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HEADER HYDROLASE 28-JUL-17 5OLU
TITLE THE CRYSTAL STRUCTURE OF A HIGHLY THERMOSTABLE CARBOXYL ESTERASE FROM
TITLE 2 BACILLUS COAGULANS IN COMPLEX WITH GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS COAGULANS DSM 1 = ATCC 7050;
SOURCE 3 ORGANISM_TAXID: 1121088;
SOURCE 4 GENE: BF29_2874;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET100D-TOPO
KEYWDS CARBOXYL ESTERASE, LIPASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.GOURLAY,C.NAKHNOUKH,M.BOLOGNESI
REVDAT 1 06-DEC-17 5OLU 0
JRNL AUTH V.DE VITIS,C.NAKHNOUKH,A.PINTO,M.L.CONTENTE,A.BARBIROLI,
JRNL AUTH 2 M.BOLOGNESI,F.MOLINARI,L.J.GOURLAY,D.ROMANO
JRNL TITL A STEREOSPECIFIC CARBOXYL ESTERASE FROM BACILLUS COAGULANS
JRNL TITL 2 HOSTING NON-LIPASE ACTIVITIES WITHIN A LIPASE-LIKE FOLD
JRNL REF FEBS J. 2017
JRNL REFN ISSN 1742-464X
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 43626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.580
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7441 - 4.3365 1.00 3221 154 0.1488 0.1670
REMARK 3 2 4.3365 - 3.4427 1.00 3048 148 0.1312 0.1378
REMARK 3 3 3.4427 - 3.0077 1.00 3007 143 0.1569 0.1787
REMARK 3 4 3.0077 - 2.7327 1.00 2993 145 0.1515 0.1578
REMARK 3 5 2.7327 - 2.5369 1.00 2970 142 0.1524 0.1916
REMARK 3 6 2.5369 - 2.3874 1.00 2956 143 0.1431 0.1681
REMARK 3 7 2.3874 - 2.2678 1.00 2947 141 0.1390 0.1652
REMARK 3 8 2.2678 - 2.1691 1.00 2938 141 0.1380 0.1612
REMARK 3 9 2.1691 - 2.0856 1.00 2926 141 0.1465 0.1750
REMARK 3 10 2.0856 - 2.0136 1.00 2943 141 0.1504 0.1941
REMARK 3 11 2.0136 - 1.9507 1.00 2939 142 0.1487 0.1789
REMARK 3 12 1.9507 - 1.8949 1.00 2902 138 0.1485 0.1817
REMARK 3 13 1.8949 - 1.8450 1.00 2918 141 0.1620 0.1879
REMARK 3 14 1.8450 - 1.8000 1.00 2918 140 0.1938 0.2178
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.920
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 : 0.007 2562
REMARK 3 ANGLE : 0.856 3472
REMARK 3 CHIRALITY : 0.055 359
REMARK 3 PLANARITY : 0.006 453
REMARK 3 DIHEDRAL : 13.001 1489
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6872 -23.3248 -12.8802
REMARK 3 T TENSOR
REMARK 3 T11: 0.1027 T22: 0.1812
REMARK 3 T33: 0.1319 T12: -0.0319
REMARK 3 T13: -0.0328 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 4.6167 L22: 2.6810
REMARK 3 L33: 0.5658 L12: -1.7333
REMARK 3 L13: 0.4173 L23: -0.3572
REMARK 3 S TENSOR
REMARK 3 S11: -0.1172 S12: -0.0917 S13: 0.3243
REMARK 3 S21: 0.1630 S22: 0.0920 S23: -0.2578
REMARK 3 S31: -0.1938 S32: 0.3346 S33: -0.0253
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7988 -29.2647 -16.0696
REMARK 3 T TENSOR
REMARK 3 T11: 0.0643 T22: 0.0822
REMARK 3 T33: 0.0858 T12: -0.0040
REMARK 3 T13: -0.0151 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 2.8251 L22: 1.1336
REMARK 3 L33: 2.0416 L12: -0.7728
REMARK 3 L13: -1.1358 L23: 0.4956
REMARK 3 S TENSOR
REMARK 3 S11: -0.0065 S12: 0.0656 S13: 0.0498
REMARK 3 S21: -0.0074 S22: -0.0034 S23: -0.0359
REMARK 3 S31: -0.1295 S32: 0.0808 S33: 0.0112
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0843 -31.9760 -12.1826
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.2180
REMARK 3 T33: 0.1315 T12: -0.0127
REMARK 3 T13: -0.0311 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 3.3850 L22: 1.4945
REMARK 3 L33: 1.2983 L12: -0.7472
REMARK 3 L13: -1.4375 L23: 0.0414
REMARK 3 S TENSOR
REMARK 3 S11: -0.1387 S12: -0.0269 S13: -0.0120
REMARK 3 S21: 0.0894 S22: 0.0799 S23: -0.2113
REMARK 3 S31: 0.0372 S32: 0.3640 S33: 0.0276
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9337 -41.4962 -11.6883
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.1217
REMARK 3 T33: 0.0831 T12: 0.0174
REMARK 3 T13: -0.0108 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 1.8900 L22: 1.7583
REMARK 3 L33: 1.5731 L12: -0.3415
REMARK 3 L13: -0.0253 L23: 0.2193
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: 0.0167 S13: -0.0880
