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PDBsum entry 3mqe

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3mqe
Jmol
Contents
Protein chains
552 a.a.
Ligands
HEM ×4
NAG ×8
NAG-NAG-NAG ×4
BOG ×2
416 ×4
Waters ×97
HEADER    OXIDOREDUCTASE                          28-APR-10   3MQE
TITLE     STRUCTURE OF SC-75416 BOUND AT THE COX-2 ACTIVE SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: MCOX-2 C DELTA (UNP RESIDUES 18 TO 604);
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   6 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   7 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   8 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   9 2;
COMPND  10 EC: 1.14.99.1;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: COX-2, COX2, PGHS-B, PTGS2, TIS10;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    COX2, COX-2, PGH2S-2, CYCLOOXYGENASE-2, DIOXYGENASE, DISULFIDE BOND,
KEYWDS   2 ENDOPLASMIC RETICULUM, FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME,
KEYWDS   3 IRON, LIPID SYNTHESIS, MEMBRANE, METAL-BINDING, MICROSOME,
KEYWDS   4 OXIDOREDUCTASE, PEROXIDASE, PHOSPHOPROTEIN, PROSTAGLANDIN
KEYWDS   5 BIOSYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.L.WANG,D.LIMBURG,M.J.GRANETO,J.SPRINGER,J.ROGIER,J.R.KIEFER
REVDAT   2   01-DEC-10 3MQE    1       JRNL
REVDAT   1   27-OCT-10 3MQE    0
JRNL        AUTH   J.L.WANG,D.LIMBURG,M.J.GRANETO,J.SPRINGER,J.R.HAMPER,S.LIAO,
JRNL        AUTH 2 J.L.PAWLITZ,R.G.KURUMBAIL,T.MAZIASZ,J.J.TALLEY,J.R.KIEFER,
JRNL        AUTH 3 J.CARTER
JRNL        TITL   THE NOVEL BENZOPYRAN CLASS OF SELECTIVE CYCLOOXYGENASE-2
JRNL        TITL 2 INHIBITORS. PART 2: THE SECOND CLINICAL CANDIDATE HAVING A
JRNL        TITL 3 SHORTER AND FAVORABLE HUMAN HALF-LIFE.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  7159 2010
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   20709553
JRNL        DOI    10.1016/J.BMCL.2010.07.054
REMARK   2
REMARK   2 RESOLUTION.    2.80 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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 73941
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) : 0.241
REMARK   3   R VALUE            (WORKING SET) : 0.236
REMARK   3   FREE R VALUE                     : 0.290
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 8264
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5313
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.94
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560
REMARK   3   BIN FREE R VALUE SET COUNT          : 587
REMARK   3   BIN FREE R VALUE                    : 0.4070
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17896
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 580
REMARK   3   SOLVENT ATOMS            : 97
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.72000
REMARK   3    B22 (A**2) : 6.86000
REMARK   3    B33 (A**2) : -2.14000
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): 0.422
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.348
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.628
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18970 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A): 12968 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25810 ; 1.270 ; 2.004
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 31484 ; 0.911 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2204 ; 5.790 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   896 ;38.807 ;24.107
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3104 ;17.075 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;18.088 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2742 ; 0.068 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20744 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  3856 ; 0.001 ; 0.020
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): 11036 ; 0.229 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4416 ; 0.049 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17936 ; 0.440 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7934 ; 0.748 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7874 ; 1.264 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     55       A     500      4
REMARK   3           1     B     55       B     500      4
REMARK   3           1     C     55       C     500      4
REMARK   3           1     D     55       D     500      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   6295 ;  0.26 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   6295 ;  0.25 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   6295 ;  0.24 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   6295 ;  0.26 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   6295 ;  0.23 ;  2.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):   6295 ;  0.24 ;  2.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):   6295 ;  0.21 ;  2.00
REMARK   3   MEDIUM THERMAL     1    D (A**2):   6295 ;  0.20 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
