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HEADER HYDROLASE 12-OCT-22 8ERL
TITLE CRYOEM STRUCTURE OF LIPOPROTEIN LIPASE DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LPL;
COMPND 5 EC: 3.1.1.34
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS DIMER, LIPASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR K.H.GUNN,S.B.NEHER
REVDAT 1 03-MAY-23 8ERL 0
JRNL AUTH K.H.GUNN,S.B.NEHER
JRNL TITL ACTIVE LIPOPROTEIN LIPASE DIMER REVEALED BY CRYO-ELECTRON
JRNL TITL 2 MICROSCOPY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, 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) : 3.900
REMARK 3 NUMBER OF PARTICLES : 527205
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8ERL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1000269269.
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 : LIPOPROTEIN LIPASE DIMER
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.55
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 TALOS ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00
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) : 5510.00
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) : 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: 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 CYS A 14
REMARK 465 LEU A 15
REMARK 465 GLN A 16
REMARK 465 SER A 17
REMARK 465 LEU A 18
REMARK 465 THR A 19
REMARK 465 VAL A 20
REMARK 465 SER A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 GLY A 24
REMARK 465 LEU A 25
REMARK 465 VAL A 26
REMARK 465 ALA A 27
REMARK 465 ALA A 28
REMARK 465 ASP A 29
REMARK 465 ARG A 30
REMARK 465 ILE A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 LYS A 35
REMARK 465 ASN A 247
REMARK 465 ILE A 248
REMARK 465 GLY A 249
REMARK 465 GLU A 250
REMARK 465 ALA A 251
REMARK 465 LEU A 252
REMARK 465 ARG A 253
REMARK 465 VAL A 254
REMARK 465 ILE A 255
REMARK 465 ALA A 256
REMARK 465 GLU A 257
REMARK 465 ARG A 258
REMARK 465 GLY A 259
REMARK 465 LEU A 260
REMARK 465 GLY A 261
REMARK 465 ASP A 262
REMARK 465 VAL A 263
REMARK 465 ASP A 264
REMARK 465 GLN A 265
REMARK 465 LEU A 266
REMARK 465 LYS A 471
REMARK 465 SER A 472
REMARK 465 LEU A 473
REMARK 465 ASN A 474
REMARK 465 ARG A 475
REMARK 465 LYS A 476
REMARK 465 SER A 477
REMARK 465 GLY A 478
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 ALA B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 CYS B 14
REMARK 465 LEU B 15
REMARK 465 GLN B 16
REMARK 465 SER B 17
REMARK 465 LEU B 18
REMARK 465 THR B 19
REMARK 465 VAL B 20
REMARK 465 SER B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 GLY B 24
REMARK 465 LEU B 25
REMARK 465 VAL B 26
REMARK 465 ALA B 27
REMARK 465 ALA B 28
REMARK 465 ASP B 29
REMARK 465 ARG B 30
REMARK 465 ILE B 31
