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PDBsum entry 3olt

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3olt
Jmol
Contents
Protein chains
551 a.a.
Ligands
EDO ×14
ACD ×2
COH ×2
NAG-NAG ×2
NAG-NAG-MAN ×2
NAG ×2
BOG
Waters ×513
HEADER    OXIDOREDUCTASE                          26-AUG-10   3OLT
TITLE     X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF R513H MURINE COX-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   8 2;
COMPND   9 EC: 1.14.99.1;
COMPND  10 ENGINEERED: YES;
COMPND  11 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: VIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    MONOTOPIC MEMBRANE PROTEIN, OXIDOREDUCTASE, N-GLYCOSYLATION, MEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI
REVDAT   4   29-JUN-11 3OLT    1       JRNL
REVDAT   3   15-JUN-11 3OLT    1       JRNL
REVDAT   2   20-APR-11 3OLT    1       JRNL
REVDAT   1   13-APR-11 3OLT    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.    2.45 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) : 2.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.86
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -6.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 50659
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) : 0.166
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : 0.219
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2707
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) : 2.45
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3619
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250
REMARK   3   BIN FREE R VALUE SET COUNT          : 210
REMARK   3   BIN FREE R VALUE                    : 0.2930
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8865
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 368
REMARK   3   SOLVENT ATOMS            : 513
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 43.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.81000
REMARK   3    B22 (A**2) : 0.26000
REMARK   3    B33 (A**2) : -1.07000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.647
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9576 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13012 ; 1.663 ; 2.004
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1118 ; 5.511 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   445 ;36.549 ;23.978
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1499 ;15.352 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;14.240 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1382 ; 0.095 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7343 ; 0.006 ; 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):  5537 ; 0.483 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9000 ; 0.957 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4039 ; 1.907 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4000 ; 3.127 ; 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    68
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2587  37.9105  60.2305
REMARK   3    T TENSOR
REMARK   3      T11:    .1025 T22:    .2682
REMARK   3      T33:    .2462 T12:    .0352
REMARK   3      T13:    .0522 T23:    .0252
REMARK   3    L TENSOR
REMARK   3      L11:    .2913 L22:   2.7403
REMARK   3      L33:   1.8461 L12:   -.0510
REMARK   3      L13:    .2958 L23:   -.5812
REMARK   3    S TENSOR
REMARK   3      S11:   -.0132 S12:   -.0751 S13:   -.0261
REMARK   3      S21:    .2399 S22:    .1427 S23:    .0341
REMARK   3      S31:   -.2947 S32:   -.5393 S33:   -.1295
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    69        A    86
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9245  18.8914  63.8880
REMARK   3    T TENSOR
REMARK   3      T11:    .3969 T22:    .4357
REMARK   3      T33:    .5777 T12:   -.1653
REMARK   3      T13:    .1003 T23:    .1154
REMARK   3    L TENSOR
REMARK   3      L11:   6.9124 L22:  11.5213
REMARK   3      L33:   6.0640 L12:  -3.3413
REMARK   3      L13:   6.4102 L23:  -3.6254
REMARK   3    S TENSOR
REMARK   3      S11:    .5237 S12:   -.3755 S13:  -1.1290
REMARK   3      S21:   -.2950 S22:    .4809 S23:    .4427
REMARK   3      S31:    .6631 S32:   -.4985 S33:  -1.0046
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    87        A   122
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2859   3.3433  66.8844
REMARK   3    T TENSOR
REMARK   3      T11:    .0821 T22:    .2061
REMARK   3      T33:    .4136 T12:   -.1030
REMARK   3      T13:    .0096 T23:    .0048
REMARK   3    L TENSOR
REMARK   3      L11:   5.0169 L22:   8.9631
REMARK   3      L33:   9.9967 L12:  -2.8468
REMARK   3      L13:  -2.1625 L23:  -1.6494
REMARK   3    S TENSOR
