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PDBsum entry 3tzi

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Oxidoreductase PDB id
3tzi
Jmol
Contents
Protein chains
551 a.a.
Ligands
ACD ×2
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG
EDO ×8
AKR ×2
Waters ×816
HEADER    OXIDOREDUCTASE                          27-SEP-11   3TZI
TITLE     X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
TITLE    2 CYCLOOXYGENASE CHANNEL OF G533V MURINE COX-2
CAVEAT     3TZI    CHIRALITY ERROR AT ATOM C1 NAG A662 AND ATOM C5 NAG B661
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 19-604;
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    OXIDOREDUCTASE, N-GLYCOSYLATION, MONOTOPIC MEMBRANE PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI
REVDAT   3   01-AUG-12 3TZI    1       JRNL
REVDAT   2   13-JUN-12 3TZI    1       JRNL
REVDAT   1   25-APR-12 3TZI    0
JRNL        AUTH   A.J.VECCHIO,B.J.ORLANDO,R.NANDAGIRI,M.G.MALKOWSKI
JRNL        TITL   INVESTIGATING SUBSTRATE PROMISCUITY IN CYCLOOXYGENASE-2: THE
JRNL        TITL 2 ROLE OF ARG-120 AND RESIDUES LINING THE HYDROPHOBIC GROOVE.
JRNL        REF    J.BIOL.CHEM.                  V. 287 24619 2012
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   22637474
JRNL        DOI    10.1074/JBC.M112.372243
REMARK   2
REMARK   2 RESOLUTION.    2.15 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) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 76377
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) : 0.172
REMARK   3   R VALUE            (WORKING SET) : 0.170
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      : 4039
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) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5537
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330
REMARK   3   BIN FREE R VALUE SET COUNT          : 311
REMARK   3   BIN FREE R VALUE                    : 0.2720
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8869
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 343
REMARK   3   SOLVENT ATOMS            : 816
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.01000
REMARK   3    B22 (A**2) : 0.06000
REMARK   3    B33 (A**2) : -1.07000
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): 0.197
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.167
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.872
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
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):  9577 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13035 ; 1.266 ; 2.003
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1123 ; 5.440 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   450 ;36.643 ;23.956
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1495 ;14.109 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;11.868 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1383 ; 0.086 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7392 ; 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):  5558 ; 0.342 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9037 ; 0.665 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4019 ; 1.390 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3988 ; 2.321 ; 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):  59.5235  38.2426  30.2784
REMARK   3    T TENSOR
REMARK   3      T11:    .0809 T22:    .2600
REMARK   3      T33:    .2299 T12:   -.0738
REMARK   3      T13:    .0623 T23:   -.0674
REMARK   3    L TENSOR
REMARK   3      L11:   1.6217 L22:   4.5305
REMARK   3      L33:   3.4836 L12:  -1.2774
REMARK   3      L13:    .7714 L23:  -1.5200
REMARK   3    S TENSOR
REMARK   3      S11:   -.0005 S12:    .1763 S13:    .0173
REMARK   3      S21:   -.0029 S22:    .0645 S23:   -.2769
REMARK   3      S31:   -.2803 S32:    .5423 S33:   -.0640
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    82
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8305  20.5337  28.0143
REMARK   3    T TENSOR
REMARK   3      T11:    .2943 T22:    .4549
REMARK   3      T33:    .6084 T12:    .1047
REMARK   3      T13:    .0932 T23:   -.1072
REMARK   3    L TENSOR
REMARK   3      L11:   1.2725 L22:  20.9530
REMARK   3      L33:   2.0375 L12:  -1.2026
REMARK   3      L13:   1.3629 L23:   1.9223
REMARK   3    S TENSOR
REMARK   3      S11:    .4694 S12:    .2189 S13:   -.3329
REMARK   3      S21:    .0359 S22:   -.1851 S23:   -.2855
REMARK   3      S31:    .6587 S32:    .2459 S33:   -.2843
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    83        A   102
REMARK   3    ORIGIN FOR THE GROUP (A):  50.0676   5.4200  17.0762
REMARK   3    T TENSOR
REMARK   3      T11:    .3288 T22:    .2416
REMARK   3      T33:    .6477 T12:    .0492
REMARK   3      T13:    .2627 T23:   -.1777
REMARK   3    L TENSOR
REMARK   3      L11:   2.5069 L22:   5.2905
REMARK   3      L33:   3.6513 L12:  -3.2744
REMARK   3      L13:   -.0466 L23:  -1.7833
REMARK   3    S TENSOR
REMARK   3      S11:   -.1350 S12:   -.1409 S13:    .0918
REMARK   3      S21:   -.2890 S22:   -.0077 S23:   -.4121
REMARK   3      S31:    .6239 S32:    .4667 S33:    .1428
