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HEADER PLANT PROTEIN 18-APR-22 7XJP
TITLE CRYO-EM STRUCTURE OF EDS1 AND SAG101 WITH ATP-APDR
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: SENESCENCE-ASSOCIATED CARBOXYLESTERASE 101;
COMPND 8 CHAIN: B;
COMPND 9 EC: 3.1.1.1;
COMPND 10 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: SAG101, AT5G14930, F2G14.50;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS NLR, PLANT PROTEIN, PLANT IMMUNE SIGNALING
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.J.HUANG,A.L.JIA,Z.F.HAN,J.J.CHAI
REVDAT 1 20-JUL-22 7XJP 0
JRNL AUTH A.L.JIA,S.J.HUANG,W.SONG,J.WANG,Y.MENG,Y.SUN,L.XU,H.LAESSLE,
JRNL AUTH 2 J.JIRSCHITZKA,J.HOU,T.ZHANG,W.YU,G.HESSLER,E.LI,S.MA,D.YU,
JRNL AUTH 3 J.GEBAUER,U.BAUMANN,X.LIU,Z.HAN,J.CHANG,J.E.PARKER,J.CHAI
JRNL TITL TIR-CATALYZED ADP-RIBOSYLATION REACTIONS PRODUCE SIGNALING
JRNL TITL 2 MOLECULES FOR PLANT IMMUNITY
JRNL REF SCIENCE 2022
JRNL REFN ESSN 1095-9203
JRNL DOI 10.1126/SCIENCE.ABQ8180
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.710
REMARK 3 NUMBER OF PARTICLES : 652337
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 7XJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1300028976.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : BINARY COMPLEX OF EDS1 AND
REMARK 245 SAG101 WITH MOLECULE ATP-ADPR
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 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 PRO A 508
REMARK 465 ASN A 509
REMARK 465 GLY A 510
REMARK 465 MET A 511
REMARK 465 ILE A 512
REMARK 465 ALA A 513
REMARK 465 GLU A 514
REMARK 465 ASP A 515
REMARK 465 VAL A 516
REMARK 465 PHE A 517
REMARK 465 TRP A 518
REMARK 465 ASN A 519
REMARK 465 LYS A 520
REMARK 465 VAL A 521
REMARK 465 ASN A 522
REMARK 465 GLY A 523
REMARK 465 LEU A 524
REMARK 465 ASN A 525
REMARK 465 LEU A 526
REMARK 465 GLY A 527
REMARK 465 LEU A 528
REMARK 465 GLN A 529
REMARK 465 LEU A 530
REMARK 465 GLU A 531
REMARK 465 GLU A 532
REMARK 465 ILE A 533
REMARK 465 GLN A 534
REMARK 465 GLU A 535
REMARK 465 THR A 536
REMARK 465 LEU A 537
REMARK 465 LYS A 538
REMARK 465 ASN A 539
REMARK 465 SER A 540
REMARK 465 GLY A 541
REMARK 465 MET A 616
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 MET B 1
REMARK 465 GLU B 2
REMARK 465 PRO B 35
REMARK 465 PRO B 36
REMARK 465 TYR B 37
REMARK 465 SER B 38
REMARK 465 ASN B 39
REMARK 465 HIS B 40
REMARK 465 ASP B 41
REMARK 465 PRO B 42
REMARK 465 GLY B 43
REMARK 465 LEU B 44
REMARK 465 GLN B 45
REMARK 465 VAL B 46
REMARK 465 SER B 47