REMARK   3      S11:   -.2444 S12:   -.0304 S13:   -.1167
REMARK   3      S21:   -.0558 S22:   -.0874 S23:    .5500
REMARK   3      S31:    .3576 S32:   -.4822 S33:    .3318
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   187
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5941  36.3462  67.2177
REMARK   3    T TENSOR
REMARK   3      T11:    .0467 T22:    .0360
REMARK   3      T33:    .0787 T12:    .0227
REMARK   3      T13:    .0213 T23:   -.0139
REMARK   3    L TENSOR
REMARK   3      L11:   1.3529 L22:    .8612
REMARK   3      L33:   4.0944 L12:   -.3741
REMARK   3      L13:   -.3308 L23:   -.2403
REMARK   3    S TENSOR
REMARK   3      S11:   -.0437 S12:   -.1608 S13:    .1290
REMARK   3      S21:    .1490 S22:    .0890 S23:    .0623
REMARK   3      S31:   -.2250 S32:   -.2135 S33:   -.0453
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   188        A   235
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0599  23.1439  66.3626
REMARK   3    T TENSOR
REMARK   3      T11:    .0480 T22:    .0794
REMARK   3      T33:    .0670 T12:   -.0070
REMARK   3      T13:   -.0168 T23:   -.0071
REMARK   3    L TENSOR
REMARK   3      L11:   1.3323 L22:   1.4608
REMARK   3      L33:   1.2220 L12:  -1.2023
REMARK   3      L13:    .1718 L23:   -.4763
REMARK   3    S TENSOR
REMARK   3      S11:   -.0854 S12:   -.1408 S13:    .1217
REMARK   3      S21:    .1066 S22:    .0464 S23:   -.1080
REMARK   3      S31:   -.1929 S32:   -.0076 S33:    .0390
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   236        A   268
REMARK   3    ORIGIN FOR THE GROUP (A):  51.2185  18.9919  55.9593
REMARK   3    T TENSOR
REMARK   3      T11:    .0134 T22:    .0694
REMARK   3      T33:    .1417 T12:   -.0036
REMARK   3      T13:    .0401 T23:    .0110
REMARK   3    L TENSOR
REMARK   3      L11:   3.2951 L22:   1.5221
REMARK   3      L33:   4.9712 L12:    .2219
REMARK   3      L13:   1.7200 L23:   -.5858
REMARK   3    S TENSOR
REMARK   3      S11:    .0376 S12:    .0605 S13:    .0858
REMARK   3      S21:   -.0748 S22:    .0108 S23:   -.1318
REMARK   3      S31:   -.0422 S32:    .4379 S33:   -.0484
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   269        A   346
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8138  16.0818  58.4174
REMARK   3    T TENSOR
REMARK   3      T11:    .0225 T22:    .0977
REMARK   3      T33:    .0921 T12:    .0123
REMARK   3      T13:    .0058 T23:    .0102
REMARK   3    L TENSOR
REMARK   3      L11:   2.0212 L22:   1.2909
REMARK   3      L33:   2.1944 L12:   -.2748
REMARK   3      L13:   -.2433 L23:   -.0917
REMARK   3    S TENSOR
REMARK   3      S11:    .0381 S12:   -.2281 S13:    .1494
REMARK   3      S21:    .0028 S22:   -.0129 S23:   -.1812
REMARK   3      S31:    .0496 S32:    .3853 S33:   -.0252
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   347        A   400
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5126  15.4448  66.2926
REMARK   3    T TENSOR
REMARK   3      T11:    .0415 T22:    .0843
REMARK   3      T33:    .1023 T12:    .0030
REMARK   3      T13:    .0368 T23:    .0462
REMARK   3    L TENSOR
REMARK   3      L11:    .5360 L22:   1.6784
REMARK   3      L33:   2.6071 L12:   -.4302
REMARK   3      L13:    .0608 L23:   -.6303
REMARK   3    S TENSOR
REMARK   3      S11:   -.0429 S12:   -.1737 S13:   -.1932
REMARK   3      S21:    .0723 S22:    .1182 S23:    .2104
REMARK   3      S31:    .1877 S32:   -.0560 S33:   -.0753
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   429
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1345  16.4818  78.5556
REMARK   3    T TENSOR
REMARK   3      T11:    .1342 T22:    .3003
REMARK   3      T33:    .0537 T12:    .0559
REMARK   3      T13:   -.0476 T23:   -.0038
REMARK   3    L TENSOR
REMARK   3      L11:   5.8858 L22:   6.7066
REMARK   3      L33:   4.3121 L12:   1.5642
REMARK   3      L13:    .3991 L23:   2.6372
REMARK   3    S TENSOR
REMARK   3      S11:    .0009 S12:   -.3892 S13:    .1502
REMARK   3      S21:    .3451 S22:   -.0071 S23:   -.1314
REMARK   3      S31:   -.0052 S32:    .5494 S33:    .0062
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   430        A   478
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2339  29.7789  75.9630
REMARK   3    T TENSOR
REMARK   3      T11:    .0833 T22:    .1225
REMARK   3      T33:    .0453 T12:    .0365
REMARK   3      T13:    .0513 T23:   -.0131
REMARK   3    L TENSOR
REMARK   3      L11:   1.6420 L22:   1.5984
REMARK   3      L33:   1.7467 L12:   -.9327
REMARK   3      L13:    .9532 L23:   -.8354
REMARK   3    S TENSOR
REMARK   3      S11:   -.1076 S12:   -.2184 S13:    .0337
REMARK   3      S21:    .1497 S22:    .1245 S23:    .0378