REMARK 465 THR B 32
REMARK 465 GLY B 33
REMARK 465 GLY B 34
REMARK 465 LYS B 35
REMARK 465 ASN B 247
REMARK 465 ILE B 248
REMARK 465 GLY B 249
REMARK 465 GLU B 250
REMARK 465 ALA B 251
REMARK 465 LEU B 252
REMARK 465 ARG B 253
REMARK 465 VAL B 254
REMARK 465 ILE B 255
REMARK 465 ALA B 256
REMARK 465 GLU B 257
REMARK 465 ARG B 258
REMARK 465 GLY B 259
REMARK 465 LEU B 260
REMARK 465 GLY B 261
REMARK 465 ASP B 262
REMARK 465 VAL B 263
REMARK 465 ASP B 264
REMARK 465 GLN B 265
REMARK 465 LEU B 266
REMARK 465 LYS B 471
REMARK 465 SER B 472
REMARK 465 LEU B 473
REMARK 465 ASN B 474
REMARK 465 ARG B 475
REMARK 465 LYS B 476
REMARK 465 SER B 477
REMARK 465 GLY B 478
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 LEU A 102 CA - CB - CG ANGL. DEV. = 19.5 DEGREES
REMARK 500 LEU A 277 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 ILE A 320 CG1 - CB - CG2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 LEU B 102 CA - CB - CG ANGL. DEV. = 19.5 DEGREES
REMARK 500 LEU B 277 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 ILE B 320 CG1 - CB - CG2 ANGL. DEV. = -16.4 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 GLU A 50 53.03 -91.82
REMARK 500 THR A 52 -65.09 -95.71
REMARK 500 ALA A 53 43.89 -141.36
REMARK 500 THR A 64 -167.80 -126.35
REMARK 500 ARG A 119 45.17 -141.05
REMARK 500 SER A 162 -125.61 58.69
REMARK 500 LEU A 185 -157.79 -90.85
REMARK 500 GLN A 227 56.85 -98.42
REMARK 500 SER A 270 -82.61 -147.15
REMARK 500 LYS A 310 -168.71 -100.77
REMARK 500 SER A 357 61.40 60.43
REMARK 500 THR A 361 -52.21 -120.60
REMARK 500 ASN A 422 -11.67 76.13
REMARK 500 TRP A 423 37.20 -154.47
REMARK 500 THR A 441 -129.42 56.50
REMARK 500 LYS A 444 76.68 -101.68
REMARK 500 LYS A 460 53.10 37.69
REMARK 500 GLU B 50 53.11 -91.90
REMARK 500 THR B 52 -65.05 -95.77
REMARK 500 ALA B 53 43.84 -141.40
REMARK 500 THR B 64 -167.77 -126.35
REMARK 500 ARG B 119 45.17 -141.04
REMARK 500 SER B 162 -125.57 58.67
REMARK 500 LEU B 185 -157.81 -90.88
REMARK 500 GLN B 227 56.90 -98.38
REMARK 500 LYS B 310 -168.76 -100.82
REMARK 500 SER B 357 61.39 60.51
REMARK 500 THR B 361 -52.24 -120.62
REMARK 500 ASN B 422 -11.72 76.08
REMARK 500 TRP B 423 37.16 -154.44
REMARK 500 THR B 441 -129.40 56.43
REMARK 500 LYS B 444 76.61 -101.61
REMARK 500 LYS B 460 53.17 37.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-28554 RELATED DB: EMDB
REMARK 900 CRYOEM STRUCTURE OF LIPOPROTEIN LIPASE DIMER
DBREF 8ERL A 1 478 UNP P11151 LIPL_BOVIN 1 478
DBREF 8ERL B 1 478 UNP P11151 LIPL_BOVIN 1 478
SEQRES 1 A 478 MET GLU SER LYS ALA LEU LEU LEU LEU ALA LEU SER VAL
SEQRES 2 A 478 CYS LEU GLN SER LEU THR VAL SER ARG GLY GLY LEU VAL
SEQRES 3 A 478 ALA ALA ASP ARG ILE THR GLY GLY LYS ASP PHE ARG ASP
