HEADER TRANSLATION 04-APR-16 5J5Y
TITLE TRANSLATION INITIATION FACTOR 4E IN COMPLEX WITH M2(7,2'O)GPPCCL2PPG
TITLE 2 MRNA 5' CAP ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MRNA CAP-BINDING PROTEIN,EIF-4F 25 KDA SUBUNIT;
COMPND 5 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: EIF4E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-LIGAND COMPLEX, TRANSLATION INITIATION FACTOR, EIF4E, M2(7,
KEYWDS 2 2'O)GPPCCL2PPG, DICHLOROMETHYLENEBISPHOSPHONATE, MRNA 5' CAP ANALOG,
KEYWDS 3 TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WARMINSKI,E.NOWAK,A.M.RYDZIK,J.KOWALSKA,J.JEMIELITY,M.NOWOTNY
REVDAT 5 10-JAN-24 5J5Y 1 REMARK
REVDAT 4 23-JAN-19 5J5Y 1 CAVEAT REMARK ATOM
REVDAT 3 27-SEP-17 5J5Y 1 CAVEAT JRNL
REVDAT 2 12-JUL-17 5J5Y 1
REVDAT 1 10-MAY-17 5J5Y 0
JRNL AUTH A.M.RYDZIK,M.WARMINSKI,P.J.SIKORSKI,M.R.BARANOWSKI,
JRNL AUTH 2 S.WALCZAK,J.KOWALSKA,J.ZUBEREK,M.LUKASZEWICZ,E.NOWAK,
JRNL AUTH 3 T.D.W CLARIDGE,E.DARZYNKIEWICZ,M.NOWOTNY,J.JEMIELITY
JRNL TITL MRNA CAP ANALOGUES SUBSTITUTED IN THE TETRAPHOSPHATE CHAIN
JRNL TITL 2 WITH CX2: IDENTIFICATION OF O-TO-CCL2 AS THE FIRST BRIDGING
JRNL TITL 3 MODIFICATION THAT CONFERS RESISTANCE TO DECAPPING WITHOUT
JRNL TITL 4 IMPAIRING TRANSLATION.
JRNL REF NUCLEIC ACIDS RES. V. 45 8661 2017
JRNL REFN ESSN 1362-4962
JRNL PMID 28666355
JRNL DOI 10.1093/NAR/GKX569
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2152: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 72986
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3650
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 37.0092 - 5.1738 0.96 2838 150 0.2405 0.2636
REMARK 3 2 5.1738 - 4.1083 0.98 2894 152 0.2072 0.2339
REMARK 3 3 4.1083 - 3.5895 0.96 2815 148 0.2130 0.2789
REMARK 3 4 3.5895 - 3.2615 0.98 2911 154 0.2178 0.2946
REMARK 3 5 3.2615 - 3.0279 0.99 2899 152 0.2295 0.2633
REMARK 3 6 3.0279 - 2.8494 0.99 2888 152 0.2364 0.2852
REMARK 3 7 2.8494 - 2.7067 0.96 2787 147 0.2353 0.3069
REMARK 3 8 2.7067 - 2.5890 0.97 2895 152 0.2402 0.3186
REMARK 3 9 2.5890 - 2.4893 0.98 2886 152 0.2505 0.2880
REMARK 3 10 2.4893 - 2.4034 0.97 2859 150 0.2546 0.3259
REMARK 3 11 2.4034 - 2.3283 0.98 2882 152 0.2463 0.3015
REMARK 3 12 2.3283 - 2.2617 0.96 2801 148 0.2339 0.2652
REMARK 3 13 2.2617 - 2.2022 0.92 2745 144 0.2460 0.2796
REMARK 3 14 2.2022 - 2.1485 0.89 2622 138 0.2406 0.3270
REMARK 3 15 2.1485 - 2.0997 0.89 2617 138 0.2473 0.2863
REMARK 3 16 2.0997 - 2.0550 0.89 2628 138 0.2463 0.2898
REMARK 3 17 2.0550 - 2.0139 0.88 2520 133 0.2534 0.3183
REMARK 3 18 2.0139 - 1.9759 0.85 2558 134 0.2601 0.3065
REMARK 3 19 1.9759 - 1.9406 0.83 2471 130 0.2635 0.2795
REMARK 3 20 1.9406 - 1.9077 0.85 2440 129 0.2748 0.3159
REMARK 3 21 1.9077 - 1.8769 0.84 2470 130 0.2703 0.3153
REMARK 3 22 1.8769 - 1.8480 0.83 2510 132 0.2733 0.3256
REMARK 3 23 1.8480 - 1.8209 0.85 2397 126 0.2805 0.3218
REMARK 3 24 1.8209 - 1.7952 0.79 2389 126 0.2827 0.3393
REMARK 3 25 1.7952 - 1.7710 0.79 2371 125 0.2791 0.3332
REMARK 3 26 1.7710 - 1.7480 0.79 2243 118 0.2757 0.3384
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.410
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 : 0.007 5657
REMARK 3 ANGLE : 0.951 7714
REMARK 3 CHIRALITY : 0.054 829
REMARK 3 PLANARITY : 0.006 971
REMARK 3 DIHEDRAL : 17.827 3303
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 33
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.2955 -77.9257 4.1249
REMARK 3 T TENSOR
REMARK 3 T11: 0.2201 T22: 0.1521
REMARK 3 T33: 0.4724 T12: 0.0974
REMARK 3 T13: 0.0537 T23: -0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 2.7534 L22: 4.0211
REMARK 3 L33: 4.6108 L12: -2.7822
REMARK 3 L13: -0.9991 L23: 2.1337
REMARK 3 S TENSOR
REMARK 3 S11: 0.2047 S12: 0.1052 S13: 0.1323
REMARK 3 S21: -0.2521 S22: 0.0498 S23: -0.6074
REMARK 3 S31: 0.0439 S32: 0.4739 S33: -0.2802
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -74.4558 -69.2941 9.8112
REMARK 3 T TENSOR
REMARK 3 T11: 0.2401 T22: 0.1021
REMARK 3 T33: 0.3535 T12: 0.0457
REMARK 3 T13: 0.0218 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 2.2848 L22: 0.1445
REMARK 3 L33: 0.7484 L12: -0.4827
REMARK 3 L13: -0.9138 L23: 0.2268
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: 0.0464 S13: 0.0348
