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HEADER HYDROLASE 10-JAN-19 6QGB
TITLE CRYSTAL STRUCTURE OF A PLASTIC DEGRADING ENZYME IN COMPLEX WITH A
TITLE 2 LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_0224;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PLASTIC-DEGRADING HYDROLASE, ALPHA/BETA HYDROLASE FOLD, I. SAKAIENSIS
KEYWDS 2 CATALYTIC TRIAD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.PALM,L.REISKY,D.BOETTCHER,H.MUELLER,E.A.P.MICHELS,C.WALCZAK,
AUTHOR 2 L.BERNDT,M.S.WEISS,U.T.BORNSCHEUER,G.WEBER
REVDAT 1 03-APR-19 6QGB 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. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 254007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2667
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 46.0965 - 5.8640 0.97 13512 143 0.1507 0.1530
REMARK 3 2 5.8640 - 4.6559 0.99 13426 143 0.1415 0.1717
REMARK 3 3 4.6559 - 4.0677 0.99 13387 142 0.1255 0.1477
REMARK 3 4 4.0677 - 3.6960 1.00 13355 142 0.1411 0.1681
REMARK 3 5 3.6960 - 3.4312 0.98 13115 139 0.1589 0.2095
REMARK 3 6 3.4312 - 3.2289 0.99 13312 141 0.1766 0.2043
REMARK 3 7 3.2289 - 3.0673 1.00 13272 141 0.1908 0.2159
REMARK 3 8 3.0673 - 2.9338 1.00 13317 141 0.1934 0.2349
REMARK 3 9 2.9338 - 2.8208 1.00 13289 141 0.2050 0.2553
REMARK 3 10 2.8208 - 2.7235 1.00 13261 141 0.2068 0.2416
REMARK 3 11 2.7235 - 2.6384 1.00 13268 141 0.2259 0.2106
REMARK 3 12 2.6384 - 2.5630 1.00 13246 140 0.2292 0.2676
REMARK 3 13 2.5630 - 2.4955 1.00 13244 141 0.2392 0.2311
REMARK 3 14 2.4955 - 2.4346 0.99 13091 139 0.2562 0.2924
REMARK 3 15 2.4346 - 2.3793 0.99 13135 139 0.2627 0.2917
REMARK 3 16 2.3793 - 2.3286 0.99 13181 140 0.2670 0.3275
REMARK 3 17 2.3286 - 2.2821 1.00 13216 140 0.2786 0.3095
REMARK 3 18 2.2821 - 2.2390 1.00 13211 140 0.2791 0.2929
REMARK 3 19 2.2390 - 2.1990 0.94 12502 133 0.2954 0.3456
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.110
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 : 0.007 25490
REMARK 3 ANGLE : 0.707 34727
REMARK 3 CHIRALITY : 0.048 3638
REMARK 3 PLANARITY : 0.005 4635
REMARK 3 DIHEDRAL : 12.754 14906
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 44
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2865 9.3285 -74.6832
REMARK 3 T TENSOR
REMARK 3 T11: 0.5037 T22: 0.4183
REMARK 3 T33: 0.4667 T12: 0.1159
REMARK 3 T13: -0.1211 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 2.9049 L22: 2.5494
REMARK 3 L33: 1.4558 L12: 1.3780
REMARK 3 L13: 0.1265 L23: 1.0752
REMARK 3 S TENSOR
REMARK 3 S11: -0.1670 S12: 0.2632 S13: 0.5124
REMARK 3 S21: -0.2748 S22: -0.0321 S23: 0.4705
REMARK 3 S31: -0.6781 S32: -0.3874 S33: 0.2090
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4381 4.3982 -62.0466
REMARK 3 T TENSOR
REMARK 3 T11: 0.3258 T22: 0.3273
REMARK 3 T33: 0.4239 T12: 0.0673
REMARK 3 T13: -0.0254 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 2.0814 L22: 1.2637
REMARK 3 L33: 0.7088 L12: 1.5794
REMARK 3 L13: 0.4328 L23: 0.0541
REMARK 3 S TENSOR
REMARK 3 S11: -0.1022 S12: -0.0651 S13: 0.1998
REMARK 3 S21: -0.1295 S22: -0.0691 S23: 0.2900
REMARK 3 S31: -0.1455 S32: -0.1014 S33: 0.1635
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9422 0.5149 -61.5993
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.2916
REMARK 3 T33: 0.3311 T12: 0.0221
REMARK 3 T13: -0.0280 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.7971 L22: 1.2632
REMARK 3 L33: 1.1955 L12: 0.2342
REMARK 3 L13: 0.3104 L23: -0.2690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0734 S12: -0.0319 S13: 0.1127
REMARK 3 S21: 0.0058 S22: -0.0825 S23: 0.1169
REMARK 3 S31: -0.0782 S32: -0.0515 S33: 0.1453
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 174 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1255 -6.9112 -64.3219
REMARK 3 T TENSOR
REMARK 3 T11: 0.2930 T22: 0.3279
REMARK 3 T33: 0.3498 T12: 0.0666
REMARK 3 T13: -0.0334 T23: -0.0474
REMARK 3 L TENSOR
REMARK 3 L11: 2.7821 L22: 2.3056
REMARK 3 L33: 1.2020 L12: 1.8913
REMARK 3 L13: -0.5932 L23: -0.8022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0304 S12: -0.0577 S13: 0.1210
REMARK 3 S21: -0.1284 S22: 0.0472 S23: 0.2851
REMARK 3 S31: -0.0500 S32: -0.1914 S33: -0.0721
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3156 -15.1763 -57.8853
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.3294
REMARK 3 T33: 0.3480 T12: 0.0138
REMARK 3 T13: -0.0091 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.1912 L22: 1.1386
REMARK 3 L33: 0.8881 L12: 0.3979
REMARK 3 L13: 0.0685 L23: -0.3080
REMARK 3 S TENSOR
REMARK 3 S11: 0.0591 S12: -0.1474 S13: -0.1222
REMARK 3 S21: -0.0320 S22: -0.1156 S23: 0.0403
REMARK 3 S31: 0.0388 S32: 0.0033 S33: 0.0470
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 272 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9849 -20.6029 -32.6721
REMARK 3 T TENSOR
REMARK 3 T11: 0.4559 T22: 0.5448
REMARK 3 T33: 0.3914 T12: -0.0782
REMARK 3 T13: -0.0752 T23: 0.1018
REMARK 3 L TENSOR
REMARK 3 L11: 2.0454 L22: 0.6954
REMARK 3 L33: 1.3406 L12: 0.1120
REMARK 3 L13: -0.2667 L23: 0.2709
REMARK 3 S TENSOR
REMARK 3 S11: 0.2222 S12: -0.5643 S13: -0.2895
REMARK 3 S21: 0.3307 S22: -0.2004 S23: -0.0439
REMARK 3 S31: 0.1500 S32: -0.2639 S33: -0.0218
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 334 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7660 -26.5073 -32.8331
REMARK 3 T TENSOR
REMARK 3 T11: 0.4460 T22: 0.5975
REMARK 3 T33: 0.4495 T12: -0.1361
REMARK 3 T13: -0.0492 T23: 0.1477
REMARK 3 L TENSOR
REMARK 3 L11: 1.5715 L22: 1.3404
REMARK 3 L33: 1.8033 L12: -0.1331
REMARK 3 L13: -0.3800 L23: -0.3210
REMARK 3 S TENSOR
REMARK 3 S11: 0.2526 S12: -0.7221 S13: -0.4290
REMARK 3 S21: 0.3823 S22: -0.1445 S23: -0.1454
REMARK 3 S31: 0.0332 S32: -0.1341 S33: -0.1507
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6022 -11.2681 -34.1541
REMARK 3 T TENSOR
REMARK 3 T11: 0.4579 T22: 0.6199
REMARK 3 T33: 0.3622 T12: -0.0533
REMARK 3 T13: 0.0104 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 5.0328 L22: 1.4296
REMARK 3 L33: 0.8422 L12: 1.4764
REMARK 3 L13: -0.0399 L23: -0.7037
REMARK 3 S TENSOR
REMARK 3 S11: 0.2781 S12: -0.9105 S13: 0.3466
REMARK 3 S21: 0.3573 S22: -0.2581 S23: 0.0432
REMARK 3 S31: -0.1390 S32: -0.3182 S33: -0.0242
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 415 THROUGH 453 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8796 -20.9190 -45.7888
REMARK 3 T TENSOR
REMARK 3 T11: 0.3347 T22: 0.5839
REMARK 3 T33: 0.3992 T12: -0.0601
REMARK 3 T13: 0.0083 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.4355 L22: 2.1472
REMARK 3 L33: 2.3171 L12: -0.1015
REMARK 3 L13: 0.4842 L23: 0.1845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0638 S12: -0.5666 S13: -0.1282
REMARK 3 S21: 0.3106 S22: -0.0627 S23: 0.1879
REMARK 3 S31: 0.2213 S32: -0.4705 S33: 0.0081
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 454 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6830 -21.2255 -59.8694
REMARK 3 T TENSOR
REMARK 3 T11: 0.3045 T22: 0.2985
REMARK 3 T33: 0.3763 T12: 0.0055
REMARK 3 T13: -0.0102 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.1253 L22: 0.6548
REMARK 3 L33: 0.8975 L12: 0.1534
REMARK 3 L13: 0.5833 L23: 0.1114
REMARK 3 S TENSOR
REMARK 3 S11: 0.1051 S12: -0.0522 S13: -0.1973
REMARK 3 S21: 0.0357 S22: -0.0593 S23: -0.0691
REMARK 3 S31: 0.1171 S32: -0.1026 S33: -0.0555
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8771 -9.3565 -55.7502
REMARK 3 T TENSOR
REMARK 3 T11: 0.2971 T22: 0.3059
REMARK 3 T33: 0.3443 T12: -0.0013
REMARK 3 T13: -0.0147 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.8872 L22: 1.1161
REMARK 3 L33: 3.5322 L12: -0.0811
REMARK 3 L13: 0.5903 L23: 0.4931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: -0.0832 S13: -0.0266
REMARK 3 S21: 0.0006 S22: -0.0042 S23: -0.1480
REMARK 3 S31: -0.0856 S32: 0.2056 S33: -0.0240
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2574 -13.2039 -45.4426
REMARK 3 T TENSOR
REMARK 3 T11: 0.3662 T22: 0.3840
REMARK 3 T33: 0.3806 T12: 0.0146
REMARK 3 T13: -0.0426 T23: 0.0566
REMARK 3 L TENSOR
REMARK 3 L11: 1.5436 L22: 0.7194
REMARK 3 L33: 1.5831 L12: 0.1878
REMARK 3 L13: 0.5265 L23: 0.7133
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.1166 S13: -0.0134
REMARK 3 S21: 0.1559 S22: 0.0384 S23: -0.2941
