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HEADER HYDROLASE 09-JAN-20 6VHE
TITLE FPHF, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES F, KT130 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PUTATIVE ESTERASE,TRIBUTYRIN ESTERASE;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: EP54_00010, EQ90_02595, HMPREF3211_01237, NCTC10654_02801,
SOURCE 5 NCTC10702_04070, RK64_00235;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: M1366
KEYWDS FPHF, FLUOROPHOSPHONATE-BINDING, SERINE HYDROLASES, SODIUM BOUND,
KEYWDS 2 ACYL, KT130, INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,P.D.MACE
REVDAT 1 16-SEP-20 6VHE 0
JRNL AUTH M.FELLNER,C.S.LENTZ,S.A.JAMIESON,J.L.BREWSTER,L.CHEN,
JRNL AUTH 2 M.BOGYO,P.D.MACE
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITOR AND SUBSTRATE SPECIFICITY
JRNL TITL 2 OF THE UNIQUE FPH SERINE HYDROLASES OF STAPHYLOCOCCUS
JRNL TITL 3 AUREUS.
JRNL REF ACS INFECT DIS. 2020
JRNL REFN ESSN 2373-8227
JRNL PMID 32865965
JRNL DOI 10.1021/ACSINFECDIS.0C00503
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV-3699
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 77403
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 6997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.2400 - 6.0200 1.00 4549 230 0.1626 0.1995
REMARK 3 2 6.0200 - 4.7800 1.00 4521 265 0.1463 0.1658
REMARK 3 3 4.7800 - 4.1800 1.00 4476 267 0.1184 0.1393
REMARK 3 4 4.1700 - 3.7900 1.00 4537 240 0.1382 0.1886
REMARK 3 5 3.7900 - 3.5200 1.00 4596 207 0.1463 0.1827
REMARK 3 6 3.5200 - 3.3100 1.00 4560 234 0.1566 0.1929
REMARK 3 7 3.3100 - 3.1500 1.00 4531 234 0.1686 0.1937
REMARK 3 8 3.1500 - 3.0100 1.00 4519 256 0.1779 0.2450
REMARK 3 9 3.0100 - 2.9000 1.00 4574 193 0.1783 0.2416
REMARK 3 10 2.9000 - 2.8000 1.00 4517 274 0.1775 0.2123
REMARK 3 11 2.8000 - 2.7100 1.00 4502 259 0.1788 0.2349
REMARK 3 12 2.7100 - 2.6300 1.00 4541 264 0.1753 0.2135
REMARK 3 13 2.6300 - 2.5600 1.00 4487 232 0.1738 0.2253
REMARK 3 14 2.5600 - 2.5000 1.00 4556 249 0.1785 0.2075
REMARK 3 15 2.5000 - 2.4400 1.00 4599 243 0.1727 0.2345
REMARK 3 16 2.4400 - 2.3900 1.00 4525 249 0.1788 0.2508
REMARK 3 17 2.3900 - 2.3400 1.00 4502 233 0.1755 0.2131
REMARK 3 18 2.3400 - 2.3000 1.00 4556 233 0.1785 0.2412
REMARK 3 19 2.3000 - 2.2600 1.00 4532 251 0.1802 0.2229
REMARK 3 20 2.2600 - 2.2200 1.00 4555 204 0.1839 0.2338
REMARK 3 21 2.2200 - 2.1800 1.00 4562 214 0.1870 0.2507
REMARK 3 22 2.1800 - 2.1500 1.00 4608 216 0.2021 0.2799
REMARK 3 23 2.1500 - 2.1200 1.00 4480 251 0.1985 0.2296
REMARK 3 24 2.1200 - 2.0900 1.00 4621 216 0.2014 0.2970
REMARK 3 25 2.0900 - 2.0600 1.00 4551 232 0.2232 0.2567
REMARK 3 26 2.0600 - 2.0300 1.00 4518 222 0.2285 0.2799
REMARK 3 27 2.0300 - 2.0100 1.00 4576 226 0.2394 0.3180
REMARK 3 28 2.0100 - 1.9800 1.00 4527 223 0.2369 0.2903
REMARK 3 29 1.9800 - 1.9600 1.00 4606 194 0.2557 0.2672
REMARK 3 30 1.9600 - 1.9400 0.99 4456 186 0.2717 0.3320
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.86
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 : 29
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2697 25.8529 -10.1819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.1609
REMARK 3 T33: 0.1915 T12: 0.0195
REMARK 3 T13: -0.0015 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 1.2358 L22: 1.6523
REMARK 3 L33: 3.3321 L12: 0.1278
REMARK 3 L13: 0.2841 L23: 0.2165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0739 S12: 0.0247 S13: -0.0639
REMARK 3 S21: -0.0492 S22: -0.0960 S23: 0.0674
REMARK 3 S31: 0.3642 S32: -0.0309 S33: 0.0226
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9385 20.2389 8.3522
REMARK 3 T TENSOR
REMARK 3 T11: 0.4187 T22: 0.3648
REMARK 3 T33: 0.2426 T12: 0.0276
REMARK 3 T13: -0.0279 T23: 0.0798
REMARK 3 L TENSOR
REMARK 3 L11: 0.3770 L22: 6.2743
REMARK 3 L33: 2.8889 L12: 0.7166
REMARK 3 L13: -0.2346 L23: 1.2540
REMARK 3 S TENSOR
REMARK 3 S11: 0.1677 S12: -0.3762 S13: -0.1644
REMARK 3 S21: 1.0385 S22: -0.1305 S23: -0.1928
REMARK 3 S31: 0.6519 S32: 0.3434 S33: -0.0423
