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HEADER HYDROLASE 20-JUL-20 6ZTH
TITLE PHOSPHOLIPASE PLAB FROM LEGIONELLA PNEUMOPHILA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLAB PHOSPHOLIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA;
SOURCE 3 ORGANISM_TAXID: 446;
SOURCE 4 GENE: PLAB, NCTC12000_01733;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOLIPASE, ALPHA/BETA HYDROLASE, VIRULENCE, INFECTIOUS DISEASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.DIWO,A.FLIEGER,W.BLANKENFELDT
REVDAT 1 02-JUN-21 6ZTH 0
JRNL AUTH M.DIWO,W.MICHEL,P.AURASS,K.KUHLE-KEINDORF,J.PIPPEL,
JRNL AUTH 2 J.KRAUSZE,S.WAMP,C.LANG,W.BLANKENFELDT,A.FLIEGER
JRNL TITL NAD(H)-MEDIATED TETRAMERIZATION CONTROLS THE ACTIVITY OF
JRNL TITL 2 LEGIONELLA PNEUMOPHILA PHOSPHOLIPASE PLAB
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.DIWO,W.MICHEL,P.AURASS,K.KUHLE-KEINDORF,J.PIPPEL,
REMARK 1 AUTH 2 J.KRAUSZE,C.LANG,W.BLANKENFELDT,A.FLIEGER
REMARK 1 TITL NAD(H)-MEDIATED TETRAMERIZATION CONTROLS THE ACTIVITY OF
REMARK 1 TITL 2 LEGIONELLA PNEUMOPHILA PHOSPHOLIPASE PLAB
REMARK 1 REF BIORXIV 2020
REMARK 1 REFN
REMARK 1 DOI 10.1101/2020.09.01.246603
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_3922
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) : 49.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 104627
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.366
REMARK 3 R VALUE (WORKING SET) : 0.364
REMARK 3 FREE R VALUE : 0.413
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5247
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 49.2400 - 7.1400 0.98 3337 177 0.4016 0.4210
REMARK 3 2 7.1400 - 5.6700 1.00 3335 175 0.3900 0.3637
REMARK 3 3 5.6700 - 4.9500 1.00 3319 175 0.3546 0.3833
REMARK 3 4 4.9500 - 4.5000 1.00 3320 174 0.3466 0.4029
REMARK 3 5 4.5000 - 4.1800 1.00 3359 177 0.3305 0.4122
REMARK 3 6 4.1800 - 3.9300 1.00 3325 175 0.3377 0.3824
REMARK 3 7 3.9300 - 3.7400 1.00 3280 172 0.3471 0.3676
REMARK 3 8 3.7400 - 3.5700 1.00 3331 177 0.3439 0.4015
REMARK 3 9 3.5700 - 3.4400 1.00 3308 173 0.3472 0.3969
REMARK 3 10 3.4400 - 3.3200 1.00 3324 175 0.3585 0.4069
REMARK 3 11 3.3200 - 3.2100 1.00 3333 175 0.3570 0.4423
REMARK 3 12 3.2100 - 3.1200 1.00 3290 174 0.3624 0.4078
REMARK 3 13 3.1200 - 3.0400 1.00 3322 174 0.3627 0.4271
REMARK 3 14 3.0400 - 2.9700 1.00 3346 176 0.3783 0.4288
REMARK 3 15 2.9700 - 2.9000 1.00 3302 174 0.3688 0.4514
REMARK 3 16 2.9000 - 2.8400 0.99 3287 172 0.3714 0.4728
REMARK 3 17 2.8400 - 2.7800 1.00 3311 176 0.3685 0.4294
REMARK 3 18 2.7800 - 2.7300 1.00 3302 173 0.3907 0.5117
REMARK 3 19 2.7300 - 2.6800 1.00 3296 174 0.3748 0.4236
REMARK 3 20 2.6800 - 2.6300 1.00 3326 175 0.3760 0.4462
REMARK 3 21 2.6300 - 2.5900 1.00 3308 173 0.3835 0.4377
REMARK 3 22 2.5900 - 2.5500 1.00 3329 177 0.3759 0.4072
REMARK 3 23 2.5500 - 2.5100 1.00 3290 173 0.3698 0.4724
REMARK 3 24 2.5100 - 2.4800 1.00 3335 170 0.3787 0.4149
REMARK 3 25 2.4800 - 2.4400 1.00 3281 166 0.3817 0.4139
REMARK 3 26 2.4400 - 2.4100 1.00 3337 186 0.3776 0.3694
REMARK 3 27 2.4100 - 2.3800 1.00 3280 177 0.3824 0.4382
REMARK 3 28 2.3800 - 2.3500 1.00 3308 182 0.3819 0.3837
REMARK 3 29 2.3500 - 2.3300 1.00 3290 187 0.3837 0.4302
REMARK 3 30 2.3300 - 2.3000 1.00 3269 163 0.3851 0.4089
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 46.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.26
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 335 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1292 -9.8213 -14.8392
REMARK 3 T TENSOR
REMARK 3 T11: 0.5424 T22: 0.5112
REMARK 3 T33: 0.3257 T12: 0.2414
REMARK 3 T13: -0.0564 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.5883 L22: 0.7370
REMARK 3 L33: 2.2642 L12: 0.3378
REMARK 3 L13: 0.1205 L23: -0.2868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: 0.4011 S13: -0.1686
REMARK 3 S21: -0.0780 S22: -0.1438 S23: -0.2315
REMARK 3 S31: 0.1532 S32: 0.5511 S33: 0.0931
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 390 THROUGH 423 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7269 0.9709 -16.8102
REMARK 3 T TENSOR
REMARK 3 T11: 0.2115 T22: 0.4364
REMARK 3 T33: 0.4243 T12: 0.0519
REMARK 3 T13: -0.0734 T23: -0.0965
REMARK 3 L TENSOR
REMARK 3 L11: 0.1778 L22: 0.6569
REMARK 3 L33: 3.9450 L12: -0.2262
REMARK 3 L13: -0.2742 L23: -0.6863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: -0.0956 S13: 0.0767
REMARK 3 S21: -0.0461 S22: 0.0530 S23: -0.1572
REMARK 3 S31: -0.0812 S32: 0.2663 S33: 0.0741
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 424 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.3039 2.4767 -28.5478
REMARK 3 T TENSOR
REMARK 3 T11: 0.3748 T22: 0.4873
REMARK 3 T33: 0.3850 T12: 0.2217
REMARK 3 T13: 0.0335 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 0.2092 L22: 0.6646
REMARK 3 L33: 2.2750 L12: 0.2406
REMARK 3 L13: -0.4666 L23: -0.7044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0815 S12: 0.0574 S13: -0.0484
REMARK 3 S21: -0.0290 S22: -0.0814 S23: 0.2171
REMARK 3 S31: -0.0771 S32: -0.1023 S33: -0.0669
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -2 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8549 -47.0127 -52.2784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3744 T22: 0.3844
REMARK 3 T33: 0.4758 T12: 0.2173
REMARK 3 T13: -0.0893 T23: -0.1438
REMARK 3 L TENSOR
REMARK 3 L11: 0.7856 L22: 1.0477
REMARK 3 L33: 0.8421 L12: -0.4816
REMARK 3 L13: -0.4920 L23: 0.3168
REMARK 3 S TENSOR
REMARK 3 S11: 0.0872 S12: 0.1434 S13: -0.0073
REMARK 3 S21: -0.2414 S22: -0.0946 S23: -0.1241
REMARK 3 S31: -0.0639 S32: -0.0282 S33: 0.0383
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9039 -32.1616 -54.9633
REMARK 3 T TENSOR
REMARK 3 T11: 0.2862 T22: 0.3782
REMARK 3 T33: 0.2921 T12: 0.2195
REMARK 3 T13: 0.0015 T23: -0.1658
REMARK 3 L TENSOR
REMARK 3 L11: 0.5676 L22: 0.7214
REMARK 3 L33: 0.4412 L12: -0.0891
REMARK 3 L13: 0.1145 L23: 0.2327
REMARK 3 S TENSOR
REMARK 3 S11: 0.1076 S12: -0.0162 S13: -0.0197
REMARK 3 S21: -0.1249 S22: -0.0652 S23: 0.0252
REMARK 3 S31: 0.1888 S32: 0.0505 S33: 0.0594
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6429 -24.6911 -65.8591
REMARK 3 T TENSOR
REMARK 3 T11: 0.2410 T22: 0.4675
REMARK 3 T33: 0.2827 T12: 0.2402
REMARK 3 T13: 0.0502 T23: -0.0977
REMARK 3 L TENSOR
REMARK 3 L11: 0.2929 L22: 0.4771
REMARK 3 L33: 0.1010 L12: -0.1906
REMARK 3 L13: 0.0920 L23: 0.1751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: 0.3897 S13: -0.1264
REMARK 3 S21: -0.1450 S22: 0.0905 S23: -0.0671
REMARK 3 S31: 0.0654 S32: 0.0994 S33: 0.0130
