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PDBsum entry 3hs7

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Oxidoreductase PDB id
3hs7
Jmol
Contents
Protein chains
551 a.a.
Ligands
AKR ×3
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG ×2
HXA ×2
EDO ×8
Waters ×330
HEADER    OXIDOREDUCTASE                          10-JUN-09   3HS7
TITLE     X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 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: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    OXIDOREDUCTASE, DIOXYGENASE, DISULFIDE BOND, ENDOPLASMIC RETICULUM,
KEYWDS   2 FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME, IRON, LIPID SYNTHESIS,
KEYWDS   3 MEMBRANE, METAL-BINDING, MICROSOME, PEROXIDASE, PHOSPHOPROTEIN,
KEYWDS   4 PROSTAGLANDIN BIOSYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI
REVDAT   3   04-AUG-10 3HS7    1       JRNL
REVDAT   2   02-JUN-10 3HS7    1       JRNL
REVDAT   1   12-MAY-10 3HS7    0
JRNL        AUTH   A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI
JRNL        TITL   STRUCTURAL BASIS OF FATTY ACID SUBSTRATE BINDING TO
JRNL        TITL 2 CYCLOOXYGENASE-2.
JRNL        REF    J.BIOL.CHEM.                  V. 285 22152 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20463020
JRNL        DOI    10.1074/JBC.M110.119867
REMARK   2
REMARK   2 RESOLUTION.    2.65 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) : 2.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 41205
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) : 0.184
REMARK   3   R VALUE            (WORKING SET) : 0.181
REMARK   3   FREE R VALUE                     : 0.234
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2074
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) : 2.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2792
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630
REMARK   3   BIN FREE R VALUE SET COUNT          : 157
REMARK   3   BIN FREE R VALUE                    : 0.3470
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8841
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 372
REMARK   3   SOLVENT ATOMS            : 330
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 50.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.34
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.37000
REMARK   3    B22 (A**2) : -0.09000
REMARK   3    B33 (A**2) : -2.28000
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): 1.619
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.312
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.664
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9520 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12944 ; 1.021 ; 2.005
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1109 ; 4.735 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   440 ;36.367 ;23.909
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1473 ;14.630 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;12.259 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1379 ; 0.073 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7321 ; 0.004 ; 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 ; 0.196 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8985 ; 0.401 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3986 ; 0.763 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3955 ; 1.426 ; 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    66
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4984   2.0790  56.3652
REMARK   3    T TENSOR
REMARK   3      T11:    .5493 T22:    .1431
REMARK   3      T33:    .3231 T12:   -.0788
REMARK   3      T13:   -.0250 T23:    .0302
REMARK   3    L TENSOR
REMARK   3      L11:   1.1648 L22:    .9502
REMARK   3      L33:   2.5296 L12:    .8407
REMARK   3      L13:   -.3848 L23:   -.2094
REMARK   3    S TENSOR
REMARK   3      S11:    .2234 S12:   -.0403 S13:   -.0049
REMARK   3      S21:    .3910 S22:   -.0086 S23:    .0478
REMARK   3      S31:    .7309 S32:   -.2922 S33:   -.2148
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    67        A    81
REMARK   3    ORIGIN FOR THE GROUP (A):  41.7304  -3.5012  59.4277
REMARK   3    T TENSOR
REMARK   3      T11:    .5847 T22:    .2433
REMARK   3      T33:    .4582 T12:    .0655
REMARK   3      T13:   -.0432 T23:    .0146
REMARK   3    L TENSOR
REMARK   3      L11:  13.7222 L22:   4.1307
REMARK   3      L33:   2.2767 L12:   1.5418
REMARK   3      L13:   2.1797 L23:    .1389
REMARK   3    S TENSOR
REMARK   3      S11:    .1206 S12:   -.1942 S13:   -.2657
REMARK   3      S21:    .0817 S22:   -.0322 S23:   -.7935
REMARK   3      S31:    .2089 S32:    .4283 S33:   -.0884
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    82        A   120
REMARK   3    ORIGIN FOR THE GROUP (A):  58.1642  17.5508  64.9542
REMARK   3    T TENSOR
REMARK   3      T11:    .3669 T22:    .4369
REMARK   3      T33:    .6082 T12:    .2515
REMARK   3      T13:   -.0569 T23:    .0962
REMARK   3    L TENSOR
REMARK   3      L11:   1.1403 L22:   5.7943
REMARK   3      L33:   7.3102 L12:   1.1921
REMARK   3      L13:   -.6670 L23:  -3.2707
