HEADER CELL CYCLE 03-MAR-15 4YJ2
TITLE CRYSTAL STRUCTURE OF TUBULIN BOUND TO MI-181
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA-1B CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ALPHA-TUBULIN UBIQUITOUS,TUBULIN K-ALPHA-1,TUBULIN ALPHA-
COMPND 5 UBIQUITOUS CHAIN;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TUBULIN BETA-2B CHAIN;
COMPND 8 CHAIN: B, D;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: STATHMIN-4;
COMPND 11 CHAIN: E;
COMPND 12 FRAGMENT: STATHMIN-LIKE DOMAIN;
COMPND 13 SYNONYM: STATHMIN-LIKE PROTEIN B3,RB3;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: TUBULIN-TYROSINE LIGASE;
COMPND 18 CHAIN: F;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 OTHER_DETAILS: BRAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: BOVINE;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 OTHER_DETAILS: BRAIN;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: STMN4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 21 MOL_ID: 4;
SOURCE 22 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 23 ORGANISM_COMMON: CHICKEN;
SOURCE 24 ORGANISM_TAXID: 9031;
SOURCE 25 GENE: TTL;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA-TUBULIN, BETA-TUBULIN, STATHMIN, MI-181, CELL CYCLE INHIBITOR
KEYWDS 2 COMPLEX, MICROTUBULE, CYTOSKELETON, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.MCNAMARA,J.Z.TORRES,T.O.YEATES
REVDAT 5 27-SEP-23 4YJ2 1 LINK
REVDAT 4 04-DEC-19 4YJ2 1 REMARK
REVDAT 3 20-SEP-17 4YJ2 1 SOURCE JRNL REMARK
REVDAT 2 01-JUL-15 4YJ2 1 JRNL
REVDAT 1 27-MAY-15 4YJ2 0
JRNL AUTH D.E.MCNAMARA,S.SENESE,T.O.YEATES,J.Z.TORRES
JRNL TITL STRUCTURES OF POTENT ANTICANCER COMPOUNDS BOUND TO TUBULIN.
JRNL REF PROTEIN SCI. V. 24 1164 2015
JRNL REFN ESSN 1469-896X
JRNL PMID 25970265
JRNL DOI 10.1002/PRO.2704
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 92595
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9261
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 90.7728 - 8.0768 0.99 2982 333 0.1664 0.2026
REMARK 3 2 8.0768 - 6.4113 0.99 2863 318 0.1690 0.1956
REMARK 3 3 6.4113 - 5.6010 1.00 2829 314 0.1809 0.2334
REMARK 3 4 5.6010 - 5.0890 1.00 2833 315 0.1728 0.2119
REMARK 3 5 5.0890 - 4.7242 0.99 2793 311 0.1425 0.1821
REMARK 3 6 4.7242 - 4.4457 1.00 2795 310 0.1352 0.1748
REMARK 3 7 4.4457 - 4.2231 1.00 2802 311 0.1492 0.1972
REMARK 3 8 4.2231 - 4.0392 1.00 2769 308 0.1638 0.2064
REMARK 3 9 4.0392 - 3.8837 1.00 2797 311 0.1713 0.2221
REMARK 3 10 3.8837 - 3.7497 1.00 2751 306 0.1829 0.2082
REMARK 3 11 3.7497 - 3.6325 1.00 2791 310 0.1859 0.2389
REMARK 3 12 3.6325 - 3.5286 1.00 2773 308 0.2027 0.2437
REMARK 3 13 3.5286 - 3.4357 1.00 2769 308 0.2102 0.2791
REMARK 3 14 3.4357 - 3.3519 1.00 2785 309 0.2149 0.2690
REMARK 3 15 3.3519 - 3.2757 1.00 2731 303 0.2147 0.2325
REMARK 3 16 3.2757 - 3.2060 1.00 2788 310 0.2271 0.2735
REMARK 3 17 3.2060 - 3.1419 1.00 2775 308 0.2314 0.2676
REMARK 3 18 3.1419 - 3.0826 1.00 2730 304 0.2318 0.2776
REMARK 3 19 3.0826 - 3.0275 1.00 2781 309 0.2314 0.2801
REMARK 3 20 3.0275 - 2.9762 1.00 2740 304 0.2370 0.2783
REMARK 3 21 2.9762 - 2.9282 1.00 2762 307 0.2406 0.2748
REMARK 3 22 2.9282 - 2.8831 1.00 2751 306 0.2426 0.2949
REMARK 3 23 2.8831 - 2.8407 1.00 2752 306 0.2473 0.3189
REMARK 3 24 2.8407 - 2.8007 1.00 2767 307 0.2494 0.3451
REMARK 3 25 2.8007 - 2.7629 1.00 2737 305 0.2644 0.2985
REMARK 3 26 2.7629 - 2.7270 1.00 2757 306 0.2718 0.3214
REMARK 3 27 2.7270 - 2.6929 1.00 2746 305 0.2688 0.3222
REMARK 3 28 2.6929 - 2.6604 0.99 2732 303 0.2807 0.3380
REMARK 3 29 2.6604 - 2.6295 1.00 2730 304 0.2892 0.3337
REMARK 3 30 2.6295 - 2.6000 0.98 2723 302 0.3116 0.3393
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.15
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 17637
REMARK 3 ANGLE : 0.551 23853
REMARK 3 CHIRALITY : 0.023 2595
REMARK 3 PLANARITY : 0.003 3088
REMARK 3 DIHEDRAL : 11.518 6513
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 1:180)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5884 88.2198 -51.8720
REMARK 3 T TENSOR
REMARK 3 T11: 0.6485 T22: 0.6126
REMARK 3 T33: 0.5169 T12: 0.1579
REMARK 3 T13: 0.1337 T23: 0.1970
REMARK 3 L TENSOR
REMARK 3 L11: 1.4426 L22: 5.7986
REMARK 3 L33: 2.7726 L12: 0.1124
REMARK 3 L13: -0.2963 L23: -1.2861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.1294 S13: 0.2169
REMARK 3 S21: 0.4150 S22: 0.3830 S23: 0.5971
REMARK 3 S31: -0.8071 S32: -0.5854 S33: -0.3732
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 181:311)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1189 82.2553 -65.9884
REMARK 3 T TENSOR
REMARK 3 T11: 0.5058 T22: 0.4462
REMARK 3 T33: 0.4618 T12: 0.0332
REMARK 3 T13: 0.0660 T23: 0.0986
REMARK 3 L TENSOR
REMARK 3 L11: 1.8764 L22: 4.4961
REMARK 3 L33: 4.4945 L12: 1.0571
REMARK 3 L13: -0.4803 L23: -1.3930
REMARK 3 S TENSOR
REMARK 3 S11: 0.1043 S12: 0.1984 S13: 0.2181
REMARK 3 S21: -0.3790 S22: 0.0221 S23: -0.1410
REMARK 3 S31: -0.3124 S32: -0.0036 S33: -0.1127
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 312:401)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8995 83.0896 -73.4226
REMARK 3 T TENSOR
REMARK 3 T11: 0.5493 T22: 0.5598
REMARK 3 T33: 0.4634 T12: 0.0025
REMARK 3 T13: 0.1552 T23: 0.0968
REMARK 3 L TENSOR
REMARK 3 L11: 1.1479 L22: 5.9860
REMARK 3 L33: 3.1452 L12: 0.3049
REMARK 3 L13: 0.7411 L23: -1.5363
REMARK 3 S TENSOR
REMARK 3 S11: -0.2045 S12: 0.3666 S13: 0.0711
REMARK 3 S21: -1.2224 S22: 0.2588 S23: -0.2422
REMARK 3 S31: -0.0094 S32: 0.0226 S33: -0.0486
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 402:436)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6647 61.8437 -60.4603
REMARK 3 T TENSOR
REMARK 3 T11: 0.5581 T22: 0.6491
REMARK 3 T33: 0.6100 T12: -0.1371
REMARK 3 T13: -0.1045 T23: 0.1479
REMARK 3 L TENSOR
REMARK 3 L11: 4.0263 L22: 6.7832
REMARK 3 L33: 2.0626 L12: 1.7310
REMARK 3 L13: -1.8055 L23: -5.3982
REMARK 3 S TENSOR
REMARK 3 S11: -0.2268 S12: 0.4054 S13: -0.3202
REMARK 3 S21: -1.0635 S22: 0.9084 S23: 0.4585
REMARK 3 S31: 1.0590 S32: -1.8495 S33: -0.5789
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 437:439)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.0835 74.4559 -54.5546
REMARK 3 T TENSOR
REMARK 3 T11: 0.5531 T22: 0.4469
REMARK 3 T33: 0.5948 T12: 0.0697
REMARK 3 T13: 0.1199 T23: 0.1714
