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PDBsum entry 1cvu

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase/peptide PDB id
1cvu
Jmol
Contents
Protein chains
552 a.a. *
Ligands
THR-LYS-THR-ALA-
THR-ILE-ASN-ALA-
SER
NAG-NAG ×2
NAG-NAG-MAN-MAN ×2
NAG ×2
BOG ×5
ACD ×2
Waters ×771
* Residue conservation analysis
HEADER    OXIDOREDUCTASE/PEPTIDE                  24-AUG-99   1CVU
TITLE     CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE
TITLE    2 ACTIVE SITE OF COX-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN H2 SYNTHASE-2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: PROSTAGLANDIN H2 SYNTHASE-2;
COMPND   5 EC: 1.14.99.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: PROTEIN (9-MER);
COMPND  10 CHAIN: F;
COMPND  11 ENGINEERED: YES;
COMPND  12 OTHER_DETAILS: SYNTHETIC
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PVL1393;
SOURCE   9 MOL_ID: 2;
SOURCE  10 SYNTHETIC: YES
KEYWDS    COX-2, CYCLOOXYGENASE, PROSTAGLANDIN, ARACHIDONATE, ENDOPEROXIDE,
KEYWDS   2 OXIDOREDUCTASE-PEPTIDE COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.R.KIEFER,J.L.PAWLITZ,K.T.MORELAND,R.A.STEGEMAN,J.K.GIERSE,
AUTHOR   2 A.M.STEVENS,D.C.GOODWIN,S.W.ROWLINSON,L.J.MARNETT,W.C.STALLINGS,
AUTHOR   3 R.G.KURUMBAIL
REVDAT   4   13-JUL-11 1CVU    1       VERSN
REVDAT   3   24-FEB-09 1CVU    1       VERSN
REVDAT   2   01-APR-03 1CVU    1       JRNL
REVDAT   1   16-MAY-00 1CVU    0
JRNL        AUTH   J.R.KIEFER,J.L.PAWLITZ,K.T.MORELAND,R.A.STEGEMAN,W.F.HOOD,
JRNL        AUTH 2 J.K.GIERSE,A.M.STEVENS,D.C.GOODWIN,S.W.ROWLINSON,
JRNL        AUTH 3 L.J.MARNETT,W.C.STALLINGS,R.G.KURUMBAIL
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE STEREOCHEMISTRY OF THE
JRNL        TITL 2 CYCLOOXYGENASE REACTION.
JRNL        REF    NATURE                        V. 405    97 2000
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   10811226
JRNL        DOI    10.1038/35011103
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.G.KURUMBAIL,A.M.STEVENS,J.J.MCDONALD,R.A.STEGEMAN,J.Y.PAK,
REMARK   1  AUTH 2 D.GILDEHAUS,J.M.MIYASHIRO,T.D.PENNING,K.SEIBERT,P.C.ISAKSON,
REMARK   1  AUTH 3 W.C.STALLINGS
REMARK   1  TITL   STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF BY
REMARK   1  TITL 2 ANTI-INFLAMMATORY AGENTS
REMARK   1  REF    NATURE                        V. 384   644 1996
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1  DOI    10.1038/384644A0
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.1
REMARK   3   NUMBER OF REFLECTIONS             : 58608
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 SET) : 0.204
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3887
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9001
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 328
REMARK   3   SOLVENT ATOMS            : 771
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.53
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  CONJUGATE GRADIENT, MOLECULAR DYNAMICS, INDIVIDUAL ATOM ISOTROPIC
REMARK   3  B, BULK
REMARK   3  SOLVENT CORRECTION
REMARK   4
REMARK   4 1CVU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-99.
