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PDBsum entry 4fa7

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4fa7
Jmol
Contents
Protein chains
546 a.a.
166 a.a.
31 a.a.
Ligands
HEM
HAS-PEO
OLC ×16
CUA
Metals
_CU
Waters ×109
HEADER    OXIDOREDUCTASE                          21-MAY-12   4FA7
TITLE     STRUCTURE OF RECOMBINANT CYTOCHROME BA3 OXIDASE MUTANT A204F FROM
TITLE    2 THERMUS THERMOPHILUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYTOCHROME C BA(3) SUBUNIT I, CYTOCHROME C OXIDASE
COMPND   5 POLYPEPTIDE I, CYTOCHROME CBA3 SUBUNIT 1;
COMPND   6 EC: 1.9.3.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND  11 CHAIN: B;
COMPND  12 SYNONYM: CYTOCHROME C BA(3) SUBUNIT II, CYTOCHROME C OXIDASE
COMPND  13 POLYPEPTIDE II, CYTOCHROME CBA3 SUBUNIT 2;
COMPND  14 EC: 1.9.3.1;
COMPND  15 ENGINEERED: YES;
COMPND  16 MOL_ID: 3;
COMPND  17 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 2A;
COMPND  18 CHAIN: C;
COMPND  19 SYNONYM: CYTOCHROME C BA(3) SUBUNIT IIA, CYTOCHROME C OXIDASE
COMPND  20 POLYPEPTIDE IIA, CYTOCHROME CBA3 SUBUNIT 2A;
COMPND  21 EC: 1.9.3.1;
COMPND  22 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE   3 ORGANISM_TAXID: 300852;
SOURCE   4 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE   5 GENE: CBAA, TTHA1135;
SOURCE   6 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMK18;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE  13 ORGANISM_TAXID: 300852;
SOURCE  14 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE  15 GENE: CBAB, CTAC, TTHA1134;
SOURCE  16 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PMK18;
SOURCE  21 MOL_ID: 3;
SOURCE  22 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE  23 ORGANISM_TAXID: 300852;
SOURCE  24 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE  25 GENE: CBAD, TTHA1133;
SOURCE  26 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PMK18
KEYWDS    PROTON PUMP, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.LI,Y.CHEN,C.D.STOUT
REVDAT   1   30-MAY-12 4FA7    0
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.83
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3
REMARK   3   NUMBER OF REFLECTIONS             : 33684
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 + TEST SET) : 0.172
REMARK   3   R VALUE            (WORKING SET) : 0.169
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1767
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2558
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250
REMARK   3   BIN FREE R VALUE SET COUNT          : 111
REMARK   3   BIN FREE R VALUE                    : 0.2760
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5828
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 456
REMARK   3   SOLVENT ATOMS            : 109
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.69
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.87000
REMARK   3    B22 (A**2) : -0.41000
REMARK   3    B33 (A**2) : 1.95000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 1.96000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.384
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.236
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6470 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8790 ; 2.077 ; 2.029
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   739 ; 6.672 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   220 ;35.772 ;22.273