REMARK 465 LYS B 48
REMARK 465 LYS B 49
REMARK 465 LYS B 50
REMARK 465 LYS B 51
REMARK 465 ASP B 52
REMARK 465 VAL B 243
REMARK 465 HIS B 244
REMARK 465 ASP B 245
REMARK 465 SER B 246
REMARK 465 GLY B 247
REMARK 465 LEU B 248
REMARK 465 SER B 536
REMARK 465 GLN B 537
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER B 365 OG
REMARK 470 ASP B 366 CG OD1 OD2
REMARK 470 SER B 368 OG
REMARK 470 GLU B 427 CG CD OE1 OE2
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 -13.05 71.71
REMARK 500 ASP A 98 140.90 -33.28
REMARK 500 HIS A 122 -162.70 -79.00
REMARK 500 GLU A 173 0.37 -66.97
REMARK 500 MET A 193 0.75 -67.34
REMARK 500 ALA A 251 24.41 44.93
REMARK 500 THR A 277 -169.92 -128.44
REMARK 500 SER A 326 31.02 -96.35
REMARK 500 CYS A 442 7.52 82.44
REMARK 500 GLN A 443 9.62 -59.31
REMARK 500 SER B 79 0.08 -65.41
REMARK 500 LEU B 160 33.86 -96.17
REMARK 500 MET B 210 35.84 -99.13
REMARK 500 SER B 365 -3.44 67.36
REMARK 500 ASP B 366 -51.64 72.81
REMARK 500 LEU B 370 76.38 55.51
REMARK 500 LYS B 371 -71.82 -37.56
REMARK 500 ARG B 372 -30.65 -142.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-33233 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF EDS1 AND SAG101 WITH ATP-APDR
DBREF 7XJP A 1 623 UNP Q9SU72 EDS1C_ARATH 1 623
DBREF 7XJP B 1 537 UNP Q4F883 SG101_ARATH 1 537
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 537 MET GLU SER SER SER SER LEU LYS GLY SER ALA LEU GLY
SEQRES 2 B 537 LYS LEU VAL VAL THR SER GLY LEU LEU HIS SER SER TRP
SEQRES 3 B 537 SER LYS ILE LEU GLU ILE HIS ASN PRO PRO TYR SER ASN
SEQRES 4 B 537 HIS ASP PRO GLY LEU GLN VAL SER LYS LYS LYS LYS ASP
SEQRES 5 B 537 SER GLY LEU GLU PHE GLN ILE HIS ARG GLU GLU LYS PHE
SEQRES 6 B 537 THR LEU VAL VAL PHE SER ALA PRO PRO ILE CYS ARG SER
SEQRES 7 B 537 SER SER SER ASP SER THR LEU LEU HIS VAL LYS ASP LYS
SEQRES 8 B 537 GLU ASN PRO PHE PRO PHE LEU CYS SER GLU ASN ASN PRO
SEQRES 9 B 537 SER PHE SER LEU HIS THR PRO ALA PHE ASN LEU PHE THR
SEQRES 10 B 537 SER ALA SER THR SER LEU THR TYR LEU LYS SER GLU LEU
SEQRES 11 B 537 LEU GLN THR LEU LYS SER GLU LYS PRO VAL ILE ILE THR
SEQRES 12 B 537 GLY ALA ALA LEU GLY GLY SER VAL ALA SER LEU TYR THR
SEQRES 13 B 537 LEU TRP LEU LEU GLU THR ILE GLU PRO THR LEU LYS ARG
SEQRES 14 B 537 PRO LEU CYS ILE THR PHE GLY SER PRO LEU ILE GLY ASP
SEQRES 15 B 537 ALA SER LEU GLN GLN ILE LEU GLU ASN SER VAL ARG ASN
SEQRES 16 B 537 SER CYS PHE LEU HIS VAL VAL SER ALA GLN THR ARG ILE
SEQRES 17 B 537 LYS MET ASP PHE PHE LYS PRO PHE GLY THR PHE LEU ILE
