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HEADER TRANSFERASE/TRANSFERASE ACTIVATOR 26-MAR-22 7XDD
TITLE CRYO-EM STRUCTURE OF EDS1 AND PAD4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE-LIKE PAD4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN ENHANCED DISEASE SUSCEPTIBILITY 9,PROTEIN
COMPND 5 PHYTOALEXIN DEFICIENT 4,ATPAD4;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN EDS1;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS;
SOURCE 3 ORGANISM_TAXID: 3701;
SOURCE 4 GENE: PAD4, EDS9, AT3G52430, F22O6.190;
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: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS NLR, PLANT PROTEIN, PLANT IMMUNE SIGNALING, TRANSFERASE-TRANSFERASE
KEYWDS 2 ACTIVATOR COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.J.HUANG,A.L.JIA,Y.SUN,Z.F.HAN,J.J.CHAI
REVDAT 1 13-JUL-22 7XDD 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. 2.93 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) : 2.930
REMARK 3 NUMBER OF PARTICLES : 133202
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 7XDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1300028588.
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 PAD4; PAD4; EDS1
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 LYS A 432
REMARK 465 VAL A 433
REMARK 465 PRO A 434
REMARK 465 GLU A 435
REMARK 465 GLU A 436
REMARK 465 CYS A 521
REMARK 465 LYS A 522
REMARK 465 MET A 523
REMARK 465 GLY A 524
REMARK 465 TYR A 525
REMARK 465 GLU A 526
REMARK 465 ASN A 527
REMARK 465 GLU A 528
REMARK 465 ILE A 529
REMARK 465 GLU A 530
REMARK 465 MET A 531
REMARK 465 VAL A 532
REMARK 465 VAL A 533
REMARK 465 ASP A 534
REMARK 465 GLU A 535
REMARK 465 SER A 536
REMARK 465 ASP A 537
REMARK 465 ALA A 538
REMARK 465 MET A 539
REMARK 465 GLU A 540
REMARK 465 THR A 541
REMARK 465 ARG B 214
REMARK 465 LYS B 215
REMARK 465 SER B 216
REMARK 465 SER B 217
REMARK 465 VAL B 218
REMARK 465 GLN B 219
REMARK 465 GLU B 220
REMARK 465 GLU B 619
REMARK 465 ILE B 620
REMARK 465 THR B 621
REMARK 465 ASP B 622
REMARK 465 THR B 623
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 LEU A 76 77.32 -101.47
REMARK 500 SER A 118 -122.80 51.47
REMARK 500 ARG B 29 -14.42 73.73
REMARK 500 TYR B 30 166.22 178.12
REMARK 500 ASP B 98 133.53 -38.36
REMARK 500 ARG B 100 1.46 -68.75
REMARK 500 SER B 123 -126.23 48.32
REMARK 500 ASN B 144 76.38 -151.55
REMARK 500 THR B 277 -167.33 -118.72
REMARK 500 LYS B 329 34.97 -98.11
REMARK 500 LYS B 403 31.72 70.79
REMARK 500 ASN B 539 42.01 37.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-33144 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF EDS1 AND PAD4
DBREF 7XDD A 4 541 UNP Q9S745 PAD4_ARATH 4 541
DBREF 7XDD B 1 623 UNP Q9SU72 EDS1C_ARATH 1 623
SEQRES 1 A 538 CYS ARG PHE GLU THR SER GLU LEU GLN ALA SER VAL MET
SEQRES 2 A 538 ILE SER THR PRO LEU PHE THR ASP SER TRP SER SER CYS
SEQRES 3 A 538 ASN THR ALA ASN CYS ASN GLY SER ILE LYS ILE HIS ASP
SEQRES 4 A 538 ILE ALA GLY ILE THR TYR VAL ALA ILE PRO ALA VAL SER
SEQRES 5 A 538 MET ILE GLN LEU GLY ASN LEU VAL GLY LEU PRO VAL THR
