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HEADER HYDROLASE 22-JUN-23 8T88
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, OXADIAZOLONE JJ004 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE E;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-0114;
SOURCE 3 ORGANISM_TAXID: 1385527;
SOURCE 4 GENE: SAUSA300_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: F1010
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 06-MAR-24 8T88 0
JRNL AUTH J.JO,T.UPADHYAY,E.C.WOODS,K.W.PARK,N.J.PEDOWITZ,
JRNL AUTH 2 J.JAWOREK-KORJAKOWSKA,S.WANG,T.A.VALDEZ,M.FELLNER,M.BOGYO
JRNL TITL DEVELOPMENT OF OXADIAZOLONE ACTIVITY-BASED PROBES TARGETING
JRNL TITL 2 FPHE FOR SPECIFIC DETECTION OF STAPHYLOCOCCUS AUREUS
JRNL TITL 3 INFECTIONS.
JRNL REF J.AM.CHEM.SOC. 2024
JRNL REFN ESSN 1520-5126
JRNL PMID 38411555
JRNL DOI 10.1021/JACS.3C13974
REMARK 2
REMARK 2 RESOLUTION. 1.54 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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 73279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 3528
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 39.9900 - 4.4900 1.00 2915 175 0.1454 0.1634
REMARK 3 2 4.4900 - 3.5600 0.96 2789 112 0.1189 0.1524
REMARK 3 3 3.5600 - 3.1100 0.98 2841 123 0.1521 0.1427
REMARK 3 4 3.1100 - 2.8300 0.99 2825 146 0.1559 0.1838
REMARK 3 5 2.8300 - 2.6300 0.99 2866 112 0.1600 0.2091
REMARK 3 6 2.6300 - 2.4700 0.99 2816 151 0.1554 0.1940
REMARK 3 7 2.4700 - 2.3500 0.99 2821 169 0.1483 0.1935
REMARK 3 8 2.3500 - 2.2500 0.99 2811 151 0.1434 0.1942
REMARK 3 9 2.2500 - 2.1600 0.99 2828 143 0.1526 0.1637
REMARK 3 10 2.1600 - 2.0800 0.99 2794 158 0.1568 0.1866
REMARK 3 11 2.0800 - 2.0200 0.97 2766 144 0.1565 0.1865
REMARK 3 12 2.0200 - 1.9600 0.94 2671 148 0.1599 0.1949
REMARK 3 13 1.9600 - 1.9100 0.98 2767 168 0.1670 0.1947
REMARK 3 14 1.9100 - 1.8600 0.98 2732 156 0.1823 0.2193
REMARK 3 15 1.8600 - 1.8200 0.98 2851 129 0.1845 0.2109
REMARK 3 16 1.8200 - 1.7800 0.98 2780 131 0.1869 0.2122
REMARK 3 17 1.7800 - 1.7500 0.98 2799 132 0.1881 0.2091
REMARK 3 18 1.7500 - 1.7100 0.98 2772 133 0.1946 0.2315
REMARK 3 19 1.7100 - 1.6800 0.98 2773 130 0.1935 0.2177
REMARK 3 20 1.6800 - 1.6500 0.97 2751 159 0.2049 0.2452
REMARK 3 21 1.6500 - 1.6300 0.97 2768 139 0.2083 0.2623
REMARK 3 22 1.6300 - 1.6000 0.97 2789 112 0.2161 0.2833
REMARK 3 23 1.6000 - 1.5800 0.97 2765 147 0.2275 0.2591
REMARK 3 24 1.5800 - 1.5600 0.97 2743 133 0.2561 0.2890
REMARK 3 25 1.5600 - 1.5400 0.95 2718 127 0.3074 0.3162
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.030
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 : 0.010 4693
REMARK 3 ANGLE : 1.077 6386
REMARK 3 CHIRALITY : 0.059 681
REMARK 3 PLANARITY : 0.017 851
REMARK 3 DIHEDRAL : 9.573 659
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0554 -10.8961 7.5090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.1173
REMARK 3 T33: 0.1619 T12: 0.0130
REMARK 3 T13: 0.0190 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.1205 L22: 1.0673
REMARK 3 L33: 1.1589 L12: 0.1409
REMARK 3 L13: 0.3464 L23: -0.0123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: 0.0180 S13: 0.1932
REMARK 3 S21: -0.0145 S22: 0.0092 S23: -0.0003
REMARK 3 S31: -0.1133 S32: 0.0199 S33: 0.0291
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0298 -15.2431 -24.2599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1357
REMARK 3 T33: 0.1965 T12: 0.0319
REMARK 3 T13: -0.0013 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.3514 L22: 1.4545
REMARK 3 L33: 2.9647 L12: 0.4725
REMARK 3 L13: 0.3669 L23: 0.6336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: 0.0278 S13: -0.2249