SEQRES 18 B 537 CYS PHE ASP SER GLY CYS VAL CYS ILE GLU ASP HIS VAL
SEQRES 19 B 537 ALA VAL THR GLU LEU LEU ASN GLY VAL HIS ASP SER GLY
SEQRES 20 B 537 LEU VAL ASP TYR SER GLN VAL LEU ASN ARG LEU ASP GLN
SEQRES 21 B 537 SER MET LEU SER LEU ALA ASP SER ARG LEU ILE PRO GLU
SEQRES 22 B 537 ASP VAL ILE LYS GLY ILE GLU LYS ARG ALA GLU MET LYS
SEQRES 23 B 537 ASN LEU ARG PHE ASP MET MET PHE LYS LYS LEU ASN ASP
SEQRES 24 B 537 MET LYS ILE SER MET ALA TYR ILE GLU TRP TYR LYS LYS
SEQRES 25 B 537 LYS CYS LYS GLU VAL LYS ILE GLY TYR TYR ASP ARG PHE
SEQRES 26 B 537 LYS THR GLN LEU ALA PHE PRO SER LYS GLU PHE ASP ILE
SEQRES 27 B 537 ASN ILE LYS ASN HIS HIS LYS SER GLU LEU ASN ARG PHE
SEQRES 28 B 537 TRP LYS SER VAL VAL GLU GLU VAL GLU ARG ARG PRO GLN
SEQRES 29 B 537 SER ASP ALA SER ILE LEU LYS ARG ARG PHE LEU PHE SER
SEQRES 30 B 537 GLY ASN ASN TYR ARG ARG MET ILE GLU PRO LEU ASP ILE
SEQRES 31 B 537 ALA GLU TYR TYR LEU GLU GLY ARG LYS GLU TYR ARG THR
SEQRES 32 B 537 THR GLY ARG SER HIS HIS TYR VAL MET LEU GLU LYS TRP
SEQRES 33 B 537 PHE GLY MET GLU SER ILE LEU ILE GLU LYS GLU ARG CYS
SEQRES 34 B 537 LYS LYS ARG ASP LEU SER ASP LEU LEU THR PHE ASP SER
SEQRES 35 B 537 CYS PHE TRP ALA GLU VAL GLU ASP SER LEU ILE VAL ILE
SEQRES 36 B 537 ASN GLN LEU ASN THR THR VAL GLY MET ARG ASP ASP VAL
SEQRES 37 B 537 ARG GLU VAL LEU THR ARG LYS LEU VAL GLU PHE GLU GLY
SEQRES 38 B 537 TYR VAL TRP GLU ILE ILE THR LYS ARG GLU VAL SER PRO
SEQRES 39 B 537 GLU ILE PHE LEU GLU GLU SER SER PHE MET LYS TRP TRP
SEQRES 40 B 537 LYS GLU TYR LYS LYS ILE LYS GLY PHE ASN SER SER TYR
SEQRES 41 B 537 LEU THR GLU PHE MET ASN THR ARG LYS TYR GLU SER TYR
SEQRES 42 B 537 GLY LYS SER GLN
HET IPA A 701 4
HET APR A 702 35
HET ATP B 601 31
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM APR ADENOSINE-5-DIPHOSPHORIBOSE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN IPA 2-PROPANOL
FORMUL 3 IPA C3 H8 O
FORMUL 4 APR C15 H23 N5 O14 P2
FORMUL 5 ATP C10 H16 N5 O13 P3
HELIX 1 AA1 ALA A 2 GLY A 8 1 7
HELIX 2 AA2 ASN A 10 ALA A 24 1 15
HELIX 3 AA3 SER A 48 PHE A 52 5 5
HELIX 4 AA4 GLU A 87 ASP A 98 1 12
HELIX 5 AA5 PRO A 99 THR A 101 5 3
HELIX 6 AA6 SER A 102 SER A 113 1 12
HELIX 7 AA7 HIS A 122 TYR A 140 1 19
HELIX 8 AA8 ASP A 163 GLU A 173 1 11
HELIX 9 AA9 ILE A 188 MET A 193 1 6
HELIX 10 AB1 ARG A 196 GLU A 201 1 6
HELIX 11 AB2 THR A 203 ASP A 212 1 10
HELIX 12 AB3 SER A 221 GLU A 246 1 26
HELIX 13 AB4 ALA A 251 SER A 260 1 10
HELIX 14 AB5 ASN A 286 THR A 297 1 12
HELIX 15 AB6 ASP A 302 TRP A 306 5 5
