HEADER RNA BINDING PROTEIN 27-DEC-16 5UDJ
TITLE IFIT1 MONOMERIC MUTANT (L457E/L464E) WITH GPPP-AAAA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: IFIT-1,INTERFERON-INDUCED 56 KDA PROTEIN,P56;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RNA (5'-D(*(G3A))-R(P*AP*AP*A)-3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IFIT1, G10P1, IFI56, IFNAI1, ISG56;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 11 ORGANISM_TAXID: 32644
KEYWDS MRNA CAP, GUANOSINE-TRIPHOSPHATE RNA, TETRATRICOPEPTIDE REPEAT, RNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.M.ABBAS,S.MARTINEZ-MONTERO,M.J.DAMHA,B.NAGAR
REVDAT 5 06-MAR-24 5UDJ 1 LINK
REVDAT 4 08-JAN-20 5UDJ 1 SEQADV
REVDAT 3 22-MAR-17 5UDJ 1 JRNL
REVDAT 2 15-MAR-17 5UDJ 1 JRNL
REVDAT 1 01-MAR-17 5UDJ 0
JRNL AUTH Y.M.ABBAS,B.T.LAUDENBACH,S.MARTINEZ-MONTERO,R.CENCIC,
JRNL AUTH 2 M.HABJAN,A.PICHLMAIR,M.J.DAMHA,J.PELLETIER,B.NAGAR
JRNL TITL STRUCTURE OF HUMAN IFIT1 WITH CAPPED RNA REVEALS ADAPTABLE
JRNL TITL 2 MRNA BINDING AND MECHANISMS FOR SENSING N1 AND N2 RIBOSE
JRNL TITL 3 2'-O METHYLATIONS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E2106 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28251928
JRNL DOI 10.1073/PNAS.1612444114
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2142
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 67662
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 3325
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 40.3103 - 4.8690 1.00 2915 162 0.1640 0.1675
REMARK 3 2 4.8690 - 3.8657 1.00 2767 154 0.1322 0.1516
REMARK 3 3 3.8657 - 3.3773 1.00 2747 141 0.1480 0.1659
REMARK 3 4 3.3773 - 3.0687 1.00 2690 155 0.1704 0.1788
REMARK 3 5 3.0687 - 2.8488 1.00 2696 152 0.1635 0.1831
REMARK 3 6 2.8488 - 2.6809 1.00 2693 129 0.1563 0.2104
REMARK 3 7 2.6809 - 2.5466 1.00 2701 142 0.1511 0.1709
REMARK 3 8 2.5466 - 2.4358 1.00 2676 129 0.1429 0.1832
REMARK 3 9 2.4358 - 2.3420 1.00 2683 124 0.1413 0.1797
REMARK 3 10 2.3420 - 2.2612 1.00 2700 127 0.1436 0.1611
REMARK 3 11 2.2612 - 2.1905 1.00 2648 143 0.1399 0.1844
REMARK 3 12 2.1905 - 2.1279 1.00 2661 129 0.1474 0.1592
REMARK 3 13 2.1279 - 2.0719 1.00 2672 140 0.1574 0.1852
REMARK 3 14 2.0719 - 2.0213 1.00 2633 154 0.1675 0.2001
REMARK 3 15 2.0213 - 1.9754 1.00 2646 147 0.1693 0.1809
REMARK 3 16 1.9754 - 1.9333 1.00 2660 122 0.1713 0.2160
REMARK 3 17 1.9333 - 1.8947 1.00 2637 146 0.1718 0.1911
REMARK 3 18 1.8947 - 1.8589 1.00 2675 130 0.1803 0.2110
REMARK 3 19 1.8589 - 1.8257 1.00 2643 119 0.1841 0.1879
REMARK 3 20 1.8257 - 1.7948 1.00 2635 147 0.1970 0.2211
REMARK 3 21 1.7948 - 1.7658 1.00 2628 137 0.2119 0.2492
REMARK 3 22 1.7658 - 1.7387 1.00 2660 132 0.2189 0.2597
REMARK 3 23 1.7387 - 1.7131 1.00 2624 140 0.2361 0.2555
REMARK 3 24 1.7131 - 1.6890 1.00 2647 124 0.2484 0.3033
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.75
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 : 0.014 4077
REMARK 3 ANGLE : 1.283 5524
REMARK 3 CHIRALITY : 0.061 588
REMARK 3 PLANARITY : 0.009 700
REMARK 3 DIHEDRAL : 12.951 2507
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.1348 18.3105-161.0563
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1505
REMARK 3 T33: 0.1575 T12: 0.0039
