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HEADER IMMUNE SYSTEM 20-NOV-18 6I8H
TITLE STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE
TITLE 2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB15
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_COMMON: LLAMA;
SOURCE 11 ORGANISM_TAXID: 9844;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 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 6I8H 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. 3.68 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) : 3.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.5
REMARK 3 NUMBER OF REFLECTIONS : 8238
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.710
REMARK 3 FREE R VALUE TEST SET COUNT : 800
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 72.9578 - 6.6884 1.00 1755 200 0.1954 0.2405
REMARK 3 2 6.6884 - 5.3092 1.00 1674 160 0.2860 0.3468
REMARK 3 3 5.3092 - 4.6382 1.00 1595 200 0.2853 0.3405
REMARK 3 4 4.6382 - 4.2142 0.97 1566 160 0.2953 0.3133
REMARK 3 5 4.2142 - 3.9122 0.45 722 80 0.3230 0.3952
REMARK 3 6 3.9122 - 3.6815 0.07 126 0 0.3890 0.0000
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) : 0.530
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.750
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 6024
REMARK 3 ANGLE : 0.608 8138
REMARK 3 CHIRALITY : 0.041 869
REMARK 3 PLANARITY : 0.005 1058
REMARK 3 DIHEDRAL : 11.016 3609
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 3 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7833 -43.3036 11.4332
REMARK 3 T TENSOR
REMARK 3 T11: 1.3089 T22: 1.2245
REMARK 3 T33: 1.5785 T12: 0.3158
REMARK 3 T13: 0.4475 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 4.0563 L22: 1.4636
REMARK 3 L33: 1.7069 L12: 1.0235
REMARK 3 L13: -0.4557 L23: -1.4619
REMARK 3 S TENSOR
REMARK 3 S11: 0.6002 S12: 0.8802 S13: 2.0997
REMARK 3 S21: 0.6159 S22: -0.0435 S23: 0.1064
REMARK 3 S31: -1.6114 S32: -0.3547 S33: 0.2178
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4871 -58.4527 15.0646
REMARK 3 T TENSOR
REMARK 3 T11: 0.8860 T22: 1.6993
REMARK 3 T33: 1.4660 T12: 0.0893
REMARK 3 T13: 0.3090 T23: 0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 2.1666 L22: 2.2192
REMARK 3 L33: 1.9252 L12: 0.4904
REMARK 3 L13: 0.2479 L23: 0.3196
REMARK 3 S TENSOR
REMARK 3 S11: 0.5280 S12: -0.6941 S13: 0.3657
REMARK 3 S21: 0.8778 S22: -0.1818 S23: 0.1705
REMARK 3 S31: -0.5185 S32: -0.3283 S33: 0.2893
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 620 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1205 -60.2724 -17.6158
REMARK 3 T TENSOR
REMARK 3 T11: 1.3752 T22: 1.3848
REMARK 3 T33: 0.8022 T12: -0.2592
REMARK 3 T13: 0.1281 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 2.4344 L22: 1.6657
REMARK 3 L33: 1.1986 L12: 0.8838
REMARK 3 L13: -1.7657 L23: -1.7498
REMARK 3 S TENSOR
REMARK 3 S11: -0.4309 S12: 0.9930 S13: -0.4790
REMARK 3 S21: -0.7451 S22: 0.3051 S23: -0.5491
REMARK 3 S31: 0.2380 S32: -0.1722 S33: 0.0084
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8184 -23.7914 -15.6190
REMARK 3 T TENSOR
REMARK 3 T11: 2.1391 T22: 1.8463
REMARK 3 T33: 2.3750 T12: 0.5876
REMARK 3 T13: -0.2557 T23: 0.0780
REMARK 3 L TENSOR
REMARK 3 L11: -0.0153 L22: 0.0061
REMARK 3 L33: 0.0686 L12: -0.0227
REMARK 3 L13: 0.0139 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.2684 S12: 0.5159 S13: -0.1729
REMARK 3 S21: -0.1278 S22: -0.2236 S23: -0.3134