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    18        A   681
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9817 -23.4941 -64.2333
REMARK   3    T TENSOR
REMARK   3      T11:   0.1385 T22:   0.0318
REMARK   3      T33:   0.1374 T12:   0.0051
REMARK   3      T13:   0.0039 T23:  -0.0136
REMARK   3    L TENSOR
REMARK   3      L11:   1.6946 L22:   0.5403
REMARK   3      L33:   0.9606 L12:   0.0176
REMARK   3      L13:  -0.0867 L23:  -0.3020
REMARK   3    S TENSOR
REMARK   3      S11:   0.0557 S12:   0.0132 S13:   0.1074
REMARK   3      S21:   0.0210 S22:  -0.0263 S23:   0.0547
REMARK   3      S31:  -0.0201 S32:  -0.1955 S33:  -0.0294
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    18        B   681
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6864 -29.5910 -55.2820
REMARK   3    T TENSOR
REMARK   3      T11:   0.1593 T22:   0.0134
REMARK   3      T33:   0.1416 T12:   0.0006
REMARK   3      T13:   0.0089 T23:  -0.0196
REMARK   3    L TENSOR
REMARK   3      L11:   1.4191 L22:   0.5934
REMARK   3      L33:   0.8264 L12:  -0.0033
REMARK   3      L13:   0.1307 L23:  -0.4658
REMARK   3    S TENSOR
REMARK   3      S11:   0.0674 S12:  -0.0406 S13:   0.1223
REMARK   3      S21:  -0.0058 S22:  -0.0745 S23:  -0.0871
REMARK   3      S31:  -0.0082 S32:   0.1417 S33:   0.0071
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    18        C   681
REMARK   3    ORIGIN FOR THE GROUP (A):  73.6882 -46.8306   0.6808
REMARK   3    T TENSOR
REMARK   3      T11:   0.1773 T22:   0.0967
REMARK   3      T33:   0.1666 T12:   0.0313
REMARK   3      T13:   0.0231 T23:   0.0268
REMARK   3    L TENSOR
REMARK   3      L11:   1.4666 L22:   0.4305
REMARK   3      L33:   1.0977 L12:   0.0985
REMARK   3      L13:   0.1032 L23:   0.2646
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0355 S12:  -0.0709 S13:  -0.1454
REMARK   3      S21:   0.0479 S22:   0.0261 S23:  -0.0663
REMARK   3      S31:   0.1085 S32:   0.2040 S33:   0.0093
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    18        D   681
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0139 -40.5752   9.5842
REMARK   3    T TENSOR
REMARK   3      T11:   0.1552 T22:   0.1318
REMARK   3      T33:   0.1420 T12:  -0.0085
REMARK   3      T13:   0.0241 T23:   0.0208
REMARK   3    L TENSOR
REMARK   3      L11:   1.2409 L22:   0.7050
REMARK   3      L33:   0.9354 L12:   0.0464
REMARK   3      L13:  -0.0738 L23:   0.4137
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0331 S12:   0.0397 S13:  -0.0985
REMARK   3      S21:   0.0172 S22:  -0.0154 S23:   0.0951
REMARK   3      S31:   0.0647 S32:  -0.1486 S33:   0.0486
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 3MQE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB058869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
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                         : CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82436
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.11200
REMARK 200   FOR THE DATA SET  : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.44700
REMARK 200   FOR SHELL         : 1.430
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   (%): 60.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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       91.85050
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.18900
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.85050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.18900
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A   570
REMARK 465     PRO A   571
REMARK 465     GLN A   572
REMARK 465     PRO A   573
REMARK 465     THR A   574
REMARK 465     LYS A   575
REMARK 465     THR A   576
REMARK 465     ALA A   577
REMARK 465     THR A   578
REMARK 465     ILE A   579
REMARK 465     ASN A   580
REMARK 465     ALA A   581
REMARK 465     SER A   582
REMARK 465     ALA A   583
REMARK 465     SER A   584
REMARK 465     HIS A   585
REMARK 465     SER A   586
REMARK 465     ARG A   587
REMARK 465     LEU A   588
REMARK 465     ASP A   589
REMARK 465     ASP A   590
REMARK 465     ILE A   591
REMARK 465     ASN A   592
REMARK 465     PRO A   593
REMARK 465     THR A   594
REMARK 465     VAL A   595
REMARK 465     LEU A   596
REMARK 465     ILE A   597
REMARK 465     LYS A   598
REMARK 465     ARG A   599
REMARK 465     ARG A   600
REMARK 465     SER A   601
REMARK 465     THR A   602
REMARK 465     GLU A   603
REMARK 465     LEU A   604
REMARK 465     ASP B   570
REMARK 465     PRO B   571
REMARK 465     GLN B   572
REMARK 465     PRO B   573
REMARK 465     THR B   574
REMARK 465     LYS B   575
REMARK 465     THR B   576
REMARK 465     ALA B   577
REMARK 465     THR B   578
REMARK 465     ILE B   579
REMARK 465     ASN B   580
REMARK 465     ALA B   581
REMARK 465     SER B   582
REMARK 465     ALA B   583
REMARK 465     SER B   584
REMARK 465     HIS B   585
REMARK 465     SER B   586
REMARK 465     ARG B   587