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   872 ;16.768 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.322 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   966 ; 0.145 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4763 ; 0.010 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3704 ; 0.895 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5972 ; 1.648 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2766 ; 2.602 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2818 ; 4.014 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 4FA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-11
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               : 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) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33684
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.830
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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   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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3S8G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM CACODYLATE, 1.6M NACL, 40%
REMARK 280  PEG400, PH 6.5, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       71.77500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.10500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.77500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.10500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B 326  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     HIS A     1
REMARK 465     ALA A     2
REMARK 465     VAL A     3
REMARK 465     ARG A     4
REMARK 465     ALA A     5
REMARK 465     SER A     6
REMARK 465     GLU A     7
REMARK 465     ILE A     8
REMARK 465     SER A     9
REMARK 465     ARG A    10
REMARK 465     VAL A    11
REMARK 465     TYR A    12
REMARK 465     GLU A    13
REMARK 465     ALA A    14
REMARK 465     GLY A   514
REMARK 465     PRO A   515
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     MET C     1
REMARK 465     GLU C     2
REMARK 465     GLU C     3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     SER A 494    OG
REMARK 470     ARG A 495    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 496    CG   CD   OE1  OE2
REMARK 470     ARG A 497    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 503    CG   CD   OE1  OE2
REMARK 470     GLU A 516    CG   CD   OE1  OE2
REMARK 470     ARG A 519    CG   CD   NE   CZ   NH1  NH2
REMARK 470     HIS B   5    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS B   9    CG   CD   CE   NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ARG A  330   CZ
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   NE2  HIS A   233     CE2  TYR A   237              1.70
REMARK 500   O    HOH A   740     O    HOH A   767              2.03
REMARK 500   O    LYS B     6     O    HOH B   338              2.14
REMARK 500   O    HOH A   728     O    HOH A   765              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B   327     O    HOH B   327     2556     2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A 133   CD1   TYR A 133   CE1    -0.104
REMARK 500    PHE A 204   CB    PHE A 204   CG     -0.135
REMARK 500    ARG A 330   NE    ARG A 330   CZ      0.944
REMARK 500    ARG A 330   CZ    ARG A 330   NH1     1.443
REMARK 500    ARG A 330   CZ    ARG A 330   NH2    -0.744
REMARK 500    VAL A 471   CB    VAL A 471   CG1     0.129
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    LEU A  25   CB  -  CG  -  CD1 ANGL. DEV. = -13.3 DEGREES
REMARK 500    VAL A 131   CB  -  CA  -  C   ANGL. DEV. =  14.5 DEGREES
