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HEADER HYDROLASE 11-APR-24 9BD4
TITLE YJFP, KLEBSIELLA PNEUMONIAE SERINE HYDROLASE, UNBOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.23;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N-TERMINAL GPG/C-TERMINAL A. EXPRESSION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: CK244_008325, NCTC13465_04963, NCTC5052_05330, NCTC9601_05351,
SOURCE 5 NCTC9617_04952, NCTC9645_01577, NCTC9661_05640, SAMEA3512100_04172,
SOURCE 6 SAMEA4873632_04766;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS SERINE HYDROLASE, KLEBSIELLA PNEUMONIAE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.T.RANDALL,M.FELLNER
REVDAT 1 30-APR-25 9BD4 0
JRNL AUTH G.T.RANDALL
JRNL TITL KLEBSIELLA PNEUMONIAE SERINE HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 106730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5335
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 45.1100 - 4.0400 1.00 3538 161 0.1431 0.1481
REMARK 3 2 4.0400 - 3.2100 1.00 3459 188 0.1474 0.1448
REMARK 3 3 3.2100 - 2.8000 1.00 3434 166 0.1596 0.1725
REMARK 3 4 2.8000 - 2.5400 1.00 3439 180 0.1609 0.1632
REMARK 3 5 2.5400 - 2.3600 1.00 3434 180 0.1554 0.1494
REMARK 3 6 2.3600 - 2.2200 1.00 3461 170 0.1545 0.1715
REMARK 3 7 2.2200 - 2.1100 1.00 3410 177 0.1532 0.1766
REMARK 3 8 2.1100 - 2.0200 1.00 3426 169 0.1469 0.1706
REMARK 3 9 2.0200 - 1.9400 1.00 3414 178 0.1524 0.1919
REMARK 3 10 1.9400 - 1.8700 1.00 3411 181 0.1475 0.1803
REMARK 3 11 1.8700 - 1.8200 1.00 3410 139 0.1515 0.1707
REMARK 3 12 1.8200 - 1.7600 1.00 3394 190 0.1488 0.1728
REMARK 3 13 1.7600 - 1.7200 0.99 3387 179 0.1517 0.1586
REMARK 3 14 1.7200 - 1.6800 0.99 3409 173 0.1537 0.1711
REMARK 3 15 1.6800 - 1.6400 0.99 3376 205 0.1642 0.2049
REMARK 3 16 1.6400 - 1.6000 0.99 3372 177 0.1577 0.1860
REMARK 3 17 1.6000 - 1.5700 0.99 3361 201 0.1551 0.1646
REMARK 3 18 1.5700 - 1.5400 0.99 3344 180 0.1576 0.1787
REMARK 3 19 1.5400 - 1.5100 0.99 3376 188 0.1702 0.1887
REMARK 3 20 1.5100 - 1.4900 0.99 3342 197 0.1784 0.1800
REMARK 3 21 1.4900 - 1.4600 0.98 3353 186 0.1843 0.1961
REMARK 3 22 1.4600 - 1.4400 0.98 3342 179 0.2017 0.2245
REMARK 3 23 1.4400 - 1.4200 0.99 3323 186 0.2163 0.2386
REMARK 3 24 1.4200 - 1.4000 0.98 3308 173 0.2156 0.2449
REMARK 3 25 1.4000 - 1.3800 0.98 3402 164 0.2195 0.2301
REMARK 3 26 1.3800 - 1.3600 0.98 3318 145 0.2241 0.2185
REMARK 3 27 1.3600 - 1.3500 0.97 3323 198 0.2333 0.2461
REMARK 3 28 1.3500 - 1.3300 0.97 3294 168 0.2345 0.2252
REMARK 3 29 1.3300 - 1.3100 0.97 3281 173 0.2420 0.2881
REMARK 3 30 1.3100 - 1.3000 0.95 3254 184 0.2657 0.2809
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 4004
REMARK 3 ANGLE : 0.886 5460
REMARK 3 CHIRALITY : 0.088 580
REMARK 3 PLANARITY : 0.008 730
REMARK 3 DIHEDRAL : 5.478 556
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0752 -4.5292 -10.3029
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.1290
REMARK 3 T33: 0.1350 T12: 0.0295
REMARK 3 T13: 0.0303 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 2.8372 L22: 6.1470
