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HEADER HYDROLASE 09-AUG-23 8TRF
TITLE CRYSTAL STRUCTURE OF SM0281, AN ALPHA/BETA HYDROLASE FROM
TITLE 2 SINORHIZOBIUM MELILOTI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBIUM MELILOTI (STRAIN 1021);
SOURCE 3 ORGANISM_TAXID: 266834;
SOURCE 4 STRAIN: 1021;
SOURCE 5 GENE: SMC00361;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV-LIC
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,E.EVDOKIMOVA,S.LEMAK,E.EDWARDS,A.YAKUNIN,A.SAVCHENKO
REVDAT 1 12-FEB-25 8TRF 0
JRNL AUTH S.LEMAK
JRNL TITL CRYSTAL STRUCTURE OF SM0281, AN ALPHA/BETA HYDROLASE FROM
JRNL TITL 2 SINORHIZOBIUM MELILOTI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20_4459
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.080
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 49653
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1775
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 29.6900 - 5.7700 0.97 4264 159 0.2300 0.2448
REMARK 3 2 5.7700 - 4.5900 0.97 4096 151 0.1797 0.2257
REMARK 3 3 4.5900 - 4.0100 0.95 4006 150 0.1607 0.2143
REMARK 3 4 4.0100 - 3.6400 0.93 3842 139 0.1635 0.2249
REMARK 3 5 3.6400 - 3.3800 0.92 3802 140 0.1876 0.2239
REMARK 3 6 3.3800 - 3.1800 0.92 3795 132 0.1985 0.2195
REMARK 3 7 3.1800 - 3.0200 0.89 3703 125 0.2106 0.2690
REMARK 3 8 3.0200 - 2.8900 0.88 3595 145 0.2341 0.3076
REMARK 3 9 2.8900 - 2.7800 0.86 3533 136 0.2196 0.2853
REMARK 3 10 2.7800 - 2.6800 0.84 3468 127 0.2267 0.2927
REMARK 3 11 2.6800 - 2.6000 0.84 3431 142 0.2301 0.2717
REMARK 3 12 2.6000 - 2.5300 0.82 3365 114 0.2343 0.2871
REMARK 3 13 2.5300 - 2.4600 0.72 2978 115 0.2665 0.3291
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.249
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.644
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.82
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 : 0.004 7997
REMARK 3 ANGLE : 0.752 10761
REMARK 3 CHIRALITY : 0.046 1201
REMARK 3 PLANARITY : 0.005 1393
REMARK 3 DIHEDRAL : 16.896 3043
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 35
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8881 36.9630 26.7597
REMARK 3 T TENSOR
REMARK 3 T11: 0.4381 T22: 0.3575
REMARK 3 T33: 0.3961 T12: -0.0232
REMARK 3 T13: -0.1203 T23: -0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 5.7211 L22: 8.7321
REMARK 3 L33: 8.7116 L12: 2.5353
REMARK 3 L13: -1.6376 L23: -2.6961
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: -0.7300 S13: 0.4206
REMARK 3 S21: 0.7220 S22: -0.2410 S23: -0.3554
REMARK 3 S31: -1.0666 S32: 0.6878 S33: 0.1531
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6949 26.6459 31.6779
REMARK 3 T TENSOR
REMARK 3 T11: 0.4441 T22: 0.3720
REMARK 3 T33: 0.3232 T12: -0.0818
REMARK 3 T13: 0.0338 T23: 0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 2.0104 L22: 4.0684
REMARK 3 L33: 5.8611 L12: 0.7049
REMARK 3 L13: -1.5933 L23: 3.1933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: -0.3803 S13: -0.0543
REMARK 3 S21: 0.5755 S22: -0.1373 S23: -0.0681
REMARK 3 S31: -0.4223 S32: 0.3743 S33: 0.2468
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8657 27.3196 37.1926
REMARK 3 T TENSOR
REMARK 3 T11: 0.5180 T22: 0.5056
REMARK 3 T33: 0.3484 T12: 0.0608
REMARK 3 T13: -0.0039 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 7.8701 L22: 7.9509
REMARK 3 L33: 4.1815 L12: -1.9752
REMARK 3 L13: 3.0552 L23: -5.4482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: -0.8730 S13: 0.0756
REMARK 3 S21: 1.0314 S22: -0.1726 S23: 0.1072
REMARK 3 S31: -0.6662 S32: 0.1153 S33: 0.1459
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1143 28.8368 20.7118
REMARK 3 T TENSOR
REMARK 3 T11: 0.1989 T22: 0.2920
REMARK 3 T33: 0.2327 T12: 0.0017
REMARK 3 T13: -0.0114 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 3.8040 L22: 6.2696
REMARK 3 L33: 6.0431 L12: 0.4257
REMARK 3 L13: 0.8345 L23: -2.8586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: -0.1700 S13: 0.0215
REMARK 3 S21: 0.2426 S22: -0.0558 S23: -0.4115
REMARK 3 S31: -0.3907 S32: 0.1883 S33: 0.1032
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9016 25.1828 12.6967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2659 T22: 0.3033
REMARK 3 T33: 0.3665 T12: 0.0092
REMARK 3 T13: -0.0058 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 1.2945 L22: 4.5797
REMARK 3 L33: 6.5450 L12: -1.9404
