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PDBsum entry 3olu

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3olu
Jmol
Contents
Protein chains
551 a.a.
Ligands
EDO ×14
1AG ×2
COH ×2
NAG-NAG ×2
NAG-NAG-MAN ×2
NAG ×2
BOG
Waters ×666
HEADER    OXIDOREDUCTASE                          26-AUG-10   3OLU
TITLE     X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL 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 3OLU    1       JRNL
REVDAT   3   15-JUN-11 3OLU    1       JRNL
REVDAT   2   20-APR-11 3OLU    1       JRNL
REVDAT   1   13-APR-11 3OLU    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.    2.35 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) : 2.35
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -6.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 56810
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) : 0.164
REMARK   3   R VALUE            (WORKING SET) : 0.162
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3024
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) : 2.35
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4092
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050
REMARK   3   BIN FREE R VALUE SET COUNT          : 213
REMARK   3   BIN FREE R VALUE                    : 0.2490
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8864
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 378
REMARK   3   SOLVENT ATOMS            : 666
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.13
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.59000
REMARK   3    B22 (A**2) : 0.31000
REMARK   3    B33 (A**2) : -0.90000
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): 0.214
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.588
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9577 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13010 ; 1.686 ; 2.005
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1116 ; 5.593 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   443 ;36.572 ;23.973
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1500 ;15.022 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;14.231 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1384 ; 0.097 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7330 ; 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):  5534 ; 0.484 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8995 ; 0.947 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4043 ; 1.922 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4004 ; 3.154 ; 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):   1.3614  37.6811  60.0257
REMARK   3    T TENSOR
REMARK   3      T11:    .0862 T22:    .2777
REMARK   3      T33:    .1911 T12:    .0357
REMARK   3      T13:    .0424 T23:    .0463
REMARK   3    L TENSOR
REMARK   3      L11:    .7509 L22:   4.7279
REMARK   3      L33:   1.9305 L12:   1.2304
REMARK   3      L13:    .2958 L23:    .6976
REMARK   3    S TENSOR
REMARK   3      S11:   -.0338 S12:   -.2056 S13:    .0818
REMARK   3      S21:    .0117 S22:    .0574 S23:    .3388
REMARK   3      S31:   -.1328 S32:   -.2671 S33:   -.0236
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    87
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1392  18.5827  64.2743
REMARK   3    T TENSOR
REMARK   3      T11:    .3094 T22:    .4607
REMARK   3      T33:    .5978 T12:   -.1152
REMARK   3      T13:    .0446 T23:    .1921
REMARK   3    L TENSOR
REMARK   3      L11:   8.5129 L22:   8.8648
REMARK   3      L33:   4.0646 L12:  -1.5016
REMARK   3      L13:   4.3088 L23:  -1.3940
REMARK   3    S TENSOR