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   103        A   122
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3543   3.7199  29.4641
REMARK   3    T TENSOR
REMARK   3      T11:    .2712 T22:    .3415
REMARK   3      T33:    .4417 T12:    .1676
REMARK   3      T13:    .0495 T23:    .0038
REMARK   3    L TENSOR
REMARK   3      L11:   2.6349 L22:   6.1723
REMARK   3      L33:  11.5997 L12:  -1.7249
REMARK   3      L13:   -.9710 L23:   2.8247
REMARK   3    S TENSOR
REMARK   3      S11:   -.0960 S12:    .0151 S13:   -.0760
REMARK   3      S21:    .5371 S22:   -.1532 S23:   -.9455
REMARK   3      S31:    .5831 S32:    .5679 S33:    .2492
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   123        A   185
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5912  37.2484  24.2988
REMARK   3    T TENSOR
REMARK   3      T11:    .0691 T22:    .0493
REMARK   3      T33:    .0821 T12:   -.0406
REMARK   3      T13:    .0314 T23:    .0001
REMARK   3    L TENSOR
REMARK   3      L11:   1.2428 L22:   1.0944
REMARK   3      L33:   4.2987 L12:    .5505
REMARK   3      L13:    .0756 L23:    .7941
REMARK   3    S TENSOR
REMARK   3      S11:   -.0714 S12:    .1531 S13:    .0413
REMARK   3      S21:   -.1259 S22:    .1197 S23:   -.1042
REMARK   3      S31:   -.3421 S32:    .2759 S33:   -.0483
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   186        A   231
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5817  24.1150  21.9634
REMARK   3    T TENSOR
REMARK   3      T11:    .0249 T22:    .0811
REMARK   3      T33:    .0729 T12:    .0265
REMARK   3      T13:   -.0091 T23:    .0091
REMARK   3    L TENSOR
REMARK   3      L11:   1.5933 L22:   1.4944
REMARK   3      L33:   3.4689 L12:   1.4112
REMARK   3      L13:    .3813 L23:    .4188
REMARK   3    S TENSOR
REMARK   3      S11:   -.0934 S12:    .1567 S13:    .1381
REMARK   3      S21:   -.1409 S22:    .0267 S23:    .1669
REMARK   3      S31:   -.1509 S32:   -.1741 S33:    .0667
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   232        A   320
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0628  19.5628  30.7525
REMARK   3    T TENSOR
REMARK   3      T11:    .0231 T22:    .1311
REMARK   3      T33:    .1229 T12:   -.0149
REMARK   3      T13:    .0362 T23:   -.0138
REMARK   3    L TENSOR
REMARK   3      L11:   2.8733 L22:   1.2740
REMARK   3      L33:   4.1006 L12:   -.0740
REMARK   3      L13:   1.0109 L23:   -.2390
REMARK   3    S TENSOR
REMARK   3      S11:    .0014 S12:    .2245 S13:    .2152
REMARK   3      S21:    .0414 S22:   -.0012 S23:    .3005
REMARK   3      S31:   -.0918 S32:   -.4521 S33:   -.0002
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   321        A   397
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7929  14.1626  30.1344
REMARK   3    T TENSOR
REMARK   3      T11:    .0662 T22:    .0271
REMARK   3      T33:    .0821 T12:    .0093
REMARK   3      T13:    .0177 T23:   -.0333
REMARK   3    L TENSOR
REMARK   3      L11:   1.5544 L22:    .9164
REMARK   3      L33:   2.2647 L12:    .7268
REMARK   3      L13:   -.4849 L23:    .1058
REMARK   3    S TENSOR
REMARK   3      S11:   -.0404 S12:    .1389 S13:   -.2228
REMARK   3      S21:    .0022 S22:    .0511 S23:   -.1715
REMARK   3      S31:    .2821 S32:    .0938 S33:   -.0107
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   398        A   429
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4487  16.6686  11.4404
REMARK   3    T TENSOR
REMARK   3      T11:    .1451 T22:    .4531
REMARK   3      T33:    .1010 T12:   -.0271
REMARK   3      T13:   -.0276 T23:   -.0449
REMARK   3    L TENSOR
REMARK   3      L11:   4.8527 L22:   4.3263
REMARK   3      L33:   5.2865 L12:  -2.5613
REMARK   3      L13:   1.6218 L23:  -3.4205
REMARK   3    S TENSOR
REMARK   3      S11:    .1970 S12:    .5608 S13:    .0809
REMARK   3      S21:   -.4343 S22:   -.1600 S23:    .2694
REMARK   3      S31:    .2427 S32:   -.8341 S33:   -.0370
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   430        A   478
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4850  29.9763  14.4558
REMARK   3    T TENSOR
REMARK   3      T11:    .1011 T22:    .1238
REMARK   3      T33:    .0330 T12:   -.0632
REMARK   3      T13:    .0451 T23:   -.0049
REMARK   3    L TENSOR
REMARK   3      L11:   2.3972 L22:   1.8787
REMARK   3      L33:   2.1209 L12:   1.2547
REMARK   3      L13:    .9360 L23:    .6821
REMARK   3    S TENSOR
REMARK   3      S11:   -.1488 S12:    .2577 S13:    .0852
REMARK   3      S21:   -.2070 S22:    .1576 S23:   -.0167
REMARK   3      S31:   -.1442 S32:    .1117 S33:   -.0087
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   479        A   537
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6024  25.7604  12.4818
REMARK   3    T TENSOR
REMARK   3      T11:    .0871 T22:    .1709
REMARK   3      T33:    .0952 T12:   -.0564
REMARK   3      T13:    .0587 T23:   -.0577
REMARK   3    L TENSOR
REMARK   3      L11:   1.4072 L22:   1.9208
REMARK   3      L33:   3.4232 L12:    .8805
REMARK   3      L13:   -.7055 L23:   -.9063
REMARK   3    S TENSOR