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9820 9.9793 -2.9588
REMARK 3 T TENSOR
REMARK 3 T11: 0.4363 T22: 0.2045
REMARK 3 T33: 0.3006 T12: 0.1007
REMARK 3 T13: -0.0160 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 2.8903 L22: 4.3754
REMARK 3 L33: 4.9899 L12: 0.8176
REMARK 3 L13: 0.1687 L23: -2.3009
REMARK 3 S TENSOR
REMARK 3 S11: 0.1437 S12: -0.1075 S13: -0.4169
REMARK 3 S21: 0.1400 S22: -0.2056 S23: -0.1818
REMARK 3 S31: 0.8483 S32: 0.2957 S33: 0.0554
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5056 43.4729 -10.1604
REMARK 3 T TENSOR
REMARK 3 T11: 0.0875 T22: 0.2305
REMARK 3 T33: 0.1926 T12: 0.0213
REMARK 3 T13: 0.0105 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 4.6242 L22: 4.4384
REMARK 3 L33: 4.8776 L12: 3.6044
REMARK 3 L13: -3.6388 L23: -1.0026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: 0.2301 S13: -0.0115
REMARK 3 S21: -0.2431 S22: 0.3960 S23: 0.2554
REMARK 3 S31: -0.0029 S32: -0.1910 S33: -0.3744
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2399 57.0384 -22.6715
REMARK 3 T TENSOR
REMARK 3 T11: 0.4966 T22: 0.5759
REMARK 3 T33: 0.3945 T12: -0.2277
REMARK 3 T13: 0.0605 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 8.3922 L22: 7.4511
REMARK 3 L33: 8.0021 L12: -5.1764
REMARK 3 L13: -6.9722 L23: 4.7796
REMARK 3 S TENSOR
REMARK 3 S11: 0.3427 S12: 0.6480 S13: 0.9735
REMARK 3 S21: -0.9078 S22: 0.3763 S23: -0.7956
REMARK 3 S31: -1.1540 S32: 0.9873 S33: -0.7634
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5540 49.5980 -5.2929
REMARK 3 T TENSOR
REMARK 3 T11: 0.1264 T22: 0.1654
REMARK 3 T33: 0.1826 T12: -0.0135
REMARK 3 T13: 0.0120 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.1609 L22: 1.6481
REMARK 3 L33: 5.0482 L12: -0.3210
REMARK 3 L13: 1.1089 L23: -1.0471
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: 0.0009 S13: 0.0472
REMARK 3 S21: 0.0335 S22: -0.0829 S23: -0.0819
REMARK 3 S31: -0.3111 S32: 0.3108 S33: 0.0258
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6715 58.2340 -0.0552
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.2149
REMARK 3 T33: 0.2143 T12: -0.0809
REMARK 3 T13: -0.0327 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 2.8468 L22: 3.1294
REMARK 3 L33: 4.9883 L12: -0.1173
REMARK 3 L13: -1.4416 L23: 0.8563
REMARK 3 S TENSOR
REMARK 3 S11: 0.1144 S12: -0.0811 S13: 0.2464
REMARK 3 S21: 0.0879 S22: 0.0015 S23: -0.2111
REMARK 3 S31: -0.7877 S32: 0.5074 S33: -0.1145
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8788 45.6259 11.1616
REMARK 3 T TENSOR
REMARK 3 T11: 0.2993 T22: 0.5189
REMARK 3 T33: 0.3112 T12: -0.0279
REMARK 3 T13: 0.0127 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 4.3958 L22: 5.8543
REMARK 3 L33: 8.8497 L12: 2.3735
REMARK 3 L13: 2.8100 L23: 7.1687
REMARK 3 S TENSOR
REMARK 3 S11: -0.2037 S12: -0.6955 S13: 0.4745
REMARK 3 S21: 0.1313 S22: -0.3284 S23: 0.7795
REMARK 3 S31: -0.2211 S32: -1.0683 S33: 0.5392
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8432 55.9384 16.8753
REMARK 3 T TENSOR
REMARK 3 T11: 0.4186 T22: 0.3321
REMARK 3 T33: 0.3298 T12: -0.0409
REMARK 3 T13: 0.0150 T23: -0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 4.6488 L22: 2.1470
REMARK 3 L33: 2.1414 L12: 6.8390
REMARK 3 L13: -0.7876 L23: -2.4457
REMARK 3 S TENSOR
REMARK 3 S11: 0.3819 S12: -0.5526 S13: -0.1459
REMARK 3 S21: 0.9931 S22: -0.3846 S23: -0.5646
REMARK 3 S31: -0.4385 S32: 0.4921 S33: -0.0012
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7443 64.3539 3.9390
REMARK 3 T TENSOR
REMARK 3 T11: 0.5386 T22: 0.2801
REMARK 3 T33: 0.2334 T12: -0.0079
REMARK 3 T13: 0.0354 T23: -0.0796
REMARK 3 L TENSOR
REMARK 3 L11: 2.0553 L22: 4.8615
REMARK 3 L33: 5.6546 L12: 0.4551
REMARK 3 L13: 4.2228 L23: -1.2161
REMARK 3 S TENSOR
REMARK 3 S11: -0.4102 S12: -0.2406 S13: 0.6214
REMARK 3 S21: 0.1611 S22: 0.1001 S23: 0.0162
REMARK 3 S31: -1.1184 S32: 0.2001 S33: 0.3291
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2500 67.6477 10.9202
REMARK 3 T TENSOR
REMARK 3 T11: 0.6869 T22: 0.3709
