| content |
HEADER LIGASE 01-DEC-17 6BRT
TITLE F-BOX PROTEIN CTH WITH HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D3-CTH-D14-D-RING;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA GLUMIPATULA;
SOURCE 3 ORGANISM_TAXID: 40148;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS UBIQUITIN LIGASE, F-BOX, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SHABEK,N.ZHENG,H.MAO,T.R.HINDS,F.TICCHIARELLI,O.LEYSER
REVDAT 1 21-NOV-18 6BRT 0
JRNL AUTH N.SHABEK,F.TICCHIARELLI,H.MAO,T.R.HINDS,O.LEYSER,N.ZHENG
JRNL TITL STRUCTURAL PLASTICITY OF D3-D14 UBIQUITIN LIGASE IN
JRNL TITL 2 STRIGOLACTONE SIGNALLING
JRNL REF NATURE 2018
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/S41586-018-0743-5
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 115552
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
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 44.1652 - 5.7626 0.99 8212 140 0.2127 0.2376
REMARK 3 2 5.7626 - 4.5755 1.00 8186 141 0.2217 0.3018
REMARK 3 3 4.5755 - 3.9975 1.00 8128 142 0.2135 0.2424
REMARK 3 4 3.9975 - 3.6322 1.00 8142 145 0.2425 0.2826
REMARK 3 5 3.6322 - 3.3720 1.00 8112 142 0.2454 0.3303
REMARK 3 6 3.3720 - 3.1732 1.00 8128 144 0.2588 0.3460
REMARK 3 7 3.1732 - 3.0144 1.00 8110 142 0.2662 0.3202
REMARK 3 8 3.0144 - 2.8832 1.00 8095 143 0.2686 0.3455
REMARK 3 9 2.8832 - 2.7722 1.00 8129 141 0.2734 0.3139
REMARK 3 10 2.7722 - 2.6766 1.00 8094 144 0.2776 0.3562
REMARK 3 11 2.6766 - 2.5929 1.00 8102 143 0.2724 0.3454
REMARK 3 12 2.5929 - 2.5188 1.00 8039 138 0.2782 0.3670
REMARK 3 13 2.5188 - 2.4525 1.00 8137 146 0.2791 0.3160
REMARK 3 14 2.4525 - 2.3926 0.98 7948 139 0.2971 0.3554
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.10
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 : 0.009 16981
REMARK 3 ANGLE : 1.089 23146
REMARK 3 CHIRALITY : 0.045 2690
REMARK 3 PLANARITY : 0.004 3000
REMARK 3 DIHEDRAL : 14.354 6013
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 38
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -16 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 146.3471 167.1404 24.1303
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.5813
REMARK 3 T33: 0.6027 T12: -0.1009
REMARK 3 T13: -0.0748 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.9488 L22: 0.4257
REMARK 3 L33: 0.4687 L12: -0.6695
REMARK 3 L13: 0.0547 L23: 0.2018
REMARK 3 S TENSOR
REMARK 3 S11: -0.1949 S12: 0.4034 S13: -0.0900
REMARK 3 S21: 0.1113 S22: 0.0654 S23: -0.9842
REMARK 3 S31: -0.5855 S32: 0.9373 S33: 0.1337
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 128.6079 160.3127 26.5176
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: 0.0595
REMARK 3 T33: 0.1077 T12: 0.0409
REMARK 3 T13: -0.0086 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.3319 L22: 2.2519
REMARK 3 L33: 2.5634 L12: 0.3878
REMARK 3 L13: -0.2229 L23: -0.7369
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: 0.0658 S13: -0.1310
REMARK 3 S21: 0.0903 S22: -0.1107 S23: 0.0171
REMARK 3 S31: 0.0291 S32: 0.2848 S33: 0.0771
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 134.7537 165.3478 12.9280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: 0.2409
REMARK 3 T33: 0.1803 T12: 0.0767
REMARK 3 T13: 0.1455 T23: 0.1164
REMARK 3 L TENSOR
REMARK 3 L11: 1.7507 L22: 1.7561
REMARK 3 L33: 1.2294 L12: -0.7016
REMARK 3 L13: 0.4444 L23: -0.2197
REMARK 3 S TENSOR
REMARK 3 S11: -0.1443 S12: 0.6388 S13: 0.2283
REMARK 3 S21: -0.4278 S22: -0.0320 S23: -0.4762
REMARK 3 S31: -0.1442 S32: 0.7418 S33: 0.0553
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 119.5416 158.5629 11.6177
REMARK 3 T TENSOR
REMARK 3 T11: 0.1380 T22: 0.1292
REMARK 3 T33: 0.0840 T12: -0.0071
REMARK 3 T13: 0.0303 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.1682 L22: 1.5143
REMARK 3 L33: 0.5774 L12: -0.8868
REMARK 3 L13: -0.5693 L23: -0.3518
REMARK 3 S TENSOR
REMARK 3 S11: -0.1306 S12: 0.1804 S13: -0.1230
REMARK 3 S21: -0.0992 S22: 0.0493 S23: 0.0397
REMARK 3 S31: 0.0571 S32: -0.1487 S33: 0.0773
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 122.1827 146.4009 20.3989
REMARK 3 T TENSOR
REMARK 3 T11: 0.2685 T22: 0.1033
REMARK 3 T33: 0.1690 T12: 0.0201
REMARK 3 T13: 0.0605 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.5723 L22: 0.6541
REMARK 3 L33: 1.8047 L12: -0.2280
REMARK 3 L13: -0.8494 L23: 0.7831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0671 S12: 0.3399 S13: -0.3306
REMARK 3 S21: -0.0747 S22: -0.1133 S23: 0.0691
REMARK 3 S31: 0.1880 S32: -0.0975 S33: 0.0608
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -16 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 116.1529 133.7852 13.6104
REMARK 3 T TENSOR
REMARK 3 T11: 0.8160 T22: 0.4002
REMARK 3 T33: 0.6459 T12: 0.0315
REMARK 3 T13: 0.0673 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 3.2244 L22: 5.3049
REMARK 3 L33: 0.3143 L12: -4.0205
REMARK 3 L13: 0.5108 L23: -0.9536
REMARK 3 S TENSOR
REMARK 3 S11: -0.3586 S12: 0.0870 S13: 0.9295
REMARK 3 S21: 0.2113 S22: 0.2286 S23: -0.0316
REMARK 3 S31: -0.6273 S32: -0.2658 S33: 0.0019
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 120.2937 111.5736 9.5153
REMARK 3 T TENSOR
REMARK 3 T11: 0.3661 T22: 0.2154
REMARK 3 T33: 0.2784 T12: 0.0160
REMARK 3 T13: -0.0472 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.4723 L22: 1.9154
REMARK 3 L33: 2.0104 L12: 0.7958
REMARK 3 L13: -0.5216 L23: 0.2635
REMARK 3 S TENSOR
REMARK 3 S11: -0.1504 S12: 0.1015 S13: -0.0361
REMARK 3 S21: -0.1671 S22: 0.1502 S23: 0.0158
REMARK 3 S31: -0.0212 S32: -0.3095 S33: -0.0169
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 121.6144 114.0889 11.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3840 T22: 0.2383
REMARK 3 T33: 0.3048 T12: 0.1115
REMARK 3 T13: 0.0550 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 3.0653 L22: 1.8632
REMARK 3 L33: 3.2254 L12: 1.1473
REMARK 3 L13: 1.4393 L23: 0.3065
REMARK 3 S TENSOR
REMARK 3 S11: -0.1075 S12: 0.1212 S13: 0.3357
REMARK 3 S21: 0.1579 S22: 0.0264 S23: 0.1762
REMARK 3 S31: -0.2220 S32: -0.1544 S33: -0.0134
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 121.8904 119.3844 23.9879
REMARK 3 T TENSOR
REMARK 3 T11: 0.3808 T22: 0.2463
REMARK 3 T33: 0.3679 T12: 0.0594
REMARK 3 T13: 0.0012 T23: -0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 3.4861 L22: 1.2280
REMARK 3 L33: 1.2464 L12: -1.2183
REMARK 3 L13: 0.7104 L23: -0.8447
REMARK 3 S TENSOR
REMARK 3 S11: -0.2092 S12: -0.0735 S13: -0.0152
REMARK 3 S21: 0.3158 S22: 0.0905 S23: 0.1015
REMARK 3 S31: -0.3170 S32: 0.0867 S33: 0.1066
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.9890 105.8003 25.3537
REMARK 3 T TENSOR
REMARK 3 T11: 0.4375 T22: 0.2522
REMARK 3 T33: 0.3484 T12: 0.0808
REMARK 3 T13: 0.0782 T23: -0.0511
REMARK 3 L TENSOR
REMARK 3 L11: 2.4842 L22: 2.2218
REMARK 3 L33: 2.3235 L12: -0.2929
REMARK 3 L13: 0.5133 L23: -0.4271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: -0.1090 S13: -0.1241
REMARK 3 S21: 0.2733 S22: -0.0998 S23: 0.1125
REMARK 3 S31: 0.2471 S32: -0.0126 S33: 0.1353
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 134.1935 97.1106 27.5707
REMARK 3 T TENSOR
REMARK 3 T11: 0.5407 T22: 0.3253
REMARK 3 T33: 0.3172 T12: 0.1647
REMARK 3 T13: -0.0926 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.5921 L22: 0.7424
