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HEADER MEMBRANE PROTEIN 01-MAR-21 7E89
TITLE CRYOEM STRUCTURE OF HUMAN KV4.2-DPP6S COMPLEX, EXTRACELLULAR REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 3 CHAIN: J, I, A, B;
COMPND 4 SYNONYM: DPPX,DIPEPTIDYL AMINOPEPTIDASE-RELATED PROTEIN,DIPEPTIDYL
COMPND 5 PEPTIDASE 6,DIPEPTIDYL PEPTIDASE IV-LIKE PROTEIN,DIPEPTIDYL PEPTIDASE
COMPND 6 VI,DPP VI;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP6;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.KISE,O.NUREKI
REVDAT 1 13-OCT-21 7E89 0
JRNL AUTH Y.KISE,G.KASUYA,H.H.OKAMOTO,D.YAMANOUCHI,K.KOBAYASHI,
JRNL AUTH 2 T.KUSAKIZAKO,T.NISHIZAWA,K.NAKAJO,O.NUREKI
JRNL TITL STRUCTURAL BASIS OF GATING MODULATION OF KV4 CHANNEL
JRNL TITL 2 COMPLEXES.
JRNL REF NATURE 2021
JRNL REFN ESSN 1476-4687
JRNL PMID 34552243
JRNL DOI 10.1038/S41586-021-03935-Z
REMARK 2
REMARK 2 RESOLUTION. 4.00 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) : 4.000
REMARK 3 NUMBER OF PARTICLES : 91974
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 7E89 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1300020960.
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 : HUMAN KV4.2-DPP6S COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
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) : 4800.00
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: J, I, 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 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 O VAL A 69 OG SER A 590 2.18
REMARK 500 O VAL J 69 OG SER J 590 2.18
REMARK 500 OG1 THR B 475 OE1 GLU B 577 2.19
REMARK 500 OG1 THR I 475 OE1 GLU I 577 2.19
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 SER J 62 -127.30 65.72
REMARK 500 GLN J 65 147.01 69.39
REMARK 500 LYS J 68 -168.91 -78.83
REMARK 500 ASN J 111 48.75 37.68
REMARK 500 GLU J 118 -169.03 -78.21
REMARK 500 SER J 124 50.55 -92.03
REMARK 500 TYR J 149 -169.17 -118.11
REMARK 500 SER J 152 47.36 -142.92
REMARK 500 TYR J 153 64.14 -67.62
REMARK 500 HIS J 164 173.43 179.53
REMARK 500 SER J 176 -165.41 -79.88
REMARK 500 VAL J 213 -50.59 -122.81
REMARK 500 ASP J 228 -169.71 -78.38
REMARK 500 ARG J 382 -166.54 -77.92
REMARK 500 THR J 443 38.71 -98.59
REMARK 500 CYS J 468 46.20 39.66
REMARK 500 MET J 485 17.29 56.44
REMARK 500 ASP J 540 -127.68 57.54
REMARK 500 PRO J 551 4.44 -69.45
REMARK 500 ALA J 552 -5.61 72.72
REMARK 500 PHE J 605 -1.39 70.05
REMARK 500 ASP J 650 -124.55 50.19
REMARK 500 ARG J 703 -4.78 69.41
REMARK 500 ALA J 716 -73.05 -64.08
REMARK 500 LEU J 717 49.90 32.16
REMARK 500 ARG I 97 -175.13 -68.49
REMARK 500 GLN I 99 -63.56 -92.89
REMARK 500 LYS I 100 42.81 -140.40
REMARK 500 ASN I 111 47.75 36.44
REMARK 500 GLU I 118 -167.40 -126.70
REMARK 500 HIS I 151 17.14 -143.56
REMARK 500 SER I 176 -165.91 -77.74
REMARK 500 GLU I 197 59.29 38.54
REMARK 500 ASP I 228 -177.20 -69.44
REMARK 500 ILE I 235 -62.02 -122.48
REMARK 500 LYS I 237 18.77 56.13
REMARK 500 TYR I 269 -50.70 -120.12
REMARK 500 TYR I 282 88.53 -150.69
REMARK 500 ARG I 315 33.09 -96.75
REMARK 500 ASN I 372 37.76 -96.80
REMARK 500 ARG I 382 -167.41 -79.02
REMARK 500 THR I 443 31.94 -94.96
REMARK 500 ASP I 469 148.88 83.73
REMARK 500 SER I 478 116.12 -160.03
REMARK 500 MET I 485 -4.77 67.92
REMARK 500 GLU I 493 23.54 48.53
REMARK 500 ASN I 517 60.79 60.57
REMARK 500 ASP I 540 -117.79 52.92
REMARK 500 ALA I 552 -4.25 69.15
REMARK 500 GLN I 606 31.92 -140.48
REMARK 500
REMARK 500 THIS ENTRY HAS 116 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-31012 RELATED DB: EMDB
REMARK 900 MEMBRANE PROTEIN
DBREF 7E89 J 59 787 UNP P42658 DPP6_HUMAN 121 849
DBREF 7E89 I 59 787 UNP P42658 DPP6_HUMAN 121 849
DBREF 7E89 A 59 787 UNP P42658 DPP6_HUMAN 121 849
DBREF 7E89 B 59 787 UNP P42658 DPP6_HUMAN 121 849
SEQRES 1 J 729 GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL THR VAL
SEQRES 2 J 729 GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS ASP PRO
SEQRES 3 J 729 GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE TYR ARG
SEQRES 4 J 729 GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL GLU THR
SEQRES 5 J 729 ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS ILE GLU
