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HEADER HYDROLASE 10-JAN-19 6QGA
TITLE CRYSTAL STRUCTURE OF A PLASTIC DEGRADING ENZYME IN COMPLEX WITH A NON-
TITLE 2 HYDROLYZABLE SUBSTRATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_0224;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PLASTIC-DEGRADING HYDROLASE, ALPHA/BETA HYDROLASE FOLD, I. SAKAIENSIS
KEYWDS 2 CATALYTIC TRIAD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.PALM,L.REISKY,D.BOETTCHER,H.MUELLER,E.A.P.MICHELS,C.WALCZAK,
AUTHOR 2 L.BERNDT,M.S.WEISS,U.T.BORNSCHEUER,G.WEBER
REVDAT 1 03-APR-19 6QGA 0
JRNL AUTH G.J.PALM,L.REISKY,D.BOETTCHER,H.MUELLER,E.A.P.MICHELS,
JRNL AUTH 2 C.WALCZAK,L.BERNDT,M.S.WEISS,U.T.BORNSCHEUER,G.WEBER
JRNL TITL STRUCTURE OF THE PLASTIC-DEGRADING I. SAKAIENSIS MHETASE
JRNL TITL 2 BOUND TO A SUBSTRATE
JRNL REF NAT COMMUN 2019
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-019-09326-3
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 293303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3081
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 49.1208 - 5.8738 0.99 13918 148 0.1585 0.1825
REMARK 3 2 5.8738 - 4.6633 1.00 13570 144 0.1450 0.1422
REMARK 3 3 4.6633 - 4.0742 1.00 13484 144 0.1191 0.1544
REMARK 3 4 4.0742 - 3.7018 1.00 13415 142 0.1292 0.1473
REMARK 3 5 3.7018 - 3.4366 1.00 13415 142 0.1374 0.1926
REMARK 3 6 3.4366 - 3.2340 1.00 13345 142 0.1520 0.1654
REMARK 3 7 3.2340 - 3.0721 1.00 13325 141 0.1600 0.1836
REMARK 3 8 3.0721 - 2.9383 1.00 13336 142 0.1638 0.1779
REMARK 3 9 2.9383 - 2.8252 1.00 13286 141 0.1721 0.2058
REMARK 3 10 2.8252 - 2.7278 1.00 13289 141 0.1783 0.2066
REMARK 3 11 2.7278 - 2.6425 1.00 13346 141 0.2021 0.2416
REMARK 3 12 2.6425 - 2.5669 1.00 13245 141 0.2120 0.2297
REMARK 3 13 2.5669 - 2.4994 1.00 13216 140 0.2155 0.2404
REMARK 3 14 2.4994 - 2.4384 1.00 13239 141 0.2172 0.2278
REMARK 3 15 2.4384 - 2.3830 1.00 13283 141 0.2198 0.2749
REMARK 3 16 2.3830 - 2.3323 1.00 13233 140 0.2277 0.2615
REMARK 3 17 2.3323 - 2.2856 1.00 13238 141 0.2319 0.2567
REMARK 3 18 2.2856 - 2.2425 1.00 13186 140 0.2317 0.2627
REMARK 3 19 2.2425 - 2.2024 1.00 13255 141 0.2493 0.2578
REMARK 3 20 2.2024 - 2.1651 0.99 13065 138 0.2701 0.2710
REMARK 3 21 2.1651 - 2.1302 0.94 12395 132 0.2824 0.3297
REMARK 3 22 2.1302 - 2.0974 0.84 11138 118 0.3080 0.3547
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 25645
REMARK 3 ANGLE : 1.040 34933
REMARK 3 CHIRALITY : 0.062 3645
REMARK 3 PLANARITY : 0.008 4665
REMARK 3 DIHEDRAL : 13.561 15024
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2712 1.3063 -64.7117
REMARK 3 T TENSOR
REMARK 3 T11: 0.2914 T22: 0.2767
REMARK 3 T33: 0.3117 T12: 0.0591
REMARK 3 T13: -0.0447 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.8812 L22: 1.1391
REMARK 3 L33: 0.7220 L12: 0.9151
REMARK 3 L13: 0.3084 L23: -0.0698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0481 S12: 0.0254 S13: 0.2079
REMARK 3 S21: -0.0368 S22: -0.0353 S23: 0.2365
REMARK 3 S31: -0.1882 S32: -0.1262 S33: 0.0667
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2567 -19.6148 -45.3504
REMARK 3 T TENSOR
REMARK 3 T11: 0.3031 T22: 0.3773
REMARK 3 T33: 0.3242 T12: -0.0386
REMARK 3 T13: -0.0198 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.4725 L22: 0.6988
REMARK 3 L33: 0.7719 L12: 0.2261
REMARK 3 L13: 0.4458 L23: 0.0140
REMARK 3 S TENSOR
REMARK 3 S11: 0.1237 S12: -0.4368 S13: -0.2063
REMARK 3 S21: 0.2224 S22: -0.1128 S23: -0.0053
REMARK 3 S31: 0.0752 S32: -0.2213 S33: -0.0138
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 524 THROUGH 602 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5448 -11.1397 -50.3382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2660 T22: 0.3094
REMARK 3 T33: 0.3504 T12: -0.0073
REMARK 3 T13: -0.0264 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.6061 L22: 0.6814
REMARK 3 L33: 2.0555 L12: -0.1683
REMARK 3 L13: 1.1080 L23: -0.0705
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: -0.1022 S13: -0.0561
REMARK 3 S21: 0.0744 S22: -0.0392 S23: -0.1207
REMARK 3 S31: -0.0290 S32: 0.1111 S33: -0.0049
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7120 -25.8581 19.5382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2594 T22: 0.2529
REMARK 3 T33: 0.2603 T12: -0.0075
REMARK 3 T13: 0.0232 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.6185 L22: 0.2871
REMARK 3 L33: 1.3751 L12: -0.1840
REMARK 3 L13: 0.7622 L23: 0.0300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0218 S12: -0.2094 S13: -0.0709
REMARK 3 S21: 0.1260 S22: 0.0190 S23: 0.0668
REMARK 3 S31: 0.0641 S32: -0.1705 S33: 0.0187
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8460 -33.9887 -5.7761
REMARK 3 T TENSOR
REMARK 3 T11: 0.2373 T22: 0.2361
REMARK 3 T33: 0.2614 T12: 0.0020
REMARK 3 T13: -0.0036 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.7461 L22: 0.5000
REMARK 3 L33: 0.8282 L12: 0.0624
REMARK 3 L13: 0.3034 L23: 0.1947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: 0.0948 S13: -0.1178
REMARK 3 S21: 0.0118 S22: -0.0004 S23: -0.0310
REMARK 3 S31: 0.1291 S32: 0.0671 S33: -0.0482
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5502 6.9518 19.1949
REMARK 3 T TENSOR
REMARK 3 T11: 0.3006 T22: 0.2385
REMARK 3 T33: 0.2741 T12: -0.0000
REMARK 3 T13: -0.0119 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 2.1213 L22: 0.5252
REMARK 3 L33: 1.2782 L12: -0.2841
REMARK 3 L13: -0.9197 L23: -0.0893
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.2049 S13: 0.0501
REMARK 3 S21: 0.1440 S22: 0.0292 S23: -0.0610
REMARK 3 S31: -0.1309 S32: 0.1217 S33: -0.0050
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8911 14.8317 -7.9410
REMARK 3 T TENSOR
REMARK 3 T11: 0.3249 T22: 0.2755
REMARK 3 T33: 0.2724 T12: 0.0106
REMARK 3 T13: 0.0249 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.1031 L22: 0.8365
REMARK 3 L33: 0.8320 L12: 0.0770
REMARK 3 L13: -0.2451 L23: -0.3173
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.2247 S13: 0.1719
REMARK 3 S21: -0.0924 S22: 0.0031 S23: -0.0277
REMARK 3 S31: -0.1942 S32: -0.0633 S33: -0.0120
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6088 14.0867 0.8809
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.3447
REMARK 3 T33: 0.2971 T12: 0.0558
REMARK 3 T13: 0.0267 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.7261 L22: 3.3618
REMARK 3 L33: 2.2450 L12: -1.0588
REMARK 3 L13: 0.4461 L23: -0.8613
REMARK 3 S TENSOR
REMARK 3 S11: 0.0679 S12: 0.2064 S13: 0.0862
REMARK 3 S21: -0.1153 S22: -0.0216 S23: 0.2644
REMARK 3 S31: -0.2652 S32: -0.3083 S33: -0.0660
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5184 13.0971 -65.0964
REMARK 3 T TENSOR
REMARK 3 T11: 0.2921 T22: 0.2808
REMARK 3 T33: 0.2956 T12: 0.0537
REMARK 3 T13: 0.0190 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 2.3000 L22: 0.9740
REMARK 3 L33: 0.8400 L12: 0.9367
REMARK 3 L13: -0.0630 L23: 0.2326
REMARK 3 S TENSOR
REMARK 3 S11: -0.0645 S12: 0.0496 S13: -0.1887
REMARK 3 S21: -0.0358 S22: 0.0369 S23: -0.1941
REMARK 3 S31: 0.1690 S32: 0.1708 S33: 0.0044
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.5517 31.3599 -42.9828
REMARK 3 T TENSOR
REMARK 3 T11: 0.2964 T22: 0.3264
REMARK 3 T33: 0.2635 T12: -0.0016
REMARK 3 T13: -0.0398 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 1.0269 L22: 0.5221
REMARK 3 L33: 0.8537 L12: 0.0077
REMARK 3 L13: -0.4033 L23: 0.0818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.2659 S13: 0.0313
REMARK 3 S21: 0.1709 S22: -0.0048 S23: -0.0565
REMARK 3 S31: -0.0054 S32: 0.2825 S33: 0.0011
