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HEADER PLANT PROTEIN 13-JUL-18 6A9D
TITLE CRYSTAL STRUCTURE OF THE STRIGOLACTONE RECEPTOR SHHTL7 FROM STRIGA
TITLE 2 HERMONTHICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE 4 ORGANISM_TAXID: 68872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RECEPTOR, STRIGOLACTONES, PROTEIN, INHIBITOR, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHANG,Z.XI,D.W.WANG
REVDAT 1 17-JUL-19 6A9D 0
JRNL AUTH Y.Y.ZHANG,Z.XI,D.W.WANG
JRNL TITL CRYSTAL STRUCTURE OF THE STRIGOLACTONE RECEPTOR SHHTL5 FROM
JRNL TITL 2 STRIGA HERMONTHICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 24987
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) : 0.183
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1271
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 39.2913 - 4.7859 0.99 2689 136 0.1703 0.2190
REMARK 3 2 4.7859 - 3.7997 0.99 2649 139 0.1518 0.2075
REMARK 3 3 3.7997 - 3.3197 0.99 2619 150 0.1779 0.2236
REMARK 3 4 3.3197 - 3.0163 1.00 2666 144 0.1983 0.2666
REMARK 3 5 3.0163 - 2.8001 1.00 2641 137 0.2141 0.2730
REMARK 3 6 2.8001 - 2.6351 1.00 2629 152 0.2255 0.2954
REMARK 3 7 2.6351 - 2.5031 1.00 2615 145 0.2151 0.2932
REMARK 3 8 2.5031 - 2.3942 1.00 2641 140 0.2229 0.3214
REMARK 3 9 2.3942 - 2.3020 0.97 2567 128 0.2336 0.2889
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.38
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 : 0.008 4318
REMARK 3 ANGLE : 1.169 5871
REMARK 3 CHIRALITY : 0.064 674
REMARK 3 PLANARITY : 0.009 750
REMARK 3 DIHEDRAL : 6.522 2590
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -6 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.0355 -10.5496 -9.3366
REMARK 3 T TENSOR
REMARK 3 T11: 0.6741 T22: 0.4110
REMARK 3 T33: 0.3100 T12: 0.0130
REMARK 3 T13: 0.0677 T23: 0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 8.0743 L22: 3.3374
REMARK 3 L33: 6.9276 L12: 4.8885
REMARK 3 L13: 4.1769 L23: 3.9097
REMARK 3 S TENSOR
REMARK 3 S11: -0.3493 S12: 0.5181 S13: 0.0353
REMARK 3 S21: -0.5506 S22: 0.2528 S23: 0.0450
REMARK 3 S31: -0.8945 S32: -0.0767 S33: 0.1912
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9276 -9.8867 -0.8939
REMARK 3 T TENSOR
REMARK 3 T11: 0.5823 T22: 0.2989
REMARK 3 T33: 0.3322 T12: -0.0206
REMARK 3 T13: 0.1077 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.4000 L22: 0.5353
REMARK 3 L33: 3.5497 L12: 0.1066
REMARK 3 L13: -0.3573 L23: 0.8482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0580 S12: 0.0304 S13: 0.1403
REMARK 3 S21: -0.0778 S22: 0.0762 S23: -0.0416
REMARK 3 S31: -0.4228 S32: 0.4685 S33: -0.1701
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8363 -29.9264 9.2844
REMARK 3 T TENSOR
REMARK 3 T11: 0.5619 T22: 0.6363
REMARK 3 T33: 0.5760 T12: 0.2293
REMARK 3 T13: 0.0448 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 4.3917 L22: 2.8581
REMARK 3 L33: 7.6329 L12: 3.5465
REMARK 3 L13: -0.2614 L23: -0.2586
REMARK 3 S TENSOR
REMARK 3 S11: -0.1848 S12: -0.4019 S13: -1.0998
REMARK 3 S21: 0.2486 S22: 0.4556 S23: -0.3212
REMARK 3 S31: 1.1410 S32: 1.0563 S33: -0.0860
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3761 -32.0204 11.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.8144 T22: 0.4625
REMARK 3 T33: 0.6072 T12: -0.0273
REMARK 3 T13: 0.1025 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 5.7636 L22: 1.6874
REMARK 3 L33: 5.3221 L12: -1.4984
REMARK 3 L13: -0.6876 L23: -0.3107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0363 S12: 0.0887 S13: -1.2901
REMARK 3 S21: -0.0668 S22: -0.1552 S23: -0.1807
REMARK 3 S31: 1.4073 S32: -0.4599 S33: 0.1169
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4945 -17.7037 16.5108
REMARK 3 T TENSOR
REMARK 3 T11: 0.6127 T22: 0.4420
REMARK 3 T33: 0.3374 T12: 0.0289
REMARK 3 T13: 0.0694 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 5.5382 L22: 2.1642
REMARK 3 L33: 2.6295 L12: -0.7871
REMARK 3 L13: 3.8026 L23: -0.6374
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.7191 S13: 0.2634
REMARK 3 S21: 0.2928 S22: -0.0722 S23: 0.0089
