HEADER OXIDOREDUCTASE 30-MAR-10 3MDL
TITLE X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL 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 FRAGMENT: UNP RESIDUES 20 TO 599;
COMPND 5 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND 6 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND 7 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND 8 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND 9 2;
COMPND 10 EC: 1.14.99.1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: 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: EXPRESSION;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS COX-2, CYCLOOXYGENASE-2, ENDOCANNABINOID, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.VECCHIO,M.G.MALKOWSKI
REVDAT 4 29-JUN-11 3MDL 1 JRNL
REVDAT 3 15-JUN-11 3MDL 1 JRNL
REVDAT 2 20-APR-11 3MDL 1 JRNL
REVDAT 1 13-APR-11 3MDL 0
JRNL AUTH A.J.VECCHIO,M.G.MALKOWSKI
JRNL TITL THE STRUCTURAL BASIS OF ENDOCANNABINOID OXYGENATION BY
JRNL TITL 2 CYCLOOXYGENASE-2.
JRNL REF J.BIOL.CHEM. V. 286 20736 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21489986
JRNL DOI 10.1074/JBC.M111.230367
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 67549
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3597
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4546
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 229
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8906
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 354
REMARK 3 SOLVENT ATOMS : 960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.06000
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): 0.233
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.189
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9605 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13054 ; 1.127 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1113 ; 5.221 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 446 ;36.597 ;23.946
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1528 ;13.612 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;12.710 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1383 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7363 ; 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): 5553 ; 0.328 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9014 ; 0.668 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4052 ; 1.288 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4036 ; 2.237 ; 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): .7944 38.0085 59.2429
REMARK 3 T TENSOR
REMARK 3 T11: .0502 T22: .1831
REMARK 3 T33: .1478 T12: .0716
REMARK 3 T13: .0406 T23: .0688
REMARK 3 L TENSOR
REMARK 3 L11: 1.3400 L22: 2.0080
REMARK 3 L33: 2.7309 L12: 1.2029
REMARK 3 L13: -.0039 L23: .3589
REMARK 3 S TENSOR
REMARK 3 S11: -.0756 S12: -.0313 S13: .0838
REMARK 3 S21: .0391 S22: .1919 S23: .2162
REMARK 3 S31: -.2180 S32: -.4567 S33: -.1163
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 92
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0204 17.3088 66.2660
REMARK 3 T TENSOR
REMARK 3 T11: .0540 T22: .2391
REMARK 3 T33: .3922 T12: -.0984
REMARK 3 T13: -.0103 T23: .1311
REMARK 3 L TENSOR
REMARK 3 L11: 2.4547 L22: 3.9107
REMARK 3 L33: 2.8985 L12: -3.0199
REMARK 3 L13: 1.8457 L23: -2.8078
REMARK 3 S TENSOR
REMARK 3 S11: .0997 S12: -.2022 S13: -.6007
REMARK 3 S21: -.1995 S22: .4235 S23: .7528
REMARK 3 S31: .3053 S32: -.5686 S33: -.5232
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 93 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2919 2.3208 64.7852
REMARK 3 T TENSOR
REMARK 3 T11: .0893 T22: .1335
REMARK 3 T33: .2360 T12: -.0988
REMARK 3 T13: .0175 T23: .0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.9080 L22: 6.4798
REMARK 3 L33: 10.7451 L12: -.5772
REMARK 3 L13: -4.0107 L23: -2.6001
REMARK 3 S TENSOR
REMARK 3 S11: -.2947 S12: .2448 S13: -.2261
REMARK 3 S21: -.1493 S22: -.0397 S23: .2744
REMARK 3 S31: .7390 S32: -.5137 S33: .3344
