HEADER OXIDOREDUCTASE 15-APR-08 2JJP
TITLE STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX WITH INHIBITOR
TITLE 2 KETOCONAZOLE (KC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 113A1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ERYTHROMYCIN B/D C-12 HYDROXYLASE, CYTOCROME P450
COMPND 5 CYP113A1;
COMPND 6 EC: 1.14.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 STRAIN: NRRL 23338;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28B;
SOURCE 9 OTHER_DETAILS: CDNA
KEYWDS IRON, HEME, MONOOXYGENASE, METAL-BINDING, ANTIBIOTIC BIOSYNTHESIS,
KEYWDS 2 TIE-ROD MECHANISM OF ACTION, OXIDOREDUCTASE, SUBSTRATE SPECIFICITY
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAVINO,G.SCIARA,A.E.MIELE,S.G.KENDREW,B.VALLONE
REVDAT 2 22-AUG-12 2JJP 1 KEYWDS JRNL REMARK VERSN
REVDAT 2 2 HETSYN FORMUL
REVDAT 1 14-JUL-09 2JJP 0
JRNL AUTH L.C.MONTEMIGLIO,S.GIANNI,B.VALLONE,C.SAVINO
JRNL TITL AZOLE DRUGS TRAP CYTOCHROME P450 ERYK IN ALTERNATIVE
JRNL TITL 2 CONFORMATIONAL STATES.
JRNL REF BIOCHEMISTRY V. 49 9199 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20845962
JRNL DOI 10.1021/BI101062V
REMARK 2
REMARK 2 RESOLUTION. 2.1 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 20602
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1109
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) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3152
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.02000
REMARK 3 B22 (A**2) : 4.54000
REMARK 3 B33 (A**2) : -2.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.79000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.309
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3320 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4545 ; 1.611 ; 2.025
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 396 ; 6.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 167 ;34.527 ;23.832
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 529 ;18.058 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;22.980 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 498 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2590 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1684 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2229 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 214 ; 0.211 ; 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): 87 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.168 ; 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): 2046 ; 1.096 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3250 ; 1.775 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1425 ; 2.380 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1293 ; 3.475 ; 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. COORDINATE START FROM A.A. 15 BECAUSE THERE
REMARK 3 WAS NOT ELECTRON DENSITY FOR PREVIOUS RESIDUES
REMARK 4
REMARK 4 2JJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-08.
REMARK 100 THE PDBE ID CODE IS EBI-35935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25326
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.50
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) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.3
REMARK 200 R MERGE FOR SHELL (I) : 0.19
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC5
REMARK 200 STARTING MODEL: PDB ENTRY 2JJN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.3
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULHATE, 0.1M
REMARK 280 BIS-TRIS PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.01900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, MET 1 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 330 TO LEU
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 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 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 OE1B GLU A 390 O HOH A 2218 2.09
REMARK 500 O HOH A 2010 O HOH A 2017 1.87
REMARK 500 O HOH A 2018 O HOH A 2195 2.17
REMARK 500 O HOH A 2138 O HOH A 2139 2.09
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 20 -86.37 -112.17
REMARK 500 VAL A 21 95.06 75.14
REMARK 500 THR A 74 6.97 -63.84
REMARK 500 ALA A 80 69.02 -64.50
REMARK 500 SER A 81 74.85 -106.22
REMARK 500 LEU A 139 -54.34 -126.73
REMARK 500 GLU A 160 98.61 -178.42
REMARK 500 GLN A 161 29.32 -144.00
REMARK 500 GLN A 173 96.16 -62.98
REMARK 500 ASP A 175 -46.12 -143.21
REMARK 500 ARG A 336 96.57 -69.29
REMARK 500 ALA A 341 94.20 -55.77
REMARK 500 ARG A 381 50.25 -103.16
REMARK 500 ASP A 383 -44.36 -143.16
REMARK 500 GLN A 391 -71.15 -136.59
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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 24.2 L L OUTSIDE RANGE
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 A 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 353 SG
REMARK 620 2 HEM A 412 NA 91.0
REMARK 620 3 HEM A 412 NB 84.1 92.3
REMARK 620 4 HEM A 412 NC 88.4 175.5 83.3
REMARK 620 5 KLN A 413 N2 170.3 91.4 86.4 88.4
REMARK 620 6 HEM A 412 ND 96.8 89.2 178.2 95.2 92.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KLN A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 415
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WIO RELATED DB: PDB
REMARK 900 STRUCTURE OF THE OPEN HISTIDINE TAGGED C.
