HEADER CELL CYCLE 28-NOV-12 4I55
TITLE CRYSTAL STRUCTURE OF TUBULIN-STATHMIN-TTL COMPLEX
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 SYNONYM: STATHMIN-LIKE PROTEIN B3, RB3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: TUBULIN TYROSINE LIGASE, TTL;
COMPND 16 CHAIN: F;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 ORGAN: BRAIN;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: STMN4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: NICO21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PET3D;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 22 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 23 ORGANISM_TAXID: 9031;
SOURCE 24 GENE: TTL;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: NSKN1;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PA23_007_GGTTL_KH6_2-378_NSKN1
KEYWDS ALPHA-TUBULIN, BETA-TUBULIN, LIGASE, MICROTUBULE, STATHMIN, CELL
KEYWDS 2 CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.PROTA,K.BARGSTEN,D.ZURWERRA,J.J.FIELD,J.F.DIAZ,K.H.ALTMANN,
AUTHOR 2 M.O.STEINMETZ
REVDAT 4 20-SEP-23 4I55 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4I55 1 REMARK
REVDAT 2 13-FEB-13 4I55 1 JRNL
REVDAT 1 23-JAN-13 4I55 0
JRNL AUTH A.E.PROTA,K.BARGSTEN,D.ZURWERRA,J.J.FIELD,J.F.DIAZ,
JRNL AUTH 2 K.H.ALTMANN,M.O.STEINMETZ
JRNL TITL MOLECULAR MECHANISM OF ACTION OF MICROTUBULE-STABILIZING
JRNL TITL 2 ANTICANCER AGENTS.
JRNL REF SCIENCE V. 339 587 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 23287720
JRNL DOI 10.1126/SCIENCE.1230582
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 149390
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 7514
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 71.8824 - 6.8340 1.00 5073 284 0.1819 0.1969
REMARK 3 2 6.8340 - 5.4250 1.00 4918 242 0.1753 0.2176
REMARK 3 3 5.4250 - 4.7394 1.00 4812 273 0.1299 0.1540
REMARK 3 4 4.7394 - 4.3061 1.00 4852 251 0.1192 0.1455
REMARK 3 5 4.3061 - 3.9975 1.00 4801 248 0.1320 0.1759
REMARK 3 6 3.9975 - 3.7618 1.00 4809 249 0.1499 0.1935
REMARK 3 7 3.7618 - 3.5734 1.00 4766 250 0.1580 0.1694
REMARK 3 8 3.5734 - 3.4179 1.00 4779 260 0.1634 0.2189
REMARK 3 9 3.4179 - 3.2863 1.00 4728 285 0.1743 0.2229
REMARK 3 10 3.2863 - 3.1729 1.00 4768 225 0.1779 0.2394
REMARK 3 11 3.1729 - 3.0737 1.00 4739 245 0.1729 0.2177
REMARK 3 12 3.0737 - 2.9858 1.00 4767 245 0.1647 0.2040
REMARK 3 13 2.9858 - 2.9072 1.00 4769 235 0.1687 0.2309
REMARK 3 14 2.9072 - 2.8363 1.00 4758 217 0.1779 0.2236
REMARK 3 15 2.8363 - 2.7718 1.00 4748 257 0.1795 0.2456
REMARK 3 16 2.7718 - 2.7128 1.00 4673 283 0.1861 0.2399
REMARK 3 17 2.7128 - 2.6586 0.99 4695 242 0.1944 0.2454
REMARK 3 18 2.6586 - 2.6084 1.00 4713 231 0.1936 0.2315
REMARK 3 19 2.6084 - 2.5618 0.99 4740 252 0.1976 0.2512
REMARK 3 20 2.5618 - 2.5184 0.99 4680 253 0.2095 0.2899
REMARK 3 21 2.5184 - 2.4777 1.00 4707 242 0.2045 0.2766
REMARK 3 22 2.4777 - 2.4396 0.99 4674 253 0.1994 0.2748
REMARK 3 23 2.4396 - 2.4037 0.99 4706 256 0.2117 0.2742
REMARK 3 24 2.4037 - 2.3699 1.00 4704 251 0.2089 0.2684
REMARK 3 25 2.3699 - 2.3379 0.99 4695 259 0.2122 0.2678
REMARK 3 26 2.3379 - 2.3075 0.99 4664 248 0.2179 0.2639
REMARK 3 27 2.3075 - 2.2786 0.99 4673 272 0.2309 0.2661
REMARK 3 28 2.2786 - 2.2512 0.99 4669 240 0.2440 0.3070
REMARK 3 29 2.2512 - 2.2250 0.97 4573 239 0.2477 0.3209
REMARK 3 30 2.2250 - 2.2000 0.90 4223 227 0.2523 0.2847
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 47.15
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.96460
REMARK 3 B22 (A**2) : 7.18040
REMARK 3 B33 (A**2) : -0.39700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 18285
REMARK 3 ANGLE : 1.111 24845
REMARK 3 CHIRALITY : 0.063 2708
REMARK 3 PLANARITY : 0.005 3229
REMARK 3 DIHEDRAL : 16.565 6864
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 26
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:180)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6709 87.5605 52.1532
REMARK 3 T TENSOR
REMARK 3 T11: 0.4231 T22: 0.3462
REMARK 3 T33: 0.2980 T12: -0.1326
REMARK 3 T13: 0.0938 T23: -0.1226
REMARK 3 L TENSOR
REMARK 3 L11: 1.0822 L22: 2.1542
REMARK 3 L33: 1.3336 L12: -0.3131
REMARK 3 L13: -0.0813 L23: 0.6965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0391 S12: 0.0856 S13: 0.0643
REMARK 3 S21: -0.3200 S22: 0.2554 S23: -0.2756
REMARK 3 S31: -0.4910 S32: 0.3546 S33: -0.1364
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 181:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0585 81.4804 66.1553
REMARK 3 T TENSOR
REMARK 3 T11: 0.3317 T22: 0.3300
REMARK 3 T33: 0.3473 T12: 0.0140
REMARK 3 T13: 0.0389 T23: -0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 0.2241 L22: 1.5459
REMARK 3 L33: 2.0514 L12: -0.2439
REMARK 3 L13: -0.0873 L23: 0.9664
REMARK 3 S TENSOR
REMARK 3 S11: 0.0459 S12: 0.0142 S13: 0.0086
REMARK 3 S21: 0.1905 S22: 0.0046 S23: 0.1083
REMARK 3 S31: -0.1344 S32: -0.0407 S33: -0.0407
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 312:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6265 82.4852 73.6142
REMARK 3 T TENSOR
REMARK 3 T11: 0.3350 T22: 0.1986
REMARK 3 T33: 0.2070 T12: 0.0110
REMARK 3 T13: 0.0525 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.7108 L22: 1.7176
REMARK 3 L33: 1.1106 L12: -0.0995
REMARK 3 L13: -0.0131 L23: 0.8849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: -0.0899 S13: 0.0659
REMARK 3 S21: 0.3657 S22: -0.0371 S23: 0.1817
REMARK 3 S31: 0.0016 S32: 0.0024 S33: -0.0248
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 402:436)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5640 61.1232 60.8133
REMARK 3 T TENSOR
REMARK 3 T11: 0.3688 T22: 0.3193
REMARK 3 T33: 0.3551 T12: 0.1288
REMARK 3 T13: -0.0737 T23: -0.1412
REMARK 3 L TENSOR
REMARK 3 L11: 0.7326 L22: 1.6040
REMARK 3 L33: 2.6500 L12: -0.1801
REMARK 3 L13: -0.2856 L23: 1.3652
REMARK 3 S TENSOR
REMARK 3 S11: -0.1520 S12: -0.0445 S13: -0.2126
REMARK 3 S21: 0.6298 S22: 0.2159 S23: -0.3086
REMARK 3 S31: 0.4553 S32: 0.7296 S33: -0.0151
