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HEADER IMMUNE SYSTEM 20-NOV-18 6I8G
TITLE STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE
TITLE 2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB73
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN EDS1L;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1-LIKE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EDS1-SPECIFIC NANOBODY;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: EDS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 10 ORGANISM_TAXID: 9844;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENHANCED DISEASE SUSCEPTIBILITY 1, PLANT INNATE IMMUNE SYSTEM,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, NANOBODY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,M.VOSS,C.TOELZER
REVDAT 1 02-OCT-19 6I8G 0
JRNL AUTH M.VOSS,C.TOELZER,D.D.BHANDARI,J.E.PARKER,K.NIEFIND
JRNL TITL ARABIDOPSIS IMMUNITY REGULATOR EDS1 IN A PAD4/SAG101-UNBOUND
JRNL TITL 2 FORM IS A MONOMER WITH AN INHERENTLY INACTIVE CONFORMATION.
JRNL REF J.STRUCT.BIOL. 2019
JRNL REFN ESSN 1095-8657
JRNL PMID 31550533
JRNL DOI 10.1016/J.JSB.2019.09.007
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,E.BRUNSTEIN,J.BAUTOR,
REMARK 1 AUTH 2 K.NIEFIND,J.E.PARKER
REMARK 1 TITL STRUCTURAL BASIS FOR SIGNALING BY EXCLUSIVE EDS1 HETEROMERIC
REMARK 1 TITL 2 COMPLEXES WITH SAG101 OR PAD4 IN PLANT INNATE IMMUNITY.
REMARK 1 REF CELL HOST MICROBE V. 14 619 2013
REMARK 1 REFN ESSN 1934-6069
REMARK 1 PMID 24331460
REMARK 1 DOI 10.1016/J.CHOM.2013.11.006
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.WAGNER,S.RIETZ,J.E.PARKER,K.NIEFIND
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 1 TITL 2 ARABIDOPSIS THALIANA EDS1, A KEY COMPONENT OF PLANT
REMARK 1 TITL 3 IMMUNITY, IN COMPLEX WITH ITS SIGNALLING PARTNER SAG101.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 67 245 2011
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 21301097
REMARK 1 DOI 10.1107/S1744309110051249
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.RIETZ,A.STAMM,S.MALONEK,S.WAGNER,D.BECKER,
REMARK 1 AUTH 2 N.MEDINA-ESCOBAR,A.C.VLOT,B.J.FEYS,K.NIEFIND,J.E.PARKER
REMARK 1 TITL DIFFERENT ROLES OF ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1)
REMARK 1 TITL 2 BOUND TO AND DISSOCIATED FROM PHYTOALEXIN DEFICIENT4 (PAD4)
REMARK 1 TITL 3 IN ARABIDOPSIS IMMUNITY.
