| content |
HEADER HYDROLASE 09-JAN-20 6VH9
TITLE FPHF, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES F, APO FORM
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, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, SODIUM BOUND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,S.A.JAMIESON,J.L.BREWSTER,P.D.MACE
REVDAT 1 16-SEP-20 6VH9 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. 1.71 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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 112050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 10223
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 43.5700 - 5.3000 1.00 6645 350 0.1759 0.1886
REMARK 3 2 5.3000 - 4.2100 1.00 6615 364 0.1360 0.1457
REMARK 3 3 4.2100 - 3.6800 1.00 6667 317 0.1426 0.1601
REMARK 3 4 3.6800 - 3.3400 1.00 6593 350 0.1513 0.1840
REMARK 3 5 3.3400 - 3.1000 1.00 6648 365 0.1692 0.1900
REMARK 3 6 3.1000 - 2.9200 1.00 6630 335 0.1730 0.2020
REMARK 3 7 2.9200 - 2.7700 1.00 6703 345 0.1731 0.2221
REMARK 3 8 2.7700 - 2.6500 1.00 6609 293 0.1770 0.2314
REMARK 3 9 2.6500 - 2.5500 1.00 6689 338 0.1820 0.2193
REMARK 3 10 2.5500 - 2.4600 1.00 6684 332 0.1811 0.1854
REMARK 3 11 2.4600 - 2.3800 1.00 6628 352 0.1823 0.2201
REMARK 3 12 2.3800 - 2.3200 1.00 6579 372 0.1780 0.2026
REMARK 3 13 2.3200 - 2.2600 1.00 6680 312 0.1754 0.1978
REMARK 3 14 2.2600 - 2.2000 1.00 6640 357 0.1742 0.2047
REMARK 3 15 2.2000 - 2.1500 1.00 6612 385 0.1856 0.2244
REMARK 3 16 2.1500 - 2.1000 1.00 6609 368 0.1955 0.2309
REMARK 3 17 2.1000 - 2.0600 1.00 6599 351 0.1975 0.2151
REMARK 3 18 2.0600 - 2.0200 1.00 6612 340 0.1948 0.2214
REMARK 3 19 2.0200 - 1.9900 1.00 6626 336 0.1997 0.2309
REMARK 3 20 1.9900 - 1.9500 1.00 6737 299 0.2244 0.2607
REMARK 3 21 1.9500 - 1.9200 1.00 6635 357 0.2281 0.2710
REMARK 3 22 1.9200 - 1.8900 1.00 6624 287 0.2308 0.2982
REMARK 3 23 1.8900 - 1.8600 1.00 6686 344 0.2423 0.2596
REMARK 3 24 1.8600 - 1.8400 1.00 6674 319 0.2495 0.2760
REMARK 3 25 1.8400 - 1.8100 1.00 6581 366 0.2723 0.3107
REMARK 3 26 1.8100 - 1.7900 1.00 6676 341 0.2763 0.3077
REMARK 3 27 1.7900 - 1.7700 1.00 6602 371 0.2831 0.2901
REMARK 3 28 1.7700 - 1.7500 1.00 6614 327 0.2782 0.3085
REMARK 3 29 1.7500 - 1.7300 1.00 6735 310 0.2957 0.3219
REMARK 3 30 1.7300 - 1.7100 0.96 6301 340 0.3164 0.3420
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.940
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0400 25.8893 -10.2606
REMARK 3 T TENSOR
REMARK 3 T11: 0.1557 T22: 0.1451
REMARK 3 T33: 0.2059 T12: -0.0016
REMARK 3 T13: 0.0128 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.1539 L22: 1.7030
REMARK 3 L33: 4.1680 L12: -0.0201
REMARK 3 L13: 0.3210 L23: -0.0355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0526 S12: 0.0187 S13: -0.1106
REMARK 3 S21: -0.0486 S22: -0.0765 S23: 0.0426
REMARK 3 S31: 0.3901 S32: -0.0881 S33: 0.0181
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9626 20.2070 8.3058
REMARK 3 T TENSOR
REMARK 3 T11: 0.3847 T22: 0.3259
REMARK 3 T33: 0.2544 T12: 0.0090
REMARK 3 T13: -0.0169 T23: 0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 1.3798 L22: 7.0748
REMARK 3 L33: 4.3421 L12: 1.9939
REMARK 3 L13: 0.3644 L23: 1.4525
