HEADER OXIDOREDUCTASE 28-JUN-05 2BVJ
TITLE LIGAND-FREE STRUCTURE OF CYTOCHROME P450 PIKC (CYP107L1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 MONOOXYGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOCHROME P450 PIKC CYP107L1, CYTOCHROME P450 HYDROXYLASE
COMPND 5 PIKC;
COMPND 6 ENGINEERED: 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 CYTOCHROME P450, PIKC, CYP107L1, MACROLIDE MONOOXYGENASE, ANTIBIOTIC
KEYWDS 2 BIOSYNTHESIS, HEME, IRON, METAL-BINDING, MONOOXYGENASE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.SHERMAN,S.LI,L.V.YERMALITSKAYA,Y.KIM,J.A.SMITH,M.R.WATERMAN,
AUTHOR 2 L.M.PODUST
REVDAT 4 13-DEC-23 2BVJ 1 LINK
REVDAT 3 24-FEB-09 2BVJ 1 VERSN
REVDAT 2 06-SEP-06 2BVJ 1 JRNL
REVDAT 1 03-JUL-06 2BVJ 0
JRNL AUTH D.H.SHERMAN,S.LI,L.V.YERMALITSKAYA,Y.KIM,J.A.SMITH,
JRNL AUTH 2 M.R.WATERMAN,L.M.PODUST
JRNL TITL THE STRUCTURAL BASIS FOR SUBSTRATE ANCHORING, ACTIVE SITE
JRNL TITL 2 SELECTIVITY, AND PRODUCT FORMATION BY P450 PIKC FROM
JRNL TITL 3 STREPTOMYCES VENEZUELAE.
JRNL REF J.BIOL.CHEM. V. 281 26289 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16825192
JRNL DOI 10.1074/JBC.M605478200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
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) : 36.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 65959.720
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 53812
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 SET) : 0.202
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5448
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6800
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 806
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 102
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.53000
REMARK 3 B22 (A**2) : -1.73000
REMARK 3 B33 (A**2) : 9.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.50000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.790 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 51.38
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE OMMITED FROM
REMARK 3 THE STRUCTURE
REMARK 4
REMARK 4 2BVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1290024623.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (220) DOUBLE CRYSTAL
REMARK 200 OPTICS : SAGITTAL FOCUSING CRYSTAL AND
REMARK 200 VERTICALLY FOCUSING DOUBLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55910
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OXA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000; 0.1 M HEPES, PH 7.5; 0.5
REMARK 280 MM DTT, PH 7.50
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 109.09500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.08550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 109.09500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.08550
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: PQS
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -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 ARG 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 PRO A 12
REMARK 465 PRO A 13
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 ARG 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 THR B 82
REMARK 465 GLU B 83
REMARK 465 ALA B 84
REMARK 465 GLU B 85
REMARK 465 ALA B 86
REMARK 465 ALA B 87
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 ARG A 34 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 180 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 182 CG OD1 OD2
REMARK 470 GLU A 300 CG CD OE1 OE2
REMARK 470 GLY A 408 CA C O
REMARK 470 ARG B 75 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 81 CG CD1 CD2
REMARK 470 LEU B 88 CG CD1 CD2
REMARK 470 ASN B 89 CG OD1 ND2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 PHE B 178 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 186 CG CD OE1 NE2
REMARK 470 GLN B 188 CG CD OE1 NE2
REMARK 470 THR B 189 OG1 CG2
REMARK 470 MET B 191 CG SD CE
REMARK 470 GLN B 208 CG CD OE1 NE2
REMARK 470 ASP B 209 CG OD1 OD2
REMARK 470 GLU B 223 CG CD OE1 OE2
REMARK 470 GLY B 408 CA C O
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 C1 BME A 1409 C1 BME A 1409 2556 1.58
REMARK 500 C1 BME B 1409 C1 BME B 1409 2557 1.77
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 GLU A 94 48.10 -97.61
REMARK 500 LEU A 148 -55.69 -145.80
REMARK 500 VAL A 179 -74.39 -54.24
REMARK 500 PHE A 180 71.24 -111.24
REMARK 500 ASP A 183 138.64 -171.85
REMARK 500 ASP A 209 50.15 -107.67
REMARK 500 LEU A 228 108.30 -161.26
REMARK 500 HIS A 245 -34.44 -154.36
REMARK 500 CYS A 354 115.42 -32.71
REMARK 500 TRP A 405 37.95 -149.06
REMARK 500 LEU B 148 -56.76 -141.50
REMARK 500 VAL B 179 -47.75 -142.35
REMARK 500 PHE B 180 68.36 -113.49
REMARK 500 ALA B 187 -79.03 -43.70
REMARK 500 GLN B 208 162.02 175.00
REMARK 500 HIS B 245 -80.21 -95.62
