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PDBsum entry 3mdl

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Oxidoreductase PDB id
3mdl
Jmol
Contents
Protein chains
552 a.a.
Ligands
1AG ×2
AKR ×5
GOL ×3
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG
Waters ×960
HEADER    OXIDOREDUCTASE                          30-MAR-10   3MDL
TITLE     X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL 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 20 TO 599;
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   6 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   7 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   8 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   9 2;
COMPND  10 EC: 1.14.99.1;
COMPND  11 ENGINEERED: YES;
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 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: EXPRESSION;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    COX-2, CYCLOOXYGENASE-2, ENDOCANNABINOID, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI
REVDAT   4   29-JUN-11 3MDL    1       JRNL
REVDAT   3   15-JUN-11 3MDL    1       JRNL
REVDAT   2   20-APR-11 3MDL    1       JRNL
REVDAT   1   13-APR-11 3MDL    0
JRNL        AUTH   A.J.VECCHIO,M.G.MALKOWSKI
JRNL        TITL   THE STRUCTURAL BASIS OF ENDOCANNABINOID OXYGENATION BY
JRNL        TITL 2 CYCLOOXYGENASE-2.
JRNL        REF    J.BIOL.CHEM.                  V. 286 20736 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21489986
JRNL        DOI    10.1074/JBC.M111.230367
REMARK   2
REMARK   2 RESOLUTION.    2.20 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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 67549
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) : 0.168
REMARK   3   R VALUE            (WORKING SET) : 0.165
REMARK   3   FREE R VALUE                     : 0.215
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3597
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) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4546
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.69
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250
REMARK   3   BIN FREE R VALUE SET COUNT          : 229
REMARK   3   BIN FREE R VALUE                    : 0.2850
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8906
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 354
REMARK   3   SOLVENT ATOMS            : 960
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.17
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.02000
REMARK   3    B22 (A**2) : 0.08000
REMARK   3    B33 (A**2) : -0.06000
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): 0.233
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.851
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9605 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13054 ; 1.127 ; 2.008
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1113 ; 5.221 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   446 ;36.597 ;23.946
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1528 ;13.612 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;12.710 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1383 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7363 ; 0.005 ; 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):  5553 ; 0.328 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9014 ; 0.668 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4052 ; 1.288 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4036 ; 2.237 ; 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  : 24
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    67
REMARK   3    ORIGIN FOR THE GROUP (A):    .7944  38.0085  59.2429
REMARK   3    T TENSOR
REMARK   3      T11:    .0502 T22:    .1831
REMARK   3      T33:    .1478 T12:    .0716
REMARK   3      T13:    .0406 T23:    .0688
REMARK   3    L TENSOR
REMARK   3      L11:   1.3400 L22:   2.0080
REMARK   3      L33:   2.7309 L12:   1.2029
REMARK   3      L13:   -.0039 L23:    .3589
REMARK   3    S TENSOR
REMARK   3      S11:   -.0756 S12:   -.0313 S13:    .0838
REMARK   3      S21:    .0391 S22:    .1919 S23:    .2162
REMARK   3      S31:   -.2180 S32:   -.4567 S33:   -.1163
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    68        A    92
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0204  17.3088  66.2660
REMARK   3    T TENSOR
REMARK   3      T11:    .0540 T22:    .2391
REMARK   3      T33:    .3922 T12:   -.0984
REMARK   3      T13:   -.0103 T23:    .1311
REMARK   3    L TENSOR
REMARK   3      L11:   2.4547 L22:   3.9107
REMARK   3      L33:   2.8985 L12:  -3.0199
REMARK   3      L13:   1.8457 L23:  -2.8078
REMARK   3    S TENSOR
REMARK   3      S11:    .0997 S12:   -.2022 S13:   -.6007
REMARK   3      S21:   -.1995 S22:    .4235 S23:    .7528
REMARK   3      S31:    .3053 S32:   -.5686 S33:   -.5232
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    93        A   122
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2919   2.3208  64.7852
REMARK   3    T TENSOR
REMARK   3      T11:    .0893 T22:    .1335
REMARK   3      T33:    .2360 T12:   -.0988
REMARK   3      T13:    .0175 T23:    .0068
REMARK   3    L TENSOR
