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HEADER HYDROLASE 06-APR-23 8SDC
TITLE CRYSTAL STRUCTURE OF FLUOROACETATE DEHALOGENASE DARO3835 APOENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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 06-SEP-23 8SDC 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. 2023
JRNL REFN ISSN 1742-464X
JRNL PMID 37437000
JRNL DOI 10.1111/FEBS.16903
REMARK 2
REMARK 2 RESOLUTION. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 40567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.127
REMARK 3 R VALUE (WORKING SET) : 0.125
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.240
REMARK 3 FREE R VALUE TEST SET COUNT : 2127
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 19.6600 - 4.5700 0.99 2673 160 0.1358 0.2012
REMARK 3 2 4.5700 - 3.6300 0.98 2653 155 0.1029 0.1205
REMARK 3 3 3.6300 - 3.1800 0.97 2632 141 0.1109 0.1601
REMARK 3 4 3.1800 - 2.8900 0.96 2618 141 0.1274 0.1546
REMARK 3 5 2.8900 - 2.6800 0.96 2563 153 0.1325 0.1705
REMARK 3 6 2.6800 - 2.5200 0.95 2583 143 0.1386 0.1975
REMARK 3 7 2.5200 - 2.4000 0.95 2584 137 0.1316 0.2048
REMARK 3 8 2.4000 - 2.2900 0.94 2607 126 0.1261 0.1867
REMARK 3 9 2.2900 - 2.2000 0.94 2529 155 0.1241 0.1758
REMARK 3 10 2.2000 - 2.1300 0.93 2503 146 0.1190 0.1826
REMARK 3 11 2.1300 - 2.0600 0.93 2478 145 0.1268 0.1858
REMARK 3 12 2.0600 - 2.0000 0.92 2526 145 0.1297 0.1876
REMARK 3 13 2.0000 - 1.9500 0.92 2486 144 0.1321 0.1921
REMARK 3 14 1.9500 - 1.9000 0.92 2497 110 0.1363 0.2187
REMARK 3 15 1.9000 - 1.8600 0.91 2508 126 0.1354 0.1895
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) : 0.147
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.583
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.44
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 : 0.008 4798
REMARK 3 ANGLE : 0.897 6530
REMARK 3 CHIRALITY : 0.056 704
REMARK 3 PLANARITY : 0.006 863
REMARK 3 DIHEDRAL : 20.195 1754
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 1:24)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5361 22.2525 65.2816
REMARK 3 T TENSOR
REMARK 3 T11: 0.1424 T22: 0.1108
REMARK 3 T33: 0.0761 T12: -0.0190
REMARK 3 T13: 0.0106 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 7.3736 L22: 4.2423
REMARK 3 L33: 4.4245 L12: -2.0831
REMARK 3 L13: -2.1621 L23: -0.3049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.3634 S13: 0.4670
REMARK 3 S21: -0.1207 S22: -0.0007 S23: -0.1972
REMARK 3 S31: -0.1706 S32: 0.1649 S33: -0.0094
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 25:141)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0870 14.2318 74.3874
REMARK 3 T TENSOR
REMARK 3 T11: 0.0619 T22: 0.0531
REMARK 3 T33: 0.0657 T12: -0.0047
REMARK 3 T13: -0.0071 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.3393 L22: 1.2745
REMARK 3 L33: 1.5037 L12: -0.0781
REMARK 3 L13: -0.3599 L23: -0.1513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.0857 S13: -0.0593
REMARK 3 S21: -0.0490 S22: -0.0103 S23: 0.0194
REMARK 3 S31: 0.0468 S32: 0.0297 S33: 0.0421
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 142:186)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8968 26.0454 92.3087
REMARK 3 T TENSOR
REMARK 3 T11: 0.0976 T22: 0.0767
REMARK 3 T33: 0.0544 T12: -0.0011
REMARK 3 T13: -0.0004 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.9980 L22: 1.4364
REMARK 3 L33: 1.6006 L12: 0.0562
REMARK 3 L13: -0.4252 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0994 S12: -0.0327 S13: 0.0195
REMARK 3 S21: 0.0601 S22: 0.1112 S23: -0.1070
REMARK 3 S31: -0.0705 S32: 0.1050 S33: -0.0092
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 187:232)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.8555 22.4821 81.7190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.0737
REMARK 3 T33: 0.0282 T12: 0.0098
