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HEADER HYDROLASE 21-MAY-23 8JGN
TITLE CRYO-EM STRUCTURE OF ALPHA/BETA HYDROLASE DANGEROUS MIX 3 (DM3) FORMS
TITLE 2 COMPARTMENTALIZED HEXAMER STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AT3G61540/F2A19_140;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN,PROLYL
COMPND 5 AMINOPEPTIDASE-LIKE PROTEIN;
COMPND 6 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: COLUMBIA ACCESSION (COL-0);
SOURCE 6 GENE: F2A19.140, AT3G61540;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: RILP
KEYWDS COMPLEX, IMMUNE RELATED ALPHA/BETA HYDROLASE, PROLYL AMINOPEPTIDASE
KEYWDS 2 2, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR G.KIM,J.J.SONG
REVDAT 1 25-DEC-24 8JGN 0
JRNL AUTH G.KIM,J.J.SONG
JRNL TITL CRYO-EM STRUCTURE OF ALPHA/BETA HYDROLASE DANGEROUS MIX 3
JRNL TITL 2 (DM3) FORMS COMPARTMENTALIZED HEXAMER STRUCTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.39 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) : 3.390
REMARK 3 NUMBER OF PARTICLES : 330509
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 8JGN 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_1300037446.
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 : HOMOHEXAMER COMPLEX OF DM3 FROM
REMARK 245 COLUMBIA ACCESSION (COL-0)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.20
REMARK 245 SAMPLE SUPPORT DETAILS : AFTER GLOW DISCHARGE, GRAPHENE
REMARK 245 OXIDE WAS TREATED ONTO THE GRID
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 GLACIOS
REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
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 : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00
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) : 200
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 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 GLU A 147 -54.51 -140.30
REMARK 500 LEU A 164 48.43 -90.01
REMARK 500 LYS A 204 13.84 54.30
REMARK 500 SER A 214 -124.00 55.74
REMARK 500 GLU A 287 46.93 -99.65
REMARK 500 SER A 288 -136.23 -103.79
REMARK 500 GLU A 289 -78.22 -98.01
REMARK 500 SER A 401 18.89 58.79
REMARK 500 ASP A 437 44.41 -100.25
REMARK 500 GLU B 147 -37.15 -135.72
REMARK 500 PHE B 185 41.84 -86.82
REMARK 500 LYS B 204 13.75 55.47
REMARK 500 SER B 214 -125.85 54.47
REMARK 500 ALA B 227 59.68 -150.02
REMARK 500 PHE B 271 77.91 -118.19
REMARK 500 ASN B 360 68.54 -119.12
REMARK 500 SER B 491 6.70 -69.36
REMARK 500 GLU C 147 -32.60 -132.06
REMARK 500 ARG C 149 71.15 -110.38
REMARK 500 THR C 162 58.67 39.84
REMARK 500 SER C 214 -125.21 51.66
REMARK 500 PHE C 271 75.53 -113.33
