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PDBsum entry 4e1g

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
4e1g
Jmol
Contents
Protein chains
551 a.a.
Ligands
LNL ×2
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG
EDO ×7
AKR ×2
Waters ×746
HEADER    OXIDOREDUCTASE                          06-MAR-12   4E1G
TITLE     X-RAY CRYSTAL STRUCTURE OF ALPHA-LINOLENIC ACID BOUND TO THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 1-604;
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;
COMPND  12 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 STRAIN: WILD TYPE;
SOURCE   6 GENE: COX-2, COX2, PGHS-B, PTGS2, TIS10;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    MONOTOPIC MEMBRANE PROTEIN, BIOLOGICAL DIMER, OXIDOREDUCTASE, COX-2,
KEYWDS   2 N-GLYCOSYLATION, MEMBRANE OF ER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI
REVDAT   3   01-AUG-12 4E1G    1       JRNL
REVDAT   2   13-JUN-12 4E1G    1       JRNL
REVDAT   1   25-APR-12 4E1G    0
JRNL        AUTH   A.J.VECCHIO,B.J.ORLANDO,R.NANDAGIRI,M.G.MALKOWSKI
JRNL        TITL   INVESTIGATING SUBSTRATE PROMISCUITY IN CYCLOOXYGENASE-2: THE
JRNL        TITL 2 ROLE OF ARG-120 AND RESIDUES LINING THE HYDROPHOBIC GROOVE.
JRNL        REF    J.BIOL.CHEM.                  V. 287 24619 2012
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   22637474
JRNL        DOI    10.1074/JBC.M112.372243
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 79080
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) : 0.161
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.203
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4154
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5579
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.17
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060
REMARK   3   BIN FREE R VALUE SET COUNT          : 289
REMARK   3   BIN FREE R VALUE                    : 0.2690
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8840
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 335
REMARK   3   SOLVENT ATOMS            : 746
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.41000
REMARK   3    B22 (A**2) : 0.15000
REMARK   3    B33 (A**2) : -0.56000
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): 0.172
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.101
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.250
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9517 ; 0.024 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12954 ; 2.044 ; 2.001
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1118 ; 6.327 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   440 ;37.343 ;23.841
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1486 ;14.697 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.417 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1381 ; 0.148 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7317 ; 0.012 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5541 ; 1.037 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9005 ; 1.757 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3976 ; 3.243 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3939 ; 4.852 ; 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  : 6
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    33        A   114
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7541  45.6869  63.8335
REMARK   3    T TENSOR
REMARK   3      T11:    .0350 T22:    .1527
REMARK   3      T33:    .1883 T12:   -.0394
REMARK   3      T13:   -.0381 T23:   -.0652
REMARK   3    L TENSOR
REMARK   3      L11:    .6320 L22:   1.0370
REMARK   3      L33:    .8200 L12:   -.6482
REMARK   3      L13:    .0323 L23:    .4310
REMARK   3    S TENSOR
REMARK   3      S11:   -.0526 S12:   -.0470 S13:    .2179
REMARK   3      S21:   -.0423 S22:    .1793 S23:   -.2238
REMARK   3      S31:   -.1111 S32:    .3047 S33:   -.1268
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 :   A   115        A   226
REMARK   3    ORIGIN FOR THE GROUP (A):  37.3441  35.8213  66.9008
REMARK   3    T TENSOR
REMARK   3      T11:    .0729 T22:    .0686
REMARK   3      T33:    .0695 T12:    .0196
REMARK   3      T13:   -.0083 T23:    .0012
REMARK   3    L TENSOR
REMARK   3      L11:    .6246 L22:    .7472
REMARK   3      L33:    .4718 L12:   -.3485
REMARK   3      L13:   -.0798 L23:    .3139
REMARK   3    S TENSOR
REMARK   3      S11:   -.0673 S12:   -.0913 S13:   -.0387
REMARK   3      S21:    .0721 S22:    .0820 S23:    .0048
REMARK   3      S31:    .0384 S32:    .0680 S33:   -.0147
