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HEADER HYDROLASE 20-JUL-20 6ZTI
TITLE PHOSPHOLIPASE PLAB FROM LEGIONELLA PNEUMOPHILA IN COMPLEX WITH THIO-
TITLE 2 NAD
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 6ZTI 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. 1.81 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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.9
REMARK 3 NUMBER OF REFLECTIONS : 161735
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 8002
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.9100 - 5.6200 1.00 6723 376 0.2270 0.2340
REMARK 3 2 5.6200 - 4.4600 1.00 6699 357 0.1583 0.1949
REMARK 3 3 4.4600 - 3.9000 1.00 6727 364 0.1480 0.2080
REMARK 3 4 3.9000 - 3.5400 0.99 6701 351 0.1539 0.2001
REMARK 3 5 3.5400 - 3.2900 0.99 6672 362 0.1549 0.2026
REMARK 3 6 3.2900 - 3.1000 0.99 6708 335 0.1625 0.2061
REMARK 3 7 3.1000 - 2.9400 0.99 6681 347 0.1751 0.2251
REMARK 3 8 2.9400 - 2.8100 0.99 6648 350 0.1666 0.2188
REMARK 3 9 2.8100 - 2.7000 0.99 6680 336 0.1749 0.2280
REMARK 3 10 2.7000 - 2.6100 0.98 6677 310 0.1867 0.2154
REMARK 3 11 2.6100 - 2.5300 0.98 6638 360 0.1838 0.2432
REMARK 3 12 2.5300 - 2.4600 0.98 6617 336 0.1835 0.2464
REMARK 3 13 2.4600 - 2.3900 0.98 6651 325 0.1926 0.2428
REMARK 3 14 2.3900 - 2.3300 0.98 6664 334 0.1905 0.2346
REMARK 3 15 2.3300 - 2.2800 0.98 6629 292 0.1905 0.2626
REMARK 3 16 2.2800 - 2.2300 0.97 6478 390 0.2166 0.2899
REMARK 3 17 2.2300 - 2.1900 0.96 6465 334 0.2020 0.2607
REMARK 3 18 2.1900 - 2.1500 0.90 6077 308 0.2022 0.2831
REMARK 3 19 2.1500 - 2.1100 0.83 5531 286 0.2159 0.2645
REMARK 3 20 2.1100 - 2.0700 0.76 5194 259 0.2333 0.2892
REMARK 3 21 2.0700 - 2.0400 0.69 4695 253 0.2460 0.2841
REMARK 3 22 2.0400 - 2.0100 0.65 4378 238 0.2456 0.2883
REMARK 3 23 2.0100 - 1.9800 0.59 3943 211 0.2519 0.2896
REMARK 3 24 1.9800 - 1.9500 0.51 3436 177 0.2488 0.2859
REMARK 3 25 1.9500 - 1.9200 0.41 2741 139 0.2537 0.2702
REMARK 3 26 1.9200 - 1.9000 0.31 2075 105 0.2688 0.3147
REMARK 3 27 1.9000 - 1.8800 0.21 1391 87 0.2552 0.3352
REMARK 3 28 1.8800 - 1.8500 0.11 726 45 0.2547 0.2970
REMARK 3 29 1.8500 - 1.8300 0.05 339 21 0.2343 0.2889
REMARK 3 30 1.8300 - 1.8100 0.02 149 14 0.2382 0.2658
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.41
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 : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2969 -46.0565 6.6840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.1291
REMARK 3 T33: 0.1290 T12: 0.0822
REMARK 3 T13: -0.0428 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 1.2146 L22: 1.6241
REMARK 3 L33: 0.6441 L12: 0.3806
REMARK 3 L13: 0.2161 L23: 0.1271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0851 S12: -0.0598 S13: -0.2606
REMARK 3 S21: 0.0531 S22: -0.0382 S23: -0.0767
REMARK 3 S31: 0.2910 S32: 0.1997 S33: 0.0530
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3926 -29.9498 -6.4792
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0922
REMARK 3 T33: 0.0442 T12: 0.0245
REMARK 3 T13: 0.0015 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.6144 L22: 0.9596
REMARK 3 L33: 0.6953 L12: -0.0704
REMARK 3 L13: 0.1385 L23: -0.0260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: 0.0173 S13: -0.0454
REMARK 3 S21: 0.0098 S22: 0.0206 S23: -0.0193
REMARK 3 S31: 0.0725 S32: 0.0791 S33: -0.0095
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 375 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0587 -3.1787 -3.8803
REMARK 3 T TENSOR
REMARK 3 T11: 0.1144 T22: 0.1233
REMARK 3 T33: 0.1006 T12: -0.0065
REMARK 3 T13: 0.0261 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 0.7002
REMARK 3 L33: 1.3171 L12: 0.4354
REMARK 3 L13: 0.4864 L23: 0.8195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: 0.0179 S13: 0.0782
REMARK 3 S21: -0.1340 S22: -0.0396 S23: 0.0162
REMARK 3 S31: -0.2985 S32: 0.0139 S33: 0.0429
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4416 15.2473 24.0758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.1109
REMARK 3 T33: 0.1133 T12: -0.0526