REMARK   3      S11:   -.1609 S12:    .3136 S13:   -.1665
REMARK   3      S21:   -.3183 S22:    .1194 S23:   -.2353
REMARK   3      S31:    .0591 S32:    .1755 S33:    .0415
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   538        A   582
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9258   5.7362  32.2630
REMARK   3    T TENSOR
REMARK   3      T11:    .1391 T22:    .0159
REMARK   3      T33:    .1265 T12:   -.0166
REMARK   3      T13:    .0353 T23:   -.0434
REMARK   3    L TENSOR
REMARK   3      L11:   1.3955 L22:   1.9018
REMARK   3      L33:   3.2634 L12:    .4324
REMARK   3      L13:    .4949 L23:   -.0905
REMARK   3    S TENSOR
REMARK   3      S11:    .0469 S12:    .1297 S13:   -.3478
REMARK   3      S21:    .0727 S22:    .0330 S23:   -.1437
REMARK   3      S31:    .5358 S32:   -.0072 S33:   -.0799
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    33        B    67
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0131   2.0529  56.9502
REMARK   3    T TENSOR
REMARK   3      T11:    .7722 T22:    .0215
REMARK   3      T33:    .2256 T12:   -.1181
REMARK   3      T13:   -.0026 T23:    .0193
REMARK   3    L TENSOR
REMARK   3      L11:   4.6086 L22:    .6716
REMARK   3      L33:   3.2543 L12:   -.1541
REMARK   3      L13:  -1.7620 L23:   -.9573
REMARK   3    S TENSOR
REMARK   3      S11:   -.1312 S12:   -.0387 S13:   -.2262
REMARK   3      S21:    .0788 S22:    .0246 S23:    .0001
REMARK   3      S31:    .8234 S32:   -.1545 S33:    .1066
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    68        B    87
REMARK   3    ORIGIN FOR THE GROUP (A):  45.7969    .1364  62.0155
REMARK   3    T TENSOR
REMARK   3      T11:    .6948 T22:    .3843
REMARK   3      T33:    .7102 T12:    .2242
REMARK   3      T13:   -.0601 T23:    .0280
REMARK   3    L TENSOR
REMARK   3      L11:   6.2324 L22:  11.4181
REMARK   3      L33:   3.8407 L12:   1.3318
REMARK   3      L13:    .7385 L23:   6.5799
REMARK   3    S TENSOR
REMARK   3      S11:   -.0806 S12:    .4165 S13:  -1.3048
REMARK   3      S21:    .6098 S22:   1.0173 S23:  -1.7518
REMARK   3      S31:    .4917 S32:    .6900 S33:   -.9367
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    88        B   122
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0036  18.9710  64.1543
REMARK   3    T TENSOR
REMARK   3      T11:    .2396 T22:    .2598
REMARK   3      T33:    .5098 T12:    .1773
REMARK   3      T13:   -.0937 T23:    .0314
REMARK   3    L TENSOR
REMARK   3      L11:   2.4140 L22:   2.4947
REMARK   3      L33:  10.2484 L12:   1.1860
REMARK   3      L13:  -2.3962 L23:  -1.9399
REMARK   3    S TENSOR
REMARK   3      S11:   -.0295 S12:   -.3099 S13:   -.6232
REMARK   3      S21:   -.0554 S22:   -.1443 S23:   -.4235
REMARK   3      S31:    .6063 S32:    .6097 S33:    .1738
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   186
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8427  19.2324  63.1009
REMARK   3    T TENSOR
REMARK   3      T11:    .1384 T22:    .0427
REMARK   3      T33:    .0861 T12:   -.0637
REMARK   3      T13:    .0074 T23:    .0111
REMARK   3    L TENSOR
REMARK   3      L11:    .6495 L22:   1.2284
REMARK   3      L33:   5.3745 L12:    .2216
REMARK   3      L13:    .7265 L23:   1.1308
REMARK   3    S TENSOR
REMARK   3      S11:    .0760 S12:   -.1146 S13:   -.0886
REMARK   3      S21:    .2762 S22:   -.1383 S23:    .0306
REMARK   3      S31:    .4511 S32:   -.3643 S33:    .0623
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   187        B   240
REMARK   3    ORIGIN FOR THE GROUP (A):  36.7601  36.2321  61.8254
REMARK   3    T TENSOR
REMARK   3      T11:    .0130 T22:    .1330
REMARK   3      T33:    .0709 T12:   -.0099
REMARK   3      T13:    .0256 T23:   -.0137
REMARK   3    L TENSOR
REMARK   3      L11:    .9363 L22:   1.9784
REMARK   3      L33:   1.8343 L12:    .7269
REMARK   3      L13:   -.9060 L23:    .4424
REMARK   3    S TENSOR
REMARK   3      S11:    .0710 S12:    .0415 S13:    .0890
REMARK   3      S21:    .0796 S22:   -.0496 S23:    .1409
REMARK   3      S31:   -.0398 S32:   -.1693 S33:   -.0214
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   241        B   268
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1947  55.4014  52.4732
REMARK   3    T TENSOR
REMARK   3      T11:    .1385 T22:    .0056
REMARK   3      T33:    .1551 T12:   -.0010
REMARK   3      T13:    .0254 T23:   -.0258
REMARK   3    L TENSOR
REMARK   3      L11:   1.3830 L22:   3.6288
REMARK   3      L33:   5.4481 L12:    .1504
REMARK   3      L13:   -.2814 L23:   2.6511
REMARK   3    S TENSOR
REMARK   3      S11:    .0122 S12:   -.0316 S13:    .3184
REMARK   3      S21:   -.3548 S22:   -.0507 S23:    .0183
REMARK   3      S31:   -.8002 S32:   -.0520 S33:    .0385
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   356
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7608  45.8868  56.1080
REMARK   3    T TENSOR
REMARK   3      T11:    .0430 T22:    .0295
REMARK   3      T33:    .0842 T12:   -.0091
REMARK   3      T13:    .0210 T23:   -.0367
REMARK   3    L TENSOR
REMARK   3      L11:   1.3621 L22:   2.0623
