HEADER OXIDOREDUCTASE(OXYGENASE) 23-NOV-93 1CPT
TITLE CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3
TITLE 2 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450-TERP;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 306
KEYWDS OXIDOREDUCTASE(OXYGENASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.HASEMANN,K.G.RAVICHANDRAN,J.A.PETERSON,J.DEISENHOFER
REVDAT 4 07-FEB-24 1CPT 1 REMARK LINK
REVDAT 3 24-FEB-09 1CPT 1 VERSN
REVDAT 2 01-APR-03 1CPT 1 JRNL
REVDAT 1 31-JAN-94 1CPT 0
JRNL AUTH C.A.HASEMANN,K.G.RAVICHANDRAN,J.A.PETERSON,J.DEISENHOFER
JRNL TITL CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450TERP AT
JRNL TITL 2 2.3 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 236 1169 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8120894
JRNL DOI 10.1016/0022-2836(94)90019-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.S.BODDUPALLI,C.A.HASEMANN,K.G.RAVICHANDRAN,J.-Y.LU,
REMARK 1 AUTH 2 E.J.GOLDSMITH,J.DEISENHOFER,J.A.PETERSON
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION ANALYSIS
REMARK 1 TITL 2 OF P450-TERP AND THE HEMOPROTEIN DOMAIN OF P450-BM-3,
REMARK 1 TITL 3 ENZYMES BELONGING TO TWO DISTINCT CLASSES OF THE CYTOCHROME
REMARK 1 TITL 4 P450 SUPERFAMILY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 5567 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.A.PETERSON,J.-Y.LU,J.GEISSELSODER,S.GRAHAM-LORENCE,
REMARK 1 AUTH 2 C.CARMONA,F.WITNEY,M.C.LORENCE
REMARK 1 TITL CYTOCHROME P450-TERP: ISOLATION AND PURIFICATION OF THE
REMARK 1 TITL 2 PROTEIN AND CLONING AND SEQUENCING OF ITS OPERON
REMARK 1 REF J.BIOL.CHEM. V. 267 14193 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3249
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 2.980
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 152.18333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 304.36667
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 228.27500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 380.45833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.09167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 152.18333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 304.36667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 380.45833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 228.27500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 76.09167
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 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 HIS A 191
REMARK 465 GLU A 192
REMARK 465 PRO A 193
REMARK 465 ASP A 194
REMARK 465 GLU A 195
REMARK 465 GLN A 196
REMARK 465 ALA A 197
REMARK 465 VAL A 198
REMARK 465 ALA A 199
REMARK 465 ALA A 200
REMARK 465 PRO A 201
REMARK 465 ARG A 202
REMARK 465 GLN A 203
REMARK 465 SER A 204
REMARK 465 ALA A 205
REMARK 465 ASP A 206
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 GLU A 207 CG CD OE1 OE2
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 HIS A 44 NE2 HIS A 44 CD2 -0.077
REMARK 500 HIS A 97 NE2 HIS A 97 CD2 -0.070
REMARK 500 HIS A 110 NE2 HIS A 110 CD2 -0.073
REMARK 500 HIS A 213 NE2 HIS A 213 CD2 -0.067
REMARK 500 HIS A 269 NE2 HIS A 269 CD2 -0.072
REMARK 500 HIS A 367 NE2 HIS A 367 CD2 -0.073
REMARK 500 HIS A 381 NE2 HIS A 381 CD2 -0.074
