HEADER TRANSLATION 03-APR-16 5J5O
TITLE TRANSLATION INITIATION FACTOR 4E IN COMPLEX WITH M7GPPPPG MRNA 5' CAP
TITLE 2 ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 28-217;
COMPND 5 SYNONYM: MRNA CAP-BINDING PROTEIN,EIF-4F 25 KDA SUBUNIT;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE 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,
KEYWDS 2 M7GPPPPG, MRNA 5' CAP ANALOG, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WARMINSKI,E.NOWAK,A.M.RYDZIK,J.KOWALSKA,J.JEMIELITY,M.NOWOTNY
REVDAT 4 10-JAN-24 5J5O 1 REMARK
REVDAT 3 27-SEP-17 5J5O 1 JRNL
REVDAT 2 12-JUL-17 5J5O 1
REVDAT 1 10-MAY-17 5J5O 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. 1.87 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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 60257
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.710
REMARK 3 FREE R VALUE TEST SET COUNT : 2234
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 36.8268 - 4.7022 0.97 3846 149 0.2171 0.2386
REMARK 3 2 4.7022 - 3.7334 0.98 3937 151 0.1951 0.2174
REMARK 3 3 3.7334 - 3.2618 0.98 3930 151 0.1980 0.2392
REMARK 3 4 3.2618 - 2.9637 0.98 3850 148 0.2122 0.2736
REMARK 3 5 2.9637 - 2.7514 0.99 3927 152 0.2217 0.2719
REMARK 3 6 2.7514 - 2.5892 0.99 3975 153 0.2304 0.2626
REMARK 3 7 2.5892 - 2.4596 0.96 3824 147 0.2294 0.2945
REMARK 3 8 2.4596 - 2.3525 0.96 3753 144 0.2397 0.2763
REMARK 3 9 2.3525 - 2.2620 0.94 3747 144 0.2277 0.3186
REMARK 3 10 2.2620 - 2.1839 0.91 3649 141 0.2365 0.3256
REMARK 3 11 2.1839 - 2.1156 0.90 3491 134 0.2399 0.2559
REMARK 3 12 2.1156 - 2.0552 0.87 3492 135 0.2358 0.2807
REMARK 3 13 2.0552 - 2.0011 0.83 3250 125 0.2406 0.2809
REMARK 3 14 2.0011 - 1.9522 0.80 3272 126 0.2493 0.2771
REMARK 3 15 1.9522 - 1.9079 0.80 3120 120 0.2635 0.3224
REMARK 3 16 1.9079 - 1.8673 0.74 2960 114 0.2913 0.3714
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) : 27.990
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 : 0.008 6212
REMARK 3 ANGLE : 1.031 8502
REMARK 3 CHIRALITY : 0.056 902
REMARK 3 PLANARITY : 0.006 1063
REMARK 3 DIHEDRAL : 18.227 3645
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): -44.6156 78.3776 -4.3929
REMARK 3 T TENSOR
REMARK 3 T11: 0.1534 T22: 0.0798
REMARK 3 T33: 0.4548 T12: -0.0683
REMARK 3 T13: 0.0016 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 2.1266 L22: 6.3177
REMARK 3 L33: 3.0788 L12: 2.8987
REMARK 3 L13: 0.4781 L23: 1.7344
REMARK 3 S TENSOR
REMARK 3 S11: 0.2426 S12: -0.1030 S13: -0.2096
REMARK 3 S21: 0.4188 S22: -0.0279 S23: -0.7823
REMARK 3 S31: 0.0898 S32: 0.3069 S33: -0.2439
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.6807 70.1535 -11.1414
REMARK 3 T TENSOR
REMARK 3 T11: 0.1847 T22: 0.0637
REMARK 3 T33: 0.2454 T12: 0.0208
REMARK 3 T13: 0.0077 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 4.3195 L22: 0.4146
REMARK 3 L33: 0.4625 L12: -1.1388
REMARK 3 L13: 0.5326 L23: -0.3294
REMARK 3 S TENSOR
REMARK 3 S11: 0.1330 S12: -0.0595 S13: -0.3959
REMARK 3 S21: -0.0288 S22: 0.0156 S23: 0.1966
REMARK 3 S31: -0.0438 S32: -0.1344 S33: -0.1108
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.3597 72.1714 -5.2460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1790 T22: 0.0805
REMARK 3 T33: 0.1982 T12: 0.0091
REMARK 3 T13: -0.0020 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 4.7290 L22: 2.3157
REMARK 3 L33: 0.5544 L12: 0.7249