REMARK 3 L13: 2.6705 L23: -3.6890
REMARK 3 S TENSOR
REMARK 3 S11: 0.2564 S12: 0.0141 S13: -0.4059
REMARK 3 S21: -0.1035 S22: -0.1133 S23: 0.0525
REMARK 3 S31: 0.5202 S32: 0.1210 S33: -0.1513
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 180 THROUGH 193 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1873 39.5300 14.0034
REMARK 3 T TENSOR
REMARK 3 T11: 0.5147 T22: 0.5659
REMARK 3 T33: 0.4489 T12: 0.0268
REMARK 3 T13: -0.0023 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 7.9426 L22: 2.5098
REMARK 3 L33: 3.8781 L12: -2.5985
REMARK 3 L13: -5.3964 L23: 2.2555
REMARK 3 S TENSOR
REMARK 3 S11: -0.1565 S12: -0.8125 S13: -0.1278
REMARK 3 S21: 1.0806 S22: 0.2485 S23: -0.3419
REMARK 3 S31: -0.1222 S32: -0.6377 S33: -0.2876
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5322 20.5270 15.6414
REMARK 3 T TENSOR
REMARK 3 T11: 0.3157 T22: 0.3756
REMARK 3 T33: 0.3822 T12: -0.0394
REMARK 3 T13: -0.0593 T23: 0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 0.8235 L22: 4.4775
REMARK 3 L33: 3.4202 L12: -0.2566
REMARK 3 L13: -0.0727 L23: -2.7501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0855 S12: -0.1535 S13: -0.2136
REMARK 3 S21: -0.1283 S22: 0.3504 S23: 0.2679
REMARK 3 S31: 0.2662 S32: -0.4455 S33: -0.2469
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9344 17.5521 26.8931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2954 T22: 0.5107
REMARK 3 T33: 0.4295 T12: -0.0386
REMARK 3 T13: 0.0805 T23: 0.1908
REMARK 3 L TENSOR
REMARK 3 L11: 2.6674 L22: 7.8464
REMARK 3 L33: 5.2630 L12: 0.7345
REMARK 3 L13: 0.8533 L23: 1.0162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0928 S12: -0.4775 S13: -0.2081
REMARK 3 S21: 0.0519 S22: 0.2750 S23: 0.5694
REMARK 3 S31: -0.2733 S32: -0.5965 S33: -0.0913
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 263 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1638 17.6155 36.5794
REMARK 3 T TENSOR
REMARK 3 T11: 0.4996 T22: 0.4969
REMARK 3 T33: 0.3460 T12: -0.0428
REMARK 3 T13: -0.0092 T23: 0.1068
REMARK 3 L TENSOR
REMARK 3 L11: 7.2474 L22: 5.6105
REMARK 3 L33: 9.3447 L12: 2.8375
REMARK 3 L13: 0.1937 L23: -2.2698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0576 S12: -0.4524 S13: -1.3726
REMARK 3 S21: 0.5958 S22: -0.1208 S23: 0.1330
REMARK 3 S31: -0.4190 S32: -0.3702 S33: 0.0748
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2161 60.8150 -3.0912
REMARK 3 T TENSOR
REMARK 3 T11: 0.4495 T22: 0.4847
REMARK 3 T33: 0.3802 T12: -0.0598
REMARK 3 T13: -0.0284 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 7.1437 L22: 7.9350
REMARK 3 L33: 4.6547 L12: -4.3412
REMARK 3 L13: -5.0230 L23: 5.1821
REMARK 3 S TENSOR
REMARK 3 S11: 0.3063 S12: 0.2624 S13: 0.7094
REMARK 3 S21: -0.8129 S22: 0.1692 S23: -0.6343
REMARK 3 S31: -0.3251 S32: -0.0844 S33: -0.5197
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 30 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0602 64.9035 7.6501
REMARK 3 T TENSOR
REMARK 3 T11: 0.3290 T22: 0.2923
REMARK 3 T33: 0.3789 T12: 0.0182
REMARK 3 T13: 0.0109 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 3.1392 L22: 2.9071
REMARK 3 L33: 1.7125 L12: -1.3838
REMARK 3 L13: -0.9518 L23: -1.2765
REMARK 3 S TENSOR
REMARK 3 S11: -0.1582 S12: -0.2454 S13: 0.7408
REMARK 3 S21: 0.0269 S22: -0.0080 S23: -0.2240
REMARK 3 S31: -0.5300 S32: 0.1417 S33: 0.1771
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0811 62.5995 2.1748
REMARK 3 T TENSOR
REMARK 3 T11: 0.2982 T22: 0.3244
REMARK 3 T33: 0.2767 T12: -0.0100
REMARK 3 T13: -0.0291 T23: 0.0869
REMARK 3 L TENSOR
REMARK 3 L11: 2.6336 L22: 4.6259
REMARK 3 L33: 3.7315 L12: -0.0687
REMARK 3 L13: -1.5682 L23: 1.8013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: 0.1905 S13: 0.1770
REMARK 3 S21: -0.2703 S22: 0.1638 S23: -0.1184
REMARK 3 S31: -0.2273 S32: -0.0897 S33: -0.1210
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1490 55.0156 4.8447
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.4646
REMARK 3 T33: 0.3450 T12: 0.0242
REMARK 3 T13: 0.0659 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 6.5177 L22: 5.0906
REMARK 3 L33: 8.5606 L12: -0.8709
REMARK 3 L13: -2.6352 L23: -3.3469
REMARK 3 S TENSOR
REMARK 3 S11: 0.2293 S12: -0.4271 S13: 0.4609
REMARK 3 S21: 0.1051 S22: -0.0337 S23: -0.7284
REMARK 3 S31: -0.2643 S32: 1.0482 S33: -0.1640
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5320 54.8697 12.5343
REMARK 3 T TENSOR