REMARK 3 T13: -0.0104 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.0619 L22: 0.1671
REMARK 3 L33: 0.1274 L12: 0.1336
REMARK 3 L13: 0.0026 L23: -0.1275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: 0.0890 S13: 0.0521
REMARK 3 S21: -0.0887 S22: -0.0197 S23: -0.0436
REMARK 3 S31: -0.0158 S32: 0.0975 S33: -0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2329 28.7131-156.2124
REMARK 3 T TENSOR
REMARK 3 T11: 0.1472 T22: 0.1162
REMARK 3 T33: 0.1905 T12: -0.0009
REMARK 3 T13: -0.0039 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.2154 L22: 0.2035
REMARK 3 L33: 0.1625 L12: 0.0507
REMARK 3 L13: -0.0219 L23: -0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: 0.0212 S13: 0.1720
REMARK 3 S21: -0.0149 S22: -0.0088 S23: 0.0741
REMARK 3 S31: -0.1102 S32: -0.0710 S33: 0.0034
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5827 6.0519-153.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.1020
REMARK 3 T33: 0.1091 T12: 0.0210
REMARK 3 T13: -0.0022 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.2364 L22: 0.4465
REMARK 3 L33: 0.6356 L12: 0.2814
REMARK 3 L13: -0.0990 L23: -0.1778
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: -0.0400 S13: 0.0075
REMARK 3 S21: 0.0420 S22: 0.0179 S23: 0.0239
REMARK 3 S31: 0.0366 S32: -0.0296 S33: 0.0014
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 285 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7016 -7.4624-176.7911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.1581
REMARK 3 T33: 0.1632 T12: -0.0203
REMARK 3 T13: -0.0208 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0776 L22: 0.0391
REMARK 3 L33: 0.0329 L12: -0.0589
REMARK 3 L13: -0.0040 L23: -0.0074
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: 0.1233 S13: -0.0144
REMARK 3 S21: 0.0230 S22: -0.0072 S23: 0.1612
REMARK 3 S31: 0.0802 S32: -0.0350 S33: -0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 312 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3770 -1.9037-182.5603
REMARK 3 T TENSOR
REMARK 3 T11: 0.1765 T22: 0.1855
REMARK 3 T33: 0.1368 T12: -0.0403
REMARK 3 T13: -0.0103 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.0272 L22: 0.0454
REMARK 3 L33: 0.0477 L12: -0.0452
REMARK 3 L13: -0.0121 L23: -0.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0834 S12: 0.1487 S13: 0.0254
REMARK 3 S21: -0.0229 S22: 0.0845 S23: 0.0250
REMARK 3 S31: -0.0092 S32: -0.0601 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 336 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1243 -5.1364-178.3700
REMARK 3 T TENSOR
REMARK 3 T11: 0.1905 T22: 0.1658
REMARK 3 T33: 0.1303 T12: 0.0128
REMARK 3 T13: -0.0077 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0335 L22: 0.0651
REMARK 3 L33: 0.0256 L12: -0.0694
REMARK 3 L13: -0.0017 L23: 0.0131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0795 S12: 0.0757 S13: 0.0647
REMARK 3 S21: -0.0445 S22: 0.0759 S23: 0.0123
REMARK 3 S31: 0.0627 S32: 0.1565 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 374 THROUGH 412 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0520 -16.8448-173.9806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2513 T22: 0.1908
REMARK 3 T33: 0.1773 T12: 0.0795