REMARK 3 S31: 0.1292 S32: 0.2811 S33: -0.0464
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7898 -20.2050 31.3507
REMARK 3 T TENSOR
REMARK 3 T11: 0.4454 T22: 0.4592
REMARK 3 T33: 0.3333 T12: 0.0480
REMARK 3 T13: 0.0605 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 4.4794 L22: 1.2345
REMARK 3 L33: 5.3999 L12: -1.7323
REMARK 3 L13: 4.3770 L23: -2.3787
REMARK 3 S TENSOR
REMARK 3 S11: -0.3377 S12: -0.7219 S13: -0.0209
REMARK 3 S21: 0.3910 S22: 0.2735 S23: 0.1502
REMARK 3 S31: -0.1484 S32: -0.5365 S33: 0.0664
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2852 -32.7798 1.9673
REMARK 3 T TENSOR
REMARK 3 T11: 0.2823 T22: 0.2505
REMARK 3 T33: 0.3133 T12: -0.0134
REMARK 3 T13: -0.0027 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.5071 L22: 0.3326
REMARK 3 L33: 0.9874 L12: -0.0917
REMARK 3 L13: 0.2119 L23: 0.1869
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: 0.0406 S13: -0.0851
REMARK 3 S21: 0.0327 S22: 0.0236 S23: 0.0165
REMARK 3 S31: 0.1443 S32: 0.0285 S33: -0.0314
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3314 -31.4918 -2.5589
REMARK 3 T TENSOR
REMARK 3 T11: 0.2940 T22: 0.2968
REMARK 3 T33: 0.2794 T12: 0.0041
REMARK 3 T13: 0.0000 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0932 L22: 0.8027
REMARK 3 L33: 0.9633 L12: 0.0189
REMARK 3 L13: 0.3219 L23: 0.1842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: 0.0661 S13: -0.0847
REMARK 3 S21: 0.0332 S22: -0.0094 S23: -0.0348
REMARK 3 S31: 0.1480 S32: 0.0939 S33: -0.0404
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7241 1.9064 31.1156
REMARK 3 T TENSOR
REMARK 3 T11: 0.4615 T22: 0.3879
REMARK 3 T33: 0.3229 T12: 0.0851
REMARK 3 T13: -0.0786 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 6.1711 L22: 0.9112
REMARK 3 L33: 6.2153 L12: -0.4075
REMARK 3 L13: -4.9875 L23: 1.5706
REMARK 3 S TENSOR
REMARK 3 S11: -0.1934 S12: -0.7369 S13: -0.0904
REMARK 3 S21: 0.4215 S22: 0.0861 S23: -0.2312
REMARK 3 S31: -0.0255 S32: 0.4118 S33: 0.0976
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 77 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7432 11.8710 5.6069
REMARK 3 T TENSOR
REMARK 3 T11: 0.3163 T22: 0.2669
REMARK 3 T33: 0.3242 T12: -0.0071
REMARK 3 T13: 0.0031 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.6575 L22: 0.6160
REMARK 3 L33: 0.7786 L12: -0.0949
REMARK 3 L13: -0.0837 L23: -0.0099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: 0.0396 S13: 0.0576
REMARK 3 S21: -0.0039 S22: 0.0172 S23: -0.0131
REMARK 3 S31: -0.1214 S32: 0.0118 S33: -0.0092
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 334 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4726 14.2160 -8.8786
REMARK 3 T TENSOR
REMARK 3 T11: 0.4033 T22: 0.3420
REMARK 3 T33: 0.3238 T12: -0.0157
REMARK 3 T13: 0.0146 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.9980 L22: 1.0335
REMARK 3 L33: 0.8259 L12: 0.0389
REMARK 3 L13: -0.1664 L23: -0.2585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.1931 S13: 0.1490
REMARK 3 S21: -0.1759 S22: -0.0066 S23: -0.0570
REMARK 3 S31: -0.1752 S32: -0.0067 S33: 0.0112
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 524 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.3761 14.2123 0.8660
REMARK 3 T TENSOR
REMARK 3 T11: 0.3424 T22: 0.3727
REMARK 3 T33: 0.3581 T12: 0.0333
REMARK 3 T13: -0.0133 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.3487 L22: 2.3659
REMARK 3 L33: 1.5101 L12: -0.3287
REMARK 3 L13: 0.1187 L23: 0.0595
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: 0.1820 S13: 0.1496
REMARK 3 S21: -0.1657 S22: -0.0625 S23: 0.3197
REMARK 3 S31: -0.2380 S32: -0.2504 S33: 0.0149
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5117 6.2237 -75.8541
REMARK 3 T TENSOR
REMARK 3 T11: 0.4846 T22: 0.3876
REMARK 3 T33: 0.4704 T12: 0.0527
REMARK 3 T13: 0.0988 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 2.8755 L22: 2.9815
REMARK 3 L33: 0.9755 L12: 1.5371
REMARK 3 L13: -0.3195 L23: -0.7404
REMARK 3 S TENSOR
REMARK 3 S11: -0.2429 S12: 0.1980 S13: -0.4194
REMARK 3 S21: -0.2498 S22: 0.0856 S23: -0.4253
REMARK 3 S31: 0.4630 S32: 0.1395 S33: 0.1571
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.5923 12.4632 -61.4249
REMARK 3 T TENSOR
REMARK 3 T11: 0.3268 T22: 0.3330
REMARK 3 T33: 0.3494 T12: 0.0332
REMARK 3 T13: 0.0050 T23: 0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 0.8428 L22: 0.6950
REMARK 3 L33: 0.8105 L12: 0.3933
REMARK 3 L13: -0.1004 L23: 0.1426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: -0.0476 S13: -0.1555
REMARK 3 S21: 0.0129 S22: -0.0241 S23: -0.1455
REMARK 3 S31: 0.1339 S32: 0.1478 S33: 0.0557
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 178 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1545 20.6044 -67.1556
REMARK 3 T TENSOR
REMARK 3 T11: 0.2930 T22: 0.3261
REMARK 3 T33: 0.3132 T12: 0.0356
REMARK 3 T13: 0.0230 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 3.0219 L22: 1.9421
REMARK 3 L33: 1.6105 L12: 1.5958
REMARK 3 L13: 0.3247 L23: 0.8679
REMARK 3 S TENSOR
REMARK 3 S11: -0.1346 S12: 0.0971 S13: -0.0313
REMARK 3 S21: -0.2378 S22: 0.1056 S23: -0.1581
REMARK 3 S31: -0.0946 S32: 0.1706 S33: 0.0299
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 218 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7544 30.2321 -41.4609
REMARK 3 T TENSOR
REMARK 3 T11: 0.3334 T22: 0.3693
REMARK 3 T33: 0.3185 T12: 0.0143
REMARK 3 T13: -0.0231 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.8527 L22: 0.4284
REMARK 3 L33: 0.5783 L12: 0.1126
REMARK 3 L13: -0.3643 L23: 0.0709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.2343 S13: 0.0100
REMARK 3 S21: 0.1350 S22: -0.0019 S23: -0.0086
REMARK 3 S31: -0.0242 S32: 0.2033 S33: -0.0002
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 334 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7233 30.5942 -31.0360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3817 T22: 0.4659
REMARK 3 T33: 0.3288 T12: -0.0098
REMARK 3 T13: -0.0596 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.1879 L22: 1.7769
REMARK 3 L33: 2.2130 L12: 0.3583
REMARK 3 L13: -0.3657 L23: -0.0557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: -0.4858 S13: -0.0102
REMARK 3 S21: 0.2546 S22: -0.0173 S23: -0.0554
REMARK 3 S31: 0.1180 S32: 0.2992 S33: -0.0291
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 415 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5740 34.0293 -52.1626
REMARK 3 T TENSOR
REMARK 3 T11: 0.3026 T22: 0.3353
REMARK 3 T33: 0.3397 T12: -0.0113
REMARK 3 T13: -0.0188 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.4646 L22: 0.5925
REMARK 3 L33: 0.7956 L12: 0.1632
REMARK 3 L13: -0.2716 L23: -0.1873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: -0.1385 S13: 0.0890
REMARK 3 S21: 0.0386 S22: -0.0238 S23: -0.1092
REMARK 3 S31: -0.0508 S32: 0.2308 S33: 0.0024
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 524 THROUGH 572 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3755 21.0728 -50.1404
REMARK 3 T TENSOR
REMARK 3 T11: 0.3044 T22: 0.2826
REMARK 3 T33: 0.3205 T12: 0.0139
REMARK 3 T13: -0.0101 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.9717 L22: 1.6355
REMARK 3 L33: 2.4709 L12: 0.3629
REMARK 3 L13: -1.3511 L23: -0.7043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0461 S12: -0.0269 S13: -0.1006
REMARK 3 S21: 0.1027 S22: 0.0355 S23: 0.0881
REMARK 3 S31: 0.0386 S32: -0.1200 S33: -0.0074
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 573 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0310 28.0449 -45.1675
REMARK 3 T TENSOR
REMARK 3 T11: 0.3344 T22: 0.3354
REMARK 3 T33: 0.3708 T12: 0.0047
REMARK 3 T13: -0.0256 T23: -0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 4.7429 L22: 4.7818
REMARK 3 L33: 3.8527 L12: 2.9219
REMARK 3 L13: -2.7279 L23: -3.7863
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: -0.0904 S13: 0.0466
REMARK 3 S21: -0.1449 S22: 0.0636 S23: 0.5499
REMARK 3 S31: 0.0209 S32: -0.1311 S33: -0.1050
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1995 -19.1282 29.1761
REMARK 3 T TENSOR
REMARK 3 T11: 0.4553 T22: 0.3238
REMARK 3 T33: 0.3934 T12: -0.0870
REMARK 3 T13: 0.0004 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 3.2843 L22: 1.6386
REMARK 3 L33: 4.3048 L12: -1.0342
REMARK 3 L13: 2.5304 L23: -1.0405
