HEADER GENE REGULATION 01-MAR-14 4CRW
TITLE COMPLEX OF HUMAN DDX6 (RECA-C) AND CNOT1 (MIF4G)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CNOT1 MIF4G DOMAIN, RESIDUES 1093-1317;
COMPND 5 SYNONYM: CNOT1, CCR4-ASSOCIATED FACTOR 1, NEGATIVE REGULATOR OF
COMPND 6 TRANSCRIPTION SUBUNIT 1 HOMOLOG, NOT1H, HNOT1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROBABLE ATP-DEPENDENT RNA HELICASE DDX6;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: DDX6 RECA-C DOMAIN, RESIDUES 307-483;
COMPND 12 SYNONYM: DDX6, ATP-DEPENDENT RNA HELICASE P54, DEAD BOX PROTEIN 6,
COMPND 13 ONCOGENE RCK, ME31B HOMOLOG;
COMPND 14 EC: 3.6.1.-;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETMCN (PNEA);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1
KEYWDS GENE REGULATION, CCR4-NOT, TRANSLATIONAL REPRESSION, MRNA DECAPPING,
KEYWDS 2 DEAD-BOX PROTEIN, P54, RCK, HELICASE, MRNA SILENCING, MRNA
KEYWDS 3 DEADENYLATION, EIF4A, TRANSLATION, MIRNA, P-BODIES
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.CHEN,A.BOLAND,E.IZAURRALDE,O.WEICHENRIEDER
REVDAT 3 20-DEC-23 4CRW 1 REMARK
REVDAT 2 18-JUN-14 4CRW 1 JRNL
REVDAT 1 07-MAY-14 4CRW 0
JRNL AUTH Y.CHEN,A.BOLAND,D.KUZUOGLU-OZTURK,P.BAWANKAR,B.LOH,
JRNL AUTH 2 C.T.CHANG,O.WEICHENRIEDER,E.IZAURRALDE
JRNL TITL A DDX6-CNOT1 COMPLEX AND W-BINDING POCKETS IN CNOT9 REVEAL
JRNL TITL 2 DIRECT LINKS BETWEEN MIRNA TARGET RECOGNITION AND SILENCING
JRNL REF MOL.CELL V. 54 737 2014
JRNL REFN ISSN 1097-2765
JRNL PMID 24768540
JRNL DOI 10.1016/J.MOLCEL.2014.03.034
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 39110
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 47.9029 - 4.2169 0.97 2792 144 0.1792 0.2258
REMARK 3 2 4.2169 - 3.3473 0.98 2685 141 0.1467 0.1840
REMARK 3 3 3.3473 - 2.9243 0.99 2678 139 0.1541 0.1719
REMARK 3 4 2.9243 - 2.6569 0.99 2671 141 0.1533 0.2174
REMARK 3 5 2.6569 - 2.4665 1.00 2666 140 0.1440 0.1955
REMARK 3 6 2.4665 - 2.3211 1.00 2655 140 0.1465 0.1985
REMARK 3 7 2.3211 - 2.2048 1.00 2631 139 0.1489 0.1803
REMARK 3 8 2.2048 - 2.1089 1.00 2641 139 0.1499 0.1907
REMARK 3 9 2.1089 - 2.0277 0.99 2645 137 0.1597 0.1860
REMARK 3 10 2.0277 - 1.9577 0.99 2631 138 0.1700 0.2199
REMARK 3 11 1.9577 - 1.8965 0.99 2624 139 0.1830 0.2225
REMARK 3 12 1.8965 - 1.8423 0.99 2600 136 0.2005 0.2334
REMARK 3 13 1.8423 - 1.7938 0.99 2643 137 0.2178 0.2648
REMARK 3 14 1.7938 - 1.7500 0.99 2590 148 0.2294 0.2674
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.30
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 : 0.011 3248
REMARK 3 ANGLE : 1.306 4376
REMARK 3 CHIRALITY : 0.051 494
REMARK 3 PLANARITY : 0.006 554
REMARK 3 DIHEDRAL : 14.746 1240
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1092 THROUGH 1105 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2027 -9.8847 -10.9956
REMARK 3 T TENSOR
REMARK 3 T11: 0.3129 T22: 0.2606
REMARK 3 T33: 0.2937 T12: -0.0019
REMARK 3 T13: 0.0078 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.1113 L22: 0.6329
REMARK 3 L33: 0.3962 L12: -0.0718
REMARK 3 L13: -0.6195 L23: -0.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.1199 S12: 0.3603 S13: -0.4644
REMARK 3 S21: -0.5771 S22: -0.0246 S23: 0.2768
REMARK 3 S31: -0.0099 S32: 0.0865 S33: -0.0009
