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PDBsum entry 4faa

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4faa
Jmol
Contents
Protein chains
535 a.a.
166 a.a.
31 a.a.
Ligands
HEM
HAS-PEO
OLC ×16
CUA
Metals
_CU
Waters ×97
HEADER    OXIDOREDUCTASE                          21-MAY-12   4FAA
TITLE     STRUCTURE OF RECOMBINANT CYTOCHROME BA3 OXIDASE MUTANT A120F+A204F
TITLE    2 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 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 HB8;
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 HB8;
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 HB8;
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   31-OCT-12 4FAA    0
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 2011_01_25_1225)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.84
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2
REMARK   3   NUMBER OF REFLECTIONS             : 25136
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.254
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120
REMARK   3   FREE R VALUE TEST SET COUNT      : 1286
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 56.8475 -  5.8227    0.95     2621   170  0.1879 0.2244
REMARK   3     2  5.8227 -  4.6223    0.97     2635   156  0.1637 0.2471
REMARK   3     3  4.6223 -  4.0382    0.97     2660   150  0.1726 0.2303
REMARK   3     4  4.0382 -  3.6691    0.98     2637   139  0.1681 0.2249
REMARK   3     5  3.6691 -  3.4061    0.98     2667   145  0.1777 0.2380
REMARK   3     6  3.4061 -  3.2053    0.98     2654   142  0.1872 0.2388
REMARK   3     7  3.2053 -  3.0448    0.98     2679   127  0.2018 0.2737
REMARK   3     8  3.0448 -  2.9123    0.98     2663   133  0.2620 0.3599
REMARK   3     9  2.9123 -  2.8002    0.97     2634   124  0.3430 0.4307
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.36
REMARK   3   B_SOL              : 41.86
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.840
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.50930
REMARK   3    B22 (A**2) : -3.23880
REMARK   3    B33 (A**2) : 7.74800
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 6.20140
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.009           6384
REMARK   3   ANGLE     :  1.151           8670
REMARK   3   CHIRALITY :  0.076            954
REMARK   3   PLANARITY :  0.005           1035
REMARK   3   DIHEDRAL  : 20.601           2248
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4FAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB072652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
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   : 25136
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.836
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
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       71.64000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.14500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.64000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.14500
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: 9020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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     VAL A    11
REMARK 465     TYR A    12
REMARK 465     LEU A   492
REMARK 465     LEU A   493
REMARK 465     SER A   494
REMARK 465     ARG A   495
REMARK 465     GLU A   496
REMARK 465     ARG A   497
REMARK 465     LYS A   498
REMARK 465     PRO A   499
REMARK 465     GLU A   500
REMARK 465     LEU A   501
REMARK 465     ALA A   502
REMARK 465     GLU A   503
REMARK 465     ALA A   504
REMARK 465     PRO A   515
REMARK 465     GLU A   516
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     GLU A  13    CG   CD   OE1  OE2
REMARK 470     ARG A  57    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 337    CD   NE   CZ   NH1  NH2
REMARK 470     PHE A 489    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG A 519    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 520    CG   CD1  CD2
REMARK 470     HIS B   5    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS B   6    CG   CD   CE   NZ
REMARK 470     LYS B   9    CG   CD   CE   NZ
REMARK 470     GLU B  61    CG   CD   OE1  OE2
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   OE2  GLU B    51     O    HOH B   309              1.89
REMARK 500   O    HOH A   722     O    HOH A   723              1.92
REMARK 500   OG1  THR A   315     O    HOH A   726              2.04
REMARK 500   OG1  THR B   108     O    HOH B   314              2.06
REMARK 500   NE2  HIS A   233     CE2  TYR A   237              2.10
REMARK 500   O    PRO B    46     O    HOH B   340              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   330     O    HOH B   330     2554     1.94
