HEADER OXIDOREDUCTASE 26-SEP-04 1XK0
TITLE CRYSTAL STRUCTURES OF THE G139A, G139A-NO AND G143H MUTANTS OF HUMAN
TITLE 2 HEME OXYGENASE-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME OXYGENASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HO-1;
COMPND 5 EC: 1.14.99.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HMOX1, HO1, HO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEME, HEME DEGREDATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LAD,A.KOSHKIN,P.R.ORTIZ DE MONTELLANO,T.L.POULOS
REVDAT 5 14-FEB-24 1XK0 1 REMARK
REVDAT 4 20-OCT-21 1XK0 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1XK0 1 VERSN
REVDAT 2 13-DEC-05 1XK0 1 AUTHOR
REVDAT 1 06-DEC-05 1XK0 0
JRNL AUTH L.LAD,A.KOSHKIN,P.R.ORTIZ DE MONTELLANO,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF THE G139A, G139A-NO AND G143H MUTANTS
JRNL TITL 2 OF HUMAN HEME OXYGENASE-1. A FINELY TUNED HYDROGEN-BONDING
JRNL TITL 3 NETWORK CONTROLS OXYGENASE VERSUS PEROXIDASE ACTIVITY.
JRNL REF J.BIOL.INORG.CHEM. V. 10 138 2005
JRNL REFN ISSN 0949-8257
JRNL PMID 15690204
JRNL DOI 10.1007/S00775-004-0620-6
REMARK 2
REMARK 2 RESOLUTION. 2.18 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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 : 29654
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) : 0.224
REMARK 3 FREE R VALUE : 0.266
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 : 3488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 161
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) : 0.006
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 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 1XK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
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) : 1.53
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 29654
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02000
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) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, HEPES, HEXANE DIOL
REMARK 280 , PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 27.03000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.64950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.98400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.64950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.03000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.98400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 GLU A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 6
REMARK 465 ASP A 7
REMARK 465 SER A 8
REMARK 465 MET A 9
REMARK 465 ASP A 224
REMARK 465 THR A 225
REMARK 465 LYS A 226
REMARK 465 ASP A 227
REMARK 465 GLN A 228
REMARK 465 SER A 229
REMARK 465 PRO A 230
REMARK 465 SER A 231
REMARK 465 ARG A 232
REMARK 465 ALA A 233
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 5
REMARK 465 PRO B 6
REMARK 465 ASP B 7
REMARK 465 SER B 8
REMARK 465 MET B 9
REMARK 465 ASP B 224
REMARK 465 THR B 225
REMARK 465 LYS B 226