REMARK 3 L13: 0.7778 L23: -0.1693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: -0.0580 S13: 0.4971
REMARK 3 S21: 0.1158 S22: -0.0192 S23: 0.0179
REMARK 3 S31: 0.1146 S32: -0.0095 S33: -0.0140
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.5389 66.3919 -16.8855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.0712
REMARK 3 T33: 0.1750 T12: -0.0056
REMARK 3 T13: 0.0234 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 1.1325 L22: 2.2787
REMARK 3 L33: 1.6331 L12: -0.4657
REMARK 3 L13: 0.3758 L23: -0.2748
REMARK 3 S TENSOR
REMARK 3 S11: -0.0661 S12: 0.0745 S13: -0.0187
REMARK 3 S21: -0.1211 S22: 0.0473 S23: -0.0964
REMARK 3 S31: 0.0429 S32: -0.0075 S33: 0.0151
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.4510 66.3836 -23.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1759 T22: 0.0906
REMARK 3 T33: 0.1831 T12: -0.0307
REMARK 3 T13: 0.0257 T23: -0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 1.9087 L22: 4.3682
REMARK 3 L33: 2.1568 L12: 1.0434
REMARK 3 L13: -0.6906 L23: -1.4320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: 0.2048 S13: -0.0305
REMARK 3 S21: -0.3648 S22: 0.0909 S23: 0.0295
REMARK 3 S31: 0.1607 S32: -0.0764 S33: -0.0563
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.8700 65.0779 -27.3197
REMARK 3 T TENSOR
REMARK 3 T11: 0.2233 T22: 0.1775
REMARK 3 T33: 0.2273 T12: -0.0034
REMARK 3 T13: 0.1725 T23: -0.0968
REMARK 3 L TENSOR
REMARK 3 L11: 2.6308 L22: 2.6454
REMARK 3 L33: 1.5048 L12: -0.9936
REMARK 3 L13: 0.7410 L23: -0.7664
REMARK 3 S TENSOR
REMARK 3 S11: 0.1780 S12: 0.3839 S13: -0.0119
REMARK 3 S21: -0.4437 S22: -0.1099 S23: -0.1973
REMARK 3 S31: 0.0750 S32: 0.3471 S33: -0.0393
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 188 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3936 62.9217 -30.4491
REMARK 3 T TENSOR
REMARK 3 T11: 0.3481 T22: 0.2118
REMARK 3 T33: 0.2208 T12: 0.0110
REMARK 3 T13: 0.0195 T23: -0.0991
REMARK 3 L TENSOR
REMARK 3 L11: 1.4169 L22: 2.9620
REMARK 3 L33: 2.4835 L12: -1.9668
REMARK 3 L13: -0.7315 L23: 0.5147
REMARK 3 S TENSOR
REMARK 3 S11: 0.3573 S12: 0.5417 S13: -0.4032
REMARK 3 S21: -0.7887 S22: -0.2654 S23: 0.1219
REMARK 3 S31: 0.0641 S32: -0.0455 S33: -0.0760
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6093 63.1025 -64.1972
REMARK 3 T TENSOR
REMARK 3 T11: 0.1275 T22: 0.2687
REMARK 3 T33: 0.3889 T12: -0.0524
REMARK 3 T13: 0.0830 T23: 0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 5.1256 L22: 2.7205
REMARK 3 L33: 7.2410 L12: 2.3175
REMARK 3 L13: -2.7693 L23: -2.4483
REMARK 3 S TENSOR
REMARK 3 S11: 0.2006 S12: 0.2617 S13: 0.7463
REMARK 3 S21: 0.0778 S22: 0.0570 S23: 0.1356
REMARK 3 S31: -0.6533 S32: 0.1700 S33: -0.3073
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.1507 37.0931 -57.3404
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.1931
REMARK 3 T33: 0.2639 T12: 0.0311
REMARK 3 T13: 0.0769 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 1.7183 L22: 5.8613
REMARK 3 L33: 0.2877 L12: 2.9877
REMARK 3 L13: -0.2250 L23: -0.8029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: 0.0036 S13: -0.2256
REMARK 3 S21: -0.0611 S22: 0.0674 S23: -0.0937
REMARK 3 S31: -0.0191 S32: -0.0080 S33: -0.0224
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0605 47.5997 -57.6331
REMARK 3 T TENSOR
REMARK 3 T11: 0.0861 T22: 0.0834
REMARK 3 T33: 0.1777 T12: 0.0152