SEQRES 6 J 729 SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO ASP ARG
SEQRES 7 J 729 GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO ILE TYR
SEQRES 8 J 729 GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER LYS ILE
SEQRES 9 J 729 PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO GLU VAL
SEQRES 10 J 729 SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY PRO LYS
SEQRES 11 J 729 GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN ILE TYR
SEQRES 12 J 729 TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG VAL VAL
SEQRES 13 J 729 SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY LEU SER
SEQRES 14 J 729 ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR HIS ILE
SEQRES 15 J 729 ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU ALA TYR
SEQRES 16 J 729 ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET GLU LEU
SEQRES 17 J 729 PRO THR TYR THR GLY SER ILE TYR PRO THR VAL LYS PRO
SEQRES 18 J 729 TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO SER ILE
SEQRES 19 J 729 SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR HIS ASP
SEQRES 20 J 729 LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET ARG GLU
SEQRES 21 J 729 TYR TYR ILE THR MET VAL LYS TRP ALA THR SER THR LYS
SEQRES 22 J 729 VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN VAL SER
SEQRES 23 J 729 ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL CYS THR
SEQRES 24 J 729 LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU HIS ARG
SEQRES 25 J 729 GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY ARG LYS
SEQRES 26 J 729 PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY ARG GLY
SEQRES 27 J 729 LYS PHE TYR HIS ILE THR VAL SER SER SER GLN PRO ASN
SEQRES 28 J 729 SER SER ASN ASP ASN ILE GLN SER ILE THR SER GLY ASP
SEQRES 29 J 729 TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU LYS GLY
SEQRES 30 J 729 ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU PRO ARG
SEQRES 31 J 729 ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY ASN PHE
SEQRES 32 J 729 ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU ASN CYS
SEQRES 33 J 729 THR TYR PHE SER ALA SER PHE SER HIS SER MET ASP PHE
SEQRES 34 J 729 PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO MET VAL
SEQRES 35 J 729 THR VAL HIS ASN THR THR ASP LYS LYS LYS MET PHE ASP
SEQRES 36 J 729 LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE ASN ASP
SEQRES 37 J 729 ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE GLU ILE
SEQRES 38 J 729 ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS PRO ALA
SEQRES 39 J 729 THR PHE THR ASP THR THR HIS TYR PRO LEU LEU LEU VAL
SEQRES 40 J 729 VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA GLU LYS
SEQRES 41 J 729 PHE GLU VAL SER TRP GLU THR VAL MET VAL SER SER HIS
SEQRES 42 J 729 GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY SER GLY
SEQRES 43 J 729 PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG ARG ARG
SEQRES 44 J 729 LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU ALA VAL
SEQRES 45 J 729 ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG THR ARG
SEQRES 46 J 729 VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR LEU SER
SEQRES 47 J 729 THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN GLY GLN
SEQRES 48 J 729 THR PHE THR CYS GLY SER ALA LEU SER PRO ILE THR ASP
SEQRES 49 J 729 PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG TYR LEU
SEQRES 50 J 729 GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU MET THR
SEQRES 51 J 729 LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU GLN GLN
SEQRES 52 J 729 PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS ILE HIS
SEQRES 53 J 729 PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU ILE ARG
SEQRES 54 J 729 GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO ASP GLU
SEQRES 55 J 729 SER HIS TYR PHE THR SER SER SER LEU LYS GLN HIS LEU
SEQRES 56 J 729 TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS PHE ARG
SEQRES 57 J 729 ILE
SEQRES 1 I 729 GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL THR VAL
SEQRES 2 I 729 GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS ASP PRO
SEQRES 3 I 729 GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE TYR ARG
