HEADER STRUCTURAL PROTEIN/PROTEIN BINDING 22-JUL-14 4U3J
TITLE TOG2:ALPHA/BETA-TUBULIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA-1 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TUBULIN BETA CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: BETA-TUBULIN;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROTEIN STU2;
COMPND 13 CHAIN: C;
COMPND 14 FRAGMENT: TOG2 DOMAIN (UNP RESIDUES 318-560);
COMPND 15 SYNONYM: SUPPRESSOR OF TUBULIN 2;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: TUB1;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JEL1;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 GENE: TUB2;
SOURCE 14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: JEL1;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 GENE: STU2;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PET-29B
KEYWDS COMPLEX, STRUCTURAL PROTEIN-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.AYAZ,L.M.RICE
REVDAT 5 27-SEP-23 4U3J 1 REMARK LINK
REVDAT 4 25-DEC-19 4U3J 1 REMARK
REVDAT 3 27-SEP-17 4U3J 1 SOURCE REMARK
REVDAT 2 01-OCT-14 4U3J 1 JRNL
REVDAT 1 20-AUG-14 4U3J 0
JRNL AUTH P.AYAZ,S.MUNYOKI,E.A.GEYER,F.A.PIEDRA,E.S.VU,R.BROMBERG,
JRNL AUTH 2 Z.OTWINOWSKI,N.V.GRISHIN,C.A.BRAUTIGAM,L.M.RICE
JRNL TITL A TETHERED DELIVERY MECHANISM EXPLAINS THE CATALYTIC ACTION
JRNL TITL 2 OF A MICROTUBULE POLYMERASE.
JRNL REF ELIFE V. 3 03069 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 25097237
JRNL DOI 10.7554/ELIFE.03069
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1627)
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 26230
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1305
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 34.0713 - 5.8357 0.99 3245 172 0.1853 0.1962
REMARK 3 2 5.8357 - 4.6357 0.99 3192 165 0.1937 0.2405
REMARK 3 3 4.6357 - 4.0508 0.99 3190 168 0.1768 0.2305
REMARK 3 4 4.0508 - 3.6809 0.99 3178 158 0.2081 0.2538
REMARK 3 5 3.6809 - 3.4173 0.98 3093 172 0.2418 0.2883
REMARK 3 6 3.4173 - 3.2160 0.95 3043 157 0.2665 0.3088
REMARK 3 7 3.2160 - 3.0551 0.85 2729 146 0.2993 0.3333
REMARK 3 8 3.0551 - 2.9221 0.66 2110 110 0.3198 0.3548
REMARK 3 9 2.9221 - 2.8097 0.36 1145 57 0.3296 0.4115
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.700
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 : 0.003 8677
REMARK 3 ANGLE : 0.656 11784
REMARK 3 CHIRALITY : 0.026 1318
REMARK 3 PLANARITY : 0.003 1526
REMARK 3 DIHEDRAL : 15.335 3151
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -79.2425 -12.7991 29.1083
REMARK 3 T TENSOR
REMARK 3 T11: 0.3924 T22: 0.5042
REMARK 3 T33: 0.3389 T12: 0.1130
REMARK 3 T13: -0.0664 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 5.1699 L22: 1.5138
REMARK 3 L33: 2.5875 L12: -1.7443
REMARK 3 L13: 0.3899 L23: 1.1625
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.2180 S13: -0.0825
REMARK 3 S21: -0.2541 S22: 0.0753 S23: 0.2486
REMARK 3 S31: -0.4820 S32: -0.4269 S33: -0.0078
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.8881 -23.5810 22.6410
REMARK 3 T TENSOR
REMARK 3 T11: 0.4799 T22: 0.4939
REMARK 3 T33: 0.3306 T12: 0.0470
REMARK 3 T13: -0.0257 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 2.8888 L22: 1.0598
REMARK 3 L33: 1.7640 L12: 1.3191
REMARK 3 L13: 0.7153 L23: 1.1244
REMARK 3 S TENSOR
REMARK 3 S11: 0.1377 S12: 0.6687 S13: -0.0915
REMARK 3 S21: -0.9382 S22: -0.1227 S23: 0.2159
REMARK 3 S31: 0.1535 S32: -0.2092 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.2537 -15.5633 30.8850
REMARK 3 T TENSOR
REMARK 3 T11: 0.4322 T22: 0.2974
REMARK 3 T33: 0.3911 T12: 0.0121
REMARK 3 T13: -0.0080 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 4.1287 L22: 1.9771
REMARK 3 L33: 0.2941 L12: 0.0185
REMARK 3 L13: -0.3750 L23: 0.3537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: 0.2895 S13: 0.3562
REMARK 3 S21: -0.1175 S22: -0.2944 S23: -0.2583
REMARK 3 S31: -0.3144 S32: 0.4087 S33: -0.0017
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.4292 -16.6918 43.9216
REMARK 3 T TENSOR
REMARK 3 T11: 0.3399 T22: 0.3278
REMARK 3 T33: 0.3519 T12: -0.0242