REMARK 3 T33: 0.4654 T12: 0.1629
REMARK 3 T13: 0.0386 T23: -0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 9.1740 L22: 8.6623
REMARK 3 L33: 6.1156 L12: 6.7665
REMARK 3 L13: 5.9141 L23: 1.4782
REMARK 3 S TENSOR
REMARK 3 S11: -0.1191 S12: -1.1909 S13: 1.2554
REMARK 3 S21: 0.9265 S22: -0.2565 S23: 0.6832
REMARK 3 S31: -1.0748 S32: -0.8729 S33: 0.3674
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3202 67.2347 1.1743
REMARK 3 T TENSOR
REMARK 3 T11: 0.5351 T22: 0.2986
REMARK 3 T33: 0.4179 T12: 0.1133
REMARK 3 T13: 0.0070 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 9.7820 L22: 7.3310
REMARK 3 L33: 8.7786 L12: 5.2444
REMARK 3 L13: 7.2766 L23: 3.2162
REMARK 3 S TENSOR
REMARK 3 S11: -0.6697 S12: -0.3134 S13: 1.2127
REMARK 3 S21: -0.5400 S22: -0.0850 S23: 0.5549
REMARK 3 S31: -1.6564 S32: -0.4214 S33: 0.7694
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5453 63.3459 -9.0463
REMARK 3 T TENSOR
REMARK 3 T11: 0.4618 T22: 0.1695
REMARK 3 T33: 0.3774 T12: 0.0356
REMARK 3 T13: -0.0609 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 8.6823 L22: 2.0652
REMARK 3 L33: 10.0053 L12: 4.0310
REMARK 3 L13: -2.5033 L23: -1.7758
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: 0.0622 S13: 1.0901
REMARK 3 S21: -0.1368 S22: -0.0943 S23: 0.2417
REMARK 3 S31: -1.3073 S32: 0.1676 S33: 0.0970
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0561 41.0618 -20.0668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1622 T22: 0.5171
REMARK 3 T33: 0.2696 T12: 0.0413
REMARK 3 T13: 0.0105 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.6055 L22: 1.2384
REMARK 3 L33: 1.6740 L12: 0.0724
REMARK 3 L13: -0.0478 L23: 0.3708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: -0.0266 S13: -0.0627
REMARK 3 S21: 0.1624 S22: 0.1226 S23: -0.1494
REMARK 3 S31: -0.0774 S32: 0.8120 S33: -0.1326
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 54 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1309 29.7058 -19.2530
REMARK 3 T TENSOR
REMARK 3 T11: 0.2148 T22: 0.4553
REMARK 3 T33: 0.1844 T12: 0.1480
REMARK 3 T13: 0.0498 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 8.4179 L22: 6.9420
REMARK 3 L33: 0.2953 L12: 1.2247
REMARK 3 L13: -0.3612 L23: -1.0400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0480 S12: -0.4235 S13: -0.3083
REMARK 3 S21: 0.2195 S22: -0.0064 S23: -0.2086
REMARK 3 S31: 0.2154 S32: 0.5539 S33: 0.0576
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 75 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9461 38.3823 -33.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1645 T22: 0.6301
REMARK 3 T33: 0.2626 T12: 0.0222
REMARK 3 T13: 0.0256 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 2.6323 L22: 1.2723
REMARK 3 L33: 0.6139 L12: -0.8420
REMARK 3 L13: -0.2191 L23: 0.0602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: 0.3303 S13: 0.0950
REMARK 3 S21: -0.1143 S22: 0.0820 S23: -0.1717
REMARK 3 S31: -0.0527 S32: 0.7586 S33: -0.1147
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 150 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7567 29.2826 -46.6961
REMARK 3 T TENSOR
REMARK 3 T11: 0.3308 T22: 0.5715
REMARK 3 T33: 0.3865 T12: 0.0930
REMARK 3 T13: 0.0262 T23: -0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 9.3959 L22: 7.8278
REMARK 3 L33: 8.4088 L12: 1.9766
REMARK 3 L13: -8.8312 L23: -1.0839
REMARK 3 S TENSOR
REMARK 3 S11: -0.7064 S12: 0.6483 S13: -1.3096
REMARK 3 S21: -0.8128 S22: -0.0821 S23: -0.5044
REMARK 3 S31: 0.9320 S32: 0.4004 S33: 0.6985
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7225 34.6997 -49.6388
REMARK 3 T TENSOR
REMARK 3 T11: 0.2778 T22: 1.1115
REMARK 3 T33: 0.2314 T12: 0.0913
REMARK 3 T13: 0.1356 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 7.0943 L22: 2.6493
REMARK 3 L33: 3.4477 L12: -0.4183
REMARK 3 L13: -0.7825 L23: 0.3661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0566 S12: 1.0722 S13: 0.5161
REMARK 3 S21: -0.5671 S22: 0.0009 S23: 0.1990
REMARK 3 S31: -0.1735 S32: 0.0907 S33: -0.0918
