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HEADER HYDROLASE 21-MAY-23 8JGM
TITLE CRYO-EM STURCUTRE OF DANGEROUS MIX 3 (DM3) FROM HOHENLIETH (HH-0)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DM3HH0;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: DANGGEROUS MIX 3, DM3;
COMPND 5 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 VARIANT: HOHENLIETH ACCESSION (HH-0);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, COMPLEX, POLYMORPHISM, HYBRID NECROSIS
EXPDTA ELECTRON MICROSCOPY
AUTHOR G.KIM,J.J.SONG
REVDAT 1 25-DEC-24 8JGM 0
JRNL AUTH G.KIM,J.J.SONG
JRNL TITL CRYO-EM STURCUTRE OF DANGEROUS MIX 3 (DM3) FROM HOHENLIETH
JRNL TITL 2 (HH-0)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.89 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) : 2.890
REMARK 3 NUMBER OF PARTICLES : 413056
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 8JGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1300037447.
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 : DANGGEROUS MIX 3 (DM3) FROM
REMARK 245 HOHENLIETH ACCESSION (HH-0)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.17
REMARK 245 SAMPLE SUPPORT DETAILS : THE GRID TREATED BY GRAPHENE
REMARK 245 OXIDE PRIOR TO USE
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 : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 900.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2300.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4980.00
REMARK 245 ILLUMINATION MODE : OTHER
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 LEU A 335
REMARK 465 VAL A 336
REMARK 465 THR A 337
REMARK 465 GLY A 338
REMARK 465 ALA A 339
REMARK 465 PRO A 340
REMARK 465 LEU B 335
REMARK 465 VAL B 336
REMARK 465 THR B 337
REMARK 465 GLY B 338
REMARK 465 ALA B 339
REMARK 465 PRO B 340
REMARK 465 LEU C 335
REMARK 465 VAL C 336
REMARK 465 THR C 337
REMARK 465 GLY C 338
REMARK 465 ALA C 339
REMARK 465 PRO C 340
REMARK 465 LEU D 335
REMARK 465 VAL D 336
REMARK 465 THR D 337
REMARK 465 GLY D 338
REMARK 465 ALA D 339
REMARK 465 PRO D 340
REMARK 465 LEU E 335
REMARK 465 VAL E 336
REMARK 465 THR E 337
REMARK 465 GLY E 338
REMARK 465 ALA E 339
REMARK 465 PRO E 340
REMARK 465 LEU F 335
REMARK 465 VAL F 336
REMARK 465 THR F 337
REMARK 465 GLY F 338
REMARK 465 ALA F 339
REMARK 465 PRO F 340
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 SER A 167 -53.22 66.20
REMARK 500 SER A 214 -118.76 52.11
REMARK 500 SER A 401 19.96 59.91
REMARK 500 GLU B 147 -24.38 -140.95
REMARK 500 SER B 167 -57.29 69.39
REMARK 500 SER B 214 -119.36 49.72
REMARK 500 ARG B 329 41.24 -102.91
REMARK 500 GLU B 436 21.49 -145.98
REMARK 500 CYS C 166 -35.76 -137.42
REMARK 500 MET C 169 164.35 175.10
REMARK 500 SER C 214 -117.46 51.75
REMARK 500 ALA C 375 -142.70 49.85
REMARK 500 CYS D 166 -152.67 -117.23
REMARK 500 SER D 167 -63.40 72.79
REMARK 500 SER D 168 58.35 -97.54
REMARK 500 MET D 169 -136.22 42.42
REMARK 500 SER D 214 -113.84 53.59
REMARK 500 GLU E 147 -30.63 -135.34
REMARK 500 MET E 169 162.40 175.35
REMARK 500 LEU E 170 152.88 -48.55
REMARK 500 SER E 214 -116.93 49.78
REMARK 500 ALA E 227 59.17 -151.10
REMARK 500 ARG E 329 42.08 -109.01
REMARK 500 SER E 401 19.81 58.10
REMARK 500 GLU F 147 -30.94 -135.34
REMARK 500 THR F 162 67.34 60.02
REMARK 500 SER F 214 -118.66 50.99
REMARK 500 SER F 401 19.90 59.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-36239 RELATED DB: EMDB
REMARK 900 CRYO-EM STURCUTRE OF DANGEROUS MIX 3 (DM3) FROM HOHENLIETH (HH-0)
DBREF1 8JGM A 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM A A0A068LMZ4 68 515
DBREF1 8JGM B 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM B A0A068LMZ4 68 515
DBREF1 8JGM C 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM C A0A068LMZ4 68 515