SEQRES 4 A 478 ILE GLU SER LYS PHE ALA LEU ARG THR PRO GLU ASP THR
SEQRES 5 A 478 ALA GLU ASP THR CYS HIS LEU ILE PRO GLY VAL THR GLU
SEQRES 6 A 478 SER VAL ALA ASN CYS HIS PHE ASN HIS SER SER LYS THR
SEQRES 7 A 478 PHE VAL VAL ILE HIS GLY TRP THR VAL THR GLY MET TYR
SEQRES 8 A 478 GLU SER TRP VAL PRO LYS LEU VAL ALA ALA LEU TYR LYS
SEQRES 9 A 478 ARG GLU PRO ASP SER ASN VAL ILE VAL VAL ASP TRP LEU
SEQRES 10 A 478 SER ARG ALA GLN GLN HIS TYR PRO VAL SER ALA GLY TYR
SEQRES 11 A 478 THR LYS LEU VAL GLY GLN ASP VAL ALA LYS PHE MET ASN
SEQRES 12 A 478 TRP MET ALA ASP GLU PHE ASN TYR PRO LEU GLY ASN VAL
SEQRES 13 A 478 HIS LEU LEU GLY TYR SER LEU GLY ALA HIS ALA ALA GLY
SEQRES 14 A 478 ILE ALA GLY SER LEU THR ASN LYS LYS VAL ASN ARG ILE
SEQRES 15 A 478 THR GLY LEU ASP PRO ALA GLY PRO ASN PHE GLU TYR ALA
SEQRES 16 A 478 GLU ALA PRO SER ARG LEU SER PRO ASP ASP ALA ASP PHE
SEQRES 17 A 478 VAL ASP VAL LEU HIS THR PHE THR ARG GLY SER PRO GLY
SEQRES 18 A 478 ARG SER ILE GLY ILE GLN LYS PRO VAL GLY HIS VAL ASP
SEQRES 19 A 478 ILE TYR PRO ASN GLY GLY THR PHE GLN PRO GLY CYS ASN
SEQRES 20 A 478 ILE GLY GLU ALA LEU ARG VAL ILE ALA GLU ARG GLY LEU
SEQRES 21 A 478 GLY ASP VAL ASP GLN LEU VAL LYS CYS SER HIS GLU ARG
SEQRES 22 A 478 SER VAL HIS LEU PHE ILE ASP SER LEU LEU ASN GLU GLU
SEQRES 23 A 478 ASN PRO SER LYS ALA TYR ARG CYS ASN SER LYS GLU ALA
SEQRES 24 A 478 PHE GLU LYS GLY LEU CYS LEU SER CYS ARG LYS ASN ARG
SEQRES 25 A 478 CYS ASN ASN MET GLY TYR GLU ILE ASN LYS VAL ARG ALA
SEQRES 26 A 478 LYS ARG SER SER LYS MET TYR LEU LYS THR ARG SER GLN
SEQRES 27 A 478 MET PRO TYR LYS VAL PHE HIS TYR GLN VAL LYS ILE HIS
SEQRES 28 A 478 PHE SER GLY THR GLU SER ASN THR TYR THR ASN GLN ALA
SEQRES 29 A 478 PHE GLU ILE SER LEU TYR GLY THR VAL ALA GLU SER GLU
SEQRES 30 A 478 ASN ILE PRO PHE THR LEU PRO GLU VAL SER THR ASN LYS
SEQRES 31 A 478 THR TYR SER PHE LEU LEU TYR THR GLU VAL ASP ILE GLY
SEQRES 32 A 478 GLU LEU LEU MET LEU LYS LEU LYS TRP ILE SER ASP SER
SEQRES 33 A 478 TYR PHE SER TRP SER ASN TRP TRP SER SER PRO GLY PHE
SEQRES 34 A 478 ASP ILE GLY LYS ILE ARG VAL LYS ALA GLY GLU THR GLN
SEQRES 35 A 478 LYS LYS VAL ILE PHE CYS SER ARG GLU LYS MET SER TYR
SEQRES 36 A 478 LEU GLN LYS GLY LYS SER PRO VAL ILE PHE VAL LYS CYS
SEQRES 37 A 478 HIS ASP LYS SER LEU ASN ARG LYS SER GLY
SEQRES 1 B 478 MET GLU SER LYS ALA LEU LEU LEU LEU ALA LEU SER VAL
SEQRES 2 B 478 CYS LEU GLN SER LEU THR VAL SER ARG GLY GLY LEU VAL
SEQRES 3 B 478 ALA ALA ASP ARG ILE THR GLY GLY LYS ASP PHE ARG ASP
SEQRES 4 B 478 ILE GLU SER LYS PHE ALA LEU ARG THR PRO GLU ASP THR
SEQRES 5 B 478 ALA GLU ASP THR CYS HIS LEU ILE PRO GLY VAL THR GLU
SEQRES 6 B 478 SER VAL ALA ASN CYS HIS PHE ASN HIS SER SER LYS THR
SEQRES 7 B 478 PHE VAL VAL ILE HIS GLY TRP THR VAL THR GLY MET TYR