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 MET A 1 CA - CB - CG ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 4 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TRP A 33 CD1 - CG - CD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TRP A 33 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TRP A 52 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 52 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TYR A 80 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 VAL A 98 CA - CB - CG2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 TYR A 113 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TRP A 120 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 120 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 161 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP A 310 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 310 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 MET A 318 CG - SD - CE ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 337 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 348 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 372 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 372 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 372 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 HIS A 381 CE1 - NE2 - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 MET A 387 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASP A 2 105.38 56.78
REMARK 500 GLN A 66 72.70 -112.04
REMARK 500 SER A 90 -70.61 -65.82
REMARK 500 ASP A 100 73.47 -101.12
REMARK 500 MET A 154 -73.65 -73.31
REMARK 500 CYS A 157 -77.28 -150.07
REMARK 500 HIS A 269 -70.01 -96.82
REMARK 500 ARG A 366 60.20 -100.01
REMARK 500 CYS A 377 107.24 -38.39
REMARK 500 PHE A 414 -80.56 -124.89
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 430 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 377 SG
REMARK 620 2 HEM A 430 NA 99.3
REMARK 620 3 HEM A 430 NB 87.9 89.2
REMARK 620 4 HEM A 430 NC 82.0 178.7 91.0
REMARK 620 5 HEM A 430 ND 97.2 90.6 174.9 89.1
REMARK 620 6 HOH A 440 O 175.1 83.4 88.0 95.3 86.9
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 430
DBREF 1CPT A 1 428 UNP P33006 CPXL_PSESP 1 428
SEQRES 1 A 428 MET ASP ALA ARG ALA THR ILE PRO GLU HIS ILE ALA ARG
SEQRES 2 A 428 THR VAL ILE LEU PRO GLN GLY TYR ALA ASP ASP GLU VAL
SEQRES 3 A 428 ILE TYR PRO ALA PHE LYS TRP LEU ARG ASP GLU GLN PRO
SEQRES 4 A 428 LEU ALA MET ALA HIS ILE GLU GLY TYR ASP PRO MET TRP
SEQRES 5 A 428 ILE ALA THR LYS HIS ALA ASP VAL MET GLN ILE GLY LYS
SEQRES 6 A 428 GLN PRO GLY LEU PHE SER ASN ALA GLU GLY SER GLU ILE
SEQRES 7 A 428 LEU TYR ASP GLN ASN ASN GLU ALA PHE MET ARG SER ILE
SEQRES 8 A 428 SER GLY GLY CYS PRO HIS VAL ILE ASP SER LEU THR SER
SEQRES 9 A 428 MET ASP PRO PRO THR HIS THR ALA TYR ARG GLY LEU THR
SEQRES 10 A 428 LEU ASN TRP PHE GLN PRO ALA SER ILE ARG LYS LEU GLU
SEQRES 11 A 428 GLU ASN ILE ARG ARG ILE ALA GLN ALA SER VAL GLN ARG
SEQRES 12 A 428 LEU LEU ASP PHE ASP GLY GLU CYS ASP PHE MET THR ASP
SEQRES 13 A 428 CYS ALA LEU TYR TYR PRO LEU HIS VAL VAL MET THR ALA
SEQRES 14 A 428 LEU GLY VAL PRO GLU ASP ASP GLU PRO LEU MET LEU LYS
SEQRES 15 A 428 LEU THR GLN ASP PHE PHE GLY VAL HIS GLU PRO ASP GLU
SEQRES 16 A 428 GLN ALA VAL ALA ALA PRO ARG GLN SER ALA ASP GLU ALA