REMARK 3 S TENSOR
REMARK 3 S11: 0.2732 S12: -0.4509 S13: -0.2114
REMARK 3 S21: 1.0212 S22: -0.3098 S23: -0.3178
REMARK 3 S31: 0.5328 S32: 0.2956 S33: 0.0316
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8071 10.0950 -3.1294
REMARK 3 T TENSOR
REMARK 3 T11: 0.4368 T22: 0.1862
REMARK 3 T33: 0.2834 T12: 0.1012
REMARK 3 T13: 0.0101 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 3.3085 L22: 4.5264
REMARK 3 L33: 4.5953 L12: 1.6319
REMARK 3 L13: 0.0413 L23: -2.2023
REMARK 3 S TENSOR
REMARK 3 S11: 0.1366 S12: -0.1212 S13: -0.4672
REMARK 3 S21: -0.0694 S22: -0.1950 S23: -0.2517
REMARK 3 S31: 0.8605 S32: 0.2397 S33: 0.0562
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2473 43.0305 -9.7334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1116 T22: 0.2087
REMARK 3 T33: 0.2133 T12: 0.0092
REMARK 3 T13: 0.0180 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 2.1905 L22: 6.2939
REMARK 3 L33: 8.9664 L12: 3.0258
REMARK 3 L13: -3.0821 L23: -3.2395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.0949 S13: 0.0686
REMARK 3 S21: -0.1542 S22: 0.2998 S23: 0.1287
REMARK 3 S31: -0.0250 S32: -0.2203 S33: -0.2654
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8060 56.3316 -23.0440
REMARK 3 T TENSOR
REMARK 3 T11: 0.4843 T22: 0.5999
REMARK 3 T33: 0.4476 T12: -0.2265
REMARK 3 T13: 0.0519 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 5.4703 L22: 5.5902
REMARK 3 L33: 9.2039 L12: -0.9385
REMARK 3 L13: -4.6567 L23: 3.9445
REMARK 3 S TENSOR
REMARK 3 S11: 0.4174 S12: 0.5169 S13: 0.9709
REMARK 3 S21: -0.4537 S22: 0.2674 S23: -0.6994
REMARK 3 S31: -1.2022 S32: 1.3275 S33: -0.6853
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7836 51.4516 -5.5295
REMARK 3 T TENSOR
REMARK 3 T11: 0.1776 T22: 0.1677
REMARK 3 T33: 0.1968 T12: -0.0402
REMARK 3 T13: 0.0011 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 2.0994 L22: 1.6527
REMARK 3 L33: 4.0614 L12: -0.0047
REMARK 3 L13: 0.1365 L23: -0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0759 S12: -0.0425 S13: 0.1426
REMARK 3 S21: 0.0148 S22: -0.0769 S23: -0.0724
REMARK 3 S31: -0.4598 S32: 0.3224 S33: 0.0054
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 122 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2094 58.2454 3.9707
REMARK 3 T TENSOR
REMARK 3 T11: 0.3719 T22: 0.2401
REMARK 3 T33: 0.1676 T12: -0.0709
REMARK 3 T13: 0.0366 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 7.6806 L22: 7.2287
REMARK 3 L33: 3.0237 L12: 2.0558
REMARK 3 L13: 2.5369 L23: -1.5181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.3787 S13: 0.2555
REMARK 3 S21: 0.1769 S22: 0.0006 S23: -0.1879
REMARK 3 S31: -0.7521 S32: 0.2424 S33: -0.0116
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0639 51.1769 14.0685
REMARK 3 T TENSOR
REMARK 3 T11: 0.3085 T22: 0.3351
REMARK 3 T33: 0.2373 T12: 0.0085
REMARK 3 T13: 0.0391 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 4.5565 L22: 8.8962
REMARK 3 L33: 7.4939 L12: 5.1457
REMARK 3 L13: 1.1570 L23: 3.0052
REMARK 3 S TENSOR
REMARK 3 S11: 0.2749 S12: -0.3609 S13: 0.2752
REMARK 3 S21: 0.7476 S22: -0.3865 S23: 0.5201
REMARK 3 S31: -0.0794 S32: -0.5769 S33: 0.1167