REMARK 3 T13: -0.0213 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 0.1315 L22: 0.0751
REMARK 3 L33: 0.1061 L12: -0.0504
REMARK 3 L13: 0.0000 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: 0.0224 S13: -0.0539
REMARK 3 S21: 0.0532 S22: 0.0652 S23: -0.0433
REMARK 3 S31: 0.1622 S32: 0.1349 S33: 0.0717
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 413 THROUGH 467 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0497 -32.9201-170.6066
REMARK 3 T TENSOR
REMARK 3 T11: 0.3116 T22: 0.1587
REMARK 3 T33: 0.3263 T12: 0.0163
REMARK 3 T13: -0.1291 T23: -0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 0.1121 L22: 0.2029
REMARK 3 L33: 0.4811 L12: 0.1290
REMARK 3 L13: -0.1527 L23: -0.2337
REMARK 3 S TENSOR
REMARK 3 S11: 0.2951 S12: -0.0992 S13: -0.2929
REMARK 3 S21: 0.0114 S22: -0.0175 S23: 0.1425
REMARK 3 S31: 0.2000 S32: -0.2899 S33: 0.1910
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 4 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6840 -4.3078-165.9430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1927 T22: 0.1654
REMARK 3 T33: 0.1520 T12: -0.0055
REMARK 3 T13: -0.0030 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0028 L22: 0.0053
REMARK 3 L33: 0.0067 L12: 0.0009
REMARK 3 L13: 0.0052 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: -0.0942 S13: -0.0746
REMARK 3 S21: 0.0477 S22: 0.0354 S23: 0.0889
REMARK 3 S31: 0.0875 S32: 0.0740 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND RESID ' 1 '
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6826 8.3360-160.4128
REMARK 3 T TENSOR
REMARK 3 T11: 0.1439 T22: 0.1252
REMARK 3 T33: 0.1547 T12: 0.0206
REMARK 3 T13: 0.0007 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0027 L22: 0.0050
REMARK 3 L33: 0.0089 L12: -0.0123
REMARK 3 L13: 0.0028 L23: 0.0099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0986 S12: 0.0593 S13: 0.0239
REMARK 3 S21: 0.0153 S22: 0.0417 S23: 0.0268
REMARK 3 S31: 0.0085 S32: -0.0398 S33: 0.0002
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 5UDJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 94
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67695
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.20
REMARK 200 R MERGE FOR SHELL (I) : 0.90400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27 - 32 % PEG 200, 0.1 M TRIS PH 8.1,
REMARK 280 200 MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 2 2
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 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z+1/2
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.73500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.73500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.73500
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 46.73500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -1.000000 0.000000 0.000000 112.53600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 112.53600
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 -280.41000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -280.41000
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 765 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 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 ASN A 4
REMARK 465 GLY A 5
REMARK 465 ASP A 6
