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HEADER HYDROLASE 03-JUN-22 8A2C
TITLE THE CRYSTAL STRUCTURE OF THE S178A MUTANT OF PET40, A PETASE ENZYME
TITLE 2 FROM AN UNCLASSIFIED AMYCOLATOPSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PET40 S178A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCLASSIFIED AMYCOLATOPSIS;
SOURCE 3 ORGANISM_TAXID: 2618356;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, PET, ENZYME, HYDROLASE, ESTERASE, PLASTIC, DEGRADATION,
KEYWDS 2 BIOTECH, ENZYME EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.COSTANZI,V.APPLEGATE,A.PORT,S.H.J.SMITS
REVDAT 1 14-JUN-23 8A2C 0
JRNL AUTH H.ZHANG,R.DIERKES,P.PEREZ-GARCIA,V.APPLEGATE,E.COSTANZI,
JRNL AUTH 2 K.PARTUS,M.GURSCHKE,C.SCHMEISSER,S.H.J.SMITS,J.CHOW,
JRNL AUTH 3 W.R.STREIT
JRNL TITL THE METAGENOME-DERIVED ESTERASE PET40 HYDROLYSES
JRNL TITL 2 POLYETHYLENE TEREPHTHALATE (PET) AND IS WELL CONSERVED IN
JRNL TITL 3 THE GC-RICH GRAM-POSITIVES AMYCOLATOPSIS AND STREPTOMYCES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 60973
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3063
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 31.5100 - 4.4800 0.93 2592 99 0.1603 0.1657
REMARK 3 2 4.4800 - 3.5600 0.96 2605 130 0.1142 0.1416
REMARK 3 3 3.5600 - 3.1100 0.97 2636 131 0.1272 0.1521
REMARK 3 4 3.1100 - 2.8200 0.98 2639 135 0.1300 0.1640
REMARK 3 5 2.8200 - 2.6200 0.97 2652 119 0.1280 0.1596
REMARK 3 6 2.6200 - 2.4700 0.98 2642 138 0.1273 0.1751
REMARK 3 7 2.4700 - 2.3400 0.99 2626 168 0.1279 0.1714
REMARK 3 8 2.3400 - 2.2400 0.99 2662 139 0.1316 0.1639
REMARK 3 9 2.2400 - 2.1600 0.99 2671 138 0.1332 0.1899
REMARK 3 10 2.1600 - 2.0800 0.98 2590 163 0.1405 0.1908
REMARK 3 11 2.0800 - 2.0200 0.99 2656 146 0.1454 0.1740
REMARK 3 12 2.0200 - 1.9600 0.98 2677 143 0.1447 0.1641
REMARK 3 13 1.9600 - 1.9100 0.98 2562 160 0.1622 0.2203
REMARK 3 14 1.9100 - 1.8600 0.98 2663 130 0.1680 0.2020
REMARK 3 15 1.8600 - 1.8200 0.98 2642 147 0.1775 0.1923
REMARK 3 16 1.8200 - 1.7800 0.98 2608 148 0.1787 0.2290
REMARK 3 17 1.7800 - 1.7400 0.98 2642 151 0.1928 0.2147
REMARK 3 18 1.7400 - 1.7100 0.98 2576 154 0.2017 0.2370
REMARK 3 19 1.7100 - 1.6800 0.98 2690 145 0.2167 0.2802
REMARK 3 20 1.6800 - 1.6500 0.98 2609 114 0.2229 0.2458
REMARK 3 21 1.6500 - 1.6300 0.98 2664 133 0.2386 0.2526
REMARK 3 22 1.6200 - 1.6000 0.97 2606 132 0.2455 0.2584
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) : 0.156
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.164
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 4219
REMARK 3 ANGLE : 1.140 5759
REMARK 3 CHIRALITY : 0.057 655
REMARK 3 PLANARITY : 0.010 739
REMARK 3 DIHEDRAL : 12.373 1488
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9147 2.4076 18.1607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.1095
REMARK 3 T33: 0.0884 T12: 0.0023
REMARK 3 T13: 0.0141 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.0546 L22: 1.3571
REMARK 3 L33: 1.2828 L12: -0.2704
REMARK 3 L13: -0.0540 L23: 0.0173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0707 S12: -0.1382 S13: -0.0177
REMARK 3 S21: 0.0674 S22: 0.0737 S23: 0.0286
REMARK 3 S31: 0.0365 S32: -0.0024 S33: 0.0061
