| content |
HEADER HYDROLASE 12-NOV-24 9EBF
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, BOROLANE-BASED COMPOUND Q41 BOUND IN CRYSTAL FORM 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED HYDROLASE SAUSA300_2518;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS USA300;
SOURCE 3 ORGANISM_TAXID: 367830;
SOURCE 4 GENE: SAUSA300_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE, BORON, SERINE-BORON,
KEYWDS 3 HISTIDINE-BORON
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 21-JAN-26 9EBF 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES E, BOROLANE-BASED COMPOUND Q41 BOUND IN CRYSTAL
JRNL TITL 3 FORM 6
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54834
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2769
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 47.4700 - 6.7800 1.00 2752 111 0.1319 0.1446
REMARK 3 2 6.7700 - 5.3900 1.00 2635 155 0.1725 0.1975
REMARK 3 3 5.3800 - 4.7000 1.00 2619 144 0.1439 0.1931
REMARK 3 4 4.7000 - 4.2700 1.00 2601 162 0.1422 0.1791
REMARK 3 5 4.2700 - 3.9700 1.00 2646 111 0.1560 0.1966
REMARK 3 6 3.9700 - 3.7300 1.00 2559 171 0.1674 0.2284
REMARK 3 7 3.7300 - 3.5500 1.00 2643 116 0.1821 0.2253
REMARK 3 8 3.5500 - 3.3900 1.00 2602 136 0.2188 0.2547
REMARK 3 9 3.3900 - 3.2600 1.00 2618 116 0.2187 0.2516
REMARK 3 10 3.2600 - 3.1500 1.00 2591 131 0.2342 0.2944
REMARK 3 11 3.1500 - 3.0500 1.00 2614 140 0.2214 0.2766
REMARK 3 12 3.0500 - 2.9600 1.00 2551 168 0.2367 0.2825
REMARK 3 13 2.9600 - 2.8900 1.00 2575 129 0.2528 0.3120
REMARK 3 14 2.8900 - 2.8200 1.00 2600 158 0.2702 0.2917
REMARK 3 15 2.8100 - 2.7500 1.00 2601 119 0.2753 0.3145
REMARK 3 16 2.7500 - 2.6900 1.00 2574 158 0.2507 0.3085
REMARK 3 17 2.6900 - 2.6400 1.00 2584 123 0.2541 0.2404
REMARK 3 18 2.6400 - 2.5900 1.00 2552 147 0.2653 0.2747
REMARK 3 19 2.5900 - 2.5400 1.00 2632 136 0.2736 0.3498
REMARK 3 20 2.5400 - 2.5000 0.97 2516 138 0.3084 0.3258
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.710
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 : 0.009 9064
REMARK 3 ANGLE : 1.008 12308
REMARK 3 CHIRALITY : 0.057 1332
REMARK 3 PLANARITY : 0.010 1612
REMARK 3 DIHEDRAL : 16.973 3376
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6745 -17.5610 -80.8968
REMARK 3 T TENSOR
REMARK 3 T11: 0.5329 T22: 0.6977
REMARK 3 T33: 0.6142 T12: -0.1080
REMARK 3 T13: 0.1254 T23: -0.2924
REMARK 3 L TENSOR
REMARK 3 L11: 4.6741 L22: 2.3181
REMARK 3 L33: 2.6053 L12: 0.1588
REMARK 3 L13: 0.5975 L23: -0.0245
REMARK 3 S TENSOR
REMARK 3 S11: 0.1321 S12: -1.0867 S13: 0.6342
REMARK 3 S21: 0.3272 S22: -0.0002 S23: 0.0586
REMARK 3 S31: -0.6313 S32: -0.0075 S33: -0.1063
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1898 -29.5336 -88.4484
REMARK 3 T TENSOR
REMARK 3 T11: 0.4219 T22: 0.6555
REMARK 3 T33: 0.5454 T12: -0.1215
REMARK 3 T13: 0.0213 T23: -0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 3.7084 L22: 0.4654
REMARK 3 L33: 2.3807 L12: -0.8978
REMARK 3 L13: 1.2690 L23: -1.1781
REMARK 3 S TENSOR
REMARK 3 S11: 0.2229 S12: -0.8482 S13: 0.1980
REMARK 3 S21: -0.1243 S22: 0.0746 S23: 0.5967
REMARK 3 S31: 0.0523 S32: -0.5238 S33: -0.3222
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7095 -50.6548 -75.0095
REMARK 3 T TENSOR
REMARK 3 T11: 0.5981 T22: 0.8079
