HEADER CELL CYCLE 20-DEC-12 4IIJ
TITLE CRYSTAL STRUCTURE OF TUBULIN-STATHMIN-TTL-APO 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, GTPASE, MICROTUBULE, STATHMIN,
KEYWDS 2 CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.PROTA,M.M.MAGIERA,M.KUIJPERS,K.BARGSTEN,D.FREY,M.WIESER,R.JAUSSI,
AUTHOR 2 C.C.HOOGENRAAD,R.A.KAMMERER,C.JANKE,M.O.STEINMETZ
REVDAT 5 20-SEP-23 4IIJ 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4IIJ 1 REMARK
REVDAT 3 20-FEB-13 4IIJ 1 JRNL
REVDAT 2 13-FEB-13 4IIJ 1 JRNL
REVDAT 1 30-JAN-13 4IIJ 0
JRNL AUTH A.E.PROTA,M.M.MAGIERA,M.KUIJPERS,K.BARGSTEN,D.FREY,M.WIESER,
JRNL AUTH 2 R.JAUSSI,C.C.HOOGENRAAD,R.A.KAMMERER,C.JANKE,M.O.STEINMETZ
JRNL TITL STRUCTURAL BASIS OF TUBULIN TYROSINATION BY TUBULIN TYROSINE
JRNL TITL 2 LIGASE.
JRNL REF J.CELL BIOL. V. 200 259 2013
JRNL REFN ISSN 0021-9525
JRNL PMID 23358242
JRNL DOI 10.1083/JCB.201211017
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 90582
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 4511
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 62.2929 - 8.0732 0.99 3077 166 0.1949 0.2062
REMARK 3 2 8.0732 - 6.4100 1.00 2966 157 0.1878 0.2108
REMARK 3 3 6.4100 - 5.6003 1.00 2939 150 0.2025 0.2437
REMARK 3 4 5.6003 - 5.0885 1.00 2903 147 0.1900 0.2472
REMARK 3 5 5.0885 - 4.7240 1.00 2880 174 0.1536 0.2000
REMARK 3 6 4.7240 - 4.4455 1.00 2880 158 0.1411 0.1644
REMARK 3 7 4.4455 - 4.2229 1.00 2908 146 0.1500 0.2074
REMARK 3 8 4.2229 - 4.0391 1.00 2882 145 0.1633 0.1975
REMARK 3 9 4.0391 - 3.8837 1.00 2889 138 0.1729 0.2099
REMARK 3 10 3.8837 - 3.7497 1.00 2862 161 0.1757 0.2144
REMARK 3 11 3.7497 - 3.6324 1.00 2862 144 0.1833 0.2238
REMARK 3 12 3.6324 - 3.5286 1.00 2855 160 0.1929 0.2449
REMARK 3 13 3.5286 - 3.4357 1.00 2845 153 0.2070 0.2597
REMARK 3 14 3.4357 - 3.3519 1.00 2846 149 0.2157 0.2497
REMARK 3 15 3.3519 - 3.2757 1.00 2838 183 0.2165 0.2699
REMARK 3 16 3.2757 - 3.2060 1.00 2871 133 0.2292 0.3000
REMARK 3 17 3.2060 - 3.1419 1.00 2855 141 0.2263 0.3040
REMARK 3 18 3.1419 - 3.0826 1.00 2868 153 0.2287 0.2628
REMARK 3 19 3.0826 - 3.0275 1.00 2818 149 0.2311 0.2780
REMARK 3 20 3.0275 - 2.9762 1.00 2855 140 0.2352 0.2755
REMARK 3 21 2.9762 - 2.9282 1.00 2851 148 0.2519 0.3114
REMARK 3 22 2.9282 - 2.8832 1.00 2851 131 0.2653 0.3089
REMARK 3 23 2.8832 - 2.8408 1.00 2862 140 0.2617 0.3053
REMARK 3 24 2.8408 - 2.8008 1.00 2839 131 0.2682 0.3120
REMARK 3 25 2.8008 - 2.7629 1.00 2857 163 0.2794 0.3165
REMARK 3 26 2.7629 - 2.7270 1.00 2792 165 0.2797 0.3366
REMARK 3 27 2.7270 - 2.6929 1.00 2870 161 0.2994 0.3216
REMARK 3 28 2.6929 - 2.6605 1.00 2807 142 0.3133 0.3197
REMARK 3 29 2.6605 - 2.6296 1.00 2824 145 0.3063 0.3620
REMARK 3 30 2.6296 - 2.6000 1.00 2819 138 0.3093 0.3437
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 : 0.32
REMARK 3 B_SOL : 43.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.90290
REMARK 3 B22 (A**2) : 18.53040
REMARK 3 B33 (A**2) : -0.18760
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 : 0.004 17278
REMARK 3 ANGLE : 0.805 23464
REMARK 3 CHIRALITY : 0.057 2560
REMARK 3 PLANARITY : 0.003 3053
REMARK 3 DIHEDRAL : 14.812 6448
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): 31.3533 87.1414 52.2594
REMARK 3 T TENSOR
REMARK 3 T11: 0.5798 T22: 0.5505
REMARK 3 T33: 0.4955 T12: -0.1522
REMARK 3 T13: 0.1024 T23: -0.1802
REMARK 3 L TENSOR
REMARK 3 L11: 0.5660 L22: 2.8805
REMARK 3 L33: 2.2345 L12: -0.6259
REMARK 3 L13: -0.2365 L23: 1.4617
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: 0.1840 S13: 0.1191
REMARK 3 S21: -0.5248 S22: 0.2653 S23: -0.2919
REMARK 3 S31: -0.6144 S32: 0.5176 S33: -0.1493
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 181:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9674 80.9612 66.2668
REMARK 3 T TENSOR
REMARK 3 T11: 0.4215 T22: 0.3742
REMARK 3 T33: 0.4539 T12: -0.0035
REMARK 3 T13: 0.0593 T23: -0.1081
REMARK 3 L TENSOR
REMARK 3 L11: 0.9967 L22: 2.4584
