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PDBsum entry 3ntg

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3ntg
Jmol
Contents
Protein chains
552 a.a.
Ligands
HEM ×4
NAG-NAG ×4
NAG ×4
BOG ×2
D72 ×4
Waters ×1077
HEADER    OXIDOREDUCTASE                          04-JUL-10   3NTG
TITLE     CRYSTAL STRUCTURE OF COX-2 WITH SELECTIVE COMPOUND 23D-(R)
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, GLUCOCORTICOID-REGULATED
COMPND   6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND   7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND   8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND   9 SYNTHASE 2, TIS10 PROTEIN;
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, MCG_5001, 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.C.CARTER,J.J.TALLEY,J.R.KIEFER
REVDAT   3   23-MAR-11 3NTG    1       COMPND DBREF  SOURCE
REVDAT   2   01-DEC-10 3NTG    1       JRNL
REVDAT   1   27-OCT-10 3NTG    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.    2.19 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 2.19
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2
REMARK   3   NUMBER OF REFLECTIONS             : 120646
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) : 0.211
REMARK   3   R VALUE            (WORKING SET) : 0.206
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 13440
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) : 2.19
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8199
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.51
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690
REMARK   3   BIN FREE R VALUE SET COUNT          : 888
REMARK   3   BIN FREE R VALUE                    : 0.3230
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17900
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 476
REMARK   3   SOLVENT ATOMS            : 1077
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.61
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.63000
REMARK   3    B22 (A**2) : 0.06000
REMARK   3    B33 (A**2) : 1.57000
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): 0.330
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.243
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.270
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18966 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A): 12911 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25818 ; 1.232 ; 2.003
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 31375 ; 0.870 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2208 ; 5.590 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   897 ;38.275 ;24.114
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3107 ;16.750 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;17.099 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2713 ; 0.070 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20864 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  3852 ; 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): 11048 ; 0.371 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4420 ; 0.077 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17959 ; 0.709 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7918 ; 1.202 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7859 ; 1.979 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 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   569
REMARK   3    ORIGIN FOR THE GROUP (A):  28.7730  28.8900   9.2420
REMARK   3    T TENSOR
REMARK   3      T11:   0.0050 T22:   0.0096
REMARK   3      T33:   0.0206 T12:   0.0004
REMARK   3      T13:   0.0028 T23:   0.0035
REMARK   3    L TENSOR
REMARK   3      L11:   1.0221 L22:   0.8460
REMARK   3      L33:   0.9009 L12:   0.0677
REMARK   3      L13:  -0.0248 L23:   0.5016
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0187 S12:  -0.0584 S13:  -0.0780
REMARK   3      S21:   0.0025 S22:  -0.0279 S23:   0.1016
REMARK   3      S31:   0.0189 S32:  -0.0696 S33:   0.0466
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   569
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2030  22.0290   2.1100
REMARK   3    T TENSOR
REMARK   3      T11:   0.0140 T22:   0.0329
REMARK   3      T33:   0.0115 T12:   0.0018
REMARK   3      T13:  -0.0002 T23:   0.0079
REMARK   3    L TENSOR
REMARK   3      L11:   1.0829 L22:   0.7138
REMARK   3      L33:   0.9328 L12:   0.0608
REMARK   3      L13:   0.1457 L23:   0.4267
REMARK   3    S TENSOR
REMARK   3      S11:   0.0099 S12:  -0.0483 S13:  -0.0186
REMARK   3      S21:   0.0421 S22:   0.0104 S23:  -0.0742
REMARK   3      S31:  -0.0004 S32:   0.1337 S33:  -0.0203
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   569
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5260  45.4940  63.5120
REMARK   3    T TENSOR
REMARK   3      T11:   0.0364 T22:   0.0820
REMARK   3      T33:   0.0265 T12:   0.0318
REMARK   3      T13:  -0.0038 T23:  -0.0210
REMARK   3    L TENSOR
REMARK   3      L11:   1.0855 L22:   0.7424
REMARK   3      L33:   1.1008 L12:  -0.0440