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 190 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4267 25.4997 -37.1271
REMARK 3 T TENSOR
REMARK 3 T11: 0.2979 T22: 0.7574
REMARK 3 T33: 0.2654 T12: 0.1774
REMARK 3 T13: 0.0807 T23: -0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 6.1207 L22: 4.5366
REMARK 3 L33: 1.1947 L12: 2.1649
REMARK 3 L13: 0.7535 L23: -0.8711
REMARK 3 S TENSOR
REMARK 3 S11: -0.0356 S12: 0.1288 S13: -0.2715
REMARK 3 S21: -0.4525 S22: -0.0072 S23: -0.4878
REMARK 3 S31: 0.3160 S32: 0.7339 S33: 0.0007
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 208 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1617 20.2277 -39.3667
REMARK 3 T TENSOR
REMARK 3 T11: 0.2921 T22: 0.8773
REMARK 3 T33: 0.3172 T12: 0.3549
REMARK 3 T13: 0.0503 T23: -0.1419
REMARK 3 L TENSOR
REMARK 3 L11: 6.7129 L22: 1.6036
REMARK 3 L33: 0.9154 L12: 0.0030
REMARK 3 L13: -1.7730 L23: -0.2797
REMARK 3 S TENSOR
REMARK 3 S11: 0.3297 S12: 0.1859 S13: -0.6640
REMARK 3 S21: -0.2401 S22: -0.0409 S23: 0.1015
REMARK 3 S31: 0.7130 S32: 0.5699 S33: -0.0425
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5366 23.8467 -24.3922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3157 T22: 0.7015
REMARK 3 T33: 0.3022 T12: 0.2674
REMARK 3 T13: 0.0373 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 9.6566 L22: 5.8296
REMARK 3 L33: 3.7636 L12: 2.5352
REMARK 3 L13: 0.8848 L23: 1.0953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: -0.1166 S13: -0.6614
REMARK 3 S21: 0.1313 S22: 0.1265 S23: -0.6273
REMARK 3 S31: 0.4318 S32: 0.8206 S33: -0.1041
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.3157 37.7517 -21.7033
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.2940
REMARK 3 T33: 0.2568 T12: 0.0524
REMARK 3 T13: -0.0159 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: -0.0467 L22: 1.7169
REMARK 3 L33: 2.6738 L12: 0.0814
REMARK 3 L13: 0.2459 L23: -1.2433
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: 0.0728 S13: -0.0120
REMARK 3 S21: 0.1217 S22: 0.0064 S23: 0.1164
REMARK 3 S31: -0.0506 S32: -0.2969 S33: -0.1121
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 54 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.3835 48.6720 -19.0777
REMARK 3 T TENSOR
REMARK 3 T11: 0.1920 T22: 0.2446
REMARK 3 T33: 0.2569 T12: 0.0874
REMARK 3 T13: -0.0357 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.7688 L22: 3.9560
REMARK 3 L33: 3.6960 L12: 1.4892
REMARK 3 L13: 1.5724 L23: 1.3444
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.0070 S13: 0.0823
REMARK 3 S21: 0.1371 S22: -0.1951 S23: 0.2780
REMARK 3 S31: -0.3443 S32: -0.3816 S33: 0.1948
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 75 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.9873 42.2003 -34.6122
REMARK 3 T TENSOR
REMARK 3 T11: 0.1611 T22: 0.3150
REMARK 3 T33: 0.2155 T12: 0.0926
REMARK 3 T13: -0.0324 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.7704 L22: 1.4207
REMARK 3 L33: 1.6302 L12: -0.4716
REMARK 3 L13: 0.1872 L23: 0.0905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: 0.1774 S13: 0.0408
REMARK 3 S21: -0.1181 S22: -0.0377 S23: 0.1953
REMARK 3 S31: -0.2187 S32: -0.3915 S33: 0.0123
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 150 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5159 52.0118 -45.0028
REMARK 3 T TENSOR
REMARK 3 T11: 0.5391 T22: 0.5811
REMARK 3 T33: 0.3291 T12: 0.0047
REMARK 3 T13: -0.0139 T23: 0.1331
REMARK 3 L TENSOR
REMARK 3 L11: 9.2416 L22: 8.7063
REMARK 3 L33: 5.0673 L12: 0.6146
REMARK 3 L13: 6.7795 L23: 1.1549
REMARK 3 S TENSOR
REMARK 3 S11: -0.5727 S12: 1.0701 S13: 1.0889
REMARK 3 S21: -0.8702 S22: 0.1243 S23: 0.3244
REMARK 3 S31: -1.5838 S32: 0.3648 S33: 0.4427
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.2658 48.5968 -50.4214
REMARK 3 T TENSOR
REMARK 3 T11: 0.3705 T22: 0.5319
REMARK 3 T33: 0.2695 T12: 0.1602
REMARK 3 T13: -0.0872 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.0349 L22: 4.7123
REMARK 3 L33: 5.0891 L12: 2.0069
REMARK 3 L13: -5.3339 L23: -1.4353