SEQRES 8 B 478 GLU SER TRP VAL PRO LYS LEU VAL ALA ALA LEU TYR LYS
SEQRES 9 B 478 ARG GLU PRO ASP SER ASN VAL ILE VAL VAL ASP TRP LEU
SEQRES 10 B 478 SER ARG ALA GLN GLN HIS TYR PRO VAL SER ALA GLY TYR
SEQRES 11 B 478 THR LYS LEU VAL GLY GLN ASP VAL ALA LYS PHE MET ASN
SEQRES 12 B 478 TRP MET ALA ASP GLU PHE ASN TYR PRO LEU GLY ASN VAL
SEQRES 13 B 478 HIS LEU LEU GLY TYR SER LEU GLY ALA HIS ALA ALA GLY
SEQRES 14 B 478 ILE ALA GLY SER LEU THR ASN LYS LYS VAL ASN ARG ILE
SEQRES 15 B 478 THR GLY LEU ASP PRO ALA GLY PRO ASN PHE GLU TYR ALA
SEQRES 16 B 478 GLU ALA PRO SER ARG LEU SER PRO ASP ASP ALA ASP PHE
SEQRES 17 B 478 VAL ASP VAL LEU HIS THR PHE THR ARG GLY SER PRO GLY
SEQRES 18 B 478 ARG SER ILE GLY ILE GLN LYS PRO VAL GLY HIS VAL ASP
SEQRES 19 B 478 ILE TYR PRO ASN GLY GLY THR PHE GLN PRO GLY CYS ASN
SEQRES 20 B 478 ILE GLY GLU ALA LEU ARG VAL ILE ALA GLU ARG GLY LEU
SEQRES 21 B 478 GLY ASP VAL ASP GLN LEU VAL LYS CYS SER HIS GLU ARG
SEQRES 22 B 478 SER VAL HIS LEU PHE ILE ASP SER LEU LEU ASN GLU GLU
SEQRES 23 B 478 ASN PRO SER LYS ALA TYR ARG CYS ASN SER LYS GLU ALA
SEQRES 24 B 478 PHE GLU LYS GLY LEU CYS LEU SER CYS ARG LYS ASN ARG
SEQRES 25 B 478 CYS ASN ASN MET GLY TYR GLU ILE ASN LYS VAL ARG ALA
SEQRES 26 B 478 LYS ARG SER SER LYS MET TYR LEU LYS THR ARG SER GLN
SEQRES 27 B 478 MET PRO TYR LYS VAL PHE HIS TYR GLN VAL LYS ILE HIS
SEQRES 28 B 478 PHE SER GLY THR GLU SER ASN THR TYR THR ASN GLN ALA
SEQRES 29 B 478 PHE GLU ILE SER LEU TYR GLY THR VAL ALA GLU SER GLU
SEQRES 30 B 478 ASN ILE PRO PHE THR LEU PRO GLU VAL SER THR ASN LYS
SEQRES 31 B 478 THR TYR SER PHE LEU LEU TYR THR GLU VAL ASP ILE GLY
SEQRES 32 B 478 GLU LEU LEU MET LEU LYS LEU LYS TRP ILE SER ASP SER
SEQRES 33 B 478 TYR PHE SER TRP SER ASN TRP TRP SER SER PRO GLY PHE
SEQRES 34 B 478 ASP ILE GLY LYS ILE ARG VAL LYS ALA GLY GLU THR GLN
SEQRES 35 B 478 LYS LYS VAL ILE PHE CYS SER ARG GLU LYS MET SER TYR
SEQRES 36 B 478 LEU GLN LYS GLY LYS SER PRO VAL ILE PHE VAL LYS CYS
SEQRES 37 B 478 HIS ASP LYS SER LEU ASN ARG LYS SER GLY
HELIX 1 AA1 TRP A 94 GLU A 106 1 13
HELIX 2 AA2 TRP A 116 ALA A 120 5 5
HELIX 3 AA3 HIS A 123 PHE A 149 1 27
HELIX 4 AA4 LEU A 163 THR A 175 1 13
HELIX 5 AA5 GLU A 196 ARG A 200 5 5
HELIX 6 AA6 SER A 202 ALA A 206 5 5
HELIX 7 AA7 GLY A 239 THR A 241 5 3
HELIX 8 AA8 SER A 270 ASN A 284 1 15
HELIX 9 AA9 SER A 296 GLY A 303 1 8
HELIX 10 AB1 GLU A 451 TYR A 455 5 5
HELIX 11 AB2 TRP B 94 GLU B 106 1 13
HELIX 12 AB3 TRP B 116 ALA B 120 5 5
HELIX 13 AB4 HIS B 123 PHE B 149 1 27
HELIX 14 AB5 LEU B 163 THR B 175 1 13
HELIX 15 AB6 GLU B 196 ARG B 200 5 5
HELIX 16 AB7 SER B 202 ALA B 206 5 5
HELIX 17 AB8 GLY B 239 THR B 241 5 3
HELIX 18 AB9 HIS B 271 ASN B 284 1 14