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 1106 THROUGH 1123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0589 -5.1988 -8.2976
REMARK 3 T TENSOR
REMARK 3 T11: 0.2565 T22: 0.3249
REMARK 3 T33: 0.3180 T12: 0.0627
REMARK 3 T13: 0.0183 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.5918 L22: 0.3594
REMARK 3 L33: 0.3373 L12: 0.2564
REMARK 3 L13: -0.2971 L23: -0.2221
REMARK 3 S TENSOR
REMARK 3 S11: 0.1920 S12: 0.3060 S13: -0.0793
REMARK 3 S21: -0.1012 S22: -0.1623 S23: -0.4142
REMARK 3 S31: 0.1673 S32: -0.0193 S33: -0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 1124 THROUGH 1142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5645 -0.6696 -15.4502
REMARK 3 T TENSOR
REMARK 3 T11: 0.2883 T22: 0.2106
REMARK 3 T33: 0.2232 T12: 0.0142
REMARK 3 T13: 0.0133 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.1330 L22: 1.0313
REMARK 3 L33: 0.8321 L12: 0.7957
REMARK 3 L13: 0.5980 L23: -0.0739
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.3289 S13: -0.3404
REMARK 3 S21: -0.4848 S22: -0.0896 S23: 0.0251
REMARK 3 S31: 0.1824 S32: -0.1342 S33: 0.0010
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 1143 THROUGH 1158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9113 5.0915 -7.8381
REMARK 3 T TENSOR
REMARK 3 T11: 0.1339 T22: 0.2054
REMARK 3 T33: 0.2229 T12: -0.0002
REMARK 3 T13: 0.0109 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0440 L22: 0.3446
REMARK 3 L33: 0.4809 L12: -0.0345
REMARK 3 L13: 0.1429 L23: -0.0466
REMARK 3 S TENSOR
REMARK 3 S11: 0.0635 S12: 0.1940 S13: -0.1784
REMARK 3 S21: 0.0675 S22: -0.1301 S23: -0.3049
REMARK 3 S31: -0.0271 S32: 0.1980 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 1159 THROUGH 1177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9559 8.6657 -19.6853
REMARK 3 T TENSOR
REMARK 3 T11: 0.2026 T22: 0.2100
REMARK 3 T33: 0.1549 T12: 0.0007
REMARK 3 T13: 0.0057 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.5726 L22: 1.3008
REMARK 3 L33: 0.8246 L12: 0.0072
REMARK 3 L13: 0.6481 L23: -0.2964
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: 0.4396 S13: -0.2347
REMARK 3 S21: -0.4376 S22: -0.1950 S23: 0.0871
REMARK 3 S31: 0.0921 S32: 0.0371 S33: -0.0057
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 1178 THROUGH 1202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4186 12.8923 -10.4134
REMARK 3 T TENSOR
REMARK 3 T11: 0.2239 T22: 0.2742
REMARK 3 T33: 0.2734 T12: 0.0279
REMARK 3 T13: 0.0307 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.4845 L22: 2.9135
REMARK 3 L33: 3.6170 L12: -0.1277
REMARK 3 L13: 0.2819 L23: -0.3982
REMARK 3 S TENSOR
REMARK 3 S11: -0.0818 S12: -0.0945 S13: -0.1220
REMARK 3 S21: 0.2097 S22: -0.0339 S23: 0.5917
REMARK 3 S31: -0.1514 S32: -0.6430 S33: -0.0017
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESID 1203 THROUGH 1228 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7711 22.7243 -18.5149
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.1976
REMARK 3 T33: 0.1713 T12: 0.0037
REMARK 3 T13: 0.0023 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.5431 L22: 1.2307
REMARK 3 L33: 1.7106 L12: 0.4677
REMARK 3 L13: -0.4351 L23: -0.0637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0805 S12: 0.2124 S13: -0.0142
REMARK 3 S21: -0.2724 S22: -0.0608 S23: 0.0499
REMARK 3 S31: -0.0678 S32: -0.0062 S33: -0.0003