REMARK 3 T11: 0.2365 T22: 0.2433
REMARK 3 T33: 0.2823 T12: 0.0016
REMARK 3 T13: -0.0120 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 8.2420 L22: 2.2116
REMARK 3 L33: 7.4677 L12: 1.9004
REMARK 3 L13: 2.5531 L23: 2.8150
REMARK 3 S TENSOR
REMARK 3 S11: -0.3203 S12: -0.6784 S13: 0.0673
REMARK 3 S21: -0.1125 S22: -0.0033 S23: -0.0775
REMARK 3 S31: -0.1276 S32: 0.2183 S33: 0.2951
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1844 49.0366 12.2159
REMARK 3 T TENSOR
REMARK 3 T11: 0.2379 T22: 0.3360
REMARK 3 T33: 0.3329 T12: -0.0121
REMARK 3 T13: 0.0000 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.9128 L22: 6.2193
REMARK 3 L33: 3.4835 L12: 2.0294
REMARK 3 L13: 1.3447 L23: 2.3513
REMARK 3 S TENSOR
REMARK 3 S11: 0.3315 S12: -0.1036 S13: 0.0185
REMARK 3 S21: 0.5087 S22: -0.0983 S23: -0.2376
REMARK 3 S31: 0.1195 S32: 0.1592 S33: -0.2463
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 193 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7181 41.4454 -5.1554
REMARK 3 T TENSOR
REMARK 3 T11: 0.3117 T22: 0.2909
REMARK 3 T33: 0.2663 T12: -0.0298
REMARK 3 T13: 0.0015 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 9.3533 L22: 2.0370
REMARK 3 L33: 8.6025 L12: -3.9839
REMARK 3 L13: 1.0764 L23: -0.2755
REMARK 3 S TENSOR
REMARK 3 S11: 0.1574 S12: -0.0491 S13: 0.0274
REMARK 3 S21: 0.2890 S22: -0.1732 S23: -0.0907
REMARK 3 S31: -0.7507 S32: 0.1039 S33: -0.0366
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 194 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1564 40.6352 2.0511
REMARK 3 T TENSOR
REMARK 3 T11: 0.3229 T22: 0.3257
REMARK 3 T33: 0.3793 T12: -0.0074
REMARK 3 T13: 0.0972 T23: 0.1015
REMARK 3 L TENSOR
REMARK 3 L11: 8.9104 L22: 1.7592
REMARK 3 L33: 7.0264 L12: 2.4838
REMARK 3 L13: 3.9223 L23: 2.1613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: 0.0871 S13: -0.2061
REMARK 3 S21: 0.2836 S22: -0.1562 S23: -0.3149
REMARK 3 S31: 0.7103 S32: 0.1475 S33: 0.2497
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1830 50.7718 18.2138
REMARK 3 T TENSOR
REMARK 3 T11: 0.3411 T22: 0.3787
REMARK 3 T33: 0.2156 T12: -0.0161
REMARK 3 T13: 0.0424 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 3.5015 L22: 5.4869
REMARK 3 L33: 2.5785 L12: 0.1024
REMARK 3 L13: -0.6693 L23: 2.5122
REMARK 3 S TENSOR
REMARK 3 S11: -0.1038 S12: -0.2661 S13: -0.1831
REMARK 3 S21: 0.2541 S22: -0.0546 S23: 0.2214
REMARK 3 S31: 0.3520 S32: 0.0167 S33: 0.1596
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9761 58.6432 17.8123
REMARK 3 T TENSOR
REMARK 3 T11: 0.2180 T22: 0.4191
REMARK 3 T33: 0.2697 T12: 0.0030
REMARK 3 T13: 0.0414 T23: -0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 5.2074 L22: 8.9566
REMARK 3 L33: 4.7382 L12: -1.4264
REMARK 3 L13: -1.1613 L23: -1.3515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: 0.3102 S13: -0.0839
REMARK 3 S21: -0.2299 S22: 0.0658 S23: 0.2752
REMARK 3 S31: -0.2173 S32: -0.0951 S33: -0.0582
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 263 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3465 68.5976 17.5236
REMARK 3 T TENSOR
REMARK 3 T11: 0.4539 T22: 0.2635
REMARK 3 T33: 0.3290 T12: 0.0363
REMARK 3 T13: 0.0871 T23: -0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 8.2485 L22: 7.0488
REMARK 3 L33: 7.0692 L12: 2.9272
REMARK 3 L13: 0.5537 L23: 1.7568
REMARK 3 S TENSOR
REMARK 3 S11: 0.0881 S12: -0.5526 S13: -0.2154
REMARK 3 S21: 0.1757 S22: -0.0415 S23: 0.4705
REMARK 3 S31: -0.3444 S32: -0.0302 S33: 0.1566
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 7 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2844 72.1953 46.0009
REMARK 3 T TENSOR
REMARK 3 T11: 0.3618 T22: 0.5715
REMARK 3 T33: 0.4703 T12: -0.0612
REMARK 3 T13: 0.0162 T23: -0.1413
REMARK 3 L TENSOR
REMARK 3 L11: 3.2766 L22: 1.7378
REMARK 3 L33: 5.7498 L12: 2.3002
REMARK 3 L13: -3.0607 L23: -1.9531
REMARK 3 S TENSOR
REMARK 3 S11: 0.3350 S12: -0.5988 S13: 0.3727
REMARK 3 S21: 0.3807 S22: -0.1280 S23: 0.0133
REMARK 3 S31: -0.4294 S32: 0.2708 S33: -0.1852
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 80 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4564 65.4584 47.4543
REMARK 3 T TENSOR
REMARK 3 T11: 0.2828 T22: 0.6113
REMARK 3 T33: 0.3795 T12: -0.0815
REMARK 3 T13: 0.0508 T23: -0.1348
REMARK 3 L TENSOR
REMARK 3 L11: 5.9540 L22: 8.8730
REMARK 3 L33: 2.3635 L12: -2.2581
REMARK 3 L13: 0.9641 L23: 1.7920
REMARK 3 S TENSOR
