HEADER CELL CYCLE 05-NOV-18 6MZG
TITLE STRUCTURAL BASIS OF TUBULIN RECRUITMENT AND ASSEMBLY BY MICROTUBULE
TITLE 2 POLYMERASES WITH TUMOR OVEREXPRESSED GENE (TOG) DOMAIN ARRAYS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA-1A CHAIN;
COMPND 3 CHAIN: A, C, G, I;
COMPND 4 SYNONYM: ALPHA-TUBULIN 1,TUBULIN ALPHA-1 CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TUBULIN BETA CHAIN;
COMPND 7 CHAIN: B, D, H, J;
COMPND 8 SYNONYM: BETA-TUBULIN;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PROTEIN STU2P/ALP14P;
COMPND 11 CHAIN: E, K;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: PROTEIN WAS OBTAINED FROM CDNA (LACHANCEA KLUYVERI
COMPND 14 NRRL Y-12651 CHROMOSOME);
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: TRUNCATED DARPIN-D1;
COMPND 17 CHAIN: F, L;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES;
COMPND 20 OTHER_DETAILS: N-TERMINAL RESIDUES (1-40) OF DARPIN-D1 WERE
COMPND 21 TRUNCATED.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 8 ORGANISM_COMMON: PIG;
SOURCE 9 ORGANISM_TAXID: 9823;
SOURCE 10 ORGAN: BRAIN;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: LACHANCEA KLUYVERI NRRL Y-12651;
SOURCE 13 ORGANISM_TAXID: 226302;
SOURCE 14 GENE: SKLU-CONT10078;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PLIC;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 22 ORGANISM_TAXID: 562;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PLIC
KEYWDS MICROTUBULE, TUBULIN, TUBULIN POLYMERIZATION, HEAT REPEATS,
KEYWDS 2 MICROTUBULE POLYMERASE, PROTOFILAMENT, TOG ARRAYS, AND UNFURLED
KEYWDS 3 ASSEMBLY., CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NITHIANANTHAM,J.AL-BASSAM
REVDAT 3 13-MAR-24 6MZG 1 LINK
REVDAT 2 01-JAN-20 6MZG 1 REMARK
REVDAT 1 28-NOV-18 6MZG 0
JRNL AUTH S.NITHIANANTHAM,B.D.COOK,M.BEANS,F.GUO,F.CHANG,J.AL-BASSAM
JRNL TITL STRUCTURAL BASIS OF TUBULIN RECRUITMENT AND ASSEMBLY BY
JRNL TITL 2 MICROTUBULE POLYMERASES WITH TUMOR OVEREXPRESSED GENE (TOG)
JRNL TITL 3 DOMAIN ARRAYS.
JRNL REF ELIFE V. 7 2018
JRNL REFN ESSN 2050-084X
JRNL PMID 30422110
JRNL DOI 10.7554/ELIFE.38922
REMARK 2
REMARK 2 RESOLUTION. 3.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.210
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.9
REMARK 3 NUMBER OF REFLECTIONS : 88337
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 4535
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 49.8624 - 8.7201 0.90 4894 262 0.1785 0.1819
REMARK 3 2 8.7201 - 6.9273 0.90 4840 220 0.1801 0.2023
REMARK 3 3 6.9273 - 6.0534 0.94 5012 253 0.2017 0.2593
REMARK 3 4 6.0534 - 5.5007 0.86 4607 224 0.2014 0.2634
REMARK 3 5 5.5007 - 5.1069 0.91 4894 284 0.1760 0.2384
REMARK 3 6 5.1069 - 4.8060 0.93 4970 257 0.1607 0.2117
REMARK 3 7 4.8060 - 4.5655 0.94 5017 270 0.1535 0.1801
REMARK 3 8 4.5655 - 4.3669 0.88 4689 249 0.1570 0.2107
REMARK 3 9 4.3669 - 4.1989 0.88 4725 228 0.1624 0.2306
REMARK 3 10 4.1989 - 4.0540 0.92 4875 236 0.1668 0.2354
REMARK 3 11 4.0540 - 3.9273 0.92 4938 294 0.1706 0.2305
REMARK 3 12 3.9273 - 3.8151 0.94 4991 256 0.1740 0.2747
REMARK 3 13 3.8151 - 3.7147 0.94 4949 268 0.1805 0.2389
REMARK 3 14 3.7147 - 3.6241 0.94 5017 256 0.1878 0.2701
REMARK 3 15 3.6241 - 3.5417 0.87 4652 230 0.1898 0.2733
REMARK 3 16 3.5417 - 3.4664 0.88 4662 257 0.2018 0.3212
REMARK 3 17 3.4664 - 3.3971 0.57 3007 158 0.2063 0.3034
REMARK 3 18 3.3971 - 3.3330 0.33 1760 91 0.2074 0.3437
REMARK 3 19 3.3330 - 3.2735 0.19 1014 51 0.2131 0.2352
REMARK 3 20 3.2735 - 3.2180 0.08 421 26 0.2412 0.3176
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 76.20
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.4900
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 NULL
REMARK 3 ANGLE : 0.501 NULL
REMARK 3 CHIRALITY : 0.039 NULL
REMARK 3 PLANARITY : 0.004 NULL
REMARK 3 DIHEDRAL : 5.783 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 64
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5610 35.1653 -9.7158
REMARK 3 T TENSOR
REMARK 3 T11: 0.3632 T22: 0.4075
REMARK 3 T33: 0.1345 T12: -0.1265
REMARK 3 T13: 0.0790 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 1.4486 L22: 0.7869
REMARK 3 L33: 1.8871 L12: -0.2451
REMARK 3 L13: 0.2141 L23: 0.1523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: 0.1730 S13: 0.3714
REMARK 3 S21: -0.3559 S22: -0.0895 S23: -0.2194
REMARK 3 S31: -0.7419 S32: 0.3465 S33: -0.0798
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2129 20.9893 0.5403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2296 T22: 0.3909
REMARK 3 T33: 0.1115 T12: 0.0904
REMARK 3 T13: 0.0144 T23: -0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 0.7404 L22: 0.9153
REMARK 3 L33: 1.7958 L12: -0.0219
REMARK 3 L13: -0.7602 L23: -0.1969
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: -0.1027 S13: -0.0021
REMARK 3 S21: 0.0916 S22: 0.0018 S23: -0.1462
REMARK 3 S31: -0.1331 S32: 0.4576 S33: -0.0902
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3916 31.1736 -1.0320
REMARK 3 T TENSOR
REMARK 3 T11: 0.4788 T22: 0.3216
REMARK 3 T33: 0.2198 T12: 0.2253
REMARK 3 T13: 0.0281 T23: -0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 0.8838 L22: 0.5111
REMARK 3 L33: 0.5835 L12: -0.3995
REMARK 3 L13: -0.4970 L23: 0.1300
REMARK 3 S TENSOR
REMARK 3 S11: 0.1004 S12: 0.2036 S13: -0.0234
REMARK 3 S21: -0.2706 S22: -0.1136 S23: 0.0807
REMARK 3 S31: -0.1222 S32: -0.1549 S33: 0.1755
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 244 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8346 37.6276 12.8083
REMARK 3 T TENSOR
REMARK 3 T11: 0.5227 T22: 0.4586
REMARK 3 T33: 0.3525 T12: 0.1137
REMARK 3 T13: 0.2319 T23: -0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 1.2958 L22: 1.0324
REMARK 3 L33: 0.9206 L12: -0.5860
REMARK 3 L13: 0.3188 L23: 0.3599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: -0.0549 S13: 0.1067
REMARK 3 S21: 0.0333 S22: -0.0339 S23: 0.0778
REMARK 3 S31: -0.3499 S32: -0.1998 S33: -0.0122
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 372 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0062 40.3780 11.6582
REMARK 3 T TENSOR
REMARK 3 T11: 0.7386 T22: 0.4626
REMARK 3 T33: 0.5787 T12: -0.0900
REMARK 3 T13: 0.1026 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 0.1442 L22: 0.0455
REMARK 3 L33: 2.5425 L12: 0.0234
REMARK 3 L13: -0.5190 L23: 0.0881
REMARK 3 S TENSOR
REMARK 3 S11: 0.1500 S12: -0.1086 S13: 0.0416
REMARK 3 S21: -0.1159 S22: -0.0996 S23: 0.0790
REMARK 3 S31: 0.0331 S32: -0.1279 S33: -0.0231
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 373 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1946 12.7038 9.8486
REMARK 3 T TENSOR
REMARK 3 T11: 0.3920 T22: 0.2995
REMARK 3 T33: 0.1075 T12: 0.1423
REMARK 3 T13: 0.2029 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.1241 L22: 0.3995
REMARK 3 L33: 0.2285 L12: -0.0543
REMARK 3 L13: -0.0451 L23: 0.1371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: -0.1754 S13: 0.0256
REMARK 3 S21: 0.0723 S22: -0.0470 S23: 0.0150
REMARK 3 S31: -0.0130 S32: -0.0783 S33: -0.1142
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7452 9.6828 -33.3477
REMARK 3 T TENSOR
REMARK 3 T11: 0.6004 T22: 0.4432
REMARK 3 T33: 0.2670 T12: 0.2272
REMARK 3 T13: 0.1198 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 2.1559 L22: 4.1017
REMARK 3 L33: 1.5658 L12: -0.5864
REMARK 3 L13: -0.3196 L23: -1.1449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: 0.1884 S13: 0.3246
REMARK 3 S21: -0.2290 S22: -0.0006 S23: -0.1137
REMARK 3 S31: -0.2324 S32: -0.0368 S33: 0.0029
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1655 -6.8539 -28.3641
REMARK 3 T TENSOR
REMARK 3 T11: 0.2272 T22: 0.3612
REMARK 3 T33: 0.1243 T12: 0.1202
REMARK 3 T13: 0.1032 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.1346 L22: 0.9096
REMARK 3 L33: 0.5411 L12: 0.3329
REMARK 3 L13: -0.2336 L23: 0.4277
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: 0.1608 S13: 0.0676
REMARK 3 S21: -0.1882 S22: -0.0630 S23: 0.0948
REMARK 3 S31: -0.0796 S32: -0.0093 S33: -0.1769
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 244 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9370 3.9576 -16.4982
REMARK 3 T TENSOR
REMARK 3 T11: 0.3598 T22: 0.4061
REMARK 3 T33: 0.2519 T12: 0.1295
REMARK 3 T13: -0.0210 T23: -0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 1.5179 L22: 2.6255
REMARK 3 L33: 1.0786 L12: 0.2094
REMARK 3 L13: -0.1222 L23: 0.1952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.3061 S13: 0.0923
REMARK 3 S21: -0.5997 S22: -0.0774 S23: 0.6175
REMARK 3 S31: -0.3564 S32: -0.3957 S33: 0.0716
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 325 THROUGH 441 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0499 -7.8477 -12.3076
REMARK 3 T TENSOR
REMARK 3 T11: 0.3050 T22: 0.3812
REMARK 3 T33: 0.1279 T12: 0.0146
REMARK 3 T13: 0.1035 T23: -0.0943
REMARK 3 L TENSOR
REMARK 3 L11: 0.2898 L22: 0.8624
REMARK 3 L33: 0.8923 L12: 0.0114
REMARK 3 L13: -0.2494 L23: 0.7445
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: -0.0189 S13: 0.1359
REMARK 3 S21: 0.1106 S22: -0.0570 S23: 0.2289
REMARK 3 S31: -0.1005 S32: -0.0896 S33: 0.0149
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6823 -38.6096 -53.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.1662
REMARK 3 T33: 0.2116 T12: -0.0892
REMARK 3 T13: 0.1150 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 0.6890 L22: 0.5346
REMARK 3 L33: 0.6983 L12: -0.3200
REMARK 3 L13: 0.1303 L23: -0.1066
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: 0.0236 S13: 0.2756
REMARK 3 S21: -0.0185 S22: -0.0728 S23: -0.1841
REMARK 3 S31: 0.0697 S32: 0.1303 S33: 0.0818
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 244 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2944 -32.1987 -41.3924
REMARK 3 T TENSOR
REMARK 3 T11: 0.2457 T22: 0.1900
REMARK 3 T33: 0.3649 T12: -0.0772
REMARK 3 T13: 0.1911 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.1884 L22: 0.1787
REMARK 3 L33: 1.7879 L12: -0.1356
REMARK 3 L13: 0.8979 L23: -0.4195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0448 S12: 0.1237 S13: 0.3420
REMARK 3 S21: 0.1624 S22: -0.0821 S23: 0.0832
REMARK 3 S31: -0.1735 S32: -0.1858 S33: -0.1862
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 338 THROUGH 439 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5214 -45.1638 -38.3254
REMARK 3 T TENSOR
REMARK 3 T11: 0.2149 T22: 0.2486
REMARK 3 T33: 0.2064 T12: -0.0648
REMARK 3 T13: 0.1230 T23: 0.0980
REMARK 3 L TENSOR
