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HEADER PLANT PROTEIN 15-MAR-25 9MB8
TITLE THE COMPLEX OF D14 AND RGSV P3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: PROTEIN DWARF 14,PROTEIN DWARF 88,PROTEIN HIGH-TILLERING
COMPND 5 DWARF 2;
COMPND 6 EC: 3.1.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: P3;
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: D14, D88, HTD2, OS03G0203200, LOC_OS03G10620;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: TENUIVIRUS ORYZABREVIS;
SOURCE 10 ORGANISM_TAXID: 3052762;
SOURCE 11 GENE: P3V, P3;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DAWRF14, PLANT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.C.HUANG
REVDAT 1 04-MAR-26 9MB8 0
JRNL AUTH G.YANG,M.WU,S.ZHANG,Y.HUANG,Y.LIU,X.YU,J.HU,L.MI,P.GAN,Y.WU,
JRNL AUTH 2 J.ZOU,B.ZHANG,Q.HU,J.HU,R.YAO,B.ZHONG,X.HUANG,H.XIE,Y.JI,
JRNL AUTH 3 Y.LI,J.ZHANG,L.YAN,S.W.DING,S.ZHAO,J.WU
JRNL TITL EDITING STRIGOLACTONE HORMONE RECEPTOR FOR ROBUST ANTIVIRAL
JRNL TITL 2 SILENCING IN RICE
JRNL REF CELL(CAMBRIDGE,MASS.) 2026
JRNL REFN ISSN 0092-8674
JRNL DOI 10.1016/J.CELL.2026.01.013
REMARK 2
REMARK 2 RESOLUTION. 3.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC
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) : 3.670
REMARK 3 NUMBER OF PARTICLES : 103509
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 9MB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1300057563.
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 : THE COMPLEX OF D14 AND RGSV P3
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 : 7.00
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 : TFS 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) : 6000.00
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A, D
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 C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 SER C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 SER C 7
REMARK 465 SER C 8
REMARK 465 MET C 9
REMARK 465 ASP C 10
REMARK 465 ILE C 11
REMARK 465 TYR C 12
REMARK 465 GLY C 13
REMARK 465 ASN C 14
REMARK 465 VAL C 15
REMARK 465 ARG C 16
REMARK 465 PRO C 17
REMARK 465 GLN C 18
REMARK 465 ASN C 19
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 SER D 4
REMARK 465 SER D 5
REMARK 465 SER D 6
REMARK 465 SER D 7
REMARK 465 SER D 8
REMARK 465 MET D 9
REMARK 465 ASP D 10
REMARK 465 ILE D 11
REMARK 465 TYR D 12
REMARK 465 GLY D 13
REMARK 465 ASN D 14
REMARK 465 VAL D 15
REMARK 465 ARG D 16
REMARK 465 PRO D 17
REMARK 465 GLN D 18
REMARK 465 ASN D 19
REMARK 465 HIS D 196
REMARK 465 HIS D 197
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 OG1 THR D 21 NH1 ARG D 46 2.15
REMARK 500 OD1 ASN C 51 NH2 ARG C 54 2.16
REMARK 500 O ILE D 61 OH TYR D 104 2.16