REMARK 3 S21: 0.0382 S22: -0.0729 S23: 0.3962
REMARK 3 S31: -0.2591 S32: -0.1995 S33: -0.0220
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.7089 -73.8152 6.9536
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.1399
REMARK 3 T33: 0.3766 T12: 0.0432
REMARK 3 T13: 0.0340 T23: -0.1556
REMARK 3 L TENSOR
REMARK 3 L11: 6.0289 L22: 0.8856
REMARK 3 L33: 1.1251 L12: -2.2176
REMARK 3 L13: -2.3349 L23: 0.7351
REMARK 3 S TENSOR
REMARK 3 S11: 0.0676 S12: 0.0633 S13: -0.2055
REMARK 3 S21: -0.0311 S22: -0.0298 S23: 0.1774
REMARK 3 S31: -0.0701 S32: -0.0424 S33: 0.1448
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.6499 -64.9107 12.2836
REMARK 3 T TENSOR
REMARK 3 T11: 0.1452 T22: 0.0896
REMARK 3 T33: 0.2360 T12: 0.0271
REMARK 3 T13: 0.0239 T23: -0.0637
REMARK 3 L TENSOR
REMARK 3 L11: 0.3730 L22: 2.6326
REMARK 3 L33: 1.1753 L12: -0.0562
REMARK 3 L13: 0.0187 L23: 0.2097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: -0.0606 S13: 0.1506
REMARK 3 S21: -0.0063 S22: -0.0028 S23: -0.0748
REMARK 3 S31: -0.1357 S32: -0.0936 S33: 0.0006
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.4905 -71.0901 19.9342
REMARK 3 T TENSOR
REMARK 3 T11: 0.1758 T22: 0.2035
REMARK 3 T33: 0.3620 T12: 0.0540
REMARK 3 T13: -0.0511 T23: -0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 1.7782 L22: 1.5284
REMARK 3 L33: 4.2956 L12: 1.2215
REMARK 3 L13: -1.5128 L23: -0.1234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0886 S12: -0.2860 S13: -0.1055
REMARK 3 S21: 0.1657 S22: -0.0912 S23: -0.6840
REMARK 3 S31: 0.3288 S32: 0.6414 S33: 0.0252
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.8572 -65.3411 21.8449
REMARK 3 T TENSOR
REMARK 3 T11: 0.2059 T22: 0.1139
REMARK 3 T33: 0.2363 T12: 0.0548
REMARK 3 T13: 0.0178 T23: -0.0881
REMARK 3 L TENSOR
REMARK 3 L11: 2.4499 L22: 6.5827
REMARK 3 L33: 2.2372 L12: -1.3238
REMARK 3 L13: 1.0694 L23: -0.8860
REMARK 3 S TENSOR
REMARK 3 S11: -0.1039 S12: -0.2779 S13: 0.0002
REMARK 3 S21: 0.6718 S22: 0.1860 S23: -0.0379
REMARK 3 S31: -0.2421 S32: -0.2021 S33: -0.1194
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.2179 -62.6262 27.5922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3441 T22: 0.1837
REMARK 3 T33: 0.2673 T12: -0.0015
REMARK 3 T13: -0.0886 T23: -0.1067
REMARK 3 L TENSOR
REMARK 3 L11: 2.1935 L22: 4.2367
REMARK 3 L33: 1.9484 L12: 2.9602
REMARK 3 L13: -0.3250 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.2438 S12: -0.3985 S13: 0.3351
REMARK 3 S21: 0.6022 S22: -0.2366 S23: 0.0814
REMARK 3 S31: -0.2623 S32: -0.0188 S33: -0.0158
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4205 -62.2065 62.7662
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.3146
REMARK 3 T33: 0.4701 T12: 0.0506
REMARK 3 T13: -0.0684 T23: 0.0792
REMARK 3 L TENSOR
REMARK 3 L11: 6.1401 L22: 4.0940
REMARK 3 L33: 7.2776 L12: -3.1346
REMARK 3 L13: 2.6418 L23: -0.8107
REMARK 3 S TENSOR
REMARK 3 S11: 0.1906 S12: -0.4774 S13: -0.7002
REMARK 3 S21: 0.0811 S22: 0.0399 S23: -0.0278
REMARK 3 S31: 0.7546 S32: 0.2992 S33: -0.2198
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.9312 -38.3761 57.2419
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: 0.2120
REMARK 3 T33: 0.3301 T12: -0.0151
REMARK 3 T13: -0.0627 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.1541 L22: 3.2765
REMARK 3 L33: 0.2901 L12: -1.7405
REMARK 3 L13: 0.3675 L23: -0.5771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: -0.1337 S13: 0.2400
REMARK 3 S21: 0.1153 S22: -0.0372 S23: 0.0558
REMARK 3 S31: -0.0670 S32: 0.0119 S33: 0.0505
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.3669 -49.8838 61.0155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0721 T22: 0.1557
REMARK 3 T33: 0.2085 T12: -0.0126
REMARK 3 T13: -0.0357 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 4.5117 L22: 1.6037
REMARK 3 L33: 2.4287 L12: -0.7859
REMARK 3 L13: 0.8906 L23: -0.8259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0451 S12: -0.2477 S13: -0.2353
REMARK 3 S21: 0.1202 S22: 0.0645 S23: 0.1491
REMARK 3 S31: -0.0750 S32: -0.1022 S33: -0.0231
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.9098 -41.2630 45.6811
REMARK 3 T TENSOR
REMARK 3 T11: 0.1603 T22: 0.1586
REMARK 3 T33: 0.2554 T12: -0.0736
REMARK 3 T13: -0.0149 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 5.1905 L22: 7.5905
