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HEADER PLANT PROTEIN 31-MAR-22 7XEY
TITLE EDS1-PAD4 COMPLEXED WITH PRIB-ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN EDS1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LIPASE-LIKE PAD4;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: PROTEIN ENHANCED DISEASE SUSCEPTIBILITY 9,PROTEIN
COMPND 10 PHYTOALEXIN DEFICIENT 4,ATPAD4;
COMPND 11 EC: 2.3.1.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS;
SOURCE 3 ORGANISM_TAXID: 3701;
SOURCE 4 GENE: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ARABIDOPSIS;
SOURCE 9 ORGANISM_TAXID: 3701;
SOURCE 10 GENE: PAD4, EDS9, AT3G52430, F22O6.190;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS EDS1, PAD4, PRIB-ADP, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HUANG,A.JIA,Y.XIAO
REVDAT 1 13-JUL-22 7XEY 0
JRNL AUTH S.HUANG,A.JIA,W.SONG,G.HESSLER,Y.MENG,Y.SUN,L.XU,H.LAESSLE,
JRNL AUTH 2 J.JIRSCHITZKA,S.MA,Y.XIAO,D.YU,J.HOU,R.LIU,H.SUN,X.LIU,
JRNL AUTH 3 Z.HAN,J.CHANG,J.PARKER,J.CHAI
JRNL TITL IDENTIFICATION AND RECEPTOR MECHANISM OF TIR-CATALYZED SMALL
JRNL TITL 2 MOLECULES IN PLANT IMMUNITY
JRNL REF SCIENCE 2022
JRNL REFN ESSN 1095-9203
JRNL DOI 10.1126/SCIENCE.ABQ3297
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 57761
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 46.0700 - 5.5100 0.97 4039 147 0.1496 0.1687
REMARK 3 2 5.5100 - 4.3800 0.97 3974 146 0.1448 0.1817
REMARK 3 3 4.3800 - 3.8200 1.00 4077 153 0.1534 0.2142
REMARK 3 4 3.8200 - 3.4700 0.97 3948 124 0.1716 0.2035
REMARK 3 5 3.4700 - 3.2200 0.98 4003 153 0.1952 0.2610
REMARK 3 6 3.2200 - 3.0300 0.99 3993 145 0.2081 0.2642
REMARK 3 7 3.0300 - 2.8800 1.00 4041 148 0.2112 0.2690
REMARK 3 8 2.8800 - 2.7600 0.98 3974 131 0.2084 0.2681
REMARK 3 9 2.7600 - 2.6500 0.98 3949 142 0.2173 0.2659
REMARK 3 10 2.6500 - 2.5600 0.99 3992 146 0.2229 0.2932
REMARK 3 11 2.5600 - 2.4800 0.99 3992 140 0.2215 0.2427
REMARK 3 12 2.4800 - 2.4100 0.99 4004 151 0.2276 0.3050
REMARK 3 13 2.4100 - 2.3400 0.99 4016 138 0.2488 0.3320
REMARK 3 14 2.3400 - 2.2900 0.93 3767 128 0.2532 0.3152
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.84
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 7XEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1300028689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57868
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.69400
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: PHENIX
REMARK 200 STARTING MODEL: 4NFU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M CITRIC ACID, 0.06 M BIS-TRIS
REMARK 280 PROPANE PH 6.4, 20% W/V POLYETHYLENE GLYCOL 3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 45.93150
REMARK 290 SMTRY3 2 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: 7970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 VAL A 218
REMARK 465 GLN A 219
REMARK 465 GLU A 220
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 MET B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 LYS B 407
REMARK 465 THR B 408
REMARK 465 TYR B 525
REMARK 465 GLU B 526
REMARK 465 ASN B 527
REMARK 465 GLU B 528
REMARK 465 ILE B 529
REMARK 465 GLU B 530
REMARK 465 MET B 531
REMARK 465 VAL B 532