REMARK 3 L TENSOR
REMARK 3 L11: 4.4451 L22: 2.0426
REMARK 3 L33: 1.4484 L12: 1.6073
REMARK 3 L13: 0.1077 L23: -0.5349
REMARK 3 S TENSOR
REMARK 3 S11: -0.1420 S12: -0.9352 S13: -0.7188
REMARK 3 S21: -0.2650 S22: -0.3531 S23: 0.3387
REMARK 3 S31: -0.2994 S32: 1.0723 S33: 0.5477
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 1:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8110 70.0978 -19.1604
REMARK 3 T TENSOR
REMARK 3 T11: 0.6412 T22: 0.4047
REMARK 3 T33: 0.5014 T12: -0.0388
REMARK 3 T13: 0.0391 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 7.0430 L22: 4.5241
REMARK 3 L33: 6.0723 L12: 2.8549
REMARK 3 L13: -1.7808 L23: -1.3280
REMARK 3 S TENSOR
REMARK 3 S11: 0.3934 S12: -0.3271 S13: 0.9745
REMARK 3 S21: 0.6528 S22: -0.2484 S23: 0.1009
REMARK 3 S31: -1.3639 S32: 0.3961 S33: -0.1514
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 89:127)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7709 56.3190 -14.5360
REMARK 3 T TENSOR
REMARK 3 T11: 0.4564 T22: 0.6493
REMARK 3 T33: 0.4796 T12: 0.0281
REMARK 3 T13: 0.0798 T23: 0.0963
REMARK 3 L TENSOR
REMARK 3 L11: 3.0458 L22: 6.0565
REMARK 3 L33: 3.2922 L12: 0.9051
REMARK 3 L13: -0.5949 L23: -0.5987
REMARK 3 S TENSOR
REMARK 3 S11: 0.1377 S12: -0.5512 S13: -0.0385
REMARK 3 S21: 0.5213 S22: 0.0718 S23: 0.5108
REMARK 3 S31: -0.4952 S32: -0.3784 S33: -0.2235
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 128:197)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0832 53.3022 -26.0547
REMARK 3 T TENSOR
REMARK 3 T11: 0.2688 T22: 0.4438
REMARK 3 T33: 0.3920 T12: -0.0531
REMARK 3 T13: 0.0327 T23: 0.1073
REMARK 3 L TENSOR
REMARK 3 L11: 3.3407 L22: 9.0354
REMARK 3 L33: 4.9444 L12: -2.4494
REMARK 3 L13: 0.4043 L23: -2.9556
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.2612 S13: 0.1782
REMARK 3 S21: 0.0291 S22: 0.0861 S23: 0.1712
REMARK 3 S31: -0.2322 S32: -0.3875 S33: -0.0643
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 198:223)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0185 50.9260 -28.2317
REMARK 3 T TENSOR
REMARK 3 T11: 0.4994 T22: 0.7287
REMARK 3 T33: 0.5794 T12: 0.0122
REMARK 3 T13: 0.0396 T23: 0.3107
REMARK 3 L TENSOR
REMARK 3 L11: 9.7904 L22: 2.9357
REMARK 3 L33: 4.9243 L12: -0.9633
REMARK 3 L13: 1.7724 L23: 0.9216
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: 0.5947 S13: -0.2376
REMARK 3 S21: 0.1479 S22: -0.1543 S23: -0.6918
REMARK 3 S31: 0.3296 S32: 1.2267 S33: 0.1298
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 224:295)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0097 62.1691 -35.7945
REMARK 3 T TENSOR
REMARK 3 T11: 0.4425 T22: 0.5125
REMARK 3 T33: 0.5128 T12: -0.0845
REMARK 3 T13: 0.0308 T23: 0.1746
REMARK 3 L TENSOR
REMARK 3 L11: 2.6174 L22: 2.4994
REMARK 3 L33: 4.3890 L12: -0.2632
REMARK 3 L13: 0.1192 L23: -0.4807
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.3067 S13: 0.5813
REMARK 3 S21: 0.0254 S22: -0.1539 S23: -0.3986
REMARK 3 S31: -0.5312 S32: 0.6893 S33: 0.1214
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 296:373)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2083 60.8154 -44.7688
REMARK 3 T TENSOR
REMARK 3 T11: 0.4239 T22: 0.6629
REMARK 3 T33: 0.5193 T12: -0.0337
REMARK 3 T13: 0.0741 T23: 0.1625
REMARK 3 L TENSOR
REMARK 3 L11: 3.5538 L22: 4.0061
REMARK 3 L33: 4.4971 L12: 1.9112
REMARK 3 L13: 1.8316 L23: 0.9885
REMARK 3 S TENSOR
REMARK 3 S11: -0.3450 S12: 0.4145 S13: 0.1368
REMARK 3 S21: -0.5914 S22: 0.1454 S23: -0.4326
REMARK 3 S31: -0.2640 S32: 0.9868 S33: 0.1684
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 374:401)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1706 42.1780 -34.0847
REMARK 3 T TENSOR
REMARK 3 T11: 0.4604 T22: 0.5234
REMARK 3 T33: 0.4869 T12: 0.0794
REMARK 3 T13: 0.0661 T23: 0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 2.5788 L22: 9.7554
REMARK 3 L33: 7.7674 L12: 5.1202
REMARK 3 L13: -3.8789 L23: -8.4745
REMARK 3 S TENSOR
REMARK 3 S11: -0.4461 S12: 0.2417 S13: -0.3915
REMARK 3 S21: -0.8383 S22: -0.1211 S23: -1.1141
REMARK 3 S31: 0.8870 S32: -0.0001 S33: 0.5336
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 402:438)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4989 38.1552 -31.0032
REMARK 3 T TENSOR
REMARK 3 T11: 0.5692 T22: 0.5890
REMARK 3 T33: 0.4814 T12: -0.0902
REMARK 3 T13: -0.0890 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 2.6362 L22: 7.3017
REMARK 3 L33: 2.1190 L12: 1.8807
REMARK 3 L13: -2.7326 L23: -5.9907
REMARK 3 S TENSOR
REMARK 3 S11: -0.5274 S12: 0.5982 S13: -0.3222
REMARK 3 S21: -1.4506 S22: 0.2136 S23: 0.2216
REMARK 3 S31: 1.5592 S32: -1.0065 S33: 0.3086
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 1:197)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1094 33.1839 12.1250
REMARK 3 T TENSOR
REMARK 3 T11: 0.3571 T22: 0.4712
REMARK 3 T33: 0.3725 T12: 0.0771
REMARK 3 T13: 0.0344 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 2.1041 L22: 4.3858
REMARK 3 L33: 2.2723 L12: 1.1129
REMARK 3 L13: 0.1258 L23: -0.1037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.3142 S13: 0.2010
REMARK 3 S21: 0.3405 S22: 0.0317 S23: 0.1591
REMARK 3 S31: -0.2379 S32: -0.2259 S33: -0.0118
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 198:440)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6646 26.0459 -3.0298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2896 T22: 0.3525
REMARK 3 T33: 0.3571 T12: 0.0765
REMARK 3 T13: 0.0390 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.1206 L22: 2.0263
REMARK 3 L33: 2.5039 L12: 0.6149
REMARK 3 L13: 0.1805 L23: -1.0583
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0610 S13: -0.0173
REMARK 3 S21: -0.0964 S22: -0.0848 S23: -0.2725
REMARK 3 S31: 0.0872 S32: 0.3991 S33: 0.1297
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 1:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8910 9.4588 44.1997
REMARK 3 T TENSOR
REMARK 3 T11: 0.7149 T22: 1.0041
REMARK 3 T33: 0.4325 T12: 0.1555
REMARK 3 T13: 0.0541 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 9.1052 L22: 8.7268
REMARK 3 L33: 4.9928 L12: 3.1933
REMARK 3 L13: -2.0746 L23: 0.6276
REMARK 3 S TENSOR
REMARK 3 S11: 0.2473 S12: -1.6976 S13: 0.3448
REMARK 3 S21: 0.8308 S22: 0.0505 S23: -0.1399
REMARK 3 S31: 0.0826 S32: 0.4009 S33: -0.3257
