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HEADER HYDROLASE 06-APR-23 8SDD
TITLE CRYSTAL STRUCTURE OF FLUOROACETATE DEHALOGENASE DARO3835 H274N MUTANT
TITLE 2 WITH D107-GLYCOLYL INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DECHLOROMONAS AROMATICA RCB;
SOURCE 3 ORGANISM_TAXID: 159087;
SOURCE 4 GENE: DARO_3835;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS FLUOROACETATE, DEHALOGENASE, HYDROLASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,T.SKARINA,A.KHUSNUTDINOVA,A.IAKOUNINE,A.SAVCHENKO
REVDAT 1 14-FEB-24 8SDD 0
JRNL AUTH A.N.KHUSNUTDINOVA,K.A.BATYROVA,G.BROWN,T.FEDORCHUK,Y.S.CHAI,
JRNL AUTH 2 T.SKARINA,R.FLICK,A.P.PETIT,A.SAVCHENKO,P.STOGIOS,
JRNL AUTH 3 A.F.YAKUNIN
JRNL TITL STRUCTURAL INSIGHTS INTO HYDROLYTIC DEFLUORINATION OF
JRNL TITL 2 DIFLUOROACETATE BY MICROBIAL FLUOROACETATE DEHALOGENASES.
JRNL REF FEBS J. V. 290 4966 2023
JRNL REFN ISSN 1742-464X
JRNL PMID 37437000
JRNL DOI 10.1111/FEBS.16903
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15_3448
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.420
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 43847
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.550
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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 30.4000 - 4.8100 0.98 3202 150 0.2164 0.2360
REMARK 3 2 4.8100 - 3.8200 0.97 3118 151 0.1861 0.2421
REMARK 3 3 3.8200 - 3.3400 0.98 3115 147 0.2076 0.2472
REMARK 3 4 3.3400 - 3.0400 0.96 3048 146 0.2194 0.2797
REMARK 3 5 3.0400 - 2.8200 0.96 3019 155 0.2356 0.2710
REMARK 3 6 2.8200 - 2.6500 0.96 3037 139 0.2365 0.2783
REMARK 3 7 2.6500 - 2.5200 0.95 2980 134 0.2332 0.2726
REMARK 3 8 2.5200 - 2.4100 0.94 2976 145 0.2349 0.3184
REMARK 3 9 2.4100 - 2.3200 0.94 3012 136 0.2298 0.2689
REMARK 3 10 2.3200 - 2.2400 0.93 2913 141 0.2271 0.2554
REMARK 3 11 2.2400 - 2.1700 0.94 2937 144 0.2240 0.2685
REMARK 3 12 2.1700 - 2.1100 0.91 2907 142 0.2295 0.2511
REMARK 3 13 2.1100 - 2.0500 0.94 2912 137 0.2358 0.2832
REMARK 3 14 2.0500 - 2.0000 0.85 2676 128 0.2441 0.3077
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.247
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.89
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 : 0.005 4770
REMARK 3 ANGLE : 0.736 6482
REMARK 3 CHIRALITY : 0.048 695
REMARK 3 PLANARITY : 0.005 857
REMARK 3 DIHEDRAL : 20.812 1738
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 1 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7203 -1.6684 136.4961
REMARK 3 T TENSOR
REMARK 3 T11: 0.1607 T22: 0.2547
REMARK 3 T33: 0.2116 T12: -0.0111
REMARK 3 T13: -0.0585 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.9594 L22: 6.9629
REMARK 3 L33: 2.8550 L12: 0.5449
REMARK 3 L13: 0.1986 L23: -1.9816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0810 S12: 0.4562 S13: 0.0003
REMARK 3 S21: -0.6520 S22: 0.1984 S23: 0.5755
REMARK 3 S31: 0.1018 S32: -0.4314 S33: -0.1016
