HEADER OXIDOREDUCTASE 11-OCT-07 2ZAX
TITLE CRYSTAL STRUCTURE OF FERRIC CYTOCHROME P450CAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450-CAM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAMPHOR 5-MONOOXYGENASE, P450CAM;
COMPND 5 EC: 1.14.15.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 GENE: CAMC, CYP101;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: M13TV19
KEYWDS P450CAM, MONOOXYGENASE, CAMPHOR-HYDROXYLASE, HEME, IRON, MEMBRANE,
KEYWDS 2 METAL-BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SAKURAI,H.SHIMADA,K.HARADA,T.HAYASHI,T.TSUKIHARA
REVDAT 5 01-NOV-23 2ZAX 1 REMARK
REVDAT 4 20-JUN-18 2ZAX 1 REMARK
REVDAT 3 24-FEB-09 2ZAX 1 VERSN
REVDAT 2 22-JAN-08 2ZAX 1 JRNL
REVDAT 1 01-JAN-08 2ZAX 0
JRNL AUTH K.HARADA,K.SAKURAI,K.IKEMURA,T.OGURA,S.HIROTA,H.SHIMADA,
JRNL AUTH 2 T.HAYASHI
JRNL TITL EVALUATION OF THE FUNCTIONAL ROLE OF THE HEME-6-PROPIONATE
JRNL TITL 2 SIDE CHAIN IN CYTOCHROME P450CAM
JRNL REF J.AM.CHEM.SOC. V. 130 432 2008
JRNL REFN ISSN 0002-7863
JRNL PMID 18088124
JRNL DOI 10.1021/JA077902L
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 65093
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3403
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4728
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.2220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3208
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 561
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.248
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3728 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5148 ; 1.502 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 496 ; 5.385 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;33.286 ;24.098
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 650 ;13.228 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;14.226 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 548 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2968 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2024 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2578 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 465 ; 0.117 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.154 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.152 ; 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): 2239 ; 0.660 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3688 ; 1.131 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1498 ; 1.744 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1428 ; 2.710 ; 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): 1 ; 2.836 ; 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 : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2ZAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000027741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.7
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 31.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.580
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 2CPP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-14% PEG 4000, 50MM TRIS-HCL, 250MM
REMARK 280 KCL, 1MM D-CAMPHOR, 10MM DITHIOERYTHRITOL(DTE), PH 7.4, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 124.83500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.76100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.76100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 187.25250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.76100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.76100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.41750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.76100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.76100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 187.25250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.76100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.76100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 62.41750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 124.83500
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 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 0
REMARK 465 THR A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 ILE A 5
REMARK 465 GLN A 6
REMARK 465 SER A 7
REMARK 465 ASN A 8
REMARK 465 ALA A 9
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 ASN A 30 65.98 -163.64
REMARK 500 TYR A 154 -52.31 -145.03
REMARK 500 ASN A 229 49.68 39.42
REMARK 500 ASP A 251 30.27 -141.97
REMARK 500 THR A 252 -80.06 -120.36
REMARK 500 ASP A 297 -157.56 -118.54
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 K A 415 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 84 O
REMARK 620 2 GLY A 93 O 84.9
REMARK 620 3 GLU A 94 O 156.7 77.3
REMARK 620 4 TYR A 96 O 101.4 84.5 92.0
REMARK 620 5 HOH A 806 O 83.5 96.2 83.6 175.2
REMARK 620 6 HOH A 813 O 102.3 167.6 98.0 84.1 94.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 417 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 357 SG
REMARK 620 2 HEM A 417 NA 102.9
REMARK 620 3 HEM A 417 NB 92.8 88.6
REMARK 620 4 HEM A 417 NC 95.1 162.0 88.8
REMARK 620 5 HEM A 417 ND 105.3 88.3 161.9 88.6
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 K A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAM A 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 423
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z97 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RECONSTITUTED WITH 7-METHYL-7-DEPROPIONATED HEMIN
REMARK 900 RELATED ID: 2ZAW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RECONSTITUTED WITH 6-METHYL-6-DEPROPIONATED HEMIN