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: 0.3911 S13: 0.4323
REMARK 3 S21: -0.2521 S22: 0.0728 S23: -0.1265
REMARK 3 S31: -0.4939 S32: 0.4334 S33: 0.1115
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 77 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5898 -33.0112 28.9892
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.3057
REMARK 3 T33: 0.3056 T12: -0.0265
REMARK 3 T13: 0.0173 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.2231 L22: 0.7522
REMARK 3 L33: 0.4818 L12: -0.0733
REMARK 3 L13: 0.6643 L23: 0.2044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0752 S12: 0.1820 S13: 0.0802
REMARK 3 S21: -0.1346 S22: 0.0235 S23: 0.0118
REMARK 3 S31: -0.1054 S32: 0.1080 S33: 0.0461
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 149 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5424 -36.4338 35.1374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2870 T22: 0.2646
REMARK 3 T33: 0.2866 T12: -0.0429
REMARK 3 T13: 0.0325 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.1460 L22: 1.6013
REMARK 3 L33: 1.0444 L12: -1.4841
REMARK 3 L13: 0.7731 L23: -0.1159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.0361 S13: 0.0812
REMARK 3 S21: -0.1485 S22: 0.0148 S23: -0.1698
REMARK 3 S31: -0.0306 S32: 0.0258 S33: -0.0169
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 213 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9335 -58.8528 39.9449
REMARK 3 T TENSOR
REMARK 3 T11: 0.3211 T22: 0.3028
REMARK 3 T33: 0.2956 T12: -0.0234
REMARK 3 T13: 0.0102 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.8508 L22: 0.6514
REMARK 3 L33: 0.4059 L12: -0.0679
REMARK 3 L13: -0.0238 L23: 0.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: -0.0454 S13: -0.1363
REMARK 3 S21: -0.0273 S22: 0.0533 S23: -0.0148
REMARK 3 S31: 0.1008 S32: -0.0097 S33: -0.0093
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7438 -44.8146 34.9280
REMARK 3 T TENSOR
REMARK 3 T11: 0.3045 T22: 0.3549
REMARK 3 T33: 0.3343 T12: -0.0281
REMARK 3 T13: -0.0105 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.2222 L22: 2.6344
REMARK 3 L33: 0.7309 L12: 0.5784
REMARK 3 L13: 0.2608 L23: 1.0146
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: 0.0113 S13: -0.0388
REMARK 3 S21: -0.0738 S22: 0.0169 S23: 0.2930
REMARK 3 S31: 0.0104 S32: -0.1072 S33: 0.0649
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9184 -55.7982 33.0031
REMARK 3 T TENSOR
REMARK 3 T11: 0.3350 T22: 0.3662
REMARK 3 T33: 0.3905 T12: -0.0520
REMARK 3 T13: -0.0079 T23: 0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 2.6866 L22: 1.5887
REMARK 3 L33: 4.6937 L12: 0.1818
REMARK 3 L13: 0.8848 L23: 1.7704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0328 S13: -0.0612
REMARK 3 S21: 0.0014 S22: -0.0409 S23: 0.2304
REMARK 3 S31: 0.2531 S32: -0.8587 S33: 0.0342
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 43 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5135 -0.9529 -95.2149
REMARK 3 T TENSOR
REMARK 3 T11: 0.4950 T22: 0.3459
REMARK 3 T33: 0.4308 T12: -0.1024
REMARK 3 T13: -0.0352 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 2.8281 L22: 1.9875
REMARK 3 L33: 3.0923 L12: -1.2774
REMARK 3 L13: 1.5099 L23: -0.7981
REMARK 3 S TENSOR
REMARK 3 S11: -0.2139 S12: 0.3522 S13: 0.4520
REMARK 3 S21: -0.4231 S22: 0.1334 S23: -0.1141
REMARK 3 S31: -0.3915 S32: 0.2826 S33: 0.1231
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 77 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5083 -14.1229 -98.5583
REMARK 3 T TENSOR
REMARK 3 T11: 0.3648 T22: 0.3843
REMARK 3 T33: 0.3271 T12: -0.0087
REMARK 3 T13: 0.0401 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 2.0877 L22: 1.2760
REMARK 3 L33: 1.1856 L12: -0.1653
REMARK 3 L13: 1.7201 L23: 0.0274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0713 S12: 0.2964 S13: 0.0253
REMARK 3 S21: -0.1518 S22: -0.0026 S23: -0.1060
REMARK 3 S31: -0.1925 S32: 0.2116 S33: 0.0631
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 111 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1494 -17.7337 -95.8784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3699 T22: 0.3177
REMARK 3 T33: 0.2978 T12: -0.0200
REMARK 3 T13: -0.0161 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.4911 L22: 1.1618
REMARK 3 L33: 0.6562 L12: 0.1609
REMARK 3 L13: 0.1322 L23: -0.2554
REMARK 3 S TENSOR
REMARK 3 S11: -0.1622 S12: 0.1406 S13: 0.0459
REMARK 3 S21: -0.1419 S22: 0.1118 S23: -0.0124
REMARK 3 S31: -0.0134 S32: 0.0665 S33: 0.0403
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 178 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6175 -15.6682 -86.9119
REMARK 3 T TENSOR
REMARK 3 T11: 0.3284 T22: 0.3060
REMARK 3 T33: 0.3469 T12: -0.0287
REMARK 3 T13: -0.0250 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 2.1033 L22: 1.2154
REMARK 3 L33: 0.4746 L12: -0.7259
REMARK 3 L13: 0.6497 L23: -0.3934
REMARK 3 S TENSOR
REMARK 3 S11: -0.2114 S12: -0.0580 S13: 0.1128
REMARK 3 S21: 0.1042 S22: 0.0692 S23: -0.0707
REMARK 3 S31: -0.0936 S32: 0.0486 S33: 0.1465
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 218 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8493 -31.1141 -85.3298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2889 T22: 0.2927
REMARK 3 T33: 0.3130 T12: 0.0199
REMARK 3 T13: 0.0042 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.6159 L22: 0.7210
REMARK 3 L33: 0.7197 L12: 0.5112
REMARK 3 L13: -0.0126 L23: 0.4729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0734 S12: -0.0346 S13: -0.0755
REMARK 3 S21: -0.0493 S22: 0.0756 S23: -0.0618
REMARK 3 S31: -0.0279 S32: 0.0957 S33: 0.0082
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 272 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0981 -53.9146 -93.9209
REMARK 3 T TENSOR
REMARK 3 T11: 0.3845 T22: 0.2922
REMARK 3 T33: 0.3957 T12: -0.0147
REMARK 3 T13: 0.0374 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 1.7182 L22: 0.5914
REMARK 3 L33: 0.4904 L12: -0.1913
REMARK 3 L13: -0.0908 L23: -0.0120
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: 0.1282 S13: -0.3237
REMARK 3 S21: -0.1090 S22: 0.0557 S23: -0.0682
REMARK 3 S31: 0.1394 S32: -0.0109 S33: -0.0227
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 383 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0788 -45.6888-102.5013
REMARK 3 T TENSOR
REMARK 3 T11: 0.4569 T22: 0.3715
REMARK 3 T33: 0.3613 T12: -0.0392
REMARK 3 T13: 0.0606 T23: -0.0642
REMARK 3 L TENSOR
REMARK 3 L11: 5.0293 L22: 1.4856
REMARK 3 L33: 1.2121 L12: 0.2009
REMARK 3 L13: 1.9226 L23: -0.1386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: 0.5321 S13: -0.1259
REMARK 3 S21: -0.3861 S22: 0.1211 S23: -0.1402
REMARK 3 S31: 0.0232 S32: 0.2018 S33: -0.0405
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 415 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5974 -42.4204 -88.1076
REMARK 3 T TENSOR
REMARK 3 T11: 0.3337 T22: 0.3630
REMARK 3 T33: 0.4818 T12: 0.0504
REMARK 3 T13: 0.0015 T23: -0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 1.1575 L22: 1.2421
REMARK 3 L33: 1.5363 L12: 0.5067
REMARK 3 L13: 0.1349 L23: -0.1303
REMARK 3 S TENSOR
REMARK 3 S11: -0.0644 S12: 0.0048 S13: -0.2756
REMARK 3 S21: 0.0128 S22: 0.0975 S23: -0.2614
REMARK 3 S31: 0.1881 S32: 0.2132 S33: -0.0226
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 453 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1436 -31.0620 -79.2126
REMARK 3 T TENSOR
REMARK 3 T11: 0.3078 T22: 0.3038
REMARK 3 T33: 0.2870 T12: 0.0203
REMARK 3 T13: 0.0001 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.0721 L22: 1.2722
REMARK 3 L33: 0.7544 L12: 0.0761
REMARK 3 L13: 0.2653 L23: 0.4844
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: -0.1024 S13: -0.0469
REMARK 3 S21: 0.0107 S22: 0.0326 S23: -0.0679
REMARK 3 S31: 0.0320 S32: 0.0439 S33: 0.0062
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 524 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2466 -27.2057 -91.5028
REMARK 3 T TENSOR
REMARK 3 T11: 0.3437 T22: 0.2975
REMARK 3 T33: 0.3147 T12: 0.0071
REMARK 3 T13: -0.0052 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.9255 L22: 1.6831
REMARK 3 L33: 2.5319 L12: 1.1145
REMARK 3 L13: 0.5648 L23: 1.4079
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: 0.0576 S13: 0.0511
