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HEADER HYDROLASE 07-OCT-15 5E4Y
TITLE ORTHORHOMBIC STRUCTURE OF THE ACETYL ESTERASE MEKB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROLASE;
COMPND 5 EC: 2.3.1.-,2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS VERONII;
SOURCE 3 ORGANISM_TAXID: 76761;
SOURCE 4 GENE: MEKB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, ALPHA/BETA HYDROLASE, METHYL ALKYL KETONE DEGRADATION
KEYWDS 2 PATHWAY, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER
REVDAT 1 16-DEC-15 5E4Y 0
JRNL AUTH C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER,K.NIEFIND
JRNL TITL A NOVEL ESTERASE SUBFAMILY WITH ALPHA/BETA-HYDROLASE FOLD
JRNL TITL 2 SUGGESTED BY STRUCTURES OF TWO BACTERIAL ENZYMES HOMOLOGOUS
JRNL TITL 3 TO L-HOMOSERINE O-ACETYL TRANSFERASES
JRNL REF FEBS LETT. 2015
JRNL REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16952
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 839
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 44.7400 - 5.0861 0.99 2822 148 0.1812 0.1942
REMARK 3 2 5.0861 - 4.0378 1.00 2686 151 0.1509 0.2155
REMARK 3 3 4.0378 - 3.5276 1.00 2669 135 0.1705 0.2358
REMARK 3 4 3.5276 - 3.2052 1.00 2640 138 0.1985 0.2616
REMARK 3 5 3.2052 - 2.9755 1.00 2673 124 0.2309 0.2824
REMARK 3 6 2.9755 - 2.8001 1.00 2623 143 0.2426 0.2961
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.130
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 : 0.002 5480
REMARK 3 ANGLE : 0.490 7430
REMARK 3 CHIRALITY : 0.019 802
REMARK 3 PLANARITY : 0.003 971
REMARK 3 DIHEDRAL : 11.839 1970
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8268 29.8426 41.0424
REMARK 3 T TENSOR
REMARK 3 T11: 0.2412 T22: 0.3677
REMARK 3 T33: 0.1534 T12: 0.0633
REMARK 3 T13: -0.0394 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 5.2591 L22: 8.7740
REMARK 3 L33: 2.5529 L12: 4.3276
REMARK 3 L13: 0.4001 L23: 1.6346
REMARK 3 S TENSOR
REMARK 3 S11: -0.1221 S12: 0.2365 S13: -0.0483
REMARK 3 S21: -0.0760 S22: 0.0902 S23: -0.0890
REMARK 3 S31: -0.1300 S32: 0.2719 S33: 0.0485
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1731 28.3481 38.3979
REMARK 3 T TENSOR
REMARK 3 T11: 0.2730 T22: 0.2767
REMARK 3 T33: 0.1281 T12: -0.0764
REMARK 3 T13: 0.0034 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 4.1581 L22: 2.3382
REMARK 3 L33: 3.4602 L12: -2.5028
REMARK 3 L13: -2.0913 L23: 2.1208
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.0056 S13: -0.1206
REMARK 3 S21: -0.1797 S22: -0.0163 S23: -0.0111
REMARK 3 S31: -0.1792 S32: 0.0508 S33: -0.0042
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3244 22.7198 45.9706
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.3422
REMARK 3 T33: 0.2982 T12: -0.0858
REMARK 3 T13: -0.0119 T23: -0.0952
REMARK 3 L TENSOR
REMARK 3 L11: 3.0110 L22: 2.3774
REMARK 3 L33: 1.2869 L12: -2.1011
REMARK 3 L13: -1.9159 L23: 1.1211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0780 S12: 0.4411 S13: -0.2501
REMARK 3 S21: 0.3002 S22: -0.3848 S23: 0.4259
REMARK 3 S31: 0.2934 S32: -0.6925 S33: 0.5066
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5241 18.4011 46.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.1998
REMARK 3 T33: 0.2007 T12: -0.0116
REMARK 3 T13: 0.0451 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 3.0015 L22: 3.4192
REMARK 3 L33: 5.5305 L12: 0.6329
REMARK 3 L13: 2.3602 L23: 1.4730
REMARK 3 S TENSOR
REMARK 3 S11: -0.0215 S12: -0.0036 S13: -0.1110
REMARK 3 S21: 0.2440 S22: 0.1158 S23: 0.1547
REMARK 3 S31: 0.3205 S32: -0.0476 S33: -0.0980
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 170 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8538 38.3617 60.8870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2692 T22: 0.4359
REMARK 3 T33: 0.1474 T12: -0.0050
REMARK 3 T13: 0.0484 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 3.9806 L22: 6.3004
REMARK 3 L33: 0.5027 L12: -1.7264
REMARK 3 L13: -0.7542 L23: 1.6468
REMARK 3 S TENSOR
REMARK 3 S11: 0.1258 S12: 0.2616 S13: 0.1517
REMARK 3 S21: 0.4661 S22: -0.2106 S23: 0.0509
REMARK 3 S31: -0.0350 S32: -0.2484 S33: 0.1184
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4002 46.8329 56.3657