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 363 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6028 -2.0987 -53.1113
REMARK 3 T TENSOR
REMARK 3 T11: 0.2058 T22: 0.2962
REMARK 3 T33: 0.3044 T12: 0.1554
REMARK 3 T13: 0.0198 T23: -0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 0.3557 L22: 1.3012
REMARK 3 L33: 1.8879 L12: 0.0418
REMARK 3 L13: 0.3669 L23: 0.9910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0757 S12: 0.0158 S13: 0.0821
REMARK 3 S21: -0.2223 S22: -0.0894 S23: 0.0133
REMARK 3 S31: -0.4917 S32: 0.2506 S33: -0.0366
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7845 9.9209 -22.3798
REMARK 3 T TENSOR
REMARK 3 T11: 0.5719 T22: 0.4402
REMARK 3 T33: 0.2923 T12: 0.2617
REMARK 3 T13: -0.0262 T23: -0.1895
REMARK 3 L TENSOR
REMARK 3 L11: 0.7669 L22: 0.0502
REMARK 3 L33: 0.4103 L12: 0.1475
REMARK 3 L13: 0.2060 L23: -0.0639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: 0.1379 S13: 0.2702
REMARK 3 S21: -0.0570 S22: -0.0545 S23: 0.1097
REMARK 3 S31: -0.2405 S32: 0.0341 S33: -0.4289
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 122 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1042 -8.0780 -17.9537
REMARK 3 T TENSOR
REMARK 3 T11: 0.3166 T22: 0.3746
REMARK 3 T33: 0.3181 T12: 0.1268
REMARK 3 T13: 0.0093 T23: -0.2168
REMARK 3 L TENSOR
REMARK 3 L11: 0.7162 L22: 0.5322
REMARK 3 L33: 0.8602 L12: 0.4512
REMARK 3 L13: -0.4498 L23: -0.0194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0577 S12: 0.1848 S13: 0.0765
REMARK 3 S21: 0.1857 S22: 0.0015 S23: -0.2630
REMARK 3 S31: 0.0100 S32: -0.2536 S33: 0.0354
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 246 THROUGH 404 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4186 -10.0642 -8.4179
REMARK 3 T TENSOR
REMARK 3 T11: 0.4140 T22: 0.3101
REMARK 3 T33: 0.2520 T12: 0.1708
REMARK 3 T13: -0.0466 T23: -0.0865
REMARK 3 L TENSOR
REMARK 3 L11: 0.5577 L22: 0.8992
REMARK 3 L33: 0.8210 L12: 0.5938
REMARK 3 L13: -0.1162 L23: 0.0601
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: -0.1113 S13: 0.0625
REMARK 3 S21: 0.0120 S22: -0.0847 S23: 0.1057
REMARK 3 S31: -0.1424 S32: -0.1116 S33: 0.0055
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 405 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4818 -36.8355 -29.1011
REMARK 3 T TENSOR
REMARK 3 T11: 0.4542 T22: 0.4056
REMARK 3 T33: 0.4787 T12: 0.1762
REMARK 3 T13: 0.0343 T23: -0.0767
REMARK 3 L TENSOR
REMARK 3 L11: 0.4656 L22: 0.4554
REMARK 3 L33: 2.1982 L12: -0.1453
REMARK 3 L13: -0.1389 L23: 0.8071
REMARK 3 S TENSOR
REMARK 3 S11: -0.1031 S12: 0.0616 S13: -0.0889
REMARK 3 S21: 0.0739 S22: -0.1075 S23: 0.0287
REMARK 3 S31: -0.0310 S32: -0.0531 S33: 0.1160
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6378 11.8602 -52.1045
REMARK 3 T TENSOR
REMARK 3 T11: 0.3188 T22: 0.5000
REMARK 3 T33: 0.4354 T12: 0.2515
REMARK 3 T13: -0.0420 T23: -0.1368
REMARK 3 L TENSOR
REMARK 3 L11: 0.6142 L22: 1.8430
REMARK 3 L33: 1.1903 L12: -0.1247
REMARK 3 L13: -0.8351 L23: 0.2510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: 0.0844 S13: 0.0022
REMARK 3 S21: -0.1086 S22: 0.0024 S23: 0.2740
REMARK 3 S31: -0.4288 S32: -0.2007 S33: -0.1355
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 99 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7709 -2.4409 -62.2871
REMARK 3 T TENSOR
REMARK 3 T11: 0.3125 T22: 0.3678
REMARK 3 T33: 0.2560 T12: 0.1537
REMARK 3 T13: -0.0068 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 0.7469 L22: 1.4226
REMARK 3 L33: 0.2691 L12: 0.2761
REMARK 3 L13: 0.1248 L23: -0.2471
REMARK 3 S TENSOR
REMARK 3 S11: 0.0401 S12: 0.2646 S13: 0.1044
REMARK 3 S21: -0.0594 S22: 0.0001 S23: 0.0851
REMARK 3 S31: -0.0569 S32: -0.1777 S33: -0.0562
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 325 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.8021 -29.6869 -54.0568
REMARK 3 T TENSOR
REMARK 3 T11: 0.2195 T22: 0.3832
REMARK 3 T33: 0.3551 T12: 0.1502
REMARK 3 T13: -0.0238 T23: -0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 0.1870 L22: 0.3354
REMARK 3 L33: 1.1197 L12: 0.0434
REMARK 3 L13: 0.0110 L23: -0.3683
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: 0.0724 S13: 0.0029
REMARK 3 S21: -0.0237 S22: 0.0089 S23: -0.0390
REMARK 3 S31: 0.3517 S32: -0.2015 S33: 0.0232
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.0857 -43.6752 -22.6434
REMARK 3 T TENSOR
REMARK 3 T11: 0.5042 T22: 0.5345
REMARK 3 T33: 0.3694 T12: 0.2063
REMARK 3 T13: -0.0138 T23: -0.1377
REMARK 3 L TENSOR
REMARK 3 L11: 1.7205 L22: 1.8153
REMARK 3 L33: 2.0106 L12: 0.0568
REMARK 3 L13: -0.8836 L23: -0.2571
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: 0.2158 S13: -0.2468
REMARK 3 S21: 0.0807 S22: 0.0018 S23: 0.0541
REMARK 3 S31: 0.4144 S32: -0.1456 S33: 0.1645
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 114 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.8845 -30.0307 -18.5353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3048 T22: 0.3588
REMARK 3 T33: 0.3762 T12: 0.2021
REMARK 3 T13: -0.0777 T23: -0.1084
REMARK 3 L TENSOR
REMARK 3 L11: 0.5962 L22: 0.3578
REMARK 3 L33: 0.5260 L12: 0.4260
REMARK 3 L13: 0.0519 L23: 0.1807
REMARK 3 S TENSOR
REMARK 3 S11: 0.1090 S12: 0.1449 S13: -0.1439
REMARK 3 S21: -0.3081 S22: -0.0331 S23: 0.0517
REMARK 3 S31: -0.1255 S32: 0.1233 S33: 0.0336
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 208 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.2947 -28.9097 -7.7664
REMARK 3 T TENSOR
REMARK 3 T11: 0.4032 T22: 0.2872
REMARK 3 T33: 0.2511 T12: 0.1368
REMARK 3 T13: 0.0220 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 0.6486 L22: 0.6964
REMARK 3 L33: 0.9529 L12: 0.3769
REMARK 3 L13: 0.1510 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.1304 S12: 0.0583 S13: -0.0529
REMARK 3 S21: 0.0269 S22: -0.1051 S23: 0.0196
REMARK 3 S31: 0.1815 S32: 0.0487 S33: -0.0169
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 6ZTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292110174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-17
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 : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104870
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.24300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.9000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.24600
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 77.8 MM NASCN, 1.67% GLYCEROL, 5.44%
REMARK 280 PEG400, 11.6% 2-PROPANOL, 4.11% TACSIMATE , SEEDING REQUIRED,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 85.28900
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MSE A -14
REMARK 465 ALA A -13
REMARK 465 SER A -12
