HEADER OXIDOREDUCTASE 26-AUG-10 3OLU
TITLE X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO THE
TITLE 2 CYCLOOXYGENASE CHANNEL OF R513H MURINE COX-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND 5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND 6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND 7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND 8 2;
COMPND 9 EC: 1.14.99.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS MONOTOPIC MEMBRANE PROTEIN, OXIDOREDUCTASE, N-GLYCOSYLATION, MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.VECCHIO,M.G.MALKOWSKI
REVDAT 4 29-JUN-11 3OLU 1 JRNL
REVDAT 3 15-JUN-11 3OLU 1 JRNL
REVDAT 2 20-APR-11 3OLU 1 JRNL
REVDAT 1 13-APR-11 3OLU 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. 2.35 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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : -6.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 56810
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3024
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 213
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 378
REMARK 3 SOLVENT ATOMS : 666
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : -0.90000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.588
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9577 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13010 ; 1.686 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1116 ; 5.593 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 443 ;36.572 ;23.973
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1500 ;15.022 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;14.231 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1384 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7330 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5534 ; 0.484 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8995 ; 0.947 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4043 ; 1.922 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4004 ; 3.154 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3614 37.6811 60.0257
REMARK 3 T TENSOR
REMARK 3 T11: .0862 T22: .2777
REMARK 3 T33: .1911 T12: .0357
REMARK 3 T13: .0424 T23: .0463
REMARK 3 L TENSOR
REMARK 3 L11: .7509 L22: 4.7279
REMARK 3 L33: 1.9305 L12: 1.2304
REMARK 3 L13: .2958 L23: .6976
REMARK 3 S TENSOR
REMARK 3 S11: -.0338 S12: -.2056 S13: .0818
REMARK 3 S21: .0117 S22: .0574 S23: .3388
REMARK 3 S31: -.1328 S32: -.2671 S33: -.0236
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 87
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1392 18.5827 64.2743
REMARK 3 T TENSOR
REMARK 3 T11: .3094 T22: .4607
REMARK 3 T33: .5978 T12: -.1152
REMARK 3 T13: .0446 T23: .1921
REMARK 3 L TENSOR
REMARK 3 L11: 8.5129 L22: 8.8648
REMARK 3 L33: 4.0646 L12: -1.5016
REMARK 3 L13: 4.3088 L23: -1.3940
REMARK 3 S TENSOR
REMARK 3 S11: .4999 S12: -.6573 S13: -1.5543
REMARK 3 S21: .2194 S22: .3481 S23: .2391
REMARK 3 S31: .8190 S32: -.6551 S33: -.8480
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5023 3.0380 66.2726
REMARK 3 T TENSOR
REMARK 3 T11: .1395 T22: .2519
REMARK 3 T33: .3979 T12: -.0761
REMARK 3 T13: .0174 T23: -.0001
REMARK 3 L TENSOR
REMARK 3 L11: 4.4499 L22: 7.0282
REMARK 3 L33: 9.6039 L12: -.7632
REMARK 3 L13: -2.4837 L23: .0533
REMARK 3 S TENSOR
REMARK 3 S11: -.3104 S12: .0661 S13: -.2207
REMARK 3 S21: .0010 S22: -.0914 S23: .6362
REMARK 3 S31: .3721 S32: -.4329 S33: .4018
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 148
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3721 33.7485 53.8737
REMARK 3 T TENSOR
REMARK 3 T11: .0199 T22: .0257
REMARK 3 T33: .0421 T12: .0087
REMARK 3 T13: .0051 T23: .0044
REMARK 3 L TENSOR
REMARK 3 L11: 2.5296 L22: 4.0309
REMARK 3 L33: 4.4712 L12: -.6903
REMARK 3 L13: 1.0571 L23: -1.0124
REMARK 3 S TENSOR
REMARK 3 S11: -.0856 S12: -.0853 S13: -.1437
REMARK 3 S21: -.0001 S22: .0546 S23: .1835
REMARK 3 S31: .1472 S32: -.1654 S33: .0310
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 149 A 233
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4715 29.8675 71.0404
