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PDBsum entry 3s33

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3s33
Jmol
Contents
Protein chains
557 a.a.
166 a.a.
33 a.a.
Ligands
HEM
HAS
CUA
Metals
_XE ×5
_CU
HEADER    OXIDOREDUCTASE                          17-MAY-11   3S33
TITLE     STRUCTURE OF THERMUS THERMOPHILUS CYTOCHROME BA3 OXIDASE 10S AFTER XE
TITLE    2 DEPRESSURIZATION
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, CBAC, 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    OXIDOREDUCTASE, XENON
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.M.LUNA,J.A.FEE,A.A.DENIZ,C.D.STOUT
REVDAT   3   12-SEP-12 3S33    1       JRNL
REVDAT   2   30-MAY-12 3S33    1       JRNL
REVDAT   1   23-MAY-12 3S33    0
JRNL        AUTH   V.M.LUNA,J.A.FEE,A.A.DENIZ,C.D.STOUT
JRNL        TITL   MOBILITY OF XE ATOMS WITHIN THE OXYGEN DIFFUSION CHANNEL OF
JRNL        TITL 2 CYTOCHROME BA(3) OXIDASE.
JRNL        REF    BIOCHEMISTRY                  V.  51  4669 2012
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   22607023
JRNL        DOI    10.1021/BI3003988
REMARK   2
REMARK   2 RESOLUTION.    4.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 4.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.06
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 6323
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) : 0.307
REMARK   3   R VALUE            (WORKING SET) : 0.305
REMARK   3   FREE R VALUE                     : 0.350
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 294
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) : 4.45
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.57
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 435
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3230
REMARK   3   BIN FREE R VALUE SET COUNT          : 18
REMARK   3   BIN FREE R VALUE                    : 0.3820
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5964
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 116
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) : 130.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.49000
REMARK   3    B22 (A**2) : -0.49000
REMARK   3    B33 (A**2) : 0.97000
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): 1.593
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 1.412
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 110.263
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.826
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.791
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6287 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8641 ; 1.267 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   753 ; 4.729 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   234 ;34.941 ;22.265
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   910 ;15.956 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.590 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   965 ; 0.075 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4777 ; 0.005 ; 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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3S33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.127
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6368
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.115
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 23.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.19300
REMARK 200   FOR THE DATA SET  : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 25.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000
REMARK 200  R SYM FOR SHELL            (I) : 0.51000
REMARK 200   FOR SHELL         : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1XME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-17% PEG 2000, 0-200MM KCL, 15-60MM
REMARK 280  BIS-TRIS PH 7.0, 6.5MM NONYL-B-D-GLUCOPYRANOSIDE, VAPOR
REMARK 280  DIFFUSION, HANGING 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       81.32000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.12500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.12500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      121.98000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.12500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.12500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.66000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.12500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.12500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      121.98000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.12500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.12500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.66000