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: 1.0668 S13: -0.2189
REMARK 3 S21: -0.3568 S22: -0.1159 S23: -0.0471
REMARK 3 S31: -0.3468 S32: -0.1505 S33: 0.1144
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 190 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1277 55.0589 -36.9284
REMARK 3 T TENSOR
REMARK 3 T11: 0.3853 T22: 0.3677
REMARK 3 T33: 0.2697 T12: 0.2214
REMARK 3 T13: -0.0601 T23: 0.0834
REMARK 3 L TENSOR
REMARK 3 L11: 5.4172 L22: 7.0612
REMARK 3 L33: 5.4912 L12: 2.0758
REMARK 3 L13: 2.7870 L23: 2.1381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: 0.0495 S13: 0.2159
REMARK 3 S21: -0.7335 S22: -0.2850 S23: 0.2849
REMARK 3 S31: -0.7129 S32: -0.4127 S33: 0.3103
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 208 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.3387 61.0848 -38.4719
REMARK 3 T TENSOR
REMARK 3 T11: 0.6509 T22: 0.3882
REMARK 3 T33: 0.3801 T12: 0.3114
REMARK 3 T13: -0.0527 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 9.4077 L22: 1.0873
REMARK 3 L33: 4.4695 L12: -0.7879
REMARK 3 L13: 5.6088 L23: -1.5215
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.2520 S13: 0.6766
REMARK 3 S21: -0.3044 S22: -0.2864 S23: -0.0091
REMARK 3 S31: -1.0465 S32: -0.1838 S33: 0.3513
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.7350 55.0773 -23.8369
REMARK 3 T TENSOR
REMARK 3 T11: 0.3749 T22: 0.3106
REMARK 3 T33: 0.2609 T12: 0.1737
REMARK 3 T13: -0.0586 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 9.7116 L22: 7.3213
REMARK 3 L33: 5.2617 L12: 1.6948
REMARK 3 L13: -0.0698 L23: -0.4947
REMARK 3 S TENSOR
REMARK 3 S11: -0.1649 S12: 0.1733 S13: 0.7985
REMARK 3 S21: 0.2632 S22: 0.0275 S23: 0.7764
REMARK 3 S31: -0.8209 S32: -0.6392 S33: 0.0651
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 6VHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1000246409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
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 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 49.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 39.30
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 32.70
REMARK 200 R MERGE FOR SHELL (I) : 1.95700
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 2.8.3
REMARK 200 STARTING MODEL: 6VH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 UL ~6.6 MG/ML FPHF+KT130 (0.2 MM
REMARK 280 KT130, 20% DMSO, 8 MM HEPES PH 7.5, 40 MM NACL) WERE MIXED WITH
REMARK 280 0.2 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR CONTAINED
REMARK 280 50 UL OF 0.8 M SODIUM FORMATE, 10% W/V PEG 8000, 10% W/V PEG
REMARK 280 1000 AND 0.1 M HEPES PH 7.0. CRYSTALS WERE SOAKED FOR ~20
REMARK 280 SECONDS IN 75% RESERVOIR SOLUTION AND 25% GLYCEROL PRIOR TO
REMARK 280 FREEZING IN LIQUID NITROGEN, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.64000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 303.28000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 227.46000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 379.10000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.82000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 151.64000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 303.28000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 379.10000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 227.46000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.82000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 OG SER C 121 O1 6WG C 301 1.44
REMARK 500 OG SER B 121 O1 6WG B 301 1.86
REMARK 500 OG SER D 121 O1 6WG D 301 1.88
REMARK 500 OG SER A 121 O1 6WG A 301 1.98
REMARK 500 O HOH D 438 O HOH D 511 1.98
REMARK 500 O HOH C 436 O HOH C 511 2.03
REMARK 500 O HOH D 446 O HOH D 509 2.08
REMARK 500 O HOH B 431 O HOH B 504 2.10
REMARK 500 O HOH C 441 O HOH D 509 2.14
REMARK 500 O HOH B 422 O HOH B 504 2.17
REMARK 500 O MET A 56 O HOH A 401 2.17
REMARK 500 O MET D 56 O HOH D 401 2.18
REMARK 500 O THR C 59 O HOH A 401 2.18
REMARK 500 O MET D 56 O HOH D 401 2.19