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.2116
REMARK 3 T33: 0.1774 T12: 0.0128
REMARK 3 T13: 0.0250 T23: -0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 4.1098 L22: 0.8852
REMARK 3 L33: 1.5513 L12: 0.4460
REMARK 3 L13: 1.7476 L23: -0.5768
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.2991 S13: 0.1188
REMARK 3 S21: -0.0665 S22: 0.0849 S23: -0.0137
REMARK 3 S31: -0.1929 S32: 0.0590 S33: 0.0204
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0539 21.9715 57.2717
REMARK 3 T TENSOR
REMARK 3 T11: 0.2298 T22: 0.2553
REMARK 3 T33: 0.1761 T12: 0.0062
REMARK 3 T13: 0.0386 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.0764 L22: 2.9516
REMARK 3 L33: 0.2110 L12: -1.7373
REMARK 3 L13: 0.2464 L23: -0.7329
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: -0.1756 S13: -0.1602
REMARK 3 S21: -0.1650 S22: -0.0237 S23: 0.1531
REMARK 3 S31: 0.0996 S32: 0.0229 S33: -0.0553
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 329 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0808 29.1107 53.2431
REMARK 3 T TENSOR
REMARK 3 T11: 0.2622 T22: 0.2799
REMARK 3 T33: 0.1138 T12: -0.0497
REMARK 3 T13: 0.0490 T23: -0.1038
REMARK 3 L TENSOR
REMARK 3 L11: 2.3276 L22: 9.2844
REMARK 3 L33: 1.3391 L12: 1.3366
REMARK 3 L13: -0.2425 L23: -2.3329
REMARK 3 S TENSOR
REMARK 3 S11: 0.0802 S12: -0.2151 S13: 0.0921
REMARK 3 S21: -0.5690 S22: -0.0692 S23: -0.5912
REMARK 3 S31: -0.1025 S32: 0.2560 S33: -0.0382
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 330 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0216 25.6141 44.3220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0780 T22: 0.3573
REMARK 3 T33: 0.2137 T12: 0.0515
REMARK 3 T13: 0.0477 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 4.0529 L22: 4.1259
REMARK 3 L33: 5.9462 L12: 0.2140
REMARK 3 L13: 0.7137 L23: 3.7383
REMARK 3 S TENSOR
REMARK 3 S11: 0.2466 S12: -0.1902 S13: -0.2807
REMARK 3 S21: -0.1181 S22: 0.0668 S23: -0.9067
REMARK 3 S31: 0.2009 S32: 0.2343 S33: -0.2400
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8198 54.3835 96.2043
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.3887
REMARK 3 T33: 0.1918 T12: 0.0147
REMARK 3 T13: 0.0747 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 3.2160 L22: 3.4107
REMARK 3 L33: 4.3716 L12: -1.0947
REMARK 3 L13: 3.5232 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.3750 S12: 0.0807 S13: 0.1059
REMARK 3 S21: -0.0107 S22: -0.2770 S23: 0.3072
REMARK 3 S31: 0.3233 S32: -0.2847 S33: -0.1424
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9966 47.1239 82.6025
REMARK 3 T TENSOR
REMARK 3 T11: 0.1816 T22: 0.2659
REMARK 3 T33: 0.1731 T12: 0.0080
REMARK 3 T13: -0.0034 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.5699 L22: 0.6825
REMARK 3 L33: 0.8611 L12: 0.1610
REMARK 3 L13: 0.2512 L23: 0.2484
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.0579 S13: -0.0089
REMARK 3 S21: -0.0106 S22: -0.0094 S23: -0.0164
REMARK 3 S31: -0.0037 S32: 0.0081 S33: 0.0528
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 308 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0752 37.6116 84.7626
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.3411
REMARK 3 T33: 0.2353 T12: 0.1164
REMARK 3 T13: -0.0383 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.4023 L22: 4.1971
REMARK 3 L33: 3.5808 L12: 1.2494
REMARK 3 L13: 0.5999 L23: 0.9057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0909 S12: 0.1573 S13: -0.0141
REMARK 3 S21: 0.2641 S22: 0.0096 S23: -0.3187
REMARK 3 S31: 0.2261 S32: 0.1825 S33: -0.1033
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 5E4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000213744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8729
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16961
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 44.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.28200
REMARK 200 FOR THE DATA SET : 6.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.08260
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: PHENIX
REMARK 200 STARTING MODEL: 5D60
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6, 5 % PEG 1000, 30 % PEG
