| 7jiz-pdb | HEADER HYDROLASE 24-JUL-20 7JIZ
TITLE SCDLH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLIMONAS SP. K1W22B-7;
SOURCE 3 ORGANISM_TAXID: 2303331;
SOURCE 4 GENE: D0B54_07315;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DIENELACTONASE, HYDROLASE, PHOSPHOTRIESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.F.SCHNETTLER FERNANDEZ,E.C.CAMPBELL,F.H.HOLLFELDER
REVDAT 1 26-JAN-22 7JIZ 0
JRNL AUTH J.D.F.SCHNETTLER FERNANDEZ,E.C.CAMPBELL,F.HOLLFELDER
JRNL TITL SCDLH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN,
REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY,
REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON,
REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL,
REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS,
REMARK 1 AUTH 6 P.D.ADAMS
REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS,
REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX.
REMARK 1 REF ACTA CRYSTALLOGR D STRUCT V. 75 861 2019
REMARK 1 REF 2 BIOL
REMARK 1 REFN ISSN 2059-7983
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 40372
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2040
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 42.7500 - 4.5600 1.00 2628 160 0.1533 0.1737
REMARK 3 2 4.5600 - 3.6200 1.00 2607 130 0.1386 0.1394
REMARK 3 3 3.6200 - 3.1600 1.00 2632 134 0.1537 0.1808
REMARK 3 4 3.1600 - 2.8700 1.00 2628 115 0.1665 0.1857
REMARK 3 5 2.8700 - 2.6700 1.00 2632 126 0.1701 0.1975
REMARK 3 6 2.6700 - 2.5100 1.00 2620 128 0.1680 0.1910
REMARK 3 7 2.5100 - 2.3900 1.00 2581 151 0.1684 0.2209
REMARK 3 8 2.3900 - 2.2800 1.00 2619 139 0.1582 0.2083
REMARK 3 9 2.2800 - 2.1900 0.70 1811 100 0.1806 0.2103
REMARK 3 10 2.1900 - 2.1200 1.00 2603 124 0.1697 0.2304
REMARK 3 11 2.1200 - 2.0500 1.00 2607 140 0.1780 0.2033
REMARK 3 12 2.0500 - 1.9900 1.00 2601 151 0.1784 0.2145
REMARK 3 13 1.9900 - 1.9400 1.00 2584 141 0.1943 0.2433
REMARK 3 14 1.9400 - 1.8900 0.99 2544 154 0.3275 0.4291
REMARK 3 15 1.8900 - 1.8500 1.00 2635 147 0.2378 0.3225
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) : 0.192
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.09
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 : 0.003 3784
REMARK 3 ANGLE : 0.572 5156
REMARK 3 CHIRALITY : 0.042 550
REMARK 3 PLANARITY : 0.004 702
REMARK 3 DIHEDRAL : 23.435 1358
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 13:34 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.284 -23.444 29.235
REMARK 3 T TENSOR
REMARK 3 T11: 0.2570 T22: 0.1861
REMARK 3 T33: 0.2287 T12: -0.0640
REMARK 3 T13: 0.0256 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 4.4823 L22: 4.0810
REMARK 3 L33: 4.0909 L12: -1.7674
REMARK 3 L13: -1.0554 L23: 0.0812
REMARK 3 S TENSOR
REMARK 3 S11: -0.1270 S12: -0.4505 S13: -0.2879
REMARK 3 S21: 0.7160 S22: -0.0243 S23: 0.4107
REMARK 3 S31: 0.3331 S32: -0.0467 S33: 0.1496
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 35:100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.036 -24.297 16.038
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1977
REMARK 3 T33: 0.1941 T12: -0.0144
REMARK 3 T13: -0.0024 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 2.0792 L22: 2.4690
REMARK 3 L33: 2.9339 L12: -0.8423
REMARK 3 L13: 0.2243 L23: -0.1867
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: 0.1859 S13: -0.1027
REMARK 3 S21: -0.0722 S22: -0.0918 S23: -0.0708
REMARK 3 S31: 0.2264 S32: 0.2893 S33: 0.0574
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 101:125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.584 -18.940 21.613
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.1647
REMARK 3 T33: 0.1842 T12: -0.0124
REMARK 3 T13: -0.0117 T23: -0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 1.5455 L22: 2.8955