REMARK 465 VAL B 533
REMARK 465 ASP B 534
REMARK 465 GLU B 535
REMARK 465 SER B 536
REMARK 465 ASP B 537
REMARK 465 ALA B 538
REMARK 465 MET B 539
REMARK 465 GLU B 540
REMARK 465 THR B 541
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY B 251 O HOH B 701 1.80
REMARK 500 O HOH A 1088 O HOH B 924 1.87
REMARK 500 O HOH B 754 O HOH B 938 1.91
REMARK 500 O HOH B 820 O HOH B 931 1.92
REMARK 500 OE1 GLN A 356 O HOH A 801 1.93
REMARK 500 O HOH B 746 O HOH B 851 1.93
REMARK 500 O HOH A 1043 O HOH B 948 1.96
REMARK 500 O HOH A 1029 O HOH A 1118 1.97
REMARK 500 O GLU A 543 O HOH A 802 1.97
REMARK 500 O SER B 136 O HOH B 702 1.97
REMARK 500 OE2 GLU A 380 O HOH A 803 2.00
REMARK 500 O HOH B 749 O HOH B 899 2.00
REMARK 500 O HOH A 1074 O HOH A 1091 2.01
REMARK 500 O HOH A 994 O HOH A 1066 2.02
REMARK 500 O HOH A 970 O HOH A 1112 2.03
REMARK 500 NH1 ARG B 231 O HOH B 703 2.06
REMARK 500 NH1 ARG A 16 O HOH A 804 2.06
REMARK 500 O SER A 46 O HOH A 805 2.08
REMARK 500 O HOH B 902 O HOH B 955 2.08
REMARK 500 O HOH B 764 O HOH B 951 2.09
REMARK 500 OG SER A 46 OD2 ASP A 51 2.09
REMARK 500 O HOH B 959 O HOH B 980 2.10
REMARK 500 O HOH B 865 O HOH B 922 2.10
REMARK 500 OD1 ASP B 24 O HOH B 704 2.10
REMARK 500 OD1 ASP A 54 O HOH A 806 2.11
REMARK 500 O LEU A 66 O HOH A 807 2.11
REMARK 500 O HOH A 1012 O HOH B 893 2.13
REMARK 500 OD2 ASP A 302 O HOH A 808 2.13
REMARK 500 O HOH B 769 O HOH B 960 2.14
REMARK 500 NH2 ARG B 163 O HOH B 705 2.15
REMARK 500 OD2 ASP B 24 O HOH B 706 2.15
REMARK 500 OG1 THR B 445 O HOH B 707 2.17
REMARK 500 OD1 ASP A 347 O HOH A 809 2.18
REMARK 500 OD1 ASP A 408 O HOH A 810 2.19
REMARK 500 O HOH A 908 O HOH A 941 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1019 O HOH B 727 1455 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 -75.65 71.97
REMARK 500 ALA A 35 103.76 -160.41
REMARK 500 ASP A 98 131.74 -39.96
REMARK 500 SER A 123 -133.70 58.49
REMARK 500 VAL A 161 -49.52 -130.25
REMARK 500 ARG A 185 -63.01 -26.49
REMARK 500 LYS A 215 83.06 64.72
REMARK 500 GLU A 394 -51.47 -129.40
REMARK 500 LYS A 487 -70.30 -86.80
REMARK 500 SER B 118 -138.95 60.22
REMARK 500 SER B 139 40.84 -92.78
REMARK 500 ALA B 222 -76.45 -103.15
REMARK 500 PRO B 255 32.97 -74.87
REMARK 500 ASP B 256 -63.31 62.50
REMARK 500 ASN B 274 1.12 -68.22
REMARK 500 ARG B 291 105.88 50.31
REMARK 500 LEU B 413 3.65 -62.67
REMARK 500 GLU B 414 65.10 -108.73
REMARK 500 LYS B 432 134.98 -1.45
REMARK 500 VAL B 433 43.86 -154.21
REMARK 500 PRO B 434 -127.37 -87.66
REMARK 500 GLU B 468 -92.16 69.50
REMARK 500 SER B 469 -78.67 51.29
REMARK 500 ILE B 482 -59.17 -136.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 78 ASP B 79 -147.72
REMARK 500 GLU B 80 PRO B 81 121.74
REMARK 500 THR B 221 ALA B 222 -148.19
REMARK 500 VAL B 431 LYS B 432 143.01
REMARK 500 VAL B 433 PRO B 434 140.62
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 A1130 DISTANCE = 5.94 ANGSTROMS
DBREF 7XEY A 1 623 UNP Q9SU72 EDS1C_ARATH 1 623
DBREF 7XEY B 1 541 UNP Q9S745 PAD4_ARATH 1 541