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       81.32000
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 13940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24980 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 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 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    SER A     9     CA   GLY B   143     3444     1.03
REMARK 500   C    GLU A     7     CA   GLU B   144     3444     1.17
REMARK 500   C    SER A     9     N    GLY B   143     3444     1.17
REMARK 500   O    SER A     9     N    GLY B   143     3444     1.19
REMARK 500   N    ILE A     8     CA   GLU B   144     3444     1.30
REMARK 500   N    ILE A     8     C    GLU B   144     3444     1.32
REMARK 500   N    ARG A    10     N    GLY B   143     3444     1.36
REMARK 500   C    GLU A     7     C    GLU B   144     3444     1.45
REMARK 500   CA   GLU A     7     CA   GLU B   144     3444     1.49
REMARK 500   NH1  ARG A    10     CB   PHE B   139     3444     1.51
REMARK 500   C    SER A     9     C    PRO B   142     3444     1.58
REMARK 500   C    SER A     9     CA   GLY B   143     3444     1.64
REMARK 500   N    VAL A    11     C    PRO B   142     3444     1.67
REMARK 500   O    GLU A     7     N    TYR B   145     3444     1.75
REMARK 500   CA   ARG A    10     N    GLY B   143     3444     1.76
REMARK 500   N    ARG A    10     C    PRO B   142     3444     1.78
REMARK 500   C    GLU A     7     N    TYR B   145     3444     1.78
REMARK 500   N    VAL A    11     CB   PRO B   142     3444     1.85
REMARK 500   O    SER A     9     C    PRO B   142     3444     1.86
REMARK 500   N    ILE A     8     N    GLU B   144     3444     1.92
REMARK 500   OE1  GLU A    13     N    VAL B   166     3444     1.96
REMARK 500   N    VAL A    11     CA   PRO B   142     3444     1.96
REMARK 500   C    GLU A     7     N    GLU B   144     3444     1.98
REMARK 500   NH1  ARG A    10     CG   PHE B   139     3444     2.01
REMARK 500   N    ILE A     8     N    TYR B   145     3444     2.01
REMARK 500   C    ARG A    10     N    GLY B   143     3444     2.02
REMARK 500   C    SER A     9     O    PRO B   142     3444     2.08
REMARK 500   O    GLU A     7     O    GLY B   143     3444     2.09
REMARK 500   CA   GLU A     7     CB   GLU B   144     3444     2.11
REMARK 500   OE2  GLU A    13     O    GLY B   143     3444     2.13
REMARK 500   CA   ARG A    10     CA   PRO B   142     3444     2.13
REMARK 500   O    SER A     9     O    PRO B   142     3444     2.13
REMARK 500   CB   ARG A    10     CA   PRO B   142     3444     2.17
REMARK 500   CD   GLU A     7     CG   GLU B   144     3444     2.17
REMARK 500   C    ARG A    10     C    PRO B   142     3444     2.18
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   7   CB    GLU A   7   CG      0.129
REMARK 500    GLY B 143   N     GLY B 143   CA      0.117
REMARK 500    GLU B 144   N     GLU B 144   CA      0.143
REMARK 500    GLU B 144   CA    GLU B 144   C       0.164
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    GLU B 144   N   -  CA  -  C   ANGL. DEV. =  16.8 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    ARG A  10      -37.78    -21.09
REMARK 500    VAL A  90      -43.68   -133.07
REMARK 500    ASN A 102       95.92    -47.33
REMARK 500    ALA A 129       49.59   -144.63
REMARK 500    LEU A 132      176.49     62.20
REMARK 500    PHE A 135       54.12     35.30
REMARK 500    PHE A 207      -74.19   -118.85
REMARK 500    PRO A 278       47.89    -82.06
REMARK 500    VAL A 279       11.32   -141.22
REMARK 500    ARG A 330     -111.09    -98.32
REMARK 500    SER A 368       45.38    -90.12
REMARK 500    PHE A 369      -94.25     44.56
REMARK 500    GLN A 388      -72.57    -92.54
REMARK 500    SER A 391      -82.27   -107.09
REMARK 500    ALA A 463       30.47    -87.37
REMARK 500    PRO A 507       60.00    -60.56
REMARK 500    ARG A 518      -64.00    -28.79
REMARK 500    GLU B   4      -57.76     64.71
REMARK 500    ALA B  87       86.34    -53.70
REMARK 500    PHE B  88       53.10     77.31
REMARK 500    ASP B 111      -86.02   -123.44
REMARK 500    GLU B 144       43.56    -81.70
REMARK 500    GLU C   3     -152.78   -156.51
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    GLU A   7        22.8      L          L   OUTSIDE RANGE
REMARK 500    GLU B 144        18.4      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                              CU A 803  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 233   ND1