REMARK 3 S21: -0.1180 S22: -0.1211 S23: 0.2063
REMARK 3 S31: -0.0653 S32: -0.2985 S33: 0.1288
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 561 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6677 -37.7254 -94.5025
REMARK 3 T TENSOR
REMARK 3 T11: 0.3486 T22: 0.3240
REMARK 3 T33: 0.3706 T12: -0.0342
REMARK 3 T13: -0.0221 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 3.2538 L22: 2.1587
REMARK 3 L33: 3.2100 L12: -0.1380
REMARK 3 L13: 1.4981 L23: 1.1823
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: -0.0891 S13: -0.1609
REMARK 3 S21: -0.1801 S22: 0.0154 S23: 0.3923
REMARK 3 S31: -0.0310 S32: -0.7256 S33: -0.0292
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 6QGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 254053
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
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) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 30% (V/V) 2,4-MPD
REMARK 280 AND 0.12 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 55.57050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 123.72050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.02400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 123.72050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.57050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 92.02400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 8
REMARK 465 ASN A 9
REMARK 465 HIS A 10
REMARK 465 LYS A 11
REMARK 465 VAL A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 MET A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 PRO A 42
REMARK 465 ASP A 56
REMARK 465 GLY A 57
REMARK 465 ASN A 58
REMARK 465 GLY A 59
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 ASP C 56
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 ASP D 56
REMARK 465 GLY D 57
REMARK 465 ASN D 58
REMARK 465 GLY D 59
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 ASP E 56
REMARK 465 GLY E 57
REMARK 465 ASN E 58
REMARK 465 GLY E 59
REMARK 465 MET F 8
REMARK 465 ASN F 9
REMARK 465 HIS F 10
REMARK 465 LYS F 11
REMARK 465 VAL F 12
REMARK 465 HIS F 13
REMARK 465 HIS F 14
REMARK 465 HIS F 15
REMARK 465 HIS F 16
REMARK 465 HIS F 17
REMARK 465 HIS F 18
REMARK 465 MET F 19
REMARK 465 GLY F 20
REMARK 465 GLY F 21
REMARK 465 GLY F 22
REMARK 465 SER F 23
REMARK 465 THR F 24
REMARK 465 PRO F 25
REMARK 465 LEU F 26
REMARK 465 PRO F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLN F 30
REMARK 465 GLN F 31
REMARK 465 GLN F 32
REMARK 465 PRO F 33
REMARK 465 PRO F 34
REMARK 465 GLN F 35
REMARK 465 GLN F 36
REMARK 465 GLU F 37
REMARK 465 PRO F 38
REMARK 465 PRO F 39
REMARK 465 PRO F 40
REMARK 465 PRO F 41
REMARK 465 PRO F 42
REMARK 465 ASP F 56
REMARK 465 GLY F 57
REMARK 465 ASN F 58
REMARK 465 GLY F 59
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 E 1136 O HOH E 1151 2.06
REMARK 500 O HOH A 1011 O HOH A 1074 2.07
REMARK 500 O HOH D 1045 O HOH D 1074 2.07
REMARK 500 O HOH E 1142 O HOH E 1151 2.08
REMARK 500 O HOH B 1277 O HOH B 1279 2.11
REMARK 500 O HOH F 1069 O HOH F 1084 2.14
REMARK 500 O HOH F 1101 O HOH F 1102 2.14
REMARK 500 O HOH A 1086 O HOH A 1087 2.15
REMARK 500 O3 SO4 E 704 O HOH E 801 2.17
REMARK 500 O HOH F 1091 O HOH F 1093 2.17
REMARK 500 O HOH F 1039 O HOH F 1075 2.19
REMARK 500 O HOH E 862 O HOH E 978 2.19
REMARK 500 O HOH D 1073 O HOH D 1105 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 1091 O HOH F 1102 2455 1.99
REMARK 500 O HOH D 1045 O HOH E 1063 2554 2.13
REMARK 500 O HOH D 1115 O HOH E 1072 2554 2.14
REMARK 500 O HOH B 923 O HOH B 1202 4545 2.16
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 31.99 -88.10
REMARK 500 ASN A 134 -149.96 56.85
REMARK 500 ASN A 171 59.42 -94.10
REMARK 500 TYR A 194 -29.64 -152.02
REMARK 500 SER A 225 -121.41 67.29
REMARK 500 ALA A 249 61.51 30.14
REMARK 500 TYR A 373 -94.49 -141.32
REMARK 500 SER A 383 -146.77 -137.19
REMARK 500 VAL A 412 -61.56 -91.93
REMARK 500 ASN A 527 -150.03 -85.15
REMARK 500 CYS A 529 -23.10 66.28
REMARK 500 ASP B 60 -52.26 166.40
REMARK 500 ALA B 67 31.44 -88.26
REMARK 500 ASN B 134 -147.08 57.55
REMARK 500 TYR B 194 -32.50 -151.49
REMARK 500 SER B 225 -126.16 66.35
REMARK 500 ALA B 249 60.88 31.11
REMARK 500 ASP B 311 13.21 -142.30
REMARK 500 TYR B 373 -97.53 -142.32
REMARK 500 SER B 383 -140.52 -135.83
REMARK 500 ASN B 408 10.30 -144.39
REMARK 500 VAL B 412 -60.37 -95.36
REMARK 500 GLU B 429 76.13 -118.95
REMARK 500 ILE B 447 -52.82 -127.87
REMARK 500 SER B 491 32.86 -99.97
REMARK 500 ASN B 527 -147.45 -90.17
REMARK 500 CYS B 529 -21.26 71.65
REMARK 500 ALA C 67 45.19 -86.58
REMARK 500 ASN C 134 -145.31 54.07
REMARK 500 ASN C 171 58.88 -95.17
REMARK 500 TYR C 194 -34.32 -152.06
REMARK 500 SER C 225 -119.50 66.35
REMARK 500 ALA C 249 54.72 39.45
REMARK 500 ASP C 311 15.89 -157.73
REMARK 500 TYR C 373 -96.93 -143.25
REMARK 500 SER C 383 -144.22 -135.70
REMARK 500 VAL C 412 -63.84 -98.48
REMARK 500 SER C 491 34.38 -98.32
REMARK 500 PHE C 517 -12.21 -142.35
REMARK 500 ASN C 527 -154.40 -89.32
REMARK 500 CYS C 529 -26.80 69.51
REMARK 500 ALA C 571 149.87 -171.96
REMARK 500 ASN D 134 -146.74 57.22
REMARK 500 TYR D 194 -30.56 -158.50
REMARK 500 SER D 225 -123.73 64.84
REMARK 500 ALA D 249 60.31 27.94
REMARK 500 TYR D 373 -89.45 -140.72
REMARK 500 SER D 383 -140.59 -138.65
REMARK 500 VAL D 412 -61.95 -93.31
REMARK 500 SER D 491 32.69 -98.64
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BEZ C 701
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 73.3
REMARK 620 3 ASP A 307 OD1 71.3 140.4
REMARK 620 4 ASP A 307 OD2 76.0 134.6 49.9
REMARK 620 5 LEU A 309 O 83.6 84.7 74.3 124.0
REMARK 620 6 ASP A 311 OD1 145.9 74.2 134.1 136.2 83.7
REMARK 620 7 ILE A 313 O 99.7 77.5 125.5 75.6 160.0 82.8
REMARK 620 8 HOH A 809 O 142.0 144.6 71.8 73.3 95.4 70.7 93.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 68.6
REMARK 620 3 ASP B 307 OD1 69.3 133.6
REMARK 620 4 ASP B 307 OD2 74.4 131.6 49.1
REMARK 620 5 LEU B 309 O 82.9 79.4 77.1 126.0
REMARK 620 6 ASP B 311 OD1 146.2 78.3 137.3 136.8 84.6
REMARK 620 7 ILE B 313 O 96.8 81.8 121.8 72.7 159.8 84.7
REMARK 620 8 HOH B 967 O 139.4 151.9 71.8 71.9 99.2 73.6 94.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 70.6
REMARK 620 3 ASP C 307 OD1 73.4 138.2
REMARK 620 4 ASP C 307 OD2 76.5 133.7 52.8
REMARK 620 5 LEU C 309 O 85.6 85.5 71.2 123.8
REMARK 620 6 ASP C 311 OD1 142.4 73.7 132.0 139.6 80.1
REMARK 620 7 ILE C 313 O 100.2 77.3 130.2 77.5 158.6 83.0
REMARK 620 8 HOH C 887 O 147.5 141.3 74.9 78.9 90.8 67.8 94.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 304 O
REMARK 620 2 ASP D 304 OD1 70.6
REMARK 620 3 ASP D 307 OD1 71.0 136.3
REMARK 620 4 ASP D 307 OD2 76.9 135.8 49.8
REMARK 620 5 LEU D 309 O 84.7 81.0 75.5 125.4
REMARK 620 6 ASP D 311 OD1 143.4 73.5 137.1 137.1 82.7
REMARK 620 7 ILE D 313 O 101.0 77.9 129.6 79.7 154.8 78.2
REMARK 620 8 HOH D 923 O 140.2 147.0 69.4 74.7 89.4 74.0 100.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 304 O
REMARK 620 2 ASP E 304 OD1 70.7
REMARK 620 3 ASP E 307 OD1 69.9 134.3
REMARK 620 4 ASP E 307 OD2 73.4 134.0 50.2
REMARK 620 5 LEU E 309 O 80.4 80.0 71.5 121.1
REMARK 620 6 ASP E 311 OD1 144.4 75.6 132.7 141.5 82.8
REMARK 620 7 ILE E 313 O 96.7 75.4 131.3 81.2 154.7 85.6
REMARK 620 8 HOH E 837 O 141.4 147.0 72.5 76.1 95.9 71.4 101.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 304 O
REMARK 620 2 ASP F 304 OD1 70.6
REMARK 620 3 ASP F 307 OD1 65.3 129.6
REMARK 620 4 ASP F 307 OD2 71.7 132.7 50.4
REMARK 620 5 LEU F 309 O 84.5 79.1 73.7 124.1
REMARK 620 6 ASP F 311 OD1 146.3 76.2 139.6 139.4 84.0
REMARK 620 7 ILE F 313 O 95.8 82.4 124.3 74.1 160.3 85.1
REMARK 620 8 HOH F 814 O 139.7 149.2 76.2 75.1 96.0 73.1 96.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ 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 CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 706
DBREF1 6QGB A 20 603 UNP MHETH_IDESA
DBREF2 6QGB A A0A0K8P8E7 20 603
DBREF1 6QGB B 20 603 UNP MHETH_IDESA
DBREF2 6QGB B A0A0K8P8E7 20 603
DBREF1 6QGB C 20 603 UNP MHETH_IDESA
DBREF2 6QGB C A0A0K8P8E7 20 603
DBREF1 6QGB D 20 603 UNP MHETH_IDESA
DBREF2 6QGB D A0A0K8P8E7 20 603
DBREF1 6QGB E 20 603 UNP MHETH_IDESA
DBREF2 6QGB E A0A0K8P8E7 20 603
DBREF1 6QGB F 20 603 UNP MHETH_IDESA
DBREF2 6QGB F A0A0K8P8E7 20 603