REMARK 465     LEU B   588
REMARK 465     ASP B   589
REMARK 465     ASP B   590
REMARK 465     ILE B   591
REMARK 465     ASN B   592
REMARK 465     PRO B   593
REMARK 465     THR B   594
REMARK 465     VAL B   595
REMARK 465     LEU B   596
REMARK 465     ILE B   597
REMARK 465     LYS B   598
REMARK 465     ARG B   599
REMARK 465     ARG B   600
REMARK 465     SER B   601
REMARK 465     THR B   602
REMARK 465     GLU B   603
REMARK 465     LEU B   604
REMARK 465     ASP C   570
REMARK 465     PRO C   571
REMARK 465     GLN C   572
REMARK 465     PRO C   573
REMARK 465     THR C   574
REMARK 465     LYS C   575
REMARK 465     THR C   576
REMARK 465     ALA C   577
REMARK 465     THR C   578
REMARK 465     ILE C   579
REMARK 465     ASN C   580
REMARK 465     ALA C   581
REMARK 465     SER C   582
REMARK 465     ALA C   583
REMARK 465     SER C   584
REMARK 465     HIS C   585
REMARK 465     SER C   586
REMARK 465     ARG C   587
REMARK 465     LEU C   588
REMARK 465     ASP C   589
REMARK 465     ASP C   590
REMARK 465     ILE C   591
REMARK 465     ASN C   592
REMARK 465     PRO C   593
REMARK 465     THR C   594
REMARK 465     VAL C   595
REMARK 465     LEU C   596
REMARK 465     ILE C   597
REMARK 465     LYS C   598
REMARK 465     ARG C   599
REMARK 465     ARG C   600
REMARK 465     SER C   601
REMARK 465     THR C   602
REMARK 465     GLU C   603
REMARK 465     LEU C   604
REMARK 465     ASP D   570
REMARK 465     PRO D   571
REMARK 465     GLN D   572
REMARK 465     PRO D   573
REMARK 465     THR D   574
REMARK 465     LYS D   575
REMARK 465     THR D   576
REMARK 465     ALA D   577
REMARK 465     THR D   578
REMARK 465     ILE D   579
REMARK 465     ASN D   580
REMARK 465     ALA D   581
REMARK 465     SER D   582
REMARK 465     ALA D   583
REMARK 465     SER D   584
REMARK 465     HIS D   585
REMARK 465     SER D   586
REMARK 465     ARG D   587
REMARK 465     LEU D   588
REMARK 465     ASP D   589
REMARK 465     ASP D   590
REMARK 465     ILE D   591
REMARK 465     ASN D   592
REMARK 465     PRO D   593
REMARK 465     THR D   594
REMARK 465     VAL D   595
REMARK 465     LEU D   596
REMARK 465     ILE D   597
REMARK 465     LYS D   598
REMARK 465     ARG D   599
REMARK 465     ARG D   600
REMARK 465     SER D   601
REMARK 465     THR D   602
REMARK 465     GLU D   603
REMARK 465     LEU D   604
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   NZ   LYS D   328     O    ASN D   546              2.13
REMARK 500   O    PHE B   128     NH2  ARG B   362              2.18
REMARK 500   ND2  ASN D    53     O5   NAG D   661              2.18
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    PRO A  20       31.08    -81.28
REMARK 500    THR A  35       50.71   -109.15
REMARK 500    THR A 115      -78.55   -128.09
REMARK 500    VAL A 151      -31.20   -130.08
REMARK 500    LYS A 155      -44.98    -29.99
REMARK 500    ARG A 171      -62.73    -92.98
REMARK 500    LEU A 210        2.89    -68.55
REMARK 500    HIS A 212       49.08     24.66
REMARK 500    ASP A 235       14.72     57.28
REMARK 500    HIS A 306       73.16   -117.38
REMARK 500    TRP A 373       52.34    -93.13
REMARK 500    GLU A 384     -109.25     32.18
REMARK 500    ASN A 425       15.01   -149.33
REMARK 500    SER A 482      -35.46     77.30
REMARK 500    ASP A 501       39.27     36.23
REMARK 500    CYS A 561       65.63     33.00
REMARK 500    SER A 565      160.95    179.02
REMARK 500    ARG B  29        0.09     82.91
REMARK 500    ARG B  46       -5.20     68.43
REMARK 500    SER B 112      116.95   -160.45
REMARK 500    THR B 115      -78.63   -135.00
REMARK 500    ARG B 171      -61.90   -101.97
REMARK 500    HIS B 212       81.32     33.81
REMARK 500    GLN B 256       19.43     87.99
REMARK 500    ASP B 333      -53.41   -120.32
REMARK 500    ASP B 348       93.35   -161.40
REMARK 500    TYR B 359       88.57    -68.55
REMARK 500    GLN B 360      159.16    178.72
REMARK 500    TRP B 373       49.62    -86.22
REMARK 500    GLU B 384     -119.06     57.29
REMARK 500    ASN B 396       79.12   -110.82
REMARK 500    ASN B 425       31.02   -143.03
REMARK 500    SER B 482      -65.32     68.44
REMARK 500    PRO C  20        0.66    -69.05
REMARK 500    ARG C  46       18.44     58.48
REMARK 500    THR C 115      -88.87   -128.55
REMARK 500    HIS C 212       58.25     31.93
REMARK 500    GLN C 270       76.34   -101.59
REMARK 500    GLU C 384     -121.65     53.49
REMARK 500    TYR C 395      -10.57     72.94
REMARK 500    SER C 482      -48.17     80.76
REMARK 500    VAL C 568       47.53    -85.82
REMARK 500    ASN D  24       53.06     71.32
REMARK 500    ARG D  29       -8.35     78.50
REMARK 500    ASP D  38       44.83   -140.71
REMARK 500    THR D  45      113.79    -35.84
REMARK 500    HIS D  80     -151.18   -133.37
REMARK 500    PHE D  81       49.02     33.03
REMARK 500    TYR D 108      -17.95    -48.42
REMARK 500    THR D 115      -83.72   -107.08
REMARK 500
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.