REMARK 620 2 HIS A 283   NE2 144.1
REMARK 620 3 HIS A 282   NE2 103.0  84.7
REMARK 620 N                    1     2
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  158.3
REMARK 620 3 CYS B 149   SG  130.5  40.7
REMARK 620 4 MET B 160   SD   95.5 103.9  91.6
REMARK 620 N                    1     2     3
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  157.5
REMARK 620 3 CYS B 153   SG  117.6  40.5
REMARK 620 4 GLN B 151   O    86.3  96.4  88.3
REMARK 620 N                    1     2     3
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 386   NE2
REMARK 620 2 HEM A 800   NA   82.8
REMARK 620 3 HEM A 800   NB   93.2  88.2
REMARK 620 4 HEM A 800   NC  103.9 173.3  90.8
REMARK 620 5 HEM A 800   ND   89.1  89.2 176.3  91.4
REMARK 620 6 HIS A  72   NE2 174.7  96.2  92.0  77.2  85.6
REMARK 620 N                    1     2     3     4     5
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   88.0
REMARK 620 3 HAS A 801   NB   91.1 178.5
REMARK 620 4 HAS A 801   NC   89.8  92.8  88.4
REMARK 620 5 HAS A 801   ND   89.2  91.4  87.3 175.6
REMARK 620 N                    1     2     3     4
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 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 XE A 563
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A 567
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S38   RELATED DB: PDB
REMARK 900 RELATED ID: 3S39   RELATED DB: PDB
REMARK 900 RELATED ID: 3S3A   RELATED DB: PDB
REMARK 900 RELATED ID: 3S3B   RELATED DB: PDB
REMARK 900 RELATED ID: 3S3C   RELATED DB: PDB
REMARK 900 RELATED ID: 3S3D   RELATED DB: PDB
DBREF  3S33 A    2   562  UNP    Q5SJ79   COX1_THET8       2    562
DBREF  3S33 B    3   168  UNP    Q5SJ80   COX2_THET8       3    168
DBREF  3S33 C    2    34  UNP    P82543   COXA_THET8       2     34
SEQADV 3S33 MET A   -5  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 HIS A   -4  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 HIS A   -3  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 HIS A   -2  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 HIS A   -1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 HIS A    0  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 3S33 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  166  ASP GLU HIS LYS ALA HIS LYS ALA ILE LEU ALA TYR GLU
SEQRES   2 B  166  LYS GLY TRP LEU ALA PHE SER LEU ALA MET LEU PHE VAL
SEQRES   3 B  166  PHE ILE ALA LEU ILE ALA TYR THR LEU ALA THR HIS THR
SEQRES   4 B  166  ALA GLY VAL ILE PRO ALA GLY LYS LEU GLU ARG VAL ASP
SEQRES   5 B  166  PRO THR THR VAL ARG GLN GLU GLY PRO TRP ALA ASP PRO
SEQRES   6 B  166  ALA GLN ALA VAL VAL GLN THR GLY PRO ASN GLN TYR THR
SEQRES   7 B  166  VAL TYR VAL LEU ALA PHE ALA PHE GLY TYR GLN PRO ASN
SEQRES   8 B  166  PRO ILE GLU VAL PRO GLN GLY ALA GLU ILE VAL PHE LYS
SEQRES   9 B  166  ILE THR SER PRO ASP VAL ILE HIS GLY PHE HIS VAL GLU
SEQRES  10 B  166  GLY THR ASN ILE ASN VAL GLU VAL LEU PRO GLY GLU VAL
SEQRES  11 B  166  SER THR VAL ARG TYR THR PHE LYS ARG PRO GLY GLU TYR
SEQRES  12 B  166  ARG ILE ILE CYS ASN GLN TYR CYS GLY LEU GLY HIS GLN
SEQRES  13 B  166  ASN MET PHE GLY THR ILE VAL VAL LYS GLU
SEQRES   1 C   33  GLU GLU LYS PRO LYS GLY ALA LEU ALA VAL ILE LEU VAL
SEQRES   2 C   33  LEU THR LEU THR ILE LEU VAL PHE TRP LEU GLY VAL TYR
SEQRES   3 C   33  ALA VAL PHE PHE ALA ARG GLY
HET     CU  A 803       1
HET    HEM  A 800      43
HET    HAS  A 801      65
HET    CUA  B 802       2
HET     XE  A 563       1
HET     XE  A 564       1
HET     XE  A 565       1
HET     XE  A 566       1
HET     XE  A 567       1
HETNAM      CU COPPER (II) ION
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     HAS HEME-AS
HETNAM     CUA DINUCLEAR COPPER ION
HETNAM      XE XENON
HETSYN     HEM HEME
FORMUL   4   CU    CU 2+
FORMUL   5  HEM    C34 H32 FE N4 O4
FORMUL   6  HAS    C54 H64 FE N4 O6
FORMUL   7  CUA    CU2
FORMUL   8   XE    5(XE)
HELIX    1   1 ARG A   10  TYR A   15  1                                   6
HELIX    2   2 PRO A   16  LEU A   37  1                                  22
HELIX    3   3 LEU A   37  TYR A   46  1                                  10
HELIX    4   4 ALA A   51  LEU A   59  1                                   9
HELIX    5   5 SER A   64  ILE A   78  1                                  15
HELIX    6   6 ILE A   78  ASN A   98  1                                  21
HELIX    7   7 ASN A  102  ALA A  126  1                                  25
HELIX    8   8 HIS A  142  ASN A  174  1                                  33