REMARK 3 L33: 7.2794 L12: -0.9193
REMARK 3 L13: 1.8083 L23: -0.5163
REMARK 3 S TENSOR
REMARK 3 S11: -0.1763 S12: 0.2955 S13: 0.4155
REMARK 3 S21: -0.2986 S22: 0.0421 S23: -0.5723
REMARK 3 S31: -0.6561 S32: 0.6015 S33: 0.1147
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.9717 -53.6438 49.1245
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.1291
REMARK 3 T33: 0.2762 T12: -0.0256
REMARK 3 T13: -0.0357 T23: -0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 2.3936 L22: 1.6060
REMARK 3 L33: 2.0042 L12: 1.0198
REMARK 3 L13: 0.4272 L23: -0.5548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: 0.2631 S13: -0.2848
REMARK 3 S21: -0.1901 S22: -0.0332 S23: 0.0838
REMARK 3 S31: 0.1433 S32: -0.1362 S33: 0.0553
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.9321 -46.4055 44.2808
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.2035
REMARK 3 T33: 0.2545 T12: -0.0356
REMARK 3 T13: -0.0413 T23: 0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 4.6675 L22: 2.1092
REMARK 3 L33: 3.8758 L12: -0.1624
REMARK 3 L13: -0.7367 L23: 0.9392
REMARK 3 S TENSOR
REMARK 3 S11: 0.0468 S12: 0.7178 S13: 0.2257
REMARK 3 S21: -0.3452 S22: 0.0712 S23: -0.0033
REMARK 3 S31: -0.2660 S32: -0.1774 S33: -0.0241
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.6668 -59.2403 40.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.2493
REMARK 3 T33: 0.2352 T12: -0.0560
REMARK 3 T13: -0.0396 T23: -0.2264
REMARK 3 L TENSOR
REMARK 3 L11: 1.2603 L22: 2.4199
REMARK 3 L33: 2.2784 L12: 1.0780
REMARK 3 L13: 0.4936 L23: -0.2651
REMARK 3 S TENSOR
REMARK 3 S11: -0.1002 S12: 0.2297 S13: -0.1669
REMARK 3 S21: -0.2863 S22: 0.1972 S23: -0.1206
REMARK 3 S31: 0.3992 S32: 0.0828 S33: -0.1154
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 187 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.6461 -49.7209 37.5079
REMARK 3 T TENSOR
REMARK 3 T11: 0.3077 T22: 0.3234
REMARK 3 T33: 0.2035 T12: -0.0516
REMARK 3 T13: -0.0834 T23: -0.1078
REMARK 3 L TENSOR
REMARK 3 L11: 1.0256 L22: 2.6818
REMARK 3 L33: 3.8457 L12: 0.9861
REMARK 3 L13: 0.1075 L23: -0.2114
REMARK 3 S TENSOR
REMARK 3 S11: -0.2565 S12: 0.3461 S13: 0.0878
REMARK 3 S21: -0.5665 S22: 0.1726 S23: 0.4672
REMARK 3 S31: -0.1264 S32: -0.3195 S33: 0.0707
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.0470 -62.5956 -7.5423
REMARK 3 T TENSOR
REMARK 3 T11: 0.5537 T22: 0.1013
REMARK 3 T33: 0.2806 T12: -0.0148
REMARK 3 T13: 0.0418 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 3.5934 L22: 6.6966
REMARK 3 L33: 5.2014 L12: -0.0404
REMARK 3 L13: -1.6785 L23: -3.3642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0673 S12: 0.1182 S13: -0.1516
REMARK 3 S21: -0.0384 S22: 0.2437 S23: 0.4973
REMARK 3 S31: 0.6163 S32: -0.3183 S33: -0.1791
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2584 -43.6420 -13.3051
REMARK 3 T TENSOR
REMARK 3 T11: 0.7934 T22: 0.3599
REMARK 3 T33: 0.7675 T12: 0.0714
REMARK 3 T13: 0.4076 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 1.1641 L22: 2.8374
REMARK 3 L33: 1.4602 L12: -1.8150
REMARK 3 L13: -0.6671 L23: 0.9624
REMARK 3 S TENSOR
REMARK 3 S11: 0.2605 S12: 0.0522 S13: 0.7387
REMARK 3 S21: -0.9827 S22: 0.0886 S23: -1.0773
REMARK 3 S31: -0.8300 S32: 0.2496 S33: -0.4546
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 56 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.6877 -48.3172 -12.2423
REMARK 3 T TENSOR
REMARK 3 T11: 0.7979 T22: 0.2885
REMARK 3 T33: 0.6120 T12: 0.1037
REMARK 3 T13: 0.3179 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.3000 L22: 2.8624
REMARK 3 L33: 0.5879 L12: -0.8527
REMARK 3 L13: 0.0996 L23: 0.2105
REMARK 3 S TENSOR
REMARK 3 S11: 0.2568 S12: 0.4404 S13: 0.3374
REMARK 3 S21: -1.4107 S22: -0.1617 S23: -0.9797
REMARK 3 S31: -0.5061 S32: 0.1217 S33: -0.1452
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 67 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.9886 -46.8734 -11.7241
REMARK 3 T TENSOR
REMARK 3 T11: 0.6486 T22: 0.2288
REMARK 3 T33: 0.4544 T12: 0.1326
REMARK 3 T13: 0.3074 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.5845 L22: 0.7120
REMARK 3 L33: 1.0417 L12: -0.5457
REMARK 3 L13: -0.6832 L23: 0.4207
REMARK 3 S TENSOR
REMARK 3 S11: 0.1919 S12: 0.1149 S13: 0.1644
