HEADER OXIDOREDUCTASE 05-JAN-02 1J51
TITLE CRYSTAL STRUCTURE OF CYTOCHROME P450CAM MUTANT (F87W/Y96F/V247L/C334A)
TITLE 2 WITH 1,3,5-TRICHLOROBENZENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450CAM;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CAMPHOR 5-MONOOXYGENASE;
COMPND 5 EC: 1.14.15.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCHX
KEYWDS CYTOCHROME P450-CAM, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.CHEN,A.CHRISTOPHER,J.JONES,Q.GUO,F.XU,R.CAO,L.L.WONG,Z.RAO
REVDAT 6 27-DEC-23 1J51 1 REMARK
REVDAT 5 10-NOV-21 1J51 1 REMARK SEQADV LINK
REVDAT 4 20-JUN-18 1J51 1 AUTHOR JRNL REMARK
REVDAT 3 24-FEB-09 1J51 1 VERSN
REVDAT 2 17-JUN-03 1J51 1 JRNL
REVDAT 1 23-JAN-02 1J51 0
JRNL AUTH X.CHEN,A.CHRISTOPHER,J.P.JONES,S.G.BELL,Q.GUO,F.XU,Z.RAO,
JRNL AUTH 2 L.L.WONG
JRNL TITL CRYSTAL STRUCTURE OF THE F87W/Y96F/V247L MUTANT OF
JRNL TITL 2 CYTOCHROME P-450CAM WITH 1,3,5-TRICHLOROBENZENE BOUND AND
JRNL TITL 3 FURTHER PROTEIN ENGINEERING FOR THE OXIDATION OF
JRNL TITL 4 PENTACHLOROBENZENE AND HEXACHLOROBENZENE
JRNL REF J.BIOL.CHEM. V. 277 37519 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12114516
JRNL DOI 10.1074/JBC.M203762200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.20
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) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 285817
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) : 0.186
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6257
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 : 12836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 203
REMARK 3 SOLVENT ATOMS : 429
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
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) : 1.740
REMARK 3 BOND ANGLES (DEGREES) : 1.740
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: CNS
REMARK 4
REMARK 4 1J51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000001621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-01
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 6.5
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 285817
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
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: NULL
REMARK 200 SOFTWARE USED: CNS 1.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM ACETATE, SODIUM
REMARK 280 CACODYLATE, PH 6.5, EVAPORATION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 THR A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 ILE A 5
REMARK 465 GLN A 6
REMARK 465 SER A 7
REMARK 465 ASN A 8
REMARK 465 ALA A 9
REMARK 465 THR B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 ILE B 5
REMARK 465 GLN B 6
REMARK 465 SER B 7
REMARK 465 ASN B 8
REMARK 465 ALA B 9
REMARK 465 THR C 1
REMARK 465 THR C 2
REMARK 465 GLU C 3
REMARK 465 THR C 4
REMARK 465 ILE C 5
REMARK 465 GLN C 6
REMARK 465 SER C 7
REMARK 465 ASN C 8
REMARK 465 ALA C 9
REMARK 465 THR D 1
REMARK 465 THR D 2
REMARK 465 GLU D 3
REMARK 465 THR D 4
REMARK 465 ILE D 5
REMARK 465 GLN D 6
REMARK 465 SER D 7
REMARK 465 ASN D 8
REMARK 465 ALA D 9
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 OD1 ASP B 182 O HOH B 2452 2.06
REMARK 500 NH1 ARG A 72 OE2 GLU A 331 2.12
REMARK 500 OH TYR C 305 O HOH C 3484 2.13
REMARK 500 OH TYR A 305 O HOH A 1479 2.15
