HEADER OXIDOREDUCTASE 06-MAR-10 3M26
TITLE CRYSTALLOGRAPHIC AND SINGLE CRYSTAL SPECTRAL ANALYSIS OF THE
TITLE 2 PEROXIDASE FERRYL INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 71-361;
COMPND 5 SYNONYM: CCP;
COMPND 6 EC: 1.11.1.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: CCP, CCP1, CPO, YKR066C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PT7
KEYWDS CYTOCHROME C PEROXIDASE (CCP), OXIDOREDUCTASE, HEME, HYDROGEN
KEYWDS 2 PEROXIDE, IRON, METAL-BINDING, MITOCHONDRION, ORGANIC RADICAL,
KEYWDS 3 PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.T.MEHARENNA,T.L.POULOS
REVDAT 4 21-FEB-24 3M26 1 REMARK
REVDAT 3 13-OCT-21 3M26 1 REMARK SEQADV LINK
REVDAT 2 19-MAY-10 3M26 1 REMARK
REVDAT 1 12-MAY-10 3M26 0
JRNL AUTH Y.T.MEHARENNA,T.DOUKOV,H.LI,S.M.SOLTIS,T.L.POULOS
JRNL TITL CRYSTALLOGRAPHIC AND SINGLE-CRYSTAL SPECTRAL ANALYSIS OF THE
JRNL TITL 2 PEROXIDASE FERRYL INTERMEDIATE.
JRNL REF BIOCHEMISTRY V. 49 2984 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20230048
JRNL DOI 10.1021/BI100238R
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.116
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.093
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 57050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 630
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2964.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2206.9
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 36595
REMARK 3 NUMBER OF RESTRAINTS : 33101
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.021
REMARK 3 ANGLE DISTANCES (A) : 0.031
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.068
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.065
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.071
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.047
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.105
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R
REMARK 3 (NO CUTOFF) BY ?
REMARK 4
REMARK 4 3M26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 65
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 19
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78010
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : 0.52700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10UL (350-400UM PROTEIN), 22% MPD,
REMARK 280 50MM TRIS PHOSHATE BUFFER PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277.2K
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 53.63900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.55150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.44350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.55150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.63900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.44350
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 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 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 GLN A 120 C GLY A 121 N 0.199
REMARK 500 ASN A 272 C GLY A 273 N 0.166
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 TYR A 23 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TYR A 23 CG - CD2 - CE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 34 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TRP A 51 CB - CG - CD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TYR A 71 CB - CG - CD2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 PHE A 91 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 MET A 119 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 GLN A 120 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 166 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
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 296 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 HEM A 296 NA 90.5
REMARK 620 3 HEM A 296 NB 88.1 89.7
REMARK 620 4 HEM A 296 NC 87.2 177.7 90.3
REMARK 620 5 HEM A 296 ND 88.1 89.8 176.2 90.0
REMARK 620 6 HOH A1040 O 178.4 89.1 90.3 93.2 93.5
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 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 299
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DSO RELATED DB: PDB
REMARK 900 RELATED ID: 2V23 RELATED DB: PDB
REMARK 900 RELATED ID: 1DSG RELATED DB: PDB
REMARK 900 RELATED ID: 5CCP RELATED DB: PDB
REMARK 900 RELATED ID: 1ZBY RELATED DB: PDB
REMARK 900 RELATED ID: 3E2O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYTOCHROME C PEROXIDASE, N184R MUTANT
REMARK 900 RELATED ID: 3E2N RELATED DB: PDB
REMARK 900 RELATED ID: 3M23 RELATED DB: PDB
REMARK 900 COMPOUND I (1) COMPOSITE STRUCTURE OF CYTOCHROME C PEROXIDASE,
REMARK 900 N184R MUTANT
REMARK 900 RELATED ID: 3M25 RELATED DB: PDB
REMARK 900 COMPOUND I (2) COMPOSITE STRUCTURE OF CYTOCHROME C PEROXIDASE,
REMARK 900 N184R MUTANT
REMARK 900 RELATED ID: 3M27 RELATED DB: PDB
REMARK 900 RELATED ID: 3M28 RELATED DB: PDB
REMARK 900 RELATED ID: 3M29 RELATED DB: PDB
REMARK 900 RELATED ID: 3M2A RELATED DB: PDB
REMARK 900 RELATED ID: 3M2B RELATED DB: PDB
REMARK 900 RELATED ID: 3M2C RELATED DB: PDB
REMARK 900 RELATED ID: 3M2D RELATED DB: PDB
REMARK 900 RELATED ID: 3M2E RELATED DB: PDB
REMARK 900 RELATED ID: 3M2F RELATED DB: PDB
REMARK 900 RELATED ID: 3M2G RELATED DB: PDB
REMARK 900 RELATED ID: 3M2H RELATED DB: PDB
REMARK 900 RELATED ID: 3M2I RELATED DB: PDB
DBREF 3M26 A 4 294 UNP P00431 CCPR_YEAST 71 361
SEQADV 3M26 ARG A 184 UNP P00431 ASN 251 ENGINEERED MUTATION
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 THR 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 ASP 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 HIS ALA LEU GLY LYS THR HIS LEU LYS ARG 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 296 43
HET PO4 A 299 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM PO4 PHOSPHATE ION
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *630(H2 O)
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 ARG A 160 1 11
HELIX 11 11 ASN A 164 GLY A 173 1 10
HELIX 12 12 ALA A 174 LEU A 177 5 4
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 200 GLU A 209 1 10
HELIX 15 15 LEU A 232 ASP A 241 1 10
HELIX 16 16 ASP A 241 ASN A 253 1 13
HELIX 17 17 ASP A 254 ASN A 272 1 19
HELIX 18 18 THR A 288 GLY A 293 1 6
SHEET 1 A 2 HIS A 6 VAL A 7 0
SHEET 2 A 2 ILE A 274 THR A 275 1 O THR A 275 N HIS A 6
SHEET 1 B 2 LYS A 179 THR A 180 0
SHEET 2 B 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 C 3 LYS A 212 LYS A 215 0
SHEET 2 C 3 GLU A 221 ASP A 224 -1 O ASP A 224 N LYS A 212
SHEET 3 C 3 MET A 230 MET A 231 -1 O MET A 231 N TRP A 223
LINK NE2 HIS A 175 FE HEM A 296 1555 1555 2.10
LINK FE HEM A 296 O HOH A1040 1555 1555 1.75
SITE 1 AC1 24 PRO A 44 ARG A 48 TRP A 51 PRO A 145
SITE 2 AC1 24 ASP A 146 ALA A 147 LEU A 171 MET A 172
SITE 3 AC1 24 ALA A 174 HIS A 175 LEU A 177 GLY A 178
SITE 4 AC1 24 LYS A 179 THR A 180 HIS A 181 ARG A 184
SITE 5 AC1 24 SER A 185 TRP A 191 LEU A 232 THR A 234
SITE 6 AC1 24 HOH A 517 HOH A 678 HOH A 679 HOH A1040
SITE 1 AC2 3 ASN A 87 ARG A 184 HOH A1103
CRYST1 107.278 74.887 51.103 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 0.009322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019568 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