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                             HEM A 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374   NE2
REMARK 620 2 HEM A 605   NA   90.8
REMARK 620 3 HEM A 605   NB   86.0  91.4
REMARK 620 4 HEM A 605   NC   88.5 179.1  88.0
REMARK 620 5 HEM A 605   ND   91.3  88.4 177.4  92.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 374   NE2
REMARK 620 2 HEM D 605   NA   85.2
REMARK 620 3 HEM D 605   NB   94.6  91.5
REMARK 620 4 HEM D 605   NC   95.6 178.6  89.6
REMARK 620 5 HEM D 605   ND   83.6  87.7 178.1  91.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 374   NE2
REMARK 620 2 HEM C 605   NA   93.0
REMARK 620 3 HEM C 605   NB   93.9  90.7
REMARK 620 4 HEM C 605   NC   87.1 179.4  88.8
REMARK 620 5 HEM C 605   ND   85.2  90.2 178.7  90.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 374   NE2
REMARK 620 2 HEM B 605   NA   92.6
REMARK 620 3 HEM B 605   NB   90.3  89.2
REMARK 620 4 HEM B 605   NC   90.2 177.2  90.8
REMARK 620 5 HEM B 605   ND   88.3  92.2 178.1  87.9
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 HEM A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 416 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 416 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 416 C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 416 D 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PXX   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DICLOFENAC BOUND AT THE COX2 ACTIVE
REMARK 900 SITE
REMARK 900 RELATED ID: 3LN1   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CELECOXIB BOUND AT THE COX2 ACTIVE SITE
DBREF  3MQE A   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3MQE B   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3MQE C   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3MQE D   18   604  UNP    Q05769   PGH2_MOUSE      18    604
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 A  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 A  587  GLU LEU
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 B  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 B  587  GLU LEU
SEQRES   1 C  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 C  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 C  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 C  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 C  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 C  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 C  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 C  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 C  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 C  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 C  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 C  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 C  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 C  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 C  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 C  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 C  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 C  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 C  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 C  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 C  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 C  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 C  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 C  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 C  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 C  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 C  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 C  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 C  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 C  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 C  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 C  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 C  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 C  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 C  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 C  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 C  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 C  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 C  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 C  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 C  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 C  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 C  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 C  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 C  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 C  587  GLU LEU
