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PDBsum entry 3hs5

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Oxidoreductase PDB id
3hs5
Jmol
Contents
Protein chains
552 a.a.
Ligands
ACD ×2
AKR ×2
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG ×2
EDO ×12
Waters ×907
HEADER    OXIDOREDUCTASE                          10-JUN-09   3HS5
TITLE     X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   8 2;
COMPND   9 EC: 1.14.99.1;
COMPND  10 ENGINEERED: YES;
COMPND  11 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS    OXIDOREDUCTASE, DIOXYGENASE, DISULFIDE BOND, ENDOPLASMIC RETICULUM,
KEYWDS   2 FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME, IRON, LIPID SYNTHESIS,
KEYWDS   3 MEMBRANE, METAL-BINDING, MICROSOME, PEROXIDASE, PHOSPHOPROTEIN,
KEYWDS   4 PROSTAGLANDIN BIOSYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI
REVDAT   3   04-AUG-10 3HS5    1       JRNL
REVDAT   2   02-JUN-10 3HS5    1       JRNL
REVDAT   1   12-MAY-10 3HS5    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.    2.10 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        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 83526
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) : 0.171
REMARK   3   R VALUE            (WORKING SET) : 0.169
REMARK   3   FREE R VALUE                     : 0.210
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4175
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) : 5736
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.31
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450
REMARK   3   BIN FREE R VALUE SET COUNT          : 314
REMARK   3   BIN FREE R VALUE                    : 0.2930
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8875
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 379
REMARK   3   SOLVENT ATOMS            : 907
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 28.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.63
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.09000
REMARK   3    B22 (A**2) : 0.09000
REMARK   3    B33 (A**2) : -0.18000
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): 0.186
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.139
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9610 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13053 ; 1.121 ; 2.008
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1117 ; 5.179 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   444 ;36.503 ;23.986
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1510 ;13.465 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;11.777 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1386 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7366 ; 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):  5546 ; 0.318 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9018 ; 0.638 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4064 ; 1.248 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4028 ; 2.136 ; 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):   1.2244  38.1953  59.8657
REMARK   3    T TENSOR
REMARK   3      T11:    .1021 T22:    .3160
REMARK   3      T33:    .2521 T12:    .0662
REMARK   3      T13:    .0538 T23:    .0772
REMARK   3    L TENSOR
REMARK   3      L11:   1.0014 L22:   4.6161
REMARK   3      L33:   3.0850 L12:    .7353
REMARK   3      L13:   -.0278 L23:   1.3357
REMARK   3    S TENSOR
REMARK   3      S11:    .0387 S12:   -.1048 S13:    .0751
REMARK   3      S21:   -.0032 S22:    .0772 S23:    .2289
REMARK   3      S31:   -.1906 S32:   -.5562 S33:   -.1159
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    94
REMARK   3    ORIGIN FOR THE GROUP (A):    .2095  16.7405  67.1545
REMARK   3    T TENSOR
REMARK   3      T11:    .2283 T22:    .4420
REMARK   3      T33:    .5833 T12:   -.1048
REMARK   3      T13:    .0256 T23:    .1681
REMARK   3    L TENSOR
REMARK   3      L11:   2.8544 L22:   6.3504
REMARK   3      L33:   2.2144 L12:  -4.0045
REMARK   3      L13:   1.7638 L23:  -3.3690
REMARK   3    S TENSOR
REMARK   3      S11:    .0919 S12:   -.0715 S13:   -.5024
REMARK   3      S21:   -.3743 S22:    .3894 S23:    .7523
REMARK   3      S31:    .3708 S32:   -.4514 S33:   -.4814
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    95        A   122
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6255   2.1907  64.6350
REMARK   3    T TENSOR
REMARK   3      T11:    .2154 T22:    .2901
REMARK   3      T33:    .4509 T12:   -.1289
REMARK   3      T13:    .0091 T23:    .0010
REMARK   3    L TENSOR
REMARK   3      L11:   2.7889 L22:   5.1024
REMARK   3      L33:  13.0009 L12:   1.8961
REMARK   3      L13:  -4.7482 L23:  -2.5327
REMARK   3    S TENSOR
REMARK   3      S11:   -.4841 S12:    .2346 S13:   -.2735
REMARK   3      S21:   -.3581 S22:    .1952 S23:    .5227