REMARK 3 L33: 3.7483 L12: 2.7088
REMARK 3 L13: -1.4470 L23: -2.9147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: 0.0069 S13: -0.1877
REMARK 3 S21: -0.2817 S22: -0.0890 S23: -0.3408
REMARK 3 S31: 0.2064 S32: 0.2736 S33: 0.1473
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3981 -0.1578 -6.6654
REMARK 3 T TENSOR
REMARK 3 T11: 0.0644 T22: 0.0784
REMARK 3 T33: 0.0902 T12: 0.0206
REMARK 3 T13: 0.0099 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.5255 L22: 1.6029
REMARK 3 L33: 1.7121 L12: 1.2585
REMARK 3 L13: 0.3546 L23: 0.2586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0371 S13: 0.0004
REMARK 3 S21: -0.0150 S22: 0.0116 S23: -0.0858
REMARK 3 S31: -0.0250 S32: 0.1243 S33: 0.0041
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6127 -16.0213 -6.2592
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.0962
REMARK 3 T33: 0.1621 T12: -0.0043
REMARK 3 T13: 0.0097 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 6.1908 L22: 2.3837
REMARK 3 L33: 6.0997 L12: 0.1214
REMARK 3 L13: 0.6034 L23: 0.3919
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: 0.3239 S13: -0.5808
REMARK 3 S21: -0.1178 S22: 0.0075 S23: 0.0511
REMARK 3 S31: 0.4507 S32: -0.1566 S33: -0.0714
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5860 -12.8855 1.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0759 T22: 0.0324
REMARK 3 T33: 0.0759 T12: 0.0023
REMARK 3 T13: 0.0115 T23: 0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 5.3318 L22: 5.0120
REMARK 3 L33: 3.0113 L12: 2.2157
REMARK 3 L13: -0.3355 L23: 2.9205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: -0.0599 S13: -0.1641
REMARK 3 S21: 0.0059 S22: -0.0411 S23: 0.0702
REMARK 3 S31: 0.0394 S32: -0.0805 S33: 0.0406
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7595 -4.5005 3.5048
REMARK 3 T TENSOR
REMARK 3 T11: 0.0845 T22: 0.1345
REMARK 3 T33: 0.1043 T12: 0.0167
REMARK 3 T13: -0.0279 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 6.8862 L22: 4.4919
REMARK 3 L33: 2.3274 L12: 2.4102
REMARK 3 L13: -1.4355 L23: -2.1062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.1657 S13: -0.1910
REMARK 3 S21: 0.1380 S22: -0.1583 S23: -0.3501
REMARK 3 S31: -0.0217 S32: 0.2950 S33: 0.1094
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5859 -0.4987 6.9301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0947 T22: 0.0916
REMARK 3 T33: 0.0954 T12: 0.0019
REMARK 3 T13: 0.0037 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.3371 L22: 0.6241
REMARK 3 L33: 0.6240 L12: 0.4367
REMARK 3 L13: 0.2654 L23: 0.0746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.0768 S13: -0.0623
REMARK 3 S21: 0.1038 S22: -0.0372 S23: -0.0050
REMARK 3 S31: 0.0362 S32: -0.0045 S33: -0.0061
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3957 10.3802 9.6770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0979 T22: 0.1178
REMARK 3 T33: 0.1130 T12: 0.0103
REMARK 3 T13: -0.0034 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 6.8853 L22: 3.5564
REMARK 3 L33: 7.2888 L12: 2.3998
