HEADER OXIDOREDUCTASE/INHIBITOR 09-NOV-17 6BL3
TITLE CRYSTAL COMPLEX OF CYCLOOXYGENASE-2 WITH INDOMETHACIN-BUTYLDIAMINE-
TITLE 2 DANSYL CONJUGATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYCLOOXYGENASE-2,COX-2,GLUCOCORTICOID-REGULATED INFLAMMATORY
COMPND 5 CYCLOOXYGENASE,GRIPGHS,MACROPHAGE ACTIVATION-ASSOCIATED MARKER
COMPND 6 PROTEIN P71/73,PES-2,PHS II,PROSTAGLANDIN H2 SYNTHASE 2,PGHS-2,
COMPND 7 PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2,TIS10 PROTEIN;
COMPND 8 EC: 1.14.99.1;
COMPND 9 ENGINEERED: 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
KEYWDS CYCLOOXYGENASE-2, FLUORESCENT INHIBITOR COMPLEX, OXIDOREDUCTASE-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XU,M.J.UDDIN,S.BANERJEE,L.J.MARNETT
REVDAT 6 04-OCT-23 6BL3 1 HETSYN
REVDAT 5 29-JUL-20 6BL3 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 12-JUN-19 6BL3 1 JRNL
REVDAT 3 15-MAY-19 6BL3 1 JRNL
REVDAT 2 13-MAR-19 6BL3 1 REMARK
REVDAT 1 14-NOV-18 6BL3 0
JRNL AUTH S.XU,M.J.UDDIN,S.BANERJEE,K.DUGGAN,J.MUSEE,J.R.KIEFER,
JRNL AUTH 2 K.GHEBRESELASIE,C.A.ROUZER,L.J.MARNETT
JRNL TITL FLUORESCENT INDOMETHACIN-DANSYL CONJUGATES UTILIZE THE
JRNL TITL 2 MEMBRANE-BINDING DOMAIN OF CYCLOOXYGENASE-2 TO BLOCK THE
JRNL TITL 3 OPENING TO THE ACTIVE SITE.
JRNL REF J.BIOL.CHEM. V. 294 8690 2019
JRNL REFN ESSN 1083-351X
JRNL PMID 31000626
JRNL DOI 10.1074/JBC.RA119.007405
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 112.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 140568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4220
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1112.5812 - 6.8877 0.97 4639 141 0.1962 0.2042
REMARK 3 2 6.8877 - 5.4670 0.98 4598 135 0.2005 0.2443
REMARK 3 3 5.4670 - 4.7759 0.98 4576 136 0.1645 0.1626
REMARK 3 4 4.7759 - 4.3392 0.98 4579 150 0.1555 0.1433
REMARK 3 5 4.3392 - 4.0282 0.98 4559 141 0.1636 0.1835
REMARK 3 6 4.0282 - 3.7907 0.98 4561 145 0.1725 0.1845
REMARK 3 7 3.7907 - 3.6009 0.99 4608 143 0.1759 0.2027
REMARK 3 8 3.6009 - 3.4441 0.99 4572 138 0.1855 0.2143
REMARK 3 9 3.4441 - 3.3115 0.99 4582 147 0.2042 0.2377
REMARK 3 10 3.3115 - 3.1972 0.99 4593 138 0.2215 0.2683
REMARK 3 11 3.1972 - 3.0972 0.98 4548 137 0.2197 0.2823
REMARK 3 12 3.0972 - 3.0087 0.98 4557 145 0.2251 0.2599
REMARK 3 13 3.0087 - 2.9295 0.99 4584 143 0.2267 0.2720
REMARK 3 14 2.9295 - 2.8580 0.99 4605 142 0.2309 0.2852
REMARK 3 15 2.8580 - 2.7930 0.99 4604 139 0.2311 0.2779
REMARK 3 16 2.7930 - 2.7336 0.99 4632 142 0.2355 0.2812
REMARK 3 17 2.7336 - 2.6789 0.99 4581 142 0.2342 0.2715
REMARK 3 18 2.6789 - 2.6283 0.99 4561 143 0.2328 0.2438
REMARK 3 19 2.6283 - 2.5814 0.99 4593 144 0.2285 0.2501
REMARK 3 20 2.5814 - 2.5376 0.98 4558 146 0.2299 0.2589
REMARK 3 21 2.5376 - 2.4967 0.99 4540 142 0.2302 0.2423
REMARK 3 22 2.4967 - 2.4583 0.99 4608 135 0.2373 0.2773
REMARK 3 23 2.4583 - 2.4221 0.99 4584 143 0.2488 0.2678
REMARK 3 24 2.4221 - 2.3880 0.99 4574 141 0.2537 0.3097
REMARK 3 25 2.3880 - 2.3557 0.99 4600 152 0.2623 0.3096
REMARK 3 26 2.3557 - 2.3251 0.99 4561 129 0.2727 0.3230
REMARK 3 27 2.3251 - 2.2961 0.98 4544 144 0.2785 0.3105
REMARK 3 28 2.2961 - 2.2684 0.98 4531 150 0.2892 0.3148
REMARK 3 29 2.2684 - 2.2420 0.95 4394 132 0.3163 0.3296
REMARK 3 30 2.2420 - 2.2168 0.80 3722 115 0.3378 0.4039
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 19164
REMARK 3 ANGLE : 0.783 26089
REMARK 3 CHIRALITY : 0.049 2753
REMARK 3 PLANARITY : 0.005 3320
REMARK 3 DIHEDRAL : 17.142 11315
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 105A)
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7338 -5.0806 23.5472
REMARK 3 T TENSOR
REMARK 3 T11: 0.5002 T22: 0.3119
REMARK 3 T33: 0.5164 T12: 0.0124
REMARK 3 T13: -0.0995 T23: -0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 0.5874 L22: 0.9889
REMARK 3 L33: 1.8385 L12: 0.0700
REMARK 3 L13: 0.6582 L23: -0.3617
REMARK 3 S TENSOR
REMARK 3 S11: -0.1824 S12: 0.0144 S13: 0.3206
REMARK 3 S21: 0.2548 S22: -0.0928 S23: 0.1385
REMARK 3 S31: -0.6470 S32: 0.0681 S33: 0.2906
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 106 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5776 -16.6114 21.3087
REMARK 3 T TENSOR
REMARK 3 T11: 0.3705 T22: 0.3878
REMARK 3 T33: 0.4035 T12: 0.0146
REMARK 3 T13: -0.0564 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 1.1909 L22: 0.5352
REMARK 3 L33: 2.6975 L12: 0.2414
REMARK 3 L13: -0.8527 L23: -0.5112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.0991 S13: 0.5910
REMARK 3 S21: 0.1750 S22: -0.0482 S23: 0.0681
REMARK 3 S31: -0.5596 S32: -0.0880 S33: 0.1063
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1665 -38.6890 20.1033
REMARK 3 T TENSOR
REMARK 3 T11: 0.2568 T22: 0.2674
REMARK 3 T33: 0.2026 T12: 0.0034
REMARK 3 T13: 0.0193 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.7742 L22: 0.8501
REMARK 3 L33: 0.6632 L12: 0.1396
REMARK 3 L13: 0.3705 L23: -0.0499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0260 S13: -0.0583