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9158 23.7307 -48.0563
REMARK 3 T TENSOR
REMARK 3 T11: 0.2574 T22: 0.2485
REMARK 3 T33: 0.2859 T12: -0.0113
REMARK 3 T13: -0.0176 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.9785 L22: 1.2871
REMARK 3 L33: 3.3168 L12: 0.0001
REMARK 3 L13: -1.5132 L23: -0.4045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.0232 S13: -0.0364
REMARK 3 S21: 0.1488 S22: -0.0144 S23: 0.1739
REMARK 3 S31: 0.0873 S32: -0.1326 S33: 0.0209
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3437 -31.7306 31.3361
REMARK 3 T TENSOR
REMARK 3 T11: 0.2594 T22: 0.2495
REMARK 3 T33: 0.2120 T12: -0.0293
REMARK 3 T13: 0.0255 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.8218 L22: 0.7846
REMARK 3 L33: 0.7191 L12: -0.4175
REMARK 3 L13: 0.7532 L23: -0.1807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0535 S12: 0.1109 S13: 0.1177
REMARK 3 S21: -0.1027 S22: 0.0339 S23: -0.0544
REMARK 3 S31: -0.0791 S32: 0.0666 S33: 0.0286
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 213 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3745 -58.3621 37.9201
REMARK 3 T TENSOR
REMARK 3 T11: 0.2652 T22: 0.2621
REMARK 3 T33: 0.2266 T12: -0.0253
REMARK 3 T13: 0.0032 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.7957 L22: 0.6621
REMARK 3 L33: 0.3030 L12: 0.0156
REMARK 3 L13: 0.1122 L23: -0.0089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: -0.0281 S13: -0.1351
REMARK 3 S21: -0.0511 S22: 0.0348 S23: 0.0416
REMARK 3 S31: 0.0830 S32: -0.0468 S33: -0.0093
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 334 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1902 -59.1863 41.0387
REMARK 3 T TENSOR
REMARK 3 T11: 0.2671 T22: 0.2640
REMARK 3 T33: 0.2381 T12: -0.0130
REMARK 3 T13: 0.0102 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 1.1125 L22: 1.0620
REMARK 3 L33: 0.4572 L12: -0.1560
REMARK 3 L13: -0.0782 L23: 0.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0516 S12: -0.0462 S13: -0.1621
REMARK 3 S21: -0.0172 S22: 0.0667 S23: -0.0460
REMARK 3 S31: 0.1156 S32: -0.0140 S33: -0.0125
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0533 -50.6729 33.8303
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.2977
REMARK 3 T33: 0.2765 T12: -0.0216
REMARK 3 T13: -0.0317 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 1.4795 L22: 3.3771
REMARK 3 L33: 2.3015 L12: 0.7530
REMARK 3 L13: 0.1151 L23: 1.7768
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: 0.0298 S13: -0.0740
REMARK 3 S21: -0.1324 S22: 0.0314 S23: 0.2981
REMARK 3 S31: 0.0918 S32: -0.2520 S33: 0.0603
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5314 -13.4537 -94.1232
REMARK 3 T TENSOR
REMARK 3 T11: 0.3230 T22: 0.3030
REMARK 3 T33: 0.2734 T12: -0.0299
REMARK 3 T13: 0.0019 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.1328 L22: 1.2094
REMARK 3 L33: 0.5655 L12: -0.6574
REMARK 3 L13: 0.8265 L23: -0.2052
REMARK 3 S TENSOR
REMARK 3 S11: -0.0726 S12: 0.1693 S13: 0.1502
REMARK 3 S21: -0.1641 S22: 0.0135 S23: -0.1395
REMARK 3 S31: -0.1351 S32: 0.1416 S33: 0.0713
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 213 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8590 -39.8360 -89.1605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2871 T22: 0.2607
REMARK 3 T33: 0.2595 T12: 0.0106
REMARK 3 T13: 0.0118 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.9611 L22: 1.0588
REMARK 3 L33: 0.5325 L12: 0.0841
REMARK 3 L13: 0.0896 L23: 0.2241
REMARK 3 S TENSOR
REMARK 3 S11: -0.0845 S12: 0.0470 S13: -0.1359
REMARK 3 S21: -0.0869 S22: 0.0879 S23: -0.0787
REMARK 3 S31: 0.0684 S32: 0.0464 S33: -0.0066
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9523 -37.4646 -94.0912
REMARK 3 T TENSOR
REMARK 3 T11: 0.2996 T22: 0.2709
REMARK 3 T33: 0.3403 T12: -0.0441
REMARK 3 T13: -0.0164 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 3.6950 L22: 1.7805
REMARK 3 L33: 6.2524 L12: -0.8362
REMARK 3 L13: 2.1720 L23: 2.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.1483 S13: -0.1987
REMARK 3 S21: -0.1528 S22: -0.0228 S23: 0.2991
REMARK 3 S31: 0.0829 S32: -0.9307 S33: 0.0285
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6QGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 293388
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19500
REMARK 200 FOR THE DATA SET : 8.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 1.05400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: 6G21
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 30% (V/V) 2,4-MPD
REMARK 280 AND 0.12 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 56.07650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 123.37600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.82300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 123.37600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.07650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.82300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 8
REMARK 465 ASN A 9
REMARK 465 HIS A 10
REMARK 465 LYS A 11
REMARK 465 VAL A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 MET A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 PRO A 42
REMARK 465 GLY A 57
REMARK 465 ASN A 58
REMARK 465 PRO A 603
REMARK 465 MET B 8
REMARK 465 ASN B 9
REMARK 465 HIS B 10
REMARK 465 LYS B 11
REMARK 465 VAL B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 MET B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 GLU B 37
REMARK 465 PRO B 38
REMARK 465 PRO B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 PRO B 42
REMARK 465 GLY B 57
REMARK 465 ASN B 58
REMARK 465 GLY B 59
REMARK 465 MET C 8
REMARK 465 ASN C 9
REMARK 465 HIS C 10
REMARK 465 LYS C 11
REMARK 465 VAL C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 HIS C 15
REMARK 465 HIS C 16
REMARK 465 HIS C 17
REMARK 465 HIS C 18
REMARK 465 MET C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 PRO C 25
REMARK 465 LEU C 26
REMARK 465 PRO C 27
REMARK 465 LEU C 28
REMARK 465 PRO C 29
REMARK 465 GLN C 30
REMARK 465 GLN C 31
REMARK 465 GLN C 32
REMARK 465 PRO C 33
REMARK 465 PRO C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 GLU C 37
REMARK 465 PRO C 38
REMARK 465 PRO C 39
REMARK 465 PRO C 40
REMARK 465 PRO C 41
REMARK 465 PRO C 42
REMARK 465 ASP C 56
REMARK 465 GLY C 57
REMARK 465 ASN C 58
REMARK 465 GLY C 59
REMARK 465 MET D 8
REMARK 465 ASN D 9
REMARK 465 HIS D 10
REMARK 465 LYS D 11
REMARK 465 VAL D 12
REMARK 465 HIS D 13
REMARK 465 HIS D 14
REMARK 465 HIS D 15
REMARK 465 HIS D 16
REMARK 465 HIS D 17
REMARK 465 HIS D 18
REMARK 465 MET D 19
REMARK 465 GLY D 20
REMARK 465 GLY D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 THR D 24
REMARK 465 PRO D 25
REMARK 465 LEU D 26
REMARK 465 PRO D 27
REMARK 465 LEU D 28
REMARK 465 PRO D 29
REMARK 465 GLN D 30
REMARK 465 GLN D 31
REMARK 465 GLN D 32
REMARK 465 PRO D 33
REMARK 465 PRO D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 GLU D 37
REMARK 465 PRO D 38
REMARK 465 PRO D 39
REMARK 465 PRO D 40
REMARK 465 PRO D 41
REMARK 465 PRO D 42
REMARK 465 GLY D 57
REMARK 465 ASN D 58
REMARK 465 MET E 8
REMARK 465 ASN E 9
REMARK 465 HIS E 10
REMARK 465 LYS E 11
REMARK 465 VAL E 12
REMARK 465 HIS E 13
REMARK 465 HIS E 14
REMARK 465 HIS E 15
REMARK 465 HIS E 16
REMARK 465 HIS E 17
REMARK 465 HIS E 18
REMARK 465 MET E 19
REMARK 465 GLY E 20
REMARK 465 GLY E 21
REMARK 465 GLY E 22
REMARK 465 SER E 23
REMARK 465 THR E 24
REMARK 465 PRO E 25
REMARK 465 LEU E 26
REMARK 465 PRO E 27
REMARK 465 LEU E 28
REMARK 465 PRO E 29
REMARK 465 GLN E 30
REMARK 465 GLN E 31
REMARK 465 GLN E 32
REMARK 465 PRO E 33
REMARK 465 PRO E 34