REMARK 3 T TENSOR
REMARK 3 T11: .0659 T22: .0447
REMARK 3 T33: .0625 T12: .0001
REMARK 3 T13: -.0075 T23: -.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.5428 L22: 1.1306
REMARK 3 L33: 1.2993 L12: -.9024
REMARK 3 L13: -.0665 L23: -.0230
REMARK 3 S TENSOR
REMARK 3 S11: -.0566 S12: -.2152 S13: .1574
REMARK 3 S21: .1477 S22: .0875 S23: -.0865
REMARK 3 S31: -.1715 S32: .0050 S33: -.0309
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 268
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6000 18.9340 55.6582
REMARK 3 T TENSOR
REMARK 3 T11: .0091 T22: .0354
REMARK 3 T33: .1469 T12: -.0008
REMARK 3 T13: .0336 T23: -.0002
REMARK 3 L TENSOR
REMARK 3 L11: 3.2463 L22: .7350
REMARK 3 L33: 5.1889 L12: .1403
REMARK 3 L13: 1.0979 L23: -.2700
REMARK 3 S TENSOR
REMARK 3 S11: .0007 S12: .0147 S13: .2473
REMARK 3 S21: -.0579 S22: -.0060 S23: -.1701
REMARK 3 S31: -.0093 S32: .3084 S33: .0053
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 269 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4741 25.8712 65.9961
REMARK 3 T TENSOR
REMARK 3 T11: .0951 T22: .1726
REMARK 3 T33: .2843 T12: .0061
REMARK 3 T13: .0103 T23: -.0875
REMARK 3 L TENSOR
REMARK 3 L11: 5.9029 L22: 1.9913
REMARK 3 L33: 4.8805 L12: 1.0328
REMARK 3 L13: -.9476 L23: -2.7585
REMARK 3 S TENSOR
REMARK 3 S11: -.0349 S12: -.4222 S13: .7273
REMARK 3 S21: .0828 S22: -.1144 S23: -.2686
REMARK 3 S31: -.2369 S32: .3877 S33: .1493
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 302 A 344
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3820 9.3251 52.2909
REMARK 3 T TENSOR
REMARK 3 T11: .0879 T22: .0404
REMARK 3 T33: .1041 T12: .0458
REMARK 3 T13: .0163 T23: .0403
REMARK 3 L TENSOR
REMARK 3 L11: 1.0726 L22: 1.2402
REMARK 3 L33: 3.7371 L12: -.7634
REMARK 3 L13: .1344 L23: -.2964
REMARK 3 S TENSOR
REMARK 3 S11: .0523 S12: -.0332 S13: -.2003
REMARK 3 S21: -.2426 S22: -.1077 S23: -.0189
REMARK 3 S31: .2505 S32: .2746 S33: .0554
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 345 A 399
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1736 15.0791 65.3407
REMARK 3 T TENSOR
REMARK 3 T11: .0403 T22: .0661
REMARK 3 T33: .1018 T12: .0008
REMARK 3 T13: .0380 T23: .0406
REMARK 3 L TENSOR
REMARK 3 L11: .8467 L22: 1.1479
REMARK 3 L33: 2.2561 L12: -.5718
REMARK 3 L13: .1558 L23: -.4708
REMARK 3 S TENSOR
REMARK 3 S11: -.0346 S12: -.1533 S13: -.1180
REMARK 3 S21: .0595 S22: .0732 S23: .1644
REMARK 3 S31: .2160 S32: -.1295 S33: -.0386
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 400 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3081 16.2265 78.4138
REMARK 3 T TENSOR
REMARK 3 T11: .1255 T22: .2286
REMARK 3 T33: .0964 T12: .0442
REMARK 3 T13: -.0259 T23: .0036
REMARK 3 L TENSOR
REMARK 3 L11: 5.5646 L22: 5.6060
REMARK 3 L33: 3.1686 L12: 2.0761
REMARK 3 L13: .2477 L23: 2.3191
REMARK 3 S TENSOR
REMARK 3 S11: -.0246 S12: -.4605 S13: .0587
REMARK 3 S21: .4013 S22: .0660 S23: -.1657
REMARK 3 S31: -.0360 S32: .4118 S33: -.0414
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 430 A 553
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5427 24.8996 72.7338
REMARK 3 T TENSOR
REMARK 3 T11: .0802 T22: .1285
REMARK 3 T33: .0705 T12: .0189
REMARK 3 T13: .0280 T23: .0362
REMARK 3 L TENSOR
REMARK 3 L11: .9894 L22: .9583
REMARK 3 L33: 1.0838 L12: -.6586
REMARK 3 L13: -.3815 L23: .3450
REMARK 3 S TENSOR
REMARK 3 S11: -.0668 S12: -.2483 S13: -.0645
REMARK 3 S21: .1173 S22: .0956 S23: .1097
REMARK 3 S31: -.0113 S32: -.1357 S33: -.0288
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 583
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9024 3.3220 64.0081
REMARK 3 T TENSOR
REMARK 3 T11: .1518 T22: .0286
REMARK 3 T33: .1407 T12: -.0434
REMARK 3 T13: .0013 T23: .0424
REMARK 3 L TENSOR
REMARK 3 L11: 2.1016 L22: 2.3949
REMARK 3 L33: 4.1812 L12: -1.5448
REMARK 3 L13: -.8540 L23: .1440
REMARK 3 S TENSOR
REMARK 3 S11: -.0147 S12: -.1321 S13: -.2621
REMARK 3 S21: .0511 S22: .1118 S23: .1568
REMARK 3 S31: .5691 S32: -.1922 S33: -.0971
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): 33.7671 1.6954 33.1921
REMARK 3 T TENSOR
REMARK 3 T11: .4075 T22: .1384