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9490 -0.3334 15.7273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.1030
REMARK 3 T33: 0.0919 T12: -0.0024
REMARK 3 T13: -0.0054 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.9276 L22: 0.7874
REMARK 3 L33: 0.6921 L12: -0.1825
REMARK 3 L13: 0.0790 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: -0.0660 S13: -0.0189
REMARK 3 S21: 0.0329 S22: 0.0166 S23: -0.0167
REMARK 3 S31: 0.0366 S32: 0.0481 S33: 0.0138
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1623 -5.9294 2.5585
REMARK 3 T TENSOR
REMARK 3 T11: 0.1201 T22: 0.1406
REMARK 3 T33: 0.0761 T12: 0.0171
REMARK 3 T13: -0.0267 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 4.4290 L22: 3.3222
REMARK 3 L33: 2.8668 L12: -0.9514
REMARK 3 L13: -1.9618 L23: -0.8543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0498 S12: 0.1306 S13: -0.2684
REMARK 3 S21: -0.2031 S22: -0.0274 S23: -0.2378
REMARK 3 S31: 0.1834 S32: 0.1215 S33: 0.0767
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1042 3.0580 -0.0417
REMARK 3 T TENSOR
REMARK 3 T11: 0.1080 T22: 0.1187
REMARK 3 T33: 0.0934 T12: 0.0014
REMARK 3 T13: -0.0172 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.8287 L22: 0.9390
REMARK 3 L33: 1.1785 L12: 0.1856
REMARK 3 L13: -0.3692 L23: -0.2693
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.0853 S13: 0.0353
REMARK 3 S21: -0.0574 S22: -0.0165 S23: -0.0399
REMARK 3 S31: 0.0180 S32: 0.0665 S33: 0.0229
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7435 -0.6261 -3.5620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1429 T22: 0.1347
REMARK 3 T33: 0.1152 T12: -0.0035
REMARK 3 T13: -0.0328 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 3.1906 L22: 0.7707
REMARK 3 L33: 3.1490 L12: 1.4793
REMARK 3 L13: -2.5390 L23: -0.8593
REMARK 3 S TENSOR
REMARK 3 S11: -0.2188 S12: 0.2740 S13: -0.1000
REMARK 3 S21: -0.1161 S22: 0.1702 S23: -0.0155
REMARK 3 S31: 0.2917 S32: -0.2059 S33: 0.0614
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 398 THROUGH 403 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9120 -1.3292 -12.8170
REMARK 3 T TENSOR
REMARK 3 T11: 0.3985 T22: 0.3840
REMARK 3 T33: 0.4525 T12: -0.0708
REMARK 3 T13: -0.0754 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 6.4762 L22: 2.0033
REMARK 3 L33: 7.3517 L12: 0.6982
REMARK 3 L13: 1.7852 L23: -0.3543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0939 S12: 0.9197 S13: -0.0403
REMARK 3 S21: -0.0896 S22: -0.0133 S23: 0.1064
REMARK 3 S31: -0.0594 S32: 0.2429 S33: 0.1756
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9244 -42.0890 16.6347
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: 0.1572
REMARK 3 T33: 0.1660 T12: -0.0138
REMARK 3 T13: -0.0071 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.2258 L22: 0.7017
REMARK 3 L33: 1.3400 L12: 0.1275
REMARK 3 L13: 0.2560 L23: -0.4226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.0746 S13: -0.0387
REMARK 3 S21: 0.0073 S22: -0.0153 S23: 0.0058
REMARK 3 S31: 0.0426 S32: -0.0933 S33: 0.0422
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9753 -26.0991 2.3906
REMARK 3 T TENSOR
REMARK 3 T11: 0.2025 T22: 0.1869
REMARK 3 T33: 0.1695 T12: -0.0274
