HEADER OXIDOREDUCTASE 14-SEP-98 1BU7
TITLE CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CYTOCHROME P450);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN;
COMPND 5 SYNONYM: FATTY ACID HYDROXYLASE;
COMPND 6 EC: 1.14.14.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 7 OTHER_DETAILS: SYNTHETIC GENE
KEYWDS FATTY ACID MONOOXYGENASE, HEMOPROTEIN, P450, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 7 07-FEB-24 1BU7 1 REMARK LINK
REVDAT 6 24-FEB-09 1BU7 1 VERSN
REVDAT 5 01-APR-03 1BU7 1 JRNL
REVDAT 4 03-MAY-00 1BU7 1 REMARK
REVDAT 3 26-APR-00 1BU7 1 KEYWDS REMARK
REVDAT 2 29-DEC-99 1BU7 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 23-SEP-98 1BU7 0
JRNL AUTH I.F.SEVRIOUKOVA,H.LI,H.ZHANG,J.A.PETERSON,T.L.POULOS
JRNL TITL STRUCTURE OF A CYTOCHROME P450-REDOX PARTNER
JRNL TITL 2 ELECTRON-TRANSFER COMPLEX.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 1863 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 10051560
JRNL DOI 10.1073/PNAS.96.5.1863
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.LI,T.L.POULOS
REMARK 1 TITL MODELING PROTEIN-SUBSTRATE INTERACTIONS IN THE HEME DOMAIN
REMARK 1 TITL 2 OF P450BM-3
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 51 21 1995
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM, 2.5%
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.197
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3055
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 128265
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.189
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2795
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 118023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 142
REMARK 3 SOLVENT ATOMS : 998
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 ANGLE DISTANCES (A) : 0.023
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
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: NULL
REMARK 4
REMARK 4 1BU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : YES
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128585
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 3.80000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 22.0000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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 (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 75.95000
REMARK 290 SMTRY3 2 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 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 O HOH B 1318 O HOH B 1343 2.09
REMARK 500 O HOH A 1026 O HOH A 1358 2.10
REMARK 500 O HOH A 1078 O HOH A 1157 2.15
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 50 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU A 148 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 398 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG B 167 CD - NE - CZ ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 398 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG B 398 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 425 CB - CG - OD1 ANGL. DEV. = 9.5 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 LYS A 15 -134.22 56.88
REMARK 500 ASP A 84 40.12 -102.28
REMARK 500 PHE A 158 29.05 -151.59
REMARK 500 ASP A 231 40.33 -91.09
REMARK 500 ASP A 370 39.98 -89.36
REMARK 500 THR A 436 -127.95 -123.67
REMARK 500 LYS B 15 -126.59 53.69
REMARK 500 ASP B 84 42.78 -101.93
REMARK 500 ASP B 231 35.72 -89.88
REMARK 500 ASP B 370 38.46 -78.83
REMARK 500 THR B 436 -131.61 -131.66
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 999 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 999 NA 96.5
REMARK 620 3 HEM A 999 NB 91.0 90.1
REMARK 620 4 HEM A 999 NC 85.1 178.3 89.5
REMARK 620 5 HEM A 999 ND 95.5 89.3 173.5 90.8