REMARK 3 S21: -0.5588 S22: 0.0134 S23: -0.5734
REMARK 3 S31: -0.2207 S32: 0.1366 S33: -0.1356
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 105 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.6830 -38.8290 -23.4261
REMARK 3 T TENSOR
REMARK 3 T11: 1.0636 T22: 0.3773
REMARK 3 T33: 0.5145 T12: 0.1482
REMARK 3 T13: 0.3442 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.1687 L22: 0.3167
REMARK 3 L33: 2.0998 L12: 0.1438
REMARK 3 L13: -0.0738 L23: 0.5702
REMARK 3 S TENSOR
REMARK 3 S11: 0.1305 S12: 0.1559 S13: -0.0468
REMARK 3 S21: -0.4047 S22: -0.2626 S23: -0.0612
REMARK 3 S31: -0.1468 S32: 0.0478 S33: 0.0365
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 126 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.6441 -44.5976 -16.3739
REMARK 3 T TENSOR
REMARK 3 T11: 0.7481 T22: 0.2299
REMARK 3 T33: 0.2471 T12: 0.1743
REMARK 3 T13: 0.1396 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 1.2653 L22: 6.0347
REMARK 3 L33: 0.8816 L12: 0.3939
REMARK 3 L13: -0.3731 L23: -0.8136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0762 S12: 0.0771 S13: 0.0478
REMARK 3 S21: -0.3089 S22: -0.0707 S23: 0.3315
REMARK 3 S31: 0.0460 S32: -0.0143 S33: 0.0025
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 139 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.2091 -56.5803 -25.6327
REMARK 3 T TENSOR
REMARK 3 T11: 1.2462 T22: 0.4142
REMARK 3 T33: 0.4133 T12: 0.2876
REMARK 3 T13: 0.0042 T23: -0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 0.7427 L22: 0.1099
REMARK 3 L33: 1.7893 L12: 0.0121
REMARK 3 L13: -1.1281 L23: -0.1101
REMARK 3 S TENSOR
REMARK 3 S11: 0.2680 S12: 0.4810 S13: -0.0876
REMARK 3 S21: -0.9911 S22: -0.4524 S23: 0.2916
REMARK 3 S31: -0.4422 S32: -0.3336 S33: 0.1666
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 149 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.8118 -43.6675 -23.9385
REMARK 3 T TENSOR
REMARK 3 T11: 0.8860 T22: 0.2928
REMARK 3 T33: 0.4459 T12: 0.1790
REMARK 3 T13: 0.3819 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 2.0476 L22: 2.6131
REMARK 3 L33: 1.0864 L12: -0.9971
REMARK 3 L13: -0.9217 L23: 1.0131
REMARK 3 S TENSOR
REMARK 3 S11: 0.1445 S12: 0.2052 S13: 0.0222
REMARK 3 S21: -0.4381 S22: -0.0961 S23: -0.1223
REMARK 3 S31: -0.2193 S32: -0.0473 S33: -0.0328
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 178 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.5608 -44.9335 -26.6151
REMARK 3 T TENSOR
REMARK 3 T11: 1.0865 T22: 0.4936
REMARK 3 T33: 0.5074 T12: 0.1000
REMARK 3 T13: -0.1994 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 2.3547 L22: 2.1404
REMARK 3 L33: 2.3835 L12: -0.1320
REMARK 3 L13: -2.3686 L23: 0.0860
REMARK 3 S TENSOR
REMARK 3 S11: 0.3461 S12: 0.8309 S13: -0.5293
REMARK 3 S21: -0.5665 S22: -0.2668 S23: -0.0417
REMARK 3 S31: 1.0179 S32: -0.5823 S33: -0.0804
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.6463 -47.1496 73.7845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.4926
REMARK 3 T33: 0.2333 T12: -0.0178
REMARK 3 T13: -0.0435 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 4.8525 L22: 5.2095
REMARK 3 L33: 8.4559 L12: 0.4536
REMARK 3 L13: 1.7711 L23: -2.1473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: -0.6918 S13: 0.0958
REMARK 3 S21: 0.3755 S22: -0.0941 S23: -0.1791
REMARK 3 S31: -0.4900 S32: 0.2938 S33: 0.1727
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.9557 -70.8727 79.5813
REMARK 3 T TENSOR
REMARK 3 T11: 0.3153 T22: 0.7089
REMARK 3 T33: 0.7771 T12: 0.0185
REMARK 3 T13: -0.0278 T23: 0.4381
REMARK 3 L TENSOR
REMARK 3 L11: 3.7313 L22: 1.0064
REMARK 3 L33: 1.4198 L12: -1.7858
REMARK 3 L13: 1.3422 L23: -1.0192
REMARK 3 S TENSOR
REMARK 3 S11: 0.0376 S12: -0.6295 S13: -0.9668
REMARK 3 S21: 0.0943 S22: 0.2925 S23: 0.3500
REMARK 3 S31: 0.2371 S32: -0.4536 S33: -0.3293
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 57 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.9887 -68.2408 77.4571
REMARK 3 T TENSOR
REMARK 3 T11: 0.2057 T22: 0.6376
REMARK 3 T33: 0.6793 T12: 0.0825
REMARK 3 T13: -0.0382 T23: 0.2587
REMARK 3 L TENSOR
REMARK 3 L11: 4.2723 L22: 1.1591
REMARK 3 L33: 1.2654 L12: -0.8681
REMARK 3 L13: 1.0877 L23: -0.2470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.6200 S13: -0.7037