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 220 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6783 65.7380 6.9807
REMARK 3 T TENSOR
REMARK 3 T11: 0.6736 T22: 0.2327
REMARK 3 T33: 0.2736 T12: 0.0252
REMARK 3 T13: 0.0273 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 9.3828 L22: 3.6943
REMARK 3 L33: 5.5973 L12: 1.8378
REMARK 3 L13: 2.6969 L23: 1.6774
REMARK 3 S TENSOR
REMARK 3 S11: -0.2545 S12: -0.4392 S13: 0.5371
REMARK 3 S21: 0.3404 S22: 0.1341 S23: 0.0824
REMARK 3 S31: -1.2321 S32: -0.0280 S33: 0.1220
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 221 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7728 68.0818 2.6591
REMARK 3 T TENSOR
REMARK 3 T11: 0.6786 T22: 0.3391
REMARK 3 T33: 0.3198 T12: 0.0732
REMARK 3 T13: 0.0833 T23: -0.0855
REMARK 3 L TENSOR
REMARK 3 L11: 8.5448 L22: 9.7264
REMARK 3 L33: 7.3141 L12: 6.1768
REMARK 3 L13: 6.8839 L23: 3.6391
REMARK 3 S TENSOR
REMARK 3 S11: -0.3968 S12: -0.2734 S13: 1.0478
REMARK 3 S21: -0.2017 S22: -0.2493 S23: 0.5000
REMARK 3 S31: -1.4919 S32: -0.3051 S33: 0.6518
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5021 63.6501 -9.0459
REMARK 3 T TENSOR
REMARK 3 T11: 0.5142 T22: 0.2221
REMARK 3 T33: 0.3534 T12: 0.0779
REMARK 3 T13: -0.0442 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 8.6577 L22: 9.4784
REMARK 3 L33: 5.0834 L12: 9.0544
REMARK 3 L13: -2.9553 L23: -2.9558
REMARK 3 S TENSOR
REMARK 3 S11: 0.1245 S12: -0.0589 S13: 0.9086
REMARK 3 S21: 0.1205 S22: -0.0575 S23: 0.3641
REMARK 3 S31: -0.8950 S32: -0.0086 S33: -0.0647
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3371 38.6684 -25.2360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1365 T22: 0.3643
REMARK 3 T33: 0.2538 T12: 0.0341
REMARK 3 T13: 0.0102 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 0.9444 L22: 1.5665
REMARK 3 L33: 2.0218 L12: 0.0102
REMARK 3 L13: -0.7918 L23: 0.5211
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.0840 S13: 0.0304
REMARK 3 S21: 0.0061 S22: 0.0244 S23: -0.0933
REMARK 3 S31: 0.0104 S32: 0.4603 S33: -0.0518
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 134 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8899 30.3145 -39.8501
REMARK 3 T TENSOR
REMARK 3 T11: 0.3224 T22: 0.5532
REMARK 3 T33: 0.2963 T12: 0.0521
REMARK 3 T13: 0.0619 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 7.9755 L22: 2.9927
REMARK 3 L33: 3.4025 L12: -1.0102
REMARK 3 L13: 2.1502 L23: -0.4079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0687 S12: 1.0840 S13: -0.5180
REMARK 3 S21: -0.4058 S22: 0.0999 S23: 0.2851
REMARK 3 S31: 0.3222 S32: 0.3488 S33: -0.1634
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 163 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3410 26.1453 -37.9699
REMARK 3 T TENSOR
REMARK 3 T11: 0.2478 T22: 0.4635
REMARK 3 T33: 0.2743 T12: 0.1311
REMARK 3 T13: 0.0298 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 3.5092 L22: 2.1649
REMARK 3 L33: 3.6734 L12: 0.5006
REMARK 3 L13: -1.8746 L23: -0.2391
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: 0.2418 S13: -0.1763
REMARK 3 S21: -0.2289 S22: -0.0353 S23: -0.1485
REMARK 3 S31: 0.2249 S32: 0.4125 S33: 0.1230
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5510 41.0266 -26.7964
REMARK 3 T TENSOR