REMARK 3 T13: 0.0303 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.7159 L22: 1.6744
REMARK 3 L33: 1.2758 L12: -0.3290
REMARK 3 L13: -0.3212 L23: 0.0225
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: 0.1319 S13: 0.2490
REMARK 3 S21: -0.0348 S22: -0.0280 S23: -0.1003
REMARK 3 S31: -0.2560 S32: 0.0981 S33: 0.0468
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4396 -1.2854 37.1249
REMARK 3 T TENSOR
REMARK 3 T11: 0.0399 T22: 0.0622
REMARK 3 T33: 0.0364 T12: 0.0012
REMARK 3 T13: -0.0136 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.8303 L22: 0.8649
REMARK 3 L33: 0.6672 L12: 0.0724
REMARK 3 L13: -0.1160 L23: 0.0091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0347 S12: 0.0130 S13: 0.0443
REMARK 3 S21: -0.0058 S22: -0.0008 S23: -0.0249
REMARK 3 S31: -0.0725 S32: 0.0208 S33: -0.0193
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 375 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9560 -27.8906 34.5244
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.1083
REMARK 3 T33: 0.1105 T12: 0.0061
REMARK 3 T13: -0.0212 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.1633 L22: 0.8835
REMARK 3 L33: 1.3230 L12: -0.3962
REMARK 3 L13: -0.4029 L23: 0.8281
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: 0.0251 S13: -0.0294
REMARK 3 S21: 0.1417 S22: -0.0275 S23: -0.0223
REMARK 3 S31: 0.3054 S32: 0.0237 S33: 0.0308
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7962 8.9107 -5.1469
REMARK 3 T TENSOR
REMARK 3 T11: 0.1537 T22: 0.1190
REMARK 3 T33: 0.1100 T12: 0.0802
REMARK 3 T13: 0.0065 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.4767 L22: 1.6001
REMARK 3 L33: 0.9111 L12: 0.1245
REMARK 3 L13: -0.4285 L23: -0.3087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0883 S12: -0.0242 S13: 0.2452
REMARK 3 S21: -0.0453 S22: -0.0990 S23: 0.0751
REMARK 3 S31: -0.3168 S32: -0.0686 S33: 0.0234
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 100 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9885 -11.3981 -10.4166
REMARK 3 T TENSOR
REMARK 3 T11: 0.0383 T22: 0.0807
REMARK 3 T33: 0.0391 T12: 0.0094
REMARK 3 T13: -0.0104 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.6610 L22: 0.9585
REMARK 3 L33: 0.6753 L12: -0.0433
REMARK 3 L13: -0.0535 L23: -0.1048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.0076 S13: 0.0424
REMARK 3 S21: -0.0467 S22: -0.0131 S23: 0.0154
REMARK 3 S31: -0.0554 S32: -0.0644 S33: -0.0188
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 375 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3997 -34.7713 3.1856
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.1054
REMARK 3 T33: 0.1127 T12: -0.0117
REMARK 3 T13: -0.0165 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0904 L22: 0.3638
REMARK 3 L33: 1.9634 L12: 0.1442
REMARK 3 L13: -0.3201 L23: -0.3893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: 0.0277 S13: -0.0724
REMARK 3 S21: -0.0219 S22: -0.0274 S23: 0.0500
REMARK 3 S31: 0.3553 S32: 0.0234 S33: -0.0024
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9447 -39.9765 35.7442
REMARK 3 T TENSOR
REMARK 3 T11: 0.1665 T22: 0.1107
REMARK 3 T33: 0.1082 T12: -0.0665
REMARK 3 T13: 0.0035 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.6953 L22: 1.3773
REMARK 3 L33: 1.1846 L12: -0.2767
REMARK 3 L13: 0.5822 L23: -0.2231
REMARK 3 S TENSOR
REMARK 3 S11: 0.0368 S12: 0.0013 S13: -0.2314
REMARK 3 S21: 0.0929 S22: -0.0354 S23: 0.0676
REMARK 3 S31: 0.2682 S32: -0.1112 S33: 0.0097
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 100 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2915 -22.4391 42.4097
REMARK 3 T TENSOR
REMARK 3 T11: 0.0450 T22: 0.0788
REMARK 3 T33: 0.0346 T12: -0.0234
REMARK 3 T13: 0.0025 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.9267 L22: 1.0395
REMARK 3 L33: 0.9515 L12: 0.0760
REMARK 3 L13: 0.0265 L23: -0.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: -0.0362 S13: -0.0269
REMARK 3 S21: 0.0607 S22: -0.0047 S23: 0.0405
REMARK 3 S31: 0.1023 S32: -0.0805 S33: -0.0259
