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HEADER HYDROLASE 11-FEB-26 10XN
TITLE CRYSTAL STRUCTURE OF A THERMOPHILIC ESTERASE FROM THERMOPLASMA
TITLE 2 ACIDOPHILUM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE RELATED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_TAXID: 2303;
SOURCE 4 GENE: TA0887;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AB HYDROLASE, ESTERASE, THERMOPHILE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DELGADO-REY,L.SANTOS,S.LARA-GONZALEZ
REVDAT 1 02-SEP-26 10XN 0
JRNL AUTH A.DELGADO-REY,M.L.LLAMAS-GARCIA,G.M.MONTERO-MORAN,L.SANTOS,
JRNL AUTH 2 S.LARA-GONZALEZ
JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO THE THERMOSTABLE
JRNL TITL 2 ESTERASE TA0887 FROM THERMOPLASMA ACIDOPHILUM.
JRNL REF FEBS OPEN BIO 2026
JRNL REFN ESSN 2211-5463
JRNL PMID 42630012
JRNL DOI 10.1002/2211-5463.70327
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54617
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2019
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 49.3300 - 4.6500 1.00 3937 153 0.2077 0.1993
REMARK 3 2 4.6500 - 3.6900 1.00 3817 149 0.1606 0.1791
REMARK 3 3 3.6900 - 3.2300 1.00 3784 143 0.1587 0.2107
REMARK 3 4 3.2300 - 2.9300 1.00 3768 146 0.1745 0.1894
REMARK 3 5 2.9300 - 2.7200 1.00 3759 144 0.1628 0.1992
REMARK 3 6 2.7200 - 2.5600 1.00 3742 144 0.1697 0.2398
REMARK 3 7 2.5600 - 2.4300 1.00 3749 141 0.1504 0.1838
REMARK 3 8 2.4300 - 2.3300 1.00 3743 144 0.1613 0.1713
REMARK 3 9 2.3300 - 2.2400 1.00 3727 145 0.1483 0.2000
REMARK 3 10 2.2400 - 2.1600 1.00 3728 145 0.1556 0.1923
REMARK 3 11 2.1600 - 2.0900 1.00 3698 142 0.1556 0.2144
REMARK 3 12 2.0900 - 2.0300 1.00 3734 143 0.1760 0.2231
REMARK 3 13 2.0300 - 1.9800 1.00 3734 141 0.1836 0.2095
REMARK 3 14 1.9800 - 1.9300 0.99 3678 139 0.1957 0.2132
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 18.189
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.14
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 : 0.012 3811
REMARK 3 ANGLE : 1.131 5174
REMARK 3 CHIRALITY : 0.065 583
REMARK 3 PLANARITY : 0.011 662
REMARK 3 DIHEDRAL : 12.855 1391
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.3482 25.0168 20.7592
REMARK 3 T TENSOR
REMARK 3 T11: 0.0994 T22: 0.1176
REMARK 3 T33: 0.1180 T12: -0.0083
REMARK 3 T13: 0.0055 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.8474 L22: 0.7282
REMARK 3 L33: 0.6179 L12: 0.2502
REMARK 3 L13: 0.2074 L23: 0.1285
REMARK 3 S TENSOR
REMARK 3 S11: 0.0539 S12: 0.0128 S13: -0.2450
REMARK 3 S21: -0.0160 S22: -0.1070 S23: -0.0151
REMARK 3 S31: 0.2233 S32: -0.0310 S33: -0.0385
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.0876 29.6875 21.3996
REMARK 3 T TENSOR
REMARK 3 T11: 0.0648 T22: 0.1130
REMARK 3 T33: 0.0952 T12: -0.0256
REMARK 3 T13: -0.0012 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.7698 L22: 1.0867
REMARK 3 L33: 0.9006 L12: 0.1008
REMARK 3 L13: -0.5680 L23: 0.1945
REMARK 3 S TENSOR
REMARK 3 S11: 0.0825 S12: -0.0811 S13: -0.1356
REMARK 3 S21: 0.0600 S22: -0.0874 S23: 0.0996
REMARK 3 S31: 0.1488 S32: -0.0466 S33: 0.0047
