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HEADER HYDROLASE 08-JUN-17 5O7G
TITLE THE CRYSTAL STRUCTURE OF A HIGHLY THERMOSTABLE CARBOXYL ESTERASE FROM
TITLE 2 BACILLUS COAGULANS
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET100D/TOPO
KEYWDS CARBOXYL ESTERASE, LIPASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.GOURLAY
REVDAT 1 06-DEC-17 5O7G 0
JRNL AUTH L.J.GOURLAY
JRNL TITL THE CRYSTAL STRUCTURE OF A HIGHLY THERMOSTABLE CARBOXYL
JRNL TITL 2 ESTERASE FROM BACILLUS COAGULANS
JRNL REF FEBS J. 2017
JRNL REFN ISSN 1742-464X
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 37654
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1895
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 39.9034 - 4.5774 1.00 2774 159 0.1618 0.1770
REMARK 3 2 4.5774 - 3.6340 1.00 2619 141 0.1698 0.1629
REMARK 3 3 3.6340 - 3.1748 1.00 2618 119 0.1998 0.2040
REMARK 3 4 3.1748 - 2.8847 1.00 2576 131 0.2297 0.2579
REMARK 3 5 2.8847 - 2.6779 1.00 2552 143 0.2388 0.2515
REMARK 3 6 2.6779 - 2.5201 1.00 2537 131 0.2404 0.2887
REMARK 3 7 2.5201 - 2.3939 1.00 2555 126 0.2507 0.2841
REMARK 3 8 2.3939 - 2.2897 1.00 2521 138 0.2480 0.3091
REMARK 3 9 2.2897 - 2.2016 1.00 2513 137 0.2559 0.2869
REMARK 3 10 2.2016 - 2.1256 0.99 2506 137 0.2587 0.3198
REMARK 3 11 2.1256 - 2.0591 0.99 2517 143 0.2601 0.3348
REMARK 3 12 2.0591 - 2.0003 0.99 2483 138 0.2650 0.2911
REMARK 3 13 2.0003 - 1.9476 0.99 2501 129 0.2678 0.2663
REMARK 3 14 1.9476 - 1.9001 0.99 2487 123 0.2694 0.3278
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.160
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 : 0.010 2527
REMARK 3 ANGLE : 0.996 3432
REMARK 3 CHIRALITY : 0.059 357
REMARK 3 PLANARITY : 0.006 450
REMARK 3 DIHEDRAL : 13.640 1467
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2534 -28.9309 -14.3078
REMARK 3 T TENSOR
REMARK 3 T11: 0.1170 T22: 0.3327
REMARK 3 T33: 0.1765 T12: -0.0093
REMARK 3 T13: -0.0293 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 0.7256 L22: 0.4171
REMARK 3 L33: 0.2873 L12: -0.1101
REMARK 3 L13: -0.0977 L23: 0.0826
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: 0.0905 S13: 0.0672
REMARK 3 S21: 0.0500 S22: 0.0843 S23: -0.0716
REMARK 3 S31: -0.0954 S32: 0.3431 S33: -0.0408
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5767 -43.1038 -14.5902
REMARK 3 T TENSOR
REMARK 3 T11: 0.1203 T22: 0.3821
REMARK 3 T33: 0.1648 T12: 0.0809
REMARK 3 T13: -0.0274 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.0852 L22: 0.3341
REMARK 3 L33: 0.1500 L12: -0.0109
REMARK 3 L13: 0.0288 L23: -0.1787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: 0.1498 S13: -0.0687
REMARK 3 S21: -0.0193 S22: 0.0447 S23: -0.0655
REMARK 3 S31: 0.0385 S32: 0.1946 S33: -0.0632
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4380 -43.5723 -31.6374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2176 T22: 0.6596
REMARK 3 T33: 0.2969 T12: 0.0245
REMARK 3 T13: 0.0006 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 2.5569 L22: 0.7980
REMARK 3 L33: 0.3892 L12: 1.4262
REMARK 3 L13: 0.9782 L23: 0.5511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0974 S13: 0.0105
REMARK 3 S21: -0.0562 S22: 0.0853 S23: -0.1291
REMARK 3 S31: -0.0984 S32: 0.2217 S33: -0.0357
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8907 -41.4075 -36.4080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2115 T22: 0.2576
REMARK 3 T33: 0.1894 T12: 0.0224
REMARK 3 T13: -0.0093 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 0.8475 L22: 1.2615
REMARK 3 L33: 0.6532 L12: -0.6378
REMARK 3 L13: -0.0281 L23: -0.6896
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: 0.1347 S13: -0.0773
REMARK 3 S21: -0.1634 S22: -0.0113 S23: -0.0109
REMARK 3 S31: 0.1056 S32: 0.0168 S33: 0.0017
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2980 -37.8216 -25.5078
REMARK 3 T TENSOR
REMARK 3 T11: 0.1340 T22: 0.5539
REMARK 3 T33: 0.2715 T12: 0.0110
REMARK 3 T13: 0.0020 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.6489 L22: 0.3033
REMARK 3 L33: 0.0114 L12: -0.4024
REMARK 3 L13: -0.0796 L23: 0.0583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: 0.1251 S13: 0.0316
REMARK 3 S21: -0.0857 S22: 0.0071 S23: -0.0651
REMARK 3 S31: 0.0162 S32: 0.1021 S33: -0.0016