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 437:450)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0581 56.1461 86.7654
REMARK 3 T TENSOR
REMARK 3 T11: 1.3451 T22: 0.7819
REMARK 3 T33: 0.6624 T12: -0.0641
REMARK 3 T13: 0.1481 T23: 0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 0.0094 L22: 0.0000
REMARK 3 L33: 0.0198 L12: -0.0022
REMARK 3 L13: -0.0136 L23: 0.0031
REMARK 3 S TENSOR
REMARK 3 S11: 0.4310 S12: -0.4206 S13: -0.2431
REMARK 3 S21: 0.4077 S22: -0.4262 S23: -0.5629
REMARK 3 S31: -0.0343 S32: 0.0548 S33: 0.0792
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3068 69.5879 19.6941
REMARK 3 T TENSOR
REMARK 3 T11: 0.3307 T22: 0.2959
REMARK 3 T33: 0.3547 T12: 0.0427
REMARK 3 T13: 0.0147 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.6852 L22: 2.3498
REMARK 3 L33: 1.6747 L12: -1.0752
REMARK 3 L13: -0.2806 L23: 0.3648
REMARK 3 S TENSOR
REMARK 3 S11: 0.1009 S12: 0.1630 S13: 0.3296
REMARK 3 S21: -0.3559 S22: -0.1091 S23: -0.0305
REMARK 3 S31: -0.5155 S32: -0.1407 S33: 0.0179
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 89:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0854 55.7628 14.6906
REMARK 3 T TENSOR
REMARK 3 T11: 0.2750 T22: 0.4372
REMARK 3 T33: 0.2966 T12: -0.0365
REMARK 3 T13: 0.0374 T23: -0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 1.2846 L22: 1.7594
REMARK 3 L33: 1.1890 L12: -0.1294
REMARK 3 L13: -0.3478 L23: -0.1134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: 0.2562 S13: -0.0079
REMARK 3 S21: -0.3399 S22: 0.1443 S23: -0.1469
REMARK 3 S31: -0.2652 S32: 0.2345 S33: -0.1236
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 128:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4513 52.8251 26.2646
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.2809
REMARK 3 T33: 0.3046 T12: -0.0080
REMARK 3 T13: 0.0434 T23: -0.1035
REMARK 3 L TENSOR
REMARK 3 L11: 1.0678 L22: 1.9585
REMARK 3 L33: 1.3372 L12: 0.4646
REMARK 3 L13: -0.0918 L23: 0.6292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0694 S12: -0.0299 S13: -0.0484
REMARK 3 S21: 0.0278 S22: 0.0747 S23: -0.2133
REMARK 3 S31: -0.1122 S32: 0.1310 S33: -0.1152
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 198:223)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3004 50.4605 28.2336
REMARK 3 T TENSOR
REMARK 3 T11: 0.0981 T22: 0.6761
REMARK 3 T33: 0.5825 T12: -0.1247
REMARK 3 T13: 0.1432 T23: -0.3773
REMARK 3 L TENSOR
REMARK 3 L11: 2.0665 L22: 0.3749
REMARK 3 L33: 0.6988 L12: -0.5536
REMARK 3 L13: 0.6373 L23: -0.4996
REMARK 3 S TENSOR
REMARK 3 S11: -0.2327 S12: 0.0464 S13: -0.3682
REMARK 3 S21: 0.1993 S22: -0.3167 S23: 0.5258
REMARK 3 S31: 0.2514 S32: -0.7809 S33: 0.0428
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 224:295)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7981 61.2179 35.4108
REMARK 3 T TENSOR
REMARK 3 T11: 0.2605 T22: 0.3767
REMARK 3 T33: 0.3919 T12: 0.0320
REMARK 3 T13: -0.0009 T23: -0.1198
REMARK 3 L TENSOR
REMARK 3 L11: 0.4759 L22: 0.9928
REMARK 3 L33: 1.2602 L12: -0.2316
REMARK 3 L13: -0.5467 L23: 0.6321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0821 S13: 0.0363
REMARK 3 S21: -0.0546 S22: -0.0331 S23: 0.1348
REMARK 3 S31: -0.2795 S32: -0.2953 S33: 0.0010
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 296:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4378 60.3111 44.9223
REMARK 3 T TENSOR
REMARK 3 T11: 0.2545 T22: 0.4635
REMARK 3 T33: 0.3169 T12: 0.0279
REMARK 3 T13: 0.0444 T23: -0.1621
REMARK 3 L TENSOR
REMARK 3 L11: 1.5915 L22: 1.2533
REMARK 3 L33: 1.5555 L12: -0.2385
REMARK 3 L13: 0.3289 L23: 0.2834
REMARK 3 S TENSOR
REMARK 3 S11: -0.1503 S12: -0.2294 S13: 0.1059
REMARK 3 S21: 0.3283 S22: -0.0975 S23: 0.3215
REMARK 3 S31: 0.0288 S32: -0.7776 S33: 0.1682
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 374:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2469 41.6297 34.1359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3031 T22: 0.3349
REMARK 3 T33: 0.3305 T12: -0.0103
REMARK 3 T13: 0.0498 T23: -0.0907
REMARK 3 L TENSOR
REMARK 3 L11: 0.8011 L22: 1.8776
REMARK 3 L33: 1.3533 L12: -0.9263
REMARK 3 L13: -0.2808 L23: 1.3807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: -0.2807 S13: -0.1040
REMARK 3 S21: 0.2209 S22: -0.0442 S23: 0.5109
REMARK 3 S31: 0.2453 S32: -0.1048 S33: 0.0716
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 402:438)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5228 37.7406 31.4652
REMARK 3 T TENSOR
REMARK 3 T11: 0.2634 T22: 0.2900
REMARK 3 T33: 0.3192 T12: 0.0052
REMARK 3 T13: -0.0345 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.3526 L22: 1.4528
REMARK 3 L33: 3.4440 L12: -0.0379
REMARK 3 L13: -0.1073 L23: 1.3207
REMARK 3 S TENSOR
REMARK 3 S11: -0.0683 S12: -0.1215 S13: -0.2138
REMARK 3 S21: 0.3718 S22: 0.0205 S23: -0.0341
REMARK 3 S31: 0.2946 S32: 0.4646 S33: 0.0502
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3533 32.5947 -12.0666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.2637
REMARK 3 T33: 0.2392 T12: -0.0528
REMARK 3 T13: 0.0348 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.0109 L22: 1.9077
REMARK 3 L33: 1.0260 L12: -0.2227
REMARK 3 L13: 0.0131 L23: 0.2775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0517 S12: 0.0635 S13: 0.1159
REMARK 3 S21: -0.1833 S22: 0.0685 S23: -0.0958
REMARK 3 S31: -0.0918 S32: 0.1050 S33: -0.0113
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 198:440)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7910 25.5839 2.9992
REMARK 3 T TENSOR
REMARK 3 T11: 0.1871 T22: 0.2509
REMARK 3 T33: 0.2577 T12: -0.0456
REMARK 3 T13: 0.0303 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 0.8240 L22: 1.1719
REMARK 3 L33: 1.3603 L12: -0.3683
REMARK 3 L13: -0.1127 L23: 0.7591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0091 S12: -0.0009 S13: 0.0954
REMARK 3 S21: 0.0673 S22: -0.0666 S23: 0.0762
REMARK 3 S31: 0.0700 S32: -0.1728 S33: 0.0498
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3505 9.1127 -44.2633
REMARK 3 T TENSOR