REMARK 3 L13: 5.4889 L23: 4.2839
REMARK 3 S TENSOR
REMARK 3 S11: -0.2206 S12: -0.3076 S13: 0.4165
REMARK 3 S21: -0.0948 S22: -0.0765 S23: 0.2295
REMARK 3 S31: -0.4001 S32: -0.2430 S33: 0.2851
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6961 11.9745 -1.0527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0734 T22: 0.0465
REMARK 3 T33: 0.0892 T12: 0.0051
REMARK 3 T13: 0.0002 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.6717 L22: 1.0475
REMARK 3 L33: 2.2774 L12: 0.1173
REMARK 3 L13: 0.6296 L23: 0.2148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: -0.0553 S13: 0.1552
REMARK 3 S21: 0.0138 S22: -0.0184 S23: -0.0146
REMARK 3 S31: -0.1316 S32: 0.0207 S33: 0.0664
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4219 4.8547 -23.1249
REMARK 3 T TENSOR
REMARK 3 T11: 0.0790 T22: 0.1759
REMARK 3 T33: 0.1296 T12: -0.0339
REMARK 3 T13: -0.0015 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 5.1146 L22: 6.2526
REMARK 3 L33: 4.7012 L12: -3.4778
REMARK 3 L13: 0.7300 L23: -1.4320
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: 0.2499 S13: 0.2677
REMARK 3 S21: -0.0809 S22: -0.1354 S23: -0.3865
REMARK 3 S31: -0.1759 S32: 0.3797 S33: 0.1298
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7094 5.2261 -23.2919
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0875
REMARK 3 T33: 0.0624 T12: -0.0160
REMARK 3 T13: 0.0011 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.6532 L22: 1.9317
REMARK 3 L33: 1.9648 L12: -0.8125
REMARK 3 L13: 0.0648 L23: 0.1835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: -0.0078 S13: 0.0697
REMARK 3 S21: -0.0056 S22: 0.0732 S23: -0.1007
REMARK 3 S31: -0.0348 S32: 0.1675 S33: -0.0217
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4066 16.0461 -26.9070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1180 T22: 0.0546
REMARK 3 T33: 0.0950 T12: 0.0085
REMARK 3 T13: -0.0376 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 5.8463 L22: 6.0635
REMARK 3 L33: 2.4075 L12: -0.3115
REMARK 3 L13: -0.3760 L23: 2.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0888 S12: -0.0882 S13: 0.1831
REMARK 3 S21: 0.0131 S22: -0.0261 S23: 0.1600
REMARK 3 S31: -0.1786 S32: -0.2268 S33: 0.0880
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1865 5.1098 -36.2489
REMARK 3 T TENSOR
REMARK 3 T11: 0.1597 T22: 0.2703
REMARK 3 T33: 0.1048 T12: -0.0426
REMARK 3 T13: 0.0334 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 5.5972 L22: 4.0506
REMARK 3 L33: 1.4003 L12: -2.6246
REMARK 3 L13: -0.0178 L23: -1.4016
REMARK 3 S TENSOR
REMARK 3 S11: 0.1011 S12: 0.4584 S13: 0.1242
REMARK 3 S21: -0.2436 S22: -0.2414 S23: -0.2536
REMARK 3 S31: -0.0200 S32: 0.4361 S33: 0.1313
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3419 1.7630 -32.8695
REMARK 3 T TENSOR
REMARK 3 T11: 0.0875 T22: 0.0892
REMARK 3 T33: 0.0888 T12: -0.0055
REMARK 3 T13: 0.0037 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.7276 L22: 2.6045
REMARK 3 L33: 1.6188 L12: -0.2613
REMARK 3 L13: 0.8072 L23: -0.4547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0449 S12: 0.0839 S13: -0.0047