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 :   A   227        A   582
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3961  47.7015  66.4355
REMARK   3    T TENSOR
REMARK   3      T11:    .0389 T22:    .0351
REMARK   3      T33:    .0532 T12:   -.0048
REMARK   3      T13:   -.0074 T23:   -.0144
REMARK   3    L TENSOR
REMARK   3      L11:    .6613 L22:    .5279
REMARK   3      L33:    .6480 L12:   -.4560
REMARK   3      L13:    .0936 L23:    .0625
REMARK   3    S TENSOR
REMARK   3      S11:   -.0271 S12:   -.1330 S13:   -.0008
REMARK   3      S21:    .0556 S22:    .0654 S23:    .0226
REMARK   3      S31:   -.0365 S32:   -.0069 S33:   -.0383
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 :   B    33        B   119
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9869  57.8689  29.1286
REMARK   3    T TENSOR
REMARK   3      T11:    .2051 T22:    .0509
REMARK   3      T33:    .1445 T12:   -.0577
REMARK   3      T13:    .0664 T23:    .0408
REMARK   3    L TENSOR
REMARK   3      L11:   1.4679 L22:   1.3492
REMARK   3      L33:   1.1293 L12:  -1.1801
REMARK   3      L13:   -.2180 L23:    .1344
REMARK   3    S TENSOR
REMARK   3      S11:    .2193 S12:    .0830 S13:    .2764
REMARK   3      S21:   -.2274 S22:   -.1146 S23:   -.3387
REMARK   3      S31:   -.4355 S32:    .1588 S33:   -.1047
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   120        B   228
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0893  41.0382  26.7697
REMARK   3    T TENSOR
REMARK   3      T11:    .0772 T22:    .0918
REMARK   3      T33:    .0462 T12:    .0477
REMARK   3      T13:   -.0160 T23:   -.0192
REMARK   3    L TENSOR
REMARK   3      L11:    .3281 L22:    .6792
REMARK   3      L33:    .7960 L12:   -.2177
REMARK   3      L13:   -.2070 L23:    .3113
REMARK   3    S TENSOR
REMARK   3      S11:    .0916 S12:    .1063 S13:   -.0175
REMARK   3      S21:   -.1366 S22:   -.0954 S23:    .0146
REMARK   3      S31:   -.1490 S32:   -.0429 S33:    .0038
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   229        B   582
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3094  29.9826  27.3896
REMARK   3    T TENSOR
REMARK   3      T11:    .0287 T22:    .0678
REMARK   3      T33:    .0493 T12:    .0130
REMARK   3      T13:    .0044 T23:   -.0345
REMARK   3    L TENSOR
REMARK   3      L11:    .4960 L22:    .7349
REMARK   3      L33:    .8355 L12:   -.3199
REMARK   3      L13:    .0696 L23:    .0156
REMARK   3    S TENSOR
REMARK   3      S11:    .0733 S12:    .1375 S13:   -.0415
REMARK   3      S21:   -.1304 S22:   -.0245 S23:   -.0341
REMARK   3      S31:   -.0611 S32:    .0110 S33:   -.0488
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4E1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071048.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9767
REMARK 200  MONOCHROMATOR                  : SI (111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79080
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.09800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.51600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.700
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: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM
REMARK 280  HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 296K
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       60.18900
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.06550
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.21900
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.18900
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.06550
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.21900
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.18900
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.06550
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.21900
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.18900
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.06550
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.21900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    10
REMARK 465     LEU A    11
REMARK 465     PHE A    12
REMARK 465     ARG A    13
REMARK 465     ALA A    14
REMARK 465     VAL A    15
REMARK 465     LEU A    16
REMARK 465     LEU A    17
REMARK 465     CYS A    18
REMARK 465     ALA A    19
REMARK 465     ALA A    20
REMARK 465     LEU A    21
REMARK 465     GLY A    22
REMARK 465     LEU A    23
REMARK 465     SER A    24
REMARK 465     GLN A    25
REMARK 465     ALA A    26
REMARK 465     ALA A    27
REMARK 465     ASN A    28
REMARK 465     HIS A    29
REMARK 465     HIS A    30
REMARK 465     HIS A    31
