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HEADER HYDROLASE 10-JAN-19 6QG9
TITLE CRYSTAL STRUCTURE OF A PLASTIC DEGRADING ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
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 (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_0224;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 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 6QG9 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. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 408224
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 20359
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 47.9522 - 6.3650 0.99 13777 723 0.1763 0.2045
REMARK 3 2 6.3650 - 5.0539 0.99 13745 718 0.1705 0.2156
REMARK 3 3 5.0539 - 4.4156 1.00 13819 728 0.1593 0.2002
REMARK 3 4 4.4156 - 4.0121 0.99 13809 724 0.1693 0.2187
REMARK 3 5 4.0121 - 3.7246 1.00 13755 723 0.1788 0.2262
REMARK 3 6 3.7246 - 3.5051 0.99 13784 733 0.1901 0.2428
REMARK 3 7 3.5051 - 3.3296 0.99 13800 728 0.2130 0.2731
REMARK 3 8 3.3296 - 3.1847 1.00 13786 727 0.2152 0.2637
REMARK 3 9 3.1847 - 3.0621 0.99 13770 724 0.2125 0.2736
REMARK 3 10 3.0621 - 2.9565 1.00 13816 727 0.2172 0.2859
REMARK 3 11 2.9565 - 2.8640 1.00 13827 729 0.2237 0.2857
REMARK 3 12 2.8640 - 2.7822 1.00 13783 725 0.2170 0.2656
REMARK 3 13 2.7822 - 2.7089 1.00 13811 727 0.2128 0.2794
REMARK 3 14 2.7089 - 2.6428 1.00 13834 727 0.2151 0.2761
REMARK 3 15 2.6428 - 2.5828 1.00 13774 727 0.2081 0.2743
REMARK 3 16 2.5828 - 2.5278 0.99 13783 728 0.2198 0.2830
REMARK 3 17 2.5278 - 2.4772 1.00 13816 729 0.2274 0.2852
REMARK 3 18 2.4772 - 2.4305 1.00 13817 728 0.2247 0.2920
REMARK 3 19 2.4305 - 2.3871 0.99 13772 728 0.2382 0.2946
REMARK 3 20 2.3871 - 2.3466 0.99 13742 720 0.2393 0.3049
REMARK 3 21 2.3466 - 2.3088 0.98 13539 710 0.2508 0.3323
REMARK 3 22 2.3088 - 2.2733 0.97 13505 715 0.2653 0.3128
REMARK 3 23 2.2733 - 2.2398 0.97 13407 706 0.2790 0.3354
REMARK 3 24 2.2398 - 2.2083 0.92 12785 681 0.2843 0.3248
REMARK 3 25 2.2083 - 2.1784 0.84 11710 603 0.2918 0.3470
REMARK 3 26 2.1784 - 2.1501 0.78 10755 542 0.3051 0.3640
REMARK 3 27 2.1501 - 2.1233 0.72 9993 507 0.3240 0.3621
REMARK 3 28 2.1233 - 2.0977 0.67 9250 482 0.3248 0.3687
REMARK 3 29 2.0977 - 2.0733 0.63 8793 473 0.3373 0.3807
REMARK 3 30 2.0733 - 2.0500 0.60 8308 417 0.3460 0.3755
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.011 42407
REMARK 3 ANGLE : 1.117 57770
REMARK 3 CHIRALITY : 0.056 6068
REMARK 3 PLANARITY : 0.008 7727
REMARK 3 DIHEDRAL : 12.218 24864
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 61
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7671 -61.1101 21.1725
REMARK 3 T TENSOR
REMARK 3 T11: 0.1418 T22: 0.1673
REMARK 3 T33: 0.1567 T12: -0.0403
REMARK 3 T13: 0.0249 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.9645 L22: 1.3299
REMARK 3 L33: 1.3736 L12: -0.4430
REMARK 3 L13: -0.6914 L23: 0.4421
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.1390 S13: -0.1527
REMARK 3 S21: -0.1218 S22: -0.0127 S23: 0.0425
REMARK 3 S31: 0.0529 S32: -0.0649 S33: 0.0413
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8675 -35.6609 34.8713
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.1909
REMARK 3 T33: 0.2287 T12: 0.0167
REMARK 3 T13: 0.0168 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.6281 L22: 0.8593
REMARK 3 L33: 0.3355 L12: 0.4988
REMARK 3 L13: -0.2101 L23: -0.1970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0474 S12: -0.0600 S13: 0.1684
REMARK 3 S21: 0.0477 S22: -0.0282 S23: 0.1586
REMARK 3 S31: -0.1279 S32: -0.1035 S33: -0.0212
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3183 -43.6845 29.3264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1888 T22: 0.2168
REMARK 3 T33: 0.2902 T12: 0.0370
REMARK 3 T13: -0.0052 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 1.1167 L22: 1.7998
REMARK 3 L33: 0.4937 L12: 0.3847
REMARK 3 L13: -0.1518 L23: -0.6687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0556 S12: -0.0248 S13: 0.0063
REMARK 3 S21: -0.0569 S22: -0.0189 S23: -0.2267
REMARK 3 S31: -0.0133 S32: 0.0742 S33: 0.0697
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8562 31.8224 39.4199
REMARK 3 T TENSOR
REMARK 3 T11: 0.3382 T22: 0.2224
REMARK 3 T33: 0.1926 T12: 0.0911
REMARK 3 T13: -0.0177 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 1.5875 L22: 1.3389
REMARK 3 L33: 1.2140 L12: 0.9161
REMARK 3 L13: 0.5464 L23: -0.0142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0251 S12: 0.0131 S13: 0.1214
REMARK 3 S21: 0.0663 S22: -0.0360 S23: 0.1710
REMARK 3 S31: -0.3999 S32: -0.1654 S33: 0.0513
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8779 7.4718 54.9421
REMARK 3 T TENSOR
REMARK 3 T11: 0.2766 T22: 0.2459
REMARK 3 T33: 0.2072 T12: 0.0356
REMARK 3 T13: -0.0102 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 0.3655 L22: 0.5336
REMARK 3 L33: 1.0542 L12: -0.0075
REMARK 3 L13: 0.1789 L23: -0.0265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: -0.1153 S13: -0.0285
REMARK 3 S21: 0.1157 S22: -0.0077 S23: 0.0440
REMARK 3 S31: 0.0248 S32: -0.0609 S33: 0.0101
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0407 17.3082 53.3037
REMARK 3 T TENSOR
REMARK 3 T11: 0.2510 T22: 0.2292
REMARK 3 T33: 0.1591 T12: -0.0001
REMARK 3 T13: -0.0183 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.0824 L22: 1.8864
REMARK 3 L33: 2.4938 L12: -0.2482
REMARK 3 L13: 0.3509 L23: 0.5520
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: -0.0706 S13: 0.0008
REMARK 3 S21: 0.2623 S22: 0.1347 S23: -0.2078
REMARK 3 S31: -0.0230 S32: 0.2976 S33: -0.0531
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4398 31.2075 -0.1835
REMARK 3 T TENSOR
REMARK 3 T11: 0.2772 T22: 0.2062
REMARK 3 T33: 0.2152 T12: 0.0606
REMARK 3 T13: -0.0194 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 2.3881 L22: 0.9402
REMARK 3 L33: 1.7042 L12: -0.9529
REMARK 3 L13: 1.1443 L23: -0.3988
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: -0.0971 S13: -0.1109
REMARK 3 S21: 0.1122 S22: 0.0369 S23: 0.1570
REMARK 3 S31: 0.0604 S32: -0.1209 S33: -0.0336
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 213 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0441 30.1386 -27.4608
REMARK 3 T TENSOR
REMARK 3 T11: 0.3816 T22: 0.3017
REMARK 3 T33: 0.1997 T12: 0.0784
REMARK 3 T13: -0.0518 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.6145 L22: 0.5111
REMARK 3 L33: 1.3873 L12: 0.0617
REMARK 3 L13: 0.2454 L23: 0.4373
REMARK 3 S TENSOR
REMARK 3 S11: -0.0716 S12: 0.1247 S13: -0.0177
REMARK 3 S21: -0.0944 S22: 0.0635 S23: 0.0168
REMARK 3 S31: 0.1003 S32: 0.1746 S33: 0.0059
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7090 27.0866 -41.8765
REMARK 3 T TENSOR
REMARK 3 T11: 0.3988 T22: 0.2872
REMARK 3 T33: 0.1718 T12: 0.0422
REMARK 3 T13: -0.0619 T23: 0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 1.0168 L22: 2.0442
REMARK 3 L33: 3.4434 L12: 0.9436
REMARK 3 L13: 0.4656 L23: 1.7019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: 0.0540 S13: 0.0593
REMARK 3 S21: -0.2981 S22: 0.0260 S23: -0.1025
REMARK 3 S31: 0.1639 S32: 0.0574 S33: -0.0785
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 383 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2550 33.7334 -25.1599
REMARK 3 T TENSOR
REMARK 3 T11: 0.3787 T22: 0.2889
REMARK 3 T33: 0.2511 T12: 0.0743
REMARK 3 T13: -0.0872 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.7631 L22: 0.9309
REMARK 3 L33: 0.9580 L12: 0.1446
REMARK 3 L13: 0.3143 L23: 0.5557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: 0.0498 S13: -0.0260
REMARK 3 S21: -0.1351 S22: -0.0071 S23: 0.1227
REMARK 3 S31: 0.0509 S32: -0.0630 S33: 0.0561
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 511 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2176 30.9441 -19.6322
REMARK 3 T TENSOR
REMARK 3 T11: 0.3269 T22: 0.3495
REMARK 3 T33: 0.2163 T12: 0.0990
REMARK 3 T13: -0.0574 T23: -0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 1.1469 L22: 2.4230
REMARK 3 L33: 1.1687 L12: -0.1589
REMARK 3 L13: 0.4872 L23: 0.1246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0378 S12: 0.1062 S13: -0.0243
REMARK 3 S21: 0.0996 S22: 0.0777 S23: -0.2239
REMARK 3 S31: 0.2018 S32: 0.2446 S33: -0.0553
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9949 -68.1699 15.8309
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.3309
REMARK 3 T33: 0.1919 T12: 0.0604
REMARK 3 T13: -0.0420 T23: -0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 3.3228 L22: 0.5739
REMARK 3 L33: 1.5255 L12: -1.3988
REMARK 3 L13: -1.6919 L23: 0.5673
REMARK 3 S TENSOR
REMARK 3 S11: -0.2466 S12: -0.3427 S13: 0.0915
REMARK 3 S21: 0.2982 S22: 0.2955 S23: 0.0082
REMARK 3 S31: 0.2746 S32: 0.2870 S33: -0.0324
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 111 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8556 -62.5265 1.1539
REMARK 3 T TENSOR
REMARK 3 T11: 0.2799 T22: 0.2531
REMARK 3 T33: 0.2343 T12: 0.0485
REMARK 3 T13: -0.0122 T23: -0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.3550 L22: 0.8160
REMARK 3 L33: 0.3475 L12: -0.1213
REMARK 3 L13: 0.0527 L23: -0.3960
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.0186 S13: -0.0560
REMARK 3 S21: 0.1189 S22: 0.0803 S23: -0.0024
REMARK 3 S31: -0.0085 S32: 0.0799 S33: -0.0750
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 272 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4795 -35.3420 -15.7507
REMARK 3 T TENSOR
REMARK 3 T11: 0.3625 T22: 0.2176
REMARK 3 T33: 0.2366 T12: 0.0401
REMARK 3 T13: 0.0216 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 3.0623 L22: 0.4736
REMARK 3 L33: 0.5011 L12: 0.5370
REMARK 3 L13: -0.4390 L23: -0.5222
REMARK 3 S TENSOR
REMARK 3 S11: 0.1279 S12: 0.2298 S13: 0.1569
REMARK 3 S21: -0.0839 S22: -0.0311 S23: 0.0064
REMARK 3 S31: -0.0542 S32: 0.0403 S33: -0.0912
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5183 -36.5190 -21.4474
REMARK 3 T TENSOR
REMARK 3 T11: 0.2754 T22: 0.2775
REMARK 3 T33: 0.1545 T12: 0.0299
REMARK 3 T13: -0.0261 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 3.0546 L22: 3.6907
REMARK 3 L33: 3.3774 L12: -0.3444
REMARK 3 L13: -1.0586 L23: 0.2440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0724 S12: 0.3667 S13: 0.2008
REMARK 3 S21: -0.0545 S22: 0.0620 S23: -0.0211
REMARK 3 S31: -0.3002 S32: 0.0322 S33: -0.1235
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 383 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3207 -53.1898 -11.8892
REMARK 3 T TENSOR
REMARK 3 T11: 0.2889 T22: 0.2504
REMARK 3 T33: 0.2251 T12: 0.0429
REMARK 3 T13: -0.0301 T23: -0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 0.7035 L22: 0.8613
REMARK 3 L33: 0.6741 L12: -0.3269
REMARK 3 L13: 0.0835 L23: -0.0841
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: 0.0666 S13: 0.0114
REMARK 3 S21: 0.0217 S22: 0.0161 S23: -0.0017
REMARK 3 S31: -0.1125 S32: 0.1617 S33: -0.0643
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0166 -51.7381 -4.7105
REMARK 3 T TENSOR
REMARK 3 T11: 0.2384 T22: 0.2134
REMARK 3 T33: 0.2827 T12: 0.0338
REMARK 3 T13: 0.0043 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.7384 L22: 3.8383
REMARK 3 L33: 0.7559 L12: -1.1991