REMARK 3 L33: 3.5815 L12: -0.3027
REMARK 3 L13: -0.4204 L23: 0.9422
REMARK 3 S TENSOR
REMARK 3 S11: 0.0905 S12: -0.0443 S13: 0.0671
REMARK 3 S21: 0.2373 S22: -0.0430 S23: 0.2407
REMARK 3 S31: -0.2407 S32: -0.0905 S33: -0.0395
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 312:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4925 81.9365 73.6684
REMARK 3 T TENSOR
REMARK 3 T11: 0.5620 T22: 0.4141
REMARK 3 T33: 0.4345 T12: -0.0008
REMARK 3 T13: 0.0769 T23: -0.1156
REMARK 3 L TENSOR
REMARK 3 L11: 0.5971 L22: 2.4558
REMARK 3 L33: 1.8482 L12: -0.4980
REMARK 3 L13: -0.0870 L23: 1.2338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: -0.2055 S13: 0.0878
REMARK 3 S21: 0.4241 S22: 0.0993 S23: 0.2066
REMARK 3 S31: -0.0405 S32: 0.0579 S33: -0.0270
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 402:436)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6797 60.7378 60.8868
REMARK 3 T TENSOR
REMARK 3 T11: 0.4803 T22: 0.4905
REMARK 3 T33: 0.5200 T12: 0.1235
REMARK 3 T13: -0.0480 T23: -0.1738
REMARK 3 L TENSOR
REMARK 3 L11: 0.4428 L22: 1.6870
REMARK 3 L33: 3.5588 L12: 0.3964
REMARK 3 L13: 0.6898 L23: 1.2920
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: 0.1286 S13: -0.4456
REMARK 3 S21: 0.4470 S22: 0.0400 S23: -0.0658
REMARK 3 S31: 0.5541 S32: 0.9504 S33: -0.1071
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 437:437)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5741 65.3923 84.2253
REMARK 3 T TENSOR
REMARK 3 T11: 1.4776 T22: 0.8656
REMARK 3 T33: 1.0400 T12: 0.2747
REMARK 3 T13: 0.4034 T23: 0.3477
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0003
REMARK 3 L33: 2.0001 L12: 2.0003
REMARK 3 L13: -3.4881 L23: 1.9999
REMARK 3 S TENSOR
REMARK 3 S11: -0.9969 S12: 1.9027 S13: 4.4576
REMARK 3 S21: -4.0872 S22: -2.7051 S23: -1.6911
REMARK 3 S31: 7.0528 S32: 1.3148 S33: 3.7165
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1327 69.1757 19.8702
REMARK 3 T TENSOR
REMARK 3 T11: 0.4459 T22: 0.4252
REMARK 3 T33: 0.4342 T12: 0.0416
REMARK 3 T13: -0.0077 T23: -0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 2.2816 L22: 3.3022
REMARK 3 L33: 2.0459 L12: -0.7891
REMARK 3 L13: -0.9216 L23: 0.4115
REMARK 3 S TENSOR
REMARK 3 S11: 0.1456 S12: 0.2933 S13: 0.4216
REMARK 3 S21: -0.3226 S22: -0.2250 S23: -0.0468
REMARK 3 S31: -0.5546 S32: -0.3209 S33: 0.1016
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 89:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0897 55.5064 14.7538
REMARK 3 T TENSOR
REMARK 3 T11: 0.3399 T22: 0.5437
REMARK 3 T33: 0.3776 T12: -0.0194
REMARK 3 T13: 0.0117 T23: -0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 1.1658 L22: 1.7399
REMARK 3 L33: 1.2751 L12: -0.3153
REMARK 3 L13: -0.4254 L23: -0.0545
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: 0.4218 S13: 0.1375
REMARK 3 S21: -0.1153 S22: 0.0113 S23: -0.0088
REMARK 3 S31: -0.1728 S32: 0.0996 S33: -0.0268
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 128:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3598 52.2340 26.2742
REMARK 3 T TENSOR
REMARK 3 T11: 0.2111 T22: 0.3428
REMARK 3 T33: 0.3838 T12: 0.0309
REMARK 3 T13: 0.0057 T23: -0.1291
REMARK 3 L TENSOR
REMARK 3 L11: 1.3656 L22: 2.1342
REMARK 3 L33: 1.9658 L12: 0.6685
REMARK 3 L13: -0.1529 L23: 0.5355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: -0.2781 S13: 0.0929
REMARK 3 S21: -0.0224 S22: -0.0520 S23: 0.0100
REMARK 3 S31: -0.1657 S32: 0.1127 S33: 0.0256
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 198:223)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3781 49.8769 28.3959
REMARK 3 T TENSOR
REMARK 3 T11: 0.3375 T22: 0.6852
REMARK 3 T33: 0.5931 T12: -0.0783
REMARK 3 T13: 0.1384 T23: -0.2976
REMARK 3 L TENSOR
REMARK 3 L11: 1.9542 L22: 1.0832
REMARK 3 L33: 1.4748 L12: -0.6444
REMARK 3 L13: -0.3036 L23: -0.4243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0657 S12: -0.1511 S13: -0.2997