REMARK 500   O    HOH B   308     O    HOH B   324     2554     2.08
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  98       59.95     39.40
REMARK 500    ALA A 129       42.28   -153.10
REMARK 500    TYR A 133        5.81    -68.00
REMARK 500    PHE A 135       61.77     34.29
REMARK 500    PHE A 207      -64.11   -133.14
REMARK 500    HIS A 233      -61.35    -91.82
REMARK 500    ILE A 250      -54.93   -121.49
REMARK 500    PRO A 278       32.76    -79.08
REMARK 500    SER A 391      -70.88   -114.48
REMARK 500    LEU A 401      -16.01    -47.71
REMARK 500    ALA A 454      -19.73    -49.22
REMARK 500    ARG A 526       70.94    -67.60
REMARK 500    HIS A 552       40.75   -145.17
REMARK 500    GLN B  60      -15.08   -143.97
REMARK 500    ASP B 111      -79.79   -129.61
REMARK 500    ASN B 124       82.52   -167.31
REMARK 500    TYR B 152      128.37    -34.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY B   48     LYS B   49                 -135.47
REMARK 500
REMARK 500 REMARK: NULL
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 140.3
REMARK 620 3 HIS A 282   NE2  86.4 106.2
REMARK 620 4 PEO A 604   O2   82.3  94.3 158.3
REMARK 620 5 PEO A 604   O1   91.3 107.5 128.9  33.7
REMARK 620 N                    1     2     3     4
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  137.3
REMARK 620 3 CYS B 149   SG  114.6  56.2
REMARK 620 4 CYS B 153   SG  106.3  56.8 112.1
REMARK 620 5 MET B 160   SD   93.7 129.0 112.0 116.8
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   79.4
REMARK 620 3 HEM A 602   NB   79.0  82.0
REMARK 620 4 HEM A 602   NC   87.7 163.4  85.3
REMARK 620 5 HEM A 602   ND   86.8  95.2 165.9  94.5
REMARK 620 6 HIS A  72   NE2 167.6  97.5  88.7  92.9 105.4
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  149.4
REMARK 620 3 CYS B 149   SG  115.5  56.5
REMARK 620 4 CYS B 153   SG  126.3  57.5 113.1
REMARK 620 N                    1     2     3
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 HIS A 384   NE2
REMARK 620 2 HAS A 603   NA   88.1
REMARK 620 3 HAS A 603   NB   97.9 174.0
REMARK 620 4 HAS A 603   NC  105.1  89.4  88.9
REMARK 620 5 HAS A 603   ND   82.0  91.3  89.7 172.9
REMARK 620 6 PEO A 604   O1  151.8  73.3 101.1  95.9  77.6
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  4FAA A    2   562  UNP    Q5SJ79   COX1_THET8       2    562
DBREF  4FAA B    1   168  UNP    Q5SJ80   COX2_THET8       1    168
DBREF  4FAA C    1    34  UNP    P82543   COXA_THET8       1     34
SEQADV 4FAA MET A   -5  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A   -4  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A   -3  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A   -2  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A   -1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A    0  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA HIS A    1  UNP  Q5SJ79              EXPRESSION TAG
SEQADV 4FAA PHE A  120  UNP  Q5SJ79    ALA   120 ENGINEERED MUTATION
SEQADV 4FAA 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 PHE 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   *97(H2 O)
HELIX    1   1 PRO A   16  LEU A   37  1                                  22
HELIX    2   2 PHE A   38  TYR A   46  1                                   9
HELIX    3   3 ALA A   51  LEU A   59  1                                   9
HELIX    4   4 SER A   64  ILE A   78  1                                  15
HELIX    5   5 ILE A   78  ASN A   98  1                                  21
HELIX    6   6 ASN A  102  LEU A  125  1                                  24
HELIX    7   7 HIS A  142  ASN A  174  1                                  33
HELIX    8   8 PRO A  180  PHE A  207  1                                  28
HELIX    9   9 PHE A  207  PHE A  213  1                                   7
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  ALA A  367  1                                  25
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  GLY A  410  1                                  20
HELIX   22  22 SER A  414  LEU A  445  1                                  32
HELIX   23  23 TYR A  452  VAL A  456  5                                   5
HELIX   24  24 TYR A  460  HIS A  462  5                                   3
HELIX   25  25 ALA A  463  VAL A  491  1                                  29
HELIX   26  26 ARG A  518  MET A  524  1                                   7
HELIX   27  27 ARG A  526  GLY A  551  1                                  26
HELIX   28  28 GLU B    4  LEU B   37  1                                  34
HELIX   29  29 ALA B   38  ILE B   45  5                                   8