REMARK   3      L11:   1.9080 L22:   6.4798
REMARK   3      L33:  10.7451 L12:   -.5772
REMARK   3      L13:  -4.0107 L23:  -2.6001
REMARK   3    S TENSOR
REMARK   3      S11:   -.2947 S12:    .2448 S13:   -.2261
REMARK   3      S21:   -.1493 S22:   -.0397 S23:    .2744
REMARK   3      S31:    .7390 S32:   -.5137 S33:    .3344
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 :   A   123        A   186
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5687  36.6243  66.1563
REMARK   3    T TENSOR
REMARK   3      T11:    .0899 T22:    .0835
REMARK   3      T33:    .0946 T12:    .0270
REMARK   3      T13:    .0025 T23:   -.0136
REMARK   3    L TENSOR
REMARK   3      L11:    .4753 L22:    .7346
REMARK   3      L33:   1.4008 L12:   -.1943
REMARK   3      L13:   -.1822 L23:   -.4155
REMARK   3    S TENSOR
REMARK   3      S11:   -.0412 S12:   -.0669 S13:    .0890
REMARK   3      S21:    .1243 S22:    .0996 S23:    .0072
REMARK   3      S31:   -.1350 S32:   -.1004 S33:   -.0584
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 :   A   187        A   233
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4871  23.4280  67.2984
REMARK   3    T TENSOR
REMARK   3      T11:    .0666 T22:    .0686
REMARK   3      T33:    .1096 T12:    .0085
REMARK   3      T13:   -.0134 T23:    .0012
REMARK   3    L TENSOR
REMARK   3      L11:    .8765 L22:    .9814
REMARK   3      L33:   1.4250 L12:   -.7511
REMARK   3      L13:    .5552 L23:   -.6133
REMARK   3    S TENSOR
REMARK   3      S11:   -.0662 S12:   -.0712 S13:    .0880
REMARK   3      S21:    .1178 S22:    .0206 S23:   -.1006
REMARK   3      S31:   -.1383 S32:    .0910 S33:    .0457
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 :   A   234        A   271
REMARK   3    ORIGIN FOR THE GROUP (A):  50.0572  19.5714  56.1051
REMARK   3    T TENSOR
REMARK   3      T11:    .0062 T22:    .0801
REMARK   3      T33:    .1288 T12:    .0062
REMARK   3      T13:    .0143 T23:    .0226
REMARK   3    L TENSOR
REMARK   3      L11:   1.8969 L22:   1.0826
REMARK   3      L33:   2.1309 L12:   -.2838
REMARK   3      L13:    .8569 L23:   -.1573
REMARK   3    S TENSOR
REMARK   3      S11:    .0160 S12:    .0386 S13:    .0728
REMARK   3      S21:   -.0634 S22:   -.0033 S23:   -.0627
REMARK   3      S31:   -.0238 S32:    .2122 S33:   -.0127
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   272        A   320
REMARK   3    ORIGIN FOR THE GROUP (A):  46.2878  18.5955  62.9160
REMARK   3    T TENSOR
REMARK   3      T11:    .0222 T22:    .1037
REMARK   3      T33:    .1302 T12:    .0149
REMARK   3      T13:    .0062 T23:    .0306
REMARK   3    L TENSOR
REMARK   3      L11:   1.4443 L22:    .7709
REMARK   3      L33:   2.9760 L12:    .1286
REMARK   3      L13:   -.0810 L23:    .3696
REMARK   3    S TENSOR
REMARK   3      S11:    .0692 S12:   -.2021 S13:    .1149
REMARK   3      S21:    .0502 S22:   -.0475 S23:   -.0772
REMARK   3      S31:   -.0508 S32:    .1309 S33:   -.0217
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   321        A   400
REMARK   3    ORIGIN FOR THE GROUP (A):  28.7925  13.9973  61.1420
REMARK   3    T TENSOR
REMARK   3      T11:    .0792 T22:    .0600
REMARK   3      T33:    .1130 T12:   -.0022
REMARK   3      T13:   -.0046 T23:    .0259
REMARK   3    L TENSOR
REMARK   3      L11:    .4878 L22:    .4647
REMARK   3      L33:   1.0978 L12:   -.2228
REMARK   3      L13:   -.2892 L23:   -.1502
REMARK   3    S TENSOR
REMARK   3      S11:   -.0580 S12:   -.1021 S13:   -.0903
REMARK   3      S21:    .0320 S22:    .0621 S23:    .0535
REMARK   3      S31:    .1152 S32:    .0213 S33:   -.0041
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   401        A   445
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3672  18.4277  80.0507
REMARK   3    T TENSOR
REMARK   3      T11:    .0898 T22:    .1250
REMARK   3      T33:    .0266 T12:    .0222
REMARK   3      T13:   -.0260 T23:   -.0069
REMARK   3    L TENSOR
REMARK   3      L11:   4.2694 L22:   1.2534
REMARK   3      L33:   1.8958 L12:  -1.1034
REMARK   3      L13:  -1.0576 L23:    .6027
REMARK   3    S TENSOR
REMARK   3      S11:   -.0997 S12:   -.4298 S13:    .0955
REMARK   3      S21:    .1412 S22:    .1617 S23:   -.1657
REMARK   3      S31:   -.0351 S32:    .3632 S33:   -.0620
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   446        A   493
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4115  31.5774  76.8399
REMARK   3    T TENSOR
REMARK   3      T11:    .1036 T22:    .1043
REMARK   3      T33:    .0521 T12:    .0824
REMARK   3      T13:    .0386 T23:    .0026
REMARK   3    L TENSOR
REMARK   3      L11:   1.6548 L22:   1.2491
REMARK   3      L33:   2.2864 L12:    .1235
REMARK   3      L13:    .3674 L23:   -.0355
REMARK   3    S TENSOR
REMARK   3      S11:   -.1204 S12:   -.2340 S13:    .0565
REMARK   3      S21:    .2700 S22:    .1708 S23:    .0889
REMARK   3      S31:   -.0660 S32:   -.2129 S33:   -.0503
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   494        A   553
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4656  20.1759  66.2711
REMARK   3    T TENSOR
REMARK   3      T11:    .0853 T22:    .0577
REMARK   3      T33:    .0873 T12:    .0177
REMARK   3      T13:    .0041 T23:    .0346
