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HEADER IMMUNE SYSTEM 12-DEC-18 6Q6Z
TITLE STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE
TITLE 2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB21
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 6Q6Z 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. 3.48 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.8
REMARK 3 NUMBER OF REFLECTIONS : 12593
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.080
REMARK 3 FREE R VALUE TEST SET COUNT : 766
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 61.5806 - 5.9418 1.00 2927 194 0.1786 0.2266
REMARK 3 2 5.9418 - 4.7167 1.00 2806 198 0.2503 0.3130
REMARK 3 3 4.7167 - 4.1207 1.00 2819 158 0.2487 0.2919
REMARK 3 4 4.1207 - 3.7440 0.75 2052 152 0.3051 0.3304
REMARK 3 5 3.7440 - 3.4756 0.43 1223 64 0.3321 0.3905
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) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.760
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 : 0.003 6011
REMARK 3 ANGLE : 0.765 8120
REMARK 3 CHIRALITY : 0.051 870
REMARK 3 PLANARITY : 0.006 1054
REMARK 3 DIHEDRAL : 10.870 3599
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5646 100.0089 156.1763
REMARK 3 T TENSOR
REMARK 3 T11: 1.0145 T22: 0.9341
REMARK 3 T33: 1.6005 T12: 0.1177
REMARK 3 T13: -0.0445 T23: -0.6269
REMARK 3 L TENSOR
REMARK 3 L11: 3.2770 L22: 1.5414
REMARK 3 L33: 2.1687 L12: -0.0213
REMARK 3 L13: -0.1591 L23: -1.1221
REMARK 3 S TENSOR
REMARK 3 S11: -0.1177 S12: -0.1913 S13: 0.4521
REMARK 3 S21: 0.1464 S22: 0.3386 S23: -0.8837
REMARK 3 S31: -0.3541 S32: 0.5256 S33: 0.0065
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8578 101.0102 160.9923
REMARK 3 T TENSOR
REMARK 3 T11: 1.1468 T22: 1.0736
REMARK 3 T33: 0.9573 T12: 0.2814
REMARK 3 T13: 0.1196 T23: -0.3502
REMARK 3 L TENSOR
REMARK 3 L11: 1.6712 L22: 1.6625
REMARK 3 L33: 0.9809 L12: 1.0238
REMARK 3 L13: 0.0576 L23: -0.4349
REMARK 3 S TENSOR
REMARK 3 S11: 0.1080 S12: 0.0775 S13: 0.2999
REMARK 3 S21: 0.4451 S22: 0.0222 S23: 0.5924
REMARK 3 S31: 0.1984 S32: -0.4348 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 616 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2739 77.8485 126.9279
REMARK 3 T TENSOR
REMARK 3 T11: 1.4544 T22: 1.0493
REMARK 3 T33: 0.8662 T12: 0.2180
REMARK 3 T13: 0.2693 T23: -0.1854
REMARK 3 L TENSOR
REMARK 3 L11: 1.9026 L22: -0.1484
REMARK 3 L33: 2.0229 L12: 0.2474
REMARK 3 L13: -0.5823 L23: -0.5068
REMARK 3 S TENSOR
REMARK 3 S11: 0.2480 S12: 0.1097 S13: 0.2581
REMARK 3 S21: -0.4616 S22: 0.0112 S23: -0.0762
REMARK 3 S31: 0.4819 S32: -0.0510 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1244 120.7402 182.4673
REMARK 3 T TENSOR
REMARK 3 T11: 2.5309 T22: 1.3930
REMARK 3 T33: 1.9992 T12: 0.2204
REMARK 3 T13: -0.0340 T23: -0.5581
REMARK 3 L TENSOR
REMARK 3 L11: 0.7280 L22: 0.0780
REMARK 3 L33: 0.0927 L12: 0.2482
REMARK 3 L13: -0.2560 L23: -0.0965
REMARK 3 S TENSOR
REMARK 3 S11: 0.3152 S12: -0.6129 S13: 0.1594
REMARK 3 S21: -1.2674 S22: -0.1406 S23: -0.5095
REMARK 3 S31: -0.0080 S32: -0.1301 S33: -0.0335
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7200 118.1624 198.9839
REMARK 3 T TENSOR
REMARK 3 T11: 1.9501 T22: 1.5952
REMARK 3 T33: 1.9650 T12: 0.3793
REMARK 3 T13: -0.2633 T23: -1.5134
REMARK 3 L TENSOR
REMARK 3 L11: 0.7237 L22: 0.0521
REMARK 3 L33: 1.0300 L12: -0.0376
REMARK 3 L13: -0.7277 L23: -0.1147
REMARK 3 S TENSOR
REMARK 3 S11: 0.5180 S12: -0.5942 S13: 0.3277