REMARK 3 S31: 0.4668 S32: -0.3556 S33: 0.1104
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.6601 -26.2036 1.3644
REMARK 3 T TENSOR
REMARK 3 T11: 0.6800 T22: 0.3009
REMARK 3 T33: 0.4750 T12: -0.0004
REMARK 3 T13: 0.1363 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 2.0048 L22: 1.6143
REMARK 3 L33: 6.1486 L12: -0.7381
REMARK 3 L13: 0.5109 L23: 1.2597
REMARK 3 S TENSOR
REMARK 3 S11: 0.1756 S12: 0.1347 S13: -1.0214
REMARK 3 S21: 0.2152 S22: -0.1761 S23: 0.1927
REMARK 3 S31: 0.5074 S32: 0.1137 S33: -0.0917
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3895 -21.9686 -1.5665
REMARK 3 T TENSOR
REMARK 3 T11: 0.5265 T22: 0.7779
REMARK 3 T33: 0.4893 T12: 0.1251
REMARK 3 T13: 0.1174 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 2.7136 L22: 7.0637
REMARK 3 L33: 4.6306 L12: 1.6912
REMARK 3 L13: -0.5146 L23: -0.1593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.1457 S13: 0.0956
REMARK 3 S21: -0.1658 S22: 0.2038 S23: 0.0296
REMARK 3 S31: 0.2000 S32: 1.1208 S33: -0.3163
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3894 -12.9424 13.3841
REMARK 3 T TENSOR
REMARK 3 T11: 0.4587 T22: 0.5430
REMARK 3 T33: 0.3564 T12: -0.0378
REMARK 3 T13: -0.0037 T23: -0.0923
REMARK 3 L TENSOR
REMARK 3 L11: 3.6580 L22: 2.4839
REMARK 3 L33: 4.7656 L12: -1.0371
REMARK 3 L13: -0.9373 L23: 1.4245
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: -0.4696 S13: 0.1104
REMARK 3 S21: 0.1741 S22: 0.3196 S23: -0.2968
REMARK 3 S31: 0.0028 S32: 1.1620 S33: -0.2944
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0962 -40.5675 -25.3544
REMARK 3 T TENSOR
REMARK 3 T11: 0.4830 T22: 0.4843
REMARK 3 T33: 0.3675 T12: 0.1899
REMARK 3 T13: 0.0652 T23: 0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 4.1200 L22: 5.4196
REMARK 3 L33: 3.6147 L12: 0.8426
REMARK 3 L13: 0.7238 L23: -0.7128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: -0.0307 S13: -0.4822
REMARK 3 S21: -0.2074 S22: 0.0385 S23: -0.3130
REMARK 3 S31: 0.7941 S32: 0.8530 S33: -0.0648
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4365 -39.7706 -26.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5923 T22: 0.5466
REMARK 3 T33: 0.3086 T12: 0.2195
REMARK 3 T13: 0.0126 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 5.4541 L22: 6.9664
REMARK 3 L33: 3.9651 L12: 4.3038
REMARK 3 L13: 1.7037 L23: 0.2784
REMARK 3 S TENSOR
REMARK 3 S11: 0.1225 S12: 0.2121 S13: -0.3626
REMARK 3 S21: 0.2083 S22: -0.1771 S23: -0.5155
REMARK 3 S31: 0.5967 S32: 0.4529 S33: -0.0259
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9233 -30.3155 -33.5647
REMARK 3 T TENSOR
REMARK 3 T11: 0.4650 T22: 0.8851
REMARK 3 T33: 0.4463 T12: 0.0872
REMARK 3 T13: 0.1123 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 3.4073 L22: 7.5910
REMARK 3 L33: 5.8935 L12: 1.2684
REMARK 3 L13: 0.7362 L23: 2.2430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0487 S12: 0.3798 S13: -0.0815
REMARK 3 S21: -0.2784 S22: 0.2032 S23: -0.8639
REMARK 3 S31: 0.2649 S32: 1.3207 S33: -0.1590
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 89 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0821 -32.9683 -35.9632
REMARK 3 T TENSOR
REMARK 3 T11: 0.4290 T22: 0.4060
REMARK 3 T33: 0.3615 T12: 0.0697
REMARK 3 T13: 0.0464 T23: 0.0811
REMARK 3 L TENSOR
REMARK 3 L11: 4.7855 L22: 7.1392
REMARK 3 L33: 8.5883 L12: 0.6733
REMARK 3 L13: -1.0369 L23: -0.2089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: 0.6645 S13: 0.3356
REMARK 3 S21: 0.5744 S22: -0.0460 S23: 0.0234
REMARK 3 S31: -0.1270 S32: 0.3647 S33: 0.0386
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0937 -26.0485 -36.8331
REMARK 3 T TENSOR
REMARK 3 T11: 0.4145 T22: 0.4070
REMARK 3 T33: 0.3091 T12: 0.0007
REMARK 3 T13: 0.0089 T23: 0.0946
REMARK 3 L TENSOR
REMARK 3 L11: 4.2753 L22: 6.0788
REMARK 3 L33: 6.2458 L12: -0.3851
REMARK 3 L13: -1.3560 L23: 0.5780
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: 0.4701 S13: 0.4099
REMARK 3 S21: -0.1163 S22: -0.0515 S23: 0.3625
REMARK 3 S31: -0.2211 S32: 0.1963 S33: 0.0927
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7182 -9.1789 -24.1242
