HEADER TRANSCRIPTION 11-SEP-13 4C5E
TITLE CRYSTAL STRUCTURE OF THE MINIMAL PHO-SFMBT COMPLEX (P21 SPACEGROUP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYCOMB PROTEIN SFMBT;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: MBT, RESIDUES 531-980;
COMPND 5 SYNONYM: SCM-LIKE WITH FOUR MBT DOMAIN-CONTAINING PROTEIN 1, DSFMBT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POLYCOMB PROTEIN PHO;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 FRAGMENT: SPACER, RESIDUES 145-172;
COMPND 11 SYNONYM: PROTEIN PLEIOHOMEOTIC, TRANSCRIPTION FACTOR YY1 HOMOLOG;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 11 ORGANISM_COMMON: FRUIT FLY;
SOURCE 12 ORGANISM_TAXID: 7227;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: GOLD
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ALFIERI,S.GLATT,C.W.MUELLER
REVDAT 2 20-DEC-23 4C5E 1 REMARK
REVDAT 1 13-NOV-13 4C5E 0
JRNL AUTH C.ALFIERI,M.C.GAMBETTA,R.MATOS,S.GLATT,P.SEHR,S.FRATERMAN,
JRNL AUTH 2 M.WILM,J.MUELLER,C.W.MUELLER
JRNL TITL STRUCTURAL BASIS FOR TARGETING THE CHROMATIN REPRESSOR SFMBT
JRNL TITL 2 TO POLYCOMB RESPONSE ELEMENTS
JRNL REF GENES DEV. V. 27 2367 2013
JRNL REFN ISSN 0890-9369
JRNL PMID 24186981
JRNL DOI 10.1101/GAD.226621.113
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 166463
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.6159 - 6.0590 0.99 5341 282 0.1799 0.2098
REMARK 3 2 6.0590 - 4.8106 1.00 5303 280 0.1661 0.1770
REMARK 3 3 4.8106 - 4.2029 1.00 5286 278 0.1341 0.1463
REMARK 3 4 4.2029 - 3.8188 1.00 5295 279 0.1458 0.1567
REMARK 3 5 3.8188 - 3.5451 1.00 5291 278 0.1577 0.1631
REMARK 3 6 3.5451 - 3.3362 1.00 5282 279 0.1623 0.1776
REMARK 3 7 3.3362 - 3.1691 1.00 5275 277 0.1733 0.1930
REMARK 3 8 3.1691 - 3.0312 1.00 5290 279 0.1749 0.1806
REMARK 3 9 3.0312 - 2.9145 1.00 5276 277 0.1823 0.2207
REMARK 3 10 2.9145 - 2.8140 1.00 5263 277 0.1796 0.1810
REMARK 3 11 2.8140 - 2.7260 1.00 5270 278 0.1724 0.1935
REMARK 3 12 2.7260 - 2.6481 1.00 5266 277 0.1802 0.1982
REMARK 3 13 2.6481 - 2.5784 1.00 5286 278 0.1816 0.2082
REMARK 3 14 2.5784 - 2.5155 1.00 5275 278 0.1951 0.2132
REMARK 3 15 2.5155 - 2.4583 1.00 5277 278 0.1868 0.2083
REMARK 3 16 2.4583 - 2.4060 1.00 5266 277 0.1936 0.2285
REMARK 3 17 2.4060 - 2.3578 1.00 5268 277 0.1954 0.2406
REMARK 3 18 2.3578 - 2.3133 1.00 5283 278 0.1975 0.2249
REMARK 3 19 2.3133 - 2.2720 1.00 5266 278 0.1992 0.2265
REMARK 3 20 2.2720 - 2.2335 1.00 5268 277 0.1986 0.2195
REMARK 3 21 2.2335 - 2.1975 1.00 5285 277 0.2090 0.2455
REMARK 3 22 2.1975 - 2.1637 1.00 5261 277 0.2119 0.2509
REMARK 3 23 2.1637 - 2.1319 1.00 5260 277 0.2110 0.2274
REMARK 3 24 2.1319 - 2.1018 1.00 5299 279 0.2144 0.2399
REMARK 3 25 2.1018 - 2.0734 1.00 5217 274 0.2193 0.2709
REMARK 3 26 2.0734 - 2.0465 1.00 5284 279 0.2332 0.2552
REMARK 3 27 2.0465 - 2.0209 1.00 5275 277 0.2482 0.2634
REMARK 3 28 2.0209 - 1.9966 1.00 5212 275 0.2504 0.2913
REMARK 3 29 1.9966 - 1.9733 1.00 5308 279 0.2596 0.2672
REMARK 3 30 1.9733 - 1.9512 0.97 5110 269 0.2775 0.2791
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.40
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 15449
REMARK 3 ANGLE : 0.772 21031
REMARK 3 CHIRALITY : 0.055 2230
REMARK 3 PLANARITY : 0.003 2722
REMARK 3 DIHEDRAL : 10.825 5511
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 534 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2768 -23.7291 7.0491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1539 T22: 0.1505
REMARK 3 T33: 0.1757 T12: 0.0126
REMARK 3 T13: -0.0394 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 1.4088 L22: 1.7111
REMARK 3 L33: 2.9002 L12: -0.3610
REMARK 3 L13: -1.3313 L23: 0.2384
REMARK 3 S TENSOR
REMARK 3 S11: 0.0866 S12: 0.2670 S13: 0.1332
REMARK 3 S21: -0.2533 S22: -0.0193 S23: 0.1846
REMARK 3 S31: -0.2195 S32: -0.3652 S33: -0.0658
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 675 THROUGH 776 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6679 -35.2257 32.9475
REMARK 3 T TENSOR
REMARK 3 T11: 0.1143 T22: 0.1998
REMARK 3 T33: 0.2762 T12: -0.0128
REMARK 3 T13: 0.0148 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 2.7775 L22: 0.6379
REMARK 3 L33: 3.5000 L12: 0.3157
REMARK 3 L13: -1.0798 L23: -0.3240
REMARK 3 S TENSOR
REMARK 3 S11: -0.1439 S12: 0.0843 S13: -0.2677
REMARK 3 S21: 0.0388 S22: 0.0395 S23: 0.2340
REMARK 3 S31: 0.1908 S32: -0.5714 S33: 0.1104
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 777 THROUGH 980 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0222 -24.0991 44.8226
REMARK 3 T TENSOR
REMARK 3 T11: 0.1381 T22: 0.2060
REMARK 3 T33: 0.1704 T12: 0.0651
REMARK 3 T13: -0.0060 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2589 L22: 1.4156
REMARK 3 L33: 2.6137 L12: 0.3465
REMARK 3 L13: -0.4762 L23: -0.1931
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.2861 S13: -0.0792
REMARK 3 S21: 0.2787 S22: 0.0631 S23: 0.0861
REMARK 3 S31: -0.1826 S32: -0.1105 S33: -0.0562
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESID 532 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2862 -22.7088 46.1713
REMARK 3 T TENSOR
REMARK 3 T11: 0.2056 T22: 0.3529
REMARK 3 T33: 0.2548 T12: -0.0082
REMARK 3 T13: -0.0216 T23: -0.1012
REMARK 3 L TENSOR
REMARK 3 L11: 1.8239 L22: 1.3951
REMARK 3 L33: 2.6731 L12: 0.5019
REMARK 3 L13: -1.0388 L23: -0.2622
REMARK 3 S TENSOR
REMARK 3 S11: 0.1524 S12: -0.5838 S13: 0.2711
REMARK 3 S21: 0.3015 S22: 0.0031 S23: -0.1576
