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PDBsum entry 3qh0

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Oxidoreductase PDB id
3qh0
Jmol
Contents
Protein chains
552 a.a.
Ligands
EDO ×23
PLM
AKR ×2
COH ×2
HSQ-NAG
NAG-NAG-MAN
NAG ×2
BOG
NAG-NDG
NAG-NAG
Waters ×753
HEADER    OXIDOREDUCTASE                          25-JAN-11   3QH0
TITLE     X-RAY CRYSTAL STRUCTURE OF PALMITIC ACID BOUND TO THE CYCLOOXYGENASE
TITLE    2 CHANNEL OF CYCLOOXYGENASE-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUE 1-608;
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED
COMPND   6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND   7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND   8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND   9 SYNTHASE 2, TIS10 PROTEIN;
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: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    BIOLOGICAL DIMER, OXIDOREDUCTASE, N-GLYCOSYLATION, MONOTOPIC MEMBRANE
KEYWDS   2 PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI
REVDAT   2   08-JUN-11 3QH0    1       JRNL
REVDAT   1   13-APR-11 3QH0    0
JRNL        AUTH   L.DONG,A.J.VECCHIO,N.P.SHARMA,B.J.JURBAN,M.G.MALKOWSKI,
JRNL        AUTH 2 W.L.SMITH
JRNL        TITL   HUMAN CYCLOOXYGENASE-2 IS A SEQUENCE HOMODIMER THAT
JRNL        TITL 2 FUNCTIONS AS A CONFORMATIONAL HETERODIMER.
JRNL        REF    J.BIOL.CHEM.                  V. 286 19035 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21467029
JRNL        DOI    10.1074/JBC.M111.231969
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 77928
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) : 0.161
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.199
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4122
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5576
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.52
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110
REMARK   3   BIN FREE R VALUE SET COUNT          : 310
REMARK   3   BIN FREE R VALUE                    : 0.2760
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8833
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 377
REMARK   3   SOLVENT ATOMS            : 753
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.19
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : -0.05000
REMARK   3    B33 (A**2) : 0.05000
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): 0.177
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.901
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9570 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13009 ; 1.329 ; 2.001
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1129 ; 5.692 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   446 ;37.361 ;23.924
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1482 ;13.632 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.880 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1380 ; 0.093 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7344 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5565 ; 0.502 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9044 ; 0.970 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4005 ; 1.841 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3952 ; 3.063 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 24
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    33        A    68
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3394  37.1273  59.8920
REMARK   3    T TENSOR
REMARK   3      T11:    .0594 T22:    .2753
REMARK   3      T33:    .1489 T12:    .0664
REMARK   3      T13:    .0495 T23:    .0758
REMARK   3    L TENSOR
REMARK   3      L11:   1.0567 L22:   3.8869
REMARK   3      L33:   1.9850 L12:   -.0687
REMARK   3      L13:    .1704 L23:   1.0562
REMARK   3    S TENSOR
REMARK   3      S11:   -.0529 S12:   -.2515 S13:    .0305
REMARK   3      S21:    .0506 S22:    .1627 S23:    .0524
REMARK   3      S31:   -.1368 S32:   -.5552 S33:   -.1097
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    69        A    86
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5201  18.1978  63.7919
REMARK   3    T TENSOR
REMARK   3      T11:    .2147 T22:    .5097
REMARK   3      T33:    .4432 T12:   -.1428
REMARK   3      T13:    .0409 T23:    .1654
REMARK   3    L TENSOR
REMARK   3      L11:   4.9645 L22:   9.9081
REMARK   3      L33:   4.1743 L12:  -3.2354
REMARK   3      L13:   4.1029 L23:  -5.1141
REMARK   3    S TENSOR
REMARK   3      S11:    .2881 S12:   -.3324 S13:   -.8992
REMARK   3      S21:   -.4332 S22:    .5422 S23:    .7747
REMARK   3      S31:    .3520 S32:   -.4681 S33:   -.8303
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    87        A   120
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2572   2.3740  66.6624
REMARK   3    T TENSOR
REMARK   3      T11:    .1581 T22:    .2294
REMARK   3      T33:    .3367 T12:   -.1614
REMARK   3      T13:    .0069 T23:    .0579
REMARK   3    L TENSOR
REMARK   3      L11:   1.8541 L22:   4.1887
REMARK   3      L33:   6.7349 L12:   -.2957
REMARK   3      L13:  -1.2977 L23:   -.7335
REMARK   3    S TENSOR
REMARK   3      S11:   -.1090 S12:   -.0229 S13:   -.4238
REMARK   3      S21:    .0914 S22:    .0543 S23:    .2639
REMARK   3      S31:    .9159 S32:   -.7527 S33:    .0547
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   186
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3088  35.4625  66.3008
REMARK   3    T TENSOR
REMARK   3      T11:    .0711 T22:    .1059