REMARK 3 L33: 1.5703 L12: -0.0135
REMARK 3 L13: 0.2197 L23: 1.1257
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: -0.3650 S13: -0.0062
REMARK 3 S21: 0.5554 S22: 0.2002 S23: 0.0659
REMARK 3 S31: 0.6687 S32: 0.2319 S33: -0.0732
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 127.2470 103.7408 23.3738
REMARK 3 T TENSOR
REMARK 3 T11: 0.4041 T22: 0.2604
REMARK 3 T33: 0.3445 T12: 0.0451
REMARK 3 T13: -0.0163 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.8651 L22: 0.0740
REMARK 3 L33: 0.8929 L12: 0.2076
REMARK 3 L13: 0.0411 L23: 0.3871
REMARK 3 S TENSOR
REMARK 3 S11: -0.1390 S12: -0.1010 S13: -0.2363
REMARK 3 S21: 0.3391 S22: 0.1507 S23: -0.0460
REMARK 3 S31: 0.2746 S32: 0.1790 S33: -0.0575
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.5922 99.2069 16.3288
REMARK 3 T TENSOR
REMARK 3 T11: 0.4641 T22: 0.3139
REMARK 3 T33: 0.3677 T12: -0.0632
REMARK 3 T13: 0.0372 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.6471 L22: 0.8140
REMARK 3 L33: 2.4825 L12: 0.4246
REMARK 3 L13: -1.0978 L23: 1.1513
REMARK 3 S TENSOR
REMARK 3 S11: -0.1958 S12: 0.0182 S13: -0.2637
REMARK 3 S21: 0.2848 S22: -0.0033 S23: 0.0082
REMARK 3 S31: 0.4592 S32: -0.2668 S33: 0.2014
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 167.3494 193.4572 10.5126
REMARK 3 T TENSOR
REMARK 3 T11: 0.2520 T22: 0.4635
REMARK 3 T33: 0.3074 T12: -0.0226
REMARK 3 T13: -0.0135 T23: -0.0764
REMARK 3 L TENSOR
REMARK 3 L11: 1.0309 L22: 2.0896
REMARK 3 L33: 2.3304 L12: 0.4965
REMARK 3 L13: -0.2241 L23: 0.1553
REMARK 3 S TENSOR
REMARK 3 S11: 0.0219 S12: 0.0956 S13: 0.0617
REMARK 3 S21: -0.0926 S22: -0.0684 S23: 0.2049
REMARK 3 S31: -0.1982 S32: -0.5374 S33: 0.0493
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 42 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 165.9199 195.7087 19.8785
REMARK 3 T TENSOR
REMARK 3 T11: 0.3018 T22: 0.6107
REMARK 3 T33: 0.4531 T12: 0.0356
REMARK 3 T13: -0.0118 T23: -0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 1.7448 L22: 0.6210
REMARK 3 L33: 1.4106 L12: 0.3150
REMARK 3 L13: 0.1625 L23: -0.3049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.3993 S13: 0.4933
REMARK 3 S21: 0.1996 S22: -0.2148 S23: 0.1981
REMARK 3 S31: 0.0127 S32: -0.1627 S33: 0.1548
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 110 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 172.7594 181.0944 25.0351
REMARK 3 T TENSOR
REMARK 3 T11: 0.3080 T22: 0.4450
REMARK 3 T33: 0.3540 T12: -0.0468
REMARK 3 T13: 0.0103 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 2.3163 L22: 0.3185
REMARK 3 L33: 1.1745 L12: -0.1454
REMARK 3 L13: 0.8226 L23: 0.6137
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: -0.0038 S13: -0.1618
REMARK 3 S21: 0.1381 S22: -0.0249 S23: 0.1000
REMARK 3 S31: -0.0019 S32: -0.2838 S33: 0.0195
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 197 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 157.6275 179.8361 18.3790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2486 T22: 0.6337
REMARK 3 T33: 0.3947 T12: -0.0572
REMARK 3 T13: 0.0071 T23: -0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 0.8742 L22: 1.2262
REMARK 3 L33: 1.8645 L12: 0.8420
REMARK 3 L13: 0.0409 L23: 0.2617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: -0.1241 S13: -0.1466
REMARK 3 S21: 0.0055 S22: -0.0676 S23: 0.3735
REMARK 3 S31: 0.0479 S32: -0.3044 S33: -0.0449
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 175.7661 197.7315 -4.0962
REMARK 3 T TENSOR
REMARK 3 T11: 0.3110 T22: 0.3787
REMARK 3 T33: 0.3579 T12: -0.0169
REMARK 3 T13: 0.0333 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 1.1199 L22: 1.7214
REMARK 3 L33: 1.6356 L12: -0.7325
REMARK 3 L13: 0.1417 L23: -0.0320
REMARK 3 S TENSOR
REMARK 3 S11: 0.0668 S12: 0.1044 S13: 0.2956
REMARK 3 S21: -0.0534 S22: -0.1265 S23: 0.0485
REMARK 3 S31: -0.2109 S32: -0.0723 S33: 0.0819
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 86 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 182.1412 187.5689 -11.4035
REMARK 3 T TENSOR
REMARK 3 T11: 0.3287 T22: 0.3664
REMARK 3 T33: 0.2835 T12: -0.0178
REMARK 3 T13: -0.0010 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 2.1466 L22: 1.5195
REMARK 3 L33: 0.7288 L12: 0.5581
REMARK 3 L13: 0.3038 L23: 0.4987
REMARK 3 S TENSOR
REMARK 3 S11: 0.1160 S12: 0.0384 S13: -0.2039
REMARK 3 S21: -0.2401 S22: -0.1266 S23: -0.2128
REMARK 3 S31: -0.2102 S32: 0.1068 S33: -0.0368
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 184 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 190.5726 190.7907 -8.6738
REMARK 3 T TENSOR
REMARK 3 T11: 0.3143 T22: 0.4192
REMARK 3 T33: 0.3284 T12: -0.0127
REMARK 3 T13: 0.0133 T23: 0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 1.5480 L22: 1.1357
REMARK 3 L33: 1.5584 L12: 0.0275
REMARK 3 L13: -0.9538 L23: -0.6146
REMARK 3 S TENSOR
REMARK 3 S11: -0.1055 S12: 0.1283 S13: 0.0397
REMARK 3 S21: -0.2652 S22: -0.0536 S23: -0.2468
REMARK 3 S31: -0.0007 S32: 0.2428 S33: 0.1485
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 3 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 127.9528 172.4531 35.8607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.0945
REMARK 3 T33: 0.1032 T12: -0.0170
REMARK 3 T13: 0.0349 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.7658 L22: 1.5112
REMARK 3 L33: 2.4890 L12: -0.4501
REMARK 3 L13: 0.0385 L23: -0.1100
REMARK 3 S TENSOR
REMARK 3 S11: 0.1265 S12: 0.0356 S13: 0.1427
REMARK 3 S21: 0.0168 S22: -0.0809 S23: 0.0112
REMARK 3 S31: -0.1147 S32: 0.2813 S33: 0.0022
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 61 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.0774 176.9225 49.7214
REMARK 3 T TENSOR
REMARK 3 T11: 0.0824 T22: 0.1100
REMARK 3 T33: 0.1503 T12: -0.0641
REMARK 3 T13: -0.0620 T23: -0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 1.3449 L22: 2.3838
REMARK 3 L33: 1.4464 L12: -0.4332
REMARK 3 L13: -0.3024 L23: -0.4152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: -0.4290 S13: 0.0549
REMARK 3 S21: 0.1521 S22: -0.0748 S23: -0.0262
REMARK 3 S31: -0.1133 S32: 0.2338 S33: 0.0346
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 138 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.2888 162.2185 48.7951
REMARK 3 T TENSOR
REMARK 3 T11: 0.1034 T22: 0.0801
REMARK 3 T33: 0.1223 T12: -0.0182
REMARK 3 T13: -0.0161 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.3267 L22: 2.1597
REMARK 3 L33: 1.7828 L12: -0.6957
REMARK 3 L13: 0.7565 L23: -1.8040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0576 S12: -0.0210 S13: 0.1149
REMARK 3 S21: -0.1779 S22: 0.0144 S23: 0.0750
REMARK 3 S31: 0.0450 S32: 0.0669 S33: -0.0674
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 196 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 115.1876 183.6155 43.6614
REMARK 3 T TENSOR
REMARK 3 T11: 0.0983 T22: 0.0884
REMARK 3 T33: 0.1878 T12: -0.0146
REMARK 3 T13: 0.0151 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 0.8127 L22: 1.0043
REMARK 3 L33: 2.9366 L12: 0.2274
REMARK 3 L13: 0.7025 L23: 0.4020
REMARK 3 S TENSOR
REMARK 3 S11: 0.1397 S12: -0.0674 S13: 0.2470
REMARK 3 S21: -0.0209 S22: -0.0935 S23: 0.0780
REMARK 3 S31: -0.0972 S32: -0.2128 S33: 0.0292
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 4 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.6043 83.5882 -13.4403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.3023