REMARK 3 S31: -0.3871 S32: 0.3196 S33: -0.1395
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 675 THROUGH 977 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6097 -29.1679 12.4375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1161 T22: 0.1857
REMARK 3 T33: 0.1911 T12: -0.0686
REMARK 3 T13: 0.0163 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 1.3271 L22: 0.7605
REMARK 3 L33: 1.4643 L12: -0.4554
REMARK 3 L13: 0.1369 L23: -0.0139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: 0.0918 S13: 0.0818
REMARK 3 S21: -0.1259 S22: 0.0159 S23: -0.1297
REMARK 3 S31: -0.1426 S32: 0.2475 S33: -0.0288
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN C AND (RESID 534 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0022 -67.4306 37.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.1659
REMARK 3 T33: 0.3384 T12: 0.0065
REMARK 3 T13: 0.0454 T23: 0.0860
REMARK 3 L TENSOR
REMARK 3 L11: 0.9737 L22: 1.7245
REMARK 3 L33: 4.5234 L12: 0.6541
REMARK 3 L13: -1.3340 L23: 0.0452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: 0.0903 S13: 0.0218
REMARK 3 S21: 0.2409 S22: 0.0514 S23: 0.3482
REMARK 3 S31: 0.1736 S32: -0.3451 S33: -0.0597
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND (RESID 675 THROUGH 980 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6340 -63.5283 -0.3261
REMARK 3 T TENSOR
REMARK 3 T11: 0.2486 T22: 0.1497
REMARK 3 T33: 0.2001 T12: -0.0498
REMARK 3 T13: -0.0047 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 1.0059 L22: 1.2242
REMARK 3 L33: 1.5653 L12: -0.3952
REMARK 3 L13: -0.2897 L23: -0.2479
REMARK 3 S TENSOR
REMARK 3 S11: -0.0363 S12: 0.1722 S13: -0.1614
REMARK 3 S21: -0.2945 S22: 0.0404 S23: 0.0788
REMARK 3 S31: 0.0474 S32: -0.1665 S33: -0.0125
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN D AND (RESID 534 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2215 -68.4428 17.6517
REMARK 3 T TENSOR
REMARK 3 T11: 0.2785 T22: 0.2055
REMARK 3 T33: 0.3712 T12: 0.0877
REMARK 3 T13: 0.0084 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.9887 L22: 1.0481
REMARK 3 L33: 3.2711 L12: 0.1538
REMARK 3 L13: -0.4265 L23: -0.3669
REMARK 3 S TENSOR
REMARK 3 S11: -0.1246 S12: -0.0403 S13: -0.3845
REMARK 3 S21: -0.0800 S22: 0.0621 S23: -0.3060
REMARK 3 S31: 0.5973 S32: 0.4426 S33: 0.0644
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN D AND (RESID 675 THROUGH 977 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.7661 -62.4713 55.5324
REMARK 3 T TENSOR
REMARK 3 T11: 0.3678 T22: 0.4291
REMARK 3 T33: 0.2811 T12: 0.0227
REMARK 3 T13: -0.0594 T23: 0.1303
REMARK 3 L TENSOR
REMARK 3 L11: 1.2138 L22: 0.7237
REMARK 3 L33: 2.0580 L12: -0.0424
REMARK 3 L13: -0.1659 L23: 0.3358
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: -0.5161 S13: -0.2300
REMARK 3 S21: 0.3464 S22: -0.0398 S23: -0.1055
REMARK 3 S31: 0.2127 S32: 0.4512 S33: 0.0383
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN E AND (RESID 141 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0915 -49.3013 17.4166
REMARK 3 T TENSOR
REMARK 3 T11: 0.4125 T22: 0.2570
REMARK 3 T33: 0.4648 T12: -0.0372
REMARK 3 T13: 0.1158 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 2.0005 L22: 2.0002
REMARK 3 L33: 4.6733 L12: -1.7050
REMARK 3 L13: -0.0609 L23: -4.8788
REMARK 3 S TENSOR
REMARK 3 S11: 0.2661 S12: -0.5806 S13: -0.8110
REMARK 3 S21: 1.2683 S22: -0.0528 S23: 1.0301
REMARK 3 S31: 0.1005 S32: -0.2116 S33: -0.2165
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN E AND (RESID 148 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9114 -36.1421 -0.4616
REMARK 3 T TENSOR
REMARK 3 T11: 0.2863 T22: 0.1575
REMARK 3 T33: 0.1535 T12: 0.0032
REMARK 3 T13: 0.0168 T23: -0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 2.8919 L22: 6.4768
REMARK 3 L33: 6.4650 L12: -1.9039
REMARK 3 L13: 2.8412 L23: -6.2511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0676 S12: 0.3327 S13: -0.2181
REMARK 3 S21: -0.5692 S22: 0.0802 S23: 0.1393
REMARK 3 S31: 0.2995 S32: 0.1370 S33: -0.1521
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN E AND (RESID 160 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6420 -36.1894 2.3655
REMARK 3 T TENSOR
REMARK 3 T11: 0.1509 T22: 0.1061
REMARK 3 T33: 0.1407 T12: -0.0345
REMARK 3 T13: -0.0192 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 3.9356 L22: 3.2850
REMARK 3 L33: 6.2046 L12: -1.2631
REMARK 3 L13: 3.3128 L23: -0.8007
REMARK 3 S TENSOR
REMARK 3 S11: 0.1009 S12: 0.2549 S13: -0.3042
REMARK 3 S21: -0.3935 S22: 0.0665 S23: 0.1148
REMARK 3 S31: 0.7871 S32: -0.0840 S33: -0.1693
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN F AND (RESID 141 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8164 -48.8973 37.1356
REMARK 3 T TENSOR
REMARK 3 T11: 0.4651 T22: 0.3445
REMARK 3 T33: 0.6502 T12: 0.0627
REMARK 3 T13: 0.1158 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 2.0002 L22: 6.1778
REMARK 3 L33: 6.3637 L12: 1.7431
REMARK 3 L13: -1.7016 L23: 5.0391
REMARK 3 S TENSOR
REMARK 3 S11: -0.2093 S12: 0.3568 S13: -1.6960
REMARK 3 S21: -1.4713 S22: -0.0019 S23: -0.8207
REMARK 3 S31: 1.1230 S32: 0.5635 S33: 0.2072
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN F AND (RESID 148 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1154 -34.6994 54.4822
REMARK 3 T TENSOR
REMARK 3 T11: 0.3329 T22: 0.4364
REMARK 3 T33: 0.2371 T12: 0.0044