REMARK 465 GLN E 35
REMARK 465 GLN E 36
REMARK 465 GLU E 37
REMARK 465 PRO E 38
REMARK 465 PRO E 39
REMARK 465 PRO E 40
REMARK 465 PRO E 41
REMARK 465 PRO E 42
REMARK 465 GLY E 57
REMARK 465 ASN E 58
REMARK 465 GLY E 59
REMARK 465 MET F 8
REMARK 465 ASN F 9
REMARK 465 HIS F 10
REMARK 465 LYS F 11
REMARK 465 VAL F 12
REMARK 465 HIS F 13
REMARK 465 HIS F 14
REMARK 465 HIS F 15
REMARK 465 HIS F 16
REMARK 465 HIS F 17
REMARK 465 HIS F 18
REMARK 465 MET F 19
REMARK 465 GLY F 20
REMARK 465 GLY F 21
REMARK 465 GLY F 22
REMARK 465 SER F 23
REMARK 465 THR F 24
REMARK 465 PRO F 25
REMARK 465 LEU F 26
REMARK 465 PRO F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLN F 30
REMARK 465 GLN F 31
REMARK 465 GLN F 32
REMARK 465 PRO F 33
REMARK 465 PRO F 34
REMARK 465 GLN F 35
REMARK 465 GLN F 36
REMARK 465 GLU F 37
REMARK 465 PRO F 38
REMARK 465 PRO F 39
REMARK 465 PRO F 40
REMARK 465 PRO F 41
REMARK 465 PRO F 42
REMARK 465 GLY F 57
REMARK 465 ASN F 58
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET C 192 CA CB CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 815 O HOH C 891 1.99
REMARK 500 O2 MPD A 705 O HOH A 801 2.01
REMARK 500 O HOH A 1078 O HOH A 1148 2.02
REMARK 500 O HOH E 1191 O HOH E 1240 2.03
REMARK 500 NH2 ARG C 506 O HOH C 801 2.04
REMARK 500 O HOH F 801 O HOH F 1095 2.05
REMARK 500 O HOH B 1086 O HOH B 1253 2.06
REMARK 500 O HOH F 1165 O HOH F 1233 2.07
REMARK 500 O HOH E 1248 O HOH E 1276 2.08
REMARK 500 O HOH B 1217 O HOH B 1283 2.08
REMARK 500 O HOH B 1135 O HOH B 1249 2.09
REMARK 500 O HOH B 1244 O HOH B 1283 2.09
REMARK 500 O HOH C 1182 O HOH C 1219 2.09
REMARK 500 O HOH D 1164 O HOH D 1211 2.09
REMARK 500 O HOH E 1184 O HOH E 1223 2.11
REMARK 500 O HOH C 1135 O HOH C 1154 2.12
REMARK 500 O HOH B 957 O HOH B 1157 2.12
REMARK 500 O HOH C 1114 O HOH C 1151 2.12
REMARK 500 O HOH F 1046 O HOH F 1049 2.12
REMARK 500 O HOH D 1199 O HOH D 1200 2.12
REMARK 500 O3 SO4 E 704 O HOH E 801 2.13
REMARK 500 O HOH C 927 O HOH C 1149 2.13
REMARK 500 O HOH E 977 O HOH E 1276 2.13
REMARK 500 O HOH A 964 O HOH A 1055 2.13
REMARK 500 O HOH C 953 O HOH C 1154 2.13
REMARK 500 O HOH D 1018 O HOH D 1194 2.13
REMARK 500 O HOH F 1186 O HOH F 1205 2.14
REMARK 500 O HOH C 1198 O HOH C 1209 2.14
REMARK 500 O HOH C 1159 O HOH C 1183 2.14
REMARK 500 O HOH F 1141 O HOH F 1194 2.15
REMARK 500 O HOH E 965 O HOH E 1130 2.15
REMARK 500 O HOH A 890 O HOH A 1171 2.16
REMARK 500 O HOH E 1215 O HOH E 1266 2.16
REMARK 500 O HOH C 1103 O HOH C 1126 2.16
REMARK 500 O HOH A 942 O HOH A 1164 2.16
REMARK 500 O HOH B 1047 O HOH B 1214 2.18
REMARK 500 O HOH B 1138 O HOH B 1241 2.18
REMARK 500 O LEU F 306 O HOH F 801 2.18
REMARK 500 NH2 ARG C 584 O ALA C 601 2.18
REMARK 500 O HOH C 1139 O HOH C 1203 2.18
REMARK 500 O HOH E 1059 O HOH E 1175 2.19
REMARK 500 O HOH E 966 O HOH E 1253 2.19
REMARK 500 O1 SO4 A 704 O HOH A 802 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1171 O HOH E 1063 4545 2.00
REMARK 500 O HOH D 1202 O HOH E 1252 2554 2.09
REMARK 500 O HOH B 1273 O HOH E 1196 4445 2.12
REMARK 500 O HOH C 1220 O HOH F 1105 2455 2.12
REMARK 500 O HOH C 1191 O HOH F 1187 2455 2.12
REMARK 500 O HOH B 1094 O HOH B 1218 4545 2.14
REMARK 500 O HOH A 1013 O HOH E 1086 4545 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 348 CB CYS A 348 SG -0.097
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 427 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO A 427 C - N - CD ANGL. DEV. = -30.8 DEGREES
REMARK 500 PRO B 427 C - N - CD ANGL. DEV. = -27.0 DEGREES
REMARK 500 CYS C 348 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 PRO C 427 C - N - CD ANGL. DEV. = -28.2 DEGREES
REMARK 500 ARG C 506 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 506 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 PRO D 427 C - N - CA ANGL. DEV. = 13.7 DEGREES
REMARK 500 PRO D 427 C - N - CD ANGL. DEV. = -31.2 DEGREES
REMARK 500 PRO E 427 C - N - CD ANGL. DEV. = -24.9 DEGREES
REMARK 500 PRO F 427 C - N - CD ANGL. DEV. = -25.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 67 36.39 -86.56
REMARK 500 ASN A 134 -146.26 56.83
REMARK 500 TYR A 194 -28.24 -151.84
REMARK 500 SER A 225 -111.73 66.58
REMARK 500 ALA A 249 64.16 21.94
REMARK 500 ASP A 311 12.83 -143.08
REMARK 500 TYR A 373 -90.14 -136.62
REMARK 500 SER A 383 -138.96 -139.70
REMARK 500 ASN A 408 10.67 -143.06
REMARK 500 PRO A 427 113.90 20.25
REMARK 500 SER A 491 30.28 -97.98
REMARK 500 ASN A 527 -147.65 -90.81
REMARK 500 CYS A 529 -21.86 63.01
REMARK 500 ALA B 67 33.26 -92.70
REMARK 500 ASN B 134 -145.22 60.41
REMARK 500 TYR B 194 -32.81 -152.06
REMARK 500 SER B 225 -110.95 65.80
REMARK 500 ALA B 249 61.49 25.99
REMARK 500 ASP B 311 12.94 -142.97
REMARK 500 TYR B 373 -104.34 -143.27
REMARK 500 SER B 383 -137.14 -143.51
REMARK 500 VAL B 412 -60.30 -93.76
REMARK 500 PRO B 427 125.83 6.67
REMARK 500 SER B 491 31.46 -98.97
REMARK 500 ASN B 527 -142.47 -91.12
REMARK 500 CYS B 529 -17.83 65.51
REMARK 500 ALA C 67 40.95 -87.71
REMARK 500 ASN C 134 -143.20 58.85
REMARK 500 TYR C 194 -32.54 -152.69
REMARK 500 SER C 225 -111.59 68.99
REMARK 500 ALA C 249 61.35 30.95
REMARK 500 ASP C 311 13.28 -144.28
REMARK 500 TYR C 373 -96.99 -143.36
REMARK 500 SER C 383 -140.74 -144.01
REMARK 500 PRO C 427 124.85 15.41
REMARK 500 SER C 456 118.09 -165.02
REMARK 500 ASN C 527 -143.46 -90.39
REMARK 500 CYS C 529 -22.64 68.02
REMARK 500 ALA C 571 144.37 -171.73
REMARK 500 ALA D 67 37.89 -86.79
REMARK 500 ASN D 134 -145.91 58.88
REMARK 500 TYR D 194 -29.85 -151.58
REMARK 500 SER D 225 -112.32 66.31
REMARK 500 ALA D 249 56.74 28.34
REMARK 500 TYR D 373 -91.06 -139.36
REMARK 500 SER D 383 -141.44 -141.10
REMARK 500 PRO D 427 116.00 17.12
REMARK 500 SER D 456 117.81 -169.68
REMARK 500 SER D 491 31.79 -99.22
REMARK 500 ASN D 527 -151.26 -88.61
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 426 PRO A 427 -91.95
REMARK 500 THR B 426 PRO B 427 -73.17
REMARK 500 THR C 426 PRO C 427 -81.05
REMARK 500 THR D 426 PRO D 427 -90.45
REMARK 500 THR E 426 PRO E 427 -79.25
REMARK 500 THR F 426 PRO F 427 -88.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1288 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C1224 DISTANCE = 5.89 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 706 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 75.9
REMARK 620 3 ASP A 307 OD1 70.8 140.1
REMARK 620 4 ASP A 307 OD2 75.0 140.1 47.5
REMARK 620 5 LEU A 309 O 84.1 81.3 74.3 121.7
REMARK 620 6 ASP A 311 OD1 149.4 74.7 131.4 134.7 83.5
REMARK 620 7 ILE A 313 O 99.4 79.6 126.5 78.9 159.1 83.3
REMARK 620 8 HOH A 822 O 136.5 147.2 67.2 68.7 94.9 72.5 96.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 706 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 71.0
REMARK 620 3 ASP B 307 OD1 73.1 138.8
REMARK 620 4 ASP B 307 OD2 74.2 134.0 48.8
REMARK 620 5 LEU B 309 O 90.0 83.9 76.6 125.4
REMARK 620 6 ASP B 311 OD1 146.5 75.6 136.3 134.5 84.3
REMARK 620 7 ILE B 313 O 95.0 79.2 123.7 74.9 159.7 80.7
REMARK 620 8 HOH B 870 O 143.7 145.4 72.5 74.5 93.2 69.7 94.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 703 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 70.7
REMARK 620 3 ASP C 307 OD1 75.7 139.0
REMARK 620 4 ASP C 307 OD2 72.3 133.5 50.4
REMARK 620 5 LEU C 309 O 85.3 80.3 74.1 123.4
REMARK 620 6 ASP C 311 OD1 146.2 75.6 132.9 137.4 86.7
REMARK 620 7 ILE C 313 O 94.5 80.1 125.9 75.7 159.3 82.0
REMARK 620 8 HOH C 826 O 147.9 140.7 73.0 82.2 93.0 65.3 97.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 304 O
REMARK 620 2 ASP D 304 OD1 74.4
