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PDBsum entry 3krk

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Oxidoreductase PDB id
3krk
Jmol
Contents
Protein chains
551 a.a.
Ligands
ACD ×2
AKR ×4
GOL ×3
COH ×2
NAG-NAG ×3
NAG ×2
BOG ×2
NAG-NAG-MAN
Waters ×632
HEADER    OXIDOREDUCTASE                          18-NOV-09   3KRK
TITLE     X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF L531F MURINE COX-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 20-604;
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   6 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   7 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   8 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   9 2;
COMPND  10 EC: 1.14.99.1;
COMPND  11 ENGINEERED: YES;
COMPND  12 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: COX-2, COX2, PGHS-B, PTGS2, 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: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS    COX-2, DIOXYGENASE, DISULFIDE BOND, ENDOPLASMIC RETICULUM, FATTY ACID
KEYWDS   2 BIOSYNTHESIS, GLYCOPROTEIN, HEME, IRON, LIPID SYNTHESIS, MEMBRANE,
KEYWDS   3 METAL-BINDING, MICROSOME, OXIDOREDUCTASE, PEROXIDASE,
KEYWDS   4 PHOSPHOPROTEIN, PROSTAGLANDIN BIOSYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI
REVDAT   3   04-AUG-10 3KRK    1       JRNL
REVDAT   2   02-JUN-10 3KRK    1       JRNL
REVDAT   1   12-MAY-10 3KRK    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.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6
REMARK   3   NUMBER OF REFLECTIONS             : 52249
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) : 0.182
REMARK   3   R VALUE            (WORKING SET) : 0.179
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2794
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) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3384
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.82
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260
REMARK   3   BIN FREE R VALUE SET COUNT          : 205
REMARK   3   BIN FREE R VALUE                    : 0.2980
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8899
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 359
REMARK   3   SOLVENT ATOMS            : 632
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 38.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.81000
REMARK   3    B22 (A**2) : 0.18000
REMARK   3    B33 (A**2) : -0.99000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.394
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.246
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.760
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9582 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13030 ; 1.470 ; 1.992
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1113 ; 5.058 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   446 ;36.949 ;23.946
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1513 ;14.383 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;13.405 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1393 ; 0.119 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7373 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5547 ; 0.260 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9007 ; 0.522 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4035 ; 0.957 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4017 ; 1.696 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 24
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    33        A    67
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8142   2.0089  56.8071
REMARK   3    T TENSOR
REMARK   3      T11:    .3152 T22:    .0188
REMARK   3      T33:    .1157 T12:   -.0758
REMARK   3      T13:    .0008 T23:    .0042
REMARK   3    L TENSOR
REMARK   3      L11:   1.8799 L22:    .4509
REMARK   3      L33:   1.8885 L12:   -.5788
REMARK   3      L13:   -.4927 L23:   -.0629
REMARK   3    S TENSOR
REMARK   3      S11:   -.0146 S12:    .0092 S13:   -.1477
REMARK   3      S21:    .1995 S22:   -.0427 S23:    .0308
REMARK   3      S31:    .3783 S32:   -.1134 S33:    .0573