REMARK 3 S21: 0.0125 S22: -0.0459 S23: -0.1607
REMARK 3 S31: 0.0288 S32: 0.0948 S33: 0.0425
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 320 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1983 -30.0382 28.9457
REMARK 3 T TENSOR
REMARK 3 T11: 0.2751 T22: 0.2551
REMARK 3 T33: 0.2070 T12: -0.0046
REMARK 3 T13: -0.0105 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.0991 L22: 0.5882
REMARK 3 L33: 0.8222 L12: 0.0653
REMARK 3 L13: 0.2929 L23: -0.1425
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: -0.1743 S13: 0.0415
REMARK 3 S21: 0.1549 S22: -0.0229 S23: -0.0714
REMARK 3 S31: -0.0541 S32: 0.0369 S33: 0.0557
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 105A)
REMARK 3 ORIGIN FOR THE GROUP (A): -80.9755 -22.3051 14.7893
REMARK 3 T TENSOR
REMARK 3 T11: 0.4030 T22: 0.5624
REMARK 3 T33: 0.4270 T12: 0.0755
REMARK 3 T13: 0.0695 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.0271 L22: 1.0582
REMARK 3 L33: 1.2217 L12: -0.4405
REMARK 3 L13: 0.5234 L23: -0.7778
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: -0.3737 S13: 0.0092
REMARK 3 S21: 0.0866 S22: 0.1388 S23: 0.3452
REMARK 3 S31: -0.2244 S32: -0.4381 S33: -0.1622
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.5294 -19.7358 10.0495
REMARK 3 T TENSOR
REMARK 3 T11: 0.3713 T22: 0.4566
REMARK 3 T33: 0.4182 T12: 0.0086
REMARK 3 T13: 0.0044 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.3806 L22: 1.9465
REMARK 3 L33: 0.5340 L12: 0.0167
REMARK 3 L13: 0.0394 L23: -0.8091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0440 S12: -0.2431 S13: 0.2625
REMARK 3 S21: 0.3665 S22: -0.0548 S23: 0.2291
REMARK 3 S31: -0.1336 S32: -0.3021 S33: 0.0299
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 139 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): -75.1009 -39.5808 1.3829
REMARK 3 T TENSOR
REMARK 3 T11: 0.3267 T22: 0.3906
REMARK 3 T33: 0.3880 T12: -0.0726
REMARK 3 T13: -0.0399 T23: 0.1106
REMARK 3 L TENSOR
REMARK 3 L11: 0.3140 L22: 0.3570
REMARK 3 L33: 0.6392 L12: -0.1681
REMARK 3 L13: 0.3632 L23: 0.0291
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: -0.0859 S13: -0.1480
REMARK 3 S21: -0.0510 S22: 0.0707 S23: 0.2730
REMARK 3 S31: 0.3369 S32: -0.3039 S33: -0.1772
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 182 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2998 -23.4384 -13.2210
REMARK 3 T TENSOR
REMARK 3 T11: 0.3378 T22: 0.2962
REMARK 3 T33: 0.2527 T12: -0.0117
REMARK 3 T13: 0.0066 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 0.6755 L22: 0.7290
REMARK 3 L33: 0.6147 L12: 0.2235
REMARK 3 L13: 0.1259 L23: -0.0686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: 0.1512 S13: 0.0561
REMARK 3 S21: -0.1853 S22: -0.0135 S23: 0.0296
REMARK 3 S31: 0.0935 S32: 0.0631 S33: -0.0030
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 270 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.7341 -20.8768 -18.4671
REMARK 3 T TENSOR
REMARK 3 T11: 0.3865 T22: 0.3328
REMARK 3 T33: 0.2749 T12: -0.0255
REMARK 3 T13: 0.0394 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.2163 L22: 1.2514
REMARK 3 L33: 1.4307 L12: -0.1597
REMARK 3 L13: 0.1875 L23: 0.0472
REMARK 3 S TENSOR
REMARK 3 S11: -0.2667 S12: 0.4495 S13: -0.0856
REMARK 3 S21: -0.5642 S22: 0.2288 S23: -0.1095
REMARK 3 S31: -0.0347 S32: 0.2393 S33: -0.0090
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 320 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.9457 -18.9319 -7.5073
REMARK 3 T TENSOR
REMARK 3 T11: 0.2797 T22: 0.2558
REMARK 3 T33: 0.2812 T12: 0.0127
REMARK 3 T13: -0.0180 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 0.9492 L22: 0.8851
REMARK 3 L33: 0.9531 L12: 0.2480
REMARK 3 L13: 0.5058 L23: -0.2859
REMARK 3 S TENSOR
REMARK 3 S11: -0.0668 S12: 0.0088 S13: 0.0967
REMARK 3 S21: -0.1438 S22: 0.0651 S23: 0.1735
REMARK 3 S31: -0.0381 S32: -0.1424 S33: -0.0179
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 33 THROUGH 105A)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0109 -57.2409 61.8715
REMARK 3 T TENSOR
REMARK 3 T11: 0.4769 T22: 0.3399
REMARK 3 T33: 0.5891 T12: 0.0508
REMARK 3 T13: -0.1094 T23: -0.0812
REMARK 3 L TENSOR
REMARK 3 L11: 1.9584 L22: 0.9591
REMARK 3 L33: 0.6963 L12: 0.2059
REMARK 3 L13: -0.0133 L23: -0.2228
REMARK 3 S TENSOR
REMARK 3 S11: 0.1419 S12: -0.1736 S13: -0.6681
REMARK 3 S21: -0.1242 S22: -0.0613 S23: -0.3065
REMARK 3 S31: 0.1888 S32: 0.1997 S33: -0.1959
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 106 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2670 -45.6851 55.7528
REMARK 3 T TENSOR
REMARK 3 T11: 0.3829 T22: 0.3610
REMARK 3 T33: 0.4171 T12: 0.0415
REMARK 3 T13: -0.0539 T23: -0.0474
REMARK 3 L TENSOR
REMARK 3 L11: 2.3645 L22: 0.5697
REMARK 3 L33: 1.4678 L12: 0.3345
REMARK 3 L13: -1.2117 L23: -0.4311
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.2092 S13: -0.4703
REMARK 3 S21: -0.0442 S22: -0.1303 S23: -0.2627