REMARK 620 3 ASP D 307 OD1 71.0 140.1
REMARK 620 4 ASP D 307 OD2 75.6 137.3 48.6
REMARK 620 5 LEU D 309 O 89.5 84.1 76.6 125.2
REMARK 620 6 ASP D 311 OD1 146.2 72.5 136.2 135.6 81.0
REMARK 620 7 ILE D 313 O 99.0 77.9 126.2 77.6 157.1 80.1
REMARK 620 8 HOH D 824 O 139.3 146.3 70.0 70.3 92.3 73.8 94.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 705 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 304 O
REMARK 620 2 ASP E 304 OD1 70.9
REMARK 620 3 ASP E 307 OD1 70.3 133.8
REMARK 620 4 ASP E 307 OD2 73.1 135.6 49.4
REMARK 620 5 LEU E 309 O 80.2 80.5 68.9 117.7
REMARK 620 6 ASP E 311 OD1 149.3 79.4 130.4 137.0 87.2
REMARK 620 7 ILE E 313 O 98.5 83.5 126.4 77.1 163.5 85.8
REMARK 620 8 HOH E 812 O 138.3 149.0 69.1 73.9 93.6 69.9 98.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 706 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 304 O
REMARK 620 2 ASP F 304 OD1 72.4
REMARK 620 3 ASP F 307 OD1 73.5 138.7
REMARK 620 4 ASP F 307 OD2 76.4 138.8 49.2
REMARK 620 5 LEU F 309 O 86.4 82.1 73.1 122.3
REMARK 620 6 ASP F 311 OD1 147.5 76.0 130.2 135.0 81.7
REMARK 620 7 ILE F 313 O 96.3 81.8 124.7 75.4 162.0 86.7
REMARK 620 8 HOH F 860 O 142.5 144.7 70.7 72.1 93.6 68.7 94.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K E 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1K F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 706
DBREF1 6QGA A 20 603 UNP MHETH_IDESA
DBREF2 6QGA A A0A0K8P8E7 20 603
DBREF1 6QGA B 20 603 UNP MHETH_IDESA
DBREF2 6QGA B A0A0K8P8E7 20 603
DBREF1 6QGA C 20 603 UNP MHETH_IDESA
DBREF2 6QGA C A0A0K8P8E7 20 603
DBREF1 6QGA D 20 603 UNP MHETH_IDESA
DBREF2 6QGA D A0A0K8P8E7 20 603
DBREF1 6QGA E 20 603 UNP MHETH_IDESA
DBREF2 6QGA E A0A0K8P8E7 20 603
DBREF1 6QGA F 20 603 UNP MHETH_IDESA
DBREF2 6QGA F A0A0K8P8E7 20 603
SEQADV 6QGA MET A 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN A 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS A 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL A 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS A 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET A 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET B 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN B 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS B 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL B 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS B 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET B 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET C 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN C 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS C 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL C 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS C 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET C 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET D 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN D 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS D 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL D 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS D 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET D 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET E 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN E 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS E 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL E 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS E 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET E 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET F 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGA ASN F 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA LYS F 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA VAL F 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA HIS F 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGA MET F 19 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 A 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 A 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 A 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 A 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 A 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 A 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 A 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 A 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 A 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 A 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 A 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 A 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 A 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 A 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 A 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 A 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 A 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 A 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 A 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 A 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 A 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 A 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 A 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 A 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 A 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 A 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 A 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 A 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 A 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 A 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 A 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 A 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 A 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 A 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 A 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 A 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 A 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 A 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 A 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 A 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 A 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 A 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 A 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 A 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 A 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 B 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 B 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 B 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 B 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 B 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 B 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 B 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 B 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 B 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 B 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 B 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 B 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 B 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 B 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 B 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 B 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 B 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 B 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 B 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 B 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 