REMARK 500 O HIS A 146 OG SER A 149 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 50 CA - N - CD ANGL. DEV. = -8.8 DEGREES
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 ALA B 54 -4.38 68.33
REMARK 500 ASP B 81 -167.12 -77.19
REMARK 500 SER B 86 -103.69 43.98
REMARK 500 SER B 108 -74.12 42.09
REMARK 500 SER B 147 -124.24 56.26
REMARK 500 ARG B 159 -163.68 -77.99
REMARK 500 ARG B 160 112.51 -39.19
REMARK 500 PRO B 272 173.35 -57.76
REMARK 500 LEU B 298 76.81 -113.50
REMARK 500 ALA B 316 -165.68 -79.16
REMARK 500 ASP C 23 -8.58 72.14
REMARK 500 ASP C 24 175.93 57.75
REMARK 500 GLU C 25 32.14 -143.44
REMARK 500 ARG C 26 157.53 69.27
REMARK 500 TYR C 27 135.68 84.27
REMARK 500 MET C 28 49.90 -95.29
REMARK 500 TYR C 104 -154.28 59.74
REMARK 500 ASN C 105 23.62 -140.22
REMARK 500 TYR C 115 52.43 -96.70
REMARK 500 ASN C 127 52.65 -95.39
REMARK 500 TYR C 142 52.30 -91.81
REMARK 500 LEU C 145 -7.92 68.00
REMARK 500 LEU C 154 124.22 -39.69
REMARK 500 ALA A 54 -64.20 61.57
REMARK 500 SER A 86 -103.34 44.27
REMARK 500 VAL A 104 -9.97 -59.23
REMARK 500 SER A 108 -75.47 43.45
REMARK 500 SER A 147 -124.84 55.24
REMARK 500 ARG A 159 -163.94 -79.08
REMARK 500 ARG A 160 112.48 -38.89
REMARK 500 LEU A 298 72.99 -112.96
REMARK 500 ALA A 316 -165.61 -79.11
REMARK 500 ALA D 22 -176.73 -65.20
REMARK 500 ASP D 23 135.13 -34.45
REMARK 500 ARG D 26 -159.12 67.72
REMARK 500 TYR D 27 -5.70 77.41
REMARK 500 MET D 28 4.70 55.78
REMARK 500 ASP D 45 56.12 -94.78
REMARK 500 TYR D 104 -155.75 57.16
REMARK 500 ASN D 105 15.69 -140.14
REMARK 500 TYR D 115 51.63 -95.94
REMARK 500 PRO D 124 -8.20 -55.18
REMARK 500 ASN D 127 49.24 -91.66
REMARK 500 TYR D 142 53.69 -90.81
REMARK 500 LEU D 145 -4.91 67.47
REMARK 500 LEU D 154 127.82 -38.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-63769 RELATED DB: EMDB
REMARK 900 THE COMPLEX OF D14 AND RGSV P3
DBREF 9MB8 B 54 318 UNP Q10QA5 D14_ORYSJ 54 318
DBREF 9MB8 C 1 195 UNP E5AXV2 E5AXV2_9VIRU 1 195
DBREF 9MB8 A 54 318 UNP Q10QA5 D14_ORYSJ 54 318
DBREF 9MB8 D 1 195 UNP E5AXV2 E5AXV2_9VIRU 1 195
SEQADV 9MB8 GLY B 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 PRO B 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 LEU B 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 GLY B 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 SER B 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 HIS C 196 UNP E5AXV2 EXPRESSION TAG
SEQADV 9MB8 HIS C 197 UNP E5AXV2 EXPRESSION TAG
SEQADV 9MB8 GLY A 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 PRO A 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 LEU A 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 GLY A 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 SER A 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 9MB8 HIS D 196 UNP E5AXV2 EXPRESSION TAG
SEQADV 9MB8 HIS D 197 UNP E5AXV2 EXPRESSION TAG