REMARK 1 REF NEW PHYTOL. V. 191 107 2011
REMARK 1 REFN ISSN 1469-8137
REMARK 1 PMID 21434927
REMARK 1 DOI 10.1111/J.1469-8137.2011.03675.X
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 71.1
REMARK 3 NUMBER OF REFLECTIONS : 31537
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1295
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 52.5833 - 4.8745 1.00 4848 202 0.1537 0.1594
REMARK 3 2 4.8745 - 3.8694 0.96 4569 199 0.1437 0.1845
REMARK 3 3 3.8694 - 3.3804 0.98 4620 199 0.1930 0.2442
REMARK 3 4 3.3804 - 3.0713 0.99 4663 198 0.2350 0.2695
REMARK 3 5 3.0713 - 2.8512 0.94 4461 182 0.2736 0.2879
REMARK 3 6 2.8512 - 2.6831 0.73 3433 157 0.2885 0.2944
REMARK 3 7 2.6831 - 2.5487 0.51 2407 91 0.2871 0.3319
REMARK 3 8 2.5487 - 2.4378 0.22 998 63 0.3096 0.3280
REMARK 3 9 2.4378 - 2.3440 0.05 243 4 0.2912 0.3445
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.740
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 6138
REMARK 3 ANGLE : 0.522 8302
REMARK 3 CHIRALITY : 0.040 890
REMARK 3 PLANARITY : 0.004 1079
REMARK 3 DIHEDRAL : 15.396 3680
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): 140.9226 -30.7636 104.9686
REMARK 3 T TENSOR
REMARK 3 T11: 0.2258 T22: 0.1315
REMARK 3 T33: 0.2307 T12: -0.0329
REMARK 3 T13: -0.0081 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.9118 L22: 1.7859
REMARK 3 L33: 2.5561 L12: -0.7885
REMARK 3 L13: -0.5838 L23: 0.4871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.0635 S13: -0.2017
REMARK 3 S21: 0.0921 S22: 0.0762 S23: 0.0262
REMARK 3 S31: 0.3075 S32: 0.0365 S33: -0.0083
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 159.5783 -31.2154 110.2968
REMARK 3 T TENSOR
REMARK 3 T11: 0.3015 T22: 0.4677
REMARK 3 T33: 0.3901 T12: 0.0939
REMARK 3 T13: -0.0714 T23: -0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 2.3673 L22: 2.8686
REMARK 3 L33: 0.8199 L12: 0.2222
REMARK 3 L13: -0.5415 L23: 0.5868
REMARK 3 S TENSOR
REMARK 3 S11: -0.1090 S12: -0.1631 S13: -0.1106
REMARK 3 S21: 0.1902 S22: 0.2694 S23: -0.5227
REMARK 3 S31: 0.1425 S32: 0.6417 S33: 0.0338
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 326 THROUGH 619 )
REMARK 3 ORIGIN FOR THE GROUP (A): 143.6273 -15.8264 72.8895
REMARK 3 T TENSOR
REMARK 3 T11: 0.2687 T22: 0.4344
REMARK 3 T33: 0.4483 T12: -0.0052
REMARK 3 T13: 0.0731 T23: 0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 2.0865 L22: 0.7598
REMARK 3 L33: 3.4215 L12: -0.0713
REMARK 3 L13: 1.1129 L23: -0.0941
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: 0.6796 S13: 0.3460
REMARK 3 S21: -0.1395 S22: -0.0432 S23: 0.0105
REMARK 3 S31: -0.0703 S32: 0.3494 S33: -0.0157
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 136.9273 -32.0743 148.3217
REMARK 3 T TENSOR
REMARK 3 T11: 0.6670 T22: 0.2444
REMARK 3 T33: 0.2667 T12: 0.0049
REMARK 3 T13: 0.0178 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.2691 L22: 0.0522
REMARK 3 L33: 0.0945 L12: -0.1422
REMARK 3 L13: 0.0495 L23: -0.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.2600 S12: -0.0924 S13: 0.2615
REMARK 3 S21: 0.0540 S22: -0.2594 S23: 0.1121
REMARK 3 S31: -0.6005 S32: 0.0581 S33: 0.0009
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 134.1452 -31.9076 136.3049
REMARK 3 T TENSOR
REMARK 3 T11: 0.5062 T22: 0.1896
REMARK 3 T33: 0.3694 T12: 0.0473
REMARK 3 T13: -0.0835 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.1465 L22: 0.2310