REMARK 3 L11: 0.2743 L22: 0.4756
REMARK 3 L33: 0.2135 L12: 0.3324
REMARK 3 L13: 0.1178 L23: 0.2305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0483 S12: -0.0107 S13: 0.0823
REMARK 3 S21: -0.0043 S22: -0.0578 S23: 0.1456
REMARK 3 S31: -0.0659 S32: 0.0720 S33: -0.4777
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1975 -66.0032 -76.8988
REMARK 3 T TENSOR
REMARK 3 T11: 0.8361 T22: 0.6322
REMARK 3 T33: 0.3025 T12: -0.0061
REMARK 3 T13: 0.1643 T23: 0.1350
REMARK 3 L TENSOR
REMARK 3 L11: 1.3443 L22: 1.8409
REMARK 3 L33: 2.5794 L12: 0.5264
REMARK 3 L13: -0.1561 L23: -1.2222
REMARK 3 S TENSOR
REMARK 3 S11: -0.0218 S12: 0.3310 S13: 0.2535
REMARK 3 S21: -0.1280 S22: 0.0606 S23: 0.1963
REMARK 3 S31: -0.5257 S32: -0.2939 S33: -0.1606
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 65 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2256 -79.5110 -67.8761
REMARK 3 T TENSOR
REMARK 3 T11: 0.3620 T22: 0.4358
REMARK 3 T33: 0.2048 T12: 0.0499
REMARK 3 T13: 0.0969 T23: -0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 0.7285 L22: 1.0051
REMARK 3 L33: 0.9970 L12: -0.1169
REMARK 3 L13: -0.1527 L23: 0.1511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.3978 S13: -0.2664
REMARK 3 S21: -0.4113 S22: -0.0594 S23: -0.0385
REMARK 3 S31: 0.0085 S32: -0.1661 S33: 0.0576
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 244 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6839 -70.6478 -60.2389
REMARK 3 T TENSOR
REMARK 3 T11: 0.3338 T22: 0.4978
REMARK 3 T33: 0.3957 T12: 0.1621
REMARK 3 T13: -0.0776 T23: -0.1287
REMARK 3 L TENSOR
REMARK 3 L11: 1.3592 L22: 1.1407
REMARK 3 L33: 0.9243 L12: 0.1888
REMARK 3 L13: -0.2768 L23: -0.2463
REMARK 3 S TENSOR
REMARK 3 S11: 0.1782 S12: 0.7068 S13: -0.1420
REMARK 3 S21: -0.4201 S22: 0.0213 S23: 0.4318
REMARK 3 S31: -0.2058 S32: -0.4195 S33: -0.0093
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 374 THROUGH 441 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6009 -88.4757 -51.2804
REMARK 3 T TENSOR
REMARK 3 T11: 0.3999 T22: 0.3923
REMARK 3 T33: 0.3316 T12: 0.1602
REMARK 3 T13: 0.2371 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.1466 L22: 0.8889
REMARK 3 L33: 0.8358 L12: -0.4982
REMARK 3 L13: -0.4387 L23: 0.3968
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: -0.0564 S13: -0.0920
REMARK 3 S21: 0.1412 S22: 0.0599 S23: 0.1049
REMARK 3 S31: 0.0088 S32: 0.0975 S33: 0.0535
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 43 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8021-115.1397 -52.3022
REMARK 3 T TENSOR
REMARK 3 T11: 0.5232 T22: 0.3662
REMARK 3 T33: 0.5240 T12: 0.0635
REMARK 3 T13: 0.1377 T23: -0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 3.9694 L22: 1.4005
REMARK 3 L33: 4.5717 L12: 2.0621
REMARK 3 L13: 4.0298 L23: 2.1668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0536 S12: 0.8913 S13: -0.5198
REMARK 3 S21: -0.1842 S22: 0.2304 S23: -1.0975
REMARK 3 S31: 0.3333 S32: 1.3668 S33: -0.2913
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 50 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1604-112.2129 -61.8318
REMARK 3 T TENSOR
REMARK 3 T11: 0.1711 T22: 0.2679
REMARK 3 T33: 0.1354 T12: 0.1474
REMARK 3 T13: -0.0157 T23: -0.0812
REMARK 3 L TENSOR
REMARK 3 L11: 1.5312 L22: 0.2986
REMARK 3 L33: 2.0566 L12: 0.3548
REMARK 3 L13: -1.5547 L23: -0.0384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: -0.0116 S13: -0.1045
REMARK 3 S21: -0.0131 S22: 0.0077 S23: -0.1338
REMARK 3 S31: 0.2179 S32: 0.1434 S33: 0.0357
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 60 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4235-120.0535 -68.0832
REMARK 3 T TENSOR
REMARK 3 T11: 0.2305 T22: 0.4120
REMARK 3 T33: 0.5620 T12: 0.0386
REMARK 3 T13: 0.1369 T23: -0.1475
REMARK 3 L TENSOR
REMARK 3 L11: 8.6505 L22: 5.4091
REMARK 3 L33: 2.8399 L12: -5.4630
REMARK 3 L13: 0.8491 L23: -1.4426
REMARK 3 S TENSOR
REMARK 3 S11: -0.1470 S12: 0.1117 S13: -0.7154
REMARK 3 S21: 0.0701 S22: -0.0281 S23: 0.8713
REMARK 3 S31: 0.3045 S32: -0.5217 S33: 0.1668
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 69 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6657-118.4142 -53.5613
REMARK 3 T TENSOR
REMARK 3 T11: 0.4954 T22: 0.3839
REMARK 3 T33: 0.2215 T12: 0.1022
REMARK 3 T13: -0.1423 T23: 0.0840
REMARK 3 L TENSOR
REMARK 3 L11: 4.0153 L22: 1.7297
REMARK 3 L33: 6.4350 L12: -2.5987
REMARK 3 L13: -4.9586 L23: 3.0882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: 0.1595 S13: -0.1885
REMARK 3 S21: 0.1021 S22: -0.1134 S23: 0.2547
REMARK 3 S31: 0.0465 S32: -0.2615 S33: 0.1765
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 83 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3896-109.7452 -59.2596
REMARK 3 T TENSOR
REMARK 3 T11: 0.4446 T22: 0.3487
REMARK 3 T33: 0.2455 T12: 0.2068
REMARK 3 T13: -0.0124 T23: 0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 0.8604 L22: 2.3860
REMARK 3 L33: 0.0214 L12: 0.1824
REMARK 3 L13: 0.0566 L23: 0.2152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: -0.3134 S13: -0.3135
REMARK 3 S21: 0.2029 S22: 0.2028 S23: 0.2373
REMARK 3 S31: 0.3654 S32: -0.1931 S33: -0.2477
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 93 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0949-115.2024 -57.0476
REMARK 3 T TENSOR
REMARK 3 T11: 0.1503 T22: 0.4469
REMARK 3 T33: 0.5448 T12: 0.0778
REMARK 3 T13: 0.1008 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 1.1370 L22: 0.4387
REMARK 3 L33: 0.5193 L12: 0.1430
REMARK 3 L13: 0.6089 L23: 0.1863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: -0.1416 S13: -0.1037
REMARK 3 S21: 0.0031 S22: -0.0958 S23: 0.1082
REMARK 3 S31: 0.0183 S32: -0.1893 S33: 0.0614
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 116 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4539-105.0611 -56.4910
REMARK 3 T TENSOR
REMARK 3 T11: 0.4367 T22: 0.4994
REMARK 3 T33: 0.5892 T12: 0.1989
REMARK 3 T13: 0.2271 T23: -0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 0.3784 L22: 2.4639
REMARK 3 L33: 0.6521 L12: -0.1257
REMARK 3 L13: 0.1795 L23: 1.1122
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: 0.0976 S13: -0.3081
REMARK 3 S21: -0.1544 S22: -0.0896 S23: -0.0496
REMARK 3 S31: 0.3936 S32: 0.1389 S33: 0.2000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 126 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5857-111.5797 -62.2603
REMARK 3 T TENSOR
REMARK 3 T11: 0.3017 T22: 0.3065
REMARK 3 T33: 0.6239 T12: -0.0387
REMARK 3 T13: 0.2402 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.0655 L22: 6.3665
REMARK 3 L33: 1.1237 L12: 0.6151
REMARK 3 L13: -0.1542 L23: -2.1137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0474 S12: 0.0304 S13: 0.2795
REMARK 3 S21: 0.1108 S22: 0.2058 S23: 0.5849
REMARK 3 S31: -0.0796 S32: -0.4196 S33: -0.2810
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 136 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9226-108.0926 -46.0600
REMARK 3 T TENSOR
REMARK 3 T11: 0.7116 T22: 0.9380
REMARK 3 T33: 0.6926 T12: 0.0176
REMARK 3 T13: -0.1421 T23: 0.1001
REMARK 3 L TENSOR
REMARK 3 L11: 1.3625 L22: 3.2517
REMARK 3 L33: 3.8458 L12: 2.1000
REMARK 3 L13: 2.2888 L23: 3.5316
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: 0.0342 S13: 0.0624
REMARK 3 S21: -0.1086 S22: -0.0182 S23: 0.0584
REMARK 3 S31: -0.0404 S32: 0.0197 S33: -0.0116
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 149 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5095 -99.5451 -51.7988
REMARK 3 T TENSOR
REMARK 3 T11: 0.7498 T22: 0.8403
REMARK 3 T33: 0.8345 T12: 0.1682
REMARK 3 T13: 0.0435 T23: -0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 5.3379 L22: 6.3600
REMARK 3 L33: 1.2292 L12: -2.9535
REMARK 3 L13: -1.1756 L23: -1.4883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: -0.1910 S13: -0.1843
REMARK 3 S21: 0.1384 S22: 0.0335 S23: 0.0526
REMARK 3 S31: 0.2473 S32: -0.1444 S33: -0.0180
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 159 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3615-103.4718 -59.2634
REMARK 3 T TENSOR
REMARK 3 T11: 0.8893 T22: 0.9722
REMARK 3 T33: 0.9447 T12: 0.2917
REMARK 3 T13: -0.0533 T23: -0.2812
REMARK 3 L TENSOR
REMARK 3 L11: 0.6835 L22: 2.4851
REMARK 3 L33: 0.1934 L12: 1.3032
REMARK 3 L13: 0.3624 L23: 0.6913
REMARK 3 S TENSOR
REMARK 3 S11: 0.0686 S12: -0.2231 S13: 0.2541
REMARK 3 S21: 0.3316 S22: -0.0195 S23: 0.3469
REMARK 3 S31: -0.1597 S32: -0.1505 S33: -0.0551
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 14 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2613 -15.5530 -10.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1921 T22: 0.2596
REMARK 3 T33: 0.2096 T12: 0.0343
REMARK 3 T13: 0.1944 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.0255 L22: 1.0173
REMARK 3 L33: 0.8913 L12: 0.0113
REMARK 3 L13: 0.1207 L23: 0.1411
REMARK 3 S TENSOR
REMARK 3 S11: -0.2181 S12: 0.0101 S13: -0.3509
REMARK 3 S21: 0.0862 S22: -0.0195 S23: -0.2369
REMARK 3 S31: 0.3781 S32: 0.2160 S33: 0.0133
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 254 THROUGH 395 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6691 -82.6608 -49.6910
REMARK 3 T TENSOR
REMARK 3 T11: 0.5785 T22: 0.5201
REMARK 3 T33: 0.7940 T12: 0.0897
REMARK 3 T13: 0.2780 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.2871 L22: 0.8886
REMARK 3 L33: 0.3726 L12: -0.0935
REMARK 3 L13: 0.0545 L23: 0.3761
REMARK 3 S TENSOR
REMARK 3 S11: -0.1435 S12: 0.0428 S13: -0.2967
REMARK 3 S21: 0.0991 S22: 0.2524 S23: -0.5728
REMARK 3 S31: 0.3366 S32: 0.5203 S33: -0.1246
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 396 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9591 -65.7179 -39.9058
REMARK 3 T TENSOR
REMARK 3 T11: 0.2573 T22: 0.2229
REMARK 3 T33: 0.2710 T12: 0.0998
REMARK 3 T13: 0.0622 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 2.0411 L22: 1.2419
REMARK 3 L33: 1.3144 L12: -1.0031
REMARK 3 L13: -0.9159 L23: 0.2472
REMARK 3 S TENSOR
REMARK 3 S11: -0.1161 S12: -0.4503 S13: 0.2191
REMARK 3 S21: 0.0841 S22: 0.0051 S23: -0.0930
REMARK 3 S31: -0.0401 S32: 0.2838 S33: -0.0214
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 2 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6861 -66.8734 -65.1224
REMARK 3 T TENSOR
REMARK 3 T11: 0.4804 T22: 0.3288
REMARK 3 T33: 0.3629 T12: 0.0812
REMARK 3 T13: -0.0363 T23: 0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 1.3929 L22: 0.4514
REMARK 3 L33: 0.9926 L12: 0.2753