REMARK 3 S21: 0.0887 S22: 0.0213 S23: -0.0693
REMARK 3 S31: 0.0880 S32: 0.2231 S33: -0.0388
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 147 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7683 -44.6815 -28.1413
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.5653
REMARK 3 T33: 0.2545 T12: 0.0517
REMARK 3 T13: 0.0412 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 5.7974 L22: 1.5524
REMARK 3 L33: 0.7652 L12: 0.9795
REMARK 3 L13: -0.7216 L23: -0.2107
REMARK 3 S TENSOR
REMARK 3 S11: -0.1507 S12: 0.4669 S13: -0.2102
REMARK 3 S21: -0.0307 S22: 0.1015 S23: -0.1325
REMARK 3 S31: 0.0955 S32: 0.5125 S33: 0.0174
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2154 -47.4326 -37.7546
REMARK 3 T TENSOR
REMARK 3 T11: 0.2249 T22: 0.2356
REMARK 3 T33: 0.1634 T12: 0.0549
REMARK 3 T13: 0.0548 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 2.0989 L22: 6.8855
REMARK 3 L33: 5.6005 L12: -0.6046
REMARK 3 L13: -0.9185 L23: -4.3206
REMARK 3 S TENSOR
REMARK 3 S11: 0.1683 S12: 0.3467 S13: 0.1460
REMARK 3 S21: -0.7710 S22: -0.0404 S23: -0.2386
REMARK 3 S31: 0.4373 S32: 0.4299 S33: -0.1108
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5313 -45.0981 -21.2524
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.1719
REMARK 3 T33: 0.1211 T12: 0.0310
REMARK 3 T13: 0.0085 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.1676 L22: 0.4973
REMARK 3 L33: 0.4255 L12: -0.1122
REMARK 3 L13: 0.1872 L23: 0.1676
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.0349 S13: -0.0320
REMARK 3 S21: -0.0471 S22: -0.0211 S23: -0.1393
REMARK 3 S31: 0.0600 S32: 0.2366 S33: 0.0263
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9875 -45.3354 -21.4963
REMARK 3 T TENSOR
REMARK 3 T11: 0.0511 T22: 0.0764
REMARK 3 T33: 0.0885 T12: 0.0192
REMARK 3 T13: 0.0188 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.0379 L22: 1.7671
REMARK 3 L33: 2.3832 L12: -1.2176
REMARK 3 L13: 2.0288 L23: -1.6020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: -0.0393 S13: -0.0571
REMARK 3 S21: 0.0212 S22: 0.1123 S23: 0.0753
REMARK 3 S31: -0.0669 S32: -0.1786 S33: -0.0903
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8302 -39.5869 -12.1188
REMARK 3 T TENSOR
REMARK 3 T11: 0.0375 T22: 0.0758
REMARK 3 T33: 0.1014 T12: 0.0335
REMARK 3 T13: 0.0170 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 3.8110 L22: 3.7407
REMARK 3 L33: 6.8415 L12: -0.1198
REMARK 3 L13: 1.2354 L23: -1.5774
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.1353 S13: -0.0942
REMARK 3 S21: 0.1951 S22: 0.1098 S23: 0.1413
REMARK 3 S31: -0.0925 S32: -0.3554 S33: -0.1008
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 5OLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43646
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 39.10
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 34.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 37.60
REMARK 200 R MERGE FOR SHELL (I) : 0.58900
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: BALBES
REMARK 200 STARTING MODEL: 3PE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HAMPTON CRYSTAL SCREEN 2 CONDITION 42.
REMARK 280 1.5 M AMMONIUM SULFATE, 12% GLYCEROL AND 0.1 M TRIS-HCL, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 41.81800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.81800
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.81800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 41.81800
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 41.81800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 41.81800
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 503 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 532 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 622 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 651 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 666 LIES ON A SPECIAL POSITION.