REMARK 3 T13: -0.0586 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.9627 L22: 1.8649
REMARK 3 L33: 0.1464 L12: -1.0127
REMARK 3 L13: 0.5336 L23: 0.3741
REMARK 3 S TENSOR
REMARK 3 S11: 0.0927 S12: -0.4198 S13: -0.0326
REMARK 3 S21: 0.1027 S22: -0.1649 S23: 0.2066
REMARK 3 S31: -0.3804 S32: 0.4144 S33: 0.0016
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.0204 -3.3803 37.4320
REMARK 3 T TENSOR
REMARK 3 T11: 0.6015 T22: 0.4293
REMARK 3 T33: 0.6213 T12: 0.0255
REMARK 3 T13: -0.0403 T23: 0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 1.4550 L22: 1.1757
REMARK 3 L33: 0.3716 L12: -1.1957
REMARK 3 L13: -0.3984 L23: 0.7430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: 0.2519 S13: 0.8920
REMARK 3 S21: -0.3891 S22: 0.1015 S23: 0.3755
REMARK 3 S31: -0.6230 S32: -0.3631 S33: 0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.0233 -5.2024 43.8677
REMARK 3 T TENSOR
REMARK 3 T11: 0.3462 T22: 0.2282
REMARK 3 T33: 0.5076 T12: -0.0328
REMARK 3 T13: -0.1335 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 0.8438 L22: 1.7264
REMARK 3 L33: 2.3286 L12: -1.1366
REMARK 3 L13: 0.6192 L23: 0.1606
REMARK 3 S TENSOR
REMARK 3 S11: 0.1289 S12: -0.1879 S13: 0.3591
REMARK 3 S21: 0.0757 S22: -0.1016 S23: -0.0962
REMARK 3 S31: -0.4590 S32: -0.0756 S33: 0.0006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 288 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.6640 0.8635 54.8549
REMARK 3 T TENSOR
REMARK 3 T11: 0.6696 T22: 0.4633
REMARK 3 T33: 0.7202 T12: 0.1011
REMARK 3 T13: -0.0141 T23: -0.0988
REMARK 3 L TENSOR
REMARK 3 L11: 0.1600 L22: 0.3546
REMARK 3 L33: 0.0830 L12: -0.2195
REMARK 3 L13: -0.0940 L23: 0.1316
REMARK 3 S TENSOR
REMARK 3 S11: -0.4055 S12: -1.3352 S13: 0.0910
REMARK 3 S21: 0.4752 S22: -0.0119 S23: 0.7012
REMARK 3 S31: -0.1379 S32: -0.2130 S33: -0.0066
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 302 THROUGH 315 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.0340 -4.5269 51.0968
REMARK 3 T TENSOR
REMARK 3 T11: 0.5025 T22: 0.3821
REMARK 3 T33: 0.6130 T12: -0.0659
REMARK 3 T13: -0.0633 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.1840 L22: 0.4702
REMARK 3 L33: 1.2234 L12: -0.3399
REMARK 3 L13: -0.1853 L23: 0.2438
REMARK 3 S TENSOR
REMARK 3 S11: 0.4308 S12: 0.1444 S13: -0.2493
REMARK 3 S21: -0.4128 S22: -0.5985 S23: -0.4852
REMARK 3 S31: -0.1685 S32: -0.0651 S33: 0.0030
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.0607 5.5632 44.8561
REMARK 3 T TENSOR
REMARK 3 T11: 0.4551 T22: 0.4603
REMARK 3 T33: 0.8512 T12: -0.0158
REMARK 3 T13: 0.0422 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.2322 L22: 0.2334
REMARK 3 L33: 0.9233 L12: -0.1796
REMARK 3 L13: 0.4956 L23: -0.3290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: -0.0121 S13: 1.5616
REMARK 3 S21: -1.8089 S22: 0.4483 S23: 0.0770
REMARK 3 S31: -0.0149 S32: 0.1513 S33: 0.0089
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 326 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.9893 12.8558 52.8979
REMARK 3 T TENSOR
REMARK 3 T11: 0.8498 T22: 0.9243
REMARK 3 T33: 1.2371 T12: -0.0176
REMARK 3 T13: -0.1977 T23: 0.2872
REMARK 3 L TENSOR
REMARK 3 L11: 0.1907 L22: 0.2418
REMARK 3 L33: 0.4315 L12: 0.0555
REMARK 3 L13: -0.1375 L23: 0.2823
REMARK 3 S TENSOR
REMARK 3 S11: 0.4742 S12: -0.4344 S13: 1.2783
REMARK 3 S21: 1.1313 S22: -0.5291 S23: 0.1566
REMARK 3 S31: 0.6138 S32: 1.1087 S33: -0.0002
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.5375 1.3887 46.0136
REMARK 3 T TENSOR
REMARK 3 T11: 0.7001 T22: 0.5171
REMARK 3 T33: 0.4419 T12: 0.0656
REMARK 3 T13: -0.0421 T23: 0.0943
REMARK 3 L TENSOR
REMARK 3 L11: 3.6289 L22: 2.1441
REMARK 3 L33: 2.6466 L12: -3.0739
REMARK 3 L13: -1.3129 L23: 0.5503
REMARK 3 S TENSOR
REMARK 3 S11: 0.3812 S12: -0.6184 S13: 0.7386
REMARK 3 S21: -0.0668 S22: -0.4835 S23: 0.2243
REMARK 3 S31: -0.3744 S32: 0.1434 S33: -0.0046
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 402 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4321 -19.8714 46.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.4007
REMARK 3 T33: 0.4960 T12: 0.0207
REMARK 3 T13: -0.0379 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.2866 L22: 2.6657