REMARK 465 TRP A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 PRO A -8
REMARK 465 GLN A -7
REMARK 465 PHE A -6
REMARK 465 GLU A -5
REMARK 465 LYS A -4
REMARK 465 GLY A -3
REMARK 465 ASP A 225
REMARK 465 ASN A 226
REMARK 465 GLY A 227
REMARK 465 ALA A 426
REMARK 465 ASP A 427
REMARK 465 ILE A 428
REMARK 465 HIS A 429
REMARK 465 MSE B -14
REMARK 465 ALA B -13
REMARK 465 SER B -12
REMARK 465 TRP B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 PRO B -8
REMARK 465 GLN B -7
REMARK 465 PHE B -6
REMARK 465 GLU B -5
REMARK 465 LYS B -4
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 LEU B 425
REMARK 465 ALA B 426
REMARK 465 ASP B 427
REMARK 465 ILE B 428
REMARK 465 HIS B 429
REMARK 465 MSE C -14
REMARK 465 ALA C -13
REMARK 465 SER C -12
REMARK 465 TRP C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 PRO C -8
REMARK 465 GLN C -7
REMARK 465 PHE C -6
REMARK 465 GLU C -5
REMARK 465 LYS C -4
REMARK 465 GLY C -3
REMARK 465 ALA C -2
REMARK 465 GLY C -1
REMARK 465 ASP C 225
REMARK 465 ASN C 226
REMARK 465 LEU C 358
REMARK 465 LEU C 425
REMARK 465 ALA C 426
REMARK 465 ASP C 427
REMARK 465 ILE C 428
REMARK 465 HIS C 429
REMARK 465 MSE D -14
REMARK 465 ALA D -13
REMARK 465 SER D -12
REMARK 465 TRP D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 PRO D -8
REMARK 465 GLN D -7
REMARK 465 PHE D -6
REMARK 465 GLU D -5
REMARK 465 LYS D -4
REMARK 465 GLY D -3
REMARK 465 ASN D 226
REMARK 465 GLY D 227
REMARK 465 GLU D 228
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 THR A 0 OG1 CG2
REMARK 470 ILE A 141 CG1 CG2 CD1
REMARK 470 VAL A 179 CG1 CG2
REMARK 470 LEU A 180 CG CD1 CD2
REMARK 470 LEU A 230 CG CD1 CD2
REMARK 470 LEU A 277 CG CD1 CD2
REMARK 470 LEU A 425 CG CD1 CD2
REMARK 470 THR B 0 OG1 CG2
REMARK 470 PHE B 138 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 139 CG CD OE1 OE2
REMARK 470 PHE B 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 314 CG CD1 CD2
REMARK 470 LEU B 332 CG CD1 CD2
REMARK 470 THR C 0 OG1 CG2
REMARK 470 PHE C 137 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 GLU C 355 CG CD OE1 OE2
REMARK 470 LYS C 403 CG CD CE NZ
REMARK 470 THR D 0 OG1 CG2
REMARK 470 ASP D 71 CG OD1 OD2
REMARK 470 ILE D 134 CG1 CG2 CD1
REMARK 470 PHE D 137 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D 141 CG1 CG2 CD1
REMARK 470 LYS D 312 CG CD CE NZ
REMARK 470 LYS D 393 CG CD CE NZ
REMARK 470 HIS D 429 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 467 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MSE D 394 N
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 HG SER D 424 HD12 ILE D 431 1.29
REMARK 500 OE2 GLU D 199 HE ARG D 207 1.46
REMARK 500 HH11 ARG D 368 O ARG D 373 1.52
REMARK 500 HZ2 LYS B 375 O HOH B 706 1.58
REMARK 500 HD1 HIS C 433 O HOH C 614 1.59
REMARK 500 OE2 GLU A 142 O HOH A 601 1.94
REMARK 500 OE1 GLN B 183 O HOH B 701 1.96
REMARK 500 NE2 GLN B 352 O HOH B 702 1.98
REMARK 500 OD2 ASP D 286 O HOH D 601 1.99
REMARK 500 O GLN C 188 O HOH C 601 2.01
REMARK 500 OD1 ASN B 297 NZ LYS B 300 2.03
REMARK 500 OD1 ASP D 474 O HOH D 602 2.04
REMARK 500 O THR D 197 O HOH D 603 2.04
REMARK 500 O ILE B 431 O HOH B 703 2.05
REMARK 500 O TYR B 196 O HOH B 704 2.05
REMARK 500 OD2 ASP B 383 O HOH B 705 2.06
REMARK 500 O HOH C 726 O HOH C 732 2.06
REMARK 500 O GLN B 281 NZ LYS B 283 2.06
REMARK 500 OG SER D 129 O HOH D 604 2.08
REMARK 500 O HOH B 739 O HOH B 772 2.09
REMARK 500 O LYS D 100 O HOH D 605 2.09
REMARK 500 O THR A 437 O HOH A 602 2.11
REMARK 500 OD2 ASP A 62 NH1 ARG A 66 2.11
REMARK 500 OG SER D 129 O HOH D 606 2.12
REMARK 500 O HOH B 727 O HOH B 793 2.12
REMARK 500 OD1 ASN A 338 O HOH A 603 2.13
REMARK 500 O GLN C 395 O HOH C 602 2.13
REMARK 500 O ALA A 124 O HOH A 604 2.14
REMARK 500 O VAL B 208 OG1 THR B 211 2.14
REMARK 500 OD1 ASN D 162 O HOH D 607 2.15
REMARK 500 OG SER D 47 O HOH D 608 2.15
REMARK 500 O ASP D 420 O HOH D 609 2.15
REMARK 500 OD1 ASP A 410 O HOH A 605 2.15
REMARK 500 O HOH B 802 O HOH B 804 2.15
REMARK 500 OE1 GLN A 411 O HOH A 605 2.15
REMARK 500 O HOH D 609 O HOH D 677 2.16
REMARK 500 NZ LYS B 375 O HOH B 706 2.16
REMARK 500 NZ LYS D 472 O HOH D 602 2.16
REMARK 500 OE2 GLU D 407 O HOH D 610 2.16
REMARK 500 NZ LYS C 145 O HOH C 603 2.17
REMARK 500 OE2 GLU A 294 O HOH A 606 2.17
REMARK 500 O MSE C 213 O HOH C 604 2.17
REMARK 500 OE1 GLU B 436 O HOH B 707 2.18
REMARK 500 NH1 ARG B 401 O HOH B 708 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 790 O HOH D 652 1655 2.15
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 SER D 424 CB SER D 424 OG -0.312
REMARK 500 ILE D 431 CG1 ILE D 431 CD1 -0.595
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 ILE D 431 CB - CG1 - CD1 ANGL. DEV. = 18.3 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 THR A 0 161.27 126.16
REMARK 500 ASP A 34 74.76 -108.48
REMARK 500 SER A 85 -128.09 56.41
REMARK 500 PHE A 99 26.72 -151.78
REMARK 500 ASN A 102 60.04 -150.32
REMARK 500 ALA A 115 61.21 39.67
REMARK 500 ALA A 117 60.80 -69.33
REMARK 500 ASP A 169 73.60 -158.57
REMARK 500 VAL A 205 -57.01 -134.64
REMARK 500 ILE A 256 21.82 -145.09
REMARK 500 LYS A 283 24.60 -141.76
REMARK 500 ASN A 323 -153.04 -100.65
REMARK 500 PRO A 351 -73.74 -36.27
REMARK 500 TYR A 353 79.85 65.00
REMARK 500 ALA A 412 -106.99 -23.05
REMARK 500 LEU A 413 -56.34 63.50
REMARK 500 SER A 424 171.32 94.56
REMARK 500 ASP B 34 66.59 -105.32
REMARK 500 ILE B 69 30.52 -145.53
REMARK 500 ARG B 78 145.24 66.78
REMARK 500 SER B 85 -126.46 59.83
REMARK 500 PHE B 99 31.19 -152.19
REMARK 500 PHE B 137 -60.70 -123.43
REMARK 500 PHE B 138 125.81 68.05
REMARK 500 GLU B 139 -25.28 149.87
REMARK 500 GLU B 142 -85.90 -97.16
REMARK 500 VAL B 205 -65.65 -142.51
REMARK 500 ASP B 225 -132.72 53.10
REMARK 500 ASN B 226 38.32 -90.16
REMARK 500 SER B 229 -62.17 161.29
REMARK 500 LEU B 230 -108.51 81.12
REMARK 500 ILE B 256 25.64 -141.02
REMARK 500 LYS B 283 23.22 -143.24
REMARK 500 LEU B 314 -8.40 -59.48
REMARK 500 ASP B 335 5.87 -68.22
REMARK 500 ASN C 15 -8.15 -56.38
REMARK 500 ASP C 34 57.05 -104.68
REMARK 500 ARG C 78 146.23 63.12
REMARK 500 SER C 85 -133.12 59.56
REMARK 500 PHE C 99 34.54 -142.79
REMARK 500 ASN C 102 82.16 -155.24
REMARK 500 PHE C 138 132.45 -12.77
REMARK 500 GLU C 139 -36.65 -167.86
REMARK 500 ILE C 141 111.08 66.17
REMARK 500 GLU C 142 -68.10 -135.99
REMARK 500 ASP C 169 76.03 -161.21
REMARK 500 VAL C 205 -48.85 -137.37
REMARK 500 GLU C 228 -135.42 -140.53
REMARK 500 SER C 229 -70.89 79.59
REMARK 500 LEU C 230 -129.27 76.95
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 423 SER A 424 149.20
REMARK 500 LEU C 230 VAL C 231 -149.92
REMARK 500 SER D 424 LEU D 425 -148.27