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN D AND RESID 89:295)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5561 -1.5462 33.2270
REMARK 3 T TENSOR
REMARK 3 T11: 0.6799 T22: 0.7123
REMARK 3 T33: 0.4854 T12: 0.0599
REMARK 3 T13: 0.0623 T23: 0.2012
REMARK 3 L TENSOR
REMARK 3 L11: 2.2325 L22: 2.0080
REMARK 3 L33: 3.6317 L12: 0.2468
REMARK 3 L13: -0.7017 L23: -0.3048
REMARK 3 S TENSOR
REMARK 3 S11: -0.0896 S12: -0.7368 S13: -0.3554
REMARK 3 S21: 0.5855 S22: 0.0863 S23: 0.1547
REMARK 3 S31: 0.4642 S32: 0.0659 S33: -0.0078
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN D AND RESID 296:401)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8308 -3.9012 21.1988
REMARK 3 T TENSOR
REMARK 3 T11: 0.5531 T22: 0.5661
REMARK 3 T33: 0.4610 T12: 0.1540
REMARK 3 T13: 0.0407 T23: 0.1320
REMARK 3 L TENSOR
REMARK 3 L11: 1.9429 L22: 2.9908
REMARK 3 L33: 3.8496 L12: 0.7232
REMARK 3 L13: -0.4652 L23: -0.4431
REMARK 3 S TENSOR
REMARK 3 S11: -0.1292 S12: -0.4446 S13: -0.3790
REMARK 3 S21: 0.1802 S22: 0.0503 S23: -0.1493
REMARK 3 S31: 0.5786 S32: 0.4219 S33: 0.0900
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 402:441)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2853 -16.2566 23.9432
REMARK 3 T TENSOR
REMARK 3 T11: 0.8986 T22: 0.6078
REMARK 3 T33: 0.7697 T12: -0.0351
REMARK 3 T13: 0.0732 T23: 0.2543
REMARK 3 L TENSOR
REMARK 3 L11: 5.9430 L22: 1.0663
REMARK 3 L33: 4.2205 L12: 0.4265
REMARK 3 L13: -3.3224 L23: 1.3353
REMARK 3 S TENSOR
REMARK 3 S11: -0.3374 S12: -0.3068 S13: -0.8316
REMARK 3 S21: 0.0728 S22: 0.1528 S23: 0.1914
REMARK 3 S31: 1.1288 S32: -0.5276 S33: 0.1190
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN E AND RESID 5:46)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6017 92.5199 -82.0578
REMARK 3 T TENSOR
REMARK 3 T11: 1.0858 T22: 0.6957
REMARK 3 T33: 0.5935 T12: 0.1042
REMARK 3 T13: -0.0456 T23: 0.1770
REMARK 3 L TENSOR
REMARK 3 L11: 5.9019 L22: 8.5955
REMARK 3 L33: 2.5514 L12: 5.0827
REMARK 3 L13: -1.3855 L23: -3.8057
REMARK 3 S TENSOR
REMARK 3 S11: -0.1434 S12: 0.4960 S13: 0.3837
REMARK 3 S21: -0.7745 S22: 0.6725 S23: 0.7893
REMARK 3 S31: 0.0320 S32: -0.6103 S33: -0.5190
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN E AND RESID 47:141)
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7199 28.8222 -4.9935
REMARK 3 T TENSOR
REMARK 3 T11: 0.4830 T22: 0.8472
REMARK 3 T33: 0.7655 T12: -0.0640
REMARK 3 T13: 0.0450 T23: 0.2460
REMARK 3 L TENSOR
REMARK 3 L11: 0.3059 L22: 3.4129
REMARK 3 L33: 4.5923 L12: 1.1570
REMARK 3 L13: -1.4741 L23: -3.5356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0441 S12: 0.0890 S13: 0.0272
REMARK 3 S21: -0.2863 S22: 0.6041 S23: 0.5662
REMARK 3 S31: 0.4545 S32: -0.9240 S33: -0.5256
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN F AND RESID 1:66)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1340 54.7053 -69.8233
REMARK 3 T TENSOR
REMARK 3 T11: 0.9858 T22: 0.6407
REMARK 3 T33: 0.6527 T12: 0.1001
REMARK 3 T13: 0.1765 T23: 0.1638
REMARK 3 L TENSOR
REMARK 3 L11: 6.4394 L22: 8.9953
REMARK 3 L33: 8.0777 L12: -3.7314
REMARK 3 L13: -1.1288 L23: -1.4598
REMARK 3 S TENSOR
REMARK 3 S11: -0.5451 S12: -0.5528 S13: -1.1455
REMARK 3 S21: 0.1300 S22: 0.2017 S23: 0.2646
REMARK 3 S31: 2.1164 S32: 0.6418 S33: 0.4125
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN F AND RESID 67:198)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8179 58.7209-104.7307
REMARK 3 T TENSOR
REMARK 3 T11: 1.0847 T22: 1.4118
REMARK 3 T33: 0.8746 T12: -0.2012
REMARK 3 T13: -0.1051 T23: -0.2710
REMARK 3 L TENSOR
REMARK 3 L11: 3.8927 L22: 4.5775
REMARK 3 L33: 4.6935 L12: -1.4076
REMARK 3 L13: -1.6643 L23: 1.6125
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 1.3280 S13: -0.9165
REMARK 3 S21: -1.1695 S22: -0.5679 S23: 1.2721
REMARK 3 S31: 0.3003 S32: -1.5629 S33: 0.5286
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN F AND RESID 199:378)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0439 56.2556 -91.8723
REMARK 3 T TENSOR
REMARK 3 T11: 1.0893 T22: 0.5169
REMARK 3 T33: 0.7032 T12: -0.0358
REMARK 3 T13: 0.1865 T23: -0.0677
REMARK 3 L TENSOR
REMARK 3 L11: 3.5702 L22: 1.8866
REMARK 3 L33: 5.3959 L12: -0.4224
REMARK 3 L13: -2.6938 L23: -0.1774
REMARK 3 S TENSOR
REMARK 3 S11: -0.6042 S12: 0.1502 S13: -0.9117
REMARK 3 S21: -0.2408 S22: 0.2852 S23: 0.0174
REMARK 3 S31: 1.4373 S32: 0.1185 S33: 0.2862
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 4YJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JANUARY 10, 2014
REMARK 200 DATA SCALING SOFTWARE : XSCALE JANUARY 10, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92610
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 90.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.10800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4O2B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES/IMIDAZOLE, 30 MM CACL2, 30
REMARK 280 MM MGCL2, 6% (W/V) PEG 4000, 7% GLYCEROL CRYO PARATONE-N OIL, PH
REMARK 280 6.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 52.41500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.82500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.41500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.82500
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 300 REMARK: THE TUBULIN-STATHMIN-TTL BIOLOGICAL ASSEMBLY CONTAINS
REMARK 300 CHAINS A, B, C, D, E, AND F
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 ASP A 438
REMARK 465 SER A 439
REMARK 465 VAL A 440
REMARK 465 GLU A 441
REMARK 465 GLY A 442
REMARK 465 GLU A 443
REMARK 465 GLY A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLU A 447
REMARK 465 GLY A 448
REMARK 465 GLU A 449
REMARK 465 GLU A 450
REMARK 465 TYR A 451
REMARK 465 THR B 276
REMARK 465 SER B 277
REMARK 465 ARG B 278
REMARK 465 GLY B 279
REMARK 465 SER B 280
REMARK 465 GLN B 281
REMARK 465 THR B 439
REMARK 465 ALA B 440
REMARK 465 ASP B 441
REMARK 465 GLU B 442
REMARK 465 GLN B 443
REMARK 465 GLY B 444
REMARK 465 GLU B 445
REMARK 465 PHE B 446
REMARK 465 GLU B 447
REMARK 465 GLU B 448
REMARK 465 GLU B 449
REMARK 465 GLU B 450
REMARK 465 GLY B 451
REMARK 465 GLU B 452
REMARK 465 ASP B 453
REMARK 465 GLU B 454
REMARK 465 ALA B 455
REMARK 465 GLU C 441
REMARK 465 GLY C 442
REMARK 465 GLU C 443
REMARK 465 GLY C 444
REMARK 465 GLU C 445
REMARK 465 GLU C 446