REMARK 3 T11: 0.1247 T22: 0.2455
REMARK 3 T33: 0.2368 T12: 0.0492
REMARK 3 T13: -0.0149 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.2014 L22: 1.5993
REMARK 3 L33: 3.2069 L12: 0.1537
REMARK 3 L13: 0.6301 L23: -0.8465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.0325 S13: 0.0245
REMARK 3 S21: 0.0027 S22: 0.0192 S23: 0.0550
REMARK 3 S31: -0.0720 S32: -0.2188 S33: 0.0048
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 134 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2256 51.5400 -39.7660
REMARK 3 T TENSOR
REMARK 3 T11: 0.3423 T22: 0.4329
REMARK 3 T33: 0.3625 T12: 0.0557
REMARK 3 T13: -0.0259 T23: 0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 3.3873 L22: 3.2042
REMARK 3 L33: 3.3917 L12: -1.2813
REMARK 3 L13: -1.2490 L23: 1.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.1192 S12: 0.5706 S13: 0.5356
REMARK 3 S21: -0.4405 S22: 0.0614 S23: -0.4682
REMARK 3 S31: -0.5071 S32: 0.0898 S33: -0.1756
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 163 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.9084 55.3567 -38.3527
REMARK 3 T TENSOR
REMARK 3 T11: 0.3268 T22: 0.3187
REMARK 3 T33: 0.2718 T12: 0.1288
REMARK 3 T13: -0.0285 T23: 0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 2.3914 L22: 2.3791
REMARK 3 L33: 5.2499 L12: 0.0377
REMARK 3 L13: 1.7457 L23: 0.3542
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: 0.2182 S13: 0.2158
REMARK 3 S21: -0.3091 S22: -0.1001 S23: 0.0799
REMARK 3 S31: -0.6352 S32: -0.3874 S33: 0.1333
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 501))
REMARK 3 SELECTION : (CHAIN B AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 501))
REMARK 3 ATOM PAIRS NUMBER : 4674
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 501))
REMARK 3 SELECTION : (CHAIN C AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 253 OR
REMARK 3 RESID 501))
REMARK 3 ATOM PAIRS NUMBER : 4674
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 501))
REMARK 3 SELECTION : (CHAIN D AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 199 OR RESID 201 THROUGH 221 OR RESID 223
REMARK 3 THROUGH 244 OR RESID 246 THROUGH 253 OR
REMARK 3 RESID 501))
REMARK 3 ATOM PAIRS NUMBER : 4674
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6VH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1000246405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-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 : 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 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112281
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 49.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 27.30
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 27.20
REMARK 200 R MERGE FOR SHELL (I) : 3.15500
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: 4RGY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL ~8.5 MG/ML FPHF (20 MM HEPES PH
REMARK 280 7.5, 10 MM NACL) WERE MIXED WITH 0.1 UL FPHF CRYSTAL SEEDS (IN
REMARK 280 54.4% TACSIMATE PH 7.0, 0.1 M BIS-TRIS PROPANE PH 6.5, 8%
REMARK 280 POLYPROPYLENE GLYCOL P 400) AND 0.2 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 50 UL OF 2.8 M SODIUM ACETATE.