REMARK 465     HIS A    32
REMARK 465     GLN A   583
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ALA A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     MET B    10
REMARK 465     LEU B    11
REMARK 465     PHE B    12
REMARK 465     ARG B    13
REMARK 465     ALA B    14
REMARK 465     VAL B    15
REMARK 465     LEU B    16
REMARK 465     LEU B    17
REMARK 465     CYS B    18
REMARK 465     ALA B    19
REMARK 465     ALA B    20
REMARK 465     LEU B    21
REMARK 465     GLY B    22
REMARK 465     LEU B    23
REMARK 465     SER B    24
REMARK 465     GLN B    25
REMARK 465     ALA B    26
REMARK 465     ALA B    27
REMARK 465     ASN B    28
REMARK 465     HIS B    29
REMARK 465     HIS B    30
REMARK 465     HIS B    31
REMARK 465     HIS B    32
REMARK 465     GLN B   583
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     GLN B   586
REMARK 465     PRO B   587
REMARK 465     THR B   588
REMARK 465     LYS B   589
REMARK 465     THR B   590
REMARK 465     ALA B   591
REMARK 465     THR B   592
REMARK 465     ILE B   593
REMARK 465     ALA B   594
REMARK 465     ALA B   595
REMARK 465     SER B   596
REMARK 465     ALA B   597
REMARK 465     SER B   598
REMARK 465     HIS B   599
REMARK 465     SER B   600
REMARK 465     ARG B   601
REMARK 465     LEU B   602
REMARK 465     ASP B   603
REMARK 465     ASP B   604
REMARK 465     ILE B   605
REMARK 465     ASN B   606
REMARK 465     PRO B   607
REMARK 465     THR B   608
REMARK 465     VAL B   609
REMARK 465     LEU B   610
REMARK 465     ILE B   611
REMARK 465     LYS B   612
REMARK 465     ARG B   613
REMARK 465     ARG B   614
REMARK 465     SER B   615
REMARK 465     THR B   616
REMARK 465     GLU B   617
REMARK 465     LEU B   618
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ASP A  53    CG   OD1  OD2
REMARK 470     GLN A  54    CD   OE1  NE2
REMARK 470     LYS A  56    CE   NZ
REMARK 470     LEU A  75    CD1  CD2
REMARK 470     LYS A  79    CG   CD   CE   NZ
REMARK 470     LEU A  81    CD1  CD2
REMARK 470     LYS A  83    CG   CD   CE   NZ
REMARK 470     LYS A  97    CD   CE   NZ
REMARK 470     LYS A 169    CD   CE   NZ
REMARK 470     GLU A 170    CD   OE1  OE2
REMARK 470     LYS A 175    NZ
REMARK 470     LYS A 215    CD   CE   NZ
REMARK 470     ASP A 239    OD1  OD2
REMARK 470     LYS A 248    CE   NZ
REMARK 470     LYS A 267    CD   CE   NZ
REMARK 470     GLU A 272    CD   OE1  OE2
REMARK 470     LYS A 358    CE   NZ
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     GLU A 416    OE1  OE2
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     LYS A 485    CE   NZ
REMARK 470     LYS A 511    CE   NZ
REMARK 470     LYS A 557    CG   CD   CE   NZ
REMARK 470     GLN B  54    CG   CD   OE1  NE2
REMARK 470     LYS B  56    CE   NZ
REMARK 470     LEU B  75    CD1  CD2
REMARK 470     LYS B  79    CE   NZ
REMARK 470     LYS B  83    CD   CE   NZ
REMARK 470     LYS B  97    CE   NZ
REMARK 470     LYS B 169    CD   CE   NZ
REMARK 470     LYS B 215    CD   CE   NZ
REMARK 470     ASP B 239    OD1  OD2
REMARK 470     LYS B 267    NZ
REMARK 470     GLU B 281    CG   CD   OE1  OE2
REMARK 470     LYS B 358    CE   NZ
REMARK 470     ASP B 399    OD1  OD2
REMARK 470     LYS B 405    CE   NZ
REMARK 470     GLU B 416    CD   OE1  OE2
REMARK 470     LYS B 473    CD   CE   NZ
REMARK 470     LYS B 492    CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   ND2  ASN B    68     O5   NAG B   703              1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A 275   CE2   TYR A 275   CD2     0.093
REMARK 500    CYS A 575   CB    CYS A 575   SG      0.114
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    LEU A 230   CB  -  CG  -  CD1 ANGL. DEV. =  10.5 DEGREES
REMARK 500    LEU A 294   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES
REMARK 500    MET A 299   CG  -  SD  -  CE  ANGL. DEV. = -12.2 DEGREES
REMARK 500    ARG B  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ASP B 173   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    LEU B 294   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES
REMARK 500    MET B 458   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG B 467   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B 467   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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  60      119.36    -36.49
REMARK 500    SER A 126      111.10   -160.33
REMARK 500    THR A 129      -96.79   -125.37
REMARK 500    TRP A 387       45.98    -90.16
REMARK 500    GLU A 398     -123.60     60.84
REMARK 500    ASN A 410       74.02   -111.28