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    68        A    87
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1325    .1774  62.4095
REMARK   3    T TENSOR
REMARK   3      T11:    .4253 T22:    .3106
REMARK   3      T33:    .6045 T12:    .1629
REMARK   3      T13:   -.2183 T23:   -.1662
REMARK   3    L TENSOR
REMARK   3      L11:   4.5922 L22:   3.6588
REMARK   3      L33:   2.2272 L12:    .7367
REMARK   3      L13:   -.5626 L23:   2.6738
REMARK   3    S TENSOR
REMARK   3      S11:    .0710 S12:    .6038 S13:   -.5293
REMARK   3      S21:    .7638 S22:    .7763 S23:  -1.2426
REMARK   3      S31:    .5675 S32:    .4573 S33:   -.8472
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):  59.0538  18.8241  64.4510
REMARK   3    T TENSOR
REMARK   3      T11:    .1640 T22:    .0562
REMARK   3      T33:    .2608 T12:    .0801
REMARK   3      T13:   -.0619 T23:    .0289
REMARK   3    L TENSOR
REMARK   3      L11:   4.2282 L22:   1.0626
REMARK   3      L33:   9.2058 L12:   1.6406
REMARK   3      L13:   -.8457 L23:  -2.0568
REMARK   3    S TENSOR
REMARK   3      S11:   -.0617 S12:   -.1521 S13:   -.4096
REMARK   3      S21:   -.0152 S22:   -.1205 S23:   -.3125
REMARK   3      S31:    .4163 S32:    .4186 S33:    .1821
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   157
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1891  18.9720  52.4193
REMARK   3    T TENSOR
REMARK   3      T11:    .1002 T22:    .0469
REMARK   3      T33:    .0775 T12:   -.0162
REMARK   3      T13:    .0061 T23:   -.0089
REMARK   3    L TENSOR
REMARK   3      L11:   2.2904 L22:    .7676
REMARK   3      L33:   1.5396 L12:    .8361
REMARK   3      L13:   -.2412 L23:    .4400
REMARK   3    S TENSOR
REMARK   3      S11:    .0360 S12:   -.0574 S13:   -.1230
REMARK   3      S21:    .1088 S22:   -.0636 S23:   -.0639
REMARK   3      S31:    .1599 S32:    .0323 S33:    .0276
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   158        A   217
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9297  28.2432  71.7410
REMARK   3    T TENSOR
REMARK   3      T11:    .1249 T22:    .1091
REMARK   3      T33:    .1236 T12:   -.0216
REMARK   3      T13:    .0167 T23:   -.0224
REMARK   3    L TENSOR
REMARK   3      L11:    .8479 L22:    .8444
REMARK   3      L33:    .8785 L12:    .6638
REMARK   3      L13:   -.2230 L23:    .1136
REMARK   3    S TENSOR
REMARK   3      S11:    .0612 S12:   -.0915 S13:    .0790
REMARK   3      S21:    .1576 S22:   -.0281 S23:    .1340
REMARK   3      S31:    .0900 S32:   -.0800 S33:   -.0331
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   218        A   268
REMARK   3    ORIGIN FOR THE GROUP (A):  36.9863  47.6481  52.3648
REMARK   3    T TENSOR
REMARK   3      T11:    .0589 T22:    .0941
REMARK   3      T33:    .1746 T12:    .0024
REMARK   3      T13:   -.0060 T23:   -.0294
REMARK   3    L TENSOR
REMARK   3      L11:    .1106 L22:   1.7399
REMARK   3      L33:    .9386 L12:    .3492
REMARK   3      L13:    .0121 L23:    .1606
REMARK   3    S TENSOR
REMARK   3      S11:   -.0318 S12:    .0041 S13:    .0998
REMARK   3      S21:   -.1194 S22:    .0792 S23:    .0921
REMARK   3      S31:   -.2004 S32:   -.0953 S33:   -.0473
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   304
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5158  50.7170  61.9361
REMARK   3    T TENSOR
REMARK   3      T11:    .1057 T22:    .0996
REMARK   3      T33:    .1607 T12:    .0136
REMARK   3      T13:    .0266 T23:   -.0369
REMARK   3    L TENSOR
REMARK   3      L11:   2.0369 L22:   4.3051
REMARK   3      L33:   1.6800 L12:  -1.4323
REMARK   3      L13:    .2329 L23:   -.7656
REMARK   3    S TENSOR
REMARK   3      S11:   -.0021 S12:   -.1686 S13:    .1772
REMARK   3      S21:    .1018 S22:    .1471 S23:    .3592
REMARK   3      S31:   -.1890 S32:   -.2914 S33:   -.1450
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   305        A   376
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0587  36.5968  52.3581
REMARK   3    T TENSOR
REMARK   3      T11:    .0363 T22:    .1185
REMARK   3      T33:    .1468 T12:    .0007