REMARK 3 T33: 0.3569 T12: 0.0567
REMARK 3 T13: 0.0470 T23: -0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 2.5153 L22: 1.7532
REMARK 3 L33: 3.1685 L12: 0.2424
REMARK 3 L13: 1.1462 L23: -0.3438
REMARK 3 S TENSOR
REMARK 3 S11: 0.1326 S12: 0.3444 S13: -0.2350
REMARK 3 S21: 0.1234 S22: 0.0966 S23: 0.3595
REMARK 3 S31: 0.1259 S32: -0.0019 S33: -0.1289
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 32 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.9535 78.1669 -19.7106
REMARK 3 T TENSOR
REMARK 3 T11: 0.3229 T22: 0.2735
REMARK 3 T33: 0.3356 T12: 0.0659
REMARK 3 T13: -0.0324 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.6476 L22: 3.7191
REMARK 3 L33: 4.7825 L12: -0.3230
REMARK 3 L13: -0.6804 L23: 1.8086
REMARK 3 S TENSOR
REMARK 3 S11: 0.2425 S12: -0.0979 S13: 0.0794
REMARK 3 S21: -0.1940 S22: 0.1297 S23: 0.1823
REMARK 3 S31: 0.2015 S32: -0.2659 S33: -0.2503
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 52 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.6298 86.7046 -2.5746
REMARK 3 T TENSOR
REMARK 3 T11: 0.4505 T22: 0.3956
REMARK 3 T33: 0.4857 T12: -0.0280
REMARK 3 T13: 0.1594 T23: -0.0894
REMARK 3 L TENSOR
REMARK 3 L11: 1.8643 L22: 1.2480
REMARK 3 L33: 0.9208 L12: 0.6868
REMARK 3 L13: 0.5482 L23: 0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0201 S12: -0.2670 S13: 0.1215
REMARK 3 S21: 0.4496 S22: -0.0659 S23: 0.4805
REMARK 3 S31: -0.2066 S32: -0.4065 S33: 0.0996
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 91 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.7766 72.1111 -0.3201
REMARK 3 T TENSOR
REMARK 3 T11: 0.4105 T22: 0.5251
REMARK 3 T33: 0.3699 T12: -0.0373
REMARK 3 T13: 0.0700 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.8942 L22: 2.0371
REMARK 3 L33: 1.9487 L12: 0.0985
REMARK 3 L13: 0.6192 L23: -0.2166
REMARK 3 S TENSOR
REMARK 3 S11: -0.2329 S12: -0.2187 S13: -0.1677
REMARK 3 S21: 0.2565 S22: -0.2671 S23: 0.0036
REMARK 3 S31: -0.1072 S32: 0.2138 S33: 0.2672
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 138 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 120.9486 84.1421 0.1890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3896 T22: 0.4066
REMARK 3 T33: 0.3242 T12: 0.0042
REMARK 3 T13: 0.0018 T23: -0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 1.1327 L22: 2.1666
REMARK 3 L33: 2.7346 L12: 0.7891
REMARK 3 L13: -0.2385 L23: 0.3582
REMARK 3 S TENSOR
REMARK 3 S11: 0.1198 S12: -0.3294 S13: -0.0188
REMARK 3 S21: 0.3682 S22: -0.0705 S23: 0.1678
REMARK 3 S31: -0.0005 S32: 0.3534 S33: -0.0820
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 169 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 110.3850 82.9886 -1.2312
REMARK 3 T TENSOR
REMARK 3 T11: 0.3393 T22: 0.4160
REMARK 3 T33: 0.3235 T12: -0.0273
REMARK 3 T13: -0.0150 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.2735 L22: 2.6971
REMARK 3 L33: 1.0320 L12: 0.8968
REMARK 3 L13: -0.2957 L23: -0.3228
REMARK 3 S TENSOR
REMARK 3 S11: 0.1114 S12: -0.1662 S13: -0.0925
REMARK 3 S21: 0.3196 S22: 0.1276 S23: -0.1271
REMARK 3 S31: -0.2527 S32: 0.1091 S33: -0.1445
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 206 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 107.3654 66.7793 -9.3510
REMARK 3 T TENSOR
REMARK 3 T11: 0.3669 T22: 0.3814
REMARK 3 T33: 0.4037 T12: 0.0179
REMARK 3 T13: 0.0026 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.3757 L22: 1.8357
REMARK 3 L33: 2.7900 L12: 0.2640
REMARK 3 L13: -1.6288 L23: -0.7727
REMARK 3 S TENSOR
REMARK 3 S11: 0.2001 S12: -0.3291 S13: -0.3401
REMARK 3 S21: 0.2850 S22: -0.0932 S23: 0.0949
REMARK 3 S31: 0.2095 S32: 0.3607 S33: -0.1145
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 4 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 129.9929 122.2332 1.2582
REMARK 3 T TENSOR
REMARK 3 T11: 0.4381 T22: 0.2360
REMARK 3 T33: 0.3373 T12: 0.0254
REMARK 3 T13: -0.0204 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 4.5677 L22: 1.7130
REMARK 3 L33: 4.2757 L12: -0.6556
REMARK 3 L13: 0.8810 L23: -0.6366
REMARK 3 S TENSOR
REMARK 3 S11: -0.1890 S12: 0.1479 S13: 0.8786
REMARK 3 S21: 0.1383 S22: -0.1834 S23: -0.1266
REMARK 3 S31: -0.3337 S32: 0.0891 S33: 0.2291
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 26 THROUGH 120 )
REMARK 3 ORIGIN FOR THE GROUP (A): 133.0814 118.8197 -6.4077
REMARK 3 T TENSOR
REMARK 3 T11: 0.4513 T22: 0.2834
REMARK 3 T33: 0.3165 T12: 0.0044
REMARK 3 T13: 0.0381 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.4364 L22: 1.7767
REMARK 3 L33: 1.9314 L12: -0.4533
REMARK 3 L13: 0.1441 L23: 0.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0245 S12: 0.0783 S13: 0.2537
REMARK 3 S21: -0.1361 S22: -0.0371 S23: -0.0408
REMARK 3 S31: -0.3283 S32: -0.0676 S33: 0.0504
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 121 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 134.4188 102.7199 -14.9475
REMARK 3 T TENSOR
REMARK 3 T11: 0.3706 T22: 0.3266
REMARK 3 T33: 0.3065 T12: 0.0417
REMARK 3 T13: 0.0305 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.6384 L22: 1.8818
REMARK 3 L33: -0.0590 L12: 0.5862
REMARK 3 L13: 0.4768 L23: -0.2160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: 0.2715 S13: -0.2954
REMARK 3 S21: -0.1754 S22: -0.0712 S23: -0.2038
REMARK 3 S31: -0.0517 S32: 0.1283 S33: -0.0459
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 206 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 147.9811 111.0352 -4.6401
REMARK 3 T TENSOR
REMARK 3 T11: 0.3875 T22: 0.3348
REMARK 3 T33: 0.4149 T12: 0.0238
REMARK 3 T13: 0.0095 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 0.8679 L22: 1.1741
REMARK 3 L33: 1.9774 L12: -0.2739
REMARK 3 L13: -0.4262 L23: -0.3509
REMARK 3 S TENSOR
REMARK 3 S11: -0.0813 S12: -0.0792 S13: 0.0052
REMARK 3 S21: -0.2843 S22: -0.0344 S23: -0.5186
REMARK 3 S31: 0.0312 S32: 0.3522 S33: 0.0707
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 4 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.3523 91.8720 -29.6340
REMARK 3 T TENSOR
REMARK 3 T11: 0.3245 T22: 0.3077
REMARK 3 T33: 0.3301 T12: 0.0928
REMARK 3 T13: 0.0042 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.0938 L22: 1.5057
REMARK 3 L33: 2.0283 L12: 0.5241
REMARK 3 L13: -0.2414 L23: 0.0154
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: 0.0870 S13: 0.1944
REMARK 3 S21: -0.0911 S22: -0.0435 S23: 0.1563
REMARK 3 S31: 0.1451 S32: -0.1333 S33: 0.0580
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 86 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.4843 92.7403 -36.9733
REMARK 3 T TENSOR
REMARK 3 T11: 0.3473 T22: 0.3164
REMARK 3 T33: 0.2873 T12: 0.0808
REMARK 3 T13: -0.0133 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.4741 L22: 2.6568
REMARK 3 L33: 0.6665 L12: -0.1534
REMARK 3 L13: 0.1721 L23: 0.2921
REMARK 3 S TENSOR
REMARK 3 S11: -0.0779 S12: 0.1162 S13: 0.1288
REMARK 3 S21: 0.0044 S22: 0.0128 S23: -0.2358
REMARK 3 S31: -0.2009 S32: 0.0172 S33: 0.0332
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 182 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.6485 100.4824 -34.2815
REMARK 3 T TENSOR
REMARK 3 T11: 0.3330 T22: 0.2883
REMARK 3 T33: 0.3309 T12: 0.0221
REMARK 3 T13: -0.0173 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.4599 L22: 1.4830