REMARK 500 O THR B 59 O HOH D 401 2.19
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 49 -10.02 88.08
REMARK 500 ASP A 78 -135.64 65.52
REMARK 500 SER A 121 -116.35 53.77
REMARK 500 GLU A 157 51.54 -97.89
REMARK 500 ASP A 233 -167.86 -116.60
REMARK 500 SER B 49 -10.68 88.55
REMARK 500 ASP B 78 -132.39 63.69
REMARK 500 SER B 121 -116.26 53.00
REMARK 500 ASP B 229 -159.85 -118.55
REMARK 500 ASP B 233 -167.80 -119.27
REMARK 500 SER C 49 -14.64 88.77
REMARK 500 ASP C 51 -159.95 -152.06
REMARK 500 ASP C 78 -134.18 66.28
REMARK 500 SER C 121 -112.61 52.45
REMARK 500 MET C 154 -38.95 63.62
REMARK 500 TRP C 158 -139.03 -101.35
REMARK 500 ASP C 233 -165.84 -118.91
REMARK 500 SER D 49 -7.58 87.13
REMARK 500 ASP D 51 -158.63 -152.66
REMARK 500 ASP D 78 -139.46 63.67
REMARK 500 SER D 121 -110.85 53.98
REMARK 500 ASP D 229 -168.70 -121.98
REMARK 500 ASP D 233 -165.83 -112.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG B 301 and SER B
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG C 301 and SER C
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG C 301 and SER C
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG D 301 and SER D
REMARK 800 121
DBREF1 6VHE A 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHE A A0A0D6GS23 2 253
DBREF1 6VHE B 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHE B A0A0D6GS23 2 253
DBREF1 6VHE C 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHE C A0A0D6GS23 2 253
DBREF1 6VHE D 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHE D A0A0D6GS23 2 253
SEQADV 6VHE GLY A -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE PRO A 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY A 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY B -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE PRO B 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY B 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY C -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE PRO C 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY C 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY D -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE PRO D 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHE GLY D 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQRES 1 A 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 A 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 A 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 A 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 A 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 A 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 A 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 A 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 A 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 A 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 A 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 A 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 A 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 A 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 A 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 A 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 A 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 A 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 A 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 A 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 B 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 B 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 B 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 B 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 B 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 B 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 B 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 B 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 B 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 B 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 B 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 B 