REMARK   3      T13:    .0105 T23:   -.0329
REMARK   3    L TENSOR
REMARK   3      L11:    .6247 L22:    .8360
REMARK   3      L33:   1.1639 L12:    .2899
REMARK   3      L13:   -.0466 L23:    .0692
REMARK   3    S TENSOR
REMARK   3      S11:    .0137 S12:   -.0878 S13:   -.0086
REMARK   3      S21:    .0966 S22:    .0063 S23:   -.1558
REMARK   3      S31:   -.0135 S32:    .1572 S33:   -.0200
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   377        A   412
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8432  39.5040  72.5605
REMARK   3    T TENSOR
REMARK   3      T11:    .0702 T22:    .1128
REMARK   3      T33:    .0819 T12:   -.0016
REMARK   3      T13:    .0115 T23:   -.0206
REMARK   3    L TENSOR
REMARK   3      L11:    .4657 L22:   2.4445
REMARK   3      L33:   2.2317 L12:   -.0079
REMARK   3      L13:   -.2095 L23:   1.4036
REMARK   3    S TENSOR
REMARK   3      S11:   -.0089 S12:   -.1463 S13:    .0754
REMARK   3      S21:    .1793 S22:    .0108 S23:    .1569
REMARK   3      S31:   -.0956 S32:   -.0119 S33:   -.0020
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   413        A   469
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0269  33.3542  73.0304
REMARK   3    T TENSOR
REMARK   3      T11:    .0666 T22:    .1154
REMARK   3      T33:    .0606 T12:    .0009
REMARK   3      T13:    .0169 T23:   -.0217
REMARK   3    L TENSOR
REMARK   3      L11:    .8661 L22:   1.2002
REMARK   3      L33:    .7800 L12:    .5038
REMARK   3      L13:    .0719 L23:    .0191
REMARK   3    S TENSOR
REMARK   3      S11:    .0426 S12:   -.1479 S13:    .0520
REMARK   3      S21:    .1146 S22:   -.0114 S23:    .0125
REMARK   3      S31:    .0647 S32:   -.0161 S33:   -.0312
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   470        A   557
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4439  21.2100  67.1377
REMARK   3    T TENSOR
REMARK   3      T11:    .1230 T22:    .0806
REMARK   3      T33:    .1152 T12:    .0054
REMARK   3      T13:   -.0298 T23:   -.0064
REMARK   3    L TENSOR
REMARK   3      L11:    .9730 L22:    .9015
REMARK   3      L33:   1.5784 L12:    .4366
REMARK   3      L13:   -.7874 L23:   -.5663
REMARK   3    S TENSOR
REMARK   3      S11:    .0096 S12:   -.1403 S13:   -.1075
REMARK   3      S21:    .1837 S22:   -.0024 S23:   -.0734
REMARK   3      S31:    .1769 S32:    .1076 S33:   -.0072
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   558        A   584
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1949  43.2934  64.0958
REMARK   3    T TENSOR
REMARK   3      T11:    .1026 T22:    .1689
REMARK   3      T33:    .1753 T12:   -.0078
REMARK   3      T13:   -.0724 T23:   -.0415
REMARK   3    L TENSOR
REMARK   3      L11:   2.0873 L22:    .4082
REMARK   3      L33:   2.4933 L12:    .3364
REMARK   3      L13:  -2.1480 L23:   -.0301
REMARK   3    S TENSOR
REMARK   3      S11:    .0880 S12:   -.3103 S13:   -.1251
REMARK   3      S21:    .1756 S22:   -.0284 S23:   -.2291
REMARK   3      S31:    .0533 S32:    .3462 S33:   -.0596
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):  59.0378  38.1608  30.6988
REMARK   3    T TENSOR
REMARK   3      T11:    .0340 T22:    .1356
REMARK   3      T33:    .1441 T12:   -.0401
REMARK   3      T13:    .0421 T23:   -.0363
REMARK   3    L TENSOR
REMARK   3      L11:   1.1728 L22:    .9389
REMARK   3      L33:   2.6506 L12:   -.3558
REMARK   3      L13:    .1243 L23:    .1617
REMARK   3    S TENSOR
REMARK   3      S11:   -.0394 S12:    .0384 S13:    .0303
REMARK   3      S21:    .0022 S22:    .1264 S23:   -.0277
REMARK   3      S31:   -.1845 S32:    .2976 S33:   -.0870
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    79
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8898  24.2193  29.1626
REMARK   3    T TENSOR
REMARK   3      T11:    .1785 T22:    .2674
REMARK   3      T33:    .2488 T12:    .0419
REMARK   3      T13:   -.0020 T23:   -.0834
REMARK   3    L TENSOR
REMARK   3      L11:   3.3778 L22:   9.4923
REMARK   3      L33:   3.6052 L12:  -2.7992
REMARK   3      L13:   -.3984 L23:  -1.6736
REMARK   3    S TENSOR
REMARK   3      S11:   -.0774 S12:    .1525 S13:   -.3160