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9523 -52.2817 -14.6668
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.2671
REMARK 3 T33: 0.1414 T12: 0.2200
REMARK 3 T13: -0.0220 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 0.0655 L22: 0.0836
REMARK 3 L33: 0.0777 L12: -0.0247
REMARK 3 L13: -0.0208 L23: 0.0509
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0100 S13: -0.0243
REMARK 3 S21: 0.0121 S22: 0.0340 S23: -0.0554
REMARK 3 S31: 0.0650 S32: 0.0887 S33: -0.0064
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 270 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8539 -46.0512 -20.9447
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.2346
REMARK 3 T33: 0.1652 T12: 0.0462
REMARK 3 T13: -0.0006 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.5986 L22: 0.5843
REMARK 3 L33: 0.3950 L12: -0.2531
REMARK 3 L13: 0.2854 L23: -0.2472
REMARK 3 S TENSOR
REMARK 3 S11: -0.0684 S12: 0.0112 S13: -0.0002
REMARK 3 S21: 0.0213 S22: 0.0306 S23: 0.0457
REMARK 3 S31: -0.0756 S32: -0.0281 S33: 0.0239
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.0317 -39.8516 -12.2927
REMARK 3 T TENSOR
REMARK 3 T11: 0.1185 T22: 0.1776
REMARK 3 T33: 0.2015 T12: 0.0941
REMARK 3 T13: 0.0093 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 1.4169 L22: 1.6644
REMARK 3 L33: 2.5367 L12: -0.1177
REMARK 3 L13: 0.2658 L23: -0.6596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: -0.1190 S13: -0.0339
REMARK 3 S21: 0.0650 S22: 0.0352 S23: 0.1249
REMARK 3 S31: -0.0164 S32: -0.2267 S33: -0.0325
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 5O7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200005309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-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 : ID23-1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 19.40
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 20.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.800
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: PACT PREMIER CRYSTALLIZATION SCREEN
REMARK 280 (MOLECULAR DIMENSIONS) CONDITION 2-11 (20% PEG3350; 0.1M SODIUM
REMARK 280 CITRATE TRIBASIC HYDRATE), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 41.88500
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 41.88500
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 41.88500
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 41.88500
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 41.88500
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 41.88500
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 -34
REMARK 465 ARG A -33
REMARK 465 GLY A -32
REMARK 465 SER 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 HIS A -25
REMARK 465 GLY A -24
REMARK 465 MET A -23
REMARK 465 ALA A -22
REMARK 465 SER A -21
REMARK 465 MET A -20
REMARK 465 THR A -19
REMARK 465 GLY A -18
REMARK 465 GLY A -17
REMARK 465 GLN A -16
REMARK 465 GLN A -15
REMARK 465 MET A -14
REMARK 465 GLY A -13
REMARK 465 ARG A -12
REMARK 465 ASP A -11
REMARK 465 LEU A -10
REMARK 465 TYR A -9
REMARK 465 ASP A -8
REMARK 465 ASP A -7
REMARK 465 ASP A -6
REMARK 465 ASP A -5
REMARK 465 LYS A -4
REMARK 465 ASP A -3
REMARK 465 HIS A -2
REMARK 465 PRO 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 470 LYS A 185 CG CD CE NZ
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 -127.02 -96.14
REMARK 500 LYS A 14 -35.75 -131.51
REMARK 500 GLU A 40 -157.71 -110.63
REMARK 500 SER A 114 -127.97 65.90
REMARK 500 ASN A 145 -5.26 74.34
REMARK 500 SER A 192 146.33 -171.96
REMARK 500 ARG A 283 -147.48 -84.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 5O7G A 1 310 UNP A0A0B5WSQ6_BACCO
DBREF2 5O7G A A0A0B5WSQ6 1 310
SEQADV 5O7G MET A -34 UNP A0A0B5WSQ INITIATING METHIONINE