REMARK 3 L33: -0.0887 L12: -1.0542
REMARK 3 L13: -0.2629 L23: 0.0510
REMARK 3 S TENSOR
REMARK 3 S11: -0.6533 S12: -0.1478 S13: 0.3046
REMARK 3 S21: 1.1470 S22: 0.5675 S23: 0.0124
REMARK 3 S31: 0.0607 S32: 0.0972 S33: -0.0103
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 403 THROUGH 415 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6341 -33.5740 33.9468
REMARK 3 T TENSOR
REMARK 3 T11: 0.3003 T22: 0.2723
REMARK 3 T33: 0.3190 T12: 0.0383
REMARK 3 T13: 0.0303 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.4162 L22: 1.0350
REMARK 3 L33: 1.4256 L12: 0.0759
REMARK 3 L13: -0.4756 L23: 0.2466
REMARK 3 S TENSOR
REMARK 3 S11: 0.3786 S12: 0.0650 S13: -0.0006
REMARK 3 S21: -0.6246 S22: -0.2538 S23: -0.2009
REMARK 3 S31: -0.2212 S32: -0.1770 S33: -0.0227
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 416 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6204 -14.4108 39.1329
REMARK 3 T TENSOR
REMARK 3 T11: 0.3902 T22: 0.5086
REMARK 3 T33: 0.5090 T12: -0.0577
REMARK 3 T13: 0.0278 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 2.5642 L22: 1.1295
REMARK 3 L33: 1.1325 L12: -1.5699
REMARK 3 L13: 1.1490 L23: -0.2588
REMARK 3 S TENSOR
REMARK 3 S11: -0.2502 S12: -0.2606 S13: 0.5489
REMARK 3 S21: -0.4177 S22: 0.4735 S23: -0.3467
REMARK 3 S31: -0.5184 S32: 0.6681 S33: 0.0084
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.1311 -57.2018 31.7535
REMARK 3 T TENSOR
REMARK 3 T11: 0.3997 T22: 0.4567
REMARK 3 T33: 0.5469 T12: -0.1112
REMARK 3 T13: -0.0246 T23: -0.0919
REMARK 3 L TENSOR
REMARK 3 L11: 4.7768 L22: 2.0502
REMARK 3 L33: 3.1165 L12: -0.5590
REMARK 3 L13: -0.7107 L23: -0.5862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: 0.4135 S13: -0.4215
REMARK 3 S21: -0.1470 S22: -0.0377 S23: 0.7076
REMARK 3 S31: 0.4234 S32: -0.6141 S33: -0.0007
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 236 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.7548 -56.9079 39.9917
REMARK 3 T TENSOR
REMARK 3 T11: 0.4247 T22: 0.3017
REMARK 3 T33: 0.4533 T12: 0.0168
REMARK 3 T13: 0.0316 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.6517 L22: 1.6896
REMARK 3 L33: 2.8475 L12: -1.0205
REMARK 3 L13: -0.2485 L23: 0.6663
REMARK 3 S TENSOR
REMARK 3 S11: -0.1160 S12: -0.0777 S13: -0.2424
REMARK 3 S21: 0.1595 S22: -0.1117 S23: 0.0169
REMARK 3 S31: 0.5857 S32: 0.0999 S33: -0.0036
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 237 THROUGH 266 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.2038 -40.8357 40.5043
REMARK 3 T TENSOR
REMARK 3 T11: 0.3970 T22: 0.3062
REMARK 3 T33: 0.3370 T12: 0.0793
REMARK 3 T13: 0.0228 T23: 0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 1.6235 L22: 3.5926
REMARK 3 L33: 3.7722 L12: 2.5809
REMARK 3 L13: -0.0433 L23: 0.4853
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: -0.3216 S13: 0.7816
REMARK 3 S21: 0.0699 S22: -0.1432 S23: 0.4463
REMARK 3 S31: 0.0087 S32: -0.1646 S33: -0.0002
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 267 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.8757 -41.6252 55.9078
REMARK 3 T TENSOR
REMARK 3 T11: 0.5265 T22: 0.4299
REMARK 3 T33: 0.5040 T12: 0.0069
REMARK 3 T13: 0.0551 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.9044 L22: 0.6498
REMARK 3 L33: 1.9337 L12: -0.9954
REMARK 3 L13: -1.3675 L23: -0.2591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: -0.4710 S13: -0.0908
REMARK 3 S21: 0.4900 S22: 0.0381 S23: 0.3750
REMARK 3 S31: 0.1375 S32: -0.1201 S33: -0.0004
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 404 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.8403 -65.6692 42.6290
REMARK 3 T TENSOR
REMARK 3 T11: 0.6652 T22: 0.4357
REMARK 3 T33: 0.5234 T12: 0.1652
REMARK 3 T13: -0.0666 T23: 0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 3.0862 L22: 1.4440
REMARK 3 L33: 1.0183 L12: 0.3536
REMARK 3 L13: -0.7967 L23: -0.8440
REMARK 3 S TENSOR
REMARK 3 S11: 0.1067 S12: -0.2224 S13: -0.5351
REMARK 3 S21: 0.2593 S22: 0.2083 S23: -0.5566
REMARK 3 S31: 0.6842 S32: 0.1213 S33: 0.0015