REMARK 3 T13: -0.0195 T23: 0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 2.3106 L22: 4.4979
REMARK 3 L33: 6.4016 L12: 1.5641
REMARK 3 L13: 3.2076 L23: 4.7586
REMARK 3 S TENSOR
REMARK 3 S11: 0.1369 S12: -0.4509 S13: -0.0373
REMARK 3 S21: 0.6780 S22: -0.0675 S23: -0.2470
REMARK 3 S31: 0.4233 S32: -0.0017 S33: -0.0701
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN F AND (RESID 160 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3981 -34.7658 51.5961
REMARK 3 T TENSOR
REMARK 3 T11: 0.2280 T22: 0.3712
REMARK 3 T33: 0.1819 T12: 0.0335
REMARK 3 T13: -0.0763 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.8967 L22: 2.9576
REMARK 3 L33: 2.0003 L12: 2.0791
REMARK 3 L13: 4.1340 L23: 3.1257
REMARK 3 S TENSOR
REMARK 3 S11: 0.1596 S12: -0.6108 S13: -0.2751
REMARK 3 S21: 0.5203 S22: 0.1527 S23: -0.3797
REMARK 3 S31: 0.6300 S32: 0.1363 S33: -0.3159
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN G AND (RESID 141 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6422 -41.6277 35.3913
REMARK 3 T TENSOR
REMARK 3 T11: 0.5462 T22: 0.2509
REMARK 3 T33: 0.4162 T12: -0.0365
REMARK 3 T13: -0.0679 T23: 0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 5.4723 L22: 4.2968
REMARK 3 L33: 4.5150 L12: 3.8699
REMARK 3 L13: -0.7928 L23: -3.1806
REMARK 3 S TENSOR
REMARK 3 S11: -0.2672 S12: 0.4761 S13: 1.2172
REMARK 3 S21: -0.5384 S22: 0.1712 S23: 0.1694
REMARK 3 S31: -1.0144 S32: -0.0301 S33: 0.0958
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN G AND (RESID 148 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3861 -54.9519 47.7736
REMARK 3 T TENSOR
REMARK 3 T11: 0.4384 T22: 0.2030
REMARK 3 T33: 0.4894 T12: 0.0327
REMARK 3 T13: 0.1786 T23: 0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 9.1156 L22: 3.5974
REMARK 3 L33: 4.4516 L12: 5.4644
REMARK 3 L13: -5.4288 L23: -3.0297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: -0.1950 S13: 0.5052
REMARK 3 S21: 0.4309 S22: 0.1505 S23: 0.8899
REMARK 3 S31: 0.0157 S32: -0.1055 S33: -0.0919
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN G AND (RESID 160 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5378 -55.0614 46.7255
REMARK 3 T TENSOR
REMARK 3 T11: 0.3787 T22: 0.1432
REMARK 3 T33: 0.4430 T12: 0.0123
REMARK 3 T13: 0.1512 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 9.5864 L22: 1.4588
REMARK 3 L33: 4.1445 L12: 0.8502
REMARK 3 L13: -4.1201 L23: 1.4473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0987 S12: 0.0335 S13: 0.8578
REMARK 3 S21: 0.5395 S22: 0.1434 S23: 0.7277
REMARK 3 S31: -0.3415 S32: -0.1337 S33: -0.2462
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN H AND (RESID 141 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5728 -42.2569 18.8626
REMARK 3 T TENSOR
REMARK 3 T11: 0.4811 T22: 0.2451
REMARK 3 T33: 0.4626 T12: 0.0758
REMARK 3 T13: -0.0751 T23: -0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 4.5528 L22: 9.2897
REMARK 3 L33: 5.2874 L12: -5.0535
REMARK 3 L13: -0.6042 L23: 4.3036
REMARK 3 S TENSOR
REMARK 3 S11: -0.3026 S12: -0.5293 S13: 1.3057
REMARK 3 S21: 0.9259 S22: 0.2947 S23: -0.2239
REMARK 3 S31: -1.0564 S32: -0.0282 S33: 0.0044
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN H AND (RESID 148 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4610 -56.3119 7.0874
REMARK 3 T TENSOR
REMARK 3 T11: 0.2179 T22: 0.2474
REMARK 3 T33: 0.2960 T12: -0.0334
REMARK 3 T13: -0.0212 T23: -0.0970
REMARK 3 L TENSOR
REMARK 3 L11: 2.0045 L22: 5.1056
REMARK 3 L33: 7.3741 L12: -3.5205
REMARK 3 L13: -5.5080 L23: 2.2088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0928 S12: 0.2422 S13: 0.2931
REMARK 3 S21: -0.1010 S22: 0.1408 S23: -0.6721
REMARK 3 S31: 0.0154 S32: 0.3483 S33: -0.0554
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN H AND (RESID 160 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.2938 -56.2237 8.1844
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.2662
REMARK 3 T33: 0.2950 T12: 0.0089
REMARK 3 T13: 0.0175 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 7.8338 L22: 3.7064
REMARK 3 L33: 2.0023 L12: -1.2273
REMARK 3 L13: -9.1692 L23: -1.2311
REMARK 3 S TENSOR
REMARK 3 S11: 0.1108 S12: -0.1395 S13: 0.3122
REMARK 3 S21: -0.1224 S22: 0.1316 S23: -0.5611
REMARK 3 S31: -0.2782 S32: 0.4806 S33: -0.2381
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 4C5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1290058290.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93927
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 166463
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 48.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.780
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.85000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3H6Z
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 73.94000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 81960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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 MET A 530
REMARK 465 ASP A 531
REMARK 465 PRO A 532
REMARK 465 THR A 533
REMARK 465 GLY A 763
REMARK 465 ARG A 764
REMARK 465 GLU A 765
REMARK 465 ALA A 766
REMARK 465 MET A 767
REMARK 465 ILE A 768
REMARK 465 GLU A 769
REMARK 465 MET B 530
REMARK 465 ASP B 531
REMARK 465 ARG B 764
REMARK 465 GLU B 765
REMARK 465 ALA B 766
REMARK 465 MET B 767
REMARK 465 ILE B 768
REMARK 465 GLU B 769
REMARK 465 VAL B 770
REMARK 465 VAL B 978
REMARK 465 ALA B 979