REMARK 3 S21: -0.0755 S22: 0.0149 S23: 0.0561
REMARK 3 S31: 0.0479 S32: 0.0758 S33: 0.0237
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 139 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0545 11.1837 -29.1372
REMARK 3 T TENSOR
REMARK 3 T11: 0.1371 T22: 0.1451
REMARK 3 T33: 0.1779 T12: 0.0310
REMARK 3 T13: -0.0445 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 2.7229 L22: 5.0353
REMARK 3 L33: 2.1918 L12: -0.9952
REMARK 3 L13: -0.8709 L23: 0.4472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.0874 S13: 0.3374
REMARK 3 S21: -0.3493 S22: -0.0756 S23: 0.3689
REMARK 3 S31: -0.3756 S32: -0.3864 S33: 0.0576
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7564 9.0051 -39.2209
REMARK 3 T TENSOR
REMARK 3 T11: 0.1621 T22: 0.1295
REMARK 3 T33: 0.1100 T12: -0.0099
REMARK 3 T13: 0.0041 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 4.9086 L22: 2.0220
REMARK 3 L33: 5.5796 L12: 0.5969
REMARK 3 L13: 1.1454 L23: 2.2538
REMARK 3 S TENSOR
REMARK 3 S11: 0.0556 S12: 0.1104 S13: 0.2904
REMARK 3 S21: 0.1749 S22: -0.1276 S23: 0.1713
REMARK 3 S31: -0.3187 S32: -0.1774 S33: 0.0878
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4759 -4.4086 -30.7909
REMARK 3 T TENSOR
REMARK 3 T11: 0.1018 T22: 0.0671
REMARK 3 T33: 0.0986 T12: -0.0213
REMARK 3 T13: 0.0002 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.8566 L22: 1.1521
REMARK 3 L33: 5.3224 L12: -0.4247
REMARK 3 L13: -0.2607 L23: 1.2601
REMARK 3 S TENSOR
REMARK 3 S11: 0.0422 S12: 0.0434 S13: -0.0354
REMARK 3 S21: -0.0739 S22: -0.0828 S23: 0.1266
REMARK 3 S31: 0.1058 S32: -0.3197 S33: 0.0441
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 205 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8265 -8.7084 -25.5336
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.0616
REMARK 3 T33: 0.0929 T12: -0.0088
REMARK 3 T13: 0.0091 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.2675 L22: 1.5638
REMARK 3 L33: 2.4890 L12: -0.2584
REMARK 3 L13: -0.0916 L23: 0.4030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0247 S12: 0.0165 S13: -0.0599
REMARK 3 S21: -0.0212 S22: -0.0132 S23: 0.0315
REMARK 3 S31: 0.2067 S32: -0.0205 S33: 0.0374
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 9BD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1000283121.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106974
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 45.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 2.79400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM SULFATE, 35% W/V PEG
REMARK 280 8,000, SODIUM ACETATE PH 5.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.35300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.09750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.35300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.09750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 437 LIES ON A SPECIAL POSITION.
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 GLY A -1
REMARK 465 PRO A 0