REMARK   3    S TENSOR
REMARK   3      S11:   -.0780 S12:   -.3577 S13:   -.6599
REMARK   3      S21:   -.0343 S22:   -.3318 S23:   -.4497
REMARK   3      S31:   1.0007 S32:    .8570 S33:    .4098
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   121        A   148
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5922  18.7275  50.5692
REMARK   3    T TENSOR
REMARK   3      T11:    .1572 T22:    .1254
REMARK   3      T33:    .1933 T12:   -.0204
REMARK   3      T13:   -.0341 T23:    .0028
REMARK   3    L TENSOR
REMARK   3      L11:   1.1777 L22:   3.6084
REMARK   3      L33:   4.3834 L12:   1.8104
REMARK   3      L13:   -.6432 L23:    .0475
REMARK   3    S TENSOR
REMARK   3      S11:    .0884 S12:   -.1537 S13:   -.2924
REMARK   3      S21:    .2056 S22:   -.0964 S23:   -.3217
REMARK   3      S31:    .4885 S32:    .1794 S33:    .0080
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   223
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4511  26.9801  68.6174
REMARK   3    T TENSOR
REMARK   3      T11:    .1524 T22:    .1736
REMARK   3      T33:    .1487 T12:   -.0420
REMARK   3      T13:    .0086 T23:   -.0276
REMARK   3    L TENSOR
REMARK   3      L11:   1.0410 L22:   1.7843
REMARK   3      L33:   2.0459 L12:    .8249
REMARK   3      L13:   -.2212 L23:    .2413
REMARK   3    S TENSOR
REMARK   3      S11:    .1332 S12:   -.1445 S13:    .0809
REMARK   3      S21:    .2133 S22:   -.1123 S23:    .2039
REMARK   3      S31:    .2437 S32:   -.3386 S33:   -.0209
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   224        A   268
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0156  49.2067  51.3152
REMARK   3    T TENSOR
REMARK   3      T11:    .1109 T22:    .1349
REMARK   3      T33:    .2368 T12:    .0170
REMARK   3      T13:    .0080 T23:   -.0506
REMARK   3    L TENSOR
REMARK   3      L11:    .7099 L22:   3.6255
REMARK   3      L33:   2.3884 L12:    .4330
REMARK   3      L13:    .2041 L23:   1.3013
REMARK   3    S TENSOR
REMARK   3      S11:   -.0304 S12:   -.0633 S13:    .1841
REMARK   3      S21:   -.0119 S22:    .0279 S23:    .2355
REMARK   3      S31:   -.3742 S32:   -.1311 S33:    .0025
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   345
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9607  47.6422  53.8822
REMARK   3    T TENSOR
REMARK   3      T11:    .0981 T22:    .1289
REMARK   3      T33:    .1716 T12:   -.0228
REMARK   3      T13:   -.0141 T23:   -.0501
REMARK   3    L TENSOR
REMARK   3      L11:    .8606 L22:   2.6988
REMARK   3      L33:   4.6618 L12:    .4734
REMARK   3      L13:    .0281 L23:  -1.1016
REMARK   3    S TENSOR
REMARK   3      S11:    .0083 S12:   -.0935 S13:    .2278
REMARK   3      S21:    .2739 S22:    .0278 S23:    .1426
REMARK   3      S31:   -.4980 S32:   -.1471 S33:   -.0361
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   346        A   412
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8607  32.6786  64.9871
REMARK   3    T TENSOR
REMARK   3      T11:    .1097 T22:    .0952
REMARK   3      T33:    .1549 T12:   -.0140
REMARK   3      T13:   -.0162 T23:    .0294
REMARK   3    L TENSOR
REMARK   3      L11:   1.3594 L22:   1.7357
REMARK   3      L33:   3.4032 L12:    .3215
REMARK   3      L13:    .1313 L23:   1.0613
REMARK   3    S TENSOR
REMARK   3      S11:    .1114 S12:   -.2178 S13:   -.0111
REMARK   3      S21:    .2511 S22:   -.0343 S23:   -.0836
REMARK   3      S31:    .0154 S32:    .0797 S33:   -.0771
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   413        A   454
REMARK   3    ORIGIN FOR THE GROUP (A):  37.7171  40.3652  75.1573
REMARK   3    T TENSOR
REMARK   3      T11:    .1669 T22:    .2699
REMARK   3      T33:    .1257 T12:   -.0321
REMARK   3      T13:    .0115 T23:   -.0753
REMARK   3    L TENSOR
REMARK   3      L11:   2.0152 L22:   1.7495
REMARK   3      L33:   2.2736 L12:   -.0656
REMARK   3      L13:   -.4425 L23:   -.7136
REMARK   3    S TENSOR
REMARK   3      S11:    .1325 S12:   -.3886 S13:    .1667
REMARK   3      S21:    .1068 S22:   -.1920 S23:   -.0594
REMARK   3      S31:   -.0446 S32:   -.0491 S33:    .0596
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   455        A   530
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4371  16.6614  73.4409
REMARK   3    T TENSOR
REMARK   3      T11:    .4117 T22:    .1804
REMARK   3      T33:    .1577 T12:   -.0628
REMARK   3      T13:   -.0409 T23:    .0413
REMARK   3    L TENSOR
REMARK   3      L11:   1.9810 L22:   2.8991
REMARK   3      L33:   3.4136 L12:    .4300
REMARK   3      L13:    .5178 L23:    .4311
REMARK   3    S TENSOR
REMARK   3      S11:    .1478 S12:   -.3557 S13:   -.2137
REMARK   3      S21:    .4327 S22:   -.1222 S23:   -.0610
REMARK   3      S31:    .5417 S32:    .0288 S33:   -.0256
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   531        A   579
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9090  37.6133  52.8051
REMARK   3    T TENSOR
REMARK   3      T11:    .0746 T22:    .2168
REMARK   3      T33:    .1980 T12:    .0340
REMARK   3      T13:   -.0065 T23:   -.0481
REMARK   3    L TENSOR