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3107 40.0698 19.8208
REMARK 3 T TENSOR
REMARK 3 T11: 0.0446 T22: 0.1280
REMARK 3 T33: 0.0869 T12: -0.0202
REMARK 3 T13: 0.0050 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 0.9629 L22: 0.7631
REMARK 3 L33: 0.1453 L12: -0.2727
REMARK 3 L13: 0.0882 L23: 0.2072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: 0.0007 S13: 0.0033
REMARK 3 S21: 0.0103 S22: -0.0378 S23: -0.0679
REMARK 3 S31: -0.0311 S32: 0.1183 S33: -0.0162
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3604 35.3894 -1.5158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.3112
REMARK 3 T33: 0.1586 T12: 0.0523
REMARK 3 T13: 0.0248 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.9066 L22: 0.6812
REMARK 3 L33: 1.7142 L12: -0.0725
REMARK 3 L13: -0.2812 L23: -1.0234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.5268 S13: -0.1355
REMARK 3 S21: -0.2922 S22: -0.0840 S23: -0.0020
REMARK 3 S31: 0.2295 S32: 0.0484 S33: 0.0081
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.6086 35.7468 5.5524
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.2062
REMARK 3 T33: 0.1672 T12: 0.0195
REMARK 3 T13: -0.0025 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.4347 L22: 0.0779
REMARK 3 L33: 0.6619 L12: 0.1818
REMARK 3 L13: 0.1026 L23: 0.0747
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: 0.0955 S13: -0.2598
REMARK 3 S21: 0.0310 S22: -0.0269 S23: -0.2020
REMARK 3 S31: 0.3014 S32: -0.0399 S33: 0.0083
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 162 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2604 50.0840 21.3821
REMARK 3 T TENSOR
REMARK 3 T11: 0.1319 T22: 0.1274
REMARK 3 T33: 0.2137 T12: 0.0132
REMARK 3 T13: -0.0037 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 2.2692 L22: 0.0203
REMARK 3 L33: 3.4567 L12: -0.0773
REMARK 3 L13: 1.9274 L23: -0.2479
REMARK 3 S TENSOR
REMARK 3 S11: -0.1805 S12: 0.0285 S13: 0.6725
REMARK 3 S21: 0.0084 S22: -0.0747 S23: -0.0677
REMARK 3 S31: -0.5290 S32: -0.1191 S33: -0.2170
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9899 37.5514 20.2257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.1751
REMARK 3 T33: 0.1173 T12: -0.0163
REMARK 3 T13: -0.0025 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.8977 L22: 0.4591
REMARK 3 L33: 0.7707 L12: 0.0904
REMARK 3 L13: -0.0338 L23: -0.0333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: 0.0035 S13: 0.0627
REMARK 3 S21: -0.0299 S22: -0.0415 S23: -0.1404
REMARK 3 S31: 0.0613 S32: 0.1847 S33: -0.0299
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5476 44.7376 -9.8745
REMARK 3 T TENSOR
REMARK 3 T11: 0.1195 T22: 0.2856
REMARK 3 T33: 0.1204 T12: -0.1002
REMARK 3 T13: 0.0119 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 0.6534 L22: 0.3746
REMARK 3 L33: 0.1552 L12: 0.3786
REMARK 3 L13: 0.0575 L23: 0.0404
REMARK 3 S TENSOR
REMARK 3 S11: -0.1378 S12: 0.3381 S13: -0.0047
REMARK 3 S21: -0.1406 S22: 0.1717 S23: 0.0438
REMARK 3 S31: 0.1463 S32: -0.1086 S33: -0.0251
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2522 43.6820 -4.6071