SEQRES   1 D  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 D  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 D  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 D  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 D  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 D  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 D  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 D  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 D  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 D  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 D  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 D  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 D  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 D  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 D  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 D  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 D  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 D  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 D  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 D  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 D  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 D  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 D  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 D  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 D  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 D  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 D  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 D  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 D  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 D  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 D  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 D  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 D  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 D  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 D  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 D  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 D  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 D  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 D  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 D  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 D  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 D  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 D  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 D  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 D  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 D  587  GLU LEU
MODRES 3MQE ASN B  130  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN A  396  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN D  130  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN B  396  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN C   53  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN C  396  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN A  130  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN B   53  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN D  396  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN A   53  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN D   53  ASN  GLYCOSYLATION SITE
MODRES 3MQE ASN C  130  ASN  GLYCOSYLATION SITE
HET    HEM  A 605      43
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 673      14
HET    NAG  A 681      14
HET    BOG  A 704      20
HET    416  A 701      22
HET    HEM  B 605      43
HET    NAG  B 661      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 673      14
HET    NAG  B 681      14
HET    416  B 701      22
HET    HEM  C 605      43
HET    NAG  C 661      14
HET    NAG  C 671      14
HET    NAG  C 672      14
HET    NAG  C 673      14
HET    NAG  C 681      14
HET    BOG  C 703      20
HET    416  C 701      22
HET    HEM  D 605      43
HET    NAG  D 661      14
HET    NAG  D 671      14
HET    NAG  D 672      14
HET    NAG  D 673      14
HET    NAG  D 681      14
HET    416  D 701      22
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     416 (2S)-7-TERT-BUTYL-6-CHLORO-2-(TRIFLUOROMETHYL)-2H-
HETNAM   2 416  CHROMENE-3-CARBOXYLIC ACID
HETSYN     HEM HEME
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   6  NAG    20(C8 H15 N O6)
FORMUL   9  BOG    2(C14 H28 O6)
FORMUL  10  416    4(C15 H14 CL F3 O3)
FORMUL  27  HOH   *97(H2 O)
HELIX    1   1 GLU A   58  LYS A   68  1                                  11
HELIX    2   2 THR A   70  THR A   79  1                                  10
HELIX    3   3 PHE A   81  ILE A   91  1                                  11
HELIX    4   4 ILE A   91  ARG A  106  1                                  16
HELIX    5   5 SER A  107  ILE A  110  5                                   4
HELIX    6   6 SER A  124  ASN A  130  1                                   7
HELIX    7   7 ASP A  159  LEU A  168  1                                  10
HELIX    8   8 ASN A  181  HIS A  193  1                                  13
HELIX    9   9 LEU A  216  GLY A  221  1                                   6
HELIX   10  10 THR A  223  ARG A  231  1                                   9
HELIX   11  11 THR A  251  GLN A  256  1                                   6
HELIX   12  12 PRO A  266  GLN A  270  5                                   5
HELIX   13  13 VAL A  277  LEU A  280  5                                   4
HELIX   14  14 VAL A  281  HIS A  306  1                                  26
HELIX   15  15 GLY A  310  ASP A  333  1                                  24
HELIX   16  16 ASP A  333  GLY A  340  1                                   8
HELIX   17  17 ASP A  348  LEU A  352  5                                   5
HELIX   18  18 ALA A  364  TYR A  371  1                                   8
HELIX   19  19 TRP A  373  LEU A  377  5                                   5
HELIX   20  20 SER A  389  LEU A  394  1                                   6
HELIX   21  21 ASN A  397  GLN A  415  1                                  19
HELIX   22  22 PRO A  427  ALA A  429  5                                   3
HELIX   23  23 VAL A  430  MET A  444  1                                  15
HELIX   24  24 SER A  448  PHE A  456  1                                   9