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESID 1229 THROUGH 1248 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6721 21.2875 -9.5148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2007 T22: 0.1952
REMARK 3 T33: 0.1999 T12: 0.0151
REMARK 3 T13: 0.0033 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.6927 L22: 2.0984
REMARK 3 L33: 1.8254 L12: 0.2622
REMARK 3 L13: -1.0346 L23: -0.5455
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: -0.2097 S13: -0.0406
REMARK 3 S21: 0.2267 S22: 0.0321 S23: 0.1707
REMARK 3 S31: -0.1514 S32: -0.1485 S33: 0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESID 1249 THROUGH 1290 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2064 29.7379 -7.6186
REMARK 3 T TENSOR
REMARK 3 T11: 0.2417 T22: 0.1852
REMARK 3 T33: 0.1607 T12: 0.0139
REMARK 3 T13: 0.0015 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 1.2370 L22: 3.3005
REMARK 3 L33: 1.8712 L12: -0.6188
REMARK 3 L13: 0.3948 L23: -0.3891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: -0.1067 S13: 0.0991
REMARK 3 S21: 0.2814 S22: 0.0844 S23: -0.0094
REMARK 3 S31: -0.2340 S32: -0.0615 S33: 0.0003
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESID 1291 THROUGH 1317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5889 33.0637 -17.4297
REMARK 3 T TENSOR
REMARK 3 T11: 0.3013 T22: 0.2563
REMARK 3 T33: 0.2785 T12: 0.0521
REMARK 3 T13: 0.0109 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.7050 L22: 2.7374
REMARK 3 L33: 1.5220 L12: -1.2712
REMARK 3 L13: -0.9941 L23: -0.4129
REMARK 3 S TENSOR
REMARK 3 S11: 0.2100 S12: 0.3152 S13: 0.0179
REMARK 3 S21: -0.3072 S22: -0.0096 S23: -0.0867
REMARK 3 S31: -0.3312 S32: -0.0233 S33: 0.0009
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESID 296 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8940 -16.5101 0.4279
REMARK 3 T TENSOR
REMARK 3 T11: 0.3081 T22: 0.2165
REMARK 3 T33: 0.3109 T12: -0.0329
REMARK 3 T13: -0.0050 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.5365 L22: 0.8306
REMARK 3 L33: 1.5796 L12: 0.6098
REMARK 3 L13: 0.1765 L23: -0.5278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0267 S12: 0.1672 S13: -0.2152
REMARK 3 S21: -0.1112 S22: 0.0375 S23: 0.0786
REMARK 3 S31: 0.2493 S32: -0.1049 S33: -0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESID 321 THROUGH 358 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9922 -11.7971 9.6501
REMARK 3 T TENSOR
REMARK 3 T11: 0.2400 T22: 0.2773
REMARK 3 T33: 0.3032 T12: 0.0023
REMARK 3 T13: -0.0122 T23: 0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 0.7946 L22: 2.0350
REMARK 3 L33: 1.0539 L12: 0.3613
REMARK 3 L13: -0.1798 L23: -0.6458
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: -0.1873 S13: -0.2758
REMARK 3 S21: -0.0435 S22: -0.1396 S23: -0.3567
REMARK 3 S31: 0.2477 S32: 0.3837 S33: -0.0104
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESID 359 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6558 -1.6581 12.9868
REMARK 3 T TENSOR
REMARK 3 T11: 0.2649 T22: 0.2992
REMARK 3 T33: 0.2201 T12: -0.0609
REMARK 3 T13: -0.0245 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 1.0192 L22: 1.0894
REMARK 3 L33: 0.6628 L12: 0.2109
REMARK 3 L13: 0.1620 L23: 0.1149
REMARK 3 S TENSOR
REMARK 3 S11: 0.0688 S12: -0.3150 S13: -0.1253