REMARK 3 T13: 0.0460 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 3.8563 L22: 6.8793
REMARK 3 L33: 2.2900 L12: 3.1800
REMARK 3 L13: -0.8775 L23: 0.2645
REMARK 3 S TENSOR
REMARK 3 S11: -0.2376 S12: 0.2343 S13: -0.0928
REMARK 3 S21: -0.8203 S22: 0.2978 S23: -0.7265
REMARK 3 S31: -0.2819 S32: 0.1510 S33: -0.0049
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 88 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5791 -30.4912 11.3037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1147 T22: 0.1487
REMARK 3 T33: 0.1580 T12: -0.0040
REMARK 3 T13: 0.0256 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.4377 L22: 1.3298
REMARK 3 L33: 0.4007 L12: 0.2714
REMARK 3 L13: 0.1633 L23: 0.0881
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: -0.0420 S13: -0.0125
REMARK 3 S21: -0.0582 S22: -0.0295 S23: -0.1446
REMARK 3 S31: -0.0161 S32: 0.0352 S33: 0.0220
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4061 -19.3948 9.5696
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.1284
REMARK 3 T33: 0.1620 T12: -0.0060
REMARK 3 T13: 0.0302 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.9940 L22: 1.4266
REMARK 3 L33: 4.3861 L12: 0.7382
REMARK 3 L13: 2.7568 L23: 0.8489
REMARK 3 S TENSOR
REMARK 3 S11: -0.1611 S12: 0.0537 S13: 0.0993
REMARK 3 S21: -0.1532 S22: 0.0605 S23: -0.1138
REMARK 3 S31: -0.2684 S32: 0.0621 S33: 0.0899
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4084 -27.0550 7.9430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.0667
REMARK 3 T33: 0.1090 T12: -0.0147
REMARK 3 T13: 0.0260 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 3.7291 L22: 1.4092
REMARK 3 L33: 1.7211 L12: 0.6260
REMARK 3 L13: 1.7420 L23: 0.6817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0339 S12: 0.0092 S13: 0.0132
REMARK 3 S21: -0.2596 S22: 0.0201 S23: 0.0286
REMARK 3 S31: -0.0562 S32: -0.0208 S33: 0.0124
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 179 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2820 -21.1476 27.4446
REMARK 3 T TENSOR
REMARK 3 T11: 0.0934 T22: 0.1046
REMARK 3 T33: 0.1317 T12: -0.0021
REMARK 3 T13: -0.0028 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2774 L22: 1.9000
REMARK 3 L33: 1.8818 L12: -0.1201
REMARK 3 L13: 0.5827 L23: -0.6426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: -0.0474 S13: 0.0422
REMARK 3 S21: 0.1868 S22: -0.0016 S23: -0.0423
REMARK 3 S31: -0.1808 S32: 0.0038 S33: 0.0440
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 252 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6372 -34.2277 24.6594
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.0960
REMARK 3 T33: 0.1070 T12: 0.0008
REMARK 3 T13: -0.0003 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.8632 L22: 2.1931
REMARK 3 L33: 2.2964 L12: 0.2045
REMARK 3 L13: 0.7305 L23: -0.2130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0827 S13: -0.0742
REMARK 3 S21: 0.0451 S22: 0.0239 S23: -0.1298
REMARK 3 S31: 0.1463 S32: 0.0912 S33: -0.0213
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3524 -34.7791 30.4170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1273 T22: 0.0990
REMARK 3 T33: 0.1183 T12: 0.0007