REMARK 3 S21: 0.0723 S22: -0.2777 S23: 0.4913
REMARK 3 S31: 0.5850 S32: -0.6597 S33: 0.1743
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 224:295)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1529 60.5418 36.5016
REMARK 3 T TENSOR
REMARK 3 T11: 0.3585 T22: 0.4687
REMARK 3 T33: 0.5007 T12: 0.0128
REMARK 3 T13: 0.0170 T23: -0.1818
REMARK 3 L TENSOR
REMARK 3 L11: 0.8078 L22: 0.8049
REMARK 3 L33: 1.1837 L12: -0.3041
REMARK 3 L13: -0.2626 L23: 0.3354
REMARK 3 S TENSOR
REMARK 3 S11: 0.1536 S12: -0.0336 S13: 0.0913
REMARK 3 S21: 0.0367 S22: -0.1256 S23: 0.2217
REMARK 3 S31: -0.1278 S32: -0.1454 S33: -0.0483
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 296:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5688 59.6816 45.0300
REMARK 3 T TENSOR
REMARK 3 T11: 0.4498 T22: 0.6910
REMARK 3 T33: 0.5733 T12: 0.0166
REMARK 3 T13: 0.0738 T23: -0.1924
REMARK 3 L TENSOR
REMARK 3 L11: 1.4292 L22: 1.8661
REMARK 3 L33: 2.0163 L12: -0.2764
REMARK 3 L13: 0.3148 L23: 0.6632
REMARK 3 S TENSOR
REMARK 3 S11: -0.2045 S12: -0.2683 S13: 0.0971
REMARK 3 S21: 0.2955 S22: 0.0259 S23: 0.4678
REMARK 3 S31: -0.0132 S32: -0.7327 S33: 0.1608
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 374:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2512 41.0902 34.1799
REMARK 3 T TENSOR
REMARK 3 T11: 0.3890 T22: 0.4138
REMARK 3 T33: 0.4208 T12: 0.0019
REMARK 3 T13: 0.0502 T23: -0.0930
REMARK 3 L TENSOR
REMARK 3 L11: 0.9156 L22: 1.5175
REMARK 3 L33: 1.3540 L12: -0.9892
REMARK 3 L13: -0.1130 L23: 0.9930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0296 S12: -0.3313 S13: -0.0084
REMARK 3 S21: 0.0868 S22: -0.0390 S23: 0.3792
REMARK 3 S31: 0.1519 S32: -0.0697 S33: 0.0239
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 402:438)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7268 37.1558 31.1382
REMARK 3 T TENSOR
REMARK 3 T11: 0.3805 T22: 0.3295
REMARK 3 T33: 0.3862 T12: -0.0050
REMARK 3 T13: -0.0586 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.3553 L22: 2.1834
REMARK 3 L33: 5.7091 L12: -0.0565
REMARK 3 L13: -0.3250 L23: 2.3552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0871 S12: -0.1718 S13: -0.3400
REMARK 3 S21: 0.5727 S22: 0.0538 S23: 0.0513
REMARK 3 S31: 0.6578 S32: 0.7328 S33: 0.0094
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4579 32.4287 -12.0454
REMARK 3 T TENSOR
REMARK 3 T11: 0.2616 T22: 0.4113
REMARK 3 T33: 0.3308 T12: -0.0682
REMARK 3 T13: 0.0302 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 1.1325 L22: 2.4736
REMARK 3 L33: 1.3405 L12: -0.7938
REMARK 3 L13: 0.0586 L23: 0.1961
REMARK 3 S TENSOR
REMARK 3 S11: -0.0827 S12: 0.2000 S13: 0.0806
REMARK 3 S21: -0.1717 S22: 0.1158 S23: -0.0573
REMARK 3 S31: -0.1007 S32: 0.1697 S33: -0.0185
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 198:440)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0717 25.2131 2.9582
REMARK 3 T TENSOR
REMARK 3 T11: 0.2410 T22: 0.3140
REMARK 3 T33: 0.3374 T12: -0.0805
REMARK 3 T13: 0.0295 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 1.0740 L22: 1.4662
REMARK 3 L33: 2.1605 L12: -0.3993
REMARK 3 L13: -0.1719 L23: 0.9469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: -0.0796 S13: 0.0352
REMARK 3 S21: 0.0606 S22: -0.0223 S23: 0.1573
REMARK 3 S31: 0.0806 S32: -0.2418 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6274 9.0856 -44.4882
REMARK 3 T TENSOR
REMARK 3 T11: 0.6796 T22: 0.8287
REMARK 3 T33: 0.4283 T12: -0.0818
REMARK 3 T13: 0.0366 T23: -0.0851
REMARK 3 L TENSOR
REMARK 3 L11: 2.6653 L22: 2.2412
REMARK 3 L33: 1.5837 L12: -0.3920
REMARK 3 L13: 0.3215 L23: 0.2184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0747 S12: 0.7021 S13: 0.0164
REMARK 3 S21: -0.4577 S22: 0.1850 S23: -0.0481
REMARK 3 S31: 0.1701 S32: -0.1000 S33: -0.0810
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 89:295)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3248 -2.7534 -33.8823