REMARK 3 S31: -0.1189 S32: -0.2640 S33: 0.0007
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5245 -27.3914 -6.2592
REMARK 3 T TENSOR
REMARK 3 T11: 1.7416 T22: 1.6041
REMARK 3 T33: 2.4918 T12: 0.4774
REMARK 3 T13: -0.1606 T23: -0.1474
REMARK 3 L TENSOR
REMARK 3 L11: 0.2009 L22: 0.1765
REMARK 3 L33: 0.2541 L12: 0.2029
REMARK 3 L13: -0.1930 L23: -0.2044
REMARK 3 S TENSOR
REMARK 3 S11: 0.3026 S12: -0.3527 S13: -0.1236
REMARK 3 S21: -1.6989 S22: -0.4263 S23: -0.9207
REMARK 3 S31: -1.8594 S32: 0.6329 S33: -0.0040
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9496 -36.8433 -17.4982
REMARK 3 T TENSOR
REMARK 3 T11: 2.5793 T22: 2.1265
REMARK 3 T33: 2.6931 T12: -0.1567
REMARK 3 T13: -0.5150 T23: -0.7592
REMARK 3 L TENSOR
REMARK 3 L11: 0.0582 L22: 0.0049
REMARK 3 L33: 0.0101 L12: 0.0304
REMARK 3 L13: 0.0323 L23: 0.0085
REMARK 3 S TENSOR
REMARK 3 S11: -0.6072 S12: 0.3946 S13: -0.1341
REMARK 3 S21: 0.5433 S22: 0.3668 S23: -0.4851
REMARK 3 S31: 1.6015 S32: -1.1922 S33: 0.0003
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1811 -36.8861 -17.0581
REMARK 3 T TENSOR
REMARK 3 T11: 1.4044 T22: 1.6245
REMARK 3 T33: 3.1242 T12: -0.0831
REMARK 3 T13: -0.2259 T23: 0.5495
REMARK 3 L TENSOR
REMARK 3 L11: 0.0494 L22: 0.1836
REMARK 3 L33: 0.2022 L12: 0.0772
REMARK 3 L13: 0.0562 L23: 0.1417
REMARK 3 S TENSOR
REMARK 3 S11: 0.3702 S12: 0.0989 S13: -0.0662
REMARK 3 S21: -1.7209 S22: -0.5614 S23: -0.4144
REMARK 3 S31: 1.1837 S32: -0.2297 S33: -0.2117
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0028 -33.0269 -21.0632
REMARK 3 T TENSOR
REMARK 3 T11: 1.3280 T22: 1.5979
REMARK 3 T33: 2.1138 T12: -0.4499
REMARK 3 T13: -0.2260 T23: -0.1380
REMARK 3 L TENSOR
REMARK 3 L11: 1.1493 L22: 0.8431
REMARK 3 L33: 0.3664 L12: -0.9910
REMARK 3 L13: 0.1962 L23: -0.1968
REMARK 3 S TENSOR
REMARK 3 S11: 0.9316 S12: -0.7947 S13: 0.3078
REMARK 3 S21: 0.0823 S22: -1.0957 S23: -1.2866
REMARK 3 S31: 0.8670 S32: -0.4771 S33: -0.0007
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7664 -24.3158 -13.0814
REMARK 3 T TENSOR
REMARK 3 T11: 0.2381 T22: 2.3906
REMARK 3 T33: 2.6895 T12: 0.2984
REMARK 3 T13: -0.2021 T23: 0.3836
REMARK 3 L TENSOR
REMARK 3 L11: 0.1221 L22: 0.0308
REMARK 3 L33: 0.2530 L12: 0.0493
REMARK 3 L13: -0.0985 L23: -0.0854
REMARK 3 S TENSOR
REMARK 3 S11: -0.4512 S12: -0.4921 S13: -0.2404
REMARK 3 S21: -0.1879 S22: -0.3205 S23: -0.0708
REMARK 3 S31: 0.0426 S32: 0.0376 S33: -1.0373
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0999 -29.7933 -21.9121
REMARK 3 T TENSOR
REMARK 3 T11: 2.5510 T22: 2.4600
REMARK 3 T33: 1.5421 T12: 0.0990
REMARK 3 T13: -0.1399 T23: 0.2064
REMARK 3 L TENSOR
REMARK 3 L11: 0.2611 L22: 0.1334
REMARK 3 L33: 0.2061 L12: -0.0763
REMARK 3 L13: -0.2576 L23: 0.0330
REMARK 3 S TENSOR
REMARK 3 S11: -1.4013 S12: -0.4646 S13: -0.6206
REMARK 3 S21: 0.2710 S22: -0.1267 S23: 0.2766
REMARK 3 S31: 1.8284 S32: -0.7425 S33: -0.0298
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 97 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2000 -37.8790 -5.2826
REMARK 3 T TENSOR
REMARK 3 T11: 1.6862 T22: 2.0746
REMARK 3 T33: 2.4886 T12: 0.1954
REMARK 3 T13: 0.4647 T23: 0.6343
REMARK 3 L TENSOR
REMARK 3 L11: 3.7348 L22: 6.6180
REMARK 3 L33: 4.3829 L12: -1.8570
REMARK 3 L13: -0.2540 L23: 5.1118
REMARK 3 S TENSOR
REMARK 3 S11: -1.3414 S12: 0.3727 S13: 0.7270
REMARK 3 S21: 0.2923 S22: -1.7843 S23: 1.6079
REMARK 3 S31: 0.5666 S32: -1.1377 S33: -1.4405