REMARK 3 S21: -0.2858 S22: -0.3251 S23: 0.1926
REMARK 3 S31: -0.3414 S32: 0.1773 S33: -0.1225
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8273 114.5026 175.0067
REMARK 3 T TENSOR
REMARK 3 T11: 2.7322 T22: 2.1820
REMARK 3 T33: 2.0128 T12: 0.9361
REMARK 3 T13: -0.4497 T23: -0.7966
REMARK 3 L TENSOR
REMARK 3 L11: -0.0044 L22: 0.0006
REMARK 3 L33: -0.0008 L12: -0.0050
REMARK 3 L13: -0.0036 L23: 0.0061
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: 0.0374 S13: 1.6730
REMARK 3 S21: 0.2399 S22: 0.0861 S23: -1.1077
REMARK 3 S31: -0.1138 S32: -0.0873 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4452 108.7204 188.9805
REMARK 3 T TENSOR
REMARK 3 T11: 2.4145 T22: 0.4432
REMARK 3 T33: 2.9790 T12: -0.3248
REMARK 3 T13: -1.1978 T23: -1.8891
REMARK 3 L TENSOR
REMARK 3 L11: 0.5057 L22: 0.1538
REMARK 3 L33: 0.1915 L12: 0.1072
REMARK 3 L13: -0.1086 L23: -0.0443
REMARK 3 S TENSOR
REMARK 3 S11: -0.1064 S12: 0.2325 S13: -0.4373
REMARK 3 S21: 0.1548 S22: -0.2448 S23: -0.5274
REMARK 3 S31: 0.3325 S32: -0.3291 S33: -0.5298
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2854 105.3231 192.5717
REMARK 3 T TENSOR
REMARK 3 T11: 1.9492 T22: 0.6929
REMARK 3 T33: 2.4329 T12: 0.8834
REMARK 3 T13: -0.5735 T23: -0.9654
REMARK 3 L TENSOR
REMARK 3 L11: 1.1730 L22: 4.0568
REMARK 3 L33: 3.1342 L12: -2.0345
REMARK 3 L13: 0.0984 L23: -1.5282
REMARK 3 S TENSOR
REMARK 3 S11: -0.7956 S12: -0.3946 S13: -0.2021
REMARK 3 S21: 0.9748 S22: 0.1329 S23: 0.1482
REMARK 3 S31: 0.0234 S32: 0.1507 S33: -1.1370
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 58 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8548 104.4948 191.4999
REMARK 3 T TENSOR
REMARK 3 T11: 1.7884 T22: 1.2475
REMARK 3 T33: 2.3260 T12: 0.0619
REMARK 3 T13: -0.1836 T23: -0.3811
REMARK 3 L TENSOR
REMARK 3 L11: 0.0796 L22: 0.0250
REMARK 3 L33: 0.2722 L12: 0.0484
REMARK 3 L13: 0.1631 L23: 0.1018
REMARK 3 S TENSOR
REMARK 3 S11: -0.6221 S12: 0.0502 S13: 0.0120
REMARK 3 S21: 0.1227 S22: -1.1218 S23: 2.1831
REMARK 3 S31: -0.0066 S32: 0.6901 S33: -0.0127
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6383 111.9316 190.2450
REMARK 3 T TENSOR
REMARK 3 T11: 2.3535 T22: 1.8424
REMARK 3 T33: 2.2116 T12: -0.6870
REMARK 3 T13: 0.3573 T23: -0.5639
REMARK 3 L TENSOR
REMARK 3 L11: 0.4172 L22: 0.0669
REMARK 3 L33: 1.5972 L12: 0.0945
REMARK 3 L13: -0.5945 L23: 0.0414
REMARK 3 S TENSOR
REMARK 3 S11: 0.4622 S12: 0.9075 S13: 0.3634
REMARK 3 S21: 0.0627 S22: 0.6382 S23: 0.5917
REMARK 3 S31: -0.3267 S32: -0.1456 S33: 0.1356
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5710 113.8062 195.2640
REMARK 3 T TENSOR
REMARK 3 T11: 1.6865 T22: 1.2171
REMARK 3 T33: 2.0525 T12: 0.1528
REMARK 3 T13: -0.1279 T23: -0.6782
REMARK 3 L TENSOR
REMARK 3 L11: 0.0601 L22: 0.1931
REMARK 3 L33: 0.6419 L12: -0.0473
REMARK 3 L13: 0.1758 L23: -0.3112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0912 S12: -0.7937 S13: 0.6786
REMARK 3 S21: -0.9230 S22: 0.0513 S23: -0.7629
REMARK 3 S31: 0.4182 S32: -0.6951 S33: 0.0100
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7276 112.8192 191.3843
REMARK 3 T TENSOR
REMARK 3 T11: 2.0080 T22: 1.6076
REMARK 3 T33: 1.9466 T12: -0.1096
REMARK 3 T13: -1.0318 T23: -1.3366
REMARK 3 L TENSOR
REMARK 3 L11: 0.0568 L22: 0.0228
REMARK 3 L33: 0.5880 L12: -0.0350
REMARK 3 L13: -0.1887 L23: 0.1208
REMARK 3 S TENSOR
REMARK 3 S11: -0.2150 S12: -0.1768 S13: 0.5010
REMARK 3 S21: -0.4003 S22: 0.1733 S23: -0.3873
REMARK 3 S31: 0.1514 S32: 0.0549 S33: 0.0966