B 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 B 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 B 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 B 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 B 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 B 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 B 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 B 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 B 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 B 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 B 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 B 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 B 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 B 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 B 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 B 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 B 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 B 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 B 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 B 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 B 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 B 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 B 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 B 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 B 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 B 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 C 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 C 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 C 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 C 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 C 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 C 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 C 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 C 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 C 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 C 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 C 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 C 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 C 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 C 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 C 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 C 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 C 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 C 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 C 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 C 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 C 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 C 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 C 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 C 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 C 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 C 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 C 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 C 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 C 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 C 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 C 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 C 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 C 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 C 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 C 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 C 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 C 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 C 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 C 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 C 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 C 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 C 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 C 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 C 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 C 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 C 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 D 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 D 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 D 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 D 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 D 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 D 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 D 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 D 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 D 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 D 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 D 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 D 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 D 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 D 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 D 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 D 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 D 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 D 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 D 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 D 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 D 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 D 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 D 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 D 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 D 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 D 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 D 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 D 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 D 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 D 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 D 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 D 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 D 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 D 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 D 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 D 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 D 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 D 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 D 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 D 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 D 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 D 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 D 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 D 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 D 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 D 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 E 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 E 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 E 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 E 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 E 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 E 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 E 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 E 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 E 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 E 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 E 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 E 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 E 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 E 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 E 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 E 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 