HEADER OXIDOREDUCTASE 24-FEB-97 1AED
TITLE SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE
TITLE 2 SITE OF CYTOCHROME C PEROXIDASE (3,4-DIMETHYLTHIAZOLE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CCP/W191G;
COMPND 5 EC: 1.11.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: CRYSTAL FORM BY
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGANELLE: MITOCHONDRIA;
SOURCE 7 CELLULAR_LOCATION: MITOCHONDRIA;
SOURCE 8 GENE: CCP;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PT7CCP;
SOURCE 14 EXPRESSION_SYSTEM_GENE: CCP (MKT)
KEYWDS OXIDOREDUCTASE, PEROXIDASE, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.MUSAH,G.M.JENSEN,M.M.FITZGERALD,D.E.MCREE,D.B.GOODIN
REVDAT 6 02-AUG-23 1AED 1 REMARK
REVDAT 5 03-NOV-21 1AED 1 REMARK SEQADV LINK
REVDAT 4 04-APR-18 1AED 1 REMARK
REVDAT 3 24-FEB-09 1AED 1 VERSN
REVDAT 2 01-APR-03 1AED 1 JRNL
REVDAT 1 04-SEP-97 1AED 0
JRNL AUTH R.A.MUSAH,G.M.JENSEN,S.W.BUNTE,R.J.ROSENFELD,D.B.GOODIN
JRNL TITL ARTIFICIAL PROTEIN CAVITIES AS SPECIFIC LIGAND-BINDING
JRNL TITL 2 TEMPLATES: CHARACTERIZATION OF AN ENGINEERED HETEROCYCLIC
JRNL TITL 3 CATION-BINDING SITE THAT PRESERVES THE EVOLVED SPECIFICITY
JRNL TITL 4 OF THE PARENT PROTEIN.
JRNL REF J.MOL.BIOL. V. 315 845 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11812152
JRNL DOI 10.1006/JMBI.2001.5287
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.FITZGERALD,M.J.CHURCHILL,D.E.MCREE,D.B.GOODIN
REMARK 1 TITL SMALL MOLECULE BINDING TO AN ARTIFICIALLY CREATED CAVITY AT
REMARK 1 TITL 2 THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE
REMARK 1 REF BIOCHEMISTRY V. 33 3807 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.B.GOODIN,D.E.MCREE
REMARK 1 TITL THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE
REMARK 1 TITL 2 REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF
REMARK 1 TITL 3 THE TRYPTOPHAN FREE RADICAL TO THE HEME
REMARK 1 REF BIOCHEMISTRY V. 32 3313 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XTALVIEW
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.5000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.0
REMARK 3 NUMBER OF REFLECTIONS : 19099
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) : NULL
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 : 2338
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 100
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 1AED 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_1000170712.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-95
REMARK 200 TEMPERATURE (KELVIN) : 290
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : XENGEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20736
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2400
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) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XTALVIEW
REMARK 200 STARTING MODEL: PDB ENTRY 1AA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% MPD, 40 MM PHOSPHATE PH 6.0. A
REMARK 280 SINGLE CRYSTAL OF W191G WAS SOAKED IN 50MM 3,4-
REMARK 280 DIMETHYLTHIAZOLIUM IODIDE IN 40% MPD AND 60 MM PHOSPHATE AT PH
REMARK 280 4.5.