REMARK 500 SER C 401 7.24 56.62
REMARK 500 GLU C 418 -31.98 -134.65
REMARK 500 SER C 491 0.48 -69.79
REMARK 500 GLU D 79 -3.27 74.31
REMARK 500 GLU D 147 -33.68 -133.56
REMARK 500 LYS D 204 19.33 52.23
REMARK 500 SER D 214 -124.90 53.55
REMARK 500 PHE D 271 75.20 -114.88
REMARK 500 ASN D 360 68.45 -117.83
REMARK 500 GLU D 409 19.57 58.09
REMARK 500 GLU E 147 -37.13 -137.39
REMARK 500 ARG E 149 77.92 -104.14
REMARK 500 LYS E 204 7.59 58.13
REMARK 500 SER E 214 -121.83 51.26
REMARK 500 PHE E 271 73.48 -113.37
REMARK 500 ASN E 360 67.39 -117.09
REMARK 500 ARG E 481 79.72 -110.72
REMARK 500 PRO F 98 -176.34 -64.20
REMARK 500 GLU F 147 -31.25 -134.29
REMARK 500 LEU F 164 49.39 -93.36
REMARK 500 PHE F 185 47.51 -106.51
REMARK 500 ARG F 186 -157.26 -105.34
REMARK 500 LYS F 204 10.22 54.20
REMARK 500 SER F 214 -126.84 51.04
REMARK 500 ALA F 227 53.26 -145.06
REMARK 500 PHE F 271 72.11 -118.03
REMARK 500 HIS F 367 -70.12 -82.37
REMARK 500 GLU F 373 32.62 -140.49
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-36240 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF ALPHA/BETA HYDROLASE DANGEROUS MIX 3 (DM3)
REMARK 900 FORMS COMPARTMENTALIZED HEXAMER STRUCTURE
DBREF 8JGN A 68 515 UNP Q9M314 Q9M314_ARATH 68 515
DBREF 8JGN B 68 515 UNP Q9M314 Q9M314_ARATH 68 515
DBREF 8JGN C 68 515 UNP Q9M314 Q9M314_ARATH 68 515
DBREF 8JGN D 68 515 UNP Q9M314 Q9M314_ARATH 68 515
DBREF 8JGN E 68 515 UNP Q9M314 Q9M314_ARATH 68 515
DBREF 8JGN F 68 515 UNP Q9M314 Q9M314_ARATH 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR A 165 LEU A 170 1 6
HELIX 3 AA3 SER A 174 VAL A 183 1 10
HELIX 4 AA4 ARG A 186 VAL A 202 1 17
HELIX 5 AA5 PRO A 203 ASP A 206 5 4
HELIX 6 AA6 SER A 214 PHE A 226 1 13
HELIX 7 AA7 ALA A 227 GLU A 229 5 3
HELIX 8 AA8 THR A 248 PHE A 271 1 24
HELIX 9 AA9 GLN A 273 GLU A 287 1 15
HELIX 10 AB1 THR A 302 GLN A 307 1 6
HELIX 11 AB2 LEU A 309 LEU A 314 1 6
HELIX 12 AB3 THR A 318 GLU A 328 1 11
HELIX 13 AB4 SER A 344 TRP A 354 1 11
HELIX 14 AB5 PRO A 361 LEU A 366 1 6
HELIX 15 AB6 HIS A 367 CYS A 372 5 6
HELIX 16 AB7 TRP A 379 ASP A 386 1 8
HELIX 17 AB8 TYR A 388 ASP A 393 1 6
HELIX 18 AB9 ASP A 393 GLU A 400 1 8
HELIX 19 AC1 TRP A 414 ILE A 419 1 6
HELIX 20 AC2 LEU A 422 PRO A 424 5 3
HELIX 21 AC3 PHE A 425 LYS A 434 1 10
HELIX 22 AC4 ASP A 443 GLN A 448 1 6
HELIX 23 AC5 ASN A 466 ALA A 474 1 9
HELIX 24 AC6 ALA A 496 ASN A 509 1 14
HELIX 25 AC7 SER B 138 CYS B 145 1 8
HELIX 26 AC8 THR B 165 LEU B 170 1 6
HELIX 27 AC9 SER B 174 VAL B 183 1 10
HELIX 28 AD1 ALA B 187 VAL B 202 1 16
HELIX 29 AD2 PRO B 203 ASP B 206 5 4
HELIX 30 AD3 SER B 214 ALA B 227 1 14