REMARK 3 T33: .1827 T12: .0604
REMARK 3 T13: -.0447 T23: -.0372
REMARK 3 L TENSOR
REMARK 3 L11: 4.5350 L22: .8695
REMARK 3 L33: 2.5786 L12: .5646
REMARK 3 L13: -1.4207 L23: -.5141
REMARK 3 S TENSOR
REMARK 3 S11: .1678 S12: .0540 S13: -.2489
REMARK 3 S21: -.2633 S22: -.1716 S23: .0210
REMARK 3 S31: .5233 S32: .1958 S33: .0038
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): 15.1809 -.4239 28.2809
REMARK 3 T TENSOR
REMARK 3 T11: .6101 T22: .3955
REMARK 3 T33: .5815 T12: -.1258
REMARK 3 T13: -.1173 T23: -.0877
REMARK 3 L TENSOR
REMARK 3 L11: 10.6495 L22: 5.3282
REMARK 3 L33: 2.6176 L12: -4.6137
REMARK 3 L13: 2.3030 L23: -3.5627
REMARK 3 S TENSOR
REMARK 3 S11: .2427 S12: -.1198 S13: -.4975
REMARK 3 S21: -.3853 S22: .4513 S23: 1.1576
REMARK 3 S31: .3170 S32: -.5582 S33: -.6940
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): 1.1326 18.5317 26.2892
REMARK 3 T TENSOR
REMARK 3 T11: .3041 T22: .2559
REMARK 3 T33: .4039 T12: -.1373
REMARK 3 T13: -.0402 T23: -.0949
REMARK 3 L TENSOR
REMARK 3 L11: 5.5950 L22: 5.2728
REMARK 3 L33: 9.1195 L12: -1.8336
REMARK 3 L13: -1.5144 L23: 1.6220
REMARK 3 S TENSOR
REMARK 3 S11: -.1152 S12: .3482 S13: -.6173
REMARK 3 S21: -.2314 S22: -.2444 S23: .4550
REMARK 3 S31: .3708 S32: -.3834 S33: .3596
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 151
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8407 19.2922 38.9279
REMARK 3 T TENSOR
REMARK 3 T11: .0785 T22: .0253
REMARK 3 T33: .0221 T12: .0217
REMARK 3 T13: -.0005 T23: -.0032
REMARK 3 L TENSOR
REMARK 3 L11: 3.2020 L22: 2.9709
REMARK 3 L33: 4.9912 L12: -1.9742
REMARK 3 L13: .6198 L23: -.2735
REMARK 3 S TENSOR
REMARK 3 S11: .1286 S12: .0755 S13: -.1094
REMARK 3 S21: -.1765 S22: -.1737 S23: .0703
REMARK 3 S31: .3126 S32: -.1522 S33: .0451
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 152 B 230
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9940 27.5285 21.8430
REMARK 3 T TENSOR
REMARK 3 T11: .0899 T22: .1040
REMARK 3 T33: .0793 T12: .0274
REMARK 3 T13: .0128 T23: .0244
REMARK 3 L TENSOR
REMARK 3 L11: 1.0999 L22: 1.3317
REMARK 3 L33: 1.7714 L12: -.9542
REMARK 3 L13: -.0769 L23: .0832
REMARK 3 S TENSOR
REMARK 3 S11: .1159 S12: .1712 S13: .0567
REMARK 3 S21: -.1999 S22: -.0758 S23: -.1256
REMARK 3 S31: .1047 S32: .2116 S33: -.0401
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 231 B 268
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5601 51.4507 38.5446
REMARK 3 T TENSOR
REMARK 3 T11: .0674 T22: .0376
REMARK 3 T33: .1146 T12: -.0204
REMARK 3 T13: .0074 T23: .0482
REMARK 3 L TENSOR
REMARK 3 L11: 2.3375 L22: 3.7454
REMARK 3 L33: 3.5589 L12: -.2740
REMARK 3 L13: 1.0351 L23: -.5012
REMARK 3 S TENSOR
REMARK 3 S11: -.0361 S12: .1996 S13: .3299
REMARK 3 S21: .2852 S22: -.0596 S23: -.2143
REMARK 3 S31: -.3951 S32: .2799 S33: .0958
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2076 50.0868 28.8326
REMARK 3 T TENSOR
REMARK 3 T11: .2884 T22: .2745
REMARK 3 T33: .2820 T12: -.2124
REMARK 3 T13: .1635 T23: -.0427
REMARK 3 L TENSOR
REMARK 3 L11: 5.0448 L22: 3.2059
REMARK 3 L33: 1.5565 L12: 1.7365
REMARK 3 L13: 1.1096 L23: -.4222
REMARK 3 S TENSOR
REMARK 3 S11: -.1044 S12: .2237 S13: .3457
REMARK 3 S21: -.4530 S22: .0677 S23: -.4496
REMARK 3 S31: -.3626 S32: .5490 S33: .0367
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 309 B 389
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1410 34.0334 36.3893
REMARK 3 T TENSOR
REMARK 3 T11: .0134 T22: .0508
REMARK 3 T33: .0805 T12: -.0042
REMARK 3 T13: -.0107 T23: .0241
REMARK 3 L TENSOR
REMARK 3 L11: .9869 L22: 1.7295
REMARK 3 L33: 1.9375 L12: -.4252
REMARK 3 L13: .0566 L23: .3998
REMARK 3 S TENSOR
REMARK 3 S11: .0515 S12: .1229 S13: -.0567
REMARK 3 S21: -.0938 S22: -.0421 S23: .2341
REMARK 3 S31: .0936 S32: -.2025 S33: -.0094
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 390 B 430
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5702 48.4233 14.6656
REMARK 3 T TENSOR
REMARK 3 T11: .1756 T22: .2979
REMARK 3 T33: .1648 T12: .0712
REMARK 3 T13: .0449 T23: .1353
REMARK 3 L TENSOR
REMARK 3 L11: 1.4054 L22: 6.7062
REMARK 3 L33: 2.6850 L12: .2779
REMARK 3 L13: -1.0794 L23: .6193