REMARK 500    SER A 496      -47.90     62.93
REMARK 500    THR B 129      -92.34   -124.86
REMARK 500    ARG B 185      -89.00    -88.14
REMARK 500    TRP B 387       46.25    -88.86
REMARK 500    GLU B 398     -117.63     59.49
REMARK 500    TYR B 409       -1.61     73.48
REMARK 500    ASN B 439       20.50   -140.83
REMARK 500    SER B 496      -54.77     66.69
REMARK 500    SER B 579     -169.57   -169.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN A  581     VAL A  582                  145.05
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    HIS A 207        24.9      L          L   OUTSIDE RANGE
REMARK 500    VAL A 582        16.9      L          L   OUTSIDE RANGE
REMARK 500    PHE B 209        24.9      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 B1135        DISTANCE =  5.07 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                             COH B 702  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 COH B 702   NA   88.8
REMARK 620 3 COH B 702   NB   92.3  89.6
REMARK 620 4 COH B 702   NC   86.9 175.1  92.9
REMARK 620 5 COH B 702   ND   80.0  88.7 172.1  88.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH A 702  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 702   NA   80.8
REMARK 620 3 COH A 702   NB   90.4  81.2
REMARK 620 4 COH A 702   NC   89.8 169.8  95.2
REMARK 620 5 COH A 702   ND   77.2  93.2 167.1  88.4
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 712
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TZI   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 G533V MURINE COX-2
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL
REMARK 900 OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3QH0   RELATED DB: PDB
REMARK 900 PALMITIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1
DBREF  4E1G A   10   618  UNP    Q05769   PGH2_MOUSE       1    604
DBREF  4E1G B   10   618  UNP    Q05769   PGH2_MOUSE       1    604
SEQADV 4E1G HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQADV 4E1G HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 4E1G ALA B  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQRES   1 A  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 A  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES   3 A  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES   4 A  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES   5 A  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES   6 A  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES   7 A  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES   8 A  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES   9 A  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES  10 A  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES  11 A  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES  12 A  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES  13 A  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES  14 A  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES  15 A  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES  16 A  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES  17 A  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES  18 A  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES  19 A  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES  20 A  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES  21 A  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES  22 A  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES  23 A  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES  24 A  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES  25 A  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES  26 A  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES  27 A  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES  28 A  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES  29 A  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES  30 A  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES  31 A  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES  32 A  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES  33 A  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES  34 A  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES  35 A  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES  36 A  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES  37 A  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES  38 A  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES  39 A  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES  40 A  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES  41 A  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES  42 A  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES  43 A  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES  44 A  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES  45 A  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES  46 A  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES  47 A  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