REMARK   3      S21:    .7237 S22:   -.1344 S23:   -.4514
REMARK   3      S31:    .3480 S32:    .4007 S33:    .2118
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    80        B   122
REMARK   3    ORIGIN FOR THE GROUP (A):  49.3972   5.5095  23.4112
REMARK   3    T TENSOR
REMARK   3      T11:    .1057 T22:    .1176
REMARK   3      T33:    .2411 T12:    .0712
REMARK   3      T13:   -.0200 T23:    .0101
REMARK   3    L TENSOR
REMARK   3      L11:   2.3941 L22:   1.8442
REMARK   3      L33:   2.7842 L12:    .9692
REMARK   3      L13:  -2.3537 L23:   -.1621
REMARK   3    S TENSOR
REMARK   3      S11:   -.1524 S12:   -.1947 S13:   -.2608
REMARK   3      S21:    .1771 S22:   -.0604 S23:   -.3199
REMARK   3      S31:    .2802 S32:    .2221 S33:    .2128
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   157
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4534  34.5298  34.4727
REMARK   3    T TENSOR
REMARK   3      T11:    .0699 T22:    .1145
REMARK   3      T33:    .1424 T12:   -.0154
REMARK   3      T13:   -.0041 T23:    .0024
REMARK   3    L TENSOR
REMARK   3      L11:    .0251 L22:   1.7513
REMARK   3      L33:    .8086 L12:    .1911
REMARK   3      L13:   -.0156 L23:    .2557
REMARK   3    S TENSOR
REMARK   3      S11:   -.0018 S12:   -.0120 S13:   -.0347
REMARK   3      S21:   -.0271 S22:    .0088 S23:   -.1707
REMARK   3      S31:   -.0242 S32:    .2120 S33:   -.0070
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   158        B   217
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5562  29.7178  14.8492
REMARK   3    T TENSOR
REMARK   3      T11:    .1853 T22:    .1293
REMARK   3      T33:    .1330 T12:   -.0342
REMARK   3      T13:   -.0090 T23:    .0021
REMARK   3    L TENSOR
REMARK   3      L11:    .9355 L22:    .2352
REMARK   3      L33:    .2758 L12:    .4066
REMARK   3      L13:   -.1511 L23:   -.0585
REMARK   3    S TENSOR
REMARK   3      S11:   -.0353 S12:    .1568 S13:    .1588
REMARK   3      S21:   -.0994 S22:    .0622 S23:    .1034
REMARK   3      S31:   -.1047 S32:    .0110 S33:   -.0269
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   218        B   236
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6862  26.6879  32.8928
REMARK   3    T TENSOR
REMARK   3      T11:    .1829 T22:    .0938
REMARK   3      T33:    .1329 T12:   -.0317
REMARK   3      T13:    .0234 T23:   -.0198
REMARK   3    L TENSOR
REMARK   3      L11:   1.8002 L22:    .1474
REMARK   3      L33:    .0742 L12:    .4706
REMARK   3      L13:   -.3627 L23:   -.0996
REMARK   3    S TENSOR
REMARK   3      S11:    .0323 S12:    .0866 S13:    .0747
REMARK   3      S21:    .0724 S22:   -.0017 S23:    .0477
REMARK   3      S31:   -.0200 S32:   -.0174 S33:   -.0306
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   237        B   321
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5855  18.9592  30.5535
REMARK   3    T TENSOR
REMARK   3      T11:    .0401 T22:    .1092
REMARK   3      T33:    .1572 T12:   -.0100
REMARK   3      T13:    .0083 T23:   -.0214
REMARK   3    L TENSOR
REMARK   3      L11:   1.3390 L22:   1.0607
REMARK   3      L33:   1.9567 L12:    .0192
REMARK   3      L13:   -.1267 L23:    .1154
REMARK   3    S TENSOR
REMARK   3      S11:    .0089 S12:    .0923 S13:    .1246
REMARK   3      S21:   -.0010 S22:    .0455 S23:    .1402
REMARK   3      S31:   -.0466 S32:   -.1935 S33:   -.0543
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   322        B   385
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8709  12.7062  33.4306
REMARK   3    T TENSOR
REMARK   3      T11:    .0803 T22:    .0530
REMARK   3      T33:    .1348 T12:    .0093
REMARK   3      T13:   -.0019 T23:   -.0125
REMARK   3    L TENSOR
REMARK   3      L11:    .5907 L22:    .3356
REMARK   3      L33:   1.2603 L12:    .2518
REMARK   3      L13:   -.3813 L23:    .1427
REMARK   3    S TENSOR
REMARK   3      S11:   -.0530 S12:    .0770 S13:   -.0919
REMARK   3      S21:    .0052 S22:    .0626 S23:   -.0431
REMARK   3      S31:    .1739 S32:    .0733 S33:   -.0095
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   386        B   429