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 405 THROUGH 430 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.4218 -51.6619 43.8344
REMARK 3 T TENSOR
REMARK 3 T11: 0.4168 T22: 0.6769
REMARK 3 T33: 0.4306 T12: 0.0744
REMARK 3 T13: -0.0380 T23: 0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 0.1303 L22: 1.2922
REMARK 3 L33: 0.7242 L12: -0.8029
REMARK 3 L13: 0.9125 L23: -0.3176
REMARK 3 S TENSOR
REMARK 3 S11: -0.5388 S12: -0.0267 S13: -0.1425
REMARK 3 S21: 0.6216 S22: 0.7246 S23: -0.6071
REMARK 3 S31: 0.2732 S32: 0.9653 S33: -0.1109
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 319 THROUGH 369 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5903 -74.5645 7.3706
REMARK 3 T TENSOR
REMARK 3 T11: 0.8178 T22: 0.7902
REMARK 3 T33: 0.4548 T12: 0.2447
REMARK 3 T13: -0.0052 T23: -0.2624
REMARK 3 L TENSOR
REMARK 3 L11: 1.2436 L22: 2.9736
REMARK 3 L33: 2.1375 L12: -1.2266
REMARK 3 L13: 0.7237 L23: 0.9302
REMARK 3 S TENSOR
REMARK 3 S11: 0.1719 S12: 0.5326 S13: -1.2200
REMARK 3 S21: 0.0677 S22: -0.0597 S23: -0.2511
REMARK 3 S31: 0.9461 S32: 0.5984 S33: 0.0498
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 370 THROUGH 445 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.6341 -60.7834 9.0511
REMARK 3 T TENSOR
REMARK 3 T11: 0.4998 T22: 0.5914
REMARK 3 T33: 0.3353 T12: 0.1280
REMARK 3 T13: 0.0135 T23: -0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 1.6665 L22: 4.3644
REMARK 3 L33: 1.9723 L12: 0.1156
REMARK 3 L13: 0.5731 L23: -1.2285
REMARK 3 S TENSOR
REMARK 3 S11: -0.1627 S12: 0.5690 S13: -0.3129
REMARK 3 S21: -0.4581 S22: 0.1014 S23: -0.0213
REMARK 3 S31: -0.0225 S32: 0.1674 S33: 0.0002
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 446 THROUGH 533 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0216 -40.5690 9.0016
REMARK 3 T TENSOR
REMARK 3 T11: 0.5635 T22: 0.6766
REMARK 3 T33: 0.3746 T12: 0.0140
REMARK 3 T13: 0.0275 T23: 0.1026
REMARK 3 L TENSOR
REMARK 3 L11: 0.2753 L22: 5.2481
REMARK 3 L33: 2.7864 L12: -0.0452
REMARK 3 L13: 0.3087 L23: 1.9787
REMARK 3 S TENSOR
REMARK 3 S11: 0.1609 S12: 0.3047 S13: 0.3646
REMARK 3 S21: -1.0080 S22: 0.1973 S23: -0.1845
REMARK 3 S31: -0.4363 S32: 0.4616 S33: 0.0094
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 534 THROUGH 559 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.6049 -25.9183 16.5537
REMARK 3 T TENSOR
REMARK 3 T11: 0.7533 T22: 0.7419
REMARK 3 T33: 0.7155 T12: -0.0060
REMARK 3 T13: 0.1681 T23: 0.1271
REMARK 3 L TENSOR
REMARK 3 L11: 0.4790 L22: 1.4125
REMARK 3 L33: 1.2723 L12: 0.6967
REMARK 3 L13: 0.5681 L23: 1.3114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.2062 S13: 1.2861
REMARK 3 S21: -0.8676 S22: 0.2859 S23: -0.5893
REMARK 3 S31: -1.6228 S32: 0.3710 S33: 0.0001
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 4U3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
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 : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.810
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 (%) : 86.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.92400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4FFB,2QK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (V/V) PEG3350, 0.25 M (NH4)2SO4,
REMARK 280 0.1 M MES, PH 6.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
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 55.95450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.78650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 55.95450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.78650
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 LYS A 281
REMARK 465 ALA A 282
REMARK 465 PHE A 283
REMARK 465 HIS A 284
REMARK 465 GLU A 285
REMARK 465 SER A 286
REMARK 465 ASN A 287
REMARK 465 ASP A 439
REMARK 465 SER A 440
REMARK 465 TYR A 441
REMARK 465 ALA A 442
REMARK 465 GLU A 443
REMARK 465 GLU A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 PHE A 447
REMARK 465 ARG B 175
REMARK 465 SER B 176
REMARK 465 ASP B 177
REMARK 465 ARG B 213
REMARK 465 THR B 214
REMARK 465 LEU B 217
REMARK 465 ASN B 218
REMARK 465 ILE B 276
REMARK 465 GLY B 277
REMARK 465 SER B 278