REMARK 3 T13: 0.0576 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.9523 L22: 1.3178
REMARK 3 L33: 3.0319 L12: -0.2845
REMARK 3 L13: -0.5578 L23: -0.9221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0422 S12: 0.1340 S13: -0.1202
REMARK 3 S21: -0.0599 S22: -0.0811 S23: -0.0179
REMARK 3 S31: 0.1667 S32: 0.1159 S33: 0.0153
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.8561 51.5426 -49.6876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1441 T22: 0.1908
REMARK 3 T33: 0.3235 T12: 0.0139
REMARK 3 T13: 0.0816 T23: -0.1121
REMARK 3 L TENSOR
REMARK 3 L11: 3.5531 L22: 0.2881
REMARK 3 L33: 0.8558 L12: -0.4269
REMARK 3 L13: 1.6038 L23: -0.3697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: 0.1661 S13: -0.1690
REMARK 3 S21: 0.0877 S22: -0.0233 S23: 0.3631
REMARK 3 S31: 0.0700 S32: -0.0130 S33: 0.0432
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 126 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6961 56.4384 -51.0014
REMARK 3 T TENSOR
REMARK 3 T11: 0.0943 T22: 0.0792
REMARK 3 T33: 0.2002 T12: 0.0189
REMARK 3 T13: 0.0792 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 2.7168 L22: 2.2327
REMARK 3 L33: 1.9961 L12: -1.8638
REMARK 3 L13: -0.3683 L23: -1.1058
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: -0.1127 S13: 0.1845
REMARK 3 S21: 0.1937 S22: -0.0587 S23: -0.0980
REMARK 3 S31: -0.1978 S32: 0.1311 S33: 0.0411
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.4432 47.4403 -45.4343
REMARK 3 T TENSOR
REMARK 3 T11: 0.0981 T22: 0.1421
REMARK 3 T33: 0.2130 T12: -0.0082
REMARK 3 T13: 0.1146 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 8.7122 L22: 1.6825
REMARK 3 L33: 3.1514 L12: 1.5838
REMARK 3 L13: 2.8239 L23: 1.2289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0792 S12: -0.6804 S13: -0.1133
REMARK 3 S21: 0.1426 S22: -0.1015 S23: 0.0266
REMARK 3 S31: 0.2128 S32: -0.2263 S33: 0.0170
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5873 60.3171 -41.8094
REMARK 3 T TENSOR
REMARK 3 T11: 0.2104 T22: 0.1946
REMARK 3 T33: 0.1896 T12: 0.0278
REMARK 3 T13: 0.0869 T23: -0.1363
REMARK 3 L TENSOR
REMARK 3 L11: 0.9908 L22: 1.4514
REMARK 3 L33: 2.9652 L12: -0.6853
REMARK 3 L13: -0.0586 L23: -0.4705
REMARK 3 S TENSOR
REMARK 3 S11: -0.1628 S12: -0.2918 S13: 0.1378
REMARK 3 S21: 0.3506 S22: 0.1526 S23: 0.0291
REMARK 3 S31: -0.3651 S32: -0.0704 S33: -0.0617
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 188 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.3988 50.9589 -38.4198
REMARK 3 T TENSOR
REMARK 3 T11: 0.2776 T22: 0.2439
REMARK 3 T33: 0.1876 T12: 0.0464
REMARK 3 T13: 0.1308 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 1.9996 L22: 3.0659
REMARK 3 L33: 3.7090 L12: -1.4512
REMARK 3 L13: -0.8527 L23: 0.2008
REMARK 3 S TENSOR
REMARK 3 S11: -0.2848 S12: -0.3563 S13: -0.1847
REMARK 3 S21: 0.4322 S22: 0.2192 S23: 0.3184
REMARK 3 S31: 0.2777 S32: -0.1154 S33: 0.0716
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.6847 63.2583 6.8962
REMARK 3 T TENSOR
REMARK 3 T11: 0.4781 T22: 0.2092
REMARK 3 T33: 0.1422 T12: -0.1088
REMARK 3 T13: 0.0374 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 0.3286 L22: 6.7566
REMARK 3 L33: 5.1792 L12: -1.4762
REMARK 3 L13: 0.8042 L23: -4.2760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.1384 S13: -0.1344
REMARK 3 S21: -0.3714 S22: 0.4723 S23: 0.1514
REMARK 3 S31: -0.0013 S32: -0.6664 S33: -0.3858
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6766 46.3963 11.7815