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 -35
REMARK 465 ARG A -34
REMARK 465 GLY A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 GLY A -25
REMARK 465 MET A -24
REMARK 465 ALA A -23
REMARK 465 SER A -22
REMARK 465 MET A -21
REMARK 465 THR A -20
REMARK 465 GLY A -19
REMARK 465 GLY A -18
REMARK 465 GLN A -17
REMARK 465 GLN A -16
REMARK 465 MET A -15
REMARK 465 GLY A -14
REMARK 465 ARG A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 TYR A -10
REMARK 465 ASP A -9
REMARK 465 ASP A -8
REMARK 465 ASP A -7
REMARK 465 ASP A -6
REMARK 465 LYS A -5
REMARK 465 ASP A -4
REMARK 465 HIS A -3
REMARK 465 PRO A -2
REMARK 465 PHE A -1
REMARK 465 LYS A 310
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 158 CG CD1 CD2 CE1 CE2 CZ OH
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 OD1 ASN A 265 O HOH A 501 2.12
REMARK 500 O HOH A 639 O HOH A 663 2.14
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 ALA A 2 -117.34 -88.83
REMARK 500 LYS A 14 -43.19 -131.19
REMARK 500 GLU A 40 -158.98 -119.06
REMARK 500 SER A 114 -122.72 62.79
REMARK 500 ASN A 145 -7.93 75.55
REMARK 500 ARG A 283 -143.22 -84.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEG A 412
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 413
DBREF1 5OLU A 1 310 UNP A0A0B5WSQ6_BACCO
DBREF2 5OLU A A0A0B5WSQ6 1 310
SEQADV 5OLU MET A -35 UNP A0A0B5WSQ INITIATING METHIONINE
SEQADV 5OLU ARG A -34 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLY A -33 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU SER A -32 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -31 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -30 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -29 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -28 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -27 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -26 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLY A -25 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU MET A -24 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ALA A -23 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU SER A -22 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU MET A -21 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU THR A -20 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLY A -19 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLY A -18 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLN A -17 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLN A -16 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU MET A -15 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU GLY A -14 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ARG A -13 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -12 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU LEU A -11 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU TYR A -10 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -9 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -8 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -7 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -6 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU LYS A -5 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU ASP A -4 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU HIS A -3 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU PRO A -2 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU PHE A -1 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5OLU THR A 0 UNP A0A0B5WSQ EXPRESSION TAG
SEQRES 1 A 346 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 346 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 A 346 ASP ASP ASP ASP LYS ASP HIS PRO PHE THR MET ALA PHE
SEQRES 4 A 346 GLN GLU LEU SER PHE GLN SER PHE ASN GLY LYS ASP ASN
SEQRES 5 A 346 VAL LYS ALA TRP ILE TYR THR PRO ILE ARG LYS PRO ARG
SEQRES 6 A 346 GLY ILE VAL GLN VAL VAL HIS GLY PHE GLY GLU HIS SER