REMARK 3 T11: 0.5865 T22: 0.6371
REMARK 3 T33: 0.2374 T12: -0.0838
REMARK 3 T13: 0.0338 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 2.5081 L22: 1.8016
REMARK 3 L33: 1.7696 L12: -0.7062
REMARK 3 L13: 0.1786 L23: 0.2743
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: 0.8295 S13: 0.1203
REMARK 3 S21: -0.6996 S22: 0.1208 S23: 0.0776
REMARK 3 S31: 0.0739 S32: -0.1403 S33: -0.0060
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 89:295)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0696 -2.6870 -33.6387
REMARK 3 T TENSOR
REMARK 3 T11: 0.4961 T22: 0.4395
REMARK 3 T33: 0.2925 T12: -0.0614
REMARK 3 T13: 0.0872 T23: -0.1696
REMARK 3 L TENSOR
REMARK 3 L11: 0.9549 L22: 1.3449
REMARK 3 L33: 1.3118 L12: -0.3016
REMARK 3 L13: -0.2380 L23: 0.3030
REMARK 3 S TENSOR
REMARK 3 S11: -0.1214 S12: 0.3565 S13: -0.1718
REMARK 3 S21: -0.3432 S22: 0.0867 S23: -0.0893
REMARK 3 S31: 0.3158 S32: -0.0456 S33: 0.0150
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 296:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9761 -4.2832 -21.3238
REMARK 3 T TENSOR
REMARK 3 T11: 0.4395 T22: 0.3675
REMARK 3 T33: 0.3116 T12: -0.0948
REMARK 3 T13: 0.0467 T23: -0.1345
REMARK 3 L TENSOR
REMARK 3 L11: 1.2258 L22: 0.7924
REMARK 3 L33: 1.5586 L12: 0.0831
REMARK 3 L13: -0.4668 L23: 0.1758
REMARK 3 S TENSOR
REMARK 3 S11: -0.2230 S12: 0.3056 S13: -0.2372
REMARK 3 S21: -0.1288 S22: 0.1227 S23: 0.0168
REMARK 3 S31: 0.3668 S32: -0.1820 S33: 0.1231
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 402:441)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3901 -16.9014 -24.1898
REMARK 3 T TENSOR
REMARK 3 T11: 0.6928 T22: 0.4093
REMARK 3 T33: 0.5376 T12: 0.0431
REMARK 3 T13: 0.1159 T23: -0.2042
REMARK 3 L TENSOR
REMARK 3 L11: 2.0879 L22: 1.0076
REMARK 3 L33: 2.1977 L12: -0.3275
REMARK 3 L13: -1.3326 L23: 0.3349
REMARK 3 S TENSOR
REMARK 3 S11: -0.0357 S12: -0.0170 S13: -0.4330
REMARK 3 S21: 0.0223 S22: 0.1236 S23: -0.1992
REMARK 3 S31: 0.2889 S32: 0.2344 S33: -0.1972
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 6:46)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4965 91.2419 82.8936
REMARK 3 T TENSOR
REMARK 3 T11: 0.7014 T22: 0.5050
REMARK 3 T33: 0.4482 T12: -0.0137
REMARK 3 T13: -0.0506 T23: -0.1571
REMARK 3 L TENSOR
REMARK 3 L11: 1.7707 L22: 0.6246
REMARK 3 L33: 2.1543 L12: -0.2889
REMARK 3 L13: -0.9489 L23: 0.4355
REMARK 3 S TENSOR
REMARK 3 S11: -0.1740 S12: -0.0792 S13: -0.0288
REMARK 3 S21: 0.6158 S22: 0.1494 S23: -0.2115
REMARK 3 S31: 0.3034 S32: 0.7295 S33: -0.0568
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 47:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9522 26.7333 3.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.3470 T22: 0.5751
REMARK 3 T33: 0.4644 T12: 0.0625
REMARK 3 T13: 0.0603 T23: -0.2104
REMARK 3 L TENSOR
REMARK 3 L11: 0.3556 L22: 0.5485
REMARK 3 L33: 0.7380 L12: -0.0506
REMARK 3 L13: -0.0998 L23: 0.6864
REMARK 3 S TENSOR
REMARK 3 S11: -0.1425 S12: -0.0845 S13: 0.0148
REMARK 3 S21: 0.1761 S22: 0.4708 S23: -0.4060
REMARK 3 S31: 0.4119 S32: 0.7801 S33: -0.1468
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 1:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0388 53.8703 70.0900
REMARK 3 T TENSOR
REMARK 3 T11: 0.7795 T22: 0.3934
REMARK 3 T33: 0.3750 T12: -0.0994
REMARK 3 T13: 0.1537 T23: -0.1537
REMARK 3 L TENSOR
REMARK 3 L11: 1.3520 L22: 2.0464
REMARK 3 L33: 0.8620 L12: 0.6324
REMARK 3 L13: -0.6362 L23: -0.3469
REMARK 3 S TENSOR
REMARK 3 S11: -0.3111 S12: 0.3421 S13: -0.1459
REMARK 3 S21: -0.0864 S22: -0.0256 S23: -0.1503
REMARK 3 S31: 0.9318 S32: -0.2050 S33: 0.1071
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 67:198)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9471 56.9867 105.3962
REMARK 3 T TENSOR
REMARK 3 T11: 0.6443 T22: 1.0244
REMARK 3 T33: 0.5482 T12: 0.2351
REMARK 3 T13: -0.0756 T23: 0.3413
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 0.9346
REMARK 3 L33: 1.5253 L12: -0.1516
REMARK 3 L13: 0.1853 L23: -0.2798
REMARK 3 S TENSOR
REMARK 3 S11: -0.2008 S12: -0.6923 S13: -0.5544
REMARK 3 S21: 0.4527 S22: -0.1431 S23: -0.5688
REMARK 3 S31: 0.4439 S32: 1.5030 S33: 0.2222
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 199:384)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8753 53.4032 94.1484
REMARK 3 T TENSOR
REMARK 3 T11: 0.6344 T22: 0.1767
REMARK 3 T33: 0.3793 T12: 0.0586
REMARK 3 T13: 0.1715 T23: 0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 1.7794 L22: 0.7602
REMARK 3 L33: 2.3729 L12: 0.2161
REMARK 3 L13: -1.5400 L23: -0.1372
REMARK 3 S TENSOR
REMARK 3 S11: -0.4596 S12: -0.1124 S13: -0.5530
REMARK 3 S21: 0.3153 S22: 0.2087 S23: -0.0715
REMARK 3 S31: 0.6212 S32: -0.0813 S33: -0.0279
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 504:504)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8075 59.2737 36.1985
REMARK 3 T TENSOR
REMARK 3 T11: 0.4877 T22: 0.7397
REMARK 3 T33: 0.6631 T12: 0.0744
REMARK 3 T13: 0.1005 T23: -0.2394
REMARK 3 L TENSOR
REMARK 3 L11: 2.5055 L22: 7.3535
REMARK 3 L33: 9.7070 L12: 4.1806
REMARK 3 L13: 4.7382 L23: 8.4374
REMARK 3 S TENSOR
REMARK 3 S11: -0.1715 S12: 0.0638 S13: 0.0599
REMARK 3 S21: 0.4961 S22: -0.4439 S23: 0.9517
REMARK 3 S31: -0.0993 S32: -0.3474 S33: 0.6075
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 505:505)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4266 51.1182 45.7007
REMARK 3 T TENSOR
REMARK 3 T11: 0.8068 T22: 1.2721
REMARK 3 T33: 0.6491 T12: -0.4282
REMARK 3 T13: 0.1386 T23: -0.2209
REMARK 3 L TENSOR
REMARK 3 L11: 2.0677 L22: 2.0858
REMARK 3 L33: 2.2995 L12: 2.0765
REMARK 3 L13: 2.1800 L23: 2.1901
REMARK 3 S TENSOR
REMARK 3 S11: -0.1633 S12: 0.2297 S13: 0.4276
REMARK 3 S21: -0.3557 S22: -0.2010 S23: 1.2292
REMARK 3 S31: -0.9791 S32: 1.0633 S33: 0.3560
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 4I55 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99995
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR, SAGITTALLY -