REMARK 3 T TENSOR
REMARK 3 T11: 0.5921 T22: 0.2062
REMARK 3 T33: 0.7386 T12: 0.0059
REMARK 3 T13: -0.3010 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.7393 L22: 2.6006
REMARK 3 L33: 3.4411 L12: 1.3507
REMARK 3 L13: -0.0211 L23: -0.7087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: 0.0448 S13: -0.4357
REMARK 3 S21: 0.3716 S22: -0.0886 S23: -1.0853
REMARK 3 S31: 0.5394 S32: 0.5256 S33: -0.0242
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 67 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.6396 45.3189 15.2940
REMARK 3 T TENSOR
REMARK 3 T11: 0.7341 T22: 0.1307
REMARK 3 T33: 0.3847 T12: -0.1299
REMARK 3 T13: -0.2378 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.1444 L22: 0.9001
REMARK 3 L33: 0.2545 L12: 0.1814
REMARK 3 L13: 0.1099 L23: -0.1621
REMARK 3 S TENSOR
REMARK 3 S11: 0.2209 S12: -0.1875 S13: -0.1103
REMARK 3 S21: 0.7310 S22: -0.1575 S23: -0.3795
REMARK 3 S31: 0.1213 S32: 0.0685 S33: -0.0602
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 143 THROUGH 156 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.0616 52.2407 22.8611
REMARK 3 T TENSOR
REMARK 3 T11: 0.7200 T22: 0.2950
REMARK 3 T33: 0.3816 T12: -0.1339
REMARK 3 T13: -0.3557 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 2.3027 L22: 1.2101
REMARK 3 L33: 3.1281 L12: 1.4304
REMARK 3 L13: 1.8562 L23: 0.8315
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.3860 S13: 0.3213
REMARK 3 S21: 0.1210 S22: -0.2624 S23: 0.0873
REMARK 3 S31: -0.4325 S32: -0.3381 S33: 0.4657
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 157 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.4742 47.0205 26.4732
REMARK 3 T TENSOR
REMARK 3 T11: 1.0117 T22: 0.3002
REMARK 3 T33: 0.2954 T12: -0.2545
REMARK 3 T13: -0.1694 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 1.6760 L22: 0.6861
REMARK 3 L33: 0.4535 L12: 0.9997
REMARK 3 L13: 0.8699 L23: 0.5158
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: -0.3536 S13: 0.2862
REMARK 3 S21: 0.7855 S22: -0.2423 S23: 0.0188
REMARK 3 S31: -0.1086 S32: -0.0957 S33: 0.1606
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 188 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.7667 40.6017 30.0835
REMARK 3 T TENSOR
REMARK 3 T11: 1.2885 T22: 0.8196
REMARK 3 T33: 0.4361 T12: -0.2337
REMARK 3 T13: -0.2624 T23: 0.1331
REMARK 3 L TENSOR
REMARK 3 L11: 0.6629 L22: 1.9632
REMARK 3 L33: 7.0799 L12: -0.6002
REMARK 3 L13: 1.1080 L23: -0.9563
REMARK 3 S TENSOR
REMARK 3 S11: 0.5709 S12: -0.3738 S13: -0.6090
REMARK 3 S21: -0.2455 S22: -0.2193 S23: 0.2909
REMARK 3 S31: 1.8439 S32: -0.8041 S33: -0.3726
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 200 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.3022 43.7769 33.8797
REMARK 3 T TENSOR
REMARK 3 T11: 1.1734 T22: 0.8630
REMARK 3 T33: 0.6038 T12: -0.2273
REMARK 3 T13: -0.3929 T23: 0.2597
REMARK 3 L TENSOR
REMARK 3 L11: 1.4245 L22: 0.3671
REMARK 3 L33: 0.0026 L12: -0.7238
REMARK 3 L13: 0.0621 L23: -0.0318
REMARK 3 S TENSOR
REMARK 3 S11: -0.1678 S12: -0.9412 S13: -0.3533
REMARK 3 S21: 0.1933 S22: 0.3747 S23: 0.1315
REMARK 3 S31: -0.0195 S32: -0.5136 S33: -0.1734
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.0853 47.8015 -75.0018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1593 T22: 0.4134
REMARK 3 T33: 0.1874 T12: 0.0705