REMARK 3 S21: 0.1438 S22: 0.1928 S23: 0.2380
REMARK 3 S31: 0.1957 S32: -0.3006 S33: -0.2034
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 67 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.7217 -58.3188 75.2367
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 0.5672
REMARK 3 T33: 0.3443 T12: -0.0420
REMARK 3 T13: -0.0729 T23: 0.1639
REMARK 3 L TENSOR
REMARK 3 L11: 1.9433 L22: 0.8519
REMARK 3 L33: 0.6203 L12: 0.6028
REMARK 3 L13: -0.0898 L23: -0.2333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: -0.2844 S13: -0.2518
REMARK 3 S21: 0.0225 S22: -0.0400 S23: 0.2175
REMARK 3 S31: 0.0695 S32: -0.1562 S33: 0.0173
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 96 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.7059 -62.8506 88.1444
REMARK 3 T TENSOR
REMARK 3 T11: 0.3444 T22: 1.2869
REMARK 3 T33: 0.6359 T12: 0.0660
REMARK 3 T13: 0.0460 T23: 0.4491
REMARK 3 L TENSOR
REMARK 3 L11: 0.1118 L22: 0.3195
REMARK 3 L33: 0.0297 L12: -0.1874
REMARK 3 L13: 0.0308 L23: -0.0553
REMARK 3 S TENSOR
REMARK 3 S11: -0.1001 S12: -0.3716 S13: -0.3978
REMARK 3 S21: 0.0691 S22: 0.0008 S23: 0.0677
REMARK 3 S31: 0.1307 S32: -0.0060 S33: 0.0210
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 126 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.9858 -52.9696 82.5530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.8429
REMARK 3 T33: 0.2584 T12: 0.0675
REMARK 3 T13: -0.0119 T23: 0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 7.1213 L22: 2.9980
REMARK 3 L33: 1.0049 L12: 3.6424
REMARK 3 L13: 0.3633 L23: -0.0850
REMARK 3 S TENSOR
REMARK 3 S11: -0.0941 S12: -0.4323 S13: 0.4862
REMARK 3 S21: 0.0315 S22: 0.1094 S23: 0.3828
REMARK 3 S31: -0.0412 S32: 0.0112 S33: 0.0500
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 139 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.5594 -57.8408 89.8891
REMARK 3 T TENSOR
REMARK 3 T11: 0.2217 T22: 1.0915
REMARK 3 T33: 0.4184 T12: -0.0327
REMARK 3 T13: -0.0189 T23: 0.2450
REMARK 3 L TENSOR
REMARK 3 L11: 1.3002 L22: 0.5043
REMARK 3 L33: 0.5811 L12: -0.5389
REMARK 3 L13: -0.0786 L23: -0.3712
REMARK 3 S TENSOR
REMARK 3 S11: 0.1690 S12: -0.9968 S13: -0.1947
REMARK 3 S21: 0.2162 S22: 0.0038 S23: 0.0342
REMARK 3 S31: 0.0438 S32: 0.1072 S33: -0.0067
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 174 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.9515 -48.9720 95.0548
REMARK 3 T TENSOR
REMARK 3 T11: 0.4795 T22: 1.6151
REMARK 3 T33: 0.4077 T12: 0.0741
REMARK 3 T13: -0.0296 T23: -0.0874
REMARK 3 L TENSOR
REMARK 3 L11: 1.2416 L22: 2.4220
REMARK 3 L33: 5.5466 L12: 1.5877
REMARK 3 L13: 2.3117 L23: 2.2589
REMARK 3 S TENSOR
REMARK 3 S11: -0.0734 S12: -0.3636 S13: 0.0850
REMARK 3 S21: 0.4069 S22: -0.1379 S23: -0.0492
REMARK 3 S31: -0.1231 S32: -0.1926 S33: 0.1915
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 188 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.6812 -60.1385 99.2234
REMARK 3 T TENSOR
REMARK 3 T11: 0.4150 T22: 1.3599
REMARK 3 T33: 0.6362 T12: -0.0251
REMARK 3 T13: 0.0184 T23: 0.4499
REMARK 3 L TENSOR
REMARK 3 L11: 0.3365 L22: 5.9369
REMARK 3 L33: 2.8268 L12: -0.6114
REMARK 3 L13: -0.2953 L23: -2.9830
REMARK 3 S TENSOR
REMARK 3 S11: -0.5574 S12: -0.7141 S13: -0.4250
REMARK 3 S21: 0.5136 S22: 0.9560 S23: 0.8288
REMARK 3 S31: -0.1528 S32: -0.0535 S33: -0.4183
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 5J5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72989
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 2.660
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
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: 1L8B
REMARK 200
REMARK 200 REMARK: THIN PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 2% 1,4-DIOXANE, 0.1 M
REMARK 280 TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 VAL A 28
REMARK 465 ALA A 29
REMARK 465 ASN A 30
REMARK 465 LYS A 206
REMARK 465 SER A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 VAL B 28
REMARK 465 ALA B 29
REMARK 465 ASN B 30
REMARK 465 LYS B 206
REMARK 465 SER B 207
REMARK 465 GLY B 208
REMARK 465 SER B 209
REMARK 465 THR B 210
REMARK 465 THR B 211
REMARK 465 VAL C 28
REMARK 465 ALA C 29
REMARK 465 ASN C 30
REMARK 465 GLU C 171
REMARK 465 ASN C 172