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 186
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5687 36.6243 66.1563
REMARK 3 T TENSOR
REMARK 3 T11: .0899 T22: .0835
REMARK 3 T33: .0946 T12: .0270
REMARK 3 T13: .0025 T23: -.0136
REMARK 3 L TENSOR
REMARK 3 L11: .4753 L22: .7346
REMARK 3 L33: 1.4008 L12: -.1943
REMARK 3 L13: -.1822 L23: -.4155
REMARK 3 S TENSOR
REMARK 3 S11: -.0412 S12: -.0669 S13: .0890
REMARK 3 S21: .1243 S22: .0996 S23: .0072
REMARK 3 S31: -.1350 S32: -.1004 S33: -.0584
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 187 A 233
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4871 23.4280 67.2984
REMARK 3 T TENSOR
REMARK 3 T11: .0666 T22: .0686
REMARK 3 T33: .1096 T12: .0085
REMARK 3 T13: -.0134 T23: .0012
REMARK 3 L TENSOR
REMARK 3 L11: .8765 L22: .9814
REMARK 3 L33: 1.4250 L12: -.7511
REMARK 3 L13: .5552 L23: -.6133
REMARK 3 S TENSOR
REMARK 3 S11: -.0662 S12: -.0712 S13: .0880
REMARK 3 S21: .1178 S22: .0206 S23: -.1006
REMARK 3 S31: -.1383 S32: .0910 S33: .0457
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 234 A 271
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0572 19.5714 56.1051
REMARK 3 T TENSOR
REMARK 3 T11: .0062 T22: .0801
REMARK 3 T33: .1288 T12: .0062
REMARK 3 T13: .0143 T23: .0226
REMARK 3 L TENSOR
REMARK 3 L11: 1.8969 L22: 1.0826
REMARK 3 L33: 2.1309 L12: -.2838
REMARK 3 L13: .8569 L23: -.1573
REMARK 3 S TENSOR
REMARK 3 S11: .0160 S12: .0386 S13: .0728
REMARK 3 S21: -.0634 S22: -.0033 S23: -.0627
REMARK 3 S31: -.0238 S32: .2122 S33: -.0127
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 320
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2878 18.5955 62.9160
REMARK 3 T TENSOR
REMARK 3 T11: .0222 T22: .1037
REMARK 3 T33: .1302 T12: .0149
REMARK 3 T13: .0062 T23: .0306
REMARK 3 L TENSOR
REMARK 3 L11: 1.4443 L22: .7709
REMARK 3 L33: 2.9760 L12: .1286
REMARK 3 L13: -.0810 L23: .3696
REMARK 3 S TENSOR
REMARK 3 S11: .0692 S12: -.2021 S13: .1149
REMARK 3 S21: .0502 S22: -.0475 S23: -.0772
REMARK 3 S31: -.0508 S32: .1309 S33: -.0217
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 400
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7925 13.9973 61.1420
REMARK 3 T TENSOR
REMARK 3 T11: .0792 T22: .0600
REMARK 3 T33: .1130 T12: -.0022
REMARK 3 T13: -.0046 T23: .0259
REMARK 3 L TENSOR
REMARK 3 L11: .4878 L22: .4647
REMARK 3 L33: 1.0978 L12: -.2228
REMARK 3 L13: -.2892 L23: -.1502
REMARK 3 S TENSOR
REMARK 3 S11: -.0580 S12: -.1021 S13: -.0903
REMARK 3 S21: .0320 S22: .0621 S23: .0535
REMARK 3 S31: .1152 S32: .0213 S33: -.0041
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 401 A 445
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3672 18.4277 80.0507
REMARK 3 T TENSOR
REMARK 3 T11: .0898 T22: .1250
REMARK 3 T33: .0266 T12: .0222
REMARK 3 T13: -.0260 T23: -.0069
REMARK 3 L TENSOR
REMARK 3 L11: 4.2694 L22: 1.2534
REMARK 3 L33: 1.8958 L12: -1.1034
REMARK 3 L13: -1.0576 L23: .6027
REMARK 3 S TENSOR
REMARK 3 S11: -.0997 S12: -.4298 S13: .0955
REMARK 3 S21: .1412 S22: .1617 S23: -.1657
REMARK 3 S31: -.0351 S32: .3632 S33: -.0620
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 446 A 493
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4115 31.5774 76.8399
REMARK 3 T TENSOR
REMARK 3 T11: .1036 T22: .1043
REMARK 3 T33: .0521 T12: .0824
REMARK 3 T13: .0386 T23: .0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.6548 L22: 1.2491
REMARK 3 L33: 2.2864 L12: .1235
REMARK 3 L13: .3674 L23: -.0355
REMARK 3 S TENSOR
REMARK 3 S11: -.1204 S12: -.2340 S13: .0565
REMARK 3 S21: .2700 S22: .1708 S23: .0889
REMARK 3 S31: -.0660 S32: -.2129 S33: -.0503
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 494 A 553
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4656 20.1759 66.2711
REMARK 3 T TENSOR
REMARK 3 T11: .0853 T22: .0577
REMARK 3 T33: .0873 T12: .0177
REMARK 3 T13: .0041 T23: .0346
REMARK 3 L TENSOR
REMARK 3 L11: .6801 L22: .7642
REMARK 3 L33: 1.8301 L12: -.2860
REMARK 3 L13: -.5181 L23: .6076
REMARK 3 S TENSOR
REMARK 3 S11: -.0415 S12: -.0921 S13: -.0966
