HEADER OXIDOREDUCTASE 13-NOV-00 1GEI
TITLE STRUCTURAL CHARACTERIZATION OF N-BUTYL-ISOCYANIDE COMPLEXES OF
TITLE 2 CYTOCHROMES P450NOR AND P450CAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 55A1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.14.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;
SOURCE 3 ORGANISM_TAXID: 5507;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSET-C
KEYWDS CYTOCROME P450NOR (FE-II), ISOCYANIDE COMPLEXE FORM, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.-S.LEE,S.-Y.PARK,K.YAMANE,Y.SHIRO
REVDAT 6 25-OCT-23 1GEI 1 REMARK LINK
REVDAT 5 24-FEB-09 1GEI 1 VERSN
REVDAT 4 01-APR-03 1GEI 1 JRNL
REVDAT 3 21-JAN-03 1GEI 1 REMARK
REVDAT 2 25-APR-01 1GEI 1 JRNL
REVDAT 1 29-NOV-00 1GEI 0
JRNL AUTH D.S.LEE,S.Y.PARK,K.YAMANE,E.OBAYASHI,H.HORI,Y.SHIRO
JRNL TITL STRUCTURAL CHARACTERIZATION OF N-BUTYL-ISOCYANIDE COMPLEXES
JRNL TITL 2 OF CYTOCHROMES P450NOR AND P450CAM.
JRNL REF BIOCHEMISTRY V. 40 2669 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11258878
JRNL DOI 10.1021/BI002225S
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.-Y.PARK,H.SHIMIZU,S.ADACHI,A.NAKAGAWA,I.TANAKA,K.NAKAHARA,
REMARK 1 AUTH 2 H.SHOUN,E.OBAYASHI,H.NAKAMURA,T.IIZUKA,Y.SHIRO
REMARK 1 TITL CRYSTAL STRUCTURE OF NITRIC OXIDE REDUCTASE FROM DENITRIFING
REMARK 1 TITL 2 FUNGUS FUSARIUM OXYSPORUM
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 827 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.207
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2372
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 324
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.70
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
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 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 1GEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000005077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.7
REMARK 200 MONOCHROMATOR : SI-111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47202
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1ROM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 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 27.37500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.11500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.11500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.37500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.82000
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 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
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 LYS A 49 CG - CD - CE ANGL. DEV. = -18.7 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 ASN A 29 70.79 -158.48
REMARK 500 ALA A 80 -9.24 -59.37
REMARK 500 CYS A 133 19.16 -150.51
REMARK 500 PHE A 144 -60.39 -143.51
REMARK 500 LYS A 207 -168.56 -123.19
REMARK 500 CYS A 352 120.69 -31.56
REMARK 500 ALA A 379 46.94 -89.11
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 352 SG
REMARK 620 2 HEM A 501 NA 94.6
REMARK 620 3 HEM A 501 NB 90.8 88.7
REMARK 620 4 HEM A 501 NC 84.0 178.1 90.0
REMARK 620 5 HEM A 501 ND 91.3 91.1 177.9 90.2
REMARK 620 6 NBN A 502 C 173.5 82.5 83.4 98.7 94.6
REMARK 620 7 NBN A 502 N 173.6 81.0 84.5 100.3 93.4 1.9
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBN A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GEJ RELATED DB: PDB
REMARK 900 1GEJ CONTAINS CYTOCHROME P450 55A1 (FE-III).
REMARK 900 RELATED ID: 1GEK RELATED DB: PDB
REMARK 900 1GEK CONTAINS CYTOCHROME P450CAM (FE-II).
REMARK 900 RELATED ID: 1GEM RELATED DB: PDB
REMARK 900 1GEM CONTAINS CYTOCHROME P450CAM (FE-III).
DBREF 1GEI A 1 403 UNP P23295 NOR_FUSOX 1 403
SEQRES 1 A 403 MET ALA SER GLY ALA PRO SER PHE PRO PHE SER ARG ALA
SEQRES 2 A 403 SER GLY PRO GLU PRO PRO ALA GLU PHE ALA LYS LEU ARG
SEQRES 3 A 403 ALA THR ASN PRO VAL SER GLN VAL LYS LEU PHE ASP GLY
SEQRES 4 A 403 SER LEU ALA TRP LEU VAL THR LYS HIS LYS ASP VAL CYS
SEQRES 5 A 403 PHE VAL ALA THR SER GLU LYS LEU SER LYS VAL ARG THR