SEQRES 1 A 623 MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 2 A 623 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 3 A 623 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 4 A 623 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 5 A 623 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 6 A 623 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 7 A 623 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 8 A 623 ASN LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN
SEQRES 9 A 623 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 10 A 623 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 11 A 623 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 12 A 623 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 13 A 623 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 14 A 623 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 15 A 623 VAL SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA
SEQRES 16 A 623 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 17 A 623 ALA GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER
SEQRES 18 A 623 GLU GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG
SEQRES 19 A 623 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 20 A 623 THR GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER
SEQRES 21 A 623 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 22 A 623 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 23 A 623 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN
SEQRES 24 A 623 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 25 A 623 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 26 A 623 SER MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 27 A 623 ASN SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER
SEQRES 28 A 623 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 29 A 623 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 30 A 623 VAL ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 31 A 623 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 32 A 623 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 33 A 623 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 34 A 623 GLY VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS
SEQRES 35 A 623 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 36 A 623 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 37 A 623 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 38 A 623 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 39 A 623 ILE TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS
SEQRES 40 A 623 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 41 A 623 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 42 A 623 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 43 A 623 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 44 A 623 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 45 A 623 MET LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP
SEQRES 46 A 623 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 47 A 623 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 48 A 623 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR
SEQRES 1 B 541 MET ASP ASP CYS ARG PHE GLU THR SER GLU LEU GLN ALA
SEQRES 2 B 541 SER VAL MET ILE SER THR PRO LEU PHE THR ASP SER TRP
SEQRES 3 B 541 SER SER CYS ASN THR ALA ASN CYS ASN GLY SER ILE LYS