REMARK 465 ARG C 173
REMARK 465 ASP C 174
REMARK 465 ALA C 175
REMARK 465 PRO C 191
REMARK 465 LYS C 192
REMARK 465 ILE C 193
REMARK 465 VAL C 194
REMARK 465 ILE C 195
REMARK 465 GLY C 196
REMARK 465 TYR C 197
REMARK 465 GLN C 198
REMARK 465 SER C 199
REMARK 465 HIS C 200
REMARK 465 ALA C 201
REMARK 465 ASP C 202
REMARK 465 THR C 203
REMARK 465 ALA C 204
REMARK 465 THR C 205
REMARK 465 LYS C 206
REMARK 465 SER C 207
REMARK 465 GLY C 208
REMARK 465 SER C 209
REMARK 465 THR C 210
REMARK 465 THR C 211
REMARK 465 LYS C 212
REMARK 465 ASN C 213
REMARK 465 ARG C 214
REMARK 465 PHE C 215
REMARK 465 VAL C 216
REMARK 465 VAL C 217
REMARK 465 VAL D 28
REMARK 465 ALA D 29
REMARK 465 ASN D 30
REMARK 465 PRO D 87
REMARK 465 GLY D 88
REMARK 465 LYS D 108
REMARK 465 ARG D 109
REMARK 465 GLY D 110
REMARK 465 ASP D 148
REMARK 465 GLU D 169
REMARK 465 CYS D 170
REMARK 465 GLU D 171
REMARK 465 PRO D 191
REMARK 465 LYS D 192
REMARK 465 ILE D 193
REMARK 465 VAL D 194
REMARK 465 ILE D 195
REMARK 465 GLY D 196
REMARK 465 ALA D 204
REMARK 465 THR D 205
REMARK 465 LYS D 206
REMARK 465 SER D 207
REMARK 465 GLY D 208
REMARK 465 SER D 209
REMARK 465 THR D 210
REMARK 465 THR D 211
REMARK 465 LYS D 212
REMARK 465 VAL D 217
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 GLU A 32 CG CD OE1 OE2
REMARK 470 HIS A 33 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 192 NZ
REMARK 470 THR A 211 OG1 CG2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 33 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 LYS B 106 CE NZ
REMARK 470 ARG B 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 192 CG CD CE NZ
REMARK 470 ILE B 193 CG1 CG2 CD1
REMARK 470 VAL B 194 CG1 CG2
REMARK 470 ARG B 214 CZ NH1 NH2
REMARK 470 HIS C 33 CG ND1 CD2 CE1 NE2
REMARK 470 PHE C 48 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 49 CG CD CE NZ
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 GLN C 57 CG CD OE1 NE2
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 90 CG OD1 OD2
REMARK 470 TRP C 102 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 102 CZ3 CH2
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 LYS C 108 CG CD CE NZ
REMARK 470 ARG C 109 CG CD NE CZ NH1 NH2
REMARK 470 TRP C 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 113 CZ3 CH2
REMARK 470 LYS C 119 CD CE NZ
REMARK 470 ARG C 122 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 128 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 143 CG OD1 OD2
REMARK 470 ASP C 144 CG OD1 OD2
REMARK 470 SER C 146 OG
REMARK 470 ASP C 147 CG OD1 OD2
REMARK 470 LYS C 159 CG CD CE NZ
REMARK 470 VAL C 176 CG1 CG2
REMARK 470 THR C 177 OG1 CG2
REMARK 470 ILE C 179 CG1 CG2 CD1
REMARK 470 ARG C 181 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 182 CG1 CG2
REMARK 470 LEU C 189 CG CD1 CD2
REMARK 470 GLU D 32 CG CD OE1 OE2
REMARK 470 HIS D 33 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 49 NZ
REMARK 470 ASN D 50 CG OD1 ND2
REMARK 470 ASP D 51 CG OD1 OD2
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 TRP D 56 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 56 CZ3 CH2
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 MET D 86 CG SD CE
REMARK 470 ASP D 90 OD1 OD2
REMARK 470 GLU D 105 CG CD OE1 OE2
REMARK 470 TRP D 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 113 CZ3 CH2
REMARK 470 LEU D 114 CD1 CD2
REMARK 470 LEU D 117 CG CD1 CD2
REMARK 470 TYR D 145 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER D 146 OG
REMARK 470 LYS D 159 CG CD CE NZ
REMARK 470 LYS D 162 CG CD CE NZ
REMARK 470 ILE D 163 CG1 CG2 CD1
REMARK 470 ILE D 165 CG1 CG2 CD1
REMARK 470 THR D 167 OG1 CG2
REMARK 470 ARG D 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 184 CG CD CE NZ
REMARK 470 TYR D 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER D 199 OG
REMARK 470 HIS D 200 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 214 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 215 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 216 CG1 CG2
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 HOH A 456 O HOH A 489 2.09
REMARK 500 O HOH A 452 O HOH A 472 2.14
REMARK 500 O HOH B 457 O HOH B 509 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 99 C PRO A 100 N 0.133