REMARK 465 ASP A 7
REMARK 465 ALA A 468
REMARK 465 ASP A 469
REMARK 465 PHE A 470
REMARK 465 GLU A 471
REMARK 465 ASN A 472
REMARK 465 SER A 473
REMARK 465 VAL A 474
REMARK 465 ARG A 475
REMARK 465 GLN A 476
REMARK 465 GLY A 477
REMARK 465 PRO A 478
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 HE ARG A 211 O HOH A 609 1.58
REMARK 500 O HOH A 691 O HOH B 121 1.67
REMARK 500 OD1 ASN A 246 O HOH A 601 2.11
REMARK 500 OD1 ASP A 171 O HOH A 602 2.16
REMARK 500 OE2 GLU A 237 O HOH A 603 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ASP A 189 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 A B 4 N7 - C8 - N9 ANGL. DEV. = -3.1 DEGREES
REMARK 500 A B 4 C8 - N9 - C4 ANGL. DEV. = 3.7 DEGREES
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 GLN A 67 70.02 -118.33
REMARK 500 HIS A 86 37.40 -145.84
REMARK 500 LYS A 433 98.00 -167.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD1
REMARK 620 2 ASP A 47 OD2 53.7
REMARK 620 3 HOH A 608 O 85.3 136.2
REMARK 620 4 HOH A 614 O 124.7 78.7 122.6
REMARK 620 5 HOH A 683 O 89.9 88.4 75.4 59.4
REMARK 620 6 HOH A 788 O 72.4 107.1 68.1 158.1 140.2
REMARK 620 7 HOH A 842 O 110.8 74.4 143.3 76.1 134.7 85.1
REMARK 620 8 HOH A 922 O 155.4 149.7 73.6 78.5 96.8 87.7 81.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 77 OE1
REMARK 620 2 GLU A 77 OE2 50.4
REMARK 620 3 HOH A 900 O 79.4 101.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UDI RELATED DB: PDB
REMARK 900 RELATED ID: 5UDK RELATED DB: PDB
REMARK 900 RELATED ID: 5UDL RELATED DB: PDB
DBREF 5UDJ A 1 478 UNP P09914 IFIT1_HUMAN 1 478
DBREF 5UDJ B 1 4 PDB 5UDJ 5UDJ 1 4
SEQADV 5UDJ SER A 0 UNP P09914 EXPRESSION TAG
SEQADV 5UDJ GLU A 457 UNP P09914 LEU 457 ENGINEERED MUTATION
SEQADV 5UDJ GLU A 464 UNP P09914 LEU 464 ENGINEERED MUTATION
SEQRES 1 A 479 SER MET SER THR ASN GLY ASP ASP HIS GLN VAL LYS ASP
SEQRES 2 A 479 SER LEU GLU GLN LEU ARG CYS HIS PHE THR TRP GLU LEU
SEQRES 3 A 479 SER ILE ASP ASP ASP GLU MET PRO ASP LEU GLU ASN ARG
SEQRES 4 A 479 VAL LEU ASP GLN ILE GLU PHE LEU ASP THR LYS TYR SER
SEQRES 5 A 479 VAL GLY ILE HIS ASN LEU LEU ALA TYR VAL LYS HIS LEU
SEQRES 6 A 479 LYS GLY GLN ASN GLU GLU ALA LEU LYS SER LEU LYS GLU
SEQRES 7 A 479 ALA GLU ASN LEU MET GLN GLU GLU HIS ASP ASN GLN ALA
SEQRES 8 A 479 ASN VAL ARG SER LEU VAL THR TRP GLY ASN PHE ALA TRP
SEQRES 9 A 479 MET TYR TYR HIS MET GLY ARG LEU ALA GLU ALA GLN THR
SEQRES 10 A 479 TYR LEU ASP LYS VAL GLU ASN ILE CYS LYS LYS LEU SER
SEQRES 11 A 479 ASN PRO PHE ARG TYR ARG MET GLU CYS PRO GLU ILE ASP
SEQRES 12 A 479 CYS GLU GLU GLY TRP ALA LEU LEU LYS CYS GLY GLY LYS
SEQRES 13 A 479 ASN TYR GLU ARG ALA LYS ALA CYS PHE GLU LYS VAL LEU
SEQRES 14 A 479 GLU VAL ASP PRO GLU ASN PRO GLU SER SER ALA GLY TYR
SEQRES 15 A 479 ALA ILE SER ALA TYR ARG LEU ASP GLY PHE LYS LEU ALA
SEQRES 16 A 479 THR LYS ASN HIS LYS PRO PHE SER LEU LEU PRO LEU ARG
SEQRES 17 A 479 GLN ALA VAL ARG LEU ASN PRO ASP ASN GLY TYR ILE LYS
SEQRES 18 A 479 VAL LEU LEU ALA LEU LYS LEU GLN ASP GLU GLY GLN GLU
SEQRES 19 A 479 ALA GLU GLY GLU LYS TYR ILE GLU GLU ALA LEU ALA ASN
SEQRES 20 A 479 MET SER SER GLN THR TYR VAL PHE ARG TYR ALA ALA LYS
SEQRES 21 A 479 PHE TYR ARG ARG LYS GLY SER VAL ASP LYS ALA LEU GLU