REMARK 3 L13: -0.1520 L23: -0.5928
REMARK 3 S TENSOR
REMARK 3 S11: -0.1393 S12: -0.4225 S13: -0.5987
REMARK 3 S21: 0.4250 S22: 0.0842 S23: 0.2173
REMARK 3 S31: 0.2935 S32: 0.1958 S33: 0.0122
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 89 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.6369 -49.8163 -66.5466
REMARK 3 T TENSOR
REMARK 3 T11: 0.2632 T22: 0.2760
REMARK 3 T33: 0.1537 T12: 0.1410
REMARK 3 T13: -0.0754 T23: 0.0519
REMARK 3 L TENSOR
REMARK 3 L11: 1.3847 L22: 1.8624
REMARK 3 L33: 1.9053 L12: -0.6138
REMARK 3 L13: 0.0792 L23: -0.0244
REMARK 3 S TENSOR
REMARK 3 S11: -0.1447 S12: -0.3073 S13: -0.1511
REMARK 3 S21: 0.3820 S22: 0.1392 S23: -0.1554
REMARK 3 S31: 0.2470 S32: 0.0180 S33: -0.0389
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 129 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.1430 -53.6362 -75.7666
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.2374
REMARK 3 T33: 0.0712 T12: 0.0452
REMARK 3 T13: 0.0239 T23: -0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 1.0394 L22: 2.1404
REMARK 3 L33: 3.3618 L12: 0.4005
REMARK 3 L13: -0.6792 L23: 1.2031
REMARK 3 S TENSOR
REMARK 3 S11: 0.1257 S12: 0.1317 S13: -0.0100
REMARK 3 S21: -0.0182 S22: 0.0676 S23: -0.1091
REMARK 3 S31: 0.0483 S32: 0.0733 S33: -0.0118
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 161 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.5288 -48.8097 -78.8595
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: 0.2867
REMARK 3 T33: 0.2160 T12: 0.0801
REMARK 3 T13: 0.1447 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 0.7616 L22: 0.9818
REMARK 3 L33: 0.7489 L12: 0.2314
REMARK 3 L13: 0.3531 L23: -0.0368
REMARK 3 S TENSOR
REMARK 3 S11: -0.0383 S12: -0.0770 S13: -0.0905
REMARK 3 S21: 0.0666 S22: 0.0195 S23: -0.0112
REMARK 3 S31: 0.0814 S32: 0.0255 S33: 0.0830
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 200 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.1170 -57.2154 -74.3318
REMARK 3 T TENSOR
REMARK 3 T11: 0.2575 T22: 0.3599
REMARK 3 T33: 0.1343 T12: -0.0064
REMARK 3 T13: 0.0073 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 5.8790 L22: 2.2460
REMARK 3 L33: 2.6901 L12: 1.4935
REMARK 3 L13: -1.6470 L23: -1.6806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.1315 S13: 0.0957
REMARK 3 S21: 0.2734 S22: 0.1106 S23: 0.4253
REMARK 3 S31: -0.1551 S32: -0.5222 S33: -0.1314
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 224 THROUGH 273 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.9824 -64.1501 -82.2432
REMARK 3 T TENSOR
REMARK 3 T11: 0.3681 T22: 0.2494
REMARK 3 T33: 0.2872 T12: 0.0149
REMARK 3 T13: 0.1637 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.9525 L22: 1.1819
REMARK 3 L33: 1.1484 L12: -0.1249
REMARK 3 L13: 0.5150 L23: 0.3731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0737 S12: 0.2160 S13: -0.0376
REMARK 3 S21: -0.1144 S22: 0.0350 S23: -0.1508
REMARK 3 S31: 0.4513 S32: 0.3458 S33: 0.0773
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 274 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -70.9761 -65.2424 -84.8408
REMARK 3 T TENSOR
REMARK 3 T11: 0.3699 T22: 0.4775
REMARK 3 T33: 0.4109 T12: -0.0673
REMARK 3 T13: 0.1101 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.3634 L22: 2.9575
REMARK 3 L33: 0.2903 L12: 0.9988
REMARK 3 L13: -0.3026 L23: -0.8780
REMARK 3 S TENSOR
REMARK 3 S11: -0.0781 S12: 0.2835 S13: -0.2613
REMARK 3 S21: -0.0359 S22: 0.1913 S23: 0.2051
REMARK 3 S31: 0.5006 S32: -0.3970 S33: -0.1006
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 312 THROUGH 372 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.7508 -71.4385 -88.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.5106 T22: 0.3926
REMARK 3 T33: 0.2485 T12: -0.0129
REMARK 3 T13: 0.1272 T23: -0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 0.4896 L22: 0.3596
REMARK 3 L33: 0.9493 L12: -0.0332
REMARK 3 L13: -0.3085 L23: 0.1130
REMARK 3 S TENSOR
REMARK 3 S11: -0.1456 S12: 0.1080 S13: -0.3240
REMARK 3 S21: 0.0687 S22: -0.2581 S23: 0.2603
REMARK 3 S31: 0.3735 S32: -0.2262 S33: 0.1372
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 373 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.1350 -42.2878 -84.7786
REMARK 3 T TENSOR
REMARK 3 T11: 0.2539 T22: 0.3979
REMARK 3 T33: 0.0708 T12: -0.0043
REMARK 3 T13: 0.0436 T23: -0.1700
REMARK 3 L TENSOR
REMARK 3 L11: 0.1390 L22: 0.6250
REMARK 3 L33: 0.4007 L12: 0.0352
REMARK 3 L13: -0.0935 L23: 0.0631
REMARK 3 S TENSOR
REMARK 3 S11: -0.1183 S12: 0.1942 S13: -0.1738
REMARK 3 S21: -0.2515 S22: 0.0253 S23: 0.0172
REMARK 3 S31: 0.0774 S32: -0.0356 S33: -0.0315
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.6949 -39.1142 -41.6045
REMARK 3 T TENSOR
REMARK 3 T11: 0.3066 T22: 0.3439
REMARK 3 T33: 0.1182 T12: 0.0089
REMARK 3 T13: 0.1665 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.6295 L22: 1.7188
REMARK 3 L33: 2.0619 L12: 0.2325
REMARK 3 L13: -0.4264 L23: -0.1861
REMARK 3 S TENSOR
REMARK 3 S11: -0.0971 S12: -0.1527 S13: -0.2319
REMARK 3 S21: 0.1281 S22: 0.0144 S23: 0.0529
REMARK 3 S31: 0.4081 S32: -0.0797 S33: 0.2496
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 65 THROUGH 295 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.7277 -25.3025 -48.7699
REMARK 3 T TENSOR
REMARK 3 T11: 0.2478 T22: 0.3408
REMARK 3 T33: 0.1033 T12: 0.0655
REMARK 3 T13: 0.1258 T23: -0.1081
REMARK 3 L TENSOR
REMARK 3 L11: 1.0566 L22: 0.4097
REMARK 3 L33: 0.7158 L12: -0.0610
REMARK 3 L13: -0.1870 L23: 0.0379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0872 S12: -0.0620 S13: -0.2255
REMARK 3 S21: 0.3023 S22: 0.0038 S23: 0.1806
REMARK 3 S31: 0.1224 S32: -0.2081 S33: 0.0967
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 296 THROUGH 441 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.8492 -23.4025 -62.3194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1891 T22: 0.3944
REMARK 3 T33: 0.2754 T12: 0.0415
REMARK 3 T13: 0.1306 T23: -0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 1.0468 L22: 1.1117
REMARK 3 L33: 1.1071 L12: 0.4554
REMARK 3 L13: -0.1012 L23: 0.3262
REMARK 3 S TENSOR
REMARK 3 S11: -0.2369 S12: 0.1820 S13: -0.1146
REMARK 3 S21: -0.0494 S22: -0.0084 S23: 0.4585
REMARK 3 S31: 0.2076 S32: -0.1515 S33: 0.1083
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.6533 -1.3641 -15.2369
REMARK 3 T TENSOR
REMARK 3 T11: 0.3183 T22: 0.3593
REMARK 3 T33: 0.3576 T12: -0.0578
REMARK 3 T13: -0.1105 T23: 0.1122
REMARK 3 L TENSOR
REMARK 3 L11: 2.3948 L22: 0.6637
REMARK 3 L33: 3.2110 L12: 0.9354
REMARK 3 L13: -0.6179 L23: 0.5620
REMARK 3 S TENSOR
REMARK 3 S11: 0.1157 S12: -0.2221 S13: -0.7826
REMARK 3 S21: 0.2098 S22: 0.0519 S23: -0.2026
REMARK 3 S31: 0.7952 S32: 0.2118 S33: 0.0024
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 48 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.5520 9.3240 -19.0306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1759 T22: 0.2000
REMARK 3 T33: 0.1883 T12: -0.0073
REMARK 3 T13: -0.0114 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.5887 L22: 2.2529
REMARK 3 L33: 1.5883 L12: 0.1841
REMARK 3 L13: -0.0699 L23: 0.2166
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.2983 S13: -0.2095
REMARK 3 S21: 0.4024 S22: 0.0503 S23: -0.1024
REMARK 3 S31: 0.2491 S32: 0.2553 S33: -0.0957
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 161 THROUGH 273 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.5026 10.7641 -28.7916
REMARK 3 T TENSOR
REMARK 3 T11: 0.2749 T22: 0.2535
REMARK 3 T33: 0.2640 T12: -0.2017
REMARK 3 T13: 0.1236 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.7249 L22: 0.5164
REMARK 3 L33: 0.5503 L12: 0.2981
REMARK 3 L13: -0.2934 L23: -0.2800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.1613 S13: -0.1323
REMARK 3 S21: 0.0710 S22: -0.0623 S23: 0.0942
REMARK 3 S31: 0.2151 S32: -0.0891 S33: -0.0671
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 274 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.9363 7.7502 -29.8400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2189 T22: 0.2434
REMARK 3 T33: 0.3792 T12: -0.0712
REMARK 3 T13: 0.2136 T23: -0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 1.6063 L22: 0.5142
REMARK 3 L33: 1.3922 L12: 0.1999
REMARK 3 L13: -0.8037 L23: 0.1447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0086 S12: 0.2752 S13: 0.1224
REMARK 3 S21: -0.0613 S22: -0.0280 S23: -0.0271
REMARK 3 S31: 0.0031 S32: -0.0662 S33: -0.3470
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 312 THROUGH 439 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.7469 11.9243 -36.4526
REMARK 3 T TENSOR
REMARK 3 T11: 0.1271 T22: 0.1774
REMARK 3 T33: 0.2698 T12: -0.0925
REMARK 3 T13: 0.0801 T23: -0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 0.4065 L22: 0.9211
REMARK 3 L33: 0.1453 L12: 0.5487
REMARK 3 L13: 0.0513 L23: -0.0402
REMARK 3 S TENSOR
REMARK 3 S11: -0.1214 S12: 0.1697 S13: -0.1419
REMARK 3 S21: -0.2344 S22: 0.1048 S23: 0.0663
REMARK 3 S31: 0.0430 S32: 0.0027 S33: -0.0591
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.6207 43.2486 0.9755
REMARK 3 T TENSOR
REMARK 3 T11: 0.8097 T22: 0.6614
REMARK 3 T33: 0.3039 T12: -0.2493
REMARK 3 T13: 0.0083 T23: -0.1224
REMARK 3 L TENSOR
REMARK 3 L11: 1.1491 L22: 1.1398
REMARK 3 L33: 1.5279 L12: 0.2817
REMARK 3 L13: -0.9598 L23: -1.1155
REMARK 3 S TENSOR
REMARK 3 S11: -0.1214 S12: -0.4566 S13: 0.0392
REMARK 3 S21: 0.3149 S22: 0.0177 S23: -0.0252
REMARK 3 S31: 0.0199 S32: 0.0197 S33: 0.1384
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 128 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.5137 50.7295 -10.2631
REMARK 3 T TENSOR
REMARK 3 T11: 0.3994 T22: 0.3030
REMARK 3 T33: 0.3604 T12: -0.1330
REMARK 3 T13: 0.0179 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 1.5118 L22: 0.3985
REMARK 3 L33: 1.1553 L12: 0.5685
REMARK 3 L13: -0.3602 L23: -0.3256
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.2237 S13: 0.0295
REMARK 3 S21: 0.2809 S22: -0.1990 S23: 0.2056
REMARK 3 S31: 0.2366 S32: -0.1766 S33: 0.1000
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 244 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.9080 43.5369 -13.7426
REMARK 3 T TENSOR
REMARK 3 T11: 0.5851 T22: 0.4916
REMARK 3 T33: 0.3029 T12: -0.1567
REMARK 3 T13: 0.0094 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 1.9790 L22: 1.7680
REMARK 3 L33: 1.0283 L12: -0.4247
REMARK 3 L13: -0.2951 L23: 0.2496
REMARK 3 S TENSOR
REMARK 3 S11: -0.0597 S12: -0.4828 S13: 0.0615