REMARK 280 600, 10 % GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 29.17300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.08850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.97300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.08850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.17300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.97300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 THR A -10
REMARK 465 MET A -9
REMARK 465 ILE A -8
REMARK 465 THR A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 TYR A 349
REMARK 465 MET B -11
REMARK 465 THR B -10
REMARK 465 MET B -9
REMARK 465 ILE B -8
REMARK 465 THR B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 TYR B 349
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 TRP A 55 -167.99 -101.79
REMARK 500 SER A 92 -169.95 -78.86
REMARK 500 SER A 139 -106.89 56.05
REMARK 500 VAL A 200 40.59 -98.47
REMARK 500 TRP A 216 -124.82 -112.92
REMARK 500 PHE A 241 -59.75 -123.48
REMARK 500 TRP B 55 -167.86 -102.10
REMARK 500 SER B 92 -169.69 -79.07
REMARK 500 SER B 139 -106.88 56.10
REMARK 500 TYR B 152 78.03 -119.91
REMARK 500 VAL B 200 39.69 -99.22
REMARK 500 TRP B 216 -125.20 -113.03
REMARK 500 PHE B 241 -60.63 -123.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5E4Y A 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5E4Y B 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
SEQADV 5E4Y MET A -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5E4Y THR A -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y MET A -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y ILE A -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y THR A -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS A -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y GLY A 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y SER A 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y MET B -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5E4Y THR B -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y MET B -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y ILE B -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y THR B -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y HIS B -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y GLY B 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5E4Y SER B 1 UNP Q0MRG5 EXPRESSION TAG
SEQRES 1 A 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 A 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 A 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 A 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 A 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 A 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 A 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 A 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 A 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 A 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 A 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 A 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 A 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 A 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 A 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 A 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 A 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 A 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 A 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 A 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 A 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 A 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 A 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 A 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 A 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 A 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 A 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 A 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 B 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 B 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 B 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 B 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 B 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 B 