REMARK 3 L33: 4.6228 L12: 0.5947
REMARK 3 L13: -0.3972 L23: -1.9179
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: 0.0088 S13: -0.0687
REMARK 3 S21: 0.1766 S22: 0.0109 S23: 0.2327
REMARK 3 S31: -0.1370 S32: -0.3849 S33: -0.0327
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 126:238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.801 -9.781 11.845
REMARK 3 T TENSOR
REMARK 3 T11: 0.1401 T22: 0.1350
REMARK 3 T33: 0.1318 T12: 0.0473
REMARK 3 T13: -0.0058 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.6073 L22: 3.6144
REMARK 3 L33: 2.4316 L12: 0.7421
REMARK 3 L13: 0.2593 L23: 0.1658
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: 0.2743 S13: -0.1441
REMARK 3 S21: -0.1841 S22: -0.1079 S23: -0.1628
REMARK 3 S31: 0.0401 S32: 0.0671 S33: -0.0065
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 13:34 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.697 22.852 29.524
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2123
REMARK 3 T33: 0.1955 T12: -0.0282
REMARK 3 T13: 0.0237 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 3.6388 L22: 2.9302
REMARK 3 L33: 2.8969 L12: -1.1627
REMARK 3 L13: 0.4150 L23: 0.0204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0281 S12: -0.4182 S13: 0.1652
REMARK 3 S21: 0.3661 S22: -0.0020 S23: -0.0625
REMARK 3 S31: -0.2887 S32: 0.1850 S33: -0.0117
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 35:55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.245 19.624 23.393
REMARK 3 T TENSOR
REMARK 3 T11: 0.1644 T22: 0.2465
REMARK 3 T33: 0.2724 T12: -0.0178
REMARK 3 T13: 0.0445 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 2.3923 L22: 4.2625
REMARK 3 L33: 6.0061 L12: -1.2263
REMARK 3 L13: 1.1243 L23: -2.0866
REMARK 3 S TENSOR
REMARK 3 S11: -0.1048 S12: -0.1480 S13: -0.2545
REMARK 3 S21: 0.3831 S22: 0.0681 S23: 0.7508
REMARK 3 S31: 0.0633 S32: -0.9728 S33: -0.0601
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 56:67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.285 24.081 21.924
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.1115
REMARK 3 T33: 0.1695 T12: -0.0284
REMARK 3 T13: -0.0043 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.4690 L22: 1.1518
REMARK 3 L33: 2.4231 L12: -0.6881
REMARK 3 L13: 0.1890 L23: -0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: 0.0139 S13: 0.1140
REMARK 3 S21: 0.1310 S22: -0.0578 S23: 0.0854
REMARK 3 S31: 0.0033 S32: -0.0402 S33: 0.0222
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 68:100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.216 27.543 8.833
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.2032
REMARK 3 T33: 0.2390 T12: 0.0108
REMARK 3 T13: 0.0070 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 1.1661 L22: 1.5098
REMARK 3 L33: 2.0189 L12: -0.6754
REMARK 3 L13: -0.4588 L23: 0.4394
REMARK 3 S TENSOR
REMARK 3 S11: 0.1540 S12: 0.2538 S13: 0.2916
REMARK 3 S21: -0.3183 S22: -0.1996 S23: 0.0266
REMARK 3 S31: -0.2291 S32: -0.0818 S33: 0.0372
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN B AND RESID 101:125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.713 18.713 22.030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1886 T22: 0.1697
REMARK 3 T33: 0.2117 T12: 0.0203
REMARK 3 T13: 0.0176 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 1.7113 L22: 2.9885
REMARK 3 L33: 5.1225 L12: 1.0125
REMARK 3 L13: 0.2352 L23: 1.9686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0632 S12: -0.0107 S13: -0.0467
REMARK 3 S21: 0.1312 S22: 0.0391 S23: -0.1948
REMARK 3 S31: 0.0647 S32: 0.4216 S33: -0.0705
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND RESID 126:171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.066 12.546 9.634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1611 T22: 0.1485