E 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 E 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 E 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 E 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 E 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 E 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 E 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 E 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 E 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 E 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 E 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 E 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 E 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 E 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 E 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 E 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 E 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 E 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 E 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 E 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 E 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 E 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 E 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 E 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 E 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 E 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 E 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 E 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 E 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 E 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 F 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 F 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 F 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 F 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 F 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 F 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 F 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 F 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 F 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 F 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 F 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 F 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 F 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 F 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 F 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 F 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 F 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 F 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 F 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 F 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 F 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 F 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 F 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 F 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 F 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 F 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 F 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 F 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 F 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 F 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 F 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 F 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 F 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 F 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 F 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 F 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 F 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 F 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 F 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 F 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 F 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 F 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 F 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 F 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 F 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 F 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
HET J1K A 701 15
HET SO4 A 702 5
HET SO4 A 703 5
HET SO4 A 704 5
HET MPD A 705 8
HET CA A 706 1
HET J1K B 701 15
HET SO4 B 702 5
HET SO4 B 703 5
HET SO4 B 704 5
HET MPD B 705 8
HET CA B 706 1
HET CL B 707 1
HET J1K C 701 15
HET J1K C 702 15
HET CA C 703 1
HET CL C 704 1
HET CL C 705 1
HET J1K D 701 15
HET CA D 702 1
HET J1K E 701 15
HET J1K E 702 15
HET J1K E 703 15
HET SO4 E 704 5
HET CA E 705 1
HET CL E 706 1
HET J1K F 701 15
HET J1K F 702 15
HET SO4 F 703 5
HET SO4 F 704 5
HET SO4 F 705 5
HET CA F 706 1
HETNAM J1K 4-(2-HYDROXYETHYLCARBAMOYL)BENZOIC ACID
HETNAM SO4 SULFATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 7 J1K 10(C10 H11 N O4)
FORMUL 8 SO4 10(O4 S 2-)
FORMUL 11 MPD 2(C6 H14 O2)
FORMUL 12 CA 6(CA 2+)
FORMUL 19 CL 4(CL 1-)
FORMUL 39 HOH *2640(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 LEU A 177 LEU A 184 5 8
HELIX 3 AA3 ASP A 185 TYR A 194 1 10
HELIX 4 AA4 TYR A 194 GLY A 213 1 20
HELIX 5 AA5 SER A 225 PHE A 238 1 14
HELIX 6 AA6 GLN A 253 PRO A 255 5 3
HELIX 7 AA7 LYS A 256 ALA A 269 1 14
HELIX 8 AA8 PRO A 270 ALA A 272 5 3
HELIX 9 AA9 LEU A 282 PHE A 287 5 6
HELIX 10 AB1 SER A 288 ASP A 304 1 17
HELIX 11 AB2 ALA A 305 GLY A 308 5 4
HELIX 12 AB3 ASN A 316 PHE A 324 1 9
HELIX 13 AB4 SER A 350 GLY A 363 1 14
HELIX 14 AB5 ASP A 379 SER A 383 5 5
HELIX 15 AB6 GLY A 414 PHE A 424 1 11
HELIX 16 AB7 PRO A 432 THR A 434 5 3
HELIX 17 AB8 GLN A 435 LYS A 442 1 8
HELIX 18 AB9 ILE A 447 TRP A 453 5 7
HELIX 19 AC1 SER A 462 GLY A 468 1 7
HELIX 20 AC2 LEU A 474 ARG A 480 1 7
HELIX 21 AC3 SER A 496 MET A 511 1 16
HELIX 22 AC4 GLY A 513 GLY A 516 5 4
HELIX 23 AC5 MET A 540 GLY A 551 1 12
HELIX 24 AC6 THR A 563 GLY A 568 5 6
HELIX 25 AC7 THR A 593 ALA A 595 5 3
HELIX 26 AC8 SER B 47 ALA B 53 1 7
HELIX 27 AC9 LEU B 54 ASP B 56 5 3
HELIX 28 AD1 LEU B 177 LEU B 184 5 8
HELIX 29 AD2 ASP B 185 TYR B 194 1 10
HELIX 30 AD3 TYR B 194 GLY B 213 1 20
HELIX 31 AD4 SER B 225 PHE B 238 1 14
HELIX 32 AD5 GLN B 253 PRO B 255 5 3
HELIX 33 AD6 LYS B 256 ALA B 269 1 14
HELIX 34 AD7 PRO B 270 ALA B 272 5 3
HELIX 35 AD8 LEU B 282 SER B 286 5 5
HELIX 36 AD9 SER B 288 ASP B 304 1 17
HELIX 37 AE1 ALA B 305 GLY B 308 5 4
HELIX 38 AE2 ASN B 316 PHE B 324 1 9
HELIX 39 AE3 SER B 350 GLY B 363 1 14
HELIX 40 AE4 ASP B 379 SER B 383 5 5
HELIX 41 AE5 GLY B 414 PHE B 424 1 11
HELIX 42 AE6 PRO B 432 THR B 434 5 3
HELIX 43 AE7 GLN B 435 PHE B 443 1 9
HELIX 44 AE8 ILE B 447 TRP B 453 5 7
HELIX 45 AE9 SER B 462 GLY B 468 1 7
HELIX 46 AF1 LEU B 474 ARG B 480 1 7
HELIX 47 AF2 SER B 496 MET B 511 1 16
HELIX 48 AF3 GLY B 513 GLY B 516 5 4
HELIX 49 AF4 MET B 540 GLY B 551 1 12
HELIX 50 AF5 THR B 563 GLY B 568 5 6
HELIX 51 AF6 THR B 593 ALA B 595 5 3
HELIX 52 AF7 SER C 47 LEU C 54 1 8
HELIX 53 AF8 LEU C 177 LEU C 184 5 8
HELIX 54 AF9 ASP C 185 TYR C 194 1 10
HELIX 55 AG1 TYR C 194 GLY C 213 1 20
HELIX 56 AG2 SER C 225 PHE C 238 1 14
HELIX 57 AG3 GLN C 253 PRO C 255 5 3
HELIX 58 AG4 LYS C 256 ALA C 269 1 14
HELIX 59 AG5 PRO C 270 ALA C 272 5 3
HELIX 60 AG6 LEU C 282 SER C 286 5 5
HELIX 61 AG7 SER C 288 ASP C 304 1 17
HELIX 62 AG8 ALA C 305 GLY C 308 5 4
HELIX 63 AG9 ASN C 316 PHE C 324 1 9
HELIX 64 AH1 SER C 350 GLY C 363 1 14
HELIX 65 AH2 ASP C 379 SER C 383 5 5
HELIX 66 AH3 GLY C 414 PHE C 424 1 11