REMARK   3      L11:   1.3452 L22:   2.4614
REMARK   3      L33:   4.2741 L12:    .0305
REMARK   3      L13:   -.2583 L23:   1.4208
REMARK   3    S TENSOR
REMARK   3      S11:    .0697 S12:   -.0064 S13:   -.0755
REMARK   3      S21:    .0280 S22:    .2505 S23:   -.3507
REMARK   3      S31:    .1530 S32:    .4956 S33:   -.3201
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   580        A   584
REMARK   3    ORIGIN FOR THE GROUP (A):  52.0177  38.5519  73.2446
REMARK   3    T TENSOR
REMARK   3      T11:    .5458 T22:    .2740
REMARK   3      T33:    .2652 T12:    .0278
REMARK   3      T13:   -.0901 T23:   -.0601
REMARK   3    L TENSOR
REMARK   3      L11:   7.6844 L22:   5.1683
REMARK   3      L33:  22.0465 L12:  -2.4484
REMARK   3      L13:  -3.6579 L23:  -2.5306
REMARK   3    S TENSOR
REMARK   3      S11:    .0670 S12:   -.9128 S13:   1.1101
REMARK   3      S21:    .8773 S22:    .2179 S23:   -.8828
REMARK   3      S31:   -.7136 S32:   1.2149 S33:   -.2849
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    66
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6058  38.0131  30.3489
REMARK   3    T TENSOR
REMARK   3      T11:    .1497 T22:    .4424
REMARK   3      T33:    .3376 T12:   -.0986
REMARK   3      T13:    .0442 T23:   -.0636
REMARK   3    L TENSOR
REMARK   3      L11:    .3987 L22:   6.5090
REMARK   3      L33:   4.4908 L12:   -.7867
REMARK   3      L13:    .8435 L23:  -1.6665
REMARK   3    S TENSOR
REMARK   3      S11:   -.0812 S12:    .2730 S13:    .1192
REMARK   3      S21:   -.2031 S22:    .2626 S23:   -.1293
REMARK   3      S31:   -.3257 S32:    .7368 S33:   -.1814
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    67        B    92
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1113  18.1930  23.6753
REMARK   3    T TENSOR
REMARK   3      T11:    .2702 T22:    .4997
REMARK   3      T33:    .5948 T12:    .1491
REMARK   3      T13:    .0292 T23:   -.1426
REMARK   3    L TENSOR
REMARK   3      L11:   4.1478 L22:  10.0553
REMARK   3      L33:   6.7735 L12:   6.4197
REMARK   3      L13:   5.1655 L23:   8.1876
REMARK   3    S TENSOR
REMARK   3      S11:    .0531 S12:    .2426 S13:   -.3895
REMARK   3      S21:    .2320 S22:    .5777 S23:   -.6146
REMARK   3      S31:    .2895 S32:    .6611 S33:   -.6308
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    93        B   122
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6362   2.4066  25.2554
REMARK   3    T TENSOR
REMARK   3      T11:    .1924 T22:    .3206
REMARK   3      T33:    .3879 T12:    .0592
REMARK   3      T13:    .0355 T23:   -.0192
REMARK   3    L TENSOR
REMARK   3      L11:    .8897 L22:   4.8615
REMARK   3      L33:  11.0714 L12:    .5747
REMARK   3      L13:  -2.0217 L23:   2.4369
REMARK   3    S TENSOR
REMARK   3      S11:   -.1789 S12:   -.1917 S13:   -.1892
REMARK   3      S21:    .0887 S22:   -.1182 S23:   -.1962
REMARK   3      S31:    .4903 S32:    .4876 S33:    .2971
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   187
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8358  36.1720  23.1309
REMARK   3    T TENSOR
REMARK   3      T11:    .1088 T22:    .1377
REMARK   3      T33:    .1670 T12:   -.0470
REMARK   3      T13:    .0034 T23:    .0027
REMARK   3    L TENSOR
REMARK   3      L11:   1.4707 L22:   1.1936
REMARK   3      L33:   3.3532 L12:    .7406
REMARK   3      L13:    .0946 L23:    .3571
REMARK   3    S TENSOR
REMARK   3      S11:   -.0748 S12:    .1899 S13:    .1348
REMARK   3      S21:   -.2051 S22:    .0718 S23:   -.1005
REMARK   3      S31:   -.3061 S32:    .3045 S33:    .0030
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   188        B   227
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4916  23.5163  21.7025
REMARK   3    T TENSOR
REMARK   3      T11:    .1579 T22:    .1553
REMARK   3      T33:    .1682 T12:    .0232
REMARK   3      T13:   -.0428 T23:    .0036
REMARK   3    L TENSOR
REMARK   3      L11:   1.7637 L22:    .9796
REMARK   3      L33:   1.5985 L12:   1.1620
REMARK   3      L13:    .1593 L23:    .5286
REMARK   3    S TENSOR
REMARK   3      S11:   -.1148 S12:    .0822 S13:    .0795
REMARK   3      S21:   -.1854 S22:   -.0303 S23:    .1811
REMARK   3      S31:   -.1823 S32:   -.0587 S33:    .1451
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   268
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9571  19.0987  33.6767
REMARK   3    T TENSOR
REMARK   3      T11:    .0756 T22:    .1002
REMARK   3      T33:    .2016 T12:   -.0153
REMARK   3      T13:    .0308 T23:   -.0155
REMARK   3    L TENSOR
REMARK   3      L11:   4.1491 L22:    .4923
REMARK   3      L33:   2.7808 L12:   -.0465
REMARK   3      L13:   1.1159 L23:   -.2402
REMARK   3    S TENSOR
REMARK   3      S11:   -.0311 S12:   -.1877 S13:    .1447
REMARK   3      S21:    .0070 S22:    .0622 S23:    .1185
REMARK   3      S31:   -.0602 S32:   -.3302 S33:   -.0311
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   331
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1316  17.0330  30.9069
REMARK   3    T TENSOR
REMARK   3      T11:    .0705 T22:    .1487
REMARK   3      T33:    .2151 T12:   -.0577