REMARK 500    ARG A 330   CD  -  NE  -  CZ  ANGL. DEV. = -31.4 DEGREES
REMARK 500    ARG A 330   NE  -  CZ  -  NH1 ANGL. DEV. = -13.7 DEGREES
REMARK 500    ARG A 330   NE  -  CZ  -  NH2 ANGL. DEV. =  15.3 DEGREES
REMARK 500    PHE A 369   N   -  CA  -  CB  ANGL. DEV. = -13.0 DEGREES
REMARK 500    LEU C  13   CA  -  CB  -  CG  ANGL. DEV. =  15.2 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    ILE A  78      -61.39   -104.96
REMARK 500    ALA A 129       42.95   -144.66
REMARK 500    VAL A 131     -166.95   -112.00
REMARK 500    LEU A 132     -156.92   -106.77
REMARK 500    PHE A 135       59.98     32.16
REMARK 500    ASN A 174       57.14   -146.25
REMARK 500    PHE A 207      -69.65   -144.57
REMARK 500    PRO A 278       42.91    -86.03
REMARK 500    ASN A 377       12.13     59.27
REMARK 500    SER A 391      -73.96   -109.36
REMARK 500    TRP A 403      -41.97   -132.18
REMARK 500    ASN A 554       68.82   -118.73
REMARK 500    ASP B 111      -80.06   -122.01
REMARK 500    ASN B 124       91.57   -160.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    HIS A 233        24.9      L          L   OUTSIDE RANGE
REMARK 500    PHE A 385        24.4      L          L   OUTSIDE RANGE
REMARK 500    ASN A 446        24.1      L          L   OUTSIDE RANGE
REMARK 500    ILE A 475        24.1      L          L   OUTSIDE RANGE
REMARK 500    ASP B 111        24.7      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 734        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH A 754        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH C 201        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH C 202        DISTANCE =  7.33 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     OLC A  607
REMARK 610     OLC A  608
REMARK 610     OLC A  609
REMARK 610     OLC A  610
REMARK 610     OLC A  611
REMARK 610     OLC A  612
REMARK 610     OLC A  613
REMARK 610     OLC A  615
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                              CU A 601  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 233   ND1
REMARK 620 2 HIS A 283   NE2 151.0
REMARK 620 3 HIS A 282   NE2  94.0  89.3
REMARK 620 4 PEO A 604   O2   94.3  96.0 152.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 201  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 114   ND1
REMARK 620 2 CUA B 201  CU1  141.5
REMARK 620 3 CYS B 149   SG  123.7  58.2
REMARK 620 4 MET B 160   SD   89.5 127.2 112.1
REMARK 620 5 CYS B 153   SG  106.1  55.5 113.7 108.8
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 602  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 386   NE2
REMARK 620 2 HEM A 602   NA   86.0
REMARK 620 3 HEM A 602   NB   92.6  91.0
REMARK 620 4 HEM A 602   NC   96.2 177.3  87.4
REMARK 620 5 HEM A 602   ND   90.0  89.4 177.3  92.1
REMARK 620 6 HIS A  72   NE2 176.2  91.0  89.8  86.9  87.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 201  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 157   ND1
REMARK 620 2 CUA B 201  CU2  158.2
REMARK 620 3 CYS B 153   SG  115.1  58.7
REMARK 620 4 CYS B 149   SG  127.1  55.2 113.8
REMARK 620 5 GLN B 151   O    94.3 107.4 103.3  93.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HAS A 603  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PEO A 604   O1
REMARK 620 2 HAS A 603   NA   81.8
REMARK 620 3 HAS A 603   NB   95.8 177.5
REMARK 620 4 HAS A 603   NC   91.7  90.4  88.8
REMARK 620 5 HAS A 603   ND   86.9  91.2  89.5 177.7