REMARK 3 S21: -0.0236 S22: -0.0454 S23: -0.0126
REMARK 3 S31: 0.2666 S32: 0.1248 S33: -0.0053
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4134 -7.6166 -30.1004
REMARK 3 T TENSOR
REMARK 3 T11: 0.1529 T22: 0.3190
REMARK 3 T33: 0.2070 T12: -0.0178
REMARK 3 T13: 0.0399 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 2.4451 L22: 1.4384
REMARK 3 L33: 3.3971 L12: -0.1544
REMARK 3 L13: 0.8007 L23: -0.2935
REMARK 3 S TENSOR
REMARK 3 S11: 0.1030 S12: 0.2084 S13: 0.0251
REMARK 3 S21: -0.1323 S22: 0.1084 S23: -0.2731
REMARK 3 S31: -0.0003 S32: 0.7373 S33: -0.1999
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8072 -15.3937 -36.8451
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.3221
REMARK 3 T33: 0.1998 T12: 0.0755
REMARK 3 T13: 0.0155 T23: -0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 1.3113 L22: 2.1636
REMARK 3 L33: 4.2620 L12: 0.2698
REMARK 3 L13: 1.4746 L23: -1.9104
REMARK 3 S TENSOR
REMARK 3 S11: 0.2027 S12: 0.3247 S13: -0.0914
REMARK 3 S21: -0.2946 S22: -0.0117 S23: -0.0959
REMARK 3 S31: 0.3048 S32: 0.5622 S33: -0.1576
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0237 -1.6332 -20.8848
REMARK 3 T TENSOR
REMARK 3 T11: 0.1745 T22: 0.1940
REMARK 3 T33: 0.2047 T12: -0.0537
REMARK 3 T13: 0.0093 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 3.2398 L22: 2.5544
REMARK 3 L33: 4.0931 L12: 0.0535
REMARK 3 L13: -0.6829 L23: 0.0677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: -0.1032 S13: 0.3385
REMARK 3 S21: -0.0028 S22: 0.1703 S23: -0.1765
REMARK 3 S31: -0.3641 S32: 0.4566 S33: -0.1302
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 97 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0785 -5.3693 -26.3189
REMARK 3 T TENSOR
REMARK 3 T11: 0.1668 T22: 0.1460
REMARK 3 T33: 0.1568 T12: 0.0141
REMARK 3 T13: -0.0164 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 2.5291 L22: 1.9653
REMARK 3 L33: 4.4250 L12: 0.3786
REMARK 3 L13: -1.1837 L23: -0.1805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: 0.1206 S13: 0.0673
REMARK 3 S21: -0.1810 S22: -0.0150 S23: 0.0218
REMARK 3 S31: -0.1861 S32: -0.0297 S33: -0.0116
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5635 -13.8624 -6.0344
REMARK 3 T TENSOR
REMARK 3 T11: 0.3000 T22: 0.2709
REMARK 3 T33: 0.2168 T12: -0.0315
REMARK 3 T13: 0.0635 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 9.5554 L22: 1.9316
REMARK 3 L33: 8.8226 L12: -3.5366
REMARK 3 L13: 8.0484 L23: -1.8791
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: -0.5522 S13: -0.0858
REMARK 3 S21: 0.0043 S22: -0.0335 S23: 0.0418
REMARK 3 S31: 0.5770 S32: -0.4622 S33: -0.0086
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2628 -21.4251 9.5409
REMARK 3 T TENSOR
REMARK 3 T11: 0.2202 T22: 0.3206
REMARK 3 T33: 0.2774 T12: -0.0275
REMARK 3 T13: 0.0201 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 5.0071 L22: 2.0534
REMARK 3 L33: 9.8600 L12: -2.7110
REMARK 3 L13: 6.9477 L23: -4.0815
REMARK 3 S TENSOR
REMARK 3 S11: 0.1292 S12: -0.2422 S13: -0.0734
REMARK 3 S21: -0.1729 S22: 0.1140 S23: 0.3391
REMARK 3 S31: 0.2392 S32: -0.6099 S33: -0.2239
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 167 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6248 -13.3749 16.8393
REMARK 3 T TENSOR
REMARK 3 T11: 0.2322 T22: 0.4208
REMARK 3 T33: 0.3017 T12: 0.0611
REMARK 3 T13: 0.0210 T23: -0.0739
REMARK 3 L TENSOR
REMARK 3 L11: 3.4144 L22: 4.0053
REMARK 3 L33: 8.1892 L12: -0.7020
REMARK 3 L13: 1.9029 L23: -4.0546
REMARK 3 S TENSOR
REMARK 3 S11: -0.2141 S12: -0.1422 S13: 0.2884
REMARK 3 S21: 0.1815 S22: 0.0882 S23: 0.4979
REMARK 3 S31: -0.5632 S32: -1.0097 S33: 0.1268