REMARK 3 L33: 1.5826 L12: 0.0595
REMARK 3 L13: 0.2097 L23: -0.4157
REMARK 3 S TENSOR
REMARK 3 S11: -0.2272 S12: -0.1322 S13: -0.0166
REMARK 3 S21: -0.1027 S22: 0.1823 S23: 0.4133
REMARK 3 S31: -0.5762 S32: -0.4898 S33: 0.0039
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 146.2132 -37.1055 143.5073
REMARK 3 T TENSOR
REMARK 3 T11: 0.5125 T22: 0.3568
REMARK 3 T33: 0.3160 T12: -0.1584
REMARK 3 T13: -0.0441 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.3401 L22: 0.0007
REMARK 3 L33: 0.8022 L12: -0.0121
REMARK 3 L13: -0.5276 L23: 0.0178
REMARK 3 S TENSOR
REMARK 3 S11: 0.1772 S12: -0.3523 S13: -0.0150
REMARK 3 S21: 0.2235 S22: -0.1051 S23: -0.2543
REMARK 3 S31: -0.4790 S32: 0.5970 S33: -0.0168
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 138.5526 -43.3439 131.3518
REMARK 3 T TENSOR
REMARK 3 T11: 0.5630 T22: 0.2734
REMARK 3 T33: 0.4247 T12: -0.0459
REMARK 3 T13: -0.0782 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.1034 L22: 0.0036
REMARK 3 L33: 0.7281 L12: -0.0026
REMARK 3 L13: 0.0096 L23: -0.0558
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: 0.1789 S13: -0.5034
REMARK 3 S21: -0.2919 S22: 0.4691 S23: 0.2708
REMARK 3 S31: 0.3739 S32: 0.2311 S33: 0.0100
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 134.6268 -40.6225 142.0638
REMARK 3 T TENSOR
REMARK 3 T11: 0.4926 T22: 0.2451
REMARK 3 T33: 0.3376 T12: -0.0063
REMARK 3 T13: -0.0463 T23: 0.0724
REMARK 3 L TENSOR
REMARK 3 L11: 0.1560 L22: 0.1467
REMARK 3 L33: 0.1866 L12: 0.1288
REMARK 3 L13: -0.0674 L23: -0.0678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1690 S12: -0.0662 S13: 0.0200
REMARK 3 S21: -0.4179 S22: -0.1698 S23: 0.2629
REMARK 3 S31: -0.2354 S32: -0.0681 S33: -0.0003
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 144.2069 -38.3669 142.9939
REMARK 3 T TENSOR
REMARK 3 T11: 0.4340 T22: 0.1997
REMARK 3 T33: 0.3223 T12: -0.0236
REMARK 3 T13: 0.0131 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.3183 L22: 0.0731
REMARK 3 L33: 0.3391 L12: 0.1230
REMARK 3 L13: -0.2100 L23: -0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.4382 S12: -0.1260 S13: 0.1176
REMARK 3 S21: -0.1040 S22: -0.3012 S23: 0.0897
REMARK 3 S31: -0.4215 S32: 0.2891 S33: 0.0134
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 144.2898 -33.1050 146.5476
REMARK 3 T TENSOR
REMARK 3 T11: 0.6282 T22: 0.2967
REMARK 3 T33: 0.3872 T12: -0.0870
REMARK 3 T13: 0.0015 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 0.2941 L22: 0.2068
REMARK 3 L33: 0.2693 L12: -0.1419
REMARK 3 L13: 0.0626 L23: 0.1186
REMARK 3 S TENSOR
REMARK 3 S11: 0.2556 S12: -0.3395 S13: 0.4651
REMARK 3 S21: 0.1362 S22: -0.1329 S23: -0.2885
REMARK 3 S31: -0.3875 S32: 0.1101 S33: 0.0218
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 6I8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-18
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 : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.967700
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018,
REMARK 200 AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AIMLESS, AUTOPROC VERSION 1.0.5,
REMARK 200 STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31550
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.344
REMARK 200 RESOLUTION RANGE LOW (A) : 83.773
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 71.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : 0.11700