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 236 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1261 -3.7326 152.8259
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.0798
REMARK 3 T33: 0.1433 T12: 0.0008
REMARK 3 T13: -0.0366 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.6830 L22: 0.4045
REMARK 3 L33: 1.4681 L12: -0.0244
REMARK 3 L13: -0.3840 L23: 0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: -0.2803 S13: 0.0006
REMARK 3 S21: -0.0253 S22: 0.0177 S23: -0.0104
REMARK 3 S31: 0.0234 S32: -0.0623 S33: 0.0124
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 237 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.5621 5.4451 154.9006
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.2273
REMARK 3 T33: 0.2225 T12: -0.0564
REMARK 3 T13: -0.0075 T23: -0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 4.1768 L22: 4.3510
REMARK 3 L33: 2.8637 L12: -1.9248
REMARK 3 L13: -0.7939 L23: 2.2463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.7473 S13: 0.5286
REMARK 3 S21: 0.2579 S22: 0.1811 S23: -0.1412
REMARK 3 S31: -0.0375 S32: 0.2261 S33: -0.1784
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 296 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.9286 11.2536 146.0567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.0802
REMARK 3 T33: 0.2373 T12: -0.0323
REMARK 3 T13: -0.0198 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 3.4304 L22: 1.4627
REMARK 3 L33: 1.9389 L12: 1.0907
REMARK 3 L13: -1.5439 L23: -1.3748
REMARK 3 S TENSOR
REMARK 3 S11: 0.2405 S12: -0.2643 S13: 0.3590
REMARK 3 S21: -0.1455 S22: -0.0835 S23: -0.0535
REMARK 3 S31: -0.4184 S32: 0.0800 S33: -0.0719
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5048 -5.7126 204.3994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2369 T22: 0.9386
REMARK 3 T33: 0.5904 T12: -0.0111
REMARK 3 T13: 0.0445 T23: -0.0870
REMARK 3 L TENSOR
REMARK 3 L11: 2.0202 L22: 7.0470
REMARK 3 L33: 2.5340 L12: -0.5005
REMARK 3 L13: -0.6124 L23: -0.8848
REMARK 3 S TENSOR
REMARK 3 S11: -0.3287 S12: -0.5148 S13: -0.5661
REMARK 3 S21: 0.2656 S22: 0.2329 S23: 0.7062
REMARK 3 S31: -0.0079 S32: -0.2150 S33: 0.1213
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1960 -8.3820 207.8609
REMARK 3 T TENSOR
REMARK 3 T11: 0.3705 T22: 0.9369
REMARK 3 T33: 0.1224 T12: 0.2060
REMARK 3 T13: 0.0366 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 0.8443 L22: 1.0332
REMARK 3 L33: 1.5814 L12: 0.5702
REMARK 3 L13: 0.9950 L23: 1.1805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: -0.5244 S13: -0.2295
REMARK 3 S21: 0.5280 S22: 0.1834 S23: 0.0615
REMARK 3 S31: 0.2760 S32: -0.2496 S33: -0.0517
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4832 -4.2008 197.4814
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.7909
REMARK 3 T33: 0.2253 T12: 0.1228
REMARK 3 T13: 0.0902 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.7917 L22: 0.7640
REMARK 3 L33: 2.0177 L12: 0.5416
REMARK 3 L13: -0.1284 L23: -0.1702