REMARK 3 S31: 0.3010 S32: 0.0010 S33: -0.1495
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 139 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1987 -23.6510 65.2833
REMARK 3 T TENSOR
REMARK 3 T11: 0.2789 T22: 0.2648
REMARK 3 T33: 0.2717 T12: -0.0076
REMARK 3 T13: -0.0367 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.8972 L22: 0.9063
REMARK 3 L33: 0.5771 L12: 0.2896
REMARK 3 L13: 0.2386 L23: -0.1429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.0449 S13: -0.0088
REMARK 3 S21: 0.1800 S22: -0.0371 S23: -0.1379
REMARK 3 S31: -0.0730 S32: 0.0380 S33: 0.0152
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 320 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5756 -32.2738 62.2471
REMARK 3 T TENSOR
REMARK 3 T11: 0.2660 T22: 0.2994
REMARK 3 T33: 0.3576 T12: -0.0003
REMARK 3 T13: -0.0419 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.0143 L22: 0.7281
REMARK 3 L33: 0.8499 L12: 0.1522
REMARK 3 L13: 0.4172 L23: -0.1013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.0774 S13: -0.1009
REMARK 3 S21: 0.1005 S22: -0.0319 S23: -0.2971
REMARK 3 S31: -0.0365 S32: 0.1955 S33: -0.0229
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8230 -34.3603 25.3730
REMARK 3 T TENSOR
REMARK 3 T11: 0.4341 T22: 0.6743
REMARK 3 T33: 0.3449 T12: -0.0380
REMARK 3 T13: 0.0555 T23: -0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 1.5972 L22: 0.3566
REMARK 3 L33: 0.6435 L12: 0.6137
REMARK 3 L13: -0.2499 L23: -0.0041
REMARK 3 S TENSOR
REMARK 3 S11: -0.1889 S12: 0.6223 S13: -0.1931
REMARK 3 S21: -0.3003 S22: 0.0546 S23: -0.0124
REMARK 3 S31: -0.0112 S32: 0.2690 S33: 0.0495
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 94 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4959 -58.5995 35.4308
REMARK 3 T TENSOR
REMARK 3 T11: 0.5545 T22: 0.5462
REMARK 3 T33: 0.4453 T12: 0.0668
REMARK 3 T13: -0.0118 T23: -0.1756
REMARK 3 L TENSOR
REMARK 3 L11: 0.5070 L22: 1.3303
REMARK 3 L33: 0.9137 L12: -0.3927
REMARK 3 L13: 0.5715 L23: -0.1969
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: 0.1813 S13: -0.3712
REMARK 3 S21: -0.2318 S22: 0.2195 S23: -0.4417
REMARK 3 S31: 0.4001 S32: 0.2978 S33: 0.1019
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 124 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1591 -23.9410 37.2561
REMARK 3 T TENSOR
REMARK 3 T11: 0.3322 T22: 0.4116
REMARK 3 T33: 0.2584 T12: -0.0609
REMARK 3 T13: -0.0069 T23: 0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 0.7996 L22: 0.4234
REMARK 3 L33: 0.3788 L12: 0.3601
REMARK 3 L13: 0.4167 L23: 0.1860
REMARK 3 S TENSOR
REMARK 3 S11: -0.2220 S12: 0.3508 S13: 0.3764
REMARK 3 S21: -0.1631 S22: 0.1114 S23: -0.0019
REMARK 3 S31: 0.0070 S32: 0.0659 S33: 0.0564
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 182 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9317 -38.9600 55.9920
REMARK 3 T TENSOR
REMARK 3 T11: 0.2873 T22: 0.2805
REMARK 3 T33: 0.2633 T12: -0.0141
REMARK 3 T13: 0.0369 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.6363 L22: 0.5843
REMARK 3 L33: 0.7854 L12: 0.0654
REMARK 3 L13: 0.2520 L23: -0.3479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: -0.0510 S13: 0.1243
REMARK 3 S21: 0.0831 S22: -0.0413 S23: 0.0890
REMARK 3 S31: -0.0221 S32: -0.1024 S33: -0.0686
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 270 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9312 -41.5819 62.5877
REMARK 3 T TENSOR
REMARK 3 T11: 0.2804 T22: 0.2475
REMARK 3 T33: 0.2565 T12: -0.0084
REMARK 3 T13: 0.0456 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.5300 L22: 1.4589
REMARK 3 L33: 1.0161 L12: -0.0261
REMARK 3 L13: 0.1041 L23: -0.2272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0954 S13: -0.0209
REMARK 3 S21: 0.1527 S22: 0.1178 S23: 0.1265
REMARK 3 S31: 0.0450 S32: -0.3406 S33: -0.0057
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 320 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8834 -43.3653 43.3151
REMARK 3 T TENSOR
REMARK 3 T11: 0.2744 T22: 0.2790
REMARK 3 T33: 0.2314 T12: -0.0068
REMARK 3 T13: 0.0104 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.2681 L22: 0.8134
REMARK 3 L33: 0.5382 L12: 0.2016
REMARK 3 L13: 0.3407 L23: -0.1908
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.2156 S13: -0.0894
REMARK 3 S21: -0.0922 S22: 0.1018 S23: 0.0540
REMARK 3 S31: 0.0770 S32: -0.0154 S33: -0.0242
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6BL3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141148
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.217
REMARK 200 RESOLUTION RANGE LOW (A) : 103.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.15350
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3NT1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MCOX-2 PROTEIN RECONSTITUTED WITH A 2
REMARK 280 -FOLD MOLAR EXCESS OF HEME IN PHOSPHTATE BUFFER, PH 6.7, 100 MM
REMARK 280 NACL, 1.2% (W/V) -OG, AND 0.1% NAN3, AND 10-FOLD MOLAR EXCESS OF