REMARK 620 6 HOH A1020 O 174.0 86.7 84.0 91.6 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1000 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B1000 NA 98.9
REMARK 620 3 HEM B1000 NB 89.5 92.3
REMARK 620 4 HEM B1000 NC 85.5 175.2 89.6
REMARK 620 5 HEM B1000 ND 93.5 87.8 176.9 90.1
REMARK 620 6 HOH B1380 O 175.8 80.6 86.3 95.2 90.7
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 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1014
DBREF 1BU7 A 1 455 UNP P14779 CPXB_BACME 1 455
DBREF 1BU7 B 1 455 UNP P14779 CPXB_BACME 1 455
SEQRES 1 A 455 THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY GLU
SEQRES 2 A 455 LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO VAL
SEQRES 3 A 455 GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU ILE
SEQRES 4 A 455 PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR LEU
SEQRES 5 A 455 SER SER GLN ARG LEU ILE LYS GLU ALA CYS ASP GLU SER
SEQRES 6 A 455 ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE VAL
SEQRES 7 A 455 ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP THR
SEQRES 8 A 455 HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN ILE LEU LEU
SEQRES 9 A 455 PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS ALA
SEQRES 10 A 455 MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS TRP
SEQRES 11 A 455 GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO GLU
SEQRES 12 A 455 ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU CYS
SEQRES 13 A 455 GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP GLN
SEQRES 14 A 455 PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU ASP
SEQRES 15 A 455 GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP ASP
SEQRES 16 A 455 PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU ASP
SEQRES 17 A 455 ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE ALA
SEQRES 18 A 455 ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU LEU
SEQRES 19 A 455 THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY GLU
SEQRES 20 A 455 PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE THR
SEQRES 21 A 455 PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU LEU
SEQRES 22 A 455 SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS VAL
SEQRES 23 A 455 LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU VAL
SEQRES 24 A 455 ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU LYS
SEQRES 25 A 455 TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU TRP
SEQRES 26 A 455 PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU ASP
SEQRES 27 A 455 THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY ASP
SEQRES 28 A 455 GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP LYS
SEQRES 29 A 455 THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO GLU
SEQRES 30 A 455 ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA PHE
SEQRES 31 A 455 LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS ILE GLY GLN
SEQRES 32 A 455 GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY MET
SEQRES 33 A 455 MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN TYR
SEQRES 34 A 455 GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO GLU
SEQRES 35 A 455 GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO LEU
SEQRES 1 B 455 THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY GLU
SEQRES 2 B 455 LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO VAL
SEQRES 3 B 455 GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU ILE
SEQRES 4 B 455 PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR LEU
SEQRES 5 B 455 SER SER GLN ARG LEU ILE LYS GLU ALA CYS ASP GLU SER
SEQRES 6 B 455 ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE VAL
SEQRES 7 B 455 ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP THR