REMARK   3      S31:    .6969 S32:   -.6672 S33:    .2889
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   123        A   187
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2760  36.5234  66.9945
REMARK   3    T TENSOR
REMARK   3      T11:    .1055 T22:    .0877
REMARK   3      T33:    .1245 T12:    .0466
REMARK   3      T13:    .0184 T23:    .0054
REMARK   3    L TENSOR
REMARK   3      L11:    .9580 L22:    .7658
REMARK   3      L33:   2.7478 L12:   -.2601
REMARK   3      L13:    .0302 L23:   -.3279
REMARK   3    S TENSOR
REMARK   3      S11:   -.0826 S12:   -.1212 S13:    .0881
REMARK   3      S21:    .1456 S22:    .1403 S23:    .0152
REMARK   3      S31:   -.1607 S32:   -.2157 S33:   -.0577
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   188        A   219
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9439  22.1107  70.6682
REMARK   3    T TENSOR
REMARK   3      T11:    .1933 T22:    .1658
REMARK   3      T33:    .1821 T12:    .0092
REMARK   3      T13:   -.0062 T23:   -.0203
REMARK   3    L TENSOR
REMARK   3      L11:   1.4824 L22:   1.1938
REMARK   3      L33:   1.3784 L12:  -1.2305
REMARK   3      L13:    .6054 L23:   -.9414
REMARK   3    S TENSOR
REMARK   3      S11:   -.0823 S12:   -.0919 S13:    .1066
REMARK   3      S21:    .1126 S22:    .0337 S23:   -.0851
REMARK   3      S31:   -.1315 S32:    .0276 S33:    .0486
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   220        A   271
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0811  21.4136  56.2827
REMARK   3    T TENSOR
REMARK   3      T11:    .0571 T22:    .0710
REMARK   3      T33:    .1663 T12:   -.0026
REMARK   3      T13:    .0161 T23:    .0221
REMARK   3    L TENSOR
REMARK   3      L11:   1.9006 L22:    .6628
REMARK   3      L33:   1.1954 L12:   -.7840
REMARK   3      L13:    .0442 L23:   -.0231
REMARK   3    S TENSOR
REMARK   3      S11:    .0772 S12:   -.0081 S13:    .1245
REMARK   3      S21:   -.0703 S22:   -.0448 S23:   -.2129
REMARK   3      S31:   -.0026 S32:    .2194 S33:   -.0324
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   272        A   318
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8733  19.3653  63.6918
REMARK   3    T TENSOR
REMARK   3      T11:    .0812 T22:    .1390
REMARK   3      T33:    .2088 T12:   -.0013
REMARK   3      T13:    .0048 T23:    .0152
REMARK   3    L TENSOR
REMARK   3      L11:   1.7025 L22:   1.4810
REMARK   3      L33:   2.7499 L12:   -.0953
REMARK   3      L13:    .0356 L23:    .3637
REMARK   3    S TENSOR
REMARK   3      S11:    .0738 S12:   -.2620 S13:    .2134
REMARK   3      S21:    .0600 S22:    .0062 S23:   -.2811
REMARK   3      S31:   -.0622 S32:    .1757 S33:   -.0800
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   319        A   389
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1287  13.1005  57.8499
REMARK   3    T TENSOR
REMARK   3      T11:    .1162 T22:    .0574
REMARK   3      T33:    .1585 T12:   -.0273
REMARK   3      T13:   -.0113 T23:    .0243
REMARK   3    L TENSOR
REMARK   3      L11:    .9920 L22:    .6756
REMARK   3      L33:   1.4536 L12:   -.3746
REMARK   3      L13:   -.4809 L23:   -.3911
REMARK   3    S TENSOR
REMARK   3      S11:   -.0436 S12:   -.0674 S13:   -.1651
REMARK   3      S21:   -.0315 S22:    .0625 S23:    .0902
REMARK   3      S31:    .2038 S32:   -.0413 S33:   -.0189
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   390        A   437
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4243  16.8981  80.0974
REMARK   3    T TENSOR
REMARK   3      T11:    .1590 T22:    .2321
REMARK   3      T33:    .0824 T12:    .0585
REMARK   3      T13:   -.0288 T23:    .0003
REMARK   3    L TENSOR
REMARK   3      L11:   4.2086 L22:    .9593
REMARK   3      L33:   2.2842 L12:   -.4198
REMARK   3      L13:   -.9937 L23:    .2010
REMARK   3    S TENSOR
REMARK   3      S11:   -.1086 S12:   -.4258 S13:    .0257
REMARK   3      S21:    .2420 S22:    .1579 S23:   -.1503
REMARK   3      S31:    .0033 S32:    .4531 S33:   -.0492
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   438        A   534
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7104  28.6262  77.1465
REMARK   3    T TENSOR
REMARK   3      T11:    .1141 T22:    .1800
REMARK   3      T33:    .1037 T12:    .0623
REMARK   3      T13:    .0462 T23:    .0221
REMARK   3    L TENSOR
REMARK   3      L11:   1.2606 L22:   1.4934
REMARK   3      L33:   2.0002 L12:   -.6184
REMARK   3      L13:    .0553 L23:   -.2006
REMARK   3    S TENSOR
REMARK   3      S11:   -.1210 S12:   -.2508 S13:   -.0773
REMARK   3      S21:    .1860 S22:    .1673 S23:    .0765
REMARK   3      S31:   -.0366 S32:   -.1907 S33:   -.0462
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   535        A   553
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7102  10.2806  47.7409
REMARK   3    T TENSOR
REMARK   3      T11:    .2314 T22:    .1348