REMARK 465 HIS B 980
REMARK 465 MET C 530
REMARK 465 ASP C 531
REMARK 465 PRO C 532
REMARK 465 THR C 533
REMARK 465 ALA C 762
REMARK 465 GLY C 763
REMARK 465 ARG C 764
REMARK 465 GLU C 765
REMARK 465 ALA C 766
REMARK 465 MET C 767
REMARK 465 ILE C 768
REMARK 465 GLU C 769
REMARK 465 VAL C 770
REMARK 465 MET D 530
REMARK 465 ASP D 531
REMARK 465 PRO D 532
REMARK 465 THR D 533
REMARK 465 ALA D 762
REMARK 465 GLY D 763
REMARK 465 ARG D 764
REMARK 465 GLU D 765
REMARK 465 ALA D 766
REMARK 465 MET D 767
REMARK 465 ILE D 768
REMARK 465 VAL D 978
REMARK 465 ALA D 979
REMARK 465 HIS D 980
REMARK 465 ILE E 171
REMARK 465 SER E 172
REMARK 465 ILE F 171
REMARK 465 SER F 172
REMARK 465 ILE G 171
REMARK 465 SER G 172
REMARK 465 ILE H 171
REMARK 465 SER H 172
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 HIS A 534 ND1 CE1 NE2
REMARK 470 LYS A 544 NZ
REMARK 470 GLU A 545 CD OE1 OE2
REMARK 470 GLU A 562 OE1 OE2
REMARK 470 SER A 582 OG
REMARK 470 ILE A 583 CG1 CD1
REMARK 470 VAL A 585 CG2
REMARK 470 GLN A 587 CG CD OE1 NE2
REMARK 470 LYS A 655 CE NZ
REMARK 470 LYS A 678 CE NZ
REMARK 470 ASN A 680 ND2
REMARK 470 LEU A 761 CG CD1 CD2
REMARK 470 GLU A 778 OE2
REMARK 470 GLN A 837 NE2
REMARK 470 ASN A 872 OD1
REMARK 470 ARG A 877 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 977 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 545 CG CD OE1 OE2
REMARK 470 GLU B 562 CD OE1 OE2
REMARK 470 ASP B 581 CG OD1 OD2
REMARK 470 PRO B 588 CG
REMARK 470 GLN B 590 CD OE1 NE2
REMARK 470 LYS B 655 CD CE NZ
REMARK 470 LYS B 678 NZ
REMARK 470 GLN B 754 CD OE1 NE2
REMARK 470 LEU B 761 CG CD1 CD2
REMARK 470 GLU B 800 OE1 OE2
REMARK 470 GLN B 837 NE2
REMARK 470 SER B 876 OG
REMARK 470 ARG B 877 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 882 CD OE1 OE2
REMARK 470 GLN B 895 NE2
REMARK 470 ARG B 900 CD NE CZ NH1 NH2
REMARK 470 GLU B 947 OE2
REMARK 470 ARG B 977 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 534 ND1 CE1
REMARK 470 LYS C 544 CE NZ
REMARK 470 GLU C 545 CD OE1 OE2
REMARK 470 ASP C 581 CG OD1 OD2
REMARK 470 ILE C 583 CG1 CG2 CD1
REMARK 470 GLN C 587 CD OE1 NE2
REMARK 470 PRO C 588 CG CD
REMARK 470 GLN C 590 CD OE1 NE2
REMARK 470 LYS C 655 CE NZ
REMARK 470 LYS C 678 CE NZ
REMARK 470 ARG C 720 NH1
REMARK 470 PHE C 722 CD2
REMARK 470 ASP C 725 OD2
REMARK 470 GLU C 772 OE1 OE2
REMARK 470 ASN C 796 OD1 ND2
REMARK 470 ARG C 877 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 886 NE CZ NH1 NH2
REMARK 470 LYS C 971 NZ
REMARK 470 ARG C 977 CG CD NE CZ NH1
REMARK 470 ALA C 979 CB
REMARK 470 HIS D 534 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 544 CD CE NZ
REMARK 470 GLU D 545 CG CD OE1 OE2
REMARK 470 GLU D 562 CD OE1 OE2
REMARK 470 ILE D 583 CG2
REMARK 470 VAL D 585 CG1
REMARK 470 GLN D 587 CD OE1 NE2
REMARK 470 PRO D 588 CB CG
REMARK 470 GLN D 590 CD OE1 NE2
REMARK 470 LYS D 655 CE NZ
REMARK 470 ARG D 700 NH2
REMARK 470 ARG D 720 CZ NH1 NH2
REMARK 470 PHE D 722 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 725 CG OD1 OD2
REMARK 470 GLN D 754 CG CD OE1 NE2
REMARK 470 ASP D 755 CG OD1 OD2
REMARK 470 LEU D 757 CD2
REMARK 470 GLU D 758 CG CD OE1 OE2
REMARK 470 GLU D 769 CG CD OE1 OE2
REMARK 470 VAL D 770 CG1 CG2
REMARK 470 GLU D 772 CG CD OE1 OE2
REMARK 470 LYS D 794 CD CE NZ
REMARK 470 GLN D 837 CD OE1 NE2
REMARK 470 ASP D 839 CG OD1 OD2
REMARK 470 LYS D 851 CE NZ
REMARK 470 ASP D 875 OD1 OD2
REMARK 470 ARG D 877 CG CD NE CZ NH1 NH2
REMARK 470 THR D 945 CG2
REMARK 470 GLU D 947 CG CD OE1 OE2
REMARK 470 ARG D 977 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 147 CG CD NE CZ NH1 NH2
REMARK 470 SER G 145 OG
REMARK 470 ARG G 147 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 147 CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 590 CD
REMARK 480 MET G 143 CA
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O MET F 143 O HOH F 2001 2.16
REMARK 500 OE2 GLU D 613 O HOH D 2055 2.16
REMARK 500 OE1 GLU C 613 O HOH C 2059 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 700 85.86 -158.01
REMARK 500 ASN A 796 49.87 -143.05
REMARK 500 SER A 797 -87.38 -114.68
REMARK 500 LEU A 824 -158.53 -88.80
REMARK 500 PRO A 921 6.09 -68.48
REMARK 500 ARG B 700 85.59 -157.54
REMARK 500 ASN B 796 54.32 -140.68
REMARK 500 SER B 797 -87.11 -117.74
REMARK 500 ASN B 811 89.72 -155.89
REMARK 500 PRO B 921 4.56 -66.82
REMARK 500 ARG C 700 86.73 -155.26
REMARK 500 SER C 797 -84.16 -106.53
REMARK 500 LEU C 804 -168.83 -160.34
REMARK 500 ASP C 839 116.31 -160.35
REMARK 500 PRO C 921 5.49 -67.74
REMARK 500 ARG D 700 84.41 -161.29
REMARK 500 SER D 797 -87.78 -110.88
REMARK 500 LEU D 824 -159.30 -97.03
REMARK 500 PRO D 921 6.41 -66.14
REMARK 500 MET E 166 -165.60 -125.48
REMARK 500 MET F 166 -164.55 -126.47
REMARK 500 MET G 166 -165.63 -129.39
REMARK 500 MET H 166 -166.10 -123.10
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 A2340 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B2347 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH C2314 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH D2217 DISTANCE = 7.52 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C5G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MINIMAL PHO SFMBT COMPLEX
REMARK 900 RELATED ID: 4C5H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MINIMAL PHO-SFMBT COMPLEX
REMARK 900 RELATED ID: 4C5I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MBTD1 YY1 COMPLEX