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7954  18.2177  11.4505
REMARK   3    T TENSOR
REMARK   3      T11:    .1123 T22:    .1488
REMARK   3      T33:    .0388 T12:   -.0069
REMARK   3      T13:   -.0203 T23:   -.0005
REMARK   3    L TENSOR
REMARK   3      L11:   4.3471 L22:   1.2995
REMARK   3      L33:   1.2079 L12:    .1325
REMARK   3      L13:    .0756 L23:   -.1185
REMARK   3    S TENSOR
REMARK   3      S11:   -.0069 S12:    .2008 S13:    .1009
REMARK   3      S21:   -.1998 S22:    .0352 S23:    .2088
REMARK   3      S31:    .0968 S32:   -.1985 S33:   -.0284
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   430        B   465
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3394  31.0537  12.6825
REMARK   3    T TENSOR
REMARK   3      T11:    .1403 T22:    .1162
REMARK   3      T33:    .0903 T12:   -.0341
REMARK   3      T13:    .0045 T23:    .0011
REMARK   3    L TENSOR
REMARK   3      L11:    .6160 L22:    .5212
REMARK   3      L33:    .8009 L12:    .5348
REMARK   3      L13:    .4185 L23:    .5146
REMARK   3    S TENSOR
REMARK   3      S11:   -.0490 S12:    .0900 S13:    .0897
REMARK   3      S21:   -.1054 S22:    .0687 S23:    .0505
REMARK   3      S31:   -.1108 S32:    .0022 S33:   -.0197
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   466        B   550
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1214  23.4613  18.5456
REMARK   3    T TENSOR
REMARK   3      T11:    .0942 T22:    .0946
REMARK   3      T33:    .1078 T12:   -.0117
REMARK   3      T13:    .0268 T23:   -.0453
REMARK   3    L TENSOR
REMARK   3      L11:    .9552 L22:   1.3712
REMARK   3      L33:   1.4657 L12:    .5566
REMARK   3      L13:   -.4444 L23:   -.7249
REMARK   3    S TENSOR
REMARK   3      S11:   -.0352 S12:    .1917 S13:   -.0312
REMARK   3      S21:   -.1725 S22:    .0690 S23:   -.1232
REMARK   3      S31:   -.0266 S32:    .0944 S33:   -.0339
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   551        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0424   3.8117  27.4408
REMARK   3    T TENSOR
REMARK   3      T11:    .1152 T22:    .0572
REMARK   3      T33:    .1267 T12:   -.0064
REMARK   3      T13:   -.0061 T23:   -.0267
REMARK   3    L TENSOR
REMARK   3      L11:    .8150 L22:   1.2156
REMARK   3      L33:   2.7240 L12:    .2796
REMARK   3      L13:    .3071 L23:   -.3235
REMARK   3    S TENSOR
REMARK   3      S11:    .0693 S12:    .1022 S13:   -.2627
REMARK   3      S21:   -.0865 S22:    .0180 S23:   -.0344
REMARK   3      S31:    .3431 S32:    .0104 S33:   -.0874
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3KRK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9777
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CUT SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55133
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8
REMARK 200  DATA REDUNDANCY                : 5.800
REMARK 200  R MERGE                    (I) : 0.17400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.100
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   (%): 53.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 0.1M
REMARK 280  HEPES PH 7.5, 0.02M 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       60.39500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.52000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.32700
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.39500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.52000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.32700
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.39500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.52000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.32700
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.39500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.52000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.32700
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: 5050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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     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  83    CD   CE   NZ
