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HEADER IMMUNE SYSTEM 13-SEP-22 8B28
TITLE STRUCTURE OF AN INTRON-RETENTION VARIANT OF THE PLANT IMMUNE
TITLE 2 SIGNALLING PROTEIN EDS1 FROM VITIS VINIFERA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VITIS VINIFERA;
SOURCE 3 ORGANISM_COMMON: WINE GRAPE;
SOURCE 4 ORGANISM_TAXID: 29760;
SOURCE 5 GENE: EDS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENHANCED DISEASE SUSCEPTIBILITY 1 PLANT INNATE IMMUNE SYSTEM INTRON
KEYWDS 2 RETENTION DURING ALTERNATIVE SPLICING, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VOSS,K.NIEFIND
REVDAT 1 05-APR-23 8B28 0
JRNL AUTH M.VOSS,L.J.CSEKE,W.GASSMANN,K.NIEFIND
JRNL TITL A SPLICING VARIANT OF EDS1 FROM VITIS VINIFERA FORMS
JRNL TITL 2 HOMODIMERS BUT NO HETERODIMERS WITH PAD4.
JRNL REF PROTEIN SCI. E4624 2023
JRNL REFN ESSN 1469-896X
JRNL PMID 36917448
JRNL DOI 10.1002/PRO.4624
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.VOSS,C.TOELZER,D.D.BHANDARI,J.E.PARKER,K.NIEFIND
REMARK 1 TITL ARABIDOPSIS IMMUNITY REGULATOR EDS1 IN A PAD4/SAG101-UNBOUND
REMARK 1 TITL 2 FORM IS A MONOMER WITH AN INHERENTLY INACTIVE CONFORMATION.
REMARK 1 REF J STRUCT BIOL V. 208 07390 2019
REMARK 1 REFN ESSN 1095-8657
REMARK 1 PMID 31550533
REMARK 1 DOI 10.1016/J.JSB.2019.09.007
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 71.3
REMARK 3 NUMBER OF REFLECTIONS : 29020
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.480
REMARK 3 FREE R VALUE TEST SET COUNT : 1010
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 43.8100 - 3.3600 0.94 5359 194 0.1470 0.1805
REMARK 3 2 3.3600 - 2.6600 0.96 5418 192 0.1647 0.1824
REMARK 3 3 2.6600 - 2.3300 0.97 5398 193 0.1837 0.2147
REMARK 3 4 2.3300 - 2.1100 0.98 5511 200 0.2062 0.2598
REMARK 3 5 2.1100 - 1.9600 0.81 4508 164 0.2385 0.2633
REMARK 3 6 1.9600 - 1.8500 0.27 1477 55 0.2713 0.2833
REMARK 3 7 1.8500 - 1.7500 0.06 339 12 0.3290 0.2187
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.182
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.538
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.38
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 2758
REMARK 3 ANGLE : 0.567 3728
REMARK 3 CHIRALITY : 0.043 398
REMARK 3 PLANARITY : 0.005 492
REMARK 3 DIHEDRAL : 12.982 1012
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0788 13.3056 26.4293
REMARK 3 T TENSOR
REMARK 3 T11: 0.1944 T22: 0.2393
REMARK 3 T33: 0.1069 T12: -0.0226
REMARK 3 T13: -0.0031 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 4.7433 L22: 3.8063
REMARK 3 L33: 4.6270 L12: 0.2619
REMARK 3 L13: 0.2523 L23: -0.0991
REMARK 3 S TENSOR
REMARK 3 S11: 0.1150 S12: 0.7726 S13: -0.6473
REMARK 3 S21: -0.6356 S22: -0.3181 S23: 0.4091
REMARK 3 S31: 0.4741 S32: -0.4622 S33: -0.0512
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1915 20.8094 45.2895
REMARK 3 T TENSOR
REMARK 3 T11: 0.0931 T22: 0.0854
REMARK 3 T33: 0.0971 T12: 0.0290
REMARK 3 T13: 0.0342 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 2.5377 L22: 1.8588
REMARK 3 L33: 1.9079 L12: 0.1015
REMARK 3 L13: 0.8146 L23: -0.2427
REMARK 3 S TENSOR
REMARK 3 S11: -0.1052 S12: -0.1195 S13: 0.2189
REMARK 3 S21: 0.0478 S22: -0.0082 S23: 0.0770
REMARK 3 S31: -0.1229 S32: -0.0849 S33: 0.0646
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9158 12.4839 54.6053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1497 T22: 0.1806
REMARK 3 T33: 0.1084 T12: -0.0013
REMARK 3 T13: 0.0011 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 1.4455 L22: 2.9144
REMARK 3 L33: 2.6163 L12: 0.4445
REMARK 3 L13: -0.3196 L23: 0.1935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0937 S12: -0.6742 S13: -0.2071
REMARK 3 S21: 0.5020 S22: -0.0308 S23: -0.0448