REMARK 3 S21: .0166 S22: -.0091 S23: .1555
REMARK 3 S31: -.0327 S32: -.1495 S33: .0506
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): 36.5765 3.5356 64.7406
REMARK 3 T TENSOR
REMARK 3 T11: .1122 T22: .0424
REMARK 3 T33: .1470 T12: -.0121
REMARK 3 T13: .0219 T23: .0491
REMARK 3 L TENSOR
REMARK 3 L11: .9657 L22: 2.6977
REMARK 3 L33: 3.1549 L12: -.6403
REMARK 3 L13: -.1089 L23: .3619
REMARK 3 S TENSOR
REMARK 3 S11: -.0314 S12: -.0447 S13: -.2121
REMARK 3 S21: .0883 S22: .0302 S23: .0613
REMARK 3 S31: .4086 S32: -.0600 S33: .0012
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): 33.2325 1.7778 33.5452
REMARK 3 T TENSOR
REMARK 3 T11: .3001 T22: .0341
REMARK 3 T33: .1198 T12: .0766
REMARK 3 T13: -.0284 T23: -.0227
REMARK 3 L TENSOR
REMARK 3 L11: 5.6239 L22: .4212
REMARK 3 L33: 3.4491 L12: .8908
REMARK 3 L13: -1.4505 L23: -.2316
REMARK 3 S TENSOR
REMARK 3 S11: .0655 S12: -.1149 S13: -.3505
REMARK 3 S21: -.1938 S22: -.0749 S23: .0162
REMARK 3 S31: .5899 S32: .2736 S33: .0094
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 89
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2421 1.0290 27.2664
REMARK 3 T TENSOR
REMARK 3 T11: .5001 T22: .1890
REMARK 3 T33: .4684 T12: -.2770
REMARK 3 T13: -.2410 T23: .0587
REMARK 3 L TENSOR
REMARK 3 L11: 7.2498 L22: 6.7230
REMARK 3 L33: 5.1094 L12: -6.7524
REMARK 3 L13: 5.8969 L23: -5.8608
REMARK 3 S TENSOR
REMARK 3 S11: .4829 S12: -.3633 S13: -1.0806
REMARK 3 S21: -.8989 S22: .5669 S23: 1.2027
REMARK 3 S31: .7744 S32: -.4925 S33: -1.0498
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 90 B 122
REMARK 3 ORIGIN FOR THE GROUP (A): .6869 19.0695 25.9556
REMARK 3 T TENSOR
REMARK 3 T11: .1695 T22: .1059
REMARK 3 T33: .2347 T12: -.1259
REMARK 3 T13: -.0247 T23: .0021
REMARK 3 L TENSOR
REMARK 3 L11: 4.5453 L22: 2.5659
REMARK 3 L33: 10.9226 L12: -2.4241
REMARK 3 L13: -1.1575 L23: 2.3546
REMARK 3 S TENSOR
REMARK 3 S11: -.0683 S12: .1347 S13: -.6463
REMARK 3 S21: .0681 S22: -.2108 S23: .3585
REMARK 3 S31: .7305 S32: -.6628 S33: .2791
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 188
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1777 19.3525 26.7035
REMARK 3 T TENSOR
REMARK 3 T11: .1155 T22: .0686
REMARK 3 T33: .0858 T12: .0316
REMARK 3 T13: .0124 T23: -.0062
REMARK 3 L TENSOR
REMARK 3 L11: .6102 L22: .8508
REMARK 3 L33: 1.7826 L12: -.2535
REMARK 3 L13: .1770 L23: -.3744
REMARK 3 S TENSOR
REMARK 3 S11: .0781 S12: .0709 S13: -.0410
REMARK 3 S21: -.1489 S22: -.0737 S23: -.0455
REMARK 3 S31: .2752 S32: .1681 S33: -.0045
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 189 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0789 35.8773 29.6002
REMARK 3 T TENSOR
REMARK 3 T11: .0480 T22: .1055
REMARK 3 T33: .1549 T12: -.0133
REMARK 3 T13: .0124 T23: .0218
REMARK 3 L TENSOR
REMARK 3 L11: .8099 L22: .8505
REMARK 3 L33: 1.2508 L12: -.6668
REMARK 3 L13: -.4511 L23: -.1713
REMARK 3 S TENSOR
REMARK 3 S11: .0469 S12: -.0295 S13: .1149
REMARK 3 S21: -.0336 S22: .0218 S23: -.1111
REMARK 3 S31: -.0409 S32: .0529 S33: -.0687
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 269
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3689 54.8537 37.7259
REMARK 3 T TENSOR
REMARK 3 T11: .0815 T22: .0517
REMARK 3 T33: .1692 T12: -.0096
REMARK 3 T13: .0109 T23: .0639
REMARK 3 L TENSOR
REMARK 3 L11: 1.9447 L22: .7843
REMARK 3 L33: 3.7267 L12: -.8438
REMARK 3 L13: 1.2778 L23: -.7502
REMARK 3 S TENSOR
REMARK 3 S11: -.0562 S12: .1563 S13: .2775
REMARK 3 S21: .0899 S22: .0485 S23: .0400
REMARK 3 S31: -.4830 S32: .1929 S33: .0076
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 270 B 302
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3137 50.2291 27.9276
REMARK 3 T TENSOR
REMARK 3 T11: .0944 T22: .1161
REMARK 3 T33: .1459 T12: -.0643
REMARK 3 T13: .0536 T23: .0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.9598 L22: 2.6772
REMARK 3 L33: 3.3613 L12: -.6681
REMARK 3 L13: -.2478 L23: .7634
REMARK 3 S TENSOR
REMARK 3 S11: .1117 S12: -.0002 S13: .2110