HELIX 19 AC1 SER B 296 GLY B 303 1 8
HELIX 20 AC2 GLU B 451 TYR B 455 5 5
SHEET 1 AA110 PHE A 44 ARG A 47 0
SHEET 2 AA110 SER A 109 VAL A 114 -1 O VAL A 113 N ALA A 45
SHEET 3 AA110 LYS A 77 ILE A 82 1 N LYS A 77 O ASN A 110
SHEET 4 AA110 VAL A 156 SER A 162 1 O HIS A 157 N VAL A 80
SHEET 5 AA110 ILE A 182 PRO A 187 1 O LEU A 185 N GLY A 160
SHEET 6 AA110 VAL A 209 LEU A 212 1 O ASP A 210 N GLY A 184
SHEET 7 AA110 VAL A 233 PRO A 237 1 O VAL A 233 N VAL A 209
SHEET 8 AA110 SER A 329 LEU A 333 1 O MET A 331 N ASP A 234
SHEET 9 AA110 ALA A 291 CYS A 294 -1 N CYS A 294 O LYS A 330
SHEET 10 AA110 CYS A 313 ASN A 314 -1 O ASN A 314 N ALA A 291
SHEET 1 AA2 5 LEU A 395 THR A 398 0
SHEET 2 AA2 5 PHE A 344 LYS A 349 -1 N PHE A 344 O THR A 398
SHEET 3 AA2 5 ARG A 435 ALA A 438 -1 O ARG A 435 N LYS A 349
SHEET 4 AA2 5 VAL A 445 CYS A 448 -1 O VAL A 445 N VAL A 436
SHEET 5 AA2 5 VAL A 466 LYS A 467 -1 O VAL A 466 N CYS A 448
SHEET 1 AA3 4 GLU A 375 PHE A 381 0
SHEET 2 AA3 4 PHE A 365 GLY A 371 -1 N PHE A 365 O PHE A 381
SHEET 3 AA3 4 LEU A 405 LYS A 411 -1 O LYS A 409 N SER A 368
SHEET 4 AA3 4 PRO A 462 ILE A 464 -1 O VAL A 463 N LEU A 410
SHEET 1 AA410 PHE B 44 ARG B 47 0
SHEET 2 AA410 SER B 109 VAL B 114 -1 O VAL B 113 N ALA B 45
SHEET 3 AA410 LYS B 77 ILE B 82 1 N LYS B 77 O ASN B 110
SHEET 4 AA410 VAL B 156 SER B 162 1 O HIS B 157 N VAL B 80
SHEET 5 AA410 ILE B 182 PRO B 187 1 O LEU B 185 N GLY B 160
SHEET 6 AA410 VAL B 209 LEU B 212 1 O ASP B 210 N GLY B 184
SHEET 7 AA410 VAL B 233 PRO B 237 1 O VAL B 233 N VAL B 209
SHEET 8 AA410 SER B 329 LEU B 333 1 O MET B 331 N ASP B 234
SHEET 9 AA410 ALA B 291 CYS B 294 -1 N CYS B 294 O LYS B 330
SHEET 10 AA410 CYS B 313 ASN B 314 -1 O ASN B 314 N ALA B 291
SHEET 1 AA5 5 LEU B 395 THR B 398 0
SHEET 2 AA5 5 PHE B 344 LYS B 349 -1 N PHE B 344 O THR B 398
SHEET 3 AA5 5 ARG B 435 ALA B 438 -1 O ARG B 435 N LYS B 349
SHEET 4 AA5 5 VAL B 445 CYS B 448 -1 O VAL B 445 N VAL B 436
SHEET 5 AA5 5 VAL B 466 LYS B 467 -1 O VAL B 466 N CYS B 448
SHEET 1 AA6 4 GLU B 375 PHE B 381 0
SHEET 2 AA6 4 PHE B 365 GLY B 371 -1 N PHE B 365 O PHE B 381
SHEET 3 AA6 4 LEU B 405 LYS B 411 -1 O LYS B 409 N SER B 368
SHEET 4 AA6 4 PRO B 462 ILE B 464 -1 O VAL B 463 N LEU B 410
SSBOND 1 CYS A 57 CYS A 70 1555 1555 2.03
SSBOND 2 CYS A 294 CYS A 305 1555 1555 2.03
SSBOND 3 CYS A 308 CYS A 313 1555 1555 2.03
SSBOND 4 CYS A 448 CYS A 468 1555 1555 2.03
SSBOND 5 CYS B 57 CYS B 70 1555 1555 2.03
SSBOND 6 CYS B 294 CYS B 305 1555 1555 2.03
SSBOND 7 CYS B 308 CYS B 313 1555 1555 2.03
SSBOND 8 CYS B 448 CYS B 468 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 3301 ASP A 470
TER 6602 ASP B 470
MASTER 303 0 0 20 38 0 0 6 6600 2 16 74
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