REMARK   3      S11:    .4999 S12:   -.6573 S13:  -1.5543
REMARK   3      S21:    .2194 S22:    .3481 S23:    .2391
REMARK   3      S31:    .8190 S32:   -.6551 S33:   -.8480
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    88        A   122
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5023   3.0380  66.2726
REMARK   3    T TENSOR
REMARK   3      T11:    .1395 T22:    .2519
REMARK   3      T33:    .3979 T12:   -.0761
REMARK   3      T13:    .0174 T23:   -.0001
REMARK   3    L TENSOR
REMARK   3      L11:   4.4499 L22:   7.0282
REMARK   3      L33:   9.6039 L12:   -.7632
REMARK   3      L13:  -2.4837 L23:    .0533
REMARK   3    S TENSOR
REMARK   3      S11:   -.3104 S12:    .0661 S13:   -.2207
REMARK   3      S21:    .0010 S22:   -.0914 S23:    .6362
REMARK   3      S31:    .3721 S32:   -.4329 S33:    .4018
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   148
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3721  33.7485  53.8737
REMARK   3    T TENSOR
REMARK   3      T11:    .0199 T22:    .0257
REMARK   3      T33:    .0421 T12:    .0087
REMARK   3      T13:    .0051 T23:    .0044
REMARK   3    L TENSOR
REMARK   3      L11:   2.5296 L22:   4.0309
REMARK   3      L33:   4.4712 L12:   -.6903
REMARK   3      L13:   1.0571 L23:  -1.0124
REMARK   3    S TENSOR
REMARK   3      S11:   -.0856 S12:   -.0853 S13:   -.1437
REMARK   3      S21:   -.0001 S22:    .0546 S23:    .1835
REMARK   3      S31:    .1472 S32:   -.1654 S33:    .0310
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   149        A   233
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4715  29.8675  71.0404
REMARK   3    T TENSOR
REMARK   3      T11:    .0659 T22:    .0447
REMARK   3      T33:    .0625 T12:    .0001
REMARK   3      T13:   -.0075 T23:   -.0223
REMARK   3    L TENSOR
REMARK   3      L11:   1.5428 L22:   1.1306
REMARK   3      L33:   1.2993 L12:   -.9024
REMARK   3      L13:   -.0665 L23:   -.0230
REMARK   3    S TENSOR
REMARK   3      S11:   -.0566 S12:   -.2152 S13:    .1574
REMARK   3      S21:    .1477 S22:    .0875 S23:   -.0865
REMARK   3      S31:   -.1715 S32:    .0050 S33:   -.0309
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   268
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6000  18.9340  55.6582
REMARK   3    T TENSOR
REMARK   3      T11:    .0091 T22:    .0354
REMARK   3      T33:    .1469 T12:   -.0008
REMARK   3      T13:    .0336 T23:   -.0002
REMARK   3    L TENSOR
REMARK   3      L11:   3.2463 L22:    .7350
REMARK   3      L33:   5.1889 L12:    .1403
REMARK   3      L13:   1.0979 L23:   -.2700
REMARK   3    S TENSOR
REMARK   3      S11:    .0007 S12:    .0147 S13:    .2473
REMARK   3      S21:   -.0579 S22:   -.0060 S23:   -.1701
REMARK   3      S31:   -.0093 S32:    .3084 S33:    .0053
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   301
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4741  25.8712  65.9961
REMARK   3    T TENSOR
REMARK   3      T11:    .0951 T22:    .1726
REMARK   3      T33:    .2843 T12:    .0061
REMARK   3      T13:    .0103 T23:   -.0875
REMARK   3    L TENSOR
REMARK   3      L11:   5.9029 L22:   1.9913
REMARK   3      L33:   4.8805 L12:   1.0328
REMARK   3      L13:   -.9476 L23:  -2.7585
REMARK   3    S TENSOR
REMARK   3      S11:   -.0349 S12:   -.4222 S13:    .7273
REMARK   3      S21:    .0828 S22:   -.1144 S23:   -.2686
REMARK   3      S31:   -.2369 S32:    .3877 S33:    .1493
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   302        A   344
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3820   9.3251  52.2909
REMARK   3    T TENSOR