REMARK 3 S21: 0.3902 S22: -0.1041 S23: 0.3701
REMARK 3 S31: 0.2015 S32: -0.2513 S33: 0.0634
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 325 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): -73.5222 37.9002 -17.6337
REMARK 3 T TENSOR
REMARK 3 T11: 0.5345 T22: 0.5815
REMARK 3 T33: 0.4174 T12: -0.2406
REMARK 3 T13: -0.0511 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 1.6973 L22: 0.7859
REMARK 3 L33: 2.3415 L12: -0.3022
REMARK 3 L13: -0.1540 L23: 0.2809
REMARK 3 S TENSOR
REMARK 3 S11: 0.0397 S12: -0.2788 S13: -0.1056
REMARK 3 S21: 0.3650 S22: -0.1031 S23: 0.5039
REMARK 3 S31: 0.1743 S32: -0.6389 S33: -0.0212
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 374 THROUGH 441 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.0010 58.9527 -23.6762
REMARK 3 T TENSOR
REMARK 3 T11: 0.2422 T22: 0.2633
REMARK 3 T33: 0.2923 T12: 0.0108
REMARK 3 T13: 0.0717 T23: -0.0995
REMARK 3 L TENSOR
REMARK 3 L11: 2.2400 L22: 2.0765
REMARK 3 L33: 0.7669 L12: 1.2624
REMARK 3 L13: 0.5743 L23: 0.3096
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: 0.1969 S13: 0.1190
REMARK 3 S21: -0.2032 S22: -0.0391 S23: 0.2567
REMARK 3 S31: -0.1833 S32: 0.2428 S33: 0.0218
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 43 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1781 86.2192 -12.7511
REMARK 3 T TENSOR
REMARK 3 T11: 0.3813 T22: 0.3133
REMARK 3 T33: 0.6789 T12: -0.0362
REMARK 3 T13: -0.2654 T23: -0.1289
REMARK 3 L TENSOR
REMARK 3 L11: 0.8840 L22: 3.7629
REMARK 3 L33: 2.3918 L12: 1.1540
REMARK 3 L13: 0.4695 L23: 1.4618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: 0.1759 S13: -0.1971
REMARK 3 S21: -0.2345 S22: 0.1668 S23: -0.1584
REMARK 3 S31: 0.0803 S32: 0.0314 S33: -0.2734
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 69 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.7158 85.0310 -18.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.3789 T22: 0.2389
REMARK 3 T33: 0.4487 T12: 0.1339
REMARK 3 T13: -0.2420 T23: -0.1619
REMARK 3 L TENSOR
REMARK 3 L11: 0.3871 L22: 1.2061
REMARK 3 L33: 0.2547 L12: 0.0496
REMARK 3 L13: -0.1930 L23: -0.1599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: 0.0059 S13: 0.0328
REMARK 3 S21: 0.1284 S22: -0.0269 S23: 0.0211
REMARK 3 S31: -0.0450 S32: -0.0033 S33: -0.0736
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 93 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.8562 86.8750 -8.5689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3820 T22: 0.4112
REMARK 3 T33: 0.6815 T12: -0.0310
REMARK 3 T13: -0.1033 T23: -0.2221
REMARK 3 L TENSOR
REMARK 3 L11: 2.6458 L22: 9.7693
REMARK 3 L33: 0.3447 L12: 0.9189
REMARK 3 L13: 0.0876 L23: 1.0235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.4587 S13: -0.0723
REMARK 3 S21: 0.6817 S22: -0.0338 S23: 0.0782
REMARK 3 S31: -0.2129 S32: -0.0234 S33: 0.0121
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.0759 84.3401 -23.0943
REMARK 3 T TENSOR
REMARK 3 T11: 0.4485 T22: 0.3368
REMARK 3 T33: 0.4667 T12: 0.0198
REMARK 3 T13: -0.0784 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 0.4740 L22: 0.0049
REMARK 3 L33: 0.7114 L12: -0.0361
REMARK 3 L13: -0.5750 L23: 0.0381
REMARK 3 S TENSOR
REMARK 3 S11: -0.1209 S12: 0.0661 S13: 0.0316
REMARK 3 S21: 0.0562 S22: 0.0197 S23: 0.0602
REMARK 3 S31: -0.0704 S32: -0.1969 S33: 0.0770
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 116 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.3417 75.1814 -17.4056
REMARK 3 T TENSOR
REMARK 3 T11: 0.4475 T22: 0.2493
REMARK 3 T33: 0.5169 T12: -0.0187
REMARK 3 T13: 0.1039 T23: -0.1535
REMARK 3 L TENSOR
REMARK 3 L11: 3.4954 L22: 2.5963
REMARK 3 L33: 1.6999 L12: -1.7977
REMARK 3 L13: -1.0368 L23: 1.9530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: -0.0014 S13: -0.1907
REMARK 3 S21: -0.0208 S22: 0.0586 S23: 0.2479
REMARK 3 S31: 0.0241 S32: -0.1614 S33: -0.0301
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 126 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.5035 81.7534 -11.4897
REMARK 3 T TENSOR
REMARK 3 T11: 0.3513 T22: 0.5618
REMARK 3 T33: 0.6532 T12: -0.0705
REMARK 3 T13: -0.0379 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 3.2902 L22: 4.0311
REMARK 3 L33: 7.7306 L12: -3.0376
REMARK 3 L13: 1.1797 L23: 1.8908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.2306 S13: -0.1998
REMARK 3 S21: 0.3022 S22: -0.0690 S23: -0.0264
REMARK 3 S31: 0.1912 S32: -0.0148 S33: 0.0316
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 136 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.8645 74.2258 -24.8044
REMARK 3 T TENSOR
REMARK 3 T11: 0.6064 T22: 0.8690
REMARK 3 T33: 0.7418 T12: -0.0940
REMARK 3 T13: -0.2676 T23: -0.0847
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0932
REMARK 3 L33: 0.0927 L12: -0.0018
REMARK 3 L13: -0.0019 L23: 0.0933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0384 S12: 0.1210 S13: -0.2414
REMARK 3 S21: -0.1067 S22: -0.0623 S23: 0.0991
REMARK 3 S31: 0.2071 S32: -0.0638 S33: 0.0421
REMARK 3 TLS GROUP : 61
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 159 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.0525 73.3006 -13.8314
REMARK 3 T TENSOR
REMARK 3 T11: 1.2934 T22: 1.2468
REMARK 3 T33: 1.2127 T12: -0.0659
REMARK 3 T13: -0.1414 T23: 0.1198
REMARK 3 L TENSOR
REMARK 3 L11: 1.1354 L22: 5.5025
REMARK 3 L33: 3.3301 L12: 2.2922
REMARK 3 L13: 1.3453 L23: 3.9484
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: -0.0630 S13: -0.3938
REMARK 3 S21: 0.2068 S22: -0.0186 S23: -0.6827
REMARK 3 S31: 0.3795 S32: 0.5159 S33: 0.0296
REMARK 3 TLS GROUP : 62
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 14 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.4793 -13.8744 -64.1591
REMARK 3 T TENSOR
REMARK 3 T11: 0.1993 T22: 0.0805
REMARK 3 T33: 0.4201 T12: 0.0249
REMARK 3 T13: 0.0353 T23: 0.0971
REMARK 3 L TENSOR
REMARK 3 L11: 0.8933 L22: 0.8185
REMARK 3 L33: 1.4624 L12: -0.0271
REMARK 3 L13: -0.2859 L23: 0.1605
REMARK 3 S TENSOR
REMARK 3 S11: -0.1435 S12: -0.0524 S13: 0.0785
REMARK 3 S21: 0.0083 S22: -0.0259 S23: -0.2124
REMARK 3 S31: 0.0185 S32: 0.0336 S33: 0.0904
REMARK 3 TLS GROUP : 63
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 254 THROUGH 388 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6798 53.6338 -23.9779
REMARK 3 T TENSOR
REMARK 3 T11: 0.3586 T22: 0.5008
REMARK 3 T33: 0.6673 T12: -0.0882
REMARK 3 T13: -0.0863 T23: 0.1945
REMARK 3 L TENSOR
REMARK 3 L11: 0.3880 L22: 1.6930
REMARK 3 L33: 0.8266 L12: -0.1312
REMARK 3 L13: -0.1489 L23: 0.8058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0406 S12: -0.1295 S13: 0.1806
REMARK 3 S21: -0.0462 S22: 0.0950 S23: -0.6180
REMARK 3 S31: -0.2908 S32: 0.4443 S33: -0.2437
REMARK 3 TLS GROUP : 64
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 389 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8602 36.8525 -34.1527
REMARK 3 T TENSOR
REMARK 3 T11: 0.3413 T22: 0.7538
REMARK 3 T33: 0.4617 T12: 0.2167
REMARK 3 T13: 0.0540 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 0.9499 L22: 1.8776
REMARK 3 L33: 1.7125 L12: 0.4169
REMARK 3 L13: -0.0736 L23: 0.6514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: 0.0877 S13: -0.1448
REMARK 3 S21: -0.0759 S22: 0.1795 S23: -0.2084
REMARK 3 S31: 0.1754 S32: 0.4128 S33: -0.1666
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE TWIN FRACTIONS WERE ADJUSTED DURING
REMARK 3 REFINEMENT
REMARK 4
REMARK 4 6MZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000237901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104265
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 149.571
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.65400
REMARK 200 R SYM FOR SHELL (I) : 0.65400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: RECTANGULAR CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM PIPES, 100 MM MGCL2 [PH 7.0],
REMARK 280 AND 10-15% PEG-8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 97.49500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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 MET A 1
REMARK 465 THR A 41
REMARK 465 ILE A 42
REMARK 465 GLY A 43
REMARK 465 GLY A 44
REMARK 465 GLY A 45
REMARK 465 ASP A 46
REMARK 465 LYS A 280
REMARK 465 ALA A 281
REMARK 465 TYR A 282
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 GLY B 58
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 GLY B 450
REMARK 465 GLU B 451
REMARK 465 GLU B 452
REMARK 465 ASP B 453
REMARK 465 GLU B 454
REMARK 465 ALA B 455
REMARK 465 MET C 1
REMARK 465 THR C 41
REMARK 465 ILE C 42
REMARK 465 HIS C 283
REMARK 465 GLU C 284
REMARK 465 VAL C 440
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 GLY D 58
REMARK 465 ASN D 59
REMARK 465 LYS D 60
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 GLY D 450
REMARK 465 GLU 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 1
REMARK 465 ALA E 2
REMARK 465 ASP E 3
REMARK 465 GLN E 4
REMARK 465 ASP E 5
REMARK 465 ASP E 6
REMARK 465 VAL E 7
REMARK 465 ASP E 8
REMARK 465 PHE E 9
REMARK 465 THR E 10
REMARK 465 THR E 11
REMARK 465 LEU E 12
REMARK 465 PRO E 13
REMARK 465 SER E 44
REMARK 465 PRO E 45
REMARK 465 GLU E 260
REMARK 465 GLN E 261
REMARK 465 GLU E 262
REMARK 465 GLN E 263
REMARK 465 GLU E 264
REMARK 465 GLN E 265
REMARK 465 ILE E 266
REMARK 465 LEU E 267
REMARK 465 GLN E 268
REMARK 465 THR E 269
REMARK 465 ASP E 270
REMARK 465 LYS E 271
REMARK 465 ASP E 272
REMARK 465 GLY E 273
REMARK 465 ASP E 274
REMARK 465 THR E 275
REMARK 465 LEU E 276
REMARK 465 MET E 277
REMARK 465 GLY E 278
REMARK 465 ASN E 279
REMARK 465 LEU E 280
REMARK 465 LEU E 281
REMARK 465 ALA E 282
REMARK 465 TYR E 283
REMARK 465 GLN E 284
REMARK 465 ASP E 285
REMARK 465 THR E 286
REMARK 465 ASN E 287
REMARK 465 ALA E 288
REMARK 465 SER E 289
REMARK 465 ALA E 290
REMARK 465 ILE E 291
REMARK 465 HIS E 292
REMARK 465 PRO E 293
REMARK 465 ALA E 294
REMARK 465 THR E 295
REMARK 465 LYS E 296
REMARK 465 PRO E 297
REMARK 465 ALA E 298
REMARK 465 VAL E 299
REMARK 465 ASP E 300
REMARK 465 ALA E 544
REMARK 465 THR E 545
REMARK 465 GLY E 546
REMARK 465 LEU E 547
REMARK 465 GLU E 548
REMARK 465 HIS E 549
REMARK 465 HIS E 550
REMARK 465 HIS E 551
REMARK 465 HIS E 552
REMARK 465 HIS E 553
REMARK 465 HIS E 554
REMARK 465 MET F 30
REMARK 465 ARG F 31
REMARK 465 GLY F 32
REMARK 465 SER F 33
REMARK 465 HIS F 34
REMARK 465 HIS F 35
REMARK 465 HIS F 36
REMARK 465 HIS F 37
REMARK 465 HIS F 38
REMARK 465 HIS F 39
REMARK 465 GLY F 40