REMARK 3 T13: 0.0085 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.6452 L22: 2.8479
REMARK 3 L33: 0.9871 L12: 0.1870
REMARK 3 L13: -0.4244 L23: -0.3017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: -0.0979 S13: 0.0481
REMARK 3 S21: -0.0801 S22: -0.0686 S23: 0.0063
REMARK 3 S31: -0.0005 S32: 0.0343 S33: 0.0657
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 233:285)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3485 6.7757 87.2352
REMARK 3 T TENSOR
REMARK 3 T11: 0.1059 T22: 0.0835
REMARK 3 T33: 0.1238 T12: 0.0377
REMARK 3 T13: 0.0137 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 1.6400 L22: 2.0781
REMARK 3 L33: 1.7424 L12: 0.8655
REMARK 3 L13: -0.1846 L23: 0.1869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0604 S12: -0.1121 S13: -0.1924
REMARK 3 S21: 0.1671 S22: -0.0098 S23: -0.0312
REMARK 3 S31: 0.1868 S32: 0.0756 S33: 0.0604
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 286:296)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0616 0.7963 76.4089
REMARK 3 T TENSOR
REMARK 3 T11: 0.1545 T22: 0.1282
REMARK 3 T33: 0.2110 T12: 0.0862
REMARK 3 T13: 0.0004 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 8.6260 L22: 9.2460
REMARK 3 L33: 6.8731 L12: 0.9164
REMARK 3 L13: -0.9740 L23: 0.7622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: 0.4199 S13: -0.6501
REMARK 3 S21: -0.0564 S22: -0.1073 S23: -0.1792
REMARK 3 S31: 0.6381 S32: 0.2089 S33: 0.0871
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 1:26)
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8170 46.9119 123.8925
REMARK 3 T TENSOR
REMARK 3 T11: 0.1671 T22: 0.1251
REMARK 3 T33: 0.0956 T12: 0.0093
REMARK 3 T13: -0.0031 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 5.1937 L22: 4.2195
REMARK 3 L33: 1.3036 L12: -2.5209
REMARK 3 L13: -1.7713 L23: 1.5247
REMARK 3 S TENSOR
REMARK 3 S11: 0.0323 S12: -0.3120 S13: 0.3718
REMARK 3 S21: 0.0654 S22: 0.0006 S23: 0.0007
REMARK 3 S31: -0.1430 S32: -0.0378 S33: -0.0433
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 27:141)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9335 33.5734 120.5970
REMARK 3 T TENSOR
REMARK 3 T11: 0.0500 T22: 0.0766
REMARK 3 T33: 0.0553 T12: -0.0026
REMARK 3 T13: -0.0142 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.0561 L22: 1.1327
REMARK 3 L33: 1.1628 L12: -0.1048
REMARK 3 L13: -0.2982 L23: 0.3505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.0919 S13: 0.0378
REMARK 3 S21: 0.0438 S22: -0.0071 S23: -0.0221
REMARK 3 S31: -0.0016 S32: -0.0189 S33: 0.0154
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 142:186)
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8742 30.9106 99.7442
REMARK 3 T TENSOR
REMARK 3 T11: 0.0976 T22: 0.0840
REMARK 3 T33: 0.0487 T12: 0.0068
REMARK 3 T13: 0.0029 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.4902 L22: 2.4200
REMARK 3 L33: 1.5102 L12: -0.0674
REMARK 3 L13: 0.1312 L23: 0.4903
REMARK 3 S TENSOR
REMARK 3 S11: -0.0802 S12: 0.0138 S13: 0.0405
REMARK 3 S21: -0.0791 S22: 0.0632 S23: 0.0147
REMARK 3 S31: -0.0900 S32: -0.0935 S33: 0.0123
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 187:232)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.5467 33.7665 110.6328
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.0752
REMARK 3 T33: 0.0176 T12: 0.0013
REMARK 3 T13: -0.0110 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 1.7665 L22: 3.3028
REMARK 3 L33: 1.6449 L12: -0.6001
REMARK 3 L13: -0.2601 L23: -0.9054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0598 S12: 0.0957 S13: -0.0084
REMARK 3 S21: 0.0855 S22: -0.0859 S23: -0.0484
REMARK 3 S31: -0.1224 S32: 0.0452 S33: 0.0054
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 233:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -56.3903 24.0587 114.3271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0816 T22: 0.1352