REMARK 3 L13: 0.3574 L23: 0.1410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0889 S12: -0.0579 S13: 0.0234
REMARK 3 S21: 0.0470 S22: 0.0352 S23: 0.3886
REMARK 3 S31: -0.2451 S32: -0.0943 S33: 0.0467
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 43 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1048 -84.5810 44.2471
REMARK 3 T TENSOR
REMARK 3 T11: 0.1458 T22: 0.1627
REMARK 3 T33: 0.2103 T12: 0.0154
REMARK 3 T13: -0.0024 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 2.4858 L22: 1.5346
REMARK 3 L33: 1.3476 L12: 1.1968
REMARK 3 L13: 0.5313 L23: 0.2832
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: 0.0989 S13: -0.1358
REMARK 3 S21: 0.0502 S22: -0.0194 S23: -0.3435
REMARK 3 S31: 0.0755 S32: 0.2215 S33: -0.0360
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 213 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1996 -71.8132 68.2840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3665 T22: 0.2856
REMARK 3 T33: 0.2039 T12: -0.0826
REMARK 3 T13: -0.0339 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.2158 L22: 0.9721
REMARK 3 L33: 0.7479 L12: 0.2211
REMARK 3 L13: -0.2792 L23: -0.1929
REMARK 3 S TENSOR
REMARK 3 S11: 0.0945 S12: -0.3453 S13: 0.0197
REMARK 3 S21: 0.4410 S22: -0.1354 S23: -0.0556
REMARK 3 S31: -0.1350 S32: 0.0606 S33: 0.0421
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5849 -67.3488 82.4273
REMARK 3 T TENSOR
REMARK 3 T11: 0.6386 T22: 0.5282
REMARK 3 T33: 0.2582 T12: -0.0941
REMARK 3 T13: -0.0771 T23: -0.0755
REMARK 3 L TENSOR
REMARK 3 L11: 1.5418 L22: 1.6595
REMARK 3 L33: 2.8683 L12: -0.8865
REMARK 3 L13: -0.5741 L23: -0.8034
REMARK 3 S TENSOR
REMARK 3 S11: -0.2414 S12: -0.4639 S13: 0.1106
REMARK 3 S21: 0.7257 S22: 0.1056 S23: -0.2506
REMARK 3 S31: -0.0089 S32: -0.4218 S33: 0.1206
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 383 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5663 -71.9276 63.1222
REMARK 3 T TENSOR
REMARK 3 T11: 0.3013 T22: 0.2003
REMARK 3 T33: 0.1649 T12: -0.0505
REMARK 3 T13: -0.0055 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.9900 L22: 0.9757
REMARK 3 L33: 0.5356 L12: 0.3414
REMARK 3 L13: 0.0699 L23: -0.3880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0626 S12: -0.1389 S13: -0.0488
REMARK 3 S21: 0.2419 S22: -0.0690 S23: -0.0746
REMARK 3 S31: -0.1025 S32: 0.0932 S33: 0.0042
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 43 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6658 23.4997 9.0972
REMARK 3 T TENSOR
REMARK 3 T11: 0.3097 T22: 0.2243
REMARK 3 T33: 0.1709 T12: 0.0253
REMARK 3 T13: -0.0364 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.4435 L22: 1.5265
REMARK 3 L33: 0.7756 L12: -0.8687
REMARK 3 L13: 0.4816 L23: -0.0284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0478 S12: 0.1377 S13: 0.1373
REMARK 3 S21: -0.1951 S22: -0.0467 S23: -0.0679
REMARK 3 S31: -0.2412 S32: -0.0190 S33: 0.0895
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 218 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5448 -6.8848 5.7401
REMARK 3 T TENSOR
REMARK 3 T11: 0.2346 T22: 0.2056
REMARK 3 T33: 0.1707 T12: 0.0515
REMARK 3 T13: -0.0287 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.8569 L22: 1.4134
REMARK 3 L33: 1.2633 L12: -0.3051
REMARK 3 L13: -0.0119 L23: 0.6011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.0088 S13: -0.1121
REMARK 3 S21: -0.1727 S22: -0.0677 S23: 0.0865
REMARK 3 S31: -0.0656 S32: -0.1220 S33: 0.0759
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 334 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3073 -6.6759 8.9453
REMARK 3 T TENSOR
REMARK 3 T11: 0.2519 T22: 0.2213
REMARK 3 T33: 0.2217 T12: 0.0687
REMARK 3 T13: -0.0267 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.6782 L22: 0.8479
REMARK 3 L33: 1.0751 L12: 0.0607
REMARK 3 L13: 0.3852 L23: 0.4032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0765 S13: -0.1158
REMARK 3 S21: -0.1025 S22: -0.0695 S23: 0.0282
REMARK 3 S31: 0.0453 S32: -0.0376 S33: 0.0602
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1726 1.7757 4.6145
REMARK 3 T TENSOR
REMARK 3 T11: 0.2865 T22: 0.3925
REMARK 3 T33: 0.3210 T12: 0.0788
REMARK 3 T13: -0.0945 T23: -0.0967
REMARK 3 L TENSOR
REMARK 3 L11: 1.1828 L22: 1.5282
REMARK 3 L33: 2.5399 L12: -0.1943
REMARK 3 L13: 0.0339 L23: -0.4577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: 0.0912 S13: -0.2204
REMARK 3 S21: -0.2589 S22: -0.0751 S23: 0.3193
REMARK 3 S31: 0.0854 S32: -0.5286 S33: 0.0532
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 40 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.1791 -12.5331 45.4289
REMARK 3 T TENSOR
REMARK 3 T11: 0.5686 T22: 0.7447
REMARK 3 T33: 0.5119 T12: 0.2714
REMARK 3 T13: 0.0213 T23: -0.1044
REMARK 3 L TENSOR
REMARK 3 L11: 0.6521 L22: 1.6310
REMARK 3 L33: 0.9396 L12: -0.1269
REMARK 3 L13: -0.3817 L23: 0.8181
REMARK 3 S TENSOR
REMARK 3 S11: -0.5069 S12: -1.0338 S13: 0.1389
REMARK 3 S21: 0.6560 S22: 0.3303 S23: 0.3476
REMARK 3 S31: -0.2851 S32: -0.1922 S33: 0.1294
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 91 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.1089 -17.9402 33.9284
REMARK 3 T TENSOR
REMARK 3 T11: 0.3506 T22: 0.3729
REMARK 3 T33: 0.4291 T12: 0.1504
REMARK 3 T13: -0.0457 T23: -0.0834
REMARK 3 L TENSOR
REMARK 3 L11: 1.3189 L22: 1.1605
REMARK 3 L33: 0.7201 L12: -0.0494
REMARK 3 L13: 0.0920 L23: -0.1216
REMARK 3 S TENSOR
REMARK 3 S11: -0.2015 S12: -0.4373 S13: 0.1182
REMARK 3 S21: 0.1962 S22: 0.1394 S23: 0.0979
REMARK 3 S31: -0.2176 S32: -0.1156 S33: 0.0653
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 149 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.5051 -19.1338 28.7993
REMARK 3 T TENSOR
REMARK 3 T11: 0.2743 T22: 0.3348
REMARK 3 T33: 0.4181 T12: 0.1173
REMARK 3 T13: -0.0669 T23: -0.0682
REMARK 3 L TENSOR
REMARK 3 L11: 1.3808 L22: 1.8377
REMARK 3 L33: 1.6887 L12: 0.8578
REMARK 3 L13: 0.5263 L23: 1.1108
REMARK 3 S TENSOR
REMARK 3 S11: -0.1929 S12: -0.1270 S13: 0.0123
REMARK 3 S21: 0.0884 S22: 0.0964 S23: 0.1026
REMARK 3 S31: -0.1592 S32: -0.1425 S33: 0.0900
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 213 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.2920 -16.3135 19.7634
REMARK 3 T TENSOR
REMARK 3 T11: 0.2822 T22: 0.3612
REMARK 3 T33: 0.3308 T12: 0.0729
REMARK 3 T13: -0.0460 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 2.4020 L22: 1.4271
REMARK 3 L33: 1.7961 L12: -0.8031
REMARK 3 L13: -0.0304 L23: 0.2384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: 0.2928 S13: 0.3288
REMARK 3 S21: -0.0447 S22: -0.0253 S23: -0.1419
REMARK 3 S31: -0.0051 S32: -0.1734 S33: 0.0306
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 272 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8663 -32.3907 10.5764
REMARK 3 T TENSOR
REMARK 3 T11: 0.3863 T22: 0.6458
REMARK 3 T33: 0.3312 T12: 0.1625
REMARK 3 T13: 0.0211 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 2.2827 L22: 2.6565
REMARK 3 L33: 0.8836 L12: -0.6769
REMARK 3 L13: 0.0054 L23: 0.1445
REMARK 3 S TENSOR
REMARK 3 S11: 0.2186 S12: 0.5422 S13: 0.0795
REMARK 3 S21: -0.4120 S22: -0.2131 S23: -0.2648
REMARK 3 S31: 0.2059 S32: 0.3948 S33: -0.0104
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 383 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0437 -37.6425 20.3491
REMARK 3 T TENSOR
REMARK 3 T11: 0.4113 T22: 0.4819
REMARK 3 T33: 0.4098 T12: 0.1311
REMARK 3 T13: -0.0113 T23: -0.0984
REMARK 3 L TENSOR
REMARK 3 L11: 0.8317 L22: 2.4488
REMARK 3 L33: 2.6340 L12: -0.0082
REMARK 3 L13: 1.1187 L23: -0.0254
REMARK 3 S TENSOR
REMARK 3 S11: 0.2196 S12: 0.3047 S13: -0.3048
REMARK 3 S21: -0.0505 S22: -0.2479 S23: 0.0813
REMARK 3 S31: 0.6278 S32: 0.5021 S33: 0.0376
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 415 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8716 -34.2178 9.2067
REMARK 3 T TENSOR
REMARK 3 T11: 0.5230 T22: 0.5013
REMARK 3 T33: 0.4070 T12: 0.1175
REMARK 3 T13: -0.1243 T23: -0.1559
REMARK 3 L TENSOR
REMARK 3 L11: 1.5168 L22: 2.8534
REMARK 3 L33: 0.3009 L12: -0.7542
REMARK 3 L13: -0.3660 L23: -0.5171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.1394 S13: -0.0427
REMARK 3 S21: -0.1172 S22: -0.1871 S23: 0.2110
REMARK 3 S31: 0.2225 S32: 0.1239 S33: 0.1253
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 453 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0636 -11.6417 14.8929
REMARK 3 T TENSOR
REMARK 3 T11: 0.3905 T22: 0.3932
REMARK 3 T33: 0.4821 T12: 0.0890
REMARK 3 T13: -0.0749 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 1.2178 L22: 1.8126
REMARK 3 L33: 1.0433 L12: 0.3872
REMARK 3 L13: 0.1595 L23: 0.0682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.4136 S13: 0.3946
REMARK 3 S21: -0.1464 S22: -0.0276 S23: -0.1393
REMARK 3 S31: 0.0620 S32: 0.2533 S33: 0.0940
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9711 -11.5619 28.9509
REMARK 3 T TENSOR
REMARK 3 T11: 0.3572 T22: 0.3759
REMARK 3 T33: 0.5717 T12: 0.0664
REMARK 3 T13: -0.1210 T23: -0.0724
REMARK 3 L TENSOR
REMARK 3 L11: 2.2573 L22: 4.1912
REMARK 3 L33: 0.7951 L12: -2.2016
REMARK 3 L13: -0.3930 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: 0.0962 S13: 0.4190
REMARK 3 S21: 0.4082 S22: -0.0503 S23: -0.6140
REMARK 3 S31: -0.1136 S32: 0.0945 S33: 0.0983
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8411 -14.7905 26.0699
REMARK 3 T TENSOR
REMARK 3 T11: 0.3572 T22: 0.5205
REMARK 3 T33: 0.6741 T12: 0.0952
REMARK 3 T13: -0.0354 T23: -0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 4.4417 L22: 1.4248
REMARK 3 L33: 1.2111 L12: -0.6296
REMARK 3 L13: 2.2116 L23: 0.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.2046 S12: 0.2831 S13: 0.7717
REMARK 3 S21: 0.1067 S22: 0.0877 S23: -0.3460
REMARK 3 S31: -0.1389 S32: 0.2800 S33: 0.1357
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3782 -58.3895 -34.0484
REMARK 3 T TENSOR
REMARK 3 T11: 0.3939 T22: 0.5238
REMARK 3 T33: 0.6375 T12: -0.0391
REMARK 3 T13: -0.0763 T23: -0.1910
REMARK 3 L TENSOR
REMARK 3 L11: 0.6809 L22: 3.8983
REMARK 3 L33: 1.1558 L12: -0.7218
REMARK 3 L13: -0.8283 L23: 1.3740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0423 S12: -0.1936 S13: 0.3367
REMARK 3 S21: 0.2780 S22: 0.1187 S23: -0.5578
REMARK 3 S31: -0.3670 S32: 0.4572 S33: -0.1061
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 77 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2041 -65.4552 -40.2983
REMARK 3 T TENSOR
REMARK 3 T11: 0.2701 T22: 0.4113
REMARK 3 T33: 0.4214 T12: -0.0142
REMARK 3 T13: -0.0461 T23: -0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 0.9508 L22: 0.5930
REMARK 3 L33: 0.9995 L12: -0.4660
REMARK 3 L13: -0.6047 L23: 0.3115
REMARK 3 S TENSOR
REMARK 3 S11: -0.1240 S12: -0.2797 S13: 0.4104
REMARK 3 S21: 0.0842 S22: 0.1794 S23: -0.1226
REMARK 3 S31: 0.0460 S32: 0.0601 S33: -0.0565
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 149 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5018 -73.4593 -41.4110
REMARK 3 T TENSOR
REMARK 3 T11: 0.2222 T22: 0.3889
REMARK 3 T33: 0.3654 T12: -0.0239
REMARK 3 T13: -0.0762 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 0.8645 L22: 2.7957
REMARK 3 L33: 1.8377 L12: -0.3745