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2796 113.4153 191.1514
REMARK 3 T TENSOR
REMARK 3 T11: 1.6622 T22: 1.2791
REMARK 3 T33: 1.8928 T12: 0.4108
REMARK 3 T13: -0.1930 T23: -0.9672
REMARK 3 L TENSOR
REMARK 3 L11: 0.0845 L22: 0.0199
REMARK 3 L33: 2.3417 L12: -0.0156
REMARK 3 L13: -0.4363 L23: -0.2455
REMARK 3 S TENSOR
REMARK 3 S11: -0.1037 S12: -0.9329 S13: 0.2761
REMARK 3 S21: -0.6273 S22: -0.7150 S23: 0.1425
REMARK 3 S31: 0.7020 S32: 1.6101 S33: -0.4307
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 6Q6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1200013395.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-17
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) : 0.976254
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 XDS VERSION JAN 26, 2018,
REMARK 200 AUTOPROC VERSION JAN 26, 2018
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC AUTOPROC (VERSION
REMARK 200 1.0.5), AIMLESS (VERSION 0.7.3),
REMARK 200 CCP4 7.0.065, STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12634
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.473
REMARK 200 RESOLUTION RANGE LOW (A) : 76.586
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 19.50
REMARK 200 R MERGE (I) : 0.18200
REMARK 200 R SYM (I) : 0.18200
REMARK 200 FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.1
REMARK 200 DATA REDUNDANCY IN SHELL : 20.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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 (%): 64.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION CONDITIONS: RESERVOIR
REMARK 280 COMPOSITION (CONDITION A11 OF MORPHEUS SCREEN): 20.0 % (V/V)
REMARK 280 GLYCEROL, 10.0 % (W/V) PEG 4000, 0.03 M MAGNESIUM CHLORIDE, 0.03
REMARK 280 M CALCIUM CHLORIDE, 0.0609 M TRIS-BASE, 0.0391 M BICINE, PH 8.5;
REMARK 280 PROTEIN STOCK SOLUTION: 4.1 MG/ML PROTEIN, 50 MM SODIUM CHLORIDE,
REMARK 280 1 % (V/V) GLYCEROL, 1 MM DTT, 50 MM HEPES, PH 8.0; DROP
REMARK 280 COMPOSITION: 150 NL PROTEIN STOCK SOLUTION PLUS 150 NL RESERVOIR
REMARK 280 SOLUTION; CRYO CONDITIONS: THE CRYSTALS WERE FLASH FROZEN
REMARK 280 DIRECTLY FROM THE EQUILIBRATED CRYSTALLIZATION DROPS., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 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: 1390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33650 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 MET A 617
REMARK 465 ASP A 618
REMARK 465 GLU A 619
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 GLN B 107A
REMARK 465 GLN B 107B
REMARK 465 ARG B 107C
REMARK 465 LEU B 107D
REMARK 465 SER B 107E
REMARK 465 ARG B 107F
REMARK 465 SER B 107G
REMARK 465 ASP B 107H
REMARK 465 VAL B 107I
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 ASP A 98 119.42 -38.35
REMARK 500 SER A 123 -132.93 57.04
REMARK 500 TYR A 140 -56.06 -120.26
REMARK 500 ASN A 144 77.35 -160.79
REMARK 500 SER A 216 35.08 -97.47
REMARK 500 LEU A 247 -37.18 -163.32
REMARK 500 THR A 248 -140.41 -87.05
REMARK 500 ALA A 251 54.29 -165.35
REMARK 500 SER B 7 148.66 -172.89
REMARK 500 ALA B 25 68.46 -102.47
REMARK 500 THR B 29 96.93 52.44
REMARK 500 PRO B 46 108.66 -52.57
REMARK 500 VAL B 53 -70.08 -107.79
REMARK 500 ARG B 58 48.76 -91.37
REMARK 500 VAL B 59 -28.38 -167.41
REMARK 500 ASN B 85 75.04 35.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6I8H RELATED DB: PDB
REMARK 900 EDS1 WITH A DIFFERENT NANOBODY
REMARK 900 RELATED ID: 6I8G RELATED DB: PDB
REMARK 900 EDS1 WITH A DIFFERENT NANOBODY
