HEADER OXIDOREDUCTASE 14-MAY-09 2WIO
TITLE STRUCTURE OF THE HISTIDINE TAGGED, OPEN CYTOCHROME
TITLE 2 P450 ERYK FROM S. ERYTHRAEA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHROMYCIN B/D C-12 HYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-397;
COMPND 5 SYNONYM: CYTOCHROME P450 CYP113A1;
COMPND 6 EC: 1.14.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (STAR);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET28B;
SOURCE 8 OTHER_DETAILS: CDNA
KEYWDS SUBSTRATE SPECIFICITY, ANTIBIOTIC BIOSYNTHESIS,
KEYWDS 2 METAL-BINDING, OXIDOREDUCTASE, CYTOCHROME P450, IRON,
KEYWDS 3 HEME, ERYTHROMICYN, MONOOXYGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAVINO,L.C.MONTEMIGLIO,G.SCIARA,A.E.MIELE,S.G.KEDREW,
AUTHOR 2 S.GIANNI,B.VALLONE
REVDAT 4 20-OCT-09 2WIO 1 JRNL
REVDAT 3 04-AUG-09 2WIO 1 JRNL
REVDAT 2 28-JUL-09 2WIO 1 TITLE
REVDAT 1 21-JUL-09 2WIO 0
JRNL AUTH C.SAVINO,L.C.MONTEMIGLIO,G.SCIARA,A.E.MIELE,
JRNL AUTH 2 S.G.KENDREW,P.JEMTH,S.GIANNI,B.VALLONE
JRNL TITL INVESTIGATING THE STRUCTURAL PLASTICITY OF A
JRNL TITL 2 CYTOCHROME P450: THREE-DIMENSIONAL STRUCTURES OF
JRNL TITL 3 P450 ERYK AND BINDING TO ITS PHYSIOLOGICAL
JRNL TITL 4 SUBSTRATE.
JRNL REF J.BIOL.CHEM. V. 284 29170 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19625248
JRNL DOI 10.1074/JBC.M109.003590
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 89.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.77
REMARK 3 NUMBER OF REFLECTIONS : 21300
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) : 0.18587
REMARK 3 R VALUE (WORKING SET) : 0.18341
REMARK 3 FREE R VALUE : 0.23202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1115
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) : 2.000
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.052
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1653
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.200
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.267
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3053
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.901
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08
REMARK 3 B22 (A**2) : -1.54
REMARK 3 B33 (A**2) : 1.61
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.266
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3173 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4346 ; 1.543 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 392 ; 6.279 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;34.134 ;23.087
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 491 ;17.156 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;20.234 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 485 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2475 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1720 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2166 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 295 ; 0.187 ; 0.200
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): 73 ; 0.203 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.229 ; 0.200
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): 2028 ; 0.874 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3194 ; 1.315 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1285 ; 2.133 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1150 ; 3.152 ; 4.500
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 : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS.
REMARK 3 THE PDB STARTS FROM A.A. 19 SINCE THERE WAS NO
REMARK 3 INTERPRETABLE ELECTRON DENSITY FOR PREVIOUS RESIDUES
REMARK 4
REMARK 4 2WIO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-09.
REMARK 100 THE PDBE ID CODE IS EBI-39810.
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) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 22549