REMARK 3 S TENSOR
REMARK 3 S11: -0.2782 S12: -0.5221 S13: 0.0376
REMARK 3 S21: 0.2335 S22: 0.2288 S23: 0.0596
REMARK 3 S31: 0.3099 S32: 0.1298 S33: 0.0600
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4299 -4.2547 200.0315
REMARK 3 T TENSOR
REMARK 3 T11: 0.3267 T22: 1.0465
REMARK 3 T33: 0.1081 T12: 0.1632
REMARK 3 T13: 0.0854 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.5011 L22: 0.5378
REMARK 3 L33: 1.0037 L12: 0.5044
REMARK 3 L13: -0.4818 L23: -0.6139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: -0.4001 S13: 0.0475
REMARK 3 S21: 0.0350 S22: 0.0402 S23: -0.0718
REMARK 3 S31: -0.2119 S32: 0.0665 S33: -0.0831
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8185 -4.2093 177.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.2368 T22: 0.5095
REMARK 3 T33: 0.1564 T12: 0.0234
REMARK 3 T13: 0.0064 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 0.1230 L22: 0.8703
REMARK 3 L33: 1.5628 L12: 0.2378
REMARK 3 L13: 0.4239 L23: 0.6847
REMARK 3 S TENSOR
REMARK 3 S11: -0.1237 S12: -0.3336 S13: 0.0068
REMARK 3 S21: 0.1806 S22: 0.1173 S23: -0.0817
REMARK 3 S31: 0.1675 S32: 0.4544 S33: 0.0064
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 162 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3552 -6.3142 183.8244
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.4761
REMARK 3 T33: 0.1746 T12: 0.0142
REMARK 3 T13: 0.0517 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 2.2557 L22: 1.6121
REMARK 3 L33: 2.4742 L12: -0.6155
REMARK 3 L13: -0.6288 L23: 0.4682
REMARK 3 S TENSOR
REMARK 3 S11: -0.1642 S12: -0.4223 S13: -0.1775
REMARK 3 S21: 0.1130 S22: 0.0279 S23: 0.1467
REMARK 3 S31: 0.1866 S32: 0.0191 S33: 0.1442
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9338 -12.3216 191.8078
REMARK 3 T TENSOR
REMARK 3 T11: 0.4442 T22: 0.9449
REMARK 3 T33: 0.2766 T12: 0.2060
REMARK 3 T13: 0.0575 T23: 0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 1.0157 L22: 0.8656
REMARK 3 L33: 1.2919 L12: 0.4582
REMARK 3 L13: 0.3467 L23: 0.2430
REMARK 3 S TENSOR
REMARK 3 S11: -0.1521 S12: -0.2989 S13: -0.1280
REMARK 3 S21: 0.1191 S22: 0.1685 S23: -0.0880
REMARK 3 S31: 0.4079 S32: 0.7515 S33: -0.0397
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 281 THROUGH 296 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7620 -19.1666 204.1487
REMARK 3 T TENSOR
REMARK 3 T11: 0.8081 T22: 0.9394
REMARK 3 T33: 0.3884 T12: 0.3325
REMARK 3 T13: 0.1631 T23: 0.2650
REMARK 3 L TENSOR
REMARK 3 L11: 1.8247 L22: 2.8190
REMARK 3 L33: 2.5882 L12: 1.0333
REMARK 3 L13: 0.5974 L23: -1.6186
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: -0.4117 S13: -0.1062
REMARK 3 S21: 0.6999 S22: -0.2250 S23: -0.2194
REMARK 3 S31: -0.3287 S32: 0.5026 S33: 0.2224
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 8SDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43884
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.09800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.30