REMARK   3    L TENSOR
REMARK   3      L11:    .6801 L22:    .7642
REMARK   3      L33:   1.8301 L12:   -.2860
REMARK   3      L13:   -.5181 L23:    .6076
REMARK   3    S TENSOR
REMARK   3      S11:   -.0415 S12:   -.0921 S13:   -.0966
REMARK   3      S21:    .0166 S22:   -.0091 S23:    .1555
REMARK   3      S31:   -.0327 S32:   -.1495 S33:    .0506
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   554        A   584
REMARK   3    ORIGIN FOR THE GROUP (A):  36.5765   3.5356  64.7406
REMARK   3    T TENSOR
REMARK   3      T11:    .1122 T22:    .0424
REMARK   3      T33:    .1470 T12:   -.0121
REMARK   3      T13:    .0219 T23:    .0491
REMARK   3    L TENSOR
REMARK   3      L11:    .9657 L22:   2.6977
REMARK   3      L33:   3.1549 L12:   -.6403
REMARK   3      L13:   -.1089 L23:    .3619
REMARK   3    S TENSOR
REMARK   3      S11:   -.0314 S12:   -.0447 S13:   -.2121
REMARK   3      S21:    .0883 S22:    .0302 S23:    .0613
REMARK   3      S31:    .4086 S32:   -.0600 S33:    .0012
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    33        B    67
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2325   1.7778  33.5452
REMARK   3    T TENSOR
REMARK   3      T11:    .3001 T22:    .0341
REMARK   3      T33:    .1198 T12:    .0766
REMARK   3      T13:   -.0284 T23:   -.0227
REMARK   3    L TENSOR
REMARK   3      L11:   5.6239 L22:    .4212
REMARK   3      L33:   3.4491 L12:    .8908
REMARK   3      L13:  -1.4505 L23:   -.2316
REMARK   3    S TENSOR
REMARK   3      S11:    .0655 S12:   -.1149 S13:   -.3505
REMARK   3      S21:   -.1938 S22:   -.0749 S23:    .0162
REMARK   3      S31:    .5899 S32:    .2736 S33:    .0094
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    68        B    89
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2421   1.0290  27.2664
REMARK   3    T TENSOR
REMARK   3      T11:    .5001 T22:    .1890
REMARK   3      T33:    .4684 T12:   -.2770
REMARK   3      T13:   -.2410 T23:    .0587
REMARK   3    L TENSOR
REMARK   3      L11:   7.2498 L22:   6.7230
REMARK   3      L33:   5.1094 L12:  -6.7524
REMARK   3      L13:   5.8969 L23:  -5.8608
REMARK   3    S TENSOR
REMARK   3      S11:    .4829 S12:   -.3633 S13:  -1.0806
REMARK   3      S21:   -.8989 S22:    .5669 S23:   1.2027
REMARK   3      S31:    .7744 S32:   -.4925 S33:  -1.0498
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    90        B   122
REMARK   3    ORIGIN FOR THE GROUP (A):    .6869  19.0695  25.9556
REMARK   3    T TENSOR
REMARK   3      T11:    .1695 T22:    .1059
REMARK   3      T33:    .2347 T12:   -.1259
REMARK   3      T13:   -.0247 T23:    .0021
REMARK   3    L TENSOR
REMARK   3      L11:   4.5453 L22:   2.5659
REMARK   3      L33:  10.9226 L12:  -2.4241
REMARK   3      L13:  -1.1575 L23:   2.3546
REMARK   3    S TENSOR
REMARK   3      S11:   -.0683 S12:    .1347 S13:   -.6463
REMARK   3      S21:    .0681 S22:   -.2108 S23:    .3585
REMARK   3      S31:    .7305 S32:   -.6628 S33:    .2791
REMARK   3
REMARK   3   TLS GROUP : 16
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   123        B   188
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1777  19.3525  26.7035
REMARK   3    T TENSOR
REMARK   3      T11:    .1155 T22:    .0686
REMARK   3      T33:    .0858 T12:    .0316
REMARK   3      T13:    .0124 T23:   -.0062
REMARK   3    L TENSOR
REMARK   3      L11:    .6102 L22:    .8508
REMARK   3      L33:   1.7826 L12:   -.2535
REMARK   3      L13:    .1770 L23:   -.3744
REMARK   3    S TENSOR
REMARK   3      S11:    .0781 S12:    .0709 S13:   -.0410
REMARK   3      S21:   -.1489 S22:   -.0737 S23:   -.0455
REMARK   3      S31:    .2752 S32:    .1681 S33:   -.0045
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   189        B   240
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0789  35.8773  29.6002
REMARK   3    T TENSOR
REMARK   3      T11:    .0480 T22:    .1055
REMARK   3      T33:    .1549 T12:   -.0133
REMARK   3      T13:    .0124 T23:    .0218
REMARK   3    L TENSOR
REMARK   3      L11:    .8099 L22:    .8505
REMARK   3      L33:   1.2508 L12:   -.6668
REMARK   3      L13:   -.4511 L23:   -.1713
REMARK   3    S TENSOR
REMARK   3      S11:    .0469 S12:   -.0295 S13:    .1149
REMARK   3      S21:   -.0336 S22:    .0218 S23:   -.1111
REMARK   3      S31:   -.0409 S32:    .0529 S33:   -.0687
REMARK   3
REMARK   3   TLS GROUP : 18
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   241        B   269
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3689  54.8537  37.7259
REMARK   3    T TENSOR
REMARK   3      T11:    .0815 T22:    .0517
REMARK   3      T33:    .1692 T12:   -.0096
REMARK   3      T13:    .0109 T23:    .0639
REMARK   3    L TENSOR
REMARK   3      L11:   1.9447 L22:    .7843
REMARK   3      L33:   3.7267 L12:   -.8438
REMARK   3      L13:   1.2778 L23:   -.7502
REMARK   3    S TENSOR
REMARK   3      S11:   -.0562 S12:    .1563 S13:    .2775
REMARK   3      S21:    .0899 S22:    .0485 S23:    .0400
REMARK   3      S31:   -.4830 S32:    .1929 S33:    .0076
REMARK   3
REMARK   3   TLS GROUP : 19
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   270        B   302
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3137  50.2291  27.9276