REMARK 3 S11: 0.1700 S12: -0.5042 S13: 0.1987
REMARK 3 S21: 0.3510 S22: -0.5662 S23: -0.0340
REMARK 3 S31: 0.1310 S32: -0.3144 S33: 0.3544
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 115 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2288 55.7925 37.7903
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.4820
REMARK 3 T33: 0.4912 T12: -0.0550
REMARK 3 T13: 0.0953 T23: -0.1409
REMARK 3 L TENSOR
REMARK 3 L11: 2.5885 L22: 8.5396
REMARK 3 L33: 6.2540 L12: 2.6640
REMARK 3 L13: -0.7494 L23: -3.6008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: -0.0030 S13: -0.3986
REMARK 3 S21: -0.0760 S22: 0.0020 S23: 0.2415
REMARK 3 S31: 0.4755 S32: -0.4545 S33: 0.0061
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 180 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.7698 47.5360 48.8943
REMARK 3 T TENSOR
REMARK 3 T11: 0.5822 T22: 0.6748
REMARK 3 T33: 0.5868 T12: -0.1165
REMARK 3 T13: 0.1230 T23: -0.0729
REMARK 3 L TENSOR
REMARK 3 L11: 8.3314 L22: 9.4579
REMARK 3 L33: 4.3460 L12: -6.1430
REMARK 3 L13: 5.1211 L23: -5.5024
REMARK 3 S TENSOR
REMARK 3 S11: -0.3660 S12: -0.2326 S13: -0.3584
REMARK 3 S21: 0.9548 S22: 0.0920 S23: -0.2715
REMARK 3 S31: -0.3055 S32: -0.1868 S33: 0.1927
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 207 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.8155 58.9877 28.3091
REMARK 3 T TENSOR
REMARK 3 T11: 0.4437 T22: 0.7052
REMARK 3 T33: 0.8105 T12: -0.1043
REMARK 3 T13: -0.0860 T23: -0.1862
REMARK 3 L TENSOR
REMARK 3 L11: 0.0448 L22: 7.8487
REMARK 3 L33: 4.2849 L12: -0.3769
REMARK 3 L13: -0.7361 L23: 1.7650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0356 S12: 0.6866 S13: -0.6036
REMARK 3 S21: -0.8268 S22: -0.3795 S23: 1.3830
REMARK 3 S31: 0.4609 S32: -1.2193 S33: 0.3046
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 219 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8376 54.4427 29.6526
REMARK 3 T TENSOR
REMARK 3 T11: 0.3432 T22: 0.4585
REMARK 3 T33: 0.2977 T12: -0.0196
REMARK 3 T13: 0.0514 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 4.1028 L22: 9.2431
REMARK 3 L33: 4.5185 L12: -1.8131
REMARK 3 L13: -0.7729 L23: -3.5075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0907 S12: -0.1418 S13: -0.2881
REMARK 3 S21: 0.2360 S22: -0.1438 S23: 0.1692
REMARK 3 S31: 0.2320 S32: -0.0012 S33: 0.2072
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 243 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8601 64.2869 30.1582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.3259
REMARK 3 T33: 0.2834 T12: -0.0075
REMARK 3 T13: 0.0762 T23: -0.0974
REMARK 3 L TENSOR
REMARK 3 L11: 2.8817 L22: 8.0363
REMARK 3 L33: 7.1512 L12: 0.9293
REMARK 3 L13: -0.5045 L23: -0.2819
REMARK 3 S TENSOR
REMARK 3 S11: 0.1013 S12: -0.0096 S13: -0.1008
REMARK 3 S21: 0.1025 S22: -0.1463 S23: -0.0854
REMARK 3 S31: 0.0178 S32: 0.2492 S33: 0.0291
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 6 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2425 55.9449 24.5685
REMARK 3 T TENSOR
REMARK 3 T11: 0.5204 T22: 0.6763
REMARK 3 T33: 0.6901 T12: 0.0970
REMARK 3 T13: -0.0769 T23: -0.2800
REMARK 3 L TENSOR
REMARK 3 L11: 4.0450 L22: 5.6402
REMARK 3 L33: 2.5003 L12: -1.7028
REMARK 3 L13: 0.3823 L23: -0.9489
REMARK 3 S TENSOR
REMARK 3 S11: 0.1817 S12: 0.4826 S13: -0.8104
REMARK 3 S21: -0.2293 S22: -0.4145 S23: 0.0603
REMARK 3 S31: 0.2995 S32: 0.2281 S33: 0.1791
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 80 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8678 49.2615 35.4223
REMARK 3 T TENSOR
REMARK 3 T11: 0.5145 T22: 0.5496
REMARK 3 T33: 0.7519 T12: 0.0273
REMARK 3 T13: -0.0118 T23: -0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 7.9740 L22: 7.6109
REMARK 3 L33: 3.3585 L12: 0.0368
REMARK 3 L13: 4.0837 L23: -2.9103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: -0.3877 S13: -1.1560
REMARK 3 S21: 0.0658 S22: 0.1367 S23: -0.7121
REMARK 3 S31: 1.0261 S32: -0.1242 S33: -0.0362
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 96 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3951 60.1784 26.1157
REMARK 3 T TENSOR
REMARK 3 T11: 0.5006 T22: 0.6187
REMARK 3 T33: 0.7408 T12: 0.0514
REMARK 3 T13: 0.0862 T23: -0.1291
REMARK 3 L TENSOR
REMARK 3 L11: 9.6880 L22: 5.4359
REMARK 3 L33: 3.8345 L12: 4.0797
REMARK 3 L13: 0.0087 L23: 3.6260
REMARK 3 S TENSOR
REMARK 3 S11: 0.1195 S12: 1.1739 S13: 0.0415
