ; 3.000
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. RESIDUES 82-89 ARE DISORDERED.
REMARK 4
REMARK 4 2X9P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1290043386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
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) : 1.11588
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34176
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 16.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZBZ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75 M AMMONIUM SULFATE, 2% PEG400,
REMARK 280 0.1 M TRIS-HCL, PH 8.5; T=23 C, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 35.02050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.02050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 59.30150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.69000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.30150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.69000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.02050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.30150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.69000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 35.02050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.30150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.69000
REMARK 290 SMTRY3 8 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 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 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 -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 GLY A 4
REMARK 465 LYS A 382
REMARK 465 GLU A 383
REMARK 465 GLY A 384
REMARK 465 GLN A 385
REMARK 465 LEU A 386
REMARK 465 SER A 387
REMARK 465 GLY A 388
REMARK 465 GLY A 389
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 5 OG
REMARK 470 LYS A 17 CD CE NZ
REMARK 470 LYS A 20 CE NZ
REMARK 470 ARG A 31 NE CZ NH1 NH2
REMARK 470 ARG A 78 CD NE CZ NH1 NH2
REMARK 470 GLN A 97 CD OE1 NE2
REMARK 470 ARG A 112 CD NE CZ NH1 NH2
REMARK 470 LYS A 120 CE NZ
REMARK 470 ARG A 164 CZ NH1 NH2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LEU A 178 CG CD1 CD2
REMARK 470 ARG A 181 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 186 NE CZ NH1 NH2
REMARK 470 ARG A 203 NE CZ NH1 NH2
REMARK 470 ARG A 357 NE CZ NH1 NH2
REMARK 470 GLU A 377 CG CD OE1 OE2
REMARK 470 GLN A 378 CD OE1 NE2
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 GLN A 256 CG GLN A 256 CD -0.167
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 THR A 146 CA - CB - CG2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLN A 256 CA - CB - CG ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG A 257 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 257 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH2 ANGL. DEV. = -3.0 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 LEU A 145 -59.28 -135.94
REMARK 500 LEU A 178 152.12 -43.14
REMARK 500 ASP A 179 -3.96 -164.85
REMARK 500 LEU A 236 -74.33 -97.04
REMARK 500 PRO A 335 45.72 -80.79
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 SER A 5 HIS A 6 -142.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PROTOPORPHYRIN IX CONTAINING FE (HEM): THIOLATE BOND TO
REMARK 600 CYS346
REMARK 600 SULFATE ION (SO4): PART OF CRYSTALLISATION CONDITIONS
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 A1398 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 346 SG
REMARK 620 2 HEM A1398 NA 100.3
REMARK 620 3 HEM A1398 NB 90.2 86.2
REMARK 620 4 HEM A1398 NC 88.5 170.7 91.0
REMARK 620 5 HEM A1398 ND 98.8 90.8 171.0 90.6
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 1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XBK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SUBSTRATE-BOUND CYTOCHROME P450 PIMD - A
REMARK 900 POLYENE MACROLIDE ANTIBIOTIC PIMARICIN EPOXIDASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES UPSTREAM OF SER 5 INCLUDING 6XHIS TAG ARE
REMARK 999 ENGINEERED
DBREF 2X9P A 5 397 UNP Q9EW92 Q9EW92_9ACTO 5 397
SEQADV 2X9P MET A -6 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P ARG A -5 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P GLY A -4 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P SER A -3 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A -2 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A -1 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A 0 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A 1 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A 2 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P HIS A 3 UNP Q9EW92 EXPRESSION TAG