SEQADV 6QGB MET A 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN A 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS A 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL A 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS A 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET A 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET B 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN B 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS B 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL B 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS B 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET B 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET C 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN C 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS C 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL C 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS C 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET C 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET D 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN D 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS D 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL D 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS D 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET D 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET E 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN E 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS E 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL E 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS E 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET E 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET F 8 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6QGB ASN F 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB LYS F 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB VAL F 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB HIS F 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QGB MET F 19 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 A 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 A 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 A 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 A 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 A 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 A 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 A 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 A 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 A 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 A 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 A 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 A 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 A 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 A 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 A 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 A 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 A 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 A 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 A 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 A 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 A 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 A 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 A 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 A 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 A 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 A 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 A 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 A 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 A 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 A 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 A 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 A 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 A 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 A 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 A 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 A 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 A 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 A 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 A 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 A 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 A 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 A 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 A 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 A 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 A 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 B 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 B 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 B 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 B 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 B 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 B 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 B 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 B 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 B 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 B 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 B 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 B 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 B 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 B 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 B 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 B 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 B 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 B 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 B 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 B 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 B 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 B 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 B 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 B 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 B 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 B 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 B 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 B 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 B 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 B 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 B 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 B 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 B 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 B 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 B 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 B 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 B 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 B 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 B 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 B 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 B 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 B 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 B 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 B 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 B 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 B 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 C 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 C 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 C 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 C 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 C 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 C 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 C 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 C 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 C 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 C 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 C 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 C 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 C 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 C 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 C 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 C 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 C 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 C 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 