REMARK   3      T33:    .0660 T12:    .0664
REMARK   3      T13:    .0060 T23:    .0074
REMARK   3    L TENSOR
REMARK   3      L11:    .5823 L22:    .6588
REMARK   3      L33:   1.6769 L12:   -.3063
REMARK   3      L13:    .1925 L23:   -.4991
REMARK   3    S TENSOR
REMARK   3      S11:   -.1028 S12:   -.1532 S13:    .0351
REMARK   3      S21:    .1144 S22:    .1555 S23:    .0320
REMARK   3      S31:   -.1028 S32:   -.1831 S33:   -.0526
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   187        A   235
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2293  22.8000  66.6822
REMARK   3    T TENSOR
REMARK   3      T11:    .0285 T22:    .0418
REMARK   3      T33:    .0629 T12:    .0067
REMARK   3      T13:   -.0110 T23:   -.0094
REMARK   3    L TENSOR
REMARK   3      L11:    .8995 L22:   1.0728
REMARK   3      L33:   1.6292 L12:   -.8327
REMARK   3      L13:    .1379 L23:   -.2955
REMARK   3    S TENSOR
REMARK   3      S11:   -.0628 S12:   -.1261 S13:    .0705
REMARK   3      S21:    .0834 S22:    .0895 S23:   -.1018
REMARK   3      S31:   -.0349 S32:   -.0293 S33:   -.0266
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   236        A   268
REMARK   3    ORIGIN FOR THE GROUP (A):  51.5671  19.0139  55.7902
REMARK   3    T TENSOR
REMARK   3      T11:    .0203 T22:    .0472
REMARK   3      T33:    .1319 T12:    .0046
REMARK   3      T13:    .0296 T23:   -.0080
REMARK   3    L TENSOR
REMARK   3      L11:   2.1833 L22:   1.7125
REMARK   3      L33:   2.2638 L12:   -.0524
REMARK   3      L13:    .8620 L23:   -.3659
REMARK   3    S TENSOR
REMARK   3      S11:    .1239 S12:    .0527 S13:    .0733
REMARK   3      S21:   -.0476 S22:   -.0058 S23:   -.1649
REMARK   3      S31:   -.0200 S32:    .2600 S33:   -.1180
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   296
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6128  26.8737  65.6095
REMARK   3    T TENSOR
REMARK   3      T11:    .0492 T22:    .0532
REMARK   3      T33:    .2295 T12:   -.0116
REMARK   3      T13:    .0262 T23:   -.0636
REMARK   3    L TENSOR
REMARK   3      L11:   5.3535 L22:   3.4482
REMARK   3      L33:   4.8179 L12:    .5336
REMARK   3      L13:  -1.0888 L23:  -1.2187
REMARK   3    S TENSOR
REMARK   3      S11:   -.0794 S12:   -.3901 S13:    .5118
REMARK   3      S21:    .1102 S22:    .0015 S23:   -.2920
REMARK   3      S31:   -.3354 S32:    .2622 S33:    .0779
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   297        A   375
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8904   9.4197  56.2276
REMARK   3    T TENSOR
REMARK   3      T11:    .0659 T22:    .0040
REMARK   3      T33:    .0926 T12:   -.0039
REMARK   3      T13:   -.0282 T23:    .0116
REMARK   3    L TENSOR
REMARK   3      L11:   1.3031 L22:    .7833
REMARK   3      L33:   1.1876 L12:   -.3199
REMARK   3      L13:   -.0334 L23:   -.2515
REMARK   3    S TENSOR
REMARK   3      S11:    .0521 S12:   -.0525 S13:   -.1195
REMARK   3      S21:   -.0386 S22:    .0030 S23:    .0837
REMARK   3      S31:    .1689 S32:   -.0251 S33:   -.0550
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   376        A   400
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9689  22.1374  73.5913
REMARK   3    T TENSOR
REMARK   3      T11:    .0760 T22:    .0863
REMARK   3      T33:    .0234 T12:    .0379
REMARK   3      T13:    .0120 T23:   -.0108
REMARK   3    L TENSOR
REMARK   3      L11:   1.8318 L22:   1.4795
REMARK   3      L33:   4.0377 L12:   -.9555
REMARK   3      L13:   1.5889 L23:  -1.3725
REMARK   3    S TENSOR
REMARK   3      S11:   -.1121 S12:   -.3429 S13:    .0369
REMARK   3      S21:    .2293 S22:    .1652 S23:   -.0143
REMARK   3      S31:   -.0742 S32:   -.0985 S33:   -.0531
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   401        A   445
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9121  18.0007  79.9808
REMARK   3    T TENSOR
REMARK   3      T11:    .0967 T22:    .1573
REMARK   3      T33:    .0318 T12:    .0486
REMARK   3      T13:   -.0354 T23:   -.0283
REMARK   3    L TENSOR
REMARK   3      L11:   3.1558 L22:   1.0357
REMARK   3      L33:   1.6793 L12:   -.9282
REMARK   3      L13:   -.7587 L23:    .2991
REMARK   3    S TENSOR
REMARK   3      S11:   -.0588 S12:   -.3008 S13:    .1569
REMARK   3      S21:    .1816 S22:    .1935 S23:   -.1337
REMARK   3      S31:   -.0364 S32:    .1790 S33:   -.1347
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   446        A   553
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2532  24.7263  71.4308
REMARK   3    T TENSOR
REMARK   3      T11:    .0567 T22:    .1362
REMARK   3      T33:    .0629 T12:    .0356
REMARK   3      T13:    .0278 T23:    .0442
REMARK   3    L TENSOR
REMARK   3      L11:    .6755 L22:    .8506
REMARK   3      L33:   1.0947 L12:   -.5657
REMARK   3      L13:   -.1355 L23:    .3026
REMARK   3    S TENSOR
REMARK   3      S11:   -.0796 S12:   -.2153 S13:   -.0706
REMARK   3      S21:    .1379 S22:    .1209 S23:    .1100
REMARK   3      S31:   -.0283 S32:   -.1927 S33:   -.0413
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   554        A   584
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0055   2.9948  64.4858
REMARK   3    T TENSOR
REMARK   3      T11:    .1187 T22:    .0350
REMARK   3      T33:    .1546 T12:   -.0034
REMARK   3      T13:   -.0065 T23:    .0381
REMARK   3    L TENSOR
REMARK   3      L11:   1.3668 L22:   2.9647
REMARK   3      L33:   3.7331 L12:   -.5151
REMARK   3      L13:    .2208 L23:    .8477
REMARK   3    S TENSOR