REMARK   3      S31:   -.0646 S32:   -.0508 S33:   -.0169
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   479        A   553
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8696  21.8695  71.1426
REMARK   3    T TENSOR
REMARK   3      T11:    .1215 T22:    .1094
REMARK   3      T33:    .1230 T12:    .0224
REMARK   3      T13:    .0154 T23:    .0552
REMARK   3    L TENSOR
REMARK   3      L11:   1.4487 L22:   1.1565
REMARK   3      L33:   2.7220 L12:   -.8787
REMARK   3      L13:   -.9653 L23:   1.3325
REMARK   3    S TENSOR
REMARK   3      S11:   -.1213 S12:   -.2889 S13:   -.1400
REMARK   3      S21:    .0355 S22:    .0716 S23:    .2076
REMARK   3      S31:    .0115 S32:   -.1066 S33:    .0497
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):  37.6256   3.3713  64.8703
REMARK   3    T TENSOR
REMARK   3      T11:    .1754 T22:    .0430
REMARK   3      T33:    .2468 T12:   -.0289
REMARK   3      T13:    .0287 T23:    .0746
REMARK   3    L TENSOR
REMARK   3      L11:    .9434 L22:   4.1073
REMARK   3      L33:   5.9903 L12:  -1.5262
REMARK   3      L13:   -.2949 L23:    .4745
REMARK   3    S TENSOR
REMARK   3      S11:   -.1062 S12:   -.1087 S13:   -.3677
REMARK   3      S21:    .0746 S22:    .0628 S23:    .2031
REMARK   3      S31:    .7448 S32:   -.2989 S33:    .0434
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):  33.6724   1.7065  33.4817
REMARK   3    T TENSOR
REMARK   3      T11:    .4398 T22:    .0790
REMARK   3      T33:    .2949 T12:    .0571
REMARK   3      T13:   -.0197 T23:   -.0320
REMARK   3    L TENSOR
REMARK   3      L11:   4.8362 L22:    .6528
REMARK   3      L33:   3.8311 L12:    .7354
REMARK   3      L13:  -1.9594 L23:   -.2192
REMARK   3    S TENSOR
REMARK   3      S11:    .1566 S12:    .0660 S13:   -.3241
REMARK   3      S21:   -.2392 S22:   -.0873 S23:   -.0975
REMARK   3      S31:    .6976 S32:    .2175 S33:   -.0693
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    87
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9260   -.2843  28.5472
REMARK   3    T TENSOR
REMARK   3      T11:    .6245 T22:    .3813
REMARK   3      T33:    .6062 T12:   -.1952
REMARK   3      T13:   -.0851 T23:   -.0354
REMARK   3    L TENSOR
REMARK   3      L11:  11.9578 L22:   7.6578
REMARK   3      L33:   1.8878 L12:  -6.7070
REMARK   3      L13:   3.2352 L23:  -2.8362
REMARK   3    S TENSOR
REMARK   3      S11:    .5317 S12:    .2560 S13:   -.5870
REMARK   3      S21:   -.5938 S22:   -.0363 S23:   1.5738
REMARK   3      S31:    .6295 S32:   -.4542 S33:   -.4954
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    88        B   122
REMARK   3    ORIGIN FOR THE GROUP (A):    .9462  18.7312  26.3953
REMARK   3    T TENSOR
REMARK   3      T11:    .2484 T22:    .1827
REMARK   3      T33:    .4317 T12:   -.1946
REMARK   3      T13:   -.0327 T23:   -.0640
REMARK   3    L TENSOR
REMARK   3      L11:   7.4868 L22:   5.3639
REMARK   3      L33:   9.9721 L12:  -3.8662
REMARK   3      L13:  -1.9623 L23:    .5854
REMARK   3    S TENSOR
REMARK   3      S11:   -.0524 S12:    .3009 S13:   -.4402
REMARK   3      S21:   -.1659 S22:   -.1126 S23:    .3235
REMARK   3      S31:    .5124 S32:   -.6884 S33:    .1650
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   148
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8359  18.8339  39.9618
REMARK   3    T TENSOR
REMARK   3      T11:    .0778 T22:    .0219
REMARK   3      T33:    .0471 T12:    .0231
REMARK   3      T13:    .0016 T23:    .0041
REMARK   3    L TENSOR
REMARK   3      L11:   2.9367 L22:   3.3141
REMARK   3      L33:   4.1893 L12:  -2.9609
REMARK   3      L13:   -.7987 L23:   -.3302
REMARK   3    S TENSOR
REMARK   3      S11:    .0304 S12:    .0584 S13:   -.2607
REMARK   3      S21:   -.1256 S22:   -.0498 S23:    .2868
REMARK   3      S31:    .3724 S32:   -.0132 S33:    .0194
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   149        B   227
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3479  27.1332  22.0448
REMARK   3    T TENSOR
REMARK   3      T11:    .0737 T22:    .0829
REMARK   3      T33:    .0852 T12:    .0252
REMARK   3      T13:    .0285 T23:    .0223
REMARK   3    L TENSOR
REMARK   3      L11:   1.0143 L22:   1.6843
REMARK   3      L33:   2.4084 L12:   -.9849
REMARK   3      L13:    .0653 L23:   -.1137
REMARK   3    S TENSOR
REMARK   3      S11:    .1180 S12:    .1653 S13:    .0502
REMARK   3      S21:   -.2099 S22:   -.0879 S23:   -.1499
REMARK   3      S31:    .1558 S32:    .2860 S33:   -.0301
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   228        B   271
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0541  50.9710  38.6910