REMARK 465 SER F 41
REMARK 465 ALA F 42
REMARK 465 LEU F 168
REMARK 465 ASN F 169
REMARK 465 MET G 1
REMARK 465 LYS G 40
REMARK 465 THR G 41
REMARK 465 ILE G 42
REMARK 465 GLY G 43
REMARK 465 GLY G 44
REMARK 465 GLY G 45
REMARK 465 ASP G 46
REMARK 465 LYS G 280
REMARK 465 ALA G 281
REMARK 465 TYR G 282
REMARK 465 HIS G 283
REMARK 465 ASP G 438
REMARK 465 SER G 439
REMARK 465 VAL G 440
REMARK 465 GLU G 441
REMARK 465 GLY G 442
REMARK 465 GLU G 443
REMARK 465 GLY G 444
REMARK 465 GLU G 445
REMARK 465 GLU G 446
REMARK 465 GLU G 447
REMARK 465 GLY G 448
REMARK 465 GLU G 449
REMARK 465 GLU G 450
REMARK 465 TYR G 451
REMARK 465 ALA H 57
REMARK 465 GLY H 58
REMARK 465 GLU H 442
REMARK 465 GLN H 443
REMARK 465 GLY H 444
REMARK 465 GLU H 445
REMARK 465 PHE H 446
REMARK 465 GLU H 447
REMARK 465 GLU H 448
REMARK 465 GLU H 449
REMARK 465 GLY H 450
REMARK 465 GLU H 451
REMARK 465 GLU H 452
REMARK 465 ASP H 453
REMARK 465 GLU H 454
REMARK 465 ALA H 455
REMARK 465 MET I 1
REMARK 465 HIS I 283
REMARK 465 GLU I 284
REMARK 465 VAL I 440
REMARK 465 GLU I 441
REMARK 465 GLY I 442
REMARK 465 GLU I 443
REMARK 465 GLY I 444
REMARK 465 GLU I 445
REMARK 465 GLU I 446
REMARK 465 GLU I 447
REMARK 465 GLY I 448
REMARK 465 GLU I 449
REMARK 465 GLU I 450
REMARK 465 TYR I 451
REMARK 465 GLY J 58
REMARK 465 ASN J 59
REMARK 465 LYS J 60
REMARK 465 GLU J 442
REMARK 465 GLN J 443
REMARK 465 GLY J 444
REMARK 465 GLU J 445
REMARK 465 PHE J 446
REMARK 465 GLU J 447
REMARK 465 GLU J 448
REMARK 465 GLU J 449
REMARK 465 GLY J 450
REMARK 465 GLU J 451
REMARK 465 GLU J 452
REMARK 465 ASP J 453
REMARK 465 GLU J 454
REMARK 465 ALA J 455
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 ASP K 3
REMARK 465 GLN K 4
REMARK 465 ASP K 5
REMARK 465 ASP K 6
REMARK 465 VAL K 7
REMARK 465 ASP K 8
REMARK 465 PHE K 9
REMARK 465 THR K 10
REMARK 465 THR K 11
REMARK 465 LEU K 12
REMARK 465 PRO K 13
REMARK 465 SER K 44
REMARK 465 PRO K 45
REMARK 465 GLU K 260
REMARK 465 GLN K 261
REMARK 465 GLU K 262
REMARK 465 GLN K 263
REMARK 465 GLU K 264
REMARK 465 GLN K 265
REMARK 465 ILE K 266
REMARK 465 LEU K 267
REMARK 465 GLN K 268
REMARK 465 THR K 269
REMARK 465 ASP K 270
REMARK 465 LYS K 271
REMARK 465 ASP K 272
REMARK 465 GLY K 273
REMARK 465 ASP K 274
REMARK 465 THR K 275
REMARK 465 LEU K 276
REMARK 465 MET K 277
REMARK 465 GLY K 278
REMARK 465 ASN K 279
REMARK 465 LEU K 280
REMARK 465 LEU K 281
REMARK 465 ALA K 282
REMARK 465 TYR K 283
REMARK 465 GLN K 284
REMARK 465 ASP K 285
REMARK 465 THR K 286
REMARK 465 ASN K 287
REMARK 465 ALA K 288
REMARK 465 SER K 289
REMARK 465 ALA K 290
REMARK 465 ILE K 291
REMARK 465 HIS K 292
REMARK 465 PRO K 293
REMARK 465 ALA K 294
REMARK 465 THR K 295
REMARK 465 LYS K 296
REMARK 465 PRO K 297
REMARK 465 ALA K 298
REMARK 465 VAL K 299
REMARK 465 ASP K 300
REMARK 465 ALA K 544
REMARK 465 THR K 545
REMARK 465 GLY K 546
REMARK 465 LEU K 547
REMARK 465 GLU K 548
REMARK 465 HIS K 549
REMARK 465 HIS K 550
REMARK 465 HIS K 551
REMARK 465 HIS K 552
REMARK 465 HIS K 553
REMARK 465 HIS K 554
REMARK 465 MET L 30
REMARK 465 ARG L 31
REMARK 465 GLY L 32
REMARK 465 SER L 33
REMARK 465 HIS L 34
REMARK 465 HIS L 35
REMARK 465 HIS L 36
REMARK 465 HIS L 37
REMARK 465 HIS L 38
REMARK 465 HIS L 39
REMARK 465 GLY L 40
REMARK 465 SER L 41
REMARK 465 ALA L 42
REMARK 465 LEU L 168
REMARK 465 ASN L 169
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 31 CD
REMARK 470 MET A 36 O
REMARK 470 ASP A 47 N
REMARK 470 ASP B 163 OD1 OD2
REMARK 470 GLN C 31 CD
REMARK 470 MET C 36 O
REMARK 470 ASP C 46 CG
REMARK 470 ASP C 47 CA C
REMARK 470 GLN I 31 CA CD
REMARK 470 GLU I 358 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 79 31.60 -80.42
REMARK 500 THR A 80 -33.26 -141.86
REMARK 500 ILE A 114 -0.88 -149.42
REMARK 500 ALA A 265 66.45 -100.48
REMARK 500 THR A 349 3.89 50.22
REMARK 500 ARG B 2 -72.79 -126.84
REMARK 500 LYS B 60 -157.19 -141.19
REMARK 500 SER B 97 -70.83 -86.95
REMARK 500 THR B 109 -81.23 -95.83
REMARK 500 SER B 128 22.45 -78.00
REMARK 500 ASN B 197 -32.36 -131.09
REMARK 500 PRO B 245 94.83 -63.37
REMARK 500 LEU B 265 62.28 -101.52
REMARK 500 ALA B 285 72.56 51.04
REMARK 500 ALA B 304 69.47 -68.30
REMARK 500 ASN B 380 76.75 -101.72
REMARK 500 ARG C 79 30.91 -82.97
REMARK 500 THR C 80 -32.06 -139.47
REMARK 500 THR C 109 -71.59 -82.55
REMARK 500 GLU C 279 -41.06 -131.67
REMARK 500 ARG D 2 -70.60 -135.22
REMARK 500 ASP D 39 -52.58 -121.53
REMARK 500 ASP D 69 141.18 -170.89
REMARK 500 GLN D 96 -73.61 -89.10
REMARK 500 THR D 109 -80.41 -102.00
REMARK 500 SER D 128 30.88 -87.17
REMARK 500 VAL D 177 -82.70 -117.38
REMARK 500 ASN D 197 -35.14 -134.67
REMARK 500 PRO D 245 92.01 -63.84
REMARK 500 ARG D 284 107.48 -51.86
REMARK 500 ALA D 304 71.89 -66.05
REMARK 500 ASN D 380 76.41 -103.40
REMARK 500 ALA E 50 36.74 -86.32
REMARK 500 VAL E 64 44.16 -98.32
REMARK 500 SER E 86 42.33 -75.23
REMARK 500 ASN E 90 68.91 -114.88
REMARK 500 ASN E 171 15.98 57.52
REMARK 500 SER E 173 -76.09 -49.46
REMARK 500 PHE E 212 -154.41 -104.49
REMARK 500 LEU E 221 -57.68 -132.31
REMARK 500 LYS E 247 10.39 -67.42
REMARK 500 GLN E 248 146.53 -171.32
REMARK 500 GLU E 258 -68.57 -96.30
REMARK 500 GLU E 303 31.80 -92.31
REMARK 500 PHE E 318 -67.99 -139.33
REMARK 500 SER E 323 62.46 -114.27
REMARK 500 LYS E 346 -12.38 -141.72
REMARK 500 ARG E 395 -57.61 -141.56
REMARK 500 PHE E 433 42.58 -145.66
REMARK 500 ASP E 434 -78.21 -63.51
REMARK 500
REMARK 500 THIS ENTRY HAS 112 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP A 600 O1G
REMARK 620 2 GTP A 600 O1B 75.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 11 OE1
REMARK 620 2 GDP B 600 O1A 81.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 600 O1G
REMARK 620 2 GTP C 600 O1B 69.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP G 600 O3G
REMARK 620 2 GTP G 600 O2B 73.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 179 OD2
REMARK 620 2 GDP H 600 O2A 101.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP I 600 O3G
REMARK 620 2 GTP I 600 O2B 68.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN J 11 OE1
REMARK 620 2 GDP J 600 O2A 71.6
REMARK 620 N 1
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 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP H 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP I 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP J 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6MZE RELATED DB: PDB
REMARK 900 SAME CITATION
REMARK 900 RELATED ID: 6MZF RELATED DB: PDB
REMARK 900 SAME CITATION
DBREF 6MZG A 1 451 UNP P02550 TBA1A_PIG 1 451
DBREF 6MZG B 1 455 UNP P02554 TBB_PIG 1 445
DBREF 6MZG C 1 451 UNP P02550 TBA1A_PIG 1 451
DBREF 6MZG D 1 455 UNP P02554 TBB_PIG 1 445
DBREF 6MZG E 1 554 PDB 6MZG 6MZG 1 554
DBREF 6MZG F 30 169 PDB 6MZG 6MZG 30 169
DBREF 6MZG G 1 451 UNP P02550 TBA1A_PIG 1 451
DBREF 6MZG H 1 455 UNP P02554 TBB_PIG 1 445
DBREF 6MZG I 1 451 UNP P02550 TBA1A_PIG 1 451
DBREF 6MZG J 1 455 UNP P02554 TBB_PIG 1 445
DBREF 6MZG K 1 554 PDB 6MZG 6MZG 1 554
DBREF 6MZG L 30 169 PDB 6MZG 6MZG 30 169
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 SER 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 GLY 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 ALA 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 THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 451 LYS VAL GLY ILE ASN TYR GLU 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 ALA 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 VAL 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 ALA 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 VAL 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 GLY GLU 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 SER 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 GLY 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 ALA 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 THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 451 LYS VAL GLY ILE ASN TYR GLU 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 ALA 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 VAL 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 ALA 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 VAL 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 GLY GLU GLU
SEQRES 35 D 445 ASP GLU ALA
SEQRES 1 E 554 MET ALA ASP GLN ASP ASP VAL ASP PHE THR THR LEU PRO
SEQRES 2 E 554 LEU GLU GLN ARG ALA SER HIS LYS VAL TRP LYS ALA ARG
SEQRES 3 E 554 LEU ASN ALA TYR GLN GLU LEU ASN ASN LEU PHE THR LYS
SEQRES 4 E 554 SER SER VAL ILE SER PRO PRO ASN ASP VAL ALA ASN TYR
SEQRES 5 E 554 TRP LEU ASP PRO GLU LEU PHE ALA SER TYR ILE VAL ASP
SEQRES 6 E 554 SER ASN VAL VAL ALA GLN GLU ASN ALA ILE ILE ALA LEU
SEQRES 7 E 554 HIS THR LEU LEU GLU TYR ILE SER GLN VAL PRO ASN VAL
SEQRES 8 E 554 SER THR SER LYS LEU ARG LEU GLN TRP ILE PRO PRO LEU
SEQRES 9 E 554 VAL GLU LYS GLY LEU SER SER SER ARG ALA ALA THR LYS
SEQRES 10 E 554 ALA LYS ALA THR ASP CYS ILE MET LEU LEU THR GLN SER
SEQRES 11 E 554 ASP THR SER ILE GLN GLN THR VAL ASN LEU MET LEU PRO
SEQRES 12 E 554 SER LEU SER ASN LYS LEU PRO ARG LEU VAL SER SER CYS
SEQRES 13 E 554 VAL LYS CYS LEU ALA THR ILE ILE GLU GLU PHE GLY PHE
SEQRES 14 E 554 ILE ASN VAL SER ASP ILE ASN ILE LEU LEU SER GLU ILE
SEQRES 15 E 554 LEU GLU PRO LEU PRO LYS LEU SER SER HIS ALA ASP ARG
SEQRES 16 E 554 ASN VAL ARG SER GLU THR MET ASN LEU ILE LEU GLN ILE
SEQRES 17 E 554 TYR LYS TRP PHE GLY LYS GLU LEU LEU GLN GLU LEU LEU
SEQRES 18 E 554 LEU GLU LYS LEU LYS PRO ILE GLN GLN ARG ASP LEU SER
SEQRES 19 E 554 ARG MET PHE GLU LYS TYR GLU GLY THR ILE PRO PRO LYS
SEQRES 20 E 554 GLN GLN PRO ARG LEU PHE GLN TRP GLN LYS GLU GLN GLU
SEQRES 21 E 554 GLN GLU GLN GLU GLN ILE LEU GLN THR ASP LYS ASP GLY
SEQRES 22 E 554 ASP THR LEU MET GLY ASN LEU LEU ALA TYR GLN ASP THR
SEQRES 23 E 554 ASN ALA SER ALA ILE HIS PRO ALA THR LYS PRO ALA VAL
SEQRES 24 E 554 ASP PRO PHE GLU LEU LEU PRO PRO SER VAL ILE LEU ASP
SEQRES 25 E 554 LYS PHE PRO ALA ASP PHE GLN THR ARG ILE SER SER THR
SEQRES 26 E 554 LYS TRP LYS ASP ARG VAL GLU ALA LEU GLU GLU ILE HIS
SEQRES 27 E 554 ASN ASN VAL LEU LYS PRO VAL LYS LYS LEU ALA HIS LYS
SEQRES 28 E 554 ASN GLN ASP TYR SER ASP TYR LEU ARG VAL LEU ALA ASN
SEQRES 29 E 554 VAL ILE GLN LYS ASP ALA ASN VAL GLN ALA VAL THR ILE
SEQRES 30 E 554 ALA ALA ASN SER VAL GLN LEU LEU CYS ASN SER LEU ARG
SEQRES 31 E 554 SER ASN PHE THR ARG SER TYR GLY ALA ILE VAL LEU VAL