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 335 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3572 -3.0115 32.8713
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.1152
REMARK 3 T33: 0.0503 T12: -0.0180
REMARK 3 T13: 0.0252 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 0.5571 L22: 0.8523
REMARK 3 L33: 0.6021 L12: -0.3139
REMARK 3 L13: 0.5411 L23: -0.5319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0255 S12: 0.1091 S13: 0.0819
REMARK 3 S21: -0.0599 S22: -0.0227 S23: -0.0879
REMARK 3 S31: 0.0422 S32: -0.1101 S33: 0.0022
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 375 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6052 3.5913 27.8092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0995 T22: 0.0930
REMARK 3 T33: 0.0938 T12: 0.0169
REMARK 3 T13: 0.0071 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.1358 L22: 0.2962
REMARK 3 L33: 1.9754 L12: -0.2172
REMARK 3 L13: 0.4315 L23: -0.5155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: -0.0268 S13: 0.0222
REMARK 3 S21: 0.0330 S22: 0.0045 S23: 0.0124
REMARK 3 S31: -0.2870 S32: -0.0036 S33: -0.0356
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 6ZTI 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_1292110176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.21233
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161898
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 46.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.39000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: XXXX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.5, 8.33% GLYCEROL,
REMARK 280 10.8% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 MET 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 ALA A -2
REMARK 465 GLY A -1
REMARK 465 LYS A 135
REMARK 465 SER A 136
REMARK 465 PHE A 137
REMARK 465 PHE A 138
REMARK 465 GLU A 139
REMARK 465 GLY A 140
REMARK 465 ILE A 141
REMARK 465 ASP A 225
REMARK 465 ASN A 226
REMARK 465 GLY A 227
REMARK 465 MET 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 ARG B 133
REMARK 465 ILE B 134
REMARK 465 LYS B 135
REMARK 465 SER B 136
REMARK 465 PHE B 137
REMARK 465 PHE B 138
REMARK 465 GLU B 139
REMARK 465 GLY B 140
REMARK 465 ILE B 141
REMARK 465 MET 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 ARG C 133
REMARK 465 ILE C 134
REMARK 465 LYS C 135
REMARK 465 SER C 136
REMARK 465 PHE C 137
REMARK 465 PHE C 138
REMARK 465 GLU C 139
REMARK 465 GLY C 140
REMARK 465 ILE C 141
REMARK 465 ASP C 225
REMARK 465 ASN C 226
REMARK 465 MET 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 ALA D -2
REMARK 465 GLY D -1
REMARK 465 ARG D 133
REMARK 465 ILE D 134
REMARK 465 LYS D 135
REMARK 465 SER D 136
REMARK 465 PHE D 137
REMARK 465 PHE D 138
REMARK 465 GLU D 139
REMARK 465 GLY D 140
REMARK 465 ILE D 141
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 ILE A 428 CG1 CG2 CD1
REMARK 470 ASP B 225 CG OD1 OD2
REMARK 470 ASN B 226 CG OD1 ND2
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 GLU C 228 CG CD OE1 OE2
REMARK 470 ILE C 428 CG1 CG2 CD1
REMARK 470 ASN D 226 CG OD1 ND2
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 85 O HOH D 605 1.51
REMARK 500 HZ3 LYS C 472 O HOH C 621 1.53
REMARK 500 HH22 ARG A 130 O2N SND A 501 1.56
REMARK 500 HE ARG C 401 OD1 ASP C 420 1.59
REMARK 500 HZ1 LYS C 128 O HOH C 616 1.59
REMARK 500 HH22 ARG D 130 O2N SND D 501 1.60
REMARK 500 OE1 GLU C 142 O HOH C 601 1.98
REMARK 500 OE1 GLU A 386 O HOH A 601 1.98
REMARK 500 O HOH B 959 O HOH B 965 1.98
REMARK 500 O HOH C 888 O HOH C 950 1.99
REMARK 500 O HOH A 628 O HOH A 810 1.99
REMARK 500 O HOH C 614 O HOH C 919 2.00
REMARK 500 O HOH D 787 O HOH D 964 2.00
REMARK 500 O HOH A 979 O HOH A 988 2.00
REMARK 500 O HOH D 604 O HOH D 869 2.01
REMARK 500 O HOH C 868 O HOH C 879 2.01
REMARK 500 O HOH D 969 O HOH D 985 2.01
REMARK 500 O HOH A 871 O HOH B 651 2.01
REMARK 500 O HOH D 752 O HOH D 996 2.02
REMARK 500 O HOH B 921 O HOH B 964 2.02
REMARK 500 O HOH A 929 O HOH A 1038 2.03
REMARK 500 O HOH C 799 O HOH C 855 2.03