REMARK   3    T TENSOR
REMARK   3      T11:    .0491 T22:    .0374
REMARK   3      T33:    .1275 T12:   -.0194
REMARK   3      T13:    .0053 T23:    .0417
REMARK   3    L TENSOR
REMARK   3      L11:   1.5355 L22:   5.2101
REMARK   3      L33:   4.1524 L12:   -.4816
REMARK   3      L13:    .6480 L23:   -.7508
REMARK   3    S TENSOR
REMARK   3      S11:    .0004 S12:    .0891 S13:    .3234
REMARK   3      S21:    .2768 S22:   -.0811 S23:   -.3093
REMARK   3      S31:   -.3789 S32:    .2875 S33:    .0807
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   272        B   304
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8997  49.9731  27.5707
REMARK   3    T TENSOR
REMARK   3      T11:    .2596 T22:    .3086
REMARK   3      T33:    .4042 T12:   -.1092
REMARK   3      T13:    .0935 T23:    .0700
REMARK   3    L TENSOR
REMARK   3      L11:   2.4974 L22:   4.3173
REMARK   3      L33:   2.1401 L12:   2.0391
REMARK   3      L13:    .3608 L23:    .5835
REMARK   3    S TENSOR
REMARK   3      S11:   -.1772 S12:    .5312 S13:    .1202
REMARK   3      S21:   -.4773 S22:    .1819 S23:   -.5344
REMARK   3      S31:   -.3838 S32:    .4595 S33:   -.0047
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   305        B   356
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0750  42.1156  38.4256
REMARK   3    T TENSOR
REMARK   3      T11:    .0168 T22:    .0697
REMARK   3      T33:    .1071 T12:    .0244
REMARK   3      T13:   -.0021 T23:    .0448
REMARK   3    L TENSOR
REMARK   3      L11:   1.1604 L22:   2.1427
REMARK   3      L33:   3.4447 L12:   -.3211
REMARK   3      L13:   -.5182 L23:    .5315
REMARK   3    S TENSOR
REMARK   3      S11:   -.0044 S12:    .0855 S13:    .0592
REMARK   3      S21:   -.0398 S22:   -.0587 S23:    .2710
REMARK   3      S31:   -.2247 S32:   -.3145 S33:    .0631
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   389
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9651  24.4764  33.6285
REMARK   3    T TENSOR
REMARK   3      T11:    .0609 T22:    .0193
REMARK   3      T33:    .0818 T12:   -.0099
REMARK   3      T13:   -.0415 T23:   -.0115
REMARK   3    L TENSOR
REMARK   3      L11:   3.3835 L22:   2.0268
REMARK   3      L33:   3.4761 L12:   -.2311
REMARK   3      L13:    .6163 L23:   -.5468
REMARK   3    S TENSOR
REMARK   3      S11:   -.0104 S12:    .0305 S13:   -.1291
REMARK   3      S21:   -.0804 S22:    .0210 S23:    .2765
REMARK   3      S31:    .2303 S32:   -.2372 S33:   -.0106
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   390        B   438
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5194  46.2458  14.2542
REMARK   3    T TENSOR
REMARK   3      T11:    .1794 T22:    .2049
REMARK   3      T33:    .0838 T12:    .0692
REMARK   3      T13:    .0207 T23:    .0906
REMARK   3    L TENSOR
REMARK   3      L11:   1.4512 L22:   7.2583
REMARK   3      L33:   2.3429 L12:   -.5187
REMARK   3      L13:   -.4276 L23:   1.9537
REMARK   3    S TENSOR
REMARK   3      S11:    .2305 S12:    .3778 S13:    .2449
REMARK   3      S21:   -.5630 S22:   -.0395 S23:   -.0997
REMARK   3      S31:   -.3807 S32:    .0371 S33:   -.1911
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   439        B   534
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8198  19.0253  16.6053
REMARK   3    T TENSOR
REMARK   3      T11:    .2548 T22:    .1333
REMARK   3      T33:    .0834 T12:    .0682
REMARK   3      T13:   -.0202 T23:   -.0432
REMARK   3    L TENSOR
REMARK   3      L11:   1.4396 L22:   1.5542
REMARK   3      L33:   2.4203 L12:   -.3917
REMARK   3      L13:    .0959 L23:   -.7135
REMARK   3    S TENSOR
REMARK   3      S11:    .1108 S12:    .2482 S13:   -.1695
REMARK   3      S21:   -.3256 S22:   -.0923 S23:    .1101
REMARK   3      S31:    .4354 S32:   -.0348 S33:   -.0185
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   535        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6605  38.3237  35.9926
REMARK   3    T TENSOR
REMARK   3      T11:    .0117 T22:    .0632
REMARK   3      T33:    .1080 T12:   -.0071
REMARK   3      T13:    .0051 T23:    .0354
REMARK   3    L TENSOR
REMARK   3      L11:   1.5083 L22:   1.6596
REMARK   3      L33:   3.4204 L12:   -.3634
REMARK   3      L13:    .2410 L23:  -1.4048
REMARK   3    S TENSOR
REMARK   3      S11:    .0597 S12:    .1046 S13:   -.0402
REMARK   3      S21:   -.0001 S22:    .1728 S23:    .3029
REMARK   3      S31:    .0372 S32:   -.3617 S33:   -.2325
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 3OLT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB061277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
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) : 0.9780
