HEADER OXIDOREDUCTASE(H2O2(A)) 04-MAY-94 1CCE
TITLE CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS
TITLE 2 LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.11.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS OXIDOREDUCTASE(H2O2(A))
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.MCREE,G.M.JENSEN,M.M.FITZGERALD,H.A.SIEGEL,D.B.GOODIN
REVDAT 4 07-FEB-24 1CCE 1 REMARK SEQADV LINK
REVDAT 3 29-NOV-17 1CCE 1 HELIX
REVDAT 2 24-FEB-09 1CCE 1 VERSN
REVDAT 1 31-JUL-94 1CCE 0
JRNL AUTH D.E.MCREE,G.M.JENSEN,M.M.FITZGERALD,H.A.SIEGEL,D.B.GOODIN
JRNL TITL CONSTRUCTION OF A BISAQUO HEME ENZYME AND BINDING BY
JRNL TITL 2 EXOGENOUS LIGANDS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 91 12847 1994
JRNL REFN ISSN 0027-8424
JRNL PMID 7809133
JRNL DOI 10.1073/PNAS.91.26.12847
REMARK 1
REMARK 1 REFERENCE 1
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. 2.30 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) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 12701
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) : 0.190
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 : 2342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 86
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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 3.100
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 1CCE 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_1000172226.
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 (%): 54.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 52.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 22.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 22.70000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.15000
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 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 -0.068
REMARK 500 HIS A 52 NE2 HIS A 52 CD2 -0.067
REMARK 500 HIS A 60 NE2 HIS A 60 CD2 -0.070
REMARK 500 HIS A 96 NE2 HIS A 96 CD2 -0.077
REMARK 500 HIS A 181 NE2 HIS A 181 CD2 -0.071
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 14 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TYR A 16 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TRP A 51 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 51 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 57 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 57 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP A 101 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 101 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TRP A 101 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 126 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 MET A 163 CG - SD - CE ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG A 166 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET A 172 CG - SD - CE ANGL. DEV. = -13.9 DEGREES
REMARK 500 TRP A 191 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 191 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 TRP A 211 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 211 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 TRP A 223 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 223 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TYR A 229 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR A 244 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 251 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TYR A 251 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 LYS A 278 CA - CB - CG ANGL. DEV. = -15.7 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 33 46.57 -94.88
REMARK 500 MET A 119 30.73 -88.35
REMARK 500 ASP A 148 40.41 -80.69
REMARK 500 ASN A 162 64.21 22.70
REMARK 500 ALA A 174 2.57 -66.28
REMARK 500 ASN A 195 12.52 -68.35
REMARK 500 ASN A 196 24.47 -152.15
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 1 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 313 O
REMARK 620 2 HEM A 1 NA 83.8
REMARK 620 3 HEM A 1 NB 87.2 87.9
REMARK 620 4 HEM A 1 NC 96.3 178.4 90.5
REMARK 620 5 HEM A 1 ND 91.3 91.3 178.4 90.3
REMARK 620 6 HOH A 387 O 176.4 94.8 96.1 85.2 85.4
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 1
DBREF 1CCE A 4 294 UNP P00431 CCPR_YEAST 71 361
SEQADV 1CCE ILE A 53 UNP P00431 THR 120 CONFLICT
SEQADV 1CCE GLY A 152 UNP P00431 ASP 219 CONFLICT
SEQADV 1CCE GLY A 175 UNP P00431 HIS 242 CONFLICT
SEQRES 1 A 291 LEU VAL HIS VAL ALA SER VAL GLU LYS GLY ARG SER TYR
SEQRES 2 A 291 GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE ALA LEU LYS
SEQRES 3 A 291 LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR ILE GLY TYR
SEQRES 4 A 291 GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS ILE SER GLY
SEQRES 5 A 291 THR TRP ASP LYS HIS ASP ASN THR GLY GLY SER TYR GLY
SEQRES 6 A 291 GLY THR TYR ARG PHE LYS LYS GLU PHE ASN ASP PRO SER
SEQRES 7 A 291 ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE LEU GLU PRO
SEQRES 8 A 291 ILE HIS LYS GLU PHE PRO TRP ILE SER SER GLY ASP LEU
SEQRES 9 A 291 PHE SER LEU GLY GLY VAL THR ALA VAL GLN GLU MET GLN
SEQRES 10 A 291 GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG VAL ASP THR
SEQRES 11 A 291 PRO GLU ASP THR THR PRO ASP ASN GLY ARG LEU PRO ASP
SEQRES 12 A 291 ALA ASP LYS ASP ALA GLY TYR VAL ARG THR PHE PHE GLN
SEQRES 13 A 291 ARG LEU ASN MET ASN ASP ARG GLU VAL VAL ALA LEU MET
SEQRES 14 A 291 GLY ALA GLY ALA LEU GLY LYS THR HIS LEU LYS ASN SER
SEQRES 15 A 291 GLY TYR GLU GLY PRO TRP GLY ALA ALA ASN ASN VAL PHE
SEQRES 16 A 291 THR ASN GLU PHE TYR LEU ASN LEU LEU ASN GLU ASP TRP
SEQRES 17 A 291 LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU GLN TRP ASP
SEQRES 18 A 291 SER LYS SER GLY TYR MET MET LEU PRO THR ASP TYR SER
SEQRES 19 A 291 LEU ILE GLN ASP PRO LYS TYR LEU SER ILE VAL LYS GLU
SEQRES 20 A 291 TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS ASP PHE SER
SEQRES 21 A 291 LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY ILE THR PHE
SEQRES 22 A 291 PRO LYS ASP ALA PRO SER PRO PHE ILE PHE LYS THR LEU
SEQRES 23 A 291 GLU GLU GLN GLY LEU
HET HEM A 1 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *86(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 1BENT AT PRO 94 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 ASN A 272 1 18
HELIX 13 J1 THR A 288 GLY A 293 1 6
SHEET 1 A 2 LYS A 179 THR A 180 0
SHEET 2 A 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 B 3 TRP A 211 LYS A 215 0
SHEET 2 B 3 GLU A 221 SER A 225 -1 N GLN A 222 O GLU A 214
SHEET 3 B 3 MET A 230 MET A 231 -1 N MET A 231 O TRP A 223
LINK FE HEM A 1 O HOH A 313 1555 1555 2.02
LINK FE HEM A 1 O HOH A 387 1555 1555 2.01
SITE 1 AC1 20 PRO A 44 VAL A 47 ARG A 48 TRP A 51
SITE 2 AC1 20 ASP A 146 LEU A 171 ALA A 174 LEU A 177
SITE 3 AC1 20 GLY A 178 LYS A 179 THR A 180 HIS A 181
SITE 4 AC1 20 ASN A 184 SER A 185 THR A 234 HOH A 302
SITE 5 AC1 20 HOH A 311 HOH A 313 HOH A 314 HOH A 387
CRYST1 105.200 74.300 45.400 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 0.009506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013459 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022026 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