REMARK 500 O LEU B 244 O LEU B 247 2.17
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 PRO A 51 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 72 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 PRO C 86 C - N - CA ANGL. DEV. = 11.0 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 30 63.61 -159.17
REMARK 500 GLU A 128 -72.36 -39.98
REMARK 500 ARG A 143 -71.70 -40.28
REMARK 500 TYR A 154 -57.19 -144.66
REMARK 500 ASN A 229 49.96 39.13
REMARK 500 THR A 252 -84.47 -126.05
REMARK 500 ASP A 297 -156.31 -115.35
REMARK 500 LYS A 314 128.85 -39.70
REMARK 500 PRO A 321 93.35 -53.56
REMARK 500 ALA A 334 53.96 37.60
REMARK 500 ASP B 25 63.19 -60.94
REMARK 500 MET B 28 -19.80 -44.20
REMARK 500 ASN B 30 66.09 -165.21
REMARK 500 ASN B 33 28.58 -77.58
REMARK 500 PHE B 96 106.05 -58.50
REMARK 500 GLU B 128 -72.45 -31.37
REMARK 500 CYS B 148 159.15 178.16
REMARK 500 TYR B 154 -54.52 -146.64
REMARK 500 SER B 190 -70.70 -52.50
REMARK 500 THR B 252 -80.79 -135.76
REMARK 500 ASP B 297 -164.76 -122.12
REMARK 500 ALA B 401 149.20 -172.00
REMARK 500 ASP C 25 68.22 -66.78
REMARK 500 ASN C 30 68.70 -161.95
REMARK 500 TYR C 154 -57.48 -146.37
REMARK 500 LYS C 214 82.04 -161.96
REMARK 500 THR C 252 -74.87 -137.89
REMARK 500 PHE C 292 40.33 -108.73
REMARK 500 ASP C 297 -160.22 -116.92
REMARK 500 THR C 348 38.62 -142.28
REMARK 500 ASP D 25 62.12 -58.47
REMARK 500 ASN D 30 79.03 -154.28
REMARK 500 SER D 35 -6.74 -55.79
REMARK 500 PRO D 51 -153.88 -58.27
REMARK 500 GLU D 128 -70.96 -25.19
REMARK 500 TYR D 154 -56.36 -150.52
REMARK 500 ARG D 186 58.50 -142.99
REMARK 500 THR D 252 -74.42 -127.18
REMARK 500 GLU D 279 -8.41 -57.00
REMARK 500 ASP D 297 -162.11 -124.98
REMARK 500 TYR D 305 145.07 -171.60
REMARK 500 GLU D 329 -9.75 -57.89
REMARK 500 ARG D 342 120.39 -29.52
REMARK 500 HIS D 352 134.01 -171.61
REMARK 500 ALA D 401 148.84 -170.86
REMARK 500 ALA D 409 -17.59 -48.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 75 0.07 SIDE CHAIN
REMARK 500 TYR C 179 0.07 SIDE CHAIN
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 K A1418 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 84 O
REMARK 620 2 GLY A 93 O 78.3
REMARK 620 3 GLU A 94 O 157.2 83.8
REMARK 620 4 PHE A 96 O 91.2 81.7 100.2
REMARK 620 5 HOH A1572 O 86.9 91.8 79.6 173.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 417 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 357 SG
REMARK 620 2 HEM A 417 NA 103.6
REMARK 620 3 HEM A 417 NB 93.4 88.2
REMARK 620 4 HEM A 417 NC 93.7 162.7 90.6
REMARK 620 5 HEM A 417 ND 105.2 87.4 161.4 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B2418 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 84 O
REMARK 620 2 GLY B 93 O 81.8
REMARK 620 3 GLU B 94 O 156.1 76.6
REMARK 620 4 PHE B 96 O 93.3 79.5 92.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 417 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 357 SG
REMARK 620 2 HEM B 417 NA 98.4
REMARK 620 3 HEM B 417 NB 97.5 87.1
REMARK 620 4 HEM B 417 NC 100.9 160.6 88.8
REMARK 620 5 HEM B 417 ND 103.1 87.7 159.3 89.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3418 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 84 O
REMARK 620 2 GLY C 93 O 77.5
REMARK 620 3 GLU C 94 O 156.7 80.8
