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HEADER HYDROLASE 25-APR-13 4KE7
TITLE CRYSTAL STRUCTURE OF MONOGLYCERIDE LIPASE FROM BACILLUS SP. H257 IN
TITLE 2 COMPLEX WITH AN 1-MYRISTOYL GLYCEROL ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 129908;
SOURCE 4 STRAIN: H-257;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A(+)
KEYWDS ALPHA/BETA HYDROLASE FOLD, MONOGLYCERIDE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
REVDAT 1 18-SEP-13 4KE7 0
JRNL AUTH S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
JRNL TITL CONFORMATIONAL PLASTICITY AND LIGAND BINDING OF BACTERIAL
JRNL TITL 2 MONOACYLGLYCEROL LIPASE
JRNL REF J.BIOL.CHEM. 2013
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 47066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2375
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 23.5574 - 4.3593 0.93 2581 143 0.1638 0.1906
REMARK 3 2 4.3593 - 3.4637 0.97 2652 125 0.1457 0.1525
REMARK 3 3 3.4637 - 3.0269 0.98 2635 164 0.1556 0.1831
REMARK 3 4 3.0269 - 2.7506 0.98 2648 132 0.1655 0.1911
REMARK 3 5 2.7506 - 2.5537 0.99 2663 154 0.1635 0.2013
REMARK 3 6 2.5537 - 2.4033 0.99 2656 157 0.1674 0.2189
REMARK 3 7 2.4033 - 2.2830 0.99 2681 139 0.1657 0.1997
REMARK 3 8 2.2830 - 2.1837 0.93 2495 134 0.2389 0.3009
REMARK 3 9 2.1837 - 2.0997 1.00 2667 143 0.1587 0.1992
REMARK 3 10 2.0997 - 2.0273 0.99 2687 132 0.1589 0.1886
REMARK 3 11 2.0273 - 1.9639 0.99 2680 127 0.1672 0.2083
REMARK 3 12 1.9639 - 1.9078 0.98 2627 125 0.2565 0.3024
REMARK 3 13 1.9078 - 1.8576 0.99 2685 153 0.1707 0.2293
REMARK 3 14 1.8576 - 1.8123 1.00 2663 138 0.1707 0.2102
REMARK 3 15 1.8123 - 1.7711 1.00 2681 137 0.1755 0.2382
REMARK 3 16 1.7711 - 1.7334 1.00 2665 142 0.1904 0.2275
REMARK 3 17 1.7334 - 1.6990 0.87 2325 130 0.2294 0.2941
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.34960
REMARK 3 B22 (A**2) : -1.23700
REMARK 3 B33 (A**2) : -0.48320
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.60550
REMARK 3 B23 (A**2) : -0.00000
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 3959
REMARK 3 ANGLE : 1.109 5390
REMARK 3 CHIRALITY : 0.070 604
REMARK 3 PLANARITY : 0.006 688
REMARK 3 DIHEDRAL : 12.057 1431
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 2:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3223 -5.2310 25.8152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0728 T22: 0.0615
REMARK 3 T33: 0.0661 T12: 0.0043
REMARK 3 T13: 0.0100 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.2699 L22: 1.9442
REMARK 3 L33: 0.9228 L12: 1.2861
REMARK 3 L13: -0.7869 L23: -0.5707
REMARK 3 S TENSOR
REMARK 3 S11: -0.1006 S12: 0.0555 S13: -0.1902
REMARK 3 S21: -0.1754 S22: 0.0183 S23: -0.2346
REMARK 3 S31: 0.1332 S32: 0.0815 S33: 0.0777
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 70:131)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0375 0.4062 24.7946
REMARK 3 T TENSOR
REMARK 3 T11: 0.0605 T22: 0.0701
REMARK 3 T33: 0.0452 T12: -0.0021
REMARK 3 T13: -0.0151 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.0415 L22: 1.5961
REMARK 3 L33: 1.5838 L12: -0.3518
REMARK 3 L13: -0.5045 L23: 0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: 0.2062 S13: 0.0104
REMARK 3 S21: -0.1740 S22: -0.0090 S23: 0.1207
REMARK 3 S31: 0.0413 S32: -0.1222 S33: -0.0206
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 132:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4699 8.1375 32.5430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1516 T22: 0.1116
REMARK 3 T33: 0.1251 T12: -0.0343
REMARK 3 T13: 0.0007 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.7487 L22: 0.6930
REMARK 3 L33: 3.5024 L12: 0.8817
REMARK 3 L13: -2.1278 L23: -0.5553
REMARK 3 S TENSOR
REMARK 3 S11: 0.1258 S12: 0.0129 S13: 0.1433
REMARK 3 S21: -0.0045 S22: 0.0666 S23: -0.0070
REMARK 3 S31: -0.4257 S32: 0.1830 S33: -0.1190
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 161:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6085 12.8567 22.1151
REMARK 3 T TENSOR
REMARK 3 T11: 0.1199 T22: 0.0779
REMARK 3 T33: 0.0865 T12: -0.0150
REMARK 3 T13: 0.0065 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 5.3680 L22: 1.3531
REMARK 3 L33: 1.3182 L12: -0.5315
REMARK 3 L13: -1.3115 L23: -0.0178
REMARK 3 S TENSOR
REMARK 3 S11: 0.1004 S12: 0.2161 S13: 0.4926
REMARK 3 S21: -0.2217 S22: -0.0288 S23: -0.0599
REMARK 3 S31: -0.1898 S32: 0.0257 S33: -0.0221
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 180:231)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8109 6.7135 37.4684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0746 T22: 0.0499
REMARK 3 T33: 0.0308 T12: -0.0032
REMARK 3 T13: 0.0076 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 3.1354 L22: 1.2881