DBREF1 8JGM D 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM D A0A068LMZ4 68 515
DBREF1 8JGM E 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM E A0A068LMZ4 68 515
DBREF1 8JGM F 68 515 UNP A0A068LMZ4_ARATH
DBREF2 8JGM F A0A068LMZ4 68 515
SEQRES 1 A 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 A 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 A 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 A 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 A 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 A 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 A 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 A 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 A 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 A 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 A 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 A 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 A 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 A 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 A 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 A 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 A 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 A 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 A 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 A 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 A 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 A 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 A 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 A 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 A 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 A 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 A 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 A 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 A 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 A 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 A 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 A 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 A 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 A 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 A 448 GLY LYS LYS PRO LEU PHE
SEQRES 1 B 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 B 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 B 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 B 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 B 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 B 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 B 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 B 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 B 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 B 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 B 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 B 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 B 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 B 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 B 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 B 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 B 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 B 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 B 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 B 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 B 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 B 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 B 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 B 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 B 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 B 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 B 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 B 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 B 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 B 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 B 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 B 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 B 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 B 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 B 448 GLY LYS LYS PRO LEU PHE
SEQRES 1 C 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 C 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 C 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 C 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 C 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 C 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 C 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 C 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 C 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 C 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 C 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 C 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 C 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 C 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 C 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 C 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 C 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 C 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 C 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 C 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 C 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 C 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 C 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 C 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 C 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 C 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 C 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 C 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 C 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 C 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 C 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 C 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 C 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 C 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 C 448 GLY LYS LYS PRO LEU PHE
SEQRES 1 D 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 D 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 D 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 D 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 D 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 D 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 D 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 D 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 D 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 D 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 D 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 D 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 D 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 D 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 D 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 D 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 D 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 D 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 D 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 D 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 D 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 D 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 D 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 D 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 D 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 D 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 D 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 D 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 D 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 D 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 D 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 D 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 D 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 D 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 D 448 GLY LYS LYS PRO LEU PHE