REMARK 280 INHIBITORS FROM 25 MM DMSO STOCKS WERE ADDED TO PROTEIN SAMPLES.
REMARK 280 MIXING 3 UL OF THE PROTEIN-INHIBITOR COMPLEX WITH 3 UL
REMARK 280 CRYSTALLIZATION SOLUTION CONTAINING 50 MM EPPS, PH 8.0, 120 MM
REMARK 280 MGCL2, 22-26% PEG MME-550 AGAINST RESERVOIR SOLUTIONS COMPRISED
REMARK 280 OF 50 MM EPPS PH 8.0, 120 MM MGCL2, 22-26% PEG MME-550, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K, EVAPORATION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 107.73700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.88800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.73700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 60.88800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 11350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 350
REMARK 350 BIOMOLECULE: 2
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: 11310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
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 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 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 465 ASP C 584
REMARK 465 PRO C 585
REMARK 465 GLN C 586
REMARK 465 PRO C 587
REMARK 465 THR C 588
REMARK 465 LYS C 589
REMARK 465 THR C 590
REMARK 465 ALA C 591
REMARK 465 THR C 592
REMARK 465 ILE C 593
REMARK 465 ASN C 594
REMARK 465 ALA C 595
REMARK 465 SER C 596
REMARK 465 ALA C 597
REMARK 465 SER C 598
REMARK 465 HIS C 599
REMARK 465 SER C 600
REMARK 465 ARG C 601
REMARK 465 LEU C 602
REMARK 465 ASP C 603
REMARK 465 ASP C 604
REMARK 465 ILE C 605
REMARK 465 ASN C 606
REMARK 465 PRO C 607
REMARK 465 THR C 608
REMARK 465 VAL C 609
REMARK 465 LEU C 610
REMARK 465 ILE C 611
REMARK 465 LYS C 612
REMARK 465 ARG C 613
REMARK 465 ARG C 614
REMARK 465 SER C 615
REMARK 465 THR C 616
REMARK 465 GLU C 617
REMARK 465 LEU C 618
REMARK 465 ASP D 584
REMARK 465 PRO D 585
REMARK 465 GLN D 586
REMARK 465 PRO D 587
REMARK 465 THR D 588
REMARK 465 LYS D 589
REMARK 465 THR D 590
REMARK 465 ALA D 591
REMARK 465 THR D 592
REMARK 465 ILE D 593
REMARK 465 ASN D 594
REMARK 465 ALA D 595
REMARK 465 SER D 596
REMARK 465 ALA D 597
REMARK 465 SER D 598
REMARK 465 HIS D 599
REMARK 465 SER D 600
REMARK 465 ARG D 601
REMARK 465 LEU D 602
REMARK 465 ASP D 603
REMARK 465 ASP D 604
REMARK 465 ILE D 605
REMARK 465 ASN D 606
REMARK 465 PRO D 607
REMARK 465 THR D 608
REMARK 465 VAL D 609
REMARK 465 LEU D 610
REMARK 465 ILE D 611
REMARK 465 LYS D 612
REMARK 465 ARG D 613
REMARK 465 ARG D 614
REMARK 465 SER D 615
REMARK 465 THR D 616
REMARK 465 GLU D 617
REMARK 465 LEU D 618
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 129 -89.88 -118.84
REMARK 500 ARG A 185 -77.33 -90.40
REMARK 500 TRP A 387 39.34 -96.15
REMARK 500 GLU A 398 -114.15 57.49
REMARK 500 SER A 496 -57.01 67.73
REMARK 500 THR B 129 -89.97 -117.93
REMARK 500 ARG B 185 -77.29 -90.62
REMARK 500 ASN B 195 -169.87 -109.62
REMARK 500 TRP B 387 39.54 -96.05
REMARK 500 GLU B 398 -115.69 57.83
REMARK 500 SER B 496 -56.83 68.36
REMARK 500 THR C 129 -89.41 -118.28
REMARK 500 ARG C 185 -77.67 -90.45
REMARK 500 ASN C 195 -169.99 -109.06
REMARK 500 TRP C 387 39.29 -96.67
REMARK 500 GLU C 398 -118.19 64.00
REMARK 500 ASN C 439 18.61 -140.08
REMARK 500 SER C 496 -55.54 67.41
REMARK 500 THR D 129 -91.63 -115.60
REMARK 500 ARG D 185 -77.01 -90.80
REMARK 500 ASN D 195 -169.66 -109.63
REMARK 500 TRP D 387 39.30 -95.96
REMARK 500 GLU D 398 -107.10 59.87
REMARK 500 SER D 496 -58.27 71.22
REMARK 500
REMARK 500 REMARK: NULL
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 HEM A 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 HEM A 705 NA 84.3
REMARK 620 3 HEM A 705 NB 95.6 89.4
REMARK 620 4 HEM A 705 NC 90.6 174.9 91.0
REMARK 620 5 HEM A 705 ND 74.7 90.0 170.3 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 HEM B 705 NA 85.2
REMARK 620 3 HEM B 705 NB 95.9 90.5
REMARK 620 4 HEM B 705 NC 94.2 179.0 90.4
REMARK 620 5 HEM B 705 ND 78.9 89.0 174.8 90.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388 NE2
REMARK 620 2 HEM C 705 NA 85.1
REMARK 620 3 HEM C 705 NB 95.2 89.7
REMARK 620 4 HEM C 705 NC 92.7 177.6 91.4
REMARK 620 5 HEM C 705 ND 77.9 89.8 173.1 88.9
REMARK 620 6 HOH C 877 O 153.5 69.2 90.9 113.0 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388 NE2
REMARK 620 2 HEM D 705 NA 82.8
REMARK 620 3 HEM D 705 NB 93.4 90.3
REMARK 620 4 HEM D 705 NC 92.6 175.3 90.3
REMARK 620 5 HEM D 705 ND 77.4 89.4 170.7 89.3
REMARK 620 N 1 2 3 4
DBREF 6BL3 A 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 6BL3 B 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 6BL3 C 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 6BL3 D 33 618 UNP Q05769 PGH2_MOUSE 18 604