REMARK 620 4 PHE C 96 O 84.8 85.3 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 417 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 357 SG
REMARK 620 2 HEM C 417 NA 105.2
REMARK 620 3 HEM C 417 NB 98.0 88.6
REMARK 620 4 HEM C 417 NC 94.3 160.5 89.3
REMARK 620 5 HEM C 417 ND 102.9 87.1 159.0 87.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D4418 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 84 O
REMARK 620 2 GLY D 93 O 84.0
REMARK 620 3 GLU D 94 O 153.3 71.2
REMARK 620 4 PHE D 96 O 94.2 78.5 90.7
REMARK 620 5 HOH D4475 O 86.7 92.4 84.5 170.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 417 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 357 SG
REMARK 620 2 HEM D 417 NA 104.8
REMARK 620 3 HEM D 417 NB 97.0 88.4
REMARK 620 4 HEM D 417 NC 93.8 161.4 89.1
REMARK 620 5 HEM D 417 ND 103.3 87.1 159.7 88.9
REMARK 620 6 HOH D4464 O 178.6 75.6 84.3 85.9 75.4
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 K A 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 2418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 4418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCZ A 1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCZ B 2450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCZ C 3450
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 417
DBREF 1J51 A 1 414 UNP P00183 CPXA_PSEPU 1 414
DBREF 1J51 B 1 414 UNP P00183 CPXA_PSEPU 1 414
DBREF 1J51 C 1 414 UNP P00183 CPXA_PSEPU 1 414
DBREF 1J51 D 1 414 UNP P00183 CPXA_PSEPU 1 414
SEQADV 1J51 TRP A 87 UNP P00183 PHE 87 ENGINEERED MUTATION
SEQADV 1J51 PHE A 96 UNP P00183 TYR 96 ENGINEERED MUTATION
SEQADV 1J51 LEU A 247 UNP P00183 VAL 247 ENGINEERED MUTATION
SEQADV 1J51 ALA A 334 UNP P00183 CYS 334 ENGINEERED MUTATION
SEQADV 1J51 TRP B 87 UNP P00183 PHE 87 ENGINEERED MUTATION
SEQADV 1J51 PHE B 96 UNP P00183 TYR 96 ENGINEERED MUTATION
SEQADV 1J51 LEU B 247 UNP P00183 VAL 247 ENGINEERED MUTATION
SEQADV 1J51 ALA B 334 UNP P00183 CYS 334 ENGINEERED MUTATION
SEQADV 1J51 TRP C 87 UNP P00183 PHE 87 ENGINEERED MUTATION
SEQADV 1J51 PHE C 96 UNP P00183 TYR 96 ENGINEERED MUTATION
SEQADV 1J51 LEU C 247 UNP P00183 VAL 247 ENGINEERED MUTATION
SEQADV 1J51 ALA C 334 UNP P00183 CYS 334 ENGINEERED MUTATION
SEQADV 1J51 TRP D 87 UNP P00183 PHE 87 ENGINEERED MUTATION
SEQADV 1J51 PHE D 96 UNP P00183 TYR 96 ENGINEERED MUTATION
SEQADV 1J51 LEU D 247 UNP P00183 VAL 247 ENGINEERED MUTATION
SEQADV 1J51 ALA D 334 UNP P00183 CYS 334 ENGINEERED MUTATION
SEQRES 1 A 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 A 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 A 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 A 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 A 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 A 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 A 414 ARG HIS PHE SER SER GLU CYS PRO TRP ILE PRO ARG GLU
SEQRES 8 A 414 ALA GLY GLU ALA PHE ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 A 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 A 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 A 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 A 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 A 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 A 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 A 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 A 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 A 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 A 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 A 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU LEU