REMARK 3 T TENSOR
REMARK 3 T11: 1.1161 T22: 0.8592
REMARK 3 T33: 0.8146 T12: 0.1847
REMARK 3 T13: -0.0043 T23: -0.1291
REMARK 3 L TENSOR
REMARK 3 L11: 4.0598 L22: 3.9062
REMARK 3 L33: 7.0442 L12: -1.6290
REMARK 3 L13: 5.3386 L23: -1.8302
REMARK 3 S TENSOR
REMARK 3 S11: -1.1870 S12: -1.3001 S13: 2.1905
REMARK 3 S21: 1.2839 S22: 0.5489 S23: 0.1348
REMARK 3 S31: -2.5688 S32: 0.2205 S33: 0.5224
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7490 -24.9602 -13.5046
REMARK 3 T TENSOR
REMARK 3 T11: 0.7017 T22: 0.5014
REMARK 3 T33: 0.3916 T12: 0.0569
REMARK 3 T13: 0.1388 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 7.2194 L22: 5.4768
REMARK 3 L33: 5.6850 L12: 0.2459
REMARK 3 L13: -0.5253 L23: 0.7044
REMARK 3 S TENSOR
REMARK 3 S11: 0.1337 S12: -0.8847 S13: 0.1053
REMARK 3 S21: 0.6977 S22: 0.0156 S23: 0.2944
REMARK 3 S31: 0.1255 S32: 0.5431 S33: -0.0453
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9894 -18.8959 -24.1297
REMARK 3 T TENSOR
REMARK 3 T11: 0.5873 T22: 0.4791
REMARK 3 T33: 0.4630 T12: -0.0693
REMARK 3 T13: 0.0555 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 7.0373 L22: 2.2851
REMARK 3 L33: 2.7121 L12: -3.5119
REMARK 3 L13: 3.9803 L23: -2.4797
REMARK 3 S TENSOR
REMARK 3 S11: -0.4000 S12: 0.5173 S13: 0.5953
REMARK 3 S21: 0.2315 S22: 0.0589 S23: -0.8601
REMARK 3 S31: -0.6595 S32: 0.2094 S33: 0.2462
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 195 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3940 -27.6021 -37.6120
REMARK 3 T TENSOR
REMARK 3 T11: 0.4113 T22: 0.4191
REMARK 3 T33: 0.3022 T12: -0.0086
REMARK 3 T13: 0.0287 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 3.7984 L22: 3.8878
REMARK 3 L33: 4.5206 L12: -0.7879
REMARK 3 L13: -1.2465 L23: 0.4892
REMARK 3 S TENSOR
REMARK 3 S11: -0.0664 S12: 0.5243 S13: 0.1441
REMARK 3 S21: -0.1377 S22: 0.0206 S23: 0.1936
REMARK 3 S31: 0.0276 S32: -0.3335 S33: 0.0548
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 232 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3345 -38.5337 -29.1676
REMARK 3 T TENSOR
REMARK 3 T11: 0.5525 T22: 0.3050
REMARK 3 T33: 0.4007 T12: -0.0052
REMARK 3 T13: 0.0565 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 1.9292 L22: 1.8950
REMARK 3 L33: 6.2008 L12: 0.3031
REMARK 3 L13: -0.2359 L23: -0.1937
REMARK 3 S TENSOR
REMARK 3 S11: -0.0480 S12: 0.1717 S13: -0.0016
REMARK 3 S21: -0.0093 S22: 0.0817 S23: 0.2636
REMARK 3 S31: 0.5485 S32: -0.4256 S33: -0.0842
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 3 THROUGH 268)
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 2416
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6A9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SHELX
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25025
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 0.2M MGCL2, 20%
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.27400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.27400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 APPLY THE FOLLOWING TO CHAINS: A, 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 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 -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 THR A 269
REMARK 465 ASP A 270
REMARK 465 HIS A 271
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 269
REMARK 465 ASP B 270
REMARK 465 HIS B 271
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 GLY A 16 NZ LYS A 45 2.04
REMARK 500 OD1 ASN A 180 O HOH A 301 2.12
REMARK 500 NE2 GLN B 213 O HOH B 401 2.16
REMARK 500 O HOH A 332 O HOH A 334 2.16
REMARK 500 OD1 ASP A -1 O HOH A 302 2.18
REMARK 500 OD2 ASP A 60 O HOH A 302 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 226 CB GLU A 226 CG 0.114
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 144 NH1 - CZ - NH2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 GLU A 226 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 LEU B 35 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 GLU B 128 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 3 141.82 -173.90