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.2147
REMARK 3 T33: 0.1225 T12: -0.0680
REMARK 3 T13: 0.0078 T23: -0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 0.5499 L22: 0.4440
REMARK 3 L33: 0.7974 L12: 0.4788
REMARK 3 L13: 0.1289 L23: -0.0545
REMARK 3 S TENSOR
REMARK 3 S11: -0.0719 S12: 0.2180 S13: -0.0526
REMARK 3 S21: -0.0752 S22: 0.0980 S23: 0.0478
REMARK 3 S31: 0.2117 S32: -0.0739 S33: -0.0051
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9127 41.4484 4.9545
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.1552
REMARK 3 T33: 0.1314 T12: -0.0277
REMARK 3 T13: 0.0052 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 0.2628 L22: 0.2251
REMARK 3 L33: 1.3239 L12: 0.1378
REMARK 3 L13: -0.3404 L23: 0.1531
REMARK 3 S TENSOR
REMARK 3 S11: -0.0384 S12: -0.0750 S13: -0.0904
REMARK 3 S21: -0.0161 S22: 0.0353 S23: -0.0574
REMARK 3 S31: 0.1346 S32: 0.0040 S33: -0.1241
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 118 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4688 57.0068 10.1838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.2102
REMARK 3 T33: 0.1597 T12: -0.0779
REMARK 3 T13: 0.0391 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 1.7096 L22: 0.4048
REMARK 3 L33: 6.3843 L12: 0.2743
REMARK 3 L13: -1.6024 L23: -1.1534
REMARK 3 S TENSOR
REMARK 3 S11: 0.2108 S12: -0.2581 S13: 0.2442
REMARK 3 S21: 0.1617 S22: 0.0920 S23: -0.0516
REMARK 3 S31: -0.5806 S32: -0.0260 S33: 0.3639
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4557 67.1091 2.0321
REMARK 3 T TENSOR
REMARK 3 T11: 0.4241 T22: 0.2952
REMARK 3 T33: 0.4153 T12: -0.0353
REMARK 3 T13: 0.0021 T23: 0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 0.7109 L22: 0.2327
REMARK 3 L33: 0.1745 L12: -0.2944
REMARK 3 L13: 0.2146 L23: -0.1991
REMARK 3 S TENSOR
REMARK 3 S11: -0.1753 S12: -0.4222 S13: 0.2725
REMARK 3 S21: 0.7212 S22: -0.1512 S23: 0.1075
REMARK 3 S31: -0.4789 S32: -0.0349 S33: -0.0042
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6257 49.8888 7.5676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1017 T22: 0.1519
REMARK 3 T33: 0.1188 T12: -0.0268
REMARK 3 T13: 0.0043 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 1.7494 L22: 1.3135
REMARK 3 L33: 0.9357 L12: 0.7484
REMARK 3 L13: -0.4254 L23: 0.3696
REMARK 3 S TENSOR
REMARK 3 S11: 0.0661 S12: -0.1444 S13: 0.0284
REMARK 3 S21: 0.1521 S22: -0.0598 S23: -0.0942
REMARK 3 S31: -0.0190 S32: 0.0528 S33: 0.0004
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 211 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3220 47.1315 -4.7435
REMARK 3 T TENSOR
REMARK 3 T11: 0.0487 T22: 0.2173
REMARK 3 T33: 0.1516 T12: -0.0214
REMARK 3 T13: 0.0422 T23: -0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 0.3004 L22: 0.5835
REMARK 3 L33: 0.1878 L12: 0.0003
REMARK 3 L13: 0.2352 L23: 0.0240
REMARK 3 S TENSOR
REMARK 3 S11: -0.1041 S12: 0.2212 S13: -0.1838
REMARK 3 S21: -0.0957 S22: 0.0364 S23: 0.0161
REMARK 3 S31: 0.0806 S32: 0.1459 S33: -0.0137
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 10XN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-26.