REMARK 900 SAVINO, CYTOCHROME P450 ERYK
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: 2JJO RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX
REMARK 900 WITH ITS NATURAL SUBSTRATE ERD
DBREF 2JJP A 1 14 PDB 2JJP 2JJP 1 14
DBREF 2JJP A 15 411 UNP P48635 CPXQ_SACEN 1 397
SEQADV 2JJP LEU A 15 UNP P48635 MET 1 ENGINEERED MUTATION
SEQADV 2JJP LEU A 344 UNP P48635 PHE 330 ENGINEERED MUTATION
SEQRES 1 A 411 MET PHE ALA ASP VAL GLU THR THR CYS CYS ALA ARG ARG
SEQRES 2 A 411 THR LEU THR THR ILE ASP GLU VAL PRO GLY MET ALA ASP
SEQRES 3 A 411 GLU THR ALA LEU LEU ASP TRP LEU GLY THR MET ARG GLU
SEQRES 4 A 411 LYS GLN PRO VAL TRP GLN ASP ARG TYR GLY VAL TRP HIS
SEQRES 5 A 411 VAL PHE ARG HIS ALA ASP VAL GLN THR VAL LEU ARG ASP
SEQRES 6 A 411 THR ALA THR PHE SER SER ASP PRO THR ARG VAL ILE GLU
SEQRES 7 A 411 GLY ALA SER PRO THR PRO GLY MET ILE HIS GLU ILE ASP
SEQRES 8 A 411 PRO PRO GLU HIS ARG ALA LEU ARG LYS VAL VAL SER SER
SEQRES 9 A 411 ALA PHE THR PRO ARG THR ILE SER ASP LEU GLU PRO ARG
SEQRES 10 A 411 ILE ARG ASP VAL THR ARG SER LEU LEU ALA ASP ALA GLY
SEQRES 11 A 411 GLU SER PHE ASP LEU VAL ASP VAL LEU ALA PHE PRO LEU
SEQRES 12 A 411 PRO VAL THR ILE VAL ALA GLU LEU LEU GLY LEU PRO PRO
SEQRES 13 A 411 MET ASP HIS GLU GLN PHE GLY ASP TRP SER GLY ALA LEU
SEQRES 14 A 411 VAL ASP ILE GLN MET ASP ASP PRO THR ASP PRO ALA LEU
SEQRES 15 A 411 ALA GLU ARG ILE ALA ASP VAL LEU ASN PRO LEU THR ALA
SEQRES 16 A 411 TYR LEU LYS ALA ARG CYS ALA GLU ARG ARG ALA ASP PRO
SEQRES 17 A 411 GLY ASP ASP LEU ILE SER ARG LEU VAL LEU ALA GLU VAL
SEQRES 18 A 411 ASP GLY ARG ALA LEU ASP ASP GLU GLU ALA ALA ASN PHE
SEQRES 19 A 411 SER THR ALA LEU LEU LEU ALA GLY HIS ILE THR THR THR
SEQRES 20 A 411 VAL LEU LEU GLY ASN ILE VAL ARG THR LEU ASP GLU HIS
SEQRES 21 A 411 PRO ALA HIS TRP ASP ALA ALA ALA GLU ASP PRO GLY ARG
SEQRES 22 A 411 ILE PRO ALA ILE VAL GLU GLU VAL LEU ARG TYR ARG PRO
SEQRES 23 A 411 PRO PHE PRO GLN MET GLN ARG THR THR THR LYS ALA THR
SEQRES 24 A 411 GLU VAL ALA GLY VAL PRO ILE PRO ALA ASP VAL MET VAL
SEQRES 25 A 411 ASN THR TRP VAL LEU SER ALA ASN ARG ASP SER ASP ALA
SEQRES 26 A 411 HIS ASP ASP PRO ASP ARG PHE ASP PRO SER ARG LYS SER
SEQRES 27 A 411 GLY GLY ALA ALA GLN LEU SER PHE GLY HIS GLY VAL HIS