SEQRES 20 A 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 A 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 A 414 LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 A 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 A 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 A 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 A 414 GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS VAL
SEQRES 27 A 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 A 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 A 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 A 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 A 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 A 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
SEQRES 1 B 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 B 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 B 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 B 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 B 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 B 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 B 414 ARG HIS PHE SER SER GLU CYS PRO TRP ILE PRO ARG GLU
SEQRES 8 B 414 ALA GLY GLU ALA PHE ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 B 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 B 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 B 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 B 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 B 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 B 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 B 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 B 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 B 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 B 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 B 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU LEU
SEQRES 20 B 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 B 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 B 414 LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 B 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 B 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 B 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 B 414 GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS VAL
SEQRES 27 B 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 B 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 B 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 B 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 B 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 B 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
SEQRES 1 C 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 C 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 C 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 C 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 C 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 C 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 C 414 ARG HIS PHE SER SER GLU CYS PRO TRP ILE PRO ARG GLU
SEQRES 8 C 414 ALA GLY GLU ALA PHE ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 C 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 C 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 C 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 C 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 C 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 C 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 C 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 C 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 C 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 C 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 C 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU LEU
SEQRES 20 C 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 C 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 C 414 LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 C 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 C 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 C 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 C 414 GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS VAL
SEQRES 27 C 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 C 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 C 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 C 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 C 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 C 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
SEQRES 1 D 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 D 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 D 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 D 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 D 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 D 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 D 414 ARG HIS PHE SER SER GLU CYS PRO TRP ILE PRO ARG GLU
SEQRES 8 D 414 ALA GLY GLU ALA PHE ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 D 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 D 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 D 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 D 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 D 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 D 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 D 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 D 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 D 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 D 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 D 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU LEU
SEQRES 20 D 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 D 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 D 414 LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 D 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 D 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 D 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 D 414 GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS VAL