REMARK 200 HORIZONTALLY FOCUSSED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149411
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 71.844
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3RYC, 3TIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% PEG 4000, 4-6% GLYCEROL, 30 MM
REMARK 280 MAGNESIUM CHLORIDE, 30 MM CALCIUM CHLORIDE, 100 MM MES/IMIDAZOLE
REMARK 280 , PH 6.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 52.08000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.74500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.74500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.08000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.23500
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: HEXAMERIC
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 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 456
REMARK 465 GLU A 457
REMARK 465 GLY A 458
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 MET D 1
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 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 ARG E 145
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 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 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 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 O HOH C 877 O HOH C 878 2.13
REMARK 500 O HOH C 764 O HOH C 765 2.13
REMARK 500 O HOH A 711 O HOH E 235 2.13
REMARK 500 OH TYR D 432 O HOH D 769 2.17
REMARK 500 OE2 GLU B 420 O HOH B 695 2.17
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 HIS A 309 46.86 -108.61
REMARK 500 PHE A 404 -2.27 78.37
REMARK 500 ARG B 2 -75.32 -125.06
REMARK 500 HIS B 37 26.59 -141.22
REMARK 500 ALA B 56 -169.40 -107.07
REMARK 500 THR B 109 -85.67 -116.05
REMARK 500 CYS B 131 84.46 -155.49
REMARK 500 ARG B 284 108.54 -48.34
REMARK 500 TYR C 108 -81.06 -118.02
REMARK 500 HIS C 283 11.70 56.08
REMARK 500 CYS C 305 171.36 179.11
REMARK 500 ALA C 314 144.63 -176.94
REMARK 500 PHE C 404 -2.76 64.56
REMARK 500 GLN D 96 -43.00 -131.79
REMARK 500 THR D 109 -79.64 -127.44
REMARK 500 THR D 180 166.03 70.55
REMARK 500 LYS E 25 133.90 -176.53
REMARK 500 ALA E 143 63.29 -165.88
REMARK 500 LEU F 87 -62.24 -104.88
REMARK 500 SER F 88 172.71 79.07
REMARK 500 GLU F 96 120.49 -38.23
REMARK 500 ARG F 142 -7.95 83.09
REMARK 500 LYS F 188 66.49 -115.39
REMARK 500 GLU F 248 -73.48 -107.55
REMARK 500 TYR F 253 108.39 -48.39
REMARK 500 ILE F 283 -45.92 -137.46
REMARK 500 ALA F 335 55.70 -146.50
REMARK 500 THR F 372 65.70 65.27
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 OD2
REMARK 620 2 ASP A 39 OD1 49.4
REMARK 620 3 THR A 41 O 100.5 82.2
REMARK 620 4 THR A 41 OG1 123.8 74.5 69.3
REMARK 620 5 GLY A 44 O 158.8 143.2 71.3 72.6
REMARK 620 6 GLU A 55 OE2 74.1 119.7 133.7 151.5 97.1
REMARK 620 7 GLU A 55 OE1 76.3 119.6 84.4 148.7 83.4 49.4
REMARK 620 8 HOH A 671 O 104.9 95.4 144.2 75.6 91.8 78.3 126.0
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 O1G
REMARK 620 2 GTP A 501 O1B 88.7
REMARK 620 3 HOH A 602 O 87.7 90.9
REMARK 620 4 HOH A 660 O 83.1 171.4 86.2
REMARK 620 5 HOH A 662 O 83.1 91.3 170.5 90.2
REMARK 620 6 HOH A 708 O 172.1 95.7 98.7 92.8 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 747 O
REMARK 620 2 HOH A 749 O 152.3
REMARK 620 3 HOH A 750 O 143.1 63.9
REMARK 620 N 1 2
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 O1A 93.3
REMARK 620 3 HOH B 624 O 71.9 91.3
REMARK 620 4 HOH B 667 O 78.6 89.5 150.5
REMARK 620 5 HOH B 729 O 151.8 93.2 80.6 128.9
REMARK 620 6 HOH C 755 O 87.2 172.6 81.9 97.8 83.0
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 OE2
REMARK 620 2 GLU B 113 OE1 43.3
REMARK 620 3 HOH B 656 O 70.4 91.0
REMARK 620 4 HOH B 677 O 58.0 101.3 59.2
REMARK 620 5 HOH B 678 O 111.0 152.6 67.0 54.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 506 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 680 O
REMARK 620 2 HOH B 689 O 68.9
REMARK 620 3 HOH B 746 O 106.7 121.2
REMARK 620 4 HOH B 747 O 87.2 145.0 89.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 39 OD2
REMARK 620 2 ASP C 39 OD1 49.7
REMARK 620 3 THR C 41 O 90.4 79.0
REMARK 620 4 THR C 41 OG1 127.5 77.9 76.0
REMARK 620 5 GLY C 44 O 153.3 154.1 87.3 77.6
REMARK 620 6 GLU C 55 OE2 78.3 123.3 128.4 147.6 82.3
REMARK 620 7 GLU C 55 OE1 76.7 120.5 77.7 143.8 76.8 50.7
REMARK 620 8 HOH C 754 O 102.6 94.3 156.2 80.3 89.5 74.4 124.4
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 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 501 O1G
REMARK 620 2 GTP C 501 O1B 85.7
REMARK 620 3 HOH C 735 O 86.3 86.2
REMARK 620 4 HOH C 753 O 88.9 87.0 172.0
REMARK 620 5 HOH C 770 O 87.9 167.0 82.2 104.1
REMARK 620 6 HOH C 880 O 176.4 93.0 90.3 94.3 92.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 11 OE1
REMARK 620 2 ASP D 179 OD1 100.0
REMARK 620 3 GDP D 600 O1A 71.7 94.5
REMARK 620 4 HOH D 753 O 69.1 167.2 88.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 318 OD2
REMARK 620 2 ACP F 703 O1G 61.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 331 OE1
REMARK 620 2 ACP F 703 O2G 88.7
REMARK 620 3 ACP F 703 O2B 85.6 74.5
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 CL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA 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 MES B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP F 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I4T RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ZAMPANOLIDE
REMARK 900 RELATED ID: 4I50 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH EPOTHILONE A
REMARK 900 RELATED ID: 4IHJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ADP
REMARK 900 RELATED ID: 4IIJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN ABSENCE OF NUCLEOTIDE IN CHAIN F
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 BRAIN TUBULIN PREPARATIONS CONTAIN THREE TUBULIN SUBPOPULATIONS:
REMARK 999 TYROSINATED (20-30%), DE-TYROSINATED (30-40%) AND DELTA-2 TUBULIN
REMARK 999 (ABOUT 40%) (LACKING THE CARBOXYTERMINAL GLUTAMYL-TYROSINE).