REMARK   3      T33:    .2278 T12:   -.0253
REMARK   3      T13:   -.0372 T23:    .0079
REMARK   3    L TENSOR
REMARK   3      L11:   1.0511 L22:   1.5789
REMARK   3      L33:   1.5874 L12:   -.8010
REMARK   3      L13:   -.9724 L23:   -.0286
REMARK   3    S TENSOR
REMARK   3      S11:    .0174 S12:    .1125 S13:   -.1666
REMARK   3      S21:   -.2106 S22:   -.0292 S23:    .1571
REMARK   3      S31:    .1716 S32:   -.1374 S33:    .0118
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):  36.9221   3.7119  65.0785
REMARK   3    T TENSOR
REMARK   3      T11:    .2309 T22:    .0927
REMARK   3      T33:    .2438 T12:   -.0174
REMARK   3      T13:    .0205 T23:    .0670
REMARK   3    L TENSOR
REMARK   3      L11:   1.5997 L22:   2.3540
REMARK   3      L33:   3.7588 L12:  -1.0053
REMARK   3      L13:   -.1265 L23:    .6041
REMARK   3    S TENSOR
REMARK   3      S11:   -.1612 S12:   -.1087 S13:   -.3181
REMARK   3      S21:   -.0337 S22:    .1017 S23:    .1382
REMARK   3      S31:    .5322 S32:   -.1249 S33:    .0595
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):  33.0846   2.2762  33.5872
REMARK   3    T TENSOR
REMARK   3      T11:    .5138 T22:    .1150
REMARK   3      T33:    .2995 T12:    .0505
REMARK   3      T13:   -.0311 T23:   -.0281
REMARK   3    L TENSOR
REMARK   3      L11:   3.2344 L22:    .3876
REMARK   3      L33:   2.2880 L12:   -.6583
REMARK   3      L13:   -.4689 L23:   -.0331
REMARK   3    S TENSOR
REMARK   3      S11:    .1164 S12:    .0169 S13:   -.1471
REMARK   3      S21:   -.3012 S22:   -.0938 S23:    .0354
REMARK   3      S31:    .7209 S32:    .0729 S33:   -.0226
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):  18.8160  -3.6732  31.2245
REMARK   3    T TENSOR
REMARK   3      T11:    .6664 T22:    .2248
REMARK   3      T33:    .4228 T12:   -.1513
REMARK   3      T13:   -.0901 T23:   -.0420
REMARK   3    L TENSOR
REMARK   3      L11:  46.3665 L22:   9.5197
REMARK   3      L33:   1.5050 L12:  -2.2326
REMARK   3      L13:   1.2987 L23:    .4921
REMARK   3    S TENSOR
REMARK   3      S11:   -.3644 S12:   -.2241 S13:  -1.7561
REMARK   3      S21:   -.3776 S22:    .2493 S23:   1.1143
REMARK   3      S31:    .6931 S32:   -.4925 S33:    .1151
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):   2.4179  17.0223  25.6309
REMARK   3    T TENSOR
REMARK   3      T11:    .3463 T22:    .3998
REMARK   3      T33:    .4553 T12:   -.2344
REMARK   3      T13:   -.0821 T23:    .0334
REMARK   3    L TENSOR
REMARK   3      L11:   1.8292 L22:   4.2121
REMARK   3      L33:   5.7252 L12:  -1.7101
REMARK   3      L13:   -.4872 L23:   2.5830
REMARK   3    S TENSOR
REMARK   3      S11:    .1386 S12:    .1346 S13:   -.6382
REMARK   3      S21:    .1198 S22:   -.3482 S23:    .5411
REMARK   3      S31:    .6135 S32:   -.7223 S33:    .2096
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   185
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7159  18.8445  28.0477
REMARK   3    T TENSOR
REMARK   3      T11:    .1861 T22:    .1111
REMARK   3      T33:    .1321 T12:    .0691
REMARK   3      T13:    .0174 T23:    .0017
REMARK   3    L TENSOR
REMARK   3      L11:    .7218 L22:    .7953
REMARK   3      L33:   2.3358 L12:   -.1598
REMARK   3      L13:    .4139 L23:   -.4931
REMARK   3    S TENSOR
REMARK   3      S11:    .1103 S12:    .1113 S13:   -.0966
REMARK   3      S21:   -.1853 S22:   -.1413 S23:   -.0309
REMARK   3      S31:    .4060 S32:    .1533 S33:    .0310
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   186        B   213
REMARK   3    ORIGIN FOR THE GROUP (A):  19.6193  35.3807  20.2063
REMARK   3    T TENSOR
REMARK   3      T11:    .1141 T22:    .1773
REMARK   3      T33:    .1617 T12:    .0477
REMARK   3      T13:    .0057 T23:    .0314
REMARK   3    L TENSOR
REMARK   3      L11:    .6202 L22:   1.3348
REMARK   3      L33:   1.8212 L12:   -.6969
REMARK   3      L13:   -.1267 L23:   -.3553
REMARK   3    S TENSOR
REMARK   3      S11:    .1656 S12:    .2141 S13:   -.0288
REMARK   3      S21:   -.2393 S22:   -.0461 S23:    .0076
REMARK   3      S31:    .0001 S32:   -.1158 S33:   -.1195
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   214        B   227
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0400  32.4527  34.7884
REMARK   3    T TENSOR
REMARK   3      T11:    .1175 T22:    .1398
REMARK   3      T33:    .1832 T12:    .0245
REMARK   3      T13:    .0029 T23:    .0316
REMARK   3    L TENSOR
REMARK   3      L11:  16.8913 L22:   5.2869
REMARK   3      L33:   8.0648 L12:  -3.0432
REMARK   3      L13:  -8.3931 L23:    .9914
REMARK   3    S TENSOR
REMARK   3      S11:    .2984 S12:    .0611 S13:   1.2056
REMARK   3      S21:   -.1794 S22:    .0950 S23:   -.7642
REMARK   3      S31:   -.2336 S32:    .4267 S33:   -.3934
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   228        B   320