REMARK 470     LYS A  97    CE   NZ
REMARK 470     LYS A 169    CD   CE   NZ
REMARK 470     GLU A 170    CD   OE1  OE2
REMARK 470     LYS A 175    CE   NZ
REMARK 470     LYS A 215    CG   CD   CE   NZ
REMARK 470     ARG A 222    NE   CZ   NH1  NH2
REMARK 470     GLU A 272    CG   CD   OE1  OE2
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 511    NZ
REMARK 470     GLN B  54    CD   OE1  NE2
REMARK 470     LEU B  75    CG   CD1  CD2
REMARK 470     ILE B  78    CD1
REMARK 470     LYS B  79    CE   NZ
REMARK 470     LEU B  81    CD1  CD2
REMARK 470     LYS B 114    NZ
REMARK 470     LYS B 169    CD   CE   NZ
REMARK 470     GLU B 170    CG   CD   OE1  OE2
REMARK 470     LYS B 175    NZ
REMARK 470     ASP B 239    OD1  OD2
REMARK 470     GLU B 281    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   ND2  ASN A   410     O5   NAG A   681              1.54
REMARK 500   O    LEU B   123     NH2  ARG B   469              2.18
REMARK 500   NH2  ARG B   240     O    GLU B   272              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    ARG A  61       19.44     59.04
REMARK 500    THR A 129      -92.52   -114.78
REMARK 500    ARG A 185      -65.59    -92.98
REMARK 500    ASP A 249       19.97     58.21
REMARK 500    TRP A 387       45.58    -88.42
REMARK 500    GLU A 398     -116.52     51.71
REMARK 500    ASN A 439       17.51   -141.90
REMARK 500    SER A 496      -38.64     70.13
REMARK 500    CYS A 575       64.18     38.69
REMARK 500    THR B 129      -92.49   -111.52
REMARK 500    ARG B 185      -98.66    -90.15
REMARK 500    GLU B 398     -106.42     53.20
REMARK 500    ASN B 410       79.49   -113.35
REMARK 500    ASN B 439       13.09   -143.77
REMARK 500    SER B 496      -48.26     70.67
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 657        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH A 679        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A 706        DISTANCE =  5.79 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 673
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF 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
DBREF  3KRK A   35   618  UNP    Q05769   PGH2_MOUSE      20    604
DBREF  3KRK B   35   618  UNP    Q05769   PGH2_MOUSE      20    604
SEQADV 3KRK HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK PHE A  531  UNP  Q05769    LEU   517 ENGINEERED
SEQADV 3KRK ALA A  594  UNP  Q05769    ASN   580 ENGINEERED
SEQADV 3KRK HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3KRK PHE B  531  UNP  Q05769    LEU   517 ENGINEERED
SEQADV 3KRK 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 PHE 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 PHE 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 3KRK ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3KRK ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3KRK ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3KRK ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3KRK ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3KRK ASN B  410  ASN  GLYCOSYLATION SITE
HET    ACD  A 700      22
HET    AKR  A 622       5
HET    AKR  A 623       5
HET    GOL  A 624       6
HET    COH  A 625      43
HET    NAG  A 661      14
HET    NAG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 681      14
HET    BOG  A 703      20
HET    GOL  A 619       6
HET    ACD  B 700      22
HET    AKR  B 622       5
HET    AKR  B 623       5
HET    GOL  B 624       6
HET    COH  B 626      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
HET    BOG  B 703      20
HETNAM     ACD ARACHIDONIC ACID
HETNAM     AKR ACRYLIC ACID
HETNAM     GOL GLYCEROL
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     MAN ALPHA-D-MANNOSE
FORMUL   3  ACD    2(C20 H32 O2)
FORMUL   4  AKR    4(C3 H4 O2)
FORMUL   6  GOL    3(C3 H8 O3)
FORMUL   7  COH    2(C34 H32 CO N4 O4)
FORMUL   8  NAG    10(C8 H15 N O6)
FORMUL  11  BOG    2(C14 H28 O6)
FORMUL  19  MAN    C6 H12 O6
FORMUL  22  HOH   *632(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  HIS A   95  1                                  11