REMARK 3 L33: 0.9888 L12: -0.2136
REMARK 3 L13: 0.5960 L23: -0.3016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: -0.1804 S13: 0.1002
REMARK 3 S21: 0.1424 S22: -0.0410 S23: 0.0816
REMARK 3 S31: -0.0458 S32: -0.0914 S33: 0.0240
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resseq 232:250)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5485 -6.2125 41.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.1413 T22: 0.0748
REMARK 3 T33: 0.0685 T12: -0.0211
REMARK 3 T13: 0.0220 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 9.4584 L22: 2.4616
REMARK 3 L33: 2.5137 L12: 3.8249
REMARK 3 L13: 4.1310 L23: 1.0374
REMARK 3 S TENSOR
REMARK 3 S11: 0.2304 S12: -0.5074 S13: 0.0227
REMARK 3 S21: 0.2129 S22: -0.2546 S23: 0.1759
REMARK 3 S31: 0.0256 S32: -0.2043 S33: 0.0289
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resseq 2:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2700 -3.7421 56.0220
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.1052
REMARK 3 T33: 0.1792 T12: 0.0288
REMARK 3 T13: 0.0483 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 4.9357 L22: 4.9775
REMARK 3 L33: 7.0141 L12: 3.7923
REMARK 3 L13: -4.6452 L23: -2.8913
REMARK 3 S TENSOR
REMARK 3 S11: -0.1769 S12: 0.2441 S13: -0.1972
REMARK 3 S21: -0.1193 S22: 0.1317 S23: -0.1839
REMARK 3 S31: 0.1103 S32: 0.1104 S33: -0.0646
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resseq 14:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7787 -4.8482 62.3438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0631
REMARK 3 T33: 0.0436 T12: 0.0080
REMARK 3 T13: 0.0064 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 2.2807 L22: 2.1923
REMARK 3 L33: 1.0535 L12: 1.1031
REMARK 3 L13: -0.3960 L23: -0.4305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: 0.1903 S13: -0.1427
REMARK 3 S21: -0.0958 S22: 0.0019 S23: -0.1818
REMARK 3 S31: 0.1144 S32: 0.0430 S33: 0.0436
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resseq 70:89)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3929 -4.4922 54.7917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0774 T22: 0.1167
REMARK 3 T33: 0.0391 T12: 0.0101
REMARK 3 T13: -0.0181 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.5701 L22: 8.9545
REMARK 3 L33: 2.3658 L12: 2.7641
REMARK 3 L13: 0.0642 L23: -0.6169
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.2118 S13: -0.0049
REMARK 3 S21: -0.3332 S22: -0.0132 S23: 0.2779
REMARK 3 S31: 0.0455 S32: -0.1383 S33: 0.0251
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resseq 90:143)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4410 5.6675 63.2271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.0655
REMARK 3 T33: 0.0633 T12: 0.0033
REMARK 3 T13: -0.0160 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.8838 L22: 1.0996
REMARK 3 L33: 1.6013 L12: -0.7575
REMARK 3 L13: -0.6898 L23: -0.2829
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: 0.1744 S13: 0.1924
REMARK 3 S21: -0.0333 S22: -0.0063 S23: -0.0021
REMARK 3 S31: -0.0809 S32: -0.0640 S33: -0.0264
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resseq 144:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2605 3.4300 72.9829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1447 T22: 0.1952
REMARK 3 T33: 0.1648 T12: -0.0396
REMARK 3 T13: -0.0617 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.8962 L22: -0.0015
REMARK 3 L33: 6.1604 L12: -0.1584
REMARK 3 L13: -3.4295 L23: 0.2778
REMARK 3 S TENSOR
REMARK 3 S11: 0.2098 S12: -0.1129 S13: -0.0479
REMARK 3 S21: 0.2034 S22: 0.0684 S23: -0.3278
REMARK 3 S31: -0.0155 S32: 0.4706 S33: -0.2243
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resseq 161:183)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4652 12.8493 58.8413
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.0693
REMARK 3 T33: 0.0842 T12: 0.0123
REMARK 3 T13: 0.0036 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 6.2105 L22: 1.6703
REMARK 3 L33: 1.6057 L12: 0.3782
REMARK 3 L13: -1.9723 L23: -0.4448
REMARK 3 S TENSOR
REMARK 3 S11: 0.1177 S12: 0.3550 S13: 0.5069
REMARK 3 S21: -0.1642 S22: 0.0206 S23: -0.0010
REMARK 3 S31: -0.1974 S32: -0.1068 S33: -0.1093
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resseq 184:231)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6367 6.4441 74.8941
REMARK 3 T TENSOR
REMARK 3 T11: 0.0861 T22: 0.0352
REMARK 3 T33: 0.0542 T12: -0.0043
REMARK 3 T13: 0.0093 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 2.4165 L22: 1.0199
REMARK 3 L33: 1.4604 L12: -0.3985
REMARK 3 L13: 0.5605 L23: -0.4895
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.1101 S13: 0.0505
REMARK 3 S21: 0.1493 S22: -0.0002 S23: 0.1269