REMARK 3 T13: 0.0645 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 5.6117 L22: 4.6211
REMARK 3 L33: 8.6862 L12: 0.8122
REMARK 3 L13: -0.3201 L23: -4.7024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: 0.0395 S13: -0.1495
REMARK 3 S21: -0.4755 S22: -0.3142 S23: -0.3500
REMARK 3 S31: 0.8851 S32: 0.3302 S33: 0.3773
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.0630 72.6324 -81.2567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2597 T22: 0.6290
REMARK 3 T33: 0.8555 T12: 0.0582
REMARK 3 T13: 0.0234 T23: 0.3530
REMARK 3 L TENSOR
REMARK 3 L11: 2.4424 L22: 0.1641
REMARK 3 L33: 1.6730 L12: -0.0215
REMARK 3 L13: 0.6226 L23: -0.5037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0725 S12: 0.6537 S13: 1.3895
REMARK 3 S21: -0.0932 S22: -0.0210 S23: -0.0518
REMARK 3 S31: -0.4732 S32: -0.2862 S33: -0.0223
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 57 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.3688 60.5155 -75.4365
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.4074
REMARK 3 T33: 0.3193 T12: 0.0288
REMARK 3 T13: 0.0557 T23: 0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 3.5758 L22: 0.5673
REMARK 3 L33: 1.4531 L12: -0.7679
REMARK 3 L13: 0.3044 L23: 0.3384
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: 0.5197 S13: 0.8219
REMARK 3 S21: -0.0397 S22: -0.0394 S23: 0.0169
REMARK 3 S31: -0.1859 S32: 0.0023 S33: -0.0165
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 79 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.5269 64.6340 -76.4002
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.5047
REMARK 3 T33: 0.3874 T12: 0.0503
REMARK 3 T13: 0.0766 T23: 0.1832
REMARK 3 L TENSOR
REMARK 3 L11: 5.5164 L22: 0.7302
REMARK 3 L33: 2.1721 L12: -0.0009
REMARK 3 L13: 1.3081 L23: -1.0805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: 0.4283 S13: 0.6650
REMARK 3 S21: -0.0634 S22: 0.1599 S23: 0.2310
REMARK 3 S31: -0.2513 S32: -0.4021 S33: -0.2591
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 89 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2529 66.6455 -85.9557
REMARK 3 T TENSOR
REMARK 3 T11: 0.1426 T22: 0.7193
REMARK 3 T33: 0.4190 T12: 0.0069
REMARK 3 T13: 0.0832 T23: 0.2984
REMARK 3 L TENSOR
REMARK 3 L11: 2.6302 L22: 0.0282
REMARK 3 L33: 0.9368 L12: 0.2685
REMARK 3 L13: -1.1627 L23: -0.0994
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: 0.3988 S13: 0.3417
REMARK 3 S21: -0.0889 S22: 0.0244 S23: -0.0637
REMARK 3 S31: -0.1016 S32: -0.0445 S33: -0.1024
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 105 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.2900 57.4094 -87.8413
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.9075
REMARK 3 T33: 0.2807 T12: 0.0113
REMARK 3 T13: -0.0082 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 2.8712 L22: 0.8337
REMARK 3 L33: 0.3076 L12: 0.5705
REMARK 3 L13: 0.2721 L23: -0.2690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: 0.9293 S13: 0.2995
REMARK 3 S21: -0.2044 S22: -0.0113 S23: 0.0526
REMARK 3 S31: -0.0610 S32: -0.0414 S33: 0.0125
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 143 THROUGH 156 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.3879 57.3105 -91.3968
REMARK 3 T TENSOR
REMARK 3 T11: 0.2718 T22: 0.9652
REMARK 3 T33: 0.3624 T12: 0.0277
REMARK 3 T13: 0.0698 T23: 0.2699
REMARK 3 L TENSOR
REMARK 3 L11: 4.5977 L22: 2.1121
REMARK 3 L33: 2.6878 L12: 0.0765
REMARK 3 L13: -1.8530 L23: -0.7895