REMARK   3    T TENSOR
REMARK   3      T11:    .0944 T22:    .1161
REMARK   3      T33:    .1459 T12:   -.0643
REMARK   3      T13:    .0536 T23:    .0151
REMARK   3    L TENSOR
REMARK   3      L11:   1.9598 L22:   2.6772
REMARK   3      L33:   3.3613 L12:   -.6681
REMARK   3      L13:   -.2478 L23:    .7634
REMARK   3    S TENSOR
REMARK   3      S11:    .1117 S12:   -.0002 S13:    .2110
REMARK   3      S21:   -.2620 S22:    .1198 S23:   -.4331
REMARK   3      S31:   -.4743 S32:    .5014 S33:   -.2315
REMARK   3
REMARK   3   TLS GROUP : 20
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   303        B   356
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9765  42.2065  37.5449
REMARK   3    T TENSOR
REMARK   3      T11:    .0455 T22:    .1059
REMARK   3      T33:    .1281 T12:    .0051
REMARK   3      T13:   -.0061 T23:    .0511
REMARK   3    L TENSOR
REMARK   3      L11:    .9119 L22:   1.1399
REMARK   3      L33:   1.2340 L12:   -.4613
REMARK   3      L13:   -.3528 L23:    .1860
REMARK   3    S TENSOR
REMARK   3      S11:   -.0173 S12:    .0594 S13:    .0433
REMARK   3      S21:   -.0043 S22:    .0108 S23:    .0892
REMARK   3      S31:   -.1071 S32:   -.2186 S33:    .0065
REMARK   3
REMARK   3   TLS GROUP : 21
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   357        B   401
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2266  29.3741  27.4792
REMARK   3    T TENSOR
REMARK   3      T11:    .0791 T22:    .0553
REMARK   3      T33:    .0994 T12:   -.0156
REMARK   3      T13:   -.0243 T23:   -.0145
REMARK   3    L TENSOR
REMARK   3      L11:   1.0305 L22:   1.1974
REMARK   3      L33:   1.9369 L12:    .0476
REMARK   3      L13:   -.2169 L23:   -.6741
REMARK   3    S TENSOR
REMARK   3      S11:    .0912 S12:    .1227 S13:   -.0536
REMARK   3      S21:   -.2037 S22:   -.0183 S23:    .1385
REMARK   3      S31:    .1031 S32:   -.0519 S33:   -.0729
REMARK   3
REMARK   3   TLS GROUP : 22
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   402        B   429
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8147  50.1267  15.9849
REMARK   3    T TENSOR
REMARK   3      T11:    .0699 T22:    .0974
REMARK   3      T33:    .0647 T12:    .0240
REMARK   3      T13:    .0369 T23:    .0708
REMARK   3    L TENSOR
REMARK   3      L11:   4.0160 L22:   4.3384
REMARK   3      L33:   2.6874 L12:    .5910
REMARK   3      L13:   -.1458 L23:    .0690
REMARK   3    S TENSOR
REMARK   3      S11:    .1647 S12:    .2772 S13:    .0807
REMARK   3      S21:   -.2764 S22:   -.0502 S23:   -.1552
REMARK   3      S31:   -.3419 S32:    .0203 S33:   -.1144
REMARK   3
REMARK   3   TLS GROUP : 23
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   430        B   531
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4801  19.6962  15.5314
REMARK   3    T TENSOR
REMARK   3      T11:    .1354 T22:    .0635
REMARK   3      T33:    .0256 T12:    .0265
REMARK   3      T13:   -.0068 T23:   -.0277
REMARK   3    L TENSOR
REMARK   3      L11:    .8835 L22:    .9511
REMARK   3      L33:   1.4713 L12:   -.3682
REMARK   3      L13:    .3625 L23:   -.4187
REMARK   3    S TENSOR
REMARK   3      S11:    .0908 S12:    .1966 S13:   -.0656
REMARK   3      S21:   -.2084 S22:   -.0604 S23:    .0366
REMARK   3      S31:    .2885 S32:    .0154 S33:   -.0304
REMARK   3
REMARK   3   TLS GROUP : 24
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   532        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9097  37.4845  35.3803
REMARK   3    T TENSOR
REMARK   3      T11:    .0087 T22:    .1082
REMARK   3      T33:    .1244 T12:   -.0172
REMARK   3      T13:   -.0062 T23:    .0349
REMARK   3    L TENSOR
REMARK   3      L11:   1.3650 L22:    .8816
REMARK   3      L33:   2.2849 L12:   -.2126
REMARK   3      L13:   -.2127 L23:   -.8053
REMARK   3    S TENSOR
REMARK   3      S11:    .0289 S12:    .0541 S13:    .0187
REMARK   3      S21:   -.0354 S22:    .0743 S23:    .1227
REMARK   3      S31:    .0559 S32:   -.2624 S33:   -.1031
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3MDL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058413.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-07
REMARK 200  TEMPERATURE           (KELVIN) : 77
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) : 0.9777
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING 5.05
REMARK 200                                   ASYMMETRIC CUT 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   : 67549
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
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     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 4.500
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.41700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.800
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   (%): 52.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID SODIUM SALT,
REMARK 280  0.1M HEPES PH 7.5, 0.02M MAGNESIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, 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       59.47900
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.88650
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.92900
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.47900