REMARK 465 GLN B 279
REMARK 465 SER B 280
REMARK 465 PHE B 281
REMARK 465 GLU B 431
REMARK 465 ASP B 432
REMARK 465 ASP B 433
REMARK 465 GLU B 434
REMARK 465 GLU B 435
REMARK 465 VAL B 436
REMARK 465 ASP B 437
REMARK 465 GLU B 438
REMARK 465 ASN B 439
REMARK 465 GLY B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 GLY B 443
REMARK 465 ALA B 444
REMARK 465 PRO B 445
REMARK 465 GLN B 446
REMARK 465 ASN B 447
REMARK 465 GLN B 448
REMARK 465 ASP B 449
REMARK 465 GLU B 450
REMARK 465 PRO B 451
REMARK 465 ILE B 452
REMARK 465 THR B 453
REMARK 465 GLU B 454
REMARK 465 ASN B 455
REMARK 465 PHE B 456
REMARK 465 GLU B 457
REMARK 465 HIS B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
REMARK 465 HIS B 461
REMARK 465 HIS B 462
REMARK 465 HIS B 463
REMARK 465 MET C 318
REMARK 465 LEU C 560
REMARK 465 HIS C 561
REMARK 465 HIS C 562
REMARK 465 HIS C 563
REMARK 465 HIS C 564
REMARK 465 HIS C 565
REMARK 465 HIS C 566
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 MET A 1 CG SD CE
REMARK 470 ARG A 2 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 38 CG OD1 OD2
REMARK 470 LYS A 42 CG CD CE NZ
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 LYS A 164 CG CD CE NZ
REMARK 470 ASN A 338 CG OD1 ND2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 LEU A 344 CG CD1 CD2
REMARK 470 CYS A 348 SG
REMARK 470 LYS A 353 CG CD CE NZ
REMARK 470 ASN A 366 CG OD1 ND2
REMARK 470 MET B 1 CG SD CE
REMARK 470 HIS B 39 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 SER B 56 OG
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 ILE B 81 CG1 CG2 CD1
REMARK 470 ASN B 83 CG OD1 ND2
REMARK 470 GLN B 94 CG CD OE1 NE2
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 LYS B 216 CG CD CE NZ
REMARK 470 THR B 274 OG1 CG2
REMARK 470 SER B 283 OG
REMARK 470 GLN B 291 CG CD OE1 NE2
REMARK 470 LYS B 320 CG CD CE NZ
REMARK 470 GLU B 343 CG CD OE1 OE2
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 VAL B 430 CG1 CG2
REMARK 470 LYS C 330 CG CD CE NZ
REMARK 470 ASP C 331 CG OD1 OD2
REMARK 470 GLU C 334 CG CD OE1 OE2
REMARK 470 GLN C 358 CG CD OE1 NE2
REMARK 470 ARG C 454 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 464 CG CD OE1 OE2
REMARK 470 LYS C 469 CG CD CE NZ
REMARK 470 LYS C 489 CG CD CE NZ
REMARK 470 LYS C 531 CG CD CE NZ
REMARK 470 LYS C 540 CG CD CE NZ
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 OD2 ASP C 546 HZ2 LYS C 549 1.51
REMARK 500 HH11 ARG C 550 OE2 GLU C 554 1.59
REMARK 500 O ASN A 187 HG1 THR A 191 1.59
REMARK 500 NH1 ARG C 550 OE2 GLU C 554 2.12
REMARK 500 OD2 ASP C 546 NZ LYS C 549 2.16
REMARK 500 OH TYR A 109 OE1 GLU A 418 2.19
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 SER A 41 -61.97 65.43
REMARK 500 GLU A 48 -92.39 179.08
REMARK 500 THR A 110 -88.80 -104.79
REMARK 500 ASP A 323 90.45 -62.13
REMARK 500 LYS A 340 95.16 88.04
REMARK 500 THR A 341 70.21 -118.86
REMARK 500 PRO A 349 -91.18 -70.49
REMARK 500 GLU B 45 -74.09 -61.83
REMARK 500 ARG B 46 47.88 -88.04
REMARK 500 ASN B 78 44.43 -92.92
REMARK 500 SER B 95 -158.50 -87.36
REMARK 500 THR B 107 -99.03 -100.52
REMARK 500 SER B 129 76.79 -160.43
REMARK 500 PRO B 173 76.43 -64.32
REMARK 500 GLN B 245 -41.91 -168.89
REMARK 500 LEU B 263 72.13 -106.21
REMARK 500 LEU B 273 -98.73 -108.99
REMARK 500 THR B 274 174.63 63.34
REMARK 500 MET B 300 30.31 -91.27
REMARK 500 ALA B 302 76.19 -65.51
REMARK 500 ASN B 337 40.58 -91.77
REMARK 500 PRO B 358 -166.55 -65.74
REMARK 500 ASN B 370 69.03 -102.71
REMARK 500 VAL C 355 -76.30 -137.03
REMARK 500 LYS C 404 -154.54 56.39
REMARK 500 PHE C 408 94.45 -67.97
REMARK 500 LYS C 489 26.63 -140.81
REMARK 500 LEU C 499 -80.72 -62.36
REMARK 500 GLU C 502 -50.55 -129.44
REMARK 500 ILE C 532 -71.35 -82.82
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 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP A 502 O3G
REMARK 620 2 GTP A 502 O2B 60.8
REMARK 620 3 HOH A 604 O 49.3 81.5
REMARK 620 4 HOH A 606 O 73.2 133.0 75.5
REMARK 620 5 HOH A 607 O 111.2 107.2 152.3 79.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP B 502 O3G
REMARK 620 2 GTP B 502 O2G 65.7