REMARK   3      T13:   -.0016 T23:   -.0371
REMARK   3    L TENSOR
REMARK   3      L11:   1.8716 L22:   1.9028
REMARK   3      L33:   3.8573 L12:   -.0780
REMARK   3      L13:   -.0926 L23:   -.5098
REMARK   3    S TENSOR
REMARK   3      S11:    .0610 S12:    .1521 S13:    .1794
REMARK   3      S21:   -.0081 S22:   -.0494 S23:    .2063
REMARK   3      S31:    .0548 S32:   -.3262 S33:   -.0116
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   332        B   408
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4958  15.2621  23.7888
REMARK   3    T TENSOR
REMARK   3      T11:    .1426 T22:    .1320
REMARK   3      T33:    .1460 T12:   -.0217
REMARK   3      T13:    .0116 T23:   -.0409
REMARK   3    L TENSOR
REMARK   3      L11:    .7493 L22:   1.0415
REMARK   3      L33:   1.3888 L12:    .5532
REMARK   3      L13:   -.3797 L23:    .3865
REMARK   3    S TENSOR
REMARK   3      S11:   -.1035 S12:    .1910 S13:   -.0925
REMARK   3      S21:   -.1280 S22:    .1363 S23:   -.1009
REMARK   3      S31:    .1676 S32:    .0226 S33:   -.0329
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   409        B   445
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2582  17.2866  10.7315
REMARK   3    T TENSOR
REMARK   3      T11:    .2137 T22:    .2311
REMARK   3      T33:    .1018 T12:   -.0634
REMARK   3      T13:   -.0574 T23:   -.0054
REMARK   3    L TENSOR
REMARK   3      L11:   5.9936 L22:   3.2053
REMARK   3      L33:   3.0234 L12:   2.6800
REMARK   3      L13:  -2.0719 L23:   -.8062
REMARK   3    S TENSOR
REMARK   3      S11:   -.0578 S12:    .2955 S13:   -.1189
REMARK   3      S21:   -.0283 S22:    .0617 S23:    .1991
REMARK   3      S31:   -.0863 S32:   -.3037 S33:   -.0039
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   446        B   497
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2348  31.8508  12.2668
REMARK   3    T TENSOR
REMARK   3      T11:    .2078 T22:    .2394
REMARK   3      T33:    .1849 T12:   -.1213
REMARK   3      T13:    .0486 T23:   -.0201
REMARK   3    L TENSOR
REMARK   3      L11:   2.1541 L22:   1.3604
REMARK   3      L33:   2.9345 L12:    .1447
REMARK   3      L13:   -.4424 L23:   -.2150
REMARK   3    S TENSOR
REMARK   3      S11:   -.1305 S12:    .4294 S13:    .0151
REMARK   3      S21:   -.2825 S22:    .1999 S23:   -.0983
REMARK   3      S31:   -.0724 S32:    .1176 S33:   -.0694
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   498        B   553
REMARK   3    ORIGIN FOR THE GROUP (A):  39.7293  18.7047  24.6554
REMARK   3    T TENSOR
REMARK   3      T11:    .1637 T22:    .1131
REMARK   3      T33:    .1590 T12:   -.0249
REMARK   3      T13:    .0368 T23:   -.0542
REMARK   3    L TENSOR
REMARK   3      L11:   1.0897 L22:    .7822
REMARK   3      L33:   2.0459 L12:    .6267
REMARK   3      L13:   -.6780 L23:   -.8917
REMARK   3    S TENSOR
REMARK   3      S11:   -.1437 S12:    .1339 S13:   -.1701
REMARK   3      S21:   -.0886 S22:    .0705 S23:   -.2329
REMARK   3      S31:    .1160 S32:    .1726 S33:    .0732
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   554        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7562   3.3475  25.6472
REMARK   3    T TENSOR
REMARK   3      T11:    .2421 T22:    .1566
REMARK   3      T33:    .2369 T12:    .0365
REMARK   3      T13:   -.0317 T23:   -.0717
REMARK   3    L TENSOR
REMARK   3      L11:   1.6980 L22:   2.7918
REMARK   3      L33:   5.7273 L12:   1.7117
REMARK   3      L13:  -1.5100 L23:   -.1192
REMARK   3    S TENSOR
REMARK   3      S11:   -.0677 S12:    .0988 S13:   -.3376
REMARK   3      S21:    .1283 S22:    .0754 S23:   -.2615
REMARK   3      S31:    .6839 S32:    .4434 S33:   -.0077
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 3HS7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-08
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) : 0.9789
REMARK 200  MONOCHROMATOR                  : NULL
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   : 41205
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : 0.12400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
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       59.64700
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.85400
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.62150
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.64700
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.85400
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.62150
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.64700
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.85400
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.62150
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.64700
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.85400
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.62150
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: 5040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.7 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     HIS A    29
REMARK 465     HIS A    30
REMARK 465     HIS A    31
REMARK 465     HIS A    32
REMARK 465     GLN A   583