SEQADV 5O7G ARG A -33 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLY A -32 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G SER A -31 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -30 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -29 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -28 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -27 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -26 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -25 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLY A -24 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G MET A -23 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ALA A -22 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G SER A -21 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G MET A -20 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G THR A -19 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLY A -18 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLY A -17 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLN A -16 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLN A -15 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G MET A -14 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G GLY A -13 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ARG A -12 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -11 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G LEU A -10 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G TYR A -9 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -8 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -7 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -6 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -5 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G LYS A -4 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G ASP A -3 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G HIS A -2 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G PRO A -1 UNP A0A0B5WSQ EXPRESSION TAG
SEQADV 5O7G THR A 0 UNP A0A0B5WSQ EXPRESSION TAG
SEQRES 1 A 345 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 345 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 A 345 ASP ASP ASP ASP LYS ASP HIS PRO THR MET ALA PHE GLN
SEQRES 4 A 345 GLU LEU SER PHE GLN SER PHE ASN GLY LYS ASP ASN VAL
SEQRES 5 A 345 LYS ALA TRP ILE TYR THR PRO ILE ARG LYS PRO ARG GLY
SEQRES 6 A 345 ILE VAL GLN VAL VAL HIS GLY PHE GLY GLU HIS SER ARG
SEQRES 7 A 345 ARG TYR LEU HIS MET ILE LEU LYS PHE ASN GLU ALA GLY
SEQRES 8 A 345 PHE VAL VAL ALA ALA ASP ASP HIS VAL GLY HIS GLY LYS
SEQRES 9 A 345 THR ALA TYR ASP SER GLY ASN TRP GLY ASP TRP GLY ASP
SEQRES 10 A 345 LYS GLY TYR MET THR MET ALA GLU ASP GLU HIS THR LEU
SEQRES 11 A 345 ARG LYS ILE VAL GLN GLU GLN TYR PRO ASP LEU PRO TYR
SEQRES 12 A 345 PHE MET PHE GLY HIS SER MET GLY SER MET ILE ALA ARG
SEQRES 13 A 345 GLY TYR ALA ALA THR HIS GLY ALA GLY LEU SER GLY LEU
SEQRES 14 A 345 ILE LEU CYS GLY THR SER GLY ARG PHE PRO ASN ALA SER
SEQRES 15 A 345 LYS LEU LEU PRO VAL LEU LYS ASN LEU ILE TYR GLU GLY
SEQRES 16 A 345 LYS GLY GLN GLU THR ASP LEU SER TYR LEU GLU GLU LEU
SEQRES 17 A 345 MET GLY TRP MET THR GLU ARG ILE GLU GLN PRO LYS THR
SEQRES 18 A 345 PRO ASN ASP TRP ILE SER SER ASP PRO ASP ILE VAL ALA
SEQRES 19 A 345 ASP HIS ALA ASN ASP PRO PHE ASN ASN PHE THR THR PRO
SEQRES 20 A 345 PRO ASN ILE ARG SER LEU TYR TYR PHE VAL GLN MET MET
SEQRES 21 A 345 GLU ILE ILE VAL GLY THR GLU TRP ALA GLU LYS VAL PRO
SEQRES 22 A 345 VAL SER ILE PRO ILE TYR ASN ILE ALA GLY ASP GLN ASP
SEQRES 23 A 345 PRO VAL GLY GLN TYR GLY GLU GLY VAL TYR ALA VAL SER
SEQRES 24 A 345 ASN TRP LEU VAL GLN THR GLY HIS HIS VAL LYS THR LYS
SEQRES 25 A 345 VAL TYR PRO GLY HIS ARG HIS GLU ILE HIS ASN ASP ARG
SEQRES 26 A 345 ASP ILE ARG ASP GLU VAL GLU GLU GLY ILE ILE SER PHE
SEQRES 27 A 345 ILE ASN GLY ILE ILE VAL LYS
FORMUL 2 HOH *50(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 TRP A 176 GLU A 179 5 4
HELIX 9 AA9 ASN A 188 SER A 192 5 5
HELIX 10 AB1 ASP A 194 ASP A 204 1 11
HELIX 11 AB2 ASN A 214 ILE A 228 1 15
HELIX 12 AB3 VAL A 229 GLU A 235 1 7
HELIX 13 AB4 ASP A 251 GLN A 255 5 5
HELIX 14 AB5 GLY A 257 THR A 270 1 14
HELIX 15 AB6 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 GLY A 133 CYS A 137 1 O ILE A 135 N MET A 110
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
CRYST1 138.608 138.608 83.770 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 0.007215 0.004165 0.000000 0.00000
SCALE2 0.000000 0.008331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011937 0.00000
TER 2458 VAL A 309
MASTER 432 0 0 15 8 0 0 6 2507 1 0 27
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