REMARK   3      L33:   3.3920 L12:    .1181
REMARK   3      L13:   -.4291 L23:   -.5756
REMARK   3    S TENSOR
REMARK   3      S11:    .0565 S12:   -.1081 S13:    .1695
REMARK   3      S21:    .0700 S22:    .1151 S23:    .0302
REMARK   3      S31:   -.3539 S32:    .0309 S33:   -.1717
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   357        B   401
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7831  29.8957  62.5972
REMARK   3    T TENSOR
REMARK   3      T11:    .0487 T22:    .0556
REMARK   3      T33:    .0610 T12:   -.0037
REMARK   3      T13:   -.0424 T23:    .0271
REMARK   3    L TENSOR
REMARK   3      L11:   1.3500 L22:   1.8425
REMARK   3      L33:   2.3773 L12:    .3573
REMARK   3      L13:    .0246 L23:    .5562
REMARK   3    S TENSOR
REMARK   3      S11:    .0360 S12:   -.1550 S13:   -.1150
REMARK   3      S21:    .1921 S22:    .0387 S23:   -.1882
REMARK   3      S31:    .1547 S32:    .2253 S33:   -.0748
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   402        B   429
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2054  50.5420  74.4126
REMARK   3    T TENSOR
REMARK   3      T11:    .1436 T22:    .1426
REMARK   3      T33:    .0886 T12:   -.0755
REMARK   3      T13:    .0636 T23:   -.0748
REMARK   3    L TENSOR
REMARK   3      L11:   4.1424 L22:   5.0157
REMARK   3      L33:   4.7239 L12:    .1709
REMARK   3      L13:  -2.0694 L23:    .3159
REMARK   3    S TENSOR
REMARK   3      S11:    .1470 S12:   -.3119 S13:    .2782
REMARK   3      S21:    .2833 S22:    .0164 S23:    .2246
REMARK   3      S31:   -.2134 S32:    .0349 S33:   -.1634
REMARK   3
REMARK   3   TLS GROUP : 22
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   430        B   469
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9614  25.2602  73.2397
REMARK   3    T TENSOR
REMARK   3      T11:    .1749 T22:    .1071
REMARK   3      T33:    .0354 T12:   -.0633
REMARK   3      T13:    .0134 T23:    .0333
REMARK   3    L TENSOR
REMARK   3      L11:   1.3434 L22:   2.6883
REMARK   3      L33:   2.5314 L12:    .7825
REMARK   3      L13:    .6935 L23:   1.9520
REMARK   3    S TENSOR
REMARK   3      S11:    .1000 S12:   -.2189 S13:    .0469
REMARK   3      S21:    .2827 S22:   -.1086 S23:    .1022
REMARK   3      S31:    .3179 S32:   -.2080 S33:    .0086
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   470        B   553
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9500  20.5200  68.2161
REMARK   3    T TENSOR
REMARK   3      T11:    .2083 T22:    .1156
REMARK   3      T33:    .1146 T12:    .0371
REMARK   3      T13:   -.0420 T23:    .0339
REMARK   3    L TENSOR
REMARK   3      L11:    .8907 L22:   1.2020
REMARK   3      L33:   1.5656 L12:    .6233
REMARK   3      L13:   -.3822 L23:   -.2475
REMARK   3    S TENSOR
REMARK   3      S11:    .0839 S12:   -.2700 S13:   -.1916
REMARK   3      S21:    .2196 S22:   -.0781 S23:   -.1113
REMARK   3      S31:    .4486 S32:    .2394 S33:   -.0058
REMARK   3
REMARK   3   TLS GROUP : 24
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   554        B   583
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2806  42.7687  61.5522
REMARK   3    T TENSOR
REMARK   3      T11:    .0155 T22:    .1904
REMARK   3      T33:    .1586 T12:   -.0005
REMARK   3      T13:   -.0294 T23:   -.0802
REMARK   3    L TENSOR
REMARK   3      L11:   1.5948 L22:   2.6705
REMARK   3      L33:   5.5231 L12:    .9504
REMARK   3      L13:   -.8711 L23:    .9765
REMARK   3    S TENSOR
REMARK   3      S11:    .0906 S12:   -.3773 S13:    .0420
REMARK   3      S21:    .1826 S22:    .1619 S23:   -.2687
REMARK   3      S31:   -.0125 S32:    .8117 S33:   -.2524
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 3TZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068115.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-09
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9780
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING 5.05
REMARK 200                                   ASYMMETRIC CUT SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76377
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
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     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : 0.08700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.44700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.300
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   (%): 54.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
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       61.13250
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.75400
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.54650
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       61.13250
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.75400
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.54650
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       61.13250
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.75400
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.54650
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       61.13250