REMARK 620 3 HOH B 608 O 135.4 80.0
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 MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP B 502
DBREF 4U3J A 1 447 UNP P09733 TBA1_YEAST 1 447
DBREF 4U3J B 1 457 UNP P02557 TBB_YEAST 1 457
DBREF 4U3J C 318 560 UNP P46675 STU2_YEAST 318 560
SEQADV 4U3J ARG B 175 UNP P02557 THR 175 ENGINEERED MUTATION
SEQADV 4U3J ARG B 179 UNP P02557 VAL 179 ENGINEERED MUTATION
SEQADV 4U3J HIS B 458 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS B 459 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS B 460 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS B 461 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS B 462 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS B 463 UNP P02557 EXPRESSION TAG
SEQADV 4U3J HIS C 561 UNP P46675 EXPRESSION TAG
SEQADV 4U3J HIS C 562 UNP P46675 EXPRESSION TAG
SEQADV 4U3J HIS C 563 UNP P46675 EXPRESSION TAG
SEQADV 4U3J HIS C 564 UNP P46675 EXPRESSION TAG
SEQADV 4U3J HIS C 565 UNP P46675 EXPRESSION TAG
SEQADV 4U3J HIS C 566 UNP P46675 EXPRESSION TAG
SEQRES 1 A 447 MET ARG GLU VAL ILE SER ILE ASN VAL GLY GLN ALA GLY
SEQRES 2 A 447 CYS GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR SER LEU
SEQRES 3 A 447 GLU HIS GLY ILE LYS PRO ASP GLY HIS LEU GLU ASP GLY
SEQRES 4 A 447 LEU SER LYS PRO LYS GLY GLY GLU GLU GLY PHE SER THR
SEQRES 5 A 447 PHE PHE HIS GLU THR GLY TYR GLY LYS PHE VAL PRO ARG
SEQRES 6 A 447 ALA ILE TYR VAL ASP LEU GLU PRO ASN VAL ILE ASP GLU
SEQRES 7 A 447 VAL ARG ASN GLY PRO TYR LYS ASP LEU PHE HIS PRO GLU
SEQRES 8 A 447 GLN LEU ILE SER GLY LYS GLU ASP ALA ALA ASN ASN TYR
SEQRES 9 A 447 ALA ARG GLY HIS TYR THR VAL GLY ARG GLU ILE LEU GLY
SEQRES 10 A 447 ASP VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS
SEQRES 11 A 447 ASP GLY LEU GLN GLY PHE LEU PHE THR HIS SER LEU GLY
SEQRES 12 A 447 GLY GLY THR GLY SER GLY LEU GLY SER LEU LEU LEU GLU
SEQRES 13 A 447 GLU LEU SER ALA GLU TYR GLY LYS LYS SER LYS LEU GLU
SEQRES 14 A 447 PHE ALA VAL TYR PRO ALA PRO GLN VAL SER THR SER VAL
SEQRES 15 A 447 VAL GLU PRO TYR ASN THR VAL LEU THR THR HIS THR THR
SEQRES 16 A 447 LEU GLU HIS ALA ASP CYS THR PHE MET VAL ASP ASN GLU
SEQRES 17 A 447 ALA ILE TYR ASP MET CYS LYS ARG ASN LEU ASP ILE PRO
SEQRES 18 A 447 ARG PRO SER PHE ALA ASN LEU ASN ASN LEU ILE ALA GLN
SEQRES 19 A 447 VAL VAL SER SER VAL THR ALA SER LEU ARG PHE ASP GLY
SEQRES 20 A 447 SER LEU ASN VAL ASP LEU ASN GLU PHE GLN THR ASN LEU
SEQRES 21 A 447 VAL PRO TYR PRO ARG ILE HIS PHE PRO LEU VAL SER TYR
SEQRES 22 A 447 SER PRO VAL LEU SER LYS SER LYS ALA PHE HIS GLU SER
SEQRES 23 A 447 ASN SER VAL SER GLU ILE THR ASN ALA CYS PHE GLU PRO
SEQRES 24 A 447 GLY ASN GLN MET VAL LYS CYS ASP PRO ARG ASP GLY LYS
SEQRES 25 A 447 TYR MET ALA THR CYS LEU LEU TYR ARG GLY ASP VAL VAL
SEQRES 26 A 447 THR ARG ASP VAL GLN ARG ALA VAL GLU GLN VAL LYS ASN
SEQRES 27 A 447 LYS LYS THR VAL GLN LEU VAL ASP TRP CYS PRO THR GLY
SEQRES 28 A 447 PHE LYS ILE GLY ILE CYS TYR GLU PRO PRO THR ALA THR
SEQRES 29 A 447 PRO ASN SER GLN LEU ALA THR VAL ASP ARG ALA VAL CYS
SEQRES 30 A 447 MET LEU SER ASN THR THR SER ILE ALA GLU ALA TRP LYS
SEQRES 31 A 447 ARG ILE ASP ARG LYS PHE ASP LEU MET TYR ALA LYS ARG
SEQRES 32 A 447 ALA PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU
SEQRES 33 A 447 GLY GLU PHE THR GLU ALA ARG GLU ASP LEU ALA ALA LEU
SEQRES 34 A 447 GLU ARG ASP TYR ILE GLU VAL GLY ALA ASP SER TYR ALA
SEQRES 35 A 447 GLU GLU GLU GLU PHE
SEQRES 1 B 463 MET ARG GLU ILE ILE HIS ILE SER THR GLY GLN CYS GLY
SEQRES 2 B 463 ASN GLN ILE GLY ALA ALA PHE TRP GLU THR ILE CYS GLY
SEQRES 3 B 463 GLU HIS GLY LEU ASP PHE ASN GLY THR TYR HIS GLY HIS
SEQRES 4 B 463 ASP ASP ILE GLN LYS GLU ARG LEU ASN VAL TYR PHE ASN
SEQRES 5 B 463 GLU ALA SER SER GLY LYS TRP VAL PRO ARG SER ILE ASN
SEQRES 6 B 463 VAL ASP LEU GLU PRO GLY THR ILE ASP ALA VAL ARG ASN
SEQRES 7 B 463 SER ALA ILE GLY ASN LEU PHE ARG PRO ASP ASN TYR ILE
SEQRES 8 B 463 PHE GLY GLN SER SER ALA GLY ASN VAL TRP ALA LYS GLY
SEQRES 9 B 463 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL MET
SEQRES 10 B 463 ASP VAL ILE ARG ARG GLU ALA GLU GLY CYS ASP SER LEU