SEQRES 22 A 479 LEU LEU LYS LYS ALA LEU GLN GLU THR PRO THR SER VAL
SEQRES 23 A 479 LEU LEU HIS HIS GLN ILE GLY LEU CYS TYR LYS ALA GLN
SEQRES 24 A 479 MET ILE GLN ILE LYS GLU ALA THR LYS GLY GLN PRO ARG
SEQRES 25 A 479 GLY GLN ASN ARG GLU LYS LEU ASP LYS MET ILE ARG SER
SEQRES 26 A 479 ALA ILE PHE HIS PHE GLU SER ALA VAL GLU LYS LYS PRO
SEQRES 27 A 479 THR PHE GLU VAL ALA HIS LEU ASP LEU ALA ARG MET TYR
SEQRES 28 A 479 ILE GLU ALA GLY ASN HIS ARG LYS ALA GLU GLU ASN PHE
SEQRES 29 A 479 GLN LYS LEU LEU CYS MET LYS PRO VAL VAL GLU GLU THR
SEQRES 30 A 479 MET GLN ASP ILE HIS PHE HIS TYR GLY ARG PHE GLN GLU
SEQRES 31 A 479 PHE GLN LYS LYS SER ASP VAL ASN ALA ILE ILE HIS TYR
SEQRES 32 A 479 LEU LYS ALA ILE LYS ILE GLU GLN ALA SER LEU THR ARG
SEQRES 33 A 479 ASP LYS SER ILE ASN SER LEU LYS LYS LEU VAL LEU ARG
SEQRES 34 A 479 LYS LEU ARG ARG LYS ALA LEU ASP LEU GLU SER LEU SER
SEQRES 35 A 479 LEU LEU GLY PHE VAL TYR LYS LEU GLU GLY ASN MET ASN
SEQRES 36 A 479 GLU ALA GLU GLU TYR TYR GLU ARG ALA GLU ARG LEU ALA
SEQRES 37 A 479 ALA ASP PHE GLU ASN SER VAL ARG GLN GLY PRO
SEQRES 1 B 4 G3A A A A
HET G3A B 1 74
HET PGE A 501 24
HET CA A 502 1
HET CA A 503 1
HETNAM G3A GUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CA CALCIUM ION
FORMUL 2 G3A C20 H27 N10 O17 P3
FORMUL 3 PGE C6 H14 O4
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *382(H2 O)
HELIX 1 AA1 HIS A 8 GLU A 15 1 8
HELIX 2 AA2 CYS A 19 TRP A 23 5 5
HELIX 3 AA3 ASP A 28 ASP A 30 5 3
HELIX 4 AA4 GLU A 31 LEU A 46 1 16
HELIX 5 AA5 SER A 51 LYS A 65 1 15
HELIX 6 AA6 GLN A 67 GLU A 85 1 19
HELIX 7 AA7 ARG A 93 GLY A 109 1 17
HELIX 8 AA8 ARG A 110 LEU A 128 1 19
HELIX 9 AA9 CYS A 138 CYS A 152 1 15
HELIX 10 AB1 GLY A 153 LYS A 155 5 3
HELIX 11 AB2 ASN A 156 GLU A 169 1 14
HELIX 12 AB3 ASN A 174 LYS A 192 1 19
HELIX 13 AB4 SER A 202 ASN A 213 1 12
HELIX 14 AB5 ASN A 216 GLU A 230 1 15
HELIX 15 AB6 GLN A 232 ALA A 245 1 14
HELIX 16 AB7 SER A 249 GLY A 265 1 17
HELIX 17 AB8 SER A 266 THR A 281 1 16
HELIX 18 AB9 SER A 284 THR A 306 1 23
HELIX 19 AC1 ARG A 311 LYS A 336 1 26
HELIX 20 AC2 PHE A 339 ALA A 353 1 15
HELIX 21 AC3 ASN A 355 CYS A 368 1 14
HELIX 22 AC4 GLU A 375 GLN A 391 1 17
HELIX 23 AC5 SER A 394 ILE A 408 1 15
HELIX 24 AC6 SER A 412 LYS A 433 1 22
HELIX 25 AC7 ASP A 436 GLY A 451 1 16
HELIX 26 AC8 ASN A 452 ALA A 467 1 16
LINK O23 G3A B 1 P A B 2 1555 1555 1.60
LINK OD1 ASP A 47 CA CA A 502 1555 1555 2.52
LINK OD2 ASP A 47 CA CA A 502 1555 1555 2.43
LINK OE1 GLU A 77 CA CA A 503 1555 1555 2.52
LINK OE2 GLU A 77 CA CA A 503 1555 1555 2.69
LINK CA CA A 502 O HOH A 608 1555 7551 2.42
LINK CA CA A 502 O HOH A 614 1555 7551 2.43
LINK CA CA A 502 O HOH A 683 1555 7551 2.21
LINK CA CA A 502 O HOH A 788 1555 1555 2.34
LINK CA CA A 502 O HOH A 842 1555 1555 2.41
LINK CA CA A 502 O HOH A 922 1555 7551 2.27
LINK CA CA A 503 O HOH A 900 1555 1555 2.71
SITE 1 AC1 3 HIS A 63 HOH A 703 HOH A 905
SITE 1 AC2 3 ASP A 47 HOH A 788 HOH A 842
SITE 1 AC3 2 GLU A 77 HOH A 900
CRYST1 112.536 112.536 93.470 90.00 90.00 90.00 P 42 2 2 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 0.008886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010699 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