REMARK 3 L13: -0.2282 L23: 1.4214
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.2396 S13: 0.0557
REMARK 3 S21: -0.0011 S22: -0.1283 S23: -0.0073
REMARK 3 S31: -0.0293 S32: -0.1218 S33: 0.0855
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 213 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0905 -82.6339 -38.3841
REMARK 3 T TENSOR
REMARK 3 T11: 0.4079 T22: 0.4349
REMARK 3 T33: 0.4838 T12: -0.0121
REMARK 3 T13: -0.1582 T23: -0.0514
REMARK 3 L TENSOR
REMARK 3 L11: 2.4208 L22: 0.4777
REMARK 3 L33: 0.5985 L12: 0.5999
REMARK 3 L13: 0.4046 L23: -0.2994
REMARK 3 S TENSOR
REMARK 3 S11: 0.2025 S12: -0.6841 S13: -0.3189
REMARK 3 S21: -0.0105 S22: -0.1646 S23: 0.0353
REMARK 3 S31: 0.3059 S32: -0.1194 S33: -0.0193
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 272 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2544 -88.6766 -53.0734
REMARK 3 T TENSOR
REMARK 3 T11: 0.4792 T22: 0.3772
REMARK 3 T33: 0.7152 T12: -0.1227
REMARK 3 T13: -0.1987 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 1.1581 L22: 0.5220
REMARK 3 L33: 1.7832 L12: -0.4560
REMARK 3 L13: -0.3218 L23: 0.6182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.0035 S13: -0.6293
REMARK 3 S21: -0.1406 S22: -0.0604 S23: 0.3191
REMARK 3 S31: 0.1376 S32: -0.1865 S33: 0.0439
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7371 -96.0369 -53.9969
REMARK 3 T TENSOR
REMARK 3 T11: 0.5288 T22: 0.2968
REMARK 3 T33: 0.7658 T12: 0.0028
REMARK 3 T13: -0.2172 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 1.3237 L22: 1.3265
REMARK 3 L33: 1.6465 L12: 0.1951
REMARK 3 L13: -0.4152 L23: 0.5753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0688 S12: 0.0901 S13: -0.2638
REMARK 3 S21: -0.2223 S22: -0.1613 S23: 0.6087
REMARK 3 S31: 0.1277 S32: -0.1058 S33: 0.1830
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 383 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4913 -88.6691 -57.0449
REMARK 3 T TENSOR
REMARK 3 T11: 0.5281 T22: 0.3411
REMARK 3 T33: 0.5810 T12: -0.0342
REMARK 3 T13: -0.2343 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 2.8317 L22: 0.4109
REMARK 3 L33: 1.2338 L12: -0.3130
REMARK 3 L13: 0.8178 L23: -0.6589
REMARK 3 S TENSOR
REMARK 3 S11: 0.2061 S12: -0.1374 S13: -0.3366
REMARK 3 S21: -0.4309 S22: 0.0738 S23: 0.3101
REMARK 3 S31: 0.4140 S32: -0.0800 S33: -0.2649
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 453 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1132 -87.5349 -33.8399
REMARK 3 T TENSOR
REMARK 3 T11: 0.4628 T22: 0.5343
REMARK 3 T33: 0.5427 T12: -0.0959
REMARK 3 T13: -0.1774 T23: 0.1235
REMARK 3 L TENSOR
REMARK 3 L11: 1.2270 L22: 1.0017
REMARK 3 L33: 1.7418 L12: -0.7532
REMARK 3 L13: 0.3319 L23: 0.1748
REMARK 3 S TENSOR
REMARK 3 S11: 0.1801 S12: -0.2948 S13: -0.3958
REMARK 3 S21: -0.0413 S22: -0.1297 S23: 0.1595
REMARK 3 S31: 0.2488 S32: -0.3702 S33: -0.0330
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9920 -72.7761 -33.8289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3248 T22: 0.6622
REMARK 3 T33: 0.4240 T12: -0.1227
REMARK 3 T13: -0.0693 T23: 0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 1.4344 L22: 0.3672
REMARK 3 L33: 2.5695 L12: -0.1077
REMARK 3 L13: 1.9106 L23: -0.2754
REMARK 3 S TENSOR
REMARK 3 S11: 0.3748 S12: -0.4775 S13: -0.3720
REMARK 3 S21: 0.0899 S22: 0.0974 S23: 0.1288
REMARK 3 S31: 0.4159 S32: -0.5862 S33: -0.4709
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1181 -75.1576 -36.9353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3916 T22: 0.7064
REMARK 3 T33: 0.6632 T12: -0.0862
REMARK 3 T13: -0.1271 T23: 0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 4.0185 L22: 0.4920
REMARK 3 L33: 0.7926 L12: -1.0825
REMARK 3 L13: 0.7636 L23: 0.1473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: -0.8087 S13: 0.0432
REMARK 3 S21: 0.0879 S22: 0.2308 S23: 0.0494
REMARK 3 S31: 0.0667 S32: -0.4688 S33: -0.1670
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2468 13.1678 49.3565
REMARK 3 T TENSOR
REMARK 3 T11: 0.8687 T22: 0.4561
REMARK 3 T33: 0.8873 T12: -0.0490
REMARK 3 T13: -0.1522 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 3.0021 L22: 1.2784
REMARK 3 L33: 7.2964 L12: 1.0959
REMARK 3 L13: 3.5111 L23: 1.6740
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: 0.1809 S13: 0.0068
REMARK 3 S21: -0.4778 S22: -0.0304 S23: 0.4646
REMARK 3 S31: -1.2332 S32: 0.3010 S33: 0.1133
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 77 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8043 1.3003 51.9057
REMARK 3 T TENSOR
REMARK 3 T11: 0.4901 T22: 0.4280
REMARK 3 T33: 0.6735 T12: -0.0150
REMARK 3 T13: -0.1789 T23: -0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 2.0128 L22: 2.2345
REMARK 3 L33: 0.6382 L12: 1.1276
REMARK 3 L13: -0.0850 L23: 0.9848
REMARK 3 S TENSOR
REMARK 3 S11: 0.3181 S12: -0.3413 S13: -0.0048
REMARK 3 S21: -0.1629 S22: -0.5407 S23: 0.5260
REMARK 3 S31: -0.2102 S32: -0.0531 S33: 0.1941
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 111 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6483 -1.4005 57.9727
REMARK 3 T TENSOR
REMARK 3 T11: 0.4602 T22: 0.4566
REMARK 3 T33: 0.6055 T12: 0.0414
REMARK 3 T13: -0.0493 T23: -0.1715
REMARK 3 L TENSOR
REMARK 3 L11: 1.7893 L22: 2.0294
REMARK 3 L33: 1.1511 L12: 0.3033
REMARK 3 L13: 0.9955 L23: -0.6751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0496 S12: -0.1006 S13: 0.1922
REMARK 3 S21: -0.1287 S22: -0.0948 S23: 0.2304
REMARK 3 S31: -0.2214 S32: -0.0274 S33: 0.0353
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 213 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8666 -24.8608 67.7867
REMARK 3 T TENSOR
REMARK 3 T11: 0.4455 T22: 0.5123
REMARK 3 T33: 0.4858 T12: 0.0033
REMARK 3 T13: 0.0130 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.0963 L22: 3.1942
REMARK 3 L33: 0.9120 L12: -0.5617
REMARK 3 L13: 0.7075 L23: -0.2768
REMARK 3 S TENSOR
REMARK 3 S11: 0.1045 S12: -0.2312 S13: -0.0857
REMARK 3 S21: 0.3898 S22: 0.0075 S23: 0.2708
REMARK 3 S31: 0.0695 S32: -0.0420 S33: -0.1054
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6104 -37.0983 73.7551
REMARK 3 T TENSOR
REMARK 3 T11: 0.5383 T22: 0.4780
REMARK 3 T33: 0.4759 T12: 0.0486
REMARK 3 T13: -0.1039 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 3.2930 L22: 5.2623
REMARK 3 L33: 2.1180 L12: -0.8133
REMARK 3 L13: 0.3337 L23: 0.5356
REMARK 3 S TENSOR
REMARK 3 S11: 0.3145 S12: -0.2356 S13: -0.2531
REMARK 3 S21: 0.3481 S22: -0.1842 S23: -0.3222
REMARK 3 S31: 0.4925 S32: -0.1352 S33: -0.1448
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 383 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5733 -21.1664 68.2649
REMARK 3 T TENSOR
REMARK 3 T11: 0.5310 T22: 0.5030
REMARK 3 T33: 0.5060 T12: -0.0446
REMARK 3 T13: -0.0794 T23: 0.1111
REMARK 3 L TENSOR
REMARK 3 L11: 1.7312 L22: 3.9166
REMARK 3 L33: 1.4693 L12: 0.5571
REMARK 3 L13: 0.3399 L23: 1.9277
REMARK 3 S TENSOR
REMARK 3 S11: 0.1556 S12: -0.2225 S13: -0.0706
REMARK 3 S21: 0.2501 S22: -0.0331 S23: -0.4088
REMARK 3 S31: 0.0917 S32: 0.3892 S33: -0.0985
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 453 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0884 -12.8394 73.9508
REMARK 3 T TENSOR
REMARK 3 T11: 0.5244 T22: 0.6753
REMARK 3 T33: 0.5688 T12: 0.1156
REMARK 3 T13: 0.0901 T23: -0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 1.9990 L22: 2.0223
REMARK 3 L33: 1.9281 L12: 0.5534
REMARK 3 L13: 0.7489 L23: 0.7773
REMARK 3 S TENSOR
REMARK 3 S11: 0.1378 S12: -0.5522 S13: 0.4939
REMARK 3 S21: 0.4547 S22: -0.1314 S23: 0.3229
REMARK 3 S31: -0.0579 S32: -0.5318 S33: -0.0311
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.6519 -19.6329 59.2285
REMARK 3 T TENSOR
REMARK 3 T11: 0.4532 T22: 0.5275
REMARK 3 T33: 0.6474 T12: 0.0271
REMARK 3 T13: -0.0269 T23: -0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 3.3168 L22: 4.0846
REMARK 3 L33: 3.4559 L12: -0.8312
REMARK 3 L13: -1.1094 L23: 1.1392
REMARK 3 S TENSOR
REMARK 3 S11: 0.2449 S12: 0.4405 S13: 0.4367
REMARK 3 S21: 0.3786 S22: -0.4521 S23: 0.5246
REMARK 3 S31: 0.2773 S32: -0.2295 S33: 0.1990
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9794 -33.6211 59.4783
REMARK 3 T TENSOR
REMARK 3 T11: 0.3775 T22: 0.7900
REMARK 3 T33: 0.8019 T12: -0.1167
REMARK 3 T13: 0.0537 T23: 0.1285
REMARK 3 L TENSOR
REMARK 3 L11: 0.1851 L22: 2.6598
REMARK 3 L33: 2.4655 L12: -0.4144
REMARK 3 L13: 0.3437 L23: -0.2668
REMARK 3 S TENSOR
REMARK 3 S11: 0.4202 S12: -0.5690 S13: -0.2129
REMARK 3 S21: 0.1678 S22: -0.1889 S23: 1.0100
REMARK 3 S31: 0.5457 S32: -0.8922 S33: -0.2001
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1861 -49.7755 -10.3289
REMARK 3 T TENSOR
REMARK 3 T11: 0.7614 T22: 1.2569
REMARK 3 T33: 0.5771 T12: 0.2460
REMARK 3 T13: 0.0129 T23: -0.1732
REMARK 3 L TENSOR
REMARK 3 L11: 0.1164 L22: 3.2483
REMARK 3 L33: 1.2401 L12: -0.0279
REMARK 3 L13: -0.1365 L23: 1.5104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0894 S12: -0.2741 S13: 0.1221
REMARK 3 S21: 0.7919 S22: -0.1195 S23: 0.6277
REMARK 3 S31: 0.0650 S32: -0.1960 S33: 0.1861
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 77 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8109 -42.7017 -23.8898
REMARK 3 T TENSOR
REMARK 3 T11: 0.5302 T22: 0.9700
REMARK 3 T33: 0.7804 T12: 0.2565
REMARK 3 T13: -0.0920 T23: -0.2405
REMARK 3 L TENSOR
REMARK 3 L11: 0.5223 L22: 1.6089
REMARK 3 L33: 0.3583 L12: -0.7980
REMARK 3 L13: 0.1315 L23: -0.2992
REMARK 3 S TENSOR
REMARK 3 S11: -0.2655 S12: -0.4912 S13: 0.3097
REMARK 3 S21: 0.4647 S22: 0.2607 S23: 0.1163
REMARK 3 S31: -0.2908 S32: -0.6294 S33: -0.0102
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 213 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8372 -32.3309 -47.6011
REMARK 3 T TENSOR
REMARK 3 T11: 0.4435 T22: 0.5212
REMARK 3 T33: 0.8271 T12: 0.1081
REMARK 3 T13: -0.1277 T23: -0.1779
REMARK 3 L TENSOR
REMARK 3 L11: 1.1154 L22: 1.2763
REMARK 3 L33: 2.0086 L12: -0.6537
REMARK 3 L13: 0.5943 L23: -0.1792
REMARK 3 S TENSOR
REMARK 3 S11: -0.1308 S12: -0.3249 S13: 0.3780
REMARK 3 S21: 0.0572 S22: 0.2711 S23: -0.1330
REMARK 3 S31: -0.2785 S32: -0.1303 S33: -0.1148
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 334 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0053 -31.7388 -55.8095
REMARK 3 T TENSOR
REMARK 3 T11: 0.4775 T22: 0.5271
REMARK 3 T33: 0.7234 T12: 0.1019
REMARK 3 T13: -0.1199 T23: -0.0906
REMARK 3 L TENSOR
REMARK 3 L11: 2.0819 L22: 2.6953
REMARK 3 L33: 2.6781 L12: -0.5184
REMARK 3 L13: 0.5065 L23: -0.3153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: -0.4688 S13: 0.3872
REMARK 3 S21: -0.1914 S22: 0.1627 S23: 0.0987
REMARK 3 S31: -0.2437 S32: -0.5309 S33: -0.1723
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 415 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3850 -24.9987 -36.9560
REMARK 3 T TENSOR
REMARK 3 T11: 0.6709 T22: 0.7836
REMARK 3 T33: 1.1214 T12: 0.2913
REMARK 3 T13: -0.1950 T23: -0.3129
REMARK 3 L TENSOR
REMARK 3 L11: 0.0343 L22: 1.5180
REMARK 3 L33: 1.4974 L12: -0.0412
REMARK 3 L13: -0.2212 L23: -0.2139
REMARK 3 S TENSOR
REMARK 3 S11: -0.2554 S12: -0.3893 S13: 0.6046
REMARK 3 S21: 0.1778 S22: 0.3546 S23: -0.1153
REMARK 3 S31: -0.4958 S32: -0.4577 S33: -0.1098