REMARK 3 S TENSOR
REMARK 3 S11: .2080 S12: .4234 S13: .3809
REMARK 3 S21: -.5078 S22: -.0699 S23: -.2502
REMARK 3 S31: -.2758 S32: .0680 S33: -.1381
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 431 B 457
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7593 29.8030 13.6802
REMARK 3 T TENSOR
REMARK 3 T11: .2057 T22: .2171
REMARK 3 T33: .0505 T12: .1109
REMARK 3 T13: .0192 T23: -.0022
REMARK 3 L TENSOR
REMARK 3 L11: 2.3548 L22: 1.4357
REMARK 3 L33: 1.2734 L12: -.8588
REMARK 3 L13: 1.1587 L23: -1.2760
REMARK 3 S TENSOR
REMARK 3 S11: .0987 S12: .1876 S13: .0762
REMARK 3 S21: -.1773 S22: -.1354 S23: -.0391
REMARK 3 S31: .1451 S32: .2109 S33: .0367
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 458 B 534
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3925 16.5373 16.8850
REMARK 3 T TENSOR
REMARK 3 T11: .2530 T22: .1277
REMARK 3 T33: .0916 T12: .0490
REMARK 3 T13: -.0403 T23: -.0420
REMARK 3 L TENSOR
REMARK 3 L11: 1.8198 L22: 2.2117
REMARK 3 L33: 3.0570 L12: -.6704
REMARK 3 L13: .2042 L23: -.0586
REMARK 3 S TENSOR
REMARK 3 S11: .1255 S12: .2739 S13: -.2188
REMARK 3 S21: -.3241 S22: -.1260 S23: .1387
REMARK 3 S31: .3377 S32: -.0552 S33: .0005
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 535 B 583
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6738 38.1478 35.8958
REMARK 3 T TENSOR
REMARK 3 T11: .0106 T22: .0550
REMARK 3 T33: .1035 T12: .0025
REMARK 3 T13: -.0004 T23: .0294
REMARK 3 L TENSOR
REMARK 3 L11: 1.2300 L22: 1.6681
REMARK 3 L33: 3.5260 L12: .0023
REMARK 3 L13: .0947 L23: -1.1794
REMARK 3 S TENSOR
REMARK 3 S11: .0753 S12: .1345 S13: -.0480
REMARK 3 S21: -.0589 S22: .0796 S23: .2236
REMARK 3 S31: .0874 S32: -.3002 S33: -.1548
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 3OLU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB061278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9780
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59835
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.57600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM
REMARK 280 HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.65600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.87700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.01100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.65600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.87700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.01100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.65600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.87700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.01100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.65600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.87700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.01100
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: 14160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 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 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 ASN 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 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 ASN 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 LYS A 79 CD CE NZ
REMARK 470 LYS A 83 CE NZ
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 473 CD CE NZ
REMARK 470 LYS A 485 CD CE NZ
REMARK 470 LYS A 557 NZ
REMARK 470 GLN B 54 CG CD OE1 NE2
REMARK 470 LEU B 75 CG 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 CD1 CD2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 97 CE NZ
REMARK 470 LYS B 169 CD CE NZ
REMARK 470 GLU B 170 CD OE1 OE2
REMARK 470 LYS B 175 NZ
REMARK 470 GLU B 186 CD OE1 OE2
REMARK 470 LYS B 215 CG CD CE NZ
REMARK 470 LYS B 267 CG CD CE NZ
REMARK 470 GLU B 272 OE1 OE2
REMARK 470 GLU B 281 CG CD OE1 OE2
REMARK 470 LYS B 358 CE NZ
REMARK 470 LYS B 405 CD CE NZ
REMARK 470 LYS B 492 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. = 15.7 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 LYS A 83 120.52 -37.40
REMARK 500 TYR A 122 -8.56 -53.22
REMARK 500 THR A 129 -94.17 -121.59
REMARK 500 TRP A 387 40.16 -95.10
REMARK 500 GLU A 398 -114.02 60.30