REMARK 3 S21: -.2620 S22: .1198 S23: -.4331
REMARK 3 S31: -.4743 S32: .5014 S33: -.2315
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 303 B 356
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9765 42.2065 37.5449
REMARK 3 T TENSOR
REMARK 3 T11: .0455 T22: .1059
REMARK 3 T33: .1281 T12: .0051
REMARK 3 T13: -.0061 T23: .0511
REMARK 3 L TENSOR
REMARK 3 L11: .9119 L22: 1.1399
REMARK 3 L33: 1.2340 L12: -.4613
REMARK 3 L13: -.3528 L23: .1860
REMARK 3 S TENSOR
REMARK 3 S11: -.0173 S12: .0594 S13: .0433
REMARK 3 S21: -.0043 S22: .0108 S23: .0892
REMARK 3 S31: -.1071 S32: -.2186 S33: .0065
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 357 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2266 29.3741 27.4792
REMARK 3 T TENSOR
REMARK 3 T11: .0791 T22: .0553
REMARK 3 T33: .0994 T12: -.0156
REMARK 3 T13: -.0243 T23: -.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.0305 L22: 1.1974
REMARK 3 L33: 1.9369 L12: .0476
REMARK 3 L13: -.2169 L23: -.6741
REMARK 3 S TENSOR
REMARK 3 S11: .0912 S12: .1227 S13: -.0536
REMARK 3 S21: -.2037 S22: -.0183 S23: .1385
REMARK 3 S31: .1031 S32: -.0519 S33: -.0729
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 402 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8147 50.1267 15.9849
REMARK 3 T TENSOR
REMARK 3 T11: .0699 T22: .0974
REMARK 3 T33: .0647 T12: .0240
REMARK 3 T13: .0369 T23: .0708
REMARK 3 L TENSOR
REMARK 3 L11: 4.0160 L22: 4.3384
REMARK 3 L33: 2.6874 L12: .5910
REMARK 3 L13: -.1458 L23: .0690
REMARK 3 S TENSOR
REMARK 3 S11: .1647 S12: .2772 S13: .0807
REMARK 3 S21: -.2764 S22: -.0502 S23: -.1552
REMARK 3 S31: -.3419 S32: .0203 S33: -.1144
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 430 B 531
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4801 19.6962 15.5314
REMARK 3 T TENSOR
REMARK 3 T11: .1354 T22: .0635
REMARK 3 T33: .0256 T12: .0265
REMARK 3 T13: -.0068 T23: -.0277
REMARK 3 L TENSOR
REMARK 3 L11: .8835 L22: .9511
REMARK 3 L33: 1.4713 L12: -.3682
REMARK 3 L13: .3625 L23: -.4187
REMARK 3 S TENSOR
REMARK 3 S11: .0908 S12: .1966 S13: -.0656
REMARK 3 S21: -.2084 S22: -.0604 S23: .0366
REMARK 3 S31: .2885 S32: .0154 S33: -.0304
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 532 B 583
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9097 37.4845 35.3803
REMARK 3 T TENSOR
REMARK 3 T11: .0087 T22: .1082
REMARK 3 T33: .1244 T12: -.0172
REMARK 3 T13: -.0062 T23: .0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.3650 L22: .8816
REMARK 3 L33: 2.2849 L12: -.2126
REMARK 3 L13: -.2127 L23: -.8053
REMARK 3 S TENSOR
REMARK 3 S11: .0289 S12: .0541 S13: .0187
REMARK 3 S21: -.0354 S22: .0743 S23: .1227
REMARK 3 S31: .0559 S32: -.2624 S33: -.1031
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3MDL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058413.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 77
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) : 0.9777
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 : 67549
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID SODIUM SALT,
REMARK 280 0.1M HEPES PH 7.5, 0.02M MAGNESIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, 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 59.47900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.88650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 89.92900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.47900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.88650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 89.92900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.47900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.88650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 89.92900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.47900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.88650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 89.92900
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 300 REMARK: ASYMMETRIC UNIT CONTAINS THE COX-2 BIOLOGICAL DIMER.