REMARK 100 THE DEPOSITION ID IS D_1000305036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 200K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54617
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.93700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
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 (%): 63.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 10% 2-
REMARK 280 PROPANOL, AND 20% POLYETHYLENE GLYCOL 4,000., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 61.14200
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 30.57100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.57100
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 61.14200
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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 HIS B 0
REMARK 465 ILE B 235
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 ARG A 42 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 ARG A 227 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 60 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 87 CG OD1 ND2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 109 CG CD CE NZ
REMARK 470 ASP B 131 CG OD1 OD2
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 470 GLU B 146 CG CD OE1 OE2
REMARK 470 LYS B 176 CG CD CE NZ
REMARK 470 GLN B 223 CG CD OE1 NE2
REMARK 470 ARG B 227 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 234 CG CD NE CZ NH1 NH2
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 87 -87.69 -102.91
REMARK 500 SER A 95 -125.92 65.46
REMARK 500 LYS A 108 -51.95 -122.19
REMARK 500 TYR A 212 -0.76 74.51
REMARK 500 LYS A 214 -134.18 -106.10
REMARK 500 SER B 95 -125.97 65.31
REMARK 500 LYS B 108 -54.29 -123.70
REMARK 500 ASN B 204 78.05 -114.79
REMARK 500 TYR B 212 -9.00 74.21
REMARK 500 LYS B 214 -133.44 -106.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 O
REMARK 620 2 ILE A 202 O 104.4
REMARK 620 3 PRO A 203 O 177.8 76.8
REMARK 620 4 ASN A 204 OD1 147.3 108.0 31.3
REMARK 620 5 SER A 205 OG 84.5 82.1 93.9 96.1
REMARK 620 6 SER A 205 OG 70.3 74.7 108.5 114.8 18.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 199 O
REMARK 620 2 ILE B 202 O 108.6
REMARK 620 3 SER B 205 OG 86.0 84.1
REMARK 620 4 HOH B 452 O 138.3 112.0 89.4
REMARK 620 5 HOH B 510 O 88.1 104.2 171.1 90.5
REMARK 620 N 1 2 3 4
DBREF 10XN A 1 235 UNP Q9HJS7 Q9HJS7_THEAC 1 235
DBREF 10XN B 1 235 UNP Q9HJS7 Q9HJS7_THEAC 1 235
SEQADV 10XN GLY A -2 UNP Q9HJS7 EXPRESSION TAG
SEQADV 10XN PRO A -1 UNP Q9HJS7 EXPRESSION TAG
SEQADV 10XN HIS A 0 UNP Q9HJS7 EXPRESSION TAG
SEQADV 10XN GLY B -2 UNP Q9HJS7 EXPRESSION TAG