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2188 -41.7026 -42.7186
REMARK 3 T TENSOR
REMARK 3 T11: 0.3349 T22: 0.4873
REMARK 3 T33: 0.8066 T12: 0.1214
REMARK 3 T13: -0.0985 T23: -0.1689
REMARK 3 L TENSOR
REMARK 3 L11: 1.0686 L22: 2.4552
REMARK 3 L33: 4.6279 L12: 1.0335
REMARK 3 L13: 1.1158 L23: 0.6046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.3471 S13: 0.5097
REMARK 3 S21: -0.0418 S22: -0.1930 S23: -0.4464
REMARK 3 S31: 0.1391 S32: -0.0224 S33: 0.2381
REMARK 3 TLS GROUP : 61
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 561 THROUGH 600 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9304 -43.2669 -56.2624
REMARK 3 T TENSOR
REMARK 3 T11: 0.4981 T22: 0.4856
REMARK 3 T33: 0.8050 T12: -0.0201
REMARK 3 T13: 0.0406 T23: -0.1031
REMARK 3 L TENSOR
REMARK 3 L11: 2.0018 L22: 1.6227
REMARK 3 L33: 1.7431 L12: -0.8867
REMARK 3 L13: -0.5271 L23: -0.3661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0591 S12: -0.1479 S13: 0.7467
REMARK 3 S21: -0.6218 S22: 0.0883 S23: -0.2846
REMARK 3 S31: -0.0016 S32: 0.4143 S33: -0.1440
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 6QG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-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 : 14.1
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 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 408240
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.21900
REMARK 200 FOR THE DATA SET : 5.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.24100
REMARK 200 FOR SHELL : 0.930
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: 6QGA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.5, 10% (V/V) PEG8000
REMARK 280 AND 0.1 M ZINC ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10
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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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 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 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 GLY C 57
REMARK 465 ASN C 58
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 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 465 MET G 8
REMARK 465 ASN G 9
REMARK 465 HIS G 10
REMARK 465 LYS G 11
REMARK 465 VAL G 12
REMARK 465 HIS G 13
REMARK 465 HIS G 14
REMARK 465 HIS G 15
REMARK 465 HIS G 16
REMARK 465 HIS G 17
REMARK 465 HIS G 18
REMARK 465 MET G 19
REMARK 465 GLY G 20
REMARK 465 GLY G 21
REMARK 465 GLY G 22
REMARK 465 SER G 23
REMARK 465 THR G 24
REMARK 465 PRO G 25
REMARK 465 LEU G 26
REMARK 465 PRO G 27
REMARK 465 LEU G 28
REMARK 465 PRO G 29
REMARK 465 GLN G 30
REMARK 465 GLN G 31
REMARK 465 GLN G 32
REMARK 465 PRO G 33
REMARK 465 PRO G 34
REMARK 465 GLN G 35
REMARK 465 GLN G 36
REMARK 465 GLU G 37
REMARK 465 PRO G 38
REMARK 465 ASP G 56
REMARK 465 GLY G 57
REMARK 465 ASN G 58
REMARK 465 MET H 8
REMARK 465 ASN H 9
REMARK 465 HIS H 10
REMARK 465 LYS H 11
REMARK 465 VAL H 12
REMARK 465 HIS H 13
REMARK 465 HIS H 14
REMARK 465 HIS H 15
REMARK 465 HIS H 16
REMARK 465 HIS H 17
REMARK 465 HIS H 18
REMARK 465 MET H 19
REMARK 465 GLY H 20
REMARK 465 GLY H 21
REMARK 465 GLY H 22
REMARK 465 SER H 23
REMARK 465 THR H 24
REMARK 465 PRO H 25
REMARK 465 LEU H 26
REMARK 465 PRO H 27
REMARK 465 LEU H 28
REMARK 465 PRO H 29
REMARK 465 GLN H 30
REMARK 465 GLN H 31
REMARK 465 GLN H 32
REMARK 465 PRO H 33
REMARK 465 PRO H 34
REMARK 465 GLN H 35
REMARK 465 GLN H 36
REMARK 465 GLU H 37
REMARK 465 PRO H 38
REMARK 465 PRO H 39
REMARK 465 PRO H 40
REMARK 465 PRO H 41
REMARK 465 PRO H 42
REMARK 465 ASP H 56
REMARK 465 GLY H 57
REMARK 465 ASN H 58
REMARK 465 PRO H 603
REMARK 465 MET I 8
REMARK 465 ASN I 9
REMARK 465 HIS I 10
REMARK 465 LYS I 11
REMARK 465 VAL I 12
REMARK 465 HIS I 13
REMARK 465 HIS I 14
REMARK 465 HIS I 15
REMARK 465 HIS I 16
REMARK 465 HIS I 17
REMARK 465 HIS I 18
REMARK 465 MET I 19
REMARK 465 GLY I 20
REMARK 465 GLY I 21
REMARK 465 GLY I 22
REMARK 465 SER I 23
REMARK 465 THR I 24
REMARK 465 PRO I 25
REMARK 465 LEU I 26
REMARK 465 PRO I 27
REMARK 465 LEU I 28
REMARK 465 PRO I 29
REMARK 465 GLN I 30
REMARK 465 GLN I 31
REMARK 465 GLN I 32
REMARK 465 PRO I 33
REMARK 465 PRO I 34
REMARK 465 GLN I 35
REMARK 465 GLN I 36
REMARK 465 GLU I 37
REMARK 465 PRO I 38
REMARK 465 PRO I 39
REMARK 465 PRO I 40
REMARK 465 PRO I 41
REMARK 465 PRO I 42
REMARK 465 GLY I 57
REMARK 465 ASN I 58
REMARK 465 MET J 8
REMARK 465 ASN J 9
REMARK 465 HIS J 10
REMARK 465 LYS J 11
REMARK 465 VAL J 12
REMARK 465 HIS J 13
REMARK 465 HIS J 14
REMARK 465 HIS J 15
REMARK 465 HIS J 16
REMARK 465 HIS J 17
REMARK 465 HIS J 18
REMARK 465 MET J 19
REMARK 465 GLY J 20
REMARK 465 GLY J 21
REMARK 465 GLY J 22
REMARK 465 SER J 23
REMARK 465 THR J 24
REMARK 465 PRO J 25
REMARK 465 LEU J 26
REMARK 465 PRO J 27
REMARK 465 LEU J 28
REMARK 465 PRO J 29
REMARK 465 GLN J 30
REMARK 465 GLN J 31
REMARK 465 GLN J 32
REMARK 465 PRO J 33
REMARK 465 PRO J 34
REMARK 465 GLN J 35
REMARK 465 GLN J 36
REMARK 465 GLU J 37
REMARK 465 PRO J 38
REMARK 465 PRO J 39
REMARK 465 PRO J 40
REMARK 465 PRO J 41
REMARK 465 PRO J 42
REMARK 465 GLY J 57
REMARK 465 ASN J 58
REMARK 465 ALA J 600
REMARK 465 ALA J 601
REMARK 465 PRO J 602
REMARK 465 PRO J 603
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 A 801 O HOH G 811 1.85
REMARK 500 OD2 ASP C 77 O HOH C 801 1.89
REMARK 500 O PHE E 287 NH2 ARG E 395 1.93
REMARK 500 O HOH D 1210 O HOH D 1214 1.97
REMARK 500 O HOH A 1162 O HOH A 1173 1.98
REMARK 500 O HOH H 829 O HOH H 1024 1.99
REMARK 500 O HOH D 1121 O HOH D 1177 2.00
REMARK 500 O HOH B 845 O HOH B 1101 2.01
REMARK 500 O HOH I 802 O HOH I 981 2.02
REMARK 500 O HOH E 969 O HOH I 854 2.03
REMARK 500 O HOH C 819 O HOH C 1130 2.04
REMARK 500 O HOH B 1124 O HOH B 1179 2.04
REMARK 500 O HOH G 1024 O HOH G 1062 2.04
REMARK 500 O HOH H 940 O HOH H 1040 2.05
REMARK 500 O HOH F 1207 O HOH F 1245 2.05
REMARK 500 NH1 ARG E 395 O GLY E 400 2.06
REMARK 500 O HOH C 931 O HOH C 1123 2.06
REMARK 500 OD1 ASN C 156 O HOH C 802 2.06
REMARK 500 OD1 ASP D 473 O HOH D 801 2.06
REMARK 500 O HOH G 811 O HOH G 996 2.07
REMARK 500 NE2 HIS H 293 O HOH H 801 2.07
REMARK 500 OE2 GLU E 90 O HOH E 801 2.07
REMARK 500 OD2 ASP I 175 O HOH I 801 2.08
REMARK 500 O ASP E 60 O HOH E 802 2.08
REMARK 500 O HOH F 833 O HOH F 1210 2.08
REMARK 500 O HOH H 1018 O HOH H 1019 2.09
REMARK 500 OD2 ASP F 77 O HOH F 801 2.10
REMARK 500 O HOH C 810 O HOH C 845 2.10
REMARK 500 O HOH D 837 O HOH D 1159 2.10
REMARK 500 O HOH F 809 O HOH F 1098 2.10
REMARK 500 O HOH B 891 O HOH B 1184 2.10
REMARK 500 OD2 ASP A 175 O HOH A 801 2.10
REMARK 500 O HOH G 871 O HOH G 1010 2.10
REMARK 500 O HOH A 922 O HOH A 1105 2.10
REMARK 500 O HOH C 1145 O HOH C 1201 2.10
REMARK 500 O HOH H 818 O HOH H 836 2.11
REMARK 500 NE2 GLN G 297 O HOH G 801 2.11
REMARK 500 O HOH C 1121 O HOH C 1154 2.11
REMARK 500 O HOH E 1033 O HOH E 1192 2.11
REMARK 500 OD2 ASP H 60 O HOH H 802 2.11
REMARK 500 O ASN H 334 N GLN H 336 2.12
REMARK 500 O HOH F 869 O HOH F 1202 2.12
REMARK 500 OE1 GLU C 505 O HOH C 803 2.12
REMARK 500 O HOH I 982 O HOH I 984 2.12
REMARK 500 O HOH C 802 O HOH C 992 2.12
REMARK 500 OG1 THR B 573 O HOH B 801 2.13
REMARK 500 O HOH D 1173 O HOH F 1021 2.13
REMARK 500 O HOH A 1146 O HOH A 1221 2.13
REMARK 500 O HOH F 805 O HOH F 1154 2.13
REMARK 500 O PRO E 428 O HOH E 803 2.13
REMARK 500
REMARK 500 THIS ENTRY HAS 112 CLOSE CONTACTS
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 1149 O HOH G 1041 1655 2.03
REMARK 500 O HOH E 1150 O HOH H 975 1456 2.12
REMARK 500 O HOH B 874 O HOH G 804 1655 2.16
REMARK 500 O HOH E 819 O HOH H 1015 1456 2.17
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 -0.135
REMARK 500 GLY A 532 C PRO A 533 N -0.184
REMARK 500 CYS G 348 CB CYS G 348 SG -0.128
REMARK 500 CYS H 51 CB CYS H 51 SG -0.096
REMARK 500 GLY I 532 C PRO I 533 N 0.141
REMARK 500 GLY J 532 C PRO J 533 N 0.181
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 ASP A 163 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 MET A 232 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 CYS A 348 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLY B 335 C - N - CA ANGL. DEV. = -17.5 DEGREES
REMARK 500 CYS B 348 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 PRO G 603 C - N - CA ANGL. DEV. = 12.1 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 39.87 -86.70
REMARK 500 SER A 131 140.81 -173.67
REMARK 500 ASN A 134 -143.52 56.39
REMARK 500 ALA A 176 35.68 -141.43
REMARK 500 TYR A 194 -34.08 -154.37
REMARK 500 SER A 225 -119.54 63.76
REMARK 500 ALA A 249 58.97 26.44
REMARK 500 CYS A 348 118.95 -171.23
REMARK 500 TYR A 373 -85.82 -129.32
REMARK 500 SER A 383 -150.41 -132.47
REMARK 500 SER A 404 147.22 -171.95
REMARK 500 HIS A 488 132.80 -175.43
REMARK 500 ASN A 527 -147.84 -78.73
REMARK 500 CYS A 529 -24.06 75.37
REMARK 500 ALA A 571 148.99 -172.57
REMARK 500 ALA B 67 47.03 -103.24
REMARK 500 ASN B 134 -150.29 57.17
REMARK 500 ASN B 171 54.66 -91.08
REMARK 500 TYR B 194 -32.81 -153.28
REMARK 500 SER B 225 -119.65 70.43
REMARK 500 ALA B 249 65.45 32.86
REMARK 500 ASP B 311 12.95 -153.32
REMARK 500 TYR B 373 -100.30 -151.19
REMARK 500 SER B 383 -136.14 -140.30
REMARK 500 SER B 404 141.17 -174.94
REMARK 500 SER B 413 3.11 -158.96
REMARK 500 GLU B 429 77.05 -118.46
REMARK 500 ILE B 447 -57.79 -124.05
REMARK 500 ALA B 469 58.51 -154.20
REMARK 500 ASN B 527 -154.23 -93.61
REMARK 500 CYS B 529 -29.51 77.23
REMARK 500 ALA B 571 149.81 -175.43
REMARK 500 TYR B 579 132.57 -38.02
REMARK 500 ASP C 60 -35.25 -149.54
REMARK 500 ALA C 67 38.82 -95.70
REMARK 500 SER C 131 145.03 -172.08
REMARK 500 ASN C 134 -137.22 62.78
REMARK 500 ASN C 171 55.27 -92.88
REMARK 500 ALA C 176 35.80 -154.78
REMARK 500 LEU C 177 32.85 72.69
REMARK 500 TYR C 194 -27.42 -151.19
REMARK 500 SER C 225 -118.08 75.61
REMARK 500 ALA C 249 54.98 37.83
REMARK 500 ASP C 311 8.05 -150.74
REMARK 500 TYR C 373 -97.63 -152.64
REMARK 500 SER C 383 -150.95 -149.94
REMARK 500 SER C 413 -11.23 -143.76
REMARK 500 MET C 431 162.10 177.55
REMARK 500 SER C 491 31.66 -98.82
REMARK 500 ASN C 527 -148.57 -86.97
REMARK 500
REMARK 500 THIS ENTRY HAS 159 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 ASP A 347 CYS A 348 -143.71
REMARK 500 GLY B 335 GLN B 336 -145.29
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 A1227 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A1228 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A1229 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1230 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B1261 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B1262 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1263 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B1264 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B1265 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B1266 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C1223 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH C1224 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH C1225 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH C1226 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH D1218 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH D1219 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH F1246 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH F1247 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH J 928 DISTANCE = 5.98 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 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 60.6