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: 11490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 ASN A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 ASP A 584
REMARK 465 PRO A 585
REMARK 465 GLN A 586
REMARK 465 PRO A 587
REMARK 465 THR A 588
REMARK 465 LYS A 589
REMARK 465 THR A 590
REMARK 465 ALA A 591
REMARK 465 THR A 592
REMARK 465 ILE A 593
REMARK 465 ALA A 594
REMARK 465 ALA A 595
REMARK 465 SER A 596
REMARK 465 ALA A 597
REMARK 465 SER A 598
REMARK 465 HIS A 599
REMARK 465 SER A 600
REMARK 465 ARG A 601
REMARK 465 LEU A 602
REMARK 465 ASP A 603
REMARK 465 ASP A 604
REMARK 465 ILE A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 VAL A 609
REMARK 465 LEU A 610
REMARK 465 ILE A 611
REMARK 465 LYS A 612
REMARK 465 ARG A 613
REMARK 465 ASN B 28
REMARK 465 HIS B 29
REMARK 465 HIS B 30
REMARK 465 HIS B 31
REMARK 465 HIS B 32
REMARK 465 GLN B 583
REMARK 465 ASP B 584
REMARK 465 PRO B 585
REMARK 465 GLN B 586
REMARK 465 PRO B 587
REMARK 465 THR B 588
REMARK 465 LYS B 589
REMARK 465 THR B 590
REMARK 465 ALA B 591
REMARK 465 THR B 592
REMARK 465 ILE B 593
REMARK 465 ALA B 594
REMARK 465 ALA B 595
REMARK 465 SER B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 HIS B 599
REMARK 465 SER B 600
REMARK 465 ARG B 601
REMARK 465 LEU B 602
REMARK 465 ASP B 603
REMARK 465 ASP B 604
REMARK 465 ILE B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 VAL B 609
REMARK 465 LEU B 610
REMARK 465 ILE B 611
REMARK 465 LYS B 612
REMARK 465 ARG B 613
REMARK 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 GLU A 170 OE1 OE2
REMARK 470 LYS A 215 CD CE NZ
REMARK 470 ASP A 239 OD1 OD2
REMARK 470 LYS A 358 CE NZ
REMARK 470 LYS A 405 CD CE NZ
REMARK 470 LYS A 557 NZ
REMARK 470 GLN A 583 CD OE1 NE2
REMARK 470 LEU B 75 CG CD1 CD2
REMARK 470 LEU B 81 CD1 CD2
REMARK 470 LYS B 83 CD CE NZ
REMARK 470 LYS B 97 CE NZ
REMARK 470 GLU B 170 OE1 OE2
REMARK 470 LYS B 175 NZ
REMARK 470 GLU B 186 CD OE1 OE2
REMARK 470 LYS B 215 NZ
REMARK 470 LYS B 267 CG CD CE NZ
REMARK 470 ASP B 268 CG OD1 OD2
REMARK 470 LYS B 358 NZ
REMARK 470 LYS B 405 CD CE NZ
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 LEU B 531 CA - CB - CG ANGL. DEV. = 14.6 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 17.31 57.18
REMARK 500 THR A 129 -92.82 -119.23
REMARK 500 ASP A 249 19.71 58.29
REMARK 500 GLU A 398 -118.64 56.01
REMARK 500 ASN A 439 15.61 -145.74
REMARK 500 SER A 496 -40.35 70.37
REMARK 500 CYS A 575 64.16 39.33
REMARK 500 THR B 129 -91.87 -119.01
REMARK 500 ARG B 185 -92.27 -94.18
REMARK 500 GLU B 398 -120.00 57.12
REMARK 500 SER B 496 -51.06 74.47
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 830 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH A 952 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A1022 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH A1023 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH A1076 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH B 634 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B 647 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B 740 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B 872 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH B 917 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH B 951 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH B 990 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH B 991 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B 994 DISTANCE = 5.52 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 615 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 COH B 615 NA 92.2
REMARK 620 3 COH B 615 NB 91.6 87.3
REMARK 620 4 COH B 615 NC 92.2 174.8 89.8
REMARK 620 5 COH B 615 ND 90.2 89.0 175.9 93.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 COH A 614 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 COH A 614 NA 92.4
REMARK 620 3 COH A 614 NB 81.7 86.7
REMARK 620 4 COH A 614 NC 89.3 176.0 89.9
REMARK 620 5 COH A 614 ND 97.6 90.7 177.3 92.7
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 1AG 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 GOL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS5 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 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: 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 3MDL A 35 613 UNP Q05769 PGH2_MOUSE 20 599
DBREF 3MDL B 35 613 UNP Q05769 PGH2_MOUSE 20 599
SEQADV 3MDL ASN A 28 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 29 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 30 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 31 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 32 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 33 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS A 34 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL ALA A 594 UNP Q05769 ASN 580 ENGINEERED