REMARK 500 O HOH C 605 O HOH C 883 2.03
REMARK 500 O HOH B 924 O HOH B 929 2.03
REMARK 500 O HOH C 914 O HOH C 1003 2.03
REMARK 500 O HOH D 941 O HOH D 952 2.04
REMARK 500 OD1 ASN A 26 O HOH A 602 2.04
REMARK 500 OD1 ASP C 286 O HOH C 602 2.04
REMARK 500 OD1 ASP D 427 O HOH D 601 2.04
REMARK 500 O HOH A 605 O HOH A 940 2.04
REMARK 500 O HOH C 793 O HOH C 989 2.05
REMARK 500 O HOH C 773 O HOH C 975 2.05
REMARK 500 O HOH A 972 O HOH A 1020 2.05
REMARK 500 O HOH B 818 O HOH D 847 2.05
REMARK 500 O HOH C 900 O HOH D 993 2.05
REMARK 500 O HOH C 945 O HOH C 1004 2.07
REMARK 500 O HOH D 668 O HOH D 996 2.07
REMARK 500 O HOH B 648 O HOH B 899 2.07
REMARK 500 OD2 ASP D 167 O HOH D 602 2.08
REMARK 500 O HOH A 1014 O HOH C 933 2.08
REMARK 500 O HOH A 934 O HOH B 982 2.08
REMARK 500 O HOH D 606 O HOH D 938 2.09
REMARK 500 O HOH A 732 O HOH A 894 2.09
REMARK 500 O HOH C 614 O HOH C 778 2.09
REMARK 500 O HOH A 650 O HOH A 884 2.10
REMARK 500 O HOH B 985 O HOH B 998 2.10
REMARK 500 O HOH A 935 O HOH A 967 2.10
REMARK 500 O HOH D 815 O HOH D 872 2.10
REMARK 500 O HOH A 824 O HOH A 904 2.11
REMARK 500 O HOH A 725 O HOH A 1002 2.11
REMARK 500
REMARK 500 THIS ENTRY HAS 80 CLOSE CONTACTS
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 904 O HOH D 807 1655 2.14
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 ASP A 34 71.12 -106.86
REMARK 500 SER A 85 -126.55 54.94
REMARK 500 PHE A 99 14.35 -143.81
REMARK 500 ASN A 101 39.90 -96.04
REMARK 500 ASN A 102 40.49 -162.57
REMARK 500 ALA A 115 55.40 39.33
REMARK 500 GLN A 183 29.52 -141.16
REMARK 500 VAL A 205 -50.18 -132.82
REMARK 500 ASN A 323 -153.01 -100.45
REMARK 500 ASP B 34 64.52 -110.85
REMARK 500 SER B 85 -121.50 55.17
REMARK 500 PHE B 99 15.82 -142.57
REMARK 500 ASN B 102 45.00 -164.07
REMARK 500 ALA B 115 51.85 39.95
REMARK 500 VAL B 205 -44.07 -132.90
REMARK 500 ASP B 225 -141.85 -82.91
REMARK 500 ILE B 256 22.44 -142.77
REMARK 500 ASN B 323 -146.50 -99.42
REMARK 500 ASP C 34 62.90 -106.34
REMARK 500 SER C 85 -129.20 58.53
REMARK 500 PHE C 99 15.61 -143.39
REMARK 500 ASN C 102 56.74 -159.15
REMARK 500 GLN C 183 28.96 -140.05
REMARK 500 ASN C 323 -148.44 -98.77
REMARK 500 ASP D 34 65.41 -110.13
REMARK 500 SER D 85 -124.67 52.72
REMARK 500 ASN D 102 46.68 -164.39
REMARK 500 VAL D 205 -50.97 -136.64
REMARK 500 ASP D 225 -132.22 -116.16
REMARK 500 ASN D 323 -151.50 -94.48
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 A1044 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1045 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A1046 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1047 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A1048 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH A1049 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH A1050 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH B1002 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH C1013 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C1014 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C1015 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH C1016 DISTANCE = 9.02 ANGSTROMS
REMARK 525 HOH D1030 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D1031 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D1032 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH D1033 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH D1034 DISTANCE = 8.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SND D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 502
DBREF1 6ZTI A 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTI A A0A378K488 1 474
DBREF1 6ZTI B 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTI B A0A378K488 1 474
DBREF1 6ZTI C 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTI C A0A378K488 1 474
DBREF1 6ZTI D 1 474 UNP A0A378K488_LEGPN
DBREF2 6ZTI D A0A378K488 1 474