SEQRES 8 B 455 HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN ILE LEU LEU
SEQRES 9 B 455 PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS ALA
SEQRES 10 B 455 MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS TRP
SEQRES 11 B 455 GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO GLU
SEQRES 12 B 455 ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU CYS
SEQRES 13 B 455 GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP GLN
SEQRES 14 B 455 PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU ASP
SEQRES 15 B 455 GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP ASP
SEQRES 16 B 455 PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU ASP
SEQRES 17 B 455 ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE ALA
SEQRES 18 B 455 ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU LEU
SEQRES 19 B 455 THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY GLU
SEQRES 20 B 455 PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE THR
SEQRES 21 B 455 PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU LEU
SEQRES 22 B 455 SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS VAL
SEQRES 23 B 455 LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU VAL
SEQRES 24 B 455 ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU LYS
SEQRES 25 B 455 TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU TRP
SEQRES 26 B 455 PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU ASP
SEQRES 27 B 455 THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY ASP
SEQRES 28 B 455 GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP LYS
SEQRES 29 B 455 THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO GLU
SEQRES 30 B 455 ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA PHE
SEQRES 31 B 455 LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS ILE GLY GLN
SEQRES 32 B 455 GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY MET
SEQRES 33 B 455 MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN TYR
SEQRES 34 B 455 GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO GLU
SEQRES 35 B 455 GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO LEU
HET HEM A 999 43
HET EDO A1001 4
HET EDO A1002 4
HET EDO A1003 4
HET EDO A1008 4
HET EDO A1013 4
HET EDO A1014 4
HET HEM B1000 43
HET EDO B1004 4
HET EDO B1005 4
HET EDO B1006 4
HET EDO B1007 4
HET EDO B1009 4
HET EDO B1010 4
HET EDO B1011 4
HET EDO B1012 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HEM HEME
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 EDO 14(C2 H6 O2)
FORMUL 19 HOH *998(H2 O)
HELIX 1 1 GLY A 12 LEU A 14 5 3
HELIX 2 2 LEU A 17 LEU A 20 5 4
HELIX 3 3 PRO A 25 LEU A 36 1 12
HELIX 4 4 GLN A 55 ALA A 61 1 7
HELIX 5 5 GLN A 73 ALA A 82 1 10
HELIX 6 6 LEU A 86 THR A 88 5 3
HELIX 7 7 LYS A 94 PHE A 107 1 14
HELIX 8 8 GLN A 109 GLU A 131 1 23
HELIX 9 9 VAL A 141 PHE A 158 1 18
HELIX 10 10 SER A 164 TYR A 166 5 3
HELIX 11 11 PRO A 172 GLN A 189 1 18
HELIX 12 12 PRO A 196 SER A 226 5 31
HELIX 13 13 LEU A 233 ASN A 239 1 7
HELIX 14 14 ASP A 251 LYS A 282 1 32
HELIX 15 15 PRO A 284 VAL A 297 1 14
HELIX 16 16 TYR A 305 GLN A 310 1 6
HELIX 17 17 LYS A 312 LEU A 324 1 13
HELIX 18 18 ILE A 357 ARG A 362 1 6
HELIX 19 19 LYS A 364 TRP A 367 1 4
HELIX 20 20 PRO A 376 PHE A 379 5 4
HELIX 21 21 PRO A 382 ALA A 384 5 3
HELIX 22 22 GLY A 396 ARG A 398 5 3
HELIX 23 23 GLN A 403 HIS A 420 1 18
HELIX 24 24 GLY B 12 LEU B 14 5 3
HELIX 25 25 LEU B 17 LEU B 20 5 4
HELIX 26 26 PRO B 25 LEU B 36 1 12
HELIX 27 27 GLN B 55 ALA B 61 1 7
HELIX 28 28 GLN B 73 ALA B 82 1 10
HELIX 29 29 LEU B 86 THR B 88 5 3
HELIX 30 30 LYS B 94 PHE B 107 1 14
HELIX 31 31 GLN B 110 ARG B 132 5 23
HELIX 32 32 VAL B 141 PHE B 158 1 18
HELIX 33 33 SER B 164 TYR B 166 5 3
HELIX 34 34 PRO B 172 GLN B 189 1 18
HELIX 35 35 PRO B 196 SER B 226 5 31