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 B 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 B 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 B 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 B 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 B 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 B 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 B 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 B 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 B 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 B 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 B 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 B 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 B 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 B 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 B 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 B 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 B 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 B 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 B 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 B 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 B 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 B 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
FORMUL 3 HOH *89(H2 O)
HELIX 1 AA1 THR A 6 GLY A 11 1 6
HELIX 2 AA2 THR A 59 TYR A 67 1 9
HELIX 3 AA3 GLY A 99 PHE A 107 5 9
HELIX 4 AA4 ARG A 111 TYR A 126 1 16
HELIX 5 AA5 SER A 139 TYR A 152 1 14
HELIX 6 AA6 SER A 169 THR A 185 1 17
HELIX 7 AA7 ASP A 186 LEU A 193 5 8
HELIX 8 AA8 SER A 196 ALA A 199 5 4
HELIX 9 AA9 VAL A 200 GLY A 215 1 16
HELIX 10 AB1 SER A 217 THR A 223 1 7
HELIX 11 AB2 GLY A 224 LEU A 229 1 6
HELIX 12 AB3 SER A 233 PHE A 241 1 9
HELIX 13 AB4 PHE A 241 ALA A 247 1 7
HELIX 14 AB5 ASP A 250 ARG A 263 1 14
HELIX 15 AB6 ASP A 265 THR A 270 5 6
HELIX 16 AB7 ASP A 273 GLY A 279 1 7
HELIX 17 AB8 THR A 297 LYS A 306 1 10
HELIX 18 AB9 GLY A 321 GLY A 327 5 7
HELIX 19 AC1 ASP A 329 SER A 346 1 18
HELIX 20 AC2 THR B 6 GLY B 11 1 6
HELIX 21 AC3 THR B 59 TYR B 67 1 9
HELIX 22 AC4 GLY B 99 PHE B 107 5 9
HELIX 23 AC5 ARG B 111 TYR B 126 1 16
HELIX 24 AC6 SER B 139 TYR B 152 1 14
HELIX 25 AC7 SER B 169 THR B 185 1 17
HELIX 26 AC8 ASP B 186 LEU B 193 5 8
HELIX 27 AC9 SER B 196 ALA B 199 5 4
HELIX 28 AD1 VAL B 200 GLY B 215 1 16
HELIX 29 AD2 SER B 217 THR B 223 1 7
HELIX 30 AD3 SER B 233 PHE B 241 1 9
HELIX 31 AD4 PHE B 241 ALA B 247 1 7
HELIX 32 AD5 ASP B 250 ARG B 263 1 14
HELIX 33 AD6 ASP B 265 HIS B 269 5 5
HELIX 34 AD7 ASP B 273 GLY B 279 1 7
HELIX 35 AD8 THR B 297 LYS B 306 1 10
HELIX 36 AD9 GLY B 321 GLY B 327 5 7
HELIX 37 AE1 ASP B 329 SER B 346 1 18
SHEET 1 AA1 8 GLU A 14 ASN A 17 0
SHEET 2 AA1 8 LEU A 33 HIS A 39 -1 O VAL A 36 N GLU A 14
SHEET 3 AA1 8 CYS A 80 VAL A 84 -1 O VAL A 83 N ALA A 37
SHEET 4 AA1 8 ALA A 49 PRO A 53 1 N ILE A 50 O ILE A 82
SHEET 5 AA1 8 LEU A 134 GLY A 138 1 O LEU A 134 N LEU A 51
SHEET 6 AA1 8 ARG A 158 ILE A 162 1 O ALA A 160 N VAL A 135
SHEET 7 AA1 8 LYS A 284 MET A 288 1 O LYS A 284 N ALA A 159
SHEET 8 AA1 8 GLU A 312 PHE A 313 1 O GLU A 312 N VAL A 287
SHEET 1 AA2 2 LEU A 21 PRO A 22 0
SHEET 2 AA2 2 CYS A 28 MET A 29 -1 O MET A 29 N LEU A 21
SHEET 1 AA3 8 GLU B 14 ASN B 17 0
SHEET 2 AA3 8 LEU B 33 HIS B 39 -1 O VAL B 36 N GLU B 14
SHEET 3 AA3 8 CYS B 80 VAL B 84 -1 O VAL B 83 N ALA B 37
SHEET 4 AA3 8 ALA B 49 PRO B 53 1 N ILE B 50 O ILE B 82
SHEET 5 AA3 8 LEU B 134 GLY B 138 1 O LEU B 134 N LEU B 51
SHEET 6 AA3 8 ARG B 158 ILE B 162 1 O ALA B 160 N VAL B 135
SHEET 7 AA3 8 LYS B 284 MET B 288 1 O LYS B 284 N ALA B 159
SHEET 8 AA3 8 SER B 311 PHE B 313 1 O GLU B 312 N THR B 285
SHEET 1 AA4 2 LEU B 21 PRO B 22 0
SHEET 2 AA4 2 CYS B 28 MET B 29 -1 O MET B 29 N LEU B 21
CISPEP 1 GLY A 11 PRO A 12 0 1.56
CISPEP 2 GLY B 11 PRO B 12 0 0.50
CRYST1 58.346 79.946 142.177 90.00 90.00 90.00 P 21 21 21 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 0.017139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012508 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007033 0.00000
TER 2674 ALA A 348
TER 5351 ALA B 348
MASTER 443 0 0 37 20 0 0 6 5427 2 0 56
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