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5672  50.6541  34.9537
REMARK   3    T TENSOR
REMARK   3      T11:    .0873 T22:    .0898
REMARK   3      T33:    .1824 T12:    .0124
REMARK   3      T13:    .0206 T23:    .0623
REMARK   3    L TENSOR
REMARK   3      L11:   1.3469 L22:   1.8911
REMARK   3      L33:   2.2386 L12:   -.1025
REMARK   3      L13:    .2192 L23:    .1155
REMARK   3    S TENSOR
REMARK   3      S11:   -.0120 S12:    .1175 S13:    .2261
REMARK   3      S21:   -.0303 S22:    .0784 S23:   -.1893
REMARK   3      S31:   -.2968 S32:    .1352 S33:   -.0665
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   321        B   389
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8367  31.8224  35.4426
REMARK   3    T TENSOR
REMARK   3      T11:    .0533 T22:    .1381
REMARK   3      T33:    .1358 T12:   -.0201
REMARK   3      T13:   -.0091 T23:    .0450
REMARK   3    L TENSOR
REMARK   3      L11:    .8135 L22:   1.0541
REMARK   3      L33:   1.4876 L12:   -.3381
REMARK   3      L13:    .0360 L23:   -.0484
REMARK   3    S TENSOR
REMARK   3      S11:    .0628 S12:    .1161 S13:   -.0728
REMARK   3      S21:   -.1226 S22:    .0103 S23:    .1521
REMARK   3      S31:    .0891 S32:   -.2365 S33:   -.0730
REMARK   3
REMARK   3   TLS GROUP : 21
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   390        B   424
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2295  49.2742  14.6452
REMARK   3    T TENSOR
REMARK   3      T11:    .2116 T22:    .2994
REMARK   3      T33:    .1953 T12:    .0822
REMARK   3      T13:    .0713 T23:    .1195
REMARK   3    L TENSOR
REMARK   3      L11:    .3993 L22:   3.1957
REMARK   3      L33:   3.4324 L12:    .2768
REMARK   3      L13:   -.3305 L23:    .7116
REMARK   3    S TENSOR
REMARK   3      S11:    .1374 S12:    .3018 S13:    .1586
REMARK   3      S21:   -.4047 S22:    .0247 S23:   -.1486
REMARK   3      S31:   -.3321 S32:   -.0398 S33:   -.1622
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   425        B   480
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8156  23.9585  17.1456
REMARK   3    T TENSOR
REMARK   3      T11:    .2278 T22:    .1643
REMARK   3      T33:    .0833 T12:    .0541
REMARK   3      T13:   -.0246 T23:   -.0222
REMARK   3    L TENSOR
REMARK   3      L11:   1.0991 L22:    .8336
REMARK   3      L33:   1.5510 L12:   -.4590
REMARK   3      L13:    .0603 L23:   -.4317
REMARK   3    S TENSOR
REMARK   3      S11:    .1215 S12:    .2261 S13:   -.0360
REMARK   3      S21:   -.2968 S22:   -.0974 S23:    .0043
REMARK   3      S31:    .3899 S32:    .0036 S33:   -.0241
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   481        B   534
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9293  18.6127  15.0864
REMARK   3    T TENSOR
REMARK   3      T11:    .2927 T22:    .1410
REMARK   3      T33:    .1330 T12:    .0278
REMARK   3      T13:   -.0563 T23:   -.0320
REMARK   3    L TENSOR
REMARK   3      L11:   2.3106 L22:   1.8773
REMARK   3      L33:   2.5233 L12:  -1.0225
REMARK   3      L13:  -1.0369 L23:    .2105
REMARK   3    S TENSOR
REMARK   3      S11:    .1364 S12:    .2158 S13:   -.2093
REMARK   3      S21:   -.3540 S22:   -.1303 S23:    .1551
REMARK   3      S31:    .3690 S32:   -.1153 S33:   -.0061
REMARK   3
REMARK   3   TLS GROUP : 24
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   535        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4190  38.7587  35.8170
REMARK   3    T TENSOR
REMARK   3      T11:    .0716 T22:    .2284
REMARK   3      T33:    .1891 T12:   -.0012
REMARK   3      T13:   -.0069 T23:    .0691
REMARK   3    L TENSOR
REMARK   3      L11:   1.1473 L22:    .7674
REMARK   3      L33:   2.4837 L12:   -.4232
REMARK   3      L13:    .1727 L23:   -.9996
REMARK   3    S TENSOR
REMARK   3      S11:    .0530 S12:    .0758 S13:    .0029
REMARK   3      S21:   -.0043 S22:    .1111 S23:    .2000
REMARK   3      S31:    .0236 S32:   -.4092 S33:   -.1642
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 3HS5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83526
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : 0.08400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.9000
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     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.58200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM
REMARK 280  HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.99150
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.27650
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.25800
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.99150
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.27650
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.25800
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.99150
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.27650