REMARK 3 S31: 0.1606 S32: -0.2031 S33: -0.0360
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0298 14.4805 42.0066
REMARK 3 T TENSOR
REMARK 3 T11: 0.0511 T22: 0.0619
REMARK 3 T33: 0.0579 T12: 0.0105
REMARK 3 T13: 0.0055 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 2.4370 L22: 2.0942
REMARK 3 L33: 1.7957 L12: -0.0237
REMARK 3 L13: -0.2218 L23: -0.5785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0460 S12: -0.0515 S13: -0.0426
REMARK 3 S21: -0.1135 S22: 0.0541 S23: 0.0017
REMARK 3 S31: 0.0741 S32: -0.1059 S33: 0.0221
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5549 20.7995 43.4805
REMARK 3 T TENSOR
REMARK 3 T11: 0.1193 T22: 0.1698
REMARK 3 T33: 0.2034 T12: -0.0275
REMARK 3 T13: -0.0038 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 2.0521 L22: 1.3314
REMARK 3 L33: 2.1994 L12: -0.7547
REMARK 3 L13: 0.1177 L23: -0.3162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0671 S12: -0.1810 S13: 0.3534
REMARK 3 S21: 0.1334 S22: -0.0156 S23: -0.2100
REMARK 3 S31: -0.2686 S32: 0.1406 S33: 0.1048
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 312 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5058 31.8941 32.8685
REMARK 3 T TENSOR
REMARK 3 T11: 0.3174 T22: 0.2905
REMARK 3 T33: 0.6313 T12: -0.1355
REMARK 3 T13: 0.1333 T23: 0.1234
REMARK 3 L TENSOR
REMARK 3 L11: 1.6983 L22: 0.0650
REMARK 3 L33: 2.2849 L12: 0.1875
REMARK 3 L13: 0.0518 L23: 0.3018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: 0.2361 S13: 0.8689
REMARK 3 S21: -0.1127 S22: -0.1237 S23: -0.9477
REMARK 3 S31: -0.8211 S32: 0.4913 S33: -0.2641
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0078 16.2338 24.5158
REMARK 3 T TENSOR
REMARK 3 T11: 0.2361 T22: 0.2608
REMARK 3 T33: 0.1378 T12: 0.0066
REMARK 3 T13: 0.0501 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 4.3529 L22: 1.0777
REMARK 3 L33: 5.6344 L12: 0.5091
REMARK 3 L13: -1.8506 L23: 1.9897
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: 0.5332 S13: 0.0300
REMARK 3 S21: -0.3348 S22: 0.0070 S23: -0.1063
REMARK 3 S31: 0.1884 S32: 0.0091 S33: -0.0604
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 8B28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292125582.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.915079
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JAN 10, 2022 (BUILT
REMARK 200 20220820)
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.0.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 43.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 71.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66800
REMARK 200 R SYM FOR SHELL (I) : 0.66800
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.20.1_4487
REMARK 200 STARTING MODEL: 6I8G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 4.5 MG/ML IN 300 MM
REMARK 280 SODIUM IODIDE, 1 % GLYCEROL, 1 MM DTT, 50 MM HEPES BUFFER, PH
REMARK 280 8.0). RESERVOIR SOLUTION: 12 % PEG3350, 300 MILLIMOLAR CSCL, 100
REMARK 280 MILLIMOLAR BIS-TRIS PUFFER, PH 8.5. CRYSTALLIZATION DROP BEFORE
REMARK 280 EQUILIBRATION: 1.5 MIKROLITER PROTEIN SOLUTION PLUS AND 1.5
REMARK 280 MIKROLITER RESERVOIR SOLUTION., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 72.27450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.53850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.27450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.53850
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: 4670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 120.28547
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 87.61019
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 643 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 675 LIES ON A SPECIAL POSITION.