SEQRES 11 B 463 GLN GLY PHE GLN ILE THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 B 463 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 B 463 GLU GLU PHE PRO ASP ARG MET MET ALA THR PHE SER VAL
SEQRES 14 B 463 LEU PRO SER PRO LYS ARG SER ASP THR ARG VAL GLU PRO
SEQRES 15 B 463 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU HIS
SEQRES 16 B 463 SER ASP GLU THR PHE CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 B 463 ASP ILE CYS GLN ARG THR LEU LYS LEU ASN GLN PRO SER
SEQRES 18 B 463 TYR GLY ASP LEU ASN ASN LEU VAL SER SER VAL MET SER
SEQRES 19 B 463 GLY VAL THR THR SER LEU ARG TYR PRO GLY GLN LEU ASN
SEQRES 20 B 463 SER ASP LEU ARG LYS LEU ALA VAL ASN LEU VAL PRO PHE
SEQRES 21 B 463 PRO ARG LEU HIS PHE PHE MET VAL GLY TYR ALA PRO LEU
SEQRES 22 B 463 THR ALA ILE GLY SER GLN SER PHE ARG SER LEU THR VAL
SEQRES 23 B 463 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 B 463 MET ALA ALA ALA ASP PRO ARG ASN GLY ARG TYR LEU THR
SEQRES 25 B 463 VAL ALA ALA PHE PHE ARG GLY LYS VAL SER VAL LYS GLU
SEQRES 26 B 463 VAL GLU ASP GLU MET HIS LYS VAL GLN SER LYS ASN SER
SEQRES 27 B 463 ASP TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL GLN THR
SEQRES 28 B 463 ALA VAL CYS SER VAL ALA PRO GLN GLY LEU ASP MET ALA
SEQRES 29 B 463 ALA THR PHE ILE ALA ASN SER THR SER ILE GLN GLU LEU
SEQRES 30 B 463 PHE LYS ARG VAL GLY ASP GLN PHE SER ALA MET PHE LYS
SEQRES 31 B 463 ARG LYS ALA PHE LEU HIS TRP TYR THR SER GLU GLY MET
SEQRES 32 B 463 ASP GLU LEU GLU PHE SER GLU ALA GLU SER ASN MET ASN
SEQRES 33 B 463 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN GLU ALA THR
SEQRES 34 B 463 VAL GLU ASP ASP GLU GLU VAL ASP GLU ASN GLY ASP PHE
SEQRES 35 B 463 GLY ALA PRO GLN ASN GLN ASP GLU PRO ILE THR GLU ASN
SEQRES 36 B 463 PHE GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 249 MET LEU PRO GLU GLU THR ILE LEU ASP LYS LEU PRO LYS
SEQRES 2 C 249 ASP PHE GLN GLU ARG ILE THR SER SER LYS TRP LYS ASP
SEQRES 3 C 249 ARG VAL GLU ALA LEU GLU GLU PHE TRP ASP SER VAL LEU
SEQRES 4 C 249 SER GLN THR LYS LYS LEU LYS SER THR SER GLN ASN TYR
SEQRES 5 C 249 SER ASN LEU LEU GLY ILE TYR GLY HIS ILE ILE GLN LYS
SEQRES 6 C 249 ASP ALA ASN ILE GLN ALA VAL ALA LEU ALA ALA GLN SER
SEQRES 7 C 249 VAL GLU LEU ILE CYS ASP LYS LEU LYS THR PRO GLY PHE
SEQRES 8 C 249 SER LYS ASP TYR VAL SER LEU VAL PHE THR PRO LEU LEU
SEQRES 9 C 249 ASP ARG THR LYS GLU LYS LYS PRO SER VAL ILE GLU ALA
SEQRES 10 C 249 ILE ARG LYS ALA LEU LEU THR ILE CYS LYS TYR TYR ASP
SEQRES 11 C 249 PRO LEU ALA SER SER GLY ARG ASN GLU ASP MET LEU LYS
SEQRES 12 C 249 ASP ILE LEU GLU HIS MET LYS HIS LYS THR PRO GLN ILE
SEQRES 13 C 249 ARG MET GLU CYS THR GLN LEU PHE ASN ALA SER MET LYS
SEQRES 14 C 249 GLU GLU LYS ASP GLY TYR SER THR LEU GLN ARG TYR LEU
SEQRES 15 C 249 LYS ASP GLU VAL VAL PRO ILE VAL ILE GLN ILE VAL ASN
SEQRES 16 C 249 ASP THR GLN PRO ALA ILE ARG THR ILE GLY PHE GLU SER
SEQRES 17 C 249 PHE ALA ILE LEU ILE LYS ILE PHE GLY MET ASN THR PHE
SEQRES 18 C 249 VAL LYS THR LEU GLU HIS LEU ASP ASN LEU LYS ARG LYS
SEQRES 19 C 249 LYS ILE GLU GLU THR VAL LYS THR LEU HIS HIS HIS HIS
SEQRES 20 C 249 HIS HIS
HET MG A 501 1
HET GTP A 502 42
HET MG B 501 1
HET GTP B 502 42
HETNAM MG MAGNESIUM ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 4 MG 2(MG 2+)
FORMUL 5 GTP 2(C10 H16 N5 O14 P3)
FORMUL 8 HOH *21(H2 O)
HELIX 1 AA1 GLY A 10 HIS A 28 1 19
HELIX 2 AA2 GLU A 72 GLY A 82 1 11
HELIX 3 AA3 ASN A 103 TYR A 109 1 7
HELIX 4 AA4 VAL A 111 ASP A 128 1 18
HELIX 5 AA5 SER A 148 TYR A 162 1 15
HELIX 6 AA6 ALA A 175 SER A 179 5 5
HELIX 7 AA7 VAL A 183 LEU A 196 1 14
HELIX 8 AA8 ASN A 207 ASN A 217 1 11
HELIX 9 AA9 SER A 224 THR A 240 1 17
HELIX 10 AB1 THR A 240 PHE A 245 1 6
HELIX 11 AB2 ASP A 252 VAL A 261 1 10
HELIX 12 AB3 VAL A 289 CYS A 296 1 8
HELIX 13 AB4 PHE A 297 GLN A 302 5 6
HELIX 14 AB5 VAL A 325 LYS A 339 1 15
HELIX 15 AB6 ILE A 385 ALA A 401 1 17
HELIX 16 AB7 PHE A 405 GLY A 411 1 7
HELIX 17 AB8 GLU A 416 GLY A 437 1 22
HELIX 18 AB9 GLY B 10 HIS B 28 1 19
HELIX 19 AC1 ASP B 41 ARG B 46 1 6
HELIX 20 AC2 LEU B 47 VAL B 49 5 3