SEQADV 6ZTI MET A -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTI ALA A -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER A -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI TRP A -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER A -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI HIS A -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PRO A -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLN A -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PHE A -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLU A -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI LYS A -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY A -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ALA A -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY A -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI THR A 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ASN A 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTI MET B -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTI ALA B -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER B -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI TRP B -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER B -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI HIS B -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PRO B -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLN B -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PHE B -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLU B -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI LYS B -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY B -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ALA B -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY B -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI THR B 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ASN B 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTI MET C -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTI ALA C -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER C -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI TRP C -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER C -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI HIS C -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PRO C -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLN C -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PHE C -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLU C -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI LYS C -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY C -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ALA C -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY C -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI THR C 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ASN C 203 UNP A0A378K48 ASP 203 CONFLICT
SEQADV 6ZTI MET D -14 UNP A0A378K48 INITIATING METHIONINE
SEQADV 6ZTI ALA D -13 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER D -12 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI TRP D -11 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI SER D -10 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI HIS D -9 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PRO D -8 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLN D -7 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI PHE D -6 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLU D -5 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI LYS D -4 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY D -3 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ALA D -2 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI GLY D -1 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI THR D 0 UNP A0A378K48 EXPRESSION TAG
SEQADV 6ZTI ASN D 203 UNP A0A378K48 ASP 203 CONFLICT