REMARK 620 3 ASP A 307 OD1 78.6 136.5
REMARK 620 4 ASP A 307 OD2 88.8 133.3 53.3
REMARK 620 5 LEU A 309 O 82.0 85.3 74.0 127.2
REMARK 620 6 ASP A 311 OD1 130.4 71.5 139.3 136.8 82.0
REMARK 620 7 ILE A 313 O 95.2 73.5 128.2 75.5 156.8 82.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 704 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 347 OD2
REMARK 620 2 HOH F 999 O 108.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 93 OE1
REMARK 620 2 GLU B 93 OE2 53.1
REMARK 620 3 HOH B1199 O 99.8 93.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 69.8
REMARK 620 3 ASP B 307 OD1 73.8 136.3
REMARK 620 4 ASP B 307 OD2 72.6 134.9 47.9
REMARK 620 5 LEU B 309 O 86.7 79.0 75.4 122.8
REMARK 620 6 ASP B 311 OD1 145.2 76.2 131.3 141.1 79.4
REMARK 620 7 ILE B 313 O 106.5 94.8 118.4 72.7 162.8 83.5
REMARK 620 8 HOH B 924 O 138.9 146.4 65.1 78.4 85.1 71.9 91.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 93 OE2
REMARK 620 2 HOH C1132 O 94.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 69.3
REMARK 620 3 ASP C 307 OD1 70.6 129.2
REMARK 620 4 ASP C 307 OD2 73.3 136.5 51.7
REMARK 620 5 LEU C 309 O 86.1 78.6 68.8 120.4
REMARK 620 6 ASP C 311 OD1 149.0 80.0 131.1 136.4 83.9
REMARK 620 7 ILE C 313 O 96.0 90.4 123.7 72.1 167.3 88.0
REMARK 620 8 HOH C 840 O 138.4 150.0 69.7 73.0 90.6 71.0 96.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 703 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 93 OE2
REMARK 620 2 HOH D1127 O 87.2
REMARK 620 N 1
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 69.0
REMARK 620 3 ASP D 307 OD1 74.2 137.1
REMARK 620 4 ASP D 307 OD2 80.3 140.6 46.9
REMARK 620 5 LEU D 309 O 77.4 77.8 73.3 119.8
REMARK 620 6 ASP D 311 OD1 142.4 75.0 131.5 136.9 84.8
REMARK 620 7 ILE D 313 O 106.2 88.1 123.6 77.0 163.2 82.7
REMARK 620 8 HOH D 969 O 140.5 147.5 66.4 70.6 94.1 72.9 93.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 175 OD1
REMARK 620 2 HIS H 293 ND1 89.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 304 O
REMARK 620 2 ASP E 304 OD1 69.0
REMARK 620 3 ASP E 307 OD1 73.2 130.8
REMARK 620 4 ASP E 307 OD2 71.1 135.2 50.3
REMARK 620 5 LEU E 309 O 88.3 77.9 70.6 120.6
REMARK 620 6 ASP E 311 OD1 139.7 70.9 140.6 142.7 86.7
REMARK 620 7 ILE E 313 O 91.5 80.8 130.9 80.6 157.2 78.8
REMARK 620 8 HOH E 842 O 136.9 153.8 68.0 69.9 95.9 83.4 99.7
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 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 304 O
REMARK 620 2 ASP F 304 OD1 67.9
REMARK 620 3 ASP F 307 OD1 61.8 126.4
REMARK 620 4 ASP F 307 OD2 85.7 144.5 47.8
REMARK 620 5 LEU F 309 O 91.8 83.9 80.3 121.7
REMARK 620 6 ASP F 311 OD1 142.7 75.2 148.1 129.8 79.2
REMARK 620 7 ILE F 313 O 97.2 82.5 120.1 77.5 159.5 82.6
REMARK 620 8 HOH F 824 O 139.9 150.4 78.4 63.0 85.1 75.8 99.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 93 OE1
REMARK 620 2 GLU G 93 OE2 52.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 304 O
REMARK 620 2 ASP G 304 OD1 69.6
REMARK 620 3 ASP G 307 OD1 78.4 146.1
REMARK 620 4 ASP G 307 OD2 74.4 123.5 54.0
REMARK 620 5 LEU G 309 O 89.3 85.7 83.0 136.0
REMARK 620 6 ASP G 311 OD1 137.3 70.1 135.7 142.5 74.3
REMARK 620 7 ILE G 313 O 98.4 72.4 124.5 71.6 152.3 82.3
REMARK 620 8 HOH G 813 O 152.8 137.4 74.5 87.8 89.6 67.9 95.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 304 O
REMARK 620 2 ASP H 304 OD1 68.1
REMARK 620 3 ASP H 307 OD1 66.2 129.7
REMARK 620 4 ASP H 307 OD2 81.0 139.2 48.8
REMARK 620 5 LEU H 309 O 83.2 77.8 77.0 125.3
REMARK 620 6 ASP H 311 OD1 146.5 78.8 139.9 130.8 84.4
REMARK 620 7 ILE H 313 O 96.7 77.7 127.2 80.4 153.6 81.3
REMARK 620 8 HOH H 866 O 146.4 144.3 80.6 73.1 94.4 65.6 99.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 304 O
REMARK 620 2 ASP I 304 OD1 69.6
REMARK 620 3 ASP I 307 OD1 79.6 145.4
REMARK 620 4 ASP I 307 OD2 77.5 134.0 47.7
REMARK 620 5 LEU I 309 O 87.2 90.7 72.1 119.4
REMARK 620 6 ASP I 311 OD1 145.2 75.6 133.1 131.0 92.3
REMARK 620 7 ILE I 313 O 96.1 76.6 123.2 75.9 164.7 76.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA J 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 304 O
REMARK 620 2 ASP J 304 OD1 59.0
REMARK 620 3 ASP J 307 OD1 76.6 132.0
REMARK 620 4 ASP J 307 OD2 81.0 128.8 51.3
REMARK 620 5 LEU J 309 O 80.4 86.8 67.6 118.7
REMARK 620 6 ASP J 311 OD1 138.8 81.9 132.2 138.7 85.6
REMARK 620 7 ILE J 313 O 101.5 79.0 130.6 79.4 161.7 81.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA I 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA J 701
DBREF1 6QG9 A 20 603 UNP MHETH_IDESA
DBREF2 6QG9 A A0A0K8P8E7 20 603
DBREF1 6QG9 B 20 603 UNP MHETH_IDESA
DBREF2 6QG9 B A0A0K8P8E7 20 603
DBREF1 6QG9 C 20 603 UNP MHETH_IDESA
DBREF2 6QG9 C A0A0K8P8E7 20 603
DBREF1 6QG9 D 20 603 UNP MHETH_IDESA
DBREF2 6QG9 D A0A0K8P8E7 20 603
DBREF1 6QG9 E 20 603 UNP MHETH_IDESA
DBREF2 6QG9 E A0A0K8P8E7 20 603
DBREF1 6QG9 F 20 603 UNP MHETH_IDESA
DBREF2 6QG9 F A0A0K8P8E7 20 603
DBREF1 6QG9 G 20 603 UNP MHETH_IDESA
DBREF2 6QG9 G A0A0K8P8E7 20 603
DBREF1 6QG9 H 20 603 UNP MHETH_IDESA
DBREF2 6QG9 H A0A0K8P8E7 20 603
DBREF1 6QG9 I 20 603 UNP MHETH_IDESA
DBREF2 6QG9 I A0A0K8P8E7 20 603
DBREF1 6QG9 J 20 603 UNP MHETH_IDESA
DBREF2 6QG9 J A0A0K8P8E7 20 603
SEQADV 6QG9 MET A 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN A 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS A 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL A 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS A 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET A 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET B 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN B 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS B 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL B 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS B 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET B 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET C 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN C 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS C 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL C 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS C 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET C 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET D 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN D 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS D 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL D 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS D 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET D 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET E 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN E 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS E 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL E 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS E 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET E 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET F 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN F 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS F 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL F 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS F 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET F 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET G 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN G 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS G 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL G 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS G 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET G 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET H 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN H 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS H 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL H 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS H 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET H 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET I 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN I 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS I 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL I 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS I 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET I 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET J 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QG9 ASN J 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 LYS J 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 VAL J 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 HIS J 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QG9 MET J 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
SEQRES 1 G 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 G 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 G 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 G 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 G 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 G 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 G 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 G 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 G 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 G 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 G 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 G 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 G 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 G 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 G 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 G 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 G 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 G 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 G 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 G 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 G 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 G 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 G 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 G 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 G 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 G 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 G 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 G 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 G 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 G 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 G 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 G 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 G 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 G 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 G 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 G 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 G 