HELIX    9   9 PRO A  180  PHE A  207  1                                  28
HELIX   10  10 PHE A  207  GLY A  214  1                                   8
HELIX   11  11 ASP A  220  HIS A  233  1                                  14
HELIX   12  12 HIS A  233  ILE A  250  1                                  18
HELIX   13  13 ILE A  250  GLY A  256  1                                   7
HELIX   14  14 SER A  261  SER A  276  1                                  16
HELIX   15  15 VAL A  279  GLN A  284  5                                   6
HELIX   16  16 ASP A  291  VAL A  305  1                                  15
HELIX   17  17 VAL A  305  ARG A  327  1                                  23
HELIX   18  18 PHE A  333  LEU A  339  1                                   7
HELIX   19  19 ASN A  343  ALA A  367  1                                  25
HELIX   20  20 SER A  368  THR A  370  5                                   3
HELIX   21  21 LEU A  371  HIS A  376  1                                   6
HELIX   22  22 ALA A  379  LEU A  387  1                                   9
HELIX   23  23 SER A  391  GLY A  410  1                                  20
HELIX   24  24 SER A  414  LEU A  445  1                                  32
HELIX   25  25 TYR A  452  ALA A  464  5                                  13
HELIX   26  26 VAL A  465  LEU A  493  1                                  29
HELIX   27  27 GLU A  516  ASP A  525  1                                  10
HELIX   28  28 ARG A  526  GLY A  551  1                                  26
HELIX   29  29 GLU B    4  THR B   39  1                                  36
HELIX   30  30 HIS B   40  ILE B   45  5                                   6
HELIX   31  31 ASP B   66  GLN B   69  5                                   4
HELIX   32  32 GLY B  156  ASN B  159  5                                   4
HELIX   33  33 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  GLN B  73  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  GLN B  91   N  LEU B  84
SHEET    1   C 4 VAL B  71  GLN B  73  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  VAL B 104   N  TYR B  79
SHEET    4   C 4 SER B 133  TYR B 137 -1  O  SER B 133   N  ILE B 107
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  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 A 233                CU    CU A 803     1555   1555  1.73
LINK         ND1 HIS B 114                CU2  CUA B 802     1555   1555  1.80
LINK         ND1 HIS B 157                CU1  CUA B 802     1555   1555  1.96
LINK         NE2 HIS A 283                CU    CU A 803     1555   1555  1.96
LINK         NE2 HIS A 386                FE   HEM A 800     1555   1555  2.02
LINK         NE2 HIS A  72                FE   HEM A 800     1555   1555  2.14
LINK         NE2 HIS A 282                CU    CU A 803     1555   1555  2.20
LINK         SG  CYS B 153                CU1  CUA B 802     1555   1555  2.36
LINK         SG  CYS B 149                CU2  CUA B 802     1555   1555  2.38
LINK         SD  MET B 160                CU2  CUA B 802     1555   1555  2.39
LINK         NE2 HIS A 384                FE   HAS A 801     1555   1555  2.48
LINK         O   GLN B 151                CU1  CUA B 802     1555   1555  2.48
CISPEP   1 PRO A  137    PRO A  138          0         1.97
CISPEP   2 GLN B   91    PRO B   92          0         0.00
CISPEP   3 ASN B   93    PRO B   94          0        -7.27
SITE     1 AC1  3 HIS A 233  HIS A 282  HIS A 283
SITE     1 AC2 24 SER A  36  GLY A  39  PRO A  40  GLN A  42
SITE     2 AC2 24 ALA A  43  TYR A  46  TYR A  65  LEU A  69
SITE     3 AC2 24 HIS A  72  ASN A  76  ALA A  77  LEU A 132
SITE     4 AC2 24 TYR A 133  PHE A 385  HIS A 386  VAL A 389
SITE     5 AC2 24 ALA A 390  THR A 394  TRP A 428  MET A 432
SITE     6 AC2 24 ARG A 449  ARG A 450  ALA A 451  LEU A 477
SITE     1 AC3 27 TYR A 133  TRP A 229  VAL A 236  TYR A 237
SITE     2 AC3 27 TRP A 239  HIS A 282  HIS A 283  SER A 309
SITE     3 AC3 27 ALA A 313  ALA A 317  TRP A 335  VAL A 350
SITE     4 AC3 27 LEU A 353  LEU A 354  PHE A 356  GLY A 360
SITE     5 AC3 27 GLY A 363  ASN A 366  ALA A 367  ASP A 372
SITE     6 AC3 27 HIS A 376  VAL A 381  HIS A 384  PHE A 385
SITE     7 AC3 27 GLN A 388  VAL A 389  ARG A 449
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  1 GLY A 232
SITE     1 AC6  1 PHE A 228
CRYST1  108.250  108.250  162.640  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      0.009238  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009238  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006149        0.00000
      
PROCHECK
Go to PROCHECK summary
 References