REMARK 465 GLU C 447
REMARK 465 GLY C 448
REMARK 465 GLU C 449
REMARK 465 GLU C 450
REMARK 465 TYR C 451
REMARK 465 THR D 276
REMARK 465 SER D 277
REMARK 465 ARG D 278
REMARK 465 GLY D 279
REMARK 465 SER D 280
REMARK 465 GLN D 281
REMARK 465 GLN D 282
REMARK 465 TYR D 283
REMARK 465 ARG D 284
REMARK 465 ALA D 285
REMARK 465 GLU D 442
REMARK 465 GLN D 443
REMARK 465 GLY D 444
REMARK 465 GLU D 445
REMARK 465 PHE D 446
REMARK 465 GLU D 447
REMARK 465 GLU D 448
REMARK 465 GLU D 449
REMARK 465 GLU D 450
REMARK 465 GLY D 451
REMARK 465 GLU D 452
REMARK 465 ASP D 453
REMARK 465 GLU D 454
REMARK 465 ALA D 455
REMARK 465 MET E 3
REMARK 465 ALA E 4
REMARK 465 ASP E 5
REMARK 465 PHE E 29
REMARK 465 ASP E 30
REMARK 465 GLY E 31
REMARK 465 VAL E 32
REMARK 465 PRO E 33
REMARK 465 GLU E 34
REMARK 465 PHE E 35
REMARK 465 ASN E 36
REMARK 465 ALA E 37
REMARK 465 SER E 38
REMARK 465 LEU E 39
REMARK 465 PRO E 40
REMARK 465 ARG E 41
REMARK 465 ARG E 42
REMARK 465 ARG E 43
REMARK 465 GLU E 142
REMARK 465 ALA E 143
REMARK 465 SER E 144
REMARK 465 ARG E 145
REMARK 465 PRO F 102
REMARK 465 THR F 103
REMARK 465 ASN F 104
REMARK 465 LEU F 105
REMARK 465 LYS F 106
REMARK 465 THR F 107
REMARK 465 PRO F 108
REMARK 465 VAL F 109
REMARK 465 ALA F 110
REMARK 465 PRO F 111
REMARK 465 ALA F 112
REMARK 465 GLN F 113
REMARK 465 ASN F 114
REMARK 465 GLY F 115
REMARK 465 ILE F 116
REMARK 465 ARG F 117
REMARK 465 HIS F 118
REMARK 465 LEU F 119
REMARK 465 ILE F 120
REMARK 465 ASN F 121
REMARK 465 ASN F 122
REMARK 465 THR F 123
REMARK 465 ARG F 124
REMARK 465 ARG F 137
REMARK 465 ARG F 138
REMARK 465 ARG F 139
REMARK 465 GLU F 140
REMARK 465 GLY F 141
REMARK 465 ARG F 142
REMARK 465 GLU F 143
REMARK 465 SER F 152
REMARK 465 ALA F 153
REMARK 465 GLY F 154
REMARK 465 ALA F 155
REMARK 465 LYS F 156
REMARK 465 GLY F 157
REMARK 465 GLU F 158
REMARK 465 GLY F 159
REMARK 465 ILE F 160
REMARK 465 LEU F 161
REMARK 465 ILE F 173
REMARK 465 ASP F 174
REMARK 465 GLU F 175
REMARK 465 GLN F 176
REMARK 465 GLY F 177
REMARK 465 GLN F 178
REMARK 465 VAL F 179
REMARK 465 ASN F 232
REMARK 465 PHE F 233
REMARK 465 GLN F 234
REMARK 465 ASP F 235
REMARK 465 LYS F 236
REMARK 465 THR F 237
REMARK 465 CYS F 238
REMARK 465 HIS F 239
REMARK 465 LEU F 240
REMARK 465 THR F 241
REMARK 465 ASN F 242
REMARK 465 HIS F 243
REMARK 465 CYS F 244
REMARK 465 ILE F 245
REMARK 465 GLN F 246
REMARK 465 LYS F 247
REMARK 465 GLU F 248
REMARK 465 TYR F 249
REMARK 465 SER F 250
REMARK 465 LYS F 251
REMARK 465 ASN F 252
REMARK 465 TYR F 253
REMARK 465 GLY F 254
REMARK 465 ARG F 255
REMARK 465 TYR F 256
REMARK 465 ASP F 363
REMARK 465 THR F 364
REMARK 465 GLY F 365
REMARK 465 GLN F 366
REMARK 465 LYS F 367
REMARK 465 THR F 368
REMARK 465 SER F 369
REMARK 465 GLN F 370
REMARK 465 PRO F 371
REMARK 465 THR F 372
REMARK 465 HIS F 379
REMARK 465 HIS F 380
REMARK 465 HIS F 381
REMARK 465 HIS F 382
REMARK 465 HIS F 383
REMARK 465 HIS F 384
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 OG1 THR A 41 O HOH A 601 2.10
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 TYR A 83 47.54 -105.59
REMARK 500 LYS A 96 -71.58 -80.28
REMARK 500 TYR A 108 -60.38 -97.30
REMARK 500 ALA A 281 -74.60 -61.64
REMARK 500 PHE A 404 -1.66 67.76
REMARK 500 HIS B 37 52.02 -144.67
REMARK 500 ASP B 39 7.48 -156.57
REMARK 500 PHE B 83 32.48 -95.57
REMARK 500 THR B 109 -83.40 -106.99
REMARK 500 ASN B 249 76.32 -110.56
REMARK 500 ASN B 339 46.99 -140.75
REMARK 500 TYR C 108 -81.23 -119.19
REMARK 500 ALA C 314 145.95 -172.04
REMARK 500 LYS C 338 -43.17 -136.93
REMARK 500 SER C 340 48.48 -91.91
REMARK 500 ASP D 39 -12.99 -150.01
REMARK 500 ALA D 56 -164.25 -105.15
REMARK 500 GLN D 96 -39.61 -137.19
REMARK 500 THR D 109 -85.81 -99.58
REMARK 500 THR D 180 -129.34 -118.33
REMARK 500 VAL D 181 -14.12 -152.22
REMARK 500 LEU E 139 31.45 -90.85
REMARK 500 LEU F 87 -59.10 -128.89
REMARK 500 SER F 88 -172.74 57.84
REMARK 500 THR F 92 -59.04 61.59
REMARK 500 SER F 230 52.35 -90.89
REMARK 500 ILE F 283 -49.15 -131.81
REMARK 500 ILE F 330 -67.79 -102.93
REMARK 500 LEU F 361 -155.08 -96.22
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 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 39 OD1
REMARK 620 2 ASP A 39 OD2 55.5
REMARK 620 3 THR A 41 O 91.0 82.7
REMARK 620 4 THR A 41 OG1 67.4 116.5 72.3
REMARK 620 5 GLY A 44 O 152.5 144.9 78.1 85.2
REMARK 620 6 GLU A 55 OE1 130.4 75.3 76.2 144.1 71.8
REMARK 620 7 GLU A 55 OE2 119.5 85.4 131.4 151.7 85.7 55.2
REMARK 620 8 HOH A 601 O 87.0 137.4 120.9 52.7 77.5 140.7 99.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP A 501 O2G
REMARK 620 2 GTP A 501 O2B 77.0
REMARK 620 3 HOH A 604 O 88.4 163.3
REMARK 620 4 HOH A 611 O 168.1 93.6 101.8
REMARK 620 5 HOH A 615 O 82.3 85.8 100.3 89.7
REMARK 620 6 HOH A 618 O 94.0 83.4 89.8 92.2 169.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 11 OE1
REMARK 620 2 GDP B 501 O2A 93.6
REMARK 620 3 HOH B 605 O 79.4 91.6
REMARK 620 4 HOH B 621 O 162.4 88.3 83.1
REMARK 620 5 HOH B 626 O 87.9 100.9 162.7 109.0
REMARK 620 6 HOH C 632 O 91.9 170.6 81.9 84.2 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 113 OE1
REMARK 620 2 GLU B 113 OE2 45.2
REMARK 620 3 HOH B 613 O 109.1 66.3
REMARK 620 4 HOH C 635 O 78.0 76.9 70.5
REMARK 620 5 HOH C 647 O 150.8 125.8 61.7 72.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 39 OD1
REMARK 620 2 ASP C 39 OD2 55.0
REMARK 620 3 THR C 41 O 91.2 83.2
REMARK 620 4 THR C 41 OG1 74.7 123.2 72.5
REMARK 620 5 GLY C 44 O 156.8 146.5 85.3 82.5
REMARK 620 6 GLU C 55 OE1 134.8 79.8 81.9 141.9 67.4
REMARK 620 7 GLU C 55 OE2 113.4 82.7 136.1 146.9 84.1 54.8
REMARK 620 8 HOH C 609 O 85.7 117.6 150.7 78.6 86.2 120.1 70.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 501 O2G
REMARK 620 2 GTP C 501 O2B 92.8
REMARK 620 3 HOH C 611 O 95.7 76.5
REMARK 620 4 HOH C 620 O 98.8 98.8 165.0
REMARK 620 5 HOH C 629 O 169.7 92.7 77.2 88.9
REMARK 620 6 HOH C 637 O 90.0 165.9 89.5 94.4 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 11 OE1
REMARK 620 2 GDP D 501 O2A 120.1
REMARK 620 3 HOH D 608 O 94.5 98.8
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 GTP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 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 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ED B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ED D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YJ3 RELATED DB: PDB