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.75400
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.54650
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: 14630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A    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     GLN A   583
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ALA A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     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     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     LEU A  75    CG   CD1  CD2
REMARK 470     ILE A  78    CG1  CD1
REMARK 470     LYS A  79    CD   CE   NZ
REMARK 470     LYS A  83    CD   CE   NZ
REMARK 470     LYS A  97    CD   CE   NZ
REMARK 470     LYS A 169    CD   CE   NZ
REMARK 470     GLU A 186    CD   OE1  OE2
REMARK 470     LYS A 215    CE   NZ
REMARK 470     GLN A 318    CD   OE1  NE2
REMARK 470     LYS A 358    CE   NZ
REMARK 470     LYS A 405    CD   CE   NZ
REMARK 470     LYS A 473    CD   CE   NZ
REMARK 470     LYS A 485    CD   CE   NZ
REMARK 470     ASP B  53    CG   OD1  OD2
REMARK 470     GLN B  54    CD   OE1  NE2
REMARK 470     LEU B  75    CD1  CD2
REMARK 470     ILE B  78    CD1
REMARK 470     LYS B  79    CD   CE   NZ
REMARK 470     LEU B  80    CD1  CD2
REMARK 470     LEU B  82    CG   CD1  CD2
REMARK 470     LYS B  83    CG   CD   CE   NZ
REMARK 470     LYS B  97    CD   CE   NZ
REMARK 470     LYS B 114    CE   NZ
REMARK 470     LYS B 169    CG   CD   CE   NZ
REMARK 470     GLU B 170    CG   CD   OE1  OE2
REMARK 470     LYS B 215    CE   NZ
REMARK 470     LYS B 248    CD   CE   NZ
REMARK 470     LYS B 267    CE   NZ
REMARK 470     GLU B 272    CD   OE1  OE2
REMARK 470     LYS B 358    CE   NZ
REMARK 470     LYS B 405    CE   NZ
REMARK 470     GLU B 416    CD   OE1  OE2
REMARK 470     LYS B 473    CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   ND2  ASN B    68     O5   NAG B   661              1.47
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    ASP A  53       37.13   -143.50
REMARK 500    THR A 129      -93.19   -124.24
REMARK 500    ARG A 185      -71.33    -90.27
REMARK 500    TRP A 387       48.21    -90.27
REMARK 500    GLU A 398     -115.87     53.81
REMARK 500    ASN A 410       79.56   -112.60
REMARK 500    SER A 496      -56.07     68.17
REMARK 500    SER A 579     -179.37   -172.56
REMARK 500    ARG B  61       18.59     59.35
REMARK 500    THR B 129      -87.98   -121.75
REMARK 500    ARG B 185      -87.76    -86.12
REMARK 500    ASP B 362       89.98   -154.92
REMARK 500    TRP B 387       45.91    -84.37
REMARK 500    GLU B 398     -116.39     59.90
REMARK 500    TYR B 409        8.17     59.35
REMARK 500    SER B 496      -53.59     70.70
REMARK 500    SER B 579     -179.45   -170.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 903        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH B 904        DISTANCE =  5.09 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   89.3
REMARK 620 3 COH B 619   NB   93.3  87.6
REMARK 620 4 COH B 619   NC   94.5 176.0  90.7
REMARK 620 5 COH B 619   ND   86.1  91.2 178.6  90.5
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   87.1
REMARK 620 3 COH A 619   NB   94.3  87.4
REMARK 620 4 COH A 619   NC   96.9 175.1  89.5
REMARK 620 5 COH A 619   ND   86.1  90.6 177.9  92.5
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 COH A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 620
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 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3KRK   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF L531F MURINE COX-2
REMARK 900 RELATED ID: 3QH0   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF PALMITIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3MDL   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF PGHS-1
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF COX-2
DBREF  3TZI A   28   618  UNP    Q05769   PGH2_MOUSE      19    604
DBREF  3TZI B   28   618  UNP    Q05769   PGH2_MOUSE      19    604
SEQADV 3TZI ALA A   27  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS A   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI VAL A  533  UNP  Q05769    GLY   519 ENGINEERED MUTATION
SEQADV 3TZI ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQADV 3TZI ALA B   27  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   29  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   30  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   31  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   32  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   33  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI HIS B   34  UNP  Q05769              EXPRESSION TAG
SEQADV 3TZI VAL B  533  UNP  Q05769    GLY   519 ENGINEERED MUTATION
SEQADV 3TZI ALA B  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION
SEQRES   1 A  593  ALA ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN
SEQRES   2 A  593  PRO CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE
SEQRES   3 A  593  ASP GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR
SEQRES   4 A  593  GLY GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE
SEQRES   5 A  593  LYS LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR
SEQRES   6 A  593  ILE LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN
SEQRES   7 A  593  ASN ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL
SEQRES   8 A  593  LEU THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR
SEQRES   9 A  593  TYR ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE
SEQRES  10 A  593  SER ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL
SEQRES  11 A  593  ALA ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN
SEQRES  12 A  593  LYS GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL
SEQRES  13 A  593  LEU LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER
SEQRES  14 A  593  ASN MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS
SEQRES  15 A  593  GLN PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE
SEQRES  16 A  593  THR ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE
SEQRES  17 A  593  TYR GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU
SEQRES  18 A  593  PHE LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY
SEQRES  19 A  593  GLU VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU
SEQRES  20 A  593  MET ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE
SEQRES  21 A  593  ALA VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU
SEQRES  22 A  593  MET MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG
SEQRES  23 A  593  VAL CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY
SEQRES  24 A  593  ASP GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE
SEQRES  25 A  593  GLY GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN
SEQRES  26 A  593  HIS LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO
SEQRES  27 A  593  GLU LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG
SEQRES  28 A  593  ILE ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO
SEQRES  29 A  593  LEU LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR
SEQRES  30 A  593  SER PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU
SEQRES  31 A  593  GLU HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG
SEQRES  32 A  593  GLN ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO
SEQRES  33 A  593  ILE ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN
SEQRES  34 A  593  SER ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG
SEQRES  35 A  593  LYS ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU
SEQRES  36 A  593  LEU THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA
SEQRES  37 A  593  LEU TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA
SEQRES  38 A  593  LEU LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY
SEQRES  39 A  593  GLU THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS
SEQRES  40 A  593  VAL LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP
SEQRES  41 A  593  LYS PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE
SEQRES  42 A  593  ILE ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN
SEQRES  43 A  593  VAL LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP
SEQRES  44 A  593  PRO GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA
SEQRES  45 A  593  SER HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU
SEQRES  46 A  593  ILE LYS ARG ARG SER THR GLU LEU
SEQRES   1 B  593  ALA ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN
SEQRES   2 B  593  PRO CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE
SEQRES   3 B  593  ASP GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR
SEQRES   4 B  593  GLY GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE
SEQRES   5 B  593  LYS LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR
SEQRES   6 B  593  ILE LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN
SEQRES   7 B  593  ASN ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL
SEQRES   8 B  593  LEU THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR
SEQRES   9 B  593  TYR ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE
SEQRES  10 B  593  SER ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL
SEQRES  11 B  593  ALA ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN
SEQRES  12 B  593  LYS GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL
SEQRES  13 B  593  LEU LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER
SEQRES  14 B  593  ASN MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS
SEQRES  15 B  593  GLN PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE
SEQRES  16 B  593  THR ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE
SEQRES  17 B  593  TYR GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU
SEQRES  18 B  593  PHE LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY
SEQRES  19 B  593  GLU VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU
SEQRES  20 B  593  MET ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE
SEQRES  21 B  593  ALA VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU
SEQRES  22 B  593  MET MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG
SEQRES  23 B  593  VAL CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY
SEQRES  24 B  593  ASP GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE
SEQRES  25 B  593  GLY GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN
SEQRES  26 B  593  HIS LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO
SEQRES  27 B  593  GLU LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG
SEQRES  28 B  593  ILE ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO
SEQRES  29 B  593  LEU LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR
SEQRES  30 B  593  SER PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU
SEQRES  31 B  593  GLU HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG
SEQRES  32 B  593  GLN ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO
SEQRES  33 B  593  ILE ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN
SEQRES  34 B  593  SER ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG
SEQRES  35 B  593  LYS ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU
SEQRES  36 B  593  LEU THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA
SEQRES  37 B  593  LEU TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA
SEQRES  38 B  593  LEU LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY
SEQRES  39 B  593  GLU THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS
SEQRES  40 B  593  VAL LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP
SEQRES  41 B  593  LYS PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE
SEQRES  42 B  593  ILE ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN
SEQRES  43 B  593  VAL LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP
SEQRES  44 B  593  PRO GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA
SEQRES  45 B  593  SER HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU
SEQRES  46 B  593  ILE LYS ARG ARG SER THR GLU LEU
MODRES 3TZI ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3TZI ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3TZI ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3TZI ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3TZI ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3TZI ASN B  410  ASN  GLYCOSYLATION SITE
HET    ACD  A   1      22
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   2       4
HET    EDO  A   5       4
HET    AKR  A   9       5
HET    AKR  A  10       5
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    EDO  B 620       4
HET    EDO  B   3       4
HET    EDO  B   4       4
HET    EDO  B   6       4
HET    EDO  B   7       4
HET    EDO  B   8       4
HETNAM     ACD ARACHIDONIC 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
HETNAM     AKR ACRYLIC ACID
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  ACD    2(C20 H32 O2)
FORMUL   4  COH    2(C34 H32 CO N4 O4)
FORMUL   5  NAG    10(C8 H15 N O6)
FORMUL   6  MAN    C6 H12 O6
FORMUL   8  BOG    C14 H28 O6
FORMUL   9  EDO    8(C2 H6 O2)
FORMUL  11  AKR    2(C3 H4 O2)
FORMUL  24  HOH   *816(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 SER A  121  1                                  17
HELIX    5   5 TYR A  122  ILE A  124  5                                   3
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 HIS A  386  LEU A  391  5                                   6
HELIX   20  20 SER A  403  LEU A  408  1                                   6
HELIX   21  21 ASN A  411  GLY A  418  1                                   8
HELIX   22  22 GLY A  418  GLN A  429  1                                  12
HELIX   23  23 PRO A  441  ALA A  443  5                                   3
HELIX   24  24 VAL A  444  MET A  458  1                                  15
HELIX   25  25 SER A  462  PHE A  470  1                                   9
HELIX   26  26 SER A  477  GLY A  483  1                                   7
HELIX   27  27 LYS A  485  SER A  496  1                                  12
HELIX   28  28 ASP A  497  MET A  501  5                                   5
HELIX   29  29 GLU A  502  GLU A  510  1                                   9
HELIX   30  30 GLY A  519  GLY A  536  1                                  18
HELIX   31  31 ASN A  537  SER A  541  5                                   5
HELIX   32  32 LYS A  546  GLY A  551  5                                   6
HELIX   33  33 GLY A  552  THR A  561  1                                  10
HELIX   34  34 SER A  563  VAL A  572  1                                  10
HELIX   35  35 GLU B   73  LEU B   82  1                                  10
HELIX   36  36 THR B   85  THR B   94  1                                  10
HELIX   37  37 PHE B   96  ASN B  104  1                                   9
HELIX   38  38 ILE B  105A TYR B  122  1                                  18
HELIX   39  39 SER B  138  ASN B  144  1                                   7
HELIX   40  40 ASP B  173  LEU B  182  1                                  10
HELIX   41  41 ASN B  195  HIS B  207  1                                  13
HELIX   42  42 LEU B  230  GLY B  235  1                                   6
HELIX   43  43 THR B  237  ARG B  245  1                                   9