REMARK   3      T11:    .0879 T22:    .0404
REMARK   3      T33:    .1041 T12:    .0458
REMARK   3      T13:    .0163 T23:    .0403
REMARK   3    L TENSOR
REMARK   3      L11:   1.0726 L22:   1.2402
REMARK   3      L33:   3.7371 L12:   -.7634
REMARK   3      L13:    .1344 L23:   -.2964
REMARK   3    S TENSOR
REMARK   3      S11:    .0523 S12:   -.0332 S13:   -.2003
REMARK   3      S21:   -.2426 S22:   -.1077 S23:   -.0189
REMARK   3      S31:    .2505 S32:    .2746 S33:    .0554
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   345        A   399
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1736  15.0791  65.3407
REMARK   3    T TENSOR
REMARK   3      T11:    .0403 T22:    .0661
REMARK   3      T33:    .1018 T12:    .0008
REMARK   3      T13:    .0380 T23:    .0406
REMARK   3    L TENSOR
REMARK   3      L11:    .8467 L22:   1.1479
REMARK   3      L33:   2.2561 L12:   -.5718
REMARK   3      L13:    .1558 L23:   -.4708
REMARK   3    S TENSOR
REMARK   3      S11:   -.0346 S12:   -.1533 S13:   -.1180
REMARK   3      S21:    .0595 S22:    .0732 S23:    .1644
REMARK   3      S31:    .2160 S32:   -.1295 S33:   -.0386
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   400        A   429
REMARK   3    ORIGIN FOR THE GROUP (A):  47.3081  16.2265  78.4138
REMARK   3    T TENSOR
REMARK   3      T11:    .1255 T22:    .2286
REMARK   3      T33:    .0964 T12:    .0442
REMARK   3      T13:   -.0259 T23:    .0036
REMARK   3    L TENSOR
REMARK   3      L11:   5.5646 L22:   5.6060
REMARK   3      L33:   3.1686 L12:   2.0761
REMARK   3      L13:    .2477 L23:   2.3191
REMARK   3    S TENSOR
REMARK   3      S11:   -.0246 S12:   -.4605 S13:    .0587
REMARK   3      S21:    .4013 S22:    .0660 S23:   -.1657
REMARK   3      S31:   -.0360 S32:    .4118 S33:   -.0414
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   430        A   553
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5427  24.8996  72.7338
REMARK   3    T TENSOR
REMARK   3      T11:    .0802 T22:    .1285
REMARK   3      T33:    .0705 T12:    .0189
REMARK   3      T13:    .0280 T23:    .0362
REMARK   3    L TENSOR
REMARK   3      L11:    .9894 L22:    .9583
REMARK   3      L33:   1.0838 L12:   -.6586
REMARK   3      L13:   -.3815 L23:    .3450
REMARK   3    S TENSOR
REMARK   3      S11:   -.0668 S12:   -.2483 S13:   -.0645
REMARK   3      S21:    .1173 S22:    .0956 S23:    .1097
REMARK   3      S31:   -.0113 S32:   -.1357 S33:   -.0288
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   583
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9024   3.3220  64.0081
REMARK   3    T TENSOR
REMARK   3      T11:    .1518 T22:    .0286
REMARK   3      T33:    .1407 T12:   -.0434
REMARK   3      T13:    .0013 T23:    .0424
REMARK   3    L TENSOR
REMARK   3      L11:   2.1016 L22:   2.3949
REMARK   3      L33:   4.1812 L12:  -1.5448
REMARK   3      L13:   -.8540 L23:    .1440
REMARK   3    S TENSOR
REMARK   3      S11:   -.0147 S12:   -.1321 S13:   -.2621
REMARK   3      S21:    .0511 S22:    .1118 S23:    .1568
REMARK   3      S31:    .5691 S32:   -.1922 S33:   -.0971
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):  33.7671   1.6954  33.1921
REMARK   3    T TENSOR
REMARK   3      T11:    .4075 T22:    .1384
REMARK   3      T33:    .1827 T12:    .0604
REMARK   3      T13:   -.0447 T23:   -.0372
REMARK   3    L TENSOR
REMARK   3      L11:   4.5350 L22:    .8695
REMARK   3      L33:   2.5786 L12:    .5646
REMARK   3      L13:  -1.4207 L23:   -.5141
REMARK   3    S TENSOR
REMARK   3      S11:    .1678 S12:    .0540 S13:   -.2489
REMARK   3      S21:   -.2633 S22:   -.1716 S23:    .0210