HELIX   30  30 ASP B   66  GLN B   69  5                                   4
HELIX   31  31 GLY B  156  ASN B  159  5                                   4
HELIX   32  32 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  GLY B  89   N  PHE B  86
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  THR B 108   N  ALA B  85
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  ILE B 147   O  GLY B 162
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  1.92
LINK         ND1 HIS B 114                CU2  CUA B 201     1555   1555  2.06
LINK         NE2 HIS A 283                CU    CU A 601     1555   1555  2.18
LINK         NE2 HIS A 386                FE   HEM A 602     1555   1555  2.25
LINK         NE2 HIS A  72                FE   HEM A 602     1555   1555  2.28
LINK         ND1 HIS B 157                CU1  CUA B 201     1555   1555  2.29
LINK         NE2 HIS A 282                CU    CU A 601     1555   1555  2.31
LINK         NE2 HIS A 384                FE   HAS A 603     1555   1555  2.38
LINK         SG  CYS B 149                CU1  CUA B 201     1555   1555  2.44
LINK         SG  CYS B 149                CU2  CUA B 201     1555   1555  2.45
LINK         SG  CYS B 153                CU1  CUA B 201     1555   1555  2.48
LINK         SG  CYS B 153                CU2  CUA B 201     1555   1555  2.50
LINK        CU    CU A 601                 O2  PEO A 604     1555   1555  2.52
LINK        FE   HAS A 603                 O1  PEO A 604     1555   1555  2.53
LINK        CU    CU A 601                 O1  PEO A 604     1555   1555  2.57
LINK         SD  MET B 160                CU2  CUA B 201     1555   1555  2.69
CISPEP   1 PRO A  137    PRO A  138          0        12.07
CISPEP   2 ALA B   87    PHE B   88          0        -5.94
CISPEP   3 GLN B   91    PRO B   92          0        -3.84
CISPEP   4 ASN B   93    PRO B   94          0         7.40
SITE     1 AC1  4 HIS A 233  HIS A 282  HIS A 283  PEO A 604
SITE     1 AC2 23 LEU A  32  GLY A  39  GLN A  42  ALA A  43
SITE     2 AC2 23 TYR A  46  TYR A  65  HIS A  72  ASN A  76
SITE     3 AC2 23 ALA A  77  LEU A 132  TYR A 133  PHE A 385
SITE     4 AC2 23 HIS A 386  VAL A 389  ALA A 390  THR A 394
SITE     5 AC2 23 MET A 432  MET A 435  ARG A 449  ARG A 450
SITE     6 AC2 23 ALA A 451  LEU A 477  HOH A 715
SITE     1 AC3 30 TYR A 133  TRP A 229  VAL A 236  TYR A 237
SITE     2 AC3 30 TRP A 239  HIS A 282  HIS A 283  SER A 309
SITE     3 AC3 30 ALA A 313  ALA A 317  LEU A 353  PHE A 356
SITE     4 AC3 30 ILE A 357  GLY A 360  GLY A 363  ILE A 364
SITE     5 AC3 30 ASN A 366  ALA A 367  ASP A 372  HIS A 376
SITE     6 AC3 30 VAL A 381  HIS A 384  PHE A 385  GLN A 388
SITE     7 AC3 30 VAL A 389  ARG A 449  PEO A 604  HOH A 701
SITE     8 AC3 30 HOH A 719  HOH A 749
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  7 PRO A 358  HIS A 440  LEU A 444  OLC B 203
SITE     2 AC5  7 GLY C  25  VAL C  29  OLC C 101
SITE     1 AC6  6 VAL A 158  TYR A 161  ILE A 475  VAL A 476
SITE     2 AC6  6 OLC A 614  OLC A 615
SITE     1 AC7  6 PHE A 213  LEU A 215  TRP A 341  TRP A 426
SITE     2 AC7  6 OLC A 614  OLC A 615
SITE     1 AC8  3 PRO A 292  VAL A 300  HOH B 304
SITE     1 AC9  6 LYS A 140  SER A 212  PHE A 213  LEU A 430
SITE     2 AC9  6 OLC A 616  HOH A 703
SITE     1 BC1  2 TRP A 111  OLC A 613
SITE     1 BC2  4 TYR A 161  LEU A 164  ARG A 168  OLC A 612
SITE     1 BC3  5 TRP A 167  ARG A 168  LYS A 171  GLY A 528
SITE     2 BC3  5 OLC A 611
SITE     1 BC4  4 GLY A 104  TRP A 111  OLC A 610  OLC A 614
SITE     1 BC5 12 ASN A 102  LEU A 108  SER A 150  VAL A 151
SITE     2 BC5 12 LEU A 154  VAL A 471  LEU A 472  OLC A 606
SITE     3 BC5 12 OLC A 607  OLC A 613  OLC A 615  HOH A 736
SITE     1 BC6  7 VAL A 205  ASP A 415  ALA A 416  ARG A 419
SITE     2 BC6  7 OLC A 606  OLC A 607  OLC A 614
SITE     1 BC7  7 ARG A 337  TRP A 341  TRP A 426  LEU A 430
SITE     2 BC7  7 ILE A 434  OLC A 609  HOH A 745
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  VAL B  28  LEU B  32  TYR B  35
SITE     2 BC9  6 OLC B 204  PHE C  31
SITE     1 CC1  9 TRP A 441  OLC A 605  GLY B 120  ARG B 141
SITE     2 CC1  9 GLU B 144  HOH B 331  VAL C  29  ARG C  33
SITE     3 CC1  9 OLC C 101
SITE     1 CC2  7 ALA B  13  TYR B  14  PHE B  21  TYR B  35
SITE     2 CC2  7 OLC B 202  LEU C   9  ILE C  12
SITE     1 CC3  3 OLC A 605  OLC B 203  THR C  18
CRYST1  143.280   98.290   95.050  90.00 127.50  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      0.006979  0.000000  0.005355        0.00000
SCALE2      0.000000  0.010174  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013261        0.00000
      
PROCHECK
Go to PROCHECK summary
 References