SEQRES 4 B 541 ILE HIS ASP ILE ALA GLY ILE THR TYR VAL ALA ILE PRO
SEQRES 5 B 541 ALA VAL SER MET ILE GLN LEU GLY ASN LEU VAL GLY LEU
SEQRES 6 B 541 PRO VAL THR GLY ASP VAL LEU PHE PRO GLY LEU SER SER
SEQRES 7 B 541 ASP GLU PRO LEU PRO MET VAL ASP ALA ALA ILE LEU LYS
SEQRES 8 B 541 LEU PHE LEU GLN LEU LYS ILE LYS GLU GLY LEU GLU LEU
SEQRES 9 B 541 GLU LEU LEU GLY LYS LYS LEU VAL VAL ILE THR GLY HIS
SEQRES 10 B 541 SER THR GLY GLY ALA LEU ALA ALA PHE THR ALA LEU TRP
SEQRES 11 B 541 LEU LEU SER GLN SER SER PRO PRO SER PHE ARG VAL PHE
SEQRES 12 B 541 CYS ILE THR PHE GLY SER PRO LEU LEU GLY ASN GLN SER
SEQRES 13 B 541 LEU SER THR SER ILE SER ARG SER ARG LEU ALA HIS ASN
SEQRES 14 B 541 PHE CYS HIS VAL VAL SER ILE HIS ASP LEU VAL PRO ARG
SEQRES 15 B 541 SER SER ASN GLU GLN PHE TRP PRO PHE GLY THR TYR LEU
SEQRES 16 B 541 PHE CYS SER ASP LYS GLY GLY VAL CYS LEU ASP ASN ALA
SEQRES 17 B 541 GLY SER VAL ARG LEU MET PHE ASN ILE LEU ASN THR THR
SEQRES 18 B 541 ALA THR GLN ASN THR GLU GLU HIS GLN ARG TYR GLY HIS
SEQRES 19 B 541 TYR VAL PHE THR LEU SER HIS MET PHE LEU LYS SER ARG
SEQRES 20 B 541 SER PHE LEU GLY GLY SER ILE PRO ASP ASN SER TYR GLN
SEQRES 21 B 541 ALA GLY VAL ALA LEU ALA VAL GLU ALA LEU GLY PHE SER
SEQRES 22 B 541 ASN ASP ASP THR SER GLY VAL LEU VAL LYS GLU CYS ILE
SEQRES 23 B 541 GLU THR ALA THR ARG ILE VAL ARG ALA PRO ILE LEU ARG
SEQRES 24 B 541 SER ALA GLU LEU ALA ASN GLU LEU ALA SER VAL LEU PRO
SEQRES 25 B 541 ALA ARG LEU GLU ILE GLN TRP TYR LYS ASP ARG CYS ASP
SEQRES 26 B 541 ALA SER GLU GLU GLN LEU GLY TYR TYR ASP PHE PHE LYS
SEQRES 27 B 541 ARG TYR SER LEU LYS ARG ASP PHE LYS VAL ASN MET SER
SEQRES 28 B 541 ARG ILE ARG LEU ALA LYS PHE TRP ASP THR VAL ILE LYS
SEQRES 29 B 541 MET VAL GLU THR ASN GLU LEU PRO PHE ASP PHE HIS LEU
SEQRES 30 B 541 GLY LYS LYS TRP ILE TYR ALA SER GLN PHE TYR GLN LEU
SEQRES 31 B 541 LEU ALA GLU PRO LEU ASP ILE ALA ASN PHE TYR LYS ASN
SEQRES 32 B 541 ARG ASP ILE LYS THR GLY GLY HIS TYR LEU GLU GLY ASN
SEQRES 33 B 541 ARG PRO LYS ARG TYR GLU VAL ILE ASP LYS TRP GLN LYS
SEQRES 34 B 541 GLY VAL LYS VAL PRO GLU GLU CYS VAL ARG SER ARG TYR
SEQRES 35 B 541 ALA SER THR THR GLN ASP THR CYS PHE TRP ALA LYS LEU
SEQRES 36 B 541 GLU GLN ALA LYS GLU TRP LEU ASP GLU ALA ARG LYS GLU
SEQRES 37 B 541 SER SER ASP PRO GLN ARG ARG SER LEU LEU ARG GLU LYS
SEQRES 38 B 541 ILE VAL PRO PHE GLU SER TYR ALA ASN THR LEU VAL THR
SEQRES 39 B 541 LYS LYS GLU VAL SER LEU ASP VAL LYS ALA LYS ASN SER
SEQRES 40 B 541 SER TYR SER VAL TRP GLU ALA ASN LEU LYS GLU PHE LYS
SEQRES 41 B 541 CYS LYS MET GLY TYR GLU ASN GLU ILE GLU MET VAL VAL
SEQRES 42 B 541 ASP GLU SER ASP ALA MET GLU THR
HET ADP A 701 27
HET RP5 A 702 13
HET TRS B 601 8
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM RP5 5-O-PHOSPHONO-BETA-D-RIBOFURANOSE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN RP5 [(2R,3S,4S,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-
HETSYN 2 RP5 YL]METHYL DIHYDROGEN PHOSPHATE; 5-O-PHOSPHONO-BETA-D-
HETSYN 3 RP5 RIBOSE; 5-O-PHOSPHONO-D-RIBOSE; 5-O-PHOSPHONO-RIBOSE
HETSYN TRS TRIS BUFFER
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 RP5 C5 H11 O8 P
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 6 HOH *610(H2 O)