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ALA A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     HIS B    29
REMARK 465     HIS B    30
REMARK 465     HIS B    31
REMARK 465     HIS B    32
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     GLN B   586
REMARK 465     PRO B   587
REMARK 465     THR B   588
REMARK 465     LYS B   589
REMARK 465     THR B   590
REMARK 465     ALA B   591
REMARK 465     THR B   592
REMARK 465     ILE B   593
REMARK 465     ALA B   594
REMARK 465     ALA B   595
REMARK 465     SER B   596
REMARK 465     ALA B   597
REMARK 465     SER B   598
REMARK 465     HIS B   599
REMARK 465     SER B   600
REMARK 465     ARG B   601
REMARK 465     LEU B   602
REMARK 465     ASP B   603
REMARK 465     ASP B   604
REMARK 465     ILE B   605
REMARK 465     ASN B   606
REMARK 465     PRO B   607
REMARK 465     THR B   608
REMARK 465     VAL B   609
REMARK 465     LEU B   610
REMARK 465     ILE B   611
REMARK 465     LYS B   612
REMARK 465     ARG B   613
REMARK 465     ARG B   614
REMARK 465     SER B   615
REMARK 465     THR B   616
REMARK 465     GLU B   617
REMARK 465     LEU B   618
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A  56    CD   CE   NZ
REMARK 470     LYS A  79    CD   CE   NZ
REMARK 470     LYS A  83    CE   NZ
REMARK 470     LYS A  97    CE   NZ
REMARK 470     LYS A 114    NZ
REMARK 470     LYS A 169    CD   CE   NZ
REMARK 470     GLU A 170    OE1  OE2
REMARK 470     LYS A 215    CD   CE   NZ
REMARK 470     ARG A 222    NE   CZ   NH1  NH2
REMARK 470     GLU A 272    CD   OE1  OE2
REMARK 470     GLU A 290    OE1  OE2
REMARK 470     LYS A 358    CE   NZ
REMARK 470     ASP A 399    CG   OD1  OD2
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     LYS A 473    CE   NZ
REMARK 470     LYS A 485    CE   NZ
REMARK 470     LYS A 557    CD   CE   NZ
REMARK 470     GLN B  54    CD   OE1  NE2
REMARK 470     LEU B  75    CD1  CD2
REMARK 470     LYS B  79    CD   CE   NZ
REMARK 470     LEU B  81    CD1  CD2
REMARK 470     LEU B  82    CD1  CD2
REMARK 470     LYS B  83    CG   CD   CE   NZ
REMARK 470     LYS B  97    CD   CE   NZ
REMARK 470     ILE B 102    CG2  CD1
REMARK 470     ILE B 105A   CD1
REMARK 470     LYS B 114    CE   NZ
REMARK 470     LYS B 169    CD   CE   NZ
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     ASP B 239    OD1  OD2
REMARK 470     LYS B 248    CE   NZ
REMARK 470     LYS B 267    CD   CE   NZ
REMARK 470     ASP B 268    CG   OD1  OD2
REMARK 470     GLU B 272    CD   OE1  OE2
REMARK 470     GLU B 281    CB   CG   CD   OE1  OE2
REMARK 470     GLN B 284    CG   CD   OE1  NE2
REMARK 470     LYS B 358    CE   NZ
REMARK 470     LYS B 360    NZ
REMARK 470     LYS B 405    CD   CE   NZ
REMARK 470     LYS B 473    CD   CE   NZ
REMARK 470     LYS B 485    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   C4   NAG A   661     C1   NAG A   662              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A 129      -81.71   -122.22
REMARK 500    ARG A 185      -71.22    -85.75
REMARK 500    ASP A 249       18.27     51.27
REMARK 500    GLU A 398     -120.44     57.21
REMARK 500    ASN A 439       14.30   -148.60
REMARK 500    SER A 496      -34.84     70.94
REMARK 500    CYS A 575       72.68     30.51
REMARK 500    ARG B  44       11.30     82.03
REMARK 500    ARG B  61       16.82     59.02
REMARK 500    THR B 129      -88.25   -112.33
REMARK 500    ARG B 185      -83.79   -106.46
REMARK 500    ASP B 347      -55.65   -120.02
REMARK 500    GLU B 398     -107.72     60.67
REMARK 500    ASN B 439       12.84   -144.73
REMARK 500    SER B 496      -38.95     71.64
REMARK 500    CYS B 575       70.88     41.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLY B 164         10.25
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 760        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH A 779        DISTANCE =  5.20 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NAG B  681
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   84.4
REMARK 620 3 COH B 619   NB   81.4  89.9
REMARK 620 4 COH B 619   NC   90.4 174.7  88.5
REMARK 620 5 COH B 619   ND   91.5  89.5 172.9  91.4
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-2
REMARK 900 RELATED ID: 1DDX   RELATED DB: PDB
REMARK 900 PGG2 BOUND TO COX-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB
REMARK 900 UNINHIBITED COX-2
REMARK 900 RELATED ID: 1IGX   RELATED DB: PDB
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO COX-1
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL
REMARK 900 OF CYCLOOXYGENASE-2
DBREF  3HS7 A   35   618  UNP    Q05769   PGH2_MOUSE      20    604
DBREF  3HS7 B   35   618  UNP    Q05769   PGH2_MOUSE      20    604
SEQADV 3HS7 HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED
SEQADV 3HS7 HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS7 ALA B  594  UNP  Q05769    ASN   580 ENGINEERED
SEQRES   1 A  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS
SEQRES   2 A  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   3 A  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   4 A  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   5 A  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   6 A  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   7 A  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   8 A  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES   9 A  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  10 A  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  11 A  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  12 A  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  13 A  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  14 A  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  15 A  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  16 A  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  17 A  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  18 A  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  19 A  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  20 A  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  21 A  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  22 A  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  23 A  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  24 A  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  25 A  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  26 A  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  27 A  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  28 A  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  29 A  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  30 A  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  31 A  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  32 A  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  33 A  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  34 A  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  35 A  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  36 A  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  37 A  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  38 A  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  39 A  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  40 A  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  41 A  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  42 A  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  43 A  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  44 A  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS
SEQRES  45 A  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  46 A  591  ARG ARG SER THR GLU LEU
SEQRES   1 B  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS
SEQRES   2 B  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   3 B  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   4 B  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   5 B  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   6 B  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   7 B  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   8 B  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES   9 B  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  10 B  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  11 B  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  12 B  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  13 B  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  14 B  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  15 B  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  16 B  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  17 B  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  18 B  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  19 B  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  20 B  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  21 B  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  22 B  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  23 B  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  24 B  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  25 B  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  26 B  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  27 B  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  28 B  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  29 B  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  30 B  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  31 B  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  32 B  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  33 B  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  34 B  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  35 B  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  36 B  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  37 B  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  38 B  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  39 B  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  40 B  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  41 B  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  42 B  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  43 B  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  44 B  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS
SEQRES  45 B  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  46 B  591  ARG ARG SER THR GLU LEU
MODRES 3HS7 ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3HS7 ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3HS7 ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3HS7 ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3HS7 ASN B  144  ASN  GLYCOSYLATION SITE
HET    AKR  A   2       5
HET    COH  A 619      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    HXA  A   1      24
HET    EDO  A 620       4
HET    EDO  A 621       4
HET    EDO  A   3       4
HET    EDO  A   5       4
HET    EDO  A   8       4
HET    AKR  B   2       5
HET    AKR  B   3       5
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    NAG  B 681      14
HET    BOG  B 703      20
HET    HXA  B   1      24
HET    EDO  B   4       4
HET    EDO  B   6       4
HET    EDO  B   7       4
HETNAM     AKR ACRYLIC ACID
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     HXA DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  AKR    3(C3 H4 O2)
FORMUL   4  COH    2(C34 H32 CO N4 O4)
FORMUL   5  NAG    10(C8 H15 N O6)
FORMUL   6  MAN    C6 H12 O6
FORMUL   8  BOG    2(C14 H28 O6)
FORMUL   9  HXA    2(C22 H32 O2)
FORMUL  10  EDO    8(C2 H6 O2)
FORMUL  26  HOH   *330(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 PHE A   96  ASN A  105  1                                  10
HELIX    4   4 ILE A  105A TYR A  122  1                                  18
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  HIS A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  295  HIS A  320  1                                  26
HELIX   13  13 GLY A  324  ASP A  347  1                                  24
HELIX   14  14 ASP A  347  GLY A  354  1                                   8
HELIX   15  15 ASP A  362  PHE A  367  5                                   6
HELIX   16  16 ALA A  378  TYR A  385  1                                   8
HELIX   17  17 TRP A  387  LEU A  391  5                                   5
HELIX   18  18 SER A  403  LEU A  408  1                                   6
HELIX   19  19 ASN A  411  GLN A  429  1                                  19
HELIX   20  20 PRO A  441  ALA A  443  5                                   3
HELIX   21  21 VAL A  444  MET A  458  1                                  15
HELIX   22  22 SER A  462  PHE A  470  1                                   9
HELIX   23  23 SER A  477  GLY A  483  1                                   7
HELIX   24  24 LYS A  485  SER A  496  1                                  12
HELIX   25  25 ASP A  497  MET A  501  5                                   5
HELIX   26  26 GLU A  502  GLU A  510  1                                   9
HELIX   27  27 GLY A  519  GLY A  536  1                                  18
HELIX   28  28 ASN A  537  SER A  541  5                                   5
HELIX   29  29 LYS A  546  GLY A  551  5                                   6
HELIX   30  30 GLY A  552  THR A  561  1                                  10
HELIX   31  31 SER A  563  VAL A  572  1                                  10
HELIX   32  32 GLU B   73  LYS B   83  1                                  11
HELIX   33  33 THR B   85  HIS B   95  1                                  11
HELIX   34  34 PHE B   96  ASN B  104  1                                   9
HELIX   35  35 ILE B  105A TYR B  122  1                                  18
HELIX   36  36 SER B  138  ASN B  144  1                                   7
HELIX   37  37 ASP B  173  LEU B  182  1                                  10
HELIX   38  38 ASN B  195  HIS B  207  1                                  13
HELIX   39  39 LEU B  230  GLY B  235  1                                   6
HELIX   40  40 THR B  237  ARG B  245  1                                   9
HELIX   41  41 THR B  265  GLN B  270  1                                   6
HELIX   42  42 PRO B  280  GLN B  284  5                                   5
HELIX   43  43 VAL B  295  HIS B  320  1                                  26
HELIX   44  44 GLY B  324  ASP B  347  1                                  24
HELIX   45  45 ASP B  347  GLY B  354  1                                   8
HELIX   46  46 ASP B  362  PHE B  367  5                                   6
HELIX   47  47 ALA B  378  TYR B  385  1                                   8
HELIX   48  48 HIS B  386  LEU B  391  5                                   6
HELIX   49  49 SER B  403  LEU B  408  1                                   6
HELIX   50  50 ASN B  411  GLN B  429  1                                  19
HELIX   51  51 PRO B  441  ALA B  443  5                                   3
HELIX   52  52 VAL B  444  MET B  458  1                                  15
HELIX   53  53 SER B  462  PHE B  470  1                                   9
HELIX   54  54 SER B  477  GLY B  483  1                                   7
HELIX   55  55 LYS B  485  SER B  496  1                                  12