SEQADV 10XN PRO B -1 UNP Q9HJS7 EXPRESSION TAG
SEQADV 10XN HIS B 0 UNP Q9HJS7 EXPRESSION TAG
SEQRES 1 A 238 GLY PRO HIS MET ASP ARG HIS SER ILE MET THR SER PHE
SEQRES 2 A 238 GLY ASN LEU SER TYR LEU GLU ARG PRO GLY SER TYR PRO
SEQRES 3 A 238 LEU VAL PHE LEU HIS GLY LEU GLY GLY SER GLY ASN ASN
SEQRES 4 A 238 TRP ILE ARG LEU ASP ARG PHE LEU ASP GLY ARG PHE ARG
SEQRES 5 A 238 MET ILE CYS PHE ASP LEU LEU GLY HIS GLY ARG SER ASP
SEQRES 6 A 238 LYS PRO ARG VAL GLU TYR THR VAL GLU VAL GLN ALA SER
SEQRES 7 A 238 ALA ILE VAL GLU ALA LEU SER LYS LEU GLY VAL ASN ARG
SEQRES 8 A 238 PHE THR LEU VAL GLY ASN SER TYR GLY GLY TRP ILE SER
SEQRES 9 A 238 LEU TYR ILE ALA LEU LYS LYS LYS VAL PRO ASP TYR LEU
SEQRES 10 A 238 VAL LEU VAL ASP SER ALA GLY LEU ASN PRO THR ILE ALA
SEQRES 11 A 238 GLU LEU GLY ASP GLU LYS LEU ASN GLU PHE VAL LYS LYS
SEQRES 12 A 238 VAL MET SER VAL GLU GLU GLY ASN ASP GLU TYR VAL ILE
SEQRES 13 A 238 ARG ASN ILE SER ILE ASN ASN SER LYS GLU GLU TRP LYS
SEQRES 14 A 238 ILE LYS ASP GLU ASP LEU ARG SER ILE LYS THR LYS THR
SEQRES 15 A 238 LEU ILE ILE TRP GLY THR ALA ASP ASN VAL LEU SER ILE
SEQRES 16 A 238 GLU TYR GLY ARG LYS PHE HIS GLU LEU ILE PRO ASN SER
SEQRES 17 A 238 LEU LEU PHE GLU ILE PRO TYR ALA LYS HIS THR PRO GLN
SEQRES 18 A 238 ILE THR HIS PRO GLN ILE VAL ALA ARG ILE ILE ASN ASP
SEQRES 19 A 238 ASN VAL ARG ILE
SEQRES 1 B 238 GLY PRO HIS MET ASP ARG HIS SER ILE MET THR SER PHE
SEQRES 2 B 238 GLY ASN LEU SER TYR LEU GLU ARG PRO GLY SER TYR PRO
SEQRES 3 B 238 LEU VAL PHE LEU HIS GLY LEU GLY GLY SER GLY ASN ASN
SEQRES 4 B 238 TRP ILE ARG LEU ASP ARG PHE LEU ASP GLY ARG PHE ARG
SEQRES 5 B 238 MET ILE CYS PHE ASP LEU LEU GLY HIS GLY ARG SER ASP
SEQRES 6 B 238 LYS PRO ARG VAL GLU TYR THR VAL GLU VAL GLN ALA SER
SEQRES 7 B 238 ALA ILE VAL GLU ALA LEU SER LYS LEU GLY VAL ASN ARG
SEQRES 8 B 238 PHE THR LEU VAL GLY ASN SER TYR GLY GLY TRP ILE SER
SEQRES 9 B 238 LEU TYR ILE ALA LEU LYS LYS LYS VAL PRO ASP TYR LEU
SEQRES 10 B 238 VAL LEU VAL ASP SER ALA GLY LEU ASN PRO THR ILE ALA
SEQRES 11 B 238 GLU LEU GLY ASP GLU LYS LEU ASN GLU PHE VAL LYS LYS
SEQRES 12 B 238 VAL MET SER VAL GLU GLU GLY ASN ASP GLU TYR VAL ILE
SEQRES 13 B 238 ARG ASN ILE SER ILE ASN ASN SER LYS GLU GLU TRP LYS
SEQRES 14 B 238 ILE LYS ASP GLU ASP LEU ARG SER ILE LYS THR LYS THR
SEQRES 15 B 238 LEU ILE ILE TRP GLY THR ALA ASP ASN VAL LEU SER ILE
SEQRES 16 B 238 GLU TYR GLY ARG LYS PHE HIS GLU LEU ILE PRO ASN SER
SEQRES 17 B 238 LEU LEU PHE GLU ILE PRO TYR ALA LYS HIS THR PRO GLN
SEQRES 18 B 238 ILE THR HIS PRO GLN ILE VAL ALA ARG ILE ILE ASN ASP
SEQRES 19 B 238 ASN VAL ARG ILE
HET NA A 301 1
HET GOL A 302 14
HET NA B 301 1
HET GOL B 302 14