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   : 53369
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 4.900
REMARK 200  R MERGE                    (I) : 0.09900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.53600
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   (%): 53.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
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       60.57400
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.02400
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.37900
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.57400
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.02400
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.37900
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.57400
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.02400
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.37900
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.57400
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.02400
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.37900
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: 16040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 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     ALA 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     ASN 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     ALA 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     ASN 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     GLN A  54    CD   OE1  NE2
REMARK 470     LYS A  56    CE   NZ
REMARK 470     LEU A  75    CG   CD1  CD2
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     GLU A 170    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 267    CE   NZ
REMARK 470     LYS A 358    CD   CE   NZ
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     LYS A 485    CD   CE   NZ
REMARK 470     LYS A 511    CE   NZ
REMARK 470     LYS A 557    NZ
REMARK 470     LEU B  75    CG   CD1  CD2
REMARK 470     LYS B  79    CD   CE   NZ
REMARK 470     LEU B  80    CD1  CD2
REMARK 470     LEU B  81    CG   CD1  CD2
REMARK 470     LYS B  83    CG   CD   CE   NZ
REMARK 470     LYS B  97    CD   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    CE   NZ
REMARK 470     ASP B 268    CG   OD1  OD2
REMARK 470     GLU B 281    CG   CD   OE1  OE2
REMARK 470     LYS B 358    CE   NZ
REMARK 470     LYS B 405    CD   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   CG   ASN A    68     O5   NAG A   661              2.15
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 531   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A 120      -81.26    -64.33
REMARK 500    SER A 121      -80.81     20.73
REMARK 500    TYR A 122       -3.19    -54.63
REMARK 500    THR A 129      -81.34   -123.58
REMARK 500    ARG A 185      -92.23    -90.34
REMARK 500    TRP A 387       47.15    -88.46
REMARK 500    GLU A 398     -115.89     65.82
REMARK 500    ASN A 410       75.98   -101.00
REMARK 500    SER A 496      -50.31     66.78
REMARK 500    CYS A 575       63.10     39.84
REMARK 500    THR B 129      -87.51   -123.86
REMARK 500    ARG B 185      -93.86    -93.74
REMARK 500    ASP B 249       19.52     59.17
REMARK 500    TRP B 387       48.61    -79.61
REMARK 500    GLU B 398     -121.31     64.83
REMARK 500    SER B 496      -48.22     71.40
REMARK 500    SER B 579     -174.10   -171.89
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 B 753        DISTANCE =  5.24 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 A 621  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 621   NA   88.5
REMARK 620 3 COH A 621   NB   90.4  83.3
REMARK 620 4 COH A 621   NC   91.9 172.6  89.3
REMARK 620 5 COH A 621   ND   85.5  95.7 175.8  91.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH B 619  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 COH B 619   NA   92.5
REMARK 620 3 COH B 619   NB   99.6  89.4
REMARK 620 4 COH B 619   NC   92.9 174.5  90.6
REMARK 620 5 COH B 619   ND   82.4  91.4 177.9  88.5
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 EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
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: 3MDL   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
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: 3OLU   RELATED DB: PDB
DBREF  3OLT A   35   618  UNP    Q05769   PGH2_MOUSE      20    604
DBREF  3OLT B   35   618  UNP    Q05769   PGH2_MOUSE      20    604
SEQADV 3OLT ALA A   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS A  513  UNP  Q05769    ARG   499 ENGINEERED MUTATION
SEQADV 3OLT ALA B   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLT HIS B  513  UNP  Q05769    ARG   499 ENGINEERED MUTATION