REMARK 3 S21: -0.3741 S22: 0.3966 S23: -0.4750
REMARK 3 S31: -0.1690 S32: 1.5992 S33: -0.5292
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6823 64.1282 40.8049
REMARK 3 T TENSOR
REMARK 3 T11: 0.3590 T22: 0.5937
REMARK 3 T33: 0.5711 T12: 0.0304
REMARK 3 T13: 0.0256 T23: -0.1092
REMARK 3 L TENSOR
REMARK 3 L11: 4.1625 L22: 4.1521
REMARK 3 L33: 4.9464 L12: -0.9696
REMARK 3 L13: 3.0591 L23: -1.0150
REMARK 3 S TENSOR
REMARK 3 S11: -0.1206 S12: -0.4012 S13: -0.1056
REMARK 3 S21: 0.1149 S22: -0.1846 S23: 0.0032
REMARK 3 S31: 0.1225 S32: -0.0945 S33: 0.2937
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 180 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3019 54.0129 48.1303
REMARK 3 T TENSOR
REMARK 3 T11: 0.5199 T22: 0.7017
REMARK 3 T33: 0.7960 T12: -0.0376
REMARK 3 T13: 0.0580 T23: -0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 6.7300 L22: 4.1233
REMARK 3 L33: 9.6856 L12: 4.3333
REMARK 3 L13: -3.5798 L23: -5.5858
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: -0.0148 S13: -0.9142
REMARK 3 S21: 0.4243 S22: -0.1800 S23: 0.1385
REMARK 3 S31: 0.0995 S32: -0.5370 S33: 0.1696
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 208 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2069 71.3587 40.5984
REMARK 3 T TENSOR
REMARK 3 T11: 0.4317 T22: 0.5725
REMARK 3 T33: 0.5795 T12: 0.0013
REMARK 3 T13: -0.1098 T23: -0.1904
REMARK 3 L TENSOR
REMARK 3 L11: 0.8449 L22: 2.8544
REMARK 3 L33: 6.8886 L12: -1.5696
REMARK 3 L13: 0.4962 L23: -0.1879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.1485 S13: -0.0829
REMARK 3 S21: 0.5807 S22: 0.1215 S23: -0.5478
REMARK 3 S31: -0.2965 S32: 0.6036 S33: -0.0628
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 233 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3747 76.1567 41.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.4056 T22: 0.5791
REMARK 3 T33: 0.6365 T12: 0.0830
REMARK 3 T13: -0.0317 T23: -0.2469
REMARK 3 L TENSOR
REMARK 3 L11: 6.4405 L22: 2.1051
REMARK 3 L33: 9.5324 L12: -3.4543
REMARK 3 L13: 1.9208 L23: -0.0251
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: -0.2401 S13: 0.4857
REMARK 3 S21: 0.1110 S22: 0.1176 S23: -0.7723
REMARK 3 S31: -0.1271 S32: 1.0113 S33: -0.1560
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 254 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1479 67.8285 33.6245
REMARK 3 T TENSOR
REMARK 3 T11: 0.3557 T22: 0.6335
REMARK 3 T33: 0.6577 T12: 0.0386
REMARK 3 T13: -0.1299 T23: -0.2457
REMARK 3 L TENSOR
REMARK 3 L11: 2.3258 L22: 3.1795
REMARK 3 L33: 7.2732 L12: -1.8787
REMARK 3 L13: -1.8070 L23: -1.0028
REMARK 3 S TENSOR
REMARK 3 S11: 0.1912 S12: 0.0377 S13: -0.1609
REMARK 3 S21: 0.0331 S22: -0.0451 S23: -0.2109
REMARK 3 S31: 0.0509 S32: 0.7231 S33: -0.1171
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 8TRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1000276500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 1.02800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.010
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 30% PEG6000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 42.76400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.21400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.08650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.21400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.76400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.08650
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -65.08650
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 68.21400
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 PRO A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 32
REMARK 465 ASN A 33
REMARK 465 PRO A 34
REMARK 465 PRO A 35
REMARK 465 ASP A 36
REMARK 465 MET A 37
REMARK 465 LYS A 38
REMARK 465 ASP A 39
REMARK 465 GLY A 136
REMARK 465 GLY A 137
REMARK 465 ALA A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 GLY A 141
REMARK 465 GLU A 142
REMARK 465 GLY A 143
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 PRO B 5
REMARK 465 ALA B 6
REMARK 465 GLY B 32
REMARK 465 ASN B 33
REMARK 465 PRO B 34
REMARK 465 PRO B 35
REMARK 465 ASP B 36
REMARK 465 MET B 37
REMARK 465 LYS B 38
REMARK 465 ASP B 39
REMARK 465 GLY B 136
REMARK 465 GLY B 137
REMARK 465 ALA B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 GLY B 141
REMARK 465 GLU B 142
REMARK 465 GLY B 143