REMARK   3      L13:  -0.0659 L23:  -0.4917
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0179 S12:  -0.0926 S13:   0.0566
REMARK   3      S21:   0.0755 S22:   0.0523 S23:   0.0986
REMARK   3      S31:  -0.0698 S32:  -0.2180 S33:  -0.0344
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   569
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8480  37.9770  70.2690
REMARK   3    T TENSOR
REMARK   3      T11:   0.0179 T22:   0.0323
REMARK   3      T33:   0.0328 T12:  -0.0016
REMARK   3      T13:  -0.0107 T23:   0.0000
REMARK   3    L TENSOR
REMARK   3      L11:   1.1640 L22:   0.8529
REMARK   3      L33:   1.1535 L12:  -0.0073
REMARK   3      L13:   0.1290 L23:  -0.5574
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0327 S12:  -0.0137 S13:   0.1118
REMARK   3      S21:   0.0135 S22:  -0.0538 S23:  -0.1263
REMARK   3      S31:  -0.0439 S32:   0.1011 S33:   0.0865
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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3NTG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-02
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                  : CRYSTAL
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   : 134127
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10800
REMARK 200   FOR THE DATA SET  : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.51100
REMARK 200   FOR SHELL         : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
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       90.13400
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.13650
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.13400
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.13650
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 300 REMARK: DIMER OF DIMERS
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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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: 10800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG C 362   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG D 455   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A  45      121.02    -38.96
REMARK 500    THR A 115      -88.44   -125.53
REMARK 500    TRP A 373       44.31    -97.57
REMARK 500    GLU A 384     -125.06     54.33
REMARK 500    SER A 482      -61.45     69.47
REMARK 500    ASP B  38       30.45   -141.33
REMARK 500    THR B 115      -90.06   -120.40
REMARK 500    ARG B 171      -65.30    -96.70
REMARK 500    ASP B 333      -52.33   -120.01
REMARK 500    HIS B 372       79.39    -69.94
REMARK 500    TRP B 373       47.29    -99.23
REMARK 500    GLU B 384     -130.15     57.97
REMARK 500    ASN B 425       22.46   -143.04
REMARK 500    SER B 482      -49.47     65.12
REMARK 500    ASP B 501       29.43     49.76
REMARK 500    CYS B 561       66.32     38.35
REMARK 500    THR C 115      -92.23   -115.96
REMARK 500    ARG C 171      -76.48    -93.20
REMARK 500    LYS C 197       69.05   -150.02
REMARK 500    TRP C 373       46.22    -96.21
REMARK 500    GLU C 384     -125.42     60.58
REMARK 500    TYR C 395       11.73     58.81
REMARK 500    ASN C 396       74.85   -117.36
REMARK 500    ASN C 425       16.61   -144.87
REMARK 500    SER C 482      -50.33     65.66
REMARK 500    THR D 115      -87.43   -126.23
REMARK 500    ASP D 333      -50.29   -123.05
REMARK 500    TRP D 373       48.73    -94.58
REMARK 500    GLU D 384     -119.66     58.05
REMARK 500    ASN D 425       18.95   -140.16
REMARK 500    SER D 482      -59.91     77.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C4349        DISTANCE =  6.62 ANGSTROMS
REMARK 525    HOH B4422        DISTANCE =  5.90 ANGSTROMS
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 B 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 374   NE2
REMARK 620 2 HEM B 601   NA   91.0
REMARK 620 3 HEM B 601   NB   91.6  90.9
REMARK 620 4 HEM B 601   NC   91.2 177.7  88.1
REMARK 620 5 HEM B 601   ND   89.4  89.2 179.0  91.7
REMARK 620 6 HOH B5274   O   170.7  80.6  84.8  97.2  94.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374   NE2
REMARK 620 2 HEM A 601   NA   93.3
REMARK 620 3 HEM A 601   NB   96.0  88.9
REMARK 620 4 HEM A 601   NC   89.8 176.9  91.0
REMARK 620 5 HEM A 601   ND   84.8  89.6 178.3  90.6
REMARK 620 6 HOH A4121   O   172.0  81.2  89.8  95.6  89.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 374   NE2
REMARK 620 2 HEM D 601   NA   89.6
REMARK 620 3 HEM D 601   NB   92.8  87.0
REMARK 620 4 HEM D 601   NC   92.5 177.4  91.4
REMARK 620 5 HEM D 601   ND   87.1  92.1 179.1  89.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 374   NE2
REMARK 620 2 HEM C 601   NA   87.6
REMARK 620 3 HEM C 601   NB   91.7  90.3
REMARK 620 4 HEM C 601   NC   94.9 177.5  89.4
REMARK 620 5 HEM C 601   ND   89.1  89.2 179.0  91.1
REMARK 620 6 HOH C4116   O   169.2  81.7  90.1  95.7  89.0
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 D 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PXX   RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH DICLOFENAC