REMARK 3 T33: 0.1056 T12: -0.0356
REMARK 3 T13: 0.0097 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.4707 L22: 2.6097
REMARK 3 L33: 2.2474 L12: -0.9563
REMARK 3 L13: 0.6915 L23: -1.2454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: 0.0507 S13: -0.0945
REMARK 3 S21: -0.1794 S22: -0.0587 S23: 0.0864
REMARK 3 S31: 0.2190 S32: -0.1458 S33: 0.0605
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 288:297)
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4121 27.9530 127.7485
REMARK 3 T TENSOR
REMARK 3 T11: 0.1624 T22: 0.2821
REMARK 3 T33: 0.1762 T12: 0.0208
REMARK 3 T13: 0.0685 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.5480 L22: 4.0936
REMARK 3 L33: 4.8592 L12: 0.5282
REMARK 3 L13: 0.4481 L23: 1.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.1182 S12: -0.7941 S13: -0.3965
REMARK 3 S21: 0.7564 S22: -0.0784 S23: 0.5771
REMARK 3 S31: 0.2738 S32: -0.4518 S33: 0.1078
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 8SDC 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_1000273599.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-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 : 40571
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 19.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.09200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.400
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 (%): 38.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG3350, 0.2 M MGCL2, 0.1 M
REMARK 280 BIS-TRIS PH 5.5, CRYOPROTECTANT 2% (V/V) PEG 200 AND PARATONE,
REMARK 280 PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 SER A 297
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 196 O HOH B 401 2.15
REMARK 500 OE2 GLU A 228 O HOH A 401 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 VAL A 13 -163.08 -106.50
REMARK 500 PRO A 38 53.87 -100.34
REMARK 500 GLU A 39 -169.01 -111.64
REMARK 500 ASP A 107 -130.48 61.36
REMARK 500 TYR A 150 43.71 -101.30
REMARK 500 ASP A 170 76.91 -163.59
REMARK 500 PHE B 2 -137.32 -107.35
REMARK 500 PRO B 38 53.56 -99.14
REMARK 500 GLU B 39 -167.88 -110.18
REMARK 500 ASP B 107 -127.72 59.86
REMARK 500 TYR B 150 46.05 -100.67
REMARK 500 ASP B 170 75.08 -162.16
REMARK 500 ASP B 264 86.08 -151.89
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 879 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A 880 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 881 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 893 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 894 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B 895 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 896 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 897 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B 898 DISTANCE = 6.56 ANGSTROMS
DBREF 8SDC A 1 297 UNP Q479B8 Q479B8_DECAR 1 297
DBREF 8SDC B 1 297 UNP Q479B8 Q479B8_DECAR 1 297
SEQRES 1 A 297 MET PHE ASP SER SER TYR VAL THR ARG ASP VAL ASP VAL
SEQRES 2 A 297 GLY ALA THR ARG ILE HIS VAL ARG VAL ARG GLU ASN GLU
SEQRES 3 A 297 GLY ARG PRO PRO LEU LEU LEU LEU HIS GLY TYR PRO GLU
SEQRES 4 A 297 THR HIS ALA MET TRP HIS LYS VAL ALA SER LEU LEU GLN
SEQRES 5 A 297 ASP ARG PHE SER LEU VAL LEU PRO ASP LEU ARG GLY TYR
SEQRES 6 A 297 GLY ASP SER GLY MET PRO ALA SER GLN ALA ASP ALA GLY
SEQRES 7 A 297 ASN GLN SER LYS ARG VAL MET ALA GLN ASP MET ALA GLU
SEQRES 8 A 297 LEU MET THR ALA LEU GLY TYR GLN ARG PHE HIS VAL ALA
SEQRES 9 A 297 ALA HIS ASP ARG GLY ALA ARG VAL LEU HIS ARG LEU CYS
SEQRES 10 A 297 LEU ASP HIS PRO GLY ARG ILE GLN THR ALA CYS ILE MET
SEQRES 11 A 297 ASP ILE ALA PRO THR ALA THR THR PHE ALA LEU THR ASN
SEQRES 12 A 297 GLN ALA LEU ALA THR SER TYR PHE HIS TRP PHE PHE LEU
SEQRES 13 A 297 ILE GLN ALA ALA PRO LEU PRO GLU ASN MET ILE ALA ALA
SEQRES 14 A 297 ASP PRO ALA SER TRP LEU LYS GLY CYS LEU SER ARG TRP