REMARK 465 GLY B 144
REMARK 465 VAL B 145
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 THR C 4
REMARK 465 PRO C 5
REMARK 465 ALA C 6
REMARK 465 ASN C 33
REMARK 465 PRO C 34
REMARK 465 PRO C 35
REMARK 465 ASP C 36
REMARK 465 MET C 37
REMARK 465 LYS C 38
REMARK 465 ASP C 39
REMARK 465 GLY C 40
REMARK 465 ASP C 41
REMARK 465 PRO C 42
REMARK 465 ARG C 43
REMARK 465 ARG C 44
REMARK 465 GLY C 136
REMARK 465 GLY C 137
REMARK 465 ALA C 138
REMARK 465 HIS C 139
REMARK 465 HIS C 140
REMARK 465 GLY C 141
REMARK 465 GLU C 142
REMARK 465 GLY C 143
REMARK 465 GLY C 144
REMARK 465 VAL C 145
REMARK 465 SER C 187
REMARK 465 GLU C 188
REMARK 465 TYR C 189
REMARK 465 SER C 190
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 THR D 3
REMARK 465 THR D 4
REMARK 465 PRO D 5
REMARK 465 ASN D 33
REMARK 465 PRO D 34
REMARK 465 PRO D 35
REMARK 465 ASP D 36
REMARK 465 MET D 37
REMARK 465 LYS D 38
REMARK 465 ASP D 39
REMARK 465 GLY D 40
REMARK 465 ASP D 41
REMARK 465 PRO D 42
REMARK 465 ARG D 43
REMARK 465 ARG D 44
REMARK 465 GLY D 136
REMARK 465 GLY D 137
REMARK 465 ALA D 138
REMARK 465 HIS D 139
REMARK 465 HIS D 140
REMARK 465 GLY D 141
REMARK 465 GLU D 142
REMARK 465 GLY D 143
REMARK 465 GLY D 144
REMARK 465 VAL D 145
REMARK 465 SER D 187
REMARK 465 GLU D 188
REMARK 465 TYR D 189
REMARK 465 SER D 190
REMARK 465 PRO D 191
REMARK 465 GLU D 192
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 SER A 121 -108.19 55.34
REMARK 500 ARG A 227 30.85 -88.30
REMARK 500 ASP A 257 -150.81 -94.48
REMARK 500 ARG B 43 57.90 -118.94
REMARK 500 ALA B 111 88.98 -66.00
REMARK 500 SER B 121 -111.87 55.61
REMARK 500 ASP B 246 116.08 -164.87
REMARK 500 ASP B 257 -155.99 -101.53
REMARK 500 LYS B 279 49.26 -97.21
REMARK 500 SER C 121 -114.48 56.75
REMARK 500 MET C 210 40.41 -81.96
REMARK 500 PRO C 244 -167.76 -72.63
REMARK 500 ASP C 247 71.84 33.61
REMARK 500 ASP C 257 -155.56 -101.44
REMARK 500 SER D 121 -114.92 55.17
REMARK 500 MET D 210 30.87 -88.61
REMARK 500 PRO D 244 37.52 -86.68
REMARK 500 ASP D 246 102.07 -167.21
REMARK 500 ASP D 257 -158.80 -103.00
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 B 529 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH C 491 DISTANCE = 6.25 ANGSTROMS
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 PE3 A 302
REMARK 610 PE3 A 303
REMARK 610 PE3 A 306
REMARK 610 PE3 B 301
REMARK 610 PE3 B 302
DBREF 8TRF A 1 280 UNP Q92KS5 Q92KS5_RHIME 1 280
DBREF 8TRF B 1 280 UNP Q92KS5 Q92KS5_RHIME 1 280
DBREF 8TRF C 1 280 UNP Q92KS5 Q92KS5_RHIME 1 280
DBREF 8TRF D 1 280 UNP Q92KS5 Q92KS5_RHIME 1 280
SEQRES 1 A 280 MET SER THR THR PRO ALA GLU THR GLU ILE THR ARG ILE
SEQRES 2 A 280 GLU VAL GLY THR GLY ALA ALA ALA ARG SER ILE ALA MET
SEQRES 3 A 280 ARG ILE PHE ARG THR GLY ASN PRO PRO ASP MET LYS ASP
SEQRES 4 A 280 GLY ASP PRO ARG ARG PRO ALA LEU VAL TRP LEU GLY GLY
SEQRES 5 A 280 TYR ARG SER ASP MET THR GLY THR LYS ALA VAL GLU VAL
SEQRES 6 A 280 GLU ARG HIS ALA ARG GLU ALA GLY THR ASP CYS ILE ARG
SEQRES 7 A 280 PHE ASP TYR SER GLY HIS GLY ALA SER ASP GLY ASP TYR
SEQRES 8 A 280 ARG ASP GLY THR ILE SER ARG TRP VAL GLU GLU SER LEU
SEQRES 9 A 280 ALA VAL ILE ASP HIS ALA ALA THR GLY ARG MET ILE LEU
SEQRES 10 A 280 ILE GLY SER SER MET GLY ALA TRP VAL ALA LEU ARG LEU
SEQRES 11 A 280 ALA GLU LYS LEU LYS GLY GLY ALA HIS HIS GLY GLU GLY
SEQRES 12 A 280 GLY VAL GLY ARG LEU CYS GLY LEU VAL LEU ILE ALA PRO
SEQRES 13 A 280 ALA PRO ASP PHE THR ALA GLU LEU ILE GLU PRO ASN LEU
SEQRES 14 A 280 THR GLU ALA GLU ARG THR SER LEU ALA GLU ARG GLY TYR
SEQRES 15 A 280 PHE GLU GLU PRO SER GLU TYR SER PRO GLU PRO ASN VAL
SEQRES 16 A 280 PHE THR ARG ALA LEU ILE GLU ASP GLY ARG ASN ASN LEU
SEQRES 17 A 280 VAL MET LYS GLY PRO ILE GLU THR GLY CYS PRO VAL HIS
SEQRES 18 A 280 ILE LEU GLN GLY MET ARG ASP PRO ASP VAL PRO TYR THR
SEQRES 19 A 280 HIS ALA LEU LYS LEU MET GLU HIS MET PRO ALA ASP ASP
SEQRES 20 A 280 VAL VAL MET THR LEU ILE ARG ASP GLY ASP HIS ARG LEU
SEQRES 21 A 280 SER ARG GLU GLU ASP ILE ALA LYS LEU LYS GLN ALA ILE
SEQRES 22 A 280 ASP ALA MET LEU THR LYS ALA
SEQRES 1 B 280 MET SER THR THR PRO ALA GLU THR GLU ILE THR ARG ILE
SEQRES 2 B 280 GLU VAL GLY THR GLY ALA ALA ALA ARG SER ILE ALA MET
SEQRES 3 B 280 ARG ILE PHE ARG THR GLY ASN PRO PRO ASP MET LYS ASP
SEQRES 4 B 280 GLY ASP PRO ARG ARG PRO ALA LEU VAL TRP LEU GLY GLY
SEQRES 5 B 280 TYR ARG SER ASP MET THR GLY THR LYS ALA VAL GLU VAL