DBREF 4YJ2 A 1 451 UNP P81947 TBA1B_BOVIN 1 451
DBREF 4YJ2 B 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4YJ2 C 1 451 UNP P81947 TBA1B_BOVIN 1 451
DBREF 4YJ2 D 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4YJ2 E 5 145 UNP P63043 STMN4_RAT 76 216
DBREF 4YJ2 F 1 378 UNP E1BQ43 E1BQ43_CHICK 1 378
SEQADV 4YJ2 MET E 3 UNP P63043 INITIATING METHIONINE
SEQADV 4YJ2 ALA E 4 UNP P63043 EXPRESSION TAG
SEQADV 4YJ2 TRP E 20 UNP P63043 PHE 91 ENGINEERED MUTATION
SEQADV 4YJ2 HIS F 379 UNP E1BQ43 EXPRESSION TAG
SEQADV 4YJ2 HIS F 380 UNP E1BQ43 EXPRESSION TAG
SEQADV 4YJ2 HIS F 381 UNP E1BQ43 EXPRESSION TAG
SEQADV 4YJ2 HIS F 382 UNP E1BQ43 EXPRESSION TAG
SEQADV 4YJ2 HIS F 383 UNP E1BQ43 EXPRESSION TAG
SEQADV 4YJ2 HIS F 384 UNP E1BQ43 EXPRESSION TAG
SEQRES 1 A 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 A 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 A 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 A 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 A 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 A 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 A 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 A 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 A 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 A 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 A 451 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 A 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 A 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 A 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 A 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 A 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 A 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 A 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE
SEQRES 19 A 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 A 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 A 451 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 A 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 A 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 A 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 A 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 A 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 A 451 ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 451 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 A 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 A 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 A 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 A 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 A 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 A 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 A 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 B 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 B 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 B 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 B 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 B 445 GLU ALA THR GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 B 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 B 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 B 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 B 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 B 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 B 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 B 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 B 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 B 445 MET PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 B 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 B 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 B 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 B 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 B 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 B 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 B 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 B 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 B 445 PRO GLU LEU THR GLN GLN MET PHE ASP SER LYS ASN MET
SEQRES 24 B 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 B 445 VAL ALA ALA ILE PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 B 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 B 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 B 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 B 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 B 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 B 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 B 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 B 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 B 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 B 445 ASP GLU ALA
SEQRES 1 C 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 C 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 C 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 C 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 C 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 C 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 C 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 C 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 C 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 C 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 C 451 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 C 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 C 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 C 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 C 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 C 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 C 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 C 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE
SEQRES 19 C 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 C 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 C 451 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 C 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 C 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 C 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 C 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 C 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 C 451 ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 451 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 C 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 C 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 C 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 C 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 C 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 C 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 C 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 D 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 D 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 D 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 D 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 D 445 GLU ALA THR GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 D 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 D 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 D 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 D 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 D 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 D 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 D 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 D 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 D 445 MET PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 D 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 D 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 D 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 D 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 D 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 D 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 D 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 D 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 D 445 PRO GLU LEU THR GLN GLN MET PHE ASP SER LYS ASN MET
SEQRES 24 D 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 D 445 VAL ALA ALA ILE PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 D 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 D 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 D 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 D 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 D 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 D 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 D 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 D 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 D 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 D 445 ASP GLU ALA
SEQRES 1 E 143 MET ALA ASP MET GLU VAL ILE GLU LEU ASN LYS CYS THR
SEQRES 2 E 143 SER GLY GLN SER TRP GLU VAL ILE LEU LYS PRO PRO SER
SEQRES 3 E 143 PHE ASP GLY VAL PRO GLU PHE ASN ALA SER LEU PRO ARG
SEQRES 4 E 143 ARG ARG ASP PRO SER LEU GLU GLU ILE GLN LYS LYS LEU
SEQRES 5 E 143 GLU ALA ALA GLU GLU ARG ARG LYS TYR GLN GLU ALA GLU
SEQRES 6 E 143 LEU LEU LYS HIS LEU ALA GLU LYS ARG GLU HIS GLU ARG
SEQRES 7 E 143 GLU VAL ILE GLN LYS ALA ILE GLU GLU ASN ASN ASN PHE
SEQRES 8 E 143 ILE LYS MET ALA LYS GLU LYS LEU ALA GLN LYS MET GLU
SEQRES 9 E 143 SER ASN LYS GLU ASN ARG GLU ALA HIS LEU ALA ALA MET
SEQRES 10 E 143 LEU GLU ARG LEU GLN GLU LYS ASP LYS HIS ALA GLU GLU
SEQRES 11 E 143 VAL ARG LYS ASN LYS GLU LEU LYS GLU GLU ALA SER ARG
SEQRES 1 F 384 MET TYR THR PHE VAL VAL ARG ASP GLU ASN SER SER VAL
SEQRES 2 F 384 TYR ALA GLU VAL SER ARG LEU LEU LEU ALA THR GLY GLN
SEQRES 3 F 384 TRP LYS ARG LEU ARG LYS ASP ASN PRO ARG PHE ASN LEU
SEQRES 4 F 384 MET LEU GLY GLU ARG ASN ARG LEU PRO PHE GLY ARG LEU
SEQRES 5 F 384 GLY HIS GLU PRO GLY LEU VAL GLN LEU VAL ASN TYR TYR
SEQRES 6 F 384 ARG GLY ALA ASP LYS LEU CYS ARG LYS ALA SER LEU VAL
SEQRES 7 F 384 LYS LEU ILE LYS THR SER PRO GLU LEU SER GLU SER CYS
SEQRES 8 F 384 THR TRP PHE PRO GLU SER TYR VAL ILE TYR PRO THR ASN
SEQRES 9 F 384 LEU LYS THR PRO VAL ALA PRO ALA GLN ASN GLY ILE ARG
SEQRES 10 F 384 HIS LEU ILE ASN ASN THR ARG THR ASP GLU ARG GLU VAL
SEQRES 11 F 384 PHE LEU ALA ALA TYR ASN ARG ARG ARG GLU GLY ARG GLU
SEQRES 12 F 384 GLY ASN VAL TRP ILE ALA LYS SER SER ALA GLY ALA LYS
SEQRES 13 F 384 GLY GLU GLY ILE LEU ILE SER SER GLU ALA SER GLU LEU
SEQRES 14 F 384 LEU ASP PHE ILE ASP GLU GLN GLY GLN VAL HIS VAL ILE
SEQRES 15 F 384 GLN LYS TYR LEU GLU LYS PRO LEU LEU LEU GLU PRO GLY
SEQRES 16 F 384 HIS ARG LYS PHE ASP ILE ARG SER TRP VAL LEU VAL ASP
SEQRES 17 F 384 HIS LEU TYR ASN ILE TYR LEU TYR ARG GLU GLY VAL LEU
SEQRES 18 F 384 ARG THR SER SER GLU PRO TYR ASN SER ALA ASN PHE GLN
SEQRES 19 F 384 ASP LYS THR CYS HIS LEU THR ASN HIS CYS ILE GLN LYS
SEQRES 20 F 384 GLU TYR SER LYS ASN TYR GLY ARG TYR GLU GLU GLY ASN
SEQRES 21 F 384 GLU MET PHE PHE GLU GLU PHE ASN GLN TYR LEU MET ASP
SEQRES 22 F 384 ALA LEU ASN THR THR LEU GLU ASN SER ILE LEU LEU GLN
SEQRES 23 F 384 ILE LYS HIS ILE ILE ARG SER CYS LEU MET CYS ILE GLU
SEQRES 24 F 384 PRO ALA ILE SER THR LYS HIS LEU HIS TYR GLN SER PHE
SEQRES 25 F 384 GLN LEU PHE GLY PHE ASP PHE MET VAL ASP GLU GLU LEU
SEQRES 26 F 384 LYS VAL TRP LEU ILE GLU VAL ASN GLY ALA PRO ALA CYS
SEQRES 27 F 384 ALA GLN LYS LEU TYR ALA GLU LEU CYS GLN GLY ILE VAL
SEQRES 28 F 384 ASP VAL ALA ILE SER SER VAL PHE PRO LEU ALA ASP THR
SEQRES 29 F 384 GLY GLN LYS THR SER GLN PRO THR SER ILE PHE ILE LYS
SEQRES 30 F 384 LEU HIS HIS HIS HIS HIS HIS
HET GTP A 501 32
HET MG A 502 1
HET CA A 503 1
HET GOL A 504 6
HET GOL A 505 6
HET GDP B 501 28
HET MG B 502 1
HET CA B 503 1
HET 4ED B 504 19
HET MES B 505 12
HET MES B 506 12
HET GOL B 507 6
HET GTP C 501 32
HET CA C 502 1
HET GOL C 503 6
HET IMD C 504 5
HET MG C 505 1
HET GDP D 501 28
HET MG D 502 1
HET 4ED D 503 19
HET GOL D 504 6
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM 4ED 5,6-DIMETHYL-2-[(E)-2-(PYRIDIN-3-YL)ETHENYL]-1,3-
HETNAM 2 4ED BENZOTHIAZOLE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM IMD IMIDAZOLE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GTP 2(C10 H16 N5 O14 P3)
FORMUL 8 MG 4(MG 2+)
FORMUL 9 CA 3(CA 2+)
FORMUL 10 GOL 5(C3 H8 O3)
FORMUL 12 GDP 2(C10 H15 N5 O11 P2)
FORMUL 15 4ED 2(C16 H14 N2 S)
FORMUL 16 MES 2(C6 H13 N O4 S)
FORMUL 22 IMD C3 H5 N2 1+
FORMUL 28 HOH *111(H2 O)
HELIX 1 AA1 GLY A 10 HIS A 28 1 19
HELIX 2 AA2 ASP A 47 THR A 51 5 5