REMARK 465 ASP B 227
REMARK 465 GLN B 228
REMARK 465 SER B 229
REMARK 465 PRO B 230
REMARK 465 SER B 231
REMARK 465 ARG B 232
REMARK 465 ALA B 233
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU B 183 O HOH B 361 2.19
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 GLN A 41 92.01 -66.51
REMARK 500 PHE A 74 -30.17 -145.55
REMARK 500 SER A 159 32.47 -71.17
REMARK 500 GLN B 11 -75.23 -67.22
REMARK 500 GLN B 145 -86.34 -61.60
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 25 NE2
REMARK 620 2 HEM A 300 NA 86.2
REMARK 620 3 HEM A 300 NB 95.4 90.0
REMARK 620 4 HEM A 300 NC 99.4 174.1 87.6
REMARK 620 5 HEM A 300 ND 89.4 90.5 175.3 91.4
REMARK 620 6 NO A 400 N 167.1 83.9 92.8 90.9 82.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 300 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 25 NE2
REMARK 620 2 HEM B 300 NA 86.5
REMARK 620 3 HEM B 300 NB 96.2 89.6
REMARK 620 4 HEM B 300 NC 91.4 177.9 90.6
REMARK 620 5 HEM B 300 ND 88.7 89.6 175.0 90.3
REMARK 620 N 1 2 3 4
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 HEM B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XJZ RELATED DB: PDB
REMARK 900 RELATED ID: 1XK1 RELATED DB: PDB
REMARK 900 RELATED ID: 1XK2 RELATED DB: PDB
REMARK 900 RELATED ID: 1XK3 RELATED DB: PDB
DBREF 1XK0 A 1 233 UNP P09601 HMOX1_HUMAN 1 233
DBREF 1XK0 B 1 233 UNP P09601 HMOX1_HUMAN 1 233
SEQADV 1XK0 ALA A 139 UNP P09601 GLY 139 ENGINEERED MUTATION
SEQADV 1XK0 GLU A 183 UNP P09601 ARG 183 CONFLICT
SEQADV 1XK0 ALA B 139 UNP P09601 GLY 139 ENGINEERED MUTATION
SEQADV 1XK0 GLU B 183 UNP P09601 ARG 183 CONFLICT
SEQRES 1 A 233 MET GLU ARG PRO GLN PRO ASP SER MET PRO GLN ASP LEU
SEQRES 2 A 233 SER GLU ALA LEU LYS GLU ALA THR LYS GLU VAL HIS THR
SEQRES 3 A 233 GLN ALA GLU ASN ALA GLU PHE MET ARG ASN PHE GLN LYS
SEQRES 4 A 233 GLY GLN VAL THR ARG ASP GLY PHE LYS LEU VAL MET ALA
SEQRES 5 A 233 SER LEU TYR HIS ILE TYR VAL ALA LEU GLU GLU GLU ILE
SEQRES 6 A 233 GLU ARG ASN LYS GLU SER PRO VAL PHE ALA PRO VAL TYR
SEQRES 7 A 233 PHE PRO GLU GLU LEU HIS ARG LYS ALA ALA LEU GLU GLN
SEQRES 8 A 233 ASP LEU ALA PHE TRP TYR GLY PRO ARG TRP GLN GLU VAL
SEQRES 9 A 233 ILE PRO TYR THR PRO ALA MET GLN ARG TYR VAL LYS ARG
SEQRES 10 A 233 LEU HIS GLU VAL GLY ARG THR GLU PRO GLU LEU LEU VAL
SEQRES 11 A 233 ALA HIS ALA TYR THR ARG TYR LEU ALA ASP LEU SER GLY
SEQRES 12 A 233 GLY GLN VAL LEU LYS LYS ILE ALA GLN LYS ALA LEU ASP
SEQRES 13 A 233 LEU PRO SER SER GLY GLU GLY LEU ALA PHE PHE THR PHE
SEQRES 14 A 233 PRO ASN ILE ALA SER ALA THR LYS PHE LYS GLN LEU TYR
SEQRES 15 A 233 GLU SER ARG MET ASN SER LEU GLU MET THR PRO ALA VAL
SEQRES 16 A 233 ARG GLN ARG VAL ILE GLU GLU ALA LYS THR ALA PHE LEU
SEQRES 17 A 233 LEU ASN ILE GLN LEU PHE GLU GLU LEU GLN GLU LEU LEU
SEQRES 18 A 233 THR HIS ASP THR LYS ASP GLN SER PRO SER ARG ALA
SEQRES 1 B 233 MET GLU ARG PRO GLN PRO ASP SER MET PRO GLN ASP LEU
SEQRES 2 B 233 SER GLU ALA LEU LYS GLU ALA THR LYS GLU VAL HIS THR
SEQRES 3 B 233 GLN ALA GLU ASN ALA GLU PHE MET ARG ASN PHE GLN LYS