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 (%): 53.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG3350, 0.2 M MGCL2, 0.1 M
REMARK 280 BIS-TRIS (PH 5.5), PH 7, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 29.24250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 VAL A 13 -158.80 -105.73
REMARK 500 PRO A 38 53.13 -99.56
REMARK 500 GLU A 39 -166.52 -111.51
REMARK 500 ALA A 77 17.08 59.37
REMARK 500 ASB A 107 -126.07 62.40
REMARK 500 TYR A 150 41.21 -100.99
REMARK 500 PRO A 161 36.82 -98.05
REMARK 500 ASP A 170 74.98 -164.48
REMARK 500 VAL B 13 -153.44 -116.88
REMARK 500 PRO B 38 52.44 -103.20
REMARK 500 ASB B 107 -127.84 57.55
REMARK 500 TYR B 150 45.10 -100.47
REMARK 500 PRO B 161 45.66 -105.41
REMARK 500 ASP B 170 74.75 -158.87
REMARK 500 ASP B 229 48.23 -140.90
REMARK 500 CYS B 272 -169.78 -160.02
REMARK 500 PHE B 275 67.11 -109.62
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 671 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 674 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 675 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 676 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 677 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 678 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 679 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 680 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A 681 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A 684 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A 685 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH A 686 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A 687 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A 688 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH A 690 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH A 691 DISTANCE = 8.86 ANGSTROMS
REMARK 525 HOH B 561 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 562 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 563 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B 564 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH B 565 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B 566 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH B 567 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH B 568 DISTANCE = 9.02 ANGSTROMS
REMARK 525 HOH B 569 DISTANCE = 9.05 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8SDC RELATED DB: PDB
DBREF 8SDD A 1 296 UNP Q479B8 Q479B8_DECAR 1 296
DBREF 8SDD B 1 296 UNP Q479B8 Q479B8_DECAR 1 296
SEQADV 8SDD ASN A 274 UNP Q479B8 HIS 274 ENGINEERED MUTATION
SEQADV 8SDD ASN B 274 UNP Q479B8 HIS 274 ENGINEERED MUTATION
SEQRES 1 A 296 MET PHE ASP SER SER TYR VAL THR ARG ASP VAL ASP VAL
SEQRES 2 A 296 GLY ALA THR ARG ILE HIS VAL ARG VAL ARG GLU ASN GLU
SEQRES 3 A 296 GLY ARG PRO PRO LEU LEU LEU LEU HIS GLY TYR PRO GLU
SEQRES 4 A 296 THR HIS ALA MET TRP HIS LYS VAL ALA SER LEU LEU GLN