SEQADV 3MDL ASN B 28 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 29 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 30 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 31 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 32 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 33 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL HIS B 34 UNP Q05769 EXPRESSION TAG
SEQADV 3MDL ALA B 594 UNP Q05769 ASN 580 ENGINEERED
SEQRES 1 A 587 ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES 2 A 587 CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES 3 A 587 GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES 4 A 587 GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES 5 A 587 LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES 6 A 587 LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES 7 A 587 ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES 8 A 587 THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES 9 A 587 ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES 10 A 587 ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES 11 A 587 ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES 12 A 587 GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES 13 A 587 LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES 14 A 587 MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES 15 A 587 PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES 16 A 587 ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES 17 A 587 GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES 18 A 587 LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES 19 A 587 VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES 20 A 587 ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES 21 A 587 VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES 22 A 587 MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES 23 A 587 CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES 24 A 587 GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES 25 A 587 GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES 26 A 587 LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES 27 A 587 LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES 28 A 587 ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES 29 A 587 LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES 30 A 587 PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES 31 A 587 HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES 32 A 587 ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES 33 A 587 ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES 34 A 587 ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES 35 A 587 ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES 36 A 587 THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES 37 A 587 TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES 38 A 587 LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU
SEQRES 39 A 587 THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES 40 A 587 LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES 41 A 587 PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES 42 A 587 ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES 43 A 587 LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES 44 A 587 GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER
SEQRES 45 A 587 HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES 46 A 587 LYS ARG
SEQRES 1 B 587 ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES 2 B 587 CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES 3 B 587 GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES 4 B 587 GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES 5 B 587 LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES 6 B 587 LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES 7 B 587 ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES 8 B 587 THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES 9 B 587 ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES 10 B 587 ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES 11 B 587 ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES 12 B 587 GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES 13 B 587 LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES 14 B 587 MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES 15 B 587 PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES 16 B 587 ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES 17 B 587 GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES 18 B 587 LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES 19 B 587 VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES 20 B 587 ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES 21 B 587 VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES 22 B 587 MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES 23 B 587 CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES 24 B 587 GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES 25 B 587 GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES 26 B 587 LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES 27 B 587 LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES 28 B 587 ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES 29 B 587 LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES 30 B 587 PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES 31 B 587 HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES 32 B 587 ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES 33 B 587 ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES 34 B 587 ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES 35 B 587 ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES 36 B 587 THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES 37 B 587 TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES 38 B 587 LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU
SEQRES 39 B 587 THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES 40 B 587 LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES 41 B 587 PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES 42 B 587 ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES 43 B 587 LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES 44 B 587 GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER
SEQRES 45 B 587 HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES 46 B 587 LYS ARG
MODRES 3MDL ASN B 68 ASN GLYCOSYLATION SITE
MODRES 3MDL ASN A 144 ASN GLYCOSYLATION SITE
MODRES 3MDL ASN B 144 ASN GLYCOSYLATION SITE
MODRES 3MDL ASN A 68 ASN GLYCOSYLATION SITE
MODRES 3MDL ASN A 410 ASN GLYCOSYLATION SITE
MODRES 3MDL ASN B 410 ASN GLYCOSYLATION SITE
HET 1AG A 1 27
HET AKR A 2 5
HET AKR A 3 5
HET GOL A 4 6
HET COH A 614 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 GOL B 7 6
HET 1AG B 1 27
HET AKR B 3 5
HET AKR B 4 5
HET AKR B 5 5
HET GOL B 6 6
HET COH B 615 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
HETNAM 1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,
HETNAM 2 1AG 14-TETRAENOATE
HETNAM AKR ACRYLIC ACID
HETNAM GOL GLYCEROL
HETNAM COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BOG B-OCTYLGLUCOSIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 1AG 2(C23 H38 O4)
FORMUL 4 AKR 5(C3 H4 O2)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 7 COH 2(C34 H32 CO N4 O4)
FORMUL 8 NAG 10(C8 H15 N O6)
FORMUL 9 MAN C6 H12 O6
FORMUL 11 BOG C14 H28 O6
FORMUL 22 HOH *960(H2 O)
HELIX 1 1 GLU A 73 LYS A 83 1 11
HELIX 2 2 THR A 85 THR A 94 1 10
HELIX 3 3 PHE A 96 ILE A 105A 1 11
HELIX 4 4 ILE A 105A TYR A 122 1 18
HELIX 5 5 SER A 138 ASN A 144 1 7
HELIX 6 6 ASP A 173 LEU A 182 1 10
HELIX 7 7 ASN A 195 HIS A 207 1 13
HELIX 8 8 LEU A 230 GLY A 235 1 6
HELIX 9 9 THR A 237 ARG A 245 1 9
HELIX 10 10 THR A 265 GLN A 270 1 6
HELIX 11 11 PRO A 280 GLN A 284 5 5
HELIX 12 12 VAL A 295 HIS A 320 1 26
HELIX 13 13 GLY A 324 ASP A 347 1 24
HELIX 14 14 ASP A 347 GLY A 354 1 8
HELIX 15 15 ASP A 362 PHE A 367 5 6
HELIX 16 16 ALA A 378 TYR A 385 1 8
HELIX 17 17 TRP A 387 LEU A 391 5 5
HELIX 18 18 SER A 403 LEU A 408 1 6
HELIX 19 19 ASN A 410 GLN A 429 1 20
HELIX 20 20 PRO A 441 ALA A 443 5 3
HELIX 21 21 VAL A 444 MET A 458 1 15
HELIX 22 22 SER A 462 PHE A 470 1 9
HELIX 23 23 SER A 477 GLY A 483 1 7
HELIX 24 24 LYS A 485 SER A 496 1 12
HELIX 25 25 ASP A 497 MET A 501 5 5
HELIX 26 26 GLU A 502 GLU A 510 1 9
HELIX 27 27 GLY A 519 GLY A 536 1 18
HELIX 28 28 ASN A 537 SER A 541 5 5
HELIX 29 29 LYS A 546 GLY A 551 5 6
HELIX 30 30 GLY A 552 THR A 561 1 10
HELIX 31 31 SER A 563 VAL A 572 1 10
HELIX 32 32 GLU B 73 LYS B 83 1 11
HELIX 33 33 THR B 85 HIS B 95 1 11
HELIX 34 34 PHE B 96 ASN B 104 1 9
HELIX 35 35 ILE B 105A TYR B 122 1 18
HELIX 36 36 SER B 138 ASN B 144 1 7
HELIX 37 37 ASP B 173 LEU B 182 1 10
HELIX 38 38 ASN B 195 HIS B 207 1 13
HELIX 39 39 LEU B 230 GLY B 235 1 6
HELIX 40 40 THR B 237 ARG B 245 1 9
HELIX 41 41 THR B 265 GLN B 270 1 6
HELIX 42 42 PRO B 280 GLN B 284 5 5
HELIX 43 43 VAL B 291 LEU B 294 5 4
HELIX 44 44 VAL B 295 HIS B 320 1 26
HELIX 45 45 GLY B 324 ASP B 347 1 24
HELIX 46 46 ASP B 347 GLY B 354 1 8
HELIX 47 47 ASP B 362 PHE B 367 5 6
HELIX 48 48 ALA B 378 TYR B 385 1 8
HELIX 49 49 HIS B 386 LEU B 391 5 6
HELIX 50 50 SER B 403 LEU B 408 1 6
HELIX 51 51 ASN B 411 GLN B 429 1 19
HELIX 52 52 PRO B 441 ALA B 443 5 3
HELIX 53 53 VAL B 444 MET B 458 1 15
HELIX 54 54 SER B 462 PHE B 470 1 9
HELIX 55 55 SER B 477 GLY B 483 1 7
HELIX 56 56 LYS B 485 SER B 496 1 12