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.88650
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.92900
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.47900
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.88650
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.92900
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.47900
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.88650
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.92900
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 300 REMARK: ASYMMETRIC UNIT CONTAINS THE COX-2 BIOLOGICAL DIMER.
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: 11490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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     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     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     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 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     LEU A  75    CG   CD1  CD2
REMARK 470     GLU A 170    OE1  OE2
REMARK 470     LYS A 215    CD   CE   NZ
REMARK 470     ASP A 239    OD1  OD2
REMARK 470     LYS A 358    CE   NZ
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     LYS A 557    NZ
REMARK 470     GLN A 583    CD   OE1  NE2
REMARK 470     LEU B  75    CG   CD1  CD2
REMARK 470     LEU B  81    CD1  CD2
REMARK 470     LYS B  83    CD   CE   NZ
REMARK 470     LYS B  97    CE   NZ
REMARK 470     GLU B 170    OE1  OE2
REMARK 470     LYS B 175    NZ
REMARK 470     GLU B 186    CD   OE1  OE2
REMARK 470     LYS B 215    NZ
REMARK 470     LYS B 267    CG   CD   CE   NZ
REMARK 470     ASP B 268    CG   OD1  OD2
REMARK 470     LYS B 358    NZ
REMARK 470     LYS B 405    CD   CE   NZ
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 B 531   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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       17.31     57.18
REMARK 500    THR A 129      -92.82   -119.23
REMARK 500    ASP A 249       19.71     58.29
REMARK 500    GLU A 398     -118.64     56.01
REMARK 500    ASN A 439       15.61   -145.74
REMARK 500    SER A 496      -40.35     70.37
REMARK 500    CYS A 575       64.16     39.33
REMARK 500    THR B 129      -91.87   -119.01
REMARK 500    ARG B 185      -92.27    -94.18
REMARK 500    GLU B 398     -120.00     57.12
REMARK 500    SER B 496      -51.06     74.47
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 A 830        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A 929        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH A 952        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A1022        DISTANCE =  7.72 ANGSTROMS
REMARK 525    HOH A1023        DISTANCE =  7.22 ANGSTROMS
REMARK 525    HOH A1076        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH B 634        DISTANCE =  5.92 ANGSTROMS
REMARK 525    HOH B 647        DISTANCE =  6.63 ANGSTROMS
REMARK 525    HOH B 740        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH B 836        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH B 872        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH B 917        DISTANCE =  5.76 ANGSTROMS
REMARK 525    HOH B 951        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH B 990        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH B 991        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH B 994        DISTANCE =  5.52 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 615  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 COH B 615   NA   92.2
REMARK 620 3 COH B 615   NB   91.6  87.3
REMARK 620 4 COH B 615   NC   92.2 174.8  89.8
REMARK 620 5 COH B 615   ND   90.2  89.0 175.9  93.8
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH A 614  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 614   NA   92.4
REMARK 620 3 COH A 614   NB   81.7  86.7
REMARK 620 4 COH A 614   NC   89.3 176.0  89.9
REMARK 620 5 COH A 614   ND   97.6  90.7 177.3  92.7
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 1AG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3KRK   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF L531F MURINE COX-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF PGHS-1
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF COX-2
DBREF  3MDL A   35   613  UNP    Q05769   PGH2_MOUSE      20    599
DBREF  3MDL B   35   613  UNP    Q05769   PGH2_MOUSE      20    599
SEQADV 3MDL ASN A   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL ALA A  594  UNP  Q05769    ASN   580 ENGINEERED
SEQADV 3MDL ASN B   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3MDL ALA B  594  UNP  Q05769    ASN   580 ENGINEERED