SEQRES 4 I 729 GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL GLU THR
SEQRES 5 I 729 ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS ILE GLU
SEQRES 6 I 729 SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO ASP ARG
SEQRES 7 I 729 GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO ILE TYR
SEQRES 8 I 729 GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER LYS ILE
SEQRES 9 I 729 PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO GLU VAL
SEQRES 10 I 729 SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY PRO LYS
SEQRES 11 I 729 GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN ILE TYR
SEQRES 12 I 729 TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG VAL VAL
SEQRES 13 I 729 SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY LEU SER
SEQRES 14 I 729 ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR HIS ILE
SEQRES 15 I 729 ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU ALA TYR
SEQRES 16 I 729 ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET GLU LEU
SEQRES 17 I 729 PRO THR TYR THR GLY SER ILE TYR PRO THR VAL LYS PRO
SEQRES 18 I 729 TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO SER ILE
SEQRES 19 I 729 SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR HIS ASP
SEQRES 20 I 729 LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET ARG GLU
SEQRES 21 I 729 TYR TYR ILE THR MET VAL LYS TRP ALA THR SER THR LYS
SEQRES 22 I 729 VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN VAL SER
SEQRES 23 I 729 ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL CYS THR
SEQRES 24 I 729 LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU HIS ARG
SEQRES 25 I 729 GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY ARG LYS
SEQRES 26 I 729 PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY ARG GLY
SEQRES 27 I 729 LYS PHE TYR HIS ILE THR VAL SER SER SER GLN PRO ASN
SEQRES 28 I 729 SER SER ASN ASP ASN ILE GLN SER ILE THR SER GLY ASP
SEQRES 29 I 729 TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU LYS GLY
SEQRES 30 I 729 ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU PRO ARG
SEQRES 31 I 729 ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY ASN PHE
SEQRES 32 I 729 ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU ASN CYS
SEQRES 33 I 729 THR TYR PHE SER ALA SER PHE SER HIS SER MET ASP PHE
SEQRES 34 I 729 PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO MET VAL
SEQRES 35 I 729 THR VAL HIS ASN THR THR ASP LYS LYS LYS MET PHE ASP
SEQRES 36 I 729 LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE ASN ASP
SEQRES 37 I 729 ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE GLU ILE
SEQRES 38 I 729 ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS PRO ALA
SEQRES 39 I 729 THR PHE THR ASP THR THR HIS TYR PRO LEU LEU LEU VAL
SEQRES 40 I 729 VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA GLU LYS
SEQRES 41 I 729 PHE GLU VAL SER TRP GLU THR VAL MET VAL SER SER HIS
SEQRES 42 I 729 GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY SER GLY
SEQRES 43 I 729 PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG ARG ARG
SEQRES 44 I 729 LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU ALA VAL
SEQRES 45 I 729 ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG THR ARG
SEQRES 46 I 729 VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR LEU SER
SEQRES 47 I 729 THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN GLY GLN
SEQRES 48 I 729 THR PHE THR CYS GLY SER ALA LEU SER PRO ILE THR ASP
SEQRES 49 I 729 PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG TYR LEU
SEQRES 50 I 729 GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU MET THR
SEQRES 51 I 729 LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU GLN GLN
SEQRES 52 I 729 PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS ILE HIS
SEQRES 53 I 729 PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU ILE ARG
SEQRES 54 I 729 GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO ASP GLU
SEQRES 55 I 729 SER HIS TYR PHE THR SER SER SER LEU LYS GLN HIS LEU
SEQRES 56 I 729 TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS PHE ARG
SEQRES 57 I 729 ILE
SEQRES 1 A 729 GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL THR VAL