HELIX 1 AA1 ALA A 2 GLY A 8 1 7
HELIX 2 AA2 ASN A 10 THR A 27 1 18
HELIX 3 AA3 SER A 48 PHE A 52 5 5
HELIX 4 AA4 GLU A 87 ASP A 98 1 12
HELIX 5 AA5 SER A 102 SER A 113 1 12
HELIX 6 AA6 SER A 123 TYR A 140 1 18
HELIX 7 AA7 PHE A 141 ASN A 144 5 4
HELIX 8 AA8 ASN A 146 GLU A 150 5 5
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 MET A 193 1 6
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 GLU A 222 THR A 248 1 27
HELIX 15 AB6 ALA A 251 SER A 260 1 10
HELIX 16 AB7 ASN A 286 THR A 297 1 12
HELIX 17 AB8 ASP A 302 ASP A 316 1 15
HELIX 18 AB9 SER A 319 MET A 327 1 9
HELIX 19 AC1 GLY A 328 LYS A 330 5 3
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 GLY A 405 SER A 413 1 9
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 LYS A 478 GLY A 483 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 PRO A 559 ASP A 580 1 22
HELIX 38 AE2 ASP A 584 PHE A 589 1 6
HELIX 39 AE3 SER A 593 ILE A 600 1 8
HELIX 40 AE4 PRO A 603 SER A 610 1 8
HELIX 41 AE5 LEU A 612 MET A 616 5 5
HELIX 42 AE6 THR B 8 THR B 19 1 12
HELIX 43 AE7 THR B 19 GLY B 36 1 18
HELIX 44 AE8 ALA B 87 LEU B 96 1 10
HELIX 45 AE9 LYS B 97 LEU B 107 1 11
HELIX 46 AF1 SER B 118 SER B 133 1 16
HELIX 47 AF2 GLN B 155 SER B 164 1 10
HELIX 48 AF3 LEU B 166 HIS B 168 5 3
HELIX 49 AF4 ASP B 178 SER B 183 1 6
HELIX 50 AF5 ASN B 207 THR B 220 1 14
HELIX 51 AF6 ASN B 225 GLN B 230 5 6
HELIX 52 AF7 ARG B 231 MET B 242 1 12
HELIX 53 AF8 PHE B 243 LYS B 245 5 3
HELIX 54 AF9 ASN B 257 GLY B 271 1 15
HELIX 55 AG1 ASP B 276 THR B 288 1 13
HELIX 56 AG2 ALA B 295 SER B 327 1 33
HELIX 57 AG3 LEU B 331 TYR B 340 1 10
HELIX 58 AG4 LEU B 342 THR B 368 1 27
HELIX 59 AG5 ASP B 374 LEU B 377 5 4
HELIX 60 AG6 GLY B 378 ARG B 404 1 27
HELIX 61 AG7 PRO B 418 GLN B 428 1 11
HELIX 62 AG8 LYS B 429 VAL B 431 5 3
HELIX 63 AG9 CYS B 450 GLU B 468 1 19
HELIX 64 AH1 PRO B 472 ILE B 482 1 11
HELIX 65 AH2 ILE B 482 LYS B 495 1 14
HELIX 66 AH3 SER B 499 ALA B 504 5 6
HELIX 67 AH4 SER B 507 MET B 523 1 17
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 SER 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 VAL A 183
SHEET 7 AA1 8 ARG A 280 VAL A 284 -1 O VAL A 282 N PHE A 275
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 7 LYS B 39 ILE B 43 0
SHEET 2 AA3 7 ILE B 46 ILE B 51 -1 O TYR B 48 N HIS B 41
SHEET 3 AA3 7 LEU B 111 HIS B 117 1 O VAL B 113 N THR B 47
SHEET 4 AA3 7 ARG B 141 PHE B 147 1 O ARG B 141 N VAL B 112
SHEET 5 AA3 7 PHE B 170 SER B 175 1 O VAL B 173 N THR B 146
SHEET 6 AA3 7 THR B 193 SER B 198 1 O LEU B 195 N VAL B 174
SHEET 7 AA3 7 GLY B 201 LEU B 205 -1 O LEU B 205 N TYR B 194
SHEET 1 AA4 2 LEU B 62 GLY B 64 0
SHEET 2 AA4 2 MET B 84 ASP B 86 -1 O VAL B 85 N VAL B 63
SHEET 1 AA5 2 GLY B 153 ASN B 154 0
SHEET 2 AA5 2 PHE B 188 TRP B 189 -1 O TRP B 189 N GLY B 153
LINK O2' ADP A 701 C1 RP5 A 702 1555 1555 1.43
CRYST1 82.357 91.863 94.271 90.00 111.79 90.00 P 1 21 1 2
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 0.012142 0.000000 0.004853 0.00000
SCALE2 0.000000 0.010886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011424 0.00000
TER 4984 ASP A 618
TER 9099 GLY B 524
MASTER 369 0 3 67 21 0 0 6 9755 2 48 90
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