REMARK 3 S21: 0.2359 S22: -0.1010 S23: -0.0813
REMARK 3 S31: -0.1847 S32: 0.1375 S33: -0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESID 380 THROUGH 391 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8583 -2.7810 15.3437
REMARK 3 T TENSOR
REMARK 3 T11: 0.7840 T22: 0.6439
REMARK 3 T33: 0.3682 T12: -0.0143
REMARK 3 T13: -0.0095 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.6083 L22: 2.4877
REMARK 3 L33: 2.3894 L12: 1.2499
REMARK 3 L13: -1.4251 L23: -2.4138
REMARK 3 S TENSOR
REMARK 3 S11: 0.1082 S12: -0.9772 S13: 0.5255
REMARK 3 S21: 1.9032 S22: 0.4280 S23: 0.2269
REMARK 3 S31: -1.5434 S32: -1.0842 S33: 0.1684
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESID 392 THROUGH 403 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8883 -12.3766 8.8938
REMARK 3 T TENSOR
REMARK 3 T11: 0.2290 T22: 0.2220
REMARK 3 T33: 0.2354 T12: -0.0465
REMARK 3 T13: 0.0166 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.7587 L22: 0.1354
REMARK 3 L33: 0.4627 L12: 0.1330
REMARK 3 L13: 0.5922 L23: 0.0964
REMARK 3 S TENSOR
REMARK 3 S11: 0.0235 S12: -0.0763 S13: -0.0823
REMARK 3 S21: 0.1261 S22: -0.0483 S23: -0.0476
REMARK 3 S31: 0.0650 S32: -0.1716 S33: 0.0002
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESID 404 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8493 -7.0511 13.0242
REMARK 3 T TENSOR
REMARK 3 T11: 0.3258 T22: 0.3033
REMARK 3 T33: 0.3112 T12: -0.0315
REMARK 3 T13: 0.0151 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.3046 L22: 0.1720
REMARK 3 L33: 0.1139 L12: -0.0733
REMARK 3 L13: 0.1028 L23: 0.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0992 S12: -0.0264 S13: 0.4521
REMARK 3 S21: -0.0165 S22: -0.0588 S23: -0.1626
REMARK 3 S31: -0.2379 S32: -0.0520 S33: 0.0006
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESID 415 THROUGH 428 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9502 -5.4836 4.0295
REMARK 3 T TENSOR
REMARK 3 T11: 0.4899 T22: 0.2340
REMARK 3 T33: 0.4335 T12: -0.0228
REMARK 3 T13: -0.0435 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 1.8269 L22: 0.2107
REMARK 3 L33: 1.2233 L12: 0.1924
REMARK 3 L13: -0.0981 L23: 0.4701
REMARK 3 S TENSOR
REMARK 3 S11: -0.1491 S12: 0.1372 S13: 0.5249
REMARK 3 S21: 0.8470 S22: 0.1101 S23: 0.3513
REMARK 3 S31: -0.8038 S32: -0.1698 S33: -0.0222
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND (RESID 429 THROUGH 453 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.2798 -17.2446 5.8114
REMARK 3 T TENSOR
REMARK 3 T11: 0.4031 T22: 0.3583
REMARK 3 T33: 0.3770 T12: -0.0439
REMARK 3 T13: -0.0256 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.7255 L22: 1.0759
REMARK 3 L33: 1.1842 L12: 0.2566
REMARK 3 L13: 0.8203 L23: 0.5552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: 0.3281 S13: -0.1060
REMARK 3 S21: -0.3213 S22: -0.0764 S23: 0.6274
REMARK 3 S31: 0.0483 S32: -0.3729 S33: -0.0265
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS WERE REFINED IN THE RIDING
REMARK 3 POSITIONS. TLS PARAMETERS WERE REFINED. SIDE CHAINS OF THE
REMARK 3 FOLLOWING RESIDUES HAVE DOUBLE CONFORMATIONS. CHAIN A, RESIDUES
REMARK 3 1127, 1140. CHAIN B, RESIDUES 374. THE FOLLOWING RESIDUES ARE
REMARK 3 DISORDERED. CHAIN A, RESIDUES 1087 TO 1091. CHAIN B, RESIDUES
REMARK 3 291 TO 295, 454 TO 472.