REMARK 100 THE RCSB ID CODE IS RCSB009571.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-98
REMARK 200  TEMPERATURE           (KELVIN) : 130
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 212739
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.24100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MONOMETHYL PEG 550, MAGNESIUM SULFATE,
REMARK 280  ARACHIDNOIC ACID, EPPS, B-OG, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       90.51800
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.98000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.41700
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       90.51800
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.98000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.41700
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       90.51800
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.98000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.41700
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       90.51800
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.98000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.41700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F
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 LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    SER F2603   C     SER F2603   O       0.183
REMARK 500    SER F2603   C     SER F2603   OXT    -0.135
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG B2216   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    SER F2603   N   -  CA  -  C   ANGL. DEV. =  18.7 DEGREES
REMARK 500    SER F2603   CA  -  C   -  O   ANGL. DEV. =  24.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A  61       12.05     56.05
REMARK 500    SER A 121      -76.63    -16.57
REMARK 500    TYR A 122        3.95    -49.65
REMARK 500    THR A 129      -94.16   -117.42
REMARK 500    ARG A 185      -71.56   -100.21
REMARK 500    ASN A 195     -168.13   -117.99
REMARK 500    GLU A 290        1.91    -64.77
REMARK 500    PRO A 389       -8.92    -57.68
REMARK 500    GLU A 398      -94.79     61.09
REMARK 500    ALA A 435     -170.16    -66.28
REMARK 500    ARG A 438       66.33     37.19
REMARK 500    ASN A 439       15.74   -143.89
REMARK 500    SER A 496      -50.57     76.82
REMARK 500    PRO A 514      102.91    -43.10
REMARK 500    TRP A 545       70.93    -69.51
REMARK 500    ARG B2061       12.04     55.87
REMARK 500    SER B2121      -76.49    -16.02
REMARK 500    TYR B2122        4.02    -49.60
REMARK 500    THR B2129      -92.92   -116.95
REMARK 500    ARG B2185      -71.46    -98.90
REMARK 500    ASN B2195     -167.50   -118.09
REMARK 500    ASP B2249       16.56     56.97
REMARK 500    MET B2273      128.91   -178.27
REMARK 500    TRP B2387       48.00    -87.37
REMARK 500    PRO B2389       -9.29    -57.62
REMARK 500    GLU B2398     -122.25     61.62
REMARK 500    TYR B2409       -5.40     94.53
REMARK 500    VAL B2434      -61.06    -93.85
REMARK 500    ALA B2435     -169.11    -65.56
REMARK 500    ARG B2438       67.37     36.25
REMARK 500    ASN B2439       15.87   -144.61
REMARK 500    SER B2496      -50.80     76.18
REMARK 500    PRO B2514      103.19    -42.73
REMARK 500    TRP B2545       70.51    -68.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 409         0.07    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER F2603        18.0      L          L   OUTSIDE RANGE
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 A3015        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A3019        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A3028        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A3054        DISTANCE =  6.04 ANGSTROMS
REMARK 525    HOH A3156        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH A3565        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH A3590        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH A3771        DISTANCE =  5.76 ANGSTROMS