HELIX 36 36 LEU B 233 ASN B 239 1 7
HELIX 37 37 ASP B 251 LYS B 282 1 32
HELIX 38 38 PRO B 284 VAL B 297 1 14
HELIX 39 39 TYR B 305 GLN B 310 1 6
HELIX 40 40 LYS B 312 LEU B 324 1 13
HELIX 41 41 LEU B 341 GLY B 343 5 3
HELIX 42 42 ILE B 357 ARG B 362 1 6
HELIX 43 43 LYS B 364 TRP B 367 1 4
HELIX 44 44 PRO B 376 PHE B 379 5 4
HELIX 45 45 PRO B 382 ALA B 384 5 3
HELIX 46 46 GLY B 396 ARG B 398 5 3
HELIX 47 47 GLN B 403 HIS B 420 1 18
SHEET 1 A 5 ILE A 39 ALA A 44 0
SHEET 2 A 5 ARG A 47 LEU A 52 -1 N TYR A 51 O PHE A 40
SHEET 3 A 5 GLU A 352 LEU A 356 1 N GLU A 352 O ARG A 50
SHEET 4 A 5 ALA A 330 ALA A 335 -1 N LEU A 333 O LEU A 353
SHEET 5 A 5 PHE A 67 LYS A 69 -1 N ASP A 68 O TYR A 334
SHEET 1 B 2 THR A 339 LEU A 341 0
SHEET 2 B 2 TYR A 345 LEU A 347 -1 N LEU A 347 O THR A 339
SHEET 1 C 2 PHE A 421 GLU A 424 0
SHEET 2 C 2 LYS A 447 SER A 450 -1 N LYS A 449 O ASP A 422
SHEET 1 D 2 ILE A 433 GLU A 435 0
SHEET 2 D 2 LEU A 439 PRO A 441 -1 N LYS A 440 O LYS A 434
SHEET 1 E 5 ILE B 39 ALA B 44 0
SHEET 2 E 5 ARG B 47 LEU B 52 -1 N TYR B 51 O PHE B 40
SHEET 3 E 5 GLU B 352 LEU B 356 1 N MET B 354 O ARG B 50
SHEET 4 E 5 ALA B 330 ALA B 335 -1 N LEU B 333 O LEU B 353
SHEET 5 E 5 PHE B 67 LYS B 69 -1 N ASP B 68 O TYR B 334
SHEET 1 F 2 THR B 339 LEU B 341 0
SHEET 2 F 2 TYR B 345 LEU B 347 -1 N LEU B 347 O THR B 339
SHEET 1 G 2 PHE B 421 GLU B 424 0
SHEET 2 G 2 LYS B 447 SER B 450 -1 N LYS B 449 O ASP B 422
SHEET 1 H 2 ILE B 433 GLU B 435 0
SHEET 2 H 2 LEU B 439 PRO B 441 -1 N LYS B 440 O LYS B 434
LINK SG CYS A 400 FE HEM A 999 1555 1555 2.38
LINK FE HEM A 999 O HOH A1020 1555 1555 2.57
LINK SG CYS B 400 FE HEM B1000 1555 1555 2.27
LINK FE HEM B1000 O HOH B1380 1555 1555 2.69
SITE 1 AC1 24 LYS A 69 LEU A 86 PHE A 87 TRP A 96
SITE 2 AC1 24 GLY A 265 THR A 268 THR A 269 PHE A 331
SITE 3 AC1 24 PRO A 392 PHE A 393 GLY A 394 ARG A 398
SITE 4 AC1 24 ALA A 399 CYS A 400 ILE A 401 GLY A 402
SITE 5 AC1 24 ALA A 406 HOH A1020 HOH A1039 HOH A1058
SITE 6 AC1 24 HOH A1087 HOH A1093 HOH A1173 HOH A1197
SITE 1 AC2 25 LYS B 69 LEU B 86 TRP B 96 ALA B 264
SITE 2 AC2 25 GLY B 265 THR B 268 THR B 269 THR B 327
SITE 3 AC2 25 PHE B 331 PRO B 392 PHE B 393 GLY B 394
SITE 4 AC2 25 ARG B 398 ALA B 399 CYS B 400 ILE B 401
SITE 5 AC2 25 GLY B 402 ALA B 406 HOH B1023 HOH B1055
SITE 6 AC2 25 HOH B1105 HOH B1144 HOH B1151 HOH B1152
SITE 7 AC2 25 HOH B1380
SITE 1 AC3 7 HIS A 100 GLY A 396 GLN A 397 ALA A 399
SITE 2 AC3 7 ILE A 401 HOH A1093 HOH A1399
SITE 1 AC4 4 GLU A 137 LYS A 447 ALA A 448 EDO A1003
SITE 1 AC5 4 TRP A 130 LEU A 133 ALA A 448 EDO A1002
SITE 1 AC6 6 HIS B 100 GLN B 397 ALA B 399 ILE B 401
SITE 2 AC6 6 HOH B1015 HOH B1151
SITE 1 AC7 5 TRP B 130 LEU B 133 ALA B 448 EDO B1006
SITE 2 AC7 5 HOH B1061
SITE 1 AC8 5 ASN B 134 GLU B 137 ALA B 448 EDO B1005
SITE 2 AC8 5 HOH B1321
SITE 1 AC9 9 THR B 245 GLY B 246 GLU B 247 VAL B 281
SITE 2 AC9 9 ASP B 425 ASN B 428 HOH B1171 HOH B1358
SITE 3 AC9 9 HOH B1392
SITE 1 BC1 4 LYS A 289 GLU A 292 GLU A 293 ARG A 296
SITE 1 BC2 3 ARG B 47 SER B 72 GLN B 73
SITE 1 BC3 2 PRO B 25 TYR B 51
SITE 1 BC4 3 GLN B 27 LYS B 31 HOH B1227
SITE 1 BC5 7 LEU B 181 ILE B 263 ALA B 264 HIS B 266
SITE 2 BC5 7 LEU B 437 HOH B1237 HOH B1429
SITE 1 BC6 7 VAL A 26 PRO A 329 GLU A 435 THR A 436
SITE 2 BC6 7 LEU A 437 HOH A1262 HOH A1414
SITE 1 BC7 3 TRP A 90 HIS A 92 TYR A 334
CRYST1 59.380 151.900 62.770 90.00 96.02 90.00 P 1 21 1 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 0.016841 0.000000 0.001776 0.00000
SCALE2 0.000000 0.006583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016019 0.00000
MTRIX1 1 -0.994274 0.024948 -0.103912 85.49720 1
MTRIX2 1 0.016992 -0.923091 -0.384206 197.64560 1
MTRIX3 1 -0.105506 -0.383772 0.917381 44.49530 1
(ATOM LINES ARE NOT SHOWN.)
END