C 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 C 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 C 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 C 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 C 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 C 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 C 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 C 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 C 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 C 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 C 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 C 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 C 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 C 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 C 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 C 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 C 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 C 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 C 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 C 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 C 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 C 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 C 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 C 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 C 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 C 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 C 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 C 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 D 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 D 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 D 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 D 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 D 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 D 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 D 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 D 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 D 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 D 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 D 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 D 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 D 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 D 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 D 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 D 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 D 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 D 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 D 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 D 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 D 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 D 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 D 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 D 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 D 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 D 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 D 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 D 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 D 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 D 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 D 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 D 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 D 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 D 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 D 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 D 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 D 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 D 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 D 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 D 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 D 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 D 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 D 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 D 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 D 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 D 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 E 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 E 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 E 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 E 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 E 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 E 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 E 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 E 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 E 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 E 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 E 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 E 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 E 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 E 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 E 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 E 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 E 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 E 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 E 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 E 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 E 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 E 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 E 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 E 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 E 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 E 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 E 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 E 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 E 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 E 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 E 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 E 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 E 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 E 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 E 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 E 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 E 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 E 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 E 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 E 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 E 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 E 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 E 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 E 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 E 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 E 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 F 596 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET GLY
SEQRES 2 F 596 GLY GLY SER THR PRO LEU PRO LEU PRO GLN GLN GLN PRO
SEQRES 3 F 596 PRO GLN GLN GLU PRO PRO PRO PRO PRO VAL PRO LEU ALA
SEQRES 4 F 596 SER ARG ALA ALA CYS GLU ALA LEU LYS ASP GLY ASN GLY
SEQRES 5 F 596 ASP MET VAL TRP PRO ASN ALA ALA THR VAL VAL GLU VAL
SEQRES 6 F 596 ALA ALA TRP ARG ASP ALA ALA PRO ALA THR ALA SER ALA
SEQRES 7 F 596 ALA ALA LEU PRO GLU HIS CYS GLU VAL SER GLY ALA ILE
SEQRES 8 F 596 ALA LYS ARG THR GLY ILE ASP GLY TYR PRO TYR GLU ILE
SEQRES 9 F 596 LYS PHE ARG LEU ARG MET PRO ALA GLU TRP ASN GLY ARG
SEQRES 10 F 596 PHE PHE MET GLU GLY GLY SER GLY THR ASN GLY SER LEU
SEQRES 11 F 596 SER ALA ALA THR GLY SER ILE GLY GLY GLY GLN ILE ALA
SEQRES 12 F 596 SER ALA LEU SER ARG ASN PHE ALA THR ILE ALA THR ASP
SEQRES 13 F 596 GLY GLY HIS ASP ASN ALA VAL ASN ASP ASN PRO ASP ALA
SEQRES 14 F 596 LEU GLY THR VAL ALA PHE GLY LEU ASP PRO GLN ALA ARG
SEQRES 15 F 596 LEU ASP MET GLY TYR ASN SER TYR ASP GLN VAL THR GLN
SEQRES 16 F 596 ALA GLY LYS ALA ALA VAL ALA ARG PHE TYR GLY ARG ALA
SEQRES 17 F 596 ALA ASP LYS SER TYR PHE ILE GLY CYS SER GLU GLY GLY
SEQRES 18 F 596 ARG GLU GLY MET MET LEU SER GLN ARG PHE PRO SER HIS
SEQRES 19 F 596 TYR ASP GLY ILE VAL ALA GLY ALA PRO GLY TYR GLN LEU
SEQRES 20 F 596 PRO LYS ALA GLY ILE SER GLY ALA TRP THR THR GLN SER
SEQRES 21 F 596 LEU ALA PRO ALA ALA VAL GLY LEU ASP ALA GLN GLY VAL
SEQRES 22 F 596 PRO LEU ILE ASN LYS SER PHE SER ASP ALA ASP LEU HIS
