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HEADER PLANT PROTEIN/HYDROLASE 10-MAR-24 8YN1
TITLE CRYO-EM STRUCTURE OF NRG1A(LRR) IN COMPLEX WITH EDS1-SAG101-(ADPR-ATP)
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;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROBABLE DISEASE RESISTANCE PROTEIN AT5G66900;
COMPND 13 CHAIN: C;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 10 ORGANISM_COMMON: THALE CRESS;
SOURCE 11 ORGANISM_TAXID: 3702;
SOURCE 12 GENE: SAG101, AT5G14930, F2G14.50;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 17 ORGANISM_COMMON: THALE CRESS;
SOURCE 18 ORGANISM_TAXID: 3702;
SOURCE 19 GENE: AT5G66900, MUD21.16;
SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PLANT IMMUNITY, ETI, NRG1A, EDS1, SAG101, ADPR-ATP, PLANT PROTEIN,
KEYWDS 2 PLANT PROTEIN-HYDROLASE COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.HUANG,Y.XIAO,J.CHAI
REVDAT 1 11-DEC-24 8YN1 0
JRNL AUTH S.HUANG,Y.XIAO,J.CHAI
JRNL TITL CRYO-EM STRUCTURE OF NRG1A(LRR) IN COMPLEX WITH
JRNL TITL 2 EDS1-SAG101-(ADPR-ATP)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.09 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) : 3.090
REMARK 3 NUMBER OF PARTICLES : 275262
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 8YN1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300045893.
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 : TERNARY COMPLEX OF NRG1A(LRR)
REMARK 245 WITH EDS1-SAG101-(ADPR-ATP)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
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) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
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 : SPOT SCAN
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 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 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 C2D APR A 701 O2' ATP B 601 1.65
REMARK 500 O LEU B 189 ND2 ASN B 195 2.14
REMARK 500 O ALA B 145 N GLY B 149 2.16
REMARK 500 O GLU A 322 OG SER A 326 2.18
REMARK 500 O LEU B 160 NH1 ARG B 194 2.18
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 -19.86 72.69
REMARK 500 TYR A 30 172.47 179.15
REMARK 500 SER A 123 -70.89 -42.50
REMARK 500 THR A 277 -169.58 -123.74
REMARK 500 LYS A 279 -33.01 -130.30
REMARK 500 SER A 351 -163.93 -78.60
REMARK 500 SER A 413 62.82 63.76
REMARK 500 LYS A 487 -61.29 -98.12
REMARK 500 PRO B 74 -177.58 -66.15
REMARK 500 PHE B 95 66.81 -115.28
REMARK 500 GLU B 137 47.72 71.18
REMARK 500 ALA B 145 -165.38 -79.47
REMARK 500 ALA B 146 -72.91 -45.39
REMARK 500 PRO B 165 7.39 -65.35
REMARK 500 SER B 196 5.09 -67.28
REMARK 500 LYS B 318 33.17 75.11
REMARK 500 PRO B 363 -178.94 -62.95
REMARK 500 SER B 365 -8.18 65.23
REMARK 500 ASP B 366 7.51 55.46
REMARK 500 LEU B 370 79.70 57.75
REMARK 500 LYS B 371 -76.97 -59.55
REMARK 500 ARG B 372 -28.99 -148.15
REMARK 500 ARG B 465 -175.27 -65.62
REMARK 500 GLU C 472 -163.04 -74.87
REMARK 500 ALA C 716 4.49 -61.36
REMARK 500 MET C 752 46.15 -140.90
REMARK 500 CYS C 755 35.60 -95.50
REMARK 500 SER C 763 -0.89 -59.88
REMARK 500 PRO C 787 0.51 -67.70
REMARK 500 MET C 808 51.09 -96.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-39411 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF NRG1A(LRR) IN COMPLEX WITH EDS1-SAG101-(ADPR-