REMARK 3 T TENSOR
REMARK 3 T11: 0.5802 T22: 0.5852
REMARK 3 T33: 0.4380 T12: -0.0563
REMARK 3 T13: 0.0866 T23: -0.1961
REMARK 3 L TENSOR
REMARK 3 L11: 1.3788 L22: 1.0253
REMARK 3 L33: 1.4846 L12: -0.0203
REMARK 3 L13: -0.1635 L23: 0.0712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0562 S12: 0.4720 S13: -0.2365
REMARK 3 S21: -0.3443 S22: 0.0486 S23: -0.1913
REMARK 3 S31: 0.3363 S32: -0.0062 S33: -0.0171
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 296:401)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2463 -4.4449 -21.5557
REMARK 3 T TENSOR
REMARK 3 T11: 0.6406 T22: 0.5529
REMARK 3 T33: 0.4830 T12: -0.1229
REMARK 3 T13: 0.0577 T23: -0.1572
REMARK 3 L TENSOR
REMARK 3 L11: 1.2672 L22: 1.1093
REMARK 3 L33: 1.8349 L12: -0.1179
REMARK 3 L13: -0.3201 L23: 0.6676
REMARK 3 S TENSOR
REMARK 3 S11: -0.1966 S12: 0.4297 S13: -0.4006
REMARK 3 S21: -0.0858 S22: 0.1133 S23: 0.0844
REMARK 3 S31: 0.4007 S32: -0.2055 S33: 0.0909
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 402:441)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7468 -17.1573 -25.1075
REMARK 3 T TENSOR
REMARK 3 T11: 0.8714 T22: 0.5552
REMARK 3 T33: 0.7070 T12: 0.0569
REMARK 3 T13: 0.0815 T23: -0.2079
REMARK 3 L TENSOR
REMARK 3 L11: 1.8516 L22: 1.2805
REMARK 3 L33: 1.5997 L12: -0.0323
REMARK 3 L13: -0.6143 L23: -0.2736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: 0.2010 S13: -0.5861
REMARK 3 S21: -0.1039 S22: -0.0444 S23: 0.0697
REMARK 3 S31: 0.3728 S32: 0.3448 S33: -0.0128
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 6:27)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1653 94.2908 84.7085
REMARK 3 T TENSOR
REMARK 3 T11: 1.1509 T22: 0.7702
REMARK 3 T33: 0.5506 T12: -0.0320
REMARK 3 T13: -0.0075 T23: -0.2109
REMARK 3 L TENSOR
REMARK 3 L11: 2.2389 L22: 6.8043
REMARK 3 L33: 1.9051 L12: -0.6168
REMARK 3 L13: 0.3423 L23: -2.4764
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: -0.5816 S13: 0.2480
REMARK 3 S21: 0.9639 S22: -0.1824 S23: -0.2758
REMARK 3 S31: 0.0294 S32: 0.8161 S33: 0.0384
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 43:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2072 28.0531 5.2453
REMARK 3 T TENSOR
REMARK 3 T11: 0.4111 T22: 0.7289
REMARK 3 T33: 0.6698 T12: 0.0727
REMARK 3 T13: 0.0326 T23: -0.2339
REMARK 3 L TENSOR
REMARK 3 L11: 0.3502 L22: 1.4537
REMARK 3 L33: 1.4119 L12: 0.1872
REMARK 3 L13: -0.0066 L23: 1.1491
REMARK 3 S TENSOR
REMARK 3 S11: -0.1473 S12: -0.0052 S13: -0.0531
REMARK 3 S21: 0.1839 S22: 0.5774 S23: -0.4016
REMARK 3 S31: 0.4021 S32: 0.8474 S33: -0.2919
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 1:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9967 53.3653 70.2710
REMARK 3 T TENSOR
REMARK 3 T11: 0.7755 T22: 0.5429
REMARK 3 T33: 0.6062 T12: -0.0370
REMARK 3 T13: 0.0758 T23: -0.1307
REMARK 3 L TENSOR
REMARK 3 L11: 2.0776 L22: 2.3338
REMARK 3 L33: 2.0785 L12: 0.7403
REMARK 3 L13: -1.5771 L23: 0.1114
REMARK 3 S TENSOR
REMARK 3 S11: -0.1169 S12: 0.3118 S13: -0.5445
REMARK 3 S21: 0.0425 S22: 0.1412 S23: -0.0970
REMARK 3 S31: 0.8257 S32: -0.0616 S33: -0.0336
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 67:97)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9472 64.3928 97.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.7013 T22: 1.0006
REMARK 3 T33: 0.4338 T12: -0.0444
REMARK 3 T13: -0.0305 T23: 0.1158
REMARK 3 L TENSOR
REMARK 3 L11: 2.0983 L22: 2.2454
REMARK 3 L33: 2.7626 L12: 0.7275
REMARK 3 L13: 0.4315 L23: -2.1835
REMARK 3 S TENSOR
REMARK 3 S11: 0.1286 S12: -0.4266 S13: 0.0256
REMARK 3 S21: 0.8318 S22: -0.0890 S23: -0.0010
REMARK 3 S31: -0.0026 S32: 0.7180 S33: -0.3619
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 185:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7673 50.7311 98.2380
REMARK 3 T TENSOR
REMARK 3 T11: 0.9360 T22: 0.5111
REMARK 3 T33: 0.8051 T12: 0.1036
REMARK 3 T13: 0.1153 T23: 0.1866
REMARK 3 L TENSOR