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5903 -10.3967 2.7664
REMARK 3 T TENSOR
REMARK 3 T11: 0.2072 T22: 0.2532
REMARK 3 T33: 0.2598 T12: 0.0327
REMARK 3 T13: -0.0383 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 8.4451 L22: 7.7097
REMARK 3 L33: 6.4517 L12: -5.6768
REMARK 3 L13: -2.9021 L23: 1.9935
REMARK 3 S TENSOR
REMARK 3 S11: -0.0301 S12: -0.4378 S13: 0.1810
REMARK 3 S21: -0.2323 S22: -0.0437 S23: 0.5469
REMARK 3 S31: -0.7060 S32: -0.4655 S33: 0.0852
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 201 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1731 -20.7296 11.4599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.1986
REMARK 3 T33: 0.1933 T12: 0.0324
REMARK 3 T13: 0.0130 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.3374 L22: 2.7284
REMARK 3 L33: 6.5357 L12: 0.7147
REMARK 3 L13: 2.8201 L23: 2.1404
REMARK 3 S TENSOR
REMARK 3 S11: 0.1330 S12: 0.1713 S13: -0.2662
REMARK 3 S21: 0.2590 S22: 0.1792 S23: -0.3368
REMARK 3 S31: 0.4071 S32: 0.6423 S33: -0.2726
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1871 -15.3288 24.9737
REMARK 3 T TENSOR
REMARK 3 T11: 0.2345 T22: 0.2015
REMARK 3 T33: 0.1196 T12: 0.0090
REMARK 3 T13: 0.0214 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.6843 L22: 2.7311
REMARK 3 L33: 2.1995 L12: 0.1744
REMARK 3 L13: 0.3711 L23: 0.5825
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.3098 S13: 0.1281
REMARK 3 S21: 0.5022 S22: -0.0454 S23: 0.0544
REMARK 3 S31: 0.0708 S32: -0.1693 S33: 0.0096
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 8T88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1000275464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 0.9537
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 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73321
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 39.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 1.05100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13 UL 19 MG/ML FPHE (10 MM HEPES PH
REMARK 280 7.5, 10 0MM NACL) WERE MIXED WITH 5 UL JJ004 (10 MM IN DMSO) AND
REMARK 280 INCUBATED AT 18C OVERNIGHT. 0.15 UL FPHE-JJ004 SOLUTION WAS
REMARK 280 MIXED WITH 0.2 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR
REMARK 280 CONTAINED 25 UL OF 0.18 M MAGNESIUM CHLORIDE, 0.1 M TRIS PH 8.5,
REMARK 280 22.5 % W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 2000. CRYSTAL
REMARK 280 WAS FROZEN IN A SOLUTION OF ~25% GLYCEROL, 75% RESERVOIR., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.13550
REMARK 290 SMTRY3 2 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: 13580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 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 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 -2
REMARK 465 PRO A -1
REMARK 465 GLY B -2
REMARK 465 PRO 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 HZ1 LYS B 175 O HOH B 402 1.60
REMARK 500 O HOH B 402 O HOH B 572 1.77
REMARK 500 O2 YW0 B 301 O HOH B 401 1.90
REMARK 500 O2 YW0 A 301 O HOH A 401 1.94
REMARK 500 NZ LYS B 175 O HOH B 402 1.97
REMARK 500 O HOH A 594 O HOH A 624 2.08
REMARK 500 O HOH A 419 O HOH A 593 2.08
REMARK 500 O HOH A 420 O HOH A 597 2.10
REMARK 500 O HOH A 626 O HOH A 633 2.15
REMARK 500 O HOH A 629 O HOH B 499 2.17
REMARK 500 O HOH A 463 O HOH B 526 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 610 O HOH A 624 2555 2.17
REMARK 500 O HOH A 544 O HOH A 624 2555 2.17
REMARK 500 O HOH A 557 O HOH B 551 1655 2.18
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 103 -132.24 60.71
REMARK 500 GLU A 201 -51.92 -127.21
REMARK 500 SER B 103 -135.57 60.13