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 B 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 B 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 B 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 B 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 B 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 B 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 B 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 B 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 C 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 C 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 C 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 C 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 C 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 C 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 C 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 C 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 C 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 C 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 C 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 C 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 C 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 C 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 C 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 C 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 C 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 C 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 C 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 C 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 D 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 D 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 D 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 D 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 D 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 D 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 D 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 D 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 D 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 D 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 D 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 D 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 D 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 D 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 D 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 D 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 D 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 D 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 D 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 D 255 ALA ILE THR TRP MET VAL ASN ASP
HET 6WG A 301 14
HET 6WG B 301 14
HET 6WG C 301 28
HET 6WG D 301 14
HETNAM 6WG (2~{R})-2-PHENYLPIPERIDINE-1-CARBALDEHYDE
FORMUL 5 6WG 4(C12 H15 N O)
FORMUL 9 HOH *499(H2 O)
HELIX 1 AA1 ASP A 26 ASN A 31 5 6
HELIX 2 AA2 THR A 53 THR A 59 1 7
HELIX 3 AA3 SER A 60 HIS A 68 1 9
HELIX 4 AA4 SER A 90 PHE A 106 1 17
HELIX 5 AA5 LYS A 111 ASP A 113 5 3
HELIX 6 AA6 SER A 121 GLN A 134 1 14
HELIX 7 AA7 GLU A 149 LEU A 156 1 8
HELIX 8 AA8 SER A 162 GLY A 168 1 7
HELIX 9 AA9 ASP A 179 GLU A 190 1 12
HELIX 10 AB1 LEU A 207 ILE A 221 1 15
HELIX 11 AB2 ASP A 235 ASN A 252 1 18
HELIX 12 AB3 ASP B 26 ASN B 31 5 6
HELIX 13 AB4 THR B 53 THR B 59 1 7
HELIX 14 AB5 SER B 60 HIS B 68 1 9
HELIX 15 AB6 SER B 90 PHE B 106 1 17
HELIX 16 AB7 LYS B 111 ASP B 113 5 3
HELIX 17 AB8 SER B 121 GLN B 134 1 14
HELIX 18 AB9 GLU B 149 ASP B 155 1 7
HELIX 19 AC1 SER B 162 GLY B 168 1 7
HELIX 20 AC2 ASP B 179 GLU B 190 1 12
HELIX 21 AC3 LEU B 207 ILE B 221 1 15
HELIX 22 AC4 ASP B 235 ASN B 252 1 18
HELIX 23 AC5 ASP C 26 ASN C 31 5 6
HELIX 24 AC6 THR C 53 THR C 59 1 7
HELIX 25 AC7 SER C 60 HIS C 68 1 9
HELIX 26 AC8 SER C 90 PHE C 106 1 17
HELIX 27 AC9 LYS C 111 ASP C 113 5 3
HELIX 28 AD1 SER C 121 GLN C 134 1 14
HELIX 29 AD2 ALA C 150 ASP C 155 1 6
HELIX 30 AD3 SER C 162 GLY C 168 1 7