REMARK 3 T33: 0.4827 T12: -0.2497
REMARK 3 T13: -0.1057 T23: 0.1199
REMARK 3 L TENSOR
REMARK 3 L11: 4.4370 L22: 3.9560
REMARK 3 L33: 3.7990 L12: -1.6031
REMARK 3 L13: 2.0429 L23: -1.0580
REMARK 3 S TENSOR
REMARK 3 S11: 0.3795 S12: -0.3520 S13: -0.4974
REMARK 3 S21: -0.1164 S22: 0.0869 S23: 0.2499
REMARK 3 S31: 0.5038 S32: -0.3275 S33: -0.4423
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8174 -61.1804 -61.1253
REMARK 3 T TENSOR
REMARK 3 T11: 0.6808 T22: 0.8330
REMARK 3 T33: 0.8119 T12: -0.1247
REMARK 3 T13: -0.3044 T23: 0.1266
REMARK 3 L TENSOR
REMARK 3 L11: 1.2341 L22: 1.7887
REMARK 3 L33: 2.5036 L12: -0.3370
REMARK 3 L13: 0.0908 L23: -0.3410
REMARK 3 S TENSOR
REMARK 3 S11: 0.3140 S12: -0.1592 S13: -0.2182
REMARK 3 S21: 0.4512 S22: -0.1284 S23: -0.5386
REMARK 3 S31: 0.5259 S32: 0.5194 S33: -0.2063
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1744 -47.5533 -56.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.6241 T22: 0.8227
REMARK 3 T33: 0.5695 T12: -0.2622
REMARK 3 T13: -0.1443 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 2.0568 L22: 1.7294
REMARK 3 L33: 2.5414 L12: -0.5484
REMARK 3 L13: 0.3731 L23: -0.2143
REMARK 3 S TENSOR
REMARK 3 S11: 0.2991 S12: -0.4093 S13: 0.0274
REMARK 3 S21: 0.4696 S22: -0.0995 S23: -0.1596
REMARK 3 S31: 0.1216 S32: 0.2239 S33: -0.2277
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3385 -41.1192 -85.8205
REMARK 3 T TENSOR
REMARK 3 T11: 0.5188 T22: 0.6313
REMARK 3 T33: 0.4524 T12: -0.1692
REMARK 3 T13: -0.0120 T23: 0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 4.2950 L22: 4.2332
REMARK 3 L33: 1.9233 L12: -3.8531
REMARK 3 L13: 3.0086 L23: -2.1190
REMARK 3 S TENSOR
REMARK 3 S11: 0.5781 S12: -0.1169 S13: -0.0236
REMARK 3 S21: -0.3754 S22: -0.4983 S23: -0.0957
REMARK 3 S31: 0.2717 S32: 0.2783 S33: -0.0616
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 201 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2679 -20.9149 -95.5293
REMARK 3 T TENSOR
REMARK 3 T11: 0.4676 T22: 0.3268
REMARK 3 T33: 0.5065 T12: -0.0125
REMARK 3 T13: 0.0779 T23: -0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 6.2489 L22: 1.1729
REMARK 3 L33: 3.4554 L12: 0.8552
REMARK 3 L13: 0.7427 L23: -0.1635
REMARK 3 S TENSOR
REMARK 3 S11: 0.1543 S12: -0.4427 S13: 0.7961
REMARK 3 S21: -0.1940 S22: -0.0165 S23: 0.2037
REMARK 3 S31: -0.4144 S32: -0.1593 S33: -0.1432
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2021 -17.6144 -87.1087
REMARK 3 T TENSOR
REMARK 3 T11: 0.5841 T22: 0.9920
REMARK 3 T33: 0.4836 T12: -0.3366
REMARK 3 T13: 0.0981 T23: -0.1436
REMARK 3 L TENSOR
REMARK 3 L11: 5.4378 L22: 2.9755
REMARK 3 L33: 3.4238 L12: -0.2346
REMARK 3 L13: -0.2760 L23: 0.5239
REMARK 3 S TENSOR
REMARK 3 S11: 0.6388 S12: -1.5855 S13: 0.2325
REMARK 3 S21: 0.4800 S22: -0.6673 S23: -0.1838
REMARK 3 S31: -0.0430 S32: 0.4382 S33: 0.0941
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 76 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9141 -13.3723 -84.1297
REMARK 3 T TENSOR
REMARK 3 T11: 0.6921 T22: 1.1200
REMARK 3 T33: 0.7671 T12: -0.3847
REMARK 3 T13: 0.2429 T23: -0.4821
REMARK 3 L TENSOR
REMARK 3 L11: 1.6525 L22: 3.8755
REMARK 3 L33: 1.7150 L12: 0.4530
REMARK 3 L13: -1.5497 L23: 0.5450
REMARK 3 S TENSOR
REMARK 3 S11: 0.7101 S12: -1.6158 S13: 1.1165