DBREF 6Q6Z A 1 623 UNP Q9XF23 EDS1L_ARATH 1 623
DBREF 6Q6Z B 1 147 PDB 6Q6Z 6Q6Z 1 147
SEQADV 6Q6Z LEU A 624 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z GLU A 625 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z HIS A 626 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z HIS A 627 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z HIS A 628 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z HIS A 629 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z HIS A 630 UNP Q9XF23 EXPRESSION TAG
SEQADV 6Q6Z 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 142 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 142 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY
SEQRES 3 B 142 PHE THR PHE ASP SER TYR HIS MET GLY TRP PHE ARG ARG
SEQRES 4 B 142 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL SER
SEQRES 5 B 142 ARG VAL THR TRP LEU ILE ASP ILE ALA ASP SER VAL LYS
SEQRES 6 B 142 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR
SEQRES 7 B 142 VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 142 ALA GLN TYR PHE CYS ALA ALA SER GLN GLN ARG LEU SER
SEQRES 9 B 142 ARG SER ASP VAL GLN TYR ASP TYR TRP GLY GLN GLY THR
SEQRES 10 B 142 GLN VAL THR VAL SER SER ALA ALA ALA TYR PRO TYR ASP
SEQRES 11 B 142 VAL PRO ASP TYR GLY 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 ARG A 196 VAL A 200 5 5
HELIX 14 AB5 THR A 203 ASP A 212 1 10
HELIX 15 AB6 SER A 221 GLU A 246 1 26
HELIX 16 AB7 ALA A 251 LEU A 262 1 12
HELIX 17 AB8 ASN A 286 THR A 297 1 12
HELIX 18 AB9 LEU A 308 ASP A 316 1 9
HELIX 19 AC1 SER A 319 SER A 326 1 8
HELIX 20 AC2 MET A 327 LYS A 330 5 4
HELIX 21 AC3 ASP A 336 GLU A 338 5 3
HELIX 22 AC4 ILE A 341 LEU A 348 1 8
HELIX 23 AC5 SER A 351 GLN A 381 1 31
HELIX 24 AC6 GLN A 381 GLU A 394 1 14
HELIX 25 AC7 GLU A 394 HIS A 402 1 9
HELIX 26 AC8 GLY A 405 SER A 413 1 9
HELIX 27 AC9 GLU A 415 LYS A 441 1 27
HELIX 28 AD1 PRO A 445 GLY A 450 5 6
HELIX 29 AD2 ASP A 451 HIS A 476 1 26
HELIX 30 AD3 LEU A 477 THR A 482 1 6
HELIX 31 AD4 PRO A 484 GLY A 489 1 6
HELIX 32 AD5 PRO A 491 LYS A 507 1 17
HELIX 33 AD6 PRO A 508 GLY A 510 5 3
HELIX 34 AD7 ILE A 512 LEU A 524 1 13
HELIX 35 AD8 GLN A 529 LEU A 537 1 9
HELIX 36 AD9 SER A 540 SER A 546 5 7
HELIX 37 AE1 CYS A 547 LYS A 556 1 10
HELIX 38 AE2 PRO A 559 GLY A 581 1 23
HELIX 39 AE3 ASP A 584 PHE A 589 1 6
HELIX 40 AE4 SER A 593 THR A 601 1 9
HELIX 41 AE5 PRO A 603 HIS A 609 1 7
HELIX 42 AE6 LEU A 612 MET A 616 5 5
HELIX 43 AE7 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 VAL A 39
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 VAL A 180 N CYS A 153
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 GLN B 5 SER B 7 0
SHEET 2 AA3 4 LEU B 19 THR B 24 -1 O SER B 22 N SER B 7
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 ASP B 81 O THR B 86
SHEET 1 AA4 6 GLY B 11 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 ALA B 105 -1 N TYR B 102 O THR B 122
SHEET 4 AA4 6 HIS B 38 ARG B 44 -1 N ARG B 44 O GLN B 101
SHEET 5 AA4 6 GLU B 51 SER B 57 -1 O VAL B 56 N MET B 39
SHEET 6 AA4 6 ILE B 65 ILE B 67 -1 O ASP B 66 N ALA B 55
SSBOND 1 CYS B 23 CYS B 104 1555 1555 2.03
CRYST1 142.192 142.192 97.802 90.00 90.00 120.00 P 3 2 1 6
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 0.007033 0.004060 0.000000 0.00000
SCALE2 0.000000 0.008121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010225 0.00000
TER 4984 MET A 616
TER 5882 ALA B 130
MASTER 528 0 0 43 20 0 0 6 5880 2 2 60
END |