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NA 2(NA 1+)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 7 HOH *308(H2 O)
HELIX 1 AA1 SER A 33 ASP A 41 5 9
HELIX 2 AA2 THR A 69 LEU A 84 1 16
HELIX 3 AA3 SER A 95 LYS A 108 1 14
HELIX 4 AA4 THR A 125 GLY A 130 1 6
HELIX 5 AA5 GLY A 130 GLU A 145 1 16
HELIX 6 AA6 ASP A 149 SER A 161 1 13
HELIX 7 AA7 LYS A 162 LYS A 166 5 5
HELIX 8 AA8 LYS A 168 ILE A 175 1 8
HELIX 9 AA9 SER A 191 ILE A 202 1 12
HELIX 10 AB1 THR A 216 HIS A 221 1 6
HELIX 11 AB2 HIS A 221 VAL A 233 1 13
HELIX 12 AB3 SER B 33 ASP B 41 5 9
HELIX 13 AB4 THR B 69 GLY B 85 1 17
HELIX 14 AB5 SER B 95 LYS B 108 1 14
HELIX 15 AB6 ILE B 126 LEU B 129 5 4
HELIX 16 AB7 GLY B 130 SER B 143 1 14
HELIX 17 AB8 ASP B 149 SER B 161 1 13
HELIX 18 AB9 LYS B 162 LYS B 166 5 5
HELIX 19 AC1 LYS B 168 ILE B 175 1 8
HELIX 20 AC2 SER B 191 ILE B 202 1 12
HELIX 21 AC3 THR B 216 HIS B 221 1 6
HELIX 22 AC4 HIS B 221 VAL B 233 1 13
SHEET 1 AA1 8 ASP A 2 THR A 8 0
SHEET 2 AA1 8 GLY A 11 ARG A 18 -1 O TYR A 15 N HIS A 4
SHEET 3 AA1 8 PHE A 48 PHE A 53 -1 O CYS A 52 N LEU A 16
SHEET 4 AA1 8 TYR A 22 LEU A 27 1 N LEU A 24 O ARG A 49
SHEET 5 AA1 8 THR A 90 ASN A 94 1 O VAL A 92 N VAL A 25
SHEET 6 AA1 8 TYR A 113 VAL A 117 1 O VAL A 117 N GLY A 93
SHEET 7 AA1 8 LYS A 178 GLY A 184 1 O ILE A 182 N LEU A 116
SHEET 8 AA1 8 SER A 205 ILE A 210 1 O ILE A 210 N TRP A 183
SHEET 1 AA2 8 ASP B 2 THR B 8 0
SHEET 2 AA2 8 GLY B 11 ARG B 18 -1 O TYR B 15 N HIS B 4
SHEET 3 AA2 8 PHE B 48 PHE B 53 -1 O CYS B 52 N LEU B 16
SHEET 4 AA2 8 TYR B 22 LEU B 27 1 N LEU B 24 O ARG B 49
SHEET 5 AA2 8 THR B 90 ASN B 94 1 O THR B 90 N VAL B 25
SHEET 6 AA2 8 TYR B 113 VAL B 117 1 O VAL B 115 N LEU B 91
SHEET 7 AA2 8 LYS B 178 GLY B 184 1 O ILE B 182 N LEU B 116
SHEET 8 AA2 8 SER B 205 ILE B 210 1 O LEU B 206 N ILE B 181
LINK O HIS A 199 NA NA A 301 1555 1555 2.47
LINK O ILE A 202 NA NA A 301 1555 1555 2.08
LINK O APRO A 203 NA NA A 301 1555 1555 3.08
LINK OD1BASN A 204 NA NA A 301 1555 6555 2.37
LINK OG ASER A 205 NA NA A 301 1555 1555 2.38
LINK OG BSER A 205 NA NA A 301 1555 1555 2.94
LINK O HIS B 199 NA NA B 301 1555 1555 2.28
LINK O ILE B 202 NA NA B 301 1555 1555 2.20
LINK OG SER B 205 NA NA B 301 1555 1555 2.53
LINK NA NA B 301 O HOH B 452 1555 1555 2.41
LINK NA NA B 301 O HOH B 510 1555 1555 2.25
CRYST1 117.046 117.046 91.713 90.00 90.00 120.00 P 32 2 1 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 0.008544 0.004933 0.000000 0.00000
SCALE2 0.000000 0.009865 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010904 0.00000
TER 3809 ILE A 235
TER 7391 ARG B 234
MASTER 515 0 4 22 16 0 0 6 4003 2 42 38
END |