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PDBsum entry 3qju

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Oxidoreductase PDB id
3qju
Jmol
Contents
Protein chains
552 a.a.
166 a.a.
33 a.a.
Ligands
HEM
HAS
CUA
CMO
Metals
CU1
HEADER    OXIDOREDUCTASE                          30-JAN-11   3QJU
TITLE     THE STRUCTURE OF AND PHOTOLYTIC INDUCED CHANGES OF CARBON MONOXIDE
TITLE    2 BINDING TO THE CYTOCHROME BA3-OXIDASE FROM 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 MOL_ID: 2;
COMPND   9 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND  10 CHAIN: B;
COMPND  11 SYNONYM: CYTOCHROME C BA(3) SUBUNIT II, CYTOCHROME C OXIDASE
COMPND  12 POLYPEPTIDE II, CYTOCHROME CBA3 SUBUNIT 2;
COMPND  13 EC: 1.9.3.1;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 2A;
COMPND  17 CHAIN: C;
COMPND  18 SYNONYM: CYTOCHROME C BA(3) SUBUNIT IIA, CYTOCHROME C OXIDASE
COMPND  19 POLYPEPTIDE IIA, CYTOCHROME CBA3 SUBUNIT 2A;
COMPND  20 EC: 1.9.3.1;
COMPND  21 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE   3 ORGANISM_TAXID: 300852;
SOURCE   4 STRAIN: HB8;
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;
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;
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    CYTOCHROME BA3 OXIDASE, CARBON MONOXIDE, CO PHOTODISSOCIATION,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.LIU,Y.ZHANG,J.T.SAGE,T.DOUKOV,Y.CHEN,C.D.STOUT,J.A FEE
REVDAT   2   04-APR-12 3QJU    1       JRNL
REVDAT   1   25-JAN-12 3QJU    0
JRNL        AUTH   B.LIU,Y.ZHANG,J.T.SAGE,S.M.SOLTIS,T.DOUKOV,Y.CHEN,C.D.STOUT,
JRNL        AUTH 2 J.A.FEE
JRNL        TITL   STRUCTURAL CHANGES THAT OCCUR UPON PHOTOLYSIS OF THE
JRNL        TITL 2 FE(II)(A3)-CO COMPLEX IN THE CYTOCHROME BA(3)-OXIDASE OF
JRNL        TITL 3 THERMUS THERMOPHILUS: A COMBINED X-RAY CRYSTALLOGRAPHIC AND
JRNL        TITL 4 INFRARED SPECTRAL STUDY DEMONSTRATES CO BINDING TO CU(B).
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1817   658 2012
JRNL        REFN                   ISSN 0006-3002
JRNL        PMID   22226917
JRNL        DOI    10.1016/J.BBABIO.2011.12.010
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.LIU,Y.CHEN,T.DOUKOV,S.M.SOLTIS,C.D.STOUT,J.A.FEE
REMARK   1  TITL   COMBINED MICROSPECTROPHOTOMETRIC AND CRYSTALLOGRAPHIC
REMARK   1  TITL 2 EXAMINATION OF CHEMICALLY-REDUCED AND X-RAY
REMARK   1  TITL 3 RADIATION-REDUCED FORMS OF CYTOCHROME BA3 OXIDASE FROM
REMARK   1  TITL 4 THERMUS THERMOPHILUS: STRUCTURE OF THE REDUCED FORM OF THE
REMARK   1  TITL 5 ENZYME
REMARK   1  REF    BIOCHEMISTRY                  V.  48   820 2009
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  DOI    19140675
REMARK   1 REFERENCE 2
REMARK   1  AUTH   B.LIU,V.M.LUNA,Y.CHEN,C.D.STOUT,J.A.FEE
REMARK   1  TITL   AN UNEXPECTED OUTCOME OF SURFACE ENGINEERING AN INTEGRAL
REMARK   1  TITL 2 MEMBRANE PROTEIN: IMPROVED CRYSTALLIZATION OF CYTOCHROME BA3
REMARK   1  TITL 3 FROM THERMUS THERMOPHILUS
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  63  1029 2007
REMARK   1  REFN                   ESSN 1744-3091
REMARK   1  DOI    18084085
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
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) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7
REMARK   3   NUMBER OF REFLECTIONS             : 20784
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) : 0.288
REMARK   3   R VALUE            (WORKING SET) : 0.286
REMARK   3   FREE R VALUE                     : 0.329
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1127
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) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1522
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600
REMARK   3   BIN FREE R VALUE SET COUNT          : 82
REMARK   3   BIN FREE R VALUE                    : 0.3790
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5924
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 113
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.63