REMARK 3 S21: 0.4475 S22: -0.5736 S23: 0.4663
REMARK 3 S31: -0.3329 S32: 0.3922 S33: -0.0303
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0613 -43.9395 -98.0877
REMARK 3 T TENSOR
REMARK 3 T11: 0.4577 T22: 0.5011
REMARK 3 T33: 0.4485 T12: -0.1117
REMARK 3 T13: 0.0311 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 3.7102 L22: 8.2471
REMARK 3 L33: 3.4069 L12: -1.1724
REMARK 3 L13: -0.4293 L23: 0.5265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0768 S12: -0.1331 S13: -0.1976
REMARK 3 S21: -0.0120 S22: -0.2188 S23: 0.6625
REMARK 3 S31: 0.2372 S32: 0.1552 S33: 0.1440
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 201 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.1615 -65.8122-102.0702
REMARK 3 T TENSOR
REMARK 3 T11: 0.7202 T22: 0.4598
REMARK 3 T33: 0.6924 T12: 0.0730
REMARK 3 T13: 0.0650 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 3.4017 L22: 4.4974
REMARK 3 L33: 4.1359 L12: 1.1394
REMARK 3 L13: 0.0839 L23: 0.2514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: -0.0002 S13: -0.8306
REMARK 3 S21: -0.7175 S22: 0.0295 S23: -0.5519
REMARK 3 S31: 1.0454 S32: 0.3945 S33: 0.0553
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1476 -56.5465 -93.6759
REMARK 3 T TENSOR
REMARK 3 T11: 0.4068 T22: 0.6214
REMARK 3 T33: 0.6882 T12: 0.0340
REMARK 3 T13: 0.0205 T23: 0.0846
REMARK 3 L TENSOR
REMARK 3 L11: 2.1529 L22: 3.6091
REMARK 3 L33: 3.3923 L12: 0.7019
REMARK 3 L13: -0.6787 L23: -0.3209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: -0.3806 S13: -0.4768
REMARK 3 S21: -0.1129 S22: -0.2163 S23: -0.9068
REMARK 3 S31: 0.3046 S32: 0.8043 S33: 0.1061
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 153 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6338 -26.2500-101.3945
REMARK 3 T TENSOR
REMARK 3 T11: 0.5346 T22: 0.4713
REMARK 3 T33: 0.3656 T12: -0.1517
REMARK 3 T13: 0.0676 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 4.9589 L22: 7.7544
REMARK 3 L33: 2.0307 L12: 0.3824
REMARK 3 L13: 0.0035 L23: 0.1115
REMARK 3 S TENSOR
REMARK 3 S11: 0.1328 S12: -0.0782 S13: 0.2528
REMARK 3 S21: -0.7867 S22: -0.1446 S23: -0.0741
REMARK 3 S31: -0.1348 S32: 0.1682 S33: -0.0088
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 201 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4225 -5.0174 -90.9682
REMARK 3 T TENSOR
REMARK 3 T11: 0.8008 T22: 0.7805
REMARK 3 T33: 1.2222 T12: -0.2868
REMARK 3 T13: 0.3043 T23: -0.4716
REMARK 3 L TENSOR
REMARK 3 L11: 2.4859 L22: 2.6164
REMARK 3 L33: 1.2142 L12: -0.5462
REMARK 3 L13: 0.7371 L23: 1.0926
REMARK 3 S TENSOR
REMARK 3 S11: 0.5638 S12: -1.1207 S13: 1.7496
REMARK 3 S21: 0.0054 S22: -0.4667 S23: 0.8101
REMARK 3 S31: -0.5845 S32: 0.0520 S33: -0.0935
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 9EBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1000290113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54846
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 47.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 31.20
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 30.50
REMARK 200 R MERGE FOR SHELL (I) : 2.17900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 UL 11.2 MG/ML FPHE (10 MM HEPES PH
REMARK 280 7.5, 100 MM NACL) WERE MIXED WITH 6 UL Q41 (50 MM IN DMSO) AND