REMARK 900 RELATED ID: 3LN1   RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH CELECOXIB
REMARK 900 RELATED ID: 3MQE   RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH SC-75416
REMARK 900 RELATED ID: 3LN0   RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH COMPOUND 5C-(S)
REMARK 900 RELATED ID: 3PGH   RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH FLURBIPROFEN
DBREF  3NTG A   18   569  UNP    Q05769   PGH2_MOUSE      18    569
DBREF  3NTG B   18   569  UNP    Q05769   PGH2_MOUSE      18    569
DBREF  3NTG C   18   569  UNP    Q05769   PGH2_MOUSE      18    569
DBREF  3NTG D   18   569  UNP    Q05769   PGH2_MOUSE      18    569
SEQRES   1 A  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 A  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 A  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 A  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 A  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 A  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 A  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 A  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 A  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 A  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 A  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 A  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 A  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 A  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 A  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 A  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 A  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 A  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 A  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 A  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 A  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 A  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 A  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 A  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 A  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 A  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 A  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 A  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 A  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 A  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 A  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 A  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 A  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 A  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 A  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 A  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 A  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 A  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 A  552  THR SER PHE ASN VAL GLN
SEQRES   1 B  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 B  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 B  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 B  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 B  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 B  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 B  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 B  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 B  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 B  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 B  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 B  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 B  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 B  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 B  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 B  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 B  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 B  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 B  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 B  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 B  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 B  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 B  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 B  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 B  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 B  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 B  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 B  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 B  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 B  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 B  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 B  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 B  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 B  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 B  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 B  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 B  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 B  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 B  552  THR SER PHE ASN VAL GLN