REMARK 3 S TENSOR
REMARK 3 S11: -0.1944 S12: 0.7124 S13: -0.0873
REMARK 3 S21: -0.3180 S22: -0.0407 S23: -0.2811
REMARK 3 S31: 0.3217 S32: 0.3265 S33: 0.4278
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 157 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.2492 62.6358 -93.9521
REMARK 3 T TENSOR
REMARK 3 T11: 0.2765 T22: 1.0439
REMARK 3 T33: 0.3167 T12: 0.0365
REMARK 3 T13: 0.0389 T23: 0.2560
REMARK 3 L TENSOR
REMARK 3 L11: 2.3409 L22: 4.1092
REMARK 3 L33: 1.9282 L12: -1.2842
REMARK 3 L13: -0.5395 L23: 0.6712
REMARK 3 S TENSOR
REMARK 3 S11: 0.1988 S12: 0.5325 S13: 0.2018
REMARK 3 S21: -0.3980 S22: 0.0325 S23: -0.2223
REMARK 3 S31: -0.1476 S32: -0.0652 S33: -0.2498
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 173 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.6336 50.6217 -96.9335
REMARK 3 T TENSOR
REMARK 3 T11: 0.4052 T22: 1.2049
REMARK 3 T33: 0.3394 T12: -0.0519
REMARK 3 T13: 0.1054 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.3997 L22: 1.5251
REMARK 3 L33: 1.6627 L12: -0.2029
REMARK 3 L13: -0.8023 L23: 0.1318
REMARK 3 S TENSOR
REMARK 3 S11: -0.1900 S12: 0.3613 S13: -0.1733
REMARK 3 S21: -0.6038 S22: -0.0174 S23: -0.3044
REMARK 3 S31: 0.2044 S32: -0.3233 S33: 0.1884
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 188 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.9322 54.1020 -98.0836
REMARK 3 T TENSOR
REMARK 3 T11: 0.6404 T22: 1.5208
REMARK 3 T33: 0.4871 T12: 0.1542
REMARK 3 T13: -0.0539 T23: 0.2790
REMARK 3 L TENSOR
REMARK 3 L11: 1.6379 L22: 1.1143
REMARK 3 L33: 7.3920 L12: -0.6335
REMARK 3 L13: 0.9701 L23: -1.9769
REMARK 3 S TENSOR
REMARK 3 S11: -0.2397 S12: -0.1239 S13: 0.1647
REMARK 3 S21: -0.6486 S22: 0.4300 S23: 0.6076
REMARK 3 S31: 0.6218 S32: -1.3736 S33: -0.2311
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 200 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.0029 64.1422-103.0068
REMARK 3 T TENSOR
REMARK 3 T11: 0.6509 T22: 1.4573
REMARK 3 T33: 0.7028 T12: -0.0828
REMARK 3 T13: -0.2339 T23: 0.3126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0354 L22: 0.0527
REMARK 3 L33: 0.0111 L12: -0.0431
REMARK 3 L13: 0.0207 L23: -0.0244
REMARK 3 S TENSOR
REMARK 3 S11: -0.3278 S12: 0.4488 S13: 0.3958
REMARK 3 S21: -1.2541 S22: 0.3665 S23: 1.3314
REMARK 3 S31: -0.0468 S32: -0.5186 S33: -0.0185
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 5J5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-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 : 60259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.867
REMARK 200 RESOLUTION RANGE LOW (A) : 36.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
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 (%): 48.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG5000MME, 0.1M TRIS, PH 8.0,
REMARK 280 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 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 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 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 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 THR A 211
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 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 VAL D 28
REMARK 465 ALA D 29
REMARK 465 ASN D 30
REMARK 465 ILE D 195
REMARK 465 GLY D 196
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 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 33 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 109 CD NE CZ NH1 NH2