HELIX    3   3 PHE A   96  ASN A  105  1                                  10
HELIX    4   4 ILE A  105A TYR A  122  1                                  18
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  HIS A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 VAL A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  ASP A  347  1                                  24
HELIX   15  15 ASP A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 TRP A  387  LEU A  391  5                                   5
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  410  GLY A  418  1                                   9
HELIX   21  21 GLY A  418  GLN A  429  1                                  12
HELIX   22  22 PRO A  441  ALA A  443  5                                   3
HELIX   23  23 VAL A  444  MET A  458  1                                  15
HELIX   24  24 SER A  462  PHE A  470  1                                   9
HELIX   25  25 SER A  477  GLY A  483  1                                   7
HELIX   26  26 LYS A  485  SER A  496  1                                  12
HELIX   27  27 ASP A  497  MET A  501  5                                   5
HELIX   28  28 GLU A  502  GLU A  510  1                                   9
HELIX   29  29 GLY A  519  GLY A  536  1                                  18
HELIX   30  30 ASN A  537  SER A  541  5                                   5
HELIX   31  31 LYS A  546  GLY A  551  5                                   6
HELIX   32  32 GLY A  552  THR A  561  1                                  10
HELIX   33  33 SER A  563  VAL A  572  1                                  10
HELIX   34  34 GLU B   73  LEU B   82  1                                  10
HELIX   35  35 THR B   85  HIS B   95  1                                  11
HELIX   36  36 PHE B   96  ASN B  104  1                                   9
HELIX   37  37 ILE B  105A TYR B  122  1                                  18
HELIX   38  38 SER B  138  ASN B  144  1                                   7
HELIX   39  39 ASP B  173  LEU B  182  1                                  10
HELIX   40  40 ASN B  195  HIS B  207  1                                  13
HELIX   41  41 LEU B  230  GLY B  235  1                                   6
HELIX   42  42 THR B  237  ARG B  245  1                                   9
HELIX   43  43 THR B  265  GLN B  270  1                                   6
HELIX   44  44 PRO B  280  GLN B  284  5                                   5
HELIX   45  45 VAL B  291  LEU B  294  5                                   4
HELIX   46  46 VAL B  295  HIS B  320  1                                  26
HELIX   47  47 GLY B  324  ASP B  347  1                                  24
HELIX   48  48 ASP B  347  GLY B  354  1                                   8
HELIX   49  49 ASP B  362  PHE B  367  5                                   6
HELIX   50  50 ALA B  378  TYR B  385  1                                   8
HELIX   51  51 HIS B  386  LEU B  391  5                                   6
HELIX   52  52 SER B  403  LEU B  408  1                                   6
HELIX   53  53 ASN B  411  GLN B  429  1                                  19
HELIX   54  54 PRO B  441  ALA B  443  5                                   3
HELIX   55  55 VAL B  444  MET B  458  1                                  15
HELIX   56  56 SER B  462  PHE B  470  1                                   9
HELIX   57  57 SER B  477  GLY B  483  1                                   7
HELIX   58  58 LYS B  485  SER B  496  1                                  12
HELIX   59  59 ASP B  497  MET B  501  5                                   5
HELIX   60  60 GLU B  502  GLU B  510  1                                   9
HELIX   61  61 GLY B  519  GLY B  536  1                                  18
HELIX   62  62 ASN B  537  SER B  541  5                                   5
HELIX   63  63 LYS B  546  GLY B  551  5                                   6
HELIX   64  64 GLY B  552  THR B  561  1                                  10
HELIX   65  65 SER B  563  VAL B  572  1                                  10