SEQRES 1 B 270 GLY PRO LEU GLY SER ALA LYS LEU LEU GLN ILE LEU ASN
SEQRES 2 B 270 VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU
SEQRES 3 B 270 SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG
SEQRES 4 B 270 VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU
SEQRES 5 B 270 TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS
SEQRES 6 B 270 PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL
SEQRES 7 B 270 ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO
SEQRES 8 B 270 ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE
SEQRES 9 B 270 GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA
SEQRES 10 B 270 LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN
SEQRES 11 B 270 ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE
SEQRES 12 B 270 GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA
SEQRES 13 B 270 TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP
SEQRES 14 B 270 VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE
SEQRES 15 B 270 ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR
SEQRES 16 B 270 VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL
SEQRES 17 B 270 ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL
SEQRES 18 B 270 SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS
SEQRES 19 B 270 LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU
SEQRES 20 B 270 GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA
SEQRES 21 B 270 GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 C 197 MET SER LEU SER SER SER SER SER MET ASP ILE TYR GLY
SEQRES 2 C 197 ASN VAL ARG PRO GLN ASN TRP THR ALA ASP ASP GLU ARG
SEQRES 3 C 197 TYR MET LEU SER LEU SER GLY LEU ARG ARG PHE LEU GLU
SEQRES 4 C 197 TYR ILE PRO HIS SER ASP ARG LEU THR VAL LEU ASN TRP
SEQRES 5 C 197 THR ARG HIS MET ALA ALA ASN ASP ILE GLN ILE GLY ALA
SEQRES 6 C 197 LEU ASN ALA PHE ARG LYS LYS VAL CYS ASP ILE MET TYR
SEQRES 7 C 197 GLU THR LYS ASP LYS ARG ILE ASN ASN GLU LEU MET LYS
SEQRES 8 C 197 LEU TYR ASN GLU LEU TRP SER LYS THR SER SER ILE TYR
SEQRES 9 C 197 ASN ILE THR PRO CYS THR THR CYS GLU ILE TYR LYS LYS
SEQRES 10 C 197 GLU LEU SER GLN ARG VAL PRO GLU SER ASN ILE ARG TYR
SEQRES 11 C 197 GLU THR GLN PHE ILE ASP SER ARG VAL PRO ILE TYR GLN
SEQRES 12 C 197 PHE LEU THR PRO ASN ASN VAL SER VAL VAL LEU VAL GLN
SEQRES 13 C 197 HIS GLY ASN ASP LEU PRO ASP LEU ASN PHE PRO ARG TYR
SEQRES 14 C 197 VAL PRO LEU GLY GLN PRO ARG HIS LYS ILE ALA TYR TYR
SEQRES 15 C 197 SER ASP SER ARG MET ILE GLY GLN PHE LEU ARG ILE ASP
SEQRES 16 C 197 HIS HIS
SEQRES 1 A 270 GLY PRO LEU GLY SER ALA LYS LEU LEU GLN ILE LEU ASN
SEQRES 2 A 270 VAL ARG VAL VAL GLY SER GLY GLU ARG VAL VAL VAL LEU
SEQRES 3 A 270 SER HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG
SEQRES 4 A 270 VAL LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU
SEQRES 5 A 270 TYR ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP HIS
SEQRES 6 A 270 PHE ASP PHE ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL
SEQRES 7 A 270 ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO
SEQRES 8 A 270 ARG CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE
SEQRES 9 A 270 GLY ILE LEU ALA SER ILE ARG ARG PRO ASP LEU PHE ALA
SEQRES 10 A 270 LYS LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN
SEQRES 11 A 270 ASP SER ASP TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE
SEQRES 12 A 270 GLN GLN VAL PHE ASP ALA MET GLY ALA ASN TYR SER ALA
SEQRES 13 A 270 TRP ALA THR GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP
SEQRES 14 A 270 VAL PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE
SEQRES 15 A 270 ASN MET ARG PRO ASP ILE SER LEU HIS VAL CYS GLN THR
SEQRES 16 A 270 VAL PHE LYS THR ASP LEU ARG GLY VAL LEU GLY MET VAL
SEQRES 17 A 270 ARG ALA PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL
SEQRES 18 A 270 SER VAL PRO ALA SER VAL ALA ALA TYR LEU LYS ALA HIS
SEQRES 19 A 270 LEU GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU
SEQRES 20 A 270 GLY HIS LEU PRO HIS LEU SER ALA PRO SER LEU LEU ALA
SEQRES 21 A 270 GLN VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 D 197 MET SER LEU SER SER SER SER SER MET ASP ILE TYR GLY
SEQRES 2 D 197 ASN VAL ARG PRO GLN ASN TRP THR ALA ASP ASP GLU ARG
SEQRES 3 D 197 TYR MET LEU SER LEU SER GLY LEU ARG ARG PHE LEU GLU
SEQRES 4 D 197 TYR ILE PRO HIS SER ASP ARG LEU THR VAL LEU ASN TRP
SEQRES 5 D 197 THR ARG HIS MET ALA ALA ASN ASP ILE GLN ILE GLY ALA
SEQRES 6 D 197 LEU ASN ALA PHE ARG LYS LYS VAL CYS ASP ILE MET TYR
SEQRES 7 D 197 GLU THR LYS ASP LYS ARG ILE ASN ASN GLU LEU MET LYS
SEQRES 8 D 197 LEU TYR ASN GLU LEU TRP SER LYS THR SER SER ILE TYR
SEQRES 9 D 197 ASN ILE THR PRO CYS THR THR CYS GLU ILE TYR LYS LYS
SEQRES 10 D 197 GLU LEU SER GLN ARG VAL PRO GLU SER ASN ILE ARG TYR
SEQRES 11 D 197 GLU THR GLN PHE ILE ASP SER ARG VAL PRO ILE TYR GLN
SEQRES 12 D 197 PHE LEU THR PRO ASN ASN VAL SER VAL VAL LEU VAL GLN
SEQRES 13 D 197 HIS GLY ASN ASP LEU PRO ASP LEU ASN PHE PRO ARG TYR
SEQRES 14 D 197 VAL PRO LEU GLY GLN PRO ARG HIS LYS ILE ALA TYR TYR
SEQRES 15 D 197 SER ASP SER ARG MET ILE GLY GLN PHE LEU ARG ILE ASP
SEQRES 16 D 197 HIS HIS
HELIX 1 AA1 LYS B 55 ASN B 61 1 7
HELIX 2 AA2 ASP B 81 SER B 86 1 6
HELIX 3 AA3 ARG B 87 LEU B 92 1 6
HELIX 4 AA4 ASN B 110 PHE B 114 5 5
HELIX 5 AA5 ASN B 121 LEU B 136 1 16
HELIX 6 AA6 SER B 147 ARG B 159 1 13
HELIX 7 AA7 ARG B 160 ASP B 162 5 3
HELIX 8 AA8 GLU B 187 ASN B 201 1 15
HELIX 9 AA9 ASN B 201 GLY B 215 1 15
HELIX 10 AB1 VAL B 218 ASN B 231 1 14
HELIX 11 AB2 ARG B 233 PHE B 245 1 13
HELIX 12 AB3 LYS B 246 ASP B 248 5 3