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 -25
REMARK 465 LYS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 PRO A -17
REMARK 465 MET A -16
REMARK 465 SER A -15
REMARK 465 ASP A -14
REMARK 465 TYR A -13
REMARK 465 ASP A -12
REMARK 465 ILE A -11
REMARK 465 PRO A -10
REMARK 465 THR A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 LEU A 332
REMARK 465 GLU A 333
REMARK 465 ASP A 334
REMARK 465 LEU A 335
REMARK 465 PRO A 336
REMARK 465 LEU A 337
REMARK 465 SER A 338
REMARK 465 SER A 339
REMARK 465 ASN A 340
REMARK 465 GLY A 341
REMARK 465 GLY A 342
REMARK 465 PRO A 343
REMARK 465 ALA A 344
REMARK 465 THR A 345
REMARK 465 VAL A 346
REMARK 465 ASN A 347
REMARK 465 ILE A 348
REMARK 465 ALA A 349
REMARK 465 LEU A 350
REMARK 465 ASN A 351
REMARK 465 ASP A 352
REMARK 465 LEU A 353
REMARK 465 GLY A 354
REMARK 465 LEU A 355
REMARK 465 VAL A 356
REMARK 465 SER A 357
REMARK 465 PHE A 358
REMARK 465 LEU A 359
REMARK 465 SER A 360
REMARK 465 CYS A 361
REMARK 465 SER A 362
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 SER A 29 77.71 -110.48
REMARK 500 SER A 123 -138.00 57.84
REMARK 500 GLN A 296 -131.28 50.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 766 DISTANCE = 6.95 ANGSTROMS
DBREF 8B28 A 1 355 UNP G3F1Q6 G3F1Q6_VITVI 1 355
SEQADV 8B28 MET A -25 UNP G3F1Q6 INITIATING METHIONINE
SEQADV 8B28 LYS A -24 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -23 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -22 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -21 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -20 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -19 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 HIS A -18 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 PRO A -17 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 MET A -16 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 SER A -15 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 ASP A -14 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 TYR A -13 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 ASP A -12 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 ILE A -11 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 PRO A -10 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 THR A -9 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 THR A -8 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 GLU A -7 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 ASN A -6 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 LEU A -5 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 TYR A -4 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 PHE A -3 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 GLN A -2 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 GLY A -1 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 ALA A 0 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 VAL A 356 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 SER A 357 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 PHE A 358 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 LEU A 359 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 SER A 360 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 CYS A 361 UNP G3F1Q6 EXPRESSION TAG
SEQADV 8B28 SER A 362 UNP G3F1Q6 EXPRESSION TAG
SEQRES 1 A 388 MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR
SEQRES 2 A 388 ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA
SEQRES 3 A 388 MET GLY GLU THR LEU GLY ASN ARG ILE ARG LEU SER GLU