HELIX 31 AD4 THR B 248 PHE B 271 1 24
HELIX 32 AD5 GLN B 273 SER B 288 1 16
HELIX 33 AD6 THR B 302 THR B 308 1 7
HELIX 34 AD7 LEU B 309 GLY B 315 1 7
HELIX 35 AD8 THR B 318 GLU B 328 1 11
HELIX 36 AD9 SER B 344 SER B 353 1 10
HELIX 37 AE1 ASN B 360 LEU B 366 1 7
HELIX 38 AE2 HIS B 367 CYS B 372 5 6
HELIX 39 AE3 TRP B 379 TYR B 388 1 10
HELIX 40 AE4 TYR B 388 ASP B 393 1 6
HELIX 41 AE5 ASP B 393 GLU B 400 1 8
HELIX 42 AE6 TRP B 414 ILE B 419 1 6
HELIX 43 AE7 HIS B 420 PRO B 424 5 5
HELIX 44 AE8 PHE B 425 LYS B 435 1 11
HELIX 45 AE9 ASP B 443 GLN B 448 1 6
HELIX 46 AF1 ASN B 466 ALA B 474 1 9
HELIX 47 AF2 SER B 491 ALA B 496 1 6
HELIX 48 AF3 ALA B 496 GLY B 510 1 15
HELIX 49 AF4 GLY C 139 CYS C 145 1 7
HELIX 50 AF5 THR C 165 LEU C 170 1 6
HELIX 51 AF6 SER C 174 VAL C 183 1 10
HELIX 52 AF7 ARG C 186 VAL C 202 1 17
HELIX 53 AF8 PRO C 203 ASP C 206 5 4
HELIX 54 AF9 SER C 214 PHE C 226 1 13
HELIX 55 AG1 ALA C 227 GLU C 229 5 3
HELIX 56 AG2 THR C 248 PHE C 271 1 24
HELIX 57 AG3 GLN C 273 SER C 288 1 16
HELIX 58 AG4 THR C 302 THR C 308 1 7
HELIX 59 AG5 LEU C 309 LEU C 314 1 6
HELIX 60 AG6 THR C 318 GLU C 328 1 11
HELIX 61 AG7 SER C 344 HIS C 355 1 12
HELIX 62 AG8 PRO C 361 LEU C 366 1 6
HELIX 63 AG9 HIS C 367 CYS C 372 5 6
HELIX 64 AH1 TRP C 379 ASP C 393 1 15
HELIX 65 AH2 ASP C 393 GLU C 400 1 8
HELIX 66 AH3 TRP C 414 ILE C 419 1 6
HELIX 67 AH4 HIS C 420 PRO C 424 5 5
HELIX 68 AH5 PHE C 425 LYS C 434 1 10
HELIX 69 AH6 ASP C 443 GLN C 448 1 6
HELIX 70 AH7 ASN C 466 ALA C 474 1 9
HELIX 71 AH8 SER C 491 ASP C 495 5 5
HELIX 72 AH9 ALA C 496 GLY C 510 1 15
HELIX 73 AI1 SER D 138 CYS D 145 1 8
HELIX 74 AI2 SER D 167 PHE D 172 5 6
HELIX 75 AI3 SER D 174 VAL D 183 1 10
HELIX 76 AI4 ARG D 186 VAL D 202 1 17
HELIX 77 AI5 PRO D 203 ASP D 206 5 4
HELIX 78 AI6 SER D 214 PHE D 226 1 13
HELIX 79 AI7 ALA D 227 GLU D 229 5 3
HELIX 80 AI8 THR D 248 PHE D 271 1 24
HELIX 81 AI9 GLN D 273 SER D 288 1 16
HELIX 82 AJ1 THR D 302 GLN D 307 1 6
HELIX 83 AJ2 LEU D 309 LEU D 314 1 6
HELIX 84 AJ3 THR D 318 ARG D 329 1 12
HELIX 85 AJ4 SER D 344 HIS D 355 1 12
HELIX 86 AJ5 PRO D 361 LEU D 366 1 6
HELIX 87 AJ6 HIS D 367 TYR D 371 5 5
HELIX 88 AJ7 TRP D 379 ASP D 393 1 15
HELIX 89 AJ8 ASP D 393 SER D 401 1 9
HELIX 90 AJ9 TRP D 414 ILE D 419 1 6
HELIX 91 AK1 HIS D 420 PRO D 424 5 5
HELIX 92 AK2 PHE D 425 LYS D 434 1 10
HELIX 93 AK3 ASP D 443 GLN D 448 1 6
HELIX 94 AK4 ASN D 466 SER D 475 1 10
HELIX 95 AK5 ALA D 496 ASN D 509 1 14
HELIX 96 AK6 SER E 138 CYS E 145 1 8
HELIX 97 AK7 SER E 167 PHE E 172 5 6
HELIX 98 AK8 SER E 174 VAL E 183 1 10
HELIX 99 AK9 ARG E 186 VAL E 202 1 17
HELIX 100 AL1 PRO E 203 ASP E 206 5 4