REMARK 3 S31: -0.0881 S32: -0.0527 S33: -0.0359
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resseq 232:250)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7607 -6.4541 76.6927
REMARK 3 T TENSOR
REMARK 3 T11: 0.1062 T22: 0.1056
REMARK 3 T33: 0.0910 T12: -0.0099
REMARK 3 T13: 0.0352 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 2.1152 L22: 2.7767
REMARK 3 L33: 4.2695 L12: 3.0143
REMARK 3 L13: 5.2514 L23: 0.6308
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.5960 S13: 0.1833
REMARK 3 S21: 0.3006 S22: -0.1059 S23: 0.3201
REMARK 3 S31: 0.1435 S32: -0.3706 S33: 0.0019
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 4KE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.81
REMARK 200 MONOCHROMATOR : SI 111, HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47227
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 71.307
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
REMARK 200 R SYM FOR SHELL (I) : 0.21500
REMARK 200 FOR SHELL : 1.800
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 (%): 34.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOLE PH 6.5, 12.5% W/V
REMARK 280 PEG 1000, 12.5% W/V PEG 3350, 12.5% V/V MPD AND 0.02 M ALCOHOLS
REMARK 280 (0.2 M 1,6-HEXANEDIOL, 0.2 M 1-BUTANOL, 0.2 M (RS)-1, 2-
REMARK 280 PROPANEDIOL, 0.2 M 2-PROPANOL, 0.2 M 1,4-BUTANEDIOL, 0.2 M 1,3-
REMARK 280 PROPANEDIOL), VAPOR DIFFUSION, TEMPERATURE 293K
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 35.62000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 THR A 133
REMARK 465 GLY A 134
REMARK 465 GLY A 135
REMARK 465 GLY A 136
REMARK 465 GLU A 137
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 MET B 132
REMARK 465 THR B 133
REMARK 465 GLY B 134
REMARK 465 GLY B 135
REMARK 465 GLY B 136
REMARK 465 GLU B 137
REMARK 465 LEU B 138
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 ASN A 18 -117.52 -132.66
REMARK 500 THR A 30 -3.16 70.90
REMARK 500 THR A 60 -80.34 -125.22
REMARK 500 SER A 97 -122.99 65.06
REMARK 500 TYR A 225 -149.74 -98.70
REMARK 500 ASN B 18 -113.67 -133.33
REMARK 500 THR B 30 -3.19 74.13
REMARK 500 THR B 60 -84.75 -121.07
REMARK 500 SER B 97 -120.99 62.95
REMARK 500 TYR B 225 -149.27 -95.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QX A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QX B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KE6 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE9 RELATED DB: PDB
REMARK 900 RELATED ID: 4KEA RELATED DB: PDB
DBREF 4KE7 A 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE7 B 1 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 4KE7 MET A -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY A -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER A -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER A -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER A -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER A -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY A -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 LEU A -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 VAL A -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 PRO A -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 ARG A -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY A -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER A -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS A 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 MET B -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY B -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER B -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER B -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER B -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER B -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY B -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 LEU B -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 VAL B -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 PRO B -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 ARG B -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 GLY B -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 SER B -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE7 HIS B 0 UNP P82597 EXPRESSION TAG