SEQRES 28 A 411 PHE CYS LEU GLY ALA PRO LEU ALA ARG LEU GLU ASN ARG
SEQRES 29 A 411 VAL ALA LEU GLU GLU ILE ILE ALA ARG PHE GLY ARG LEU
SEQRES 30 A 411 THR VAL ASP ARG ASP ASP GLU ARG LEU ARG HIS PHE GLU
SEQRES 31 A 411 GLN ILE VAL LEU GLY THR ARG HIS LEU PRO VAL LEU ALA
SEQRES 32 A 411 GLY SER SER PRO ARG GLN SER ALA
HET HEM A 412 43
HET KLN A 413 36
HET SO4 A 414 5
HET SO4 A 415 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETNAM KLN 1-ACETYL-4-(4-{[(2S,4R)-2-(2,4-
HETNAM 2 KLN DICHLOROPHENYL)-2-(1H-IMIDAZOL-1-YLMETHYL)-1,3-DIOXOLAN-4-
HETNAM 3 KLN YL]METHOXY}PHENYL)PIPERAZINE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 KLN C26 H28 CL2 N4 O4
FORMUL 5 HOH *229(H2 O)
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 VAL A 76 5 5
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 GLY A 163 ASP A 171 1 9
HELIX 11 11 PRO A 180 ASP A 207 1 28
HELIX 12 12 ASP A 211 ALA A 219 1 9
HELIX 13 13 ASP A 227 HIS A 260 1 34
HELIX 14 14 PRO A 261 ASP A 270 1 10
HELIX 15 15 ARG A 273 ARG A 285 1 13
HELIX 16 16 VAL A 316 ARG A 321 1 6
HELIX 17 17 GLN A 343 GLY A 347 5 5
HELIX 18 18 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 LEU A 402 -1 O VAL A 401 N PHE A 133
SHEET 3 AB 3 THR A 378 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
LINK FE HEM A 412 SG CYS A 353 1555 1555 2.24
LINK FE HEM A 412 N2 KLN A 413 1555 1555 1.96
CISPEP 1 PRO A 92 PRO A 93 0 6.09
SITE 1 AC1 20 ILE A 87 HIS A 88 HIS A 95 ARG A 99
SITE 2 AC1 20 ALA A 241 THR A 245 MET A 291 ARG A 293
SITE 3 AC1 20 SER A 345 PHE A 346 GLY A 347 VAL A 350
SITE 4 AC1 20 HIS A 351 CYS A 353 GLY A 355 ALA A 359
SITE 5 AC1 20 KLN A 413 HOH A2064 HOH A2065 HOH A2228
SITE 1 AC2 14 HIS A 88 MET A 174 ALA A 237 LEU A 240
SITE 2 AC2 14 ALA A 241 PHE A 288 GLN A 290 MET A 291
SITE 3 AC2 14 GLN A 292 ILE A 392 HEM A 412 HOH A2114
SITE 4 AC2 14 HOH A2174 HOH A2219
SITE 1 AC3 4 ARG A 381 ARG A 385 LEU A 386 HIS A 388
SITE 1 AC4 5 HIS A 326 ASP A 327 ARG A 336 LYS A 337
SITE 2 AC4 5 SER A 338
CRYST1 53.243 68.038 57.687 90.00 100.71 90.00 P 1 21 1 2
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 0.018782 0.000000 0.003552 0.00000
SCALE2 0.000000 0.014698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017642 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