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 67 21.09 -145.47
REMARK 500 ASP A 143 -143.42 60.79
REMARK 500 ASP A 144 34.40 -87.75
REMARK 500 ILE B 63 -60.42 -90.53
REMARK 500 ASP B 67 23.93 -146.08
REMARK 500 PRO B 100 48.43 -80.90
REMARK 500 ASP B 143 -136.33 57.90
REMARK 500 TYR C 34 -9.62 -153.70
REMARK 500 ASP C 51 112.10 -165.95
REMARK 500 ILE C 63 -63.58 -91.89
REMARK 500 ASP C 67 19.66 -146.70
REMARK 500 ASP C 143 -122.55 54.58
REMARK 500 TYR C 145 40.73 -80.19
REMARK 500 THR C 177 -63.18 -103.66
REMARK 500 GLU D 32 8.32 -69.50
REMARK 500 ILE D 63 -83.55 -88.02
REMARK 500 ASP D 67 22.36 -144.10
REMARK 500 PRO D 100 75.57 -66.80
REMARK 500 ASN D 118 -162.85 -115.90
REMARK 500 ASP D 143 -125.14 58.45
REMARK 500 CYS D 150 -62.34 -105.33
REMARK 500 ARG D 214 -74.43 -113.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 90 TYR B 91 149.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 6G6 A 300
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G6 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G6 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
DBREF 5J5Y A 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5Y B 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5Y C 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5Y D 28 217 UNP P63073 IF4E_MOUSE 28 217
SEQRES 1 A 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 A 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 A 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 A 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 A 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 A 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 A 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 A 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 A 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 A 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 A 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 A 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 A 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 A 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 A 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 B 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 B 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 B 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 B 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 B 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 B 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 B 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 B 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 B 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 B 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 B 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 B 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 B 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 B 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 B 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 C 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 C 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 C 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 C 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 C 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 C 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 C 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 C 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 C 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 C 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 C 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 C 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 C 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 C 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 C 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 D 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 D 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 D 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 D 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 D 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 D 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 D 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 D 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 D 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 D 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 D 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 D 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 D 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 D 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 D 190 THR THR LYS ASN ARG PHE VAL VAL