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 G 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 G 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 G 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 G 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 G 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 G 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 G 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 G 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 G 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 H 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 H 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 H 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 H 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 H 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 H 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 H 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 H 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 H 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 H 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 H 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 H 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 H 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 H 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 H 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 H 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 H 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 H 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 H 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 H 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 H 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 H 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 H 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 H 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 H 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 H 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 H 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 H 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 H 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 H 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 H 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 H 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 H 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 H 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 H 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 H 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 H 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 H 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 H 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 H 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 H 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 H 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 H 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 H 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 H 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 H 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 I 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 I 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 I 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 I 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 I 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 I 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 I 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 I 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 I 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 I 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 I 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 I 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 I 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 I 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 I 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 I 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 I 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 I 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 I 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 I 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 I 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 I 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 I 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 I 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 I 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 I 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 I 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 I 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 I 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 I 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 I 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 I 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 I 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 I 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 I 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 I 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 I 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 I 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 I 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 I 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 I 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 I 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 I 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 I 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 I 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 I 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 J 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 J 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 J 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 J 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 J 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 J 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 J 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 J 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 J 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 J 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 J 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 J 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 J 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 J 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 J 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 J 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 J 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 J 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 J 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 J 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 J 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 J 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 J 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 J 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 J 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 J 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 J 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 J 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 J 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 J 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 J 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 J 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 J 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 J 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 J 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 J 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 J 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 J 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 J 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 J 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 J 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 J 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 J 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 J 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 J 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 J 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
HET EDO A 701 4
HET CA A 702 1
HET ZN A 703 1
HET ZN A 704 1
HET CA B 701 1
HET ZN B 702 1
HET CA C 701 1
HET ZN C 702 1
HET ACT D 701 4
HET CA D 702 1
HET ZN D 703 1
HET CA E 701 1
HET ZN E 702 1
HET ZN E 703 1
HET ACT F 701 4
HET CA F 702 1
HET ZN F 703 1
HET CA G 701 1
HET ZN G 702 1
HET CA H 701 1
HET ZN H 702 1
HET CA I 701 1
HET ZN I 702 1
HET CA J 701 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 11 EDO C2 H6 O2
FORMUL 12 CA 10(CA 2+)
FORMUL 13 ZN 11(ZN 2+)
FORMUL 19 ACT 2(C2 H3 O2 1-)
FORMUL 35 HOH *3445(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 PHE A 287 5 6
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 GLY A 414 PHE A 424 1 11
HELIX 17 AB8 PRO A 432 THR A 434 5 3
HELIX 18 AB9 GLN A 435 PHE A 443 1 9
HELIX 19 AC1 ILE A 447 TRP A 453 5 7
HELIX 20 AC2 SER A 462 GLY A 468 1 7
HELIX 21 AC3 LEU A 474 ARG A 480 1 7
HELIX 22 AC4 SER A 496 MET A 511 1 16
HELIX 23 AC5 GLY A 513 GLY A 516 5 4
HELIX 24 AC6 MET A 540 GLY A 551 1 12
HELIX 25 AC7 THR A 563 GLY A 568 5 6
HELIX 26 AC8 THR A 593 ALA A 595 5 3
HELIX 27 AC9 SER B 47 LEU B 54 1 8
HELIX 28 AD1 ALA B 152 ASN B 156 5 5
HELIX 29 AD2 LEU B 177 LEU B 184 5 8
HELIX 30 AD3 ASP B 185 TYR B 194 1 10
HELIX 31 AD4 TYR B 194 GLY B 213 1 20
HELIX 32 AD5 SER B 225 PHE B 238 1 14
HELIX 33 AD6 GLN B 253 PRO B 255 5 3
HELIX 34 AD7 LYS B 256 ALA B 269 1 14
HELIX 35 AD8 PRO B 270 ALA B 272 5 3
HELIX 36 AD9 LEU B 282 SER B 286 5 5
HELIX 37 AE1 SER B 288 ASP B 304 1 17
HELIX 38 AE2 ALA B 305 GLY B 308 5 4
HELIX 39 AE3 ASN B 316 PHE B 324 1 9
HELIX 40 AE4 SER B 350 GLY B 363 1 14
HELIX 41 AE5 ASP B 379 SER B 383 5 5
HELIX 42 AE6 TRP B 394 LEU B 399 1 6
HELIX 43 AE7 GLY B 414 PHE B 424 1 11
HELIX 44 AE8 PRO B 432 THR B 434 5 3
HELIX 45 AE9 GLN B 435 PHE B 443 1 9
HELIX 46 AF1 ILE B 447 TRP B 453 5 7
HELIX 47 AF2 SER B 462 GLY B 468 1 7
HELIX 48 AF3 LEU B 474 ARG B 480 1 7
HELIX 49 AF4 SER B 496 MET B 511 1 16
HELIX 50 AF5 GLY B 513 GLY B 516 5 4
HELIX 51 AF6 MET B 540 GLY B 551 1 12
HELIX 52 AF7 THR B 563 GLY B 568 5 6
HELIX 53 AF8 THR B 593 ALA B 595 5 3
HELIX 54 AF9 SER C 47 ALA C 53 1 7
HELIX 55 AG1 ALA C 152 ASN C 156 5 5
HELIX 56 AG2 LEU C 177 LEU C 184 5 8
HELIX 57 AG3 ASP C 185 TYR C 194 1 10
HELIX 58 AG4 TYR C 194 GLY C 213 1 20
HELIX 59 AG5 SER C 225 PHE C 238 1 14
HELIX 60 AG6 GLN C 253 PRO C 255 5 3
HELIX 61 AG7 LYS C 256 ALA C 269 1 14
HELIX 62 AG8 PRO C 270 ALA C 272 5 3
HELIX 63 AG9 LEU C 282 PHE C 287 5 6
HELIX 64 AH1 SER C 288 ASP C 304 1 17
HELIX 65 AH2 ALA C 305 GLY C 308 5 4
HELIX 66 AH3 ASN C 316 PHE C 324 1 9
HELIX 67 AH4 SER C 350 GLY C 363 1 14
HELIX 68 AH5 ASP C 379 SER C 383 5 5
HELIX 69 AH6 GLY C 414 PHE C 424 1 11
HELIX 70 AH7 PRO C 432 THR C 434 5 3
HELIX 71 AH8 GLN C 435 PHE C 443 1 9
HELIX 72 AH9 ILE C 447 TRP C 453 5 7
HELIX 73 AI1 SER C 462 GLY C 468 1 7