HELIX 67 AH4 PRO C 432 THR C 434 5 3
HELIX 68 AH5 GLN C 435 PHE C 443 1 9
HELIX 69 AH6 ILE C 447 TRP C 453 5 7
HELIX 70 AH7 SER C 462 GLY C 468 1 7
HELIX 71 AH8 LEU C 474 ARG C 480 1 7
HELIX 72 AH9 SER C 496 MET C 511 1 16
HELIX 73 AI1 GLY C 513 GLY C 516 5 4
HELIX 74 AI2 MET C 540 GLY C 551 1 12
HELIX 75 AI3 THR C 563 GLY C 568 5 6
HELIX 76 AI4 THR C 593 ALA C 595 5 3
HELIX 77 AI5 SER D 47 LEU D 54 1 8
HELIX 78 AI6 ALA D 152 ASN D 156 5 5
HELIX 79 AI7 LEU D 177 LEU D 184 5 8
HELIX 80 AI8 ASP D 185 TYR D 194 1 10
HELIX 81 AI9 TYR D 194 GLY D 213 1 20
HELIX 82 AJ1 SER D 225 PHE D 238 1 14
HELIX 83 AJ2 GLN D 253 PRO D 255 5 3
HELIX 84 AJ3 LYS D 256 ALA D 269 1 14
HELIX 85 AJ4 PRO D 270 ALA D 272 5 3
HELIX 86 AJ5 LEU D 282 SER D 286 5 5
HELIX 87 AJ6 SER D 288 ASP D 304 1 17
HELIX 88 AJ7 ALA D 305 GLY D 308 5 4
HELIX 89 AJ8 ASN D 316 PHE D 324 1 9
HELIX 90 AJ9 SER D 350 GLY D 363 1 14
HELIX 91 AK1 ASP D 379 SER D 383 5 5
HELIX 92 AK2 GLY D 414 PHE D 424 1 11
HELIX 93 AK3 PRO D 432 THR D 434 5 3
HELIX 94 AK4 GLN D 435 PHE D 443 1 9
HELIX 95 AK5 ILE D 447 TRP D 453 5 7
HELIX 96 AK6 SER D 462 GLY D 468 1 7
HELIX 97 AK7 LEU D 474 ARG D 480 1 7
HELIX 98 AK8 SER D 496 MET D 511 1 16
HELIX 99 AK9 GLY D 513 GLY D 516 5 4
HELIX 100 AL1 MET D 540 GLY D 551 1 12
HELIX 101 AL2 THR D 563 GLY D 568 5 6
HELIX 102 AL3 THR D 593 ALA D 595 5 3
HELIX 103 AL4 SER E 47 LEU E 54 1 8
HELIX 104 AL5 ALA E 152 ASN E 156 5 5
HELIX 105 AL6 LEU E 177 LEU E 184 5 8
HELIX 106 AL7 ASP E 185 TYR E 194 1 10
HELIX 107 AL8 TYR E 194 GLY E 213 1 20
HELIX 108 AL9 SER E 225 PHE E 238 1 14
HELIX 109 AM1 GLN E 253 PRO E 255 5 3
HELIX 110 AM2 LYS E 256 ALA E 269 1 14
HELIX 111 AM3 PRO E 270 ALA E 272 5 3
HELIX 112 AM4 LEU E 282 SER E 286 5 5
HELIX 113 AM5 SER E 288 ASP E 304 1 17
HELIX 114 AM6 ALA E 305 GLY E 308 5 4
HELIX 115 AM7 ASN E 316 PHE E 324 1 9
HELIX 116 AM8 SER E 350 GLY E 363 1 14
HELIX 117 AM9 ASP E 379 SER E 383 5 5
HELIX 118 AN1 GLY E 414 PHE E 424 1 11
HELIX 119 AN2 PRO E 432 THR E 434 5 3
HELIX 120 AN3 GLN E 435 PHE E 443 1 9
HELIX 121 AN4 ILE E 447 TRP E 453 5 7
HELIX 122 AN5 SER E 462 GLY E 468 1 7
HELIX 123 AN6 LEU E 474 ARG E 480 1 7
HELIX 124 AN7 SER E 496 MET E 511 1 16
HELIX 125 AN8 GLY E 513 GLY E 516 5 4
HELIX 126 AN9 MET E 540 GLY E 551 1 12
HELIX 127 AO1 THR E 563 GLY E 568 5 6
HELIX 128 AO2 THR E 593 ALA E 595 5 3
HELIX 129 AO3 SER F 47 ALA F 53 1 7
HELIX 130 AO4 ALA F 152 ASN F 156 5 5
HELIX 131 AO5 LEU F 177 LEU F 184 5 8
HELIX 132 AO6 ASP F 185 TYR F 194 1 10
HELIX 133 AO7 TYR F 194 GLY F 213 1 20
HELIX 134 AO8 SER F 225 PHE F 238 1 14
HELIX 135 AO9 GLN F 253 PRO F 255 5 3
HELIX 136 AP1 LYS F 256 ALA F 269 1 14
HELIX 137 AP2 PRO F 270 ALA F 272 5 3
HELIX 138 AP3 LEU F 282 SER F 286 5 5
HELIX 139 AP4 SER F 288 ASP F 304 1 17
HELIX 140 AP5 ALA F 305 GLY F 308 5 4
HELIX 141 AP6 ASN F 316 PHE F 324 1 9
HELIX 142 AP7 SER F 350 GLY F 363 1 14
HELIX 143 AP8 ASP F 379 SER F 383 5 5
HELIX 144 AP9 GLY F 414 ASP F 423 1 10
HELIX 145 AQ1 PRO F 432 THR F 434 5 3
HELIX 146 AQ2 GLN F 435 PHE F 443 1 9
HELIX 147 AQ3 ILE F 447 TRP F 453 5 7
HELIX 148 AQ4 SER F 462 HIS F 467 1 6
HELIX 149 AQ5 LEU F 474 ARG F 480 1 7
HELIX 150 AQ6 SER F 496 MET F 511 1 16
HELIX 151 AQ7 GLY F 513 GLY F 516 5 4
HELIX 152 AQ8 MET F 540 GLY F 551 1 12
HELIX 153 AQ9 THR F 563 GLY F 568 5 6
HELIX 154 AR1 THR F 593 ALA F 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O ALA A 97 N VAL A 69
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O VAL A 523 N HIS A 488
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 598 N ARG A 584
SHEET 1 AA5 9 THR B 68 ARG B 76 0
SHEET 2 AA5 9 HIS B 91 THR B 102 -1 O HIS B 91 N ARG B 76
SHEET 3 AA5 9 PRO B 108 PRO B 118 -1 O LEU B 115 N VAL B 94
SHEET 4 AA5 9 ALA B 158 THR B 162 -1 O THR B 159 N ARG B 116
SHEET 5 AA5 9 ARG B 124 GLU B 128 1 N ARG B 124 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O ARG B 519 N LEU B 486
SHEET 1 AA6 2 LEU B 385 SER B 386 0
SHEET 2 AA6 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA7 2 ILE B 557 TRP B 560 0
SHEET 2 AA7 2 THR B 573 LEU B 576 -1 O LEU B 576 N ILE B 557
SHEET 1 AA8 2 ILE B 582 TYR B 585 0
SHEET 2 AA8 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SHEET 1 AA9 9 THR C 68 ARG C 76 0
SHEET 2 AA9 9 HIS C 91 THR C 102 -1 O ALA C 97 N VAL C 69
SHEET 3 AA9 9 PRO C 108 PRO C 118 -1 O LEU C 115 N VAL C 94
SHEET 4 AA9 9 ALA C 158 THR C 162 -1 O THR C 159 N ARG C 116
SHEET 5 AA9 9 ARG C 124 GLU C 128 1 N PHE C 126 O ALA C 158
SHEET 6 AA9 9 LYS C 218 CYS C 224 1 O TYR C 220 N PHE C 125
SHEET 7 AA9 9 GLY C 244 GLY C 248 1 O GLY C 248 N GLY C 223
SHEET 8 AA9 9 LYS C 483 GLY C 489 1 O LYS C 483 N ILE C 245
SHEET 9 AA9 9 ALA C 518 VAL C 523 1 O ARG C 519 N LEU C 486
SHEET 1 AB1 2 LEU C 385 SER C 386 0
SHEET 2 AB1 2 THR C 389 TYR C 390 -1 O THR C 389 N SER C 386
SHEET 1 AB2 2 ILE C 557 TRP C 560 0
SHEET 2 AB2 2 THR C 573 LEU C 576 -1 O LEU C 576 N ILE C 557
SHEET 1 AB3 2 ILE C 582 TYR C 585 0
SHEET 2 AB3 2 PHE C 597 ALA C 600 -1 O ALA C 600 N ILE C 582
SHEET 1 AB4 9 THR D 68 ARG D 76 0
SHEET 2 AB4 9 HIS D 91 THR D 102 -1 O HIS D 91 N ARG D 76
SHEET 3 AB4 9 PRO D 108 PRO D 118 -1 O LEU D 115 N VAL D 94
SHEET 4 AB4 9 ALA D 158 THR D 162 -1 O THR D 159 N ARG D 116
SHEET 5 AB4 9 ARG D 124 GLU D 128 1 N ARG D 124 O ALA D 158
SHEET 6 AB4 9 LYS D 218 CYS D 224 1 O TYR D 220 N PHE D 125
SHEET 7 AB4 9 GLY D 244 GLY D 248 1 O GLY D 248 N GLY D 223
SHEET 8 AB4 9 LYS D 483 GLY D 489 1 O ILE D 485 N ALA D 247
SHEET 9 AB4 9 ALA D 518 VAL D 523 1 O ARG D 519 N LEU D 486
SHEET 1 AB5 2 LEU D 385 SER D 386 0
SHEET 2 AB5 2 THR D 389 TYR D 390 -1 O THR D 389 N SER D 386
SHEET 1 AB6 2 ILE D 557 TRP D 560 0
SHEET 2 AB6 2 THR D 573 LEU D 576 -1 O LEU D 576 N ILE D 557
SHEET 1 AB7 2 ILE D 582 TYR D 585 0
SHEET 2 AB7 2 PHE D 597 ALA D 600 -1 O ALA D 598 N ARG D 584
SHEET 1 AB8 9 THR E 68 ARG E 76 0
SHEET 2 AB8 9 HIS E 91 THR E 102 -1 O GLU E 93 N ALA E 74
SHEET 3 AB8 9 PRO E 108 PRO E 118 -1 O LEU E 115 N VAL E 94
SHEET 4 AB8 9 ALA E 158 THR E 162 -1 O THR E 159 N ARG E 116
SHEET 5 AB8 9 ARG E 124 GLU E 128 1 N PHE E 126 O ALA E 158
SHEET 6 AB8 9 LYS E 218 CYS E 224 1 O TYR E 220 N PHE E 125
SHEET 7 AB8 9 GLY E 244 GLY E 248 1 O GLY E 248 N GLY E 223
SHEET 8 AB8 9 LYS E 483 GLY E 489 1 O LYS E 483 N ILE E 245
SHEET 9 AB8 9 ALA E 518 VAL E 523 1 O ARG E 519 N LEU E 486
SHEET 1 AB9 2 LEU E 385 SER E 386 0
SHEET 2 AB9 2 THR E 389 TYR E 390 -1 O THR E 389 N SER E 386
SHEET 1 AC1 2 ILE E 557 TRP E 560 0
SHEET 2 AC1 2 THR E 573 LEU E 576 -1 O LEU E 576 N ILE E 557
SHEET 1 AC2 2 ILE E 582 TYR E 585 0
SHEET 2 AC2 2 PHE E 597 ALA E 600 -1 O ALA E 598 N ARG E 584
SHEET 1 AC3 9 THR F 68 ARG F 76 0
SHEET 2 AC3 9 HIS F 91 THR F 102 -1 O GLU F 93 N ALA F 74
SHEET 3 AC3 9 PRO F 108 PRO F 118 -1 O LEU F 115 N VAL F 94
SHEET 4 AC3 9 ALA F 158 THR F 162 -1 O THR F 159 N ARG F 116
SHEET 5 AC3 9 ARG F 124 GLU F 128 1 N PHE F 126 O ALA F 158
SHEET 6 AC3 9 LYS F 218 CYS F 224 1 O TYR F 220 N PHE F 125
SHEET 7 AC3 9 GLY F 244 GLY F 248 1 O GLY F 248 N GLY F 223
SHEET 8 AC3 9 LYS F 483 GLY F 489 1 O ILE F 485 N ILE F 245
SHEET 9 AC3 9 ALA F 518 VAL F 523 1 O ARG F 519 N LEU F 486
SHEET 1 AC4 2 LEU F 385 SER F 386 0
SHEET 2 AC4 2 THR F 389 TYR F 390 -1 O THR F 389 N SER F 386
SHEET 1 AC5 3 ARG F 537 PHE F 538 0
SHEET 2 AC5 3 ILE F 557 TRP F 560 -1 O TRP F 560 N ARG F 537
SHEET 3 AC5 3 THR F 573 LEU F 576 -1 O LEU F 576 N ILE F 557
SHEET 1 AC6 2 ILE F 582 TYR F 585 0
SHEET 2 AC6 2 PHE F 597 ALA F 600 -1 O ALA F 600 N ILE F 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.09
