HEADER RNA BINDING PROTEIN 28-OCT-16 5M83
TITLE TRANSLATION INITIATION FACTOR 4E IN COMPLEX WITH (RP)-M2(7,2'O)GPPSPA
TITLE 2 MRNA 5' CAP ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A, B;
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: 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, M2(7,
KEYWDS 2 2'O)GPPSPA, PHOSPHOROTHIOATE, MRNA 5' CAP ANALOG, TRANSLATION, RNA
KEYWDS 3 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WARMINSKI,E.NOWAK,J.KOWALSKA,J.JEMIELITY,M.NOWOTNY
REVDAT 2 17-JAN-24 5M83 1 ATOM
REVDAT 1 20-DEC-17 5M83 0
JRNL AUTH M.WARMINSKI,E.NOWAK,D.KUBACKA,J.KOWALSKA,M.NOWOTNY,
JRNL AUTH 2 J.JEMIELITY
JRNL TITL TRANSLATION INITIATION FACTOR 4E IN COMPLEX WITH
JRNL TITL 2 (RP)-M2(7,2'O)GPPSPA MRNA 5' CAP ANALOG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 34740
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.350
REMARK 3 FREE R VALUE TEST SET COUNT : 817
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 37.0758 - 3.3756 1.00 5768 140 0.1785 0.2089
REMARK 3 2 3.3756 - 2.6796 1.00 5682 137 0.2053 0.2484
REMARK 3 3 2.6796 - 2.3409 1.00 5651 136 0.2230 0.3093
REMARK 3 4 2.3409 - 2.1269 1.00 5597 135 0.2268 0.2997
REMARK 3 5 2.1269 - 1.9745 1.00 5642 136 0.2501 0.2925
REMARK 3 6 1.9745 - 1.8581 0.99 5583 133 0.2978 0.3463
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) : 29.010
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 2894
REMARK 3 ANGLE : 0.969 3960
REMARK 3 CHIRALITY : 0.057 421
REMARK 3 PLANARITY : 0.005 497
REMARK 3 DIHEDRAL : 15.316 1662
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -89.6393 -13.9313 45.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.4036 T22: 0.2227
REMARK 3 T33: 0.5823 T12: -0.0126
REMARK 3 T13: -0.0096 T23: -0.0792
REMARK 3 L TENSOR
REMARK 3 L11: 5.3395 L22: 3.3920
REMARK 3 L33: 4.7686 L12: 4.2019
REMARK 3 L13: 2.2673 L23: 2.3481
REMARK 3 S TENSOR
REMARK 3 S11: -0.2733 S12: 0.4547 S13: -0.7290
REMARK 3 S21: -0.0165 S22: 0.4328 S23: -0.5513
REMARK 3 S31: 0.9573 S32: 0.3106 S33: -0.1937
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A):-100.1347 10.2327 49.6310
REMARK 3 T TENSOR
REMARK 3 T11: 0.2173 T22: 0.2434
REMARK 3 T33: 0.3562 T12: -0.0403
REMARK 3 T13: -0.0594 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 5.9246 L22: 8.8493
REMARK 3 L33: 0.4962 L12: -7.0015
REMARK 3 L13: -1.3782 L23: 1.3906
REMARK 3 S TENSOR
REMARK 3 S11: 0.2147 S12: 0.3581 S13: 0.0405
REMARK 3 S21: -0.3082 S22: -0.3552 S23: 0.4710
REMARK 3 S31: -0.0740 S32: -0.1163 S33: 0.1552
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -89.6126 5.2642 45.9938
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.2058
REMARK 3 T33: 0.2401 T12: -0.0444
REMARK 3 T13: -0.0865 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 2.7541 L22: 3.1376
REMARK 3 L33: 2.3412 L12: -0.2565
REMARK 3 L13: -1.9967 L23: -0.7474
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: 0.1338 S13: -0.0674
REMARK 3 S21: -0.1978 S22: -0.0799 S23: -0.0660
REMARK 3 S31: -0.1543 S32: -0.0024 S33: 0.0870
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A):-102.4357 2.9330 61.7696
REMARK 3 T TENSOR
REMARK 3 T11: 0.2717 T22: 0.4028
REMARK 3 T33: 0.2621 T12: -0.0556
REMARK 3 T13: 0.0308 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 8.1285 L22: 6.1554
REMARK 3 L33: 7.5919 L12: -2.8231