SEQRES   1 A  592  ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES   2 A  592  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES   3 A  592  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES   4 A  592  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES   5 A  592  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES   6 A  592  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES   7 A  592  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES   8 A  592  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES   9 A  592  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES  10 A  592  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES  11 A  592  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES  12 A  592  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES  13 A  592  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES  14 A  592  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  15 A  592  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES  16 A  592  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES  17 A  592  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES  18 A  592  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES  19 A  592  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES  20 A  592  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES  21 A  592  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES  22 A  592  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  23 A  592  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES  24 A  592  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES  25 A  592  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES  26 A  592  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES  27 A  592  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES  28 A  592  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES  29 A  592  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES  30 A  592  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES  31 A  592  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES  32 A  592  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES  33 A  592  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES  34 A  592  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES  35 A  592  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES  36 A  592  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES  37 A  592  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES  38 A  592  LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU
SEQRES  39 A  592  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  40 A  592  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES  41 A  592  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES  42 A  592  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES  43 A  592  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES  44 A  592  GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER
SEQRES  45 A  592  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES  46 A  592  LYS ARG ARG SER THR GLU LEU
SEQRES   1 B  592  ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES   2 B  592  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES   3 B  592  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES   4 B  592  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES   5 B  592  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES   6 B  592  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES   7 B  592  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES   8 B  592  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES   9 B  592  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES  10 B  592  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES  11 B  592  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES  12 B  592  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES  13 B  592  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES  14 B  592  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  15 B  592  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES  16 B  592  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES  17 B  592  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES  18 B  592  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES  19 B  592  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES  20 B  592  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES  21 B  592  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES  22 B  592  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  23 B  592  