SEQRES 1 E 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 E 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 E 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 E 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 E 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 E 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 E 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 E 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 E 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 E 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 E 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 E 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 E 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 E 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 E 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 E 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 E 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 E 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 E 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 E 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 E 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 E 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 E 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 E 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 E 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 E 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 E 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 E 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 E 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 E 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 E 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 E 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 E 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 E 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 E 448 GLY LYS LYS PRO LEU PHE
SEQRES 1 F 448 GLU HIS VAL THR GLY LYS TRP PHE SER VAL PRO GLU LEU
SEQRES 2 F 448 ARG LEU ARG ASP HIS ARG PHE ILE VAL PRO LEU ASP TYR
SEQRES 3 F 448 SER LYS SER SER PRO LYS ILE THR VAL PHE ALA ARG GLU
SEQRES 4 F 448 ILE VAL ALA VAL GLY LYS GLU GLU GLN ALA MET PRO TYR
SEQRES 5 F 448 LEU LEU TYR LEU GLN GLY GLY PRO GLY PHE GLU GLY PRO
SEQRES 6 F 448 ARG PRO SER GLU ALA SER GLY TRP ILE GLN ARG ALA CYS
SEQRES 7 F 448 GLU GLU PHE ARG VAL VAL LEU LEU ASP GLN ARG GLY THR
SEQRES 8 F 448 GLY LEU SER THR PRO LEU ILE CYS SER SER MET LEU GLN
SEQRES 9 F 448 PHE LYS SER ALA LYS GLU LEU ALA ASP TYR LEU VAL HIS
SEQRES 10 F 448 PHE ARG ALA ASP ASN ILE VAL LYS ASP ALA GLU PHE ILE
SEQRES 11 F 448 ARG VAL ARG LEU VAL PRO LYS ALA ASP PRO TRP THR ILE
SEQRES 12 F 448 LEU GLY GLN SER PHE GLY GLY PHE CYS ALA LEU THR TYR
SEQRES 13 F 448 LEU SER PHE ALA PRO GLU GLY LEU LYS GLN VAL LEU ILE
SEQRES 14 F 448 THR GLY GLY ILE PRO PRO ILE GLY LYS ALA CYS THR ALA
SEQRES 15 F 448 ASP ASP VAL TYR GLU ALA GLY PHE GLU GLN VAL ALA ARG
SEQRES 16 F 448 GLN ASN GLU LYS TYR TYR LYS ARG PHE PRO GLN ASP ILE
SEQRES 17 F 448 GLU ILE VAL ARG GLU LEU VAL ASN TYR LEU ALA GLU SER
SEQRES 18 F 448 GLU GLY GLY GLY VAL PRO LEU PRO SER GLY GLY ILE LEU
SEQRES 19 F 448 THR PRO LYS GLY LEU GLN THR LEU GLY LEU SER GLY LEU