REMARK   3      S11:   -.0961 S12:   -.1480 S13:   -.4013
REMARK   3      S21:    .0551 S22:    .0502 S23:    .2406
REMARK   3      S31:    .3826 S32:   -.2077 S33:    .0458
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):  34.4097   1.9099  33.1464
REMARK   3    T TENSOR
REMARK   3      T11:    .3103 T22:    .0534
REMARK   3      T33:    .1601 T12:    .0630
REMARK   3      T13:   -.0618 T23:   -.0456
REMARK   3    L TENSOR
REMARK   3      L11:   2.9754 L22:    .3923
REMARK   3      L33:   2.3630 L12:   -.1115
REMARK   3      L13:  -1.1250 L23:   -.0297
REMARK   3    S TENSOR
REMARK   3      S11:    .1084 S12:    .0284 S13:   -.0427
REMARK   3      S21:   -.2478 S22:   -.0395 S23:    .0117
REMARK   3      S31:    .5275 S32:    .0547 S33:   -.0690
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    81
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7895  -3.7018  30.1323
REMARK   3    T TENSOR
REMARK   3      T11:    .3346 T22:    .1334
REMARK   3      T33:    .2644 T12:   -.0522
REMARK   3      T13:   -.0700 T23:   -.0527
REMARK   3    L TENSOR
REMARK   3      L11:  15.9484 L22:   2.4515
REMARK   3      L33:   2.5035 L12:   2.0424
REMARK   3      L13:   1.5208 L23:   -.3607
REMARK   3    S TENSOR
REMARK   3      S11:   -.2384 S12:   -.0520 S13:   -.4182
REMARK   3      S21:   -.0816 S22:    .1468 S23:    .3555
REMARK   3      S31:    .3138 S32:   -.3471 S33:    .0916
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    82        B   120
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1954  16.6729  25.0434
REMARK   3    T TENSOR
REMARK   3      T11:    .2704 T22:    .1863
REMARK   3      T33:    .3904 T12:   -.1501
REMARK   3      T13:   -.0543 T23:   -.0860
REMARK   3    L TENSOR
REMARK   3      L11:   2.3969 L22:   2.1782
REMARK   3      L33:   5.2192 L12:  -1.2917
REMARK   3      L13:   -.6623 L23:   2.3904
REMARK   3    S TENSOR
REMARK   3      S11:    .0365 S12:    .1937 S13:   -.4712
REMARK   3      S21:    .1566 S22:   -.3866 S23:    .4277
REMARK   3      S31:    .6574 S32:   -.7484 S33:    .3501
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   121        B   188
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3348  19.3274  26.3919
REMARK   3    T TENSOR
REMARK   3      T11:    .1308 T22:    .0822
REMARK   3      T33:    .0515 T12:    .1024
REMARK   3      T13:    .0004 T23:   -.0036
REMARK   3    L TENSOR
REMARK   3      L11:    .5947 L22:    .5184
REMARK   3      L33:   1.5008 L12:   -.1048
REMARK   3      L13:    .2798 L23:   -.1524
REMARK   3    S TENSOR
REMARK   3      S11:    .1399 S12:    .1120 S13:   -.1026
REMARK   3      S21:   -.2033 S22:   -.1604 S23:    .0105
REMARK   3      S31:    .2096 S32:    .1235 S33:    .0205
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   189        B   234
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2521  34.7795  28.0386
REMARK   3    T TENSOR
REMARK   3      T11:    .0625 T22:    .0567
REMARK   3      T33:    .0820 T12:    .0269
REMARK   3      T13:    .0048 T23:    .0201
REMARK   3    L TENSOR
REMARK   3      L11:    .7912 L22:   1.0323
REMARK   3      L33:   1.2503 L12:   -.8136
REMARK   3      L13:    .1186 L23:   -.1528
REMARK   3    S TENSOR
REMARK   3      S11:    .0404 S12:    .0801 S13:    .0558
REMARK   3      S21:   -.0845 S22:   -.0641 S23:   -.0629
REMARK   3      S31:    .0116 S32:    .1389 S33:    .0237
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   235        B   268
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6925  52.7082  38.8209
REMARK   3    T TENSOR
REMARK   3      T11:    .0665 T22:    .0141
REMARK   3      T33:    .0990 T12:   -.0110
REMARK   3      T13:   -.0226 T23:    .0008
REMARK   3    L TENSOR
REMARK   3      L11:   1.6692 L22:   2.6959
REMARK   3      L33:   2.8517 L12:   -.3781
REMARK   3      L13:    .7073 L23:  -1.0446
REMARK   3    S TENSOR
REMARK   3      S11:   -.1123 S12:   -.0142 S13:    .2588
REMARK   3      S21:    .1809 S22:    .0748 S23:   -.1658
REMARK   3      S31:   -.3157 S32:    .1079 S33:    .0375
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   286
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5920  54.5075  29.0998
REMARK   3    T TENSOR
REMARK   3      T11:    .4071 T22:    .3325
REMARK   3      T33:    .3694 T12:   -.2397
REMARK   3      T13:   -.0260 T23:    .0900
REMARK   3    L TENSOR
REMARK   3      L11:   1.3472 L22:   7.7115
REMARK   3      L33:   9.1587 L12:    .8824
REMARK   3      L13:    .1328 L23:   5.2232
REMARK   3    S TENSOR
REMARK   3      S11:   -.4989 S12:    .2613 S13:    .2689
REMARK   3      S21:  -1.1470 S22:    .4025 S23:   -.6736
REMARK   3      S31:  -1.3388 S32:   1.1241 S33:    .0965
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   287        B   376
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9862  37.6197  36.1886
REMARK   3    T TENSOR
REMARK   3      T11:    .0121 T22:    .0553
REMARK   3      T33:    .0708 T12:    .0128
REMARK   3      T13:   -.0166 T23:    .0203
REMARK   3    L TENSOR
REMARK   3      L11:    .7768 L22:   1.2224
REMARK   3      L33:   1.2314 L12:   -.2174
REMARK   3      L13:    .1436 L23:    .0876
REMARK   3    S TENSOR
REMARK   3      S11:    .0094 S12:    .0169 S13:   -.0581
REMARK   3      S21:   -.0475 S22:    .0145 S23:    .1130
REMARK   3      S31:    .0042 S32:   -.0954 S33:   -.0239
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   377        B   416
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3669  40.5599  17.9436
REMARK   3    T TENSOR