SEQRES 27 D 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 D 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 D 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 D 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 D 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 D 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
HET K A1418 1
HET HEM A 417 43
HET TCZ A1450 9
HET K B2418 1
HET HEM B 417 43
HET TCZ B2450 9
HET K C3418 1
HET HEM C 417 43
HET TCZ C3450 9
HET K D4418 1
HET HEM D 417 43
HETNAM K POTASSIUM ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM TCZ 1,3,5-TRICHLORO-BENZENE
HETSYN HEM HEME
FORMUL 5 K 4(K 1+)
FORMUL 6 HEM 4(C34 H32 FE N4 O4)
FORMUL 7 TCZ 3(C6 H3 CL3)
FORMUL 16 HOH *429(H2 O)
HELIX 1 1 PRO A 19 VAL A 23 5 5
HELIX 2 2 ASN A 33 ALA A 36 5 4
HELIX 3 3 GLY A 37 ALA A 43 1 7
HELIX 4 4 VAL A 44 GLU A 47 5 4
HELIX 5 5 ARG A 57 GLY A 61 5 5
HELIX 6 6 ARG A 67 ASP A 77 1 11
HELIX 7 7 PRO A 89 PHE A 96 1 8
HELIX 8 8 GLU A 107 GLY A 120 1 14
HELIX 9 9 GLY A 120 ARG A 143 1 24
HELIX 10 10 PHE A 150 TYR A 154 1 5
HELIX 11 11 GLU A 156 ALA A 167 1 12
HELIX 12 12 PRO A 170 GLU A 172 5 3
HELIX 13 13 ASP A 173 ARG A 186 1 14
HELIX 14 14 THR A 192 ARG A 212 1 21
HELIX 15 15 ASP A 218 ASN A 225 1 8
HELIX 16 16 THR A 234 ASP A 251 1 18
HELIX 17 17 THR A 252 LYS A 266 1 15
HELIX 18 18 SER A 267 ARG A 277 1 11
HELIX 19 19 ARG A 280 PHE A 292 1 13
HELIX 20 20 PRO A 321 ASP A 328 5 8
HELIX 21 21 GLY A 359 ILE A 378 1 20
HELIX 22 22 ASP A 407 THR A 411 5 5
HELIX 23 23 PRO B 19 VAL B 23 5 5
HELIX 24 24 ASN B 33 ALA B 36 5 4
HELIX 25 25 GLY B 37 ALA B 43 1 7
HELIX 26 26 VAL B 44 GLU B 47 5 4
HELIX 27 27 ARG B 67 ASP B 77 1 11
HELIX 28 28 PRO B 89 PHE B 96 1 8
HELIX 29 29 PRO B 106 GLY B 120 1 15
HELIX 30 30 GLY B 120 ARG B 143 1 24
HELIX 31 31 PHE B 150 TYR B 154 1 5
HELIX 32 32 GLU B 156 ALA B 167 1 12
HELIX 33 33 PRO B 170 GLU B 172 5 3
HELIX 34 34 ASP B 173 ARG B 186 1 14
HELIX 35 35 THR B 192 LYS B 214 1 23
HELIX 36 36 ASP B 218 ASN B 225 1 8
HELIX 37 37 THR B 234 LEU B 250 1 17
HELIX 38 38 THR B 252 LYS B 266 1 15
HELIX 39 39 SER B 267 ARG B 277 1 11
HELIX 40 40 ARG B 280 PHE B 292 1 13
HELIX 41 41 PRO B 321 SER B 325 5 5
HELIX 42 42 HIS B 352 LEU B 356 5 5
HELIX 43 43 GLY B 359 ILE B 378 1 20
HELIX 44 44 ASP B 407 THR B 411 5 5
HELIX 45 45 PRO C 19 VAL C 23 5 5
HELIX 46 46 ASN C 33 ALA C 36 5 4
HELIX 47 47 GLY C 37 VAL C 44 1 8
HELIX 48 48 LEU C 45 GLU C 47 5 3
HELIX 49 49 ARG C 57 GLY C 61 5 5
HELIX 50 50 ARG C 67 ASP C 77 1 11
HELIX 51 51 PRO C 89 PHE C 96 1 8
HELIX 52 52 GLU C 107 GLY C 120 1 14
HELIX 53 53 GLY C 120 LYS C 126 1 7
HELIX 54 54 LEU C 127 ARG C 143 1 17
HELIX 55 55 PHE C 150 TYR C 154 1 5
HELIX 56 56 GLU C 156 GLY C 168 1 13
HELIX 57 57 PRO C 170 GLU C 172 5 3
HELIX 58 58 ASP C 173 ARG C 186 1 14
HELIX 59 59 THR C 192 LYS C 214 1 23
HELIX 60 60 ASP C 218 ASN C 225 1 8
HELIX 61 61 THR C 234 ASP C 251 1 18
HELIX 62 62 THR C 252 LYS C 266 1 15
HELIX 63 63 SER C 267 ARG C 277 1 11
HELIX 64 64 ARG C 280 PHE C 292 1 13
HELIX 65 65 PRO C 321 ASP C 328 5 8
HELIX 66 66 GLY C 359 ILE C 378 1 20
HELIX 67 67 ASP C 407 THR C 411 5 5
HELIX 68 68 PRO D 19 VAL D 23 5 5
HELIX 69 69 ASN D 33 ALA D 36 5 4
HELIX 70 70 GLY D 37 ALA D 43 1 7
HELIX 71 71 VAL D 44 GLU D 47 5 4
HELIX 72 72 ARG D 57 GLY D 61 5 5
HELIX 73 73 ARG D 67 ASP D 77 1 11
HELIX 74 74 PRO D 89 PHE D 96 1 8
HELIX 75 75 GLN D 108 GLY D 120 1 13