SEQRES 15 A 297 SER MET GLY ASN GLU GLU ALA PHE ASP PRO ALA VAL VAL
SEQRES 16 A 297 SER GLU TYR VAL ARG CYS PHE SER ASN PRO GLU ALA ILE
SEQRES 17 A 297 ARG CYS SER CYS ASP ASP TYR ARG ALA ALA ALA GLY ILE
SEQRES 18 A 297 ASP LEU GLN HIS ASP GLY GLU ASP ALA GLU ARG ARG ILE
SEQRES 19 A 297 SER CYS PRO LEU LEU VAL LEU TRP GLY ASN LYS GLY PHE
SEQRES 20 A 297 VAL GLY ARG ASN TYR ASP VAL VAL ALA LEU TRP ARG GLU
SEQRES 21 A 297 LYS ALA LEU ASP VAL SER GLY LYS GLY LEU PRO CYS GLY
SEQRES 22 A 297 HIS PHE LEU PRO GLU GLU LEU PRO ASN ASP VAL ALA ARG
SEQRES 23 A 297 GLU LEU VAL GLU PHE ILE ALA ARG HIS SER SER
SEQRES 1 B 297 MET PHE ASP SER SER TYR VAL THR ARG ASP VAL ASP VAL
SEQRES 2 B 297 GLY ALA THR ARG ILE HIS VAL ARG VAL ARG GLU ASN GLU
SEQRES 3 B 297 GLY ARG PRO PRO LEU LEU LEU LEU HIS GLY TYR PRO GLU
SEQRES 4 B 297 THR HIS ALA MET TRP HIS LYS VAL ALA SER LEU LEU GLN
SEQRES 5 B 297 ASP ARG PHE SER LEU VAL LEU PRO ASP LEU ARG GLY TYR
SEQRES 6 B 297 GLY ASP SER GLY MET PRO ALA SER GLN ALA ASP ALA GLY
SEQRES 7 B 297 ASN GLN SER LYS ARG VAL MET ALA GLN ASP MET ALA GLU
SEQRES 8 B 297 LEU MET THR ALA LEU GLY TYR GLN ARG PHE HIS VAL ALA
SEQRES 9 B 297 ALA HIS ASP ARG GLY ALA ARG VAL LEU HIS ARG LEU CYS
SEQRES 10 B 297 LEU ASP HIS PRO GLY ARG ILE GLN THR ALA CYS ILE MET
SEQRES 11 B 297 ASP ILE ALA PRO THR ALA THR THR PHE ALA LEU THR ASN
SEQRES 12 B 297 GLN ALA LEU ALA THR SER TYR PHE HIS TRP PHE PHE LEU
SEQRES 13 B 297 ILE GLN ALA ALA PRO LEU PRO GLU ASN MET ILE ALA ALA
SEQRES 14 B 297 ASP PRO ALA SER TRP LEU LYS GLY CYS LEU SER ARG TRP
SEQRES 15 B 297 SER MET GLY ASN GLU GLU ALA PHE ASP PRO ALA VAL VAL
SEQRES 16 B 297 SER GLU TYR VAL ARG CYS PHE SER ASN PRO GLU ALA ILE
SEQRES 17 B 297 ARG CYS SER CYS ASP ASP TYR ARG ALA ALA ALA GLY ILE
SEQRES 18 B 297 ASP LEU GLN HIS ASP GLY GLU ASP ALA GLU ARG ARG ILE
SEQRES 19 B 297 SER CYS PRO LEU LEU VAL LEU TRP GLY ASN LYS GLY PHE
SEQRES 20 B 297 VAL GLY ARG ASN TYR ASP VAL VAL ALA LEU TRP ARG GLU
SEQRES 21 B 297 LYS ALA LEU ASP VAL SER GLY LYS GLY LEU PRO CYS GLY
SEQRES 22 B 297 HIS PHE LEU PRO GLU GLU LEU PRO ASN ASP VAL ALA ARG
SEQRES 23 B 297 GLU LEU VAL GLU PHE ILE ALA ARG HIS SER SER
HET CL A 301 1
HET CL B 301 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *979(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 ASP 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 169 1 9
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 ALA A 219 1 16
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 MET B 43 5 4
HELIX 20 AC2 TRP B 44 GLN B 52 1 9
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 ASP 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 ASN B 186 PHE B 190 5 5
HELIX 30 AD3 ASP B 191 SER B 203 1 13
HELIX 31 AD4 ASN B 204 GLY B 220 1 17
HELIX 32 AD5 GLY B 220 ASP B 229 1 10
HELIX 33 AD6 GLY B 246 TYR B 252 1 7
HELIX 34 AD7 ASP B 253 GLU B 260 1 8
HELIX 35 AD8 PHE B 275 LEU B 280 1 6
HELIX 36 AD9 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 31 O SER A 56
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 GLN A 125 N PHE A 101
SHEET 7 AA1 8 LEU A 238 GLY A 243 1 O LEU A 239 N ALA A 127
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 ILE B 18 N VAL B 11
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 CYS B 128 N ALA B 105
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 LEU B 270 N TRP B 242
CISPEP 1 TYR A 37 PRO A 38 0 -1.36
CISPEP 2 ALA A 160 PRO A 161 0 2.27
CISPEP 3 TYR B 37 PRO B 38 0 -1.30
CISPEP 4 ALA B 160 PRO B 161 0 4.63
CRYST1 45.172 45.224 75.185 87.63 75.57 63.04 P 1 2
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 0.022138 -0.011263 -0.006656 0.00000
SCALE2 0.000000 0.024809 0.002065 0.00000
SCALE3 0.000000 0.000000 0.013782 0.00000
TER 2335 SER A 296
TER 4675 SER B 297
MASTER 447 0 2 36 16 0 0 6 5623 2 0 46
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