REMARK 3 L33: 0.8535 L12: -0.0638
REMARK 3 L13: 0.1202 L23: -0.6014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: 0.0366 S13: 0.1620
REMARK 3 S21: -0.1595 S22: -0.0907 S23: -0.1407
REMARK 3 S31: -0.1697 S32: 0.1276 S33: 0.0675
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 6BRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1000231340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-15
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115751
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.393
REMARK 200 RESOLUTION RANGE LOW (A) : 44.158
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17200
REMARK 200 FOR THE DATA SET : 60.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
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) : 0.69900
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M AMINO ACID MIXTURE (GLU, ALA,
REMARK 280 GLY, LYS, AND SER); IMIDAZOLE; 0.1 M MES MONOHYDRATE, PH 6.5, 40%
REMARK 280 GLYCEROL, 20% PEG4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.44133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.22067
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.83100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.61033
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 128.05167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP C -16
REMARK 465 LEU C -15
REMARK 465 MET C -14
REMARK 465 PHE C -13
REMARK 465 THR C -12
REMARK 465 GLU C -11
REMARK 465 MET C -10
REMARK 465 ARG C -9
REMARK 465 ALA C -8
REMARK 465 GLU C -7
REMARK 465 SER C -6
REMARK 465 TRP C -5
REMARK 465 LEU C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 ASP D -16
REMARK 465 LEU D -15
REMARK 465 MET D -14
REMARK 465 PHE D -13
REMARK 465 THR D -12
REMARK 465 GLU D -11
REMARK 465 MET D -10
REMARK 465 ARG D -9
REMARK 465 ALA D -8
REMARK 465 GLU D -7
REMARK 465 SER D -6
REMARK 465 TRP D -5
REMARK 465 LEU D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 ASP E -16
REMARK 465 LEU E -15
REMARK 465 MET E -14
REMARK 465 PHE E -13
REMARK 465 THR E -12
REMARK 465 GLU E -11
REMARK 465 MET E -10
REMARK 465 ARG E -9
REMARK 465 ALA E -8
REMARK 465 GLU E -7
REMARK 465 SER E -6
REMARK 465 TRP E -5
REMARK 465 LEU E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 GLY E 0
REMARK 465 SER E 1
REMARK 465 SER E 2
REMARK 465 ASP F -16
REMARK 465 LEU F -15
REMARK 465 MET F -14
REMARK 465 PHE F -13
REMARK 465 THR F -12
REMARK 465 GLU F -11
REMARK 465 MET F -10
REMARK 465 ARG F -9
REMARK 465 ALA F -8
REMARK 465 GLU F -7
REMARK 465 SER F -6
REMARK 465 TRP F -5
REMARK 465 LEU F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 GLY F 0
REMARK 465 SER F 1
REMARK 465 SER F 2
REMARK 465 GLY F 3
REMARK 465 ASP G -16
REMARK 465 LEU G -15
REMARK 465 MET G -14
REMARK 465 PHE G -13
REMARK 465 THR G -12
REMARK 465 GLU G -11
REMARK 465 MET G -10
REMARK 465 ARG G -9
REMARK 465 ALA G -8
REMARK 465 GLU G -7
REMARK 465 SER G -6
REMARK 465 TRP G -5
REMARK 465 LEU G -4
REMARK 465 ARG G -3
REMARK 465 GLY G -2
REMARK 465 SER G -1
REMARK 465 GLY G 0
REMARK 465 SER G 1
REMARK 465 SER G 2
REMARK 465 GLY G 3
REMARK 465 ASP H -16
REMARK 465 LEU H -15
REMARK 465 MET H -14
REMARK 465 PHE H -13
REMARK 465 THR H -12
REMARK 465 GLU H -11
REMARK 465 MET H -10
REMARK 465 ARG H -9
REMARK 465 ALA H -8
REMARK 465 GLU H -7
REMARK 465 SER H -6
REMARK 465 TRP H -5
REMARK 465 LEU H -4
REMARK 465 ARG H -3
REMARK 465 GLY H -2
REMARK 465 SER H -1
REMARK 465 GLY H 0
REMARK 465 SER H 1
REMARK 465 SER H 2
REMARK 465 GLY H 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 ARG C 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 230 CG CD CE NZ
REMARK 470 ARG D 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 230 CG CD CE NZ
REMARK 470 ARG E 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 230 CG CD CE NZ
REMARK 470 ARG F 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 230 CG CD CE NZ
REMARK 470 ARG G 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 230 CG CD CE NZ
REMARK 470 ARG H 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 230 CG CD CE NZ
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 OD2 ASP E 185 NH1 ARG E 263 5565 2.10
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 -3 N - CA - C ANGL. DEV. = -23.3 DEGREES
REMARK 500 SER A 1 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASN A 151 N - CA - C ANGL. DEV. = -19.9 DEGREES
REMARK 500 LEU B -15 N - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 SER C 130 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASN C 151 CB - CA - C ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASN C 151 N - CA - C ANGL. DEV. = -29.0 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 1 -137.60 49.14
REMARK 500 TYR A 69 38.83 -95.40
REMARK 500 SER A 97 -125.30 56.37
REMARK 500 LYS A 116 149.03 -170.02
REMARK 500 ASN A 151 116.11 -167.46
REMARK 500 LEU A 248 68.47 -119.20
REMARK 500 TYR B 69 45.52 -93.70
REMARK 500 SER B 97 -125.96 60.53
REMARK 500 ARG B 125 131.28 -172.98
REMARK 500 ASP B 131 40.41 -109.26
REMARK 500 ASN B 151 85.67 -157.51
REMARK 500 ARG B 217 51.60 -140.85
REMARK 500 LEU B 248 69.14 -119.27
REMARK 500 ALA B 253 49.98 -144.28
REMARK 500 TYR C 69 41.48 -95.84
REMARK 500 SER C 97 -128.40 58.24
REMARK 500 ARG C 125 127.29 -174.77
REMARK 500 ASP C 167 105.31 -59.85
REMARK 500 ALA C 253 48.28 -153.32
REMARK 500 VAL D 54 -15.54 -45.31
REMARK 500 ASN D 60 107.79 -58.89
REMARK 500 PHE D 64 87.88 -67.47
REMARK 500 TYR D 69 51.09 -104.41
REMARK 500 SER D 97 -118.94 46.49
REMARK 500 TYR D 132 114.19 -161.39
REMARK 500 ASN D 151 87.67 -155.78
REMARK 500 LEU D 248 64.52 -119.98
REMARK 500 TYR E 69 39.93 -86.81
REMARK 500 SER E 97 -122.41 60.96
REMARK 500 LEU E 248 71.03 -119.30
REMARK 500 TYR F 69 42.19 -91.85
REMARK 500 ARG F 87 34.06 70.53
REMARK 500 SER F 97 -122.07 53.89
REMARK 500 ARG F 125 114.78 -161.11
REMARK 500 ASN F 151 87.91 -156.03
REMARK 500 LEU F 248 75.33 -117.28
REMARK 500 ALA F 253 57.06 -144.80
REMARK 500 ASN G 60 105.12 -59.33
REMARK 500 TYR G 69 44.74 -109.16
REMARK 500 SER G 97 -120.78 45.00
REMARK 500 LEU G 248 69.38 -108.42
REMARK 500 ASN H 60 105.99 -56.63
REMARK 500 TYR H 69 45.23 -106.82
REMARK 500 SER H 97 -116.92 48.67
REMARK 500 ASP H 131 54.83 -141.20
REMARK 500 ASN H 151 89.70 -164.97
REMARK 500 ARG H 217 85.84 -154.03
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 355 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH C 340 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH D 372 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH D 373 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH D 374 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH D 375 DISTANCE = 9.19 ANGSTROMS
REMARK 525 HOH D 376 DISTANCE = 9.68 ANGSTROMS
REMARK 525 HOH E 409 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH F 343 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH F 344 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH G 366 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH G 367 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH G 368 DISTANCE = 7.45 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H3M A 401
DBREF1 6BRT A 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT A A0A0D9Z3L0 22 284