HELIX 76 76 GLY D 120 ARG D 143 1 24
HELIX 77 77 PHE D 150 TYR D 154 1 5
HELIX 78 78 GLU D 156 GLY D 168 1 13
HELIX 79 79 PRO D 170 GLU D 172 5 3
HELIX 80 80 ASP D 173 ARG D 186 1 14
HELIX 81 81 THR D 192 LYS D 214 1 23
HELIX 82 82 ASP D 218 ASN D 225 1 8
HELIX 83 83 THR D 234 LEU D 250 1 17
HELIX 84 84 THR D 252 ALA D 265 1 14
HELIX 85 85 SER D 267 ARG D 277 1 11
HELIX 86 86 ARG D 280 PHE D 292 1 13
HELIX 87 87 GLY D 359 ILE D 378 1 20
HELIX 88 88 ASP D 407 THR D 411 5 5
SHEET 1 A 5 LEU A 53 THR A 56 0
SHEET 2 A 5 HIS A 62 ALA A 65 -1 O HIS A 62 N THR A 56
SHEET 3 A 5 GLN A 317 LEU A 320 1 O GLN A 317 N TRP A 63
SHEET 4 A 5 ASP A 297 LEU A 301 -1 N ARG A 299 O ILE A 318
SHEET 5 A 5 PHE A 81 SER A 82 -1 N SER A 82 O ILE A 300
SHEET 1 B 3 GLN A 147 ASN A 149 0
SHEET 2 B 3 PRO A 403 VAL A 405 -1 O LEU A 404 N CYS A 148
SHEET 3 B 3 SER A 382 ILE A 383 -1 N SER A 382 O VAL A 405
SHEET 1 C 2 GLN A 227 VAL A 228 0
SHEET 2 C 2 ARG A 231 PRO A 232 -1 O ARG A 231 N VAL A 228
SHEET 1 D 2 TYR A 305 PHE A 307 0
SHEET 2 D 2 VAL A 310 LEU A 312 -1 O LEU A 312 N TYR A 305
SHEET 1 E 2 HIS A 391 LYS A 392 0
SHEET 2 E 2 GLY A 398 VAL A 399 -1 O GLY A 398 N LYS A 392
SHEET 1 F 5 LEU B 53 THR B 56 0
SHEET 2 F 5 HIS B 62 ALA B 65 -1 O HIS B 62 N THR B 56
SHEET 3 F 5 GLN B 317 LEU B 320 1 O LEU B 319 N TRP B 63
SHEET 4 F 5 ASP B 297 LEU B 301 -1 N ARG B 299 O ILE B 318
SHEET 5 F 5 PHE B 81 SER B 82 -1 N SER B 82 O ILE B 300
SHEET 1 G 3 GLN B 147 ASN B 149 0
SHEET 2 G 3 PRO B 403 VAL B 405 -1 O LEU B 404 N CYS B 148
SHEET 3 G 3 SER B 382 ILE B 383 -1 N SER B 382 O VAL B 405
SHEET 1 H 2 GLN B 227 VAL B 228 0
SHEET 2 H 2 ARG B 231 PRO B 232 -1 O ARG B 231 N VAL B 228
SHEET 1 I 2 TYR B 305 PHE B 307 0
SHEET 2 I 2 VAL B 310 LEU B 312 -1 O VAL B 310 N PHE B 307
SHEET 1 J 2 HIS B 391 LYS B 392 0
SHEET 2 J 2 GLY B 398 VAL B 399 -1 O GLY B 398 N LYS B 392
SHEET 1 K 5 LEU C 53 THR C 56 0
SHEET 2 K 5 HIS C 62 ALA C 65 -1 O HIS C 62 N THR C 56
SHEET 3 K 5 GLN C 317 LEU C 320 1 O GLN C 317 N TRP C 63
SHEET 4 K 5 ASP C 297 LEU C 301 -1 N ARG C 299 O ILE C 318
SHEET 5 K 5 PHE C 81 SER C 82 -1 N SER C 82 O ILE C 300
SHEET 1 L 3 GLN C 147 ASN C 149 0
SHEET 2 L 3 PRO C 403 VAL C 405 -1 O LEU C 404 N CYS C 148
SHEET 3 L 3 SER C 382 ILE C 383 -1 N SER C 382 O VAL C 405
SHEET 1 M 2 GLN C 227 VAL C 228 0
SHEET 2 M 2 ARG C 231 PRO C 232 -1 O ARG C 231 N VAL C 228
SHEET 1 N 2 TYR C 305 PHE C 307 0
SHEET 2 N 2 VAL C 310 LEU C 312 -1 O VAL C 310 N PHE C 307
SHEET 1 O 2 HIS C 391 LYS C 392 0
SHEET 2 O 2 GLY C 398 VAL C 399 -1 O GLY C 398 N LYS C 392
SHEET 1 P 5 LEU D 53 THR D 56 0
SHEET 2 P 5 HIS D 62 ALA D 65 -1 O HIS D 62 N THR D 56
SHEET 3 P 5 GLN D 317 LEU D 320 1 O GLN D 317 N TRP D 63
SHEET 4 P 5 ASP D 297 LEU D 301 -1 N ARG D 299 O ILE D 318
SHEET 5 P 5 PHE D 81 SER D 82 -1 N SER D 82 O ILE D 300
SHEET 1 Q 3 GLN D 147 ASN D 149 0
SHEET 2 Q 3 PRO D 403 VAL D 405 -1 O LEU D 404 N CYS D 148
SHEET 3 Q 3 SER D 382 ILE D 383 -1 N SER D 382 O VAL D 405
SHEET 1 R 2 GLN D 227 VAL D 228 0
SHEET 2 R 2 ARG D 231 PRO D 232 -1 O ARG D 231 N VAL D 228
SHEET 1 S 2 TYR D 305 PHE D 307 0
SHEET 2 S 2 VAL D 310 LEU D 312 -1 O LEU D 312 N TYR D 305
SHEET 1 T 2 HIS D 391 LYS D 392 0
SHEET 2 T 2 GLY D 398 VAL D 399 -1 O GLY D 398 N LYS D 392
LINK O GLU A 84 K K A1418 1555 1555 2.80