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 15.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.87000
REMARK 200 R SYM FOR SHELL (I) : 0.87000
REMARK 200 FOR SHELL : 1.500
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: 4NFU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 17.5 % (W/V)
REMARK 280 PEG3350, 0.2 M SODIUM CITRATE, 0.1 M BIS-TRIS BUFFER, PH 8.5;
REMARK 280 PROTEIN STOCK SOLUTION: 2.8 MG/ML PROTEIN IN 50 MM SODIUM
REMARK 280 CHLORIDE, 1 % (V/V) GLYCEROLE, 1MM DTT, 50 MM HEPES, PH 8.0;
REMARK 280 DROP COMPOSITION: 1 MIKROLITER PROTEIN STOCK SOLUTION + 1
REMARK 280 MIKROLITER RESERVOIR SOLUTION; CRYSTALS WERE CRYOPROTECTED IN
REMARK 280 17.5 % (W/V) PEG3350, 20 % (V/V) ETHYLENE GLYCOL, 0.2 M SODIUM
REMARK 280 CITRATE, 0.1 M BIS-TRIS BUFFER, PH 8.5., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.75200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.11600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.75200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.11600
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 1
REMARK 465 ILE A 620
REMARK 465 THR A 621
REMARK 465 ASP A 622
REMARK 465 THR A 623
REMARK 465 LEU A 624
REMARK 465 GLU A 625
REMARK 465 HIS A 626
REMARK 465 HIS A 627
REMARK 465 HIS A 628
REMARK 465 HIS A 629
REMARK 465 HIS A 630
REMARK 465 HIS A 631
REMARK 465 ALA B 131
REMARK 465 TYR B 132
REMARK 465 PRO B 133
REMARK 465 TYR B 134
REMARK 465 ASP B 135
REMARK 465 VAL B 136
REMARK 465 PRO B 137
REMARK 465 ASP B 138
REMARK 465 TYR B 139
REMARK 465 GLY B 140
REMARK 465 SER B 141
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 HIS B 144
REMARK 465 HIS B 145
REMARK 465 HIS B 146
REMARK 465 HIS B 147
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 ARG A 29 -62.91 67.79
REMARK 500 SER A 123 -136.47 62.70
REMARK 500 TYR A 140 -58.05 -124.04
REMARK 500 VAL A 218 36.52 -89.21
REMARK 500 GLN A 219 73.18 51.51
REMARK 500 GLU A 220 -108.10 -77.41
REMARK 500 THR A 248 6.52 -165.18
REMARK 500 ALA A 251 -104.02 55.10
REMARK 500 ALA A 253 -75.67 -117.14
REMARK 500 THR A 257 -154.71 -74.15
REMARK 500 LEU A 258 -14.64 67.02
REMARK 500 PHE A 261 -65.27 -96.96
REMARK 500 LEU A 262 68.70 -106.12
REMARK 500 CYS A 298 31.49 -96.07
REMARK 500 SER A 301 -37.84 -130.34
REMARK 500 VAL B 110 70.86 53.57
REMARK 500 SER B 128 -118.04 -75.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6I8G A 1 623 UNP Q9XF23 EDS1L_ARATH 1 623
DBREF 6I8G B 1 147 PDB 6I8G 6I8G 1 147
SEQADV 6I8G LEU A 624 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G GLU A 625 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 626 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 627 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 628 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 629 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 630 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8G HIS A 631 UNP Q9XF23 EXPRESSION TAG
SEQRES 1 A 631 MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 2 A 631 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 3 A 631 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 4 A 631 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 5 A 631 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 6 A 631 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 7 A 631 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 8 A 631 ASN LEU GLU ALA VAL ILE ASP PRO ARG THR SER PHE GLN