DBREF1 6BRT B 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT B A0A0D9Z3L0 22 284
DBREF1 6BRT C 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT C A0A0D9Z3L0 22 284
DBREF1 6BRT D 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT D A0A0D9Z3L0 22 284
DBREF1 6BRT E 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT E A0A0D9Z3L0 22 284
DBREF1 6BRT F 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT F A0A0D9Z3L0 22 284
DBREF1 6BRT G 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT G A0A0D9Z3L0 22 284
DBREF1 6BRT H 6 268 UNP A0A0D9Z3L0_9ORYZ
DBREF2 6BRT H A0A0D9Z3L0 22 284
SEQADV 6BRT ASP A -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU A -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET A -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE A -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR A -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU A -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET A -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG A -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA A -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU A -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER A -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP A -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU A -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG A -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY A -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER A -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY A 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER A 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER A 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY A 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA A 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER A 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP B -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU B -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET B -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE B -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR B -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU B -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET B -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG B -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA B -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU B -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER B -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP B -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU B -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG B -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY B -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER B -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY B 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER B 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER B 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY B 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA B 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER B 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP C -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU C -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET C -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE C -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR C -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU C -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET C -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG C -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA C -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU C -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER C -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP C -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU C -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG C -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY C -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER C -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY C 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER C 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER C 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY C 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA C 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER C 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP D -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU D -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET D -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE D -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR D -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU D -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET D -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG D -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA D -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU D -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER D -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP D -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU D -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG D -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY D -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER D -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY D 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER D 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER D 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY D 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA D 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER D 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP E -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU E -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET E -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE E -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR E -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU E -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET E -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG E -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA E -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU E -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER E -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP E -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU E -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG E -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY E -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER E -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY E 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER E 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER E 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY E 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA E 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER E 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP F -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU F -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET F -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE F -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR F -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU F -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET F -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG F -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA F -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU F -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER F -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP F -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU F -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG F -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY F -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER F -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY F 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER F 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER F 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY F 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA F 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER F 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP G -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU G -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET G -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE G -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR G -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU G -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET G -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG G -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA G -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU G -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER G -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP G -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU G -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG G -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY G -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER G -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY G 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER G 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER G 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY G 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA G 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER G 5 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ASP H -16 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU H -15 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET H -14 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT PHE H -13 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT THR H -12 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU H -11 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT MET H -10 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG H -9 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ALA H -8 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLU H -7 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER H -6 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT TRP H -5 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT LEU H -4 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT ARG H -3 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY H -2 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT SER H -1 UNP A0A0D9Z3L EXPRESSION TAG
SEQADV 6BRT GLY H 0 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER H 1 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER H 2 UNP A0A0D9Z3L LINKER
SEQADV 6BRT GLY H 3 UNP A0A0D9Z3L LINKER
SEQADV 6BRT ALA H 4 UNP A0A0D9Z3L LINKER
SEQADV 6BRT SER H 5 UNP A0A0D9Z3L LINKER
SEQRES 1 A 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 A 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 A 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 A 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 A 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 A 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 A 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 A 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 A 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 A 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 A 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 A 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 A 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 A 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 A 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 A 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 A 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 A 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 A 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 A 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 A 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 A 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 B 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 B 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 B 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 B 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 B 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 B 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 B 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 B 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 B 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 B 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 B 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 B 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 B 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 B 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 B 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 B 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 B 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 B 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 B 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 B 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 B 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 B 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 C 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 C 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 C 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 C 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 C 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 C 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 C 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 C 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 C 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 C 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 C 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 C 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 C 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 C 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 C 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 C 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 C 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 C 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 C 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 C 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 C 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 C 