SEQRES 4 B 233 GLY GLN VAL THR ARG ASP GLY PHE LYS LEU VAL MET ALA
SEQRES 5 B 233 SER LEU TYR HIS ILE TYR VAL ALA LEU GLU GLU GLU ILE
SEQRES 6 B 233 GLU ARG ASN LYS GLU SER PRO VAL PHE ALA PRO VAL TYR
SEQRES 7 B 233 PHE PRO GLU GLU LEU HIS ARG LYS ALA ALA LEU GLU GLN
SEQRES 8 B 233 ASP LEU ALA PHE TRP TYR GLY PRO ARG TRP GLN GLU VAL
SEQRES 9 B 233 ILE PRO TYR THR PRO ALA MET GLN ARG TYR VAL LYS ARG
SEQRES 10 B 233 LEU HIS GLU VAL GLY ARG THR GLU PRO GLU LEU LEU VAL
SEQRES 11 B 233 ALA HIS ALA TYR THR ARG TYR LEU ALA ASP LEU SER GLY
SEQRES 12 B 233 GLY GLN VAL LEU LYS LYS ILE ALA GLN LYS ALA LEU ASP
SEQRES 13 B 233 LEU PRO SER SER GLY GLU GLY LEU ALA PHE PHE THR PHE
SEQRES 14 B 233 PRO ASN ILE ALA SER ALA THR LYS PHE LYS GLN LEU TYR
SEQRES 15 B 233 GLU SER ARG MET ASN SER LEU GLU MET THR PRO ALA VAL
SEQRES 16 B 233 ARG GLN ARG VAL ILE GLU GLU ALA LYS THR ALA PHE LEU
SEQRES 17 B 233 LEU ASN ILE GLN LEU PHE GLU GLU LEU GLN GLU LEU LEU
SEQRES 18 B 233 THR HIS ASP THR LYS ASP GLN SER PRO SER ARG ALA
HET HEM A 300 43
HET NO A 400 2
HET HEM B 300 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NO NITRIC OXIDE
HETSYN HEM HEME
HETSYN NO NITROGEN MONOXIDE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 NO N O
FORMUL 6 HOH *161(H2 O)
HELIX 1 1 ASP A 12 THR A 21 1 10
HELIX 2 2 THR A 21 ASN A 30 1 10
HELIX 3 3 ALA A 31 LYS A 39 1 9
HELIX 4 4 THR A 43 LYS A 69 1 27
HELIX 5 5 PHE A 74 TYR A 78 5 5
HELIX 6 6 PHE A 79 HIS A 84 1 6
HELIX 7 7 ARG A 85 GLY A 98 1 14
HELIX 8 8 ARG A 100 ILE A 105 1 6
HELIX 9 9 THR A 108 GLU A 125 1 18
HELIX 10 10 LEU A 128 GLY A 143 1 16
HELIX 11 11 GLY A 143 ASP A 156 1 14
HELIX 12 12 LEU A 164 THR A 168 5 5
HELIX 13 13 SER A 174 LEU A 189 1 16
HELIX 14 14 THR A 192 THR A 222 1 31
HELIX 15 15 ASP B 12 THR B 21 1 10
HELIX 16 16 THR B 21 ASN B 30 1 10
HELIX 17 17 ALA B 31 GLY B 40 1 10
HELIX 18 18 THR B 43 LYS B 69 1 27
HELIX 19 19 PHE B 74 TYR B 78 5 5
HELIX 20 20 PHE B 79 HIS B 84 1 6
HELIX 21 21 ARG B 85 GLY B 98 1 14
HELIX 22 22 ARG B 100 ILE B 105 1 6
HELIX 23 23 THR B 108 GLU B 125 1 18
HELIX 24 24 LEU B 128 ASP B 156 1 29
HELIX 25 25 LEU B 164 THR B 168 5 5
HELIX 26 26 SER B 174 ASN B 187 1 14
HELIX 27 27 THR B 192 HIS B 223 1 32
LINK NE2 HIS A 25 FE HEM A 300 1555 1555 2.15
LINK FE HEM A 300 N NO A 400 1555 1555 1.97
LINK NE2 HIS B 25 FE HEM B 300 1555 1555 2.11
SITE 1 AC1 13 LYS A 18 HIS A 25 GLU A 29 MET A 34
SITE 2 AC1 13 GLN A 38 TYR A 134 THR A 135 ALA A 139
SITE 3 AC1 13 PHE A 207 ASN A 210 PHE A 214 NO A 400
SITE 4 AC1 13 HOH A 419
SITE 1 AC2 13 LYS B 18 HIS B 25 GLU B 29 GLN B 38
SITE 2 AC2 13 TYR B 134 ARG B 136 ALA B 139 LYS B 179
SITE 3 AC2 13 GLU B 183 PHE B 207 ASN B 210 PHE B 214
SITE 4 AC2 13 HOH B 361
SITE 1 AC3 4 ALA A 139 GLY A 143 HEM A 300 HOH A 455
CRYST1 54.060 75.968 105.299 90.00 90.00 90.00 P 21 21 21 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 0.018498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