SEQRES 6 B 280 GLU ARG HIS ALA ARG GLU ALA GLY THR ASP CYS ILE ARG
SEQRES 7 B 280 PHE ASP TYR SER GLY HIS GLY ALA SER ASP GLY ASP TYR
SEQRES 8 B 280 ARG ASP GLY THR ILE SER ARG TRP VAL GLU GLU SER LEU
SEQRES 9 B 280 ALA VAL ILE ASP HIS ALA ALA THR GLY ARG MET ILE LEU
SEQRES 10 B 280 ILE GLY SER SER MET GLY ALA TRP VAL ALA LEU ARG LEU
SEQRES 11 B 280 ALA GLU LYS LEU LYS GLY GLY ALA HIS HIS GLY GLU GLY
SEQRES 12 B 280 GLY VAL GLY ARG LEU CYS GLY LEU VAL LEU ILE ALA PRO
SEQRES 13 B 280 ALA PRO ASP PHE THR ALA GLU LEU ILE GLU PRO ASN LEU
SEQRES 14 B 280 THR GLU ALA GLU ARG THR SER LEU ALA GLU ARG GLY TYR
SEQRES 15 B 280 PHE GLU GLU PRO SER GLU TYR SER PRO GLU PRO ASN VAL
SEQRES 16 B 280 PHE THR ARG ALA LEU ILE GLU ASP GLY ARG ASN ASN LEU
SEQRES 17 B 280 VAL MET LYS GLY PRO ILE GLU THR GLY CYS PRO VAL HIS
SEQRES 18 B 280 ILE LEU GLN GLY MET ARG ASP PRO ASP VAL PRO TYR THR
SEQRES 19 B 280 HIS ALA LEU LYS LEU MET GLU HIS MET PRO ALA ASP ASP
SEQRES 20 B 280 VAL VAL MET THR LEU ILE ARG ASP GLY ASP HIS ARG LEU
SEQRES 21 B 280 SER ARG GLU GLU ASP ILE ALA LYS LEU LYS GLN ALA ILE
SEQRES 22 B 280 ASP ALA MET LEU THR LYS ALA
SEQRES 1 C 280 MET SER THR THR PRO ALA GLU THR GLU ILE THR ARG ILE
SEQRES 2 C 280 GLU VAL GLY THR GLY ALA ALA ALA ARG SER ILE ALA MET
SEQRES 3 C 280 ARG ILE PHE ARG THR GLY ASN PRO PRO ASP MET LYS ASP
SEQRES 4 C 280 GLY ASP PRO ARG ARG PRO ALA LEU VAL TRP LEU GLY GLY
SEQRES 5 C 280 TYR ARG SER ASP MET THR GLY THR LYS ALA VAL GLU VAL
SEQRES 6 C 280 GLU ARG HIS ALA ARG GLU ALA GLY THR ASP CYS ILE ARG
SEQRES 7 C 280 PHE ASP TYR SER GLY HIS GLY ALA SER ASP GLY ASP TYR
SEQRES 8 C 280 ARG ASP GLY THR ILE SER ARG TRP VAL GLU GLU SER LEU
SEQRES 9 C 280 ALA VAL ILE ASP HIS ALA ALA THR GLY ARG MET ILE LEU
SEQRES 10 C 280 ILE GLY SER SER MET GLY ALA TRP VAL ALA LEU ARG LEU
SEQRES 11 C 280 ALA GLU LYS LEU LYS GLY GLY ALA HIS HIS GLY GLU GLY
SEQRES 12 C 280 GLY VAL GLY ARG LEU CYS GLY LEU VAL LEU ILE ALA PRO
SEQRES 13 C 280 ALA PRO ASP PHE THR ALA GLU LEU ILE GLU PRO ASN LEU
SEQRES 14 C 280 THR GLU ALA GLU ARG THR SER LEU ALA GLU ARG GLY TYR
SEQRES 15 C 280 PHE GLU GLU PRO SER GLU TYR SER PRO GLU PRO ASN VAL
SEQRES 16 C 280 PHE THR ARG ALA LEU ILE GLU ASP GLY ARG ASN ASN LEU
SEQRES 17 C 280 VAL MET LYS GLY PRO ILE GLU THR GLY CYS PRO VAL HIS
SEQRES 18 C 280 ILE LEU GLN GLY MET ARG ASP PRO ASP VAL PRO TYR THR
SEQRES 19 C 280 HIS ALA LEU LYS LEU MET GLU HIS MET PRO ALA ASP ASP
SEQRES 20 C 280 VAL VAL MET THR LEU ILE ARG ASP GLY ASP HIS ARG LEU
SEQRES 21 C 280 SER ARG GLU GLU ASP ILE ALA LYS LEU LYS GLN ALA ILE
SEQRES 22 C 280 ASP ALA MET LEU THR LYS ALA
SEQRES 1 D 280 MET SER THR THR PRO ALA GLU THR GLU ILE THR ARG ILE
SEQRES 2 D 280 GLU VAL GLY THR GLY ALA ALA ALA ARG SER ILE ALA MET
SEQRES 3 D 280 ARG ILE PHE ARG THR GLY ASN PRO PRO ASP MET LYS ASP
SEQRES 4 D 280 GLY ASP PRO ARG ARG PRO ALA LEU VAL TRP LEU GLY GLY
SEQRES 5 D 280 TYR ARG SER ASP MET THR GLY THR LYS ALA VAL GLU VAL
SEQRES 6 D 280 GLU ARG HIS ALA ARG GLU ALA GLY THR ASP CYS ILE ARG
SEQRES 7 D 280 PHE ASP TYR SER GLY HIS GLY ALA SER ASP GLY ASP TYR
SEQRES 8 D 280 ARG ASP GLY THR ILE SER ARG TRP VAL GLU GLU SER LEU
SEQRES 9 D 280 ALA VAL ILE ASP HIS ALA ALA THR GLY ARG MET ILE LEU
SEQRES 10 D 280 ILE GLY SER SER MET GLY ALA TRP VAL ALA LEU ARG LEU
SEQRES 11 D 280 ALA GLU LYS LEU LYS GLY GLY ALA HIS HIS GLY GLU GLY
SEQRES 12 D 280 GLY VAL GLY ARG LEU CYS GLY LEU VAL LEU ILE ALA PRO
SEQRES 13 D 280 ALA PRO ASP PHE THR ALA GLU LEU ILE GLU PRO ASN LEU
SEQRES 14 D 280 THR GLU ALA GLU ARG THR SER LEU ALA GLU ARG GLY TYR
SEQRES 15 D 280 PHE GLU GLU PRO SER GLU TYR SER PRO GLU PRO ASN VAL
SEQRES 16 D 280 PHE THR ARG ALA LEU ILE GLU ASP GLY ARG ASN ASN LEU
SEQRES 17 D 280 VAL MET LYS GLY PRO ILE GLU THR GLY CYS PRO VAL HIS
SEQRES 18 D 280 ILE LEU GLN GLY MET ARG ASP PRO ASP VAL PRO TYR THR
SEQRES 19 D 280 HIS ALA LEU LYS LEU MET GLU HIS MET PRO ALA ASP ASP
SEQRES 20 D 280 VAL VAL MET THR LEU ILE ARG ASP GLY ASP HIS ARG LEU
SEQRES 21 D 280 SER ARG GLU GLU ASP ILE ALA LYS LEU LYS GLN ALA ILE
SEQRES 22 D 280 ASP ALA MET LEU THR LYS ALA
HET GOL A 301 6
HET PE3 A 302 13
HET PE3 A 303 16
HET GOL A 304 6
HET GOL A 305 6
HET PE3 A 306 17
HET PE3 B 301 17
HET PE3 B 302 13
HET GOL B 303 6
HET CL B 304 1
HET GOL C 301 6
HETNAM GOL GLYCEROL
HETNAM PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-