HELIX   56  56 ASP B  497  MET B  501  5                                   5
HELIX   57  57 GLU B  502  GLU B  510  1                                   9
HELIX   58  58 GLY B  519  GLY B  536  1                                  18
HELIX   59  59 ASN B  537  SER B  541  5                                   5
HELIX   60  60 LYS B  546  GLY B  551  5                                   6
HELIX   61  61 GLY B  552  THR B  561  1                                  10
HELIX   62  62 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  LYS A  56   N  MET A  48
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65
SHEET    1   C 2 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130
SHEET    1   D 2 GLN A 255  ILE A 257  0
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   E 2 PHE A 395  ILE A 397  0
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   F 2 GLU B  46  SER B  49  0
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  LYS B  56   N  MET B  48
SHEET    1   G 2 PHE B  64  TYR B  65  0
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   H 2 TYR B 130  ASN B 131  0
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   I 2 GLN B 255  ILE B 257  0
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   J 2 PHE B 395  ILE B 397  0
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  GLN B 400   N  ILE B 397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
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  2.05
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.04
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.04
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.44
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.41
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.45
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         NE2AHIS B 388                CO   COH B 619     1555   1555  2.63
CISPEP   1 SER A  126    PRO A  127          0         1.98
CISPEP   2 SER B  126    PRO B  127          0         4.15
CISPEP   3 VAL B  582    GLN B  583          0        -9.23
SITE     1 AC1  3 SER A 477  PHE A 478  LYS A 492
SITE     1 AC2 12 GLN A 203  HIS A 207  PHE A 210  THR A 212
SITE     2 AC2 12 HIS A 214  VAL A 295  ASN A 382  TYR A 385
SITE     3 AC2 12 HIS A 386  HIS A 388  LEU A 391  GLN A 454
SITE     1 AC3  5 TYR A  55  GLU A  67  ASN A  68  HOH A 628
SITE     2 AC3  5 NAG A 662
SITE     1 AC4  2 NAG A 661  HOH A 747
SITE     1 AC5  6 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC5  6 NAG A 672  HOH A 677
SITE     1 AC6  3 ARG A 216  NAG A 671  MAN A 673
SITE     1 AC7  1 NAG A 672
SITE     1 AC8  6 GLN A 406  ASN A 410  SER A 412  ILE A 413
SITE     2 AC8  6 GLU A 416  HOH A 695
SITE     1 AC9 11 GLU A 179  LYS A 180  ARG A 184  ARG A 185
SITE     2 AC9 11 ARG A 438  GLU A 486  GLU A 490  GLU B 179
SITE     3 AC9 11 ARG B 184  GLN B 445  BOG B 703
SITE     1 BC1 16 ARG A 120  PHE A 205  PHE A 209  TYR A 348
SITE     2 BC1 16 LEU A 352  SER A 353  TYR A 355  ILE A 377
SITE     3 BC1 16 PHE A 381  TYR A 385  TRP A 387  ALA A 527
SITE     4 BC1 16 SER A 530  LEU A 531  GLY A 533  LEU A 534
SITE     1 BC2  5 ASP A 239  ARG A 240  LYS A 243  VAL A 271
SITE     2 BC2  5 GLU A 272
SITE     1 BC3  7 HIS A  90  GLN A 192  LEU A 352  ARG A 513
SITE     2 BC3  7 ALA A 516  PHE A 518  VAL A 523
SITE     1 BC4  5 LYS A 251  TYR A 254  VAL A 261  ASN A 310
SITE     2 BC4  5 HOH A 651
SITE     1 BC5  1 LEU A 415
SITE     1 BC6  5 PRO A 162  SER A 455  ARG A 456  LYS A 459
SITE     2 BC6  5 TYR A 460
SITE     1 BC7  4 SER B 477  PHE B 478  GLU B 479  LYS B 492
SITE     1 BC8  4 ARG B 240  LYS B 243  VAL B 271  GLU B 272
SITE     1 BC9 13 ALA B 199  GLN B 203  HIS B 207  PHE B 210
SITE     2 BC9 13 LYS B 211  THR B 212  HIS B 214  VAL B 295
SITE     3 BC9 13 ASN B 382  TYR B 385  HIS B 386  HIS B 388
SITE     4 BC9 13 LEU B 391
SITE     1 CC1  5 TYR B  55  GLU B  67  ASN B  68  HOH B 628
SITE     2 CC1  5 NAG B 662
SITE     1 CC2  1 NAG B 661
SITE     1 CC3  6 LEU A 238  ASN B 144  ARG B 216  NAG B 672
SITE     2 CC3  6 HOH B 704  HOH B 722
SITE     1 CC4  3 HOH B  27  ARG B 216  NAG B 671
SITE     1 CC5  6 ASN B 410  SER B 412  ILE B 413  GLU B 416
SITE     2 CC5  6 HOH B 693  HOH B 696
SITE     1 CC6 11 LYS A 180  ARG A 184  ARG A 185  ARG A 438
SITE     2 CC6 11 GLU A 486  GLU A 490  BOG A 703  GLU B 179
SITE     3 CC6 11 ARG B 184  ARG B 185  GLN B 445
SITE     1 CC7 15 ARG B 120  PHE B 205  PHE B 209  TYR B 348
SITE     2 CC7 15 VAL B 349  SER B 353  TYR B 355  PHE B 381
SITE     3 CC7 15 TYR B 385  TRP B 387  GLY B 526  ALA B 527
SITE     4 CC7 15 SER B 530  GLY B 533  LEU B 534
SITE     1 CC8  5 HOH B   9  PRO B 162  ARG B 456  LYS B 459
SITE     2 CC8  5 TYR B 460
SITE     1 CC9  8 HIS B  90  GLN B 192  LEU B 352  ARG B 513
SITE     2 CC9  8 ALA B 516  ILE B 517  PHE B 518  VAL B 523
SITE     1 DC1  1 GLN B 583
CRYST1  119.294  131.708  179.243  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      0.008383  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007593  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005579        0.00000
      
PROCHECK
Go to PROCHECK summary
 References