SEQRES 32 E 554 PRO LEU LEU GLU ARG THR LYS GLU LYS LYS PRO SER VAL
SEQRES 33 E 554 ASN GLU ALA ILE CYS SER ALA LEU ASP ALA VAL ALA THR
SEQRES 34 E 554 TYR CYS GLY PHE ASP ASP CYS LEU GLU GLU THR LEU ASN
SEQRES 35 E 554 TYR MET LYS HIS LYS THR PRO GLN VAL ARG ILE GLU CYS
SEQRES 36 E 554 THR LYS PHE LEU THR ARG MET LEU GLN GLY TRP LYS SER
SEQRES 37 E 554 ASP GLY PRO LEU GLN ASN GLN LEU LEU PHE LYS LEU LEU
SEQRES 38 E 554 PRO GLU VAL THR THR ALA VAL LEU LYS ILE VAL ASN ASP
SEQRES 39 E 554 THR GLN PRO THR THR ARG ASN THR GLY PHE GLU CYS PHE
SEQRES 40 E 554 ALA THR LEU MET LYS LEU VAL GLY GLU ARG GLU LEU ALA
SEQRES 41 E 554 ASP PRO LEU GLU LYS LEU ASP ASN LEU LYS LYS LYS LYS
SEQRES 42 E 554 ILE TYR GLU TYR TYR GLU LYS VAL GLU VAL ALA THR GLY
SEQRES 43 E 554 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 140 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 F 140 THR ASP ALA SER GLY LEU THR PRO LEU HIS LEU ALA ALA
SEQRES 3 F 140 THR TYR GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS
SEQRES 4 F 140 HIS GLY ALA ASP VAL ASN ALA ILE ASP ILE MET GLY SER
SEQRES 5 F 140 THR PRO LEU HIS LEU ALA ALA LEU ILE GLY HIS LEU GLU
SEQRES 6 F 140 ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN
SEQRES 7 F 140 ALA VAL ASP THR TRP GLY ASP THR PRO LEU HIS LEU ALA
SEQRES 8 F 140 ALA ILE MET GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU
SEQRES 9 F 140 LYS HIS GLY ALA ASP VAL ASN ALA GLN ASP LYS PHE GLY
SEQRES 10 F 140 LYS THR ALA PHE ASP ILE SER ILE ASP ASN GLY ASN GLU
SEQRES 11 F 140 ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
SEQRES 1 G 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 G 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 G 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 G 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 G 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 G 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 G 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 G 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 G 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 G 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 G 451 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 G 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 G 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 G 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 G 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 G 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 G 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 G 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 G 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 G 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 G 451 PRO TYR PRO ARG ALA HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 G 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 G 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 G 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 G 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 G 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 G 451 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 G 451 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 G 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 G 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 G 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 G 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 G 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 G 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 G 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 H 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 H 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 H 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 H 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 H 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 H 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 H 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 H 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 H 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 H 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 H 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 H 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 H 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 H 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 H 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 H 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 H 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 H 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 H 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 H 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 H 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 H 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 H 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 H 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 H 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 H 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 H 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 H 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 H 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 H 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 H 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 H 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 H 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 H 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLY GLU GLU
SEQRES 35 H 445 ASP GLU ALA
SEQRES 1 I 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 I 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 I 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 I 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 I 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 I 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 I 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 I 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 I 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 I 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 I 451 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 I 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 I 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 I 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 I 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 I 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 I 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 I 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 I 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 I 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 I 451 PRO TYR PRO ARG ALA HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 I 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 I 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 I 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 I 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 I 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 I 451 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 I 451 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 I 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 I 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 I 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 I 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 I 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 I 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 I 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 J 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 J 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 J 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 J 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 J 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 J 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 J 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 J 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 J 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 J 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 J 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 J 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 J 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 J 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 J 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 J 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 J 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 J 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 J 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 J 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 J 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 J 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 J 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 J 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 J 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 J 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 J 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 J 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 J 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 J 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 J 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 J 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 J 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 J 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLY GLU GLU
SEQRES 35 J 445 ASP GLU ALA
SEQRES 1 K 554 MET ALA ASP GLN ASP ASP VAL ASP PHE THR THR LEU PRO
SEQRES 2 K 554 LEU GLU GLN ARG ALA SER HIS LYS VAL TRP LYS ALA ARG
SEQRES 3 K 554 LEU ASN ALA TYR GLN GLU LEU ASN ASN LEU PHE THR LYS
SEQRES 4 K 554 SER SER VAL ILE SER PRO PRO ASN ASP VAL ALA ASN TYR
SEQRES 5 K 554 TRP LEU ASP PRO GLU LEU PHE ALA SER TYR ILE VAL ASP
SEQRES 6 K 554 SER ASN VAL VAL ALA GLN GLU ASN ALA ILE ILE ALA LEU
SEQRES 7 K 554 HIS THR LEU LEU GLU TYR ILE SER GLN VAL PRO ASN VAL
SEQRES 8 K 554 SER THR SER LYS LEU ARG LEU GLN TRP ILE PRO PRO LEU
SEQRES 9 K 554 VAL GLU LYS GLY LEU SER SER SER ARG ALA ALA THR LYS
SEQRES 10 K 554 ALA LYS ALA THR ASP CYS ILE MET LEU LEU THR GLN SER
SEQRES 11 K 554 ASP THR SER ILE GLN GLN THR VAL ASN LEU MET LEU PRO
SEQRES 12 K 554 SER LEU SER ASN LYS LEU PRO ARG LEU VAL SER SER CYS
SEQRES 13 K 554 VAL LYS CYS LEU ALA THR ILE ILE GLU GLU PHE GLY PHE