REMARK 4
REMARK 4 4CRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1290059865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRRORS
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39120
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 65.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.79000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2WAX (CHAIN A), 4GML (CHAIN A)
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-CL PH=8, 16% PEG6000,, PH
REMARK 280 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.88500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.42000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.88500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.42000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 GLY A 1087
REMARK 465 PRO A 1088
REMARK 465 HIS A 1089
REMARK 465 MET A 1090
REMARK 465 LEU A 1091
REMARK 465 GLY B 291
REMARK 465 PRO B 292
REMARK 465 GLN B 293
REMARK 465 ASP B 294
REMARK 465 PRO B 295
REMARK 465 ASP B 454
REMARK 465 LYS B 455
REMARK 465 SER B 456
REMARK 465 LEU B 457
REMARK 465 TYR B 458
REMARK 465 VAL B 459
REMARK 465 ALA B 460
REMARK 465 GLU B 461
REMARK 465 TYR B 462
REMARK 465 HIS B 463
REMARK 465 SER B 464
REMARK 465 GLU B 465
REMARK 465 PRO B 466
REMARK 465 VAL B 467
REMARK 465 GLU B 468
REMARK 465 ASP B 469
REMARK 465 GLU B 470
REMARK 465 LYS B 471
REMARK 465 PRO B 472
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 OE2 GLU A 1125 HZ2 LYS A 1218 3544 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A1138 -70.22 -111.01
REMARK 500 THR A1203 -88.46 -118.08
REMARK 500 PRO A1255 37.02 -92.66
REMARK 500 ASN B 324 -75.42 -81.12
REMARK 500 LYS B 356 50.45 -93.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GML RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NOT1 MIF4G DOMAIN
REMARK 900 RELATED ID: 4GMJ RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NOT1 MIF4G DOMAIN CO-CRYSTALLIZED WITH CAF1
REMARK 900 RELATED ID: 2WAX RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN DDX6 C-TERMINAL DOMAIN IN COMPLEX WITH AN
REMARK 900 EDC3-FDF PEPTIDE
REMARK 900 RELATED ID: 2WAY RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN DDX6 C-TERMINAL DOMAIN IN COMPLEX WITH AN
REMARK 900 EDC3-FDF PEPTIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SIX N-TERMINAL RESIDUES REMAIN FROM THE EXPRESSION TAG
REMARK 999 OF CHAIN A.
REMARK 999 THE FIVE N-TERMINAL RESIDUES REMAIN FROM THE EXPRESSION
REMARK 999 TAG OF CHAIN B. SEQUENCE NUMBERS ARE SHIFTED BY -11
REMARK 999 RESIDUES ACCORDING TO PDB 2WAX AND NCBI GI 458727.