REMARK   3      T11:    .0985 T22:    .1597
REMARK   3      T33:    .0482 T12:    .0466
REMARK   3      T13:    .0298 T23:    .0214
REMARK   3    L TENSOR
REMARK   3      L11:    .6783 L22:   3.0221
REMARK   3      L33:   2.1355 L12:   -.7495
REMARK   3      L13:    .3859 L23:  -1.5934
REMARK   3    S TENSOR
REMARK   3      S11:    .2083 S12:    .2358 S13:    .0589
REMARK   3      S21:   -.3966 S22:   -.2078 S23:   -.0524
REMARK   3      S31:    .0470 S32:    .3079 S33:   -.0005
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   417        B   429
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8664  49.7504  16.7382
REMARK   3    T TENSOR
REMARK   3      T11:    .1074 T22:    .1285
REMARK   3      T33:    .0908 T12:    .0439
REMARK   3      T13:   -.0014 T23:    .0217
REMARK   3    L TENSOR
REMARK   3      L11:   2.8639 L22:  11.7041
REMARK   3      L33:   4.4600 L12:   1.8539
REMARK   3      L13:    .6332 L23:   2.2756
REMARK   3    S TENSOR
REMARK   3      S11:    .0690 S12:    .2082 S13:    .0596
REMARK   3      S21:   -.1694 S22:    .0581 S23:   -.0235
REMARK   3      S31:   -.1169 S32:    .0316 S33:   -.1272
REMARK   3
REMARK   3   TLS GROUP : 23
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   430        B   468
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5570  25.4508  16.8981
REMARK   3    T TENSOR
REMARK   3      T11:    .1753 T22:    .1387
REMARK   3      T33:    .0098 T12:    .1200
REMARK   3      T13:    .0108 T23:   -.0121
REMARK   3    L TENSOR
REMARK   3      L11:   1.1690 L22:   1.4340
REMARK   3      L33:    .9758 L12:   -.3295
REMARK   3      L13:    .8164 L23:   -.3672
REMARK   3    S TENSOR
REMARK   3      S11:    .2036 S12:    .2538 S13:   -.0309
REMARK   3      S21:   -.2803 S22:   -.1890 S23:    .0289
REMARK   3      S31:    .1901 S32:    .2156 S33:   -.0147
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   469        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0330  25.5901  23.7865
REMARK   3    T TENSOR
REMARK   3      T11:    .1051 T22:    .0607
REMARK   3      T33:    .0762 T12:    .0169
REMARK   3      T13:   -.0635 T23:   -.0121
REMARK   3    L TENSOR
REMARK   3      L11:    .8854 L22:    .7145
REMARK   3      L33:    .6536 L12:   -.4827
REMARK   3      L13:    .0145 L23:   -.2688
REMARK   3    S TENSOR
REMARK   3      S11:    .1177 S12:    .1463 S13:   -.1451
REMARK   3      S21:   -.1968 S22:   -.0787 S23:    .1283
REMARK   3      S31:    .2014 S32:   -.0269 S33:   -.0390
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 3QH0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9769
REMARK 200  MONOCHROMATOR                  : SI (111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77928
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
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     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.09600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.56200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.900
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   (%): 52.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM
REMARK 280  HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.95300
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.44400
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.98400
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.95300
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.44400
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.98400
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.95300
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.44400
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.98400
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.95300
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.44400
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.98400
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: 16450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 46.0 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     MET A    10
REMARK 465     LEU A    11
REMARK 465     PHE A    12
REMARK 465     ARG A    13
REMARK 465     ALA A    14
REMARK 465     VAL A    15
REMARK 465     LEU A    16
REMARK 465     LEU A    17
REMARK 465     CYS A    18
REMARK 465     ALA A    19
REMARK 465     ALA A    20
REMARK 465     LEU A    21
REMARK 465     GLY A    22
REMARK 465     LEU A    23
REMARK 465     SER A    24
REMARK 465     GLN A    25
REMARK 465     ALA A    26
REMARK 465     ALA A    27
REMARK 465     ASN A    28
REMARK 465     HIS A    29
REMARK 465     HIS A    30
REMARK 465     HIS A    31
REMARK 465     HIS A    32
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ALA A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     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     MET B    10
REMARK 465     LEU B    11
REMARK 465     PHE B    12
REMARK 465     ARG B    13
REMARK 465     ALA B    14
REMARK 465     VAL B    15
REMARK 465     LEU B    16
REMARK 465     LEU B    17
REMARK 465     CYS B    18
REMARK 465     ALA B    19
REMARK 465     ALA B    20
REMARK 465     LEU B    21
REMARK 465     GLY B    22
REMARK 465     LEU B    23
REMARK 465     SER B    24
REMARK 465     GLN B    25
REMARK 465     ALA B    26
REMARK 465     ALA B    27
REMARK 465     ASN B    28
REMARK 465     HIS B    29
REMARK 465     HIS B    30
REMARK 465     HIS B    31
REMARK 465     HIS B    32
REMARK 465     GLN B   583
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     GLN B   586