HELIX   25  25 SER A  463  GLY A  469  1                                   7
HELIX   26  26 LYS A  471  SER A  482  1                                  12
HELIX   27  27 ASP A  483  MET A  487  5                                   5
HELIX   28  28 GLU A  488  LEU A  494  1                                   7
HELIX   29  29 GLY A  505  MET A  521  1                                  17
HELIX   30  30 ASN A  523  SER A  527  5                                   5
HELIX   31  31 LYS A  532  GLY A  537  5                                   6
HELIX   32  32 GLY A  538  THR A  547  1                                  10
HELIX   33  33 SER A  549  VAL A  558  1                                  10
HELIX   34  34 GLU B   58  LYS B   68  1                                  11
HELIX   35  35 THR B   70  THR B   79  1                                  10
HELIX   36  36 PHE B   81  ILE B   91  1                                  11
HELIX   37  37 ILE B   91  TYR B  108  1                                  18
HELIX   38  38 SER B  124  ASN B  130  1                                   7
HELIX   39  39 ASP B  159  LEU B  168  1                                  10
HELIX   40  40 ASN B  181  HIS B  193  1                                  13
HELIX   41  41 LEU B  216  GLY B  221  1                                   6
HELIX   42  42 THR B  223  LEU B  230  1                                   8
HELIX   43  43 THR B  251  GLN B  256  1                                   6
HELIX   44  44 PRO B  266  GLN B  270  5                                   5
HELIX   45  45 VAL B  277  LEU B  280  5                                   4
HELIX   46  46 VAL B  281  HIS B  306  1                                  26
HELIX   47  47 GLY B  310  ASP B  333  1                                  24
HELIX   48  48 ASP B  333  GLY B  340  1                                   8
HELIX   49  49 ASP B  348  PHE B  353  5                                   6
HELIX   50  50 ALA B  364  TYR B  371  1                                   8
HELIX   51  51 HIS B  372  LEU B  377  5                                   6
HELIX   52  52 SER B  389  LEU B  394  1                                   6
HELIX   53  53 ASN B  397  GLN B  415  1                                  19
HELIX   54  54 PRO B  427  ALA B  429  5                                   3
HELIX   55  55 VAL B  430  MET B  444  1                                  15
HELIX   56  56 SER B  448  PHE B  456  1                                   9
HELIX   57  57 SER B  463  GLY B  469  1                                   7
HELIX   58  58 LYS B  471  SER B  482  1                                  12
HELIX   59  59 ASP B  483  MET B  487  5                                   5
HELIX   60  60 GLU B  488  GLU B  496  1                                   9
HELIX   61  61 GLY B  505  GLY B  522  1                                  18
HELIX   62  62 ASN B  523  SER B  527  5                                   5
HELIX   63  63 LYS B  532  GLY B  537  5                                   6
HELIX   64  64 GLY B  538  ALA B  548  1                                  11
HELIX   65  65 SER B  549  VAL B  558  1                                  10
HELIX   66  66 GLU C   58  LYS C   68  1                                  11
HELIX   67  67 THR C   70  THR C   79  1                                  10
HELIX   68  68 PHE C   81  ASN C   89  1                                   9
HELIX   69  69 ILE C   91  TYR C  108  1                                  18
HELIX   70  70 SER C  124  ASN C  130  1                                   7
HELIX   71  71 ASP C  159  LEU C  168  1                                  10
HELIX   72  72 ASN C  181  HIS C  193  1                                  13
HELIX   73  73 LEU C  216  GLY C  221  1                                   6
HELIX   74  74 THR C  223  LEU C  230  1                                   8
HELIX   75  75 THR C  251  GLN C  256  1                                   6
HELIX   76  76 PRO C  266  GLN C  270  5                                   5
HELIX   77  77 VAL C  281  HIS C  306  1                                  26
HELIX   78  78 GLY C  310  ASP C  333  1                                  24
HELIX   79  79 ASP C  333  GLY C  340  1                                   8
HELIX   80  80 ASP C  348  PHE C  353  5                                   6
HELIX   81  81 ALA C  364  TYR C  371  1                                   8
HELIX   82  82 TRP C  373  LEU C  377  5                                   5
HELIX   83  83 SER C  389  LEU C  394  1                                   6
HELIX   84  84 ASN C  397  GLN C  415  1                                  19
HELIX   85  85 PRO C  427  ALA C  429  5                                   3
HELIX   86  86 VAL C  430  MET C  444  1                                  15
HELIX   87  87 SER C  448  PHE C  456  1                                   9
HELIX   88  88 SER C  463  GLY C  469  1                                   7
HELIX   89  89 LYS C  471  SER C  482  1                                  12
HELIX   90  90 ASP C  483  MET C  487  5                                   5
HELIX   91  91 GLU C  488  GLU C  496  1                                   9
HELIX   92  92 GLY C  505  MET C  521  1                                  17
HELIX   93  93 ASN C  523  SER C  527  5                                   5
HELIX   94  94 LYS C  532  PHE C  536  5                                   5
HELIX   95  95 GLY C  538  THR C  547  1                                  10