DBREF 4C5E A 531 980 UNP Q9VK33 SMBT_DROME 531 980
DBREF 4C5E B 531 980 UNP Q9VK33 SMBT_DROME 531 980
DBREF 4C5E C 531 980 UNP Q9VK33 SMBT_DROME 531 980
DBREF 4C5E D 531 980 UNP Q9VK33 SMBT_DROME 531 980
DBREF 4C5E E 145 172 UNP Q8ST83 PHO_DROME 145 172
DBREF 4C5E F 145 172 UNP Q8ST83 PHO_DROME 145 172
DBREF 4C5E G 145 172 UNP Q8ST83 PHO_DROME 145 172
DBREF 4C5E H 145 172 UNP Q8ST83 PHO_DROME 145 172
SEQADV 4C5E MET A 530 UNP Q9VK33 EXPRESSION TAG
SEQADV 4C5E MET B 530 UNP Q9VK33 EXPRESSION TAG
SEQADV 4C5E MET C 530 UNP Q9VK33 EXPRESSION TAG
SEQADV 4C5E MET D 530 UNP Q9VK33 EXPRESSION TAG
SEQADV 4C5E GLY E 141 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA E 142 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E MET E 143 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA E 144 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E GLY F 141 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA F 142 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E MET F 143 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA F 144 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E GLY G 141 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA G 142 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E MET G 143 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA G 144 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E GLY H 141 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA H 142 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E MET H 143 UNP Q8ST83 EXPRESSION TAG
SEQADV 4C5E ALA H 144 UNP Q8ST83 EXPRESSION TAG
SEQRES 1 A 451 MET ASP PRO THR HIS SER TYR ASP TRP LEU PRO ARG LEU
SEQRES 2 A 451 SER LYS GLU ASN PHE ASN ALA ALA PRO VAL THR CYS PHE
SEQRES 3 A 451 PRO HIS ALA PRO GLY CYS GLU VAL TRP ASP ASN LEU GLY
SEQRES 4 A 451 VAL GLY MET LYS VAL GLU VAL GLU ASN THR ASP CYS ASP
SEQRES 5 A 451 SER ILE GLU VAL ILE GLN PRO GLY GLN THR PRO THR SER
SEQRES 6 A 451 PHE TRP VAL ALA THR ILE LEU GLU ILE LYS GLY TYR LYS
SEQRES 7 A 451 ALA LEU MET SER TYR GLU GLY PHE ASP THR ASP SER HIS
SEQRES 8 A 451 ASP PHE TRP VAL ASN LEU CYS ASN ALA GLU VAL HIS SER
SEQRES 9 A 451 VAL GLY TRP CYS ALA THR ARG GLY LYS PRO LEU ILE PRO
SEQRES 10 A 451 PRO ARG THR ILE GLU HIS LYS TYR LYS ASP TRP LYS ASP
SEQRES 11 A 451 PHE LEU VAL GLY ARG LEU SER GLY ALA ARG THR LEU PRO
SEQRES 12 A 451 SER ASN PHE TYR ASN LYS ILE ASN ASP SER LEU GLN SER
SEQRES 13 A 451 ARG PHE ARG LEU GLY LEU ASN LEU GLU CYS VAL ASP LYS
SEQRES 14 A 451 ASP ARG ILE SER GLN VAL ARG LEU ALA THR VAL THR LYS
SEQRES 15 A 451 ILE VAL GLY LYS ARG LEU PHE LEU ARG TYR PHE ASP SER
SEQRES 16 A 451 ASP ASP GLY PHE TRP CYS HIS GLU ASP SER PRO ILE ILE
SEQRES 17 A 451 HIS PRO VAL GLY TRP ALA THR THR VAL GLY HIS ASN LEU
SEQRES 18 A 451 ALA ALA PRO GLN ASP TYR LEU GLU ARG MET LEU ALA GLY
SEQRES 19 A 451 ARG GLU ALA MET ILE GLU VAL HIS GLU ASP ASP ALA THR
SEQRES 20 A 451 ILE GLU LEU PHE LYS MET ASN PHE THR PHE ASP GLU TYR
SEQRES 21 A 451 TYR SER ASP GLY LYS THR ASN SER PHE VAL GLU GLY MET
SEQRES 22 A 451 LYS LEU GLU ALA VAL ASP PRO LEU ASN LEU SER SER ILE
SEQRES 23 A 451 CYS PRO ALA THR VAL MET ALA VAL LEU LYS PHE GLY TYR
SEQRES 24 A 451 MET MET ILE ARG ILE ASP SER TYR GLN PRO ASP ALA SER
SEQRES 25 A 451 GLY SER ASP TRP PHE CYS TYR HIS GLU LYS SER PRO CYS
SEQRES 26 A 451 ILE PHE PRO ALA GLY PHE CYS SER VAL ASN ASN ILE SER
SEQRES 27 A 451 VAL THR PRO PRO ASN GLY TYR ASP SER ARG THR PHE THR
SEQRES 28 A 451 TRP GLU GLY TYR LEU ARG ASP THR GLY ALA VAL ALA ALA
SEQRES 29 A 451 GLY GLN HIS LEU PHE HIS ARG ILE ILE PRO ASP HIS GLY
SEQRES 30 A 451 PHE GLU VAL GLY MET SER LEU GLU CYS ALA ASP LEU MET
SEQRES 31 A 451 ASP PRO ARG LEU VAL CYS VAL ALA THR VAL ALA ARG VAL
SEQRES 32 A 451 VAL GLY ARG LEU LEU LYS VAL HIS PHE ASP GLY TRP THR
SEQRES 33 A 451 ASP GLU TYR ASP GLN TRP LEU ASP CYS GLU SER ALA ASP
SEQRES 34 A 451 ILE TYR PRO VAL GLY TRP CYS VAL LEU VAL ASN HIS LYS
SEQRES 35 A 451 LEU GLU GLY PRO PRO ARG VAL ALA HIS
SEQRES 1 B 451 MET ASP PRO THR HIS SER TYR ASP TRP LEU PRO ARG LEU
SEQRES 2 B 451 SER LYS GLU ASN PHE ASN ALA ALA PRO VAL THR CYS PHE
SEQRES 3 B 451 PRO HIS ALA PRO GLY CYS GLU VAL TRP ASP ASN LEU GLY
SEQRES 4 B 451 VAL GLY MET LYS VAL GLU VAL GLU ASN THR ASP CYS ASP
SEQRES 5 B 451 SER ILE GLU VAL ILE GLN PRO GLY GLN THR PRO THR SER
SEQRES 6 B 451 PHE TRP VAL ALA THR ILE LEU GLU ILE LYS GLY TYR LYS
SEQRES 7 B 451 ALA LEU MET SER TYR GLU GLY PHE ASP THR ASP SER HIS
SEQRES 8 B 451 ASP PHE TRP VAL ASN LEU CYS ASN ALA GLU VAL HIS SER
SEQRES 9 B 451 VAL GLY TRP CYS ALA THR ARG GLY LYS PRO LEU ILE PRO
SEQRES 10 B 451 PRO ARG THR ILE GLU HIS LYS TYR LYS ASP TRP LYS ASP
SEQRES 11 B 451 PHE LEU VAL GLY ARG LEU SER GLY ALA ARG THR LEU PRO
SEQRES 12 B 451 SER ASN PHE TYR ASN LYS ILE ASN ASP SER LEU GLN SER
SEQRES 13 B 451 ARG PHE ARG LEU GLY LEU ASN LEU GLU CYS VAL ASP LYS
SEQRES 14 B 451 ASP ARG ILE SER GLN VAL ARG LEU ALA THR VAL THR LYS
SEQRES 15 B 451 ILE VAL GLY LYS ARG LEU PHE LEU ARG TYR PHE ASP SER
SEQRES 16 B 451 ASP ASP GLY PHE TRP CYS HIS GLU ASP SER PRO ILE ILE
SEQRES 17 B 451 HIS PRO VAL GLY TRP ALA THR THR VAL GLY HIS ASN LEU
SEQRES 18 B 451 ALA ALA PRO GLN ASP TYR LEU GLU ARG MET LEU ALA GLY
SEQRES 19 B 451 ARG GLU ALA MET ILE GLU VAL HIS GLU ASP ASP ALA THR
SEQRES 20 B 451 ILE GLU LEU PHE LYS MET ASN PHE THR PHE ASP GLU TYR
SEQRES 21 B 451 TYR SER ASP GLY LYS THR ASN SER PHE VAL GLU GLY MET