REMARK 3 T13: 0.0109 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 2.6960 L22: 0.5154
REMARK 3 L33: 4.5266 L12: 1.1212
REMARK 3 L13: 2.4408 L23: 1.0909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.2522 S13: 0.0283
REMARK 3 S21: 0.0123 S22: -0.0403 S23: 0.0521
REMARK 3 S31: -0.0817 S32: -0.3452 S33: 0.0325
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 398 THROUGH 403 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4542 -29.9586 40.3907
REMARK 3 T TENSOR
REMARK 3 T11: 0.5614 T22: 0.6735
REMARK 3 T33: 0.7383 T12: 0.0208
REMARK 3 T13: -0.0138 T23: 0.0581
REMARK 3 L TENSOR
REMARK 3 L11: 5.9582 L22: 2.8151
REMARK 3 L33: 2.4903 L12: -1.1405
REMARK 3 L13: 1.8569 L23: -0.3010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0756 S12: -0.2399 S13: 0.1546
REMARK 3 S21: 0.1527 S22: -0.0831 S23: 0.1811
REMARK 3 S31: -0.1747 S32: 0.0065 S33: 0.0708
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 8A2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1292123469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-22
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61003
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 110.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07500
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: ALPHAFOLD MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 10% V/V ETHYLENGLYCOL, 0.1 M HEPES PH 7.5, 15% V/V PEG SMEAR
REMARK 280 MEDIUM, 5% V/V 2-PROPANOL, VAPOR DIFFUSION, TEMPERATURE 285K
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 55.00100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 47
REMARK 465 VAL A 390
REMARK 465 ASP A 391
REMARK 465 LYS A 392
REMARK 465 LEU A 393
REMARK 465 ALA A 394
REMARK 465 ALA A 395
REMARK 465 ALA A 396
REMARK 465 LEU A 397
REMARK 465 HIS A 404
REMARK 465 MET B 47
REMARK 465 ALA B 48
REMARK 465 VAL B 390
REMARK 465 ASP B 391
REMARK 465 LYS B 392
REMARK 465 LEU B 393
REMARK 465 ALA B 394
REMARK 465 ALA B 395
REMARK 465 ALA B 396
REMARK 465 LEU B 397
REMARK 465 HIS B 404
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 111 -9.75 72.69
REMARK 500 ALA A 178 -128.46 66.64
REMARK 500 HIS A 232 -83.94 -123.22
REMARK 500 THR B 111 -2.89 71.86
REMARK 500 ALA B 178 -126.08 66.99
REMARK 500 HIS B 232 -83.73 -124.81
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 A1021 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A1022 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A1023 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH B 893 DISTANCE = 5.96 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 613 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 195 OE1
REMARK 620 2 PHE A 277 O 95.0
REMARK 620 3 ASN A 280 OD1 161.1 85.9
REMARK 620 4 HOH A 868 O 73.7 76.3 88.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 506 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 195 OE1
REMARK 620 2 PHE B 277 O 104.3
REMARK 620 3 ASN B 280 OD1 155.3 90.7
REMARK 620 4 HOH B 665 O 76.9 173.3 86.1
REMARK 620 5 HOH B 672 O 64.2 79.9 139.1 106.3
REMARK 620 6 HOH B 717 O 76.7 79.9 86.8 94.1 129.4
REMARK 620 N 1 2 3 4 5
DBREF 8A2C A 47 404 PDB 8A2C 8A2C 47 404
DBREF 8A2C B 47 404 PDB 8A2C 8A2C 47 404
SEQRES 1 A 278 MET ALA GLU ASN PRO TYR GLU ARG GLY PRO ALA PRO THR