REMARK 620 6 HIS A 384   NE2 172.1  92.1  90.3  93.3  88.3
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 CU A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAS A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC C 101
DBREF  4FA7 A    2   562  UNP    Q5SJ79   COX1_THET8       2    562
DBREF  4FA7 B    1   168  UNP    Q5SJ80   COX2_THET8       1    168
DBREF  4FA7 C    1    34  UNP    P82543   COXA_THET8       1     34
SEQADV 4FA7 MET A   -5  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A   -4  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A   -3  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A   -2  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A   -1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A    0  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 HIS A    1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FA7 PHE A  204  UNP  Q5SJ79    ALA   204 ENGINEERED MUTATION
SEQRES   1 A  568  MET HIS HIS HIS HIS HIS HIS ALA VAL ARG ALA SER GLU
SEQRES   2 A  568  ILE SER ARG VAL TYR GLU ALA TYR PRO GLU LYS LYS ALA
SEQRES   3 A  568  THR LEU TYR PHE LEU VAL LEU GLY PHE LEU ALA LEU ILE
SEQRES   4 A  568  VAL GLY SER LEU PHE GLY PRO PHE GLN ALA LEU ASN TYR
SEQRES   5 A  568  GLY ASN VAL ASP ALA TYR PRO LEU LEU LYS ARG LEU LEU
SEQRES   6 A  568  PRO PHE VAL GLN SER TYR TYR GLN GLY LEU THR LEU HIS
SEQRES   7 A  568  GLY VAL LEU ASN ALA ILE VAL PHE THR GLN LEU PHE ALA
SEQRES   8 A  568  GLN ALA ILE MET VAL TYR LEU PRO ALA ARG GLU LEU ASN
SEQRES   9 A  568  MET ARG PRO ASN MET GLY LEU MET TRP LEU SER TRP TRP
SEQRES  10 A  568  MET ALA PHE ILE GLY LEU VAL VAL ALA ALA LEU PRO LEU
SEQRES  11 A  568  LEU ALA ASN GLU ALA THR VAL LEU TYR THR PHE TYR PRO
SEQRES  12 A  568  PRO LEU LYS GLY HIS TRP ALA PHE TYR LEU GLY ALA SER
SEQRES  13 A  568  VAL PHE VAL LEU SER THR TRP VAL SER ILE TYR ILE VAL
SEQRES  14 A  568  LEU ASP LEU TRP ARG ARG TRP LYS ALA ALA ASN PRO GLY
SEQRES  15 A  568  LYS VAL THR PRO LEU VAL THR TYR MET ALA VAL VAL PHE
SEQRES  16 A  568  TRP LEU MET TRP PHE LEU ALA SER LEU GLY LEU VAL LEU
SEQRES  17 A  568  GLU PHE VAL LEU PHE LEU LEU PRO TRP SER PHE GLY LEU
SEQRES  18 A  568  VAL GLU GLY VAL ASP PRO LEU VAL ALA ARG THR LEU PHE
SEQRES  19 A  568  TRP TRP THR GLY HIS PRO ILE VAL TYR PHE TRP LEU LEU
SEQRES  20 A  568  PRO ALA TYR ALA ILE ILE TYR THR ILE LEU PRO LYS GLN
SEQRES  21 A  568  ALA GLY GLY LYS LEU VAL SER ASP PRO MET ALA ARG LEU
SEQRES  22 A  568  ALA PHE LEU LEU PHE LEU LEU LEU SER THR PRO VAL GLY
SEQRES  23 A  568  PHE HIS HIS GLN PHE ALA ASP PRO GLY ILE ASP PRO THR
SEQRES  24 A  568  TRP LYS MET ILE HIS SER VAL LEU THR LEU PHE VAL ALA
SEQRES  25 A  568  VAL PRO SER LEU MET THR ALA PHE THR VAL ALA ALA SER
SEQRES  26 A  568  LEU GLU PHE ALA GLY ARG LEU ARG GLY GLY ARG GLY LEU
SEQRES  27 A  568  PHE GLY TRP ILE ARG ALA LEU PRO TRP ASP ASN PRO ALA
SEQRES  28 A  568  PHE VAL ALA PRO VAL LEU GLY LEU LEU GLY PHE ILE PRO
SEQRES  29 A  568  GLY GLY ALA GLY GLY ILE VAL ASN ALA SER PHE THR LEU
SEQRES  30 A  568  ASP TYR VAL VAL HIS ASN THR ALA TRP VAL PRO GLY HIS
SEQRES  31 A  568  PHE HIS LEU GLN VAL ALA SER LEU VAL THR LEU THR ALA
SEQRES  32 A  568  MET GLY SER LEU TYR TRP LEU LEU PRO ASN LEU THR GLY
SEQRES  33 A  568  LYS PRO ILE SER ASP ALA GLN ARG ARG LEU GLY LEU ALA
SEQRES  34 A  568  VAL VAL TRP LEU TRP PHE LEU GLY MET MET ILE MET ALA
SEQRES  35 A  568  VAL GLY LEU HIS TRP ALA GLY LEU LEU ASN VAL PRO ARG
SEQRES  36 A  568  ARG ALA TYR ILE ALA GLN VAL PRO ASP ALA TYR PRO HIS