REMARK 465     PRO B   587
REMARK 465     THR B   588
REMARK 465     LYS B   589
REMARK 465     THR B   590
REMARK 465     ALA B   591
REMARK 465     THR B   592
REMARK 465     ILE B   593
REMARK 465     ALA B   594
REMARK 465     ALA B   595
REMARK 465     SER B   596
REMARK 465     ALA B   597
REMARK 465     SER B   598
REMARK 465     HIS B   599
REMARK 465     SER B   600
REMARK 465     ARG B   601
REMARK 465     LEU B   602
REMARK 465     ASP B   603
REMARK 465     ASP B   604
REMARK 465     ILE B   605
REMARK 465     ASN B   606
REMARK 465     PRO B   607
REMARK 465     THR B   608
REMARK 465     VAL B   609
REMARK 465     LEU B   610
REMARK 465     ILE B   611
REMARK 465     LYS B   612
REMARK 465     ARG B   613
REMARK 465     ARG B   614
REMARK 465     SER B   615
REMARK 465     THR B   616
REMARK 465     GLU B   617
REMARK 465     LEU B   618
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLN A  54    CD   OE1  NE2
REMARK 470     LYS A  56    CE   NZ
REMARK 470     LEU A  75    CD1  CD2
REMARK 470     ILE A  78    CD1
REMARK 470     LYS A  79    NZ
REMARK 470     LEU A  80    CD1
REMARK 470     LEU A  81    CG   CD1  CD2
REMARK 470     LYS A  83    CG   CD   CE   NZ
REMARK 470     LYS A  97    CD   CE   NZ
REMARK 470     ILE A 105A   CD1
REMARK 470     LYS A 169    CD   CE   NZ
REMARK 470     LYS A 175    NZ
REMARK 470     LYS A 215    CG   CD   CE   NZ
REMARK 470     LYS A 267    NZ
REMARK 470     GLU A 272    CD   OE1  OE2
REMARK 470     LYS A 317    NZ
REMARK 470     LYS A 358    CD   CE   NZ
REMARK 470     LYS A 405    CG   CD   CE   NZ
REMARK 470     LYS A 473    CD   CE   NZ
REMARK 470     LYS A 511    NZ
REMARK 470     LYS A 557    CD   CE   NZ
REMARK 470     GLN A 583    CG   CD   OE1  NE2
REMARK 470     GLN B  54    CD   OE1  NE2
REMARK 470     LYS B  56    CE   NZ
REMARK 470     LEU B  75    CG   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    CD   CE   NZ
REMARK 470     LYS B  97    CD   CE   NZ
REMARK 470     ASN B 101    OD1
REMARK 470     ILE B 102    CG1  CD1
REMARK 470     LYS B 169    CD   CE   NZ
REMARK 470     GLU B 170    OE1  OE2
REMARK 470     GLU B 186    CD   OE1  OE2
REMARK 470     LYS B 215    CD   CE   NZ
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 281    CG   CD   OE1  OE2
REMARK 470     ASN B 282    CG   OD1
REMARK 470     LYS B 358    CE   NZ
REMARK 470     ASP B 399    OD1  OD2
REMARK 470     LYS B 405    CE   NZ
REMARK 470     ARG B 428    CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 473    CD   CE   NZ
REMARK 470     LYS B 485    CE   NZ
REMARK 470     LYS B 492    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   ND2  ASN B    68     O5   NAG B   661              1.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 456   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 456   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A 129      -89.62   -118.65
REMARK 500    ARG A 185      -65.94    -91.61
REMARK 500    TRP A 387       52.54    -91.63
REMARK 500    GLU A 398     -123.37     53.12
REMARK 500    ASN A 410       73.65   -110.58
REMARK 500    ASN A 439       14.41   -141.69
REMARK 500    SER A 496      -44.76     63.80
REMARK 500    ARG B  61       15.51     58.25
REMARK 500    THR B 129      -89.10   -124.12
REMARK 500    ARG B 185      -91.10    -94.25
REMARK 500    TRP B 387       49.88    -82.66
REMARK 500    GLU B 398     -118.44     55.29
REMARK 500    ASN B 410       76.96   -103.88
REMARK 500    ASN B 439       19.41   -142.72
REMARK 500    SER B 496      -47.30     69.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN B  581     VAL B  582                  145.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    VAL B 582        22.4      L          L   OUTSIDE RANGE
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 A1023        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH B 858        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH B 859        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH B 973        DISTANCE =  6.49 ANGSTROMS
REMARK 525    HOH B1040        DISTANCE =  5.53 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HSQ A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL
REMARK 900 OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB
REMARK 900 UNINHIBITED COX-2
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-2
DBREF  3QH0 A   10   618  UNP    Q05769   PGH2_MOUSE       1    604
DBREF  3QH0 B   10   618  UNP    Q05769   PGH2_MOUSE       1    604
SEQADV 3QH0 HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQADV 3QH0 HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3QH0 ALA B  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQRES   1 A  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 A  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES   3 A  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES   4 A  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES   5 A  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES   6 A  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES   7 A  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES   8 A  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES   9 A  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES  10 A  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES  11 A  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES  12 A  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES  13 A  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES  14 A  