SEQRES   1 C  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 C  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 C  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 C  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 C  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 C  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 C  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 C  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 C  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 C  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 C  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 C  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 C  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 C  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 C  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 C  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 C  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 C  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 C  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 C  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 C  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 C  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 C  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 C  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 C  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 C  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 C  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 C  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 C  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 C  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 C  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 C  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 C  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 C  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 C  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 C  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 C  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 C  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 C  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 C  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 C  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 C  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 C  552  THR SER PHE ASN VAL GLN
SEQRES   1 D  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 D  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 D  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 D  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 D  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 D  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 D  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 D  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 D  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 D  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 D  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 D  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 D  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 D  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 D  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 D  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 D  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 D  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 D  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 D  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 D  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 D  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 D  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 D  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 D  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 D  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 D  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 D  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 D  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 D  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 D  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 D  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 D  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 D  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 D  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 D  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 D  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 D  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 D  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 D  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 D  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 D  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 D  552  THR SER PHE ASN VAL GLN
MODRES 3NTG ASN B  130  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN C  396  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN A  396  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN B  396  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN A  130  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN D  130  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN C  130  ASN  GLYCOSYLATION SITE
MODRES 3NTG ASN D  396  ASN  GLYCOSYLATION SITE
HET    HEM  A 601      43
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 681      14
HET    BOG  A 703      20
HET    D72  A 701      24
HET    HEM  B 601      43
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 681      14
HET    D72  B 701      24
HET    HEM  C 601      43
HET    NAG  C 671      14
HET    NAG  C 672      14
HET    NAG  C 681      14
HET    D72  C 701      24
HET    HEM  D 601      43
HET    NAG  D 671      14
HET    NAG  D 672      14
HET    NAG  D 681      14
HET    BOG  D 703      20
HET    D72  D 701      24
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     D72 (2R)-6,8-DICHLORO-7-(2-METHYLPROPOXY)-2-
HETNAM   2 D72  (TRIFLUOROMETHYL)-2H-CHROMENE-3-CARBOXYLIC ACID
HETSYN     HEM HEME
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   6  NAG    12(C8 H15 N O6)
FORMUL   8  BOG    2(C14 H28 O6)
FORMUL   9  D72    4(C15 H13 CL2 F3 O4)
FORMUL  23  HOH   *1077(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  ASN A   90  1                                  10
HELIX    4   4 ILE A   91  TYR A  108  1                                  18
HELIX    5   5 SER A  124  ASN A  130  1                                   7
HELIX    6   6 ASP A  159  LEU A  168  1                                  10
HELIX    7   7 ASN A  181  HIS A  193  1                                  13
HELIX    8   8 LEU A  216  GLY A  221  1                                   6
HELIX    9   9 THR A  223  ARG A  231  1                                   9
HELIX   10  10 THR A  251  GLN A  256  1                                   6
HELIX   11  11 PRO A  266  GLN A  270  5                                   5
HELIX   12  12 VAL A  277  LEU A  280  5                                   4
HELIX   13  13 VAL A  281  HIS A  306  1                                  26
HELIX   14  14 GLY A  310  ASP A  333  1                                  24
HELIX   15  15 ASP A  333  GLY A  340  1                                   8
HELIX   16  16 ASP A  348  PHE A  353  5                                   6
HELIX   17  17 ALA A  364  TYR A  371  1                                   8
HELIX   18  18 TRP A  373  LEU A  377  5                                   5
HELIX   19  19 SER A  389  LEU A  394  1                                   6
HELIX   20  20 ASN A  397  GLY A  404  1                                   8
HELIX   21  21 GLY A  404  GLN A  415  1                                  12
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  GLU A  496  1                                   9
HELIX   29  29 GLY A  505  GLY A  522  1                                  18
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  LEU B   67  1                                  10
HELIX   35  35 THR B   70  HIS B   80  1                                  11
HELIX   36  36 PHE B   81  ASN B   90  1                                  10
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  ARG B  231  1                                   9
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  THR B  547  1                                  10
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   90  1                                  10
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  ARG C  231  1                                   9
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  277  LEU C  280  5                                   4
HELIX   78  78 VAL C  281  HIS C  306  1                                  26
HELIX   79  79 GLY C  310  ASP C  333  1                                  24
HELIX   80  80 ASP C  333  GLY C  340  1                                   8
HELIX   81  81 ASP C  348  PHE C  353  5                                   6
HELIX   82  82 ALA C  364  TYR C  371  1                                   8
HELIX   83  83 HIS C  372  LEU C  377  5                                   6
HELIX   84  84 SER C  389  LEU C  394  1                                   6
HELIX   85  85 ASN C  397  GLN C  415  1                                  19
HELIX   86  86 PRO C  427  ALA C  429  5                                   3
HELIX   87  87 VAL C  430  MET C  444  1                                  15
HELIX   88  88 SER C  448  PHE C  456  1                                   9
HELIX   89  89 SER C  463  GLY C  469  1                                   7
HELIX   90  90 LYS C  471  SER C  482  1                                  12
HELIX   91  91 ASP C  483  MET C  487  5                                   5
HELIX   92  92 GLU C  488  GLU C  496  1                                   9