SEQRES 9 A 631 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 10 A 631 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 11 A 631 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 12 A 631 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 13 A 631 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 14 A 631 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 15 A 631 VAL THR ARG PHE ASP ILE VAL PRO ARG ILE THR LEU ALA
SEQRES 16 A 631 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 17 A 631 ALA GLN LEU ASP PRO ARG ASN SER SER VAL GLN GLU SER
SEQRES 18 A 631 GLU GLN ARG ILE THR GLU PHE TYR THR SER VAL MET ARG
SEQRES 19 A 631 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 20 A 631 THR GLY SER ALA GLU ALA ILE LEU GLU THR LEU SER SER
SEQRES 21 A 631 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 22 A 631 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 23 A 631 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR CYS GLN
SEQRES 24 A 631 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 25 A 631 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 26 A 631 SER MET GLY MET LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 27 A 631 ASN SER ILE GLU SER SER LEU ASN ASP LEU GLY VAL SER
SEQRES 28 A 631 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 29 A 631 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 30 A 631 VAL ILE GLN GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 31 A 631 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 32 A 631 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 33 A 631 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 34 A 631 GLY VAL PHE ASP GLU VAL LEU GLY LEU LEU LYS LYS CYS
SEQRES 35 A 631 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 36 A 631 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 37 A 631 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 38 A 631 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 39 A 631 ILE TYR ALA GLN ARG GLY TYR GLU HIS HIS ILE LEU LYS
SEQRES 40 A 631 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 41 A 631 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 42 A 631 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 43 A 631 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 44 A 631 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 45 A 631 MET LEU ARG GLU TRP ILE THR ALA GLY GLU VAL ASP GLU
SEQRES 46 A 631 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 47 A 631 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 48 A 631 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR LEU
SEQRES 49 A 631 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 143 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 143 ALA GLY GLY SER LEU ARG LEU SER CYS ALA THR SER THR
SEQRES 3 B 143 HIS THR ALA GLY GLN TYR THR MET ALA TRP PHE ARG GLN
SEQRES 4 B 143 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL LEU ARG
SEQRES 5 B 143 TRP SER ASP TYR SER THR ASP TYR ALA ASN SER VAL LYS
SEQRES 6 B 143 ASN ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR
SEQRES 7 B 143 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 143 ALA VAL TYR TYR CYS ALA ALA GLY TRP PRO VAL LYS VAL
SEQRES 9 B 143 ILE SER SER ALA ASP GLU TYR ILE ASN TRP GLY GLN GLY