SEQRES 6 A 538 GLY ASP VAL LEU PHE PRO GLY LEU SER SER ASP GLU PRO
SEQRES 7 A 538 LEU PRO MET VAL ASP ALA ALA ILE LEU LYS LEU PHE LEU
SEQRES 8 A 538 GLN LEU LYS ILE LYS GLU GLY LEU GLU LEU GLU LEU LEU
SEQRES 9 A 538 GLY LYS LYS LEU VAL VAL ILE THR GLY HIS SER THR GLY
SEQRES 10 A 538 GLY ALA LEU ALA ALA PHE THR ALA LEU TRP LEU LEU SER
SEQRES 11 A 538 GLN SER SER PRO PRO SER PHE ARG VAL PHE CYS ILE THR
SEQRES 12 A 538 PHE GLY SER PRO LEU LEU GLY ASN GLN SER LEU SER THR
SEQRES 13 A 538 SER ILE SER ARG SER ARG LEU ALA HIS ASN PHE CYS HIS
SEQRES 14 A 538 VAL VAL SER ILE HIS ASP LEU VAL PRO ARG SER SER ASN
SEQRES 15 A 538 GLU GLN PHE TRP PRO PHE GLY THR TYR LEU PHE CYS SER
SEQRES 16 A 538 ASP LYS GLY GLY VAL CYS LEU ASP ASN ALA GLY SER VAL
SEQRES 17 A 538 ARG LEU MET PHE ASN ILE LEU ASN THR THR ALA THR GLN
SEQRES 18 A 538 ASN THR GLU GLU HIS GLN ARG TYR GLY HIS TYR VAL PHE
SEQRES 19 A 538 THR LEU SER HIS MET PHE LEU LYS SER ARG SER PHE LEU
SEQRES 20 A 538 GLY GLY SER ILE PRO ASP ASN SER TYR GLN ALA GLY VAL
SEQRES 21 A 538 ALA LEU ALA VAL GLU ALA LEU GLY PHE SER ASN ASP ASP
SEQRES 22 A 538 THR SER GLY VAL LEU VAL LYS GLU CYS ILE GLU THR ALA
SEQRES 23 A 538 THR ARG ILE VAL ARG ALA PRO ILE LEU ARG SER ALA GLU
SEQRES 24 A 538 LEU ALA ASN GLU LEU ALA SER VAL LEU PRO ALA ARG LEU
SEQRES 25 A 538 GLU ILE GLN TRP TYR LYS ASP ARG CYS ASP ALA SER GLU
SEQRES 26 A 538 GLU GLN LEU GLY TYR TYR ASP PHE PHE LYS ARG TYR SER
SEQRES 27 A 538 LEU LYS ARG ASP PHE LYS VAL ASN MET SER ARG ILE ARG
SEQRES 28 A 538 LEU ALA LYS PHE TRP ASP THR VAL ILE LYS MET VAL GLU
SEQRES 29 A 538 THR ASN GLU LEU PRO PHE ASP PHE HIS LEU GLY LYS LYS
SEQRES 30 A 538 TRP ILE TYR ALA SER GLN PHE TYR GLN LEU LEU ALA GLU
SEQRES 31 A 538 PRO LEU ASP ILE ALA ASN PHE TYR LYS ASN ARG ASP ILE
SEQRES 32 A 538 LYS THR GLY GLY HIS TYR LEU GLU GLY ASN ARG PRO LYS
SEQRES 33 A 538 ARG TYR GLU VAL ILE ASP LYS TRP GLN LYS GLY VAL LYS
SEQRES 34 A 538 VAL PRO GLU GLU CYS VAL ARG SER ARG TYR ALA SER THR
SEQRES 35 A 538 THR GLN ASP THR CYS PHE TRP ALA LYS LEU GLU GLN ALA
SEQRES 36 A 538 LYS GLU TRP LEU ASP GLU ALA ARG LYS GLU SER SER ASP
SEQRES 37 A 538 PRO GLN ARG ARG SER LEU LEU ARG GLU LYS ILE VAL PRO
SEQRES 38 A 538 PHE GLU SER TYR ALA ASN THR LEU VAL THR LYS LYS GLU
SEQRES 39 A 538 VAL SER LEU ASP VAL LYS ALA LYS ASN SER SER TYR SER
SEQRES 40 A 538 VAL TRP GLU ALA ASN LEU LYS GLU PHE LYS CYS LYS MET
SEQRES 41 A 538 GLY TYR GLU ASN GLU ILE GLU MET VAL VAL ASP GLU SER
SEQRES 42 A 538 ASP ALA MET GLU THR
SEQRES 1 B 623 MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 2 B 623 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 3 B 623 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 4 B 623 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 5 B 623 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 6 B 623 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 7 B 623 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 8 B 623 ASN LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN
SEQRES 9 B 623 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 10 B 623 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 11 B 623 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 12 B 623 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 13 B 623 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 14 B 623 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 15 B 623 VAL SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA
SEQRES 16 B 623 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 17 B 623 ALA GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER
SEQRES 18 B 623 GLU GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG
SEQRES 19 B 623 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 20 B 623 THR GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER
SEQRES 21 B 623 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 22 B 623 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 23 B 623 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN
SEQRES 24 B 623 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 25 B 623 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 26 B 623 SER MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 27 B 623 ASN SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER
SEQRES 28 B 623 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 29 B 623 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 30 B 623 VAL ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 31 B 623 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 32 B 623 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 33 B 623 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 34 B 623 GLY VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS
SEQRES 35 B 623 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 36 B 623 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 37 B 623 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 38 B 623 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 39 B 623 ILE TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS
SEQRES 40 B 623 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 41 B 623 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 42 B 623 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 43 B 623 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 44 B 623 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 45 B 623 MET LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP
SEQRES 46 B 623 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 47 B 623 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 48 B 623 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR
HELIX 1 AA1 THR A 8 THR A 19 1 12
HELIX 2 AA2 THR A 19 GLY A 36 1 18
HELIX 3 AA3 ALA A 87 LYS A 97 1 11
HELIX 4 AA4 LYS A 97 LEU A 104 1 8
HELIX 5 AA5 SER A 118 SER A 133 1 16
HELIX 6 AA6 GLN A 155 SER A 164 1 10
HELIX 7 AA7 LEU A 166 HIS A 168 5 3
HELIX 8 AA8 ASN A 207 ALA A 222 1 16
HELIX 9 AA9 THR A 226 GLN A 230 5 5
HELIX 10 AB1 ARG A 231 SER A 240 1 10
HELIX 11 AB2 HIS A 241 LYS A 245 5 5