HET 6G6 A 300 36
HET 6G6 B 301 40
HET GOL B 302 6
HETNAM 6G6 2-AMINO-9-{5-O-[(R)-{[(S)-{DICHLORO[(R)-
HETNAM 2 6G6 HYDROXY(PHOSPHONOOXY)PHOSPHORYL]METHYL}(HYDROXY)
HETNAM 3 6G6 PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]-2-O-METHYL-BETA-D-
HETNAM 4 6G6 RIBOFURANOSYL}-7-METHYL-9H-PURIN-7-IUM-6-OLATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 6G6 2(C13 H21 CL2 N5 O16 P4)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *269(H2 O)
HELIX 1 AA1 TRP A 56 ALA A 58 5 3
HELIX 2 AA2 VAL A 69 ILE A 79 1 11
HELIX 3 AA3 LEU A 81 LEU A 85 5 5
HELIX 4 AA4 GLN A 120 ASP A 125 1 6
HELIX 5 AA5 ASP A 125 GLY A 139 1 15
HELIX 6 AA6 PHE A 142 ASP A 147 5 6
HELIX 7 AA7 ASN A 172 LEU A 187 1 16
HELIX 8 AA8 HIS A 200 ALA A 204 1 5
HELIX 9 AA9 TRP B 56 ALA B 58 5 3
HELIX 10 AB1 VAL B 69 ILE B 79 1 11
HELIX 11 AB2 LEU B 81 LEU B 85 5 5
HELIX 12 AB3 GLN B 120 ASP B 125 1 6
HELIX 13 AB4 ASP B 125 GLY B 139 1 15
HELIX 14 AB5 PHE B 142 ASP B 147 5 6
HELIX 15 AB6 ASN B 172 LEU B 187 1 16
HELIX 16 AB7 HIS B 200 ALA B 204 1 5
HELIX 17 AB8 THR C 55 ASN C 59 1 5
HELIX 18 AB9 VAL C 69 ILE C 79 1 11
HELIX 19 AC1 LEU C 81 LEU C 85 5 5
HELIX 20 AC2 ASP C 104 LYS C 108 5 5
HELIX 21 AC3 GLN C 120 ASP C 125 1 6
HELIX 22 AC4 ASP C 125 GLY C 139 1 15
HELIX 23 AC5 THR C 177 LEU C 187 1 11
HELIX 24 AC6 TRP D 56 ALA D 58 5 3
HELIX 25 AC7 VAL D 69 ILE D 79 1 11
HELIX 26 AC8 LEU D 81 LEU D 85 5 5
HELIX 27 AC9 GLN D 120 ASP D 125 1 6
HELIX 28 AD1 ASP D 125 GLY D 139 1 15
HELIX 29 AD2 PHE D 142 SER D 146 5 5
HELIX 30 AD3 ARG D 173 GLY D 188 1 16
SHEET 1 AA1 8 LEU A 60 THR A 68 0
SHEET 2 AA1 8 PRO A 38 PHE A 48 -1 N LEU A 45 O SER A 64
SHEET 3 AA1 8 ASP A 90 LYS A 95 -1 O SER A 92 N TRP A 46
SHEET 4 AA1 8 VAL A 149 ASN A 155 -1 O ALA A 152 N LEU A 93
SHEET 5 AA1 8 LYS A 162 THR A 167 -1 O TRP A 166 N GLY A 151
SHEET 6 AA1 8 GLY A 111 THR A 116 -1 N ILE A 115 O ILE A 163
SHEET 7 AA1 8 ILE A 195 SER A 199 -1 O GLN A 198 N ARG A 112
SHEET 8 AA1 8 PHE A 215 VAL A 217 -1 O PHE A 215 N TYR A 197
SHEET 1 AA2 8 LEU B 60 THR B 68 0
SHEET 2 AA2 8 PRO B 38 PHE B 48 -1 N PHE B 47 O ARG B 61
SHEET 3 AA2 8 ASP B 90 LYS B 95 -1 O SER B 92 N TRP B 46
SHEET 4 AA2 8 VAL B 149 ASN B 155 -1 O VAL B 154 N TYR B 91
SHEET 5 AA2 8 LYS B 162 THR B 167 -1 O LYS B 162 N ASN B 155
SHEET 6 AA2 8 GLY B 111 THR B 116 -1 N ILE B 115 O ILE B 163
SHEET 7 AA2 8 ILE B 195 SER B 199 -1 O GLY B 196 N LEU B 114
SHEET 8 AA2 8 PHE B 215 VAL B 217 -1 O VAL B 217 N ILE B 195
SHEET 1 AA3 6 LEU C 60 THR C 68 0
SHEET 2 AA3 6 PRO C 38 PHE C 48 -1 N LEU C 39 O ASP C 67
SHEET 3 AA3 6 CYS C 89 LYS C 95 -1 O SER C 92 N TRP C 46
SHEET 4 AA3 6 VAL C 149 VAL C 156 -1 O ALA C 152 N LEU C 93
SHEET 5 AA3 6 ASP C 161 THR C 167 -1 O LYS C 162 N ASN C 155
SHEET 6 AA3 6 GLY C 111 LEU C 117 -1 N ILE C 115 O ILE C 163
SHEET 1 AA4 6 LEU D 60 THR D 68 0
SHEET 2 AA4 6 PRO D 38 PHE D 48 -1 N TRP D 43 O PHE D 66
SHEET 3 AA4 6 ASP D 90 LYS D 95 -1 O SER D 92 N TRP D 46
SHEET 4 AA4 6 GLY D 151 ASN D 155 -1 O ALA D 152 N LEU D 93
SHEET 5 AA4 6 LYS D 162 TRP D 166 -1 O LYS D 162 N ASN D 155
SHEET 6 AA4 6 ARG D 112 THR D 116 -1 N TRP D 113 O ILE D 165
SITE 1 AC1 11 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC1 11 ASP A 143 ARG A 157 LYS A 162 HOH A 429
SITE 3 AC1 11 HOH A 461 HOH A 464 HOH A 478
SITE 1 AC2 10 TRP B 56 MET B 101 TRP B 102 GLU B 103
SITE 2 AC2 10 ARG B 157 LYS B 159 HOH B 422 HOH B 425
SITE 3 AC2 10 HOH B 453 HOH B 471
SITE 1 AC3 5 LYS B 95 ILE B 98 GLN B 120 ASP B 147
SITE 2 AC3 5 VAL B 149
CRYST1 38.040 38.060 146.740 88.36 95.63 103.54 P 1 4
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 0.026288 0.006333 0.002552 0.00000
SCALE2 0.000000 0.027026 -0.000160 0.00000
SCALE3 0.000000 0.000000 0.006848 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