REMARK 900 ATP)
DBREF 8YN1 A 2 615 UNP Q9SU72 EDS1C_ARATH 2 615
DBREF 8YN1 B 3 535 UNP Q4F883 SG101_ARATH 3 535
DBREF 8YN1 C 404 809 UNP Q9FKZ1 DRL42_ARATH 404 809
SEQRES 1 A 614 ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU ILE
SEQRES 2 A 614 THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU THR
SEQRES 3 A 614 GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL ILE
SEQRES 4 A 614 PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE PHE
SEQRES 5 A 614 ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS LEU
SEQRES 6 A 614 ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY LYS
SEQRES 7 A 614 GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS ASN
SEQRES 8 A 614 LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN ALA
SEQRES 9 A 614 SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE VAL
SEQRES 10 A 614 PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE LEU
SEQRES 11 A 614 ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG ASN
SEQRES 12 A 614 PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE GLY
SEQRES 13 A 614 ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA LEU
SEQRES 14 A 614 GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE VAL
SEQRES 15 A 614 SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA ARG
SEQRES 16 A 614 LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU ALA
SEQRES 17 A 614 GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER GLU
SEQRES 18 A 614 GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG ASP
SEQRES 19 A 614 THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU THR
SEQRES 20 A 614 GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER PHE
SEQRES 21 A 614 LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE VAL
SEQRES 22 A 614 PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN SER
SEQRES 23 A 614 ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN ALA
SEQRES 24 A 614 SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG SER
SEQRES 25 A 614 ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN SER
SEQRES 26 A 614 MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU ASN
SEQRES 27 A 614 SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER THR
SEQRES 28 A 614 ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU GLU
SEQRES 29 A 614 LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN VAL
SEQRES 30 A 614 ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP ILE
SEQRES 31 A 614 GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS ASN
SEQRES 32 A 614 GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU ASN
SEQRES 33 A 614 ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA GLY
SEQRES 34 A 614 VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS GLN
SEQRES 35 A 614 LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE LYS
SEQRES 36 A 614 LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU ASP
SEQRES 37 A 614 ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP THR
SEQRES 38 A 614 GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR ILE
SEQRES 39 A 614 TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS PRO
SEQRES 40 A 614 ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS VAL