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 54.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.65000
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 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 MET A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
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 LYS A 12 NZ
REMARK 470 LYS A 260 NZ
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 6 NE2 HIS A 6 CD2 -0.070
REMARK 500 HIS A 60 NE2 HIS A 60 CD2 -0.067
REMARK 500 HIS A 96 NE2 HIS A 96 CD2 -0.069
REMARK 500 HIS A 175 NE2 HIS A 175 CD2 -0.069
REMARK 500 HIS A 181 NE2 HIS A 181 CD2 -0.072
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 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 51 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 51 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 TRP A 51 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 51 CG - CD2 - CE3 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 57 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 57 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR A 71 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TRP A 101 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 101 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 126 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP A 126 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 127 CB - CG - CD ANGL. DEV. = -19.2 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 130 CG - CD - NE ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASN A 162 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASN A 162 CA - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG A 166 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 211 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 211 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP A 223 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 223 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR A 229 CB - CG - CD2 ANGL. DEV. = -3.8 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 ASN A 141 153.53 -48.19
REMARK 500 ASN A 162 75.82 -2.32
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 295 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 HEM A 295 NA 91.5
REMARK 620 3 HEM A 295 NB 93.9 89.9
REMARK 620 4 HEM A 295 NC 89.0 178.6 88.8
REMARK 620 5 HEM A 295 ND 85.9 90.6 179.5 90.7
REMARK 620 6 HOH A 313 O 176.8 88.5 89.2 91.1 91.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AVE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: REMOVAL OF TRP 191 FORMS AN INTERNAL CAVITY
REMARK 800 BELOW THE HEME RELATIVE TO THE ACTIVE SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTI A 296
DBREF 1AED A 4 294 UNP P00431 CCPR_YEAST 71 361
SEQADV 1AED ILE A 53 UNP P00431 THR 120 VARIANT
SEQADV 1AED GLY A 152 UNP P00431 ASP 219 VARIANT
SEQADV 1AED GLY A 191 UNP P00431 TRP 258 ENGINEERED MUTATION
SEQADV 1AED ASP A 272 UNP P00431 ASN 339 CONFLICT
SEQRES 1 A 294 MET LYS THR LEU VAL HIS VAL ALA SER VAL GLU LYS GLY
SEQRES 2 A 294 ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE
SEQRES 3 A 294 ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR
SEQRES 4 A 294 ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS
SEQRES 5 A 294 ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY
SEQRES 6 A 294 SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN
SEQRES 7 A 294 ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE
SEQRES 8 A 294 LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER
SEQRES 9 A 294 GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN
SEQRES 10 A 294 GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG
SEQRES 11 A 294 VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG
SEQRES 12 A 294 LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL ARG THR
SEQRES 13 A 294 PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL
SEQRES 14 A 294 ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU
SEQRES 15 A 294 LYS ASN SER GLY TYR GLU GLY PRO GLY GLY ALA ALA ASN
SEQRES 16 A 294 ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN
SEQRES 17 A 294 GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU
SEQRES 18 A 294 GLN TRP ASP SER LYS SER GLY TYR MET MET LEU PRO THR
SEQRES 19 A 294 ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE
SEQRES 20 A 294 VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS
SEQRES 21 A 294 ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU ASP GLY
SEQRES 22 A 294 ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE
SEQRES 23 A 294 LYS THR LEU GLU GLU GLN GLY LEU
HET HEM A 295 43
HET DTI A 296 15
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM DTI 3,4-DIMETHYLTHIAZOLIUM ION
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 DTI C5 H8 N S 1+
FORMUL 4 HOH *100(H2 O)
HELIX 1 A SER A 15 ASP A 33 1 19
HELIX 2 B TYR A 42 SER A 54 1 13
HELIX 3 B1 PHE A 73 ASN A 78 1 6
HELIX 4 C GLY A 84 PHE A 99 1 16
HELIX 5 D SER A 103 MET A 119 1 17
HELIX 6 E ASP A 150 PHE A 158 1 9
HELIX 7 F ASN A 164 LEU A 177 1 14
HELIX 8 F1 HIS A 181 GLY A 186 1 6
HELIX 9 G GLU A 201 GLU A 209 1 9
HELIX 10 H LEU A 232 GLN A 240 1 9
HELIX 11 I ASP A 241 ASN A 253 1 13
HELIX 12 J GLN A 255 ASP A 272 1 18
HELIX 13 J1 THR A 288 GLY A 293 1 6
SHEET 1 A 2 TRP A 211 LYS A 215 0
SHEET 2 A 2 GLU A 221 SER A 225 -1 N ASP A 224 O LYS A 212
LINK NE2 HIS A 175 FE HEM A 295 1555 1555 2.00
LINK FE HEM A 295 O HOH A 313 1555 1555 1.95
SITE 1 AVE 3 ARG A 48 TRP A 51 HIS A 52
SITE 1 AC1 21 PRO A 44 VAL A 47 ARG A 48 TRP A 51
SITE 2 AC1 21 PRO A 145 ASP A 146 MET A 172 ALA A 174
SITE 3 AC1 21 HIS A 175 LEU A 177 GLY A 178 LYS A 179
SITE 4 AC1 21 THR A 180 HIS A 181 ASN A 184 SER A 185
SITE 5 AC1 21 DTI A 296 HOH A 302 HOH A 311 HOH A 313
SITE 6 AC1 21 HOH A 314
SITE 1 AC2 8 HIS A 175 LYS A 179 THR A 180 GLY A 191
SITE 2 AC2 8 LEU A 232 ASP A 235 HEM A 295 HOH A 405
CRYST1 108.000 77.300 51.800 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 0.009259 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