SEQRES   1 B  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 B  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES   3 B  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES   4 B  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES   5 B  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES   6 B  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES   7 B  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES   8 B  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES   9 B  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES  10 B  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES  11 B  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES  12 B  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES  13 B  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES  14 B  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES  15 B  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES  16 B  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES  17 B  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES  18 B  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES  19 B  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES  20 B  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES  21 B  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES  22 B  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES  23 B  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES  24 B  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES  25 B  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES  26 B  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES  27 B  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES  28 B  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES  29 B  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES  30 B  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES  31 B  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES  32 B  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES  33 B  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES  34 B  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES  35 B  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES  36 B  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES  37 B  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES  38 B  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES  39 B  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES  40 B  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES  41 B  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES  42 B  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES  43 B  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES  44 B  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES  45 B  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES  46 B  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES  47 B  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
MODRES 4E1G ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 4E1G ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 4E1G ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 4E1G ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 4E1G ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 4E1G ASN A  410  ASN  GLYCOSYLATION SITE
HET    LNL  A 701      20
HET    COH  A 702      43
HET    NAG  A 703      14
HET    NAG  A 704      14
HET    NAG  A 705      14
HET    NAG  A 706      14
HET    MAN  A 707      11
HET    NAG  A 708      14
HET    BOG  A 709      20
HET    EDO  A 710       4
HET    EDO  A 711       4
HET    AKR  A 712       5
HET    AKR  A 713       5
HET    LNL  B 701      20
HET    COH  B 702      43
HET    NAG  B 703      14
HET    NAG  B 704      14
HET    NAG  B 705      14
HET    NAG  B 706      14
HET    NAG  B 707      14
HET    EDO  B 708       4
HET    EDO  B 709       4
HET    EDO  B 710       4
HET    EDO  B 711       4
HET    EDO  B 712       4
HETNAM     LNL ALPHA-LINOLENIC ACID
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     AKR ACRYLIC ACID
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  LNL    2(C18 H30 O2)