SEQRES 41 A 614 ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE GLN
SEQRES 42 A 614 GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER CYS
SEQRES 43 A 614 PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO TYR
SEQRES 44 A 614 GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY MET
SEQRES 45 A 614 LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP LYS
SEQRES 46 A 614 GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP TRP
SEQRES 47 A 614 ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO LEU
SEQRES 48 A 614 ARG ASP TYR
SEQRES 1 B 533 SER SER SER SER LEU LYS GLY SER ALA LEU GLY LYS LEU
SEQRES 2 B 533 VAL VAL THR SER GLY LEU LEU HIS SER SER TRP SER LYS
SEQRES 3 B 533 ILE LEU GLU ILE HIS ASN PRO PRO TYR SER ASN HIS ASP
SEQRES 4 B 533 PRO GLY LEU GLN VAL SER LYS LYS LYS LYS ASP SER GLY
SEQRES 5 B 533 LEU GLU PHE GLN ILE HIS ARG GLU GLU LYS PHE THR LEU
SEQRES 6 B 533 VAL VAL PHE SER ALA PRO PRO ILE CYS ARG SER SER SER
SEQRES 7 B 533 SER ASP SER THR LEU LEU HIS VAL LYS ASP LYS GLU ASN
SEQRES 8 B 533 PRO PHE PRO PHE LEU CYS SER GLU ASN ASN PRO SER PHE
SEQRES 9 B 533 SER LEU HIS THR PRO ALA PHE ASN LEU PHE THR SER ALA
SEQRES 10 B 533 SER THR SER LEU THR TYR LEU LYS SER GLU LEU LEU GLN
SEQRES 11 B 533 THR LEU LYS SER GLU LYS PRO VAL ILE ILE THR GLY ALA
SEQRES 12 B 533 ALA LEU GLY GLY SER VAL ALA SER LEU TYR THR LEU TRP
SEQRES 13 B 533 LEU LEU GLU THR ILE GLU PRO THR LEU LYS ARG PRO LEU
SEQRES 14 B 533 CYS ILE THR PHE GLY SER PRO LEU ILE GLY ASP ALA SER
SEQRES 15 B 533 LEU GLN GLN ILE LEU GLU ASN SER VAL ARG ASN SER CYS
SEQRES 16 B 533 PHE LEU HIS VAL VAL SER ALA GLN THR ARG ILE LYS MET
SEQRES 17 B 533 ASP PHE PHE LYS PRO PHE GLY THR PHE LEU ILE CYS PHE
SEQRES 18 B 533 ASP SER GLY CYS VAL CYS ILE GLU ASP HIS VAL ALA VAL
SEQRES 19 B 533 THR GLU LEU LEU ASN GLY VAL HIS ASP SER GLY LEU VAL
SEQRES 20 B 533 ASP TYR SER GLN VAL LEU ASN ARG LEU ASP GLN SER MET
SEQRES 21 B 533 LEU SER LEU ALA ASP SER ARG LEU ILE PRO GLU ASP VAL
SEQRES 22 B 533 ILE LYS GLY ILE GLU LYS ARG ALA GLU MET LYS ASN LEU
SEQRES 23 B 533 ARG PHE ASP MET MET PHE LYS LYS LEU ASN ASP MET LYS
SEQRES 24 B 533 ILE SER MET ALA TYR ILE GLU TRP TYR LYS LYS LYS CYS
SEQRES 25 B 533 LYS GLU VAL LYS ILE GLY TYR TYR ASP ARG PHE LYS THR
SEQRES 26 B 533 GLN LEU ALA PHE PRO SER LYS GLU PHE ASP ILE ASN ILE
SEQRES 27 B 533 LYS ASN HIS HIS LYS SER GLU LEU ASN ARG PHE TRP LYS
SEQRES 28 B 533 SER VAL VAL GLU GLU VAL GLU ARG ARG PRO GLN SER ASP
SEQRES 29 B 533 ALA SER ILE LEU LYS ARG ARG PHE LEU PHE SER GLY ASN
SEQRES 30 B 533 ASN TYR ARG ARG MET ILE GLU PRO LEU ASP ILE ALA GLU
SEQRES 31 B 533 TYR TYR LEU GLU GLY ARG LYS GLU TYR ARG THR THR GLY
SEQRES 32 B 533 ARG SER HIS HIS TYR VAL MET LEU GLU LYS TRP PHE GLY
SEQRES 33 B 533 MET GLU SER ILE LEU ILE GLU LYS GLU ARG CYS LYS LYS
SEQRES 34 B 533 ARG ASP LEU SER ASP LEU LEU THR PHE ASP SER CYS PHE
SEQRES 35 B 533 TRP ALA GLU VAL GLU ASP SER LEU ILE VAL ILE ASN GLN
SEQRES 36 B 533 LEU ASN THR THR VAL GLY MET ARG ASP ASP VAL ARG GLU
SEQRES 37 B 533 VAL LEU THR ARG LYS LEU VAL GLU PHE GLU GLY TYR VAL
SEQRES 38 B 533 TRP GLU ILE ILE THR LYS ARG GLU VAL SER PRO GLU ILE
SEQRES 39 B 533 PHE LEU GLU GLU SER SER PHE MET LYS TRP TRP LYS GLU
SEQRES 40 B 533 TYR LYS LYS ILE LYS GLY PHE ASN SER SER TYR LEU THR