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 29.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.2
REMARK 200 DATA REDUNDANCY : 4.8
REMARK 200 R MERGE (I) : 0.19
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.90
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.7
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.10
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 1OXA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M NACL, 0.1M
REMARK 280 TRIS PH 8.0
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 18.96612
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.77850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.67062
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.77850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.96604
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.67050
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 GENERATING THE BIOMOLECULE
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 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 PHE A 2
REMARK 465 ALA A 3
REMARK 465 ASP A 4
REMARK 465 VAL A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 CYS A 9
REMARK 465 CYS A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 ARG A 13
REMARK 465 THR A 14
REMARK 465 LEU A 15
REMARK 465 THR A 16
REMARK 465 THR A 17
REMARK 465 ILE A 18
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 OE2 GLU A 229 - O HOH A 2185 2.15
REMARK 500 O HOH A 2025 - O HOH A 2229 1.97
REMARK 500 O HOH A 2058 - O HOH A 2123 2.17
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 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 GLN A 41 71.86 -154.29
REMARK 500 ASP A 210 74.44 -101.63
REMARK 500 VAL A 221 -75.44 -111.36
REMARK 500 ASP A 222 67.73 -115.79
REMARK 500 ASP A 309 33.51 70.42
REMARK 500 CYS A 353 116.75 -28.33
REMARK 500 GLN A 391 -80.63 -133.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN A 391 24.5 L L OUTSIDE RANGE
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 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 A1412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 353 SG
REMARK 620 2 HEM A1412 NA 102.8
REMARK 620 3 HEM A1412 NB 92.8 86.7
REMARK 620 4 HEM A1412 ND 98.8 93.1 168.1
REMARK 620 5 HOH A2307 O 165.7 75.1 73.0 95.4
REMARK 620 6 HEM A1412 NC 90.4 166.2 88.7 88.7 91.2
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 A1412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VRU RELATED DB: PDB
REMARK 900 STRUCTURE OF OPEN HISTIDINE TAGGED CYTOCHROME
REMARK 900 P450 ERYK
REMARK 900 RELATED ID: 2JJN RELATED DB: PDB
REMARK 900 STRUCTURE OF CLOSED CYTOCHROME P450 ERYK
REMARK 900 RELATED ID: 2VRV RELATED DB: PDB
REMARK 900 STRUCTURE OF HISTIDINE TAGGED CYTOCHROME P450
REMARK 900 ERYK IN COMPLEX WITH INHIBITOR CLOTRIMAZOLE
REMARK 900 (CLT)
REMARK 900 RELATED ID: 2JJP RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX
REMARK 900 WITH INHIBITOR KETOCONAZOLE (KC)
REMARK 900 RELATED ID: 2JJO RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX
REMARK 900 WITH ITS NATURAL SUBSTRATE ERD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MGSSHHHHHHSSGLVPRGSH ADDED BECAUSE OF THE EXPRESSION
REMARK 999 VECTOR
DBREF 2WIO A -19 15 PDB 2WIO 2WIO -19 15
DBREF 2WIO A 16 411 UNP P48635 CPXQ_SACEN 2 397
SEQADV 2WIO LEU A 344 UNP P48635 PHE 330 CONFLICT
SEQRES 1 A 431 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 431 LEU VAL PRO ARG GLY SER HIS MET PHE ALA ASP VAL GLU
SEQRES 3 A 431 THR THR CYS CYS ALA ARG ARG THR LEU THR THR ILE ASP
SEQRES 4 A 431 GLU VAL PRO GLY MET ALA ASP GLU THR ALA LEU LEU ASP
SEQRES 5 A 431 TRP LEU GLY THR MET ARG GLU LYS GLN PRO VAL TRP GLN
SEQRES 6 A 431 ASP ARG TYR GLY VAL TRP HIS VAL PHE ARG HIS ALA ASP
SEQRES 7 A 431 VAL GLN THR VAL LEU ARG ASP THR ALA THR PHE SER SER