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 GLY B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 317 O HOH A 455 2.11
REMARK 500 O HOH A 443 O HOH A 447 2.11
REMARK 500 O HOH A 312 O HOH A 326 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 39 -157.86 -95.92
REMARK 500 SER A 116 -124.61 64.24
REMARK 500 SER A 116 -124.94 63.34
REMARK 500 PRO A 130 1.89 -69.93
REMARK 500 THR A 150 -37.67 -130.16
REMARK 500 PHE A 152 55.23 39.75
REMARK 500 ARG A 220 -143.35 -92.91
REMARK 500 HIS A 238 -39.12 -134.18
REMARK 500 SER B 39 -157.59 -97.66
REMARK 500 SER B 116 -125.24 64.43
REMARK 500 SER B 116 -124.01 62.42
REMARK 500 PHE B 152 59.54 36.97
REMARK 500 GLN B 170 54.27 -164.07
REMARK 500 ARG B 220 -147.57 -91.56
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9BD4 A 2 239 UNP A0A060VRI4_KLEPN
DBREF2 9BD4 A A0A060VRI4 1 238
DBREF1 9BD4 B 2 239 UNP A0A060VRI4_KLEPN
DBREF2 9BD4 B A0A060VRI4 1 238
SEQADV 9BD4 GLY A -1 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 PRO A 0 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 GLY A 1 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 ALA A 240 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 GLY B -1 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 PRO B 0 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 GLY B 1 UNP A0A060VRI EXPRESSION TAG
SEQADV 9BD4 ALA B 240 UNP A0A060VRI EXPRESSION TAG
SEQRES 1 A 242 GLY PRO GLY MET ILE ALA LEU GLU MET ARG ASN LEU GLY
SEQRES 2 A 242 GLY GLY GLU ILE LEU HIS ALA CYS PRO GLN GLU SER LEU
SEQRES 3 A 242 ASP LYS PRO LEU PRO CYS ILE VAL PHE TYR HIS GLY PHE
SEQRES 4 A 242 THR SER SER LYS LEU VAL TYR SER TYR PHE ALA VAL ALA
SEQRES 5 A 242 LEU ALA GLU ALA GLY PHE ARG VAL ILE MET PRO ASP ALA
SEQRES 6 A 242 PRO GLU HIS GLY ALA ARG TYR GLN GLY ASP GLU ALA GLY
SEQRES 7 A 242 ARG MET GLN ARG PHE TRP PRO ILE LEU GLN GLN ASN PHE
SEQRES 8 A 242 ARG GLU PHE PRO ALA LEU ARG GLU ALA ILE ILE ALA GLU
SEQRES 9 A 242 GLY TRP LEU GLU GLY GLU ARG LEU ALA VAL ALA GLY ALA
SEQRES 10 A 242 SER MET GLY GLY MET THR ALA LEU GLY ILE MET THR HIS
SEQRES 11 A 242 HIS PRO GLU LEU ASN SER VAL ALA CYS LEU MET GLY SER
SEQRES 12 A 242 GLY TYR PHE ARG SER LEU SER GLN THR LEU PHE PRO SER
SEQRES 13 A 242 PRO ASP PHE ASP VAL ASP SER LEU ASN GLU TRP ASP VAL
SEQRES 14 A 242 SER HIS GLN LEU ALA SER LEU ALA ARG ARG PRO LEU LEU
SEQRES 15 A 242 LEU TRP HIS GLY ASP ALA ASP ASP VAL VAL PRO PRO GLU
SEQRES 16 A 242 GLU THR PHE ARG LEU GLU GLN ALA LEU ARG GLN GLY ASP
SEQRES 17 A 242 LEU ALA ALA ARG LEU THR CYS VAL TRP GLN LYS GLY VAL
SEQRES 18 A 242 ARG HIS ARG ILE THR PRO GLU ALA LEU ALA THR THR VAL
SEQRES 19 A 242 ALA PHE PHE GLN GLN HIS LEU ALA
SEQRES 1 B 242 GLY PRO GLY MET ILE ALA LEU GLU MET ARG ASN LEU GLY
SEQRES 2 B 242 GLY GLY GLU ILE LEU HIS ALA CYS PRO GLN GLU SER LEU
SEQRES 3 B 242 ASP LYS PRO LEU PRO CYS ILE VAL PHE TYR HIS GLY PHE
SEQRES 4 B 242 THR SER SER LYS LEU VAL TYR SER TYR PHE ALA VAL ALA
SEQRES 5 B 242 LEU ALA GLU ALA GLY PHE ARG VAL ILE MET PRO ASP ALA
SEQRES 6 B 242 PRO GLU HIS GLY ALA ARG TYR GLN GLY ASP GLU ALA GLY