LINK O GLY A 93 K K A1418 1555 1555 2.91
LINK O GLU A 94 K K A1418 1555 1555 2.84
LINK O PHE A 96 K K A1418 1555 1555 2.96
LINK SG CYS A 357 FE HEM A 417 1555 1555 2.23
LINK K K A1418 O HOH A1572 1555 1555 3.20
LINK O GLU B 84 K K B2418 1555 1555 2.77
LINK O GLY B 93 K K B2418 1555 1555 3.10
LINK O GLU B 94 K K B2418 1555 1555 3.01
LINK O PHE B 96 K K B2418 1555 1555 2.90
LINK SG CYS B 357 FE HEM B 417 1555 1555 2.07
LINK O GLU C 84 K K C3418 1555 1555 2.82
LINK O GLY C 93 K K C3418 1555 1555 2.86
LINK O GLU C 94 K K C3418 1555 1555 2.90
LINK O PHE C 96 K K C3418 1555 1555 2.99
LINK SG CYS C 357 FE HEM C 417 1555 1555 2.20
LINK O GLU D 84 K K D4418 1555 1555 2.76
LINK O GLY D 93 K K D4418 1555 1555 3.15
LINK O GLU D 94 K K D4418 1555 1555 3.10
LINK O PHE D 96 K K D4418 1555 1555 2.88
LINK SG CYS D 357 FE HEM D 417 1555 1555 2.09
LINK FE HEM D 417 O HOH D4464 1555 1555 2.99
LINK K K D4418 O HOH D4475 1555 1555 2.97
CISPEP 1 ILE A 88 PRO A 89 0 0.08
CISPEP 2 ILE A 99 PRO A 100 0 0.41
CISPEP 3 PRO A 105 PRO A 106 0 0.17
CISPEP 4 ILE B 88 PRO B 89 0 0.24
CISPEP 5 ILE B 99 PRO B 100 0 0.39
CISPEP 6 PRO B 105 PRO B 106 0 0.10
CISPEP 7 ILE C 88 PRO C 89 0 0.59
CISPEP 8 ILE C 99 PRO C 100 0 0.88
CISPEP 9 PRO C 105 PRO C 106 0 0.25
CISPEP 10 ILE D 88 PRO D 89 0 0.39
CISPEP 11 ILE D 99 PRO D 100 0 0.71
CISPEP 12 PRO D 105 PRO D 106 0 0.22
SITE 1 AC1 4 GLU A 84 GLY A 93 GLU A 94 PHE A 96
SITE 1 AC2 4 GLU B 84 GLY B 93 GLU B 94 PHE B 96
SITE 1 AC3 4 GLU C 84 GLY C 93 GLU C 94 PHE C 96
SITE 1 AC4 5 GLU D 84 GLY D 93 GLU D 94 PHE D 96
SITE 2 AC4 5 HOH D4475
SITE 1 AC5 21 PRO A 100 THR A 101 GLN A 108 ARG A 112
SITE 2 AC5 21 LEU A 244 LEU A 245 GLY A 248 GLY A 249
SITE 3 AC5 21 THR A 252 ASP A 297 ARG A 299 GLN A 322
SITE 4 AC5 21 THR A 349 PHE A 350 GLY A 351 HIS A 355
SITE 5 AC5 21 CYS A 357 GLY A 359 ALA A 363 TCZ A1450
SITE 6 AC5 21 HOH A1452
SITE 1 AC6 7 TRP A 87 LEU A 244 GLY A 248 THR A 252
SITE 2 AC6 7 VAL A 295 ASP A 297 HEM A 417
SITE 1 AC7 20 PRO B 100 THR B 101 GLN B 108 ARG B 112
SITE 2 AC7 20 LEU B 245 GLY B 248 THR B 252 VAL B 253
SITE 3 AC7 20 ASP B 297 ARG B 299 GLN B 322 THR B 349
SITE 4 AC7 20 PHE B 350 GLY B 351 HIS B 355 LEU B 356
SITE 5 AC7 20 CYS B 357 ALA B 363 TCZ B2450 HOH B2480
SITE 1 AC8 6 TRP B 87 PHE B 96 LEU B 244 LEU B 247
SITE 2 AC8 6 VAL B 295 HEM B 417
SITE 1 AC9 22 PRO C 100 THR C 101 GLN C 108 ARG C 112
SITE 2 AC9 22 LEU C 244 LEU C 245 GLY C 248 GLY C 249
SITE 3 AC9 22 THR C 252 VAL C 295 ASP C 297 ARG C 299
SITE 4 AC9 22 GLN C 322 THR C 349 PHE C 350 GLY C 351
SITE 5 AC9 22 HIS C 355 CYS C 357 LEU C 358 GLY C 359
SITE 6 AC9 22 TCZ C3450 HOH C3462
SITE 1 BC1 7 TRP C 87 LEU C 244 GLY C 248 THR C 252
SITE 2 BC1 7 VAL C 295 ASP C 297 HEM C 417
SITE 1 BC2 19 PRO D 100 THR D 101 GLN D 108 ARG D 112
SITE 2 BC2 19 LEU D 244 LEU D 245 GLY D 248 THR D 252
SITE 3 BC2 19 ASP D 297 ARG D 299 GLN D 322 THR D 349
SITE 4 BC2 19 PHE D 350 GLY D 351 HIS D 355 CYS D 357
SITE 5 BC2 19 ALA D 363 HOH D4464 HOH D4502
CRYST1 66.870 62.440 95.520 89.98 90.30 90.09 P 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 0.014954 0.000023 0.000078 0.00000
SCALE2 0.000000 0.016015 -0.000005 0.00000
SCALE3 0.000000 0.000000 0.010469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