REMARK 500 TYR A 409 13.38 59.58
REMARK 500 ASN A 410 79.81 -100.22
REMARK 500 ASN A 439 15.36 -142.52
REMARK 500 SER A 471 32.32 70.84
REMARK 500 SER A 496 -50.86 68.72
REMARK 500 CYS A 575 66.03 39.73
REMARK 500 ARG B 61 11.39 59.89
REMARK 500 THR B 129 -91.08 -122.84
REMARK 500 ARG B 185 -98.41 -89.61
REMARK 500 ASP B 249 16.94 57.37
REMARK 500 TRP B 387 45.74 -87.30
REMARK 500 GLU B 398 -123.45 60.60
REMARK 500 TYR B 409 10.86 57.81
REMARK 500 SER B 496 -45.26 67.78
REMARK 500 SER B 579 -174.89 -174.85
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 750 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH A 916 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH B 917 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH B 935 DISTANCE = 5.88 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 86.8
REMARK 620 3 COH B 619 NB 91.0 90.5
REMARK 620 4 COH B 619 NC 98.4 174.1 86.7
REMARK 620 5 COH B 619 ND 91.3 92.0 176.7 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 COH A 620 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 COH A 620 NA 96.1
REMARK 620 3 COH A 620 NB 98.4 83.6
REMARK 620 4 COH A 620 NC 92.2 169.7 89.2
REMARK 620 5 COH A 620 ND 84.4 94.8 176.9 91.9
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 EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
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: 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: 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: 3OLT RELATED DB: PDB
DBREF 3OLU A 35 618 UNP Q05769 PGH2_MOUSE 20 604
DBREF 3OLU B 35 618 UNP Q05769 PGH2_MOUSE 20 604
SEQADV 3OLU ALA A 28 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 29 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 30 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 31 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 32 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 33 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 34 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS A 513 UNP Q05769 ARG 499 ENGINEERED MUTATION
SEQADV 3OLU ALA B 28 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 29 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 30 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 31 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 32 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 33 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 34 UNP Q05769 EXPRESSION TAG
SEQADV 3OLU HIS B 513 UNP Q05769 ARG 499 ENGINEERED MUTATION
SEQRES 1 A 592 ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES 2 A 592 CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES 3 A 592 GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES 4 A 592 GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES 5 A 592 LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES 6 A 592 LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES 7 A 592 ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES 8 A 592 THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES 9 A 592 ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES 10 A 592 ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES 11 A 592 ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES 12 A 592 GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES 13 A 592 LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES 14 A 592 MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES 15 A 592 PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES 16 A 592 ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES 17 A 592 GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES 18 A 592 LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES 19 A 592 VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES 20 A 592 ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES 21 A 592 VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES 22 A 592 MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES 23 A 592 CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES 24 A 592 GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES 25 A 592 GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES 26 A 592 LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES 27 A 592 LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES 28 A 592 ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES 29 A 592 LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES 30 A 592 PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES 31 A 592 HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES 32 A 592 ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES 33 A 592 ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES 34 A 592 ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES 35 A 592 ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES 36 A 592 THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES 37 A 592 TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES 38 A 592 LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU
SEQRES 39 A 592 THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES 40 A 592 LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES 41 A 592 PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES 42 A 592 ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES 43 A 592 LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES 44 A 592 GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER
SEQRES 45 A 592 HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES 46 A 592 LYS ARG ARG SER THR GLU LEU
SEQRES 1 B 592 ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO
SEQRES 2 B 592 CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP
SEQRES 3 B 592 GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY
SEQRES 4 B 592 GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS
SEQRES 5 B 592 LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE
SEQRES 6 B 592 LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN
SEQRES 7 B 592 ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU
SEQRES 8 B 592 THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR
SEQRES 9 B 592 ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER
SEQRES 10 B 592 ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA
SEQRES 11 B 592 ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS
SEQRES 12 B 592 GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU
SEQRES 13 B 592 LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN
SEQRES 14 B 592 MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES 15 B 592 PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR
SEQRES 16 B 592 ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR
SEQRES 17 B 592 GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE
SEQRES 18 B 592 LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU
SEQRES 19 B 592 VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET
SEQRES 20 B 592 ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA
SEQRES 21 B 592 VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET
SEQRES 22 B 592 MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES 23 B 592 CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP
SEQRES 24 B 592 GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY
SEQRES 25 B 592 GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS
SEQRES 26 B 592 LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU
SEQRES 27 B 592 LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE
SEQRES 28 B 592 ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU
SEQRES 29 B 592 LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER
SEQRES 30 B 592 PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU
SEQRES 31 B 592 HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN
SEQRES 32 B 592 ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE
SEQRES 33 B 592 ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER
SEQRES 34 B 592 ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS
SEQRES 35 B 592 ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU
SEQRES 36 B 592 THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU
SEQRES 37 B 592 TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU
SEQRES 38 B 592 LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU
SEQRES 39 B 592 THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY
SEQRES 40 B 592 LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS
SEQRES 41 B 592 PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE
SEQRES 42 B 592 ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL
SEQRES 43 B 592 LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO
SEQRES 44 B 592 GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER
SEQRES 45 B 592 HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE
SEQRES 46 B 592 LYS ARG ARG SER THR GLU LEU
MODRES 3OLU ASN A 144 ASN GLYCOSYLATION SITE
MODRES 3OLU ASN A 410 ASN GLYCOSYLATION SITE
MODRES 3OLU ASN B 68 ASN GLYCOSYLATION SITE
MODRES 3OLU ASN B 410 ASN GLYCOSYLATION SITE
MODRES 3OLU ASN A 68 ASN GLYCOSYLATION SITE
MODRES 3OLU ASN B 144 ASN GLYCOSYLATION SITE
HET EDO A 1 4
HET EDO A 4 4
HET EDO A 5 4
HET EDO A 12 4
HET EDO A 13 4
HET EDO A 14 4
HET EDO A 15 4
HET 1AG A 619 27
HET COH A 620 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 B 2 4
HET EDO B 3 4
HET EDO B 6 4
HET EDO B 7 4
HET EDO B 8 4
HET EDO B 9 4
HET EDO B 11 4
HET 1AG B 1 27
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 MAN B 673 11
HET NAG B 681 14
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,
HETNAM 2 1AG 14-TETRAENOATE
HETNAM COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BOG B-OCTYLGLUCOSIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 14(C2 H6 O2)
FORMUL 10 1AG 2(C23 H38 O4)
FORMUL 11 COH 2(C34 H32 CO N4 O4)
FORMUL 12 NAG 10(C8 H15 N O6)
FORMUL 13 MAN 2(C6 H12 O6)
FORMUL 15 BOG C14 H28 O6
FORMUL 28 HOH *666(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 ARG A 120 1 16
HELIX 5 5 SER A 138 ASN A 144 1 7
HELIX 6 6 ASP A 173 LEU A 182 1 10
HELIX 7 7 ASN A 195 HIS A 207 1 13
HELIX 8 8 LEU A 230 GLY A 235 1 6
HELIX 9 9 THR A 237 ARG A 245 1 9
HELIX 10 10 THR A 265 GLN A 270 1 6
HELIX 11 11 PRO A 280 GLN A 284 5 5
HELIX 12 12 VAL A 291 LEU A 294 5 4
HELIX 13 13 VAL A 295 HIS A 320 1 26
HELIX 14 14 GLY A 324 ASP A 347 1 24
HELIX 15 15 ASP A 347 GLY A 354 1 8
HELIX 16 16 ASP A 362 PHE A 367 5 6
HELIX 17 17 ALA A 378 TYR A 385 1 8
HELIX 18 18 HIS A 386 LEU A 391 5 6
HELIX 19 19 SER A 403 LEU A 408 1 6
HELIX 20 20 ASN A 410 GLN A 429 1 20
HELIX 21 21 PRO A 441 ALA A 443 5 3
HELIX 22 22 VAL A 444 MET A 458 1 15
HELIX 23 23 SER A 462 PHE A 470 1 9
HELIX 24 24 SER A 477 GLY A 483 1 7
HELIX 25 25 LYS A 485 SER A 496 1 12
HELIX 26 26 ASP A 497 MET A 501 5 5
HELIX 27 27 GLU A 502 GLU A 510 1 9
HELIX 28 28 GLY A 519 GLY A 536 1 18
HELIX 29 29 ASN A 537 SER A 541 5 5
HELIX 30 30 LYS A 546 GLY A 551 5 6
HELIX 31 31 GLY A 552 THR A 561 1 10
HELIX 32 32 SER A 563 VAL A 572 1 10
HELIX 33 33 GLU B 73 LYS B 83 1 11
HELIX 34 34 THR B 85 THR B 94 1 10
HELIX 35 35 PHE B 96 ASN B 104 1 9
HELIX 36 36 ILE B 105A TYR B 122 1 18
HELIX 37 37 SER B 138 ASN B 144 1 7
HELIX 38 38 ASP B 173 LEU B 182 1 10
HELIX 39 39 ASN B 195 HIS B 207 1 13
HELIX 40 40 LEU B 230 GLY B 235 1 6
HELIX 41 41 THR B 237 ARG B 245 1 9
HELIX 42 42 THR B 265 GLN B 270 1 6
HELIX 43 43 PRO B 280 GLN B 284 5 5
HELIX 44 44 VAL B 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 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 GLN A 400 N ILE A 397
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 THR B 212 ASP B 213 0
SHEET 2 G 2 GLY B 217 THR B 221 -1 O GLY B 217 N ASP B 213
SHEET 1 H 2 GLN B 255 ILE B 257 0
SHEET 2 H 2 GLU B 260 TYR B 262 -1 O GLU B 260 N ILE B 257
SHEET 1 I 2 PHE B 395 ILE B 397 0
SHEET 2 I 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.07
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.05
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.03
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.06
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.05
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.07
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.04
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.04
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.06
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.07
LINK ND2 ASN A 144 C1 NAG A 671 1555 1555 1.36