HELIX 57 57 ASP B 497 MET B 501 5 5
HELIX 58 58 GLU B 502 GLU B 510 1 9
HELIX 59 59 GLY B 519 GLY B 536 1 18
HELIX 60 60 ASN B 537 SER B 541 5 5
HELIX 61 61 LYS B 546 GLY B 551 5 6
HELIX 62 62 GLY B 552 THR B 561 1 10
HELIX 63 63 SER B 563 VAL B 572 1 10
SHEET 1 A 2 GLU A 46 SER A 49 0
SHEET 2 A 2 TYR A 55 ASP A 58 -1 O ASP A 58 N GLU A 46
SHEET 1 B 2 PHE A 64 TYR A 65 0
SHEET 2 B 2 THR A 71 PRO A 72 -1 O THR A 71 N TYR A 65
SHEET 1 C 2 TYR A 130 ASN A 131 0
SHEET 2 C 2 THR A 149 ARG A 150 -1 O ARG A 150 N TYR A 130
SHEET 1 D 2 GLN A 255 ILE A 257 0
SHEET 2 D 2 GLU A 260 TYR A 262 -1 O TYR A 262 N GLN A 255
SHEET 1 E 2 PHE A 395 ILE A 397 0
SHEET 2 E 2 GLN A 400 TYR A 402 -1 O TYR A 402 N PHE A 395
SHEET 1 F 2 GLU B 46 SER B 49 0
SHEET 2 F 2 TYR B 55 ASP B 58 -1 O ASP B 58 N GLU B 46
SHEET 1 G 2 PHE B 64 TYR B 65 0
SHEET 2 G 2 THR B 71 PRO B 72 -1 O THR B 71 N TYR B 65
SHEET 1 H 2 TYR B 130 ASN B 131 0
SHEET 2 H 2 THR B 149 ARG B 150 -1 O ARG B 150 N TYR B 130
SHEET 1 I 2 GLN B 255 ILE B 257 0
SHEET 2 I 2 GLU B 260 TYR B 262 -1 O TYR B 262 N GLN B 255
SHEET 1 J 2 PHE B 395 ILE B 397 0
SHEET 2 J 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.05
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.03
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.05
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.05
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.04
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.03
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 1.44
LINK ND2 ASN A 144 C1 NAG A 671 1555 1555 1.44
LINK ND2 ASN B 144 C1 NAG B 671 1555 1555 1.44
LINK ND2 ASN A 68 C1 NAG A 661 1555 1555 1.44
LINK ND2 ASN A 410 C1 NAG A 681 1555 1555 1.44
LINK ND2 ASN B 410 C1 NAG B 681 1555 1555 1.44
LINK O4 NAG B 661 C1 NAG B 662 1555 1555 1.44
LINK O4 NAG A 671 C1 NAG A 672 1555 1555 1.45
LINK O4 NAG B 671 C1 NAG B 672 1555 1555 1.45
LINK O4 NAG A 661 C1 NAG A 662 1555 1555 1.45
LINK O4 NAG A 672 C1 MAN A 673 1555 1555 1.46
LINK NE2AHIS B 388 CO COH B 615 1555 1555 2.27
LINK NE2AHIS A 388 CO COH A 614 1555 1555 2.27
CISPEP 1 SER A 126 PRO A 127 0 1.86
CISPEP 2 SER B 126 PRO B 127 0 1.00
SITE 1 AC1 20 VAL A 116 ARG A 120 PHE A 205 TYR A 348
SITE 2 AC1 20 VAL A 349 LEU A 352 SER A 353 TYR A 355
SITE 3 AC1 20 PHE A 381 TYR A 385 TRP A 387 PHE A 518
SITE 4 AC1 20 MET A 522 VAL A 523 GLY A 526 ALA A 527
SITE 5 AC1 20 SER A 530 LEU A 531 LEU A 534 HOH A1034
SITE 1 AC2 3 SER A 477 PHE A 478 GLU A 479
SITE 1 AC3 5 ARG A 240 LYS A 243 VAL A 271 GLU A 272
SITE 2 AC3 5 HOH A 846
SITE 1 AC4 10 HIS A 34 CYS A 36 CYS A 37 PRO A 154
SITE 2 AC4 10 VAL A 155 ALA A 156 CYS A 159 HOH A 676
SITE 3 AC4 10 HOH A 687 HOH A 968
SITE 1 AC5 17 ALA A 199 PHE A 200 ALA A 202 GLN A 203
SITE 2 AC5 17 HIS A 207 PHE A 210 LYS A 211 THR A 212
SITE 3 AC5 17 HIS A 214 VAL A 295 ASN A 382 TYR A 385
SITE 4 AC5 17 HIS A 386 HIS A 388 LEU A 391 HOH A 853
SITE 5 AC5 17 HOH A1090
SITE 1 AC6 5 TYR A 55 GLU A 67 ASN A 68 NAG A 662
SITE 2 AC6 5 HOH A 792
SITE 1 AC7 1 NAG A 661
SITE 1 AC8 9 GLU A 140 ASN A 144 TYR A 147 ARG A 216
SITE 2 AC8 9 PHE A 220 HOH A 666 NAG A 672 HOH A 994
SITE 3 AC8 9 HOH A 998
SITE 1 AC9 3 ARG A 216 NAG A 671 MAN A 673
SITE 1 BC1 4 NAG A 672 HOH A 930 HOH A1027 HOH A1065
SITE 1 BC2 6 GLN A 406 ASN A 410 SER A 412 ILE A 413
SITE 2 BC2 6 GLU A 416 HOH A 932
SITE 1 BC3 12 LYS A 180 ARG A 184 ARG A 185 ARG A 438
SITE 2 BC3 12 ILE A 442 GLU A 486 GLU A 490 GLU B 179
SITE 3 BC3 12 ARG B 184 ARG B 185 ILE B 442 GLN B 445
SITE 1 BC4 5 GLN A 543 ARG B 44 ARG B 61 HOH B 683
SITE 2 BC4 5 HOH B1141
SITE 1 BC5 15 VAL B 116 PHE B 205 PHE B 209 VAL B 349
SITE 2 BC5 15 TYR B 355 ILE B 377 PHE B 381 TYR B 385
SITE 3 BC5 15 VAL B 523 ALA B 527 SER B 530 LEU B 531
SITE 4 BC5 15 GLY B 533 LEU B 534 HOH B 630
SITE 1 BC6 4 SER B 477 PHE B 478 GLU B 479 LYS B 492
SITE 1 BC7 4 ASP B 239 ARG B 240 LYS B 243 GLU B 272
SITE 1 BC8 1 ASN B 87
SITE 1 BC9 9 HIS B 34 CYS B 36 CYS B 37 PRO B 154
SITE 2 BC9 9 ALA B 156 HOH B 762 HOH B 964 HOH B 995
SITE 3 BC9 9 HOH B1106
SITE 1 CC1 16 ALA B 199 PHE B 200 ALA B 202 GLN B 203
SITE 2 CC1 16 HIS B 207 PHE B 210 LYS B 211 THR B 212
SITE 3 CC1 16 VAL B 295 ASN B 382 TYR B 385 HIS B 386
SITE 4 CC1 16 HIS B 388 LEU B 391 GLN B 454 HOH B 743
SITE 1 CC2 5 TYR B 55 GLU B 67 ASN B 68 NAG B 662
SITE 2 CC2 5 HOH B 803
SITE 1 CC3 1 NAG B 661
SITE 1 CC4 8 GLU B 140 ASN B 144 TYR B 147 ARG B 216
SITE 2 CC4 8 HOH B 625 NAG B 672 HOH B 697 HOH B 922
SITE 1 CC5 4 ARG B 216 NAG B 671 HOH B 906 HOH B1020
SITE 1 CC6 5 GLN B 406 ASN B 410 ILE B 413 HOH B 676
SITE 2 CC6 5 HOH B1096
CRYST1 118.958 131.773 179.858 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 0.008406 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007589 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