REMARK 500 GLU B 287 59.48 -140.35
REMARK 500 ASN B 392 118.36 177.64
REMARK 500 TRP B 405 25.57 -141.35
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 96.7
REMARK 620 3 HEM A1408 NB 84.0 91.4
REMARK 620 4 HEM A1408 NC 81.9 178.3 89.5
REMARK 620 5 HEM A1408 ND 98.2 89.1 177.7 90.1
REMARK 620 6 HOH A2087 O 167.1 89.6 84.6 92.0 93.2
REMARK 620 N 1 2 3 4 5
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 99.3
REMARK 620 3 HEM B1408 NB 87.4 91.3
REMARK 620 4 HEM B1408 NC 83.5 177.1 88.7
REMARK 620 5 HEM B1408 ND 96.7 89.7 175.6 90.0
REMARK 620 6 HOH B2101 O 167.7 80.4 80.4 96.8 95.5
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 A1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A1410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B1409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C6H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND 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: 2CA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2CD8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST 20 RESIDUES INCLUDING 6X HIS-TAG AND THROMBIN
REMARK 999 CLEAVAGE SITE ARE FROM THE CLONING VECTOR PET28A
DBREF 2BVJ A -19 0 PDB 2BVJ 2BVJ -19 0
DBREF 2BVJ A 1 416 UNP O87605 O87605_9ACTO 1 416
DBREF 2BVJ B -19 0 PDB 2BVJ 2BVJ -19 0
DBREF 2BVJ B 1 416 UNP O87605 O87605_9ACTO 1 416
SEQRES 1 A 436 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 436 LEU VAL PRO ARG 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 ASP 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 ARG 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 ASP 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 BME A1409 4
HET DTT A1410 8
HET HEM B1408 43
HET BME B1409 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN HEM HEME
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 BME 2(C2 H6 O S)
FORMUL 5 DTT C4 H10 O2 S2
FORMUL 8 HOH *315(H2 O)
HELIX 1 1 LEU A 20 ASP A 27 1 8
HELIX 2 2 PRO A 28 GLY A 39 1 12
HELIX 3 3 GLY A 57 ASP A 67 1 11
HELIX 4 4 ASP A 73 SER A 77 5 5
HELIX 5 5 THR A 82 ASN A 89 1 8
HELIX 6 6 PRO A 98 ALA A 108 1 11
HELIX 7 7 ARG A 109 PHE A 111 5 3
HELIX 8 8 THR A 112 LEU A 118 1 7
HELIX 9 9 LEU A 119 LEU A 135 1 17
HELIX 10 10 LEU A 144 LEU A 148 1 5
HELIX 11 11 TRP A 150 LEU A 161 1 12
HELIX 12 12 PRO A 164 ASP A 167 5 4
HELIX 13 13 ARG A 168 PHE A 180 1 13
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 ALA A 243 1 15
HELIX 17 17 HIS A 245 SER A 261 1 17
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 18 LEU B 20 5 3
HELIX 24 24 GLY B 21 ASP B 27 1 7
HELIX 25 25 PRO B 28 GLY B 39 1 12
HELIX 26 26 GLY B 57 ASP B 67 1 11
HELIX 27 27 ASP B 73 SER B 77 5 5
HELIX 28 28 ASN B 91 SER B 95 5 5
HELIX 29 29 PRO B 98 ARG B 109 1 12
HELIX 30 30 THR B 112 LEU B 119 1 8
HELIX 31 31 LEU B 119 LEU B 135 1 17
HELIX 32 32 LEU B 144 LEU B 148 1 5
HELIX 33 33 TRP B 150 LEU B 161 1 12
HELIX 34 34 PRO B 164 PHE B 178 1 15
HELIX 35 35 ASP B 183 ARG B 206 1 24
HELIX 36 36 ASP B 212 THR B 220 1 9
HELIX 37 37 THR B 229 HIS B 245 1 17
HELIX 38 38 HIS B 245 SER B 261 1 17
HELIX 39 39 HIS B 262 ASP B 272 1 11
HELIX 40 40 LEU B 275 GLY B 288 1 14
HELIX 41 41 VAL B 318 HIS B 323 1 6
HELIX 42 42 GLY B 356 CYS B 375 1 20
HELIX 43 43 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 N ARG B 45 O 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 2.63
LINK FE HEM A1408 O HOH A2087 1555 1555 2.99
LINK SG CYS B 354 FE HEM B1408 1555 1555 2.68
LINK FE HEM B1408 O HOH B2101 1555 1555 2.88
CISPEP 1 PRO A 97 PRO A 98 0 0.23
CISPEP 2 PRO B 97 PRO B 98 0 0.18
SITE 1 AC1 26 LYS A 72 MET A 92 LEU A 93 HIS A 100
SITE 2 AC1 26 ARG A 104 PHE A 111 ALA A 243 GLY A 244
SITE 3 AC1 26 THR A 247 THR A 248 LEU A 251 PRO A 289
SITE 4 AC1 26 ALA A 293 THR A 294 ARG A 296 ALA A 346
SITE 5 AC1 26 PHE A 347 GLY A 348 ILE A 351 HIS A 352
SITE 6 AC1 26 CYS A 354 ILE A 355 GLY A 356 ALA A 360
SITE 7 AC1 26 HOH A2087 HOH A2144
SITE 1 AC2 5 LEU A 135 ARG A 374 CYS A 375 TRP A 405
SITE 2 AC2 5 HOH A2143
SITE 1 AC3 7 ARG A 120 ASP A 277 ARG A 365 ARG A 369
SITE 2 AC3 7 HOH A2098 GLY B 21 GLN B 22
SITE 1 AC4 24 LYS B 72 MET B 92 LEU B 93 HIS B 100
SITE 2 AC4 24 ARG B 104 PHE B 111 LEU B 240 ALA B 243
SITE 3 AC4 24 GLY B 244 THR B 247 THR B 248 LEU B 251
SITE 4 AC4 24 ALA B 293 THR B 294 ARG B 296 ALA B 346
SITE 5 AC4 24 PHE B 347 GLY B 348 HIS B 352 CYS B 354
SITE 6 AC4 24 ILE B 355 ALA B 360 HOH B2101 HOH B2140
SITE 1 AC5 6 LEU B 135 ARG B 374 CYS B 375 TRP B 405
SITE 2 AC5 6 HOH B2168 HOH B2169
CRYST1 218.190 64.171 73.593 90.00 107.15 90.00 C 1 2 1 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 0.004583 0.000000 0.001414 0.00000
SCALE2 0.000000 0.015583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014221 0.00000
(ATOM LINES ARE NOT SHOWN.)
END