REMARK   3      S31:    .5233 S32:    .1958 S33:    .0038
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):  15.1809   -.4239  28.2809
REMARK   3    T TENSOR
REMARK   3      T11:    .6101 T22:    .3955
REMARK   3      T33:    .5815 T12:   -.1258
REMARK   3      T13:   -.1173 T23:   -.0877
REMARK   3    L TENSOR
REMARK   3      L11:  10.6495 L22:   5.3282
REMARK   3      L33:   2.6176 L12:  -4.6137
REMARK   3      L13:   2.3030 L23:  -3.5627
REMARK   3    S TENSOR
REMARK   3      S11:    .2427 S12:   -.1198 S13:   -.4975
REMARK   3      S21:   -.3853 S22:    .4513 S23:   1.1576
REMARK   3      S31:    .3170 S32:   -.5582 S33:   -.6940
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):   1.1326  18.5317  26.2892
REMARK   3    T TENSOR
REMARK   3      T11:    .3041 T22:    .2559
REMARK   3      T33:    .4039 T12:   -.1373
REMARK   3      T13:   -.0402 T23:   -.0949
REMARK   3    L TENSOR
REMARK   3      L11:   5.5950 L22:   5.2728
REMARK   3      L33:   9.1195 L12:  -1.8336
REMARK   3      L13:  -1.5144 L23:   1.6220
REMARK   3    S TENSOR
REMARK   3      S11:   -.1152 S12:    .3482 S13:   -.6173
REMARK   3      S21:   -.2314 S22:   -.2444 S23:    .4550
REMARK   3      S31:    .3708 S32:   -.3834 S33:    .3596
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   151
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8407  19.2922  38.9279
REMARK   3    T TENSOR
REMARK   3      T11:    .0785 T22:    .0253
REMARK   3      T33:    .0221 T12:    .0217
REMARK   3      T13:   -.0005 T23:   -.0032
REMARK   3    L TENSOR
REMARK   3      L11:   3.2020 L22:   2.9709
REMARK   3      L33:   4.9912 L12:  -1.9742
REMARK   3      L13:    .6198 L23:   -.2735
REMARK   3    S TENSOR
REMARK   3      S11:    .1286 S12:    .0755 S13:   -.1094
REMARK   3      S21:   -.1765 S22:   -.1737 S23:    .0703
REMARK   3      S31:    .3126 S32:   -.1522 S33:    .0451
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   152        B   230
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9940  27.5285  21.8430
REMARK   3    T TENSOR
REMARK   3      T11:    .0899 T22:    .1040
REMARK   3      T33:    .0793 T12:    .0274
REMARK   3      T13:    .0128 T23:    .0244
REMARK   3    L TENSOR
REMARK   3      L11:   1.0999 L22:   1.3317
REMARK   3      L33:   1.7714 L12:   -.9542
REMARK   3      L13:   -.0769 L23:    .0832
REMARK   3    S TENSOR
REMARK   3      S11:    .1159 S12:    .1712 S13:    .0567
REMARK   3      S21:   -.1999 S22:   -.0758 S23:   -.1256
REMARK   3      S31:    .1047 S32:    .2116 S33:   -.0401
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   231        B   268
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5601  51.4507  38.5446
REMARK   3    T TENSOR
REMARK   3      T11:    .0674 T22:    .0376
REMARK   3      T33:    .1146 T12:   -.0204
REMARK   3      T13:    .0074 T23:    .0482
REMARK   3    L TENSOR
REMARK   3      L11:   2.3375 L22:   3.7454
REMARK   3      L33:   3.5589 L12:   -.2740
REMARK   3      L13:   1.0351 L23:   -.5012
REMARK   3    S TENSOR
REMARK   3      S11:   -.0361 S12:    .1996 S13:    .3299
REMARK   3      S21:    .2852 S22:   -.0596 S23:   -.2143
REMARK   3      S31:   -.3951 S32:    .2799 S33:    .0958
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   269        B   308
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2076  50.0868  28.8326
REMARK   3    T TENSOR
REMARK   3      T11:    .2884 T22:    .2745
REMARK   3      T33:    .2820 T12:   -.2124
REMARK   3      T13:    .1635 T23:   -.0427
REMARK   3    L TENSOR
REMARK   3      L11:   5.0448 L22:   3.2059
REMARK   3      L33:   1.5565 L12:   1.7365