SEQRES 7 B 242 ARG MET GLN ARG PHE TRP PRO ILE LEU GLN GLN ASN PHE
SEQRES 8 B 242 ARG GLU PHE PRO ALA LEU ARG GLU ALA ILE ILE ALA GLU
SEQRES 9 B 242 GLY TRP LEU GLU GLY GLU ARG LEU ALA VAL ALA GLY ALA
SEQRES 10 B 242 SER MET GLY GLY MET THR ALA LEU GLY ILE MET THR HIS
SEQRES 11 B 242 HIS PRO GLU LEU ASN SER VAL ALA CYS LEU MET GLY SER
SEQRES 12 B 242 GLY TYR PHE ARG SER LEU SER GLN THR LEU PHE PRO SER
SEQRES 13 B 242 PRO ASP PHE ASP VAL ASP SER LEU ASN GLU TRP ASP VAL
SEQRES 14 B 242 SER HIS GLN LEU ALA SER LEU ALA ARG ARG PRO LEU LEU
SEQRES 15 B 242 LEU TRP HIS GLY ASP ALA ASP ASP VAL VAL PRO PRO GLU
SEQRES 16 B 242 GLU THR PHE ARG LEU GLU GLN ALA LEU ARG GLN GLY ASP
SEQRES 17 B 242 LEU ALA ALA ARG LEU THR CYS VAL TRP GLN LYS GLY VAL
SEQRES 18 B 242 ARG HIS ARG ILE THR PRO GLU ALA LEU ALA THR THR VAL
SEQRES 19 B 242 ALA PHE PHE GLN GLN HIS LEU ALA
FORMUL 3 HOH *305(H2 O)
HELIX 1 AA1 GLU A 22 LEU A 24 5 3
HELIX 2 AA2 SER A 45 ALA A 54 1 10
HELIX 3 AA3 HIS A 66 TYR A 70 5 5
HELIX 4 AA4 ASP A 73 GLN A 79 1 7
HELIX 5 AA5 ARG A 80 GLU A 91 1 12
HELIX 6 AA6 GLU A 91 GLU A 102 1 12
HELIX 7 AA7 SER A 116 HIS A 129 1 14
HELIX 8 AA8 TYR A 143 SER A 148 1 6
HELIX 9 AA9 ASP A 158 ASN A 163 5 6
HELIX 10 AB1 ASP A 166 HIS A 169 5 4
HELIX 11 AB2 GLN A 170 ALA A 175 1 6
HELIX 12 AB3 PRO A 191 GLY A 205 1 15
HELIX 13 AB4 THR A 224 LEU A 239 1 16
HELIX 14 AB5 GLU B 22 LEU B 24 5 3
HELIX 15 AB6 SER B 45 ALA B 54 1 10
HELIX 16 AB7 HIS B 66 TYR B 70 5 5
HELIX 17 AB8 ASP B 73 GLN B 79 1 7
HELIX 18 AB9 ARG B 80 GLU B 91 1 12
HELIX 19 AC1 GLU B 91 GLU B 102 1 12
HELIX 20 AC2 SER B 116 HIS B 129 1 14
HELIX 21 AC3 TYR B 143 SER B 148 1 6
HELIX 22 AC4 ASP B 158 ASN B 163 5 6
HELIX 23 AC5 ASP B 166 ARG B 176 5 11
HELIX 24 AC6 PRO B 192 GLY B 205 1 14
HELIX 25 AC7 THR B 224 ALA B 240 1 17
SHEET 1 AA116 LEU A 211 GLN A 216 0
SHEET 2 AA116 LEU A 179 GLY A 184 1 N LEU A 179 O THR A 212
SHEET 3 AA116 VAL A 135 LEU A 138 1 N CYS A 137 O LEU A 180
SHEET 4 AA116 LEU A 105 ALA A 115 1 N GLY A 114 O LEU A 138
SHEET 5 AA116 LEU A 28 TYR A 34 1 N VAL A 32 O ALA A 113
SHEET 6 AA116 ARG A 57 PRO A 61 1 O ARG A 57 N PRO A 29
SHEET 7 AA116 GLY A 13 PRO A 20 -1 N LEU A 16 O MET A 60
SHEET 8 AA116 ILE A 3 LEU A 10 -1 N ARG A 8 O ILE A 15
SHEET 9 AA116 ILE B 3 LEU B 10 -1 O ILE B 3 N LEU A 5
SHEET 10 AA116 GLY B 13 PRO B 20 -1 O ILE B 15 N ARG B 8
SHEET 11 AA116 ARG B 57 PRO B 61 -1 O VAL B 58 N ALA B 18
SHEET 12 AA116 LEU B 28 TYR B 34 1 N ILE B 31 O ILE B 59
SHEET 13 AA116 LEU B 105 ALA B 115 1 O ALA B 113 N VAL B 32
SHEET 14 AA116 VAL B 135 LEU B 138 1 O LEU B 138 N GLY B 114
SHEET 15 AA116 LEU B 179 GLY B 184 1 O LEU B 180 N CYS B 137
SHEET 16 AA116 LEU B 211 GLN B 216 1 O THR B 212 N LEU B 179
CRYST1 102.706 68.195 65.363 90.00 77.16 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009737 0.000000 -0.002219 0.00000
SCALE2 0.000000 0.014664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015692 0.00000
TER 1948 ALA A 240
TER 3890 ALA B 240
MASTER 540 0 0 25 16 0 0 6 4055 2 0 38
END |