REMARK 3 L13: -2.4212 L23: 4.1837
REMARK 3 S TENSOR
REMARK 3 S11: -0.1460 S12: -0.5540 S13: -0.0821
REMARK 3 S21: 0.5652 S22: -0.3350 S23: 0.8488
REMARK 3 S31: 0.4616 S32: -1.0457 S33: 0.4440
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.0549 13.9029 58.8260
REMARK 3 T TENSOR
REMARK 3 T11: 0.4084 T22: 0.4897
REMARK 3 T33: 0.4350 T12: -0.1534
REMARK 3 T13: -0.1647 T23: -0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 0.7510 L22: 1.6585
REMARK 3 L33: 4.0312 L12: -0.7928
REMARK 3 L13: -0.7827 L23: -0.7890
REMARK 3 S TENSOR
REMARK 3 S11: 0.1299 S12: -0.6122 S13: 0.4596
REMARK 3 S21: 0.4040 S22: -0.4499 S23: -0.5425
REMARK 3 S31: -0.6791 S32: 0.4146 S33: 0.2583
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -86.5398 -0.0384 57.3615
REMARK 3 T TENSOR
REMARK 3 T11: 0.1716 T22: 0.2618
REMARK 3 T33: 0.3261 T12: -0.0474
REMARK 3 T13: -0.0992 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 4.2773 L22: 2.4446
REMARK 3 L33: 3.9904 L12: -0.4334
REMARK 3 L13: -1.3060 L23: 1.4818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0127 S12: -0.4930 S13: -0.5257
REMARK 3 S21: 0.2882 S22: -0.1661 S23: -0.3735
REMARK 3 S31: 0.2444 S32: 0.2195 S33: 0.1743
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -87.3764 5.8738 66.7584
REMARK 3 T TENSOR
REMARK 3 T11: 0.3600 T22: 0.5890
REMARK 3 T33: 0.2799 T12: -0.1135
REMARK 3 T13: -0.1436 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 2.0789 L22: 1.3161
REMARK 3 L33: 2.3553 L12: -0.7799
REMARK 3 L13: 1.0855 L23: -1.1201
REMARK 3 S TENSOR
REMARK 3 S11: 0.1225 S12: -1.0071 S13: -0.0146
REMARK 3 S21: 0.5291 S22: -0.0812 S23: -0.2206
REMARK 3 S31: -0.2446 S32: 0.0006 S33: -0.0232
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -89.5687 9.9600 33.7884
REMARK 3 T TENSOR
REMARK 3 T11: 0.3914 T22: 0.4753
REMARK 3 T33: 0.2857 T12: -0.2486
REMARK 3 T13: -0.1013 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 8.3277 L22: 7.5393
REMARK 3 L33: 8.9248 L12: 1.4787
REMARK 3 L13: -6.1431 L23: -0.8846
REMARK 3 S TENSOR
REMARK 3 S11: 0.3973 S12: 0.5059 S13: -0.0413
REMARK 3 S21: -0.3873 S22: 0.1371 S23: 0.1867
REMARK 3 S31: -0.4991 S32: -0.7102 S33: -0.5115
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.1608 4.7951 28.3041
REMARK 3 T TENSOR
REMARK 3 T11: 0.7023 T22: 0.5574
REMARK 3 T33: 1.0323 T12: -0.2135
REMARK 3 T13: 0.3018 T23: -0.3760
REMARK 3 L TENSOR
REMARK 3 L11: 2.5998 L22: 4.4484
REMARK 3 L33: 3.1976 L12: 1.0505
REMARK 3 L13: -0.6573 L23: -1.2272
REMARK 3 S TENSOR
REMARK 3 S11: -0.2704 S12: 0.2754 S13: -0.7970
REMARK 3 S21: -0.5676 S22: 0.2173 S23: -1.6157
REMARK 3 S31: 0.4179 S32: 0.5605 S33: -0.0904
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.3438 15.4838 33.9027
REMARK 3 T TENSOR
REMARK 3 T11: 0.4905 T22: 0.4096
REMARK 3 T33: 0.5138 T12: -0.1991
REMARK 3 T13: 0.1071 T23: -0.2025
REMARK 3 L TENSOR
REMARK 3 L11: 2.0179 L22: 1.8216
REMARK 3 L33: 1.8547 L12: 1.2876
REMARK 3 L13: -0.7003 L23: -0.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.1832 S12: 0.3184 S13: -0.3329
REMARK 3 S21: -0.4107 S22: 0.4749 S23: -0.8157
REMARK 3 S31: -0.0729 S32: 0.3680 S33: -0.2836
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 89 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.7098 4.7169 22.0614
REMARK 3 T TENSOR
REMARK 3 T11: 0.8180 T22: 0.5334