REMARK   3      L13:   1.1096 L23:   -.4222
REMARK   3    S TENSOR
REMARK   3      S11:   -.1044 S12:    .2237 S13:    .3457
REMARK   3      S21:   -.4530 S22:    .0677 S23:   -.4496
REMARK   3      S31:   -.3626 S32:    .5490 S33:    .0367
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   309        B   389
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1410  34.0334  36.3893
REMARK   3    T TENSOR
REMARK   3      T11:    .0134 T22:    .0508
REMARK   3      T33:    .0805 T12:   -.0042
REMARK   3      T13:   -.0107 T23:    .0241
REMARK   3    L TENSOR
REMARK   3      L11:    .9869 L22:   1.7295
REMARK   3      L33:   1.9375 L12:   -.4252
REMARK   3      L13:    .0566 L23:    .3998
REMARK   3    S TENSOR
REMARK   3      S11:    .0515 S12:    .1229 S13:   -.0567
REMARK   3      S21:   -.0938 S22:   -.0421 S23:    .2341
REMARK   3      S31:    .0936 S32:   -.2025 S33:   -.0094
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   390        B   430
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5702  48.4233  14.6656
REMARK   3    T TENSOR
REMARK   3      T11:    .1756 T22:    .2979
REMARK   3      T33:    .1648 T12:    .0712
REMARK   3      T13:    .0449 T23:    .1353
REMARK   3    L TENSOR
REMARK   3      L11:   1.4054 L22:   6.7062
REMARK   3      L33:   2.6850 L12:    .2779
REMARK   3      L13:  -1.0794 L23:    .6193
REMARK   3    S TENSOR
REMARK   3      S11:    .2080 S12:    .4234 S13:    .3809
REMARK   3      S21:   -.5078 S22:   -.0699 S23:   -.2502
REMARK   3      S31:   -.2758 S32:    .0680 S33:   -.1381
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   431        B   457
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7593  29.8030  13.6802
REMARK   3    T TENSOR
REMARK   3      T11:    .2057 T22:    .2171
REMARK   3      T33:    .0505 T12:    .1109
REMARK   3      T13:    .0192 T23:   -.0022
REMARK   3    L TENSOR
REMARK   3      L11:   2.3548 L22:   1.4357
REMARK   3      L33:   1.2734 L12:   -.8588
REMARK   3      L13:   1.1587 L23:  -1.2760
REMARK   3    S TENSOR
REMARK   3      S11:    .0987 S12:    .1876 S13:    .0762
REMARK   3      S21:   -.1773 S22:   -.1354 S23:   -.0391
REMARK   3      S31:    .1451 S32:    .2109 S33:    .0367
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   458        B   534
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3925  16.5373  16.8850
REMARK   3    T TENSOR
REMARK   3      T11:    .2530 T22:    .1277
REMARK   3      T33:    .0916 T12:    .0490
REMARK   3      T13:   -.0403 T23:   -.0420
REMARK   3    L TENSOR
REMARK   3      L11:   1.8198 L22:   2.2117
REMARK   3      L33:   3.0570 L12:   -.6704
REMARK   3      L13:    .2042 L23:   -.0586
REMARK   3    S TENSOR
REMARK   3      S11:    .1255 S12:    .2739 S13:   -.2188
REMARK   3      S21:   -.3241 S22:   -.1260 S23:    .1387
REMARK   3      S31:    .3377 S32:   -.0552 S33:    .0005
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):   6.6738  38.1478  35.8958
REMARK   3    T TENSOR
REMARK   3      T11:    .0106 T22:    .0550
REMARK   3      T33:    .1035 T12:    .0025
REMARK   3      T13:   -.0004 T23:    .0294
REMARK   3    L TENSOR
REMARK   3      L11:   1.2300 L22:   1.6681
REMARK   3      L33:   3.5260 L12:    .0023
REMARK   3      L13:    .0947 L23:  -1.1794
REMARK   3    S TENSOR
REMARK   3      S11:    .0753 S12:    .1345 S13:   -.0480
REMARK   3      S21:   -.0589 S22:    .0796 S23:    .2236
REMARK   3      S31:    .0874 S32:   -.3002 S33:   -.1548
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 3OLU 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 RCSB061278.