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7561 -26.4931 -22.0896
REMARK 3 T TENSOR
REMARK 3 T11: 2.5313 T22: 1.9742
REMARK 3 T33: 1.7623 T12: 0.2632
REMARK 3 T13: -0.0679 T23: 0.1411
REMARK 3 L TENSOR
REMARK 3 L11: 0.0258 L22: 0.0120
REMARK 3 L33: 0.1224 L12: 0.0062
REMARK 3 L13: 0.0295 L23: -0.0335
REMARK 3 S TENSOR
REMARK 3 S11: -0.4880 S12: 0.2154 S13: -0.2402
REMARK 3 S21: 0.5217 S22: 0.1367 S23: -0.6097
REMARK 3 S31: 0.2474 S32: -0.1182 S33: 0.0004
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 6I8H 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_1200012986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018,
REMARK 200 AUTOPROC VERSION JAN 26, 2018
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC VERSION 1.0.5, AIMLESS,
REMARK 200 AIMLESS, STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8246
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.682
REMARK 200 RESOLUTION RANGE LOW (A) : 97.361
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : 0.11100
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 1.34900
REMARK 200 R SYM FOR SHELL (I) : 1.34900
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 (%): 53.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 12.5 % (V/V)
REMARK 280 (RS)-2-METHYL-2,4-PENTANEDIOL, 12.5 % (W/V) PEG 1000, 12.5 % (W/
REMARK 280 V) PEG3350, 0.03 M MAGNESIUM CHLORIDE, 0.03 M CALCIUM CHLORIDE,
REMARK 280 0.0612 M MES, 0.0388 M IMIDAZOLE, PH 6.5; PROTEIN STOCK SOLUTION:
REMARK 280 4.1 MG/ML PROTEIN, 50 MM SODIUM CHLORIDE, 1 % (V/V) GLYCEROLE,
REMARK 280 1 MM DTT, 50 MM HEPES, PH 8.0; DROP COMPOSITION: 150 NL PROTEIN
REMARK 280 STOCK SOLUTION PLUS 225 NL RESERVOIR SOLUTION; CRYO CONDITIONS:
REMARK 280 THE CRYSTALS WERE FLASH FROZEN DIRECTLY FROM THE EQUILIBRATED
REMARK 280 CRYSTALLIZATION DROPS., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277.15K
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 76.38500
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 76.38500
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 76.38500
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 76.38500
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 76.38500
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 76.38500
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: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 ALA A 2
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 GLN B 1
REMARK 465 VAL B 2
REMARK 465 ALA B 129
REMARK 465 ALA B 130
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 -59.04 61.82
REMARK 500 ASP A 98 119.67 -38.13
REMARK 500 SER A 123 -132.68 57.06
REMARK 500 ASN A 144 78.19 -159.82
REMARK 500 PRO A 145 92.55 -69.67
REMARK 500 VAL A 161 -51.20 -120.29
REMARK 500 SER A 216 35.24 -97.51
REMARK 500 GLN B 14 -160.35 -79.12
REMARK 500 ARG B 28 90.81 -63.75
REMARK 500 THR B 29 -70.27 -100.48
REMARK 500 PHE B 30 -107.28 17.92
REMARK 500 PRO B 46 105.29 -56.01
REMARK 500 ARG B 50 74.15 -63.00
REMARK 500 VAL B 53 -65.38 -93.15
REMARK 500 SER B 57 49.51 -82.32
REMARK 500 SER B 58 -120.62 52.95
REMARK 500 ASP B 69 -85.41 56.52
REMARK 500 LYS B 72 105.66 -40.54
REMARK 500 ARG B 75 -42.50 -137.53
REMARK 500 LEU B 109 9.45 58.74
REMARK 500 ASN B 116 14.38 -157.21
REMARK 500 SER B 127 -149.34 -103.56
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6I8H A 1 623 UNP Q9XF23 EDS1L_ARATH 1 623
DBREF 6I8H B 1 147 PDB 6I8H 6I8H 1 147