HELIX   96  96 SER C  549  ASN C  556  1                                   8
HELIX   97  97 GLU D   58  LYS D   68  1                                  11
HELIX   98  98 THR D   70  THR D   79  1                                  10
HELIX   99  99 PHE D   81  ASN D   90  1                                  10
HELIX  100 100 ILE D   91  ARG D  106  1                                  16
HELIX  101 101 SER D  107  ILE D  110  5                                   4
HELIX  102 102 SER D  124  ASN D  130  1                                   7
HELIX  103 103 ASP D  159  LEU D  168  1                                  10
HELIX  104 104 ASN D  181  HIS D  193  1                                  13
HELIX  105 105 LEU D  216  GLY D  221  1                                   6
HELIX  106 106 THR D  223  ARG D  231  1                                   9
HELIX  107 107 THR D  251  GLN D  256  1                                   6
HELIX  108 108 PRO D  266  GLN D  270  5                                   5
HELIX  109 109 VAL D  277  LEU D  280  5                                   4
HELIX  110 110 VAL D  281  HIS D  306  1                                  26
HELIX  111 111 GLY D  310  ASP D  333  1                                  24
HELIX  112 112 ASP D  333  GLY D  340  1                                   8
HELIX  113 113 ASP D  348  PHE D  353  5                                   6
HELIX  114 114 ALA D  364  TYR D  371  1                                   8
HELIX  115 115 HIS D  372  LEU D  377  5                                   6
HELIX  116 116 SER D  389  LEU D  394  1                                   6
HELIX  117 117 ASN D  397  GLN D  415  1                                  19
HELIX  118 118 PRO D  427  ALA D  429  5                                   3
HELIX  119 119 VAL D  430  MET D  444  1                                  15
HELIX  120 120 SER D  448  PHE D  456  1                                   9
HELIX  121 121 SER D  463  GLY D  469  1                                   7
HELIX  122 122 LYS D  471  SER D  482  1                                  12
HELIX  123 123 ASP D  483  MET D  487  5                                   5
HELIX  124 124 GLU D  488  GLU D  496  1                                   9
HELIX  125 125 GLY D  505  GLY D  522  1                                  18
HELIX  126 126 ASN D  523  SER D  527  5                                   5
HELIX  127 127 LYS D  532  GLY D  537  5                                   6
HELIX  128 128 GLY D  538  THR D  547  1                                  10
HELIX  129 129 SER D  549  VAL D  558  1                                  10
SHEET    1   A 2 GLU A  31  SER A  34  0
SHEET    2   A 2 TYR A  40  ASP A  43 -1  O  ASP A  43   N  GLU A  31
SHEET    1   B 2 PHE A  49  TYR A  50  0
SHEET    2   B 2 THR A  56  PRO A  57 -1  O  THR A  56   N  TYR A  50
SHEET    1   C 2 GLN A 241  ILE A 243  0
SHEET    2   C 2 GLU A 246  TYR A 248 -1  O  TYR A 248   N  GLN A 241
SHEET    1   D 2 PHE A 381  ILE A 383  0
SHEET    2   D 2 GLN A 386  TYR A 388 -1  O  GLN A 386   N  ILE A 383
SHEET    1   E 2 GLU B  31  GLY B  36  0
SHEET    2   E 2 GLN B  39  ASP B  43 -1  O  ASP B  43   N  GLU B  31
SHEET    1   F 2 PHE B  49  TYR B  50  0
SHEET    2   F 2 THR B  56  PRO B  57 -1  O  THR B  56   N  TYR B  50
SHEET    1   G 2 GLN B 241  ILE B 243  0
SHEET    2   G 2 GLU B 246  TYR B 248 -1  O  TYR B 248   N  GLN B 241
SHEET    1   H 2 GLU C  31  SER C  34  0
SHEET    2   H 2 TYR C  40  ASP C  43 -1  O  LYS C  41   N  MET C  33
SHEET    1   I 2 PHE C  49  TYR C  50  0
SHEET    2   I 2 THR C  56  PRO C  57 -1  O  THR C  56   N  TYR C  50
SHEET    1   J 2 GLN C 241  VAL C 242  0
SHEET    2   J 2 VAL C 247  TYR C 248 -1  O  TYR C 248   N  GLN C 241
SHEET    1   K 2 PHE C 381  ILE C 383  0
SHEET    2   K 2 GLN C 386  TYR C 388 -1  O  TYR C 388   N  PHE C 381
SHEET    1   L 2 GLU D  31  SER D  34  0
SHEET    2   L 2 TYR D  40  ASP D  43 -1  O  ASP D  43   N  GLU D  31
SHEET    1   M 2 PHE D  49  TYR D  50  0
SHEET    2   M 2 THR D  56  PRO D  57 -1  O  THR D  56   N  TYR D  50
SHEET    1   N 2 TYR D 116  ASN D 117  0
SHEET    2   N 2 THR D 135  ARG D 136 -1  O  ARG D 136   N  TYR D 116
SHEET    1   O 2 GLN D 241  VAL D 242  0
SHEET    2   O 2 VAL D 247  TYR D 248 -1  O  TYR D 248   N  GLN D 241
SHEET    1   P 2 PHE D 381  ILE D 383  0
SHEET    2   P 2 GLN D 386  TYR D 388 -1  O  TYR D 388   N  PHE D 381
SSBOND   1 CYS A   21    CYS A   32                          1555   1555  2.03
SSBOND   2 CYS A   22    CYS A  145                          1555   1555  2.03
SSBOND   3 CYS A   26    CYS A   42                          1555   1555  2.04
SSBOND   4 CYS A   44    CYS A   54                          1555   1555  2.04
SSBOND   5 CYS A  555    CYS A  561                          1555   1555  2.03
SSBOND   6 CYS B   21    CYS B   32                          1555   1555  2.04
SSBOND   7 CYS B   22    CYS B  145                          1555   1555  2.05
SSBOND   8 CYS B   26    CYS B   42                          1555   1555  2.09
SSBOND   9 CYS B   44    CYS B   54                          1555   1555  2.06
SSBOND  10 CYS B  555    CYS B  561                          1555   1555  2.03
SSBOND  11 CYS C   21    CYS C   32                          1555   1555  2.05
SSBOND  12 CYS C   22    CYS C  145                          1555   1555  2.03
SSBOND  13 CYS C   26    CYS C   42                          1555   1555  2.03
SSBOND  14 CYS C   44    CYS C   54                          1555   1555  2.04