REMARK 3 L11: 0.9690 L22: 1.2408
REMARK 3 L33: 1.6280 L12: 0.2790
REMARK 3 L13: -0.4505 L23: -0.1792
REMARK 3 S TENSOR
REMARK 3 S11: -0.4603 S12: -0.2699 S13: -0.6999
REMARK 3 S21: -0.0928 S22: 0.0843 S23: -0.5546
REMARK 3 S31: 1.1828 S32: -0.2020 S33: 0.2015
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 259:362)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1228 55.8455 91.8113
REMARK 3 T TENSOR
REMARK 3 T11: 0.7827 T22: 0.4728
REMARK 3 T33: 0.6283 T12: 0.0386
REMARK 3 T13: 0.1164 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 2.0604 L22: 0.6818
REMARK 3 L33: 2.0501 L12: -0.1320
REMARK 3 L13: -1.4034 L23: 0.6358
REMARK 3 S TENSOR
REMARK 3 S11: -0.2075 S12: -0.0537 S13: -0.5605
REMARK 3 S21: 0.2878 S22: 0.2290 S23: -0.0126
REMARK 3 S31: 0.2594 S32: -0.1612 S33: -0.0188
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 371:384)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4686 66.7846 89.8743
REMARK 3 T TENSOR
REMARK 3 T11: 1.2099 T22: 0.8717
REMARK 3 T33: 0.6931 T12: -0.0646
REMARK 3 T13: -0.0903 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.1091 L22: 3.4208
REMARK 3 L33: 2.7913 L12: -0.7836
REMARK 3 L13: -0.8598 L23: 0.3338
REMARK 3 S TENSOR
REMARK 3 S11: -0.1905 S12: -0.3211 S13: 0.0986
REMARK 3 S21: 0.2151 S22: -0.5244 S23: 0.7876
REMARK 3 S31: -1.8359 S32: -0.7390 S33: 0.6984
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 4IIJ 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_1000076795.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-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 : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999870
REMARK 200 MONOCHROMATOR : VERTICALLY COLLIMATING MIRROR
REMARK 200 (M1, FOCUS AT INFINITY),
REMARK 200 FOLLOWED BY A BARTELS
REMARK 200 MONOCHROMATOR WITH DUAL CHANNEL
REMARK 200 CUT CRYSTALS (DCCM) IN (+--+)
REMARK 200 GEOMETRY, AND A TOROIDAL MIRROR
REMARK 200 (M2) TO VERTICALLY AND
REMARK 200 HORIZONTALLY FOCUS THE BEAM AT
REMARK 200 THE SAMPLE POSITION (WITH 2:1
REMARK 200 HORIZONTAL DEMAGNIFICATION)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90604
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 62.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 26.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.5000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 25.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: PHENIX 1.7.3_928
REMARK 200 STARTING MODEL: PDB ENTRY 4I4T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4-10% 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 51.76500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.51000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.95500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.51000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.76500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.95500
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 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 GLN B 282
REMARK 465 TYR B 283
REMARK 465 ARG B 284
REMARK 465 ALA B 285
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 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 SER E 28
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 SER E 144
REMARK 465 ARG E 145
REMARK 465 TYR F 98
REMARK 465 VAL F 99
REMARK 465 ILE F 100
REMARK 465 TYR F 101
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 THR F 125
REMARK 465 ASP F 126
REMARK 465 GLU F 127
REMARK 465 ARG F 128
REMARK 465 GLU F 129
REMARK 465 VAL F 130
REMARK 465 PHE F 131
REMARK 465 LEU F 132
REMARK 465 ALA F 133
REMARK 465 ALA F 134
REMARK 465 TYR F 135
REMARK 465 ASN F 136
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 GLY F 144
REMARK 465 ASN F 145
REMARK 465 VAL F 146
REMARK 465 TRP F 147
REMARK 465 ILE F 148
REMARK 465 ALA F 149
REMARK 465 LYS F 150
REMARK 465 SER F 151
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 162