SEQRES 1 A 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 A 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 A 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 A 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 A 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 A 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 A 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 A 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 A 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 A 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 A 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 A 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 A 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 A 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 A 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 A 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 A 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 A 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 A 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 A 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 A 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 A 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 A 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 A 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 A 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 A 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 A 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 A 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 A 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 A 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 A 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 A 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 A 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 A 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 A 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 A 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 A 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 A 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 A 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 A 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 A 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 A 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 A 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 A 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 A 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 A 587 GLU LEU
SEQRES 1 B 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 B 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 B 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 B 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 B 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 B 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 B 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 B 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 B 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 B 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 B 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 B 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 B 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 B 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 B 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 B 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 B 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 B 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 B 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 B 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 B 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 B 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 B 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 B 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 B 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 B 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 B 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 B 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 B 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 B 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 B 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 B 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 B 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 B 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 B 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 B 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 B 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 B 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 B 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 B 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 B 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 B 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 B 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 B 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 B 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 B 587 GLU LEU
SEQRES 1 C 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 C 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 C 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 C 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 C 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 C 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 C 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 C 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 C 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 C 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 C 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 C 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 C 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 C 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 C 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 C 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 C 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 C 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 C 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 C 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 C 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 C 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 C 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 C 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 C 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 C 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 C 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 C 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 C 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 C 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 C 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 C 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 C 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 C 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 C 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 C 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 C 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 C 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 C 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 C 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 C 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 C 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 C 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 C 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 C 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 C 587 GLU LEU
SEQRES 1 D 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 D 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 D 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 D 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 D 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 D 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 D 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 D 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 D 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 D 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 D 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 D 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 D 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 D 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 D 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 D 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 D 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 D 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 D 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 D 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 D 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 D 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 D 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 D 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 D 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 D 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 D 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 D 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 D 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 D 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 D 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 D 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 D 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 D 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 D 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 D 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 D 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 D 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 D 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 D 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 D 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 D 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 D 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 D 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 D 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 D 587 GLU LEU