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES  15 A  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES  16 A  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES  17 A  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES  18 A  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES  19 A  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES  20 A  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES  21 A  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES  22 A  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES  23 A  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES  24 A  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES  25 A  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES  26 A  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES  27 A  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES  28 A  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES  29 A  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES  30 A  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES  31 A  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES  32 A  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES  33 A  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES  34 A  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES  35 A  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES  36 A  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES  37 A  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES  38 A  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES  39 A  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES  40 A  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES  41 A  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES  42 A  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES  43 A  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES  44 A  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES  45 A  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES  46 A  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES  47 A  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
SEQRES   1 B  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 B  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES   3 B  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES   4 B  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES   5 B  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES   6 B  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES   7 B  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES   8 B  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES   9 B  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES  10 B  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES  11 B  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES  12 B  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES  13 B  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES  14 B  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES  15 B  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES  16 B  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES  17 B  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES  18 B  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES  19 B  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES  20 B  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES  21 B  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES  22 B  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES  23 B  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES  24 B  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES  25 B  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES  26 B  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES  27 B  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES  28 B  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES  29 B  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES  30 B  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES  31 B  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES  32 B  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES  33 B  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES  34 B  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES  35 B  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES  36 B  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES  37 B  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES  38 B  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES  39 B  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES  40 B  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES  41 B  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES  42 B  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES  43 B  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES  44 B  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES  45 B  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES  46 B  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES  47 B  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
MODRES 3QH0 ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3QH0 ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3QH0 ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3QH0 ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3QH0 ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3QH0 ASN A   68  ASN  GLYCOSYLATION SITE
HET    EDO  A   1       4
HET    EDO  A   4       4
HET    EDO  A   5       4
HET    EDO  A 619       4