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES  24 B  592  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES  25 B  592  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES  26 B  592  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES  27 B  592  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES  28 B  592  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES  29 B  592  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES  30 B  592  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES  31 B  592  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES  32 B  592  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES  33 B  592  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES  34 B  592  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES  35 B  592  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES  36 B  592  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES  37 B  592  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES  38 B  592  LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU
SEQRES  39 B  592  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  40 B  592  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES  41 B  592  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES  42 B  592  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES  43 B  592  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES  44 B  592  GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER
SEQRES  45 B  592  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES  46 B  592  LYS ARG ARG SER THR GLU LEU
MODRES 3OLT ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3OLT ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3OLT ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3OLT ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3OLT ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3OLT ASN B  144  ASN  GLYCOSYLATION SITE
HET    EDO  A   1       4
HET    EDO  A 619       4
HET    EDO  A   4       4
HET    EDO  A   5       4
HET    EDO  A  12       4
HET    EDO  A  13       4
HET    EDO  A  14       4
HET    ACD  A 620      22
HET    COH  A 621      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    EDO  B   2       4
HET    EDO  B   3       4
HET    EDO  B   6       4
HET    EDO  B   7       4
HET    EDO  B   8       4
HET    EDO  B   9       4
HET    EDO  B  11       4
HET    ACD  B   1      22
HET    COH  B 619      43
HET    NAG  B 661      14
HET    NAG  B 662      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    MAN  B 673      11
HET    NAG  B 681      14
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     ACD ARACHIDONIC ACID
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  EDO    14(C2 H6 O2)
FORMUL  10  ACD    2(C20 H32 O2)
FORMUL  11  COH    2(C34 H32 CO N4 O4)
FORMUL  12  NAG    10(C8 H15 N O6)
FORMUL  13  MAN    2(C6 H12 O6)
FORMUL  15  BOG    C14 H28 O6
FORMUL  28  HOH   *513(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  104  1                                   9
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  HIS B   95  1                                  11
HELIX   35  35 PHE B   96  ILE B  105A 1                                  11
HELIX   36  36 ILE B  105A ARG B  120  1                                  16
HELIX   37  37 SER B  121  ILE B  124  5                                   4
HELIX   38  38 SER B  138  ASN B  144  1                                   7
HELIX   39  39 ASP B  173  LEU B  182  1                                  10
HELIX   40  40 ASN B  195  HIS B  207  1                                  13
HELIX   41  41 LEU B  230  GLY B  235  1                                   6
HELIX   42  42 THR B  237  ARG B  245  1                                   9
HELIX   43  43 THR B  265  GLN B  270  1                                   6
HELIX   44  44 PRO B  280  GLN B  284  5                                   5
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  410  GLY B  418  1                                   9
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  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 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
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 GLN B 255  ILE B 257  0
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   H 2 PHE B 395  ILE B 397  0
SHEET    2   H 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  2.06
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.05
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.08
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.07
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.07