REMARK 470 LYS A 192 CG CD CE NZ
REMARK 470 HIS B 33 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 54 NZ
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 LYS B 119 CE NZ
REMARK 470 ARG B 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 192 NZ
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 ARG B 214 NE CZ NH1 NH2
REMARK 470 HIS C 33 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 LYS C 54 CE NZ
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 ARG C 109 NE CZ NH1 NH2
REMARK 470 SER C 146 OG
REMARK 470 LYS C 159 CG CD CE NZ
REMARK 470 ARG C 173 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 181 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 184 CG CD CE NZ
REMARK 470 LYS C 192 CG CD CE NZ
REMARK 470 ARG C 214 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 33 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 90 CG OD1 OD2
REMARK 470 TRP D 102 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 102 CZ3 CH2
REMARK 470 LYS D 108 CG CD CE NZ
REMARK 470 ARG D 109 CG CD NE CZ NH1 NH2
REMARK 470 TRP D 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 113 CZ3 CH2
REMARK 470 LEU D 114 CG CD1 CD2
REMARK 470 ASP D 143 CG OD1 OD2
REMARK 470 LYS D 159 CG CD CE NZ
REMARK 470 GLU D 169 CG CD OE1 OE2
REMARK 470 ARG D 173 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 181 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 184 CG CD CE NZ
REMARK 470 GLU D 185 CG CD OE1 OE2
REMARK 470 ARG D 186 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 192 CG CD CE NZ
REMARK 470 ILE D 193 CG1 CG2 CD1
REMARK 470 VAL D 194 CG1 CG2
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 PHE D 215 CG CD1 CD2 CE1 CE2 CZ
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 OE1 GLU D 132 O HOH D 401 2.14
REMARK 500 NZ LYS A 108 O HOH A 401 2.16
REMARK 500 O HOH A 440 O HOH A 526 2.18
REMARK 500 O LYS A 212 O HOH A 402 2.18
REMARK 500 O HOH B 487 O HOH B 488 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 409 O HOH C 416 1545 2.09
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 B 99 C PRO B 100 N 0.134
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 19.37 -142.33
REMARK 500 ASP A 143 -131.58 55.66
REMARK 500 ALA A 204 0.91 -67.48
REMARK 500 TYR B 34 -2.72 -148.30
REMARK 500 ASP B 67 25.76 -145.06
REMARK 500 ASP B 143 -139.50 61.88
REMARK 500 TYR C 34 -5.21 -150.17
REMARK 500 ASP C 51 94.02 -163.34
REMARK 500 ASP C 67 26.84 -155.32
REMARK 500 ASP C 143 -130.61 60.11
REMARK 500 TYR D 34 -3.35 -154.05
REMARK 500 ILE D 63 -71.53 -89.76
REMARK 500 ASP D 67 24.42 -143.43
REMARK 500 ASP D 143 -128.80 57.42
REMARK 500 PRO D 191 6.69 -68.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G0 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G0 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G0 C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6G0 D 300
DBREF 5J5O A 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5O B 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5O C 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5J5O 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 6G0 A 301 37
HET GOL A 302 6
HET 6G0 B 301 37
HET GOL B 302 6
HET 6G0 C 300 37
HET 6G0 D 300 37
HETNAM 6G0 5'-O-[(R)-HYDROXY{[(R)-HYDROXY{[(S)-
HETNAM 2 6G0 HYDROXY(PHOSPHONOOXY)