HELIX 74 AI2 LEU C 474 ASP C 479 1 6
HELIX 75 AI3 SER C 496 MET C 511 1 16
HELIX 76 AI4 GLY C 513 GLY C 516 5 4
HELIX 77 AI5 MET C 540 GLY C 551 1 12
HELIX 78 AI6 THR C 563 PHE C 567 5 5
HELIX 79 AI7 THR C 593 ALA C 595 5 3
HELIX 80 AI8 SER D 47 LEU D 54 1 8
HELIX 81 AI9 ALA D 152 ASN D 156 5 5
HELIX 82 AJ1 ASN D 173 LEU D 184 5 12
HELIX 83 AJ2 ASP D 185 TYR D 194 1 10
HELIX 84 AJ3 TYR D 194 GLY D 213 1 20
HELIX 85 AJ4 SER D 225 PHE D 238 1 14
HELIX 86 AJ5 GLN D 253 PRO D 255 5 3
HELIX 87 AJ6 LYS D 256 ALA D 269 1 14
HELIX 88 AJ7 PRO D 270 ALA D 272 5 3
HELIX 89 AJ8 LEU D 282 SER D 286 5 5
HELIX 90 AJ9 SER D 288 ASP D 304 1 17
HELIX 91 AK1 ALA D 305 GLY D 308 5 4
HELIX 92 AK2 ASN D 316 PHE D 324 1 9
HELIX 93 AK3 SER D 350 ALA D 362 1 13
HELIX 94 AK4 ASP D 379 SER D 383 5 5
HELIX 95 AK5 TRP D 394 LEU D 399 1 6
HELIX 96 AK6 GLY D 414 PHE D 424 1 11
HELIX 97 AK7 PRO D 432 THR D 434 5 3
HELIX 98 AK8 GLN D 435 PHE D 443 1 9
HELIX 99 AK9 ILE D 447 TRP D 453 5 7
HELIX 100 AL1 SER D 462 HIS D 467 1 6
HELIX 101 AL2 LEU D 474 ARG D 480 1 7
HELIX 102 AL3 SER D 496 MET D 511 1 16
HELIX 103 AL4 GLY D 513 GLY D 516 5 4
HELIX 104 AL5 MET D 540 GLY D 551 1 12
HELIX 105 AL6 THR D 563 GLY D 568 5 6
HELIX 106 AL7 THR D 593 ALA D 595 5 3
HELIX 107 AL8 SER E 47 ALA E 53 1 7
HELIX 108 AL9 ALA E 152 ASN E 156 5 5
HELIX 109 AM1 VAL E 180 LEU E 184 5 5
HELIX 110 AM2 ASP E 185 TYR E 194 1 10
HELIX 111 AM3 TYR E 194 GLY E 213 1 20
HELIX 112 AM4 SER E 225 PHE E 238 1 14
HELIX 113 AM5 GLN E 253 PRO E 255 5 3
HELIX 114 AM6 LYS E 256 ALA E 269 1 14
HELIX 115 AM7 PRO E 270 ALA E 272 5 3
HELIX 116 AM8 LEU E 282 SER E 286 5 5
HELIX 117 AM9 SER E 288 ASP E 304 1 17
HELIX 118 AN1 ALA E 305 GLY E 308 5 4
HELIX 119 AN2 ASN E 316 PHE E 324 1 9
HELIX 120 AN3 SER E 350 GLY E 363 1 14
HELIX 121 AN4 ASP E 379 SER E 383 5 5
HELIX 122 AN5 GLY E 414 PHE E 424 1 11
HELIX 123 AN6 PRO E 432 THR E 434 5 3
HELIX 124 AN7 GLN E 435 PHE E 443 1 9
HELIX 125 AN8 ILE E 447 TRP E 453 5 7
HELIX 126 AN9 SER E 462 HIS E 467 1 6
HELIX 127 AO1 LEU E 474 ARG E 480 1 7
HELIX 128 AO2 SER E 496 MET E 511 1 16
HELIX 129 AO3 GLY E 513 GLY E 516 5 4
HELIX 130 AO4 MET E 540 GLY E 551 1 12
HELIX 131 AO5 THR E 563 GLY E 568 5 6
HELIX 132 AO6 THR E 593 ALA E 595 5 3
HELIX 133 AO7 SER F 47 ALA F 53 1 7
HELIX 134 AO8 ALA F 152 ASN F 156 5 5
HELIX 135 AO9 LEU F 177 LEU F 184 5 8
HELIX 136 AP1 ASP F 185 TYR F 194 1 10
HELIX 137 AP2 TYR F 194 GLY F 213 1 20
HELIX 138 AP3 SER F 225 PHE F 238 1 14
HELIX 139 AP4 GLN F 253 PRO F 255 5 3
HELIX 140 AP5 LYS F 256 ALA F 269 1 14
HELIX 141 AP6 PRO F 270 ALA F 272 5 3
HELIX 142 AP7 LEU F 282 PHE F 287 5 6
HELIX 143 AP8 SER F 288 ASP F 304 1 17
HELIX 144 AP9 ALA F 305 GLY F 308 5 4
HELIX 145 AQ1 ASN F 316 PHE F 324 1 9
HELIX 146 AQ2 SER F 350 GLY F 363 1 14
HELIX 147 AQ3 ASP F 379 SER F 383 5 5
HELIX 148 AQ4 GLY F 414 PHE F 424 1 11
HELIX 149 AQ5 PRO F 432 THR F 434 5 3
HELIX 150 AQ6 GLN F 435 PHE F 443 1 9
HELIX 151 AQ7 ILE F 447 TRP F 453 5 7
HELIX 152 AQ8 SER F 462 GLY F 468 1 7
HELIX 153 AQ9 LEU F 474 ARG F 480 1 7
HELIX 154 AR1 SER F 496 MET F 511 1 16
HELIX 155 AR2 GLY F 513 GLY F 516 5 4
HELIX 156 AR3 MET F 540 GLY F 551 1 12
HELIX 157 AR4 THR F 563 GLY F 568 5 6
HELIX 158 AR5 THR F 593 ALA F 595 5 3
HELIX 159 AR6 SER G 47 ALA G 53 1 7
HELIX 160 AR7 LEU G 177 LEU G 184 5 8
HELIX 161 AR8 ASP G 185 TYR G 194 1 10
HELIX 162 AR9 TYR G 194 GLY G 213 1 20
HELIX 163 AS1 SER G 225 PHE G 238 1 14
HELIX 164 AS2 PRO G 239 TYR G 242 5 4
HELIX 165 AS3 GLN G 253 PRO G 255 5 3
HELIX 166 AS4 LYS G 256 ALA G 269 1 14
HELIX 167 AS5 PRO G 270 ALA G 272 5 3
HELIX 168 AS6 LEU G 282 PHE G 287 5 6
HELIX 169 AS7 SER G 288 ASP G 304 1 17
HELIX 170 AS8 ALA G 305 GLY G 308 5 4
HELIX 171 AS9 ASN G 316 PHE G 324 1 9
HELIX 172 AT1 SER G 350 GLY G 363 1 14
HELIX 173 AT2 ASP G 379 SER G 383 5 5
HELIX 174 AT3 TRP G 394 LEU G 399 1 6
HELIX 175 AT4 ALA G 409 GLY G 414 1 6
HELIX 176 AT5 GLY G 414 PHE G 424 1 11
HELIX 177 AT6 PRO G 432 THR G 434 5 3
HELIX 178 AT7 GLN G 435 PHE G 443 1 9
HELIX 179 AT8 ILE G 447 TRP G 453 5 7
HELIX 180 AT9 SER G 462 GLY G 468 1 7
HELIX 181 AU1 LEU G 474 ARG G 480 1 7
HELIX 182 AU2 SER G 496 MET G 511 1 16
HELIX 183 AU3 GLY G 513 GLY G 516 5 4
HELIX 184 AU4 MET G 540 GLY G 551 1 12
HELIX 185 AU5 THR G 563 GLY G 568 5 6
HELIX 186 AU6 THR G 593 ALA G 595 5 3
HELIX 187 AU7 SER H 47 LEU H 54 1 8
HELIX 188 AU8 ALA H 152 ASN H 156 5 5
HELIX 189 AU9 LEU H 177 LEU H 184 5 8
HELIX 190 AV1 ASP H 185 TYR H 194 1 10
HELIX 191 AV2 TYR H 194 GLY H 213 1 20
HELIX 192 AV3 SER H 225 PHE H 238 1 14
HELIX 193 AV4 GLN H 253 PRO H 255 5 3
HELIX 194 AV5 LYS H 256 ALA H 269 1 14
HELIX 195 AV6 PRO H 270 ALA H 272 5 3
HELIX 196 AV7 LEU H 282 PHE H 287 5 6
HELIX 197 AV8 SER H 288 ASP H 304 1 17
HELIX 198 AV9 ALA H 305 GLY H 308 5 4
HELIX 199 AW1 ASN H 316 ALA H 322 1 7
HELIX 200 AW2 ASP H 325 ALA H 329 5 5
HELIX 201 AW3 SER H 350 GLY H 363 1 14
HELIX 202 AW4 ASP H 379 SER H 383 5 5
HELIX 203 AW5 GLY H 414 PHE H 424 1 11
HELIX 204 AW6 PRO H 432 THR H 434 5 3
HELIX 205 AW7 GLN H 435 PHE H 443 1 9
HELIX 206 AW8 ILE H 447 ALA H 454 5 8
HELIX 207 AW9 SER H 462 HIS H 467 1 6
HELIX 208 AX1 LEU H 474 ARG H 480 1 7
HELIX 209 AX2 SER H 496 MET H 511 1 16
HELIX 210 AX3 GLY H 513 GLY H 516 5 4
HELIX 211 AX4 MET H 540 GLY H 551 1 12
HELIX 212 AX5 THR H 563 GLY H 568 5 6
HELIX 213 AX6 THR H 593 ALA H 595 5 3
HELIX 214 AX7 SER I 47 ALA I 53 1 7
HELIX 215 AX8 ALA I 152 ASN I 156 5 5
HELIX 216 AX9 LEU I 177 LEU I 184 5 8
HELIX 217 AY1 ASP I 185 TYR I 194 1 10
HELIX 218 AY2 TYR I 194 GLY I 213 1 20
HELIX 219 AY3 SER I 225 PHE I 238 1 14
HELIX 220 AY4 PRO I 239 TYR I 242 5 4
HELIX 221 AY5 GLN I 253 PRO I 255 5 3
HELIX 222 AY6 LYS I 256 ALA I 269 1 14
HELIX 223 AY7 PRO I 270 ALA I 272 5 3
HELIX 224 AY8 LEU I 282 PHE I 287 5 6
HELIX 225 AY9 SER I 288 ASP I 304 1 17
HELIX 226 AZ1 ALA I 305 GLY I 308 5 4
HELIX 227 AZ2 ASN I 316 PHE I 324 1 9
HELIX 228 AZ3 SER I 350 ALA I 362 1 13
HELIX 229 AZ4 ASP I 379 SER I 383 5 5
HELIX 230 AZ5 TRP I 394 LEU I 399 1 6
HELIX 231 AZ6 GLY I 414 ASP I 423 1 10
HELIX 232 AZ7 GLN I 435 PHE I 443 1 9
HELIX 233 AZ8 ILE I 447 ALA I 454 5 8
HELIX 234 AZ9 SER I 462 GLY I 468 1 7
HELIX 235 BA1 LEU I 474 ARG I 480 1 7
HELIX 236 BA2 SER I 496 MET I 511 1 16
HELIX 237 BA3 GLY I 513 GLY I 516 5 4
HELIX 238 BA4 MET I 540 GLY I 551 1 12
HELIX 239 BA5 THR I 563 GLY I 568 5 6
HELIX 240 BA6 THR I 593 ALA I 595 5 3
HELIX 241 BA7 SER J 47 ALA J 53 1 7
HELIX 242 BA8 SER J 151 ASN J 156 5 6
HELIX 243 BA9 LEU J 177 LEU J 184 5 8
HELIX 244 BB1 ASP J 185 TYR J 194 1 10
HELIX 245 BB2 TYR J 194 GLY J 213 1 20
HELIX 246 BB3 SER J 225 PHE J 238 1 14
HELIX 247 BB4 GLN J 253 PRO J 255 5 3
HELIX 248 BB5 LYS J 256 ALA J 269 1 14
HELIX 249 BB6 PRO J 270 ALA J 272 5 3
HELIX 250 BB7 LEU J 282 SER J 286 5 5
HELIX 251 BB8 SER J 288 ASP J 304 1 17
HELIX 252 BB9 ALA J 305 GLY J 308 5 4
HELIX 253 BC1 ASN J 316 ALA J 322 1 7
HELIX 254 BC2 SER J 350 GLY J 363 1 14
HELIX 255 BC3 ASP J 379 SER J 383 5 5
HELIX 256 BC4 GLY J 414 PHE J 424 1 11
HELIX 257 BC5 PRO J 432 THR J 434 5 3
HELIX 258 BC6 GLN J 435 LYS J 442 1 8
HELIX 259 BC7 ASP J 448 TRP J 453 5 6
HELIX 260 BC8 SER J 462 GLY J 468 1 7
HELIX 261 BC9 LEU J 474 ARG J 480 1 7
HELIX 262 BD1 SER J 496 MET J 511 1 16
HELIX 263 BD2 GLY J 513 GLY J 516 5 4
HELIX 264 BD3 MET J 540 GLY J 551 1 12
HELIX 265 BD4 THR J 563 GLY J 568 5 6
HELIX 266 BD5 THR J 593 ALA J 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 HIS A 91 N ARG A 76
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 VAL A 246 N PHE A 221
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ALA A 247
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O ARG A 519 N LEU A 486
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 600 N ILE A 582
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 MET B 127
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 244 N PHE B 221
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 598 N ARG B 584
SHEET 1 AA9 9 THR C 68 ARG C 76 0
SHEET 2 AA9 9 HIS C 91 THR C 102 -1 O GLU C 93 N ALA C 74
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 ILE C 160
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 ILE C 485 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 3 ARG C 537 PHE C 538 0
SHEET 2 AB2 3 ILE C 557 TRP C 560 -1 O TRP C 560 N ARG C 537
SHEET 3 AB2 3 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 598 N ARG C 584
SHEET 1 AB4 9 THR D 68 ARG D 76 0
SHEET 2 AB4 9 HIS D 91 THR D 102 -1 O ALA D 97 N VAL D 69
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 LYS D 483 N ILE D 245
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 600 N ILE D 582
SHEET 1 AB8 9 THR E 68 ARG E 76 0
SHEET 2 AB8 9 HIS E 91 THR E 102 -1 O HIS E 91 N ARG E 76
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 ILE E 485 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 HIS F 91 N ARG F 76
SHEET 3 AC3 9 PRO F 108 PRO F 118 -1 O MET F 117 N CYS F 92
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 ARG F 124 O ALA F 158
SHEET 6 AC3 9 LYS F 218 CYS F 224 1 O TYR F 220 N MET F 127
SHEET 7 AC3 9 GLY F 244 GLY F 248 1 O GLY F 244 N PHE F 221
SHEET 8 AC3 9 LYS F 483 GLY F 489 1 O LYS F 483 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 ARG F 574 N ALA F 559
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
SHEET 1 AC7 9 THR G 68 ARG G 76 0
SHEET 2 AC7 9 HIS G 91 THR G 102 -1 O GLU G 93 N ALA G 74
SHEET 3 AC7 9 PRO G 108 PRO G 118 -1 O LEU G 115 N VAL G 94
SHEET 4 AC7 9 ALA G 158 THR G 162 -1 O THR G 159 N ARG G 116
SHEET 5 AC7 9 ARG G 124 GLU G 128 1 N PHE G 126 O ALA G 158
SHEET 6 AC7 9 LYS G 218 CYS G 224 1 O TYR G 220 N PHE G 125
SHEET 7 AC7 9 GLY G 244 GLY G 248 1 O VAL G 246 N PHE G 221
SHEET 8 AC7 9 LYS G 483 GLY G 489 1 O ILE G 485 N ILE G 245
SHEET 9 AC7 9 ALA G 518 VAL G 523 1 O ARG G 519 N LEU G 486
SHEET 1 AC8 2 LEU G 385 SER G 386 0
SHEET 2 AC8 2 THR G 389 TYR G 390 -1 O THR G 389 N SER G 386
SHEET 1 AC9 3 ARG G 537 PHE G 538 0
SHEET 2 AC9 3 ILE G 557 TRP G 560 -1 O TRP G 560 N ARG G 537
SHEET 3 AC9 3 THR G 573 LEU G 576 -1 O LEU G 576 N ILE G 557
SHEET 1 AD1 2 ILE G 582 TYR G 585 0
SHEET 2 AD1 2 PHE G 597 ALA G 600 -1 O ALA G 600 N ILE G 582
SHEET 1 AD2 9 THR H 68 ARG H 76 0
SHEET 2 AD2 9 HIS H 91 THR H 102 -1 O HIS H 91 N ARG H 76
SHEET 3 AD2 9 PRO H 108 PRO H 118 -1 O LEU H 115 N VAL H 94
SHEET 4 AD2 9 ALA H 158 THR H 162 -1 O THR H 159 N ARG H 116
SHEET 5 AD2 9 ARG H 124 GLU H 128 1 N PHE H 126 O ALA H 158
SHEET 6 AD2 9 LYS H 218 CYS H 224 1 O TYR H 220 N PHE H 125
SHEET 7 AD2 9 GLY H 244 GLY H 248 1 O GLY H 248 N GLY H 223
SHEET 8 AD2 9 LYS H 483 GLY H 489 1 O ILE H 485 N ALA H 247
SHEET 9 AD2 9 ALA H 518 VAL H 523 1 O ARG H 519 N LEU H 486
SHEET 1 AD3 2 LEU H 385 SER H 386 0
SHEET 2 AD3 2 THR H 389 TYR H 390 -1 O THR H 389 N SER H 386
SHEET 1 AD4 3 ARG H 537 PHE H 538 0
SHEET 2 AD4 3 ILE H 557 TRP H 560 -1 O TRP H 560 N ARG H 537
SHEET 3 AD4 3 THR H 573 LEU H 576 -1 O ARG H 574 N ALA H 559
SHEET 1 AD5 2 ILE H 582 TYR H 585 0
SHEET 2 AD5 2 PHE H 597 ALA H 600 -1 O ALA H 600 N ILE H 582
SHEET 1 AD6 9 VAL I 69 ARG I 76 0
SHEET 2 AD6 9 HIS I 91 THR I 102 -1 O HIS I 91 N ARG I 76