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG A 701 14
HET NAG A 704 14
HET HEM A 705 43
HET L7M A 706 46
HET BOG A 707 20
HET BOG A 708 20
HET NAG B 701 14
HET NAG B 704 14
HET HEM B 705 43
HET L7M B 706 46
HET BOG B 707 20
HET NAG C 701 14
HET NAG C 704 14
HET HEM C 705 43
HET L7M C 706 46
HET BOG C 707 20
HET BOG C 708 20
HET NAG D 701 14
HET NAG D 704 14
HET HEM D 705 43
HET L7M D 706 46
HET BOG D 707 20
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM L7M 2-[1-(4-CHLOROBENZENE-1-CARBONYL)-5-METHOXY-2-METHYL-
HETNAM 2 L7M 1H-INDOL-3-YL]-N-[4-({[5-(DIMETHYLAMINO)NAPHTHALEN-1-
HETNAM 3 L7M YL]SULFONYL}AMINO)BUTYL]ACETAMIDE
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN HEM HEME
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 11 HEM 4(C34 H32 FE N4 O4)
FORMUL 12 L7M 4(C35 H37 CL N4 O5 S)
FORMUL 13 BOG 6(C14 H28 O6)
FORMUL 31 HOH *856(H2 O)
HELIX 1 AA1 GLU A 73 LYS A 83 1 11
HELIX 2 AA2 THR A 85 THR A 94 1 10
HELIX 3 AA3 PHE A 96 ASN A 105 1 10
HELIX 4 AA4 ILE A 105A TYR A 122 1 18
HELIX 5 AA5 SER A 138 ASN A 144 1 7
HELIX 6 AA6 ASP A 173 LEU A 182 1 10
HELIX 7 AA7 ASN A 195 HIS A 207 1 13
HELIX 8 AA8 LEU A 230 GLY A 235 1 6
HELIX 9 AA9 THR A 237 ARG A 245 1 9
HELIX 10 AB1 THR A 265 GLN A 270 1 6
HELIX 11 AB2 PRO A 280 GLN A 284 5 5
HELIX 12 AB3 VAL A 295 HIS A 320 1 26
HELIX 13 AB4 GLY A 324 ASP A 347 1 24
HELIX 14 AB5 ASP A 347 GLY A 354 1 8
HELIX 15 AB6 ASP A 362 PHE A 367 5 6
HELIX 16 AB7 ALA A 378 TYR A 385 1 8
HELIX 17 AB8 TRP A 387 LEU A 391 5 5
HELIX 18 AB9 SER A 403 LEU A 408 1 6
HELIX 19 AC1 ASN A 411 GLN A 429 1 19
HELIX 20 AC2 PRO A 441 ALA A 443 5 3
HELIX 21 AC3 VAL A 444 MET A 458 1 15
HELIX 22 AC4 SER A 462 PHE A 470 1 9
HELIX 23 AC5 SER A 477 GLY A 483 1 7
HELIX 24 AC6 LYS A 485 SER A 496 1 12
HELIX 25 AC7 ASP A 497 MET A 501 5 5
HELIX 26 AC8 GLU A 502 GLU A 510 1 9
HELIX 27 AC9 GLY A 519 GLY A 536 1 18
HELIX 28 AD1 ASN A 537 SER A 541 5 5
HELIX 29 AD2 LYS A 546 GLY A 551 5 6
HELIX 30 AD3 GLY A 552 THR A 561 1 10
HELIX 31 AD4 SER A 563 VAL A 572 1 10
HELIX 32 AD5 GLU B 73 LYS B 83 1 11
HELIX 33 AD6 THR B 85 THR B 94 1 10
HELIX 34 AD7 PHE B 96 ASN B 105 1 10
HELIX 35 AD8 ILE B 105A TYR B 122 1 18
HELIX 36 AD9 SER B 138 ASN B 144 1 7
HELIX 37 AE1 ASP B 173 LEU B 182 1 10
HELIX 38 AE2 ASN B 195 HIS B 207 1 13
HELIX 39 AE3 LEU B 230 GLY B 235 1 6
HELIX 40 AE4 THR B 237 ARG B 245 1 9
HELIX 41 AE5 THR B 265 GLN B 270 1 6
HELIX 42 AE6 PRO B 280 GLN B 284 5 5
HELIX 43 AE7 VAL B 295 HIS B 320 1 26
HELIX 44 AE8 GLY B 324 ASP B 347 1 24
HELIX 45 AE9 ASP B 347 GLY B 354 1 8
HELIX 46 AF1 ASP B 362 PHE B 367 5 6
HELIX 47 AF2 ALA B 378 TYR B 385 1 8
HELIX 48 AF3 TRP B 387 LEU B 391 5 5
HELIX 49 AF4 SER B 403 LEU B 408 1 6
HELIX 50 AF5 ASN B 411 GLN B 429 1 19
HELIX 51 AF6 PRO B 441 ALA B 443 5 3
HELIX 52 AF7 VAL B 444 MET B 458 1 15
HELIX 53 AF8 SER B 462 PHE B 470 1 9
HELIX 54 AF9 SER B 477 GLY B 483 1 7
HELIX 55 AG1 LYS B 485 SER B 496 1 12
HELIX 56 AG2 ASP B 497 MET B 501 5 5
HELIX 57 AG3 GLU B 502 GLU B 510 1 9
HELIX 58 AG4 GLY B 519 GLY B 536 1 18
HELIX 59 AG5 ASN B 537 SER B 541 5 5
HELIX 60 AG6 LYS B 546 GLY B 551 5 6
HELIX 61 AG7 GLY B 552 THR B 561 1 10
HELIX 62 AG8 SER B 563 VAL B 572 1 10
HELIX 63 AG9 GLU C 73 LYS C 83 1 11
HELIX 64 AH1 THR C 85 HIS C 95 1 11
HELIX 65 AH2 PHE C 96 ASN C 105 1 10
HELIX 66 AH3 ILE C 105A TYR C 122 1 18
HELIX 67 AH4 SER C 138 ASN C 144 1 7
HELIX 68 AH5 ASP C 173 LEU C 182 1 10
HELIX 69 AH6 ASN C 195 HIS C 207 1 13
HELIX 70 AH7 LEU C 230 GLY C 235 1 6
HELIX 71 AH8 THR C 237 ARG C 245 1 9
HELIX 72 AH9 THR C 265 GLN C 270 1 6
HELIX 73 AI1 PRO C 280 GLN C 284 5 5
HELIX 74 AI2 VAL C 295 HIS C 320 1 26
HELIX 75 AI3 GLY C 324 ASP C 347 1 24
HELIX 76 AI4 ASP C 347 GLY C 354 1 8
HELIX 77 AI5 ASP C 362 PHE C 367 5 6
HELIX 78 AI6 ALA C 378 TYR C 385 1 8
HELIX 79 AI7 TRP C 387 LEU C 391 5 5
HELIX 80 AI8 SER C 403 LEU C 408 1 6
HELIX 81 AI9 ASN C 411 GLN C 429 1 19
HELIX 82 AJ1 PRO C 441 ALA C 443 5 3
HELIX 83 AJ2 VAL C 444 MET C 458 1 15
HELIX 84 AJ3 SER C 462 PHE C 470 1 9
HELIX 85 AJ4 SER C 477 GLY C 483 1 7
HELIX 86 AJ5 LYS C 485 SER C 496 1 12
HELIX 87 AJ6 ASP C 497 MET C 501 5 5
HELIX 88 AJ7 GLU C 502 GLU C 510 1 9
HELIX 89 AJ8 GLY C 519 GLY C 536 1 18
HELIX 90 AJ9 ASN C 537 SER C 541 5 5
HELIX 91 AK1 LYS C 546 GLY C 551 5 6
HELIX 92 AK2 GLY C 552 THR C 561 1 10
HELIX 93 AK3 SER C 563 VAL C 572 1 10
HELIX 94 AK4 GLU D 73 LYS D 83 1 11
HELIX 95 AK5 THR D 85 THR D 94 1 10
HELIX 96 AK6 PHE D 96 ASN D 105 1 10
HELIX 97 AK7 ILE D 105A TYR D 122 1 18
HELIX 98 AK8 SER D 138 ASN D 144 1 7
HELIX 99 AK9 ASP D 173 LEU D 182 1 10
HELIX 100 AL1 ASN D 195 HIS D 207 1 13
HELIX 101 AL2 LEU D 230 GLY D 235 1 6
HELIX 102 AL3 THR D 237 ARG D 245 1 9
HELIX 103 AL4 THR D 265 GLN D 270 1 6
HELIX 104 AL5 PRO D 280 GLN D 284 5 5