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.06
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.06
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.02
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.03
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.07
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.09
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.08
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.06
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.03
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.06
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.08
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.08
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.02
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.05
SSBOND 16 CYS D 51 CYS D 92 1555 1555 2.09
SSBOND 17 CYS D 224 CYS D 529 1555 1555 2.08
SSBOND 18 CYS D 303 CYS D 320 1555 1555 2.05
SSBOND 19 CYS D 340 CYS D 348 1555 1555 2.04
SSBOND 20 CYS D 577 CYS D 599 1555 1555 2.04
SSBOND 21 CYS E 51 CYS E 92 1555 1555 2.08
SSBOND 22 CYS E 224 CYS E 529 1555 1555 2.06
SSBOND 23 CYS E 303 CYS E 320 1555 1555 2.08
SSBOND 24 CYS E 340 CYS E 348 1555 1555 2.04
SSBOND 25 CYS E 577 CYS E 599 1555 1555 2.08
SSBOND 26 CYS F 51 CYS F 92 1555 1555 2.07
SSBOND 27 CYS F 224 CYS F 529 1555 1555 2.07
SSBOND 28 CYS F 303 CYS F 320 1555 1555 2.07
SSBOND 29 CYS F 340 CYS F 348 1555 1555 2.05
SSBOND 30 CYS F 577 CYS F 599 1555 1555 2.07
LINK O ASP A 304 CA CA A 706 1555 1555 2.61
LINK OD1 ASP A 304 CA CA A 706 1555 1555 2.27
LINK OD1 ASP A 307 CA CA A 706 1555 1555 2.75
LINK OD2 ASP A 307 CA CA A 706 1555 1555 2.58
LINK O LEU A 309 CA CA A 706 1555 1555 2.40
LINK OD1 ASP A 311 CA CA A 706 1555 1555 2.55
LINK O ILE A 313 CA CA A 706 1555 1555 2.38
LINK O ASP B 304 CA CA B 706 1555 1555 2.50
LINK OD1 ASP B 304 CA CA B 706 1555 1555 2.46
LINK OD1 ASP B 307 CA CA B 706 1555 1555 2.61
LINK OD2 ASP B 307 CA CA B 706 1555 1555 2.69
LINK O LEU B 309 CA CA B 706 1555 1555 2.29
LINK OD1 ASP B 311 CA CA B 706 1555 1555 2.51
LINK O ILE B 313 CA CA B 706 1555 1555 2.44
LINK O ASP C 304 CA CA C 703 1555 1555 2.39
LINK OD1 ASP C 304 CA CA C 703 1555 1555 2.41
LINK OD1 ASP C 307 CA CA C 703 1555 1555 2.47
LINK OD2 ASP C 307 CA CA C 703 1555 1555 2.62
LINK O LEU C 309 CA CA C 703 1555 1555 2.42
LINK OD1 ASP C 311 CA CA C 703 1555 1555 2.43
LINK O ILE C 313 CA CA C 703 1555 1555 2.41
LINK O ASP D 304 CA CA D 702 1555 1555 2.61
LINK OD1 ASP D 304 CA CA D 702 1555 1555 2.36
LINK OD1 ASP D 307 CA CA D 702 1555 1555 2.71
LINK OD2 ASP D 307 CA CA D 702 1555 1555 2.58
LINK O LEU D 309 CA CA D 702 1555 1555 2.30
LINK OD1 ASP D 311 CA CA D 702 1555 1555 2.67
LINK O ILE D 313 CA CA D 702 1555 1555 2.35
LINK O ASP E 304 CA CA E 705 1555 1555 2.65
LINK OD1 ASP E 304 CA CA E 705 1555 1555 2.33
LINK OD1 ASP E 307 CA CA E 705 1555 1555 2.64
LINK OD2 ASP E 307 CA CA E 705 1555 1555 2.50
LINK O LEU E 309 CA CA E 705 1555 1555 2.41
LINK OD1 ASP E 311 CA CA E 705 1555 1555 2.37
LINK O ILE E 313 CA CA E 705 1555 1555 2.33
LINK O ASP F 304 CA CA F 706 1555 1555 2.58
LINK OD1 ASP F 304 CA CA F 706 1555 1555 2.44
LINK OD1 ASP F 307 CA CA F 706 1555 1555 2.66
LINK OD2 ASP F 307 CA CA F 706 1555 1555 2.54
LINK O LEU F 309 CA CA F 706 1555 1555 2.35
LINK OD1 ASP F 311 CA CA F 706 1555 1555 2.40
LINK O ILE F 313 CA CA F 706 1555 1555 2.35
LINK CA CA A 706 O HOH A 822 1555 1555 2.60
LINK CA CA B 706 O HOH B 870 1555 1555 2.55
LINK CA CA C 703 O HOH C 826 1555 1555 2.51
LINK CA CA D 702 O HOH D 824 1555 1555 2.49
LINK CA CA E 705 O HOH E 812 1555 1555 2.58
LINK CA CA F 706 O HOH F 860 1555 1555 2.48
CISPEP 1 TYR A 579 PRO A 580 0 3.72
CISPEP 2 TYR B 579 PRO B 580 0 3.24
CISPEP 3 TYR C 579 PRO C 580 0 6.05
CISPEP 4 TYR D 579 PRO D 580 0 7.74
CISPEP 5 TYR E 579 PRO E 580 0 5.71
CISPEP 6 TYR F 579 PRO F 580 0 8.94
SITE 1 AC1 15 SER A 131 GLY A 132 SER A 225 GLU A 226
SITE 2 AC1 15 LEU A 254 ALA A 257 TRP A 397 ARG A 411
SITE 3 AC1 15 PHE A 415 SER A 416 HIS A 528 CYS A 529
SITE 4 AC1 15 HOH A 854 HOH A 896 HOH A1048
SITE 1 AC2 3 GLU A 120 TRP A 121 ASN D 122
SITE 1 AC3 1 ARG A 519
SITE 1 AC4 7 ARG A 480 HOH A 802 HOH A 812 HOH A1026
SITE 2 AC4 7 HOH A1042 HOH A1060 GLN F 199
SITE 1 AC5 5 PRO A 64 HOH A 801 LYS F 205 J1K F 702
SITE 2 AC5 5 HOH F1059
SITE 1 AC6 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC6 6 ILE A 313 HOH A 822
SITE 1 AC7 15 SER B 131 GLY B 132 SER B 225 GLU B 226
SITE 2 AC7 15 LEU B 254 TRP B 397 ARG B 411 PHE B 415
SITE 3 AC7 15 SER B 416 PHE B 495 HIS B 528 HOH B 803
SITE 4 AC7 15 HOH B 927 HOH B 950 HOH B1189
SITE 1 AC8 8 ASN B 65 GLN B 199 HOH B 807 HOH B 808
SITE 2 AC8 8 HOH B 819 HOH B 930 HOH B1111 ARG C 480
SITE 1 AC9 5 ARG B 480 HOH B 994 HOH B1064 ASN C 65
SITE 2 AC9 5 GLN C 199
SITE 1 AD1 1 ASN B 122
SITE 1 AD2 4 TRP B 263 GLN B 266 ARG B 359 HOH B 843
SITE 1 AD3 6 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AD3 6 ILE B 313 HOH B 870
SITE 1 AD4 5 GLY B 258 GLY B 261 ARG B 411 ALA B 417
SITE 2 AD4 5 MET B 440
SITE 1 AD5 10 LYS B 205 ALA B 209 HOH B1071 HOH B1224
SITE 2 AD5 10 VAL C 62 ARG C 210 HOH C 808 HOH C 823
SITE 3 AD5 10 HOH C 848 HOH C1040
SITE 1 AD6 13 SER C 131 GLY C 132 SER C 225 GLU C 226
SITE 2 AD6 13 LEU C 254 TRP C 397 ARG C 411 PHE C 415
SITE 3 AD6 13 SER C 416 HIS C 528 HOH C 805 HOH C 863
SITE 4 AD6 13 HOH C 933
SITE 1 AD7 6 ASP C 304 ASP C 307 LEU C 309 ASP C 311
SITE 2 AD7 6 ILE C 313 HOH C 826
SITE 1 AD8 5 GLY C 258 GLY C 261 ARG C 411 ALA C 417
SITE 2 AD8 5 MET C 440
SITE 1 AD9 6 TRP C 63 PRO C 64 ASN C 65 THR C 68
SITE 2 AD9 6 ALA C 203 HOH C 822
SITE 1 AE1 14 SER D 131 GLY D 132 SER D 225 GLU D 226
SITE 2 AE1 14 LEU D 254 ALA D 257 TRP D 397 ARG D 411
SITE 3 AE1 14 PHE D 415 SER D 416 HIS D 528 HOH D 801
SITE 4 AE1 14 HOH D 850 HOH D 876
SITE 1 AE2 6 ASP D 304 ASP D 307 LEU D 309 ASP D 311
SITE 2 AE2 6 ILE D 313 HOH D 824
SITE 1 AE3 14 ALA B 81 ALA B 86 ALA B 87 HOH B 936
SITE 2 AE3 14 HOH B 995 THR E 82 ALA E 83 ALA E 86
SITE 3 AE3 14 ILE E 149 ALA E 150 ARG E 155 HOH E 893
SITE 4 AE3 14 HOH E1033 HOH E1038
SITE 1 AE4 5 VAL D 62 ALA D 206 LYS E 205 HOH E 828
SITE 2 AE4 5 HOH E 841
SITE 1 AE5 13 SER E 131 GLY E 132 SER E 225 GLU E 226
SITE 2 AE5 13 LEU E 254 TRP E 397 ARG E 411 PHE E 415
SITE 3 AE5 13 SER E 416 HIS E 528 HOH E 906 HOH E 931
SITE 4 AE5 13 HOH E 963
SITE 1 AE6 6 ARG D 480 ASN E 65 GLN E 199 HOH E 801
SITE 2 AE6 6 HOH E 807 HOH E 829
SITE 1 AE7 6 ASP E 304 ASP E 307 LEU E 309 ASP E 311
SITE 2 AE7 6 ILE E 313 HOH E 812
SITE 1 AE8 4 GLY E 258 GLY E 261 ARG E 411 MET E 440
SITE 1 AE9 12 SER F 131 GLY F 132 SER F 225 GLU F 226
SITE 2 AE9 12 LEU F 254 TRP F 397 ARG F 411 PHE F 415
SITE 3 AE9 12 SER F 416 HIS F 528 HOH F 824 HOH F 923
SITE 1 AF1 11 LYS A 205 ALA A 215 MPD A 705 HOH A 801
SITE 2 AF1 11 VAL F 62 PRO F 64 ALA F 206 ARG F 210
SITE 3 AF1 11 HOH F 805 HOH F 814 HOH F 991
SITE 1 AF2 2 GLN F 581 HOH F 825
SITE 1 AF3 7 ASN A 65 GLN A 199 ARG F 480 HOH F 806
SITE 2 AF3 7 HOH F 816 HOH F 821 HOH F1087
SITE 1 AF4 2 GLY F 562 HOH F1105
SITE 1 AF5 6 ASP F 304 ASP F 307 LEU F 309 ASP F 311
SITE 2 AF5 6 ILE F 313 HOH F 860
CRYST1 112.153 183.646 246.752 90.00 90.00 90.00 P 21 21 21 24
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 0.008916 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004053 0.00000
TER 4122 PRO A 602
TER 8259 PRO B 603
TER 12382 PRO C 603
TER 16512 PRO D 603
TER 20638 PRO E 603
TER 24773 PRO F 603
MASTER 1192 0 32 154 91 0 72 627612 6 336 276
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