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 A 730 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 731 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B 817 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 818 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH B 819 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 820 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 821 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH B 822 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH B 823 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH B 824 DISTANCE = 8.51 ANGSTROMS
REMARK 525 HOH B 825 DISTANCE = 9.10 ANGSTROMS
REMARK 525 HOH C 734 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH C 735 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C 736 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 737 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C 738 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH C 739 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH C 740 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH C 741 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH C 742 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH C 743 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH C 744 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH C 745 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH C 746 DISTANCE = 8.53 ANGSTROMS
REMARK 525 HOH C 747 DISTANCE = 9.81 ANGSTROMS
REMARK 525 HOH C 748 DISTANCE = 10.11 ANGSTROMS
REMARK 525 HOH D 732 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH D 733 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH D 734 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH D 735 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH D 736 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH D 737 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH D 738 DISTANCE = 8.59 ANGSTROMS
REMARK 525 HOH D 739 DISTANCE = 10.09 ANGSTROMS
DBREF1 6ZTH A 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTH A A0A378K488 1 474
DBREF1 6ZTH B 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTH B A0A378K488 1 474
DBREF1 6ZTH C 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTH C A0A378K488 1 474
DBREF1 6ZTH D 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTH D A0A378K488 1 474
SEQADV 6ZTH MSE A -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTH ALA A -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER A -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH TRP A -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER A -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH HIS A -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PRO A -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLN A -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PHE A -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLU A -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH LYS A -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY A -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ALA A -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY A -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH THR A 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ASN A 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTH MSE B -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTH ALA B -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER B -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH TRP B -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER B -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH HIS B -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PRO B -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLN B -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PHE B -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLU B -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH LYS B -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY B -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ALA B -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY B -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH THR B 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ASN B 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTH MSE C -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTH ALA C -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER C -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH TRP C -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER C -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH HIS C -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PRO C -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLN C -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PHE C -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLU C -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH LYS C -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY C -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ALA C -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY C -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH THR C 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ASN C 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTH MSE D -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTH ALA D -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER D -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH TRP D -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH SER D -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH HIS D -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PRO D -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLN D -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH PHE D -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLU D -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH LYS D -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY D -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ALA D -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH GLY D -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH THR D 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTH ASN D 203 UNP A0A378K48 ASP 203 CONFLICT
SEQRES 1 A 489 MSE ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 489 GLY THR MSE ILE VAL ILE PHE VAL HIS GLY TRP SER VAL
SEQRES 3 A 489 THR HIS THR ASN THR TYR GLY GLU LEU PRO GLN TRP LEU
SEQRES 4 A 489 GLU ASN GLN SER LYS GLN GLY LYS LEU ASP ILE GLN VAL
SEQRES 5 A 489 GLY ASN ILE TYR LEU GLY ARG TYR ILE SER PHE ASP ASP