DBREF 2ZAX A 0 414 UNP P00183 CPXA_PSEPU 1 415
SEQRES 1 A 415 MET THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA
SEQRES 2 A 415 PRO LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP
SEQRES 3 A 415 PHE ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL
SEQRES 4 A 415 GLN GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO
SEQRES 5 A 415 ASP LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE
SEQRES 6 A 415 ALA THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP
SEQRES 7 A 415 TYR ARG HIS PHE SER SER GLU CYS PRO PHE ILE PRO ARG
SEQRES 8 A 415 GLU ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET
SEQRES 9 A 415 ASP PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN
SEQRES 10 A 415 GLN VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN
SEQRES 11 A 415 ARG ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU
SEQRES 12 A 415 ARG PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA
SEQRES 13 A 415 GLU PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY
SEQRES 14 A 415 LEU PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR
SEQRES 15 A 415 ASP GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA
SEQRES 16 A 415 GLU ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE
SEQRES 17 A 415 ILE GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE
SEQRES 18 A 415 SER ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE
SEQRES 19 A 415 THR SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU
SEQRES 20 A 415 VAL GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE
SEQRES 21 A 415 SER MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN
SEQRES 22 A 415 GLU LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS
SEQRES 23 A 415 GLU GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY
SEQRES 24 A 415 ARG ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN
SEQRES 25 A 415 LEU LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU
SEQRES 26 A 415 SER GLY LEU ASP GLU ARG GLU ASN ALA CYS PRO MET HIS
SEQRES 27 A 415 VAL ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE
SEQRES 28 A 415 GLY HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA
SEQRES 29 A 415 ARG ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR
SEQRES 30 A 415 ARG ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE
SEQRES 31 A 415 GLN HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU
SEQRES 32 A 415 PRO LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
HET K A 415 1
HET HEM A 417 44
HET CAM A 422 11
HET TRS A 423 8
HETNAM K POTASSIUM ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CAM CAMPHOR
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN HEM HEME
HETSYN TRS TRIS BUFFER
FORMUL 2 K K 1+
FORMUL 3 HEM C34 H32 FE N4 O4
FORMUL 4 CAM C10 H16 O
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 6 HOH *561(H2 O)
HELIX 1 1 PRO A 19 VAL A 23 5 5
HELIX 2 2 ASN A 33 ALA A 36 5 4
HELIX 3 3 GLY A 37 ALA A 43 1 7
HELIX 4 4 VAL A 44 GLU A 47 5 4
HELIX 5 5 ARG A 57 GLY A 61 5 5
HELIX 6 6 ARG A 67 ASP A 77 1 11
HELIX 7 7 PRO A 89 TYR A 96 1 8
HELIX 8 8 GLN A 108 GLY A 120 1 13
HELIX 9 9 GLY A 120 ARG A 143 1 24
HELIX 10 10 PHE A 150 TYR A 154 1 5
HELIX 11 11 GLU A 156 GLY A 168 1 13
HELIX 12 12 PRO A 170 GLU A 172 5 3
HELIX 13 13 ASP A 173 ARG A 186 1 14
HELIX 14 14 THR A 192 LYS A 214 1 23
HELIX 15 15 ASP A 218 ASN A 225 1 8
HELIX 16 16 THR A 234 THR A 252 1 19
HELIX 17 17 THR A 252 SER A 267 1 16
HELIX 18 18 SER A 267 ARG A 277 1 11
HELIX 19 19 ARG A 280 PHE A 292 1 13
HELIX 20 20 PRO A 321 ASP A 328 5 8
HELIX 21 21 HIS A 352 LEU A 356 5 5
HELIX 22 22 GLY A 359 ILE A 378 1 20
HELIX 23 23 ASP A 407 THR A 411 5 5
SHEET 1 A 5 LEU A 53 THR A 56 0
SHEET 2 A 5 HIS A 62 ALA A 65 -1 O HIS A 62 N THR A 56
SHEET 3 A 5 GLN A 317 LEU A 320 1 O LEU A 319 N TRP A 63
SHEET 4 A 5 ASP A 297 LEU A 301 -1 N ARG A 299 O ILE A 318
SHEET 5 A 5 PHE A 81 SER A 82 -1 N SER A 82 O ILE A 300
SHEET 1 B 3 GLN A 147 ASN A 149 0
SHEET 2 B 3 PRO A 403 VAL A 405 -1 O LEU A 404 N CYS A 148
SHEET 3 B 3 SER A 382 ILE A 383 -1 N SER A 382 O VAL A 405
SHEET 1 C 2 GLN A 227 VAL A 228 0
SHEET 2 C 2 ARG A 231 PRO A 232 -1 O ARG A 231 N VAL A 228
SHEET 1 D 2 TYR A 305 PHE A 307 0
SHEET 2 D 2 VAL A 310 LEU A 312 -1 O VAL A 310 N PHE A 307
SHEET 1 E 2 HIS A 391 LYS A 392 0
SHEET 2 E 2 GLY A 398 VAL A 399 -1 O GLY A 398 N LYS A 392
LINK O GLU A 84 K K A 415 1555 1555 2.58
LINK O GLY A 93 K K A 415 1555 1555 2.82
LINK O GLU A 94 K K A 415 1555 1555 2.80
LINK O TYR A 96 K K A 415 1555 1555 2.64
LINK SG CYS A 357 FE HEM A 417 1555 1555 2.38
LINK K K A 415 O HOH A 806 1555 1555 2.84
LINK K K A 415 O HOH A 813 1555 1555 2.75
CISPEP 1 ILE A 88 PRO A 89 0 3.79
CISPEP 2 ILE A 99 PRO A 100 0 6.90
CISPEP 3 PRO A 105 PRO A 106 0 3.29
SITE 1 AC1 6 GLU A 84 GLY A 93 GLU A 94 TYR A 96
SITE 2 AC1 6 HOH A 806 HOH A 813
SITE 1 AC2 21 PRO A 100 THR A 101 GLN A 108 ARG A 112
SITE 2 AC2 21 LEU A 244 LEU A 245 GLY A 248 GLY A 249
SITE 3 AC2 21 THR A 252 ASP A 297 ARG A 299 GLN A 322
SITE 4 AC2 21 THR A 349 PHE A 350 GLY A 351 HIS A 355
SITE 5 AC2 21 CYS A 357 GLY A 359 CAM A 422 HOH A 437
SITE 6 AC2 21 HOH A 659
SITE 1 AC3 5 PHE A 87 TYR A 96 LEU A 244 VAL A 295
SITE 2 AC3 5 HEM A 417
SITE 1 AC4 7 HIS A 21 VAL A 23 PHE A 24 ASN A 49
SITE 2 AC4 7 VAL A 50 PRO A 51 HOH A 802
CRYST1 63.522 63.522 249.670 90.00 90.00 90.00 P 43 21 2 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 0.015743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015743 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