SEQRES 1 A 489 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 489 GLY THR MET 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 MET ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 A 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MET 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 MET 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 MET 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 MET THR ARG THR GLN PRO MET 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 MET 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 MET 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 MET GLU GLY GLY
SEQRES 32 A 489 ILE ASN THR PRO LYS MET 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 MET VAL
SEQRES 36 A 489 GLU ILE MET 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 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 489 GLY THR MET 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 MET ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 B 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MET 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 MET 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 MET 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 MET THR ARG THR GLN PRO MET 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 MET 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 MET 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 MET GLU GLY GLY
SEQRES 32 B 489 ILE ASN THR PRO LYS MET 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 MET VAL
SEQRES 36 B 489 GLU ILE MET 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 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 C 489 GLY THR MET 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 MET ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 C 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MET 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 MET 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 MET 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 MET THR ARG THR GLN PRO MET 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 MET 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 MET 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 MET GLU GLY GLY
SEQRES 32 C 489 ILE ASN THR PRO LYS MET 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 MET VAL
SEQRES 36 C 489 GLU ILE MET 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 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 D 489 GLY THR MET 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 MET ASP LEU TYR PHE LYS ASN ASN
SEQRES 10 D 489 LEU ALA LYS CYS PRO LEU SER HIS LEU ILE MET 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 MET 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 MET 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 MET THR ARG THR GLN PRO MET 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 MET 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 MET 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 MET GLU GLY GLY
SEQRES 32 D 489 ILE ASN THR PRO LYS MET 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 MET VAL
SEQRES 36 D 489 GLU ILE MET 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
HET SND A 501 70
HET SND A 502 70
HET GOL A 503 14
HET SND B 501 70
HET SND B 502 71
HET SND B 503 70
HET GOL B 504 14
HET SND C 501 71
HET SND C 502 70
HET GOL C 503 14
HET SND D 501 71
HET GOL D 502 14
HETNAM SND THIONICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SND 8(C21 H27 N7 O13 P2 S)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 17 HOH *1702(H2 O)
HELIX 1 AA1 HIS A 13 GLY A 18 5 6
HELIX 2 AA2 GLU A 19 LYS A 29 1 11
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 LEU A 123 GLN A 125 5 3
HELIX 7 AA7 LEU A 126 ILE A 134 1 9
HELIX 8 AA8 GLY A 144 GLU A 152 1 9
HELIX 9 AA9 SER A 155 LEU A 166 1 12
HELIX 10 AB1 CYS A 170 GLY A 174 5 5
HELIX 11 AB2 ASP A 186 TYR A 190 5 5
HELIX 12 AB3 ASN A 194 GLU A 199 5 6
HELIX 13 AB4 ARG A 207 ASN A 212 1 6
HELIX 14 AB5 ASN A 266 THR A 269 5 4
HELIX 15 AB6 HIS A 270 VAL A 282 1 13
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 GLN B 30 1 12
HELIX 20 AC2 THR B 53 ASP B 75 1 23
HELIX 21 AC3 THR B 86 LYS B 100 1 15
HELIX 22 AC4 ASN B 101 CYS B 106 5 6
HELIX 23 AC5 SER B 121 GLN B 125 5 5