SEQRES 6 A 489 THR VAL THR VAL ASP ASP ILE ALA ARG ALA PHE ASP GLN
SEQRES 7 A 489 ALA VAL ARG ASP GLU ILE ALA ASP LYS LEU ARG ASP GLY
SEQRES 8 A 489 GLN ARG PHE ALA CYS ILE THR HIS SER THR GLY GLY PRO
SEQRES 9 A 489 ILE VAL ARG LYS TRP MSE ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 A 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MSE LEU ALA
SEQRES 11 A 489 PRO ALA ASN HIS GLY SER ALA LEU ALA GLN LEU GLY LYS
SEQRES 12 A 489 SER ARG LEU GLY ARG ILE LYS SER PHE PHE GLU GLY ILE
SEQRES 13 A 489 GLU PRO GLY LYS CYS VAL LEU ASP TRP LEU GLU LEU GLY
SEQRES 14 A 489 SER ASP MSE SER TRP GLN LEU ASN GLU SER TRP LEU ASP
SEQRES 15 A 489 TYR ASP CYS THR ALA ASN GLY VAL TYR SER PHE VAL LEU
SEQRES 16 A 489 THR GLY GLN LYS ILE ASP ARG GLN PHE TYR ASP ALA VAL
SEQRES 17 A 489 ASN SER TYR THR GLY GLU SER GLY SER ASN GLY VAL VAL
SEQRES 18 A 489 ARG VAL ALA ALA THR ASN MSE ASN TYR SER LEU LEU LYS
SEQRES 19 A 489 LEU HIS GLN GLU GLY ASP ASN GLY GLU SER LEU VAL VAL
SEQRES 20 A 489 ALA LYS MSE THR ARG THR GLN PRO MSE ALA PHE GLY VAL
SEQRES 21 A 489 LEU PRO GLY LEU SER HIS SER GLY LYS ASN ILE GLY ILE
SEQRES 22 A 489 ILE ARG SER ILE THR MSE ALA ASN ALA ALA THR HIS PRO
SEQRES 23 A 489 THR ALA ILE TRP ILE LEU ARG CYS LEU GLN VAL LYS SER
SEQRES 24 A 489 ARG ASP SER TYR ASN LYS LEU VAL LYS GLU LEU ASP ASN
SEQRES 25 A 489 ILE THR LYS GLU THR GLN LYS ASN GLU HIS LYS GLU PHE
SEQRES 26 A 489 VAL LYS THR LEU VAL PHE THR ARG GLU TYR ILE THR ASN
SEQRES 27 A 489 ARG TYR SER MSE ILE ILE PHE ARG LEU ILE ASP ASP ARG
SEQRES 28 A 489 GLY ASN HIS LEU ILE ASP TYR ASP LEU TYR LEU THR ALA
SEQRES 29 A 489 GLY PRO GLN TYR SER GLU GLN ALA LEU PRO ALA GLY PHE
SEQRES 30 A 489 PHE VAL ASP ARG GLN ARG ASN LEU ASN ASN ARG GLY LYS
SEQRES 31 A 489 LEU THR TYR PHE LEU ASP TYR ASP ILE MSE GLU GLY GLY
SEQRES 32 A 489 ILE ASN THR PRO LYS MSE GLN GLY ASN LEU GLY PHE ARG
SEQRES 33 A 489 VAL LYS ALA TYR PRO GLU SER SER ASP GLN ALA LEU ALA
SEQRES 34 A 489 TYR TYR ARG LEU LEU ASP PHE HIS SER SER LEU ALA ASP
SEQRES 35 A 489 ILE HIS LYS ILE LEU HIS PRO ASN GLU THR VAL MSE VAL
SEQRES 36 A 489 GLU ILE MSE LEU GLN ARG ARG VAL ASP ARG THR VAL PHE
SEQRES 37 A 489 ARG ILE SER ASN ASN LEU THR PRO ALA LYS ILE SER GLY
SEQRES 38 A 489 LYS PRO THR GLY LYS LYS ILE ASP
SEQRES 1 B 489 MSE ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 489 GLY THR MSE ILE VAL ILE PHE VAL HIS GLY TRP SER VAL
SEQRES 3 B 489 THR HIS THR ASN THR TYR GLY GLU LEU PRO GLN TRP LEU
SEQRES 4 B 489 GLU ASN GLN SER LYS GLN GLY LYS LEU ASP ILE GLN VAL
SEQRES 5 B 489 GLY ASN ILE TYR LEU GLY ARG TYR ILE SER PHE ASP ASP
SEQRES 6 B 489 THR VAL THR VAL ASP ASP ILE ALA ARG ALA PHE ASP GLN
SEQRES 7 B 489 ALA VAL ARG ASP GLU ILE ALA ASP LYS LEU ARG ASP GLY
SEQRES 8 B 489 GLN ARG PHE ALA CYS ILE THR HIS SER THR GLY GLY PRO
SEQRES 9 B 489 ILE VAL ARG LYS TRP MSE ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 B 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MSE LEU ALA
SEQRES 11 B 489 PRO ALA ASN HIS GLY SER ALA LEU ALA GLN LEU GLY LYS
SEQRES 12 B 489 SER ARG LEU GLY ARG ILE LYS SER PHE PHE GLU GLY ILE
SEQRES 13 B 489 GLU PRO GLY LYS CYS VAL LEU ASP TRP LEU GLU LEU GLY
SEQRES 14 B 489 SER ASP MSE SER TRP GLN LEU ASN GLU SER TRP LEU ASP
SEQRES 15 B 489 TYR ASP CYS THR ALA ASN GLY VAL TYR SER PHE VAL LEU
SEQRES 16 B 489 THR GLY GLN LYS ILE ASP ARG GLN PHE TYR ASP ALA VAL
SEQRES 17 B 489 ASN SER TYR THR GLY GLU SER GLY SER ASN GLY VAL VAL
SEQRES 18 B 489 ARG VAL ALA ALA THR ASN MSE ASN TYR SER LEU LEU LYS
SEQRES 19 B 489 LEU HIS GLN GLU GLY ASP ASN GLY GLU SER LEU VAL VAL
SEQRES 20 B 489 ALA LYS MSE THR ARG THR GLN PRO MSE ALA PHE GLY VAL
SEQRES 21 B 489 LEU PRO GLY LEU SER HIS SER GLY LYS ASN ILE GLY ILE
SEQRES 22 B 489 ILE ARG SER ILE THR MSE ALA ASN ALA ALA THR HIS PRO
SEQRES 23 B 489 THR ALA ILE TRP ILE LEU ARG CYS LEU GLN VAL LYS SER
SEQRES 24 B 489 ARG ASP SER TYR ASN LYS LEU VAL LYS GLU LEU ASP ASN
SEQRES 25 B 489 ILE THR LYS GLU THR GLN LYS ASN GLU HIS LYS GLU PHE
SEQRES 26 B 489 VAL LYS THR LEU VAL PHE THR ARG GLU TYR ILE THR ASN
SEQRES 27 B 489 ARG TYR SER MSE ILE ILE PHE ARG LEU ILE ASP ASP ARG
SEQRES 28 B 489 GLY ASN HIS LEU ILE ASP TYR ASP LEU TYR LEU THR ALA
SEQRES 29 B 489 GLY PRO GLN TYR SER GLU GLN ALA LEU PRO ALA GLY PHE
SEQRES 30 B 489 PHE VAL ASP ARG GLN ARG ASN LEU ASN ASN ARG GLY LYS
SEQRES 31 B 489 LEU THR TYR PHE LEU ASP TYR ASP ILE MSE GLU GLY GLY
SEQRES 32 B 489 ILE ASN THR PRO LYS MSE GLN GLY ASN LEU GLY PHE ARG
SEQRES 33 B 489 VAL LYS ALA TYR PRO GLU SER SER ASP GLN ALA LEU ALA
SEQRES 34 B 489 TYR TYR ARG LEU LEU ASP PHE HIS SER SER LEU ALA ASP
SEQRES 35 B 489 ILE HIS LYS ILE LEU HIS PRO ASN GLU THR VAL MSE VAL
SEQRES 36 B 489 GLU ILE MSE LEU GLN ARG ARG VAL ASP ARG THR VAL PHE
SEQRES 37 B 489 ARG ILE SER ASN ASN LEU THR PRO ALA LYS ILE SER GLY
SEQRES 38 B 489 LYS PRO THR GLY LYS LYS ILE ASP
SEQRES 1 C 489 MSE ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 C 489 GLY THR MSE ILE VAL ILE PHE VAL HIS GLY TRP SER VAL
SEQRES 3 C 489 THR HIS THR ASN THR TYR GLY GLU LEU PRO GLN TRP LEU
SEQRES 4 C 489 GLU ASN GLN SER LYS GLN GLY LYS LEU ASP ILE GLN VAL
SEQRES 5 C 489 GLY ASN ILE TYR LEU GLY ARG TYR ILE SER PHE ASP ASP
SEQRES 6 C 489 THR VAL THR VAL ASP ASP ILE ALA ARG ALA PHE ASP GLN
SEQRES 7 C 489 ALA VAL ARG ASP GLU ILE ALA ASP LYS LEU ARG ASP GLY
SEQRES 8 C 489 GLN ARG PHE ALA CYS ILE THR HIS SER THR GLY GLY PRO
SEQRES 9 C 489 ILE VAL ARG LYS TRP MSE ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 C 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MSE LEU ALA
SEQRES 11 C 489 PRO ALA ASN HIS GLY SER ALA LEU ALA GLN LEU GLY LYS
SEQRES 12 C 489 SER ARG LEU GLY ARG ILE LYS SER PHE PHE GLU GLY ILE
SEQRES 13 C 489 GLU PRO GLY LYS CYS VAL LEU ASP TRP LEU GLU LEU GLY
SEQRES 14 C 489 SER ASP MSE SER TRP GLN LEU ASN GLU SER TRP LEU ASP
SEQRES 15 C 489 TYR ASP CYS THR ALA ASN GLY VAL TYR SER PHE VAL LEU
SEQRES 16 C 489 THR GLY GLN LYS ILE ASP ARG GLN PHE TYR ASP ALA VAL
SEQRES 17 C 489 ASN SER TYR THR GLY GLU SER GLY SER ASN GLY VAL VAL
SEQRES 18 C 489 ARG VAL ALA ALA THR ASN MSE ASN TYR SER LEU LEU LYS
SEQRES 19 C 489 LEU HIS GLN GLU GLY ASP ASN GLY GLU SER LEU VAL VAL
SEQRES 20 C 489 ALA LYS MSE THR ARG THR GLN PRO MSE ALA PHE GLY VAL
SEQRES 21 C 489 LEU PRO GLY LEU SER HIS SER GLY LYS ASN ILE GLY ILE
SEQRES 22 C 489 ILE ARG SER ILE THR MSE ALA ASN ALA ALA THR HIS PRO
SEQRES 23 C 489 THR ALA ILE TRP ILE LEU ARG CYS LEU GLN VAL LYS SER
SEQRES 24 C 489 ARG ASP SER TYR ASN LYS LEU VAL LYS GLU LEU ASP ASN
SEQRES 25 C 489 ILE THR LYS GLU THR GLN LYS ASN GLU HIS LYS GLU PHE
SEQRES 26 C 489 VAL LYS THR LEU VAL PHE THR ARG GLU TYR ILE THR ASN