LINK ND2 ASN A 410 C1 NAG A 681 1555 1555 1.36
LINK ND2 ASN B 68 C1 NAG B 661 1555 1555 1.37
LINK ND2 ASN B 410 C1 NAG B 681 1555 1555 1.37
LINK ND2 ASN A 68 C1 NAG A 661 1555 1555 1.39
LINK O4 NAG B 671 C1 NAG B 672 1555 1555 1.43
LINK ND2 ASN B 144 C1 NAG B 671 1555 1555 1.44
LINK O4 NAG A 661 C1 NAG A 662 1555 1555 1.45
LINK O4 NAG A 671 C1 NAG A 672 1555 1555 1.45
LINK O4 NAG B 672 C1 MAN B 673 1555 1555 1.46
LINK O4 NAG A 672 C1 MAN A 673 1555 1555 1.47
LINK O4 NAG B 661 C1 NAG B 662 1555 1555 1.47
LINK NE2AHIS B 388 CO COH B 619 1555 1555 2.17
LINK NE2 HIS A 388 CO COH A 620 1555 1555 2.46
LINK ND2 ASN A 68 O5 NAG A 661 1555 1555 1.43
LINK ND2 ASN B 68 O5 NAG B 661 1555 1555 1.49
LINK ND2 ASN A 410 O5 NAG A 681 1555 1555 1.50
LINK ND2 ASN B 410 O5 NAG B 681 1555 1555 1.49
LINK ND2 ASN A 144 O5 NAG A 671 1555 1555 1.53
CISPEP 1 SER A 126 PRO A 127 0 -0.86
CISPEP 2 SER B 126 PRO B 127 0 -1.91
SITE 1 AC1 3 ASP A 157 CYS A 159 LYS A 459
SITE 1 AC2 6 PRO A 162 SER A 455 ARG A 456 LYS A 459
SITE 2 AC2 6 TYR A 460 HOH A 768
SITE 1 AC3 2 HOH A 905 MAN B 673
SITE 1 AC4 7 GLU A 308 ARG A 311 GLU A 339 SER A 566
SITE 2 AC4 7 LEU A 567 ASN A 570 HOH A 645
SITE 1 AC5 5 LYS A 251 TYR A 254 ASN A 310 HOH A 831
SITE 2 AC5 5 HOH A 858
SITE 1 AC6 4 ASP A 239 ARG A 240 LYS A 243 GLU A 272
SITE 1 AC7 10 HIS A 90 GLN A 192 LEU A 352 SER A 353
SITE 2 AC7 10 HIS A 513 ALA A 516 ILE A 517 PHE A 518
SITE 3 AC7 10 VAL A 523 HOH A 844
SITE 1 AC8 18 ARG A 120 PHE A 205 PHE A 209 TYR A 348
SITE 2 AC8 18 VAL A 349 SER A 353 TYR A 355 ILE A 377
SITE 3 AC8 18 PHE A 381 TYR A 385 TRP A 387 MET A 522
SITE 4 AC8 18 GLY A 526 ALA A 527 SER A 530 LEU A 531
SITE 5 AC8 18 GLY A 533 LEU A 534
SITE 1 AC9 15 ALA A 199 GLN A 203 HIS A 207 PHE A 210
SITE 2 AC9 15 LYS A 211 THR A 212 VAL A 295 ASN A 382
SITE 3 AC9 15 TYR A 385 HIS A 386 HIS A 388 LEU A 391
SITE 4 AC9 15 VAL A 447 HOH A 724 HOH A 909
SITE 1 BC1 5 TYR A 55 GLU A 67 ASN A 68 NAG A 662
SITE 2 BC1 5 HOH A 811
SITE 1 BC2 2 NAG A 661 HOH A 667
SITE 1 BC3 10 HOH A 27 GLU A 140 ASN A 144 TYR A 147
SITE 2 BC3 10 ARG A 216 PHE A 220 HOH A 639 HOH A 670
SITE 3 BC3 10 NAG A 672 LEU B 238
SITE 1 BC4 3 ARG A 216 NAG A 671 MAN A 673
SITE 1 BC5 1 NAG A 672
SITE 1 BC6 7 GLN A 406 ASN A 410 SER A 412 ILE A 413
SITE 2 BC6 7 GLU A 416 HOH A 813 HOH A 878
SITE 1 BC7 12 GLU A 179 LYS A 180 ARG A 184 ARG A 185
SITE 2 BC7 12 ARG A 438 GLU A 486 GLU A 490 GLU B 179
SITE 3 BC7 12 ARG B 184 ARG B 185 ILE B 442 GLN B 445
SITE 1 BC8 8 HIS B 90 GLN B 192 LEU B 352 SER B 353
SITE 2 BC8 8 ALA B 516 ILE B 517 PHE B 518 HOH B 659
SITE 1 BC9 6 LYS B 251 TYR B 254 VAL B 261 ASN B 310
SITE 2 BC9 6 HOH B 760 HOH B 862
SITE 1 CC1 5 PRO B 162 ARG B 456 LYS B 459 TYR B 460
SITE 2 CC1 5 HOH B 649
SITE 1 CC2 7 PRO A 547 SER A 548 GLU A 553 MET B 48
SITE 2 CC2 7 LYS B 56 ASP B 58 HOH B 838
SITE 1 CC3 7 GLU B 308 ARG B 311 GLU B 339 SER B 566
SITE 2 CC3 7 LEU B 567 ASN B 570 HOH B 677
SITE 1 CC4 3 LEU A 145 SER B 143 HOH B 652
SITE 1 CC5 5 ASP B 239 ARG B 240 LYS B 243 VAL B 271
SITE 2 CC5 5 GLU B 272
SITE 1 CC6 16 ARG B 120 PHE B 205 PHE B 209 VAL B 349
SITE 2 CC6 16 TYR B 355 ASN B 375 ILE B 377 PHE B 381
SITE 3 CC6 16 TYR B 385 GLY B 526 ALA B 527 SER B 530
SITE 4 CC6 16 LEU B 531 GLY B 533 LEU B 534 HOH B 789
SITE 1 CC7 14 ALA B 199 PHE B 200 GLN B 203 HIS B 207
SITE 2 CC7 14 PHE B 210 LYS B 211 THR B 212 HIS B 214
SITE 3 CC7 14 VAL B 295 ASN B 382 TYR B 385 HIS B 386
SITE 4 CC7 14 HIS B 388 LEU B 391
SITE 1 CC8 5 TYR B 55 GLU B 67 ASN B 68 NAG B 662
SITE 2 CC8 5 HOH B 730
SITE 1 CC9 3 NAG B 661 HOH B 732 HOH B 922
SITE 1 DC1 9 GLU B 140 ASN B 144 TYR B 147 ARG B 216
SITE 2 DC1 9 PHE B 220 HOH B 627 NAG B 672 HOH B 701
SITE 3 DC1 9 HOH B 703
SITE 1 DC2 5 HOH A 679 ARG B 216 NAG B 671 MAN B 673
SITE 2 DC2 5 HOH B 674
SITE 1 DC3 7 EDO A 5 HOH A 905 HOH B 644 HOH B 651
SITE 2 DC3 7 HOH B 657 NAG B 672 HOH B 674
SITE 1 DC4 5 ASN B 410 SER B 412 ILE B 413 GLU B 416
SITE 2 DC4 5 HOH B 914
CRYST1 121.312 131.754 180.022 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 0.008243 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