REMARK 525    HOH B3246        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH B3252        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH B3255        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH B3314        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH B3318        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH B3363        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH B3414        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH B3631        DISTANCE =  5.69 ANGSTROMS
REMARK 525    HOH B3669        DISTANCE =  6.10 ANGSTROMS
REMARK 525    HOH B3751        DISTANCE =  5.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
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 MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 2673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 2674
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 2702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 2704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 2701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF PROTEIN (9-MER)
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6COX   RELATED DB: PDB
REMARK 900 CYCLOOXYGENASE-2 COMPLEXED WITH SELECTIVE INHIBITOR SC-558
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB
REMARK 900 CYCLOOXYGENASE-2 WITHOUT BOUND INHIBITORS
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB
REMARK 900 CYCLOOXYGENASE-1 STRUCTURE
REMARK 900 RELATED ID: 1LOX   RELATED DB: PDB
REMARK 900 15-LIPOXYGENASE STRUCTURE
DBREF  1CVU A   33   583  UNP    Q05769   PGH2_MOUSE      18    569
DBREF  1CVU B 2033  2583  UNP    Q05769   PGH2_MOUSE      18    569
DBREF  1CVU F 2595  2603  PDB    1CVU     1CVU          2595   2603
SEQADV 1CVU GLN A  310  UNP  Q05769    ASN   296 ENGINEERED
SEQADV 1CVU LYS A  333  UNP  Q05769    ARG   319 ENGINEERED
SEQADV 1CVU GLN B 2310  UNP  Q05769    ASN   296 ENGINEERED
SEQADV 1CVU LYS B 2333  UNP  Q05769    ARG   319 ENGINEERED
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 ALA 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 GLN 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 LYS 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 ALA 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 GLN 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 LYS 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 F    9  THR LYS THR ALA THR ILE ASN ALA SER
MODRES 1CVU ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1CVU ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1CVU ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 1CVU ASN B 2068  ASN  GLYCOSYLATION SITE
MODRES 1CVU ASN B 2144  ASN  GLYCOSYLATION SITE
MODRES 1CVU ASN B 2410  ASN  GLYCOSYLATION SITE
HET    NAG  A 661      14
HET    NAG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    MAN  A 673      11
HET    MAN  A 674      11
HET    NAG  A 681      14
HET    NAG  B2661      14
HET    NAG  B2662      14
HET    NAG  B2671      14
HET    NAG  B2672      14
HET    MAN  B2673      11
HET    MAN  B2674      11
HET    NAG  B2681      14
HET    BOG  A 702      20
HET    BOG  A 703      20
HET    BOG  A 704      20
HET    BOG  B2702      20
HET    BOG  B2704      20
HET    ACD  A 701      22
HET    ACD  B2701      22
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     ACD ARACHIDONIC ACID
FORMUL   4  NAG    10(C8 H15 N O6)
FORMUL   5  MAN    4(C6 H12 O6)
FORMUL  10  BOG    5(C14 H28 O6)
FORMUL  15  ACD    2(C20 H32 O2)
FORMUL  17  HOH   *771(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 PHE A   96  ASN A  105  1                                  10
HELIX    4   4 ILE A  105A TYR A  122  1                                  18
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  ALA A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 VAL A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  ASP A  347  1                                  24
HELIX   15  15 ASP A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 TRP A  387  LEU A  391  5                                   5
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  410  GLY A  418  1                                   9
HELIX   21  21 HIS A  417  GLN A  429  1                                  13
HELIX   22  22 PRO A  441  ALA A  443  5                                   3