SEQRES 14 K 554 ILE ASN VAL SER ASP ILE ASN ILE LEU LEU SER GLU ILE
SEQRES 15 K 554 LEU GLU PRO LEU PRO LYS LEU SER SER HIS ALA ASP ARG
SEQRES 16 K 554 ASN VAL ARG SER GLU THR MET ASN LEU ILE LEU GLN ILE
SEQRES 17 K 554 TYR LYS TRP PHE GLY LYS GLU LEU LEU GLN GLU LEU LEU
SEQRES 18 K 554 LEU GLU LYS LEU LYS PRO ILE GLN GLN ARG ASP LEU SER
SEQRES 19 K 554 ARG MET PHE GLU LYS TYR GLU GLY THR ILE PRO PRO LYS
SEQRES 20 K 554 GLN GLN PRO ARG LEU PHE GLN TRP GLN LYS GLU GLN GLU
SEQRES 21 K 554 GLN GLU GLN GLU GLN ILE LEU GLN THR ASP LYS ASP GLY
SEQRES 22 K 554 ASP THR LEU MET GLY ASN LEU LEU ALA TYR GLN ASP THR
SEQRES 23 K 554 ASN ALA SER ALA ILE HIS PRO ALA THR LYS PRO ALA VAL
SEQRES 24 K 554 ASP PRO PHE GLU LEU LEU PRO PRO SER VAL ILE LEU ASP
SEQRES 25 K 554 LYS PHE PRO ALA ASP PHE GLN THR ARG ILE SER SER THR
SEQRES 26 K 554 LYS TRP LYS ASP ARG VAL GLU ALA LEU GLU GLU ILE HIS
SEQRES 27 K 554 ASN ASN VAL LEU LYS PRO VAL LYS LYS LEU ALA HIS LYS
SEQRES 28 K 554 ASN GLN ASP TYR SER ASP TYR LEU ARG VAL LEU ALA ASN
SEQRES 29 K 554 VAL ILE GLN LYS ASP ALA ASN VAL GLN ALA VAL THR ILE
SEQRES 30 K 554 ALA ALA ASN SER VAL GLN LEU LEU CYS ASN SER LEU ARG
SEQRES 31 K 554 SER ASN PHE THR ARG SER TYR GLY ALA ILE VAL LEU VAL
SEQRES 32 K 554 PRO LEU LEU GLU ARG THR LYS GLU LYS LYS PRO SER VAL
SEQRES 33 K 554 ASN GLU ALA ILE CYS SER ALA LEU ASP ALA VAL ALA THR
SEQRES 34 K 554 TYR CYS GLY PHE ASP ASP CYS LEU GLU GLU THR LEU ASN
SEQRES 35 K 554 TYR MET LYS HIS LYS THR PRO GLN VAL ARG ILE GLU CYS
SEQRES 36 K 554 THR LYS PHE LEU THR ARG MET LEU GLN GLY TRP LYS SER
SEQRES 37 K 554 ASP GLY PRO LEU GLN ASN GLN LEU LEU PHE LYS LEU LEU
SEQRES 38 K 554 PRO GLU VAL THR THR ALA VAL LEU LYS ILE VAL ASN ASP
SEQRES 39 K 554 THR GLN PRO THR THR ARG ASN THR GLY PHE GLU CYS PHE
SEQRES 40 K 554 ALA THR LEU MET LYS LEU VAL GLY GLU ARG GLU LEU ALA
SEQRES 41 K 554 ASP PRO LEU GLU LYS LEU ASP ASN LEU LYS LYS LYS LYS
SEQRES 42 K 554 ILE TYR GLU TYR TYR GLU LYS VAL GLU VAL ALA THR GLY
SEQRES 43 K 554 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 L 140 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 L 140 THR ASP ALA SER GLY LEU THR PRO LEU HIS LEU ALA ALA
SEQRES 3 L 140 THR TYR GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS
SEQRES 4 L 140 HIS GLY ALA ASP VAL ASN ALA ILE ASP ILE MET GLY SER
SEQRES 5 L 140 THR PRO LEU HIS LEU ALA ALA LEU ILE GLY HIS LEU GLU
SEQRES 6 L 140 ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN
SEQRES 7 L 140 ALA VAL ASP THR TRP GLY ASP THR PRO LEU HIS LEU ALA
SEQRES 8 L 140 ALA ILE MET GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU
SEQRES 9 L 140 LYS HIS GLY ALA ASP VAL ASN ALA GLN ASP LYS PHE GLY
SEQRES 10 L 140 LYS THR ALA PHE ASP ILE SER ILE ASP ASN GLY ASN GLU
SEQRES 11 L 140 ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
HET GTP A 600 32
HET MG A 601 1
HET GDP B 600 28
HET MG B 601 1
HET GTP C 600 32
HET MG C 601 1
HET GDP D 600 28
HET MG D 601 1
HET GTP G 600 32
HET MG G 601 1
HET GDP H 600 28
HET MG H 601 1
HET GTP I 600 32
HET MG I 601 1
HET GDP J 600 28
HET MG J 601 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 13 GTP 4(C10 H16 N5 O14 P3)
FORMUL 14 MG 8(MG 2+)
FORMUL 15 GDP 4(C10 H15 N5 O11 P2)
HELIX 1 AA1 GLY A 10 GLY A 29 1 20
HELIX 2 AA2 ASP A 47 THR A 51 5 5
HELIX 3 AA3 PRO A 72 ARG A 79 1 8
HELIX 4 AA4 HIS A 88 GLU A 90 5 3
HELIX 5 AA5 ASN A 102 TYR A 108 1 7
HELIX 6 AA6 ILE A 110 GLU A 113 5 4
HELIX 7 AA7 ILE A 114 GLN A 128 1 15
HELIX 8 AA8 GLY A 143 TYR A 161 1 19
HELIX 9 AA9 VAL A 182 LEU A 195 1 14
HELIX 10 AB1 ASN A 206 LEU A 217 1 12
HELIX 11 AB2 THR A 223 PHE A 244 1 22
HELIX 12 AB3 ASP A 251 VAL A 260 1 10
HELIX 13 AB4 SER A 287 CYS A 295 1 9
HELIX 14 AB5 PHE A 296 GLN A 301 5 6
HELIX 15 AB6 ASP A 306 GLY A 310 5 5
HELIX 16 AB7 VAL A 324 THR A 337 1 14
HELIX 17 AB8 ILE A 384 ALA A 400 1 17
HELIX 18 AB9 PHE A 404 GLY A 410 1 7
HELIX 19 AC1 GLU A 415 VAL A 437 1 23
HELIX 20 AC2 GLY B 10 HIS B 28 1 19
HELIX 21 AC3 ASP B 41 ARG B 48 1 6
HELIX 22 AC4 PRO B 72 SER B 80 1 9
HELIX 23 AC5 ARG B 88 ASP B 90 5 3
HELIX 24 AC6 ASN B 102 TYR B 108 1 7
HELIX 25 AC7 GLY B 111 SER B 128 1 18
HELIX 26 AC8 GLY B 144 TYR B 161 1 18
HELIX 27 AC9 SER B 174 SER B 178 5 5
HELIX 28 AD1 VAL B 182 THR B 198 1 17
HELIX 29 AD2 ASN B 206 THR B 216 1 11
HELIX 30 AD3 THR B 223 THR B 239 1 17
HELIX 31 AD4 THR B 239 PHE B 244 1 6
HELIX 32 AD5 ASP B 251 VAL B 260 1 10
HELIX 33 AD6 THR B 287 PHE B 296 1 10
HELIX 34 AD7 ASP B 297 MET B 301 5 5
HELIX 35 AD8 ASP B 306 GLY B 310 5 5
HELIX 36 AD9 SER B 324 ASN B 339 1 16
HELIX 37 AE1 SER B 340 PHE B 343 5 4
HELIX 38 AE2 ILE B 384 ARG B 400 1 17
HELIX 39 AE3 LEU B 405 GLY B 410 1 6
HELIX 40 AE4 ASP B 414 ALA B 438 1 25
HELIX 41 AE5 GLY C 10 GLY C 29 1 20
HELIX 42 AE6 ASP C 47 THR C 51 5 5
HELIX 43 AE7 PRO C 72 ARG C 79 1 8
HELIX 44 AE8 HIS C 88 GLU C 90 5 3
HELIX 45 AE9 ASN C 102 TYR C 108 1 7
HELIX 46 AF1 ILE C 110 GLN C 128 1 19
HELIX 47 AF2 GLY C 143 TYR C 161 1 19
HELIX 48 AF3 VAL C 182 LEU C 195 1 14
HELIX 49 AF4 ASN C 206 LEU C 217 1 12
HELIX 50 AF5 THR C 223 PHE C 244 1 22
HELIX 51 AF6 ASP C 251 VAL C 260 1 10
HELIX 52 AF7 SER C 287 ALA C 294 1 8
HELIX 53 AF8 CYS C 295 GLN C 301 5 7
HELIX 54 AF9 ASP C 306 GLY C 310 5 5
HELIX 55 AG1 VAL C 324 THR C 337 1 14
HELIX 56 AG2 ILE C 384 ALA C 400 1 17
HELIX 57 AG3 PHE C 404 GLY C 410 1 7
HELIX 58 AG4 GLU C 415 GLY C 436 1 22
HELIX 59 AG5 GLY D 10 HIS D 28 1 19
HELIX 60 AG6 ASP D 41 ARG D 48 1 6
HELIX 61 AG7 PRO D 72 SER D 80 1 9
HELIX 62 AG8 ARG D 88 ASP D 90 5 3
HELIX 63 AG9 ASN D 102 TYR D 108 1 7
HELIX 64 AH1 GLY D 111 SER D 128 1 18
HELIX 65 AH2 GLY D 144 TYR D 161 1 18
HELIX 66 AH3 VAL D 182 THR D 198 1 17
HELIX 67 AH4 ASN D 206 THR D 216 1 11
HELIX 68 AH5 THR D 223 THR D 239 1 17
HELIX 69 AH6 THR D 239 PHE D 244 1 6
HELIX 70 AH7 ASP D 251 VAL D 260 1 10
HELIX 71 AH8 THR D 287 PHE D 296 1 10
HELIX 72 AH9 ASP D 306 GLY D 310 5 5
HELIX 73 AI1 SER D 324 ASN D 339 1 16
HELIX 74 AI2 SER D 340 PHE D 343 5 4
HELIX 75 AI3 ILE D 384 ARG D 400 1 17
HELIX 76 AI4 PHE D 404 GLY D 410 1 7
HELIX 77 AI5 ASP D 414 ALA D 438 1 25
HELIX 78 AI6 LEU E 14 HIS E 20 5 7
HELIX 79 AI7 VAL E 22 SER E 40 1 19
HELIX 80 AI8 ASN E 47 ASN E 51 5 5
HELIX 81 AI9 PRO E 56 ILE E 63 1 8
HELIX 82 AJ1 ASN E 67 ILE E 85 1 19
HELIX 83 AJ2 SER E 92 GLY E 108 1 17
HELIX 84 AJ3 ARG E 113 SER E 130 1 18
HELIX 85 AJ4 ILE E 134 LEU E 142 1 9
HELIX 86 AJ5 PRO E 143 ASN E 147 5 5
HELIX 87 AJ6 LEU E 149 PHE E 167 1 19
HELIX 88 AJ7 ASP E 174 GLU E 184 1 11
HELIX 89 AJ8 PRO E 185 SER E 190 1 6
HELIX 90 AJ9 ASP E 194 PHE E 212 1 19
HELIX 91 AK1 LYS E 214 LEU E 221 1 8
HELIX 92 AK2 LEU E 222 LEU E 225 5 4
HELIX 93 AK3 LYS E 226 LYS E 239 1 14
HELIX 94 AK4 PHE E 253 GLN E 259 1 7
HELIX 95 AK5 LYS E 326 ASN E 340 1 15
HELIX 96 AK6 TYR E 355 ASP E 369 1 15
HELIX 97 AK7 ASN E 371 LEU E 389 1 19
HELIX 98 AK8 ARG E 395 ARG E 408 1 14
HELIX 99 AK9 THR E 409 GLU E 411 5 3
HELIX 100 AL1 LYS E 413 THR E 429 1 17
HELIX 101 AL2 ASP E 435 LYS E 445 1 11
HELIX 102 AL3 THR E 448 GLY E 465 1 18
HELIX 103 AL4 ASN E 474 LYS E 479 1 6
HELIX 104 AL5 GLU E 483 ASN E 493 1 11
HELIX 105 AL6 GLN E 496 VAL E 514 1 19
HELIX 106 AL7 LEU E 519 LYS E 525 1 7
HELIX 107 AL8 ASP E 527 VAL E 541 1 15
HELIX 108 AL9 THR F 49 TYR F 57 1 9
HELIX 109 AM1 HIS F 59 HIS F 69 1 11
HELIX 110 AM2 THR F 82 GLY F 91 1 10
HELIX 111 AM3 HIS F 92 HIS F 102 1 11
HELIX 112 AM4 THR F 115 MET F 123 1 9
HELIX 113 AM5 HIS F 125 HIS F 135 1 11
HELIX 114 AM6 THR F 148 ASN F 156 1 9
HELIX 115 AM7 ASN F 158 LYS F 167 1 10
HELIX 116 AM8 GLY G 10 HIS G 28 1 19
HELIX 117 AM9 ASP G 47 THR G 51 5 5
HELIX 118 AN1 THR G 73 ARG G 79 1 7
HELIX 119 AN2 HIS G 88 GLU G 90 5 3
HELIX 120 AN3 ASN G 102 TYR G 108 1 7
HELIX 121 AN4 ILE G 110 GLN G 128 1 19
HELIX 122 AN5 GLY G 143 TYR G 161 1 19
HELIX 123 AN6 VAL G 182 LEU G 195 1 14
HELIX 124 AN7 ASN G 206 LEU G 217 1 12
HELIX 125 AN8 THR G 223 PHE G 244 1 22
HELIX 126 AN9 ASP G 251 VAL G 260 1 10
HELIX 127 AO1 SER G 287 CYS G 295 1 9
HELIX 128 AO2 PHE G 296 GLN G 301 5 6
HELIX 129 AO3 ASP G 306 GLY G 310 5 5
HELIX 130 AO4 VAL G 324 ARG G 339 1 16
HELIX 131 AO5 ILE G 384 ALA G 400 1 17
HELIX 132 AO6 PHE G 404 GLY G 410 1 7
HELIX 133 AO7 GLU G 415 VAL G 437 1 23
HELIX 134 AO8 GLY H 10 HIS H 28 1 19
HELIX 135 AO9 ASP H 41 ARG H 48 1 6
HELIX 136 AP1 ILE H 49 VAL H 51 5 3
HELIX 137 AP2 PRO H 72 SER H 80 1 9
HELIX 138 AP3 ARG H 88 ASP H 90 5 3
HELIX 139 AP4 ASN H 102 TYR H 108 1 7
HELIX 140 AP5 GLY H 111 SER H 128 1 18
HELIX 141 AP6 GLY H 144 TYR H 161 1 18
HELIX 142 AP7 SER H 174 SER H 178 5 5
HELIX 143 AP8 VAL H 182 THR H 198 1 17
HELIX 144 AP9 ASN H 206 THR H 216 1 11
HELIX 145 AQ1 THR H 223 THR H 239 1 17
HELIX 146 AQ2 THR H 239 PHE H 244 1 6
HELIX 147 AQ3 ASP H 251 VAL H 260 1 10
HELIX 148 AQ4 THR H 287 PHE H 296 1 10
HELIX 149 AQ5 ASP H 297 MET H 301 5 5
HELIX 150 AQ6 ASP H 306 GLY H 310 5 5
HELIX 151 AQ7 SER H 324 ASN H 339 1 16
HELIX 152 AQ8 SER H 340 PHE H 343 5 4
HELIX 153 AQ9 ILE H 384 ARG H 400 1 17
HELIX 154 AR1 LEU H 405 GLY H 410 1 6
HELIX 155 AR2 ASP H 414 ALA H 438 1 25
HELIX 156 AR3 GLY I 10 GLY I 29 1 20
HELIX 157 AR4 ASP I 47 THR I 51 5 5
HELIX 158 AR5 PRO I 72 ARG I 79 1 8
HELIX 159 AR6 HIS I 88 GLU I 90 5 3
HELIX 160 AR7 ASN I 102 TYR I 108 1 7
HELIX 161 AR8 ILE I 110 GLN I 128 1 19
HELIX 162 AR9 GLY I 143 TYR I 161 1 19
HELIX 163 AS1 VAL I 182 LEU I 195 1 14
HELIX 164 AS2 ASN I 206 LEU I 217 1 12
HELIX 165 AS3 THR I 223 PHE I 244 1 22
HELIX 166 AS4 ASP I 251 VAL I 260 1 10
HELIX 167 AS5 SER I 287 CYS I 295 1 9
HELIX 168 AS6 PHE I 296 GLN I 301 5 6
HELIX 169 AS7 ASP I 306 GLY I 310 5 5
HELIX 170 AS8 VAL I 324 THR I 337 1 14
HELIX 171 AS9 ILE I 384 ALA I 400 1 17
HELIX 172 AT1 PHE I 404 GLY I 410 1 7
HELIX 173 AT2 GLU I 415 GLY I 436 1 22
HELIX 174 AT3 GLY J 10 HIS J 28 1 19
HELIX 175 AT4 ASP J 41 ARG J 48 1 6
HELIX 176 AT5 PRO J 72 SER J 80 1 9
HELIX 177 AT6 ARG J 88 ASP J 90 5 3
HELIX 178 AT7 ASN J 102 TYR J 108 1 7
HELIX 179 AT8 GLY J 111 SER J 128 1 18
HELIX 180 AT9 GLY J 144 TYR J 161 1 18
HELIX 181 AU1 VAL J 182 THR J 198 1 17
HELIX 182 AU2 ASN J 206 THR J 216 1 11
HELIX 183 AU3 THR J 223 THR J 239 1 17
HELIX 184 AU4 THR J 239 PHE J 244 1 6
HELIX 185 AU5 ASP J 251 VAL J 260 1 10
HELIX 186 AU6 THR J 287 GLN J 293 1 7
HELIX 187 AU7 ASP J 297 MET J 301 5 5
HELIX 188 AU8 ASP J 306 GLY J 310 5 5
HELIX 189 AU9 SER J 324 ASN J 339 1 16
HELIX 190 AV1 SER J 340 PHE J 343 5 4
HELIX 191 AV2 ILE J 384 ARG J 400 1 17