REMARK 280 CRYSTALS WERE SOAKED FOR ~20 SECONDS IN 75% RESERVOIR SOLUTION
REMARK 280 AND 25% ETHYLENGLYCOL PRIOR TO FREEZING IN LIQUID NITROGEN,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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 151.20000
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 302.40000
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 226.80000
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 378.00000
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 75.60000
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 151.20000
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 302.40000
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 378.00000
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 226.80000
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 75.60000
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: 11640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 O HOH A 706 O HOH B 700 1.38
REMARK 500 O HOH A 706 O HOH B 664 1.57
REMARK 500 O HOH A 625 O HOH B 700 1.92
REMARK 500 O HOH C 700 O HOH D 627 1.98
REMARK 500 O HOH C 652 O HOH C 700 1.99
REMARK 500 O HOH B 664 O HOH B 700 2.03
REMARK 500 O HOH A 618 O HOH B 645 2.05
REMARK 500 O HOH D 653 O HOH D 712 2.05
REMARK 500 O HOH A 614 O HOH A 687 2.05
REMARK 500 O HOH B 620 O HOH B 674 2.07
REMARK 500 O HOH B 674 O HOH B 697 2.11
REMARK 500 OG1 THR B 54 O HOH B 601 2.12
REMARK 500 O HOH B 671 O HOH C 688 2.12
REMARK 500 O HOH B 702 O HOH C 688 2.13
REMARK 500 O MET A 56 O HOH A 601 2.13
REMARK 500 O HOH A 609 O HOH A 688 2.15
REMARK 500 O HOH A 713 O HOH D 697 2.17
REMARK 500 O MET A 56 O HOH A 601 2.17
REMARK 500 O HOH A 710 O HOH D 702 2.17
REMARK 500 O THR A 59 O HOH A 601 2.18
REMARK 500 NE2 GLN D 27 O HOH D 602 2.18
REMARK 500 O HOH D 653 O HOH D 713 2.19
REMARK 500 O ASN D 31 O HOH D 603 2.19
REMARK 500 O HOH D 609 O HOH D 709 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 156 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 LEU B 156 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 LYS B 196 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG B 245 CB - CG - CD ANGL. DEV. = 19.0 DEGREES
REMARK 500 ARG B 245 CG - CD - NE ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG B 245 CG - CD - NE ANGL. DEV. = -14.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 49 -11.89 89.43
REMARK 500 ASP A 78 -137.63 64.55
REMARK 500 SER A 121 -120.22 61.54
REMARK 500 GLU A 157 56.47 -103.72
REMARK 500 ASP A 229 -168.63 -126.88
REMARK 500 ASP A 233 -168.15 -120.59
REMARK 500 SER B 49 -13.37 90.69
REMARK 500 ASP B 78 -136.81 64.28
REMARK 500 SER B 121 -118.67 61.42
REMARK 500 GLU B 157 51.05 -94.45
REMARK 500 ASN B 159 116.18 -38.63
REMARK 500 ASP B 229 -168.13 -126.45
REMARK 500 ASP B 233 -167.26 -120.59
REMARK 500 ASN B 252 -95.06 -84.91
REMARK 500 SER C 49 -12.73 89.96
REMARK 500 ASP C 78 -137.33 63.88
REMARK 500 SER C 121 -118.60 62.57
REMARK 500 ASN C 159 116.30 -37.39
REMARK 500 ASP C 191 52.24 39.38
REMARK 500 ASP C 229 -167.60 -125.87
REMARK 500 ASP C 233 -166.28 -120.23
REMARK 500 SER D 49 -12.48 88.21
REMARK 500 ASP D 78 -137.71 63.94
REMARK 500 SER D 121 -120.04 61.57
REMARK 500 GLU D 157 52.62 -96.93
REMARK 500 ASN D 159 116.34 -39.46
REMARK 500 ASP D 229 -168.85 -128.07
REMARK 500 ASP D 233 -167.28 -120.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 18 -14.58
REMARK 500 ARG A 245 -12.05
REMARK 500 ARG A 245 -12.58
REMARK 500 ARG B 245 -11.22
REMARK 500 ARG C 245 -11.43
REMARK 500 ARG C 245 -12.14
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 121 OG
REMARK 620 2 HOH A 607 O 62.2
REMARK 620 3 HOH A 701 O 89.9 85.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 121 OG