SEQRES  37 A  568  ALA ALA VAL PRO MET VAL PHE ASN VAL LEU ALA GLY ILE
SEQRES  38 A  568  VAL LEU LEU VAL ALA LEU LEU LEU PHE ILE TYR GLY LEU
SEQRES  39 A  568  PHE SER VAL LEU LEU SER ARG GLU ARG LYS PRO GLU LEU
SEQRES  40 A  568  ALA GLU ALA PRO LEU PRO PHE ALA GLU VAL ILE SER GLY
SEQRES  41 A  568  PRO GLU ASP ARG ARG LEU VAL LEU ALA MET ASP ARG ILE
SEQRES  42 A  568  GLY PHE TRP PHE ALA VAL ALA ALA ILE LEU VAL VAL LEU
SEQRES  43 A  568  ALA TYR GLY PRO THR LEU VAL GLN LEU PHE GLY HIS LEU
SEQRES  44 A  568  ASN PRO VAL PRO GLY TRP ARG LEU TRP
SEQRES   1 B  168  MET VAL ASP GLU HIS LYS ALA HIS LYS ALA ILE LEU ALA
SEQRES   2 B  168  TYR GLU LYS GLY TRP LEU ALA PHE SER LEU ALA MET LEU
SEQRES   3 B  168  PHE VAL PHE ILE ALA LEU ILE ALA TYR THR LEU ALA THR
SEQRES   4 B  168  HIS THR ALA GLY VAL ILE PRO ALA GLY LYS LEU GLU ARG
SEQRES   5 B  168  VAL ASP PRO THR THR VAL ARG GLN GLU GLY PRO TRP ALA
SEQRES   6 B  168  ASP PRO ALA GLN ALA VAL VAL GLN THR GLY PRO ASN GLN
SEQRES   7 B  168  TYR THR VAL TYR VAL LEU ALA PHE ALA PHE GLY TYR GLN
SEQRES   8 B  168  PRO ASN PRO ILE GLU VAL PRO GLN GLY ALA GLU ILE VAL
SEQRES   9 B  168  PHE LYS ILE THR SER PRO ASP VAL ILE HIS GLY PHE HIS
SEQRES  10 B  168  VAL GLU GLY THR ASN ILE ASN VAL GLU VAL LEU PRO GLY
SEQRES  11 B  168  GLU VAL SER THR VAL ARG TYR THR PHE LYS ARG PRO GLY
SEQRES  12 B  168  GLU TYR ARG ILE ILE CYS ASN GLN TYR CYS GLY LEU GLY
SEQRES  13 B  168  HIS GLN ASN MET PHE GLY THR ILE VAL VAL LYS GLU
SEQRES   1 C   34  MET GLU GLU LYS PRO LYS GLY ALA LEU ALA VAL ILE LEU
SEQRES   2 C   34  VAL LEU THR LEU THR ILE LEU VAL PHE TRP LEU GLY VAL
SEQRES   3 C   34  TYR ALA VAL PHE PHE ALA ARG GLY
HET     CU  A 601       1
HET    HEM  A 602      43
HET    HAS  A 603      65
HET    PEO  A 604       2
HET    OLC  A 605      25
HET    OLC  A 606      25
HET    OLC  A 607      23
HET    OLC  A 608      21
HET    OLC  A 609      18
HET    OLC  A 610      17
HET    OLC  A 611       8
HET    OLC  A 612      15
HET    OLC  A 613      20
HET    OLC  A 614      25
HET    OLC  A 615      21
HET    OLC  A 616      25
HET    CUA  B 201       2
HET    OLC  B 202      25
HET    OLC  B 203      25
HET    OLC  B 204      25
HET    OLC  C 101      25
HETNAM      CU COPPER (II) ION
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     HAS HEME-AS
HETNAM     PEO HYDROGEN PEROXIDE
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM     CUA DINUCLEAR COPPER ION
HETSYN     HEM HEME
HETSYN     OLC 1-OLEOYL-R-GLYCEROL
FORMUL   4   CU    CU 2+
FORMUL   5  HEM    C34 H32 FE N4 O4
FORMUL   6  HAS    C54 H64 FE N4 O6
FORMUL   7  PEO    H2 O2
FORMUL   8  OLC    16(C21 H40 O4)
FORMUL  20  CUA    CU2
FORMUL  25  HOH   *109(H2 O)
HELIX    1   1 PRO A   16  TYR A   46  1                                  31
HELIX    2   2 ALA A   51  LEU A   59  1                                   9
HELIX    3   3 SER A   64  ILE A   78  1                                  15
HELIX    4   4 ILE A   78  ASN A   98  1                                  21
HELIX    5   5 ASN A  102  ALA A  126  1                                  25
HELIX    6   6 HIS A  142  ASN A  174  1                                  33
HELIX    7   7 PRO A  180  SER A  197  1                                  18
HELIX    8   8 SER A  197  PHE A  207  1                                  11
HELIX    9   9 PHE A  207  GLY A  214  1                                   8
HELIX   10  10 ASP A  220  HIS A  233  1                                  14
HELIX   11  11 HIS A  233  ILE A  250  1                                  18