HELIX   23  23 VAL A  444  MET A  458  1                                  15
HELIX   24  24 SER A  462  PHE A  470  1                                   9
HELIX   25  25 SER A  477  GLY A  483  1                                   7
HELIX   26  26 LYS A  485  SER A  496  1                                  12
HELIX   27  27 ASP A  497  MET A  501  5                                   5
HELIX   28  28 GLU A  502  GLU A  510  1                                   9
HELIX   29  29 GLY A  519  GLY A  536  1                                  18
HELIX   30  30 ASN A  537  SER A  541  5                                   5
HELIX   31  31 LYS A  546  GLY A  551  5                                   6
HELIX   32  32 GLY A  552  THR A  561  1                                  10
HELIX   33  33 SER A  563  VAL A  572  1                                  10
HELIX   34  34 GLU B 2073  LYS B 2083  1                                  11
HELIX   35  35 THR B 2085  THR B 2094  1                                  10
HELIX   36  36 PHE B 2096  ASN B 2105  1                                  10
HELIX   37  37 ILE B  105B TYR B 2122  1                                  18
HELIX   38  38 SER B 2138  ASN B 2144  1                                   7
HELIX   39  39 ASP B 2173  LEU B 2182  1                                  10
HELIX   40  40 ASN B 2195  ALA B 2207  1                                  13
HELIX   41  41 LEU B 2230  GLY B 2235  1                                   6
HELIX   42  42 THR B 2237  ARG B 2245  1                                   9
HELIX   43  43 THR B 2265  GLN B 2270  1                                   6
HELIX   44  44 PRO B 2280  GLN B 2284  5                                   5
HELIX   45  45 VAL B 2295  HIS B 2320  1                                  26
HELIX   46  46 GLY B 2324  ASP B 2347  1                                  24
HELIX   47  47 ASP B 2347  GLY B 2354  1                                   8
HELIX   48  48 ASP B 2362  PHE B 2367  5                                   6
HELIX   49  49 ALA B 2378  TYR B 2385  1                                   8
HELIX   50  50 TRP B 2387  LEU B 2391  5                                   5
HELIX   51  51 PHE B 2404  LEU B 2408  5                                   5
HELIX   52  52 ASN B 2411  GLY B 2418  1                                   8
HELIX   53  53 HIS B 2417  GLN B 2429  1                                  13
HELIX   54  54 PRO B 2441  ALA B 2443  5                                   3
HELIX   55  55 VAL B 2444  MET B 2458  1                                  15
HELIX   56  56 SER B 2462  PHE B 2470  1                                   9
HELIX   57  57 SER B 2477  GLY B 2483  1                                   7
HELIX   58  58 LYS B 2485  SER B 2496  1                                  12
HELIX   59  59 ASP B 2497  MET B 2501  5                                   5
HELIX   60  60 GLU B 2502  GLU B 2510  1                                   9
HELIX   61  61 GLY B 2519  GLY B 2536  1                                  18
HELIX   62  62 ASN B 2537  SER B 2541  5                                   5
HELIX   63  63 LYS B 2546  GLY B 2551  5                                   6
HELIX   64  64 GLY B 2552  THR B 2561  1                                  10
HELIX   65  65 SER B 2563  VAL B 2572  1                                  10
HELIX   66  66 THR F 2595  SER F 2603  1                                   9
SHEET    1   A 2 GLU A  46  GLY A  51  0
SHEET    2   A 2 GLN A  54  ASP A  58 -1  O  GLN A  54   N  THR A  50
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  N  THR A  71   O  TYR A  65
SHEET    1   C 2 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257
SHEET    1   D 2 PHE A 395  ILE A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  N  GLN A 400   O  ILE A 397
SHEET    1   E 2 GLU B2046  GLY B2051  0
SHEET    2   E 2 GLN B2054  ASP B2058 -1  O  GLN B2054   N  THR B2050
SHEET    1   F 2 PHE B2064  TYR B2065  0
SHEET    2   F 2 THR B2071  PRO B2072 -1  N  THR B2071   O  TYR B2065
SHEET    1   G 2 GLN B2255  ILE B2257  0
SHEET    2   G 2 GLU B2260  TYR B2262 -1  O  GLU B2260   N  ILE B2257
SHEET    1   H 2 PHE B2395  ILE B2397  0