FORMUL   4  COH    2(C34 H32 CO N4 O4)
FORMUL   5  NAG    10(C8 H15 N O6)
FORMUL   6  MAN    C6 H12 O6
FORMUL   8  BOG    C14 H28 O6
FORMUL   9  EDO    7(C2 H6 O2)
FORMUL  11  AKR    2(C3 H4 O2)
FORMUL  23  HOH   *746(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  HIS 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 HIS A  386  LEU A  391  5                                   6
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  410  GLN A  429  1                                  20
HELIX   21  21 PRO A  441  ALA A  443  5                                   3
HELIX   22  22 VAL A  444  MET A  458  1                                  15
HELIX   23  23 SER A  462  PHE A  470  1                                   9
HELIX   24  24 SER A  477  GLY A  483  1                                   7
HELIX   25  25 LYS A  485  SER A  496  1                                  12
HELIX   26  26 ASP A  497  MET A  501  5                                   5
HELIX   27  27 GLU A  502  GLU A  510  1                                   9
HELIX   28  28 GLY A  519  GLY A  536  1                                  18
HELIX   29  29 ASN A  537  SER A  541  5                                   5
HELIX   30  30 LYS A  546  GLY A  551  5                                   6
HELIX   31  31 GLY A  552  THR A  561  1                                  10
HELIX   32  32 SER A  563  VAL A  572  1                                  10
HELIX   33  33 GLU B   73  LYS B   83  1                                  11
HELIX   34  34 THR B   85  THR B   94  1                                  10
HELIX   35  35 PHE B   96  ASN B  105  1                                  10
HELIX   36  36 ILE B  105A LEU B  123  1                                  19
HELIX   37  37 SER B  138  ASN B  144  1                                   7
HELIX   38  38 ASP B  173  LEU B  182  1                                  10
HELIX   39  39 ASN B  195  HIS B  207  1                                  13
HELIX   40  40 LEU B  230  GLY B  235  1                                   6
HELIX   41  41 THR B  237  ARG B  245  1                                   9
HELIX   42  42 THR B  265  GLN B  270  1                                   6
HELIX   43  43 PRO B  280  GLN B  284  5                                   5
HELIX   44  44 VAL B  291  LEU B  294  5                                   4
HELIX   45  45 VAL B  295  HIS B  320  1                                  26
HELIX   46  46 GLY B  324  ASP B  347  1                                  24
HELIX   47  47 ASP B  347  GLY B  354  1                                   8
HELIX   48  48 ASP B  362  PHE B  367  5                                   6
HELIX   49  49 ALA B  378  TYR B  385  1                                   8
HELIX   50  50 HIS B  386  LEU B  391  5                                   6
HELIX   51  51 SER B  403  LEU B  408  1                                   6
HELIX   52  52 ASN B  411  GLY B  418  1                                   8
HELIX   53  53 GLY B  418  GLN B  429  1                                  12
HELIX   54  54 PRO B  441  ALA B  443  5                                   3
HELIX   55  55 VAL B  444  MET B  458  1                                  15
HELIX   56  56 SER B  462  PHE B  470  1                                   9
HELIX   57  57 SER B  477  GLY B  483  1                                   7
HELIX   58  58 LYS B  485  SER B  496  1                                  12
HELIX   59  59 ASP B  497  MET B  501  5                                   5
HELIX   60  60 GLU B  502  GLU B  510  1                                   9
HELIX   61  61 GLY B  519  GLY B  536  1                                  18
HELIX   62  62 ASN B  537  SER B  541  5                                   5
HELIX   63  63 LYS B  546  GLY B  551  5                                   6
HELIX   64  64 GLY B  552  THR B  561  1                                  10
HELIX   65  65 SER B  563  VAL B  572  1                                  10
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  O  THR A  71   N  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  O  TYR A 402   N  PHE A 395
SHEET    1   E 2 GLU B  46  SER B  49  0
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46
SHEET    1   F 2 PHE B  64  TYR B  65  0
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   G 2 THR B 212  ASP B 213  0
SHEET    2   G 2 GLY B 217  THR B 221 -1  O  GLY B 217   N  ASP B 213
SHEET    1   H 2 GLN B 255  ILE B 257  0
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   I 2 PHE B 395  ILE B 397  0
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.08