REMARK 280 INCUBATED AT 18C OVERNIGHT. 0.15 UL FPHE-Q41 SOLUTION WAS MIXED
REMARK 280 WITH 0.3 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR
REMARK 280 CONTAINED 25 UL OF 180 MM POTASSIUM THIOCYANATE, 100 MM SODIUM
REMARK 280 ACETATE PH 5.5, 22.5% PEG 2000 MME. CRYSTAL WAS FROZEN IN A
REMARK 280 SOLUTION OF ~25% GLYCEROL, 75% RESERVOIR., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 106.14300
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 106.14300
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 106.14300
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 106.14300
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 106.14300
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 106.14300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 12790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY B -2
REMARK 465 GLY C -2
REMARK 465 GLY D -2
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 B 103 O1 XPU B 301 2.01
REMARK 500 NE2 HIS C 257 OG SER D 103 2.14
REMARK 500 OG SER C 103 NE2 HIS D 257 2.15
REMARK 500 OG SER A 103 NE2 HIS B 257 2.17
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 -132.19 57.95
REMARK 500 PRO A 129 30.59 -96.50
REMARK 500 ASP A 136 31.18 -97.03
REMARK 500 THR A 153 -72.37 -108.55
REMARK 500 GLU A 201 -54.76 -125.02
REMARK 500 GLN B 7 108.50 -48.59
REMARK 500 SER B 103 -131.51 57.44
REMARK 500 GLU B 127 70.09 48.39
REMARK 500 THR B 153 -73.40 -120.80
REMARK 500 SER C 103 -130.26 53.13
REMARK 500 TYR C 116 58.08 -145.09
REMARK 500 ASP C 136 36.41 -97.73
REMARK 500 THR C 153 -72.45 -114.63
REMARK 500 TYR C 218 43.45 -141.49
REMARK 500 ALA D 9 149.21 -174.80
REMARK 500 SER D 103 -130.62 57.80
REMARK 500 ASP D 136 38.56 -98.76
REMARK 500 GLU D 201 -55.46 -122.16
REMARK 500 TYR D 218 36.75 -92.25
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9EBF A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9EBF B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9EBF C 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9EBF D 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 9EBF GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY B 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY C -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF PRO C -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY C 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY D -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF PRO D -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EBF GLY D 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
SEQRES 1 C 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 C 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 C 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 C 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 C 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 C 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 C 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 C 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 C 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 C 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 C 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 C 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 C 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 