REMARK 500 GLU B 201 -51.78 -125.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 231 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 641 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 617 DISTANCE = 6.15 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 273 OD1
REMARK 620 2 HOH A 531 O 88.4
REMARK 620 3 HOH A 575 O 97.7 92.1
REMARK 620 4 HOH B 490 O 88.1 174.5 92.6
REMARK 620 5 HOH B 496 O 174.7 94.8 86.4 88.3
REMARK 620 6 HOH B 532 O 90.2 83.6 170.9 92.1 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 443 O
REMARK 620 2 HOH A 508 O 83.4
REMARK 620 3 HOH B 436 O 175.7 92.6
REMARK 620 4 HOH B 458 O 90.2 88.9 91.2
REMARK 620 5 HOH B 513 O 88.3 84.8 89.9 173.7
REMARK 620 N 1 2 3 4
DBREF 8T88 A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 8T88 B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 8T88 GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T88 PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T88 GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T88 GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T88 PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T88 GLY B 0 UNP Q2FDS6 EXPRESSION TAG
SEQRES 1 A 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 A 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 A 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 A 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 A 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 A 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 A 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 A 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 A 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 A 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 A 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 A 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 A 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 A 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 A 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 A 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 A 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 A 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 A 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 A 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 A 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 A 279 LEU LEU ASN MET TRP GLY
SEQRES 1 B 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 B 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 B 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 B 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 B 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 B 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 B 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 B 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 B 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 B 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 B 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 B 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 B 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 B 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 B 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 B 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 B 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 B 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 B 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 B 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 B 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 B 279 LEU LEU ASN MET TRP GLY
HET YW0 A 301 53
HET MG A 302 1