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.10
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.09
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.14
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.07
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.02
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.07
LINK         ND2 ASN B  68                 C1  NAG B 703     1555   1555  1.34
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.43
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.43
LINK         ND2 ASN B 144                 C1  NAG B 705     1555   1555  1.43
LINK         ND2 ASN A  68                 C1  NAG A 703     1555   1555  1.44
LINK         ND2 ASN A 144                 C1  NAG A 705     1555   1555  1.44
LINK         O4  NAG A 705                 C1  NAG A 706     1555   1555  1.45
LINK         ND2 ASN B 410                 C1  NAG B 707     1555   1555  1.45
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.45
LINK         O4  NAG A 706                 C1  MAN A 707     1555   1555  1.45
LINK         ND2 ASN A 410                 C1  NAG A 708     1555   1555  1.46
LINK         NE2AHIS B 388                CO   COH B 702     1555   1555  2.38
LINK         NE2BHIS A 388                CO   COH A 702     1555   1555  2.72
CISPEP   1 SER A  126    PRO A  127          0        -0.92
CISPEP   2 SER B  126    PRO B  127          0         1.15
SITE     1 AC1 13 ARG A 120  PHE A 205  PHE A 209  TYR A 348
SITE     2 AC1 13 VAL A 349  TYR A 355  ILE A 377  PHE A 381
SITE     3 AC1 13 TYR A 385  ALA A 527  SER A 530  GLY A 533
SITE     4 AC1 13 LEU A 534
SITE     1 AC2 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210
SITE     2 AC2 15 THR A 212  HIS A 214  VAL A 295  ASN A 382
SITE     3 AC2 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391
SITE     4 AC2 15 LEU A 408  VAL A 447  HOH A1080
SITE     1 AC3  7 TYR A  55  GLU A  67  ASN A  68  NAG A 704
SITE     2 AC3  7 HOH A 882  HOH A1078  HOH A1162
SITE     1 AC4  3 NAG A 703  HOH A1078  HOH A1153
SITE     1 AC5  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC5  9 NAG A 706  HOH A 847  HOH A 904  HOH A 914
SITE     3 AC5  9 HOH A1077
SITE     1 AC6  3 ARG A 216  NAG A 705  MAN A 707
SITE     1 AC7  2 NAG A 706  HOH A1180
SITE     1 AC8  3 ASN A 410  SER A 412  ILE A 413
SITE     1 AC9 11 GLU A 179  LYS A 180  ARG A 184  ARG A 185
SITE     2 AC9 11 ARG A 438  GLU A 486  GLU A 490  GLU B 179
SITE     3 AC9 11 ARG B 185  ILE B 442  GLN B 445
SITE     1 BC1  6 PRO A 162  SER A 455  ARG A 456  LYS A 459
SITE     2 BC1  6 TYR A 460  HOH A 942
SITE     1 BC2  8 GLU A 308  ARG A 311  GLU A 339  SER A 566
SITE     2 BC2  8 LEU A 567  ASN A 570  ASN A 571  HOH A 845
SITE     1 BC3  5 SER A 477  PHE A 478  GLU A 479  LYS A 492
SITE     2 BC3  5 HOH A1076
SITE     1 BC4  6 ASP A 239  ARG A 240  LYS A 243  VAL A 271
SITE     2 BC4  6 GLU A 272  HOH A1114
SITE     1 BC5 14 ARG B 120  PHE B 205  PHE B 209  TYR B 348
SITE     2 BC5 14 VAL B 349  LEU B 352  TYR B 355  ILE B 377
SITE     3 BC5 14 PHE B 381  TYR B 385  ALA B 527  SER B 530
SITE     4 BC5 14 GLY B 533  LEU B 534
SITE     1 BC6 17 ALA B 199  GLN B 203  HIS B 207  PHE B 210
SITE     2 BC6 17 LYS B 211  THR B 212  HIS B 214  VAL B 295
SITE     3 BC6 17 ASN B 382  TYR B 385  HIS B 386  TRP B 387
SITE     4 BC6 17 HIS B 388  LEU B 391  LEU B 408  VAL B 447
SITE     5 BC6 17 HOH B1119
SITE     1 BC7  5 TYR B  55  GLU B  67  ASN B  68  NAG B 704
SITE     2 BC7  5 HOH B1004
SITE     1 BC8  1 NAG B 703
SITE     1 BC9  9 LEU A 238  GLU B 140  ASN B 144  ARG B 216
SITE     2 BC9  9 NAG B 706  HOH B 802  HOH B 916  HOH B1019
SITE     3 BC9  9 HOH B1117
SITE     1 CC1  3 ARG B 216  NAG B 705  HOH B1091
SITE     1 CC2  6 GLN B 406  ASN B 410  ILE B 413  HOH B 937
SITE     2 CC2  6 HOH B 938  HOH B1125
SITE     1 CC3  5 PRO B 162  ARG B 456  LYS B 459  TYR B 460
SITE     2 CC3  5 HOH B 914
SITE     1 CC4  5 ARG B 240  LYS B 243  GLN B 270  VAL B 271
SITE     2 CC4  5 GLU B 272
SITE     1 CC5  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310
SITE     2 CC5  6 HOH B 857  HOH B1007
SITE     1 CC6  6 LEU A 224  SER B 143  HOH B 867  HOH B 911
SITE     2 CC6  6 HOH B 954  HOH B1093
SITE     1 CC7  7 GLU B 308  ARG B 311  GLU B 339  SER B 566
SITE     2 CC7  7 LEU B 567  ASN B 570  HOH B 854
CRYST1  120.378  132.131  180.438  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      0.008307  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007568  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005542        0.00000
      
PROCHECK
Go to PROCHECK summary
 References