SEQRES 41 B 533 GLU PHE MET ASN THR ARG LYS TYR GLU SER TYR GLY LYS
SEQRES 1 C 406 SER PHE ASP ALA LEU ASP PRO ASN LEU LYS GLU CYS PHE
SEQRES 2 C 406 LEU ASP MET GLY SER PHE LEU GLU ASP GLN LYS ILE ARG
SEQRES 3 C 406 ALA SER VAL ILE ILE ASP MET TRP VAL GLU LEU TYR GLY
SEQRES 4 C 406 LYS GLY SER SER ILE LEU TYR MET TYR LEU GLU ASP LEU
SEQRES 5 C 406 ALA SER GLN ASN LEU LEU LYS LEU VAL PRO LEU GLY THR
SEQRES 6 C 406 ASN GLU HIS GLU ASP GLY PHE TYR ASN ASP PHE LEU VAL
SEQRES 7 C 406 THR GLN HIS ASP ILE LEU ARG GLU LEU ALA ILE CYS GLN
SEQRES 8 C 406 SER GLU PHE LYS GLU ASN LEU GLU ARG LYS ARG LEU ASN
SEQRES 9 C 406 LEU GLU ILE LEU GLU ASN THR PHE PRO ASP TRP CYS LEU
SEQRES 10 C 406 ASN THR ILE ASN ALA SER LEU LEU SER ILE SER THR ASP
SEQRES 11 C 406 ASP LEU PHE SER SER LYS TRP LEU GLU MET ASP CYS PRO
SEQRES 12 C 406 ASN VAL GLU ALA LEU VAL LEU ASN LEU SER SER SER ASP
SEQRES 13 C 406 TYR ALA LEU PRO SER PHE ILE SER GLY MET LYS LYS LEU
SEQRES 14 C 406 LYS VAL LEU THR ILE THR ASN HIS GLY PHE TYR PRO ALA
SEQRES 15 C 406 ARG LEU SER ASN PHE SER CYS LEU SER SER LEU PRO ASN
SEQRES 16 C 406 LEU LYS ARG ILE ARG LEU GLU LYS VAL SER ILE THR LEU
SEQRES 17 C 406 LEU ASP ILE PRO GLN LEU GLN LEU SER SER LEU LYS LYS
SEQRES 18 C 406 LEU SER LEU VAL MET CYS SER PHE GLY GLU VAL PHE TYR
SEQRES 19 C 406 ASP THR GLU ASP ILE VAL VAL SER ASN ALA LEU SER LYS
SEQRES 20 C 406 LEU GLN GLU ILE ASP ILE ASP TYR CYS TYR ASP LEU ASP
SEQRES 21 C 406 GLU LEU PRO TYR TRP ILE SER GLU ILE VAL SER LEU LYS
SEQRES 22 C 406 THR LEU SER ILE THR ASN CYS ASN LYS LEU SER GLN LEU
SEQRES 23 C 406 PRO GLU ALA ILE GLY ASN LEU SER ARG LEU GLU VAL LEU
SEQRES 24 C 406 ARG LEU CYS SER SER MET ASN LEU SER GLU LEU PRO GLU
SEQRES 25 C 406 ALA THR GLU GLY LEU SER ASN LEU ARG PHE LEU ASP ILE
SEQRES 26 C 406 SER HIS CYS LEU GLY LEU ARG LYS LEU PRO GLN GLU ILE
SEQRES 27 C 406 GLY LYS LEU GLN ASN LEU LYS LYS ILE SER MET ARG LYS
SEQRES 28 C 406 CYS SER GLY CYS GLU LEU PRO GLU SER VAL THR ASN LEU
SEQRES 29 C 406 GLU ASN LEU GLU VAL LYS CYS ASP GLU GLU THR GLY LEU
SEQRES 30 C 406 LEU TRP GLU ARG LEU LYS PRO LYS MET ARG ASN LEU ARG
SEQRES 31 C 406 VAL GLN GLU GLU GLU ILE GLU HIS ASN LEU ASN LEU LEU
SEQRES 32 C 406 GLN MET PHE
HET APR A 701 35
HET ATP B 601 31
HETNAM APR ADENOSINE-5-DIPHOSPHORIBOSE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
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 GLU A 87 ASP A 98 1 12
HELIX 4 AA4 PRO A 99 SER A 102 5 4
HELIX 5 AA5 PHE A 103 SER A 113 1 11
HELIX 6 AA6 HIS A 122 TYR A 140 1 19
HELIX 7 AA7 ASN A 146 LEU A 149 5 4
HELIX 8 AA8 ASP A 163 GLU A 173 1 11
HELIX 9 AA9 ILE A 188 ALA A 195 5 8
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 GLU A 303 SER A 307 5 5
HELIX 16 AB7 LEU A 308 HIS A 317 1 10
HELIX 17 AB8 SER A 319 SER A 326 1 8
HELIX 18 AB9 SER A 340 LEU A 348 1 9
HELIX 19 AC1 SER A 351 GLN A 381 1 31
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 LYS A 441 1 27
HELIX 24 AC6 GLU A 447 GLY A 450 5 4
HELIX 25 AC7 ASP A 451 HIS A 476 1 26
HELIX 26 AC8 LEU A 477 ASP A 481 5 5
HELIX 27 AC9 PRO A 484 GLY A 489 1 6
HELIX 28 AD1 PRO A 491 LYS A 507 1 17
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 SER A 593 ILE A 600 1 8
HELIX 32 AD5 PRO A 603 SER A 608 1 6
HELIX 33 AD6 SER B 4 GLY B 20 1 17