SHEET 3 AD6 9 PRO I 108 PRO I 118 -1 O LEU I 115 N VAL I 94
SHEET 4 AD6 9 ALA I 158 THR I 162 -1 O THR I 159 N ARG I 116
SHEET 5 AD6 9 ARG I 124 GLU I 128 1 N ARG I 124 O ALA I 158
SHEET 6 AD6 9 LYS I 218 CYS I 224 1 O TYR I 220 N PHE I 125
SHEET 7 AD6 9 GLY I 244 GLY I 248 1 O GLY I 244 N PHE I 221
SHEET 8 AD6 9 LYS I 483 GLY I 489 1 O ILE I 485 N ALA I 247
SHEET 9 AD6 9 ALA I 518 VAL I 523 1 O ARG I 519 N LEU I 486
SHEET 1 AD7 2 LEU I 385 SER I 386 0
SHEET 2 AD7 2 THR I 389 TYR I 390 -1 O THR I 389 N SER I 386
SHEET 1 AD8 3 ARG I 537 PHE I 538 0
SHEET 2 AD8 3 ILE I 557 TRP I 560 -1 O TRP I 560 N ARG I 537
SHEET 3 AD8 3 THR I 573 LEU I 576 -1 O LEU I 576 N ILE I 557
SHEET 1 AD9 2 ILE I 582 TYR I 585 0
SHEET 2 AD9 2 PHE I 597 ALA I 600 -1 O ALA I 600 N ILE I 582
SHEET 1 AE1 9 THR J 68 ARG J 76 0
SHEET 2 AE1 9 HIS J 91 GLY J 103 -1 O GLU J 93 N ALA J 74
SHEET 3 AE1 9 GLY J 106 PRO J 118 -1 O LEU J 115 N VAL J 94
SHEET 4 AE1 9 ALA J 158 THR J 162 -1 O THR J 159 N ARG J 116
SHEET 5 AE1 9 ARG J 124 GLU J 128 1 N PHE J 126 O ALA J 158
SHEET 6 AE1 9 LYS J 218 CYS J 224 1 O TYR J 220 N PHE J 125
SHEET 7 AE1 9 GLY J 244 GLY J 248 1 O GLY J 248 N GLY J 223
SHEET 8 AE1 9 LYS J 483 GLY J 489 1 O ILE J 485 N ILE J 245
SHEET 9 AE1 9 ALA J 518 VAL J 523 1 O ARG J 519 N LEU J 486
SHEET 1 AE2 2 LEU J 385 SER J 386 0
SHEET 2 AE2 2 THR J 389 TYR J 390 -1 O THR J 389 N SER J 386
SHEET 1 AE3 3 ARG J 537 PHE J 538 0
SHEET 2 AE3 3 ILE J 557 TRP J 560 -1 O TRP J 560 N ARG J 537
SHEET 3 AE3 3 THR J 573 LEU J 576 -1 O ARG J 574 N ALA J 559
SHEET 1 AE4 2 ARG J 584 TYR J 585 0
SHEET 2 AE4 2 PHE J 597 ALA J 598 -1 O ALA J 598 N ARG J 584
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.10
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.10
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.05
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.04
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.08
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.13
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.06
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.13
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.04
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.06
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.07
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.14
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.09
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.06
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.09
SSBOND 16 CYS D 51 CYS D 92 1555 1555 2.09
SSBOND 17 CYS D 224 CYS D 529 1555 1555 2.11
SSBOND 18 CYS D 303 CYS D 320 1555 1555 2.14
SSBOND 19 CYS D 340 CYS D 348 1555 1555 2.04
SSBOND 20 CYS D 577 CYS D 599 1555 1555 2.06
SSBOND 21 CYS E 51 CYS E 92 1555 1555 2.09
SSBOND 22 CYS E 224 CYS E 529 1555 1555 2.10
SSBOND 23 CYS E 303 CYS E 320 1555 1555 2.07
SSBOND 24 CYS E 340 CYS E 348 1555 1555 2.06
SSBOND 25 CYS E 577 CYS E 599 1555 1555 2.09
SSBOND 26 CYS F 51 CYS F 92 1555 1555 2.09
SSBOND 27 CYS F 224 CYS F 529 1555 1555 2.11
SSBOND 28 CYS F 303 CYS F 320 1555 1555 2.12
SSBOND 29 CYS F 340 CYS F 348 1555 1555 2.08
SSBOND 30 CYS F 577 CYS F 599 1555 1555 2.08
SSBOND 31 CYS G 51 CYS G 92 1555 1555 2.05
SSBOND 32 CYS G 224 CYS G 529 1555 1555 2.11
SSBOND 33 CYS G 303 CYS G 320 1555 1555 2.07
SSBOND 34 CYS G 340 CYS G 348 1555 1555 2.04
SSBOND 35 CYS G 577 CYS G 599 1555 1555 2.06
SSBOND 36 CYS H 51 CYS H 92 1555 1555 2.07
SSBOND 37 CYS H 224 CYS H 529 1555 1555 2.10
SSBOND 38 CYS H 303 CYS H 320 1555 1555 2.07
SSBOND 39 CYS H 340 CYS H 348 1555 1555 2.06
SSBOND 40 CYS H 577 CYS H 599 1555 1555 2.06
SSBOND 41 CYS I 51 CYS I 92 1555 1555 2.06
SSBOND 42 CYS I 224 CYS I 529 1555 1555 2.06
SSBOND 43 CYS I 303 CYS I 320 1555 1555 2.09
SSBOND 44 CYS I 340 CYS I 348 1555 1555 2.05
SSBOND 45 CYS I 577 CYS I 599 1555 1555 2.04
SSBOND 46 CYS J 51 CYS J 92 1555 1555 2.04
SSBOND 47 CYS J 224 CYS J 529 1555 1555 2.06
SSBOND 48 CYS J 303 CYS J 320 1555 1555 2.05
SSBOND 49 CYS J 340 CYS J 348 1555 1555 2.04
SSBOND 50 CYS J 577 CYS J 599 1555 1555 2.06
LINK OE2 GLU A 93 ZN ZN A 703 1555 1555 2.31
LINK O ASP A 304 CA CA A 702 1555 1555 2.53
LINK OD1 ASP A 304 CA CA A 702 1555 1555 2.62
LINK OD1 ASP A 307 CA CA A 702 1555 1555 2.46
LINK OD2 ASP A 307 CA CA A 702 1555 1555 2.43
LINK O LEU A 309 CA CA A 702 1555 1555 2.25
LINK OD1 ASP A 311 CA CA A 702 1555 1555 2.37
LINK O ILE A 313 CA CA A 702 1555 1555 2.51
LINK OD2 ASP A 347 ZN ZN A 704 1555 1555 2.18
LINK OE1 GLU B 93 ZN ZN B 702 1555 1555 2.43
LINK OE2 GLU B 93 ZN ZN B 702 1555 1555 2.46
LINK O ASP B 304 CA CA B 701 1555 1555 2.48
LINK OD1 ASP B 304 CA CA B 701 1555 1555 2.31
LINK OD1 ASP B 307 CA CA B 701 1555 1555 2.67
LINK OD2 ASP B 307 CA CA B 701 1555 1555 2.73
LINK O LEU B 309 CA CA B 701 1555 1555 2.43
LINK OD1 ASP B 311 CA CA B 701 1555 1555 2.55
LINK O ILE B 313 CA CA B 701 1555 1555 2.44
LINK OE2 GLU C 93 ZN ZN C 702 1555 1555 2.48
LINK O ASP C 304 CA CA C 701 1555 1555 2.49
LINK OD1 ASP C 304 CA CA C 701 1555 1555 2.41
LINK OD1 ASP C 307 CA CA C 701 1555 1555 2.60
LINK OD2 ASP C 307 CA CA C 701 1555 1555 2.40
LINK O LEU C 309 CA CA C 701 1555 1555 2.55
LINK OD1 ASP C 311 CA CA C 701 1555 1555 2.42
LINK O ILE C 313 CA CA C 701 1555 1555 2.31
LINK OE2 GLU D 93 ZN ZN D 703 1555 1555 2.49
LINK O ASP D 304 CA CA D 702 1555 1555 2.37
LINK OD1 ASP D 304 CA CA D 702 1555 1555 2.40
LINK OD1 ASP D 307 CA CA D 702 1555 1555 2.77
LINK OD2 ASP D 307 CA CA D 702 1555 1555 2.79
LINK O LEU D 309 CA CA D 702 1555 1555 2.45
LINK OD1 ASP D 311 CA CA D 702 1555 1555 2.43
LINK O ILE D 313 CA CA D 702 1555 1555 2.33
LINK OE2 GLU E 93 ZN ZN E 703 1555 1555 2.01
LINK OD1 ASP E 175 ZN ZN E 702 1555 1555 2.29
LINK O ASP E 304 CA CA E 701 1555 1555 2.52
LINK OD1 ASP E 304 CA CA E 701 1555 1555 2.44
LINK OD1 ASP E 307 CA CA E 701 1555 1555 2.75
LINK OD2 ASP E 307 CA CA E 701 1555 1555 2.47
LINK O LEU E 309 CA CA E 701 1555 1555 2.24
LINK OD1 ASP E 311 CA CA E 701 1555 1555 2.52
LINK O ILE E 313 CA CA E 701 1555 1555 2.46
LINK OE2 GLU F 93 ZN ZN F 703 1555 1555 2.31
LINK O ASP F 304 CA CA F 702 1555 1555 2.56
LINK OD1 ASP F 304 CA CA F 702 1555 1555 2.39
LINK OD1 ASP F 307 CA CA F 702 1555 1555 2.73
LINK OD2 ASP F 307 CA CA F 702 1555 1555 2.65
LINK O LEU F 309 CA CA F 702 1555 1555 2.36
LINK OD1 ASP F 311 CA CA F 702 1555 1555 2.31
LINK O ILE F 313 CA CA F 702 1555 1555 2.36
LINK OE1 GLU G 93 ZN ZN G 702 1555 1555 2.53
LINK OE2 GLU G 93 ZN ZN G 702 1555 1555 2.47
LINK O ASP G 304 CA CA G 701 1555 1555 2.44
LINK OD1 ASP G 304 CA CA G 701 1555 1555 2.67
LINK OD1 ASP G 307 CA CA G 701 1555 1555 2.27
LINK OD2 ASP G 307 CA CA G 701 1555 1555 2.55
LINK O LEU G 309 CA CA G 701 1555 1555 2.38
LINK OD1 ASP G 311 CA CA G 701 1555 1555 2.50
LINK O ILE G 313 CA CA G 701 1555 1555 2.37
LINK OE1 GLU H 93 ZN ZN H 702 1555 1555 2.50
LINK O ASP H 304 CA CA H 701 1555 1555 2.55
LINK OD1 ASP H 304 CA CA H 701 1555 1555 2.32
LINK OD1 ASP H 307 CA CA H 701 1555 1555 2.65
LINK OD2 ASP H 307 CA CA H 701 1555 1555 2.68
LINK O LEU H 309 CA CA H 701 1555 1555 2.33
LINK OD1 ASP H 311 CA CA H 701 1555 1555 2.37
LINK O ILE H 313 CA CA H 701 1555 1555 2.51
LINK OD1 ASP I 175 ZN ZN I 702 1555 1555 2.41
LINK O ASP I 304 CA CA I 701 1555 1555 2.60
LINK OD1 ASP I 304 CA CA I 701 1555 1555 2.43
LINK OD1 ASP I 307 CA CA I 701 1555 1555 2.55
LINK OD2 ASP I 307 CA CA I 701 1555 1555 2.86
LINK O LEU I 309 CA CA I 701 1555 1555 2.24
LINK OD1 ASP I 311 CA CA I 701 1555 1555 2.77
LINK O ILE I 313 CA CA I 701 1555 1555 2.45
LINK O ASP J 304 CA CA J 701 1555 1555 3.05
LINK OD1 ASP J 304 CA CA J 701 1555 1555 2.41
LINK OD1 ASP J 307 CA CA J 701 1555 1555 2.68
LINK OD2 ASP J 307 CA CA J 701 1555 1555 2.35
LINK O LEU J 309 CA CA J 701 1555 1555 2.46
LINK OD1 ASP J 311 CA CA J 701 1555 1555 2.66
LINK O ILE J 313 CA CA J 701 1555 1555 2.25
LINK ZN ZN A 704 O HOH F 999 1555 1555 2.65
LINK CA CA B 701 O HOH B 924 1555 1555 2.24
LINK ZN ZN B 702 O HOH B1199 1555 1555 2.63
LINK CA CA C 701 O HOH C 840 1555 1555 2.67
LINK ZN ZN C 702 O HOH C1132 1555 1555 2.64
LINK CA CA D 702 O HOH D 969 1555 1555 2.26
LINK ZN ZN D 703 O HOH D1127 1555 1555 2.68
LINK CA CA E 701 O HOH E 842 1555 1555 2.39
LINK CA CA F 702 O HOH F 824 1555 1555 2.59
LINK CA CA G 701 O HOH G 813 1555 1555 2.84
LINK CA CA H 701 O HOH H 866 1555 1555 2.65
LINK ND1 HIS H 293 ZN ZN E 702 1555 1554 2.41
CISPEP 1 THR A 426 PRO A 427 0 0.31
CISPEP 2 TYR A 579 PRO A 580 0 9.20
CISPEP 3 THR B 426 PRO B 427 0 4.98
CISPEP 4 TYR B 579 PRO B 580 0 1.43
CISPEP 5 THR C 426 PRO C 427 0 -1.61
CISPEP 6 TYR C 579 PRO C 580 0 11.19
CISPEP 7 THR D 426 PRO D 427 0 -5.19
CISPEP 8 TYR D 579 PRO D 580 0 0.22
CISPEP 9 THR E 426 PRO E 427 0 1.07
CISPEP 10 TYR E 579 PRO E 580 0 8.12
CISPEP 11 THR F 426 PRO F 427 0 0.67
CISPEP 12 TYR F 579 PRO F 580 0 -0.31
CISPEP 13 THR G 426 PRO G 427 0 -2.64
CISPEP 14 TYR G 579 PRO G 580 0 1.44
CISPEP 15 THR H 426 PRO H 427 0 -0.80
CISPEP 16 TYR H 579 PRO H 580 0 0.07
CISPEP 17 THR I 426 PRO I 427 0 -1.57
CISPEP 18 TYR I 579 PRO I 580 0 -2.70
CISPEP 19 THR J 426 PRO J 427 0 2.59
CISPEP 20 TYR J 579 PRO J 580 0 4.40
SITE 1 AC1 8 TYR A 317 LEU A 522 CYS A 577 TYR A 579
SITE 2 AC1 8 PRO A 580 GLN A 581 ILE A 582 HOH A 863
SITE 1 AC2 5 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC2 5 ILE A 313
SITE 1 AC3 2 GLU A 93 HOH A1139
SITE 1 AC4 2 ASP A 347 HOH F 999
SITE 1 AC5 6 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AC5 6 ILE B 313 HOH B 924
SITE 1 AC6 4 GLU B 93 ARG B 116 HOH B1118 HOH B1199
SITE 1 AC7 6 ASP C 304 ASP C 307 LEU C 309 ASP C 311
SITE 2 AC7 6 ILE C 313 HOH C 840
SITE 1 AC8 3 GLU C 93 HOH C1132 HOH C1156
SITE 1 AC9 2 HIS D 293 HOH D1094
SITE 1 AD1 6 ASP D 304 ASP D 307 LEU D 309 ASP D 311
SITE 2 AD1 6 ILE D 313 HOH D 969
SITE 1 AD2 3 ARG D 76 GLU D 93 HOH D1127
SITE 1 AD3 6 ASP E 304 ASP E 307 LEU E 309 ASP E 311
SITE 2 AD3 6 ILE E 313 HOH E 842
SITE 1 AD4 2 ASP E 175 HIS H 293
SITE 1 AD5 2 GLU E 93 ARG E 116
SITE 1 AD6 9 LEU F 254 ALA F 257 TRP F 397 ARG F 411
SITE 2 AD6 9 SER F 416 HOH F 934 HOH F1005 HOH F1045
SITE 3 AD6 9 HOH F1078
SITE 1 AD7 6 ASP F 304 ASP F 307 LEU F 309 ASP F 311
SITE 2 AD7 6 ILE F 313 HOH F 824
SITE 1 AD8 1 GLU F 93
SITE 1 AD9 6 ASP G 304 ASP G 307 LEU G 309 ASP G 311
SITE 2 AD9 6 ILE G 313 HOH G 813
SITE 1 AE1 3 GLU G 93 ARG G 116 HOH G1027
SITE 1 AE2 6 ASP H 304 ASP H 307 LEU H 309 ASP H 311
SITE 2 AE2 6 ILE H 313 HOH H 866
SITE 1 AE3 2 GLU H 93 HOH H1027
SITE 1 AE4 5 ASP I 304 ASP I 307 LEU I 309 ASP I 311
SITE 2 AE4 5 ILE I 313
SITE 1 AE5 3 HOH B1077 ASP I 175 HOH I 990
SITE 1 AE6 5 ASP J 304 ASP J 307 LEU J 309 ASP J 311
SITE 2 AE6 5 ILE J 313
CRYST1 111.286 137.949 137.051 83.01 66.88 68.45 P 1 10
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 0.008986 -0.003549 -0.003931 0.00000
SCALE2 0.000000 0.007794 0.000205 0.00000
SCALE3 0.000000 0.000000 0.007937 0.00000
TER 4130 PRO A 603
TER 8260 PRO B 603
TER 12390 PRO C 603
TER 16520 PRO D 603
TER 20658 PRO E 603
TER 24788 PRO F 603
TER 28938 PRO G 603
TER 33052 PRO H 602
TER 37182 PRO I 603
TER 41287 CYS J 599
MASTER 2077 0 24 266 156 0 37 644755 10 237 460
END |