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.18000
REMARK   3    B22 (A**2) : 0.18000
REMARK   3    B33 (A**2) : -0.36000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.532
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.443
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.348
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.897
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6248 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8588 ; 1.761 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   748 ; 6.966 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;36.213 ;22.284
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   901 ;18.789 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;22.545 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   956 ; 0.110 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4743 ; 0.008 ; 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):  3582 ; 0.000 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5786 ; 0.000 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2399 ; 0.000 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2441 ; 0.000 ; 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  : 3
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    11        A   562
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7495 -35.7929   8.2742
REMARK   3    T TENSOR
REMARK   3      T11:   0.1458 T22:   0.1629
REMARK   3      T33:   0.1092 T12:   0.0038
REMARK   3      T13:  -0.0246 T23:   0.0129
REMARK   3    L TENSOR
REMARK   3      L11:   3.2602 L22:   2.0574
REMARK   3      L33:   1.3588 L12:  -1.2595
REMARK   3      L13:  -0.0096 L23:   0.4248
REMARK   3    S TENSOR
REMARK   3      S11:   0.0709 S12:  -0.0144 S13:  -0.5905
REMARK   3      S21:  -0.0818 S22:  -0.0484 S23:   0.2489
REMARK   3      S31:   0.1993 S32:   0.0560 S33:  -0.0226
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     3        B   168
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4484 -12.9367  -2.2308
REMARK   3    T TENSOR
REMARK   3      T11:   0.2996 T22:   0.2308
REMARK   3      T33:   0.0672 T12:   0.0536
REMARK   3      T13:  -0.1083 T23:  -0.0133
REMARK   3    L TENSOR
REMARK   3      L11:   4.4259 L22:   1.9374
REMARK   3      L33:   1.8475 L12:  -1.4190
REMARK   3      L13:  -0.1206 L23:  -0.2704
REMARK   3    S TENSOR
REMARK   3      S11:   0.2251 S12:   0.4475 S13:   0.0370
REMARK   3      S21:  -0.5376 S22:  -0.2687 S23:   0.2827
REMARK   3      S31:  -0.3004 S32:  -0.0750 S33:   0.0436
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     2        C    34
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1960 -30.9664 -15.7497
REMARK   3    T TENSOR
REMARK   3      T11:   0.2268 T22:   0.2281
REMARK   3      T33:   0.0375 T12:   0.0720
REMARK   3      T13:   0.0102 T23:   0.0012
REMARK   3    L TENSOR
REMARK   3      L11:   7.7676 L22:   6.3535
REMARK   3      L33:   0.5228 L12:  -4.5093
REMARK   3      L13:  -0.1364 L23:  -0.1698
REMARK   3    S TENSOR
REMARK   3      S11:   0.1740 S12:   0.3512 S13:   0.1506
REMARK   3      S21:  -0.3476 S22:  -0.2144 S23:  -0.4349
REMARK   3      S31:   0.0007 S32:   0.1295 S33:   0.0404
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 3QJU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063735.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946
REMARK 200  MONOCHROMATOR                  : FLAT MIRROR (VERTICAL FOCUSING),
REMARK 200                                   SINGLE CRYSTAL FOCUSING, SI(111)
REMARK 200                                   BENT MONOCHROMATOR (HORIZONTAL
REMARK 200                                   FOCUSING)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22314
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6
REMARK 200  DATA REDUNDANCY                : 6.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10800
REMARK 200   FOR THE DATA SET  : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.35700