SEQRES 2 A 278 THR SER SER ILE GLU ALA SER ARG GLY SER PHE ALA THR
SEQRES 3 A 278 SER THR VAL THR VAL SER ARG LEU ALA VAL SER GLY PHE
SEQRES 4 A 278 GLY GLY GLY THR ILE TYR TYR PRO THR SER THR THR ALA
SEQRES 5 A 278 GLY THR PHE GLY ALA ILE SER ILE ALA PRO GLY PHE THR
SEQRES 6 A 278 ALA LEU GLN SER SER ILE ALA TRP LEU GLY PRO ARG LEU
SEQRES 7 A 278 ALA SER GLN GLY PHE VAL VAL PHE THR ILE ASP THR LEU
SEQRES 8 A 278 THR THR SER ASP GLN PRO ASP SER ARG GLY ARG GLN LEU
SEQRES 9 A 278 LEU ALA ALA LEU ASP TYR LEU THR GLN GLN SER SER VAL
SEQRES 10 A 278 ARG SER ARG ILE ASP SER SER ARG LEU GLY VAL VAL GLY
SEQRES 11 A 278 HIS ALA MET GLY GLY GLY GLY THR LEU GLU ALA ALA ARG
SEQRES 12 A 278 SER ARG PRO SER LEU GLN ALA ALA ILE PRO LEU THR GLY
SEQRES 13 A 278 TRP ASN LEU THR LYS THR TRP SER THR VAL ARG VAL PRO
SEQRES 14 A 278 THR LEU VAL VAL GLY ALA GLN ALA ASP THR VAL ALA PRO
SEQRES 15 A 278 VAL ALA SER HIS SER ILE PRO PHE TYR ASN SER LEU PRO
SEQRES 16 A 278 SER SER LEU ASP LYS ALA TYR LEU GLU LEU ARG GLY ALA
SEQRES 17 A 278 SER HIS PHE ALA PRO ASN SER SER ASN THR THR ILE ALA
SEQRES 18 A 278 LYS TYR THR LEU SER TRP LEU LYS ARG PHE ILE ASP ASN
SEQRES 19 A 278 ASP THR ARG TYR GLU GLN PHE LEU CYS PRO ILE PRO SER
SEQRES 20 A 278 THR SER LEU SER ILE SER ASP TYR ARG GLY ASN CYS PRO
SEQRES 21 A 278 HIS ASN GLY VAL ASP LYS LEU ALA ALA ALA LEU UNK HIS
SEQRES 22 A 278 HIS HIS HIS HIS HIS
SEQRES 1 B 278 MET ALA GLU ASN PRO TYR GLU ARG GLY PRO ALA PRO THR
SEQRES 2 B 278 THR SER SER ILE GLU ALA SER ARG GLY SER PHE ALA THR
SEQRES 3 B 278 SER THR VAL THR VAL SER ARG LEU ALA VAL SER GLY PHE
SEQRES 4 B 278 GLY GLY GLY THR ILE TYR TYR PRO THR SER THR THR ALA
SEQRES 5 B 278 GLY THR PHE GLY ALA ILE SER ILE ALA PRO GLY PHE THR
SEQRES 6 B 278 ALA LEU GLN SER SER ILE ALA TRP LEU GLY PRO ARG LEU
SEQRES 7 B 278 ALA SER GLN GLY PHE VAL VAL PHE THR ILE ASP THR LEU
SEQRES 8 B 278 THR THR SER ASP GLN PRO ASP SER ARG GLY ARG GLN LEU
SEQRES 9 B 278 LEU ALA ALA LEU ASP TYR LEU THR GLN GLN SER SER VAL
SEQRES 10 B 278 ARG SER ARG ILE ASP SER SER ARG LEU GLY VAL VAL GLY
SEQRES 11 B 278 HIS ALA MET GLY GLY GLY GLY THR LEU GLU ALA ALA ARG
SEQRES 12 B 278 SER ARG PRO SER LEU GLN ALA ALA ILE PRO LEU THR GLY
SEQRES 13 B 278 TRP ASN LEU THR LYS THR TRP SER THR VAL ARG VAL PRO
SEQRES 14 B 278 THR LEU VAL VAL GLY ALA GLN ALA ASP THR VAL ALA PRO
SEQRES 15 B 278 VAL ALA SER HIS SER ILE PRO PHE TYR ASN SER LEU PRO
SEQRES 16 B 278 SER SER LEU ASP LYS ALA TYR LEU GLU LEU ARG GLY ALA
SEQRES 17 B 278 SER HIS PHE ALA PRO ASN SER SER ASN THR THR ILE ALA
SEQRES 18 B 278 LYS TYR THR LEU SER TRP LEU LYS ARG PHE ILE ASP ASN
SEQRES 19 B 278 ASP THR ARG TYR GLU GLN PHE LEU CYS PRO ILE PRO SER
SEQRES 20 B 278 THR SER LEU SER ILE SER ASP TYR ARG GLY ASN CYS PRO
SEQRES 21 B 278 HIS ASN GLY VAL ASP LYS LEU ALA ALA ALA LEU UNK HIS
SEQRES 22 B 278 HIS HIS HIS HIS HIS
HET EPE A 601 32
HET EDO A 602 10
HET EDO A 603 10
HET EDO A 604 10
HET EDO A 605 10
HET CL A 606 1
HET CL A 607 1
HET CL A 608 1
HET CL A 609 1
HET CL A 610 1
HET CL A 611 1
HET CL A 612 1
HET MG A 613 1
HET EDO B 501 10
HET EPE B 502 32
HET CL B 503 1
HET CL B 504 1
HET CL B 505 1
HET MG B 506 1