DBREF 4CRW A 1093 1317 UNP A5YKK6 CNOT1_HUMAN 1093 1317
DBREF 4CRW B 296 472 UNP P26196 DDX6_HUMAN 307 483
SEQADV 4CRW GLY A 1087 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW PRO A 1088 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW HIS A 1089 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW MET A 1090 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW LEU A 1091 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW GLU A 1092 UNP A5YKK6 EXPRESSION TAG
SEQADV 4CRW GLY B 291 UNP P26196 EXPRESSION TAG
SEQADV 4CRW PRO B 292 UNP P26196 EXPRESSION TAG
SEQADV 4CRW GLN B 293 UNP P26196 EXPRESSION TAG
SEQADV 4CRW ASP B 294 UNP P26196 EXPRESSION TAG
SEQADV 4CRW PRO B 295 UNP P26196 EXPRESSION TAG
SEQRES 1 A 231 GLY PRO HIS MET LEU GLU GLU ASN ILE GLN GLU LYS ILE
SEQRES 2 A 231 ALA PHE ILE PHE ASN ASN LEU SER GLN SER ASN MET THR
SEQRES 3 A 231 GLN LYS VAL GLU GLU LEU LYS GLU THR VAL LYS GLU GLU
SEQRES 4 A 231 PHE MET PRO TRP VAL SER GLN TYR LEU VAL MET LYS ARG
SEQRES 5 A 231 VAL SER ILE GLU PRO ASN PHE HIS SER LEU TYR SER ASN
SEQRES 6 A 231 PHE LEU ASP THR LEU LYS ASN PRO GLU PHE ASN LYS MET
SEQRES 7 A 231 VAL LEU ASN GLU THR TYR ARG ASN ILE LYS VAL LEU LEU
SEQRES 8 A 231 THR SER ASP LYS ALA ALA ALA ASN PHE SER ASP ARG SER
SEQRES 9 A 231 LEU LEU LYS ASN LEU GLY HIS TRP LEU GLY MET ILE THR
SEQRES 10 A 231 LEU ALA LYS ASN LYS PRO ILE LEU HIS THR ASP LEU ASP
SEQRES 11 A 231 VAL LYS SER LEU LEU LEU GLU ALA TYR VAL LYS GLY GLN
SEQRES 12 A 231 GLN GLU LEU LEU TYR VAL VAL PRO PHE VAL ALA LYS VAL
SEQRES 13 A 231 LEU GLU SER SER ILE ARG SER VAL VAL PHE ARG PRO PRO
SEQRES 14 A 231 ASN PRO TRP THR MET ALA ILE MET ASN VAL LEU ALA GLU
SEQRES 15 A 231 LEU HIS GLN GLU HIS ASP LEU LYS LEU ASN LEU LYS PHE
SEQRES 16 A 231 GLU ILE GLU VAL LEU CYS LYS ASN LEU ALA LEU ASP ILE
SEQRES 17 A 231 ASN GLU LEU LYS PRO GLY ASN LEU LEU LYS ASP LYS ASP
SEQRES 18 A 231 ARG LEU LYS ASN LEU ASP GLU GLN LEU SER
SEQRES 1 B 182 GLY PRO GLN ASP PRO LYS GLY VAL THR GLN TYR TYR ALA
SEQRES 2 B 182 TYR VAL THR GLU ARG GLN LYS VAL HIS CYS LEU ASN THR
SEQRES 3 B 182 LEU PHE SER ARG LEU GLN ILE ASN GLN SER ILE ILE PHE
SEQRES 4 B 182 CYS ASN SER SER GLN ARG VAL GLU LEU LEU ALA LYS LYS
SEQRES 5 B 182 ILE SER GLN LEU GLY TYR SER CYS PHE TYR ILE HIS ALA
SEQRES 6 B 182 LYS MET ARG GLN GLU HIS ARG ASN ARG VAL PHE HIS ASP
SEQRES 7 B 182 PHE ARG ASN GLY LEU CYS ARG ASN LEU VAL CYS THR ASP