HELIX 24 AC6 LEU B 126 GLY B 132 1 7
HELIX 25 AC7 GLY B 144 GLU B 152 1 9
HELIX 26 AC8 SER B 155 LEU B 166 1 12
HELIX 27 AC9 CYS B 170 GLY B 174 5 5
HELIX 28 AD1 ASP B 186 TYR B 190 5 5
HELIX 29 AD2 ASN B 194 GLU B 199 5 6
HELIX 30 AD3 ARG B 207 ASN B 212 1 6
HELIX 31 AD4 ASN B 266 THR B 269 5 4
HELIX 32 AD5 HIS B 270 VAL B 282 1 13
HELIX 33 AD6 SER B 284 GLU B 306 1 23
HELIX 34 AD7 TYR B 382 ASN B 390 1 9
HELIX 35 AD8 HIS C 13 GLY C 18 5 6
HELIX 36 AD9 GLU C 19 GLN C 30 1 12
HELIX 37 AE1 THR C 53 ASP C 75 1 23
HELIX 38 AE2 THR C 86 LYS C 100 1 15
HELIX 39 AE3 ASN C 102 CYS C 106 5 5
HELIX 40 AE4 SER C 121 GLN C 125 5 5
HELIX 41 AE5 LEU C 126 GLY C 132 1 7
HELIX 42 AE6 GLY C 144 GLU C 152 1 9
HELIX 43 AE7 SER C 155 LEU C 166 1 12
HELIX 44 AE8 CYS C 170 GLY C 174 5 5
HELIX 45 AE9 ASP C 186 TYR C 190 5 5
HELIX 46 AF1 ASN C 194 GLU C 199 5 6
HELIX 47 AF2 ARG C 207 ASN C 212 1 6
HELIX 48 AF3 ASN C 266 THR C 269 5 4
HELIX 49 AF4 HIS C 270 VAL C 282 1 13
HELIX 50 AF5 SER C 284 GLU C 306 1 23
HELIX 51 AF6 TYR C 382 ASN C 390 1 9
HELIX 52 AF7 HIS D 13 GLY D 18 5 6
HELIX 53 AF8 GLU D 19 GLN D 30 1 12
HELIX 54 AF9 THR D 53 ASP D 75 1 23
HELIX 55 AG1 THR D 86 PHE D 99 1 14
HELIX 56 AG2 LYS D 100 CYS D 106 5 7
HELIX 57 AG3 LEU D 123 GLN D 125 5 3
HELIX 58 AG4 LEU D 126 GLY D 132 1 7
HELIX 59 AG5 GLY D 144 GLU D 152 1 9
HELIX 60 AG6 SER D 155 LEU D 166 1 12
HELIX 61 AG7 CYS D 170 GLY D 174 5 5
HELIX 62 AG8 ASP D 186 TYR D 190 5 5
HELIX 63 AG9 ASN D 194 GLU D 199 5 6
HELIX 64 AH1 ARG D 207 ASN D 212 1 6
HELIX 65 AH2 ASN D 266 THR D 269 5 4
HELIX 66 AH3 HIS D 270 VAL D 282 1 13
HELIX 67 AH4 SER D 284 GLU D 306 1 23
HELIX 68 AH5 TYR D 382 ASN D 390 1 9
SHEET 1 AA1 7 ALA A 242 VAL A 245 0
SHEET 2 AA1 7 TYR A 176 THR A 181 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 MET 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 LEU A 217 O THR A 236
SHEET 3 AA2 6 THR A 437 LEU A 444 1 O MET A 439 N LEU A 218
SHEET 4 AA2 6 TYR A 325 ASP A 334 1 N ILE A 329 O VAL A 440
SHEET 5 AA2 6 LYS A 375 ASP A 381 -1 O LEU A 376 N PHE A 330
SHEET 6 AA2 6 PHE A 363 ARG A 368 -1 N GLN A 367 O THR A 377
SHEET 1 AA3 2 LYS A 308 LYS A 312 0
SHEET 2 AA3 2 THR A 317 ILE A 321 -1 O TYR A 320 N GLU A 309
SHEET 1 AA4 3 TYR A 343 ALA A 349 0
SHEET 2 AA4 3 ASN A 397 ALA A 404 -1 O ARG A 401 N TYR A 346
SHEET 3 AA4 3 LEU A 419 SER A 424 -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 MET B 1 VAL B 6 1 N VAL B 3 O TYR B 41
SHEET 4 AA6 7 ARG B 78 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 PHE B 178 N LEU B 111
SHEET 7 AA6 7 ALA B 242 LEU B 246 1 O LEU B 246 N THR B 181
SHEET 1 AA7 6 LEU B 230 ARG B 237 0
SHEET 2 AA7 6 SER B 216 GLU B 223 -1 N GLU B 223 O LEU B 230
SHEET 3 AA7 6 THR B 437 LEU B 444 1 O MET B 439 N LEU B 218
SHEET 4 AA7 6 TYR B 325 ASP B 334 1 N ARG B 331 O ILE B 442
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 ALA B 349 0
SHEET 2 AA9 3 ASN B 397 ALA B 404 -1 O ARG B 401 N TYR B 346
SHEET 3 AA9 3 LEU B 419 SER B 424 -1 O PHE B 421 N PHE B 400
SHEET 1 AB1 2 ALA B 414 TYR B 416 0
SHEET 2 AB1 2 ARG B 446 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 THR C 181 O GLY C 244
SHEET 3 AB2 7 LEU C 108 LEU C 114 1 N LEU C 111 O PHE C 178
SHEET 4 AB2 7 ARG C 78 HIS C 84 1 N CYS C 81 O ILE C 112
SHEET 5 AB2 7 MET C 1 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 SER D 456 N LEU C 42
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 GLU C 436 LEU C 444 1 O MET C 439 N LEU C 218
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 LYS C 312 0
SHEET 2 AB4 2 THR C 317 ILE C 321 -1 O ARG C 318 N VAL C 311
SHEET 1 AB5 3 TYR C 343 ALA C 349 0
SHEET 2 AB5 3 ASN C 397 ALA C 404 -1 O ARG C 401 N TYR C 346
SHEET 3 AB5 3 LEU C 419 SER C 424 -1 O PHE C 421 N PHE C 400
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 MET D 1 VAL D 6 1 N VAL D 3 O TYR D 41
SHEET 4 AB7 7 ARG D 78 HIS D 84 1 O ALA D 80 N ILE D 2
SHEET 5 AB7 7 LEU D 108 LEU D 114 1 O ILE D 112 N CYS D 81
SHEET 6 AB7 7 TYR D 176 THR D 181 1 O PHE D 178 N LEU D 111