SEQRES 27 C 489 ARG TYR SER MSE ILE ILE PHE ARG LEU ILE ASP ASP ARG
SEQRES 28 C 489 GLY ASN HIS LEU ILE ASP TYR ASP LEU TYR LEU THR ALA
SEQRES 29 C 489 GLY PRO GLN TYR SER GLU GLN ALA LEU PRO ALA GLY PHE
SEQRES 30 C 489 PHE VAL ASP ARG GLN ARG ASN LEU ASN ASN ARG GLY LYS
SEQRES 31 C 489 LEU THR TYR PHE LEU ASP TYR ASP ILE MSE GLU GLY GLY
SEQRES 32 C 489 ILE ASN THR PRO LYS MSE GLN GLY ASN LEU GLY PHE ARG
SEQRES 33 C 489 VAL LYS ALA TYR PRO GLU SER SER ASP GLN ALA LEU ALA
SEQRES 34 C 489 TYR TYR ARG LEU LEU ASP PHE HIS SER SER LEU ALA ASP
SEQRES 35 C 489 ILE HIS LYS ILE LEU HIS PRO ASN GLU THR VAL MSE VAL
SEQRES 36 C 489 GLU ILE MSE LEU GLN ARG ARG VAL ASP ARG THR VAL PHE
SEQRES 37 C 489 ARG ILE SER ASN ASN LEU THR PRO ALA LYS ILE SER GLY
SEQRES 38 C 489 LYS PRO THR GLY LYS LYS ILE ASP
SEQRES 1 D 489 MSE ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 D 489 GLY THR MSE ILE VAL ILE PHE VAL HIS GLY TRP SER VAL
SEQRES 3 D 489 THR HIS THR ASN THR TYR GLY GLU LEU PRO GLN TRP LEU
SEQRES 4 D 489 GLU ASN GLN SER LYS GLN GLY LYS LEU ASP ILE GLN VAL
SEQRES 5 D 489 GLY ASN ILE TYR LEU GLY ARG TYR ILE SER PHE ASP ASP
SEQRES 6 D 489 THR VAL THR VAL ASP ASP ILE ALA ARG ALA PHE ASP GLN
SEQRES 7 D 489 ALA VAL ARG ASP GLU ILE ALA ASP LYS LEU ARG ASP GLY
SEQRES 8 D 489 GLN ARG PHE ALA CYS ILE THR HIS SER THR GLY GLY PRO
SEQRES 9 D 489 ILE VAL ARG LYS TRP MSE ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 D 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MSE LEU ALA
SEQRES 11 D 489 PRO ALA ASN HIS GLY SER ALA LEU ALA GLN LEU GLY LYS
SEQRES 12 D 489 SER ARG LEU GLY ARG ILE LYS SER PHE PHE GLU GLY ILE
SEQRES 13 D 489 GLU PRO GLY LYS CYS VAL LEU ASP TRP LEU GLU LEU GLY
SEQRES 14 D 489 SER ASP MSE SER TRP GLN LEU ASN GLU SER TRP LEU ASP
SEQRES 15 D 489 TYR ASP CYS THR ALA ASN GLY VAL TYR SER PHE VAL LEU
SEQRES 16 D 489 THR GLY GLN LYS ILE ASP ARG GLN PHE TYR ASP ALA VAL
SEQRES 17 D 489 ASN SER TYR THR GLY GLU SER GLY SER ASN GLY VAL VAL
SEQRES 18 D 489 ARG VAL ALA ALA THR ASN MSE ASN TYR SER LEU LEU LYS
SEQRES 19 D 489 LEU HIS GLN GLU GLY ASP ASN GLY GLU SER LEU VAL VAL
SEQRES 20 D 489 ALA LYS MSE THR ARG THR GLN PRO MSE ALA PHE GLY VAL
SEQRES 21 D 489 LEU PRO GLY LEU SER HIS SER GLY LYS ASN ILE GLY ILE
SEQRES 22 D 489 ILE ARG SER ILE THR MSE ALA ASN ALA ALA THR HIS PRO
SEQRES 23 D 489 THR ALA ILE TRP ILE LEU ARG CYS LEU GLN VAL LYS SER
SEQRES 24 D 489 ARG ASP SER TYR ASN LYS LEU VAL LYS GLU LEU ASP ASN
SEQRES 25 D 489 ILE THR LYS GLU THR GLN LYS ASN GLU HIS LYS GLU PHE
SEQRES 26 D 489 VAL LYS THR LEU VAL PHE THR ARG GLU TYR ILE THR ASN
SEQRES 27 D 489 ARG TYR SER MSE ILE ILE PHE ARG LEU ILE ASP ASP ARG
SEQRES 28 D 489 GLY ASN HIS LEU ILE ASP TYR ASP LEU TYR LEU THR ALA
SEQRES 29 D 489 GLY PRO GLN TYR SER GLU GLN ALA LEU PRO ALA GLY PHE
SEQRES 30 D 489 PHE VAL ASP ARG GLN ARG ASN LEU ASN ASN ARG GLY LYS
SEQRES 31 D 489 LEU THR TYR PHE LEU ASP TYR ASP ILE MSE GLU GLY GLY
SEQRES 32 D 489 ILE ASN THR PRO LYS MSE GLN GLY ASN LEU GLY PHE ARG
SEQRES 33 D 489 VAL LYS ALA TYR PRO GLU SER SER ASP GLN ALA LEU ALA
SEQRES 34 D 489 TYR TYR ARG LEU LEU ASP PHE HIS SER SER LEU ALA ASP
SEQRES 35 D 489 ILE HIS LYS ILE LEU HIS PRO ASN GLU THR VAL MSE VAL
SEQRES 36 D 489 GLU ILE MSE LEU GLN ARG ARG VAL ASP ARG THR VAL PHE
SEQRES 37 D 489 ARG ILE SER ASN ASN LEU THR PRO ALA LYS ILE SER GLY
SEQRES 38 D 489 LYS PRO THR GLY LYS LYS ILE ASP
MODRES 6ZTH MSE A 1 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 95 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 113 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 157 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 213 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 235 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 241 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 264 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 327 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 385 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 394 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 439 MET MODIFIED RESIDUE
MODRES 6ZTH MSE A 443 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 1 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 95 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 113 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 157 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 213 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 235 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 241 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 264 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 327 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 385 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 394 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 439 MET MODIFIED RESIDUE
MODRES 6ZTH MSE B 443 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 1 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 95 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 113 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 157 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 213 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 235 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 241 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 264 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 327 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 385 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 394 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 439 MET MODIFIED RESIDUE
MODRES 6ZTH MSE C 443 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 1 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 95 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 113 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 157 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 213 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 235 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 241 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 264 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 327 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 385 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 394 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 439 MET MODIFIED RESIDUE
MODRES 6ZTH MSE D 443 MET MODIFIED RESIDUE
HET MSE A 1 17
HET MSE A 95 17
HET MSE A 113 17
HET MSE A 157 17
HET MSE A 213 17
HET MSE A 235 17
HET MSE A 241 17
HET MSE A 264 17
HET MSE A 327 17
HET MSE A 385 17
HET MSE A 394 17
HET MSE A 439 17
HET MSE A 443 17
HET MSE B 1 17