SEQRES 23 F 596 LEU LEU SER GLN ALA ILE LEU GLY THR CYS ASP ALA LEU
SEQRES 24 F 596 ASP GLY LEU ALA ASP GLY ILE VAL ASP ASN TYR ARG ALA
SEQRES 25 F 596 CYS GLN ALA ALA PHE ASP PRO ALA THR ALA ALA ASN PRO
SEQRES 26 F 596 ALA ASN GLY GLN ALA LEU GLN CYS VAL GLY ALA LYS THR
SEQRES 27 F 596 ALA ASP CYS LEU SER PRO VAL GLN VAL THR ALA ILE LYS
SEQRES 28 F 596 ARG ALA MET ALA GLY PRO VAL ASN SER ALA GLY THR PRO
SEQRES 29 F 596 LEU TYR ASN ARG TRP ALA TRP ASP ALA GLY MET SER GLY
SEQRES 30 F 596 LEU SER GLY THR THR TYR ASN GLN GLY TRP ARG SER TRP
SEQRES 31 F 596 TRP LEU GLY SER PHE ASN SER SER ALA ASN ASN ALA GLN
SEQRES 32 F 596 ARG VAL SER GLY PHE SER ALA ARG SER TRP LEU VAL ASP
SEQRES 33 F 596 PHE ALA THR PRO PRO GLU PRO MET PRO MET THR GLN VAL
SEQRES 34 F 596 ALA ALA ARG MET MET LYS PHE ASP PHE ASP ILE ASP PRO
SEQRES 35 F 596 LEU LYS ILE TRP ALA THR SER GLY GLN PHE THR GLN SER
SEQRES 36 F 596 SER MET ASP TRP HIS GLY ALA THR SER THR ASP LEU ALA
SEQRES 37 F 596 ALA PHE ARG ASP ARG GLY GLY LYS MET ILE LEU TYR HIS
SEQRES 38 F 596 GLY MET SER ASP ALA ALA PHE SER ALA LEU ASP THR ALA
SEQRES 39 F 596 ASP TYR TYR GLU ARG LEU GLY ALA ALA MET PRO GLY ALA
SEQRES 40 F 596 ALA GLY PHE ALA ARG LEU PHE LEU VAL PRO GLY MET ASN
SEQRES 41 F 596 HIS CYS SER GLY GLY PRO GLY THR ASP ARG PHE ASP MET
SEQRES 42 F 596 LEU THR PRO LEU VAL ALA TRP VAL GLU ARG GLY GLU ALA
SEQRES 43 F 596 PRO ASP GLN ILE SER ALA TRP SER GLY THR PRO GLY TYR
SEQRES 44 F 596 PHE GLY VAL ALA ALA ARG THR ARG PRO LEU CYS PRO TYR
SEQRES 45 F 596 PRO GLN ILE ALA ARG TYR LYS GLY SER GLY ASP ILE ASN
SEQRES 46 F 596 THR GLU ALA ASN PHE ALA CYS ALA ALA PRO PRO
HET BEZ A 701 9
HET CA A 702 1
HET CL A 703 1
HET CL A 704 1
HET SO4 A 705 5
HET SO4 A 706 5
HET MPD B 801 8
HET BEZ B 802 9
HET CA B 803 1
HET CL B 804 1
HET SO4 B 805 5
HET SO4 B 806 5
HET SO4 B 807 5
HET BEZ C 701 8
HET CA C 702 1
HET CL C 703 1
HET SO4 C 704 5
HET BEZ D 701 9
HET CA D 702 1
HET CL D 703 1
HET SO4 D 704 5
HET BEZ E 701 9
HET CA E 702 1
HET CL E 703 1
HET SO4 E 704 5
HET BEZ F 701 9
HET CA F 702 1
HET CL F 703 1
HET CL F 704 1
HET SO4 F 705 5
HET SO4 F 706 5
HETNAM BEZ BENZOIC ACID
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 7 BEZ 6(C7 H6 O2)
FORMUL 8 CA 6(CA 2+)
FORMUL 9 CL 8(CL 1-)
FORMUL 11 SO4 10(O4 S 2-)
FORMUL 13 MPD C6 H14 O2
FORMUL 38 HOH *1984(H2 O)
HELIX 1 AA1 SER A 47 LEU A 54 1 8
HELIX 2 AA2 ASN A 173 LEU A 184 5 12
HELIX 3 AA3 ASP A 185 TYR A 194 1 10
HELIX 4 AA4 TYR A 194 GLY A 213 1 20
HELIX 5 AA5 SER A 225 PHE A 238 1 14
HELIX 6 AA6 GLN A 253 PRO A 255 5 3
HELIX 7 AA7 LYS A 256 ALA A 269 1 14
HELIX 8 AA8 PRO A 270 ALA A 272 5 3
HELIX 9 AA9 LEU A 282 PHE A 287 5 6
HELIX 10 AB1 SER A 288 ASP A 304 1 17
HELIX 11 AB2 ALA A 305 GLY A 308 5 4
HELIX 12 AB3 ASN A 316 PHE A 324 1 9
HELIX 13 AB4 SER A 350 GLY A 363 1 14
HELIX 14 AB5 ASP A 379 SER A 383 5 5
HELIX 15 AB6 TRP A 394 LEU A 399 1 6
HELIX 16 AB7 GLY A 414 ASP A 423 1 10
HELIX 17 AB8 PRO A 432 THR A 434 5 3
HELIX 18 AB9 GLN A 435 LYS A 442 1 8
HELIX 19 AC1 ILE A 447 ALA A 454 5 8
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 ALA B 53 1 7
HELIX 28 AD1 LEU B 54 ASP B 56 5 3
HELIX 29 AD2 ALA B 152 ASN B 156 5 5
HELIX 30 AD3 LEU B 177 LEU B 184 5 8
HELIX 31 AD4 ASP B 185 TYR B 194 1 10
HELIX 32 AD5 TYR B 194 GLY B 213 1 20
HELIX 33 AD6 SER B 225 PHE B 238 1 14
HELIX 34 AD7 GLN B 253 PRO B 255 5 3
HELIX 35 AD8 LYS B 256 ALA B 269 1 14
HELIX 36 AD9 PRO B 270 ALA B 272 5 3
HELIX 37 AE1 LEU B 282 SER B 286 5 5
HELIX 38 AE2 SER B 288 ASP B 304 1 17
HELIX 39 AE3 ALA B 305 GLY B 308 5 4
HELIX 40 AE4 ASN B 316 PHE B 324 1 9
HELIX 41 AE5 SER B 350 GLY B 363 1 14
HELIX 42 AE6 ASP B 379 SER B 383 5 5
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 LEU C 54 1 8
HELIX 55 AG1 LEU C 177 LEU C 184 5 8
HELIX 56 AG2 ASP C 185 TYR C 194 1 10
HELIX 57 AG3 TYR C 194 GLY C 213 1 20
HELIX 58 AG4 SER C 225 PHE C 238 1 14
HELIX 59 AG5 GLN C 253 PRO C 255 5 3
HELIX 60 AG6 LYS C 256 ALA C 269 1 14
HELIX 61 AG7 PRO C 270 ALA C 272 5 3
HELIX 62 AG8 LEU C 282 SER C 286 5 5
HELIX 63 AG9 SER C 288 ASP C 304 1 17
HELIX 64 AH1 ALA C 305 GLY C 308 5 4
HELIX 65 AH2 ASN C 316 PHE C 324 1 9
HELIX 66 AH3 SER C 350 GLY C 363 1 14
HELIX 67 AH4 ASP C 379 SER C 383 5 5
HELIX 68 AH5 TRP C 394 LEU C 399 1 6
HELIX 69 AH6 GLY C 414 ASP C 423 1 10
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 ARG C 480 1 7
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 GLY C 568 5 6
HELIX 79 AI7 THR C 593 ALA C 595 5 3
HELIX 80 AI8 SER D 47 ALA D 53 1 7
HELIX 81 AI9 ALA D 152 ASN D 156 5 5
HELIX 82 AJ1 LEU D 177 LEU D 184 5 8
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 PHE D 287 5 6
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 GLY D 363 1 14
HELIX 94 AK4 ASP D 379 SER D 383 5 5
HELIX 95 AK5 GLY D 414 ASP D 423 1 10
HELIX 96 AK6 PRO D 432 THR D 434 5 3
HELIX 97 AK7 GLN D 435 LYS D 442 1 8
HELIX 98 AK8 ILE D 447 TRP D 453 5 7
HELIX 99 AK9 SER D 462 HIS D 467 1 6
HELIX 100 AL1 LEU D 474 ARG D 480 1 7
HELIX 101 AL2 SER D 496 MET D 511 1 16
HELIX 102 AL3 GLY D 513 GLY D 516 5 4
HELIX 103 AL4 MET D 540 GLY D 551 1 12
HELIX 104 AL5 THR D 563 PHE D 567 5 5
HELIX 105 AL6 THR D 593 ALA D 595 5 3
HELIX 106 AL7 SER E 47 ALA E 53 1 7
HELIX 107 AL8 ALA E 152 ASN E 156 5 5
HELIX 108 AL9 LEU E 177 LEU E 184 5 8
HELIX 109 AM1 ASP E 185 TYR E 194 1 10
HELIX 110 AM2 TYR E 194 GLY E 213 1 20
HELIX 111 AM3 SER E 225 PHE E 238 1 14
HELIX 112 AM4 GLN E 253 PRO E 255 5 3
HELIX 113 AM5 LYS E 256 ALA E 269 1 14
HELIX 114 AM6 PRO E 270 ALA E 272 5 3
HELIX 115 AM7 LEU E 282 SER E 286 5 5
HELIX 116 AM8 SER E 288 ASP E 304 1 17
HELIX 117 AM9 ALA E 305 GLY E 308 5 4
HELIX 118 AN1 ASN E 316 PHE E 324 1 9
HELIX 119 AN2 SER E 350 GLY E 363 1 14
HELIX 120 AN3 ASP E 379 SER E 383 5 5
HELIX 121 AN4 GLY E 414 PHE E 424 1 11
HELIX 122 AN5 PRO E 432 THR E 434 5 3
HELIX 123 AN6 GLN E 435 PHE E 443 1 9
HELIX 124 AN7 ILE E 447 TRP E 453 5 7
HELIX 125 AN8 SER E 462 GLY E 468 1 7
HELIX 126 AN9 LEU E 474 ARG E 480 1 7
HELIX 127 AO1 SER E 496 MET E 511 1 16
HELIX 128 AO2 GLY E 513 GLY E 516 5 4
HELIX 129 AO3 MET E 540 GLY E 551 1 12
HELIX 130 AO4 THR E 563 GLY E 568 5 6
HELIX 131 AO5 THR E 593 ALA E 595 5 3
HELIX 132 AO6 SER F 47 ALA F 53 1 7
HELIX 133 AO7 ALA F 152 ASN F 156 5 5
HELIX 134 AO8 LEU F 177 LEU F 184 5 8
HELIX 135 AO9 ASP F 185 TYR F 194 1 10
HELIX 136 AP1 TYR F 194 GLY F 213 1 20
HELIX 137 AP2 SER F 225 PHE F 238 1 14
HELIX 138 AP3 GLN F 253 PRO F 255 5 3
HELIX 139 AP4 LYS F 256 ALA F 269 1 14
HELIX 140 AP5 PRO F 270 ALA F 272 5 3
HELIX 141 AP6 LEU F 282 SER F 286 5 5
HELIX 142 AP7 SER F 288 ASP F 304 1 17
HELIX 143 AP8 ALA F 305 GLY F 308 5 4
HELIX 144 AP9 ASN F 316 PHE F 324 1 9
HELIX 145 AQ1 SER F 350 GLY F 363 1 14
HELIX 146 AQ2 ASP F 379 SER F 383 5 5
HELIX 147 AQ3 TRP F 394 LEU F 399 1 6
HELIX 148 AQ4 GLY F 414 ASP F 423 1 10
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 HIS F 467 1 6
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
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O ALA A 97 N VAL A 69
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N 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 PHE B 126 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O VAL B 523 N HIS B 488
SHEET 1 AA6 2 LEU B 385 SER B 386 0
SHEET 2 AA6 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA7 2 ILE B 557 TRP B 560 0
SHEET 2 AA7 2 THR B 573 LEU B 576 -1 O LEU B 576 N ILE B 557
SHEET 1 AA8 2 ILE B 582 TYR B 585 0
SHEET 2 AA8 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SHEET 1 AA9 9 THR C 68 ARG C 76 0
SHEET 2 AA9 9 HIS C 91 THR C 102 -1 O HIS C 91 N ARG C 76
SHEET 3 AA9 9 PRO C 108 PRO C 118 -1 O LEU C 115 N VAL C 94
SHEET 4 AA9 9 ALA C 158 THR C 162 -1 O THR C 159 N ARG C 116
SHEET 5 AA9 9 ARG C 124 GLU C 128 1 N PHE C 126 O ALA C 158
SHEET 6 AA9 9 LYS C 218 CYS C 224 1 O TYR C 220 N PHE C 125
SHEET 7 AA9 9 GLY C 244 GLY C 248 1 O GLY C 248 N GLY C 223
SHEET 8 AA9 9 LYS C 483 GLY C 489 1 O LYS C 483 N ILE C 245
SHEET 9 AA9 9 ALA C 518 VAL C 523 1 O ARG C 519 N LEU C 486
SHEET 1 AB1 2 LEU C 385 SER C 386 0
SHEET 2 AB1 2 THR C 389 TYR C 390 -1 O THR C 389 N SER C 386
SHEET 1 AB2 2 ILE C 557 TRP C 560 0
SHEET 2 AB2 2 THR C 573 LEU C 576 -1 O LEU C 576 N ILE C 557
SHEET 1 AB3 2 ILE C 582 TYR C 585 0