SEQRES 20 F 448 GLY SER SER THR GLY PHE GLU ARG LEU HIS TYR MET LEU
SEQRES 21 F 448 GLU ARG VAL TRP ASP PRO ILE LEU VAL THR GLY ALA PRO
SEQRES 22 F 448 LYS CYS ILE SER GLN PHE PHE LEU ASN ALA PHE GLU SER
SEQRES 23 F 448 TRP HIS SER PHE ASP ALA ASN PRO LEU TYR ALA LEU LEU
SEQRES 24 F 448 HIS GLU ALA ILE TYR CYS GLU GLY ALA SER SER GLY TRP
SEQRES 25 F 448 SER ALA HIS ARG LEU ARG ASP LYS TYR GLU TYR LYS PHE
SEQRES 26 F 448 ASP ALA MET LYS ALA VAL LYS GLU SER GLN PRO VAL LEU
SEQRES 27 F 448 PHE THR GLY GLU MET ILE PHE PRO TRP MET PHE ASP GLU
SEQRES 28 F 448 ILE HIS ALA LEU LYS PRO PHE LYS ALA ALA ALA ASP LEU
SEQRES 29 F 448 LEU ALA LYS LYS GLU ASP TRP PRO PRO LEU TYR ASP VAL
SEQRES 30 F 448 PRO ARG LEU GLN ASN ASN LYS VAL PRO VAL ALA ALA ALA
SEQRES 31 F 448 VAL TYR TYR GLU ASP MET TYR VAL ASN PHE LYS LEU VAL
SEQRES 32 F 448 THR GLU THR ALA SER HIS ILE SER GLY ILE ARG LEU TRP
SEQRES 33 F 448 VAL THR ASN GLU PHE MET HIS SER GLY LEU ARG ASP ALA
SEQRES 34 F 448 GLY ARG GLN ILE ILE ASP HIS LEU LEU GLY MET ILE ASN
SEQRES 35 F 448 GLY LYS LYS PRO LEU PHE
HELIX 1 AA1 SER A 138 GLU A 146 1 9
HELIX 2 AA2 SER A 174 VAL A 183 1 10
HELIX 3 AA3 ARG A 186 VAL A 202 1 17
HELIX 4 AA4 SER A 214 PHE A 226 1 13
HELIX 5 AA5 ALA A 227 GLU A 229 5 3
HELIX 6 AA6 THR A 248 PHE A 271 1 24
HELIX 7 AA7 GLN A 273 SER A 288 1 16
HELIX 8 AA8 THR A 302 THR A 308 1 7
HELIX 9 AA9 LEU A 309 LEU A 314 1 6
HELIX 10 AB1 THR A 318 GLU A 328 1 11
HELIX 11 AB2 SER A 344 TRP A 354 1 11
HELIX 12 AB3 PRO A 361 HIS A 367 1 7
HELIX 13 AB4 GLU A 368 CYS A 372 5 5
HELIX 14 AB5 TRP A 379 ASP A 386 1 8
HELIX 15 AB6 TYR A 388 ASP A 393 1 6
HELIX 16 AB7 ASP A 393 GLU A 400 1 8
HELIX 17 AB8 TRP A 414 ILE A 419 1 6
HELIX 18 AB9 HIS A 420 PRO A 424 5 5
HELIX 19 AC1 PHE A 425 LYS A 435 1 11
HELIX 20 AC2 ASP A 443 GLN A 448 1 6
HELIX 21 AC3 ASN A 466 ALA A 474 1 9
HELIX 22 AC4 ALA A 496 ASN A 509 1 14
HELIX 23 AC5 SER B 138 CYS B 145 1 8
HELIX 24 AC6 SER B 174 VAL B 183 1 10
HELIX 25 AC7 ARG B 186 VAL B 202 1 17
HELIX 26 AC8 SER B 214 PHE B 226 1 13
HELIX 27 AC9 ALA B 227 GLU B 229 5 3
HELIX 28 AD1 THR B 248 PHE B 271 1 24
HELIX 29 AD2 GLN B 273 SER B 288 1 16
HELIX 30 AD3 GLU B 289 GLY B 292 5 4
HELIX 31 AD4 THR B 302 THR B 308 1 7
HELIX 32 AD5 LEU B 309 LEU B 314 1 6
HELIX 33 AD6 THR B 318 GLU B 328 1 11
HELIX 34 AD7 SER B 344 TRP B 354 1 11
HELIX 35 AD8 ASN B 360 LEU B 366 1 7
HELIX 36 AD9 GLU B 368 CYS B 372 5 5
HELIX 37 AE1 TRP B 379 ASP B 386 1 8
HELIX 38 AE2 TYR B 388 ASP B 393 1 6
HELIX 39 AE3 ASP B 393 GLU B 400 1 8
HELIX 40 AE4 TRP B 414 ILE B 419 1 6
HELIX 41 AE5 HIS B 420 PRO B 424 5 5
HELIX 42 AE6 PHE B 425 LYS B 435 1 11
HELIX 43 AE7 ASP B 443 GLN B 448 1 6
HELIX 44 AE8 ASN B 466 ALA B 474 1 9
HELIX 45 AE9 SER B 475 ILE B 477 5 3
HELIX 46 AF1 ALA B 496 ASN B 509 1 14
HELIX 47 AF2 SER C 138 CYS C 145 1 8
HELIX 48 AF3 SER C 174 VAL C 183 1 10
HELIX 49 AF4 ARG C 186 VAL C 202 1 17
HELIX 50 AF5 SER C 214 PHE C 226 1 13
HELIX 51 AF6 ALA C 227 GLU C 229 5 3
HELIX 52 AF7 THR C 248 PHE C 271 1 24
HELIX 53 AF8 GLN C 273 SER C 288 1 16
HELIX 54 AF9 GLU C 289 GLY C 292 5 4
HELIX 55 AG1 THR C 302 THR C 308 1 7
HELIX 56 AG2 LEU C 309 LEU C 314 1 6
HELIX 57 AG3 THR C 318 GLU C 328 1 11
HELIX 58 AG4 SER C 344 SER C 353 1 10
HELIX 59 AG5 ASN C 360 LEU C 366 1 7
HELIX 60 AG6 GLU C 368 CYS C 372 5 5
HELIX 61 AG7 TRP C 379 ASP C 393 1 15
HELIX 62 AG8 ASP C 393 GLU C 400 1 8
HELIX 63 AG9 TRP C 414 ILE C 419 1 6
HELIX 64 AH1 HIS C 420 PRO C 424 5 5
HELIX 65 AH2 PHE C 425 LYS C 435 1 11
HELIX 66 AH3 ASP C 443 GLN C 448 1 6
HELIX 67 AH4 ASN C 466 ALA C 474 1 9
HELIX 68 AH5 GLY C 497 ASN C 509 1 13
HELIX 69 AH6 SER D 138 CYS D 145 1 8
HELIX 70 AH7 SER D 174 VAL D 183 1 10
HELIX 71 AH8 ARG D 186 VAL D 202 1 17
HELIX 72 AH9 SER D 214 PHE D 226 1 13