C 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 C 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 C 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 C 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 C 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 C 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 C 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 C 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 C 279 LEU LEU ASN MET TRP GLY
SEQRES 1 D 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 D 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 D 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 D 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 D 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 D 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 D 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 D 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 D 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 D 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 D 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 D 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 D 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 D 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 D 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 D 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 D 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 D 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 D 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 D 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 D 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 D 279 LEU LEU ASN MET TRP GLY
HET XPU A 301 13
HET XPU B 301 13
HET XPU C 301 13
HET XPU D 301 13
HETNAM XPU 2-METHYL-4-(4,4,5,5-TETRAMETHYL-1,3,2-DIOXABOROLAN-2-
HETNAM 2 XPU YL)BENZENE-1-SULFONAMIDE
FORMUL 5 XPU 4(C13 H20 B N O4 S)
FORMUL 9 HOH *76(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 SER A 70 5 5
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 THR A 153 1 18
HELIX 7 AA7 THR A 153 LEU A 167 1 15
HELIX 8 AA8 ALA A 170 SER A 178 1 9
HELIX 9 AA9 THR A 183 GLU A 201 1 19
HELIX 10 AB1 GLU A 201 HIS A 207 1 7
HELIX 11 AB2 THR A 211 LYS A 217 1 7
HELIX 12 AB3 TYR A 218 ASP A 220 5 3
HELIX 13 AB4 SER A 233 GLY A 247 1 15
HELIX 14 AB5 LEU A 258 LYS A 263 1 6
HELIX 15 AB6 LYS A 263 GLY A 276 1 14
HELIX 16 AB7 THR B 31 ILE B 34 5 4
HELIX 17 AB8 PHE B 35 LYS B 43 1 9
HELIX 18 AB9 PRO B 66 ASN B 71 5 6
HELIX 19 AC1 ASP B 75 SER B 93 1 19
HELIX 20 AC2 SER B 103 TYR B 116 1 14
HELIX 21 AC3 ASP B 136 THR B 153 1 18
HELIX 22 AC4 THR B 153 LEU B 167 1 15
HELIX 23 AC5 ALA B 170 SER B 178 1 9
HELIX 24 AC6 THR B 183 GLU B 201 1 19
HELIX 25 AC7 GLU B 201 HIS B 207 1 7
HELIX 26 AC8 THR B 211 LYS B 217 1 7
HELIX 27 AC9 TYR B 218 ASP B 220 5 3
HELIX 28 AD1 SER B 233 GLY B 247 1 15
HELIX 29 AD2 LEU B 258 LYS B 263 1 6
HELIX 30 AD3 LYS B 263 GLY B 276 1 14
HELIX 31 AD4 THR C 31 ILE C 34 5 4
HELIX 32 AD5 PHE C 35 LYS C 43 1 9
HELIX 33 AD6 PRO C 66 ASN C 71 5 6
HELIX 34 AD7 ASP C 75 SER C 93 1 19
HELIX 35 AD8 SER C 103 TYR C 116 1 14
HELIX 36 AD9 ASP C 136 THR C 153 1 18
HELIX 37 AE1 THR C 153 LEU C 167 1 15
HELIX 38 AE2 ALA C 170 GLN C 179 1 10