SEQRES 5 A 296 ASP ARG PHE SER LEU VAL LEU PRO ASP LEU ARG GLY TYR
SEQRES 6 A 296 GLY ASP SER GLY MET PRO ALA SER GLN ALA ASP ALA GLY
SEQRES 7 A 296 ASN GLN SER LYS ARG VAL MET ALA GLN ASP MET ALA GLU
SEQRES 8 A 296 LEU MET THR ALA LEU GLY TYR GLN ARG PHE HIS VAL ALA
SEQRES 9 A 296 ALA HIS ASB ARG GLY ALA ARG VAL LEU HIS ARG LEU CYS
SEQRES 10 A 296 LEU ASP HIS PRO GLY ARG ILE GLN THR ALA CYS ILE MET
SEQRES 11 A 296 ASP ILE ALA PRO THR ALA THR THR PHE ALA LEU THR ASN
SEQRES 12 A 296 GLN ALA LEU ALA THR SER TYR PHE HIS TRP PHE PHE LEU
SEQRES 13 A 296 ILE GLN ALA ALA PRO LEU PRO GLU ASN MET ILE ALA ALA
SEQRES 14 A 296 ASP PRO ALA SER TRP LEU LYS GLY CYS LEU SER ARG TRP
SEQRES 15 A 296 SER MET GLY ASN GLU GLU ALA PHE ASP PRO ALA VAL VAL
SEQRES 16 A 296 SER GLU TYR VAL ARG CYS PHE SER ASN PRO GLU ALA ILE
SEQRES 17 A 296 ARG CYS SER CYS ASP ASP TYR ARG ALA ALA ALA GLY ILE
SEQRES 18 A 296 ASP LEU GLN HIS ASP GLY GLU ASP ALA GLU ARG ARG ILE
SEQRES 19 A 296 SER CYS PRO LEU LEU VAL LEU TRP GLY ASN LYS GLY PHE
SEQRES 20 A 296 VAL GLY ARG ASN TYR ASP VAL VAL ALA LEU TRP ARG GLU
SEQRES 21 A 296 LYS ALA LEU ASP VAL SER GLY LYS GLY LEU PRO CYS GLY
SEQRES 22 A 296 ASN PHE LEU PRO GLU GLU LEU PRO ASN ASP VAL ALA ARG
SEQRES 23 A 296 GLU LEU VAL GLU PHE ILE ALA ARG HIS SER
SEQRES 1 B 296 MET PHE ASP SER SER TYR VAL THR ARG ASP VAL ASP VAL
SEQRES 2 B 296 GLY ALA THR ARG ILE HIS VAL ARG VAL ARG GLU ASN GLU
SEQRES 3 B 296 GLY ARG PRO PRO LEU LEU LEU LEU HIS GLY TYR PRO GLU
SEQRES 4 B 296 THR HIS ALA MET TRP HIS LYS VAL ALA SER LEU LEU GLN
SEQRES 5 B 296 ASP ARG PHE SER LEU VAL LEU PRO ASP LEU ARG GLY TYR
SEQRES 6 B 296 GLY ASP SER GLY MET PRO ALA SER GLN ALA ASP ALA GLY
SEQRES 7 B 296 ASN GLN SER LYS ARG VAL MET ALA GLN ASP MET ALA GLU
SEQRES 8 B 296 LEU MET THR ALA LEU GLY TYR GLN ARG PHE HIS VAL ALA
SEQRES 9 B 296 ALA HIS ASB ARG GLY ALA ARG VAL LEU HIS ARG LEU CYS
SEQRES 10 B 296 LEU ASP HIS PRO GLY ARG ILE GLN THR ALA CYS ILE MET
SEQRES 11 B 296 ASP ILE ALA PRO THR ALA THR THR PHE ALA LEU THR ASN
SEQRES 12 B 296 GLN ALA LEU ALA THR SER TYR PHE HIS TRP PHE PHE LEU
SEQRES 13 B 296 ILE GLN ALA ALA PRO LEU PRO GLU ASN MET ILE ALA ALA
SEQRES 14 B 296 ASP PRO ALA SER TRP LEU LYS GLY CYS LEU SER ARG TRP
SEQRES 15 B 296 SER MET GLY ASN GLU GLU ALA PHE ASP PRO ALA VAL VAL
SEQRES 16 B 296 SER GLU TYR VAL ARG CYS PHE SER ASN PRO GLU ALA ILE
SEQRES 17 B 296 ARG CYS SER CYS ASP ASP TYR ARG ALA ALA ALA GLY ILE
SEQRES 18 B 296 ASP LEU GLN HIS ASP GLY GLU ASP ALA GLU ARG ARG ILE
SEQRES 19 B 296 SER CYS PRO LEU LEU VAL LEU TRP GLY ASN LYS GLY PHE
SEQRES 20 B 296 VAL GLY ARG ASN TYR ASP VAL VAL ALA LEU TRP ARG GLU
SEQRES 21 B 296 LYS ALA LEU ASP VAL SER GLY LYS GLY LEU PRO CYS GLY
SEQRES 22 B 296 ASN PHE LEU PRO GLU GLU LEU PRO ASN ASP VAL ALA ARG
SEQRES 23 B 296 GLU LEU VAL GLU PHE ILE ALA ARG HIS SER
MODRES 8SDD ASB A 107 ASP MODIFIED RESIDUE
MODRES 8SDD ASB B 107 ASP MODIFIED RESIDUE
HET ASB A 107 12
HET ASB B 107 12