HELIX 21 AC3 GLU B 69 ASN B 78 1 10
HELIX 22 AC4 ARG B 86 ASP B 88 5 3
HELIX 23 AC5 VAL B 100 TYR B 106 1 7
HELIX 24 AC6 LEU B 112 GLY B 126 1 15
HELIX 25 AC7 GLY B 142 PHE B 159 1 18
HELIX 26 AC8 VAL B 180 SER B 196 1 17
HELIX 27 AC9 ASN B 204 GLN B 212 1 9
HELIX 28 AD1 SER B 221 THR B 237 1 17
HELIX 29 AD2 THR B 237 TYR B 242 1 6
HELIX 30 AD3 ASP B 249 VAL B 258 1 10
HELIX 31 AD4 THR B 285 ASP B 295 1 11
HELIX 32 AD5 ALA B 296 MET B 299 5 4
HELIX 33 AD6 ASP B 304 GLY B 308 5 5
HELIX 34 AD7 SER B 322 ASN B 337 1 16
HELIX 35 AD8 SER B 338 PHE B 341 5 4
HELIX 36 AD9 ILE B 374 LYS B 390 1 17
HELIX 37 AE1 LEU B 395 SER B 400 1 6
HELIX 38 AE2 ASP B 404 GLU B 427 1 24
HELIX 39 AE3 ILE C 324 LEU C 328 5 5
HELIX 40 AE4 ASP C 331 THR C 337 1 7
HELIX 41 AE5 LYS C 340 VAL C 355 1 16
HELIX 42 AE6 LEU C 356 THR C 359 5 4
HELIX 43 AE7 TYR C 369 ASP C 383 1 15
HELIX 44 AE8 ASN C 385 LYS C 404 1 20
HELIX 45 AE9 SER C 409 ARG C 423 1 15
HELIX 46 AF1 THR C 424 GLU C 426 5 3
HELIX 47 AF2 LYS C 428 TYR C 446 1 19
HELIX 48 AF3 ASN C 455 MET C 466 1 12
HELIX 49 AF4 THR C 470 GLU C 488 1 19
HELIX 50 AF5 TYR C 492 TYR C 498 1 7
HELIX 51 AF6 GLU C 502 ASN C 512 1 11
HELIX 52 AF7 GLN C 515 GLY C 534 1 20
HELIX 53 AF8 PHE C 538 GLU C 543 1 6
HELIX 54 AF9 ASP C 546 THR C 559 1 14
SHEET 1 AA1 6 LEU A 93 SER A 95 0
SHEET 2 AA1 6 ALA A 66 ASP A 70 1 N TYR A 68 O ILE A 94
SHEET 3 AA1 6 VAL A 4 VAL A 9 1 N ASN A 8 O ILE A 67
SHEET 4 AA1 6 GLY A 135 SER A 141 1 O THR A 139 N ILE A 7
SHEET 5 AA1 6 SER A 166 TYR A 173 1 O PHE A 170 N PHE A 138
SHEET 6 AA1 6 CYS A 201 ASP A 206 1 O PHE A 203 N GLU A 169
SHEET 1 AA2 2 PHE A 54 GLU A 56 0
SHEET 2 AA2 2 PHE A 62 PRO A 64 -1 O VAL A 63 N HIS A 55
SHEET 1 AA3 4 LEU A 270 SER A 274 0
SHEET 2 AA3 4 ARG A 374 THR A 382 -1 O SER A 380 N LEU A 270
SHEET 3 AA3 4 TYR A 313 GLY A 322 -1 N LEU A 319 O CYS A 377
SHEET 4 AA3 4 PHE A 352 CYS A 357 1 O GLY A 355 N TYR A 320
SHEET 1 AA410 TYR B 90 PHE B 92 0
SHEET 2 AA410 SER B 63 ASP B 67 1 N ASN B 65 O ILE B 91
SHEET 3 AA410 ILE B 4 THR B 9 1 N SER B 8 O VAL B 66
SHEET 4 AA410 GLY B 132 SER B 138 1 O GLN B 134 N ILE B 7
SHEET 5 AA410 MET B 163 LEU B 170 1 O PHE B 167 N ILE B 135
SHEET 6 AA410 GLU B 198 ASP B 203 1 O PHE B 200 N THR B 166
SHEET 7 AA410 PHE B 265 ALA B 271 1 O PHE B 266 N THR B 199
SHEET 8 AA410 MET B 363 SER B 371 -1 O ALA B 365 N ALA B 271
SHEET 9 AA410 TYR B 310 GLY B 319 -1 N PHE B 316 O THR B 366
SHEET 10 AA410 VAL B 349 CYS B 354 1 O GLN B 350 N VAL B 313
SHEET 1 AA5 2 PHE B 51 GLU B 53 0
SHEET 2 AA5 2 TRP B 59 PRO B 61 -1 O VAL B 60 N ASN B 52
LINK MG MG A 501 O3G GTP A 502 1555 1555 2.95
LINK MG MG A 501 O2B GTP A 502 1555 1555 2.35
LINK MG MG A 501 O HOH A 604 1555 1555 2.33
LINK MG MG A 501 O HOH A 606 1555 1555 2.03
LINK MG MG A 501 O HOH A 607 1555 1555 2.35
LINK MG MG B 501 O3G GTP B 502 1555 1555 2.00
LINK MG MG B 501 O2G GTP B 502 1555 1555 2.50
LINK MG MG B 501 O HOH B 608 1555 1555 2.16
CISPEP 1 GLY A 46 GLU A 47 0 0.81
CISPEP 2 SER A 274 PRO A 275 0 1.00
CISPEP 3 VAL A 342 GLN A 343 0 -2.45
CISPEP 4 PRO B 243 GLY B 244 0 -0.21
CISPEP 5 ALA B 271 PRO B 272 0 2.16
CISPEP 6 GLN B 359 GLY B 360 0 0.65
CISPEP 7 THR C 405 PRO C 406 0 1.12
SITE 1 AC1 6 GLN A 11 GLU A 72 GTP A 502 HOH A 604
SITE 2 AC1 6 HOH A 606 HOH A 607
SITE 1 AC2 24 GLY A 10 GLN A 11 ALA A 12 GLN A 15
SITE 2 AC2 24 ALA A 101 ASN A 102 SER A 141 GLY A 144
SITE 3 AC2 24 GLY A 145 THR A 146 GLY A 147 VAL A 178
SITE 4 AC2 24 THR A 180 GLU A 184 ASN A 207 PHE A 225
SITE 5 AC2 24 ASN A 229 ILE A 232 MG A 501 HOH A 604
SITE 6 AC2 24 HOH A 606 HOH A 607 HOH A 609 LYS B 252
SITE 1 AC3 2 GTP B 502 HOH B 608
SITE 1 AC4 17 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC4 17 ALA B 97 ASN B 99 SER B 138 GLY B 141
SITE 3 AC4 17 GLY B 142 THR B 143 GLY B 144 GLU B 181
SITE 4 AC4 17 ASN B 204 TYR B 222 ASN B 226 MG B 501
SITE 5 AC4 17 HOH B 608
CRYST1 111.909 89.573 135.508 90.00 112.31 90.00 C 1 2 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 0.008936 0.000000 0.003666 0.00000
SCALE2 0.000000 0.011164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