SEQRES   1 A  587  ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES   2 A  587  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES   3 A  587  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES   4 A  587  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES   5 A  587  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES   6 A  587  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES   7 A  587  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES   8 A  587  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES   9 A  587  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES  10 A  587  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES  11 A  587  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES  12 A  587  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES  13 A  587  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES  14 A  587  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  15 A  587  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES  16 A  587  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES  17 A  587  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES  18 A  587  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES  19 A  587  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES  20 A  587  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES  21 A  587  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES  22 A  587  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  23 A  587  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES  24 A  587  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES  25 A  587  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES  26 A  587  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES  27 A  587  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES  28 A  587  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES  29 A  587  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES  30 A  587  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES  31 A  587  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES  32 A  587  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES  33 A  587  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES  34 A  587  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES  35 A  587  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES  36 A  587  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES  37 A  587  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES  38 A  587  LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU
SEQRES  39 A  587  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  40 A  587  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES  41 A  587  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES  42 A  587  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES  43 A  587  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES  44 A  587  GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER
SEQRES  45 A  587  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES  46 A  587  LYS ARG
SEQRES   1 B  587  ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES   2 B  587  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES   3 B  587  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES   4 B  587  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES   5 B  587  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES   6 B  587  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES   7 B  587  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES   8 B  587  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES   9 B  587  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES  10 B  587  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES  11 B  587  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES  12 B  587  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES  13 B  587  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES  14 B  587  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  15 B  587  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES  16 B  587  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES  17 B  587  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES  18 B  587  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES  19 B  587  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES  20 B  587  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES  21 B  587  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES  22 B  587  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  23 B  587  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES  24 B  587  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES  25 B  587  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES  26 B  587  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES  27 B  587  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES  28 B  587  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES  29 B  587  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES  30 B  587  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES  31 B  587  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES  32 B  587  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES  33 B  587  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES  34 B  587  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES  35 B  587  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES  36 B  587  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES  37 B  587  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES  38 B  587  LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU
SEQRES  39 B  587  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  40 B  587  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES  41 B  587  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES  42 B  587  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES  43 B  587  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES  44 B  587  GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER
SEQRES  45 B  587  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES  46 B  587  LYS ARG
MODRES 3MDL ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3MDL ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3MDL ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3MDL ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3MDL ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3MDL ASN B  410  ASN  GLYCOSYLATION SITE
HET    1AG  A   1      27
HET    AKR  A   2       5
HET    AKR  A   3       5
HET    GOL  A   4       6
HET    COH  A 614      43
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    NAG  A 681      14
HET    BOG  A 703      20
HET    GOL  B   7       6
HET    1AG  B   1      27
HET    AKR  B   3       5
HET    AKR  B   4       5
HET    AKR  B   5       5
HET    GOL  B   6       6
HET    COH  B 615      43
HET    NAG  B 661      14
HET    NAG  B 662      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 681      14
HETNAM     1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,
HETNAM   2 1AG  14-TETRAENOATE
HETNAM     AKR ACRYLIC ACID
HETNAM     GOL GLYCEROL
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  1AG    2(C23 H38 O4)
FORMUL   4  AKR    5(C3 H4 O2)
FORMUL   6  GOL    3(C3 H8 O3)
FORMUL   7  COH    2(C34 H32 CO N4 O4)
FORMUL   8  NAG    10(C8 H15 N O6)
FORMUL   9  MAN    C6 H12 O6
FORMUL  11  BOG    C14 H28 O6
FORMUL  22  HOH   *960(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  ILE A  105A 1                                  11
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  295  HIS A  320  1                                  26
HELIX   13  13 GLY A  324  ASP A  347  1                                  24
HELIX   14  14 ASP A  347  GLY A  354  1                                   8
HELIX   15  15 ASP A  362  PHE A  367  5                                   6
HELIX   16  16 ALA A  378  TYR A  385  1                                   8
HELIX   17  17 TRP A  387  LEU A  391  5                                   5
HELIX   18  18 SER A  403  LEU A  408  1                                   6
HELIX   19  19 ASN A  410  GLN A  429  1                                  20
HELIX   20  20 PRO A  441  ALA A  443  5                                   3
HELIX   21  21 VAL A  444  MET A  458  1                                  15
HELIX   22  22 SER A  462  PHE A  470  1                                   9
HELIX   23  23 SER A  477  GLY A  483  1                                   7
HELIX   24  24 LYS A  485  SER A  496  1                                  12
HELIX   25  25 ASP A  497  MET A  501  5                                   5
HELIX   26  26 GLU A  502  GLU A  510  1                                   9
HELIX   27  27 GLY A  519  GLY A  536  1                                  18
HELIX   28  28 ASN A  537  SER A  541  5                                   5
HELIX   29  29 LYS A  546  GLY A  551  5                                   6
HELIX   30  30 GLY A  552  THR A  561  1                                  10
HELIX   31  31 SER A  563  VAL A  572  1                                  10
HELIX   32  32 GLU B   73  LYS B   83  1                                  11
HELIX   33  33 THR B   85  HIS B   95  1                                  11
HELIX   34  34 PHE B   96  ASN B  104  1                                   9
HELIX   35  35 ILE B  105A TYR B  122  1                                  18
HELIX   36  36 SER B  138  ASN B  144  1                                   7
HELIX   37  37 ASP B  173  LEU B  182  1                                  10
HELIX   38  38 ASN B  195  HIS B  207  1                                  13
HELIX   39  39 LEU B  230  GLY B  235  1                                   6
HELIX   40  40 THR B  237  ARG B  245  1                                   9
HELIX   41  41 THR B  265  GLN B  270  1                                   6
HELIX   42  42 PRO B  280  GLN B  284  5                                   5
HELIX   43  43 VAL B  291  LEU B  294  5                                   4
HELIX   44  44 VAL B  295  HIS B  320  1                                  26
HELIX   45  45 GLY B  324  ASP B  347  1                                  24
HELIX   46  46 ASP B  347  GLY B  354  1                                   8
HELIX   47  47 ASP B  362  PHE B  367  5                                   6
HELIX   48  48 ALA B  378  TYR B  385  1                                   8
HELIX   49  49 HIS B  386  LEU B  391  5                                   6
HELIX   50  50 SER B  403  LEU B  408  1                                   6
HELIX   51  51 ASN B  411  GLN B  429  1                                  19
HELIX   52  52 PRO B  441  ALA B  443  5                                   3
HELIX   53  53 VAL B  444  MET B  458  1                                  15
HELIX   54  54 SER B  462  PHE B  470  1                                   9