HET MSE B 95 17
HET MSE B 113 17
HET MSE B 157 17
HET MSE B 213 17
HET MSE B 235 17
HET MSE B 241 17
HET MSE B 264 17
HET MSE B 327 17
HET MSE B 385 17
HET MSE B 394 17
HET MSE B 439 17
HET MSE B 443 17
HET MSE C 1 17
HET MSE C 95 17
HET MSE C 113 17
HET MSE C 157 17
HET MSE C 213 17
HET MSE C 235 17
HET MSE C 241 17
HET MSE C 264 17
HET MSE C 327 17
HET MSE C 385 17
HET MSE C 394 17
HET MSE C 439 17
HET MSE C 443 17
HET MSE D 1 17
HET MSE D 95 17
HET MSE D 113 17
HET MSE D 157 17
HET MSE D 213 17
HET MSE D 235 17
HET MSE D 241 17
HET MSE D 264 17
HET MSE D 327 17
HET MSE D 385 17
HET MSE D 394 17
HET MSE D 439 17
HET MSE D 443 17
HET NAD A 501 70
HET NAD A 502 70
HET NAD B 601 70
HET NAD B 602 70
HET NAD C 501 70
HET NAD C 502 70
HET NAD D 501 70
HET NAD D 502 70
HETNAM MSE SELENOMETHIONINE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 1 MSE 52(C5 H11 N O2 SE)
FORMUL 5 NAD 8(C21 H27 N7 O14 P2)
FORMUL 13 HOH *543(H2 O)
HELIX 1 AA1 HIS A 13 GLY A 18 5 6
HELIX 2 AA2 GLU A 19 GLN A 30 1 12
HELIX 3 AA3 THR A 53 ASP A 75 1 23
HELIX 4 AA4 THR A 86 LYS A 100 1 15
HELIX 5 AA5 ASN A 101 CYS A 106 5 6
HELIX 6 AA6 SER A 121 LEU A 126 5 6
HELIX 7 AA7 GLY A 127 ARG A 133 1 7
HELIX 8 AA8 GLY A 144 GLU A 152 1 9
HELIX 9 AA9 SER A 155 TRP A 165 1 11
HELIX 10 AB1 LEU A 166 TYR A 168 5 3
HELIX 11 AB2 CYS A 170 GLY A 174 5 5
HELIX 12 AB3 ASP A 186 TYR A 190 5 5
HELIX 13 AB4 ASN A 194 GLU A 199 5 6
HELIX 14 AB5 ARG A 207 ASN A 212 1 6
HELIX 15 AB6 HIS A 270 GLN A 281 1 12
HELIX 16 AB7 SER A 284 GLU A 306 1 23
HELIX 17 AB8 TYR A 382 ASN A 390 1 9
HELIX 18 AB9 HIS B 13 GLY B 18 5 6
HELIX 19 AC1 GLU B 19 LYS B 29 1 11
HELIX 20 AC2 THR B 53 GLY B 76 1 24
HELIX 21 AC3 THR B 86 LYS B 100 1 15
HELIX 22 AC4 ASN B 102 CYS B 106 5 5
HELIX 23 AC5 SER B 121 GLY B 127 5 7
HELIX 24 AC6 LYS B 128 ARG B 133 1 6
HELIX 25 AC7 GLY B 144 GLU B 152 1 9
HELIX 26 AC8 SER B 155 TRP B 165 1 11
HELIX 27 AC9 LEU B 166 TYR B 168 5 3
HELIX 28 AD1 CYS B 170 GLY B 174 5 5
HELIX 29 AD2 ASP B 186 TYR B 190 5 5
HELIX 30 AD3 ASN B 194 GLU B 199 5 6
HELIX 31 AD4 ARG B 207 ASN B 212 1 6
HELIX 32 AD5 ASN B 266 THR B 269 5 4
HELIX 33 AD6 HIS B 270 GLN B 281 1 12
HELIX 34 AD7 SER B 284 GLU B 306 1 23
HELIX 35 AD8 TYR B 382 ASN B 390 1 9
HELIX 36 AD9 HIS C 13 GLY C 18 5 6
HELIX 37 AE1 GLU C 19 GLN C 30 1 12
HELIX 38 AE2 THR C 53 ASP C 75 1 23
HELIX 39 AE3 THR C 86 PHE C 99 1 14
HELIX 40 AE4 ASN C 102 CYS C 106 5 5
HELIX 41 AE5 LEU C 123 LEU C 126 5 4
HELIX 42 AE6 GLY C 127 ARG C 133 1 7
HELIX 43 AE7 GLY C 144 GLU C 152 1 9
HELIX 44 AE8 SER C 155 SER C 164 1 10
HELIX 45 AE9 TRP C 165 TYR C 168 5 4
HELIX 46 AF1 CYS C 170 GLY C 174 5 5
HELIX 47 AF2 ASP C 186 TYR C 190 5 5
HELIX 48 AF3 ASN C 194 GLU C 199 5 6
HELIX 49 AF4 ARG C 207 ASN C 212 1 6
HELIX 50 AF5 ASN C 266 THR C 269 5 4
HELIX 51 AF6 HIS C 270 VAL C 282 1 13
HELIX 52 AF7 SER C 284 GLU C 306 1 23
HELIX 53 AF8 TYR C 382 ASN C 390 1 9
HELIX 54 AF9 THR C 391 GLN C 395 5 5
HELIX 55 AG1 HIS D 13 GLY D 18 5 6
HELIX 56 AG2 GLU D 19 GLN D 30 1 12
HELIX 57 AG3 THR D 53 ILE D 69 1 17
HELIX 58 AG4 ILE D 69 ASP D 75 1 7
HELIX 59 AG5 THR D 86 PHE D 99 1 14
HELIX 60 AG6 ASN D 102 CYS D 106 5 5
HELIX 61 AG7 SER D 121 LEU D 126 1 6
HELIX 62 AG8 GLY D 127 ARG D 133 1 7
HELIX 63 AG9 GLY D 144 GLU D 152 1 9
HELIX 64 AH1 SER D 155 TRP D 165 1 11
HELIX 65 AH2 LEU D 166 TYR D 168 5 3
HELIX 66 AH3 CYS D 170 GLY D 174 5 5
HELIX 67 AH4 ASP D 186 TYR D 190 5 5
HELIX 68 AH5 ASN D 194 GLU D 199 5 6
HELIX 69 AH6 ARG D 207 ASN D 212 1 6
HELIX 70 AH7 ASN D 266 THR D 269 5 4
HELIX 71 AH8 HIS D 270 GLN D 281 1 12
HELIX 72 AH9 SER D 284 GLU D 306 1 23
HELIX 73 AI1 SER D 354 LEU D 358 5 5
HELIX 74 AI2 TYR D 382 ASN D 390 1 9
HELIX 75 AI3 THR D 391 GLN D 395 5 5
SHEET 1 AA1 7 ALA A 242 LEU A 246 0
SHEET 2 AA1 7 TYR A 176 GLY A 182 1 N VAL A 179 O GLY A 244
SHEET 3 AA1 7 LEU A 108 LEU A 114 1 N LEU A 111 O PHE A 178
SHEET 4 AA1 7 ARG A 78 HIS A 84 1 N PHE A 79 O SER A 109
SHEET 5 AA1 7 MSE A 1 VAL A 6 1 N ILE A 2 O ALA A 80
SHEET 6 AA1 7 ILE A 40 TYR A 45 1 O TYR A 41 N VAL A 3
SHEET 7 AA1 7 PHE B 453 SER B 456 -1 O SER B 456 N LEU A 42
SHEET 1 AA2 6 LEU A 230 ARG A 237 0
SHEET 2 AA2 6 SER A 216 GLU A 223 -1 N GLU A 223 O LEU A 230
SHEET 3 AA2 6 GLU A 436 LEU A 444 1 O MSE A 439 N LEU A 218
SHEET 4 AA2 6 TYR A 325 ASP A 334 1 N ILE A 333 O LEU A 444
SHEET 5 AA2 6 LEU A 376 ASP A 381 -1 O LEU A 376 N PHE A 330
SHEET 6 AA2 6 PHE A 363 ARG A 368 -1 N ASP A 365 O PHE A 379
SHEET 1 AA3 2 LYS A 308 LYS A 312 0
SHEET 2 AA3 2 THR A 317 ILE A 321 -1 O ARG A 318 N VAL A 311
SHEET 1 AA4 3 TYR A 343 THR A 348 0
SHEET 2 AA4 3 LEU A 398 ALA A 404 -1 O LYS A 403 N ASP A 344
SHEET 3 AA4 3 LEU A 419 SER A 423 -1 O PHE A 421 N PHE A 400
SHEET 1 AA5 2 ALA A 414 TYR A 415 0
SHEET 2 AA5 2 ARG A 447 VAL A 448 -1 O ARG A 447 N TYR A 415
SHEET 1 AA6 7 PHE A 453 SER A 456 0
SHEET 2 AA6 7 ILE B 40 TYR B 45 -1 O LEU B 42 N SER A 456
SHEET 3 AA6 7 ILE B 2 VAL B 6 1 N VAL B 3 O TYR B 41
SHEET 4 AA6 7 PHE B 79 HIS B 84 1 O ALA B 80 N ILE B 2
SHEET 5 AA6 7 LEU B 108 LEU B 114 1 O ILE B 112 N CYS B 81
SHEET 6 AA6 7 TYR B 176 GLY B 182 1 O LEU B 180 N MSE B 113
SHEET 7 AA6 7 ALA B 242 LEU B 246 1 O LEU B 246 N THR B 181
SHEET 1 AA7 6 VAL B 231 ARG B 237 0
SHEET 2 AA7 6 SER B 216 GLN B 222 -1 N LYS B 219 O LYS B 234
SHEET 3 AA7 6 GLU B 436 LEU B 444 1 O MSE B 443 N LEU B 220
SHEET 4 AA7 6 TYR B 325 ASP B 334 1 N MSE B 327 O VAL B 438
SHEET 5 AA7 6 LYS B 375 ASP B 381 -1 O LEU B 376 N PHE B 330
SHEET 6 AA7 6 PHE B 363 ARG B 368 -1 N GLN B 367 O THR B 377
SHEET 1 AA8 2 LYS B 308 LYS B 312 0
SHEET 2 AA8 2 THR B 317 ILE B 321 -1 O TYR B 320 N GLU B 309
SHEET 1 AA9 3 TYR B 343 THR B 348 0
SHEET 2 AA9 3 LEU B 398 ALA B 404 -1 O LYS B 403 N ASP B 344
SHEET 3 AA9 3 LEU B 419 SER B 423 -1 O PHE B 421 N PHE B 400
SHEET 1 AB1 2 ALA B 414 TYR B 415 0
SHEET 2 AB1 2 ARG B 447 VAL B 448 -1 O ARG B 447 N TYR B 415
SHEET 1 AB2 7 ALA C 242 VAL C 245 0
SHEET 2 AB2 7 TYR C 176 THR C 181 1 N VAL C 179 O GLY C 244
SHEET 3 AB2 7 LEU C 108 LEU C 114 1 N MSE C 113 O LEU C 180
SHEET 4 AB2 7 PHE C 79 HIS C 84 1 N THR C 83 O ILE C 112
SHEET 5 AB2 7 ILE C 2 VAL C 6 1 N ILE C 2 O ALA C 80
SHEET 6 AB2 7 ILE C 40 TYR C 45 1 O TYR C 41 N VAL C 3
SHEET 7 AB2 7 PHE D 453 SER D 456 -1 O ARG D 454 N ARG C 44
SHEET 1 AB3 6 LEU C 230 ARG C 237 0
SHEET 2 AB3 6 SER C 216 GLU C 223 -1 N LYS C 219 O LYS C 234
SHEET 3 AB3 6 THR C 437 LEU C 444 1 O GLU C 441 N LEU C 220
SHEET 4 AB3 6 TYR C 325 ASP C 334 1 N ILE C 329 O VAL C 440
SHEET 5 AB3 6 LYS C 375 ASP C 381 -1 O LEU C 376 N PHE C 330
SHEET 6 AB3 6 PHE C 363 ARG C 368 -1 N GLN C 367 O THR C 377