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   : 59835
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 4.900
REMARK 200  R MERGE                    (I) : 0.12400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600
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   (%): 53.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
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       60.65600
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.87700
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.01100
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.65600
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.87700
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.01100
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.65600
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.87700
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.01100
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.65600
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.87700
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.01100
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: 14160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 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     LEU A  75    CG   CD1  CD2
REMARK 470     LYS A  79    CD   CE   NZ
REMARK 470     LYS A  83    CE   NZ
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 473    CD   CE   NZ
REMARK 470     LYS A 485    CD   CE   NZ
REMARK 470     LYS A 557    NZ
REMARK 470     GLN B  54    CG   CD   OE1  NE2
REMARK 470     LEU B  75    CG   CD1  CD2
REMARK 470     ILE B  78    CD1
REMARK 470     LYS B  79    CD   CE   NZ
REMARK 470     LEU B  80    CD1  CD2
REMARK 470     LEU B  82    CD1  CD2
REMARK 470     LYS B  83    CG   CD   CE   NZ
REMARK 470     LYS B  97    CE   NZ
REMARK 470     LYS B 169    CD   CE   NZ
REMARK 470     GLU B 170    CD   OE1  OE2
REMARK 470     LYS B 175    NZ
REMARK 470     GLU B 186    CD   OE1  OE2
REMARK 470     LYS B 215    CG   CD   CE   NZ
REMARK 470     LYS B 267    CG   CD   CE   NZ
REMARK 470     GLU B 272    OE1  OE2
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 470     LYS B 492    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. =  15.7 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    LYS A  83      120.52    -37.40
REMARK 500    TYR A 122       -8.56    -53.22
REMARK 500    THR A 129      -94.17   -121.59
REMARK 500    TRP A 387       40.16    -95.10
REMARK 500    GLU A 398     -114.02     60.30
REMARK 500    TYR A 409       13.38     59.58
REMARK 500    ASN A 410       79.81   -100.22
REMARK 500    ASN A 439       15.36   -142.52
REMARK 500    SER A 471       32.32     70.84
REMARK 500    SER A 496      -50.86     68.72
REMARK 500    CYS A 575       66.03     39.73
REMARK 500    ARG B  61       11.39     59.89
REMARK 500    THR B 129      -91.08   -122.84
REMARK 500    ARG B 185      -98.41    -89.61
REMARK 500    ASP B 249       16.94     57.37
REMARK 500    TRP B 387       45.74    -87.30
REMARK 500    GLU B 398     -123.45     60.60
REMARK 500    TYR B 409       10.86     57.81
REMARK 500    SER B 496      -45.26     67.78
REMARK 500    SER B 579     -174.89   -174.85
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 750        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A 916        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH B 917        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH B 935        DISTANCE =  5.88 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 619  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 COH B 619   NA   86.8
REMARK 620 3 COH B 619   NB   91.0  90.5
REMARK 620 4 COH B 619   NC   98.4 174.1  86.7
REMARK 620 5 COH B 619   ND   91.3  92.0 176.7  90.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH A 620  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 620   NA   96.1
REMARK 620 3 COH A 620   NB   98.4  83.6
REMARK 620 4 COH A 620   NC   92.2 169.7  89.2
REMARK 620 5 COH A 620   ND   84.4  94.8 176.9  91.9
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 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 620
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 1AG 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: 3OLT   RELATED DB: PDB
DBREF  3OLU A   35   618  UNP    Q05769   PGH2_MOUSE      20    604
DBREF  3OLU B   35   618  UNP    Q05769   PGH2_MOUSE      20    604
SEQADV 3OLU ALA A   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS A  513  UNP  Q05769    ARG   499 ENGINEERED MUTATION