HELIX 16 AB7 SER A 307 HIS A 317 1 11
HELIX 17 AB8 SER A 319 SER A 326 1 8
HELIX 18 AB9 ILE A 341 GLY A 349 1 9
HELIX 19 AC1 SER A 351 GLU A 380 1 30
HELIX 20 AC2 GLN A 381 GLU A 394 1 14
HELIX 21 AC3 GLU A 394 HIS A 402 1 9
HELIX 22 AC4 GLY A 405 SER A 413 1 9
HELIX 23 AC5 GLU A 415 CYS A 442 1 28
HELIX 24 AC6 ASP A 446 ASP A 451 1 6
HELIX 25 AC7 ILE A 452 HIS A 476 1 25
HELIX 26 AC8 LYS A 478 GLY A 483 1 6
HELIX 27 AC9 PRO A 484 GLY A 489 1 6
HELIX 28 AD1 PRO A 491 LEU A 506 1 16
HELIX 29 AD2 CYS A 547 LYS A 556 1 10
HELIX 30 AD3 PRO A 559 GLY A 581 1 23
HELIX 31 AD4 ASP A 584 PHE A 589 1 6
HELIX 32 AD5 SER A 593 THR A 601 1 9
HELIX 33 AD6 PRO A 603 HIS A 609 1 7
HELIX 34 AD7 SER B 4 GLY B 20 1 17
HELIX 35 AD8 GLY B 20 ASN B 34 1 15
HELIX 36 AD9 ARG B 77 SER B 81 5 5
HELIX 37 AE1 THR B 110 SER B 136 1 27
HELIX 38 AE2 LEU B 147 LEU B 160 1 14
HELIX 39 AE3 ALA B 183 LEU B 189 1 7
HELIX 40 AE4 ARG B 194 SER B 196 5 3
HELIX 41 AE5 ASP B 232 ASN B 241 1 10
HELIX 42 AE6 ASP B 250 MET B 262 1 13
HELIX 43 AE7 PRO B 272 VAL B 317 1 46
HELIX 44 AE8 GLY B 320 PHE B 331 1 12
HELIX 45 AE9 LYS B 334 HIS B 343 1 10
HELIX 46 AF1 HIS B 343 GLU B 360 1 18
HELIX 47 AF2 ARG B 372 GLU B 396 1 25
HELIX 48 AF3 GLU B 400 GLY B 405 1 6
HELIX 49 AF4 SER B 407 ILE B 422 1 16
HELIX 50 AF5 CYS B 443 THR B 461 1 19
HELIX 51 AF6 ASP B 466 LYS B 489 1 24
HELIX 52 AF7 SER B 493 LEU B 498 5 6
HELIX 53 AF8 SER B 501 LYS B 514 1 14
HELIX 54 AF9 SER B 519 THR B 527 1 9
SHEET 1 AA1 8 HIS A 31 ALA A 35 0
SHEET 2 AA1 8 VAL A 38 PHE A 43 -1 O ILE A 40 N GLU A 33
SHEET 3 AA1 8 GLN A 116 GLY A 121 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 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 7 GLU B 56 ARG B 61 0
SHEET 2 AA3 7 THR B 66 SER B 71 -1 O LEU B 67 N HIS B 60
SHEET 3 AA3 7 VAL B 140 GLY B 144 1 O ILE B 141 N THR B 66
SHEET 4 AA3 7 CYS B 172 PHE B 175 1 O ILE B 173 N GLY B 144
SHEET 5 AA3 7 PHE B 198 SER B 203 1 O LEU B 199 N THR B 174
SHEET 6 AA3 7 THR B 218 CYS B 222 1 O CYS B 222 N VAL B 202
SHEET 7 AA3 7 CYS B 227 ILE B 230 -1 O ILE B 230 N PHE B 219
SHEET 1 AA4 2 SER B 83 THR B 84 0
SHEET 2 AA4 2 LEU B 108 HIS B 109 -1 O LEU B 108 N THR B 84
SHEET 1 AA5 2 GLY B 181 ASP B 182 0
SHEET 2 AA5 2 PHE B 213 LYS B 214 -1 O LYS B 214 N GLY B 181
LINK C1D APR A 702 O2' ATP B 601 1555 1555 1.42
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 4721 TYR A 615
TER 8862 LYS B 535
MASTER 221 0 3 54 21 0 0 6 8930 2 70 90
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