HELIX 31 AD4 ASP C 179 GLU C 190 1 12
HELIX 32 AD5 LEU C 207 ILE C 221 1 15
HELIX 33 AD6 ASP C 235 ASN C 252 1 18
HELIX 34 AD7 ASP D 26 ASN D 31 5 6
HELIX 35 AD8 THR D 53 THR D 59 1 7
HELIX 36 AD9 SER D 60 HIS D 68 1 9
HELIX 37 AE1 SER D 90 PHE D 106 1 17
HELIX 38 AE2 LYS D 111 ASP D 113 5 3
HELIX 39 AE3 SER D 121 GLN D 134 1 14
HELIX 40 AE4 GLU D 149 LEU D 156 1 8
HELIX 41 AE5 SER D 162 GLY D 168 1 7
HELIX 42 AE6 ASP D 179 GLU D 190 1 12
HELIX 43 AE7 LEU D 207 ILE D 221 1 15
HELIX 44 AE8 ASP D 235 ASN D 252 1 18
SHEET 1 AA116 GLN A 226 GLY A 230 0
SHEET 2 AA116 LYS A 196 GLY A 202 1 N ILE A 199 O GLN A 226
SHEET 3 AA116 LYS A 140 LEU A 144 1 N ALA A 141 O LYS A 196
SHEET 4 AA116 ASN A 115 HIS A 120 1 N GLY A 119 O LEU A 144
SHEET 5 AA116 LYS A 40 LEU A 45 1 N LEU A 45 O ALA A 118
SHEET 6 AA116 LEU A 70 MET A 74 1 O ILE A 73 N LEU A 44
SHEET 7 AA116 MET A 15 PRO A 24 -1 N THR A 20 O MET A 74
SHEET 8 AA116 GLY A 1 SER A 10 -1 N LEU A 6 O LEU A 19
SHEET 9 AA116 GLY D 1 SER D 10 -1 O SER D 5 N SER A 5
SHEET 10 AA116 MET D 15 PRO D 24 -1 O LEU D 19 N LEU D 6
SHEET 11 AA116 LEU D 70 MET D 74 -1 O MET D 74 N THR D 20
SHEET 12 AA116 LYS D 40 LEU D 45 1 N LEU D 44 O ILE D 73
SHEET 13 AA116 ASN D 115 HIS D 120 1 O ALA D 118 N LEU D 45
SHEET 14 AA116 LYS D 140 LEU D 144 1 O LEU D 144 N GLY D 119
SHEET 15 AA116 LYS D 196 MET D 200 1 O LYS D 196 N ALA D 141
SHEET 16 AA116 GLN D 226 GLU D 228 1 O GLN D 226 N ILE D 199
SHEET 1 AA216 GLN B 226 GLU B 228 0
SHEET 2 AA216 LYS B 196 MET B 200 1 N ILE B 199 O GLN B 226
SHEET 3 AA216 LYS B 140 LEU B 144 1 N ALA B 141 O LYS B 196
SHEET 4 AA216 ASN B 115 HIS B 120 1 N GLY B 119 O LEU B 144
SHEET 5 AA216 THR B 41 LEU B 45 1 N LEU B 45 O ALA B 118
SHEET 6 AA216 ALA B 71 MET B 74 1 O ILE B 73 N LEU B 44
SHEET 7 AA216 MET B 15 PRO B 24 -1 N THR B 20 O MET B 74
SHEET 8 AA216 GLY B 1 SER B 10 -1 N LEU B 6 O LEU B 19
SHEET 9 AA216 GLY C 1 SER C 10 -1 O SER C 5 N SER B 5
SHEET 10 AA216 MET C 15 PRO C 24 -1 O LEU C 19 N LEU C 6
SHEET 11 AA216 LEU C 70 MET C 74 -1 O MET C 74 N THR C 20
SHEET 12 AA216 LYS C 40 LEU C 45 1 N LEU C 44 O ILE C 73
SHEET 13 AA216 ASN C 115 HIS C 120 1 O PHE C 116 N MET C 43
SHEET 14 AA216 LYS C 140 LEU C 144 1 O LEU C 144 N GLY C 119
SHEET 15 AA216 LYS C 196 MET C 200 1 O LYS C 196 N ALA C 141
SHEET 16 AA216 GLN C 226 GLU C 228 1 O GLN C 226 N ILE C 199
LINK OG SER A 121 C12 6WG A 301 1555 1555 1.38
LINK OG SER B 121 C12 6WG B 301 1555 1555 1.38
LINK OG SER C 121 C12A6WG C 301 1555 1555 1.38
LINK OG SER C 121 C12B6WG C 301 1555 1555 1.38
LINK OG SER D 121 C12 6WG D 301 1555 1555 1.38
SITE 1 AC1 10 LEU A 48 SER A 121 MET A 122 VAL A 147
SITE 2 AC1 10 ASN A 152 LEU A 153 TRP A 158 PHE A 206
SITE 3 AC1 10 HIS A 234 HOH A 432
SITE 1 AC2 15 LEU B 48 HIS B 120 MET B 122 GLY B 123
SITE 2 AC2 15 GLY B 124 TYR B 125 LEU B 144 SER B 145
SITE 3 AC2 15 VAL B 147 ASN B 152 LEU B 153 TRP B 158
SITE 4 AC2 15 PHE B 206 LEU B 207 HIS B 234
SITE 1 AC3 17 GLY C 47 LEU C 48 HIS C 120 MET C 122
SITE 2 AC3 17 GLY C 123 GLY C 124 TYR C 125 LEU C 144
SITE 3 AC3 17 SER C 145 VAL C 147 ASN C 152 LEU C 153
SITE 4 AC3 17 LEU C 156 TRP C 158 PHE C 206 HIS C 234
SITE 5 AC3 17 HOH C 490
SITE 1 AC4 17 GLY C 47 LEU C 48 HIS C 120 MET C 122
SITE 2 AC4 17 GLY C 123 GLY C 124 TYR C 125 LEU C 144
SITE 3 AC4 17 SER C 145 VAL C 147 ASN C 152 LEU C 153
SITE 4 AC4 17 LEU C 156 TRP C 158 PHE C 206 HIS C 234
SITE 5 AC4 17 HOH C 490
SITE 1 AC5 14 LEU D 48 HIS D 120 MET D 122 GLY D 123
SITE 2 AC5 14 GLY D 124 TYR D 125 LEU D 144 SER D 145
SITE 3 AC5 14 VAL D 147 LEU D 153 TRP D 158 LEU D 207
SITE 4 AC5 14 HIS D 234 HOH D 430
CRYST1 87.126 87.126 454.920 90.00 90.00 120.00 P 61 2 2 48
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011478 0.006627 0.000000 0.00000
SCALE2 0.000000 0.013253 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002198 0.00000
TER 2068 ASP A 253
TER 4136 ASP B 253
TER 6285 ASP C 253
TER 8353 ASP D 253
MASTER 783 0 4 44 32 0 21 6 8791 4 74 80
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