HELIX 101 AL2 SER E 214 PHE E 226 1 13
HELIX 102 AL3 ALA E 227 GLU E 229 5 3
HELIX 103 AL4 THR E 248 PHE E 271 1 24
HELIX 104 AL5 GLN E 273 SER E 288 1 16
HELIX 105 AL6 GLU E 289 GLY E 292 5 4
HELIX 106 AL7 THR E 302 GLN E 307 1 6
HELIX 107 AL8 LEU E 309 SER E 316 1 8
HELIX 108 AL9 THR E 318 GLU E 328 1 11
HELIX 109 AM1 SER E 344 HIS E 355 1 12
HELIX 110 AM2 PRO E 361 LEU E 366 1 6
HELIX 111 AM3 HIS E 367 CYS E 372 5 6
HELIX 112 AM4 TRP E 379 ASP E 386 1 8
HELIX 113 AM5 TYR E 388 ASP E 393 1 6
HELIX 114 AM6 ASP E 393 GLU E 400 1 8
HELIX 115 AM7 TRP E 414 ILE E 419 1 6
HELIX 116 AM8 HIS E 420 PRO E 424 5 5
HELIX 117 AM9 PHE E 425 LYS E 434 1 10
HELIX 118 AN1 ASP E 443 GLN E 448 1 6
HELIX 119 AN2 ASN E 466 SER E 475 1 10
HELIX 120 AN3 ALA E 496 GLY E 510 1 15
HELIX 121 AN4 SER F 138 CYS F 145 1 8
HELIX 122 AN5 THR F 165 LEU F 170 1 6
HELIX 123 AN6 SER F 174 VAL F 183 1 10
HELIX 124 AN7 ARG F 186 VAL F 202 1 17
HELIX 125 AN8 PRO F 203 ASP F 206 5 4
HELIX 126 AN9 SER F 214 ALA F 227 1 14
HELIX 127 AO1 THR F 248 PHE F 271 1 24
HELIX 128 AO2 GLN F 273 SER F 288 1 16
HELIX 129 AO3 GLU F 289 GLY F 292 5 4
HELIX 130 AO4 THR F 302 THR F 308 1 7
HELIX 131 AO5 LEU F 309 LEU F 314 1 6
HELIX 132 AO6 THR F 318 GLU F 328 1 11
HELIX 133 AO7 SER F 344 HIS F 355 1 12
HELIX 134 AO8 PRO F 361 LEU F 366 1 6
HELIX 135 AO9 HIS F 367 CYS F 372 5 6
HELIX 136 AP1 TRP F 379 ASP F 386 1 8
HELIX 137 AP2 TYR F 388 ASP F 393 1 6
HELIX 138 AP3 ASP F 393 SER F 401 1 9
HELIX 139 AP4 TRP F 414 ILE F 419 1 6
HELIX 140 AP5 HIS F 420 PRO F 424 5 5
HELIX 141 AP6 PHE F 425 LYS F 434 1 10
HELIX 142 AP7 ASP F 443 GLN F 448 1 6
HELIX 143 AP8 ASN F 466 ALA F 474 1 9
HELIX 144 AP9 SER F 491 ASP F 495 5 5
HELIX 145 AQ1 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 PHE A 75 O LEU A 82
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 ILE A 100 N VAL A 89
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 VAL A 151
SHEET 6 AA2 9 TRP A 208 GLN A 213 1 O LEU A 211 N LEU A 123
SHEET 7 AA2 9 LEU A 231 THR A 237 1 O LEU A 235 N ILE A 210
SHEET 8 AA2 9 VAL A 454 TYR A 459 1 O ALA A 457 N ILE A 236
SHEET 9 AA2 9 ARG A 481 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 LEU B 153 -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 123
SHEET 7 AA5 9 LEU B 231 THR B 237 1 O LEU B 235 N ILE B 210
SHEET 8 AA5 9 VAL B 454 TYR B 459 1 O ALA B 457 N ILE B 236
SHEET 9 AA5 9 ILE B 480 THR B 485 1 O TRP B 483 N ALA B 456
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 VAL C 108 N ARG C 81
SHEET 4 AA8 9 VAL C 151 ASP C 154 -1 O LEU C 152 N ARG C 105
SHEET 5 AA8 9 LEU C 120 LEU C 123 1 N LEU C 120 O VAL C 151