HET YW0 B 301 53
HET MG B 302 1
HETNAM YW0 METHYL 2-FORMYL-2-[4-(UNDEC-10-YNAMIDO)
HETNAM 2 YW0 PHENYL]HYDRAZINE-1-CARBOXYLATE
HETNAM MG MAGNESIUM ION
FORMUL 3 YW0 2(C20 H27 N3 O4)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *458(H2 O)
HELIX 1 AA1 THR A 31 ILE A 34 5 4
HELIX 2 AA2 PHE A 35 LYS A 43 1 9
HELIX 3 AA3 PRO A 66 ASN A 71 5 6
HELIX 4 AA4 ASP A 75 SER A 93 1 19
HELIX 5 AA5 SER A 103 TYR A 116 1 14
HELIX 6 AA6 ASP A 136 LEU A 167 1 32
HELIX 7 AA7 ALA A 170 GLN A 179 1 10
HELIX 8 AA8 THR A 183 GLU A 201 1 19
HELIX 9 AA9 GLU A 201 HIS A 207 1 7
HELIX 10 AB1 THR A 211 LYS A 217 1 7
HELIX 11 AB2 TYR A 218 ASP A 220 5 3
HELIX 12 AB3 SER A 233 GLY A 247 1 15
HELIX 13 AB4 LEU A 258 LYS A 263 1 6
HELIX 14 AB5 LYS A 263 GLY A 276 1 14
HELIX 15 AB6 THR B 31 ILE B 34 5 4
HELIX 16 AB7 PHE B 35 LYS B 43 1 9
HELIX 17 AB8 PRO B 66 ASN B 71 5 6
HELIX 18 AB9 ASP B 75 SER B 93 1 19
HELIX 19 AC1 SER B 103 TYR B 116 1 14
HELIX 20 AC2 ASP B 136 THR B 153 1 18
HELIX 21 AC3 THR B 153 LEU B 167 1 15
HELIX 22 AC4 ALA B 170 SER B 178 1 9
HELIX 23 AC5 THR B 183 GLU B 201 1 19
HELIX 24 AC6 GLU B 201 HIS B 207 1 7
HELIX 25 AC7 THR B 211 LYS B 217 1 7
HELIX 26 AC8 TYR B 218 ASP B 220 5 3
HELIX 27 AC9 SER B 233 GLY B 247 1 15
HELIX 28 AD1 LEU B 258 LYS B 263 1 6
HELIX 29 AD2 LYS B 263 GLY B 276 1 14
SHEET 1 AA1 3 GLU A 2 LEU A 6 0
SHEET 2 AA1 3 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA1 3 GLU A 60 LEU A 61 -1 O GLU A 60 N LYS A 10
SHEET 1 AA2 8 GLU A 2 LEU A 6 0
SHEET 2 AA2 8 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA2 8 THR A 47 VAL A 51 -1 O VAL A 48 N VAL A 16
SHEET 4 AA2 8 VAL A 21 ILE A 25 1 N PHE A 24 O VAL A 49
SHEET 5 AA2 8 VAL A 97 SER A 102 1 O TYR A 98 N ILE A 23
SHEET 6 AA2 8 VAL A 120 HIS A 126 1 O LYS A 121 N VAL A 97
SHEET 7 AA2 8 ILE B 222 GLY B 227 1 O LEU B 225 N PHE A 125
SHEET 8 AA2 8 ILE B 250 ILE B 253 1 O VAL B 251 N LEU B 224
SHEET 1 AA3 8 ILE A 250 ILE A 253 0
SHEET 2 AA3 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA3 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA3 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA3 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA3 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA3 8 ALA B 9 GLY B 17 -1 N VAL B 16 O VAL B 48
SHEET 8 AA3 8 GLU B 2 LEU B 6 -1 N LEU B 6 O ALA B 9
SHEET 1 AA4 8 ILE A 250 ILE A 253 0
SHEET 2 AA4 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA4 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA4 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA4 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA4 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA4 8 ALA B 9 GLY B 17 -1 N VAL B 16 O VAL B 48
SHEET 8 AA4 8 GLU B 60 LEU B 61 -1 O GLU B 60 N LYS B 10
LINK OG SER A 103 C16 YW0 A 301 1555 1555 1.49
LINK OG SER B 103 C16 YW0 B 301 1555 1555 1.44
LINK OD1 ASN A 273 MG MG A 302 1555 1555 2.04
LINK MG MG A 302 O HOH A 531 1555 1555 2.07
LINK MG MG A 302 O HOH A 575 1555 1555 2.07
LINK MG MG A 302 O HOH B 490 1555 1454 2.20
LINK MG MG A 302 O HOH B 496 1555 1454 2.17
LINK MG MG A 302 O HOH B 532 1555 1454 2.10
LINK O HOH A 443 MG MG B 302 1455 1555 2.20
LINK O HOH A 508 MG MG B 302 1455 1555 2.10
LINK MG MG B 302 O HOH B 436 1555 1555 2.14
LINK MG MG B 302 O HOH B 458 1555 1555 2.06
LINK MG MG B 302 O HOH B 513 1555 1555 2.08
CRYST1 46.743 74.271 73.638 90.00 91.70 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021394 0.000000 0.000635 0.00000
SCALE2 0.000000 0.013464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013586 0.00000
TER 4436 GLY A 276
TER 8913 GLY B 276
MASTER 522 0 4 29 27 0 0 6 4900 2 116 44
END |