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.25800
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.99150
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.27650
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.25800
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: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.8 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     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     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    OE1  NE2
REMARK 470     LYS A  83    CE   NZ
REMARK 470     LYS A 114    NZ
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     ARG A 222    NE   CZ   NH1  NH2
REMARK 470     GLU A 272    CD   OE1  OE2
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     LYS A 473    CD   CE   NZ
REMARK 470     LYS A 485    CE   NZ
REMARK 470     LYS A 557    CD   CE   NZ
REMARK 470     GLN A 583    CD   OE1  NE2
REMARK 470     ASP B  53    OD1  OD2
REMARK 470     GLN B  54    CD   OE1  NE2
REMARK 470     LEU B  75    CG   CD1  CD2
REMARK 470     LYS B  79    CE   NZ
REMARK 470     LEU B  81    CD1  CD2
REMARK 470     LYS B  83    CD   CE   NZ
REMARK 470     LYS B  97    CE   NZ
REMARK 470     LYS B 169    CE   NZ
REMARK 470     GLU B 170    CD   OE1  OE2
REMARK 470     GLU B 186    CD   OE1  OE2
REMARK 470     LYS B 215    CD   CE   NZ
REMARK 470     GLU B 281    CD   OE1  OE2
REMARK 470     LYS B 358    CD   CE   NZ
REMARK 470     LYS B 405    CE   NZ
REMARK 470     ARG B 428    NE   CZ   NH1  NH2
REMARK 470     LYS B 473    CD   CE   NZ
REMARK 470     LYS B 573    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   OE1  GLU A    46     O    HOH A  1337              2.17
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    ASP A 497   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A  61       18.63     56.95
REMARK 500    THR A 129      -94.15   -121.89
REMARK 500    ARG A 185      -66.00    -90.54
REMARK 500    GLU A 398     -118.39     56.17
REMARK 500    ASN A 410       79.11   -116.30
REMARK 500    SER A 496      -47.25     70.74
REMARK 500    THR B 129      -92.48   -120.37
REMARK 500    ARG B 185      -83.61   -101.33
REMARK 500    GLU B 398     -113.53     56.36
REMARK 500    TYR B 409       14.15     57.38
REMARK 500    ASN B 410       77.75   -108.34
REMARK 500    SER B 496      -53.73     70.41
REMARK 500    SER B 579     -178.46   -174.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 755        DISTANCE =  5.85 ANGSTROMS
REMARK 525    HOH B 910        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A1209        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH B1325        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH B1358        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH B1389        DISTANCE =  7.46 ANGSTROMS
REMARK 525    HOH B1412        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH B1413        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH A1332        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH B1427        DISTANCE =  7.73 ANGSTROMS
REMARK 525    HOH B1429        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH A1351        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH A1378        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH A1434        DISTANCE =  6.15 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH B 619  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 COH B 619   NA   94.5
REMARK 620 3 COH B 619   NB   91.2  89.4
REMARK 620 4 COH B 619   NC   87.8 177.4  89.3
REMARK 620 5 COH B 619   ND   88.2  88.9 178.1  92.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH A 619  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 619   NA   88.4
REMARK 620 3 COH A 619   NB   89.7  87.3
REMARK 620 4 COH A 619   NC   87.7 175.4  90.4
REMARK 620 5 COH A 619   ND   84.4  90.3 173.6  91.6
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
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 EDO A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619
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 NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-2
REMARK 900 RELATED ID: 1DDX   RELATED DB: PDB
REMARK 900 PGG2 BOUND TO COX-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB
REMARK 900 UNINHIBITED COX-2
REMARK 900 RELATED ID: 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
DBREF  3HS5 A   35   618  UNP    Q05769   PGH2_MOUSE      20    604
DBREF  3HS5 B   35   618  UNP    Q05769   PGH2_MOUSE      20    604
SEQADV 3HS5 HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED
SEQADV 3HS5 HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3HS5 ALA B  594  UNP  Q05769    ASN   580 ENGINEERED
SEQRES   1 A  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS
SEQRES   2 A  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   3 A  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   4 A  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   5 A  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   6 A  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   7 A  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   8 A  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES   9 A  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  10 A  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  11 A  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  12 A  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  13 A  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  14 A  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  15 A  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  16 A  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  17 A  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  18 A  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  19 A  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  20 A  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  21 A  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  22 A  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  23 A  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  24 A  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  25 A  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  26 A  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  27 A  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  28 A  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  29 A  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  30 A  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  31 A  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  32 A  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  33 A  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  34 A  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  35 A  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  36 A  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  37 A  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  38 A  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  39 A  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  40 A  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  41 A  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  42 A  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  43 A  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  44 A  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS
SEQRES  45 A  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  46 A  591  ARG ARG SER THR GLU LEU
SEQRES   1 B  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS
SEQRES   2 B  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   3 B  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   4 B  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   5 B  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   6 B  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   7 B  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   8 B  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES   9 B  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  10 B  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  11 B  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  12 B  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  13 B  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  14 B  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  15 B  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  16 B  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  17 B  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  18 B  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  19 B  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  20 B  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  21 B  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  22 B  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  23 B  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  24 B  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  25 B  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  26 B  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  27 B  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  28 B  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  29 B  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  30 B  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  31 B  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  32 B  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  33 B  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  34 B  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  35 B  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  36 B  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  37 B  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  38 B  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  39 B  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  40 B  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  41 B  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  42 B  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  43 B  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  44 B  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS
SEQRES  45 B  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  46 B  591  ARG ARG SER THR GLU LEU
MODRES 3HS5 ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3HS5 ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3HS5 ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3HS5 ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3HS5 ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3HS5 ASN B  410  ASN  GLYCOSYLATION SITE
HET    ACD  A   1      44
HET    AKR  A   2       5
HET    AKR  A   3       5
HET    COH  A 619      43
HET    NAG  A 661      14
HET    NAG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    MAN  A 673      11
HET    NAG  A 681      14
HET    BOG  A 703      20
HET    EDO  A 620       4
HET    EDO  A   4       4
HET    EDO  A   5       4
HET    EDO  A  12       4
HET    ACD  B   1      22
HET    COH  B 619      43
HET    NAG  B 661      14
HET    NAG  B 662      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 681      14
HET    BOG  B 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  10       4
HET    EDO  B  11       4
HETNAM     ACD ARACHIDONIC ACID
HETNAM     AKR ACRYLIC ACID
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  ACD    2(C20 H32 O2)
FORMUL   4  AKR    2(C3 H4 O2)
FORMUL   6  COH    2(C34 H32 CO N4 O4)
FORMUL   7  NAG    10(C8 H15 N O6)
FORMUL   8  MAN    C6 H12 O6
FORMUL  10  BOG    2(C14 H28 O6)
FORMUL  11  EDO    12(C2 H6 O2)
FORMUL  29  HOH   *907(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 PHE A   96  ASN A  105  1                                  10
HELIX    4   4 ILE A  105A ARG A  120  1                                  16
HELIX    5   5 SER A  121  ILE A  124  5                                   4
HELIX    6   6 SER A  138  ASN A  144  1                                   7
HELIX    7   7 ASP A  173  LEU A  182  1                                  10
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 LEU A  230  GLY A  235  1                                   6
HELIX   10  10 THR A  237  ARG A  245  1                                   9
HELIX   11  11 THR A  265  GLN A  270  1                                   6
HELIX   12  12 PRO A  280  GLN A  284  5                                   5
HELIX   13  13 VAL A  291  LEU A  294  5                                   4
HELIX   14  14 VAL A  295  HIS A  320  1                                  26
HELIX   15  15 GLY A  324  ASP A  347  1                                  24
HELIX   16  16 ASP A  347  GLY A  354  1                                   8
HELIX   17  17 ASP A  362  PHE A  367  5                                   6
HELIX   18  18 ALA A  378  TYR A  385  1                                   8
HELIX   19  19 TRP A  387  LEU A  391  5                                   5
HELIX   20  20 SER A  403  LEU A  408  1                                   6
HELIX   21  21 ASN A  410  GLN A  429  1                                  20
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  LYS B   83  1                                  11
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 ARG B  120  1                                  16
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  GLY B  418  1                                   8
HELIX   54  54 GLY B  418  GLN B  429  1                                  12
HELIX   55  55 PRO B  441  ALA B  443  5                                   3
HELIX   56  56 VAL B  444  MET B  458  1                                  15
HELIX   57  57 SER B  462  PHE B  470  1                                   9
HELIX   58  58 SER B  477  GLY B  483  1                                   7
HELIX   59  59 LYS B  485  SER B  496  1                                  12
HELIX   60  60 ASP B  497  MET B  501  5                                   5
HELIX   61  61 GLU B  502  GLU B  510  1                                   9
HELIX   62  62 GLY B  519  GLY B  536  1                                  18
HELIX   63  63 ASN B  537  SER B  541  5                                   5
HELIX   64  64 LYS B  546  GLY B  551  5                                   6
HELIX   65  65 GLY B  552  THR B  561  1                                  10
HELIX   66  66 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 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 TYR B 130  ASN B 131  0