HELIX   55  55 SER B  477  GLY B  483  1                                   7
HELIX   56  56 LYS B  485  SER B  496  1                                  12
HELIX   57  57 ASP B  497  MET B  501  5                                   5
HELIX   58  58 GLU B  502  GLU B  510  1                                   9
HELIX   59  59 GLY B  519  GLY B  536  1                                  18
HELIX   60  60 ASN B  537  SER B  541  5                                   5
HELIX   61  61 LYS B  546  GLY B  551  5                                   6
HELIX   62  62 GLY B  552  THR B  561  1                                  10
HELIX   63  63 SER B  563  VAL B  572  1                                  10
SHEET    1   A 2 GLU A  46  SER A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46
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 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130
SHEET    1   D 2 GLN A 255  ILE A 257  0
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   E 2 PHE A 395  ILE A 397  0
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   F 2 GLU B  46  SER B  49  0
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46
SHEET    1   G 2 PHE B  64  TYR B  65  0
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   H 2 TYR B 130  ASN B 131  0
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   I 2 GLN B 255  ILE B 257  0
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   J 2 PHE B 395  ILE B 397  0
SHEET    2   J 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  2.05
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.05
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.02
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.44
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.45
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46
LINK         NE2AHIS B 388                CO   COH B 615     1555   1555  2.27
LINK         NE2AHIS A 388                CO   COH A 614     1555   1555  2.27
CISPEP   1 SER A  126    PRO A  127          0         1.86
CISPEP   2 SER B  126    PRO B  127          0         1.00
SITE     1 AC1 20 VAL A 116  ARG A 120  PHE A 205  TYR A 348
SITE     2 AC1 20 VAL A 349  LEU A 352  SER A 353  TYR A 355
SITE     3 AC1 20 PHE A 381  TYR A 385  TRP A 387  PHE A 518
SITE     4 AC1 20 MET A 522  VAL A 523  GLY A 526  ALA A 527
SITE     5 AC1 20 SER A 530  LEU A 531  LEU A 534  HOH A1034
SITE     1 AC2  3 SER A 477  PHE A 478  GLU A 479
SITE     1 AC3  5 ARG A 240  LYS A 243  VAL A 271  GLU A 272
SITE     2 AC3  5 HOH A 846
SITE     1 AC4 10 HIS A  34  CYS A  36  CYS A  37  PRO A 154
SITE     2 AC4 10 VAL A 155  ALA A 156  CYS A 159  HOH A 676
SITE     3 AC4 10 HOH A 687  HOH A 968
SITE     1 AC5 17 ALA A 199  PHE A 200  ALA A 202  GLN A 203
SITE     2 AC5 17 HIS A 207  PHE A 210  LYS A 211  THR A 212
SITE     3 AC5 17 HIS A 214  VAL A 295  ASN A 382  TYR A 385
SITE     4 AC5 17 HIS A 386  HIS A 388  LEU A 391  HOH A 853
SITE     5 AC5 17 HOH A1090
SITE     1 AC6  5 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 AC6  5 HOH A 792
SITE     1 AC7  1 NAG A 661
SITE     1 AC8  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC8  9 PHE A 220  HOH A 666  NAG A 672  HOH A 994
SITE     3 AC8  9 HOH A 998
SITE     1 AC9  3 ARG A 216  NAG A 671  MAN A 673
SITE     1 BC1  4 NAG A 672  HOH A 930  HOH A1027  HOH A1065
SITE     1 BC2  6 GLN A 406  ASN A 410  SER A 412  ILE A 413
SITE     2 BC2  6 GLU A 416  HOH A 932
SITE     1 BC3 12 LYS A 180  ARG A 184  ARG A 185  ARG A 438
SITE     2 BC3 12 ILE A 442  GLU A 486  GLU A 490  GLU B 179
SITE     3 BC3 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445
SITE     1 BC4  5 GLN A 543  ARG B  44  ARG B  61  HOH B 683
SITE     2 BC4  5 HOH B1141
SITE     1 BC5 15 VAL B 116  PHE B 205  PHE B 209  VAL B 349
SITE     2 BC5 15 TYR B 355  ILE B 377  PHE B 381  TYR B 385
SITE     3 BC5 15 VAL B 523  ALA B 527  SER B 530  LEU B 531
SITE     4 BC5 15 GLY B 533  LEU B 534  HOH B 630
SITE     1 BC6  4 SER B 477  PHE B 478  GLU B 479  LYS B 492
SITE     1 BC7  4 ASP B 239  ARG B 240  LYS B 243  GLU B 272
SITE     1 BC8  1 ASN B  87
SITE     1 BC9  9 HIS B  34  CYS B  36  CYS B  37  PRO B 154
SITE     2 BC9  9 ALA B 156  HOH B 762  HOH B 964  HOH B 995
SITE     3 BC9  9 HOH B1106
SITE     1 CC1 16 ALA B 199  PHE B 200  ALA B 202  GLN B 203
SITE     2 CC1 16 HIS B 207  PHE B 210  LYS B 211  THR B 212
SITE     3 CC1 16 VAL B 295  ASN B 382  TYR B 385  HIS B 386
SITE     4 CC1 16 HIS B 388  LEU B 391  GLN B 454  HOH B 743
SITE     1 CC2  5 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     2 CC2  5 HOH B 803
SITE     1 CC3  1 NAG B 661
SITE     1 CC4  8 GLU B 140  ASN B 144  TYR B 147  ARG B 216
SITE     2 CC4  8 HOH B 625  NAG B 672  HOH B 697  HOH B 922
SITE     1 CC5  4 ARG B 216  NAG B 671  HOH B 906  HOH B1020
SITE     1 CC6  5 GLN B 406  ASN B 410  ILE B 413  HOH B 676
SITE     2 CC6  5 HOH B1096
CRYST1  118.958  131.773  179.858  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      0.008406  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007589  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005560        0.00000
      
PROCHECK
Go to PROCHECK summary
 References