REMARK 3 T33: 0.8464 T12: -0.3944
REMARK 3 T13: 0.3849 T23: -0.4165
REMARK 3 L TENSOR
REMARK 3 L11: 0.5501 L22: 1.7187
REMARK 3 L33: 1.5266 L12: 0.6942
REMARK 3 L13: 0.3359 L23: 1.3006
REMARK 3 S TENSOR
REMARK 3 S11: -0.1736 S12: 0.3939 S13: -0.5512
REMARK 3 S21: -0.4629 S22: 0.3731 S23: -0.6994
REMARK 3 S31: 0.1708 S32: 0.2731 S33: -0.2082
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 105 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.4794 18.6873 17.4559
REMARK 3 T TENSOR
REMARK 3 T11: 1.1124 T22: 0.8379
REMARK 3 T33: 0.6190 T12: -0.5774
REMARK 3 T13: 0.3596 T23: -0.3425
REMARK 3 L TENSOR
REMARK 3 L11: 0.1426 L22: 0.0021
REMARK 3 L33: 0.5064 L12: 0.0187
REMARK 3 L13: 0.2649 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.4281 S12: 0.4314 S13: -0.1741
REMARK 3 S21: -0.6134 S22: 0.4097 S23: -0.2809
REMARK 3 S31: -0.0790 S32: 0.1993 S33: -0.2106
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 126 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -75.6136 18.8193 23.3114
REMARK 3 T TENSOR
REMARK 3 T11: 0.7630 T22: 0.5198
REMARK 3 T33: 0.3094 T12: -0.3143
REMARK 3 T13: 0.1057 T23: -0.0835
REMARK 3 L TENSOR
REMARK 3 L11: 5.8823 L22: 3.7640
REMARK 3 L33: 7.2235 L12: 0.4386
REMARK 3 L13: -1.2219 L23: -0.1769
REMARK 3 S TENSOR
REMARK 3 S11: -0.1835 S12: 0.4029 S13: 0.2619
REMARK 3 S21: -0.9445 S22: 0.4610 S23: 0.0780
REMARK 3 S31: -0.2395 S32: -0.5934 S33: -0.2287
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -70.6912 12.1540 16.3180
REMARK 3 T TENSOR
REMARK 3 T11: 1.0273 T22: 0.8075
REMARK 3 T33: 0.6403 T12: -0.5627
REMARK 3 T13: 0.3792 T23: -0.3419
REMARK 3 L TENSOR
REMARK 3 L11: 3.1345 L22: 2.2070
REMARK 3 L33: 1.0690 L12: 1.2793
REMARK 3 L13: 0.5688 L23: 1.0828
REMARK 3 S TENSOR
REMARK 3 S11: -0.3321 S12: 0.4486 S13: -0.0821
REMARK 3 S21: -0.6943 S22: 0.3250 S23: -0.1018
REMARK 3 S31: 0.1422 S32: -0.1263 S33: 0.2089
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.8215 17.9314 10.4643
REMARK 3 T TENSOR
REMARK 3 T11: 1.4114 T22: 0.8068
REMARK 3 T33: 0.3920 T12: -0.4362
REMARK 3 T13: 0.1467 T23: -0.0989
REMARK 3 L TENSOR
REMARK 3 L11: 4.2522 L22: 4.9748
REMARK 3 L33: 2.9794 L12: -3.4498
REMARK 3 L13: -0.0432 L23: 1.2434
REMARK 3 S TENSOR
REMARK 3 S11: -0.0818 S12: 0.9418 S13: -0.2086
REMARK 3 S21: -0.9734 S22: -0.1293 S23: -0.1793
REMARK 3 S31: -0.0772 S32: -0.0882 S33: 0.1384
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 5M83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200001926.
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 : 34747
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.436
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.45
REMARK 200 R MERGE FOR SHELL (I) : 0.90900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.020
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 PLATE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 10000, 0.2M CH3COONA, 0.1M
REMARK 280 TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 23.53000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.87000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 23.53000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.87000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 462 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 488 LIES ON A SPECIAL POSITION.