HELIX 34 AD7 GLY B 20 ASN B 34 1 15
HELIX 35 AD8 THR B 110 SER B 136 1 27
HELIX 36 AD9 ALA B 145 LEU B 160 1 16
HELIX 37 AE1 ALA B 183 LEU B 189 1 7
HELIX 38 AE2 SER B 192 SER B 196 5 5
HELIX 39 AE3 ASP B 232 ASN B 241 1 10
HELIX 40 AE4 ASP B 250 MET B 262 1 13
HELIX 41 AE5 PRO B 272 VAL B 317 1 46
HELIX 42 AE6 GLY B 320 PHE B 331 1 12
HELIX 43 AE7 LYS B 334 GLU B 360 1 27
HELIX 44 AE8 ARG B 372 GLU B 396 1 25
HELIX 45 AE9 GLU B 400 GLY B 405 1 6
HELIX 46 AF1 SER B 407 ILE B 422 1 16
HELIX 47 AF2 CYS B 443 THR B 461 1 19
HELIX 48 AF3 ASP B 466 LYS B 489 1 24
HELIX 49 AF4 SER B 493 LEU B 498 5 6
HELIX 50 AF5 SER B 501 GLY B 515 1 15
HELIX 51 AF6 SER B 519 THR B 527 1 9
HELIX 52 AF7 LYS B 529 TYR B 533 5 5
HELIX 53 AF8 ASP C 409 ASP C 418 1 10
HELIX 54 AF9 MET C 419 PHE C 422 5 4
HELIX 55 AG1 ALA C 430 GLY C 442 1 13
HELIX 56 AG2 GLY C 444 GLN C 458 1 15
HELIX 57 AG3 HIS C 484 GLN C 494 1 11
HELIX 58 AG4 GLU C 499 ARG C 503 5 5
HELIX 59 AG5 PRO C 563 MET C 569 5 7
HELIX 60 AG6 PHE C 590 LEU C 596 5 7
HELIX 61 AG7 LEU C 612 LEU C 617 1 6
HELIX 62 AG8 VAL C 643 LEU C 648 1 6
HELIX 63 AG9 TYR C 667 ILE C 672 5 6
HELIX 64 AH1 ALA C 692 LEU C 696 5 5
HELIX 65 AH2 PRO C 714 LEU C 720 5 7
HELIX 66 AH3 GLU C 740 LEU C 744 5 5
HELIX 67 AH4 PRO C 761 LEU C 767 5 7
HELIX 68 AH5 ASP C 775 ARG C 784 1 10
HELIX 69 AH6 LEU C 785 MET C 789 5 5
HELIX 70 AH7 LEU C 803 MET C 808 5 6
SHEET 1 AA1 8 TYR A 30 ALA A 35 0
SHEET 2 AA1 8 VAL A 38 PHE A 43 -1 O ALA A 42 N HIS A 31
SHEET 3 AA1 8 GLN A 116 GLY A 121 1 O VAL A 118 N PHE A 41
SHEET 4 AA1 8 PRO A 151 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 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 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 GLU B 56 ARG B 61 0
SHEET 2 AA3 7 THR B 66 SER B 71 -1 O SER B 71 N GLU B 56
SHEET 3 AA3 7 VAL B 140 GLY B 144 1 O ILE B 141 N VAL B 68
SHEET 4 AA3 7 LEU B 171 PHE B 175 1 O LEU B 171 N ILE B 142
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 LEU B 220 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 HIS B 87 0
SHEET 2 AA4 2 SER B 105 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
SHEET 1 AA6 3 ILE C 428 ARG C 429 0
SHEET 2 AA6 3 PHE C 479 THR C 482 -1 O VAL C 481 N ILE C 428
SHEET 3 AA6 3 LYS C 462 PRO C 465 -1 N VAL C 464 O LEU C 480
SHEET 1 AA7 8 ARG C 505 GLU C 509 0
SHEET 2 AA7 8 LEU C 527 SER C 531 1 O SER C 529 N LEU C 508
SHEET 3 AA7 8 ALA C 550 LEU C 555 1 O ASN C 554 N ILE C 530
SHEET 4 AA7 8 VAL C 574 ASN C 579 1 O THR C 578 N LEU C 553
SHEET 5 AA7 8 ARG C 601 GLU C 605 1 O ARG C 603 N LEU C 575
SHEET 6 AA7 8 LYS C 624 VAL C 628 1 O SER C 626 N LEU C 604
SHEET 7 AA7 8 GLU C 653 ASP C 657 1 O ASP C 655 N LEU C 627
SHEET 8 AA7 8 SER C 679 THR C 681 1 O SER C 679 N ILE C 656
SHEET 1 AA8 3 ASP C 559 ALA C 561 0
SHEET 2 AA8 3 ALA C 585 SER C 588 1 O ARG C 586 N TYR C 560
SHEET 3 AA8 3 VAL C 607 SER C 608 1 O SER C 608 N ALA C 585
SHEET 1 AA9 3 LYS C 749 SER C 751 0
SHEET 2 AA9 3 GLU C 771 CYS C 774 1 O LYS C 773 N ILE C 750
SHEET 3 AA9 3 ARG C 793 GLU C 796 1 O ARG C 793 N VAL C 772
LINK C1D APR A 701 O2' ATP B 601 1555 1555 1.37
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 8871 LYS B 535
TER 12123 PHE C 809
MASTER 225 0 2 70 38 0 0 612186 3 66 121
END |