REMARK 999 TUBULIN-TYROSINE LIGASE BINDS ALL THREE VARIANTS, BUT ONLY CAN
REMARK 999 MODIFY DE-TYROSINATED TUBULIN. ALTHOUGH ALL SUBPOPULATIONS ARE
REMARK 999 PRESENT IN THE CRYSTAL, ONLY THE DE-TYROSINATED FORM WAS MODELED
REMARK 999 WITH A TERMINAL CARBOXYLATE TO DESCRIBE THE LIGASE REACTION. IN THE
REMARK 999 SEQRES RECORD FOR CHAIN A THE TERMINAL TYR WAS OMITTED TO MATCH THE
REMARK 999 MODELED VARIANT OF ALPHA-TUBULIN.
DBREF 4I55 A 1 450 UNP P81947 TBA1B_BOVIN 1 450
DBREF 4I55 B 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4I55 C 1 450 UNP P81947 TBA1B_BOVIN 1 450
DBREF 4I55 D 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4I55 E 3 145 UNP P63043 STMN4_RAT 47 189
DBREF 4I55 F 1 378 UNP E1BQ43 E1BQ43_CHICK 1 378
SEQADV 4I55 MET E 3 UNP P63043 ILE 47 CLONING ARTIFACT
SEQADV 4I55 ALA E 4 UNP P63043 SER 48 CLONING ARTIFACT
SEQADV 4I55 HIS F 379 UNP E1BQ43 EXPRESSION TAG
SEQADV 4I55 HIS F 380 UNP E1BQ43 EXPRESSION TAG
SEQADV 4I55 HIS F 381 UNP E1BQ43 EXPRESSION TAG
SEQADV 4I55 HIS F 382 UNP E1BQ43 EXPRESSION TAG
SEQADV 4I55 HIS F 383 UNP E1BQ43 EXPRESSION TAG
SEQADV 4I55 HIS F 384 UNP E1BQ43 EXPRESSION TAG
SEQRES 1 A 450 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 A 450 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 A 450 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 A 450 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 A 450 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 A 450 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 A 450 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 A 450 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 A 450 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 A 450 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 A 450 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 A 450 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 A 450 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 A 450 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 A 450 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 A 450 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 A 450 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 A 450 PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE
SEQRES 19 A 450 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 A 450 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 A 450 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 A 450 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 A 450 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 A 450 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 A 450 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 A 450 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 A 450 ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 450 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 A 450 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 A 450 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 A 450 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 A 450 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 A 450 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 A 450 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 A 450 GLU GLY GLU GLU GLU GLY GLU GLU
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 450 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 C 450 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 C 450 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 C 450 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 C 450 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 C 450 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 C 450 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 C 450 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 C 450 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 C 450 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 C 450 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 C 450 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 C 450 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 C 450 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 C 450 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 C 450 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 C 450 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 C 450 PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE
SEQRES 19 C 450 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 C 450 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 C 450 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 C 450 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 C 450 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 C 450 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 C 450 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 C 450 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 C 450 ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 450 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 C 450 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 C 450 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 C 450 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 C 450 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 C 450 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 C 450 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 C 450 GLU GLY GLU GLU GLU GLY GLU GLU
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 PHE 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 42
HET MG A 502 1
HET CA A 503 1
HET CL A 504 1
HET CA A 505 1
HET GDP B 501 38
HET MG B 502 1
HET CA B 503 1
HET MES B 504 25
HET MES B 505 25
HET MG B 506 1
HET GTP C 501 42
HET MG C 502 1
HET CA C 503 1
HET GDP D 600 38
HET MG D 601 1
HET MG F 701 1
HET MG F 702 1
HET ACP F 703 48
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 7 GTP 2(C10 H16 N5 O14 P3)
FORMUL 8 MG 7(MG 2+)
FORMUL 9 CA 4(CA 2+)
FORMUL 10 CL CL 1-
FORMUL 12 GDP 2(C10 H15 N5 O11 P2)
FORMUL 15 MES 2(C6 H13 N O4 S)
FORMUL 25 ACP C11 H18 N5 O12 P3
FORMUL 26 HOH *765(H2 O)
HELIX 1 1 GLY A 10 GLY A 29 1 20
HELIX 2 2 ASP A 47 THR A 51 5 5
HELIX 3 3 VAL A 74 GLY A 81 1 8
HELIX 4 4 HIS A 88 GLU A 90 5 3
HELIX 5 5 ASN A 102 TYR A 108 1 7
HELIX 6 6 ILE A 110 GLN A 128 1 19
HELIX 7 7 GLY A 143 TYR A 161 1 19
HELIX 8 8 VAL A 182 LEU A 195 1 14
HELIX 9 9 GLU A 196 SER A 198 5 3
HELIX 10 10 ASN A 206 ASP A 218 1 13
HELIX 11 11 THR A 223 PHE A 244 1 22
HELIX 12 12 ASP A 251 VAL A 260 1 10
HELIX 13 13 SER A 287 CYS A 295 1 9
HELIX 14 14 PHE A 296 GLN A 301 5 6
HELIX 15 15 ASP A 306 GLY A 310 5 5
HELIX 16 16 VAL A 324 THR A 337 1 14
HELIX 17 17 ILE A 384 ALA A 400 1 17
HELIX 18 18 PHE A 404 GLY A 410 1 7
HELIX 19 19 GLU A 415 VAL A 437 1 23
HELIX 20 20 GLY B 10 HIS B 28 1 19
HELIX 21 21 SER B 40 LEU B 46 5 5
HELIX 22 22 ARG B 48 VAL B 51 5 4
HELIX 23 23 PRO B 72 GLY B 81 1 10
HELIX 24 24 ARG B 88 ASP B 90 5 3
HELIX 25 25 ASN B 102 TYR B 108 1 7
HELIX 26 26 THR B 109 SER B 128 1 20
HELIX 27 27 GLY B 144 TYR B 161 1 18
HELIX 28 28 SER B 174 SER B 178 5 5
HELIX 29 29 VAL B 182 THR B 198 1 17
HELIX 30 30 ASN B 206 THR B 216 1 11
HELIX 31 31 THR B 223 THR B 239 1 17
HELIX 32 32 THR B 239 PHE B 244 1 6
HELIX 33 33 ASP B 251 VAL B 260 1 10
HELIX 34 34 THR B 287 PHE B 296 1 10
HELIX 35 35 ASP B 297 MET B 301 5 5
HELIX 36 36 ASP B 306 GLY B 310 5 5
HELIX 37 37 SER B 324 ASN B 339 1 16
HELIX 38 38 SER B 340 PHE B 343 5 4
HELIX 39 39 ILE B 384 ARG B 400 1 17
HELIX 40 40 LEU B 405 GLY B 410 1 6
HELIX 41 41 ASP B 414 ASP B 437 1 24
HELIX 42 42 GLY C 10 GLY C 29 1 20
HELIX 43 43 ASP C 47 THR C 51 5 5
HELIX 44 44 PRO C 72 THR C 80 1 9
HELIX 45 45 HIS C 88 GLU C 90 5 3
HELIX 46 46 ASN C 102 TYR C 108 1 7
HELIX 47 47 ILE C 110 GLU C 113 5 4
HELIX 48 48 ILE C 114 GLN C 128 1 15
HELIX 49 49 GLY C 143 GLY C 162 1 20
HELIX 50 50 VAL C 182 LEU C 195 1 14
HELIX 51 51 GLU C 196 SER C 198 5 3
HELIX 52 52 ASN C 206 LEU C 217 1 12
HELIX 53 53 THR C 223 PHE C 244 1 22
HELIX 54 54 ASP C 251 VAL C 260 1 10
HELIX 55 55 SER C 277 TYR C 282 1 6
HELIX 56 56 SER C 287 CYS C 295 1 9
HELIX 57 57 PHE C 296 GLN C 301 5 6
HELIX 58 58 ASP C 306 GLY C 310 5 5
HELIX 59 59 VAL C 324 ARG C 339 1 16
HELIX 60 60 ILE C 384 ALA C 400 1 17
HELIX 61 61 PHE C 404 GLY C 410 1 7
HELIX 62 62 GLU C 414 VAL C 437 1 24
HELIX 63 63 GLY D 10 GLY D 29 1 20
HELIX 64 64 SER D 40 LEU D 46 5 5
HELIX 65 65 ARG D 48 VAL D 51 5 4
HELIX 66 66 PRO D 72 GLY D 81 1 10
HELIX 67 67 PHE D 83 PHE D 87 5 5
HELIX 68 68 ARG D 88 ASP D 90 5 3
HELIX 69 69 ASN D 102 THR D 109 1 8
HELIX 70 70 THR D 109 SER D 128 1 20
HELIX 71 71 GLY D 144 TYR D 161 1 18
HELIX 72 72 VAL D 182 THR D 198 1 17
HELIX 73 73 ASN D 206 ARG D 215 1 10
HELIX 74 74 THR D 223 PHE D 244 1 22
HELIX 75 75 ASP D 251 VAL D 260 1 10
HELIX 76 76 THR D 287 PHE D 296 1 10
HELIX 77 77 ASP D 297 MET D 301 5 5
HELIX 78 78 ASP D 306 GLY D 310 5 5
HELIX 79 79 SER D 324 ASN D 339 1 16
HELIX 80 80 SER D 340 PHE D 343 5 4
HELIX 81 81 ILE D 384 ARG D 400 1 17
HELIX 82 82 LEU D 405 GLY D 410 1 6
HELIX 83 83 ASP D 414 ALA D 438 1 25
HELIX 84 84 SER E 46 GLU E 141 1 96
HELIX 85 85 SER F 11 THR F 24 1 14
HELIX 86 86 PRO F 48 LEU F 52 5 5
HELIX 87 87 GLY F 67 LEU F 71 5 5
HELIX 88 88 ARG F 73 SER F 84 1 12
HELIX 89 89 GLU F 127 ARG F 142 1 16
HELIX 90 90 GLU F 165 GLN F 176 1 12
HELIX 91 91 ASN F 242 GLU F 248 1 7
HELIX 92 92 PHE F 264 ASN F 276 1 13
HELIX 93 93 THR F 278 ILE F 283 1 6