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 D 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 D 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 D 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 D 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 D 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 D 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 D 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 D 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 D 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 D 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 D 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 D 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 D 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 D 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 D 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 D 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 D 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 D 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 D 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 D 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 D 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 D 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 E 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 E 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 E 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 E 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 E 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 E 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 E 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 E 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 E 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 E 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 E 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 E 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 E 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 E 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 E 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 E 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 E 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 E 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 E 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 E 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 E 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 E 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 F 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 F 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 F 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 F 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 F 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 F 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 F 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 F 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 F 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 F 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 F 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 F 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 F 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 F 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 F 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 F 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 F 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 F 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 F 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 F 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 F 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 F 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 G 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 G 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 G 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 G 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 G 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 G 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 G 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 G 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 G 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 G 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 G 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 G 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 G 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 G 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 G 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 G 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 G 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 G 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 G 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 G 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 G 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 G 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 H 285 ASP LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU
SEQRES 2 H 285 ARG GLY SER GLY SER SER GLY ALA SER LEU LEU GLN ILE
SEQRES 3 H 285 LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL
SEQRES 4 H 285 VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP
SEQRES 5 H 285 SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL
SEQRES 6 H 285 VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO
SEQRES 7 H 285 ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA
SEQRES 8 H 285 TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG
SEQRES 9 H 285 ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA
SEQRES 10 H 285 MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU
SEQRES 11 H 285 PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE
SEQRES 12 H 285 LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU
SEQRES 13 H 285 GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR
SEQRES 14 H 285 SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY
SEQRES 15 H 285 ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 H 285 LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS
SEQRES 17 H 285 GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY
SEQRES 18 H 285 MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG
SEQRES 19 H 285 ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS
SEQRES 20 H 285 ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN
SEQRES 21 H 285 THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU
SEQRES 22 H 285 LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
HET H3M A 401 8
HETNAM H3M (5R)-5-HYDROXY-3-METHYLFURAN-2(5H)-ONE
FORMUL 9 H3M C5 H6 O3
FORMUL 10 HOH *548(H2 O)
HELIX 1 AA1 ASP A -16 ARG A -3 1 14
HELIX 2 AA2 SER A 2 LEU A 10 1 9
HELIX 3 AA3 ASP A 31 SER A 36 5 6
HELIX 4 AA4 VAL A 38 LEU A 42 5 5
HELIX 5 AA5 ASN A 60 PHE A 64 5 5
HELIX 6 AA6 ASN A 71 ARG A 87 1 17
HELIX 7 AA7 SER A 97 ARG A 110 1 14
HELIX 8 AA8 GLU A 137 ASN A 151 1 15
HELIX 9 AA9 ASN A 151 GLY A 165 1 15
HELIX 10 AB1 VAL A 168 MET A 182 1 15
HELIX 11 AB2 ARG A 183 THR A 197 1 15
HELIX 12 AB3 LEU A 199 VAL A 206 5 8
HELIX 13 AB4 PRO A 222 LEU A 233 1 12
HELIX 14 AB5 LEU A 248 ALA A 253 1 6
HELIX 15 AB6 ALA A 253 LEU A 265 1 13
HELIX 16 AB7 PHE B -13 LEU B -4 1 10
