HEADER OXIDOREDUCTASE 18-APR-03 1P3V
TITLE CRYSTAL STRUCTURES OF THE NO-AND CO-BOUND HEME OXYGENASE FROM
TITLE 2 NEISSERIA MENINGITIDIS: IMPLICATIONS FOR OXYGEN ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME OXYGENASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HO-1; HEME OXYGENASE (DECYCLIZING) 1;
COMPND 5 EC: 1.14.99.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: HEME-COMPLEXED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 GENE: HEMO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PWMZ1651
KEYWDS HEME OXYGENASE, HEME DEGRADATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FRIEDMAN,L.LAD,R.DESHMUKH,H.LI,A.WILKS,T.L.POULOS
REVDAT 4 16-AUG-23 1P3V 1 REMARK LINK
REVDAT 3 16-NOV-11 1P3V 1 VERSN HETATM
REVDAT 2 24-FEB-09 1P3V 1 VERSN
REVDAT 1 09-DEC-03 1P3V 0
JRNL AUTH J.FRIEDMAN,L.LAD,R.DESHMUKH,H.LI,A.WILKS,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF THE NO- AND CO-BOUND HEME OXYGENASE
JRNL TITL 2 FROM NEISSERIAE MENINGITIDIS. IMPLICATIONS FOR O2 ACTIVATION
JRNL REF J.BIOL.CHEM. V. 278 34654 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12819228
JRNL DOI 10.1074/JBC.M302985200
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 9467
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 SET) : 0.249
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 505
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 9.26
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3157
REMARK 3 BIN FREE R VALUE : 0.3409
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 47
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 : 1578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.74
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.402
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1P3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 119
REMARK 200 PH : 8.5
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 : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9467
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : 0.59900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.390
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1J77
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, SODIUM ACETATE, PEG 3350, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 51.18050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.22450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.22450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.77075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.22450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.22450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.59025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.22450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.22450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.77075
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.22450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.22450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.59025
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 51.18050
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 452 LIES ON A SPECIAL POSITION.
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 SER A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 ASN A 6
REMARK 465 GLN A 7
REMARK 465 HIS A 207
REMARK 465 ARG A 208
REMARK 465 HIS A 209
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 LEU A 9 -90.95 -80.90
REMARK 500 GLN A 34 71.96 45.38
REMARK 500 LEU A 88 46.09 -99.80
REMARK 500 PRO A 92 104.33 -55.52
REMARK 500 TYR A 93 147.56 -36.90
REMARK 500 ALA A 121 -8.96 -57.03
REMARK 500 LEU A 131 12.22 -64.63
REMARK 500 ASP A 132 32.31 74.27
REMARK 500 ASN A 134 -168.00 -162.00
REMARK 500 ASN A 164 79.69 34.64
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 300 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 23 NE2
REMARK 620 2 HEM A 300 NA 94.4
REMARK 620 3 HEM A 300 NB 100.1 89.2
REMARK 620 4 HEM A 300 NC 90.0 175.3 88.4
REMARK 620 5 HEM A 300 ND 85.4 92.9 174.0 89.0
REMARK 620 6 CMO A 400 C 176.5 86.0 83.4 89.6 91.1
REMARK 620 7 CMO A 400 O 175.7 89.7 79.2 85.8 95.2 5.7
REMARK 620 N 1 2 3 4 5 6
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 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OYK RELATED DB: PDB
REMARK 900 RELATED ID: 1OYL RELATED DB: PDB
REMARK 900 RELATED ID: 1OZE RELATED DB: PDB
REMARK 900 RELATED ID: 1OZL RELATED DB: PDB
REMARK 900 RELATED ID: 1OZR RELATED DB: PDB
REMARK 900 RELATED ID: 1OZW RELATED DB: PDB
REMARK 900 RELATED ID: 1P3T RELATED DB: PDB
REMARK 900 RELATED ID: 1P3U RELATED DB: PDB
DBREF 1P3V A 1 209 UNP Q9RGD9 Q9RGD9_NEIME 22 230
SEQRES 1 A 209 MET SER GLU THR GLU ASN GLN ALA LEU THR PHE ALA LYS
SEQRES 2 A 209 ARG LEU LYS ALA ASP THR THR ALA VAL HIS ASP SER VAL
SEQRES 3 A 209 ASP ASN LEU VAL MET SER VAL GLN PRO PHE VAL SER LYS
SEQRES 4 A 209 GLU ASN TYR ILE LYS PHE LEU LYS LEU GLN SER VAL PHE
SEQRES 5 A 209 HIS LYS ALA VAL ASP HIS ILE TYR LYS ASP ALA GLU LEU
SEQRES 6 A 209 ASN LYS ALA ILE PRO GLU LEU GLU TYR MET ALA ARG TYR
SEQRES 7 A 209 ASP ALA VAL THR GLN ASP LEU LYS ASP LEU GLY GLU GLU
SEQRES 8 A 209 PRO TYR LYS PHE ASP LYS GLU LEU PRO TYR GLU ALA GLY
SEQRES 9 A 209 ASN LYS ALA ILE GLY TRP LEU TYR CYS ALA GLU GLY SER
SEQRES 10 A 209 ASN LEU GLY ALA ALA PHE LEU PHE LYS HIS ALA GLN LYS
SEQRES 11 A 209 LEU ASP TYR ASN GLY GLU HIS GLY ALA ARG HIS LEU ALA
SEQRES 12 A 209 PRO HIS PRO ASP GLY ARG GLY LYS HIS TRP ARG ALA PHE
SEQRES 13 A 209 VAL GLU HIS LEU ASN ALA LEU ASN LEU THR PRO GLU ALA
SEQRES 14 A 209 GLU ALA GLU ALA ILE GLN GLY ALA ARG GLU ALA PHE ALA
SEQRES 15 A 209 PHE TYR LYS VAL VAL LEU ARG GLU THR PHE GLY LEU ALA
SEQRES 16 A 209 ALA ASP ALA GLU ALA PRO GLU GLY MET MET PRO HIS ARG
SEQRES 17 A 209 HIS
HET HEM A 300 43
HET CMO A 400 2
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CMO CARBON MONOXIDE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CMO C O
FORMUL 4 HOH *52(H2 O)
HELIX 1 1 THR A 10 VAL A 33 1 24
HELIX 2 2 SER A 38 LYS A 61 1 24
HELIX 3 3 ASP A 62 ILE A 69 1 8
HELIX 4 4 GLU A 71 ALA A 76 5 6
HELIX 5 5 ARG A 77 LEU A 88 1 12
HELIX 6 6 ALA A 103 ALA A 121 1 19
HELIX 7 7 ALA A 121 LEU A 131 1 11
HELIX 8 8 ALA A 139 ALA A 143 5 5
HELIX 9 9 GLY A 148 LEU A 163 1 16
HELIX 10 10 THR A 166 PHE A 192 1 27
LINK NE2 HIS A 23 FE HEM A 300 1555 1555 2.16
LINK FE HEM A 300 C CMO A 400 1555 1555 1.97
LINK FE HEM A 300 O CMO A 400 1555 1555 3.14
SITE 1 AC1 15 LYS A 16 HIS A 23 ASP A 27 VAL A 30
SITE 2 AC1 15 MET A 31 TYR A 112 CYS A 113 GLY A 116
SITE 3 AC1 15 SER A 117 LEU A 119 GLY A 120 PHE A 123
SITE 4 AC1 15 LEU A 124 TYR A 184 CMO A 400
SITE 1 AC2 4 SER A 117 GLY A 120 ALA A 121 HEM A 300
CRYST1 60.449 60.449 102.361 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 0.016543 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009769 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