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 A 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 A 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 A 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 A 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 A 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 A 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 A 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 A 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 A 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 A 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 A 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 A 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 A 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 A 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 A 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 A 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 A 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 A 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 A 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 B 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 B 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 B 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 B 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 B 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 B 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 B 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 B 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 B 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 B 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 B 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 B 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 B 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 B 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 B 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 B 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 B 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 B 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 B 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 B 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
MODRES 4KE7 SER B 97 SER 1.58
MODRES 4KE7 SER A 97 SER 1.62
HET 1QX A 301 21
HET MPD A 302 8
HET 1QX B 301 21
HET MPD B 302 8
HETNAM 1QX DODECYL HYDROGEN (S)-(3-AZIDOPROPYL)PHOSPHONATE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 1QX 2(C15 H32 N3 O3 P)
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 7 HOH *408(H2 O)
HELIX 1 1 THR A 32 SER A 35 5 4
HELIX 2 2 MET A 36 ALA A 46 1 11
HELIX 3 3 HIS A 61 ARG A 67 1 7
HELIX 4 4 THR A 69 GLN A 86 1 18
HELIX 5 5 SER A 97 HIS A 110 1 14
HELIX 6 6 ILE A 125 MET A 132 1 8
HELIX 7 7 THR A 164 LYS A 180 1 17
HELIX 8 8 LEU A 181 ILE A 184 5 4
HELIX 9 9 GLY A 202 ILE A 211 1 10
HELIX 10 10 VAL A 227 ASP A 231 5 5
HELIX 11 11 ASP A 233 ALA A 249 1 17
HELIX 12 12 THR B 32 SER B 35 5 4
HELIX 13 13 MET B 36 ALA B 46 1 11
HELIX 14 14 HIS B 61 ARG B 67 1 7
HELIX 15 15 THR B 69 GLN B 86 1 18
HELIX 16 16 SER B 97 HIS B 110 1 14
HELIX 17 17 ILE B 125 GLY B 131 1 7
HELIX 18 18 THR B 164 LYS B 180 1 17
HELIX 19 19 LEU B 181 ILE B 184 5 4
HELIX 20 20 GLY B 202 ILE B 211 1 10
HELIX 21 21 VAL B 227 ASP B 231 5 5
HELIX 22 22 ASP B 233 ALA B 249 1 17
SHEET 1 A 5 PHE A 14 ALA A 16 0
SHEET 2 A 5 THR A 49 LEU A 52 -1 O LEU A 52 N PHE A 14
SHEET 3 A 5 VAL A 21 VAL A 26 1 N LEU A 25 O CYS A 51
SHEET 4 A 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 A 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 B 2 TYR A 141 ASP A 143 0
SHEET 2 B 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 C 2 ALA A 188 SER A 193 0
SHEET 2 C 2 LYS A 216 LEU A 221 1 O LEU A 221 N VAL A 192
SHEET 1 D 5 PHE B 14 ALA B 16 0
SHEET 2 D 5 THR B 49 LEU B 52 -1 O LEU B 52 N PHE B 14
SHEET 3 D 5 VAL B 21 VAL B 26 1 N LEU B 25 O CYS B 51
SHEET 4 D 5 THR B 90 LEU B 96 1 O THR B 90 N GLY B 22
SHEET 5 D 5 GLY B 115 ILE B 119 1 O ILE B 119 N GLY B 95
SHEET 1 E 2 TYR B 141 ASP B 143 0
SHEET 2 E 2 LYS B 161 PRO B 163 -1 O THR B 162 N LEU B 142
SHEET 1 F 2 ALA B 188 SER B 193 0
SHEET 2 F 2 LYS B 216 LEU B 221 1 O LEU B 221 N VAL B 192
LINK OG SER B 97 P1 1QX B 301 1555 1555 1.59
LINK OG SER A 97 P1 1QX A 301 1555 1555 1.64
SITE 1 AC1 11 PHE A 29 THR A 30 SER A 97 MET A 98
SITE 2 AC1 11 ILE A 125 ALA A 127 GLY A 131 MET A 132
SITE 3 AC1 11 LEU A 170 VAL A 198 HIS A 226
SITE 1 AC2 6 VAL A 21 ALA A 46 GLY A 47 TYR A 48
SITE 2 AC2 6 HOH A 414 HOH A 442
SITE 1 AC3 10 GLY B 28 PHE B 29 THR B 30 SER B 97
SITE 2 AC3 10 MET B 98 ILE B 125 LEU B 167 LEU B 170
SITE 3 AC3 10 HIS B 226 HOH B 601
SITE 1 AC4 1 ILE B 206
CRYST1 43.750 71.240 72.900 90.00 102.00 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 0.022857 0.000000 0.004858 0.00000
SCALE2 0.000000 0.014037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014024 0.00000
TER 1910 GLY A 250
TER 3804 GLY B 250
MASTER 530 0 4 22 18 0 9 6 4234 2 60 42
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