SEQRES 6 A 403 ARG GLN GLY PHE PRO GLU LEU SER ALA SER GLY LYS GLN
SEQRES 7 A 403 ALA ALA LYS ALA LYS PRO THR PHE VAL ASP MET ASP PRO
SEQRES 8 A 403 PRO GLU HIS MET HIS GLN ARG SER MET VAL GLU PRO THR
SEQRES 9 A 403 PHE THR PRO GLU ALA VAL LYS ASN LEU GLN PRO TYR ILE
SEQRES 10 A 403 GLN ARG THR VAL ASP ASP LEU LEU GLU GLN MET LYS GLN
SEQRES 11 A 403 LYS GLY CYS ALA ASN GLY PRO VAL ASP LEU VAL LYS GLU
SEQRES 12 A 403 PHE ALA LEU PRO VAL PRO SER TYR ILE ILE TYR THR LEU
SEQRES 13 A 403 LEU GLY VAL PRO PHE ASN ASP LEU GLU TYR LEU THR GLN
SEQRES 14 A 403 GLN ASN ALA ILE ARG THR ASN GLY SER SER THR ALA ARG
SEQRES 15 A 403 GLU ALA SER ALA ALA ASN GLN GLU LEU LEU ASP TYR LEU
SEQRES 16 A 403 ALA ILE LEU VAL GLU GLN ARG LEU VAL GLU PRO LYS ASP
SEQRES 17 A 403 ASP ILE ILE SER LYS LEU CYS THR GLU GLN VAL LYS PRO
SEQRES 18 A 403 GLY ASN ILE ASP LYS SER ASP ALA VAL GLN ILE ALA PHE
SEQRES 19 A 403 LEU LEU LEU VAL ALA GLY ASN ALA THR MET VAL ASN MET
SEQRES 20 A 403 ILE ALA LEU GLY VAL ALA THR LEU ALA GLN HIS PRO ASP
SEQRES 21 A 403 GLN LEU ALA GLN LEU LYS ALA ASN PRO SER LEU ALA PRO
SEQRES 22 A 403 GLN PHE VAL GLU GLU LEU CYS ARG TYR HIS THR ALA SER
SEQRES 23 A 403 ALA LEU ALA ILE LYS ARG THR ALA LYS GLU ASP VAL MET
SEQRES 24 A 403 ILE GLY ASP LYS LEU VAL ARG ALA ASN GLU GLY ILE ILE
SEQRES 25 A 403 ALA SER ASN GLN SER ALA ASN ARG ASP GLU GLU VAL PHE
SEQRES 26 A 403 GLU ASN PRO ASP GLU PHE ASN MET ASN ARG LYS TRP PRO
SEQRES 27 A 403 PRO GLN ASP PRO LEU GLY PHE GLY PHE GLY ASP HIS ARG
SEQRES 28 A 403 CYS ILE ALA GLU HIS LEU ALA LYS ALA GLU LEU THR THR
SEQRES 29 A 403 VAL PHE SER THR LEU TYR GLN LYS PHE PRO ASP LEU LYS
SEQRES 30 A 403 VAL ALA VAL PRO LEU GLY LYS ILE ASN TYR THR PRO LEU
SEQRES 31 A 403 ASN ARG ASP VAL GLY ILE VAL ASP LEU PRO VAL ILE PHE
HET HEM A 501 43
HET NBN A 502 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NBN N-BUTYL ISOCYANIDE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 NBN C5 H9 N
FORMUL 4 HOH *285(H2 O)
HELIX 1 1 ALA A 20 ASN A 29 1 10
HELIX 2 2 LYS A 47 SER A 57 1 11
HELIX 3 3 SER A 73 ALA A 80 1 8
HELIX 4 4 THR A 85 MET A 89 5 5
HELIX 5 5 PRO A 92 SER A 99 1 8
HELIX 6 6 MET A 100 PHE A 105 5 6
HELIX 7 7 THR A 106 LYS A 131 1 26
HELIX 8 8 LEU A 140 PHE A 144 1 5
HELIX 9 9 LEU A 146 GLY A 158 1 13
HELIX 10 10 PRO A 160 ASN A 162 5 3
HELIX 11 11 ASP A 163 ASN A 176 1 14
HELIX 12 12 THR A 180 GLU A 205 1 26
HELIX 13 13 ASP A 209 GLN A 218 1 10
HELIX 14 14 ASP A 225 HIS A 258 1 34
HELIX 15 15 HIS A 258 ASN A 268 1 11
HELIX 16 16 LEU A 271 HIS A 283 1 13
HELIX 17 17 SER A 314 ASN A 319 1 6
HELIX 18 18 ALA A 354 SER A 367 1 14
HELIX 19 19 THR A 368 PHE A 373 1 6
HELIX 20 20 PRO A 381 ILE A 385 5 5
SHEET 1 A 5 VAL A 31 LYS A 35 0
SHEET 2 A 5 LEU A 41 VAL A 45 -1 O ALA A 42 N VAL A 34
SHEET 3 A 5 GLY A 310 ALA A 313 1 O GLY A 310 N TRP A 43
SHEET 4 A 5 LYS A 291 ALA A 294 -1 O ARG A 292 N ILE A 311
SHEET 5 A 5 LEU A 60 SER A 61 -1 N SER A 61 O THR A 293
SHEET 1 B 3 VAL A 138 ASP A 139 0
SHEET 2 B 3 PRO A 400 ILE A 402 -1 N VAL A 401 O VAL A 138
SHEET 3 B 3 LYS A 377 VAL A 378 -1 N LYS A 377 O ILE A 402
SHEET 1 C 2 VAL A 298 ILE A 300 0
SHEET 2 C 2 LYS A 303 VAL A 305 -1 O LYS A 303 N ILE A 300
SHEET 1 D 2 ASN A 386 TYR A 387 0
SHEET 2 D 2 ILE A 396 ASP A 398 -1 N VAL A 397 O ASN A 386
LINK SG CYS A 352 FE HEM A 501 1555 1555 2.36
LINK FE HEM A 501 C NBN A 502 1555 1555 1.85
LINK FE HEM A 501 N NBN A 502 1555 1555 2.93
CISPEP 1 PHE A 8 PRO A 9 0 0.46
CISPEP 2 PRO A 91 PRO A 92 0 -0.01
SITE 1 AC1 24 PHE A 86 VAL A 87 HIS A 94 ARG A 98
SITE 2 AC1 24 PHE A 105 ILE A 153 LEU A 236 ALA A 239
SITE 3 AC1 24 GLY A 240 THR A 243 MET A 244 MET A 247
SITE 4 AC1 24 SER A 286 GLY A 344 PHE A 345 GLY A 346
SITE 5 AC1 24 PHE A 347 HIS A 350 CYS A 352 ALA A 354
SITE 6 AC1 24 NBN A 502 HOH A 514 HOH A 532 HOH A 572
SITE 1 AC2 4 ALA A 239 GLY A 240 SER A 286 HEM A 501
CRYST1 54.750 81.640 86.230 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 0.018265 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