SEQADV 3OLU ALA B   28  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3OLU 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 3OLU ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3OLU ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3OLU ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3OLU ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3OLU ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3OLU ASN B  144  ASN  GLYCOSYLATION SITE
HET    EDO  A   1       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    EDO  A  15       4
HET    1AG  A 619      27
HET    COH  A 620      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    1AG  B   1      27
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     1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,
HETNAM   2 1AG  14-TETRAENOATE
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  1AG    2(C23 H38 O4)
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   *666(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 ARG A  120  1                                  16
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  HIS A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 VAL A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  ASP A  347  1                                  24
HELIX   15  15 ASP A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 HIS A  386  LEU A  391  5                                   6
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  410  GLN A  429  1                                  20
HELIX   21  21 PRO A  441  ALA A  443  5                                   3
HELIX   22  22 VAL A  444  MET A  458  1                                  15
HELIX   23  23 SER A  462  PHE A  470  1                                   9
HELIX   24  24 SER A  477  GLY A  483  1                                   7
HELIX   25  25 LYS A  485  SER A  496  1                                  12
HELIX   26  26 ASP A  497  MET A  501  5                                   5
HELIX   27  27 GLU A  502  GLU A  510  1                                   9
HELIX   28  28 GLY A  519  GLY A  536  1                                  18
HELIX   29  29 ASN A  537  SER A  541  5                                   5
HELIX   30  30 LYS A  546  GLY A  551  5                                   6
HELIX   31  31 GLY A  552  THR A  561  1                                  10
HELIX   32  32 SER A  563  VAL A  572  1                                  10
HELIX   33  33 GLU B   73  LYS B   83  1                                  11
HELIX   34  34 THR B   85  THR B   94  1                                  10
HELIX   35  35 PHE B   96  ASN B  104  1                                   9
HELIX   36  36 ILE B  105A TYR B  122  1                                  18
HELIX   37  37 SER B  138  ASN B  144  1                                   7
HELIX   38  38 ASP B  173  LEU B  182  1                                  10
HELIX   39  39 ASN B  195  HIS B  207  1                                  13
HELIX   40  40 LEU B  230  GLY B  235  1                                   6
HELIX   41  41 THR B  237  ARG B  245  1                                   9
HELIX   42  42 THR B  265  GLN B  270  1                                   6
HELIX   43  43 PRO B  280  GLN B  284  5                                   5
HELIX   44  44 VAL B  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 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257
SHEET    1   D 2 PHE A 395  ILE A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  GLN A 400   N  ILE A 397
SHEET    1   E 2 GLU B  46  SER B  49  0
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46
SHEET    1   F 2 PHE B  64  TYR B  65  0
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   G 2 THR B 212  ASP B 213  0
SHEET    2   G 2 GLY B 217  THR B 221 -1  O  GLY B 217   N  ASP B 213
SHEET    1   H 2 GLN B 255  ILE B 257  0
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  GLU B 260   N  ILE B 257
SHEET    1   I 2 PHE B 395  ILE B 397  0
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.07
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.05
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.07
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04
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  2.07
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.36
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.36
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.37
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.37
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.39
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.43
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         O4  NAG B 672                 C1  MAN B 673     1555   1555  1.46