REMARK 500 THR A 28 -167.26 -121.54
REMARK 500 LYS A 88 60.20 33.17
REMARK 500 SER A 95 -107.50 46.62
REMARK 500 ARG A 123 133.96 -171.85
REMARK 500 THR A 127 -166.82 -128.55
REMARK 500 ASN A 149 94.96 -167.85
REMARK 500 SER A 168 143.82 -32.46
REMARK 500 LYS B 88 64.86 32.74
REMARK 500 SER B 95 -115.13 49.14
REMARK 500 ARG B 123 135.56 -172.73
REMARK 500 SER B 168 142.14 -35.18
REMARK 500 MET B 252 58.78 -140.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 149 PHE B 150 -140.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU B 128 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
DBREF1 6A9D A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 6A9D A A0A0M3PNA2 1 271
DBREF1 6A9D B 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 6A9D B A0A0M3PNA2 1 271
SEQADV 6A9D MET A -13 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ALA A -12 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D SER A -11 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D MET A -10 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D THR A -9 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY A -8 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY A -7 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLN A -6 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLN A -5 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D MET A -4 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY A -3 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ARG A -2 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ASP A -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D PRO A 0 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D MET B -13 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ALA B -12 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D SER B -11 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D MET B -10 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D THR B -9 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY B -8 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY B -7 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLN B -6 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLN B -5 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D MET B -4 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D GLY B -3 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ARG B -2 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D ASP B -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 6A9D PRO B 0 UNP A0A0M3PNA EXPRESSION TAG
SEQRES 1 A 285 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG ASP
SEQRES 2 A 285 PRO MET SER SER ILE GLY LEU ALA HIS ASN VAL THR ILE
SEQRES 3 A 285 LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY
SEQRES 4 A 285 TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL PRO
SEQRES 5 A 285 TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP HIS
SEQRES 6 A 285 MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE
SEQRES 7 A 285 ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU
SEQRES 8 A 285 ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS ILE
SEQRES 9 A 285 TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA VAL
SEQRES 10 A 285 ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU VAL
SEQRES 11 A 285 MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU GLU
SEQRES 12 A 285 TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU THR
SEQRES 13 A 285 LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER LEU
SEQRES 14 A 285 GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER
SEQRES 15 A 285 ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN MET
SEQRES 16 A 285 ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE CYS
SEQRES 17 A 285 GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR VAL
SEQRES 18 A 285 PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET VAL
SEQRES 19 A 285 PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU GLY
SEQRES 20 A 285 GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY HIS