HELIX 73 AI1 ALA D 227 GLU D 229 5 3
HELIX 74 AI2 THR D 248 PHE D 271 1 24
HELIX 75 AI3 GLN D 273 SER D 288 1 16
HELIX 76 AI4 THR D 302 THR D 308 1 7
HELIX 77 AI5 LEU D 309 LEU D 314 1 6
HELIX 78 AI6 THR D 318 GLU D 328 1 11
HELIX 79 AI7 SER D 344 SER D 353 1 10
HELIX 80 AI8 PRO D 361 HIS D 367 1 7
HELIX 81 AI9 GLU D 368 CYS D 372 5 5
HELIX 82 AJ1 TRP D 379 ASP D 393 1 15
HELIX 83 AJ2 ASP D 393 GLU D 400 1 8
HELIX 84 AJ3 TRP D 414 ILE D 419 1 6
HELIX 85 AJ4 HIS D 420 PRO D 424 5 5
HELIX 86 AJ5 PHE D 425 LYS D 434 1 10
HELIX 87 AJ6 ASP D 443 GLN D 448 1 6
HELIX 88 AJ7 ASN D 466 ALA D 474 1 9
HELIX 89 AJ8 SER D 475 ILE D 477 5 3
HELIX 90 AJ9 SER D 491 ASP D 495 5 5
HELIX 91 AK1 ALA D 496 ASN D 509 1 14
HELIX 92 AK2 SER E 138 CYS E 145 1 8
HELIX 93 AK3 SER E 174 VAL E 183 1 10
HELIX 94 AK4 ARG E 186 VAL E 202 1 17
HELIX 95 AK5 SER E 214 ALA E 227 1 14
HELIX 96 AK6 THR E 248 PHE E 271 1 24
HELIX 97 AK7 GLN E 273 SER E 288 1 16
HELIX 98 AK8 THR E 302 THR E 308 1 7
HELIX 99 AK9 LEU E 309 LEU E 314 1 6
HELIX 100 AL1 THR E 318 GLU E 328 1 11
HELIX 101 AL2 SER E 344 TRP E 354 1 11
HELIX 102 AL3 PRO E 361 HIS E 367 1 7
HELIX 103 AL4 GLU E 368 CYS E 372 5 5
HELIX 104 AL5 TRP E 379 ASP E 386 1 8
HELIX 105 AL6 TYR E 388 ASP E 393 1 6
HELIX 106 AL7 ASP E 393 GLU E 400 1 8
HELIX 107 AL8 TRP E 414 ILE E 419 1 6
HELIX 108 AL9 HIS E 420 PRO E 424 5 5
HELIX 109 AM1 PHE E 425 LYS E 435 1 11
HELIX 110 AM2 ASP E 443 GLN E 448 1 6
HELIX 111 AM3 ASN E 466 ALA E 474 1 9
HELIX 112 AM4 SER E 475 ILE E 477 5 3
HELIX 113 AM5 ALA E 496 ASN E 509 1 14
HELIX 114 AM6 SER F 138 CYS F 145 1 8
HELIX 115 AM7 SER F 174 VAL F 183 1 10
HELIX 116 AM8 ARG F 186 VAL F 202 1 17
HELIX 117 AM9 SER F 214 PHE F 226 1 13
HELIX 118 AN1 ALA F 227 GLU F 229 5 3
HELIX 119 AN2 THR F 248 PHE F 271 1 24
HELIX 120 AN3 GLN F 273 SER F 288 1 16
HELIX 121 AN4 GLU F 289 GLY F 292 5 4
HELIX 122 AN5 THR F 302 GLN F 307 1 6
HELIX 123 AN6 LEU F 309 LEU F 314 1 6
HELIX 124 AN7 THR F 318 GLU F 328 1 11
HELIX 125 AN8 SER F 344 SER F 353 1 10
HELIX 126 AN9 ASN F 360 LEU F 366 1 7
HELIX 127 AO1 GLU F 368 CYS F 372 5 5
HELIX 128 AO2 TRP F 379 ASP F 386 1 8
HELIX 129 AO3 TYR F 388 ASP F 393 1 6
HELIX 130 AO4 ASP F 393 GLU F 400 1 8
HELIX 131 AO5 TRP F 414 ILE F 419 1 6
HELIX 132 AO6 HIS F 420 PRO F 424 5 5
HELIX 133 AO7 PHE F 425 LYS F 435 1 11
HELIX 134 AO8 ASP F 443 GLN F 448 1 6
HELIX 135 AO9 ASN F 466 ALA F 474 1 9
HELIX 136 AP1 SER F 475 ILE F 477 5 3
HELIX 137 AP2 SER F 491 ASP F 495 5 5
HELIX 138 AP3 ALA F 496 ASN F 509 1 14
SHEET 1 AA1 3 HIS A 69 THR A 71 0
SHEET 2 AA1 3 LEU A 80 PRO A 90 -1 O ARG A 86 N VAL A 70
SHEET 3 AA1 3 PHE A 75 VAL A 77 -1 N VAL A 77 O LEU A 80
SHEET 1 AA2 9 HIS A 69 THR A 71 0
SHEET 2 AA2 9 LEU A 80 PRO A 90 -1 O ARG A 86 N VAL A 70
SHEET 3 AA2 9 LYS A 99 ALA A 109 -1 O ALA A 104 N HIS A 85
SHEET 4 AA2 9 ARG A 149 ASP A 154 -1 O VAL A 150 N ILE A 107
SHEET 5 AA2 9 TYR A 119 LEU A 123 1 N LEU A 120 O ARG A 149
SHEET 6 AA2 9 TRP A 208 GLN A 213 1 O LEU A 211 N LEU A 121
SHEET 7 AA2 9 LEU A 231 THR A 237 1 O LYS A 232 N TRP A 208
SHEET 8 AA2 9 VAL A 454 TYR A 459 1 O ALA A 457 N ILE A 236
SHEET 9 AA2 9 ILE A 480 THR A 485 1 O TRP A 483 N VAL A 458
SHEET 1 AA3 2 VAL A 293 PRO A 294 0
SHEET 2 AA3 2 ILE A 300 LEU A 301 -1 O LEU A 301 N VAL A 293
SHEET 1 AA4 3 HIS B 69 THR B 71 0
SHEET 2 AA4 3 LEU B 80 PRO B 90 -1 O ARG B 86 N VAL B 70
SHEET 3 AA4 3 PHE B 75 VAL B 77 -1 N VAL B 77 O LEU B 80
SHEET 1 AA5 9 HIS B 69 THR B 71 0
SHEET 2 AA5 9 LEU B 80 PRO B 90 -1 O ARG B 86 N VAL B 70
SHEET 3 AA5 9 LYS B 99 ALA B 109 -1 O ILE B 100 N VAL B 89
SHEET 4 AA5 9 ARG B 149 ASP B 154 -1 O VAL B 150 N ILE B 107
SHEET 5 AA5 9 TYR B 119 LEU B 123 1 N LEU B 120 O VAL B 151
SHEET 6 AA5 9 TRP B 208 GLN B 213 1 O LEU B 211 N LEU B 121