SEQRES 4 A 388 GLU ILE VAL ASN ARG ALA ALA SER GLN ALA MET ARG ALA
SEQRES 5 A 388 HIS ASN SER ALA GLY ARG PRO PHE LEU LEU ASP LYS THR
SEQRES 6 A 388 ARG GLY PHE ALA ILE PHE ALA PHE ALA GLY SER TRP LEU
SEQRES 7 A 388 SER ASP ASP TRP PHE THR HIS PRO PRO PHE GLY GLU THR
SEQRES 8 A 388 LYS MET ASP ALA SER THR PHE PRO SER LEU ARG SER VAL
SEQRES 9 A 388 GLY ASN ASP GLU VAL ALA VAL VAL ASN ALA SER PHE LEU
SEQRES 10 A 388 ARG ARG PHE LYS ALA ILE LEU ASP GLN LEU PRO LEU GLU
SEQRES 11 A 388 ARG GLU VAL GLN LYS VAL ILE ALA ASP ARG ARG GLN VAL
SEQRES 12 A 388 VAL PHE THR GLY HIS SER TRP GLY GLY ALA MET ALA ILE
SEQRES 13 A 388 LEU ALA THR LEU TYR PHE LEU GLU LYS ALA GLY PRO ASN
SEQRES 14 A 388 GLN ASN PRO PRO ARG CYS ILE THR PHE GLY SER PRO LEU
SEQRES 15 A 388 VAL GLY ASP ARG ILE PHE GLY HIS ALA VAL ARG ARG GLU
SEQRES 16 A 388 LYS TRP SER ASP HIS PHE ILE HIS PHE VAL MET ARG PHE
SEQRES 17 A 388 ASP VAL ILE PRO ARG ILE MET LEU GLY PRO ALA SER THR
SEQRES 18 A 388 GLU HIS GLN GLN ILE LEU ASN PHE PHE ASN PRO ARG SER
SEQRES 19 A 388 GLN PHE TYR ARG GLU PRO LEU ASP PRO PRO LEU GLY PHE
SEQRES 20 A 388 TYR LEU ASN VAL MET ARG SER ALA SER SER VAL ALA ILE
SEQRES 21 A 388 HIS ASP ALA CYS ILE LEU MET GLY CYS THR ASN PRO LEU
SEQRES 22 A 388 LEU GLU THR LEU ARG ASN PHE THR GLU LEU SER PRO TYR
SEQRES 23 A 388 ARG PRO PHE GLY THR TYR ILE PHE CYS THR GLY ASN GLY
SEQRES 24 A 388 LYS LEU VAL VAL LEU LYS ASN PRO ASP ALA VAL LEU GLN
SEQRES 25 A 388 ILE LEU PHE TYR CYS ALA GLN LEU SER GLN GLU GLU ALA
SEQRES 26 A 388 ALA GLU ILE ALA GLN ARG SER LEU HIS GLU HIS LEU ALA
SEQRES 27 A 388 TYR GLU ASN GLU LEU GLN GLU SER LEU GLY MET GLN ASN
SEQRES 28 A 388 VAL VAL TYR LEU ASP SER LEU GLU ASP LEU PRO LEU SER
SEQRES 29 A 388 SER ASN GLY GLY PRO ALA THR VAL ASN ILE ALA LEU ASN
SEQRES 30 A 388 ASP LEU GLY LEU VAL SER PHE LEU SER CYS SER
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 8(C2 H6 O2)
FORMUL 10 HOH *266(H2 O)
HELIX 1 AA1 THR A 4 ARG A 10 1 7
HELIX 2 AA2 SER A 12 HIS A 27 1 16
HELIX 3 AA3 LEU A 52 TRP A 56 5 5
HELIX 4 AA4 PHE A 72 ARG A 76 5 5
HELIX 5 AA5 ALA A 88 LEU A 101 1 14
HELIX 6 AA6 PRO A 102 ASP A 113 1 12
HELIX 7 AA7 SER A 123 ALA A 140 1 18
HELIX 8 AA8 ASP A 159 GLU A 169 1 11
HELIX 9 AA9 TRP A 171 ASP A 173 5 3
HELIX 10 AB1 VAL A 184 MET A 189 1 6
HELIX 11 AB2 GLU A 196 ASN A 205 1 10
HELIX 12 AB3 PRO A 206 TYR A 211 5 6
HELIX 13 AB4 GLY A 220 MET A 241 1 22
HELIX 14 AB5 THR A 244 ARG A 252 1 9
HELIX 15 AB6 ASN A 280 CYS A 291 1 12
HELIX 16 AB7 GLU A 301 LEU A 311 1 11
HELIX 17 AB8 ALA A 312 MET A 323 1 12
SHEET 1 AA1 8 PHE A 34 THR A 39 0
SHEET 2 AA1 8 PHE A 42 PHE A 47 -1 O ILE A 44 N ASP A 37
SHEET 3 AA1 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 45
SHEET 4 AA1 8 ARG A 148 PHE A 152 1 O ARG A 148 N PHE A 119
SHEET 5 AA1 8 PHE A 175 MET A 180 1 O PHE A 178 N THR A 151
SHEET 6 AA1 8 THR A 265 GLY A 271 1 O THR A 265 N HIS A 177
SHEET 7 AA1 8 LYS A 274 LEU A 278 -1 O VAL A 276 N PHE A 268
SHEET 8 AA1 8 ASN A 325 TYR A 328 1 O VAL A 327 N VAL A 277
SHEET 1 AA2 2 GLU A 64 LYS A 66 0
SHEET 2 AA2 2 VAL A 85 ASN A 87 -1 O VAL A 86 N THR A 65
CISPEP 1 PRO A 60 PRO A 61 0 -0.01
CRYST1 144.549 65.077 45.454 90.00 105.48 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 0.006918 0.000000 0.001916 0.00000
SCALE2 0.000000 0.015366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022828 0.00000
TER 2663 SER A 331
MASTER 427 0 8 17 10 0 0 6 2933 1 32 30
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