SEQRES 22 B 451 LYS LEU GLU ALA VAL ASP PRO LEU ASN LEU SER SER ILE
SEQRES 23 B 451 CYS PRO ALA THR VAL MET ALA VAL LEU LYS PHE GLY TYR
SEQRES 24 B 451 MET MET ILE ARG ILE ASP SER TYR GLN PRO ASP ALA SER
SEQRES 25 B 451 GLY SER ASP TRP PHE CYS TYR HIS GLU LYS SER PRO CYS
SEQRES 26 B 451 ILE PHE PRO ALA GLY PHE CYS SER VAL ASN ASN ILE SER
SEQRES 27 B 451 VAL THR PRO PRO ASN GLY TYR ASP SER ARG THR PHE THR
SEQRES 28 B 451 TRP GLU GLY TYR LEU ARG ASP THR GLY ALA VAL ALA ALA
SEQRES 29 B 451 GLY GLN HIS LEU PHE HIS ARG ILE ILE PRO ASP HIS GLY
SEQRES 30 B 451 PHE GLU VAL GLY MET SER LEU GLU CYS ALA ASP LEU MET
SEQRES 31 B 451 ASP PRO ARG LEU VAL CYS VAL ALA THR VAL ALA ARG VAL
SEQRES 32 B 451 VAL GLY ARG LEU LEU LYS VAL HIS PHE ASP GLY TRP THR
SEQRES 33 B 451 ASP GLU TYR ASP GLN TRP LEU ASP CYS GLU SER ALA ASP
SEQRES 34 B 451 ILE TYR PRO VAL GLY TRP CYS VAL LEU VAL ASN HIS LYS
SEQRES 35 B 451 LEU GLU GLY PRO PRO ARG VAL ALA HIS
SEQRES 1 C 451 MET ASP PRO THR HIS SER TYR ASP TRP LEU PRO ARG LEU
SEQRES 2 C 451 SER LYS GLU ASN PHE ASN ALA ALA PRO VAL THR CYS PHE
SEQRES 3 C 451 PRO HIS ALA PRO GLY CYS GLU VAL TRP ASP ASN LEU GLY
SEQRES 4 C 451 VAL GLY MET LYS VAL GLU VAL GLU ASN THR ASP CYS ASP
SEQRES 5 C 451 SER ILE GLU VAL ILE GLN PRO GLY GLN THR PRO THR SER
SEQRES 6 C 451 PHE TRP VAL ALA THR ILE LEU GLU ILE LYS GLY TYR LYS
SEQRES 7 C 451 ALA LEU MET SER TYR GLU GLY PHE ASP THR ASP SER HIS
SEQRES 8 C 451 ASP PHE TRP VAL ASN LEU CYS ASN ALA GLU VAL HIS SER
SEQRES 9 C 451 VAL GLY TRP CYS ALA THR ARG GLY LYS PRO LEU ILE PRO
SEQRES 10 C 451 PRO ARG THR ILE GLU HIS LYS TYR LYS ASP TRP LYS ASP
SEQRES 11 C 451 PHE LEU VAL GLY ARG LEU SER GLY ALA ARG THR LEU PRO
SEQRES 12 C 451 SER ASN PHE TYR ASN LYS ILE ASN ASP SER LEU GLN SER
SEQRES 13 C 451 ARG PHE ARG LEU GLY LEU ASN LEU GLU CYS VAL ASP LYS
SEQRES 14 C 451 ASP ARG ILE SER GLN VAL ARG LEU ALA THR VAL THR LYS
SEQRES 15 C 451 ILE VAL GLY LYS ARG LEU PHE LEU ARG TYR PHE ASP SER
SEQRES 16 C 451 ASP ASP GLY PHE TRP CYS HIS GLU ASP SER PRO ILE ILE
SEQRES 17 C 451 HIS PRO VAL GLY TRP ALA THR THR VAL GLY HIS ASN LEU
SEQRES 18 C 451 ALA ALA PRO GLN ASP TYR LEU GLU ARG MET LEU ALA GLY
SEQRES 19 C 451 ARG GLU ALA MET ILE GLU VAL HIS GLU ASP ASP ALA THR
SEQRES 20 C 451 ILE GLU LEU PHE LYS MET ASN PHE THR PHE ASP GLU TYR
SEQRES 21 C 451 TYR SER ASP GLY LYS THR ASN SER PHE VAL GLU GLY MET
SEQRES 22 C 451 LYS LEU GLU ALA VAL ASP PRO LEU ASN LEU SER SER ILE
SEQRES 23 C 451 CYS PRO ALA THR VAL MET ALA VAL LEU LYS PHE GLY TYR
SEQRES 24 C 451 MET MET ILE ARG ILE ASP SER TYR GLN PRO ASP ALA SER
SEQRES 25 C 451 GLY SER ASP TRP PHE CYS TYR HIS GLU LYS SER PRO CYS
SEQRES 26 C 451 ILE PHE PRO ALA GLY PHE CYS SER VAL ASN ASN ILE SER
SEQRES 27 C 451 VAL THR PRO PRO ASN GLY TYR ASP SER ARG THR PHE THR
SEQRES 28 C 451 TRP GLU GLY TYR LEU ARG ASP THR GLY ALA VAL ALA ALA
SEQRES 29 C 451 GLY GLN HIS LEU PHE HIS ARG ILE ILE PRO ASP HIS GLY
SEQRES 30 C 451 PHE GLU VAL GLY MET SER LEU GLU CYS ALA ASP LEU MET
SEQRES 31 C 451 ASP PRO ARG LEU VAL CYS VAL ALA THR VAL ALA ARG VAL
SEQRES 32 C 451 VAL GLY ARG LEU LEU LYS VAL HIS PHE ASP GLY TRP THR
SEQRES 33 C 451 ASP GLU TYR ASP GLN TRP LEU ASP CYS GLU SER ALA ASP
SEQRES 34 C 451 ILE TYR PRO VAL GLY TRP CYS VAL LEU VAL ASN HIS LYS
SEQRES 35 C 451 LEU GLU GLY PRO PRO ARG VAL ALA HIS
SEQRES 1 D 451 MET ASP PRO THR HIS SER TYR ASP TRP LEU PRO ARG LEU
SEQRES 2 D 451 SER LYS GLU ASN PHE ASN ALA ALA PRO VAL THR CYS PHE
SEQRES 3 D 451 PRO HIS ALA PRO GLY CYS GLU VAL TRP ASP ASN LEU GLY
SEQRES 4 D 451 VAL GLY MET LYS VAL GLU VAL GLU ASN THR ASP CYS ASP
SEQRES 5 D 451 SER ILE GLU VAL ILE GLN PRO GLY GLN THR PRO THR SER
SEQRES 6 D 451 PHE TRP VAL ALA THR ILE LEU GLU ILE LYS GLY TYR LYS
SEQRES 7 D 451 ALA LEU MET SER TYR GLU GLY PHE ASP THR ASP SER HIS
SEQRES 8 D 451 ASP PHE TRP VAL ASN LEU CYS ASN ALA GLU VAL HIS SER
SEQRES 9 D 451 VAL GLY TRP CYS ALA THR ARG GLY LYS PRO LEU ILE PRO
SEQRES 10 D 451 PRO ARG THR ILE GLU HIS LYS TYR LYS ASP TRP LYS ASP
SEQRES 11 D 451 PHE LEU VAL GLY ARG LEU SER GLY ALA ARG THR LEU PRO
SEQRES 12 D 451 SER ASN PHE TYR ASN LYS ILE ASN ASP SER LEU GLN SER
SEQRES 13 D 451 ARG PHE ARG LEU GLY LEU ASN LEU GLU CYS VAL ASP LYS
SEQRES 14 D 451 ASP ARG ILE SER GLN VAL ARG LEU ALA THR VAL THR LYS
SEQRES 15 D 451 ILE VAL GLY LYS ARG LEU PHE LEU ARG TYR PHE ASP SER
SEQRES 16 D 451 ASP ASP GLY PHE TRP CYS HIS GLU ASP SER PRO ILE ILE
SEQRES 17 D 451 HIS PRO VAL GLY TRP ALA THR THR VAL GLY HIS ASN LEU
SEQRES 18 D 451 ALA ALA PRO GLN ASP TYR LEU GLU ARG MET LEU ALA GLY
SEQRES 19 D 451 ARG GLU ALA MET ILE GLU VAL HIS GLU ASP ASP ALA THR
SEQRES 20 D 451 ILE GLU LEU PHE LYS MET ASN PHE THR PHE ASP GLU TYR
SEQRES 21 D 451 TYR SER ASP GLY LYS THR ASN SER PHE VAL GLU GLY MET
SEQRES 22 D 451 LYS LEU GLU ALA VAL ASP PRO LEU ASN LEU SER SER ILE
SEQRES 23 D 451 CYS PRO ALA THR VAL MET ALA VAL LEU LYS PHE GLY TYR
SEQRES 24 D 451 MET MET ILE ARG ILE ASP SER TYR GLN PRO ASP ALA SER
SEQRES 25 D 451 GLY SER ASP TRP PHE CYS TYR HIS GLU LYS SER PRO CYS
SEQRES 26 D 451 ILE PHE PRO ALA GLY PHE CYS SER VAL ASN ASN ILE SER
SEQRES 27 D 451 VAL THR PRO PRO ASN GLY TYR ASP SER ARG THR PHE THR
SEQRES 28 D 451 TRP GLU GLY TYR LEU ARG ASP THR GLY ALA VAL ALA ALA
SEQRES 29 D 451 GLY GLN HIS LEU PHE HIS ARG ILE ILE PRO ASP HIS GLY
SEQRES 30 D 451 PHE GLU VAL GLY MET SER LEU GLU CYS ALA ASP LEU MET
SEQRES 31 D 451 ASP PRO ARG LEU VAL CYS VAL ALA THR VAL ALA ARG VAL