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.06
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.04
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.08
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.36
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.37
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.37
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.37
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.38
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.46
LINK         O4  NAG B 672                 C1  MAN B 673     1555   1555  1.46
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.47
LINK         NE2AHIS A 388                CO   COH A 621     1555   1555  2.29
LINK         NE2 HIS B 388                CO   COH B 619     1555   1555  2.74
LINK         ND2 ASN A  68                 O5  NAG A 661     1555   1555  1.50
LINK         ND2 ASN A 410                 O5  NAG A 681     1555   1555  1.50
LINK         ND2 ASN B  68                 O5  NAG B 661     1555   1555  1.49
LINK         ND2 ASN B 410                 O5  NAG B 681     1555   1555  1.49
LINK         ND2 ASN A 144                 O5  NAG A 671     1555   1555  1.52
CISPEP   1 SER A  126    PRO A  127          0         4.31
CISPEP   2 SER B  126    PRO B  127          0        -0.98
SITE     1 AC1  2 CYS A 159  LYS A 459
SITE     1 AC2  7 HIS A  90  GLN A 192  LEU A 352  SER A 353
SITE     2 AC2  7 ALA A 516  ILE A 517  PHE A 518
SITE     1 AC3  6 PRO A 162  SER A 455  ARG A 456  LYS A 459
SITE     2 AC3  6 TYR A 460  HOH A 755
SITE     1 AC4  1 MAN B 673
SITE     1 AC5  8 HOH A  23  GLU A 308  ARG A 311  GLU A 339
SITE     2 AC5  8 ALA A 562  SER A 566  LEU A 567  ASN A 570
SITE     1 AC6  5 LYS A 251  TYR A 254  ASN A 310  HOH A 653
SITE     2 AC6  5 HOH A 770
SITE     1 AC7  4 ASP A 239  ARG A 240  LYS A 243  GLU A 272
SITE     1 AC8  9 LEU A 117  PHE A 205  VAL A 349  TYR A 355
SITE     2 AC8  9 TYR A 385  VAL A 523  GLY A 526  SER A 530
SITE     3 AC8  9 HOH A 795
SITE     1 AC9 16 ALA A 199  GLN A 203  HIS A 207  PHE A 210
SITE     2 AC9 16 LYS A 211  THR A 212  VAL A 295  ASN A 382
SITE     3 AC9 16 TYR A 385  HIS A 386  HIS A 388  LEU A 391
SITE     4 AC9 16 LEU A 408  VAL A 447  HOH A 783  HOH A 789
SITE     1 BC1  5 PRO A  40  TYR A  55  GLU A  67  ASN A  68
SITE     2 BC1  5 NAG A 662
SITE     1 BC2  2 NAG A 661  HOH A 725
SITE     1 BC3  7 GLU A 140  ASN A 144  TYR A 147  HOH A 632
SITE     2 BC3  7 NAG A 672  HOH A 705  HOH A 737
SITE     1 BC4  4 ARG A 216  NAG A 671  MAN A 673  HOH A 876
SITE     1 BC5  1 NAG A 672
SITE     1 BC6  5 GLN A 406  ASN A 410  ILE A 413  GLU A 416
SITE     2 BC6  5 HOH A 728
SITE     1 BC7 10 GLU A 179  ARG A 184  ARG A 185  ARG A 438
SITE     2 BC7 10 GLU A 486  GLU A 490  GLU B 179  ARG B 184
SITE     3 BC7 10 ARG B 185  GLN B 445
SITE     1 BC8  6 HIS B  90  GLN B 192  LEU B 352  SER B 353
SITE     2 BC8  6 ALA B 516  ILE B 517
SITE     1 BC9  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310
SITE     2 BC9  6 HOH B 744  HOH B 812
SITE     1 CC1  5 PRO B 162  LEU B 171  ARG B 456  TYR B 460
SITE     2 CC1  5 HOH B 628
SITE     1 CC2  5 SER A 548  GLU A 553  MET B  48  LYS B  56
SITE     2 CC2  5 ASP B  58
SITE     1 CC3  8 GLU B 308  ARG B 311  GLU B 339  ALA B 562
SITE     2 CC3  8 SER B 566  LEU B 567  ASN B 570  HOH B 636
SITE     1 CC4  5 LEU A 145  LEU A 224  HOH B  13  SER B 143
SITE     2 CC4  5 HOH B 844
SITE     1 CC5  6 ASP B 239  ARG B 240  LYS B 243  GLN B 270
SITE     2 CC5  6 VAL B 271  GLU B 272
SITE     1 CC6 12 ARG B 120  PHE B 205  PHE B 209  TYR B 355
SITE     2 CC6 12 ILE B 377  PHE B 381  TYR B 385  GLY B 526
SITE     3 CC6 12 ALA B 527  SER B 530  GLY B 533  LEU B 534
SITE     1 CC7 14 ALA B 199  PHE B 200  GLN B 203  HIS B 207
SITE     2 CC7 14 PHE B 210  THR B 212  HIS B 214  VAL B 295
SITE     3 CC7 14 ASN B 382  TYR B 385  HIS B 386  HIS B 388
SITE     4 CC7 14 LEU B 391  GLN B 454
SITE     1 CC8  4 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     1 CC9  2 NAG B 661  HOH B 735
SITE     1 DC1  7 GLU B 140  ASN B 144  ARG B 216  PHE B 220
SITE     2 DC1  7 HOH B 627  HOH B 653  NAG B 672
SITE     1 DC2  4 ARG B 216  NAG B 671  MAN B 673  HOH B 815
SITE     1 DC3  4 EDO A   5  HOH B 656  NAG B 672  HOH B 737
SITE     1 DC4  6 GLN B 406  ASN B 410  SER B 412  ILE B 413
SITE     2 DC4  6 GLU B 416  HOH B 743
CRYST1  121.148  132.048  180.758  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      0.008254  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007573  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005532        0.00000
      
PROCHECK
Go to PROCHECK summary
 References