HELIX 17 AB8 SER B 1 LEU B 10 1 10
HELIX 18 AB9 ASP B 31 SER B 36 5 6
HELIX 19 AC1 VAL B 38 LEU B 42 5 5
HELIX 20 AC2 ASN B 60 PHE B 64 5 5
HELIX 21 AC3 ASN B 71 LEU B 86 1 16
HELIX 22 AC4 SER B 97 ARG B 110 1 14
HELIX 23 AC5 GLU B 137 ASN B 151 1 15
HELIX 24 AC6 ASN B 151 GLY B 165 1 15
HELIX 25 AC7 VAL B 168 MET B 182 1 15
HELIX 26 AC8 ARG B 183 THR B 197 1 15
HELIX 27 AC9 LEU B 199 VAL B 206 5 8
HELIX 28 AD1 PRO B 222 LEU B 233 1 12
HELIX 29 AD2 LEU B 248 ALA B 253 1 6
HELIX 30 AD3 ALA B 253 LEU B 265 1 13
HELIX 31 AD4 SER C 5 LEU C 10 1 6
HELIX 32 AD5 ASP C 31 SER C 36 5 6
HELIX 33 AD6 VAL C 38 LEU C 42 5 5
HELIX 34 AD7 ASN C 60 PHE C 64 5 5
HELIX 35 AD8 ARG C 67 ASN C 71 5 5
HELIX 36 AD9 LEU C 72 LEU C 86 1 15
HELIX 37 AE1 SER C 97 ARG C 110 1 14
HELIX 38 AE2 GLU C 137 ASN C 151 1 15
HELIX 39 AE3 TYR C 152 GLY C 165 1 14
HELIX 40 AE4 VAL C 168 ASN C 181 1 14
HELIX 41 AE5 ARG C 183 THR C 197 1 15
HELIX 42 AE6 LEU C 199 VAL C 206 5 8
HELIX 43 AE7 PRO C 222 LEU C 233 1 12
HELIX 44 AE8 LEU C 248 ALA C 253 1 6
HELIX 45 AE9 ALA C 253 LEU C 265 1 13
HELIX 46 AF1 SER D 5 LEU D 10 1 6
HELIX 47 AF2 ASP D 31 SER D 36 5 6
HELIX 48 AF3 VAL D 38 LEU D 42 5 5
HELIX 49 AF4 ASN D 60 PHE D 64 5 5
HELIX 50 AF5 LEU D 72 LEU D 86 1 15
HELIX 51 AF6 SER D 97 ARG D 110 1 14
HELIX 52 AF7 GLU D 137 ASN D 151 1 15
HELIX 53 AF8 ASN D 151 GLY D 165 1 15
HELIX 54 AF9 VAL D 168 ASN D 181 1 14
HELIX 55 AG1 ARG D 183 THR D 197 1 15
HELIX 56 AG2 LEU D 199 VAL D 206 5 8
HELIX 57 AG3 PRO D 222 LEU D 233 1 12
HELIX 58 AG4 LEU D 248 ALA D 253 1 6
HELIX 59 AG5 ALA D 253 LEU D 265 1 13
HELIX 60 AG6 ALA E 4 LEU E 10 1 7
HELIX 61 AG7 ASP E 31 SER E 36 5 6
HELIX 62 AG8 VAL E 38 LEU E 42 5 5
HELIX 63 AG9 ASN E 60 PHE E 64 5 5
HELIX 64 AH1 ARG E 67 ASN E 71 5 5
HELIX 65 AH2 LEU E 72 ARG E 87 1 16
HELIX 66 AH3 SER E 97 ARG E 110 1 14
HELIX 67 AH4 GLU E 137 ASN E 151 1 15
HELIX 68 AH5 ASN E 151 GLY E 165 1 15
HELIX 69 AH6 VAL E 168 MET E 182 1 15
HELIX 70 AH7 ARG E 183 LYS E 196 1 14
HELIX 71 AH8 VAL E 202 VAL E 206 5 5
HELIX 72 AH9 PRO E 222 LEU E 233 1 12
HELIX 73 AI1 LEU E 248 ALA E 253 1 6
HELIX 74 AI2 ALA E 253 LEU E 265 1 13
HELIX 75 AI3 SER F 5 LEU F 10 1 6
HELIX 76 AI4 ASP F 31 SER F 36 5 6
HELIX 77 AI5 VAL F 38 LEU F 42 5 5
HELIX 78 AI6 ARG F 67 ASN F 71 5 5
HELIX 79 AI7 LEU F 72 LEU F 86 1 15
HELIX 80 AI8 SER F 97 ARG F 110 1 14
HELIX 81 AI9 GLU F 137 ASN F 151 1 15
HELIX 82 AJ1 ASN F 151 GLY F 165 1 15
HELIX 83 AJ2 VAL F 168 ASN F 181 1 14
HELIX 84 AJ3 ARG F 183 THR F 197 1 15
HELIX 85 AJ4 LEU F 199 VAL F 206 5 8
HELIX 86 AJ5 PRO F 222 LEU F 233 1 12
HELIX 87 AJ6 LEU F 248 ALA F 253 1 6
HELIX 88 AJ7 ALA F 253 LEU F 265 1 13
HELIX 89 AJ8 SER G 5 LEU G 10 1 6
HELIX 90 AJ9 ASP G 31 SER G 36 5 6
HELIX 91 AK1 VAL G 38 LEU G 42 5 5
HELIX 92 AK2 ASN G 60 PHE G 64 5 5
HELIX 93 AK3 LEU G 72 LEU G 86 1 15
HELIX 94 AK4 SER G 97 ARG G 110 1 14
HELIX 95 AK5 GLU G 137 ASN G 151 1 15
HELIX 96 AK6 ASN G 151 GLY G 165 1 15
HELIX 97 AK7 VAL G 168 ASN G 181 1 14
HELIX 98 AK8 ARG G 183 LYS G 196 1 14
HELIX 99 AK9 LEU G 199 VAL G 206 5 8
HELIX 100 AL1 PRO G 222 LEU G 233 1 12
HELIX 101 AL2 LEU G 248 ALA G 253 1 6
HELIX 102 AL3 ALA G 253 LEU G 265 1 13
HELIX 103 AL4 SER H 5 LEU H 10 1 6
HELIX 104 AL5 ASP H 31 SER H 36 5 6
HELIX 105 AL6 LEU H 39 ARG H 44 1 6
HELIX 106 AL7 ASN H 60 PHE H 64 5 5
HELIX 107 AL8 LEU H 72 LEU H 86 1 15
HELIX 108 AL9 SER H 97 ARG H 110 1 14
HELIX 109 AM1 GLU H 137 ASN H 151 1 15
HELIX 110 AM2 ASN H 151 GLY H 165 1 15
HELIX 111 AM3 VAL H 168 MET H 182 1 15
HELIX 112 AM4 ARG H 183 THR H 197 1 15
HELIX 113 AM5 LEU H 199 VAL H 206 5 8
HELIX 114 AM6 PRO H 222 LEU H 233 1 12
HELIX 115 AM7 LEU H 248 ALA H 253 1 6
HELIX 116 AM8 ALA H 253 LEU H 265 1 13
SHEET 1 AA1 7 ARG A 13 GLY A 16 0
SHEET 2 AA1 7 ARG A 47 LEU A 50 -1 O VAL A 48 N VAL A 15
SHEET 3 AA1 7 VAL A 21 SER A 25 1 N VAL A 22 O VAL A 49
SHEET 4 AA1 7 CYS A 91 HIS A 96 1 O VAL A 94 N VAL A 23
SHEET 5 AA1 7 PHE A 114 ILE A 120 1 O ALA A 115 N CYS A 91
SHEET 6 AA1 7 CYS A 210 GLN A 214 1 O VAL A 213 N LEU A 119
SHEET 7 AA1 7 THR A 237 PHE A 241 1 O THR A 238 N VAL A 212
SHEET 1 AA2 7 ARG B 13 VAL B 15 0
SHEET 2 AA2 7 ARG B 47 LEU B 50 -1 O VAL B 48 N VAL B 15
SHEET 3 AA2 7 VAL B 21 SER B 25 1 N VAL B 22 O VAL B 49
SHEET 4 AA2 7 CYS B 91 HIS B 96 1 O ALA B 92 N VAL B 21
SHEET 5 AA2 7 PHE B 114 ILE B 120 1 O ALA B 115 N CYS B 91
SHEET 6 AA2 7 CYS B 210 THR B 215 1 O VAL B 213 N LEU B 119
SHEET 7 AA2 7 THR B 237 LEU B 242 1 O LEU B 242 N GLN B 214
SHEET 1 AA3 7 ARG C 13 VAL C 15 0
SHEET 2 AA3 7 ARG C 47 LEU C 50 -1 O VAL C 48 N VAL C 15
SHEET 3 AA3 7 VAL C 21 SER C 25 1 N VAL C 22 O VAL C 49
SHEET 4 AA3 7 CYS C 91 HIS C 96 1 O ALA C 92 N VAL C 23
SHEET 5 AA3 7 PHE C 114 ILE C 120 1 O ALA C 115 N CYS C 91
SHEET 6 AA3 7 CYS C 210 THR C 216 1 O VAL C 213 N LEU C 119
SHEET 7 AA3 7 THR C 237 GLU C 245 1 O THR C 238 N VAL C 212
SHEET 1 AA4 7 ARG D 13 VAL D 15 0
SHEET 2 AA4 7 ARG D 47 LEU D 50 -1 O VAL D 48 N VAL D 15
SHEET 3 AA4 7 VAL D 21 SER D 25 1 N LEU D 24 O VAL D 49
SHEET 4 AA4 7 CYS D 91 HIS D 96 1 O ALA D 92 N VAL D 21
SHEET 5 AA4 7 PHE D 114 ILE D 120 1 O ILE D 120 N GLY D 95
SHEET 6 AA4 7 CYS D 210 GLN D 214 1 O VAL D 213 N LEU D 119
SHEET 7 AA4 7 THR D 237 PHE D 241 1 O THR D 238 N VAL D 212
SHEET 1 AA5 7 ARG E 13 GLY E 16 0
SHEET 2 AA5 7 ARG E 47 LEU E 50 -1 O VAL E 48 N VAL E 15
SHEET 3 AA5 7 VAL E 21 SER E 25 1 N VAL E 22 O VAL E 49
SHEET 4 AA5 7 CYS E 91 HIS E 96 1 O ALA E 92 N VAL E 23
SHEET 5 AA5 7 PHE E 114 ILE E 120 1 O VAL E 118 N GLY E 95
SHEET 6 AA5 7 CYS E 210 GLN E 214 1 O VAL E 213 N LEU E 119
SHEET 7 AA5 7 THR E 237 PHE E 241 1 O GLU E 240 N VAL E 212
SHEET 1 AA6 7 ARG F 13 GLY F 16 0
SHEET 2 AA6 7 ARG F 47 LEU F 50 -1 O VAL F 48 N VAL F 15
SHEET 3 AA6 7 VAL F 21 SER F 25 1 N VAL F 22 O VAL F 49
SHEET 4 AA6 7 CYS F 91 HIS F 96 1 O ALA F 92 N VAL F 21
SHEET 5 AA6 7 PHE F 114 ILE F 120 1 O LYS F 116 N PHE F 93
SHEET 6 AA6 7 CYS F 210 GLN F 214 1 O VAL F 213 N LEU F 119
SHEET 7 AA6 7 THR F 237 PHE F 241 1 O GLU F 240 N GLN F 214
SHEET 1 AA7 7 ARG G 13 VAL G 15 0
SHEET 2 AA7 7 ARG G 47 LEU G 50 -1 O VAL G 48 N VAL G 15
SHEET 3 AA7 7 VAL G 21 SER G 25 1 N VAL G 22 O VAL G 49
SHEET 4 AA7 7 CYS G 91 HIS G 96 1 O ALA G 92 N VAL G 21
SHEET 5 AA7 7 PHE G 114 ILE G 120 1 O ILE G 120 N GLY G 95
SHEET 6 AA7 7 CYS G 210 GLN G 214 1 O VAL G 213 N LEU G 119
SHEET 7 AA7 7 THR G 237 PHE G 241 1 O THR G 238 N VAL G 212
SHEET 1 AA8 7 ARG H 13 VAL H 15 0
SHEET 2 AA8 7 ARG H 47 LEU H 50 -1 O VAL H 48 N VAL H 15
SHEET 3 AA8 7 VAL H 21 SER H 25 1 N LEU H 24 O VAL H 49
SHEET 4 AA8 7 CYS H 91 HIS H 96 1 O ALA H 92 N VAL H 23
SHEET 5 AA8 7 PHE H 114 ILE H 120 1 O ILE H 120 N GLY H 95
SHEET 6 AA8 7 CYS H 210 GLN H 214 1 O VAL H 211 N LEU H 117
SHEET 7 AA8 7 THR H 237 PHE H 241 1 O THR H 238 N VAL H 212
SITE 1 AC1 4 PHE A 28 TYR A 159 CYS A 191 PHE A 195
CRYST1 183.843 183.843 153.662 90.00 90.00 120.00 P 65 48
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 0.005439 0.003140 0.000000 0.00000
SCALE2 0.000000 0.006281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006508 0.00000
TER 2191 TYR A 268
TER 4382 TYR B 268
TER 6420 TYR C 268
TER 8458 TYR D 268
TER 10500 TYR E 268
TER 12538 TYR F 268
TER 14576 TYR G 268
TER 16614 TYR H 268
MASTER 1087 0 1 116 56 0 1 617162 8 8 176
END |