SHEET 2 AB3 2 PHE C 597 ALA C 600 -1 O ALA C 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 GLU D 93 N ALA D 74
SHEET 3 AB4 9 PRO D 108 PRO D 118 -1 O LEU D 115 N VAL D 94
SHEET 4 AB4 9 ALA D 158 THR D 162 -1 O THR D 159 N ARG D 116
SHEET 5 AB4 9 ARG D 124 GLU D 128 1 N ARG D 124 O ALA D 158
SHEET 6 AB4 9 LYS D 218 CYS D 224 1 O TYR D 220 N PHE D 125
SHEET 7 AB4 9 GLY D 244 GLY D 248 1 O GLY D 248 N GLY D 223
SHEET 8 AB4 9 LYS D 483 GLY D 489 1 O ILE D 485 N 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 3 ARG D 537 PHE D 538 0
SHEET 2 AB6 3 ILE D 557 TRP D 560 -1 O TRP D 560 N ARG D 537
SHEET 3 AB6 3 THR D 573 LEU D 576 -1 O LEU D 576 N ILE D 557
SHEET 1 AB7 2 ILE D 582 TYR D 585 0
SHEET 2 AB7 2 PHE D 597 ALA D 600 -1 O ALA D 598 N ARG D 584
SHEET 1 AB8 9 THR E 68 ARG E 76 0
SHEET 2 AB8 9 HIS E 91 THR E 102 -1 O 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 600 N ILE E 582
SHEET 1 AC3 9 THR F 68 ARG F 76 0
SHEET 2 AC3 9 HIS F 91 THR F 102 -1 O GLU F 93 N ALA F 74
SHEET 3 AC3 9 PRO F 108 PRO F 118 -1 O LEU F 115 N VAL F 94
SHEET 4 AC3 9 ALA F 158 THR F 162 -1 O THR F 159 N ARG F 116
SHEET 5 AC3 9 ARG F 124 GLU F 128 1 N PHE F 126 O ALA F 158
SHEET 6 AC3 9 LYS F 218 CYS F 224 1 O TYR F 220 N PHE F 125
SHEET 7 AC3 9 GLY F 244 GLY F 248 1 O GLY F 248 N GLY F 223
SHEET 8 AC3 9 LYS F 483 GLY F 489 1 O ILE F 485 N ILE F 245
SHEET 9 AC3 9 ALA F 518 VAL F 523 1 O ARG F 519 N LEU F 486
SHEET 1 AC4 2 LEU F 385 SER F 386 0
SHEET 2 AC4 2 THR F 389 TYR F 390 -1 O THR F 389 N SER F 386
SHEET 1 AC5 2 ILE F 557 TRP F 560 0
SHEET 2 AC5 2 THR F 573 LEU F 576 -1 O LEU F 576 N ILE F 557
SHEET 1 AC6 2 ILE F 582 TYR F 585 0
SHEET 2 AC6 2 PHE F 597 ALA F 600 -1 O ALA F 600 N ILE F 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.06
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.05
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.05
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.03
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.02
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.05
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.06
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.05
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.04
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.03
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.04
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.06
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.04
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.03
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.04
SSBOND 16 CYS D 51 CYS D 92 1555 1555 2.06
SSBOND 17 CYS D 224 CYS D 529 1555 1555 2.05
SSBOND 18 CYS D 303 CYS D 320 1555 1555 2.04
SSBOND 19 CYS D 340 CYS D 348 1555 1555 2.04
SSBOND 20 CYS D 577 CYS D 599 1555 1555 2.03
SSBOND 21 CYS E 51 CYS E 92 1555 1555 2.05
SSBOND 22 CYS E 224 CYS E 529 1555 1555 2.06
SSBOND 23 CYS E 303 CYS E 320 1555 1555 2.06
SSBOND 24 CYS E 340 CYS E 348 1555 1555 2.04
SSBOND 25 CYS E 577 CYS E 599 1555 1555 2.04
SSBOND 26 CYS F 51 CYS F 92 1555 1555 2.05
SSBOND 27 CYS F 224 CYS F 529 1555 1555 2.07
SSBOND 28 CYS F 303 CYS F 320 1555 1555 2.05
SSBOND 29 CYS F 340 CYS F 348 1555 1555 2.05
SSBOND 30 CYS F 577 CYS F 599 1555 1555 2.04
LINK O ASP A 304 CA CA A 702 1555 1555 2.50
LINK OD1 ASP A 304 CA CA A 702 1555 1555 2.26
LINK OD1 ASP A 307 CA CA A 702 1555 1555 2.63
LINK OD2 ASP A 307 CA CA A 702 1555 1555 2.52
LINK O LEU A 309 CA CA A 702 1555 1555 2.37
LINK OD1 ASP A 311 CA CA A 702 1555 1555 2.60
LINK O ILE A 313 CA CA A 702 1555 1555 2.32
LINK O ASP B 304 CA CA B 803 1555 1555 2.65
LINK OD1 ASP B 304 CA CA B 803 1555 1555 2.38
LINK OD1 ASP B 307 CA CA B 803 1555 1555 2.58
LINK OD2 ASP B 307 CA CA B 803 1555 1555 2.65
LINK O LEU B 309 CA CA B 803 1555 1555 2.33
LINK OD1 ASP B 311 CA CA B 803 1555 1555 2.41
LINK O ILE B 313 CA CA B 803 1555 1555 2.44
LINK O ASP C 304 CA CA C 702 1555 1555 2.40
LINK OD1 ASP C 304 CA CA C 702 1555 1555 2.40
LINK OD1 ASP C 307 CA CA C 702 1555 1555 2.46
LINK OD2 ASP C 307 CA CA C 702 1555 1555 2.47
LINK O LEU C 309 CA CA C 702 1555 1555 2.38
LINK OD1 ASP C 311 CA CA C 702 1555 1555 2.55
LINK O ILE C 313 CA CA C 702 1555 1555 2.44
LINK O ASP D 304 CA CA D 702 1555 1555 2.60
LINK OD1 ASP D 304 CA CA D 702 1555 1555 2.39
LINK OD1 ASP D 307 CA CA D 702 1555 1555 2.62
LINK OD2 ASP D 307 CA CA D 702 1555 1555 2.57
LINK O LEU D 309 CA CA D 702 1555 1555 2.28
LINK OD1 ASP D 311 CA CA D 702 1555 1555 2.78
LINK O ILE D 313 CA CA D 702 1555 1555 2.35
LINK O ASP E 304 CA CA E 702 1555 1555 2.54
LINK OD1 ASP E 304 CA CA E 702 1555 1555 2.45
LINK OD1 ASP E 307 CA CA E 702 1555 1555 2.56
LINK OD2 ASP E 307 CA CA E 702 1555 1555 2.57
LINK O LEU E 309 CA CA E 702 1555 1555 2.44
LINK OD1 ASP E 311 CA CA E 702 1555 1555 2.35
LINK O ILE E 313 CA CA E 702 1555 1555 2.34
LINK O ASP F 304 CA CA F 702 1555 1555 2.61
LINK OD1 ASP F 304 CA CA F 702 1555 1555 2.38
LINK OD1 ASP F 307 CA CA F 702 1555 1555 2.60
LINK OD2 ASP F 307 CA CA F 702 1555 1555 2.51
LINK O LEU F 309 CA CA F 702 1555 1555 2.31
LINK OD1 ASP F 311 CA CA F 702 1555 1555 2.40
LINK O ILE F 313 CA CA F 702 1555 1555 2.42
LINK CA CA A 702 O HOH A 809 1555 1555 2.47
LINK CA CA B 803 O HOH B 967 1555 1555 2.36
LINK CA CA C 702 O HOH C 887 1555 1555 2.37
LINK CA CA D 702 O HOH D 923 1555 1555 2.45
LINK CA CA E 702 O HOH E 837 1555 1555 2.40
LINK CA CA F 702 O HOH F 814 1555 1555 2.45
CISPEP 1 THR A 426 PRO A 427 0 0.26
CISPEP 2 TYR A 579 PRO A 580 0 5.43
CISPEP 3 THR B 426 PRO B 427 0 -1.44
CISPEP 4 TYR B 579 PRO B 580 0 2.77
CISPEP 5 THR C 426 PRO C 427 0 0.46
CISPEP 6 TYR C 579 PRO C 580 0 4.10
CISPEP 7 THR D 426 PRO D 427 0 -3.64
CISPEP 8 TYR D 579 PRO D 580 0 4.50
CISPEP 9 THR E 426 PRO E 427 0 -0.29
CISPEP 10 TYR E 579 PRO E 580 0 6.28
CISPEP 11 THR F 426 PRO F 427 0 -0.62
CISPEP 12 TYR F 579 PRO F 580 0 4.70
SITE 1 AC1 11 GLY A 132 SER A 225 LEU A 254 ALA A 257
SITE 2 AC1 11 TRP A 397 ARG A 411 PHE A 415 SER A 416
SITE 3 AC1 11 PHE A 495 HOH A 815 HOH A 921
SITE 1 AC2 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC2 6 ILE A 313 HOH A 809
SITE 1 AC3 1 GLY A 147
SITE 1 AC4 1 ASP A 590
SITE 1 AC5 3 TRP A 121 ASN A 122 ASN D 122
SITE 1 AC6 1 ARG A 519
SITE 1 AC7 4 TRP B 263 GLN B 266 SER B 267 ARG B 359
SITE 1 AC8 11 GLY B 132 SER B 225 LEU B 254 ALA B 257
SITE 2 AC8 11 TRP B 397 ARG B 411 PHE B 415 SER B 416
SITE 3 AC8 11 PHE B 495 HOH B1010 HOH B1016
SITE 1 AC9 6 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AC9 6 ILE B 313 HOH B 967
SITE 1 AD1 2 ASN B 122 TRP E 121
SITE 1 AD2 5 ARG B 480 HOH B 902 HOH B 907 ASN C 65
SITE 2 AD2 5 GLN C 199
SITE 1 AD3 1 ARG B 519
SITE 1 AD4 9 GLY C 132 SER C 225 LEU C 254 TRP C 397
SITE 2 AD4 9 PHE C 415 SER C 416 PHE C 495 HOH C 835
SITE 3 AD4 9 HOH C 930
SITE 1 AD5 6 ASP C 304 ASP C 307 LEU C 309 ASP C 311
SITE 2 AD5 6 ILE C 313 HOH C 887
SITE 1 AD6 1 ASP C 590
SITE 1 AD7 2 ARG C 519 HOH C1020
SITE 1 AD8 11 GLY D 132 SER D 225 LEU D 254 ALA D 257
SITE 2 AD8 11 TRP D 397 ARG D 411 PHE D 415 SER D 416
SITE 3 AD8 11 PHE D 495 HOH D 817 HOH D 942
SITE 1 AD9 6 ASP D 304 ASP D 307 LEU D 309 ASP D 311
SITE 2 AD9 6 ILE D 313 HOH D 923
SITE 1 AE1 11 GLY E 132 SER E 225 LEU E 254 ALA E 257
SITE 2 AE1 11 TRP E 397 ARG E 411 PHE E 415 SER E 416
SITE 3 AE1 11 PHE E 495 HOH E 922 HOH E1007
SITE 1 AE2 6 ASP E 304 ASP E 307 LEU E 309 ASP E 311
SITE 2 AE2 6 ILE E 313 HOH E 837
SITE 1 AE3 3 ALA E 515 GLY E 516 ARG E 519
SITE 1 AE4 3 TYR A 585 LYS A 586 HOH E 801
SITE 1 AE5 12 GLY F 132 SER F 225 LEU F 254 ALA F 257
SITE 2 AE5 12 TRP F 397 ARG F 411 PHE F 415 SER F 416
SITE 3 AE5 12 PHE F 495 HIS F 528 HOH F 909 HOH F 965
SITE 1 AE6 6 ASP F 304 ASP F 307 LEU F 309 ASP F 311
SITE 2 AE6 6 ILE F 313 HOH F 814
SITE 1 AE7 1 ASP F 590
SITE 1 AE8 1 ARG F 519
SITE 1 AE9 3 ARG F 124 HOH F 827 HOH F 942
CRYST1 111.141 184.048 247.441 90.00 90.00 90.00 P 21 21 21 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008998 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004041 0.00000
TER 4117 PRO A 603
TER 8247 PRO B 603
TER 12369 PRO C 603
TER 16487 PRO D 603
TER 20605 PRO E 603
TER 24723 PRO F 603
MASTER 1450 0 31 158 91 0 46 626826 6 231 276
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