SEQRES 32 D 451 VAL GLY ARG LEU LEU LYS VAL HIS PHE ASP GLY TRP THR
SEQRES 33 D 451 ASP GLU TYR ASP GLN TRP LEU ASP CYS GLU SER ALA ASP
SEQRES 34 D 451 ILE TYR PRO VAL GLY TRP CYS VAL LEU VAL ASN HIS LYS
SEQRES 35 D 451 LEU GLU GLY PRO PRO ARG VAL ALA HIS
SEQRES 1 E 32 GLY ALA MET ALA SER ARG ARG TRP GLU GLN LYS LEU VAL
SEQRES 2 E 32 HIS ILE LYS THR MET GLU GLY GLU PHE SER VAL THR MET
SEQRES 3 E 32 TRP ALA SER GLY ILE SER
SEQRES 1 F 32 GLY ALA MET ALA SER ARG ARG TRP GLU GLN LYS LEU VAL
SEQRES 2 F 32 HIS ILE LYS THR MET GLU GLY GLU PHE SER VAL THR MET
SEQRES 3 F 32 TRP ALA SER GLY ILE SER
SEQRES 1 G 32 GLY ALA MET ALA SER ARG ARG TRP GLU GLN LYS LEU VAL
SEQRES 2 G 32 HIS ILE LYS THR MET GLU GLY GLU PHE SER VAL THR MET
SEQRES 3 G 32 TRP ALA SER GLY ILE SER
SEQRES 1 H 32 GLY ALA MET ALA SER ARG ARG TRP GLU GLN LYS LEU VAL
SEQRES 2 H 32 HIS ILE LYS THR MET GLU GLY GLU PHE SER VAL THR MET
SEQRES 3 H 32 TRP ALA SER GLY ILE SER
FORMUL 9 HOH *1528(H2 O)
HELIX 1 1 TRP A 538 SER A 543 1 6
HELIX 2 2 PRO A 551 PHE A 555 5 5
HELIX 3 3 GLY A 560 LEU A 567 5 8
HELIX 4 4 GLY A 635 ARG A 640 1 6
HELIX 5 5 TRP A 657 SER A 666 1 10
HELIX 6 6 ASN A 674 SER A 682 1 9
HELIX 7 7 GLY A 741 GLY A 747 1 7
HELIX 8 8 PRO A 753 ALA A 762 1 10
HELIX 9 9 THR A 776 PHE A 780 5 5
HELIX 10 10 THR A 785 TYR A 789 5 5
HELIX 11 11 GLY A 859 ASN A 864 1 6
HELIX 12 12 THR A 880 GLY A 889 1 10
HELIX 13 13 GLY A 894 PHE A 898 5 5
HELIX 14 14 THR A 945 ASP A 949 5 5
HELIX 15 15 GLY A 963 ASN A 969 1 7
HELIX 16 16 TRP B 538 SER B 543 1 6
HELIX 17 17 PRO B 551 PHE B 555 5 5
HELIX 18 18 GLY B 560 LEU B 567 5 8
HELIX 19 19 GLY B 635 ARG B 640 1 6
HELIX 20 20 PRO B 647 TYR B 654 5 8
HELIX 21 21 TRP B 657 SER B 666 1 10
HELIX 22 22 ASN B 674 SER B 682 1 9
HELIX 23 23 GLY B 741 GLY B 747 1 7
HELIX 24 24 PRO B 753 LEU B 761 1 9
HELIX 25 25 THR B 776 PHE B 780 5 5
HELIX 26 26 THR B 785 TYR B 789 5 5
HELIX 27 27 GLY B 859 ASN B 864 1 6
HELIX 28 28 THR B 880 GLY B 889 1 10
HELIX 29 29 GLY B 894 PHE B 898 5 5
HELIX 30 30 THR B 945 ASP B 949 5 5
HELIX 31 31 GLY B 963 ASN B 969 1 7
HELIX 32 32 TRP C 538 SER C 543 1 6
HELIX 33 33 PRO C 551 PHE C 555 5 5
HELIX 34 34 VAL C 563 LEU C 567 5 5
HELIX 35 35 GLY C 635 ARG C 640 1 6
HELIX 36 36 PRO C 647 GLU C 651 5 5
HELIX 37 37 TRP C 657 SER C 666 1 10
HELIX 38 38 ASN C 674 SER C 682 1 9
HELIX 39 39 GLY C 741 GLY C 747 1 7
HELIX 40 40 PRO C 753 LEU C 761 1 9
HELIX 41 41 THR C 776 PHE C 780 5 5
HELIX 42 42 THR C 785 TYR C 789 5 5
HELIX 43 43 GLY C 859 ASN C 864 1 6
HELIX 44 44 THR C 880 GLY C 889 1 10
HELIX 45 45 GLY C 894 PHE C 898 5 5
HELIX 46 46 THR C 945 ASP C 949 5 5
HELIX 47 47 GLY C 963 ASN C 969 1 7
HELIX 48 48 TRP D 538 SER D 543 1 6
HELIX 49 49 PRO D 551 PHE D 555 5 5
HELIX 50 50 GLY D 560 LEU D 567 5 8
HELIX 51 51 GLY D 635 ARG D 640 1 6
HELIX 52 52 ILE D 650 TYR D 654 5 5
HELIX 53 53 TRP D 657 SER D 666 1 10
HELIX 54 54 ASN D 674 SER D 682 1 9
HELIX 55 55 GLY D 741 GLY D 747 1 7
HELIX 56 56 PRO D 753 LEU D 761 1 9
HELIX 57 57 THR D 776 PHE D 780 5 5
HELIX 58 58 THR D 785 TYR D 789 5 5
HELIX 59 59 GLY D 859 ASN D 864 1 6
HELIX 60 60 THR D 880 GLY D 889 1 10
HELIX 61 61 GLY D 894 PHE D 898 5 5
HELIX 62 62 THR D 945 ASP D 949 5 5
HELIX 63 63 GLY D 963 ASN D 969 1 7
SHEET 1 AA 5 PHE A 622 ASN A 625 0
SHEET 2 AA 5 LYS A 607 TYR A 612 -1 O ALA A 608 N VAL A 624
SHEET 3 AA 5 PHE A 595 LYS A 604 -1 O THR A 599 N SER A 611
SHEET 4 AA 5 LYS A 572 GLU A 576 -1 O VAL A 573 N ALA A 598
SHEET 5 AA 5 VAL A 631 HIS A 632 -1 O HIS A 632 N GLU A 574
SHEET 1 AB 4 GLY A 727 HIS A 731 0
SHEET 2 AB 4 ARG A 716 TYR A 721 -1 O LEU A 717 N CYS A 730
SHEET 3 AB 4 ARG A 700 VAL A 713 -1 O THR A 708 N ARG A 720
SHEET 4 AB 4 ASN A 749 ALA A 751 1 O ASN A 749 N VAL A 704
SHEET 1 AC 5 GLY A 727 HIS A 731 0
SHEET 2 AC 5 ARG A 716 TYR A 721 -1 O LEU A 717 N CYS A 730
SHEET 3 AC 5 ARG A 700 VAL A 713 -1 O THR A 708 N ARG A 720
SHEET 4 AC 5 ASN A 692 ASP A 697 -1 O LEU A 693 N ALA A 707
SHEET 5 AC 5 ILE A 737 HIS A 738 -1 O HIS A 738 N GLU A 694
SHEET 1 AD 2 ASN A 749 ALA A 751 0
SHEET 2 AD 2 ARG A 700 VAL A 713 1 O SER A 702 N ASN A 749
SHEET 1 AE 5 PHE A 846 HIS A 849 0
SHEET 2 AE 5 TYR A 828 ILE A 833 -1 O MET A 829 N TYR A 848
SHEET 3 AE 5 ASN A 811 VAL A 823 -1 O THR A 819 N ARG A 832
SHEET 4 AE 5 LYS A 803 ASP A 808 -1 O LEU A 804 N ALA A 818
SHEET 5 AE 5 ILE A 855 PHE A 856 -1 O PHE A 856 N GLU A 805
SHEET 1 AF 4 GLN A 950 ASP A 953 0
SHEET 2 AF 4 LEU A 936 PHE A 941 -1 O LEU A 937 N LEU A 952
SHEET 3 AF 4 VAL A 924 VAL A 933 -1 O THR A 928 N HIS A 940
SHEET 4 AF 4 LEU A 972 GLU A 973 1 O GLU A 973 N VAL A 926
SHEET 1 AG 5 GLN A 950 ASP A 953 0
SHEET 2 AG 5 LEU A 936 PHE A 941 -1 O LEU A 937 N LEU A 952
SHEET 3 AG 5 VAL A 924 VAL A 933 -1 O THR A 928 N HIS A 940
SHEET 4 AG 5 SER A 912 ALA A 916 -1 O LEU A 913 N ALA A 927
SHEET 5 AG 5 ILE A 959 TYR A 960 -1 O TYR A 960 N GLU A 914
SHEET 1 AH 2 LEU A 972 GLU A 973 0
SHEET 2 AH 2 VAL A 924 VAL A 933 1 O VAL A 924 N GLU A 973
SHEET 1 BA 5 PHE B 622 ASN B 625 0
SHEET 2 BA 5 LYS B 607 TYR B 612 -1 O ALA B 608 N VAL B 624
SHEET 3 BA 5 PHE B 595 LYS B 604 -1 O THR B 599 N SER B 611
SHEET 4 BA 5 LYS B 572 GLU B 576 -1 O VAL B 573 N ALA B 598
SHEET 5 BA 5 VAL B 631 HIS B 632 -1 O HIS B 632 N GLU B 574
SHEET 1 BB 4 GLY B 727 HIS B 731 0
SHEET 2 BB 4 ARG B 716 TYR B 721 -1 O LEU B 717 N CYS B 730