HELIX 94 94 ILE F 283 SER F 303 1 21
HELIX 95 95 ALA F 339 LYS F 341 5 3
HELIX 96 96 LEU F 342 ALA F 354 1 13
SHEET 1 A 6 LEU A 92 THR A 94 0
SHEET 2 A 6 ALA A 65 ASP A 69 1 N PHE A 67 O ILE A 93
SHEET 3 A 6 CYS A 4 VAL A 9 1 N HIS A 8 O VAL A 68
SHEET 4 A 6 GLY A 134 SER A 140 1 O LEU A 136 N ILE A 7
SHEET 5 A 6 SER A 165 TYR A 172 1 O LEU A 167 N VAL A 137
SHEET 6 A 6 CYS A 200 ASP A 205 1 O VAL A 204 N SER A 170
SHEET 1 B 2 PHE A 53 GLU A 55 0
SHEET 2 B 2 HIS A 61 PRO A 63 -1 O VAL A 62 N SER A 54
SHEET 1 C 6 LEU A 269 ALA A 273 0
SHEET 2 C 6 ARG A 373 THR A 381 -1 O SER A 379 N LEU A 269
SHEET 3 C 6 TYR A 312 GLY A 321 -1 N LEU A 318 O CYS A 376
SHEET 4 C 6 THR A 349 ASN A 356 1 O GLY A 354 N TYR A 319
SHEET 5 C 6 GLY E 17 LYS E 25 -1 O PHE E 20 N VAL A 353
SHEET 6 C 6 GLU E 7 CYS E 14 -1 N ASN E 12 O SER E 19
SHEET 1 D10 PHE B 92 PHE B 94 0
SHEET 2 D10 ALA B 65 ASP B 69 1 N LEU B 67 O VAL B 93
SHEET 3 D10 ILE B 4 ALA B 9 1 N GLN B 8 O VAL B 68
SHEET 4 D10 GLY B 134 SER B 140 1 O GLN B 136 N ILE B 7
SHEET 5 D10 ILE B 165 MET B 172 1 O ILE B 165 N PHE B 135
SHEET 6 D10 GLU B 200 ASP B 205 1 O ILE B 204 N MET B 172
SHEET 7 D10 PHE B 267 ALA B 273 1 O PHE B 268 N THR B 201
SHEET 8 D10 MET B 373 SER B 381 -1 O GLY B 379 N MET B 269
SHEET 9 D10 TYR B 312 GLY B 321 -1 N LEU B 313 O ASN B 380
SHEET 10 D10 VAL B 351 CYS B 356 1 O LYS B 352 N ALA B 317
SHEET 1 E 2 TYR B 53 GLU B 55 0
SHEET 2 E 2 TYR B 61 PRO B 63 -1 O VAL B 62 N ASN B 54
SHEET 1 F 6 LEU C 92 THR C 94 0
SHEET 2 F 6 ALA C 65 ASP C 69 1 N PHE C 67 O ILE C 93
SHEET 3 F 6 CYS C 4 VAL C 9 1 N HIS C 8 O VAL C 68
SHEET 4 F 6 GLY C 134 SER C 140 1 O PHE C 138 N ILE C 7
SHEET 5 F 6 SER C 165 TYR C 172 1 O LEU C 167 N VAL C 137
SHEET 6 F 6 CYS C 200 ASP C 205 1 O PHE C 202 N GLU C 168
SHEET 1 G 2 PHE C 53 GLU C 55 0
SHEET 2 G 2 HIS C 61 PRO C 63 -1 O VAL C 62 N SER C 54
SHEET 1 H 4 LEU C 269 ALA C 273 0
SHEET 2 H 4 ARG C 373 THR C 381 -1 O SER C 379 N LEU C 269
SHEET 3 H 4 TYR C 312 GLY C 321 -1 N MET C 313 O ASN C 380
SHEET 4 H 4 LYS C 352 ASN C 356 1 O LYS C 352 N LEU C 317
SHEET 1 I10 PHE D 92 PHE D 94 0
SHEET 2 I10 ALA D 65 ASP D 69 1 N LEU D 67 O VAL D 93
SHEET 3 I10 ILE D 4 ALA D 9 1 N GLN D 8 O ILE D 66
SHEET 4 I10 GLY D 134 SER D 140 1 O GLN D 136 N ILE D 7
SHEET 5 I10 ILE D 165 MET D 172 1 O PHE D 169 N LEU D 137
SHEET 6 I10 GLU D 200 ASP D 205 1 O TYR D 202 N THR D 168
SHEET 7 I10 PHE D 267 ALA D 273 1 O PHE D 268 N THR D 201
SHEET 8 I10 MET D 373 SER D 381 -1 O GLY D 379 N MET D 269
SHEET 9 I10 TYR D 312 GLY D 321 -1 N LEU D 313 O ASN D 380
SHEET 10 I10 VAL D 351 CYS D 356 1 O ALA D 354 N PHE D 319
SHEET 1 J 2 TYR D 53 ALA D 56 0
SHEET 2 J 2 LYS D 60 PRO D 63 -1 O LYS D 60 N ALA D 56
SHEET 1 K 5 TRP F 27 ARG F 29 0
SHEET 2 K 5 TYR F 2 VAL F 6 1 N TYR F 2 O LYS F 28
SHEET 3 K 5 LEU F 39 LEU F 41 1 O LEU F 41 N VAL F 5
SHEET 4 K 5 LEU F 61 VAL F 62 1 O LEU F 61 N MET F 40
SHEET 5 K 5 GLN F 310 SER F 311 1 O GLN F 310 N VAL F 62
SHEET 1 L 4 SER F 97 ILE F 100 0
SHEET 2 L 4 HIS F 180 LYS F 184 -1 O HIS F 180 N ILE F 100
SHEET 3 L 4 TRP F 147 SER F 151 -1 N ILE F 148 O GLN F 183
SHEET 4 L 4 ILE F 160 SER F 163 -1 O SER F 163 N TRP F 147
SHEET 1 M 5 GLU F 261 PHE F 263 0
SHEET 2 M 5 VAL F 220 THR F 223 -1 N LEU F 221 O MET F 262
SHEET 3 M 5 PHE F 199 VAL F 207 -1 N ARG F 202 O VAL F 220
SHEET 4 M 5 GLN F 313 VAL F 321 -1 O PHE F 319 N ILE F 201
SHEET 5 M 5 VAL F 327 ASN F 333 -1 O ASN F 333 N GLY F 316
SHEET 1 N 5 GLU F 261 PHE F 263 0
SHEET 2 N 5 VAL F 220 THR F 223 -1 N LEU F 221 O MET F 262
SHEET 3 N 5 PHE F 199 VAL F 207 -1 N ARG F 202 O VAL F 220
SHEET 4 N 5 ILE F 213 TYR F 216 -1 O TYR F 214 N LEU F 206
SHEET 5 N 5 PHE F 375 LEU F 378 -1 O LEU F 378 N ILE F 213
LINK OD2 ASP A 39 CA CA A 503 1555 1555 2.58
LINK OD1 ASP A 39 CA CA A 503 1555 1555 2.65
LINK O THR A 41 CA CA A 503 1555 1555 2.45
LINK OG1 THR A 41 CA CA A 503 1555 1555 2.95
LINK O GLY A 44 CA CA A 503 1555 1555 2.53
LINK OE2 GLU A 55 CA CA A 503 1555 1555 2.58
LINK OE1 GLU A 55 CA CA A 503 1555 1555 2.71
LINK O1G GTP A 501 MG MG A 502 1555 1555 2.12
LINK O1B GTP A 501 MG MG A 502 1555 1555 2.18
LINK MG MG A 502 O HOH A 602 1555 1555 2.19
LINK MG MG A 502 O HOH A 660 1555 1555 2.33
LINK MG MG A 502 O HOH A 662 1555 1555 2.28
LINK MG MG A 502 O HOH A 708 1555 1555 2.11
LINK CA CA A 503 O HOH A 671 1555 1555 2.56
LINK CA CA A 505 O HOH A 747 1555 1555 2.70
LINK CA CA A 505 O HOH A 749 1555 1555 2.98
LINK CA CA A 505 O HOH A 750 1555 1555 2.97
LINK OE1 GLN B 11 MG MG B 502 1555 1555 2.32
LINK OE2 GLU B 113 CA CA B 503 1555 1555 2.72
LINK OE1 GLU B 113 CA CA B 503 1555 1555 3.17
LINK O1A GDP B 501 MG MG B 502 1555 1555 2.32
LINK MG MG B 502 O HOH B 624 1555 1555 2.58