HELIX 39 AE3 THR C 183 GLU C 201 1 19
HELIX 40 AE4 GLU C 201 HIS C 207 1 7
HELIX 41 AE5 LEU C 212 LYS C 217 1 6
HELIX 42 AE6 TYR C 218 ASP C 220 5 3
HELIX 43 AE7 SER C 233 GLY C 247 1 15
HELIX 44 AE8 LEU C 258 LYS C 263 1 6
HELIX 45 AE9 LYS C 263 GLY C 276 1 14
HELIX 46 AF1 THR D 31 ILE D 34 5 4
HELIX 47 AF2 PHE D 35 LYS D 43 1 9
HELIX 48 AF3 PRO D 66 ASN D 71 5 6
HELIX 49 AF4 ASP D 75 SER D 93 1 19
HELIX 50 AF5 SER D 103 TYR D 116 1 14
HELIX 51 AF6 ASP D 136 THR D 153 1 18
HELIX 52 AF7 THR D 153 LEU D 167 1 15
HELIX 53 AF8 ALA D 170 GLN D 179 1 10
HELIX 54 AF9 THR D 183 GLU D 201 1 19
HELIX 55 AG1 GLU D 201 HIS D 207 1 7
HELIX 56 AG2 LEU D 212 LYS D 217 1 6
HELIX 57 AG3 TYR D 218 ASP D 220 5 3
HELIX 58 AG4 SER D 233 GLY D 247 1 15
HELIX 59 AG5 LEU D 258 LYS D 263 1 6
HELIX 60 AG6 LYS D 263 GLY D 276 1 14
SHEET 1 AA1 3 GLU A 2 GLU A 5 0
SHEET 2 AA1 3 ALA A 9 VAL A 16 -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 GLU A 5 0
SHEET 2 AA2 8 ALA A 9 VAL A 16 -1 O LEU A 11 N LEU A 4
SHEET 3 AA2 8 THR A 47 ASP A 52 -1 O ALA A 50 N HIS A 14
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 HIS A 126 N GLY A 101
SHEET 7 AA2 8 ILE B 222 GLY B 227 1 O THR B 223 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 THR A 223
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 HIS B 14 O ALA B 50
SHEET 8 AA3 8 GLU B 2 LEU B 6 -1 N LEU B 4 O LEU B 11
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 THR A 223
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 HIS B 14 O ALA B 50
SHEET 8 AA4 8 GLU B 60 LEU B 61 -1 O GLU B 60 N LYS B 10
SHEET 1 AA5 3 GLU C 2 LEU C 6 0
SHEET 2 AA5 3 ALA C 9 GLY C 17 -1 O LEU C 11 N LEU C 4
SHEET 3 AA5 3 GLU C 60 LEU C 61 -1 O GLU C 60 N LYS C 10
SHEET 1 AA6 8 GLU C 2 LEU C 6 0
SHEET 2 AA6 8 ALA C 9 GLY C 17 -1 O LEU C 11 N LEU C 4
SHEET 3 AA6 8 THR C 47 ASP C 52 -1 O ALA C 50 N HIS C 14
SHEET 4 AA6 8 VAL C 21 ILE C 25 1 N PHE C 24 O VAL C 49
SHEET 5 AA6 8 VAL C 97 SER C 102 1 O TYR C 98 N ILE C 23
SHEET 6 AA6 8 VAL C 120 HIS C 126 1 O LYS C 121 N VAL C 97
SHEET 7 AA6 8 ILE D 222 GLY D 227 1 O THR D 223 N ILE C 123
SHEET 8 AA6 8 ILE D 250 ILE D 253 1 O VAL D 251 N LEU D 224
SHEET 1 AA7 8 ILE C 250 ILE C 253 0
SHEET 2 AA7 8 ILE C 222 GLY C 227 1 N LEU C 224 O VAL C 251
SHEET 3 AA7 8 VAL D 120 HIS D 126 1 O PHE D 125 N THR C 223
SHEET 4 AA7 8 VAL D 97 SER D 102 1 N VAL D 97 O LYS D 121
SHEET 5 AA7 8 VAL D 21 ILE D 25 1 N ILE D 23 O TYR D 98
SHEET 6 AA7 8 THR D 47 VAL D 51 1 O VAL D 49 N PHE D 24
SHEET 7 AA7 8 ALA D 9 VAL D 16 -1 N HIS D 14 O ALA D 50
SHEET 8 AA7 8 GLU D 2 LEU D 6 -1 N LEU D 4 O LEU D 11
LINK OG SER A 103 B1 XPU A 301 1555 1555 1.39
LINK NE2 HIS A 257 B1 XPU B 301 1555 1555 1.44
LINK B1 XPU A 301 NE2 HIS B 257 1555 1555 1.44
LINK OG SER B 103 B1 XPU B 301 1555 1555 1.40
LINK OG SER C 103 B1 XPU C 301 1555 1555 1.40
LINK NE2 HIS C 257 B1 XPU D 301 1555 1555 1.43
LINK B1 XPU C 301 NE2 HIS D 257 1555 1555 1.44
LINK OG SER D 103 B1 XPU D 301 1555 1555 1.40
CRYST1 212.286 212.286 212.286 90.00 90.00 90.00 I 2 3 96
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 0.004711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004711 0.00000
TER 2201 GLY A 276
TER 4402 GLY B 276
TER 6603 GLY C 276
TER 8804 GLY D 276
MASTER 579 0 4 60 46 0 0 6 8928 4 60 88
END |