SHEET 7 AA5 9 LEU B 231 THR B 237 1 O LYS B 232 N TRP B 208
SHEET 8 AA5 9 VAL B 454 TYR B 459 1 O ALA B 457 N ILE B 236
SHEET 9 AA5 9 ARG B 481 THR B 485 1 O TRP B 483 N VAL B 458
SHEET 1 AA6 2 VAL B 293 PRO B 294 0
SHEET 2 AA6 2 ILE B 300 LEU B 301 -1 O LEU B 301 N VAL B 293
SHEET 1 AA7 3 HIS C 69 THR C 71 0
SHEET 2 AA7 3 LEU C 80 PRO C 90 -1 O ARG C 86 N VAL C 70
SHEET 3 AA7 3 PHE C 75 VAL C 77 -1 N PHE C 75 O LEU C 82
SHEET 1 AA8 9 HIS C 69 THR C 71 0
SHEET 2 AA8 9 LEU C 80 PRO C 90 -1 O ARG C 86 N VAL C 70
SHEET 3 AA8 9 LYS C 99 ALA C 109 -1 O ALA C 104 N HIS C 85
SHEET 4 AA8 9 ARG C 149 ASP C 154 -1 O VAL C 150 N ILE C 107
SHEET 5 AA8 9 TYR C 119 LEU C 123 1 N LEU C 120 O VAL C 151
SHEET 6 AA8 9 TRP C 208 GLN C 213 1 O THR C 209 N LEU C 121
SHEET 7 AA8 9 LEU C 231 THR C 237 1 O LYS C 232 N TRP C 208
SHEET 8 AA8 9 VAL C 454 TYR C 459 1 O ALA C 457 N ILE C 236
SHEET 9 AA8 9 ARG C 481 THR C 485 1 O TRP C 483 N VAL C 458
SHEET 1 AA9 2 VAL C 293 PRO C 294 0
SHEET 2 AA9 2 ILE C 300 LEU C 301 -1 O LEU C 301 N VAL C 293
SHEET 1 AB1 3 HIS D 69 THR D 71 0
SHEET 2 AB1 3 LEU D 80 PRO D 90 -1 O ARG D 86 N VAL D 70
SHEET 3 AB1 3 PHE D 75 VAL D 77 -1 N VAL D 77 O LEU D 80
SHEET 1 AB2 9 HIS D 69 THR D 71 0
SHEET 2 AB2 9 LEU D 80 PRO D 90 -1 O ARG D 86 N VAL D 70
SHEET 3 AB2 9 LYS D 99 ALA D 109 -1 O ILE D 100 N VAL D 89
SHEET 4 AB2 9 ARG D 149 ASP D 154 -1 O VAL D 150 N ILE D 107
SHEET 5 AB2 9 TYR D 119 LEU D 123 1 N LEU D 120 O VAL D 151
SHEET 6 AB2 9 TRP D 208 GLN D 213 1 O LEU D 211 N LEU D 121
SHEET 7 AB2 9 LEU D 231 THR D 237 1 O LYS D 232 N TRP D 208
SHEET 8 AB2 9 VAL D 454 TYR D 459 1 O ALA D 457 N ILE D 236
SHEET 9 AB2 9 ILE D 480 THR D 485 1 O TRP D 483 N VAL D 458
SHEET 1 AB3 2 VAL D 293 PRO D 294 0
SHEET 2 AB3 2 ILE D 300 LEU D 301 -1 O LEU D 301 N VAL D 293
SHEET 1 AB4 3 HIS E 69 THR E 71 0
SHEET 2 AB4 3 LEU E 80 PRO E 90 -1 O ARG E 86 N VAL E 70
SHEET 3 AB4 3 PHE E 75 VAL E 77 -1 N VAL E 77 O LEU E 80
SHEET 1 AB5 9 HIS E 69 THR E 71 0
SHEET 2 AB5 9 LEU E 80 PRO E 90 -1 O ARG E 86 N VAL E 70
SHEET 3 AB5 9 LYS E 99 ALA E 109 -1 O ILE E 100 N VAL E 89
SHEET 4 AB5 9 ARG E 149 ASP E 154 -1 O VAL E 150 N ILE E 107
SHEET 5 AB5 9 TYR E 119 LEU E 123 1 N LEU E 120 O VAL E 151
SHEET 6 AB5 9 TRP E 208 GLN E 213 1 O THR E 209 N LEU E 121
SHEET 7 AB5 9 LEU E 231 THR E 237 1 O LYS E 232 N TRP E 208
SHEET 8 AB5 9 VAL E 454 TYR E 459 1 O ALA E 457 N ILE E 236
SHEET 9 AB5 9 ILE E 480 THR E 485 1 O TRP E 483 N ALA E 456
SHEET 1 AB6 2 VAL E 293 PRO E 294 0
SHEET 2 AB6 2 ILE E 300 LEU E 301 -1 O LEU E 301 N VAL E 293
SHEET 1 AB7 3 HIS F 69 THR F 71 0
SHEET 2 AB7 3 LEU F 80 PRO F 90 -1 O ARG F 86 N VAL F 70
SHEET 3 AB7 3 PHE F 75 VAL F 77 -1 N VAL F 77 O LEU F 80
SHEET 1 AB8 9 HIS F 69 THR F 71 0
SHEET 2 AB8 9 LEU F 80 PRO F 90 -1 O ARG F 86 N VAL F 70
SHEET 3 AB8 9 LYS F 99 ALA F 109 -1 O ILE F 100 N VAL F 89
SHEET 4 AB8 9 ARG F 149 ASP F 154 -1 O LEU F 152 N ARG F 105
SHEET 5 AB8 9 TYR F 119 LEU F 123 1 N LEU F 120 O VAL F 151
SHEET 6 AB8 9 TRP F 208 GLN F 213 1 O THR F 209 N LEU F 121
SHEET 7 AB8 9 LEU F 231 THR F 237 1 O LYS F 232 N TRP F 208
SHEET 8 AB8 9 VAL F 454 TYR F 459 1 O ALA F 457 N ILE F 236
SHEET 9 AB8 9 ARG F 481 THR F 485 1 O TRP F 483 N ALA F 456
SHEET 1 AB9 2 VAL F 293 PRO F 294 0
SHEET 2 AB9 2 ILE F 300 LEU F 301 -1 O LEU F 301 N VAL F 293
CISPEP 1 SER A 97 PRO A 98 0 -2.45
CISPEP 2 SER B 97 PRO B 98 0 -6.30
CISPEP 3 SER C 97 PRO C 98 0 -7.05
CISPEP 4 SER D 97 PRO D 98 0 -6.89
CISPEP 5 SER E 97 PRO E 98 0 -5.42
CISPEP 6 SER F 97 PRO F 98 0 -7.45
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 3521 PHE A 515
TER 7042 PHE B 515
TER 10563 PHE C 515
TER 14084 PHE D 515
TER 17605 PHE E 515
TER 21126 PHE F 515
MASTER 190 0 0 138 84 0 0 621120 6 0 210
END |