SEQADV 6I8H LEU A 624 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H GLU A 625 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H HIS A 626 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H HIS A 627 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H HIS A 628 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H HIS A 629 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H HIS A 630 UNP Q9XF23 EXPRESSION TAG
SEQADV 6I8H 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 137 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 137 ALA GLY GLY SER LEU ARG LEU SER CYS ALA GLY SER GLY
SEQRES 3 B 137 ARG THR PHE SER THR TYR ASP MET ALA TRP PHE ARG GLN
SEQRES 4 B 137 ALA PRO GLY LYS GLU ARG GLU PHE VAL SER SER ILE SER
SEQRES 5 B 137 SER SER GLY GLY ASN VAL VAL TYR ARG ASP SER VAL LYS
SEQRES 6 B 137 GLY ARG PHE THR ILE ALA ARG ASP ASN ALA ALA ASN ALA
SEQRES 7 B 137 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 137 ALA VAL TYR TYR CYS ALA ALA LYS TRP LEU ALA ALA ASP
SEQRES 9 B 137 TYR ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER
SEQRES 10 B 137 SER ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY
SEQRES 11 B 137 SER HIS HIS HIS HIS HIS HIS
HELIX 1 AA1 PHE A 3 GLY A 8 1 6
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 PHE A 141 ASN A 144 5 4
HELIX 10 AB1 ASP A 163 GLU A 173 1 11
HELIX 11 AB2 TRP A 175 ARG A 177 5 3
HELIX 12 AB3 ILE A 188 ALA A 195 5 8
HELIX 13 AB4 THR A 203 ASP A 212 1 10
HELIX 14 AB5 SER A 221 THR A 248 1 28
HELIX 15 AB6 ALA A 251 LEU A 262 1 12
HELIX 16 AB7 ASN A 286 THR A 297 1 12
HELIX 17 AB8 LEU A 308 ASP A 316 1 9
HELIX 18 AB9 SER A 319 SER A 326 1 8
HELIX 19 AC1 MET A 327 LYS A 330 5 4
HELIX 20 AC2 ASP A 336 GLU A 338 5 3
HELIX 21 AC3 ILE A 341 LEU A 348 1 8
HELIX 22 AC4 SER A 351 GLN A 381 1 31
HELIX 23 AC5 GLN A 381 GLU A 394 1 14
HELIX 24 AC6 GLU A 394 HIS A 402 1 9
HELIX 25 AC7 ASN A 404 SER A 413 1 10
HELIX 26 AC8 GLU A 415 LYS A 441 1 27
HELIX 27 AC9 PRO A 445 GLY A 450 5 6
HELIX 28 AD1 ASP A 451 HIS A 476 1 26
HELIX 29 AD2 LEU A 477 THR A 482 1 6
HELIX 30 AD3 PRO A 484 GLY A 489 1 6
HELIX 31 AD4 PRO A 491 LYS A 507 1 17
HELIX 32 AD5 PRO A 508 GLY A 510 5 3
HELIX 33 AD6 ILE A 512 LEU A 524 1 13
HELIX 34 AD7 GLN A 529 LEU A 537 1 9
HELIX 35 AD8 SER A 540 SER A 546 5 7
HELIX 36 AD9 CYS A 547 LYS A 556 1 10
HELIX 37 AE1 VAL A 563 ALA A 580 1 18
HELIX 38 AE2 ASP A 584 PHE A 589 1 6
HELIX 39 AE3 SER A 593 THR A 601 1 9
HELIX 40 AE4 PRO A 603 HIS A 609 1 7
HELIX 41 AE5 LEU A 612 MET A 616 5 5
HELIX 42 AE6 LYS B 95 THR B 99 5 5
SHEET 1 AA1 8 TYR A 30 ALA A 35 0
SHEET 2 AA1 8 VAL A 38 PHE A 43 -1 O VAL A 38 N ALA A 35
SHEET 3 AA1 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 41
SHEET 4 AA1 8 ARG A 152 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 GLY B 25 -1 O ALA B 24 N GLN B 5
SHEET 3 AA3 4 ALA 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 ALA B 79 O TYR B 88
SHEET 1 AA4 4 ARG B 50 SER B 55 0
SHEET 2 AA4 4 ALA B 40 GLN B 44 -1 N TRP B 41 O SER B 54
SHEET 3 AA4 4 ALA B 100 CYS B 104 -1 O TYR B 103 N PHE B 42
SHEET 4 AA4 4 THR B 122 VAL B 124 -1 O THR B 122 N TYR B 102
SSBOND 1 CYS B 23 CYS B 104 1555 1555 2.03
CRYST1 145.887 145.887 152.770 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 0.006855 0.003958 0.000000 0.00000
SCALE2 0.000000 0.007915 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006546 0.00000
TER 5012 ILE A 620
TER 5895 SER B 128
MASTER 529 0 0 42 18 0 0 6 5893 2 2 60
END |