REMARK 620 2 HOH B 609 O 62.7
REMARK 620 3 HOH B 660 O 75.0 81.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 121 OG
REMARK 620 2 HOH C 607 O 62.1
REMARK 620 3 HOH C 692 O 83.8 104.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 121 OG
REMARK 620 2 HOH D 601 O 53.8
REMARK 620 3 HOH D 659 O 71.9 81.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 501
DBREF1 6VH9 A 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VH9 A A0A0D6GS23 2 253
DBREF1 6VH9 B 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VH9 B A0A0D6GS23 2 253
DBREF1 6VH9 C 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VH9 C A0A0D6GS23 2 253
DBREF1 6VH9 D 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VH9 D A0A0D6GS23 2 253
SEQADV 6VH9 GLY A -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 PRO A 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY A 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY B -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 PRO B 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY B 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY C -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 PRO C 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY C 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 GLY D -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 PRO D 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VH9 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 NA A 501 1
HET NA B 501 1
HET NA C 501 1
HET NA D 501 1
HETNAM NA SODIUM ION
FORMUL 5 NA 4(NA 1+)
FORMUL 9 HOH *457(H2 O)
HELIX 1 AA1 ASP A 26 PHE A 30 5 5
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 ALA A 150 ASP A 155 1 6
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 GLU C 149 ASP C 155 1 7
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 ASP C 253 1 19
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 ASP D 155 1 7
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 ASP D 253 1 19
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 42
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 42 O ILE D 73
SHEET 13 AA116 ASN D 115 HIS D 120 1 O PHE D 116 N MET D 43
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 LYS B 40 LEU B 45 1 N LEU B 45 O ALA B 118
SHEET 6 AA216 LEU B 70 MET B 74 1 O ILE B 73 N LEU B 42
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 ASN C 7 N TYR B 3
SHEET 10 AA216 MET C 15 PRO C 24 -1 O LEU C 19 N LEU C 6
SHEET 11 AA216 LEU C 70 PRO C 75 -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 NA NA A 501 1555 1555 2.34
LINK NA NA A 501 O HOH A 607 1555 1555 2.26
LINK NA NA A 501 O HOH A 701 1555 1555 1.95
LINK OG SER B 121 NA NA B 501 1555 1555 2.38
LINK NA NA B 501 O HOH B 609 1555 1555 2.24
LINK NA NA B 501 O HOH B 660 1555 1555 2.25
LINK OG SER C 121 NA NA C 501 1555 1555 2.46
LINK NA NA C 501 O HOH C 607 1555 1555 2.29
LINK NA NA C 501 O HOH C 692 1555 1555 2.16
LINK OG SER D 121 NA NA D 501 1555 1555 2.48
LINK NA NA D 501 O HOH D 601 1555 1555 1.96
LINK NA NA D 501 O HOH D 659 1555 1555 2.21
SITE 1 AC1 5 LEU A 48 SER A 121 MET A 122 HOH A 607
SITE 2 AC1 5 HOH A 701
SITE 1 AC2 5 LEU B 48 SER B 121 MET B 122 HOH B 609
SITE 2 AC2 5 HOH B 660
SITE 1 AC3 5 LEU C 48 SER C 121 MET C 122 HOH C 607
SITE 2 AC3 5 HOH C 692
SITE 1 AC4 6 GLY D 47 LEU D 48 SER D 121 MET D 122
SITE 2 AC4 6 HOH D 601 HOH D 659
CRYST1 87.145 87.145 453.600 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 0.011475 0.006625 0.000000 0.00000
SCALE2 0.000000 0.013250 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002205 0.00000
TER 2095 ASP A 253
TER 4190 ASP B 253
TER 6269 ASP C 253
TER 8337 ASP D 253
MASTER 724 0 4 44 32 0 8 6 8697 4 16 80
END |