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.47
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.47
LINK         NE2AHIS B 388                CO   COH B 619     1555   1555  2.17
LINK         NE2 HIS A 388                CO   COH A 620     1555   1555  2.46
LINK         ND2 ASN A  68                 O5  NAG A 661     1555   1555  1.43
LINK         ND2 ASN B  68                 O5  NAG B 661     1555   1555  1.49
LINK         ND2 ASN A 410                 O5  NAG A 681     1555   1555  1.50
LINK         ND2 ASN B 410                 O5  NAG B 681     1555   1555  1.49
LINK         ND2 ASN A 144                 O5  NAG A 671     1555   1555  1.53
CISPEP   1 SER A  126    PRO A  127          0        -0.86
CISPEP   2 SER B  126    PRO B  127          0        -1.91
SITE     1 AC1  3 ASP A 157  CYS A 159  LYS A 459
SITE     1 AC2  6 PRO A 162  SER A 455  ARG A 456  LYS A 459
SITE     2 AC2  6 TYR A 460  HOH A 768
SITE     1 AC3  2 HOH A 905  MAN B 673
SITE     1 AC4  7 GLU A 308  ARG A 311  GLU A 339  SER A 566
SITE     2 AC4  7 LEU A 567  ASN A 570  HOH A 645
SITE     1 AC5  5 LYS A 251  TYR A 254  ASN A 310  HOH A 831
SITE     2 AC5  5 HOH A 858
SITE     1 AC6  4 ASP A 239  ARG A 240  LYS A 243  GLU A 272
SITE     1 AC7 10 HIS A  90  GLN A 192  LEU A 352  SER A 353
SITE     2 AC7 10 HIS A 513  ALA A 516  ILE A 517  PHE A 518
SITE     3 AC7 10 VAL A 523  HOH A 844
SITE     1 AC8 18 ARG A 120  PHE A 205  PHE A 209  TYR A 348
SITE     2 AC8 18 VAL A 349  SER A 353  TYR A 355  ILE A 377
SITE     3 AC8 18 PHE A 381  TYR A 385  TRP A 387  MET A 522
SITE     4 AC8 18 GLY A 526  ALA A 527  SER A 530  LEU A 531
SITE     5 AC8 18 GLY A 533  LEU A 534
SITE     1 AC9 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210
SITE     2 AC9 15 LYS A 211  THR A 212  VAL A 295  ASN A 382
SITE     3 AC9 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391
SITE     4 AC9 15 VAL A 447  HOH A 724  HOH A 909
SITE     1 BC1  5 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 BC1  5 HOH A 811
SITE     1 BC2  2 NAG A 661  HOH A 667
SITE     1 BC3 10 HOH A  27  GLU A 140  ASN A 144  TYR A 147
SITE     2 BC3 10 ARG A 216  PHE A 220  HOH A 639  HOH A 670
SITE     3 BC3 10 NAG A 672  LEU B 238
SITE     1 BC4  3 ARG A 216  NAG A 671  MAN A 673
SITE     1 BC5  1 NAG A 672
SITE     1 BC6  7 GLN A 406  ASN A 410  SER A 412  ILE A 413
SITE     2 BC6  7 GLU A 416  HOH A 813  HOH A 878
SITE     1 BC7 12 GLU A 179  LYS A 180  ARG A 184  ARG A 185
SITE     2 BC7 12 ARG A 438  GLU A 486  GLU A 490  GLU B 179
SITE     3 BC7 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445
SITE     1 BC8  8 HIS B  90  GLN B 192  LEU B 352  SER B 353
SITE     2 BC8  8 ALA B 516  ILE B 517  PHE B 518  HOH B 659
SITE     1 BC9  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310
SITE     2 BC9  6 HOH B 760  HOH B 862
SITE     1 CC1  5 PRO B 162  ARG B 456  LYS B 459  TYR B 460
SITE     2 CC1  5 HOH B 649
SITE     1 CC2  7 PRO A 547  SER A 548  GLU A 553  MET B  48
SITE     2 CC2  7 LYS B  56  ASP B  58  HOH B 838
SITE     1 CC3  7 GLU B 308  ARG B 311  GLU B 339  SER B 566
SITE     2 CC3  7 LEU B 567  ASN B 570  HOH B 677
SITE     1 CC4  3 LEU A 145  SER B 143  HOH B 652
SITE     1 CC5  5 ASP B 239  ARG B 240  LYS B 243  VAL B 271
SITE     2 CC5  5 GLU B 272
SITE     1 CC6 16 ARG B 120  PHE B 205  PHE B 209  VAL B 349
SITE     2 CC6 16 TYR B 355  ASN B 375  ILE B 377  PHE B 381
SITE     3 CC6 16 TYR B 385  GLY B 526  ALA B 527  SER B 530
SITE     4 CC6 16 LEU B 531  GLY B 533  LEU B 534  HOH B 789
SITE     1 CC7 14 ALA B 199  PHE B 200  GLN B 203  HIS B 207
SITE     2 CC7 14 PHE B 210  LYS B 211  THR B 212  HIS B 214
SITE     3 CC7 14 VAL B 295  ASN B 382  TYR B 385  HIS B 386
SITE     4 CC7 14 HIS B 388  LEU B 391
SITE     1 CC8  5 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     2 CC8  5 HOH B 730
SITE     1 CC9  3 NAG B 661  HOH B 732  HOH B 922
SITE     1 DC1  9 GLU B 140  ASN B 144  TYR B 147  ARG B 216
SITE     2 DC1  9 PHE B 220  HOH B 627  NAG B 672  HOH B 701
SITE     3 DC1  9 HOH B 703
SITE     1 DC2  5 HOH A 679  ARG B 216  NAG B 671  MAN B 673
SITE     2 DC2  5 HOH B 674
SITE     1 DC3  7 EDO A   5  HOH A 905  HOH B 644  HOH B 651
SITE     2 DC3  7 HOH B 657  NAG B 672  HOH B 674
SITE     1 DC4  5 ASN B 410  SER B 412  ILE B 413  GLU B 416
SITE     2 DC4  5 HOH B 914
CRYST1  121.312  131.754  180.022  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      0.008243  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007590  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005555        0.00000
      
PROCHECK
Go to PROCHECK summary
 References