SEQRES 8 B 182 LEU PHE THR ARG GLY ILE ASP ILE GLN ALA VAL ASN VAL
SEQRES 9 B 182 VAL ILE ASN PHE ASP PHE PRO LYS LEU ALA GLU THR TYR
SEQRES 10 B 182 LEU HIS ARG ILE GLY ARG SER GLY ARG PHE GLY HIS LEU
SEQRES 11 B 182 GLY LEU ALA ILE ASN LEU ILE THR TYR ASP ASP ARG PHE
SEQRES 12 B 182 ASN LEU LYS SER ILE GLU GLU GLN LEU GLY THR GLU ILE
SEQRES 13 B 182 LYS PRO ILE PRO SER ASN ILE ASP LYS SER LEU TYR VAL
SEQRES 14 B 182 ALA GLU TYR HIS SER GLU PRO VAL GLU ASP GLU LYS PRO
HET GOL A1801 14
HET GOL A1802 14
HET GOL A1803 14
HET GOL A1804 14
HET GOL B1801 14
HET GOL B1802 14
HET GOL B1803 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 7(C3 H8 O3)
FORMUL 10 HOH *193(H2 O)
HELIX 1 1 GLU A 1093 ASN A 1104 1 12
HELIX 2 2 MET A 1111 THR A 1121 1 11
HELIX 3 3 MET A 1127 LYS A 1137 1 11
HELIX 4 4 HIS A 1146 LEU A 1156 1 11
HELIX 5 5 PRO A 1159 LEU A 1177 1 19
HELIX 6 6 PHE A 1186 ILE A 1202 1 17
HELIX 7 7 VAL A 1217 LYS A 1227 1 11
HELIX 8 8 GLN A 1229 LEU A 1243 1 15
HELIX 9 9 PRO A 1257 GLN A 1271 1 15
HELIX 10 10 LEU A 1277 ASN A 1289 1 13
HELIX 11 11 LYS A 1306 LYS A 1310 1 5
HELIX 12 12 LYS B 310 ARG B 320 1 11
HELIX 13 13 SER B 333 GLN B 345 1 13
HELIX 14 14 GLN B 359 ARG B 370 1 12
HELIX 15 15 ALA B 404 ILE B 411 1 8
HELIX 16 16 ARG B 432 LEU B 442 1 11
SHEET 1 BA 7 CYS B 350 ILE B 353 0
SHEET 2 BA 7 ASN B 376 CYS B 379 1 O ASN B 376 N PHE B 351
SHEET 3 BA 7 GLN B 325 PHE B 329 1 O SER B 326 N LEU B 377
SHEET 4 BA 7 VAL B 392 ASN B 397 1 N ASN B 393 O GLN B 325
SHEET 5 BA 7 GLY B 421 ILE B 427 1 O LEU B 422 N VAL B 395
SHEET 6 BA 7 VAL B 298 TYR B 304 1 O THR B 299 N ALA B 423
SHEET 7 BA 7 LYS B 447 PRO B 448 1 O LYS B 447 N TYR B 302
CISPEP 1 PRO A 1254 PRO A 1255 0 2.84
SITE 1 AC1 5 ASN A1144 PHE A1145 HIS A1273 HOH A2123
SITE 2 AC1 5 ASN B 371
SITE 1 AC2 4 MET A1136 SER A1140 ASN A1172 HOH A2124
SITE 1 AC3 6 GLU A1116 LYS A1119 THR A1155 LEU A1156
SITE 2 AC3 6 LYS A1157 HOH A2018
SITE 1 AC4 6 SER A1147 MET A1201 GLU A1284 HOH A2085
SITE 2 AC4 6 HOH A2086 HOH A2125
SITE 1 AC5 4 PHE B 351 TYR B 352 MET B 357 HIS B 361
SITE 1 AC6 5 GLU B 307 ARG B 335 LYS B 342 PHE B 398
SITE 2 AC6 5 HOH B2011
SITE 1 AC7 5 HIS B 312 LYS B 436 GLU B 439 HOH B2060
SITE 2 AC7 5 HOH B2068
CRYST1 43.900 90.840 95.770 90.00 90.00 90.00 P 21 21 21 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 0.022779 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010442 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