REMARK 465 SER F 163
REMARK 465 SER F 164
REMARK 465 GLU F 165
REMARK 465 ALA F 166
REMARK 465 SER F 167
REMARK 465 GLU F 168
REMARK 465 LEU F 169
REMARK 465 LEU F 170
REMARK 465 ASP F 171
REMARK 465 PHE F 172
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 HIS F 180
REMARK 465 VAL F 181
REMARK 465 ILE F 182
REMARK 465 GLN F 183
REMARK 465 LYS F 184
REMARK 465 TYR F 228
REMARK 465 ASN F 229
REMARK 465 SER F 230
REMARK 465 ALA F 231
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 GLU F 257
REMARK 465 GLU F 258
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 OD1 ASN C 228 HN1 GTP C 501 1.58
REMARK 500 NE2 GLN C 285 OE1 GLN C 372 2.12
REMARK 500 OD1 ASP A 69 O HOH A 611 2.13
REMARK 500 O THR D 409 NZ LYS E 140 2.14
REMARK 500 OH TYR B 108 OE2 GLU B 417 2.14
REMARK 500 OE1 GLU C 71 OG1 THR C 73 2.14
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 55.07 -105.92
REMARK 500 ALA A 314 149.12 175.12
REMARK 500 ASP A 322 90.17 -68.39
REMARK 500 PHE A 404 -9.16 72.98
REMARK 500 ARG B 2 -69.29 -146.37
REMARK 500 HIS B 37 50.41 -141.52
REMARK 500 ASP B 69 149.24 -171.41
REMARK 500 THR B 109 -86.32 -117.24
REMARK 500 SER B 128 40.48 -97.77
REMARK 500 CYS B 131 88.28 -166.77
REMARK 500 THR B 216 -61.16 -95.11
REMARK 500 LYS B 299 0.07 -67.14
REMARK 500 ASN B 339 29.36 -147.24
REMARK 500 SER B 340 -3.07 -57.24
REMARK 500 PRO B 360 -177.31 -62.93
REMARK 500 TYR C 83 30.12 -99.77
REMARK 500 TYR C 108 -88.47 -116.24
REMARK 500 ALA C 314 148.87 -176.31
REMARK 500 PHE C 404 -10.49 72.09
REMARK 500 GLN D 11 -72.44 -55.02
REMARK 500 THR D 57 134.34 -34.05
REMARK 500 PHE D 83 45.63 -94.71
REMARK 500 GLN D 96 -42.15 -145.30
REMARK 500 THR D 109 -76.34 -105.12
REMARK 500 CYS D 131 112.27 -166.67
REMARK 500 SER D 147 -74.60 -67.91
REMARK 500 TYR D 161 59.12 -150.29
REMARK 500 PHE E 20 -174.76 -178.08
REMARK 500 LYS F 74 -58.50 -29.50
REMARK 500 SER F 88 162.46 82.09
REMARK 500 CYS F 91 103.89 125.57
REMARK 500 ASP F 273 -62.36 -97.42
REMARK 500 ILE F 283 -50.31 -137.40
REMARK 500 THR F 304 41.71 -109.38
REMARK 500 ILE F 330 -72.98 -88.75
REMARK 500 THR F 372 73.68 66.79
REMARK 500 HIS F 380 115.06 -161.05
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 44.2
REMARK 620 3 THR A 41 OG1 66.5 101.8
REMARK 620 4 GLY A 44 O 110.5 105.3 65.1
REMARK 620 5 GLU A 55 OE2 126.6 82.5 146.0 81.2
REMARK 620 6 GLU A 55 OE1 101.8 67.1 105.5 51.2 44.8
REMARK 620 N 1 2 3 4 5
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 69.7
REMARK 620 3 HOH A 601 O 64.2 68.9
REMARK 620 4 HOH A 610 O 82.8 94.1 146.2
REMARK 620 5 HOH A 611 O 146.8 94.6 83.0 128.7
REMARK 620 6 HOH A 612 O 70.4 135.9 77.2 99.0 108.8
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 O1A 81.9
REMARK 620 N 1
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 47.3
REMARK 620 3 THR C 41 O 77.7 75.9
REMARK 620 4 THR C 41 OG1 115.9 71.6 69.6
REMARK 620 5 GLY C 44 O 151.9 144.2 82.3 74.3
REMARK 620 6 GLU C 55 OE2 86.2 124.5 129.0 155.5 91.3
REMARK 620 7 GLU C 55 OE1 61.2 107.9 82.0 151.0 96.7 48.4
REMARK 620 N 1 2 3 4 5 6
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 63.9
REMARK 620 3 HOH C 602 O 59.8 66.6
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 GDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 401
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: 4I55 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH AMPPCP
REMARK 900 RELATED ID: 4IHJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ADP
DBREF 4IIJ A 1 451 UNP P81947 TBA1B_BOVIN 1 451
DBREF 4IIJ B 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4IIJ C 1 451 UNP P81947 TBA1B_BOVIN 1 451
DBREF 4IIJ D 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4IIJ E 3 145 UNP P63043 STMN4_RAT 47 189
DBREF 4IIJ F 1 378 UNP E1BQ43 E1BQ43_CHICK 1 378
SEQADV 4IIJ MET E 3 UNP P63043 ILE 47 CLONING ARTIFACT
SEQADV 4IIJ ALA E 4 UNP P63043 SER 48 CLONING ARTIFACT