HET    EDO  A 620       4
HET    EDO  A 621       4
HET    EDO  A 622       4
HET    EDO  A 623       4
HET    EDO  A 624       4
HET    PLM  A 625      18
HET    AKR  A   2       5
HET    AKR  A   3       5
HET    COH  A 626      43
HET    HSQ  A 661      14
HET    NAG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    MAN  A 673      11
HET    NAG  A 681      14
HET    BOG  A 703      20
HET    EDO  B   2       4
HET    EDO  B   3       4
HET    EDO  B   6       4
HET    EDO  B   7       4
HET    EDO  B   8       4
HET    EDO  B   9       4
HET    EDO  B 619       4
HET    EDO  B 620       4
HET    EDO  B 621       4
HET    EDO  B 622       4
HET    EDO  B 623       4
HET    EDO  B 624       4
HET    EDO  B 625       4
HET    EDO  B 626       4
HET    COH  B 627      43
HET    NAG  B 661      14
HET    NDG  B 662      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 681      14
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     PLM PALMITIC ACID
HETNAM     AKR ACRYLIC ACID
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     HSQ 2-(ACETYLAMINO)-2-DEOXY-ALPHA-L-IDOPYRANOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  EDO    23(C2 H6 O2)
FORMUL  12  PLM    C16 H32 O2
FORMUL  13  AKR    2(C3 H4 O2)
FORMUL  15  COH    2(C34 H32 CO N4 O4)
FORMUL  16  HSQ    C8 H15 N O6
FORMUL  16  NAG    8(C8 H15 N O6)
FORMUL  17  MAN    C6 H12 O6
FORMUL  19  BOG    C14 H28 O6
FORMUL  35  NDG    C8 H15 N O6
FORMUL  38  HOH   *753(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 PHE A   96  ILE A  105A 1                                  11
HELIX    4   4 ILE A  105A TYR A  122  1                                  18
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  HIS A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 VAL A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  ASP A  347  1                                  24
HELIX   15  15 ASP A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 HIS A  386  LEU A  391  5                                   6
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  410  GLN A  429  1                                  20
HELIX   21  21 PRO A  441  ALA A  443  5                                   3
HELIX   22  22 VAL A  444  MET A  458  1                                  15
HELIX   23  23 SER A  462  PHE A  470  1                                   9
HELIX   24  24 SER A  477  GLY A  483  1                                   7
HELIX   25  25 LYS A  485  SER A  496  1                                  12
HELIX   26  26 ASP A  497  MET A  501  5                                   5
HELIX   27  27 GLU A  502  GLU A  510  1                                   9
HELIX   28  28 GLY A  519  GLY A  536  1                                  18
HELIX   29  29 ASN A  537  SER A  541  5                                   5
HELIX   30  30 LYS A  546  GLY A  551  5                                   6
HELIX   31  31 GLY A  552  THR A  561  1                                  10
HELIX   32  32 SER A  563  VAL A  572  1                                  10
HELIX   33  33 GLU B   73  LEU B   82  1                                  10
HELIX   34  34 THR B   85  THR B   94  1                                  10
HELIX   35  35 PHE B   96  ASN B  104  1                                   9
HELIX   36  36 ILE B  105A TYR B  122  1                                  18
HELIX   37  37 SER B  138  ASN B  144  1                                   7
HELIX   38  38 ASP B  173  LEU B  182  1                                  10
HELIX   39  39 ASN B  195  HIS B  207  1                                  13
HELIX   40  40 LEU B  230  GLY B  235  1                                   6
HELIX   41  41 THR B  237  ARG B  245  1                                   9
HELIX   42  42 THR B  265  GLN B  270  1                                   6
HELIX   43  43 PRO B  280  GLN B  284  5                                   5
HELIX   44  44 VAL B  291  LEU B  294  5                                   4
HELIX   45  45 VAL B  295  HIS B  320  1                                  26
HELIX   46  46 GLY B  324  ASP B  347  1                                  24
HELIX   47  47 ASP B  347  GLY B  354  1                                   8
HELIX   48  48 ASP B  362  PHE B  367  5                                   6
HELIX   49  49 ALA B  378  TYR B  385  1                                   8
HELIX   50  50 HIS B  386  LEU B  391  5                                   6
HELIX   51  51 SER B  403  LEU B  408  1                                   6
HELIX   52  52 ASN B  410  GLY B  418  1                                   9
HELIX   53  53 GLY B  418  GLN B  429  1                                  12
HELIX   54  54 PRO B  441  ALA B  443  5                                   3
HELIX   55  55 VAL B  444  MET B  458  1                                  15
HELIX   56  56 SER B  462  PHE B  470  1                                   9
HELIX   57  57 SER B  477  GLY B  483  1                                   7
HELIX   58  58 LYS B  485  SER B  496  1                                  12
HELIX   59  59 ASP B  497  MET B  501  5                                   5
HELIX   60  60 GLU B  502  GLU B  510  1                                   9
HELIX   61  61 GLY B  519  GLY B  536  1                                  18
HELIX   62  62 ASN B  537  SER B  541  5                                   5
HELIX   63  63 LYS B  546  GLY B  551  5                                   6
HELIX   64  64 GLY B  552  THR B  561  1                                  10