SHEET 3 BB 4 ARG B 700 VAL B 713 -1 O THR B 708 N ARG B 720
SHEET 4 BB 4 ASN B 749 ALA B 751 1 O ASN B 749 N VAL B 704
SHEET 1 BC 5 GLY B 727 HIS B 731 0
SHEET 2 BC 5 ARG B 716 TYR B 721 -1 O LEU B 717 N CYS B 730
SHEET 3 BC 5 ARG B 700 VAL B 713 -1 O THR B 708 N ARG B 720
SHEET 4 BC 5 ASN B 692 ASP B 697 -1 O LEU B 693 N ALA B 707
SHEET 5 BC 5 ILE B 737 HIS B 738 -1 O HIS B 738 N GLU B 694
SHEET 1 BD 2 ASN B 749 ALA B 751 0
SHEET 2 BD 2 ARG B 700 VAL B 713 1 O SER B 702 N ASN B 749
SHEET 1 BE 5 PHE B 846 HIS B 849 0
SHEET 2 BE 5 TYR B 828 ILE B 833 -1 O MET B 829 N TYR B 848
SHEET 3 BE 5 ASN B 811 VAL B 823 -1 O THR B 819 N ARG B 832
SHEET 4 BE 5 LYS B 803 ASP B 808 -1 O LEU B 804 N ALA B 818
SHEET 5 BE 5 ILE B 855 PHE B 856 -1 O PHE B 856 N GLU B 805
SHEET 1 BF 4 GLN B 950 ASP B 953 0
SHEET 2 BF 4 LEU B 936 PHE B 941 -1 O LEU B 937 N LEU B 952
SHEET 3 BF 4 VAL B 924 VAL B 933 -1 O THR B 928 N HIS B 940
SHEET 4 BF 4 LEU B 972 GLU B 973 1 O GLU B 973 N VAL B 926
SHEET 1 BG 5 GLN B 950 ASP B 953 0
SHEET 2 BG 5 LEU B 936 PHE B 941 -1 O LEU B 937 N LEU B 952
SHEET 3 BG 5 VAL B 924 VAL B 933 -1 O THR B 928 N HIS B 940
SHEET 4 BG 5 SER B 912 ALA B 916 -1 O LEU B 913 N ALA B 927
SHEET 5 BG 5 ILE B 959 TYR B 960 -1 O TYR B 960 N GLU B 914
SHEET 1 BH 2 LEU B 972 GLU B 973 0
SHEET 2 BH 2 VAL B 924 VAL B 933 1 O VAL B 924 N GLU B 973
SHEET 1 CA 5 PHE C 622 ASN C 625 0
SHEET 2 CA 5 LYS C 607 TYR C 612 -1 O ALA C 608 N VAL C 624
SHEET 3 CA 5 PHE C 595 LYS C 604 -1 O THR C 599 N SER C 611
SHEET 4 CA 5 LYS C 572 GLU C 576 -1 O VAL C 573 N ALA C 598
SHEET 5 CA 5 VAL C 631 HIS C 632 -1 O HIS C 632 N GLU C 574
SHEET 1 CB 4 GLY C 727 HIS C 731 0
SHEET 2 CB 4 ARG C 716 TYR C 721 -1 O LEU C 717 N CYS C 730
SHEET 3 CB 4 ARG C 700 VAL C 713 -1 O THR C 708 N ARG C 720
SHEET 4 CB 4 ASN C 749 ALA C 751 1 O ASN C 749 N VAL C 704
SHEET 1 CC 5 GLY C 727 HIS C 731 0
SHEET 2 CC 5 ARG C 716 TYR C 721 -1 O LEU C 717 N CYS C 730
SHEET 3 CC 5 ARG C 700 VAL C 713 -1 O THR C 708 N ARG C 720
SHEET 4 CC 5 ASN C 692 ASP C 697 -1 O LEU C 693 N ALA C 707
SHEET 5 CC 5 ILE C 737 HIS C 738 -1 O HIS C 738 N GLU C 694
SHEET 1 CD 2 ASN C 749 ALA C 751 0
SHEET 2 CD 2 ARG C 700 VAL C 713 1 O SER C 702 N ASN C 749
SHEET 1 CE 5 PHE C 846 HIS C 849 0
SHEET 2 CE 5 TYR C 828 ILE C 833 -1 O MET C 829 N TYR C 848
SHEET 3 CE 5 ASN C 811 VAL C 823 -1 O THR C 819 N ARG C 832
SHEET 4 CE 5 LYS C 803 ASP C 808 -1 O LEU C 804 N ALA C 818
SHEET 5 CE 5 ILE C 855 PHE C 856 -1 O PHE C 856 N GLU C 805
SHEET 1 CF 4 GLN C 950 ASP C 953 0
SHEET 2 CF 4 LEU C 936 PHE C 941 -1 O LEU C 937 N LEU C 952
SHEET 3 CF 4 VAL C 924 VAL C 933 -1 O THR C 928 N HIS C 940
SHEET 4 CF 4 LEU C 972 GLU C 973 1 O GLU C 973 N VAL C 926
SHEET 1 CG 5 GLN C 950 ASP C 953 0
SHEET 2 CG 5 LEU C 936 PHE C 941 -1 O LEU C 937 N LEU C 952
SHEET 3 CG 5 VAL C 924 VAL C 933 -1 O THR C 928 N HIS C 940
SHEET 4 CG 5 SER C 912 ALA C 916 -1 O LEU C 913 N ALA C 927
SHEET 5 CG 5 ILE C 959 TYR C 960 -1 O TYR C 960 N GLU C 914
SHEET 1 CH 2 LEU C 972 GLU C 973 0
SHEET 2 CH 2 VAL C 924 VAL C 933 1 O VAL C 924 N GLU C 973
SHEET 1 DA 5 PHE D 622 ASN D 625 0
SHEET 2 DA 5 LYS D 607 TYR D 612 -1 O ALA D 608 N VAL D 624
SHEET 3 DA 5 PHE D 595 LYS D 604 -1 O THR D 599 N SER D 611
SHEET 4 DA 5 LYS D 572 GLU D 576 -1 O VAL D 573 N ALA D 598
SHEET 5 DA 5 VAL D 631 HIS D 632 -1 O HIS D 632 N GLU D 574
SHEET 1 DB 4 GLY D 727 HIS D 731 0
SHEET 2 DB 4 ARG D 716 TYR D 721 -1 O LEU D 717 N CYS D 730
SHEET 3 DB 4 ARG D 700 VAL D 713 -1 O THR D 708 N ARG D 720
SHEET 4 DB 4 ASN D 749 ALA D 751 1 O ASN D 749 N VAL D 704
SHEET 1 DC 5 GLY D 727 HIS D 731 0
SHEET 2 DC 5 ARG D 716 TYR D 721 -1 O LEU D 717 N CYS D 730
SHEET 3 DC 5 ARG D 700 VAL D 713 -1 O THR D 708 N ARG D 720
SHEET 4 DC 5 ASN D 692 ASP D 697 -1 O LEU D 693 N ALA D 707
SHEET 5 DC 5 ILE D 737 HIS D 738 -1 O HIS D 738 N GLU D 694
SHEET 1 DD 2 ASN D 749 ALA D 751 0
SHEET 2 DD 2 ARG D 700 VAL D 713 1 O SER D 702 N ASN D 749
SHEET 1 DE 5 PHE D 846 HIS D 849 0
SHEET 2 DE 5 TYR D 828 ILE D 833 -1 O MET D 829 N TYR D 848
SHEET 3 DE 5 ASN D 811 VAL D 823 -1 O THR D 819 N ARG D 832
SHEET 4 DE 5 LYS D 803 ASP D 808 -1 O LEU D 804 N ALA D 818
SHEET 5 DE 5 ILE D 855 PHE D 856 -1 O PHE D 856 N GLU D 805
SHEET 1 DF 4 GLN D 950 ASP D 953 0
SHEET 2 DF 4 LEU D 936 PHE D 941 -1 O LEU D 937 N LEU D 952
SHEET 3 DF 4 VAL D 924 VAL D 933 -1 O THR D 928 N HIS D 940
SHEET 4 DF 4 LEU D 972 GLU D 973 1 O GLU D 973 N VAL D 926
SHEET 1 DG 5 GLN D 950 ASP D 953 0
SHEET 2 DG 5 LEU D 936 PHE D 941 -1 O LEU D 937 N LEU D 952
SHEET 3 DG 5 VAL D 924 VAL D 933 -1 O THR D 928 N HIS D 940
SHEET 4 DG 5 SER D 912 ALA D 916 -1 O LEU D 913 N ALA D 927
SHEET 5 DG 5 ILE D 959 TYR D 960 -1 O TYR D 960 N GLU D 914
SHEET 1 DH 2 LEU D 972 GLU D 973 0
SHEET 2 DH 2 VAL D 924 VAL D 933 1 O VAL D 924 N GLU D 973
SHEET 1 EA 2 TRP E 148 THR E 157 0
SHEET 2 EA 2 GLY E 160 SER E 169 -1 O GLY E 160 N THR E 157
SHEET 1 FA 2 TRP F 148 THR F 157 0
SHEET 2 FA 2 GLY F 160 SER F 169 -1 O GLY F 160 N THR F 157
SHEET 1 GA 2 TRP G 148 THR G 157 0
SHEET 2 GA 2 GLY G 160 SER G 169 -1 O GLY G 160 N THR G 157
SHEET 1 HA 2 TRP H 148 THR H 157 0
SHEET 2 HA 2 GLY H 160 SER H 169 -1 O GLY H 160 N THR H 157
CRYST1 87.510 147.880 97.880 90.00 112.26 90.00 P 1 21 1 8
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 0.011427 0.000000 0.004677 0.00000
SCALE2 0.000000 0.006762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