REMARK 200   FOR SHELL         : 2.000
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 1XME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEK 2K, 50 MM KCL, 20 MM BIS-TRIS
REMARK 280  PH 7.0, 6.5 MM N-NONYL-BETA-D-GLUCOPYRANOSIDE, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       82.38500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.87500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.87500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      123.57750
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.87500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.87500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.19250
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.87500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.87500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      123.57750
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.87500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.87500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.19250
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.38500
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: 12970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 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 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     MET B     1
REMARK 465     VAL B     2
REMARK 465     MET C     1
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   ND1  HIS A   233    CU    CU1 A   803              1.69
REMARK 500   NE2  HIS A   233     CE2  TYR A   237              1.88
REMARK 500   O    ARG B   141     OH   TYR B   145              2.04
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    GLU A 500   CD    GLU A 500   OE1     0.069
REMARK 500    CYS B 153   CB    CYS B 153   SG     -0.114
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 102      108.40    -51.49
REMARK 500    LEU A 132      165.00     66.28
REMARK 500    PHE A 135       66.34     32.64
REMARK 500    LEU A 139      107.54    -57.28
REMARK 500    SER A 155      -55.70    -28.72
REMARK 500    PHE A 207      -71.23   -128.33
REMARK 500    ILE A 250      -38.14   -130.71
REMARK 500    PRO A 278       38.81    -87.32
REMARK 500    PHE A 281       -1.56    -56.14
REMARK 500    ARG A 327       35.61    -93.86
REMARK 500    ARG A 330      -97.16    -81.24
REMARK 500    ILE A 357      -73.76    -50.20
REMARK 500    SER A 368       47.41    -83.39
REMARK 500    PHE A 369      -94.84     52.11
REMARK 500    THR A 378     -169.19   -105.00
REMARK 500    HIS A 384      -78.91    -36.08
REMARK 500    SER A 391      -88.44   -102.56
REMARK 500    ASN A 446       -3.67     70.49
REMARK 500    ARG A 495       34.80    -79.65
REMARK 500    ARG A 518      -80.21    -12.23
REMARK 500    ARG A 526       66.09    -67.70
REMARK 500    ASN A 554       74.87   -119.16
REMARK 500    GLU B   4      -56.53     59.79
REMARK 500    VAL B  44       -7.33    -58.93
REMARK 500    ARG B  59       31.89    -99.98
REMARK 500    ALA B  87       85.41    -44.48
REMARK 500    PHE B  88       31.74     99.76
REMARK 500    ASP B 111     -111.78   -126.09
REMARK 500    ASN B 124       73.43   -155.94
REMARK 500    TYR B 152      125.56    -39.98
REMARK 500    LYS C   4      129.45    -27.44
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        23.1      L          L   OUTSIDE RANGE
REMARK 500    GLU C   3        24.8      L          L   OUTSIDE RANGE
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                             CUA B 802  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 157   ND1
REMARK 620 2 CUA B 802  CU2  160.1
REMARK 620 3 CYS B 149   SG  146.6  50.3
REMARK 620 4 CYS B 153   SG  113.3  49.8  99.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HAS A 801  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 384   NE2
REMARK 620 2 HAS A 801   NA   99.7
REMARK 620 3 HAS A 801   NB   96.2 164.1
REMARK 620 4 HAS A 801   NC  102.3  89.2  86.6