HELIX   93  93 GLY C  505  GLY C  522  1                                  18
HELIX   94  94 ASN C  523  SER C  527  5                                   5
HELIX   95  95 LYS C  532  GLY C  537  5                                   6
HELIX   96  96 GLY C  538  THR C  547  1                                  10
HELIX   97  97 SER C  549  VAL C  558  1                                  10
HELIX   98  98 ASN D   19  ASN D   24  5                                   6
HELIX   99  99 GLU D   58  LYS D   68  1                                  11
HELIX  100 100 THR D   70  THR D   79  1                                  10
HELIX  101 101 PHE D   81  ASN D   90  1                                  10
HELIX  102 102 ILE D   91  TYR D  108  1                                  18
HELIX  103 103 SER D  124  ASN D  130  1                                   7
HELIX  104 104 ASP D  159  LEU D  168  1                                  10
HELIX  105 105 ASN D  181  HIS D  193  1                                  13
HELIX  106 106 LEU D  216  GLY D  221  1                                   6
HELIX  107 107 THR D  223  ARG D  231  1                                   9
HELIX  108 108 THR D  251  GLN D  256  1                                   6
HELIX  109 109 VAL D  281  HIS D  306  1                                  26
HELIX  110 110 GLY D  310  ASP D  333  1                                  24
HELIX  111 111 ASP D  333  GLY D  340  1                                   8
HELIX  112 112 ASP D  348  PHE D  353  5                                   6
HELIX  113 113 ALA D  364  TYR D  371  1                                   8
HELIX  114 114 HIS D  372  LEU D  377  5                                   6
HELIX  115 115 SER D  389  LEU D  394  1                                   6
HELIX  116 116 ASN D  396  GLY D  404  1                                   9
HELIX  117 117 GLY D  404  GLN D  415  1                                  12
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 TYR A 116  ASN A 117  0
SHEET    2   C 2 THR A 135  ARG A 136 -1  O  ARG A 136   N  TYR A 116
SHEET    1   D 2 GLN A 241  ILE A 243  0
SHEET    2   D 2 GLU A 246  TYR A 248 -1  O  TYR A 248   N  GLN A 241
SHEET    1   E 2 PHE A 381  ILE A 383  0
SHEET    2   E 2 GLN A 386  TYR A 388 -1  O  TYR A 388   N  PHE A 381
SHEET    1   F 2 GLU B  31  GLY B  36  0
SHEET    2   F 2 GLN B  39  ASP B  43 -1  O  ASP B  43   N  GLU B  31
SHEET    1   G 2 PHE B  49  TYR B  50  0
SHEET    2   G 2 THR B  56  PRO B  57 -1  O  THR B  56   N  TYR B  50
SHEET    1   H 2 TYR B 116  ASN B 117  0
SHEET    2   H 2 THR B 135  ARG B 136 -1  O  ARG B 136   N  TYR B 116
SHEET    1   I 2 GLN B 241  ILE B 243  0
SHEET    2   I 2 GLU B 246  TYR B 248 -1  O  TYR B 248   N  GLN B 241
SHEET    1   J 2 PHE B 381  ILE B 383  0
SHEET    2   J 2 GLN B 386  TYR B 388 -1  O  TYR B 388   N  PHE B 381
SHEET    1   K 2 GLU C  31  GLY C  36  0
SHEET    2   K 2 GLN C  39  ASP C  43 -1  O  LYS C  41   N  MET C  33
SHEET    1   L 2 PHE C  49  TYR C  50  0
SHEET    2   L 2 THR C  56  PRO C  57 -1  O  THR C  56   N  TYR C  50
SHEET    1   M 2 GLN C 241  ILE C 243  0
SHEET    2   M 2 GLU C 246  TYR C 248 -1  O  TYR C 248   N  GLN C 241
SHEET    1   N 2 PHE C 381  ILE C 383  0
SHEET    2   N 2 GLN C 386  TYR C 388 -1  O  TYR C 388   N  PHE C 381
SHEET    1   O 2 GLU D  31  SER D  34  0
SHEET    2   O 2 TYR D  40  ASP D  43 -1  O  ASP D  43   N  GLU D  31
SHEET    1   P 2 PHE D  49  TYR D  50  0
SHEET    2   P 2 THR D  56  PRO D  57 -1  O  THR D  56   N  TYR D  50
SHEET    1   Q 2 TYR D 116  ASN D 117  0
SHEET    2   Q 2 THR D 135  ARG D 136 -1  O  ARG D 136   N  TYR D 116
SHEET    1   R 2 GLN D 241  ILE D 243  0
SHEET    2   R 2 GLU D 246  TYR D 248 -1  O  TYR D 248   N  GLN D 241
SHEET    1   S 2 PHE D 381  ILE D 383  0
SHEET    2   S 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  2.06
SSBOND   2 CYS A   22    CYS A  145                          1555   1555  2.05
SSBOND   3 CYS A   26    CYS A   42                          1555   1555  2.05
SSBOND   4 CYS A   44    CYS A   54                          1555   1555  2.06
SSBOND   5 CYS A  555    CYS A  561                          1555   1555  2.06
SSBOND   6 CYS B   21    CYS B   32                          1555   1555  2.06
SSBOND   7 CYS B   22    CYS B  145                          1555   1555  2.05
SSBOND   8 CYS B   26    CYS B   42                          1555   1555  2.03
SSBOND   9 CYS B   44    CYS B   54                          1555   1555  2.05
SSBOND  10 CYS B  555    CYS B  561                          1555   1555  2.04
SSBOND  11 CYS C   21    CYS C   32                          1555   1555  2.06
SSBOND  12 CYS C   22    CYS C  145                          1555   1555  2.05
SSBOND  13 CYS C   26    CYS C   42                          1555   1555  2.03
SSBOND  14 CYS C   44    CYS C   54                          1555   1555  2.05
SSBOND  15 CYS C  555    CYS C  561                          1555   1555  2.05
SSBOND  16 CYS D   21    CYS D   32                          1555   1555  2.05