SHEET 6 AA8 9 TRP C 208 GLN C 213 1 O LEU C 211 N LEU C 121
SHEET 7 AA8 9 LEU C 231 THR C 237 1 O LEU C 235 N ILE C 210
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 ARG C 481 N VAL C 454
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 ALA D 104 N HIS D 85
SHEET 4 AB2 9 ARG D 149 ASP D 154 -1 O LEU D 152 N ARG D 105
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 123
SHEET 7 AB2 9 LEU D 231 THR D 237 1 O THR D 237 N GLY D 212
SHEET 8 AB2 9 VAL D 454 TYR D 459 1 O ALA D 457 N ILE D 236
SHEET 9 AB2 9 ARG D 481 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 2 TRP D 331 ASP D 332 0
SHEET 2 AB4 2 CYS D 342 ILE D 343 -1 O CYS D 342 N ASP D 332
SHEET 1 AB5 3 HIS E 69 THR E 71 0
SHEET 2 AB5 3 LEU E 80 PRO E 90 -1 O ARG E 86 N VAL E 70
SHEET 3 AB5 3 PHE E 75 VAL E 77 -1 N VAL E 77 O LEU E 80
SHEET 1 AB6 9 HIS E 69 THR E 71 0
SHEET 2 AB6 9 LEU E 80 PRO E 90 -1 O ARG E 86 N VAL E 70
SHEET 3 AB6 9 LYS E 99 ALA E 109 -1 O ALA E 104 N HIS E 85
SHEET 4 AB6 9 VAL E 151 ASP E 154 -1 O LEU E 152 N ARG E 105
SHEET 5 AB6 9 LEU E 120 LEU E 123 1 N LEU E 120 O VAL E 151
SHEET 6 AB6 9 TRP E 208 GLN E 213 1 O LEU E 211 N LEU E 123
SHEET 7 AB6 9 LEU E 231 THR E 237 1 O LEU E 235 N ILE E 210
SHEET 8 AB6 9 VAL E 454 TYR E 459 1 O ALA E 455 N VAL E 234
SHEET 9 AB6 9 ARG E 481 THR E 485 1 O ARG E 481 N VAL E 454
SHEET 1 AB7 2 VAL E 293 PRO E 294 0
SHEET 2 AB7 2 ILE E 300 LEU E 301 -1 O LEU E 301 N VAL E 293
SHEET 1 AB8 3 HIS F 69 THR F 71 0
SHEET 2 AB8 3 LEU F 80 PRO F 90 -1 O ARG F 86 N VAL F 70
SHEET 3 AB8 3 PHE F 75 VAL F 77 -1 N PHE F 75 O LEU F 82
SHEET 1 AB9 9 HIS F 69 THR F 71 0
SHEET 2 AB9 9 LEU F 80 PRO F 90 -1 O ARG F 86 N VAL F 70
SHEET 3 AB9 9 LYS F 99 ALA F 109 -1 O GLU F 106 N ARG F 83
SHEET 4 AB9 9 ARG F 149 ASP F 154 -1 O VAL F 150 N ILE F 107
SHEET 5 AB9 9 TYR F 119 LEU F 123 1 N LEU F 120 O VAL F 151
SHEET 6 AB9 9 TRP F 208 GLN F 213 1 O LEU F 211 N LEU F 121
SHEET 7 AB9 9 LEU F 231 THR F 237 1 O LYS F 232 N TRP F 208
SHEET 8 AB9 9 VAL F 454 TYR F 459 1 O ALA F 457 N ILE F 236
SHEET 9 AB9 9 ARG F 481 THR F 485 1 O TRP F 483 N VAL F 458
SHEET 1 AC1 2 VAL F 293 PRO F 294 0
SHEET 2 AC1 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 -10.21
CISPEP 2 SER B 97 PRO B 98 0 -7.59
CISPEP 3 SER C 97 PRO C 98 0 4.43
CISPEP 4 SER D 97 PRO D 98 0 -5.43
CISPEP 5 SER E 97 PRO E 98 0 -7.34
CISPEP 6 SER F 97 PRO F 98 0 -10.33
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 3561 PHE A 515
TER 7122 PHE B 515
TER 10683 PHE C 515
TER 14244 PHE D 515
TER 17805 PHE E 515
TER 21366 PHE F 515
MASTER 171 0 0 145 86 0 0 621360 6 0 210
END |