HELIX 3 AA3 ILE A 75 THR A 80 1 6
HELIX 4 AA4 HIS A 88 GLU A 90 5 3
HELIX 5 AA5 ASN A 102 TYR A 108 1 7
HELIX 6 AA6 ILE A 110 ASP A 127 1 18
HELIX 7 AA7 GLY A 143 TYR A 161 1 19
HELIX 8 AA8 ALA A 174 SER A 178 5 5
HELIX 9 AA9 VAL A 182 LEU A 195 1 14
HELIX 10 AB1 GLU A 196 SER A 198 5 3
HELIX 11 AB2 ASN A 206 LEU A 217 1 12
HELIX 12 AB3 THR A 223 PHE A 244 1 22
HELIX 13 AB4 ASP A 251 VAL A 260 1 10
HELIX 14 AB5 SER A 287 ALA A 294 1 8
HELIX 15 AB6 CYS A 295 GLN A 301 5 7
HELIX 16 AB7 ASP A 306 GLY A 310 5 5
HELIX 17 AB8 VAL A 324 THR A 337 1 14
HELIX 18 AB9 ILE A 384 ALA A 400 1 17
HELIX 19 AC1 PHE A 404 GLY A 410 1 7
HELIX 20 AC2 GLU A 415 GLY A 436 1 22
HELIX 21 AC3 GLY B 10 HIS B 28 1 19
HELIX 22 AC4 SER B 40 LEU B 46 5 5
HELIX 23 AC5 ARG B 48 VAL B 51 5 4
HELIX 24 AC6 PRO B 72 SER B 80 1 9
HELIX 25 AC7 PHE B 83 PHE B 87 5 5
HELIX 26 AC8 ARG B 88 ASP B 90 5 3
HELIX 27 AC9 ASN B 102 TYR B 108 1 7
HELIX 28 AD1 GLU B 110 GLU B 113 5 4
HELIX 29 AD2 LEU B 114 SER B 128 1 15
HELIX 30 AD3 GLY B 144 TYR B 161 1 18
HELIX 31 AD4 SER B 174 SER B 178 5 5
HELIX 32 AD5 VAL B 182 THR B 198 1 17
HELIX 33 AD6 ASN B 206 THR B 216 1 11
HELIX 34 AD7 THR B 223 THR B 239 1 17
HELIX 35 AD8 THR B 239 PHE B 244 1 6
HELIX 36 AD9 ASP B 251 VAL B 260 1 10
HELIX 37 AE1 THR B 287 ASP B 297 1 11
HELIX 38 AE2 SER B 298 MET B 301 5 4
HELIX 39 AE3 ASP B 306 GLY B 310 5 5
HELIX 40 AE4 SER B 324 ASN B 339 1 16
HELIX 41 AE5 SER B 340 PHE B 343 5 4
HELIX 42 AE6 ILE B 384 ARG B 400 1 17
HELIX 43 AE7 LEU B 405 GLY B 410 1 6
HELIX 44 AE8 ASP B 414 ASP B 437 1 24
HELIX 45 AE9 GLY C 10 GLY C 29 1 20
HELIX 46 AF1 ASP C 47 THR C 51 5 5
HELIX 47 AF2 PRO C 72 THR C 80 1 9
HELIX 48 AF3 HIS C 88 GLU C 90 5 3
HELIX 49 AF4 ASN C 102 TYR C 108 1 7
HELIX 50 AF5 ILE C 110 GLU C 113 5 4
HELIX 51 AF6 ILE C 114 ASP C 127 1 14
HELIX 52 AF7 GLY C 143 GLY C 162 1 20
HELIX 53 AF8 VAL C 182 LEU C 195 1 14
HELIX 54 AF9 GLU C 196 SER C 198 5 3
HELIX 55 AG1 ASN C 206 LEU C 217 1 12
HELIX 56 AG2 THR C 223 PHE C 244 1 22
HELIX 57 AG3 ASP C 251 VAL C 260 1 10
HELIX 58 AG4 SER C 277 TYR C 282 1 6
HELIX 59 AG5 SER C 287 CYS C 295 1 9
HELIX 60 AG6 PHE C 296 GLN C 301 5 6
HELIX 61 AG7 ASP C 306 GLY C 310 5 5
HELIX 62 AG8 VAL C 324 LYS C 336 1 13
HELIX 63 AG9 ILE C 384 ALA C 400 1 17
HELIX 64 AH1 VAL C 405 GLY C 410 1 6
HELIX 65 AH2 GLU C 414 VAL C 435 1 22
HELIX 66 AH3 GLY D 10 GLY D 29 1 20
HELIX 67 AH4 SER D 40 LEU D 46 5 5
HELIX 68 AH5 ARG D 48 VAL D 51 5 4
HELIX 69 AH6 GLU D 71 GLY D 81 1 11
HELIX 70 AH7 ARG D 88 ASP D 90 5 3
HELIX 71 AH8 ASN D 102 TYR D 108 1 7
HELIX 72 AH9 GLU D 110 GLU D 113 5 4
HELIX 73 AI1 LEU D 114 GLU D 127 1 14
HELIX 74 AI2 GLY D 144 TYR D 161 1 18
HELIX 75 AI3 SER D 174 SER D 178 5 5
HELIX 76 AI4 VAL D 182 THR D 198 1 17
HELIX 77 AI5 ASN D 206 THR D 216 1 11
HELIX 78 AI6 THR D 223 THR D 239 1 17
HELIX 79 AI7 THR D 239 PHE D 244 1 6
HELIX 80 AI8 ASP D 251 VAL D 260 1 10
HELIX 81 AI9 THR D 287 PHE D 296 1 10
HELIX 82 AJ1 ASP D 297 MET D 301 5 5
HELIX 83 AJ2 ASP D 306 GLY D 310 5 5
HELIX 84 AJ3 SER D 324 ASN D 339 1 16
HELIX 85 AJ4 SER D 340 PHE D 343 5 4
HELIX 86 AJ5 ILE D 384 ARG D 400 1 17
HELIX 87 AJ6 LEU D 405 GLY D 410 1 6
HELIX 88 AJ7 ASP D 414 ALA D 438 1 25
HELIX 89 AJ8 SER E 46 LEU E 139 1 94
HELIX 90 AJ9 VAL F 13 THR F 24 1 12
HELIX 91 AK1 PRO F 48 LEU F 52 5 5
HELIX 92 AK2 ALA F 68 ARG F 73 1 6
HELIX 93 AK3 ARG F 73 SER F 84 1 12
HELIX 94 AK4 GLU F 127 ASN F 136 1 10
HELIX 95 AK5 ALA F 166 ASP F 171 1 6
HELIX 96 AK6 GLU F 257 GLY F 259 5 3
HELIX 97 AK7 PHE F 263 LEU F 275 1 13
HELIX 98 AK8 THR F 278 ILE F 283 1 6
HELIX 99 AK9 ILE F 283 ILE F 298 1 16
HELIX 100 AL1 ILE F 298 SER F 303 1 6
HELIX 101 AL2 ALA F 339 LYS F 341 5 3
HELIX 102 AL3 LEU F 342 ILE F 355 1 14
SHEET 1 AA1 6 LEU A 92 THR A 94 0
SHEET 2 AA1 6 ALA A 65 ASP A 69 1 N PHE A 67 O ILE A 93
SHEET 3 AA1 6 CYS A 4 VAL A 9 1 N HIS A 8 O VAL A 66
SHEET 4 AA1 6 GLY A 134 SER A 140 1 O LEU A 136 N ILE A 7
SHEET 5 AA1 6 SER A 165 TYR A 172 1 O LEU A 167 N PHE A 135
SHEET 6 AA1 6 CYS A 200 ASP A 205 1 O VAL A 204 N SER A 170
SHEET 1 AA2 2 PHE A 53 GLU A 55 0
SHEET 2 AA2 2 HIS A 61 PRO A 63 -1 O VAL A 62 N SER A 54
SHEET 1 AA3 6 LEU A 269 ALA A 273 0
SHEET 2 AA3 6 ARG A 373 THR A 381 -1 O SER A 379 N LEU A 269
SHEET 3 AA3 6 TYR A 312 GLY A 321 -1 N ARG A 320 O ALA A 374
SHEET 4 AA3 6 THR A 349 ASN A 356 1 O GLY A 354 N TYR A 319
SHEET 5 AA3 6 GLY E 17 LYS E 25 -1 O LYS E 25 N THR A 349
SHEET 6 AA3 6 GLU E 7 CYS E 14 -1 N CYS E 14 O GLY E 17
SHEET 1 AA410 PHE B 92 PHE B 94 0
SHEET 2 AA410 ALA B 65 ASP B 69 1 N LEU B 67 O VAL B 93
SHEET 3 AA410 GLU B 3 ALA B 9 1 N GLN B 8 O VAL B 68
SHEET 4 AA410 LEU B 132 SER B 140 1 O GLN B 136 N ILE B 7
SHEET 5 AA410 ILE B 165 MET B 172 1 O PHE B 169 N LEU B 137
SHEET 6 AA410 GLU B 200 ASP B 205 1 O ILE B 204 N MET B 172
SHEET 7 AA410 PHE B 267 ALA B 273 1 O PHE B 268 N THR B 201
SHEET 8 AA410 SER B 374 SER B 381 -1 O ALA B 375 N ALA B 273
SHEET 9 AA410 TYR B 312 ARG B 320 -1 N ALA B 316 O ILE B 378
SHEET 10 AA410 VAL B 351 CYS B 356 1 O CYS B 356 N PHE B 319
SHEET 1 AA5 2 TYR B 53 GLU B 55 0
SHEET 2 AA5 2 TYR B 61 PRO B 63 -1 O VAL B 62 N ASN B 54
SHEET 1 AA6 6 LEU C 92 THR C 94 0
SHEET 2 AA6 6 ALA C 65 ASP C 69 1 N PHE C 67 O ILE C 93
SHEET 3 AA6 6 CYS C 4 VAL C 9 1 N HIS C 8 O VAL C 68
SHEET 4 AA6 6 GLY C 134 SER C 140 1 O LEU C 136 N ILE C 7
SHEET 5 AA6 6 SER C 165 TYR C 172 1 O LEU C 167 N VAL C 137
SHEET 6 AA6 6 CYS C 200 ASP C 205 1 O PHE C 202 N GLU C 168
SHEET 1 AA7 2 PHE C 53 GLU C 55 0
SHEET 2 AA7 2 HIS C 61 PRO C 63 -1 O VAL C 62 N SER C 54
SHEET 1 AA8 4 LEU C 269 ALA C 273 0
SHEET 2 AA8 4 ARG C 373 THR C 381 -1 O SER C 379 N LEU C 269
SHEET 3 AA8 4 TYR C 312 GLY C 321 -1 N MET C 313 O ASN C 380
SHEET 4 AA8 4 LYS C 352 ASN C 356 1 O LYS C 352 N LEU C 317
SHEET 1 AA910 PHE D 92 PHE D 94 0
SHEET 2 AA910 ALA D 65 ASP D 69 1 N LEU D 67 O VAL D 93
SHEET 3 AA910 ARG D 2 ALA D 9 1 N GLN D 8 O VAL D 68
SHEET 4 AA910 CYS D 131 SER D 140 1 O GLN D 133 N GLU D 3
SHEET 5 AA910 ILE D 165 MET D 172 1 O PHE D 169 N LEU D 137
SHEET 6 AA910 GLU D 200 ASP D 205 1 O TYR D 202 N THR D 168
SHEET 7 AA910 PHE D 267 ALA D 273 1 O PHE D 268 N THR D 201
SHEET 8 AA910 SER D 374 SER D 381 -1 O GLY D 379 N MET D 269
SHEET 9 AA910 TYR D 312 ARG D 320 -1 N ALA D 316 O ILE D 378