HELIX   65  65 SER B  563  VAL B  572  1                                  10
SHEET    1   A 2 GLU A  46  SER A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65
SHEET    1   C 2 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   D 2 PHE A 395  ILE A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   E 2 GLU B  46  SER B  49  0
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46
SHEET    1   F 2 PHE B  64  TYR B  65  0
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   G 2 GLN B 255  ILE B 257  0
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   H 2 PHE B 395  ILE B 397  0
SHEET    2   H 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.02
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.07
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.05
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.07
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.37
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.42
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44
LINK         O4  HSQ A 661                 C1  NAG A 662     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46
LINK         O4  NAG B 661                 C1  NDG B 662     1555   1555  1.46
LINK         ND2 ASN A  68                 C1  HSQ A 661     1555   1555  1.44
CISPEP   1 SER A  126    PRO A  127          0         5.62
CISPEP   2 SER B  126    PRO B  127          0        -0.62
SITE     1 AC1  8 HIS A  90  GLN A 192  LEU A 352  ARG A 513
SITE     2 AC1  8 ALA A 516  ILE A 517  PHE A 518  VAL A 523
SITE     1 AC2  8 PRO A 162  MET A 163  SER A 455  ARG A 456
SITE     2 AC2  8 LYS A 459  TYR A 460  EDO A 623  HOH A 743
SITE     1 AC3  2 CYS A  59  HOH A 892
SITE     1 AC4  8 GLU A 308  ARG A 311  GLU A 339  SER A 566
SITE     2 AC4  8 LEU A 567  ASN A 570  ASN A 571  HOH A 737
SITE     1 AC5  5 LYS A 251  TYR A 254  ASN A 310  HOH A 688
SITE     2 AC5  5 HOH A 744
SITE     1 AC6  4 LEU A 246  LYS A 253  TYR A 254  HOH A 959
SITE     1 AC7  5 SER A 143  EDO A 624  HOH A 793  LEU B 145
SITE     2 AC7  5 LEU B 224
SITE     1 AC8  8 EDO A   4  VAL A 155  ALA A 156  ASP A 157
SITE     2 AC8  8 CYS A 159  THR A 161  PRO A 162  LYS A 459
SITE     1 AC9  3 EDO A 622  HOH B 899  HOH B 926
SITE     1 BC1 12 VAL A 116  ARG A 120  PHE A 205  TYR A 348
SITE     2 BC1 12 VAL A 349  SER A 353  TYR A 355  TYR A 385
SITE     3 BC1 12 ALA A 527  SER A 530  LEU A 531  HOH A1048
SITE     1 BC2  4 SER A 477  PHE A 478  GLU A 479  LYS A 492
SITE     1 BC3  5 THR A 237  ASP A 239  ARG A 240  LYS A 243
SITE     2 BC3  5 GLU A 272
SITE     1 BC4 13 GLN A 203  HIS A 207  PHE A 210  LYS A 211
SITE     2 BC4 13 THR A 212  HIS A 214  ASN A 382  TYR A 385
SITE     3 BC4 13 HIS A 386  TRP A 387  HIS A 388  LEU A 391
SITE     4 BC4 13 VAL A 447
SITE     1 BC5  4 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     1 BC6  1 HSQ A 661
SITE     1 BC7  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 BC7  9 NAG A 672  HOH A 706  HOH A 790  HOH A 906
SITE     3 BC7  9 HOH A 943
SITE     1 BC8  3 ARG A 216  NAG A 671  MAN A 673
SITE     1 BC9  3 NAG A 672  HOH A 685  HOH A 853
SITE     1 CC1  4 ASN A 410  SER A 412  ILE A 413  GLU A 416
SITE     1 CC2 12 GLU A 179  LYS A 180  ARG A 184  ARG A 185
SITE     2 CC2 12 ARG A 438  GLU A 486  GLU A 490  GLU B 179
SITE     3 CC2 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445
SITE     1 CC3  8 HIS B  90  GLN B 192  LEU B 352  ARG B 513
SITE     2 CC3  8 ALA B 516  ILE B 517  PHE B 518  VAL B 523
SITE     1 CC4  5 LYS B 251  TYR B 254  ASN B 310  HOH B 872
SITE     2 CC4  5 HOH B1076
SITE     1 CC5  6 PRO B 162  LEU B 171  ARG B 456  LYS B 459
SITE     2 CC5  6 TYR B 460  HOH B 783
SITE     1 CC6  2 SER A 548  MET B  48
SITE     1 CC7  7 GLU B 308  ARG B 311  GLU B 339  SER B 566
SITE     2 CC7  7 LEU B 567  ASN B 570  HOH B 746
SITE     1 CC8  5 LEU A 145  HOH A 891  SER B 143  HOH B 631
SITE     2 CC8  5 HOH B 683
SITE     1 CC9  6 ASP B 239  ARG B 240  LYS B 243  GLN B 270
SITE     2 CC9  6 VAL B 271  GLU B 272
SITE     1 DC1  3 ARG B 428  VAL B 582  HOH B 753
SITE     1 DC2  7 LYS B 175  GLN B 445  ALA B 446  LYS B 449
SITE     2 DC2  7 HOH B 654  HOH B 764  HOH B 880
SITE     1 DC3  3 VAL B 349  TYR B 355  HOH B1078
SITE     1 DC4  2 SER B 530  HOH B1078
SITE     1 DC5  5 VAL A 554  LEU B 246  LYS B 253  TYR B 254
SITE     2 DC5  5 HOH B 635
SITE     1 DC6  8 PHE A 142  GLY B 225  HIS B 226  ASN B 375
SITE     2 DC6  8 GLY B 536  PRO B 538  HOH B 684  HOH B 926
SITE     1 DC7  2 CYS B 569  ASN B 570
SITE     1 DC8 14 ALA B 199  GLN B 203  HIS B 207  PHE B 210
SITE     2 DC8 14 THR B 212  HIS B 214  VAL B 295  ASN B 382
SITE     3 DC8 14 TYR B 385  HIS B 386  HIS B 388  LEU B 391
SITE     4 DC8 14 VAL B 447  HOH B 864
SITE     1 DC9  5 TYR B  55  GLU B  67  ASN B  68  NDG B 662
SITE     2 DC9  5 HOH B 933
SITE     1 EC1  2 NAG B 661  HOH B 906
SITE     1 EC2  9 GLU B 140  ASN B 144  TYR B 147  ARG B 216
SITE     2 EC2  9 HOH B 670  NAG B 672  HOH B 775  HOH B 825
SITE     3 EC2  9 HOH B 833
SITE     1 EC3  5 ASP A 239  ARG B 216  NAG B 671  HOH B 919
SITE     2 EC3  5 HOH B1055
SITE     1 EC4  6 ASN B 410  ILE B 413  GLU B 416  HOH B 765
SITE     2 EC4  6 HOH B 866  HOH B1007
CRYST1  121.906  130.888  179.968  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      0.008203  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007640  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005557        0.00000
      
PROCHECK
Go to PROCHECK summary
 References