HELIX 105 AL6 VAL D 295 HIS D 320 1 26
HELIX 106 AL7 GLY D 324 ASP D 347 1 24
HELIX 107 AL8 ASP D 347 GLY D 354 1 8
HELIX 108 AL9 ASP D 362 PHE D 367 5 6
HELIX 109 AM1 ALA D 378 TYR D 385 1 8
HELIX 110 AM2 TRP D 387 LEU D 391 5 5
HELIX 111 AM3 SER D 403 LEU D 408 1 6
HELIX 112 AM4 ASN D 411 GLN D 429 1 19
HELIX 113 AM5 PRO D 441 ALA D 443 5 3
HELIX 114 AM6 VAL D 444 MET D 458 1 15
HELIX 115 AM7 SER D 462 PHE D 470 1 9
HELIX 116 AM8 SER D 477 GLY D 483 1 7
HELIX 117 AM9 LYS D 485 SER D 496 1 12
HELIX 118 AN1 ASP D 497 MET D 501 5 5
HELIX 119 AN2 GLU D 502 GLU D 510 1 9
HELIX 120 AN3 GLY D 519 GLY D 536 1 18
HELIX 121 AN4 ASN D 537 SER D 541 5 5
HELIX 122 AN5 LYS D 546 GLY D 551 5 6
HELIX 123 AN6 GLY D 552 THR D 561 1 10
HELIX 124 AN7 SER D 563 VAL D 572 1 10
SHEET 1 AA1 2 GLU A 46 SER A 49 0
SHEET 2 AA1 2 TYR A 55 ASP A 58 -1 O ASP A 58 N GLU A 46
SHEET 1 AA2 2 PHE A 64 TYR A 65 0
SHEET 2 AA2 2 THR A 71 PRO A 72 -1 O THR A 71 N TYR A 65
SHEET 1 AA3 2 TYR A 130 ASN A 131 0
SHEET 2 AA3 2 THR A 149 ARG A 150 -1 O ARG A 150 N TYR A 130
SHEET 1 AA4 2 GLN A 255 ILE A 257 0
SHEET 2 AA4 2 GLU A 260 TYR A 262 -1 O TYR A 262 N GLN A 255
SHEET 1 AA5 2 PHE A 395 ILE A 397 0
SHEET 2 AA5 2 GLN A 400 TYR A 402 -1 O TYR A 402 N PHE A 395
SHEET 1 AA6 2 GLU B 46 SER B 49 0
SHEET 2 AA6 2 TYR B 55 ASP B 58 -1 O ASP B 58 N GLU B 46
SHEET 1 AA7 2 PHE B 64 TYR B 65 0
SHEET 2 AA7 2 THR B 71 PRO B 72 -1 O THR B 71 N TYR B 65
SHEET 1 AA8 2 TYR B 130 ASN B 131 0
SHEET 2 AA8 2 THR B 149 ARG B 150 -1 O ARG B 150 N TYR B 130
SHEET 1 AA9 2 GLN B 255 ILE B 257 0
SHEET 2 AA9 2 GLU B 260 TYR B 262 -1 O TYR B 262 N GLN B 255
SHEET 1 AB1 2 PHE B 395 ILE B 397 0
SHEET 2 AB1 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SHEET 1 AB2 2 GLU C 46 SER C 49 0
SHEET 2 AB2 2 TYR C 55 ASP C 58 -1 O ASP C 58 N GLU C 46
SHEET 1 AB3 2 PHE C 64 TYR C 65 0
SHEET 2 AB3 2 THR C 71 PRO C 72 -1 O THR C 71 N TYR C 65
SHEET 1 AB4 2 TYR C 130 ASN C 131 0
SHEET 2 AB4 2 THR C 149 ARG C 150 -1 O ARG C 150 N TYR C 130
SHEET 1 AB5 2 GLN C 255 ILE C 257 0
SHEET 2 AB5 2 GLU C 260 TYR C 262 -1 O TYR C 262 N GLN C 255
SHEET 1 AB6 2 PHE C 395 ILE C 397 0
SHEET 2 AB6 2 GLN C 400 TYR C 402 -1 O TYR C 402 N PHE C 395
SHEET 1 AB7 2 GLU D 46 SER D 49 0
SHEET 2 AB7 2 TYR D 55 ASP D 58 -1 O ASP D 58 N GLU D 46
SHEET 1 AB8 2 PHE D 64 TYR D 65 0
SHEET 2 AB8 2 THR D 71 PRO D 72 -1 O THR D 71 N TYR D 65
SHEET 1 AB9 2 TYR D 130 ASN D 131 0
SHEET 2 AB9 2 THR D 149 ARG D 150 -1 O ARG D 150 N TYR D 130
SHEET 1 AC1 2 GLN D 255 ILE D 257 0
SHEET 2 AC1 2 GLU D 260 TYR D 262 -1 O TYR D 262 N GLN D 255
SHEET 1 AC2 2 PHE D 395 ILE D 397 0
SHEET 2 AC2 2 GLN D 400 TYR D 402 -1 O TYR D 402 N PHE D 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.03
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 2.03
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.03
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.03
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.03
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.03
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.03
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.04
SSBOND 11 CYS C 36 CYS C 47 1555 1555 2.04
SSBOND 12 CYS C 37 CYS C 159 1555 1555 2.03
SSBOND 13 CYS C 41 CYS C 57 1555 1555 2.03
SSBOND 14 CYS C 59 CYS C 69 1555 1555 2.03
SSBOND 15 CYS C 569 CYS C 575 1555 1555 2.03
SSBOND 16 CYS D 36 CYS D 47 1555 1555 2.03
SSBOND 17 CYS D 37 CYS D 159 1555 1555 2.03
SSBOND 18 CYS D 41 CYS D 57 1555 1555 2.03
SSBOND 19 CYS D 59 CYS D 69 1555 1555 2.03
SSBOND 20 CYS D 569 CYS D 575 1555 1555 2.04
LINK ND2 ASN A 68 C1 NAG A 701 1555 1555 1.45
LINK ND2 ASN A 144 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 410 C1 NAG A 704 1555 1555 1.43
LINK ND2 ASN B 68 C1 NAG B 701 1555 1555 1.45
LINK ND2 ASN B 144 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 410 C1 NAG B 704 1555 1555 1.43
LINK ND2 ASN C 68 C1 NAG C 701 1555 1555 1.45
LINK ND2 ASN C 144 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN C 410 C1 NAG C 704 1555 1555 1.43
LINK ND2 ASN D 68 C1 NAG D 701 1555 1555 1.45
LINK ND2 ASN D 144 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN D 410 C1 NAG D 704 1555 1555 1.43
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK NE2 HIS A 388 FE HEM A 705 1555 1555 2.60
LINK NE2 HIS B 388 FE HEM B 705 1555 1555 2.59
LINK NE2 HIS C 388 FE HEM C 705 1555 1555 2.62
LINK FE HEM C 705 O HOH C 877 1555 1555 2.73
LINK NE2 HIS D 388 FE HEM D 705 1555 1555 2.62
CISPEP 1 SER A 126 PRO A 127 0 1.82
CISPEP 2 SER B 126 PRO B 127 0 1.36
CISPEP 3 SER C 126 PRO C 127 0 2.03
CISPEP 4 SER D 126 PRO D 127 0 1.18
CRYST1 215.474 121.776 134.800 90.00 123.48 90.00 C 1 2 1 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 0.004641 0.000000 0.003069 0.00000
SCALE2 0.000000 0.008212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008894 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