SHEET 10 AA910 VAL D 351 CYS D 356 1 O ALA D 354 N PHE D 319
SHEET 1 AB1 2 TYR D 53 GLU D 55 0
SHEET 2 AB1 2 TYR D 61 PRO D 63 -1 O VAL D 62 N ASN D 54
SHEET 1 AB2 5 TRP F 27 ARG F 29 0
SHEET 2 AB2 5 TYR F 2 VAL F 6 1 N TYR F 2 O LYS F 28
SHEET 3 AB2 5 LEU F 39 LEU F 41 1 O LEU F 41 N VAL F 5
SHEET 4 AB2 5 LEU F 61 VAL F 62 1 O LEU F 61 N MET F 40
SHEET 5 AB2 5 GLN F 310 SER F 311 1 O GLN F 310 N VAL F 62
SHEET 1 AB3 3 SER F 97 VAL F 99 0
SHEET 2 AB3 3 VAL F 181 LYS F 184 -1 O ILE F 182 N TYR F 98
SHEET 3 AB3 3 TRP F 147 LYS F 150 -1 N ILE F 148 O GLN F 183
SHEET 1 AB4 5 GLU F 261 MET F 262 0
SHEET 2 AB4 5 VAL F 220 ARG F 222 -1 N LEU F 221 O MET F 262
SHEET 3 AB4 5 ILE F 201 VAL F 207 -1 N ARG F 202 O VAL F 220
SHEET 4 AB4 5 GLN F 313 VAL F 321 -1 O PHE F 315 N VAL F 205
SHEET 5 AB4 5 VAL F 327 ASN F 333 -1 O TRP F 328 N MET F 320
SHEET 1 AB5 5 GLU F 261 MET F 262 0
SHEET 2 AB5 5 VAL F 220 ARG F 222 -1 N LEU F 221 O MET F 262
SHEET 3 AB5 5 ILE F 201 VAL F 207 -1 N ARG F 202 O VAL F 220
SHEET 4 AB5 5 ILE F 213 TYR F 216 -1 O TYR F 214 N LEU F 206
SHEET 5 AB5 5 PHE F 375 LYS F 377 -1 O ILE F 376 N LEU F 215
LINK OD1 ASP A 39 CA CA A 503 1555 1555 2.36
LINK OD2 ASP A 39 CA CA A 503 1555 1555 2.36
LINK O THR A 41 CA CA A 503 1555 1555 2.36
LINK OG1 THR A 41 CA CA A 503 1555 1555 2.36
LINK O GLY A 44 CA CA A 503 1555 1555 2.34
LINK OE1 GLU A 55 CA CA A 503 1555 1555 2.39
LINK OE2 GLU A 55 CA CA A 503 1555 1555 2.35
LINK O2G GTP A 501 MG MG A 502 1555 1555 2.05
LINK O2B GTP A 501 MG MG A 502 1555 1555 2.18
LINK MG MG A 502 O HOH A 604 1555 1555 2.08
LINK MG MG A 502 O HOH A 611 1555 1555 2.07
LINK MG MG A 502 O HOH A 615 1555 1555 2.07
LINK MG MG A 502 O HOH A 618 1555 1555 2.07
LINK CA CA A 503 O HOH A 601 1555 1555 2.37
LINK OE1 GLN B 11 MG MG B 502 1555 1555 2.07
LINK OE1 GLU B 113 CA CA B 503 1555 1555 3.08
LINK OE2 GLU B 113 CA CA B 503 1555 1555 2.42
LINK O2A GDP B 501 MG MG B 502 1555 1555 2.27
LINK MG MG B 502 O HOH B 605 1555 1555 2.08
LINK MG MG B 502 O HOH B 621 1555 1555 2.07
LINK MG MG B 502 O HOH B 626 1555 1555 2.09
LINK MG MG B 502 O HOH C 632 1555 1555 2.10
LINK CA CA B 503 O HOH B 613 1555 1555 2.39
LINK CA CA B 503 O HOH C 635 1555 4455 2.42
LINK CA CA B 503 O HOH C 647 1555 4455 2.55
LINK OD1 ASP C 39 CA CA C 502 1555 1555 2.40
LINK OD2 ASP C 39 CA CA C 502 1555 1555 2.35
LINK O THR C 41 CA CA C 502 1555 1555 2.37
LINK OG1 THR C 41 CA CA C 502 1555 1555 2.40
LINK O GLY C 44 CA CA C 502 1555 1555 2.38
LINK OE1 GLU C 55 CA CA C 502 1555 1555 2.40
LINK OE2 GLU C 55 CA CA C 502 1555 1555 2.37
LINK O2G GTP C 501 MG MG C 505 1555 1555 2.01
LINK O2B GTP C 501 MG MG C 505 1555 1555 2.09
LINK CA CA C 502 O HOH C 609 1555 1555 2.40
LINK MG MG C 505 O HOH C 611 1555 1555 2.07
LINK MG MG C 505 O HOH C 620 1555 1555 2.07
LINK MG MG C 505 O HOH C 629 1555 1555 2.06
LINK MG MG C 505 O HOH C 637 1555 1555 2.07
LINK OE1 GLN D 11 MG MG D 502 1555 1555 2.12
LINK O2A GDP D 501 MG MG D 502 1555 1555 2.29
LINK MG MG D 502 O HOH D 608 1555 1555 2.08
CISPEP 1 ALA A 273 PRO A 274 0 -3.43
CISPEP 2 ALA B 273 PRO B 274 0 -2.87
CISPEP 3 ALA C 273 PRO C 274 0 -2.33
CISPEP 4 ALA D 273 PRO D 274 0 -1.51
CISPEP 5 THR F 125 ASP F 126 0 0.10
CISPEP 6 GLU F 193 PRO F 194 0 0.72
SITE 1 AC1 27 GLY A 10 GLN A 11 ALA A 12 GLN A 15
SITE 2 AC1 27 ASP A 98 ALA A 99 ALA A 100 ASN A 101
SITE 3 AC1 27 SER A 140 GLY A 143 GLY A 144 THR A 145
SITE 4 AC1 27 GLY A 146 VAL A 177 SER A 178 GLU A 183
SITE 5 AC1 27 ASN A 206 TYR A 224 ASN A 228 ILE A 231
SITE 6 AC1 27 MG A 502 HOH A 604 HOH A 610 HOH A 611
SITE 7 AC1 27 HOH A 615 HOH A 618 LYS B 254
SITE 1 AC2 6 GLU A 71 GTP A 501 HOH A 604 HOH A 611
SITE 2 AC2 6 HOH A 615 HOH A 618
SITE 1 AC3 5 ASP A 39 THR A 41 GLY A 44 GLU A 55
SITE 2 AC3 5 HOH A 601
SITE 1 AC4 5 ASN A 216 PRO A 274 VAL A 275 ALA A 294
SITE 2 AC4 5 ASN A 300
SITE 1 AC5 5 HIS A 309 THR A 382 ALA A 383 GLU A 386
SITE 2 AC5 5 ARG F 66
SITE 1 AC6 22 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC6 22 SER B 140 GLY B 143 GLY B 144 THR B 145
SITE 3 AC6 22 GLY B 146 VAL B 177 ASP B 179 GLU B 183
SITE 4 AC6 22 ASN B 206 TYR B 224 ASN B 228 MG B 502
SITE 5 AC6 22 HOH B 603 HOH B 604 HOH B 606 HOH B 609
SITE 6 AC6 22 HOH B 620 HOH B 621
SITE 1 AC7 6 GLN B 11 GDP B 501 HOH B 605 HOH B 621
SITE 2 AC7 6 HOH B 626 HOH C 632
SITE 1 AC8 4 GLU B 113 HOH B 613 HOH C 635 HOH C 647
SITE 1 AC9 13 GLN B 136 ASN B 167 GLU B 200 TYR B 202
SITE 2 AC9 13 VAL B 238 THR B 239 CYS B 241 LEU B 242
SITE 3 AC9 13 LEU B 252 LEU B 255 ALA B 316 ILE B 318
SITE 4 AC9 13 HOH B 602
SITE 1 AD1 7 ARG B 158 ASP B 163 ARG B 164 ILE B 165
SITE 2 AD1 7 ASN B 197 ASP B 199 ARG B 253
SITE 1 AD2 9 PHE B 296 ASP B 297 SER B 298 ARG B 308
SITE 2 AD2 9 TYR B 312 VAL B 335 ASN B 339 TYR B 342
SITE 3 AD2 9 HOH B 601
SITE 1 AD3 3 PRO B 222 TYR B 224 HOH B 629
SITE 1 AD4 29 GLY C 10 GLN C 11 ALA C 12 GLN C 15
SITE 2 AD4 29 ASP C 69 ASP C 98 ALA C 99 ALA C 100
SITE 3 AD4 29 ASN C 101 SER C 140 GLY C 143 GLY C 144
SITE 4 AD4 29 THR C 145 GLY C 146 ILE C 171 VAL C 177
SITE 5 AD4 29 GLU C 183 ASN C 206 TYR C 224 ASN C 228
SITE 6 AD4 29 ILE C 231 MG C 505 HOH C 611 HOH C 612
SITE 7 AD4 29 HOH C 620 HOH C 622 HOH C 629 HOH C 637
SITE 8 AD4 29 LYS D 254
SITE 1 AD5 5 ASP C 39 THR C 41 GLY C 44 GLU C 55
SITE 2 AD5 5 HOH C 609
SITE 1 AD6 4 ARG C 221 THR C 223 TYR C 224 GLN D 247
SITE 1 AD7 2 ASP C 431 HOH C 643
SITE 1 AD8 5 GTP C 501 HOH C 611 HOH C 620 HOH C 629
SITE 2 AD8 5 HOH C 637
SITE 1 AD9 17 GLY D 10 GLN D 11 CYS D 12 GLN D 15
SITE 2 AD9 17 ASN D 101 SER D 140 GLY D 143 GLY D 144
SITE 3 AD9 17 THR D 145 GLY D 146 VAL D 177 GLU D 183
SITE 4 AD9 17 ASN D 206 TYR D 224 ASN D 228 MG D 502
SITE 5 AD9 17 HOH D 605
SITE 1 AE1 5 GLN D 11 ASP D 179 GDP D 501 HOH D 602
SITE 2 AE1 5 HOH D 608
SITE 1 AE2 18 GLN D 136 ASN D 167 PHE D 169 GLU D 200
SITE 2 AE2 18 TYR D 202 VAL D 238 THR D 239 CYS D 241
SITE 3 AE2 18 LEU D 242 LEU D 248 ASN D 249 LEU D 252
SITE 4 AE2 18 LEU D 255 ALA D 316 ILE D 318 ALA D 354
SITE 5 AE2 18 ILE D 378 HOH D 607
SITE 1 AE3 7 TRP C 407 ARG D 158 ASP D 163 ARG D 164
SITE 2 AE3 7 ILE D 165 ASP D 199 ARG D 253
CRYST1 104.830 157.650 181.030 90.00 90.00 90.00 P 21 21 21 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 0.009539 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