SHEET 1 AB4 2 LYS C 308 THR C 313 0
SHEET 2 AB4 2 PHE C 316 ILE C 321 -1 O TYR C 320 N GLU C 309
SHEET 1 AB5 3 TYR C 343 ALA C 349 0
SHEET 2 AB5 3 LEU C 398 ALA C 404 -1 O GLY C 399 N THR C 348
SHEET 3 AB5 3 LEU C 419 SER C 423 -1 O SER C 423 N LEU C 398
SHEET 1 AB6 2 ALA C 414 TYR C 415 0
SHEET 2 AB6 2 ARG C 447 VAL C 448 -1 O ARG C 447 N TYR C 415
SHEET 1 AB7 7 PHE C 453 SER C 456 0
SHEET 2 AB7 7 ILE D 40 TYR D 45 -1 O LEU D 42 N SER C 456
SHEET 3 AB7 7 ILE D 2 VAL D 6 1 N VAL D 3 O TYR D 41
SHEET 4 AB7 7 PHE D 79 THR D 83 1 O ALA D 80 N ILE D 2
SHEET 5 AB7 7 LEU D 108 MSE D 113 1 O ILE D 112 N CYS D 81
SHEET 6 AB7 7 TYR D 176 GLY D 182 1 O LEU D 180 N MSE D 113
SHEET 7 AB7 7 ALA D 242 LEU D 246 1 O LEU D 246 N THR D 181
SHEET 1 AB8 6 LEU D 230 ARG D 237 0
SHEET 2 AB8 6 SER D 216 GLU D 223 -1 N GLU D 223 O LEU D 230
SHEET 3 AB8 6 GLU D 436 LEU D 444 1 O MSE D 439 N LEU D 218
SHEET 4 AB8 6 TYR D 325 ASP D 334 1 N MSE D 327 O VAL D 438
SHEET 5 AB8 6 LEU D 376 ASP D 381 -1 O LEU D 376 N PHE D 330
SHEET 6 AB8 6 PHE D 363 ARG D 368 -1 N ASP D 365 O PHE D 379
SHEET 1 AB9 2 LYS D 308 LYS D 312 0
SHEET 2 AB9 2 THR D 317 ILE D 321 -1 O TYR D 320 N GLU D 309
SHEET 1 AC1 3 LEU D 345 ALA D 349 0
SHEET 2 AC1 3 LEU D 398 VAL D 402 -1 O GLY D 399 N THR D 348
SHEET 3 AC1 3 LEU D 419 SER D 423 -1 O SER D 423 N LEU D 398
SHEET 1 AC2 2 ALA D 414 TYR D 415 0
SHEET 2 AC2 2 ARG D 447 VAL D 448 -1 O ARG D 447 N TYR D 415
LINK C THR A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N ILE A 2 1555 1555 1.33
LINK C TRP A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N ASP A 96 1555 1555 1.34
LINK C ILE A 112 N MSE A 113 1555 1555 1.33
LINK C MSE A 113 N LEU A 114 1555 1555 1.34
LINK C ASP A 156 N MSE A 157 1555 1555 1.33
LINK C MSE A 157 N SER A 158 1555 1555 1.34
LINK C ASN A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N ASN A 214 1555 1555 1.33
LINK C LYS A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N THR A 236 1555 1555 1.33
LINK C PRO A 240 N MSE A 241 1555 1555 1.33
LINK C MSE A 241 N ALA A 242 1555 1555 1.33
LINK C THR A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N ALA A 265 1555 1555 1.34
LINK C SER A 326 N MSE A 327 1555 1555 1.33
LINK C MSE A 327 N ILE A 328 1555 1555 1.33
LINK C ILE A 384 N MSE A 385 1555 1555 1.33
LINK C MSE A 385 N GLU A 386 1555 1555 1.34
LINK C LYS A 393 N MSE A 394 1555 1555 1.33
LINK C MSE A 394 N GLN A 395 1555 1555 1.33
LINK C VAL A 438 N MSE A 439 1555 1555 1.33
LINK C MSE A 439 N VAL A 440 1555 1555 1.33
LINK C ILE A 442 N MSE A 443 1555 1555 1.33
LINK C MSE A 443 N LEU A 444 1555 1555 1.33
LINK C THR B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ILE B 2 1555 1555 1.33
LINK C TRP B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N ASP B 96 1555 1555 1.34
LINK C ILE B 112 N MSE B 113 1555 1555 1.33
LINK C MSE B 113 N LEU B 114 1555 1555 1.33
LINK C ASP B 156 N MSE B 157 1555 1555 1.33
LINK C MSE B 157 N SER B 158 1555 1555 1.34
LINK C ASN B 212 N MSE B 213 1555 1555 1.33
LINK C MSE B 213 N ASN B 214 1555 1555 1.33
LINK C LYS B 234 N MSE B 235 1555 1555 1.33
LINK C MSE B 235 N THR B 236 1555 1555 1.33
LINK C PRO B 240 N MSE B 241 1555 1555 1.33
LINK C MSE B 241 N ALA B 242 1555 1555 1.33
LINK C THR B 263 N MSE B 264 1555 1555 1.33
LINK C MSE B 264 N ALA B 265 1555 1555 1.34
LINK C SER B 326 N MSE B 327 1555 1555 1.33
LINK C MSE B 327 N ILE B 328 1555 1555 1.33
LINK C ILE B 384 N MSE B 385 1555 1555 1.33
LINK C MSE B 385 N GLU B 386 1555 1555 1.33
LINK C LYS B 393 N MSE B 394 1555 1555 1.33
LINK C MSE B 394 N GLN B 395 1555 1555 1.33
LINK C VAL B 438 N MSE B 439 1555 1555 1.33
LINK C MSE B 439 N VAL B 440 1555 1555 1.33
LINK C ILE B 442 N MSE B 443 1555 1555 1.33
LINK C MSE B 443 N LEU B 444 1555 1555 1.33
LINK C THR C 0 N MSE C 1 1555 1555 1.33
LINK C MSE C 1 N ILE C 2 1555 1555 1.33
LINK C TRP C 94 N MSE C 95 1555 1555 1.33
LINK C MSE C 95 N ASP C 96 1555 1555 1.33
LINK C ILE C 112 N MSE C 113 1555 1555 1.33
LINK C MSE C 113 N LEU C 114 1555 1555 1.33
LINK C ASP C 156 N MSE C 157 1555 1555 1.33
LINK C MSE C 157 N SER C 158 1555 1555 1.34
LINK C ASN C 212 N MSE C 213 1555 1555 1.33
LINK C MSE C 213 N ASN C 214 1555 1555 1.33
LINK C LYS C 234 N MSE C 235 1555 1555 1.33
LINK C MSE C 235 N THR C 236 1555 1555 1.33
LINK C PRO C 240 N MSE C 241 1555 1555 1.33
LINK C MSE C 241 N ALA C 242 1555 1555 1.33
LINK C THR C 263 N MSE C 264 1555 1555 1.33
LINK C MSE C 264 N ALA C 265 1555 1555 1.33
LINK C SER C 326 N MSE C 327 1555 1555 1.33
LINK C MSE C 327 N ILE C 328 1555 1555 1.33
LINK C ILE C 384 N MSE C 385 1555 1555 1.33
LINK C MSE C 385 N GLU C 386 1555 1555 1.34
LINK C LYS C 393 N MSE C 394 1555 1555 1.33
LINK C MSE C 394 N GLN C 395 1555 1555 1.33
LINK C VAL C 438 N MSE C 439 1555 1555 1.32
LINK C MSE C 439 N VAL C 440 1555 1555 1.33
LINK C ILE C 442 N MSE C 443 1555 1555 1.33
LINK C MSE C 443 N LEU C 444 1555 1555 1.33
LINK C THR D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N ILE D 2 1555 1555 1.33
LINK C TRP D 94 N MSE D 95 1555 1555 1.33
LINK C MSE D 95 N ASP D 96 1555 1555 1.34
LINK C ILE D 112 N MSE D 113 1555 1555 1.33
LINK C MSE D 113 N LEU D 114 1555 1555 1.33
LINK C ASP D 156 N MSE D 157 1555 1555 1.33
LINK C MSE D 157 N SER D 158 1555 1555 1.33
LINK C ASN D 212 N MSE D 213 1555 1555 1.33
LINK C MSE D 213 N ASN D 214 1555 1555 1.33
LINK C LYS D 234 N MSE D 235 1555 1555 1.33
LINK C MSE D 235 N THR D 236 1555 1555 1.33
LINK C PRO D 240 N MSE D 241 1555 1555 1.33
LINK C MSE D 241 N ALA D 242 1555 1555 1.33
LINK C THR D 263 N MSE D 264 1555 1555 1.33
LINK C MSE D 264 N ALA D 265 1555 1555 1.33
LINK C SER D 326 N MSE D 327 1555 1555 1.33
LINK C MSE D 327 N ILE D 328 1555 1555 1.33
LINK C ILE D 384 N MSE D 385 1555 1555 1.33
LINK C MSE D 385 N GLU D 386 1555 1555 1.33
LINK C LYS D 393 N MSE D 394 1555 1555 1.33
LINK C MSE D 394 N GLN D 395 1555 1555 1.33
LINK C VAL D 438 N MSE D 439 1555 1555 1.33
LINK C MSE D 439 N VAL D 440 1555 1555 1.33
LINK C ILE D 442 N MSE D 443 1555 1555 1.33
LINK C MSE D 443 N LEU D 444 1555 1555 1.33
CISPEP 1 TYR A 405 PRO A 406 0 -3.55
CISPEP 2 GLY B 227 GLU B 228 0 2.87
CISPEP 3 TYR B 405 PRO B 406 0 -3.71
CISPEP 4 TYR C 405 PRO C 406 0 2.72
CISPEP 5 TYR D 405 PRO D 406 0 -1.67
CRYST1 75.806 170.578 93.485 90.00 92.86 90.00 P 1 21 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 0.013192 0.000000 0.000659 0.00000
SCALE2 0.000000 0.005862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010710 0.00000
TER 7445 ASP A 474
TER 14863 ASP B 474
TER 22281 ASP C 474
TER 29713 ASP D 474
MASTER 841 0 60 75 80 0 0 615798 4 1548 152
END |