LINK MG MG B 502 O HOH B 667 1555 1555 2.56
LINK MG MG B 502 O HOH B 729 1555 1555 2.20
LINK MG MG B 502 O HOH C 755 1555 1555 2.52
LINK CA CA B 503 O HOH B 656 1555 1555 2.60
LINK CA CA B 503 O HOH B 677 1555 1555 2.79
LINK CA CA B 503 O HOH B 678 1555 1555 2.66
LINK MG MG B 506 O HOH B 680 1555 1555 2.84
LINK MG MG B 506 O HOH B 689 1555 1555 2.63
LINK MG MG B 506 O HOH B 746 1555 1555 2.78
LINK MG MG B 506 O HOH B 747 1555 1555 2.85
LINK OD2 ASP C 39 CA CA C 503 1555 1555 2.56
LINK OD1 ASP C 39 CA CA C 503 1555 1555 2.66
LINK O THR C 41 CA CA C 503 1555 1555 2.45
LINK OG1 THR C 41 CA CA C 503 1555 1555 2.57
LINK O GLY C 44 CA CA C 503 1555 1555 2.56
LINK OE2 GLU C 55 CA CA C 503 1555 1555 2.58
LINK OE1 GLU C 55 CA CA C 503 1555 1555 2.60
LINK O1G GTP C 501 MG MG C 502 1555 1555 2.19
LINK O1B GTP C 501 MG MG C 502 1555 1555 2.25
LINK MG MG C 502 O HOH C 735 1555 1555 2.25
LINK MG MG C 502 O HOH C 753 1555 1555 2.22
LINK MG MG C 502 O HOH C 770 1555 1555 2.28
LINK MG MG C 502 O HOH C 880 1555 1555 2.15
LINK CA CA C 503 O HOH C 754 1555 1555 2.52
LINK OE1 GLN D 11 MG MG D 601 1555 1555 2.85
LINK OD1 ASP D 179 MG MG D 601 1555 1555 2.85
LINK O1A GDP D 600 MG MG D 601 1555 1555 2.67
LINK MG MG D 601 O HOH D 753 1555 1555 2.81
LINK OD2 ASP F 318 MG MG F 701 1555 1555 2.97
LINK OE1 GLU F 331 MG MG F 702 1555 1555 2.81
LINK MG MG F 701 O1G ACP F 703 1555 1555 2.42
LINK MG MG F 702 O2G ACP F 703 1555 1555 2.70
LINK MG MG F 702 O2B ACP F 703 1555 1555 2.79
CISPEP 1 ALA A 273 PRO A 274 0 -0.23
CISPEP 2 ALA B 273 PRO B 274 0 -2.97
CISPEP 3 ALA C 273 PRO C 274 0 5.30
CISPEP 4 THR D 180 VAL D 181 0 -12.11
CISPEP 5 ALA D 273 PRO D 274 0 -3.58
CISPEP 6 ALA E 143 SER E 144 0 0.40
CISPEP 7 GLU F 193 PRO F 194 0 1.89
CISPEP 8 GLU F 258 GLY F 259 0 -1.39
CISPEP 9 GLY F 259 ASN F 260 0 -2.51
CISPEP 10 PRO F 371 THR F 372 0 -0.32
SITE 1 AC1 28 GLY A 10 GLN A 11 ALA A 12 GLN A 15
SITE 2 AC1 28 ASP A 98 ALA A 99 ALA A 100 ASN A 101
SITE 3 AC1 28 SER A 140 GLY A 143 GLY A 144 THR A 145
SITE 4 AC1 28 GLY A 146 VAL A 177 GLU A 183 ASN A 206
SITE 5 AC1 28 TYR A 224 ASN A 228 ILE A 231 MG A 502
SITE 6 AC1 28 HOH A 601 HOH A 602 HOH A 613 HOH A 637
SITE 7 AC1 28 HOH A 660 HOH A 662 HOH A 669 LYS B 254
SITE 1 AC2 5 GTP A 501 HOH A 602 HOH A 660 HOH A 662
SITE 2 AC2 5 HOH A 708
SITE 1 AC3 5 ASP A 39 THR A 41 GLY A 44 GLU A 55
SITE 2 AC3 5 HOH A 671
SITE 1 AC4 4 TYR A 161 GLY A 162 LYS A 163 LYS A 164
SITE 1 AC5 4 HOH A 747 HOH A 749 HOH A 750 ASP E 44
SITE 1 AC6 23 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC6 23 SER B 140 GLY B 143 GLY B 144 THR B 145
SITE 3 AC6 23 GLY B 146 VAL B 177 ASP B 179 GLU B 183
SITE 4 AC6 23 ASN B 206 TYR B 224 ASN B 228 MG B 502
SITE 5 AC6 23 HOH B 601 HOH B 602 HOH B 607 HOH B 658
SITE 6 AC6 23 HOH B 659 HOH B 662 HOH B 667
SITE 1 AC7 6 GLN B 11 GDP B 501 HOH B 624 HOH B 667
SITE 2 AC7 6 HOH B 729 HOH C 755
SITE 1 AC8 5 GLU B 113 HOH B 656 HOH B 677 HOH B 678
SITE 2 AC8 5 GLU C 284
SITE 1 AC9 9 TRP A 407 ARG B 158 PRO B 162 ASP B 163
SITE 2 AC9 9 ARG B 164 MET B 166 ASN B 197 ASP B 199
SITE 3 AC9 9 ARG B 253
SITE 1 BC1 6 PHE B 296 ASP B 297 SER B 298 ARG B 308
SITE 2 BC1 6 ASN B 339 HOH B 691
SITE 1 BC2 4 HOH B 680 HOH B 689 HOH B 746 HOH B 747
SITE 1 BC3 29 GLY C 10 GLN C 11 ALA C 12 GLN C 15
SITE 2 BC3 29 ASP C 98 ALA C 99 ALA C 100 ASN C 101
SITE 3 BC3 29 SER C 140 GLY C 143 GLY C 144 THR C 145
SITE 4 BC3 29 GLY C 146 VAL C 177 GLU C 183 ASN C 206
SITE 5 BC3 29 TYR C 224 ASN C 228 ILE C 231 MG C 502
SITE 6 BC3 29 HOH C 650 HOH C 670 HOH C 735 HOH C 737
SITE 7 BC3 29 HOH C 743 HOH C 753 HOH C 770 HOH C 833
SITE 8 BC3 29 LYS D 254
SITE 1 BC4 5 GTP C 501 HOH C 735 HOH C 753 HOH C 770
SITE 2 BC4 5 HOH C 880
SITE 1 BC5 5 ASP C 39 THR C 41 GLY C 44 GLU C 55
SITE 2 BC5 5 HOH C 754
SITE 1 BC6 18 GLY D 10 GLN D 11 CYS D 12 GLN D 15
SITE 2 BC6 18 SER D 140 GLY D 143 GLY D 144 THR D 145
SITE 3 BC6 18 GLY D 146 VAL D 177 GLU D 183 ASN D 206
SITE 4 BC6 18 TYR D 224 ASN D 228 MG D 601 HOH D 705
SITE 5 BC6 18 HOH D 741 HOH D 773
SITE 1 BC7 4 GLN D 11 ASP D 179 GDP D 600 HOH D 753
SITE 1 BC8 3 ASP F 318 GLU F 331 ACP F 703
SITE 1 BC9 5 GLU A 450 LYS F 74 GLU F 331 ASN F 333
SITE 2 BC9 5 ACP F 703
SITE 1 CC1 20 GLU A 450 LYS F 74 ILE F 148 LYS F 150
SITE 2 CC1 20 GLN F 183 LYS F 184 TYR F 185 LEU F 186
SITE 3 CC1 20 LYS F 198 ASP F 200 HIS F 239 THR F 241
SITE 4 CC1 20 ASN F 242 ASP F 318 MET F 320 ILE F 330
SITE 5 CC1 20 GLU F 331 ASN F 333 MG F 701 MG F 702
CRYST1 104.160 156.470 181.490 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 0.009601 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006391 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005510 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