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 PRO B 190
REMARK 465 PRO B 191
REMARK 465 ALA B 204
REMARK 465 THR B 205
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 LYS B 212
REMARK 465 ASN B 213
REMARK 465 ARG B 214
REMARK 465 PHE B 215
REMARK 465 VAL B 216
REMARK 465 VAL B 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 GLN A 57 CD OE1 NE2
REMARK 470 LYS A 106 CE NZ
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 185 CG CD OE1 OE2
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 ILE A 193 CG1 CG2 CD1
REMARK 470 VAL A 194 CG1 CG2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 PHE A 215 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 ILE B 35 CD1
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 ASN B 50 CG OD1 ND2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 THR B 55 OG1 CG2
REMARK 470 GLN B 57 CG CD OE1 NE2
REMARK 470 LEU B 60 CD1 CD2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 63 CG1 CG2 CD1
REMARK 470 ASP B 90 CG OD1 OD2
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 LYS B 106 CG CD CE NZ
REMARK 470 LYS B 108 CG CD CE NZ
REMARK 470 ARG B 109 CG CD NE CZ NH1 NH2
REMARK 470 THR B 116 OG1 CG2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 ARG B 122 CZ NH1 NH2
REMARK 470 ASP B 144 CG OD1 OD2
REMARK 470 TYR B 145 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 146 OG
REMARK 470 VAL B 156 CG1 CG2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 162 NZ
REMARK 470 ILE B 165 CG1 CG2 CD1
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 GLU B 171 CG CD OE1 OE2
REMARK 470 ARG B 173 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 174 CG OD1 OD2
REMARK 470 ARG B 181 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 182 CG1 CG2
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 GLU B 185 CG CD OE1 OE2
REMARK 470 ARG B 186 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 ILE B 195 CG1 CG2 CD1
REMARK 470 TYR B 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 199 OG
REMARK 470 HIS B 200 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 203 OG1 CG2
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 NH2 ARG A 109 OE1 GLU A 169 2156 2.08
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 0.150
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 21.27 -143.87
REMARK 500 ASP A 143 -136.89 60.69
REMARK 500 ASP B 67 25.61 -146.81
REMARK 500 ASP B 125 -30.18 -130.14
REMARK 500 ASP B 143 -139.80 62.85
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 YDZ A 301
REMARK 610 YDZ B 300
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YDZ 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 YDZ B 300
DBREF 5M83 A 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 5M83 B 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
HET YDZ A 301 34
HET GOL A 302 6
HET YDZ B 300 34
HETNAM YDZ [[[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-
HETNAM 2 YDZ BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-
HETNAM 3 YDZ PHOSPHORYL]OXY-SULFANYL-PHOSPHORYL] [(2~{R},3~{R},
HETNAM 4 YDZ 4~{R},5~{R})-5-(2-AZANYL-7-METHYL-6-OXIDANYL-PURIN-7-
HETNAM 5 YDZ IUM-9-YL)-4-METHOXY-3-OXIDANYL-OXOLAN-2-YL]METHYL
HETNAM 6 YDZ HYDROGEN PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 YDZ 2(C22 H32 N10 O16 P3 S 1+)
FORMUL 4 GOL C3 H8 O3
FORMUL 6 HOH *151(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 GLY A 188 1 17
HELIX 8 AA8 HIS A 200 ALA A 204 1 5
HELIX 9 AA9 THR B 55 ASN B 59 1 5
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 ASP B 104 ARG B 109 1 6
HELIX 13 AB4 GLN B 120 ASP B 125 1 6
HELIX 14 AB5 ASP B 125 GLY B 139 1 15
HELIX 15 AB6 PHE B 142 ASP B 147 5 6
HELIX 16 AB7 ASN B 172 GLY B 188 1 17
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 CYS A 150 N LYS A 95
SHEET 5 AA1 8 ASP A 161 THR A 167 -1 O LYS A 162 N ASN A 155
SHEET 6 AA1 8 GLY A 111 LEU A 117 -1 N ILE A 115 O ILE A 163
SHEET 7 AA1 8 ILE A 195 SER A 199 -1 O GLY A 196 N LEU A 114
SHEET 8 AA1 8 PHE A 215 VAL A 217 -1 O PHE A 215 N TYR A 197
SHEET 1 AA2 7 LEU B 60 THR B 68 0
SHEET 2 AA2 7 PRO B 38 LYS B 49 -1 N LEU B 39 O ASP B 67
SHEET 3 AA2 7 CYS B 89 LYS B 95 -1 O SER B 92 N TRP B 46
SHEET 4 AA2 7 VAL B 149 VAL B 156 -1 O VAL B 156 N CYS B 89
SHEET 5 AA2 7 LYS B 162 THR B 167 -1 O LYS B 162 N ASN B 155
SHEET 6 AA2 7 GLY B 111 THR B 116 -1 N TRP B 113 O ILE B 165
SHEET 7 AA2 7 GLY B 196 SER B 199 -1 O GLN B 198 N ARG B 112
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 408
SITE 3 AC1 11 HOH A 428 HOH A 438 HOH A 465
SITE 1 AC2 4 THR A 116 GLN A 121 ILE A 195 HOH A 401
SITE 1 AC3 7 TRP B 56 MET B 101 TRP B 102 GLU B 103
SITE 2 AC3 7 ARG B 157 LYS B 162 HOH B 424
CRYST1 47.060 59.740 149.180 90.00 96.32 90.00 C 1 2 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 0.021249 0.000000 0.002353 0.00000
SCALE2 0.000000 0.016739 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