SEQRES 17 A 428 ALA ARG ARG PHE HIS GLU THR ILE ALA THR PHE TYR ASP
SEQRES 18 A 428 TYR PHE ASN GLY PHE THR VAL ASP ARG ARG SER CYS PRO
SEQRES 19 A 428 LYS ASP ASP VAL MET SER LEU LEU ALA ASN SER LYS LEU
SEQRES 20 A 428 ASP GLY ASN TYR ILE ASP ASP LYS TYR ILE ASN ALA TYR
SEQRES 21 A 428 TYR VAL ALA ILE ALA THR ALA GLY HIS ASP THR THR SER
SEQRES 22 A 428 SER SER SER GLY GLY ALA ILE ILE GLY LEU SER ARG ASN
SEQRES 23 A 428 PRO GLU GLN LEU ALA LEU ALA LYS SER ASP PRO ALA LEU
SEQRES 24 A 428 ILE PRO ARG LEU VAL ASP GLU ALA VAL ARG TRP THR ALA
SEQRES 25 A 428 PRO VAL LYS SER PHE MET ARG THR ALA LEU ALA ASP THR
SEQRES 26 A 428 GLU VAL ARG GLY GLN ASN ILE LYS ARG GLY ASP ARG ILE
SEQRES 27 A 428 MET LEU SER TYR PRO SER ALA ASN ARG ASP GLU GLU VAL
SEQRES 28 A 428 PHE SER ASN PRO ASP GLU PHE ASP ILE THR ARG PHE PRO
SEQRES 29 A 428 ASN ARG HIS LEU GLY PHE GLY TRP GLY ALA HIS MET CYS
SEQRES 30 A 428 LEU GLY GLN HIS LEU ALA LYS LEU GLU MET LYS ILE PHE
SEQRES 31 A 428 PHE GLU GLU LEU LEU PRO LYS LEU LYS SER VAL GLU LEU
SEQRES 32 A 428 SER GLY PRO PRO ARG LEU VAL ALA THR ASN PHE VAL GLY
SEQRES 33 A 428 GLY PRO LYS ASN VAL PRO ILE ARG PHE THR LYS ALA
HET HEM A 430 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *221(H2 O)
HELIX 1 A3 GLN A 19 ALA A 22 5 4
HELIX 2 A' GLU A 9 ILE A 16 1 8
HELIX 3 A ASP A 24 GLU A 37 1 14
HELIX 4 B HIS A 57 LYS A 65 1 9
HELIX 5 B' GLN A 82 ILE A 91 1 10
HELIX 6 B3 LEU A 102 SER A 104 5 3
HELIX 7 C PRO A 108 LEU A 118 1 11
HELIX 8 C' PRO A 123 ILE A 126 1 4
HELIX 9 C3 ARG A 127 LEU A 129 5 3
HELIX 10 D GLU A 130 LEU A 145 1 16
HELIX 11 E' PHE A 153 ASP A 156 1 4
HELIX 12 E TYR A 160 LEU A 170 1 11
HELIX 13 D3 GLU A 174 ASP A 176 5 3
HELIX 14 F GLU A 177 GLN A 185 1 9
HELIX 15 G ALA A 208 ARG A 231 1 24
HELIX 16 H VAL A 238 ASN A 244 1 7
HELIX 17 I ASP A 254 ARG A 285 1 32
HELIX 18 J PRO A 287 SER A 295 1 9
HELIX 19 E3 PRO A 297 LEU A 299 5 3
HELIX 20 K ILE A 300 THR A 311 1 12
HELIX 21 K' TYR A 342 ASN A 346 1 5
HELIX 22 L GLN A 380 LEU A 394 1 15
HELIX 23 F3 LEU A 395 LYS A 397 5 3
SHEET 1 1 5 PRO A 39 ALA A 43 0
SHEET 2 1 5 PRO A 50 THR A 55 -1
SHEET 3 1 5 GLY A 335 SER A 341 1
SHEET 4 1 5 PHE A 317 LEU A 322 -1
SHEET 5 1 5 LEU A 69 SER A 71 -1
SHEET 1 2 2 THR A 325 VAL A 327 0
SHEET 2 2 2 GLN A 330 ILE A 332 -1
SHEET 1 3 3 GLY A 149 PHE A 153 0
SHEET 2 3 3 VAL A 421 ALA A 428 -1
SHEET 3 3 3 LYS A 397 SER A 404 -1
SHEET 1 4 2 ARG A 408 VAL A 410 0
SHEET 2 4 2 GLY A 417 ASN A 420 -1
SHEET 1 5 2 SER A 245 LEU A 247 0
SHEET 2 5 2 ASN A 250 ILE A 252 -1
LINK SG CYS A 377 FE HEM A 430 1555 1555 2.15
LINK FE HEM A 430 O HOH A 440 1555 1555 2.09
CISPEP 1 PRO A 107 PRO A 108 0 1.72
CISPEP 2 PHE A 363 PRO A 364 0 -17.24
SITE 1 AC1 27 LEU A 102 THR A 103 HIS A 110 ARG A 114
SITE 2 AC1 27 ALA A 267 GLY A 268 THR A 271 SER A 275
SITE 3 AC1 27 PRO A 313 VAL A 314 PHE A 317 ARG A 319
SITE 4 AC1 27 TYR A 342 GLY A 369 PHE A 370 GLY A 371
SITE 5 AC1 27 TRP A 372 HIS A 375 MET A 376 CYS A 377
SITE 6 AC1 27 GLY A 379 LEU A 382 MET A 387 HOH A 440
SITE 7 AC1 27 HOH A 522 HOH A 554 HOH A 590
CRYST1 69.440 69.440 456.550 90.00 90.00 120.00 P 61 2 2 12
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 0.014401 0.008314 0.000000 0.00000
SCALE2 0.000000 0.016629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