REMARK 620 5 HAS A 801   ND   95.6  89.3  90.0 162.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 802  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 114   ND1
REMARK 620 2 CUA B 802  CU1  151.7
REMARK 620 3 CYS B 149   SG  124.3  49.4
REMARK 620 4 CYS B 153   SG  117.6  54.2 103.1
REMARK 620 5 MET B 160   SD   88.7 119.2 102.7 120.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CU1 A 803  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 283   NE2
REMARK 620 2 HIS A 282   NE2  84.4
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 800  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  72   NE2
REMARK 620 2 HEM A 800   NA   91.8
REMARK 620 3 HEM A 800   NB   78.2  85.7
REMARK 620 4 HEM A 800   NC   84.9 176.4  92.2
REMARK 620 5 HEM A 800   ND   98.4  89.4 173.9  92.5
REMARK 620 6 HIS A 386   NE2 171.5  89.3  93.5  93.7  90.0
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 CU1 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAS A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 563
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QPD   RELATED DB: PDB
REMARK 900 APO-I-K258R MUTANT
REMARK 900 RELATED ID: 2QPE   RELATED DB: PDB
REMARK 900 APO-I-K258R/II-E4Q MUTANT
REMARK 900 RELATED ID: 3EH3   RELATED DB: PDB
REMARK 900 APO_REDUCED I-K258R/II-E4Q MUTANT
REMARK 900 RELATED ID: 3EH4   RELATED DB: PDB
REMARK 900 APO_REDUCED I-K258R/II-E4Q MUTANT
REMARK 900 RELATED ID: 3EH5   RELATED DB: PDB
REMARK 900 APO_REDUCED I-K258R/II-E4Q MUTANT
REMARK 900 RELATED ID: 3QJQ   RELATED DB: PDB
REMARK 900 RELATED ID: 3QJR   RELATED DB: PDB
REMARK 900 RELATED ID: 3QJS   RELATED DB: PDB
REMARK 900 RELATED ID: 3QJT   RELATED DB: PDB
REMARK 900 RELATED ID: 3QJV   RELATED DB: PDB
DBREF  3QJU A    2   562  UNP    Q5SJ79   COX1_THET8       2    562
DBREF  3QJU B    1   168  UNP    Q5SJ80   COX2_THET8       1    168
DBREF  3QJU C    1    34  UNP    P82543   COXA_THET8       1     34
SEQADV 3QJU MET A   -5  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A   -4  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A   -3  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A   -2  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A   -1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A    0  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3QJU HIS A    1  UNP  Q5SJ79              EXPRESSION TAG
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 ALA 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    CU1  A 803       1
HET    HEM  A 800      43
HET    HAS  A 801      65
HET    CUA  B 802       2
HET    CMO  A 563       2
HETNAM     CU1 COPPER (I) ION
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     HAS HEME-AS
HETNAM     CUA DINUCLEAR COPPER ION
HETNAM     CMO CARBON MONOXIDE
HETSYN     HEM HEME
FORMUL   4  CU1    CU 1+
FORMUL   5  HEM    C34 H32 FE N4 O4
FORMUL   6  HAS    C54 H64 FE N4 O6
FORMUL   7  CUA    CU2
FORMUL   8  CMO    C O
HELIX    1   1 PRO A   16  LEU A   37  1                                  22
HELIX    2   2 LEU A   37  TYR A   46  1                                  10
HELIX    3   3 ALA A   51  LEU A   59  1                                   9
HELIX    4   4 SER A   64  ASN A   98  1                                  35
HELIX    5   5 ASN A  102  LEU A  125  1                                  24
HELIX    6   6 HIS A  142  ASN A  174  1                                  33
HELIX    7   7 PRO A  180  PHE A  207  1                                  28
HELIX    8   8 PHE A  207  PHE A  213  1                                   7
HELIX    9   9 ASP A  220  HIS A  233  1                                  14
HELIX   10  10 HIS A  233  ILE A  250  1                                  18
HELIX   11  11 ILE A  250  ALA A  255  1                                   6
HELIX   12  12 SER A  261  SER A  276  1                                  16
HELIX   13  13 VAL A  279  HIS A  283  5                                   5
HELIX   14  14 ASP A  291  ALA A  306  1                                  16