HETNAM 3 6G0 PHOSPHORYL]OXY}PHOSPHORYL]OXY}PHOSPHORYL]-7-
HETNAM 4 6G0 METHYLGUANOSINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 6G0 4(C11 H20 N5 O17 P4 1+)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *353(H2 O)
HELIX 1 AA1 TRP A 56 ALA A 58 5 3
HELIX 2 AA2 VAL A 69 ASN A 77 1 9
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 VAL B 69 ASN B 77 1 9
HELIX 10 AB1 LEU B 81 LEU B 85 5 5
HELIX 11 AB2 GLN B 120 ASP B 125 1 6
HELIX 12 AB3 ASP B 125 GLY B 139 1 15
HELIX 13 AB4 PHE B 142 ASP B 147 5 6
HELIX 14 AB5 ASN B 172 GLY B 188 1 17
HELIX 15 AB6 HIS B 200 ALA B 204 1 5
HELIX 16 AB7 THR C 55 ASN C 59 1 5
HELIX 17 AB8 VAL C 69 ILE C 79 1 11
HELIX 18 AB9 LEU C 81 LEU C 85 5 5
HELIX 19 AC1 GLN C 120 ASP C 125 1 6
HELIX 20 AC2 ASP C 125 GLY C 139 1 15
HELIX 21 AC3 PHE C 142 ASP C 147 5 6
HELIX 22 AC4 ASN C 172 GLY C 188 1 17
HELIX 23 AC5 ALA C 201 THR C 203 5 3
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 ASP D 104 ARG D 109 1 6
HELIX 28 AD1 GLN D 120 ASP D 125 1 6
HELIX 29 AD2 ASP D 125 GLY D 139 1 15
HELIX 30 AD3 PHE D 142 ASP D 147 5 6
HELIX 31 AD4 ASN D 172 GLY D 188 1 17
HELIX 32 AD5 HIS D 200 ALA D 204 1 5
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 ILE A 63
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 CYS A 150
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 LEU B 45 O ILE B 63
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 GLN B 198 N ARG B 112
SHEET 8 AA2 8 PHE B 215 VAL B 217 -1 O VAL B 217 N ILE B 195
SHEET 1 AA3 8 LEU C 60 THR C 68 0
SHEET 2 AA3 8 PRO C 38 PHE C 48 -1 N TRP C 43 O PHE C 66
SHEET 3 AA3 8 CYS C 89 LYS C 95 -1 O SER C 92 N TRP C 46
SHEET 4 AA3 8 VAL C 149 VAL C 156 -1 O ALA C 152 N LEU C 93
SHEET 5 AA3 8 LYS C 162 THR C 167 -1 O LYS C 162 N ASN C 155
SHEET 6 AA3 8 GLY C 111 THR C 116 -1 N ILE C 115 O ILE C 163
SHEET 7 AA3 8 ILE C 195 SER C 199 -1 O GLY C 196 N LEU C 114
SHEET 8 AA3 8 PHE C 215 VAL C 217 -1 O PHE C 215 N TYR C 197
SHEET 1 AA4 7 LEU D 60 THR D 68 0
SHEET 2 AA4 7 PRO D 38 PHE D 48 -1 N TRP D 43 O PHE D 66
SHEET 3 AA4 7 CYS D 89 LYS D 95 -1 O SER D 92 N TRP D 46
SHEET 4 AA4 7 VAL D 149 VAL D 156 -1 O VAL D 156 N CYS D 89
SHEET 5 AA4 7 LYS D 162 THR D 167 -1 O TRP D 166 N CYS D 150
SHEET 6 AA4 7 GLY D 111 THR D 116 -1 N ILE D 115 O ILE D 163
SHEET 7 AA4 7 GLN D 198 SER D 199 -1 O GLN D 198 N ARG D 112
SITE 1 AC1 15 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC1 15 ARG A 157 LYS A 162 HOH A 409 HOH A 413
SITE 3 AC1 15 HOH A 427 HOH A 429 HOH A 438 HOH A 477
SITE 4 AC1 15 HOH A 480 HOH A 482 HOH A 491
SITE 1 AC2 6 ILE A 115 THR A 116 GLN A 121 ILE A 195
SITE 2 AC2 6 HOH A 407 HOH A 420
SITE 1 AC3 14 TRP B 56 MET B 101 TRP B 102 GLU B 103
SITE 2 AC3 14 ARG B 157 LYS B 159 LYS B 162 HOH B 403
SITE 3 AC3 14 HOH B 413 HOH B 427 HOH B 467 HOH B 468
SITE 4 AC3 14 HOH B 476 HOH B 477
SITE 1 AC4 7 LYS B 95 ILE B 98 LYS B 106 GLN B 120
SITE 2 AC4 7 ASP B 147 VAL B 149 HOH B 405
SITE 1 AC5 7 TRP C 56 PRO C 100 MET C 101 TRP C 102
SITE 2 AC5 7 GLU C 103 ARG C 157 LYS C 162
SITE 1 AC6 6 TRP D 56 MET D 101 TRP D 102 GLU D 103
SITE 2 AC6 6 ARG D 157 LYS D 162
CRYST1 37.990 38.030 146.640 88.55 84.70 76.67 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 0.026323 -0.006238 -0.002415 0.00000
SCALE2 0.000000 0.027023 -0.000111 0.00000
SCALE3 0.000000 0.000000 0.006849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