SEQADV 4IIJ HIS F 379 UNP E1BQ43 EXPRESSION TAG
SEQADV 4IIJ HIS F 380 UNP E1BQ43 EXPRESSION TAG
SEQADV 4IIJ HIS F 381 UNP E1BQ43 EXPRESSION TAG
SEQADV 4IIJ HIS F 382 UNP E1BQ43 EXPRESSION TAG
SEQADV 4IIJ HIS F 383 UNP E1BQ43 EXPRESSION TAG
SEQADV 4IIJ 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 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 GDP B 501 38
HET MG B 502 1
HET CA B 503 1
HET MES B 504 25
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 401 1
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
FORMUL 7 GTP 2(C10 H16 N5 O14 P3)
FORMUL 8 MG 5(MG 2+)
FORMUL 9 CA 3(CA 2+)
FORMUL 10 CL CL 1-
FORMUL 11 GDP 2(C10 H15 N5 O11 P2)
FORMUL 14 MES C6 H13 N O4 S
FORMUL 21 HOH *92(H2 O)
HELIX 1 1 GLY A 10 HIS A 28 1 19
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 TYR A 108 ASP A 127 1 20
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 ARG A 339 1 16
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 414 VAL A 437 1 24
HELIX 20 20 GLY B 10 HIS B 28 1 19
HELIX 21 21 ASP B 41 ARG B 48 1 6
HELIX 22 22 ILE B 49 VAL B 51 5 3
HELIX 23 23 PRO B 72 GLY B 81 1 10
HELIX 24 24 PHE B 83 PHE B 87 5 5
HELIX 25 25 ARG B 88 ASP B 90 5 3
HELIX 26 26 ASN B 102 TYR B 108 1 7
HELIX 27 27 THR B 109 SER B 128 1 20
HELIX 28 28 GLY B 144 TYR B 161 1 18
HELIX 29 29 SER B 174 SER B 178 5 5
HELIX 30 30 VAL B 182 THR B 198 1 17
HELIX 31 31 ASN B 206 THR B 216 1 11
HELIX 32 32 THR B 223 THR B 239 1 17
HELIX 33 33 THR B 239 PHE B 244 1 6
HELIX 34 34 ASP B 251 VAL B 260 1 10
HELIX 35 35 THR B 287 MET B 295 1 9
HELIX 36 36 ASP B 297 MET B 301 5 5
HELIX 37 37 ASP B 306 GLY B 310 5 5
HELIX 38 38 SER B 324 LYS B 338 1 15
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 TYR B 435 1 22
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 GLY C 81 1 10
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 ASP C 127 1 14
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 435 1 22
HELIX 63 63 GLY D 10 HIS D 28 1 19
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 GLU D 71 ARG D 79 1 9
HELIX 67 67 SER D 80 GLN D 85 5 6
HELIX 68 68 ARG D 88 ASP D 90 5 3
HELIX 69 69 ASN D 102 TYR D 108 1 7
HELIX 70 70 THR D 109 GLU D 127 1 19
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 PHE D 404 GLY D 410 1 7
HELIX 83 83 ASP D 414 ALA D 438 1 25
HELIX 84 84 SER E 46 GLU E 142 1 97
HELIX 85 85 SER F 11 ALA F 23 1 13
HELIX 86 86 PRO F 48 LEU F 52 5 5
HELIX 87 87 ALA F 68 ARG F 73 1 6
HELIX 88 88 ARG F 73 SER F 84 1 12
HELIX 89 89 PHE F 264 LEU F 275 1 12
HELIX 90 90 THR F 278 ILE F 283 1 6
HELIX 91 91 ILE F 283 SER F 303 1 21
HELIX 92 92 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 PHE A 202 N GLU A 168
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 MET A 377 N THR A 271
SHEET 3 C 6 TYR A 312 GLY A 321 -1 N CYS A 316 O LEU A 378
SHEET 4 C 6 GLY A 350 ASN A 356 1 O GLY A 354 N TYR A 319
SHEET 5 C 6 GLY E 17 ILE E 23 -1 O GLN E 18 N ILE A 355
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 GLU B 3 ALA B 9 1 N GLN B 8 O VAL B 68
SHEET 4 D10 LEU B 132 SER B 140 1 O GLN B 136 N ILE B 7
SHEET 5 D10 ILE B 165 MET B 172 1 O PHE B 169 N LEU B 137
SHEET 6 D10 GLU B 200 ASP B 205 1 O TYR B 202 N THR B 168
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 PHE B 377 N GLY B 271
SHEET 9 D10 TYR B 312 GLY B 321 -1 N ARG B 320 O SER B 374
SHEET 10 D10 VAL B 351 CYS B 356 1 O CYS B 356 N PHE B 319
SHEET 1 E 2 TYR B 53 ALA B 56 0
SHEET 2 E 2 LYS B 60 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 LEU C 136 N ILE C 7
SHEET 5 F 6 SER C 165 TYR C 172 1 O LEU C 167 N PHE C 135
SHEET 6 F 6 CYS C 200 ASP C 205 1 O VAL C 204 N SER C 170
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 LEU C 318 O CYS C 376
SHEET 4 H 4 LYS C 352 ASN C 356 1 O GLY C 354 N TYR C 319
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 GLU D 3 ALA D 9 1 N GLN D 8 O VAL D 68
SHEET 4 I10 LEU D 132 SER D 140 1 O GLN D 133 N GLU D 3