REMARK 3 T33: 0.1303 T12: 0.0391
REMARK 3 T13: 0.0191 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 1.4566 L22: 3.2691
REMARK 3 L33: 1.9520 L12: 0.8020
REMARK 3 L13: -0.3491 L23: -0.2731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.1965 S13: -0.0035
REMARK 3 S21: -0.2949 S22: 0.0234 S23: 0.0114
REMARK 3 S31: -0.0774 S32: 0.0267 S33: -0.0227
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN B AND RESID 172:218 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.315 8.853 9.137
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.1748
REMARK 3 T33: 0.2511 T12: 0.0606
REMARK 3 T13: -0.0088 T23: 0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 3.2817 L22: 2.6398
REMARK 3 L33: 2.1832 L12: 0.3491
REMARK 3 L13: -0.6760 L23: 0.1598
REMARK 3 S TENSOR
REMARK 3 S11: 0.1980 S12: 0.3380 S13: 0.4512
REMARK 3 S21: -0.2787 S22: -0.1089 S23: 0.4206
REMARK 3 S31: -0.2874 S32: -0.3162 S33: -0.0681
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN B AND RESID 219:231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.252 5.825 21.946
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.1919
REMARK 3 T33: 0.2459 T12: -0.0012
REMARK 3 T13: 0.0485 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 4.3198 L22: 3.6863
REMARK 3 L33: 3.1567 L12: 2.0214
REMARK 3 L13: 2.3394 L23: 1.4559
REMARK 3 S TENSOR
REMARK 3 S11: 0.2139 S12: -0.4908 S13: 0.2284
REMARK 3 S21: 0.2308 S22: -0.2392 S23: 0.4734
REMARK 3 S31: 0.1500 S32: -0.3179 S33: 0.0303
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN B AND RESID 232:238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.543 6.360 25.423
REMARK 3 T TENSOR
REMARK 3 T11: 0.2088 T22: 0.1851
REMARK 3 T33: 0.1318 T12: 0.0328
REMARK 3 T13: 0.0001 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 4.8688 L22: 7.0932
REMARK 3 L33: 5.3308 L12: 1.7485
REMARK 3 L13: 0.6871 L23: 1.4568
REMARK 3 S TENSOR
REMARK 3 S11: 0.1369 S12: -0.2899 S13: -0.2561
REMARK 3 S21: 0.5050 S22: -0.0900 S23: -0.4492
REMARK 3 S31: 0.4317 S32: 0.3688 S33: -0.1346
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 7JIZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1000250601.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40398
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 42.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08356
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53640
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3F67
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3000, 0.1 M TRIS, PH 7, 0.2
REMARK 280 M CALCIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 292K
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 61.80200
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: 1360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 TRP A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 PRO A -6
REMARK 465 GLN A -5
REMARK 465 PHE A -4
REMARK 465 GLU A -3
REMARK 465 LYS A -2
REMARK 465 GLY A -1
REMARK 465 ASN A 239
REMARK 465 MET B -12
REMARK 465 ALA B -11
REMARK 465 SER B -10
REMARK 465 TRP B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 PRO B -6
REMARK 465 GLN B -5
REMARK 465 PHE B -4
REMARK 465 GLU B -3
REMARK 465 LYS B -2
REMARK 465 GLY B -1
REMARK 465 ASN B 239
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 383 O HOH B 415 1.95
REMARK 500 O HOH A 486 O HOH A 511 1.96
REMARK 500 O HOH B 357 O HOH B 460 1.96
REMARK 500 O HOH A 459 O HOH A 494 1.99
REMARK 500 O HOH A 457 O HOH A 536 2.00
REMARK 500 O HOH A 318 O HOH A 320 2.04
REMARK 500 O HOH B 461 O HOH B 477 2.05
REMARK 500 NH2 ARG B 29 O HOH B 301 2.06
REMARK 500 O SER A 72 O HOH A 301 2.10
REMARK 500 O GLY A 27 O HOH A 302 2.11
REMARK 500 O HOH A 464 O HOH B 516 2.12
REMARK 500 O HOH B 370 O HOH B 495 2.14
REMARK 500 O HOH B 467 O HOH B 521 2.15