SEQRES 7 A 346 ARG ARG TYR LEU HIS MET ILE LEU LYS PHE ASN GLU ALA
SEQRES 8 A 346 GLY PHE VAL VAL ALA ALA ASP ASP HIS VAL GLY HIS GLY
SEQRES 9 A 346 LYS THR ALA TYR ASP SER GLY ASN TRP GLY ASP TRP GLY
SEQRES 10 A 346 ASP LYS GLY TYR MET THR MET ALA GLU ASP GLU HIS THR
SEQRES 11 A 346 LEU ARG LYS ILE VAL GLN GLU GLN TYR PRO ASP LEU PRO
SEQRES 12 A 346 TYR PHE MET PHE GLY HIS SER MET GLY SER MET ILE ALA
SEQRES 13 A 346 ARG GLY TYR ALA ALA THR HIS GLY ALA GLY LEU SER GLY
SEQRES 14 A 346 LEU ILE LEU CYS GLY THR SER GLY ARG PHE PRO ASN ALA
SEQRES 15 A 346 SER LYS LEU LEU PRO VAL LEU LYS ASN LEU ILE TYR GLU
SEQRES 16 A 346 GLY LYS GLY GLN GLU THR ASP LEU SER TYR LEU GLU GLU
SEQRES 17 A 346 LEU MET GLY TRP MET THR GLU ARG ILE GLU GLN PRO LYS
SEQRES 18 A 346 THR PRO ASN ASP TRP ILE SER SER ASP PRO ASP ILE VAL
SEQRES 19 A 346 ALA ASP HIS ALA ASN ASP PRO PHE ASN ASN PHE THR THR
SEQRES 20 A 346 PRO PRO ASN ILE ARG SER LEU TYR TYR PHE VAL GLN MET
SEQRES 21 A 346 MET GLU ILE ILE VAL GLY THR GLU TRP ALA GLU LYS VAL
SEQRES 22 A 346 PRO VAL SER ILE PRO ILE TYR ASN ILE ALA GLY ASP GLN
SEQRES 23 A 346 ASP PRO VAL GLY GLN TYR GLY GLU GLY VAL TYR ALA VAL
SEQRES 24 A 346 SER ASN TRP LEU VAL GLN THR GLY HIS HIS VAL LYS THR
SEQRES 25 A 346 LYS VAL TYR PRO GLY HIS ARG HIS GLU ILE HIS ASN ASP
SEQRES 26 A 346 ARG ASP ILE ARG ASP GLU VAL GLU GLU GLY ILE ILE SER
SEQRES 27 A 346 PHE ILE ASN GLY ILE ILE VAL LYS
HET GOL A 401 14
HET GOL A 402 14
HET GOL A 403 14
HET CL A 404 1
HET CL A 405 1
HET CL A 406 1
HET CL A 407 1
HET CL A 408 1
HET CL A 409 1
HET CL A 410 1
HET CL A 411 1
HET PEG A 412 15
HET ACT A 413 7
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 3(C3 H8 O3)
FORMUL 5 CL 8(CL 1-)
FORMUL 13 PEG C4 H10 O3
FORMUL 14 ACT C2 H3 O2 1-
FORMUL 15 HOH *192(H2 O)
HELIX 1 AA1 HIS A 41 ARG A 44 5 4
HELIX 2 AA2 TYR A 45 ALA A 55 1 11
HELIX 3 AA3 HIS A 67 GLY A 75 1 9
HELIX 4 AA4 MET A 86 TYR A 103 1 18
HELIX 5 AA5 SER A 114 HIS A 127 1 14
HELIX 6 AA6 ASN A 145 GLU A 159 1 15
HELIX 7 AA7 ASP A 166 GLY A 175 1 10
HELIX 8 AA8 ASN A 188 SER A 192 5 5
HELIX 9 AA9 ASP A 194 ASP A 204 1 11
HELIX 10 AB1 ASN A 214 ILE A 227 1 14
HELIX 11 AB2 VAL A 229 GLU A 235 1 7
HELIX 12 AB3 ASP A 251 GLN A 255 5 5
HELIX 13 AB4 GLY A 257 THR A 270 1 14
HELIX 14 AB5 ILE A 292 VAL A 309 1 18
SHEET 1 AA1 8 GLN A 4 GLN A 9 0
SHEET 2 AA1 8 ASN A 16 TYR A 22 -1 O VAL A 17 N PHE A 8
SHEET 3 AA1 8 PHE A 57 ASP A 63 -1 O VAL A 59 N TYR A 22
SHEET 4 AA1 8 GLY A 30 VAL A 35 1 N VAL A 32 O VAL A 58
SHEET 5 AA1 8 TYR A 108 HIS A 113 1 O PHE A 111 N GLN A 33
SHEET 6 AA1 8 LEU A 131 CYS A 137 1 O SER A 132 N TYR A 108
SHEET 7 AA1 8 ILE A 243 GLY A 248 1 O TYR A 244 N LEU A 136
SHEET 8 AA1 8 VAL A 274 TYR A 279 1 O TYR A 279 N ALA A 247
SITE 1 AC1 9 PHE A 38 GLU A 40 HIS A 113 SER A 114
SITE 2 AC1 9 HIS A 201 PHE A 209 HIS A 284 GLU A 285
SITE 3 AC1 9 HOH A 527
SITE 1 AC2 7 ASP A 200 ASN A 288 ARG A 290 HOH A 539
SITE 2 AC2 7 HOH A 544 HOH A 620 HOH A 649
SITE 1 AC3 6 GLN A 4 GLU A 5 TYR A 72 PRO A 205
SITE 2 AC3 6 PHE A 206 HOH A 514
SITE 1 AC4 3 TYR A 103 PRO A 104 ASP A 105
SITE 1 AC5 5 ARG A 26 ASP A 194 ILE A 197 ARG A 290
SITE 2 AC5 5 HOH A 670
SITE 1 AC6 3 GLY A 162 ARG A 216 HOH A 631
SITE 1 AC7 6 GLY A 141 ARG A 142 PHE A 143 MET A 225
SITE 2 AC7 6 GLU A 226 VAL A 229
SITE 1 AC8 1 HOH A 672
SITE 1 AC9 2 ARG A 142 TRP A 266
SITE 1 AD1 5 LYS A 185 ASP A 189 VAL A 198 HOH A 599
SITE 2 AD1 5 HOH A 610
SITE 1 AD2 3 PHE A 8 GLN A 9 HOH A 689
SITE 1 AD3 5 TRP A 77 PRO A 205 ASN A 207 ASN A 208
SITE 2 AD3 5 THR A 211
SITE 1 AD4 3 ARG A 26 HOH A 505 HOH A 507
CRYST1 137.644 137.644 83.636 90.00 90.00 120.00 P 63 2 2 12
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 0.007265 0.004195 0.000000 0.00000
SCALE2 0.000000 0.008389 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011957 0.00000
TER 4808 VAL A 309
MASTER 528 0 13 14 8 0 21 6 2689 1 64 27
END |