HETNAM 2 PE3 TRIDECAOXAHENTETRACONTANE-1,41-DIOL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN PE3 POLYETHYLENE GLYCOL
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 6 PE3 5(C28 H58 O15)
FORMUL 14 CL CL 1-
FORMUL 16 HOH *389(H2 O)
HELIX 1 AA1 THR A 17 ALA A 21 5 5
HELIX 2 AA2 GLY A 59 GLY A 73 1 15
HELIX 3 AA3 ASP A 90 GLY A 94 5 5
HELIX 4 AA4 THR A 95 ALA A 110 1 16
HELIX 5 AA5 MET A 122 LEU A 134 1 13
HELIX 6 AA6 ASP A 159 LEU A 164 1 6
HELIX 7 AA7 ILE A 165 LEU A 169 5 5
HELIX 8 AA8 THR A 170 ARG A 180 1 11
HELIX 9 AA9 ARG A 198 ASN A 206 1 9
HELIX 10 AB1 PRO A 232 HIS A 242 1 11
HELIX 11 AB2 ARG A 262 LYS A 279 1 18
HELIX 12 AB3 THR B 17 ALA B 21 5 5
HELIX 13 AB4 GLY B 59 GLY B 73 1 15
HELIX 14 AB5 ASP B 90 GLY B 94 5 5
HELIX 15 AB6 THR B 95 ALA B 110 1 16
HELIX 16 AB7 MET B 122 LEU B 134 1 13
HELIX 17 AB8 ASP B 159 LEU B 164 1 6
HELIX 18 AB9 ILE B 165 LEU B 169 5 5
HELIX 19 AC1 THR B 170 GLY B 181 1 12
HELIX 20 AC2 ARG B 198 ASN B 206 1 9
HELIX 21 AC3 PRO B 232 HIS B 242 1 11
HELIX 22 AC4 ARG B 262 LYS B 279 1 18
HELIX 23 AC5 THR C 17 ALA C 21 5 5
HELIX 24 AC6 GLY C 59 GLY C 73 1 15
HELIX 25 AC7 ASP C 90 GLY C 94 5 5
HELIX 26 AC8 THR C 95 ALA C 111 1 17
HELIX 27 AC9 SER C 121 LEU C 134 1 14
HELIX 28 AD1 ASP C 159 LEU C 164 1 6
HELIX 29 AD2 ILE C 165 LEU C 169 5 5
HELIX 30 AD3 THR C 170 ARG C 180 1 11
HELIX 31 AD4 ARG C 198 ASN C 206 1 9
HELIX 32 AD5 PRO C 232 HIS C 242 1 11
HELIX 33 AD6 ARG C 262 LYS C 279 1 18
HELIX 34 AD7 THR D 17 ALA D 21 5 5
HELIX 35 AD8 GLY D 59 GLY D 73 1 15
HELIX 36 AD9 ASP D 90 GLY D 94 5 5
HELIX 37 AE1 THR D 95 ALA D 111 1 17
HELIX 38 AE2 MET D 122 LEU D 134 1 13
HELIX 39 AE3 ASP D 159 LEU D 164 1 6
HELIX 40 AE4 ILE D 165 LEU D 169 5 5
HELIX 41 AE5 THR D 170 GLU D 179 1 10
HELIX 42 AE6 ARG D 198 ARG D 205 1 8
HELIX 43 AE7 ASN D 206 LEU D 208 5 3
HELIX 44 AE8 PRO D 232 HIS D 242 1 11
HELIX 45 AE9 ARG D 262 LYS D 279 1 18
SHEET 1 AA1 8 THR A 11 VAL A 15 0
SHEET 2 AA1 8 ARG A 22 PHE A 29 -1 O MET A 26 N THR A 11
SHEET 3 AA1 8 ASP A 75 PHE A 79 -1 O ARG A 78 N ARG A 27
SHEET 4 AA1 8 ALA A 46 LEU A 50 1 N LEU A 47 O ILE A 77
SHEET 5 AA1 8 MET A 115 SER A 120 1 O ILE A 118 N VAL A 48
SHEET 6 AA1 8 LEU A 148 ILE A 154 1 O CYS A 149 N MET A 115
SHEET 7 AA1 8 VAL A 220 GLY A 225 1 O LEU A 223 N LEU A 153
SHEET 8 AA1 8 VAL A 248 ILE A 253 1 O THR A 251 N ILE A 222
SHEET 1 AA2 2 TYR A 182 GLU A 185 0
SHEET 2 AA2 2 ASN A 194 THR A 197 -1 O ASN A 194 N GLU A 185
SHEET 1 AA316 ILE B 10 VAL B 15 0
SHEET 2 AA316 ARG B 22 PHE B 29 -1 O ARG B 22 N VAL B 15
SHEET 3 AA316 ASP B 75 PHE B 79 -1 O ARG B 78 N ARG B 27
SHEET 4 AA316 ALA B 46 LEU B 50 1 N LEU B 47 O ILE B 77
SHEET 5 AA316 ARG B 114 SER B 120 1 O ILE B 118 N VAL B 48
SHEET 6 AA316 ARG B 147 ILE B 154 1 O CYS B 149 N MET B 115
SHEET 7 AA316 VAL B 220 GLY B 225 1 O LEU B 223 N LEU B 153
SHEET 8 AA316 VAL B 248 ILE B 253 1 O THR B 251 N ILE B 222
SHEET 9 AA316 VAL C 248 ILE C 253 -1 O MET C 250 N LEU B 252
SHEET 10 AA316 VAL C 220 GLY C 225 1 N GLN C 224 O ILE C 253
SHEET 11 AA316 LEU C 148 ILE C 154 1 N LEU C 153 O LEU C 223
SHEET 12 AA316 MET C 115 SER C 120 1 N GLY C 119 O ILE C 154
SHEET 13 AA316 ALA C 46 LEU C 50 1 N VAL C 48 O ILE C 118
SHEET 14 AA316 CYS C 76 PHE C 79 1 O ILE C 77 N LEU C 47
SHEET 15 AA316 ARG C 22 PHE C 29 -1 N PHE C 29 O CYS C 76
SHEET 16 AA316 ILE C 10 VAL C 15 -1 N THR C 11 O MET C 26
SHEET 1 AA4 2 TYR B 182 GLU B 185 0
SHEET 2 AA4 2 ASN B 194 THR B 197 -1 O ASN B 194 N GLU B 185
SHEET 1 AA5 2 TYR C 182 GLU C 185 0
SHEET 2 AA5 2 ASN C 194 THR C 197 -1 O ASN C 194 N GLU C 185
SHEET 1 AA6 8 THR D 11 VAL D 15 0
SHEET 2 AA6 8 ARG D 22 PHE D 29 -1 O ARG D 22 N VAL D 15
SHEET 3 AA6 8 ASP D 75 PHE D 79 -1 O ARG D 78 N ARG D 27
SHEET 4 AA6 8 ALA D 46 LEU D 50 1 N LEU D 47 O ILE D 77
SHEET 5 AA6 8 MET D 115 SER D 120 1 O ILE D 118 N VAL D 48
SHEET 6 AA6 8 LEU D 148 ILE D 154 1 O ILE D 154 N GLY D 119
SHEET 7 AA6 8 VAL D 220 GLY D 225 1 O LEU D 223 N LEU D 153
SHEET 8 AA6 8 VAL D 248 ILE D 253 1 O THR D 251 N ILE D 222
SHEET 1 AA7 2 TYR D 182 GLU D 185 0
SHEET 2 AA7 2 ASN D 194 THR D 197 -1 O PHE D 196 N PHE D 183
CRYST1 85.528 130.173 136.428 90.00 90.00 90.00 P 21 21 21 16
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 0.011692 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007330 0.00000
TER 1990 ALA A 280
TER 3969 ALA B 280
TER 5878 ALA C 280
TER 7776 ALA D 280
MASTER 923 0 11 45 40 0 0 6 8268 4 106 88
END |