REMARK 500 O HOH A 397 O HOH B 411 2.15
REMARK 500 O HOH A 414 O HOH A 497 2.15
REMARK 500 O HOH A 496 O HOH A 508 2.16
REMARK 500 O ALA A 0 O HOH A 303 2.19
REMARK 500 O HOH B 502 O HOH B 546 2.19
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 306 O HOH A 315 1556 1.91
REMARK 500 O HOH A 312 O HOH B 504 2646 2.04
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 PRO A 12 74.41 -58.33
REMARK 500 THR A 13 111.83 61.27
REMARK 500 CYS A 119 -122.77 57.44
REMARK 500 CYS A 119 -117.86 52.29
REMARK 500 HIS A 142 59.73 39.20
REMARK 500 ALA A 199 -139.26 -122.89
REMARK 500 LEU B 41 99.89 -67.98
REMARK 500 CYS B 119 -120.18 54.62
REMARK 500 CYS B 119 -119.85 58.82
REMARK 500 HIS B 142 57.37 39.44
REMARK 500 ASP B 189 97.13 -68.57
REMARK 500 ALA B 199 -144.15 -124.03
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 556 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 557 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 558 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 559 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 560 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B 548 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 549 DISTANCE = 5.88 ANGSTROMS
DBREF1 7JIZ A 1 239 UNP A0A346MYW6_9GAMM
DBREF2 7JIZ A A0A346MYW6 1 239
DBREF1 7JIZ B 1 239 UNP A0A346MYW6_9GAMM
DBREF2 7JIZ B A0A346MYW6 1 239
SEQADV 7JIZ MET A -12 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ ALA A -11 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER A -10 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ TRP A -9 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER A -8 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ HIS A -7 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ PRO A -6 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLN A -5 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ PHE A -4 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLU A -3 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ LYS A -2 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLY A -1 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ ALA A 0 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER A 73 UNP A0A346MYW ASP 73 CONFLICT
SEQADV 7JIZ MET B -12 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ ALA B -11 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER B -10 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ TRP B -9 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER B -8 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ HIS B -7 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ PRO B -6 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLN B -5 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ PHE B -4 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLU B -3 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ LYS B -2 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ GLY B -1 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ ALA B 0 UNP A0A346MYW EXPRESSION TAG
SEQADV 7JIZ SER B 73 UNP A0A346MYW ASP 73 CONFLICT
SEQRES 1 A 252 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 252 MET ARG LYS GLN LYS ILE GLU TYR GLY ASN GLY PRO THR
SEQRES 3 A 252 GLN PHE HIS GLY TRP LEU ILE ARG ASP ASP SER LEU ASP
SEQRES 4 A 252 GLY VAL ARG PRO GLY VAL LEU VAL PHE PRO GLU ALA TYR
SEQRES 5 A 252 GLY LEU ASN GLU HIS ALA ILE GLU ARG ALA GLU ARG LEU
SEQRES 6 A 252 ALA GLN LEU GLY TYR VAL ALA LEU ALA ALA ASP MET HIS
SEQRES 7 A 252 GLY GLY GLY VAL VAL TYR SER SER THR ALA THR LEU GLY
SEQRES 8 A 252 PRO ALA ILE ARG SER LEU PHE GLY ASP ARG ALA GLU TRP
SEQRES 9 A 252 ARG ALA ARG ALA GLN ALA ALA LEU ASP ALA LEU LEU ALA
SEQRES 10 A 252 GLN PRO GLN VAL ASP ARG ASP ARG VAL ALA ALA ILE GLY