SEQRES 8 A 431 ASP PRO THR ARG VAL ILE GLU GLY ALA SER PRO THR PRO
SEQRES 9 A 431 GLY MET ILE HIS GLU ILE ASP PRO PRO GLU HIS ARG ALA
SEQRES 10 A 431 LEU ARG LYS VAL VAL SER SER ALA PHE THR PRO ARG THR
SEQRES 11 A 431 ILE SER ASP LEU GLU PRO ARG ILE ARG ASP VAL THR ARG
SEQRES 12 A 431 SER LEU LEU ALA ASP ALA GLY GLU SER PHE ASP LEU VAL
SEQRES 13 A 431 ASP VAL LEU ALA PHE PRO LEU PRO VAL THR ILE VAL ALA
SEQRES 14 A 431 GLU LEU LEU GLY LEU PRO PRO MET ASP HIS GLU GLN PHE
SEQRES 15 A 431 GLY ASP TRP SER GLY ALA LEU VAL ASP ILE GLN MET ASP
SEQRES 16 A 431 ASP PRO THR ASP PRO ALA LEU ALA GLU ARG ILE ALA ASP
SEQRES 17 A 431 VAL LEU ASN PRO LEU THR ALA TYR LEU LYS ALA ARG CYS
SEQRES 18 A 431 ALA GLU ARG ARG ALA ASP PRO GLY ASP ASP LEU ILE SER
SEQRES 19 A 431 ARG LEU VAL LEU ALA GLU VAL ASP GLY ARG ALA LEU ASP
SEQRES 20 A 431 ASP GLU GLU ALA ALA ASN PHE SER THR ALA LEU LEU LEU
SEQRES 21 A 431 ALA GLY HIS ILE THR THR THR VAL LEU LEU GLY ASN ILE
SEQRES 22 A 431 VAL ARG THR LEU ASP GLU HIS PRO ALA HIS TRP ASP ALA
SEQRES 23 A 431 ALA ALA GLU ASP PRO GLY ARG ILE PRO ALA ILE VAL GLU
SEQRES 24 A 431 GLU VAL LEU ARG TYR ARG PRO PRO PHE PRO GLN MET GLN
SEQRES 25 A 431 ARG THR THR THR LYS ALA THR GLU VAL ALA GLY VAL PRO
SEQRES 26 A 431 ILE PRO ALA ASP VAL MET VAL ASN THR TRP VAL LEU SER
SEQRES 27 A 431 ALA ASN ARG ASP SER ASP ALA HIS ASP ASP PRO ASP ARG
SEQRES 28 A 431 PHE ASP PRO SER ARG LYS SER GLY GLY ALA ALA GLN LEU
SEQRES 29 A 431 SER PHE GLY HIS GLY VAL HIS PHE CYS LEU GLY ALA PRO
SEQRES 30 A 431 LEU ALA ARG LEU GLU ASN ARG VAL ALA LEU GLU GLU ILE
SEQRES 31 A 431 ILE ALA ARG PHE GLY ARG LEU THR VAL ASP ARG ASP ASP
SEQRES 32 A 431 GLU ARG LEU ARG HIS PHE GLU GLN ILE VAL LEU GLY THR
SEQRES 33 A 431 ARG HIS LEU PRO VAL LEU ALA GLY SER SER PRO ARG GLN
SEQRES 34 A 431 SER ALA
HET HEM A1412 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *308(H2 O1)
HELIX 1 1 ASP A 26 GLN A 41 1 16
HELIX 2 2 ARG A 55 ASP A 65 1 11
HELIX 3 3 ASP A 72 ILE A 77 5 6
HELIX 4 4 MET A 86 ILE A 90 5 5
HELIX 5 5 PRO A 93 PHE A 106 1 14
HELIX 6 6 THR A 107 ASP A 113 1 7
HELIX 7 7 LEU A 114 ASP A 128 1 15
HELIX 8 8 LEU A 135 LEU A 139 1 5
HELIX 9 9 PHE A 141 GLY A 153 1 13
HELIX 10 10 PRO A 155 MET A 157 5 3
HELIX 11 11 ASP A 158 GLN A 173 1 16
HELIX 12 12 ALA A 181 ASP A 207 1 27
HELIX 13 13 ASP A 211 ALA A 219 1 9
HELIX 14 14 ASP A 227 HIS A 260 1 34
HELIX 15 15 PRO A 261 ASP A 270 1 10
HELIX 16 16 ARG A 273 ARG A 285 1 13
HELIX 17 17 VAL A 316 ARG A 321 1 6
HELIX 18 18 GLY A 339 GLN A 343 5 5
HELIX 19 19 GLN A 343 GLY A 347 5 5
HELIX 20 20 GLY A 355 GLY A 375 1 21
SHEET 1 AA 5 VAL A 43 GLN A 45 0
SHEET 2 AA 5 TRP A 51 VAL A 53 -1 O HIS A 52 N TRP A 44
SHEET 3 AA 5 MET A 311 TRP A 315 1 O MET A 311 N TRP A 51
SHEET 4 AA 5 GLN A 290 THR A 295 -1 O MET A 291 N THR A 314
SHEET 5 AA 5 PHE A 69 SER A 70 -1 O SER A 70 N THR A 294
SHEET 1 AB 3 SER A 132 ASP A 134 0
SHEET 2 AB 3 PRO A 400 ALA A 403 -1 O VAL A 401 N PHE A 133
SHEET 3 AB 3 LEU A 377 VAL A 379 -1 O THR A 378 N LEU A 402
SHEET 1 AC 2 THR A 299 VAL A 301 0
SHEET 2 AC 2 VAL A 304 ILE A 306 -1 O VAL A 304 N VAL A 301
SHEET 1 AD 2 ARG A 387 HIS A 388 0
SHEET 2 AD 2 THR A 396 HIS A 398 -1 N ARG A 397 O ARG A 387
LINK FE HEM A1412 SG CYS A 353 1555 1555 2.31
LINK FE HEM A1412 O HOH A2307 1555 1555 2.29
CISPEP 1 PRO A 92 PRO A 93 0 -2.55
SITE 1 AC1 25 ILE A 87 HIS A 88 HIS A 95 ARG A 99
SITE 2 AC1 25 PHE A 106 LEU A 238 ALA A 241 GLY A 242
SITE 3 AC1 25 THR A 245 THR A 246 LEU A 249 PHE A 288
SITE 4 AC1 25 ARG A 293 SER A 345 PHE A 346 GLY A 347
SITE 5 AC1 25 HIS A 351 CYS A 353 GLY A 355 LEU A 358
SITE 6 AC1 25 ALA A 359 HOH A2078 HOH A2306 HOH A2307
SITE 7 AC1 25 HOH A2308
CRYST1 37.932 57.341 179.557 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.026363 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