HELIX   12  12 ILE A  250  ALA A  255  1                                   6
HELIX   13  13 SER A  261  SER A  276  1                                  16
HELIX   14  14 VAL A  279  GLN A  284  5                                   6
HELIX   15  15 ASP A  291  ALA A  306  1                                  16
HELIX   16  16 ALA A  306  ARG A  327  1                                  22
HELIX   17  17 PHE A  333  ALA A  338  1                                   6
HELIX   18  18 ASN A  343  SER A  368  1                                  26
HELIX   19  19 LEU A  371  HIS A  376  1                                   6
HELIX   20  20 ALA A  379  VAL A  389  1                                  11
HELIX   21  21 SER A  391  LEU A  401  1                                  11
HELIX   22  22 TRP A  403  GLY A  410  1                                   8
HELIX   23  23 SER A  414  LEU A  445  1                                  32
HELIX   24  24 TYR A  452  VAL A  456  5                                   5
HELIX   25  25 TYR A  460  HIS A  462  5                                   3
HELIX   26  26 ALA A  463  SER A  494  1                                  32
HELIX   27  27 LYS A  498  GLU A  503  1                                   6
HELIX   28  28 ASP A  517  ASP A  525  1                                   9
HELIX   29  29 ARG A  526  HIS A  552  1                                  27
HELIX   30  30 GLU B    4  ALA B   38  1                                  35
HELIX   31  31 THR B   39  ILE B   45  5                                   7
HELIX   32  32 ASP B   66  GLN B   69  5                                   4
HELIX   33  33 GLY B  156  ASN B  159  5                                   4
HELIX   34  34 PRO C    5  ARG C   33  1                                  29
SHEET    1   A 2 GLY A 218  VAL A 219  0
SHEET    2   A 2 VAL A 556  PRO A 557 -1  O  VAL A 556   N  VAL A 219
SHEET    1   B 3 VAL B  71  GLY B  75  0
SHEET    2   B 3 GLN B  78  PHE B  86 -1  O  THR B  80   N  VAL B  72
SHEET    3   B 3 GLY B  89  GLN B  91 -1  O  GLY B  89   N  PHE B  86
SHEET    1   C 4 VAL B  71  GLY B  75  0
SHEET    2   C 4 GLN B  78  PHE B  86 -1  O  THR B  80   N  VAL B  72
SHEET    3   C 4 GLU B 102  THR B 108  1  O  LYS B 106   N  VAL B  81
SHEET    4   C 4 SER B 133  THR B 138 -1  O  TYR B 137   N  ILE B 103
SHEET    1   D 5 ILE B  95  PRO B  98  0
SHEET    2   D 5 PHE B 161  LYS B 167  1  O  VAL B 165   N  ILE B  95
SHEET    3   D 5 GLY B 143  ILE B 148 -1  N  GLY B 143   O  VAL B 166
SHEET    4   D 5 HIS B 114  VAL B 118 -1  N  HIS B 117   O  ILE B 148
SHEET    5   D 5 ASN B 124  VAL B 127 -1  O  VAL B 127   N  HIS B 114
LINK         ND1 HIS A 233                CU    CU A 601     1555   1555  1.96
LINK         NE2 HIS A 283                CU    CU A 601     1555   1555  1.96
LINK         ND1 HIS B 114                CU2  CUA B 201     1555   1555  2.00
LINK         NE2 HIS A 386                FE   HEM A 602     1555   1555  2.01
LINK         NE2 HIS A 282                CU    CU A 601     1555   1555  2.07
LINK         ND1 HIS B 157                CU1  CUA B 201     1555   1555  2.08
LINK         NE2 HIS A  72                FE   HEM A 602     1555   1555  2.10
LINK        FE   HAS A 603                 O1  PEO A 604     1555   1555  2.17
LINK         NE2 HIS A 384                FE   HAS A 603     1555   1555  2.25
LINK         SG  CYS B 149                CU2  CUA B 201     1555   1555  2.29
LINK         SG  CYS B 153                CU1  CUA B 201     1555   1555  2.32