SHEET    2   G 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   H 2 GLN B 255  ILE B 257  0
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   I 2 PHE B 395  ILE B 397  0
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
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  2.04
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  2.02
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  1.42
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.43
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
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         NE2AHIS B 388                CO   COH B 619     1555   1555  2.28
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 A 672                 C1  MAN A 673     1555   1555  1.45
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.43
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         NE2AHIS A 388                CO   COH A 619     1555   1555  2.71
CISPEP   1 SER A  126    PRO A  127          0        -0.38
CISPEP   2 SER B  126    PRO B  127          0         1.67
SITE     1 AC1 14 VAL A 116  ARG A 120  PHE A 205  TYR A 348
SITE     2 AC1 14 VAL A 349  SER A 353  TYR A 355  TYR A 385
SITE     3 AC1 14 TRP A 387  VAL A 523  GLY A 526  SER A 530
SITE     4 AC1 14 LEU A 531  HOH A 806
SITE     1 AC2  4 SER A 477  PHE A 478  GLU A 479  LYS A 492
SITE     1 AC3  5 ASP A 239  ARG A 240  GLN A 270  VAL A 271
SITE     2 AC3  5 GLU A 272
SITE     1 AC4 15 ALA A 202  GLN A 203  HIS A 207  PHE A 210
SITE     2 AC4 15 THR A 212  HIS A 214  VAL A 295  ASN A 382
SITE     3 AC4 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391
SITE     4 AC4 15 HOH A 670  HOH A1058  HOH A1345
SITE     1 AC5  6 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 AC5  6 HOH A 689  HOH A 754
SITE     1 AC6  2 NAG A 661  HOH A 689
SITE     1 AC7  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC7  9 HOH A 626  NAG A 672  HOH A 684  HOH A 796
SITE     3 AC7  9 HOH A 845
SITE     1 AC8  4 ARG A 216  NAG A 671  MAN A 673  ASP B 239
SITE     1 AC9  1 NAG A 672
SITE     1 BC1  6 GLN A 406  ASN A 410  SER A 412  ILE A 413
SITE     2 BC1  6 GLU A 416  HOH A 844
SITE     1 BC2 14 LYS A 180  ARG A 184  ARG A 185  ARG A 438
SITE     2 BC2 14 ILE A 442  GLU A 486  GLU A 490  LYS B 175
SITE     3 BC2 14 GLU B 179  ILE B 442  GLN B 445  BOG B 703
SITE     4 BC2 14 HOH B 921  HOH B1425
SITE     1 BC3  8 HIS A  90  GLN A 192  LEU A 352  ARG A 513
SITE     2 BC3  8 ALA A 516  ILE A 517  PHE A 518  VAL A 523
SITE     1 BC4  7 PRO A 162  LEU A 171  SER A 455  ARG A 456
SITE     2 BC4  7 LYS A 459  TYR A 460  HOH A 642
SITE     1 BC5  4 CYS A  57  ASP A  58  CYS A  59  GLU B 553
SITE     1 BC6  7 GLU A 308  ARG A 311  GLU A 339  SER A 566
SITE     2 BC6  7 LEU A 567  ASN A 570  HOH A 697
SITE     1 BC7 14 PHE B 205  PHE B 209  TYR B 348  VAL B 349
SITE     2 BC7 14 TYR B 355  ILE B 377  PHE B 381  TYR B 385
SITE     3 BC7 14 ALA B 527  SER B 530  LEU B 531  GLY B 533
SITE     4 BC7 14 LEU B 534  HOH B 778
SITE     1 BC8 14 TYR B 148  ALA B 199  GLN B 203  HIS B 207
SITE     2 BC8 14 PHE B 210  LYS B 211  THR B 212  VAL B 295
SITE     3 BC8 14 ASN B 382  TYR B 385  HIS B 386  HIS B 388
SITE     4 BC8 14 LEU B 391  GLN B 454
SITE     1 BC9  4 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     1 CC1  2 NAG B 661  HOH B 916
SITE     1 CC2  9 HOH B  15  GLU B 140  ASN B 144  TYR B 147
SITE     2 CC2  9 ARG B 216  NAG B 672  HOH B 793  HOH B 872
SITE     3 CC2  9 HOH B 915
SITE     1 CC3  4 ARG B 216  HOH B 620  NAG B 671  HOH B 772
SITE     1 CC4  4 GLN B 406  ASN B 410  ILE B 413  GLU B 416
SITE     1 CC5 12 LYS A 180  ARG A 185  ARG A 438  GLU A 486
SITE     2 CC5 12 GLU A 490  BOG A 703  GLU B 179  ARG B 184
SITE     3 CC5 12 ARG B 185  ILE B 442  GLN B 445  HOH B 921
SITE     1 CC6  9 HIS B  90  GLN B 192  LEU B 352  ARG B 513
SITE     2 CC6  9 ALA B 516  ILE B 517  PHE B 518  VAL B 523
SITE     3 CC6  9 HOH B 774
SITE     1 CC7  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310
SITE     2 CC7  6 HOH B 834  HOH B 847
SITE     1 CC8  6 PRO B 162  LEU B 171  ARG B 456  LYS B 459
SITE     2 CC8  6 TYR B 460  HOH B 641
SITE     1 CC9  4 SER A 548  MET B  48  LYS B  56  HOH B 889
SITE     1 DC1  7 GLU B 308  ARG B 311  GLU B 339  SER B 566
SITE     2 DC1  7 LEU B 567  ASN B 570  HOH B 792
SITE     1 DC2  6 LEU A 224  SER B 143  HOH B 810  HOH B 859
SITE     2 DC2  6 HOH B 879  HOH B1428
SITE     1 DC3  4 ASP B 325  GLU B 326  HOH B 737  HOH B 891
SITE     1 DC4  5 ARG B 240  LYS B 243  GLN B 270  VAL B 271
SITE     2 DC4  5 GLU B 272
CRYST1  119.983  132.553  180.516  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      0.008335  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007544  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005540        0.00000
      
PROCHECK
Go to PROCHECK summary
 References