SEQRES 10 B 143 THR GLN VAL THR VAL SER SER ALA ALA ALA TYR PRO TYR
SEQRES 11 B 143 ASP VAL PRO ASP TYR GLY SER HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *169(H2 O)
HELIX 1 AA1 ALA A 2 GLY A 8 1 7
HELIX 2 AA2 ASN A 10 ALA A 24 1 15
HELIX 3 AA3 TYR A 25 THR A 27 5 3
HELIX 4 AA4 SER A 48 PHE A 52 5 5
HELIX 5 AA5 GLU A 87 ASP A 98 1 12
HELIX 6 AA6 PRO A 99 THR A 101 5 3
HELIX 7 AA7 SER A 102 SER A 113 1 12
HELIX 8 AA8 SER A 123 TYR A 140 1 18
HELIX 9 AA9 ASP A 163 GLU A 173 1 11
HELIX 10 AB1 TRP A 175 ARG A 177 5 3
HELIX 11 AB2 ILE A 188 ALA A 195 5 8
HELIX 12 AB3 ARG A 196 GLU A 201 1 6
HELIX 13 AB4 THR A 203 ASP A 212 1 10
HELIX 14 AB5 SER A 221 GLY A 249 1 29
HELIX 15 AB6 ASN A 286 THR A 297 1 12
HELIX 16 AB7 LEU A 308 ASP A 316 1 9
HELIX 17 AB8 SER A 319 SER A 326 1 8
HELIX 18 AB9 ILE A 341 LEU A 348 1 8
HELIX 19 AC1 SER A 351 GLN A 381 1 31
HELIX 20 AC2 GLN A 381 GLU A 394 1 14
HELIX 21 AC3 GLU A 394 HIS A 402 1 9
HELIX 22 AC4 ASN A 404 SER A 413 1 10
HELIX 23 AC5 GLU A 415 LYS A 441 1 27
HELIX 24 AC6 GLU A 447 GLY A 450 5 4
HELIX 25 AC7 ASP A 451 HIS A 476 1 26
HELIX 26 AC8 LEU A 477 THR A 482 1 6
HELIX 27 AC9 PRO A 484 GLY A 489 1 6
HELIX 28 AD1 PRO A 491 LYS A 507 1 17
HELIX 29 AD2 PRO A 508 GLY A 510 5 3
HELIX 30 AD3 ILE A 512 LEU A 524 1 13
HELIX 31 AD4 GLN A 529 LEU A 537 1 9
HELIX 32 AD5 SER A 540 SER A 546 5 7
HELIX 33 AD6 CYS A 547 LYS A 556 1 10
HELIX 34 AD7 VAL A 563 ALA A 580 1 18
HELIX 35 AD8 SER A 593 THR A 601 1 9
HELIX 36 AD9 PRO A 603 HIS A 609 1 7
HELIX 37 AE1 LEU A 612 MET A 616 5 5
HELIX 38 AE2 LYS B 95 THR B 99 5 5
HELIX 39 AE3 SER B 112A ASP B 113 5 3
SHEET 1 AA1 8 TYR A 30 ALA A 35 0
SHEET 2 AA1 8 VAL A 38 PHE A 43 -1 O ILE A 40 N GLU A 33
SHEET 3 AA1 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 41
SHEET 4 AA1 8 PRO A 151 PHE A 156 1 O ARG A 152 N PHE A 119
SHEET 5 AA1 8 PHE A 179 THR A 184 1 O PHE A 182 N THR A 155
SHEET 6 AA1 8 THR A 272 SER A 276 1 O VAL A 274 N ASN A 181
SHEET 7 AA1 8 ARG A 280 VAL A 284 -1 O VAL A 284 N PHE A 273
SHEET 8 AA1 8 LEU A 331 HIS A 334 1 O LEU A 331 N LEU A 281
SHEET 1 AA2 2 GLU A 63 LYS A 65 0
SHEET 2 AA2 2 THR A 84 ASN A 86 -1 O VAL A 85 N ILE A 64
SHEET 1 AA3 4 LEU B 4 SER B 7 0
SHEET 2 AA3 4 LEU B 19 THR B 25 -1 O ALA B 24 N GLN B 5
SHEET 3 AA3 4 THR B 86 MET B 91 -1 O MET B 91 N LEU B 19
SHEET 4 AA3 4 PHE B 76 ASP B 81 -1 N THR B 77 O GLN B 90
SHEET 1 AA4 6 LEU B 12 GLN B 14 0
SHEET 2 AA4 6 THR B 122 SER B 127 1 O THR B 125 N VAL B 13
SHEET 3 AA4 6 ALA B 100 GLY B 107 -1 N TYR B 102 O THR B 122
SHEET 4 AA4 6 THR B 38 GLN B 44 -1 N GLN B 44 O VAL B 101
SHEET 5 AA4 6 GLU B 51 LEU B 56 -1 O GLU B 51 N ARG B 43
SHEET 6 AA4 6 THR B 65 TYR B 67 -1 O ASP B 66 N VAL B 55
SHEET 1 AA5 4 LEU B 12 GLN B 14 0
SHEET 2 AA5 4 THR B 122 SER B 127 1 O THR B 125 N VAL B 13
SHEET 3 AA5 4 ALA B 100 GLY B 107 -1 N TYR B 102 O THR B 122
SHEET 4 AA5 4 TYR B 115 TRP B 118 -1 O ASN B 117 N ALA B 106
SSBOND 1 CYS B 23 CYS B 104 1555 1555 2.04
CISPEP 1 TRP B 108 PRO B 109 0 0.78
CRYST1 177.504 68.232 105.273 90.00 123.44 90.00 C 1 2 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 0.005634 0.000000 0.003721 0.00000
SCALE2 0.000000 0.014656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011384 0.00000
TER 5030 GLU A 619
TER 6003 ALA B 130
MASTER 460 0 0 39 24 0 0 6 6149 2 2 60
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