SEQRES 11 A 252 PHE CYS PHE GLY GLY ALA THR CYS LEU GLU LEU ALA ARG
SEQRES 12 A 252 SER GLY ALA PRO LEU SER ALA LEU VAL THR PHE HIS ALA
SEQRES 13 A 252 GLY LEU GLN PRO PRO LEU GLU ALA ASP ALA GLY ARG ILE
SEQRES 14 A 252 THR GLY LYS VAL LEU ILE CYS HIS GLY ALA GLU ASP PRO
SEQRES 15 A 252 LEU MET LYS PRO GLU ALA LEU ASN ALA VAL LEU ALA GLU
SEQRES 16 A 252 LEU SER ARG ASP ARG VAL ASP TRP GLN LEU LEU SER PHE
SEQRES 17 A 252 GLY GLY VAL ALA HIS SER PHE THR ASN PRO ASP ALA ASP
SEQRES 18 A 252 ALA ARG GLY ALA PRO GLY PHE ALA TYR ASN ALA ASN ALA
SEQRES 19 A 252 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU PHE ALA
SEQRES 20 A 252 GLU VAL PHE ALA ASN
SEQRES 1 B 252 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 252 MET ARG LYS GLN LYS ILE GLU TYR GLY ASN GLY PRO THR
SEQRES 3 B 252 GLN PHE HIS GLY TRP LEU ILE ARG ASP ASP SER LEU ASP
SEQRES 4 B 252 GLY VAL ARG PRO GLY VAL LEU VAL PHE PRO GLU ALA TYR
SEQRES 5 B 252 GLY LEU ASN GLU HIS ALA ILE GLU ARG ALA GLU ARG LEU
SEQRES 6 B 252 ALA GLN LEU GLY TYR VAL ALA LEU ALA ALA ASP MET HIS
SEQRES 7 B 252 GLY GLY GLY VAL VAL TYR SER SER THR ALA THR LEU GLY
SEQRES 8 B 252 PRO ALA ILE ARG SER LEU PHE GLY ASP ARG ALA GLU TRP
SEQRES 9 B 252 ARG ALA ARG ALA GLN ALA ALA LEU ASP ALA LEU LEU ALA
SEQRES 10 B 252 GLN PRO GLN VAL ASP ARG ASP ARG VAL ALA ALA ILE GLY
SEQRES 11 B 252 PHE CYS PHE GLY GLY ALA THR CYS LEU GLU LEU ALA ARG
SEQRES 12 B 252 SER GLY ALA PRO LEU SER ALA LEU VAL THR PHE HIS ALA
SEQRES 13 B 252 GLY LEU GLN PRO PRO LEU GLU ALA ASP ALA GLY ARG ILE
SEQRES 14 B 252 THR GLY LYS VAL LEU ILE CYS HIS GLY ALA GLU ASP PRO
SEQRES 15 B 252 LEU MET LYS PRO GLU ALA LEU ASN ALA VAL LEU ALA GLU
SEQRES 16 B 252 LEU SER ARG ASP ARG VAL ASP TRP GLN LEU LEU SER PHE
SEQRES 17 B 252 GLY GLY VAL ALA HIS SER PHE THR ASN PRO ASP ALA ASP
SEQRES 18 B 252 ALA ARG GLY ALA PRO GLY PHE ALA TYR ASN ALA ASN ALA
SEQRES 19 B 252 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU PHE ALA
SEQRES 20 B 252 GLU VAL PHE ALA ASN
FORMUL 3 HOH *509(H2 O)
HELIX 1 AA1 ASN A 42 LEU A 55 1 14
HELIX 2 AA2 SER A 73 ASP A 87 1 15
HELIX 3 AA3 ASP A 87 ALA A 104 1 18
HELIX 4 AA4 CYS A 119 SER A 131 1 13
HELIX 5 AA5 LEU A 149 ALA A 153 5 5
HELIX 6 AA6 LYS A 172 ASP A 186 1 15
HELIX 7 AA7 ASN A 218 PHE A 237 1 20
HELIX 8 AA8 ASN B 42 LEU B 55 1 14
HELIX 9 AA9 SER B 73 GLY B 86 1 14
HELIX 10 AB1 ASP B 87 ALA B 104 1 18
HELIX 11 AB2 CYS B 119 SER B 131 1 13
HELIX 12 AB3 LEU B 149 ALA B 153 5 5
HELIX 13 AB4 LYS B 172 ASP B 186 1 15
HELIX 14 AB5 ASN B 218 PHE B 237 1 20
SHEET 1 AA116 ARG A 2 TYR A 8 0
SHEET 2 AA116 PHE A 15 ARG A 21 -1 O LEU A 19 N GLN A 4
SHEET 3 AA116 VAL A 58 ALA A 61 -1 O ALA A 61 N TRP A 18
SHEET 4 AA116 ARG A 29 PHE A 35 1 N PRO A 30 O VAL A 58
SHEET 5 AA116 VAL A 108 PHE A 118 1 O ASP A 109 N ARG A 29
SHEET 6 AA116 ALA A 137 PHE A 141 1 O PHE A 141 N GLY A 117
SHEET 7 AA116 LYS A 159 GLY A 165 1 O CYS A 163 N THR A 140
SHEET 8 AA116 TRP A 190 PHE A 195 1 O LEU A 193 N ILE A 162
SHEET 9 AA116 TRP B 190 PHE B 195 -1 O SER B 194 N LEU A 192
SHEET 10 AA116 LYS B 159 GLY B 165 1 N ILE B 162 O LEU B 193
SHEET 11 AA116 ALA B 137 PHE B 141 1 N THR B 140 O CYS B 163
SHEET 12 AA116 VAL B 108 PHE B 118 1 N GLY B 117 O PHE B 141
SHEET 13 AA116 ARG B 29 PHE B 35 1 N ARG B 29 O ASP B 109
SHEET 14 AA116 VAL B 58 ALA B 61 1 O VAL B 58 N PRO B 30
SHEET 15 AA116 PHE B 15 ARG B 21 -1 N TRP B 18 O ALA B 61
SHEET 16 AA116 ARG B 2 TYR B 8 -1 N GLN B 4 O LEU B 19
CRYST1 43.550 123.604 46.655 90.00 100.98 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 0.022962 0.000000 0.004455 0.00000
SCALE2 0.000000 0.008090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021834 0.00000
TER 1854 ALA A 238
TER 3692 ALA B 238
MASTER 537 0 0 14 16 0 0 6 4105 2 0 40
END
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