HELIX 12 AB3 ASN A 257 LEU A 270 1 14
HELIX 13 AB4 ASP A 276 ALA A 326 1 51
HELIX 14 AB5 GLY A 332 ARG A 339 1 8
HELIX 15 AB6 LEU A 342 ASN A 369 1 28
HELIX 16 AB7 GLY A 378 ASN A 403 1 26
HELIX 17 AB8 PRO A 418 GLY A 430 1 13
HELIX 18 AB9 CYS A 450 GLU A 468 1 19
HELIX 19 AC1 ASP A 471 LYS A 495 1 25
HELIX 20 AC2 SER A 499 LYS A 503 5 5
HELIX 21 AC3 SER A 507 LYS A 520 1 14
HELIX 22 AC4 ALA B 2 GLY B 8 1 7
HELIX 23 AC5 ASN B 10 ALA B 24 1 15
HELIX 24 AC6 SER B 48 PHE B 53 1 6
HELIX 25 AC7 GLU B 87 ASP B 98 1 12
HELIX 26 AC8 SER B 102 SER B 113 1 12
HELIX 27 AC9 SER B 123 TYR B 140 1 18
HELIX 28 AD1 ASP B 163 GLU B 173 1 11
HELIX 29 AD2 ILE B 188 MET B 193 1 6
HELIX 30 AD3 ARG B 196 GLU B 201 1 6
HELIX 31 AD4 THR B 203 ASP B 212 1 10
HELIX 32 AD5 GLU B 222 THR B 248 1 27
HELIX 33 AD6 ALA B 251 SER B 260 1 10
HELIX 34 AD7 ASN B 286 THR B 297 1 12
HELIX 35 AD8 ASP B 302 ASP B 316 1 15
HELIX 36 AD9 SER B 319 MET B 327 1 9
HELIX 37 AE1 GLY B 328 LYS B 330 5 3
HELIX 38 AE2 ILE B 341 LEU B 348 1 8
HELIX 39 AE3 SER B 351 GLN B 381 1 31
HELIX 40 AE4 GLN B 381 GLU B 394 1 14
HELIX 41 AE5 GLU B 394 HIS B 402 1 9
HELIX 42 AE6 GLY B 405 VAL B 412 1 8
HELIX 43 AE7 GLU B 415 LYS B 441 1 27
HELIX 44 AE8 PRO B 445 GLY B 450 5 6
HELIX 45 AE9 ASP B 451 HIS B 476 1 26
HELIX 46 AF1 LEU B 477 ASP B 481 5 5
HELIX 47 AF2 PRO B 484 GLY B 489 1 6
HELIX 48 AF3 PRO B 491 LYS B 507 1 17
HELIX 49 AF4 PRO B 508 GLY B 510 5 3
HELIX 50 AF5 ILE B 512 ASN B 525 1 14
HELIX 51 AF6 GLN B 529 LEU B 537 1 9
HELIX 52 AF7 CYS B 544 SER B 546 5 3
HELIX 53 AF8 CYS B 547 LYS B 556 1 10
HELIX 54 AF9 PRO B 559 GLU B 562 5 4
HELIX 55 AG1 VAL B 563 ASP B 580 1 18
HELIX 56 AG2 ASP B 584 PHE B 589 1 6
HELIX 57 AG3 SER B 593 ILE B 600 1 8
HELIX 58 AG4 PRO B 603 SER B 610 1 8
SHEET 1 AA1 7 LYS A 39 ILE A 43 0
SHEET 2 AA1 7 ILE A 46 ILE A 51 -1 O TYR A 48 N HIS A 41
SHEET 3 AA1 7 LEU A 111 HIS A 117 1 O VAL A 113 N THR A 47
SHEET 4 AA1 7 ARG A 141 PHE A 147 1 O PHE A 143 N ILE A 114
SHEET 5 AA1 7 PHE A 170 SER A 175 1 O CYS A 171 N THR A 146
SHEET 6 AA1 7 THR A 193 CYS A 197 1 O LEU A 195 N VAL A 174
SHEET 7 AA1 7 GLY A 202 LEU A 205 -1 O LEU A 205 N TYR A 194
SHEET 1 AA2 2 LEU A 62 GLY A 64 0
SHEET 2 AA2 2 MET A 84 ASP A 86 -1 O VAL A 85 N VAL A 63
SHEET 1 AA3 2 GLY A 153 ASN A 154 0
SHEET 2 AA3 2 PHE A 188 TRP A 189 -1 O TRP A 189 N GLY A 153
SHEET 1 AA4 8 HIS B 31 ALA B 35 0
SHEET 2 AA4 8 VAL B 38 PHE B 43 -1 O ILE B 40 N GLU B 33
SHEET 3 AA4 8 GLN B 116 HIS B 122 1 O VAL B 118 N PHE B 41
SHEET 4 AA4 8 ARG B 152 PHE B 156 1 O ARG B 152 N PHE B 119
SHEET 5 AA4 8 PHE B 179 SER B 184 1 O VAL B 180 N THR B 155
SHEET 6 AA4 8 THR B 272 SER B 276 1 O VAL B 274 N VAL B 183
SHEET 7 AA4 8 ARG B 280 VAL B 284 -1 O VAL B 284 N PHE B 273
SHEET 8 AA4 8 LEU B 331 HIS B 334 1 O ASN B 333 N ALA B 283
SHEET 1 AA5 2 GLU B 63 LYS B 65 0
SHEET 2 AA5 2 THR B 84 ASN B 86 -1 O VAL B 85 N ILE B 64
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 4063 LYS A 520
TER 9023 ASP B 618
MASTER 172 0 0 58 21 0 0 6 9021 2 0 90
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