SSBOND  17 CYS D   22    CYS D  145                          1555   1555  2.03
SSBOND  18 CYS D   26    CYS D   42                          1555   1555  2.04
SSBOND  19 CYS D   44    CYS D   54                          1555   1555  2.05
SSBOND  20 CYS D  555    CYS D  561                          1555   1555  2.06
LINK         ND2 ASN B 130                 C1  NAG B 671     1555   1555  1.43
LINK         ND2 ASN C 396                 C1  NAG C 681     1555   1555  1.44
LINK         ND2 ASN A 396                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 396                 C1  NAG B 681     1555   1555  1.44
LINK         ND2 ASN A 130                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN D 130                 C1  NAG D 671     1555   1555  1.44
LINK         ND2 ASN C 130                 C1  NAG C 671     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44
LINK         O4  NAG D 671                 C1  NAG D 672     1555   1555  1.44
LINK         O4  NAG C 671                 C1  NAG C 672     1555   1555  1.44
LINK         ND2 ASN D 396                 C1  NAG D 681     1555   1555  1.45
LINK         NE2 HIS B 374                FE   HEM B 601     1555   1555  2.09
LINK         NE2 HIS A 374                FE   HEM A 601     1555   1555  2.16
LINK         NE2 HIS D 374                FE   HEM D 601     1555   1555  2.22
LINK         NE2 HIS C 374                FE   HEM C 601     1555   1555  2.34
LINK        FE   HEM A 601                 O   HOH A4121     1555   1555  2.39
LINK        FE   HEM C 601                 O   HOH C4116     1555   1555  2.45
LINK        FE   HEM B 601                 O   HOH B5274     1555   1555  2.54
CISPEP   1 SER A  112    PRO A  113          0         0.42
CISPEP   2 SER B  112    PRO B  113          0        -0.46
CISPEP   3 SER C  112    PRO C  113          0         1.63
CISPEP   4 SER D  112    PRO D  113          0         3.31
SITE     1 AC1 16 ALA A 185  PHE A 186  GLN A 189  HIS A 193
SITE     2 AC1 16 PHE A 196  LYS A 197  THR A 198  HIS A 200
SITE     3 AC1 16 VAL A 281  ASN A 368  TYR A 371  HIS A 372
SITE     4 AC1 16 HIS A 374  LEU A 377  VAL A 433  HOH A4121
SITE     1 AC2  7 GLU A 126  ASN A 130  TYR A 133  ARG A 202
SITE     2 AC2  7 NAG A 672  HOH A4017  HOH A4298
SITE     1 AC3  3 ARG A 202  NAG A 671  ASP B 225
SITE     1 AC4  4 ASN A 396  SER A 398  ILE A 399  GLU A 402
SITE     1 AC5 10 GLU A 165  ARG A 170  ILE A 428  GLN A 431
SITE     2 AC5 10 HOH A5372  ARG B 170  ARG B 171  ARG B 424
SITE     3 AC5 10 GLU B 472  GLU B 476
SITE     1 AC6  8 ARG A 106  VAL A 335  TYR A 341  LEU A 345
SITE     2 AC6  8 VAL A 509  ALA A 513  SER A 516  LEU A 517
SITE     1 AC7 14 ALA B 185  PHE B 186  GLN B 189  HIS B 193
SITE     2 AC7 14 PHE B 196  LYS B 197  THR B 198  HIS B 200
SITE     3 AC7 14 ASN B 368  TYR B 371  HIS B 372  HIS B 374
SITE     4 AC7 14 LEU B 377  HOH B5274
SITE     1 AC8  9 LEU A 224  GLU B 126  ASN B 130  TYR B 133
SITE     2 AC8  9 ARG B 202  NAG B 672  HOH B4045  HOH B4370
SITE     3 AC8  9 HOH B4889
SITE     1 AC9  3 ARG B 202  NAG B 671  HOH B4882
SITE     1 BC1  3 GLN B 392  ASN B 396  ILE B 399
SITE     1 BC2 10 ARG B 106  VAL B 335  TYR B 341  LEU B 345
SITE     2 BC2 10 MET B 508  VAL B 509  GLY B 512  ALA B 513
SITE     3 BC2 10 SER B 516  LEU B 517
SITE     1 BC3 16 ALA C 185  PHE C 186  ALA C 188  GLN C 189
SITE     2 BC3 16 HIS C 193  PHE C 196  LYS C 197  THR C 198
SITE     3 BC3 16 HIS C 200  VAL C 281  ASN C 368  TYR C 371
SITE     4 BC3 16 HIS C 372  HIS C 374  LEU C 377  HOH C4116
SITE     1 BC4  8 GLU C 126  ASN C 130  TYR C 133  ARG C 202
SITE     2 BC4  8 NAG C 672  HOH C4085  HOH C4331  HOH C4757
SITE     1 BC5  3 ARG C 202  NAG C 671  ASP D 225
SITE     1 BC6  4 LYS C 391  GLN C 392  ASN C 396  ILE C 399
SITE     1 BC7  8 ARG C 106  VAL C 335  TYR C 341  LEU C 345
SITE     2 BC7  8 VAL C 509  GLY C 512  ALA C 513  LEU C 517
SITE     1 BC8 15 ALA D 185  PHE D 186  GLN D 189  HIS D 193
SITE     2 BC8 15 PHE D 196  LYS D 197  THR D 198  HIS D 200
SITE     3 BC8 15 ASN D 368  TYR D 371  HIS D 372  HIS D 374
SITE     4 BC8 15 LEU D 377  LEU D 394  VAL D 433
SITE     1 BC9  7 GLU D 126  ASN D 130  TYR D 133  ARG D 202
SITE     2 BC9  7 NAG D 672  HOH D4013  HOH D4295
SITE     1 CC1  2 ARG D 202  NAG D 671
SITE     1 CC2  4 GLN D 392  ASN D 396  SER D 398  ILE D 399
SITE     1 CC3 11 LYS C 166  ARG C 170  ARG C 171  ARG C 424
SITE     2 CC3 11 GLU C 472  GLU C 476  GLU D 165  ARG D 170
SITE     3 CC3 11 ARG D 171  ILE D 428  GLN D 431
SITE     1 CC4 10 ARG D 106  VAL D 335  TYR D 341  LEU D 345
SITE     2 CC4 10 TRP D 373  PHE D 504  VAL D 509  GLY D 512
SITE     3 CC4 10 ALA D 513  LEU D 517
CRYST1  180.268  134.273  122.615  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      0.005547  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007448  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008156        0.00000
      
PROCHECK
Go to PROCHECK summary
 References