SEQADV 2X9P GLY A 4 UNP Q9EW92 EXPRESSION TAG
SEQRES 1 A 404 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER HIS
SEQRES 2 A 404 ASP LEU PRO CYS LEU ASN LEU GLU PRO PRO LYS MET LEU
SEQRES 3 A 404 LYS LEU SER PRO LEU LEU ARG ALA LEU GLN ASP ARG GLY
SEQRES 4 A 404 PRO ILE HIS ARG VAL ARG THR PRO ALA GLY ASP GLU ALA
SEQRES 5 A 404 TRP LEU VAL THR ARG HIS ALA GLU LEU LYS GLN LEU LEU
SEQRES 6 A 404 HIS ASP GLU ARG ILE GLY ARG THR HIS PRO ASP PRO PRO
SEQRES 7 A 404 SER ALA ALA GLN TYR VAL ARG SER PRO PHE LEU ASP LEU
SEQRES 8 A 404 LEU ILE SER ASP ALA ASP ALA GLU SER GLY ARG ARG GLN
SEQRES 9 A 404 HIS ALA GLU THR ARG ARG LEU LEU THR PRO LEU PHE SER
SEQRES 10 A 404 ALA ARG ARG VAL LEU GLU MET GLN PRO LYS VAL GLU GLU
SEQRES 11 A 404 ALA ALA ASP THR LEU LEU ASP ALA PHE ILE ALA GLN GLY
SEQRES 12 A 404 PRO PRO GLY ASP LEU HIS GLY GLU LEU THR VAL PRO PHE
SEQRES 13 A 404 ALA LEU THR VAL LEU CYS GLU VAL ILE GLY VAL PRO PRO
SEQRES 14 A 404 GLN ARG ARG ALA GLU LEU THR THR LEU LEU ALA GLY ILE
SEQRES 15 A 404 ALA LYS LEU ASP ASP ARG GLU GLY ALA VAL ARG ALA GLN
SEQRES 16 A 404 ASP ASP LEU PHE GLY TYR VAL ALA GLY LEU VAL GLU HIS
SEQRES 17 A 404 LYS ARG ALA GLU PRO GLY PRO ASP ILE ILE SER ARG LEU
SEQRES 18 A 404 ASN ASP GLY GLU LEU THR GLU ASP ARG VAL ALA HIS LEU
SEQRES 19 A 404 ALA MET GLY LEU LEU PHE ALA GLY LEU ASP SER VAL ALA
SEQRES 20 A 404 SER ILE MET ASP ASN GLY VAL VAL LEU LEU ALA ALA HIS
SEQRES 21 A 404 PRO ASP GLN ARG ALA ALA ALA LEU ALA ASP PRO ASP VAL
SEQRES 22 A 404 MET ALA ARG ALA VAL GLU GLU VAL LEU ARG THR ALA ARG
SEQRES 23 A 404 ALA GLY GLY SER VAL LEU PRO PRO ARG TYR ALA SER GLU
SEQRES 24 A 404 ASP MET GLU PHE GLY GLY VAL THR ILE ARG ALA GLY ASP
SEQRES 25 A 404 LEU VAL LEU PHE ASP LEU GLY LEU PRO ASN PHE ASP GLU
SEQRES 26 A 404 ARG ALA PHE THR GLY PRO GLU GLU PHE ASP ALA ALA ARG
SEQRES 27 A 404 THR PRO ASN PRO HIS LEU THR PHE GLY HIS GLY ILE TRP
SEQRES 28 A 404 HIS CYS ILE GLY ALA PRO LEU ALA ARG LEU GLU LEU ARG
SEQRES 29 A 404 THR MET PHE THR LYS LEU PHE THR ARG LEU PRO GLU LEU
SEQRES 30 A 404 ARG PRO GLU LEU PRO VAL GLU GLN LEU ARG LEU LYS GLU
SEQRES 31 A 404 GLY GLN LEU SER GLY GLY PHE ALA GLU LEU ARG VAL VAL
SEQRES 32 A 404 TRP
HET HEM A1398 43
HET SO4 A1399 5
HET SO4 A1400 5
HET SO4 A1401 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *177(H2 O)
HELIX 1 1 SER A 22 GLY A 32 1 11
HELIX 2 2 ARG A 50 HIS A 59 1 10
HELIX 3 3 ASP A 69 ALA A 73 5 5
HELIX 4 4 SER A 79 LEU A 84 1 6
HELIX 5 5 ASP A 90 THR A 106 1 17
HELIX 6 6 PRO A 107 PHE A 109 5 3
HELIX 7 7 SER A 110 GLN A 135 1 26
HELIX 8 8 LEU A 141 GLY A 159 1 19
HELIX 9 9 PRO A 161 LYS A 177 1 17
HELIX 10 10 ASP A 180 GLU A 205 1 26
HELIX 11 11 ASP A 209 GLY A 217 1 9
HELIX 12 12 THR A 220 LEU A 236 1 17
HELIX 13 13 LEU A 236 HIS A 253 1 18
HELIX 14 14 HIS A 253 ASP A 263 1 11
HELIX 15 15 ASP A 263 ALA A 278 1 16
HELIX 16 16 LEU A 311 PHE A 316 1 6
HELIX 17 17 HIS A 341 HIS A 345 5 5
HELIX 18 18 GLY A 348 LEU A 367 1 20
HELIX 19 19 PRO A 375 LEU A 381 1 7
SHEET 1 AA 5 ILE A 34 ARG A 38 0
SHEET 2 AA 5 GLU A 44 VAL A 48 -1 O ALA A 45 N VAL A 37
SHEET 3 AA 5 LEU A 306 LEU A 308 1 O LEU A 306 N TRP A 46
SHEET 4 AA 5 ARG A 288 ALA A 290 -1 O ARG A 288 N VAL A 307
SHEET 5 AA 5 ILE A 63 GLY A 64 -1 O GLY A 64 N TYR A 289
SHEET 1 AB 3 GLY A 139 ASP A 140 0
SHEET 2 AB 3 ARG A 394 VAL A 396 -1 O VAL A 395 N GLY A 139
SHEET 3 AB 3 ARG A 371 PRO A 372 -1 O ARG A 371 N VAL A 396
SHEET 1 AC 2 MET A 294 PHE A 296 0
SHEET 2 AC 2 VAL A 299 ILE A 301 -1 O VAL A 299 N PHE A 296
SSBOND 1 CYS A 10 CYS A 10 1555 3554 2.07
LINK SG CYS A 346 FE HEM A1398 1555 1555 2.31
CISPEP 1 PRO A 137 PRO A 138 0 -11.90
CISPEP 2 THR A 332 PRO A 333 0 -9.63
SITE 1 AC1 25 ARG A 65 HIS A 98 ARG A 102 LEU A 105
SITE 2 AC1 25 PHE A 109 LEU A 154 ALA A 234 GLY A 235
SITE 3 AC1 25 SER A 238 VAL A 239 LEU A 285 PRO A 286
SITE 4 AC1 25 ARG A 288 LEU A 311 THR A 338 PHE A 339
SITE 5 AC1 25 GLY A 340 ILE A 343 TRP A 344 HIS A 345
SITE 6 AC1 25 CYS A 346 GLY A 348 ALA A 352 HOH A2103
SITE 7 AC1 25 HOH A2175
SITE 1 AC2 3 ASP A 30 ARG A 50 HOH A2176
SITE 1 AC3 4 HIS A 253 PRO A 254 ASP A 255 GLN A 256
SITE 1 AC4 3 HIS A 345 ARG A 353 HOH A2177
CRYST1 118.603 139.380 70.041 90.00 90.00 90.00 C 2 2 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 0.008431 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014277 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