HELIX 13 AB4 LEU B 249 GLY B 254 1 6
HELIX 14 AB5 ALA B 273 HIS B 282 1 10
HELIX 15 AB6 LEU B 298 ALA B 303 1 6
HELIX 16 AB7 ALA B 303 LEU B 315 1 13
HELIX 17 AB8 ARG C 35 GLU C 39 5 5
HELIX 18 AB9 ARG C 46 ALA C 58 1 13
HELIX 19 AC1 GLN C 62 LYS C 81 1 20
HELIX 20 AC2 LYS C 83 ILE C 103 1 21
HELIX 21 AC3 CYS C 109 TYR C 115 1 7
HELIX 22 AC4 TYR C 115 SER C 120 1 6
HELIX 23 AC5 ALA A 54 ASN A 61 1 8
HELIX 24 AC6 ASP A 81 SER A 86 1 6
HELIX 25 AC7 ARG A 87 LEU A 92 1 6
HELIX 26 AC8 ASN A 110 PHE A 114 5 5
HELIX 27 AC9 ASN A 121 LEU A 136 1 16
HELIX 28 AD1 SER A 147 ARG A 159 1 13
HELIX 29 AD2 GLU A 187 ASN A 201 1 15
HELIX 30 AD3 TYR A 202 GLY A 215 1 14
HELIX 31 AD4 VAL A 218 ASN A 231 1 14
HELIX 32 AD5 ARG A 233 LYS A 246 1 14
HELIX 33 AD6 LEU A 249 VAL A 256 5 8
HELIX 34 AD7 ALA A 273 HIS A 282 1 10
HELIX 35 AD8 LEU A 298 ALA A 303 1 6
HELIX 36 AD9 ALA A 303 LEU A 315 1 13
HELIX 37 AE1 GLY D 33 LEU D 38 1 6
HELIX 38 AE2 HIS D 43 ASP D 45 5 3
HELIX 39 AE3 ARG D 46 ALA D 58 1 13
HELIX 40 AE4 GLN D 62 LYS D 81 1 20
HELIX 41 AE5 LYS D 83 ILE D 103 1 21
HELIX 42 AE6 CYS D 109 TYR D 115 1 7
HELIX 43 AE7 TYR D 115 GLN D 121 1 7
SHEET 1 AA1 6 PHE B 164 LEU B 167 0
SHEET 2 AA1 6 CYS B 141 VAL B 144 1 N CYS B 141 O ALA B 165
SHEET 3 AA1 6 VAL B 71 LEU B 74 1 N VAL B 73 O VAL B 144
SHEET 4 AA1 6 ARG B 97 VAL B 99 1 O VAL B 99 N VAL B 72
SHEET 5 AA1 6 VAL B 64 GLY B 66 -1 N VAL B 65 O VAL B 98
SHEET 6 AA1 6 TYR C 130 THR C 132 -1 O THR C 132 N VAL B 64
SHEET 1 AA2 2 CYS B 260 THR B 265 0
SHEET 2 AA2 2 THR B 287 LEU B 292 1 O LEU B 292 N GLN B 264
SHEET 1 AA3 3 ILE C 135 ASP C 136 0
SHEET 2 AA3 3 SER C 151 VAL C 152 -1 O VAL C 152 N ILE C 135
SHEET 3 AA3 3 TYR C 181 TYR C 182 -1 O TYR C 182 N SER C 151
SHEET 1 AA4 2 TYR C 169 PRO C 171 0
SHEET 2 AA4 2 LEU C 192 ILE C 194 -1 O ARG C 193 N VAL C 170
SHEET 1 AA5 6 PHE A 164 LEU A 167 0
SHEET 2 AA5 6 CYS A 141 VAL A 144 1 N CYS A 141 O ALA A 165
SHEET 3 AA5 6 VAL A 71 LEU A 74 1 N VAL A 73 O VAL A 144
SHEET 4 AA5 6 ARG A 97 VAL A 99 1 O VAL A 99 N VAL A 72
SHEET 5 AA5 6 VAL A 64 GLY A 66 -1 N VAL A 65 O VAL A 98
SHEET 6 AA5 6 TYR D 130 THR D 132 -1 O THR D 132 N VAL A 64
SHEET 1 AA6 2 CYS A 260 THR A 265 0
SHEET 2 AA6 2 THR A 287 LEU A 292 1 O GLU A 290 N VAL A 262
SHEET 1 AA7 3 ILE D 135 ASP D 136 0
SHEET 2 AA7 3 SER D 151 VAL D 152 -1 O VAL D 152 N ILE D 135
SHEET 3 AA7 3 TYR D 181 TYR D 182 -1 O TYR D 182 N SER D 151
SHEET 1 AA8 2 TYR D 169 PRO D 171 0
SHEET 2 AA8 2 LEU D 192 ILE D 194 -1 O ARG D 193 N VAL D 170
SSBOND 1 CYS C 109 CYS C 112 1555 1555 2.03
SSBOND 2 CYS D 109 CYS D 112 1555 1555 2.03
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 2080 TYR B 318
TER 3568 HIS C 197
TER 5648 TYR A 318
TER 7116 ASP D 195
MASTER 239 0 0 43 26 0 0 6 7112 4 4 74
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