HELIX   44  44 THR B  265  GLN B  270  1                                   6
HELIX   45  45 PRO B  280  GLN B  284  5                                   5
HELIX   46  46 VAL B  291  LEU B  294  5                                   4
HELIX   47  47 VAL B  295  HIS B  320  1                                  26
HELIX   48  48 GLY B  324  ASP B  347  1                                  24
HELIX   49  49 ASP B  347  GLY B  354  1                                   8
HELIX   50  50 ASP B  362  PHE B  367  5                                   6
HELIX   51  51 ALA B  378  TYR B  385  1                                   8
HELIX   52  52 HIS B  386  LEU B  391  5                                   6
HELIX   53  53 SER B  403  LEU B  408  1                                   6
HELIX   54  54 ASN B  411  GLN B  429  1                                  19
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  GLY A  51  0
SHEET    2   A 2 GLN A  54  ASP A  58 -1  O  ASP A  58   N  GLU A  46
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65
SHEET    1   C 2 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257
SHEET    1   D 2 PHE A 395  ILE A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  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  2.06
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01
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  2.04
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  2.05
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.38
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.43
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.43
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.45
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.45
LINK         NE2 HIS B 388                CO   COH B 619     1555   1555  2.42
LINK         NE2 HIS A 388                CO   COH A 619     1555   1555  2.55
CISPEP   1 SER A  126    PRO A  127          0         3.06
CISPEP   2 SER B  126    PRO B  127          0         3.43
SITE     1 AC1 10 PHE A 205  TYR A 348  TYR A 355  TYR A 385
SITE     2 AC1 10 TRP A 387  MET A 522  GLY A 526  ALA A 527
SITE     3 AC1 10 SER A 530  LEU A 531
SITE     1 AC2 17 ALA A 199  PHE A 200  GLN A 203  HIS A 207
SITE     2 AC2 17 PHE A 210  LYS A 211  THR A 212  HIS A 214
SITE     3 AC2 17 VAL A 295  ASN A 382  TYR A 385  HIS A 386
SITE     4 AC2 17 HIS A 388  LEU A 391  LEU A 408  HOH A 930
SITE     5 AC2 17 HOH A 934
SITE     1 AC3  5 TYR A  55  GLU A  67  ASN A  68  NAG A 662
SITE     2 AC3  5 HOH A 700
SITE     1 AC4  2 NAG A 661  HOH A 965
SITE     1 AC5  8 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC5  8 NAG A 672  HOH A 738  HOH A 904  HOH A 984
SITE     1 AC6  4 ARG A 216  NAG A 671  MAN A 673  ASP B 239
SITE     1 AC7  3 NAG A 672  HOH A1063  ASP B 239
SITE     1 AC8  6 ASN A 410  SER A 412  ILE A 413  GLU A 416
SITE     2 AC8  6 HOH A 690  HOH A 725
SITE     1 AC9 13 GLU A 179  LYS A 180  ARG A 184  ARG A 185
SITE     2 AC9 13 ARG A 438  GLU A 486  GLU A 490  HOH A 878
SITE     3 AC9 13 GLU B 179  ARG B 184  ARG B 185  ILE B 442
SITE     4 AC9 13 GLN B 445
SITE     1 BC1  8 PRO A 162  MET A 163  LEU A 171  SER A 455
SITE     2 BC1  8 ARG A 456  LYS A 459  TYR A 460  HOH A 921
SITE     1 BC2  7 GLU A 308  ARG A 311  GLU A 339  SER A 566
SITE     2 BC2  7 LEU A 567  ASN A 570  HOH A 682
SITE     1 BC3  4 SER A 477  PHE A 478  GLU A 479  LYS A 492
SITE     1 BC4  6 ASP A 239  ARG A 240  LYS A 243  VAL A 271
SITE     2 BC4  6 GLU A 272  HOH A 933
SITE     1 BC5  8 PHE B 205  VAL B 349  SER B 353  TYR B 355
SITE     2 BC5  8 TYR B 385  GLY B 526  ALA B 527  SER B 530
SITE     1 BC6 16 EDO B   8  ALA B 199  GLN B 203  HIS B 207
SITE     2 BC6 16 PHE B 210  LYS B 211  THR B 212  ASN B 382
SITE     3 BC6 16 TYR B 385  HIS B 386  HIS B 388  LEU B 391
SITE     4 BC6 16 VAL B 447  GLN B 454  HOH B 932  HOH B 979
SITE     1 BC7  4 TYR B  55  GLU B  67  ASN B  68  NAG B 662
SITE     1 BC8  2 NAG B 661  HOH B 964
SITE     1 BC9 10 LEU A 238  GLU B 140  ASN B 144  TYR B 147
SITE     2 BC9 10 ARG B 216  HOH B 628  HOH B 634  NAG B 672
SITE     3 BC9 10 HOH B 685  HOH B1048
SITE     1 CC1  4 HOH A 987  ARG B 216  NAG B 671  HOH B 783
SITE     1 CC2  4 ASN B 410  ILE B 413  HOH B 678  HOH B 982
SITE     1 CC3  6 LYS B 251  TYR B 254  ASN B 310  HOH B 889
SITE     2 CC3  6 HOH B 980  HOH B1010
SITE     1 CC4  7 PRO B 162  LEU B 171  SER B 455  ARG B 456
SITE     2 CC4  7 LYS B 459  TYR B 460  HOH B 887
SITE     1 CC5  3 ARG B 240  LYS B 243  GLU B 272
SITE     1 CC6  6 LEU B 145  LEU B 224  HOH B 866  HOH B 909
SITE     2 CC6  6 HOH B 910  HOH B 981
SITE     1 CC7  7 LYS B 175  LEU B 178  GLN B 445  ALA B 446
SITE     2 CC7  7 LYS B 449  HOH B 656  HOH B 901
SITE     1 CC8  4 LEU B 294  VAL B 295  COH B 619  HOH B 841
CRYST1  122.265  133.508  181.093  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      0.008179  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007490  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005522        0.00000
      
PROCHECK
Go to PROCHECK summary
 References