HETNAM ASB ASPARTIC ACID-4-CARBOXYMETHYL ESTER
FORMUL 1 ASB 2(C6 H9 N O6)
FORMUL 3 HOH *660(H2 O)
HELIX 1 AA1 THR A 40 MET A 43 5 4
HELIX 2 AA2 TRP A 44 GLN A 52 1 9
HELIX 3 AA3 ALA A 77 GLN A 80 5 4
HELIX 4 AA4 SER A 81 LEU A 96 1 16
HELIX 5 AA5 ASB A 107 HIS A 120 1 14
HELIX 6 AA6 PRO A 134 LEU A 141 1 8
HELIX 7 AA7 ASN A 143 TYR A 150 1 8
HELIX 8 AA8 PHE A 151 LEU A 156 1 6
HELIX 9 AA9 PRO A 161 ALA A 168 1 8
HELIX 10 AB1 ASP A 170 SER A 183 1 14
HELIX 11 AB2 ASN A 186 PHE A 190 5 5
HELIX 12 AB3 ASP A 191 SER A 203 1 13
HELIX 13 AB4 ASN A 204 GLY A 220 1 17
HELIX 14 AB5 GLY A 220 ASP A 229 1 10
HELIX 15 AB6 GLY A 246 TYR A 252 1 7
HELIX 16 AB7 ASP A 253 GLU A 260 1 8
HELIX 17 AB8 PHE A 275 LEU A 280 1 6
HELIX 18 AB9 LEU A 280 HIS A 295 1 16
HELIX 19 AC1 THR B 40 HIS B 45 5 6
HELIX 20 AC2 LYS B 46 GLN B 52 1 7
HELIX 21 AC3 ALA B 77 GLN B 80 5 4
HELIX 22 AC4 SER B 81 LEU B 96 1 16
HELIX 23 AC5 ASB B 107 HIS B 120 1 14
HELIX 24 AC6 PRO B 134 LEU B 141 1 8
HELIX 25 AC7 ASN B 143 TYR B 150 1 8
HELIX 26 AC8 PHE B 151 LEU B 156 1 6
HELIX 27 AC9 PRO B 161 ALA B 169 1 9
HELIX 28 AD1 ASP B 170 SER B 183 1 14
HELIX 29 AD2 ASP B 191 SER B 203 1 13
HELIX 30 AD3 ASN B 204 ALA B 219 1 16
HELIX 31 AD4 GLY B 220 ASP B 229 1 10
HELIX 32 AD5 GLY B 246 TYR B 252 1 7
HELIX 33 AD6 ASP B 253 GLU B 260 1 8
HELIX 34 AD7 PHE B 275 LEU B 280 1 6
HELIX 35 AD8 LEU B 280 HIS B 295 1 16
SHEET 1 AA1 8 VAL A 7 ASP A 12 0
SHEET 2 AA1 8 ARG A 17 ARG A 23 -1 O VAL A 22 N VAL A 7
SHEET 3 AA1 8 SER A 56 PRO A 60 -1 O LEU A 59 N ARG A 21
SHEET 4 AA1 8 PRO A 30 LEU A 34 1 N LEU A 33 O VAL A 58
SHEET 5 AA1 8 PHE A 101 HIS A 106 1 O HIS A 102 N LEU A 32
SHEET 6 AA1 8 ILE A 124 MET A 130 1 O CYS A 128 N ALA A 105
SHEET 7 AA1 8 LEU A 238 GLY A 243 1 O LEU A 239 N ILE A 129
SHEET 8 AA1 8 VAL A 265 LEU A 270 1 O LEU A 270 N TRP A 242
SHEET 1 AA2 8 VAL B 7 ASP B 12 0
SHEET 2 AA2 8 ARG B 17 ARG B 23 -1 O VAL B 20 N ARG B 9
SHEET 3 AA2 8 SER B 56 PRO B 60 -1 O LEU B 59 N ARG B 21
SHEET 4 AA2 8 PRO B 30 LEU B 34 1 N LEU B 31 O SER B 56
SHEET 5 AA2 8 PHE B 101 HIS B 106 1 O HIS B 102 N LEU B 32
SHEET 6 AA2 8 ILE B 124 MET B 130 1 O GLN B 125 N PHE B 101
SHEET 7 AA2 8 LEU B 238 GLY B 243 1 O LEU B 239 N ILE B 129
SHEET 8 AA2 8 VAL B 265 LEU B 270 1 O SER B 266 N VAL B 240
LINK C HIS A 106 N ASB A 107 1555 1555 1.34
LINK C ASB A 107 N ARG A 108 1555 1555 1.34
LINK C HIS B 106 N ASB B 107 1555 1555 1.33
LINK C ASB B 107 N ARG B 108 1555 1555 1.33
CISPEP 1 TYR A 37 PRO A 38 0 -1.18
CISPEP 2 ALA A 160 PRO A 161 0 0.01
CISPEP 3 TYR B 37 PRO B 38 0 -1.22
CISPEP 4 ALA B 160 PRO B 161 0 0.90
CRYST1 42.937 58.485 138.188 90.00 93.02 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 0.023290 0.000000 0.001230 0.00000
SCALE2 0.000000 0.017098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007247 0.00000
TER 2333 SER A 296
TER 4654 SER B 296
MASTER 459 0 2 35 16 0 0 6 5300 2 28 46
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