HELIX 192 AV3 PHE J 404 GLY J 410 1 7
HELIX 193 AV4 ASP J 414 ALA J 438 1 25
HELIX 194 AV5 LEU K 14 HIS K 20 5 7
HELIX 195 AV6 VAL K 22 LYS K 39 1 18
HELIX 196 AV7 PRO K 56 ILE K 63 1 8
HELIX 197 AV8 ASN K 67 ILE K 85 1 19
HELIX 198 AV9 SER K 92 GLY K 108 1 17
HELIX 199 AW1 ARG K 113 SER K 130 1 18
HELIX 200 AW2 ILE K 134 LEU K 142 1 9
HELIX 201 AW3 PRO K 143 ASN K 147 5 5
HELIX 202 AW4 LEU K 149 GLU K 166 1 18
HELIX 203 AW5 ASP K 174 GLU K 184 1 11
HELIX 204 AW6 PRO K 185 SER K 190 1 6
HELIX 205 AW7 ASP K 194 LYS K 210 1 17
HELIX 206 AW8 LYS K 214 LEU K 221 1 8
HELIX 207 AW9 LEU K 222 LEU K 225 5 4
HELIX 208 AX1 LYS K 226 TYR K 240 1 15
HELIX 209 AX2 PHE K 253 GLN K 259 1 7
HELIX 210 AX3 LYS K 326 ASN K 340 1 15
HELIX 211 AX4 TYR K 355 ASP K 369 1 15
HELIX 212 AX5 ASN K 371 LEU K 389 1 19
HELIX 213 AX6 VAL K 401 ARG K 408 1 8
HELIX 214 AX7 THR K 409 GLU K 411 5 3
HELIX 215 AX8 LYS K 413 GLY K 432 1 20
HELIX 216 AX9 ASP K 435 LYS K 445 1 11
HELIX 217 AY1 THR K 448 GLY K 465 1 18
HELIX 218 AY2 LEU K 476 LEU K 481 1 6
HELIX 219 AY3 GLU K 483 ASN K 493 1 11
HELIX 220 AY4 GLN K 496 VAL K 514 1 19
HELIX 221 AY5 GLY K 515 GLU K 518 5 4
HELIX 222 AY6 LEU K 519 LYS K 525 1 7
HELIX 223 AY7 ASP K 527 VAL K 541 1 15
HELIX 224 AY8 THR L 49 TYR L 57 1 9
HELIX 225 AY9 HIS L 59 HIS L 69 1 11
HELIX 226 AZ1 THR L 82 GLY L 91 1 10
HELIX 227 AZ2 HIS L 92 HIS L 102 1 11
HELIX 228 AZ3 THR L 115 MET L 123 1 9
HELIX 229 AZ4 HIS L 125 HIS L 135 1 11
HELIX 230 AZ5 THR L 148 ASN L 156 1 9
HELIX 231 AZ6 ASN L 158 LEU L 165 1 8
SHEET 1 AA1 6 LEU A 92 THR A 94 0
SHEET 2 AA1 6 ALA A 65 ASP A 69 1 N PHE A 67 O ILE A 93
SHEET 3 AA1 6 GLU A 3 VAL A 9 1 N HIS A 8 O VAL A 68
SHEET 4 AA1 6 LEU A 132 SER A 140 1 O SER A 136 N ILE A 7
SHEET 5 AA1 6 SER A 165 TYR A 172 1 O LEU A 167 N VAL A 137
SHEET 6 AA1 6 CYS A 200 ASP A 205 1 O PHE A 202 N GLU A 168
SHEET 1 AA2 2 PHE A 53 GLU A 55 0
SHEET 2 AA2 2 HIS A 61 PRO A 63 -1 O VAL A 62 N SER A 54
SHEET 1 AA3 4 LEU A 269 ALA A 273 0
SHEET 2 AA3 4 ARG A 373 THR A 381 -1 O MET A 377 N THR A 271
SHEET 3 AA3 4 TYR A 312 GLY A 321 -1 N CYS A 316 O LEU A 378
SHEET 4 AA3 4 LYS A 352 ASN A 356 1 O LYS A 352 N LEU A 317
SHEET 1 AA410 PHE B 92 PHE B 94 0
SHEET 2 AA410 ALA B 65 ASP B 69 1 N LEU B 67 O VAL B 93
SHEET 3 AA410 GLU B 3 ALA B 9 1 N GLN B 8 O VAL B 68
SHEET 4 AA410 LEU B 132 SER B 140 1 O GLN B 133 N GLU B 3
SHEET 5 AA410 ILE B 165 VAL B 172 1 O PHE B 169 N LEU B 137
SHEET 6 AA410 GLU B 200 ASP B 205 1 O ILE B 204 N VAL B 172
SHEET 7 AA410 PHE B 267 ALA B 273 1 O PHE B 268 N THR B 201
SHEET 8 AA410 SER B 374 SER B 381 -1 O PHE B 377 N GLY B 271
SHEET 9 AA410 TYR B 312 ARG B 320 -1 N ALA B 316 O ILE B 378
SHEET 10 AA410 VAL B 351 CYS B 356 1 O LYS B 352 N ALA B 317
SHEET 1 AA5 2 TYR B 53 ASN B 54 0
SHEET 2 AA5 2 VAL B 62 PRO B 63 -1 O VAL B 62 N ASN B 54
SHEET 1 AA6 6 LEU C 92 THR C 94 0
SHEET 2 AA6 6 ALA C 65 ASP C 69 1 N PHE C 67 O ILE C 93
SHEET 3 AA6 6 GLU C 3 VAL C 9 1 N HIS C 8 O VAL C 68
SHEET 4 AA6 6 LEU C 132 SER C 140 1 O SER C 136 N ILE C 7
SHEET 5 AA6 6 SER C 165 TYR C 172 1 O LEU C 167 N VAL C 137
SHEET 6 AA6 6 CYS C 200 ASP C 205 1 O PHE C 202 N GLU C 168
SHEET 1 AA7 2 PHE C 53 GLU C 55 0
SHEET 2 AA7 2 HIS C 61 PRO C 63 -1 O VAL C 62 N SER C 54
SHEET 1 AA8 4 LEU C 269 ALA C 273 0
SHEET 2 AA8 4 ARG C 373 THR C 381 -1 O SER C 379 N LEU C 269
SHEET 3 AA8 4 TYR C 312 GLY C 321 -1 N CYS C 316 O LEU C 378
SHEET 4 AA8 4 LYS C 352 ASN C 356 1 O LYS C 352 N LEU C 317
SHEET 1 AA910 PHE D 92 PHE D 94 0
SHEET 2 AA910 ALA D 65 ASP D 69 1 N LEU D 67 O VAL D 93
SHEET 3 AA910 GLU D 3 ALA D 9 1 N GLN D 8 O VAL D 68
SHEET 4 AA910 LEU D 132 SER D 140 1 O GLN D 133 N GLU D 3
SHEET 5 AA910 ILE D 165 VAL D 172 1 O PHE D 169 N LEU D 137
SHEET 6 AA910 GLU D 200 ASP D 205 1 O ILE D 204 N VAL D 172
SHEET 7 AA910 PHE D 267 ALA D 273 1 O PHE D 268 N THR D 201
SHEET 8 AA910 SER D 374 SER D 381 -1 O GLY D 379 N MET D 269
SHEET 9 AA910 TYR D 312 ARG D 320 -1 N ALA D 316 O ILE D 378
SHEET 10 AA910 VAL D 351 CYS D 356 1 O LYS D 352 N ALA D 317
SHEET 1 AB1 2 TYR D 53 ASN D 54 0
SHEET 2 AB1 2 VAL D 62 PRO D 63 -1 O VAL D 62 N ASN D 54
SHEET 1 AB2 6 LEU G 92 THR G 94 0
SHEET 2 AB2 6 ALA G 65 ASP G 69 1 N PHE G 67 O ILE G 93
SHEET 3 AB2 6 GLU G 3 VAL G 9 1 N HIS G 8 O VAL G 68
SHEET 4 AB2 6 LEU G 132 SER G 140 1 O PHE G 138 N ILE G 7
SHEET 5 AB2 6 SER G 165 TYR G 172 1 O LEU G 167 N VAL G 137
SHEET 6 AB2 6 CYS G 200 ASP G 205 1 O PHE G 202 N GLU G 168
SHEET 1 AB3 2 PHE G 53 GLU G 55 0
SHEET 2 AB3 2 HIS G 61 PRO G 63 -1 O VAL G 62 N SER G 54
SHEET 1 AB4 4 LEU G 269 ALA G 273 0
SHEET 2 AB4 4 ARG G 373 THR G 381 -1 O SER G 379 N LEU G 269
SHEET 3 AB4 4 TYR G 312 GLY G 321 -1 N CYS G 316 O LEU G 378
SHEET 4 AB4 4 LYS G 352 ASN G 356 1 O LYS G 352 N LEU G 317
SHEET 1 AB510 PHE H 92 PHE H 94 0
SHEET 2 AB510 ALA H 65 ASP H 69 1 N LEU H 67 O VAL H 93
SHEET 3 AB510 GLU H 3 ALA H 9 1 N GLN H 8 O VAL H 68
SHEET 4 AB510 LEU H 132 SER H 140 1 O GLN H 133 N GLU H 3
SHEET 5 AB510 ILE H 165 VAL H 172 1 O PHE H 169 N LEU H 137
SHEET 6 AB510 GLU H 200 ASP H 205 1 O ILE H 204 N VAL H 172
SHEET 7 AB510 PHE H 267 ALA H 273 1 O PHE H 268 N THR H 201
SHEET 8 AB510 SER H 374 SER H 381 -1 O PHE H 377 N GLY H 271
SHEET 9 AB510 TYR H 312 ARG H 320 -1 N ALA H 316 O ILE H 378
SHEET 10 AB510 VAL H 351 CYS H 356 1 O LYS H 352 N ALA H 317
SHEET 1 AB6 2 TYR H 53 GLU H 55 0
SHEET 2 AB6 2 TYR H 61 PRO H 63 -1 O VAL H 62 N ASN H 54
SHEET 1 AB7 6 LEU I 92 THR I 94 0
SHEET 2 AB7 6 ALA I 65 ASP I 69 1 N PHE I 67 O ILE I 93
SHEET 3 AB7 6 GLU I 3 VAL I 9 1 N HIS I 8 O VAL I 68
SHEET 4 AB7 6 LEU I 132 SER I 140 1 O SER I 136 N ILE I 7
SHEET 5 AB7 6 SER I 165 TYR I 172 1 O LEU I 167 N VAL I 137
SHEET 6 AB7 6 CYS I 200 ASP I 205 1 O PHE I 202 N GLU I 168
SHEET 1 AB8 2 PHE I 53 GLU I 55 0
SHEET 2 AB8 2 HIS I 61 PRO I 63 -1 O VAL I 62 N SER I 54
SHEET 1 AB9 4 LEU I 269 ALA I 273 0
SHEET 2 AB9 4 ARG I 373 THR I 381 -1 O MET I 377 N THR I 271
SHEET 3 AB9 4 TYR I 312 GLY I 321 -1 N CYS I 316 O LEU I 378
SHEET 4 AB9 4 LYS I 352 ASN I 356 1 O LYS I 352 N LEU I 317
SHEET 1 AC110 PHE J 92 PHE J 94 0
SHEET 2 AC110 ALA J 65 ASP J 69 1 N LEU J 67 O VAL J 93
SHEET 3 AC110 GLU J 3 ALA J 9 1 N GLN J 8 O VAL J 68
SHEET 4 AC110 LEU J 132 SER J 140 1 O GLN J 133 N GLU J 3
SHEET 5 AC110 ILE J 165 VAL J 172 1 O PHE J 169 N LEU J 137
SHEET 6 AC110 GLU J 200 ASP J 205 1 O ILE J 204 N VAL J 172
SHEET 7 AC110 PHE J 267 ALA J 273 1 O PHE J 268 N THR J 201
SHEET 8 AC110 SER J 374 SER J 381 -1 O PHE J 377 N GLY J 271
SHEET 9 AC110 TYR J 312 ARG J 320 -1 N ALA J 316 O ILE J 378
SHEET 10 AC110 VAL J 351 CYS J 356 1 O LYS J 352 N ALA J 317
SHEET 1 AC2 2 TYR J 53 ASN J 54 0
SHEET 2 AC2 2 VAL J 62 PRO J 63 -1 O VAL J 62 N ASN J 54
LINK O1G GTP A 600 MG MG A 601 1555 1555 2.50
LINK O1B GTP A 600 MG MG A 601 1555 1555 2.11
LINK OE1 GLN B 11 MG MG B 601 1555 1555 2.25
LINK O1A GDP B 600 MG MG B 601 1555 1555 2.12
LINK O1G GTP C 600 MG MG C 601 1555 1555 2.65
LINK O1B GTP C 600 MG MG C 601 1555 1555 2.27
LINK O1A GDP D 600 MG MG D 601 1555 1555 2.35
LINK O3G GTP G 600 MG MG G 601 1555 1555 2.11
LINK O2B GTP G 600 MG MG G 601 1555 1555 2.60
LINK OD2 ASP H 179 MG MG H 601 1555 1555 2.88
LINK O2A GDP H 600 MG MG H 601 1555 1555 2.54
LINK O3G GTP I 600 MG MG I 601 1555 1555 2.28
LINK O2B GTP I 600 MG MG I 601 1555 1555 2.73
LINK OE1 GLN J 11 MG MG J 601 1555 1555 2.57
LINK O2A GDP J 600 MG MG J 601 1555 1555 2.27
CISPEP 1 ALA A 273 PRO A 274 0 -1.42
CISPEP 2 ALA B 273 PRO B 274 0 -2.46
CISPEP 3 ALA C 273 PRO C 274 0 -1.50
CISPEP 4 ALA D 273 PRO D 274 0 -1.52
CISPEP 5 VAL E 88 PRO E 89 0 -5.54
CISPEP 6 GLY E 470 PRO E 471 0 -4.01
CISPEP 7 ALA G 273 PRO G 274 0 -1.80
CISPEP 8 ALA H 273 PRO H 274 0 -2.07
CISPEP 9 ALA I 273 PRO I 274 0 -2.50
CISPEP 10 ALA J 273 PRO J 274 0 -2.81
CISPEP 11 VAL K 88 PRO K 89 0 -1.62
SITE 1 AC1 20 GLY A 10 GLN A 11 ALA A 12 GLN A 15
SITE 2 AC1 20 ASP A 98 ALA A 99 ALA A 100 ASN A 101
SITE 3 AC1 20 SER A 140 GLY A 143 GLY A 144 THR A 145
SITE 4 AC1 20 GLY A 146 VAL A 177 GLU A 183 ASN A 206
SITE 5 AC1 20 TYR A 224 ASN A 228 MG A 601 LYS B 254
SITE 1 AC2 2 GLU A 71 GTP A 600
SITE 1 AC3 16 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC3 16 ASN B 101 SER B 140 GLY B 143 GLY B 144
SITE 3 AC3 16 THR B 145 GLY B 146 VAL B 177 GLU B 183
SITE 4 AC3 16 ASN B 206 TYR B 224 ASN B 228 MG B 601
SITE 1 AC4 3 GLN B 11 ASP B 179 GDP B 600
SITE 1 AC5 21 GLY C 10 GLN C 11 ALA C 12 GLN C 15
SITE 2 AC5 21 ASP C 98 ALA C 99 ALA C 100 ASN C 101
SITE 3 AC5 21 SER C 140 GLY C 143 GLY C 144 THR C 145
SITE 4 AC5 21 GLY C 146 VAL C 177 GLU C 183 ASN C 206
SITE 5 AC5 21 TYR C 224 ASN C 228 ILE C 231 MG C 601
SITE 6 AC5 21 LYS D 254
SITE 1 AC6 2 GLU C 71 GTP C 600
SITE 1 AC7 16 GLY D 10 GLN D 11 CYS D 12 GLN D 15
SITE 2 AC7 16 ASN D 101 SER D 140 GLY D 143 GLY D 144
SITE 3 AC7 16 THR D 145 GLY D 146 VAL D 177 GLU D 183
SITE 4 AC7 16 ASN D 206 TYR D 224 ASN D 228 MG D 601
SITE 1 AC8 2 GLN D 11 GDP D 600
SITE 1 AC9 22 GLY G 10 GLN G 11 ALA G 12 GLN G 15
SITE 2 AC9 22 ASP G 98 ALA G 99 ALA G 100 ASN G 101
SITE 3 AC9 22 SER G 140 GLY G 143 GLY G 144 THR G 145
SITE 4 AC9 22 GLY G 146 ILE G 171 VAL G 177 GLU G 183
SITE 5 AC9 22 ASN G 206 TYR G 224 ASN G 228 ILE G 231
SITE 6 AC9 22 MG G 601 LYS H 254
SITE 1 AD1 2 GLU G 71 GTP G 600
SITE 1 AD2 17 GLY H 10 GLN H 11 CYS H 12 GLN H 15
SITE 2 AD2 17 ASN H 101 SER H 140 GLY H 143 GLY H 144
SITE 3 AD2 17 THR H 145 GLY H 146 VAL H 177 ASP H 179
SITE 4 AD2 17 GLU H 183 ASN H 206 TYR H 224 ASN H 228
SITE 5 AD2 17 MG H 601
SITE 1 AD3 4 GLN H 11 ASN H 101 ASP H 179 GDP H 600
SITE 1 AD4 20 GLY I 10 GLN I 11 ALA I 12 GLN I 15
SITE 2 AD4 20 ASP I 98 ALA I 99 ALA I 100 ASN I 101
SITE 3 AD4 20 SER I 140 GLY I 143 GLY I 144 THR I 145
SITE 4 AD4 20 GLY I 146 VAL I 177 GLU I 183 ASN I 206
SITE 5 AD4 20 TYR I 224 ASN I 228 MG I 601 LYS J 254
SITE 1 AD5 2 GLU I 71 GTP I 600
SITE 1 AD6 17 GLY J 10 GLN J 11 CYS J 12 GLN J 15
SITE 2 AD6 17 ASN J 101 SER J 140 GLY J 143 GLY J 144
SITE 3 AD6 17 THR J 145 GLY J 146 PRO J 173 VAL J 177
SITE 4 AD6 17 GLU J 183 ASN J 206 TYR J 224 ASN J 228
SITE 5 AD6 17 MG J 601
SITE 1 AD7 2 GLN J 11 GDP J 600
CRYST1 115.130 194.990 149.570 90.00 90.19 90.00 P 1 21 1 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 0.008686 0.000000 0.000029 0.00000
SCALE2 0.000000 0.005128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006686 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