HELIX   15  15 ALA A  306  ARG A  327  1                                  22
HELIX   16  16 PHE A  333  ALA A  338  1                                   6
HELIX   17  17 ASN A  343  SER A  368  1                                  26
HELIX   18  18 LEU A  371  HIS A  376  1                                   6
HELIX   19  19 ALA A  379  ALA A  390  1                                  12
HELIX   20  20 SER A  391  GLY A  410  1                                  20
HELIX   21  21 SER A  414  LEU A  445  1                                  32
HELIX   22  22 TYR A  452  HIS A  462  5                                  11
HELIX   23  23 ALA A  463  LEU A  493  1                                  31
HELIX   24  24 GLU A  516  ASP A  525  1                                  10
HELIX   25  25 ARG A  526  HIS A  552  1                                  27
HELIX   26  26 HIS B    5  LEU B   37  1                                  33
HELIX   27  27 ALA B   38  ILE B   45  5                                   8
HELIX   28  28 ASP B   66  GLN B   69  5                                   4
HELIX   29  29 GLY B  156  ASN B  159  5                                   4
HELIX   30  30 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  83
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  THR B 163   N  ILE B  95
SHEET    3   D 5 GLY B 143  ILE B 148 -1  N  TYR B 145   O  ILE B 164
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 B 157                CU1  CUA B 802     1555   1555  1.79
LINK         NE2 HIS A 384                FE   HAS A 801     1555   1555  1.97
LINK         ND1 HIS B 114                CU2  CUA B 802     1555   1555  2.00
LINK         NE2 HIS A 283                CU   CU1 A 803     1555   1555  2.04
LINK         NE2 HIS A 282                CU   CU1 A 803     1555   1555  2.07
LINK         SG  CYS B 149                CU1  CUA B 802     1555   1555  2.08
LINK         SG  CYS B 149                CU2  CUA B 802     1555   1555  2.11
LINK         SG  CYS B 153                CU2  CUA B 802     1555   1555  2.12
LINK         NE2 HIS A  72                FE   HEM A 800     1555   1555  2.23
LINK         SG  CYS B 153                CU1  CUA B 802     1555   1555  2.25
LINK         NE2 HIS A 386                FE   HEM A 800     1555   1555  2.27
LINK         SD  MET B 160                CU2  CUA B 802     1555   1555  2.35
CISPEP   1 PRO A  137    PRO A  138          0         5.60
CISPEP   2 GLN B   91    PRO B   92          0        -0.94
CISPEP   3 ASN B   93    PRO B   94          0         1.31
SITE     1 AC1  4 HIS A 233  HIS A 282  HIS A 283  CMO A 563
SITE     1 AC2 22 LEU A  32  GLY A  39  PRO A  40  GLN A  42
SITE     2 AC2 22 ALA A  43  TYR A  46  TYR A  65  LEU A  69
SITE     3 AC2 22 HIS A  72  ASN A  76  ALA A  77  LEU A 132
SITE     4 AC2 22 TYR A 133  PHE A 385  HIS A 386  VAL A 389
SITE     5 AC2 22 ALA A 390  MET A 435  ARG A 449  ARG A 450
SITE     6 AC2 22 ALA A 451  LEU A 477
SITE     1 AC3 29 TYR A 133  TRP A 229  VAL A 236  TYR A 237
SITE     2 AC3 29 TRP A 239  LEU A 240  HIS A 282  THR A 302
SITE     3 AC3 29 SER A 309  LEU A 310  ALA A 313  LEU A 353
SITE     4 AC3 29 PHE A 356  ILE A 357  GLY A 360  GLY A 363
SITE     5 AC3 29 ASN A 366  ALA A 367  ASP A 372  HIS A 376
SITE     6 AC3 29 VAL A 381  HIS A 384  PHE A 385  GLN A 388
SITE     7 AC3 29 VAL A 389  ARG A 449  CMO A 563  VAL C  11
SITE     8 AC3 29 LEU C  15
SITE     1 AC4  6 HIS B 114  CYS B 149  GLN B 151  CYS B 153
SITE     2 AC4  6 HIS B 157  MET B 160
SITE     1 AC5  6 HIS A 233  VAL A 236  HIS A 282  HIS A 283
SITE     2 AC5  6 HAS A 801  CU1 A 803
CRYST1  109.750  109.750  164.770  90.00  90.00  90.00 P 43 21 2     8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.009112  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009112  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006069        0.00000
      
PROCHECK
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 References