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 ILE D 204 N MET D 172
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 ALA D 375 N ALA D 273
SHEET 9 I10 TYR D 312 GLY D 321 -1 N ALA D 316 O ILE D 378
SHEET 10 I10 VAL D 351 CYS D 356 1 O CYS D 356 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 VAL D 62 N ASN D 54
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 5 GLU F 261 PHE F 263 0
SHEET 2 L 5 VAL F 220 THR F 223 -1 N LEU F 221 O MET F 262
SHEET 3 L 5 PHE F 199 VAL F 207 -1 N ARG F 202 O VAL F 220
SHEET 4 L 5 GLN F 313 VAL F 321 -1 O PHE F 315 N VAL F 205
SHEET 5 L 5 VAL F 327 ASN F 333 -1 O ILE F 330 N ASP F 318
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 ILE F 213 TYR F 216 -1 O TYR F 214 N LEU F 206
SHEET 5 M 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 2.82
LINK OD2 ASP A 39 CA CA A 503 1555 1555 2.99
LINK OG1 THR A 41 CA CA A 503 1555 1555 2.70
LINK O GLY A 44 CA CA A 503 1555 1555 2.91
LINK OE2 GLU A 55 CA CA A 503 1555 1555 2.86
LINK OE1 GLU A 55 CA CA A 503 1555 1555 2.90
LINK O1G GTP A 501 MG MG A 502 1555 1555 2.48
LINK O1B GTP A 501 MG MG A 502 1555 1555 2.58
LINK MG MG A 502 O HOH A 601 1555 1555 2.48
LINK MG MG A 502 O HOH A 610 1555 1555 2.50
LINK MG MG A 502 O HOH A 611 1555 1555 2.44
LINK MG MG A 502 O HOH A 612 1555 1555 2.43
LINK OE1 GLN B 11 MG MG B 502 1555 1555 2.61
LINK OE1 GLU B 113 CA CA B 503 1555 1555 2.79
LINK O1A GDP B 501 MG MG B 502 1555 1555 2.44
LINK OD2 ASP C 39 CA CA C 503 1555 1555 2.59
LINK OD1 ASP C 39 CA CA C 503 1555 1555 2.85
LINK O THR C 41 CA CA C 503 1555 1555 2.62
LINK OG1 THR C 41 CA CA C 503 1555 1555 2.67
LINK O GLY C 44 CA CA C 503 1555 1555 2.94
LINK OE2 GLU C 55 CA CA C 503 1555 1555 2.65
LINK OE1 GLU C 55 CA CA C 503 1555 1555 2.71
LINK O1G GTP C 501 MG MG C 502 1555 1555 2.58
LINK O1B GTP C 501 MG MG C 502 1555 1555 2.68
LINK MG MG C 502 O HOH C 602 1555 1555 2.51
LINK O1A GDP D 600 MG MG D 601 1555 1555 2.81
CISPEP 1 ALA A 273 PRO A 274 0 1.46
CISPEP 2 ALA B 273 PRO B 274 0 2.75
CISPEP 3 ALA C 273 PRO C 274 0 -3.69
CISPEP 4 ALA D 273 PRO D 274 0 -1.65
CISPEP 5 GLU F 193 PRO F 194 0 3.54
CISPEP 6 GLY F 259 ASN F 260 0 -0.73
CISPEP 7 PRO F 371 THR F 372 0 0.55
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 ILE A 171 VAL A 177 THR A 179
SITE 5 AC1 28 GLU A 183 ASN A 206 TYR A 224 ASN A 228
SITE 6 AC1 28 ILE A 231 MG A 502 HOH A 601 HOH A 610
SITE 7 AC1 28 HOH A 612 HOH A 613 HOH A 627 LYS B 254
SITE 1 AC2 6 GLU A 71 GTP A 501 HOH A 601 HOH A 610
SITE 2 AC2 6 HOH A 611 HOH A 612
SITE 1 AC3 4 ASP A 39 THR A 41 GLY A 44 GLU A 55
SITE 1 AC4 4 TYR A 161 GLY A 162 LYS A 163 LYS A 164
SITE 1 AC5 18 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC5 18 SER B 140 GLY B 143 GLY B 144 THR B 145
SITE 3 AC5 18 GLY B 146 VAL B 177 GLU B 183 ASN B 206
SITE 4 AC5 18 TYR B 224 ASN B 228 MG B 502 HOH B 601
SITE 5 AC5 18 HOH B 602 HOH B 605
SITE 1 AC6 3 GLN B 11 ASP B 179 GDP B 501
SITE 1 AC7 2 GLU B 113 GLU C 284
SITE 1 AC8 7 ARG B 158 PRO B 162 ASP B 163 ARG B 164
SITE 2 AC8 7 ASN B 197 ASP B 199 ARG B 253
SITE 1 AC9 23 GLY C 10 GLN C 11 ALA C 12 GLN C 15
SITE 2 AC9 23 ASP C 98 ALA C 99 ASN C 101 SER C 140
SITE 3 AC9 23 GLY C 143 GLY C 144 THR C 145 GLY C 146
SITE 4 AC9 23 ILE C 171 VAL C 177 GLU C 183 ASN C 206
SITE 5 AC9 23 TYR C 224 ASN C 228 ILE C 231 MG C 502
SITE 6 AC9 23 HOH C 602 HOH C 605 LYS D 254
SITE 1 BC1 3 GLU C 71 GTP C 501 HOH C 602
SITE 1 BC2 4 ASP C 39 THR C 41 GLY C 44 GLU C 55
SITE 1 BC3 18 GLY D 10 GLN D 11 CYS D 12 GLN D 15
SITE 2 BC3 18 SER D 140 GLY D 143 GLY D 144 THR D 145
SITE 3 BC3 18 GLY D 146 VAL D 177 GLU D 183 ASN D 206
SITE 4 BC3 18 TYR D 224 ASN D 228 MG D 601 HOH D 702
SITE 5 BC3 18 HOH D 705 HOH D 706
SITE 1 BC4 3 GLN D 11 ASN D 101 GDP D 600
SITE 1 BC5 1 GLU F 331
CRYST1 103.530 155.910 181.020 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 0.009659 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