SHEET 7 AB7 7 ALA D 242 VAL D 245 1 O GLY D 244 N VAL D 179
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 MET D 439 N LEU D 218
SHEET 4 AB8 6 TYR D 325 ASP D 334 1 N ARG D 331 O ILE D 442
SHEET 5 AB8 6 LYS D 375 ASP D 381 -1 O LEU D 376 N PHE D 330
SHEET 6 AB8 6 PHE D 363 ARG D 368 -1 N GLN D 367 O THR D 377
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 TYR D 343 ALA D 349 0
SHEET 2 AC1 3 ASN D 397 ALA D 404 -1 O ARG D 401 N TYR D 346
SHEET 3 AC1 3 LEU D 419 SER D 424 -1 O PHE D 421 N PHE D 400
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
CISPEP 1 TYR A 405 PRO A 406 0 -1.79
CISPEP 2 TYR B 405 PRO B 406 0 -2.85
CISPEP 3 TYR C 405 PRO C 406 0 -1.29
CISPEP 4 TYR D 405 PRO D 406 0 -0.13
SITE 1 AC1 22 GLN A 125 ARG A 130 VAL A 193 ASN A 194
SITE 2 AC1 22 SER A 195 TYR A 196 ASP A 365 HOH A 650
SITE 3 AC1 22 HOH A 710 HOH A 739 HOH A 759 HOH A 764
SITE 4 AC1 22 HOH A 786 HOH A 879 TYR C 343 LEU C 345
SITE 5 AC1 22 ARG C 366 ARG C 368 LEU C 376 TYR C 378
SITE 6 AC1 22 SND C 501 HOH C 622
SITE 1 AC2 23 ARG A 187 TYR A 190 ALA A 192 VAL A 193
SITE 2 AC2 23 ARG A 318 TYR A 320 HOH A 685 HOH A 742
SITE 3 AC2 23 HOH A 761 HOH A 780 HOH A 823 TYR C 346
SITE 4 AC2 23 LEU C 347 GLU C 355 GLN C 356 ALA C 357
SITE 5 AC2 23 LEU C 358 ALA C 360 GLY C 361 PHE C 362
SITE 6 AC2 23 PHE C 363 ARG C 366 TYR C 378
SITE 1 AC3 7 THR A 16 SER A 252 GLY A 253 ARG A 260
SITE 2 AC3 7 HOH A 694 HOH A 749 HOH A 826
SITE 1 AC4 20 GLN B 125 ARG B 130 VAL B 193 ASN B 194
SITE 2 AC4 20 SER B 195 TYR B 196 ASP B 365 HOH B 620
SITE 3 AC4 20 HOH B 691 HOH B 759 HOH B 807 HOH B 865
SITE 4 AC4 20 TYR D 343 LEU D 345 ARG D 366 ARG D 368
SITE 5 AC4 20 LEU D 376 TYR D 378 SND D 501 HOH D 808
SITE 1 AC5 23 ARG B 187 TYR B 190 ALA B 192 VAL B 193
SITE 2 AC5 23 ARG B 318 TYR B 320 HOH B 676 HOH B 722
SITE 3 AC5 23 HOH B 744 HOH B 762 HOH B 813 TYR D 346
SITE 4 AC5 23 LEU D 347 GLU D 355 GLN D 356 ALA D 357
SITE 5 AC5 23 LEU D 358 ALA D 360 GLY D 361 PHE D 362
SITE 6 AC5 23 PHE D 363 ARG D 366 TYR D 378
SITE 1 AC6 25 TYR B 346 LEU B 347 GLU B 355 GLN B 356
SITE 2 AC6 25 ALA B 357 LEU B 358 ALA B 360 GLY B 361
SITE 3 AC6 25 PHE B 362 PHE B 363 ARG B 366 TYR B 378
SITE 4 AC6 25 HOH B 683 HOH B 725 HOH B 735 HOH B 763
SITE 5 AC6 25 HOH B 818 ARG D 187 TYR D 190 ALA D 192
SITE 6 AC6 25 VAL D 193 ARG D 318 TYR D 320 HOH D 759
SITE 7 AC6 25 HOH D 823
SITE 1 AC7 6 THR B 16 SER B 252 GLY B 253 ARG B 260
SITE 2 AC7 6 HOH B 635 HOH B 754
SITE 1 AC8 21 TYR A 343 LEU A 345 ARG A 366 ARG A 368
SITE 2 AC8 21 LEU A 376 TYR A 378 SND A 501 GLN C 125
SITE 3 AC8 21 ARG C 130 ASN C 194 SER C 195 TYR C 196
SITE 4 AC8 21 ASP C 365 HOH C 622 HOH C 678 HOH C 711
SITE 5 AC8 21 HOH C 723 HOH C 739 HOH C 767 HOH C 811
SITE 6 AC8 21 HOH C 821
SITE 1 AC9 22 TYR A 346 LEU A 347 GLU A 355 GLN A 356
SITE 2 AC9 22 ALA A 357 LEU A 358 ALA A 360 GLY A 361
SITE 3 AC9 22 PHE A 362 PHE A 363 ARG A 366 TYR A 378
SITE 4 AC9 22 ARG C 187 TYR C 190 ALA C 192 VAL C 193
SITE 5 AC9 22 ARG C 318 TYR C 320 HOH C 695 HOH C 718
SITE 6 AC9 22 HOH C 719 HOH C 778
SITE 1 AD1 9 THR C 16 HIS C 84 SER C 252 GLY C 253
SITE 2 AD1 9 ARG C 260 HOH C 632 HOH C 636 HOH C 709
SITE 3 AD1 9 HOH C 799
SITE 1 AD2 26 TYR B 343 LEU B 345 ARG B 366 ARG B 368
SITE 2 AD2 26 LEU B 376 TYR B 378 SND B 501 HOH B 620
SITE 3 AD2 26 HOH B 623 GLN D 125 ARG D 130 VAL D 193
SITE 4 AD2 26 ASN D 194 SER D 195 TYR D 196 ASP D 365
SITE 5 AD2 26 ARG D 366 HOH D 610 HOH D 612 HOH D 661
SITE 6 AD2 26 HOH D 750 HOH D 759 HOH D 775 HOH D 780
SITE 7 AD2 26 HOH D 792 HOH D 856
SITE 1 AD3 6 THR D 16 SER D 252 GLY D 253 ARG D 260
SITE 2 AD3 6 HOH D 629 HOH D 636
CRYST1 75.831 90.725 92.790 78.44 90.26 75.41 P 1 4
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 0.013187 -0.003433 0.000791 0.00000
SCALE2 0.000000 0.011390 -0.002424 0.00000
SCALE3 0.000000 0.000000 0.011019 0.00000
TER 7465 ASP A 474
TER 14973 ASP B 474
TER 22411 ASP C 474
TER 29856 ASP D 474
MASTER 730 0 12 68 80 0 58 616886 4 619 152
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