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN EPE HEPES
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EPE 2(C8 H18 N2 O4 S)
FORMUL 4 EDO 5(C2 H6 O2)
FORMUL 8 CL 10(CL 1-)
FORMUL 15 MG 2(MG 2+)
FORMUL 22 HOH *616(H2 O)
HELIX 1 AA1 THR A 59 ALA A 65 1 7
HELIX 2 AA2 SER A 78 VAL A 82 5 5
HELIX 3 AA3 LEU A 113 ALA A 118 5 6
HELIX 4 AA4 TRP A 119 SER A 126 1 8
HELIX 5 AA5 GLN A 142 GLN A 160 1 19
HELIX 6 AA6 VAL A 163 SER A 165 5 3
HELIX 7 AA7 ALA A 178 ARG A 191 1 14
HELIX 8 AA8 HIS A 232 LEU A 240 1 9
HELIX 9 AA9 PHE A 257 SER A 261 5 5
HELIX 10 AB1 ASN A 263 ASP A 279 1 17
HELIX 11 AB2 ASP A 281 ARG A 283 5 3
HELIX 12 AB3 TYR A 284 CYS A 289 1 6
HELIX 13 AB4 THR B 59 ALA B 65 1 7
HELIX 14 AB5 SER B 78 VAL B 82 5 5
HELIX 15 AB6 LEU B 113 ALA B 118 5 6
HELIX 16 AB7 TRP B 119 SER B 126 1 8
HELIX 17 AB8 GLN B 142 GLN B 160 1 19
HELIX 18 AB9 VAL B 163 SER B 165 5 3
HELIX 19 AC1 ALA B 178 ARG B 191 1 14
HELIX 20 AC2 HIS B 232 LEU B 240 1 9
HELIX 21 AC3 PHE B 257 SER B 261 5 5
HELIX 22 AC4 ASN B 263 ASP B 279 1 17
HELIX 23 AC5 ASP B 281 LEU B 288 5 8
SHEET 1 AA1 6 THR A 72 VAL A 77 0
SHEET 2 AA1 6 GLY A 88 PRO A 93 -1 O GLY A 88 N VAL A 77
SHEET 3 AA1 6 VAL A 130 ILE A 134 -1 O VAL A 131 N TYR A 91
SHEET 4 AA1 6 PHE A 101 ALA A 107 1 N ILE A 106 O ILE A 134
SHEET 5 AA1 6 ILE A 167 HIS A 177 1 O ASP A 168 N PHE A 101
SHEET 6 AA1 6 ALA A 196 LEU A 200 1 O LEU A 200 N GLY A 176
SHEET 1 AA2 4 THR A 216 ALA A 221 0
SHEET 2 AA2 4 LYS A 246 LEU A 251 1 O LEU A 251 N GLY A 220
SHEET 3 AA2 4 ILE A 298 ASN A 304 -1 O ASP A 300 N GLU A 250
SHEET 4 AA2 4 HIS A 399 HIS A 402 -1 O HIS A 402 N TYR A 301
SHEET 1 AA3 6 THR B 72 VAL B 77 0
SHEET 2 AA3 6 GLY B 88 PRO B 93 -1 O GLY B 88 N VAL B 77
SHEET 3 AA3 6 VAL B 130 ILE B 134 -1 O VAL B 131 N TYR B 91
SHEET 4 AA3 6 PHE B 101 ALA B 107 1 N ILE B 106 O ILE B 134
SHEET 5 AA3 6 ILE B 167 HIS B 177 1 O ASP B 168 N PHE B 101
SHEET 6 AA3 6 ALA B 196 LEU B 200 1 O LEU B 200 N GLY B 176
SHEET 1 AA4 4 THR B 216 ALA B 221 0
SHEET 2 AA4 4 LYS B 246 LEU B 251 1 O ALA B 247 N VAL B 218
SHEET 3 AA4 4 ILE B 298 ASN B 304 -1 O ARG B 302 N TYR B 248
SHEET 4 AA4 4 HIS B 399 HIS B 402 -1 O HIS B 400 N GLY B 303
SSBOND 1 CYS A 289 CYS A 305 1555 1555 2.12
SSBOND 2 CYS B 289 CYS B 305 1555 1555 2.17
LINK OE1 GLN A 195 MG MG A 613 1555 1555 2.35
LINK O PHE A 277 MG MG A 613 1555 1555 2.49
LINK OD1 ASN A 280 MG MG A 613 1555 1555 2.19
LINK MG MG A 613 O HOH A 868 1555 1555 2.65
LINK OE1 GLN B 195 MG MG B 506 1555 1555 2.26
LINK O PHE B 277 MG MG B 506 1555 1555 2.34
LINK OD1 ASN B 280 MG MG B 506 1555 1555 2.25
LINK MG MG B 506 O HOH B 665 1555 1555 2.14
LINK MG MG B 506 O HOH B 672 1555 1555 2.83
LINK MG MG B 506 O HOH B 717 1555 1555 2.59
CISPEP 1 CYS A 289 PRO A 290 0 -6.02
CISPEP 2 CYS A 305 PRO A 306 0 -1.50
CISPEP 3 CYS B 289 PRO B 290 0 -3.67
CISPEP 4 CYS B 305 PRO B 306 0 -7.60
CRYST1 46.038 110.002 47.962 90.00 95.74 90.00 P 1 21 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 0.021721 0.000000 0.002183 0.00000
SCALE2 0.000000 0.009091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020955 0.00000
TER 4040 HIS A 403
TER 8033 HIS B 403
MASTER 524 0 19 23 20 0 0 6 4698 2 131 44
END |