SSBOND  15 CYS C  555    CYS C  561                          1555   1555  2.05
SSBOND  16 CYS D   21    CYS D   32                          1555   1555  2.04
SSBOND  17 CYS D   22    CYS D  145                          1555   1555  2.04
SSBOND  18 CYS D   26    CYS D   42                          1555   1555  2.04
SSBOND  19 CYS D   44    CYS D   54                          1555   1555  2.04
SSBOND  20 CYS D  555    CYS D  561                          1555   1555  2.04
LINK         ND2 ASN B 130                 C1  NAG B 671     1555   1555  1.43
LINK         ND2 ASN A 396                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN D 130                 C1  NAG D 671     1555   1555  1.44
LINK         ND2 ASN B 396                 C1  NAG B 681     1555   1555  1.44
LINK         ND2 ASN C  53                 C1  NAG C 661     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         O4  NAG C 671                 C1  NAG C 672     1555   1555  1.45
LINK         O4  NAG A 672                 C1  NAG A 673     1555   1555  1.45
LINK         ND2 ASN C 396                 C1  NAG C 681     1555   1555  1.45
LINK         ND2 ASN A 130                 C1  NAG A 671     1555   1555  1.45
LINK         O4  NAG D 671                 C1  NAG D 672     1555   1555  1.45
LINK         ND2 ASN B  53                 C1  NAG B 661     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         ND2 ASN D 396                 C1  NAG D 681     1555   1555  1.45
LINK         ND2 ASN A  53                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN D  53                 C1  NAG D 661     1555   1555  1.46
LINK         O4  NAG D 672                 C1  NAG D 673     1555   1555  1.46
LINK         O4  NAG C 672                 C1  NAG C 673     1555   1555  1.46
LINK         O4  NAG B 672                 C1  NAG B 673     1555   1555  1.46
LINK         ND2 ASN C 130                 C1  NAG C 671     1555   1555  1.47
LINK         NE2 HIS A 374                FE   HEM A 605     1555   1555  2.21
LINK         NE2 HIS D 374                FE   HEM D 605     1555   1555  2.39
LINK         NE2 HIS C 374                FE   HEM C 605     1555   1555  2.49
LINK         NE2 HIS B 374                FE   HEM B 605     1555   1555  2.56
CISPEP   1 SER A  112    PRO A  113          0         6.55
CISPEP   2 SER B  112    PRO B  113          0         2.69
CISPEP   3 SER C  112    PRO C  113          0        -0.60
CISPEP   4 SER D  112    PRO D  113          0        10.21
SITE     1 AC1 12 GLN A 189  HIS A 193  PHE A 196  LYS A 197
SITE     2 AC1 12 THR A 198  ASN A 368  TYR A 371  HIS A 372
SITE     3 AC1 12 HIS A 374  LEU A 377  VAL A 433  HOH A 610
SITE     1 AC2  4 SER A  23  TYR A  40  GLU A  52  ASN A  53
SITE     1 AC3  6 GLU A 126  ASN A 130  TYR A 133  ARG A 202
SITE     2 AC3  6 NAG A 672  LEU B 224
SITE     1 AC4  3 ARG A 202  NAG A 671  NAG A 673
SITE     1 AC5  1 NAG A 672
SITE     1 AC6  3 ASN A 396  ILE A 399  HOH A 629
SITE     1 AC7  9 GLU A 165  ARG A 171  ARG A 424  GLU A 472
SITE     2 AC7  9 GLU A 476  GLU B 165  ARG B 170  ILE B 428
SITE     3 AC7  9 GLN B 431
SITE     1 AC8  9 ARG A 106  TYR A 334  VAL A 335  TYR A 341
SITE     2 AC8  9 TYR A 371  VAL A 509  GLY A 512  ALA A 513
SITE     3 AC8  9 SER A 516
SITE     1 AC9 11 ALA B 188  GLN B 189  HIS B 193  THR B 198
SITE     2 AC9 11 ASN B 368  TYR B 371  HIS B 372  HIS B 374
SITE     3 AC9 11 LEU B 377  VAL B 433  ALA B 436
SITE     1 BC1  3 TYR B  40  GLU B  52  ASN B  53
SITE     1 BC2  5 LEU A 224  ASN B 130  TYR B 133  ARG B 202
SITE     2 BC2  5 NAG B 672
SITE     1 BC3  3 ARG B 202  NAG B 671  NAG B 673
SITE     1 BC4  1 NAG B 672
SITE     1 BC5  2 GLN B 392  ASN B 396
SITE     1 BC6  7 ARG B 106  VAL B 335  TYR B 341  TYR B 371
SITE     2 BC6  7 GLY B 512  ALA B 513  SER B 516
SITE     1 BC7  9 GLN C 189  HIS C 193  PHE C 196  THR C 198
SITE     2 BC7  9 HIS C 200  ASN C 368  TYR C 371  HIS C 372
SITE     3 BC7  9 HIS C 374
SITE     1 BC8  4 PRO C  25  TYR C  40  GLU C  52  ASN C  53
SITE     1 BC9  5 GLU C 126  ASN C 130  TYR C 133  ARG C 202
SITE     2 BC9  5 NAG C 672
SITE     1 CC1  3 ARG C 202  NAG C 671  NAG C 673
SITE     1 CC2  1 NAG C 672
SITE     1 CC3  2 HOH C   9  ASN C 396
SITE     1 CC4 10 GLU C 165  LYS C 166  ARG C 170  ARG C 171
SITE     2 CC4 10 ARG C 424  GLU C 472  GLU C 476  LYS D 161
SITE     3 CC4 10 GLU D 165  ARG D 170
SITE     1 CC5  9 ARG C 106  VAL C 335  TYR C 341  TYR C 371
SITE     2 CC5  9 TRP C 373  VAL C 509  GLY C 512  ALA C 513
SITE     3 CC5  9 SER C 516
SITE     1 CC6 12 ALA D 185  GLN D 189  HIS D 193  PHE D 196
SITE     2 CC6 12 LYS D 197  THR D 198  HIS D 200  VAL D 281
SITE     3 CC6 12 ASN D 368  HIS D 372  HIS D 374  LEU D 377
SITE     1 CC7  3 TYR D  40  GLU D  52  ASN D  53
SITE     1 CC8  6 LEU C 224  GLU D 126  ASN D 130  TYR D 133
SITE     2 CC8  6 ARG D 202  NAG D 672
SITE     1 CC9  4 HOH D  15  ARG D 202  NAG D 671  NAG D 673
SITE     1 DC1  3 HOH D  15  HOH D 609  NAG D 672
SITE     1 DC2  3 GLN D 392  ASN D 396  GLU D 402
SITE     1 DC3  9 VAL D 335  LEU D 338  TYR D 341  TYR D 371
SITE     2 DC3  9 TRP D 373  VAL D 509  GLY D 512  ALA D 513
SITE     3 DC3  9 SER D 516
CRYST1  183.701  140.378  129.737  90.00  90.00  90.00 P 21 21 2    16
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      0.005444  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007124  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007708        0.00000
      
PROCHECK
Go to PROCHECK summary
 References