LINK         SG  CYS B 149                CU1  CUA B 201     1555   1555  2.37
LINK         SD  MET B 160                CU2  CUA B 201     1555   1555  2.39
LINK         SG  CYS B 153                CU2  CUA B 201     1555   1555  2.40
LINK        CU    CU A 601                 O2  PEO A 604     1555   1555  2.43
LINK         O   GLN B 151                CU1  CUA B 201     1555   1555  2.66
CISPEP   1 PRO A  137    PRO A  138          0        10.91
CISPEP   2 ALA B   87    PHE B   88          0        -5.38
CISPEP   3 GLN B   91    PRO B   92          0        -6.21
CISPEP   4 ASN B   93    PRO B   94          0         5.63
SITE     1 AC1  4 HIS A 233  HIS A 282  HIS A 283  PEO A 604
SITE     1 AC2 27 LEU A  32  GLY A  39  PRO A  40  GLN A  42
SITE     2 AC2 27 ALA A  43  TYR A  46  TYR A  65  LEU A  69
SITE     3 AC2 27 HIS A  72  ASN A  76  ALA A  77  LEU A 132
SITE     4 AC2 27 TYR A 133  PHE A 385  HIS A 386  VAL A 389
SITE     5 AC2 27 ALA A 390  THR A 394  TRP A 428  MET A 432
SITE     6 AC2 27 MET A 435  ARG A 449  ARG A 450  ALA A 451
SITE     7 AC2 27 LEU A 477  HOH A 715  HOH A 721
SITE     1 AC3 28 TYR A 133  TRP A 229  VAL A 236  TYR A 237
SITE     2 AC3 28 HIS A 282  HIS A 283  THR A 302  SER A 309
SITE     3 AC3 28 ALA A 313  LEU A 320  LEU A 353  LEU A 354
SITE     4 AC3 28 PHE A 356  GLY A 360  GLY A 363  ASN A 366
SITE     5 AC3 28 ALA A 367  ASP A 372  HIS A 376  HIS A 384
SITE     6 AC3 28 PHE A 385  GLN A 388  VAL A 389  ARG A 449
SITE     7 AC3 28 PEO A 604  HOH A 704  HOH A 709  HOH A 724
SITE     1 AC4  5 HIS A 233  VAL A 236  HIS A 283   CU A 601
SITE     2 AC4  5 HAS A 603
SITE     1 AC5 10 PRO A 358  MET A 433  HIS A 440  OLC B 203
SITE     2 AC5 10 VAL C  21  PHE C  22  GLY C  25  VAL C  29
SITE     3 AC5 10 ALA C  32  OLC C 101
SITE     1 AC6  4 TYR A 161  ILE A 475  OLC A 614  OLC A 615
SITE     1 AC7  8 PHE A 213  LEU A 215  TRP A 341  TRP A 426
SITE     2 AC7  8 LEU A 430  OLC A 613  OLC A 614  OLC A 615
SITE     1 AC8  1 THR A 293
SITE     1 AC9  6 LYS A 140  TRP A 143  SER A 212  PHE A 213
SITE     2 AC9  6 LEU A 430  OLC A 616
SITE     1 BC1  3 TRP A 111  OLC A 613  HOH A 730
SITE     1 BC2  5 TYR A 161  LEU A 164  ASP A 165  ARG A 168
SITE     2 BC2  5 OLC A 612
SITE     1 BC3  3 ARG A 168  GLY A 528  OLC A 611
SITE     1 BC4 10 GLY A 104  TRP A 111  ALA A 464  VAL A 465
SITE     2 BC4 10 VAL A 468  PHE A 469  OLC A 607  OLC A 610
SITE     3 BC4 10 OLC A 614  OLC A 616
SITE     1 BC5 11 ASN A 102  GLY A 104  LEU A 105  LEU A 209
SITE     2 BC5 11 VAL A 471  LEU A 472  OLC A 606  OLC A 607
SITE     3 BC5 11 OLC A 613  OLC A 615  HOH A 748
SITE     1 BC6  6 ASP A 415  ARG A 419  OLC A 606  OLC A 607
SITE     2 BC6  6 OLC A 614  HOH A 751
SITE     1 BC7  4 ARG A 337  TRP A 341  OLC A 609  OLC A 613
SITE     1 BC8  6 HIS B 114  CYS B 149  GLN B 151  CYS B 153
SITE     2 BC8  6 HIS B 157  MET B 160
SITE     1 BC9  6 PHE B  21  LEU B  32  TYR B  35  OLC B 204
SITE     2 BC9  6 TYR C  27  PHE C  31
SITE     1 CC1  6 TRP A 441  OLC A 605  ARG B 141  GLU B 144
SITE     2 CC1  6 TYR B 145  ARG C  33
SITE     1 CC2  5 ALA B  13  TYR B  14  TYR B  35  OLC B 202
SITE     2 CC2  5 ILE C  12
SITE     1 CC3  2 OLC A 605  THR C  18
CRYST1  143.550   98.210   94.860  90.00 127.92  90.00 C 1 2 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      0.006966  0.000000  0.005427        0.00000
SCALE2      0.000000  0.010182  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013363        0.00000
      
PROCHECK
Go to PROCHECK summary
 References