SHEET    2   H 2 GLN B2400  TYR B2402 -1  N  GLN B2400   O  ILE B2397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.02
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03
SSBOND   6 CYS B 2036    CYS B 2047                          1555   1555  2.03
SSBOND   7 CYS B 2037    CYS B 2159                          1555   1555  2.03
SSBOND   8 CYS B 2041    CYS B 2057                          1555   1555  2.03
SSBOND   9 CYS B 2059    CYS B 2069                          1555   1555  2.03
SSBOND  10 CYS B 2569    CYS B 2575                          1555   1555  2.03
LINK         C1  NAG A 661                 ND2 ASN A  68     1555   1555  1.46
LINK         C1  NAG A 671                 ND2 ASN A 144     1555   1555  1.44
LINK         C1  NAG A 681                 ND2 ASN A 410     1555   1555  1.47
LINK         C1  NAG B2661                 ND2 ASN B2068     1555   1555  1.45
LINK         C1  NAG B2671                 ND2 ASN B2144     1555   1555  1.44
LINK         C1  NAG B2681                 ND2 ASN B2410     1555   1555  1.43
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.40
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.36
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.41
LINK         O6  MAN A 673                 C1  MAN A 674     1555   1555  1.50
LINK         O4  NAG B2661                 C1  NAG B2662     1555   1555  1.40
LINK         O4  NAG B2671                 C1  NAG B2672     1555   1555  1.34
LINK         O4  NAG B2672                 C1  MAN B2673     1555   1555  1.40
LINK         O6  MAN B2673                 C1  MAN B2674     1555   1555  1.49
CISPEP   1 SER A  126    PRO A  127          0         1.27
CISPEP   2 SER B 2126    PRO B 2127          0         0.89
SITE     1 AC1  6 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 AC1  6 HOH A3137  HOH A3173
SITE     1 AC2  1 NAG A 661
SITE     1 AC3  8 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC3  8 PHE A 220  NAG A 672  HOH A3080  HOH A3648
SITE     1 AC4  5 ARG A 216  NAG A 671  MAN A 673  LEU B2238
SITE     2 AC4  5 ASP B2239
SITE     1 AC5  3 NAG A 672  MAN A 674  HOH A3748
SITE     1 AC6  1 MAN A 673
SITE     1 AC7  5 TYR A 402  GLN A 406  ASN A 410  ILE A 413
SITE     2 AC7  5 HOH A3667
SITE     1 AC8  5 TYR B2055  GLU B2067  ASN B2068  NAG B2662
SITE     2 AC8  5 HOH B3652
SITE     1 AC9  3 NAG B2661  HOH B3642  HOH B3676
SITE     1 BC1  6 GLU B2140  ASN B2144  TYR B2147  ARG B2216
SITE     2 BC1  6 NAG B2672  HOH B3420
SITE     1 BC2  4 ASP A 239  ARG B2216  NAG B2671  MAN B2673
SITE     1 BC3  2 NAG B2672  MAN B2674
SITE     1 BC4  1 MAN B2673
SITE     1 BC5  5 TYR B2402  ASN B2410  SER B2412  ILE B2413
SITE     2 BC5  5 GLU B2416
SITE     1 BC6  6 ASN A  87  THR A  88  TYR A  91  HOH A3004
SITE     2 BC6  6 HOH A3158  HOH A3519
SITE     1 BC7 12 GLU A 179  ARG A 184  ARG A 185  ILE A 442
SITE     2 BC7 12 GLN A 445  LYS B2180  ARG B2184  ARG B2185
SITE     3 BC7 12 ARG B2438  ILE B2442  GLU B2486  GLU B2490
SITE     1 BC8  9 GLN A 203  THR A 212  HIS A 214  ASN A 382
SITE     2 BC8  9 TYR A 385  HIS A 386  TRP A 387  LEU A 390
SITE     3 BC8  9 GLN A 454
SITE     1 BC9  6 THR B2088  TYR B2091  PHE B2096  PRO B2514
SITE     2 BC9  6 HOH B3695  HOH B3777
SITE     1 CC1  9 GLN B2203  PHE B2210  THR B2212  HIS B2214
SITE     2 CC1  9 ASN B2382  TYR B2385  HIS B2386  TRP B2387
SITE     3 CC1  9 GLN B2454
SITE     1 CC2  9 PHE A 205  ILE A 345  VAL A 349  TYR A 385
SITE     2 CC2  9 TRP A 387  GLY A 526  SER A 530  LEU A 534
SITE     3 CC2  9 HOH A3651
SITE     1 CC3 11 LEU B2117  ARG B2120  PHE B2205  ILE B2345
SITE     2 CC3 11 TYR B2348  VAL B2349  TYR B2385  GLY B2526
SITE     3 CC3 11 SER B2530  LEU B2534  HOH B3411
SITE     1 CC4 13 ILE A 257  GLY A 258  GLU A 260  TYR A 262
SITE     2 CC4 13 ASN A 282  LEU A 415  GLU A 416  HOH A3110
SITE     3 CC4 13 HOH A3593  HOH A3782  CYS B2569  ASN B2570
SITE     4 CC4 13 CYS B2575
CRYST1  181.036  133.960  124.834  90.00  90.00  90.00 I 2 2 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      0.005524  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007465  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008011        0.00000
      
PROCHECK
Go to PROCHECK summary
 References