SEQRES 21 A 285 LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO VAL
SEQRES 22 A 285 VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 1 B 285 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG ASP
SEQRES 2 B 285 PRO MET SER SER ILE GLY LEU ALA HIS ASN VAL THR ILE
SEQRES 3 B 285 LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY
SEQRES 4 B 285 TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL PRO
SEQRES 5 B 285 TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP HIS
SEQRES 6 B 285 MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE
SEQRES 7 B 285 ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP LEU
SEQRES 8 B 285 ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS ILE
SEQRES 9 B 285 TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA VAL
SEQRES 10 B 285 ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU VAL
SEQRES 11 B 285 MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU GLU
SEQRES 12 B 285 TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU THR
SEQRES 13 B 285 LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER LEU
SEQRES 14 B 285 GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU SER
SEQRES 15 B 285 ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN MET
SEQRES 16 B 285 ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE CYS
SEQRES 17 B 285 GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR VAL
SEQRES 18 B 285 PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET VAL
SEQRES 19 B 285 PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU GLY
SEQRES 20 B 285 GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY HIS
SEQRES 21 B 285 LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO VAL
SEQRES 22 B 285 VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
HET GOL B 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *61(H2 O)
HELIX 1 AA1 SER A 3 HIS A 8 1 6
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 LEU A 70 PHE A 84 1 15
HELIX 6 AA6 SER A 95 ARG A 108 1 14
HELIX 7 AA7 GLU A 135 ASN A 149 1 15
HELIX 8 AA8 ASN A 149 ALA A 163 1 15
HELIX 9 AA9 SER A 168 PHE A 179 1 12
HELIX 10 AB1 ARG A 182 GLY A 195 1 14
HELIX 11 AB2 LEU A 198 GLY A 203 1 6
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 MET A 252 1 6
HELIX 14 AB5 MET A 252 GLN A 266 1 15
HELIX 15 AB6 ILE B 4 HIS B 8 1 5
HELIX 16 AB7 ASP B 29 LYS B 34 5 6
HELIX 17 AB8 LEU B 36 LEU B 40 5 5
HELIX 18 AB9 ASN B 58 PHE B 62 5 5
HELIX 19 AC1 ASP B 63 SER B 68 1 6
HELIX 20 AC2 LEU B 70 PHE B 84 1 15
HELIX 21 AC3 SER B 95 ARG B 108 1 14
HELIX 22 AC4 GLU B 135 ALA B 163 1 29
HELIX 23 AC5 SER B 168 PHE B 179 1 12
HELIX 24 AC6 ARG B 182 GLY B 195 1 14
HELIX 25 AC7 LEU B 198 GLY B 203 1 6
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 MET B 252 1 6
HELIX 28 AD1 MET B 252 GLN B 266 1 15
SHEET 1 AA1 7 THR A 11 GLY A 14 0
SHEET 2 AA1 7 LYS A 45 LEU A 48 -1 O LEU A 48 N THR A 11
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N VAL A 20 O LYS A 45
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 92 N GLY A 23
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N TYR A 91
SHEET 6 AA1 7 CYS A 209 ASN A 216 1 O HIS A 210 N LEU A 115
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O VAL A 237 N ILE A 211
SHEET 1 AA2 7 THR B 11 GLY B 14 0
SHEET 2 AA2 7 LYS B 45 LEU B 48 -1 O LEU B 48 N THR B 11
SHEET 3 AA2 7 THR B 19 GLY B 23 1 N VAL B 20 O LYS B 45
SHEET 4 AA2 7 CYS B 89 HIS B 94 1 O VAL B 92 N VAL B 21
SHEET 5 AA2 7 PHE B 112 ILE B 118 1 O VAL B 116 N TYR B 91
SHEET 6 AA2 7 CYS B 209 ASN B 216 1 O ILE B 212 N MET B 117
SHEET 7 AA2 7 SER B 236 GLU B 244 1 O VAL B 237 N ILE B 211
CISPEP 1 GLU A 128 GLU A 129 0 -21.00
SITE 1 AC1 3 ASP A 65 ALA B 163 ASP B 165
CRYST1 92.548 92.500 75.428 90.00 116.92 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010805 0.000000 0.005486 0.00000
SCALE2 0.000000 0.010811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014869 0.00000
TER 2144 ILE A 268
TER 4218 ILE B 268
MASTER 628 0 1 28 14 0 1 6 4283 2 6 44
END |