SHEET    1   A 2 GLU A  46  SER A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  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  ASP B  58   N  GLU B  46
SHEET    1   G 2 PHE B  64  TYR B  65  0
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   H 2 TYR B 130  ASN B 131  0
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   I 2 GLN B 255  ILE B 257  0
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   J 2 PHE B 395  ILE B 397  0
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
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  2.06
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05
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  2.05
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.04
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.43
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.38
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN B 410                 C1  NAG B 681     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  1.44
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44
LINK         O4  NAG B 672                 C1  MAN B 673     1555   1555  1.45
CISPEP   1 SER A  126    PRO A  127          0         2.91
CISPEP   2 SER B  126    PRO B  127          0         1.24
SITE     1 AC1 13 ARG A 120  PHE A 205  TYR A 348  LEU A 352
SITE     2 AC1 13 TYR A 355  ILE A 377  TYR A 385  TRP A 387
SITE     3 AC1 13 VAL A 523  SER A 530  PHE A 531  GLY A 533
SITE     4 AC1 13 LEU A 534
SITE     1 AC2  5 SER A 477  PHE A 478  GLU A 479  LYS A 492
SITE     2 AC2  5 HOH A 917
SITE     1 AC3  6 ASP A 239  ARG A 240  LYS A 243  GLN A 270
SITE     2 AC3  6 VAL A 271  GLU A 272
SITE     1 AC4  7 HIS A  34  CYS A  36  PRO A 154  VAL A 155
SITE     2 AC4  7 ALA A 156  HOH A 800  HOH A 810
SITE     1 AC5 12 GLN A 203  HIS A 207  PHE A 210  THR A 212
SITE     2 AC5 12 HIS A 214  ASN A 382  TYR A 385  HIS A 386
SITE     3 AC5 12 HIS A 388  LEU A 391  GLN A 454  HOH A 634
SITE     1 AC6  6 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 AC6  6 HOH A 749  HOH A 778
SITE     1 AC7  1 NAG A 661
SITE     1 AC8  7 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC8  7 NAG A 672  HOH A 740  HOH A 811
SITE     1 AC9  6 ARG A 216  NAG A 671  HOH A 676  HOH A 763
SITE     2 AC9  6 HOH A 877  ASP B 239
SITE     1 BC1  5 GLN A 406  ASN A 410  ILE A 413  GLU A 416
SITE     2 BC1  5 HOH A 816
SITE     1 BC2 12 GLU A 179  ARG A 184  ARG A 185  ARG A 438
SITE     2 BC2 12 GLU A 486  GLU A 490  GLU B 179  ARG B 184
SITE     3 BC2 12 ARG B 185  ILE B 442  GLN B 445  BOG B 703
SITE     1 BC3  5 THR A  60  ARG A  61  TYR A 122  GLN B 543
SITE     2 BC3  5 LYS B 546
SITE     1 BC4 19 ARG B 120  PHE B 205  PHE B 209  TYR B 348
SITE     2 BC4 19 VAL B 349  LEU B 352  SER B 353  TYR B 355
SITE     3 BC4 19 ILE B 377  PHE B 381  TYR B 385  TRP B 387
SITE     4 BC4 19 MET B 522  VAL B 523  GLY B 526  SER B 530
SITE     5 BC4 19 PHE B 531  GLY B 533  LEU B 534
SITE     1 BC5  4 SER B 477  PHE B 478  GLU B 479  LYS B 492
SITE     1 BC6  4 ARG B 240  LYS B 243  VAL B 271  GLU B 272
SITE     1 BC7  7 CYS B  36  CYS B  37  PRO B 154  VAL B 155
SITE     2 BC7  7 ALA B 156  CYS B 159  HOH B 643
SITE     1 BC8 10 GLN B 203  HIS B 207  PHE B 210  THR B 212
SITE     2 BC8 10 HIS B 214  ASN B 382  TYR B 385  HIS B 386
SITE     3 BC8 10 HIS B 388  LEU B 391
SITE     1 BC9  5 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     2 BC9  5 HOH B 894
SITE     1 CC1  1 NAG B 661
SITE     1 CC2  7 GLU B 140  ASN B 144  TYR B 147  ARG B 216
SITE     2 CC2  7 HOH B 631  NAG B 672  HOH B 801
SITE     1 CC3  4 ARG B 216  NAG B 671  MAN B 673  HOH B 908
SITE     1 CC4  2 NAG B 672  HOH B 830
SITE     1 CC5  7 GLN B 406  ASN B 410  SER B 412  ILE B 413
SITE     2 CC5  7 GLU B 416  HOH B 630  HOH B 871
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
CRYST1  120.790  133.040  180.654  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      0.008279  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007517  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005535        0.00000
      
PROCHECK
Go to PROCHECK summary
 References