SEQRES 2 A 729 GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS ASP PRO
SEQRES 3 A 729 GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE TYR ARG
SEQRES 4 A 729 GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL GLU THR
SEQRES 5 A 729 ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS ILE GLU
SEQRES 6 A 729 SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO ASP ARG
SEQRES 7 A 729 GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO ILE TYR
SEQRES 8 A 729 GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER LYS ILE
SEQRES 9 A 729 PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO GLU VAL
SEQRES 10 A 729 SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY PRO LYS
SEQRES 11 A 729 GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN ILE TYR
SEQRES 12 A 729 TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG VAL VAL
SEQRES 13 A 729 SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY LEU SER
SEQRES 14 A 729 ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR HIS ILE
SEQRES 15 A 729 ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU ALA TYR
SEQRES 16 A 729 ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET GLU LEU
SEQRES 17 A 729 PRO THR TYR THR GLY SER ILE TYR PRO THR VAL LYS PRO
SEQRES 18 A 729 TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO SER ILE
SEQRES 19 A 729 SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR HIS ASP
SEQRES 20 A 729 LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET ARG GLU
SEQRES 21 A 729 TYR TYR ILE THR MET VAL LYS TRP ALA THR SER THR LYS
SEQRES 22 A 729 VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN VAL SER
SEQRES 23 A 729 ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL CYS THR
SEQRES 24 A 729 LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU HIS ARG
SEQRES 25 A 729 GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY ARG LYS
SEQRES 26 A 729 PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY ARG GLY
SEQRES 27 A 729 LYS PHE TYR HIS ILE THR VAL SER SER SER GLN PRO ASN
SEQRES 28 A 729 SER SER ASN ASP ASN ILE GLN SER ILE THR SER GLY ASP
SEQRES 29 A 729 TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU LYS GLY
SEQRES 30 A 729 ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU PRO ARG
SEQRES 31 A 729 ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY ASN PHE
SEQRES 32 A 729 ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU ASN CYS
SEQRES 33 A 729 THR TYR PHE SER ALA SER PHE SER HIS SER MET ASP PHE
SEQRES 34 A 729 PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO MET VAL
SEQRES 35 A 729 THR VAL HIS ASN THR THR ASP LYS LYS LYS MET PHE ASP
SEQRES 36 A 729 LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE ASN ASP
SEQRES 37 A 729 ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE GLU ILE
SEQRES 38 A 729 ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS PRO ALA
SEQRES 39 A 729 THR PHE THR ASP THR THR HIS TYR PRO LEU LEU LEU VAL
SEQRES 40 A 729 VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA GLU LYS
SEQRES 41 A 729 PHE GLU VAL SER TRP GLU THR VAL MET VAL SER SER HIS
SEQRES 42 A 729 GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY SER GLY
SEQRES 43 A 729 PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG ARG ARG
SEQRES 44 A 729 LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU ALA VAL
SEQRES 45 A 729 ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG THR ARG
SEQRES 46 A 729 VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR LEU SER
SEQRES 47 A 729 THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN GLY GLN
SEQRES 48 A 729 THR PHE THR CYS GLY SER ALA LEU SER PRO ILE THR ASP
SEQRES 49 A 729 PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG TYR LEU
SEQRES 50 A 729 GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU MET THR
SEQRES 51 A 729 LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU GLN GLN
SEQRES 52 A 729 PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS ILE HIS
SEQRES 53 A 729 PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU ILE ARG
SEQRES 54 A 729 GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO ASP GLU
SEQRES 55 A 729 SER HIS TYR PHE THR SER SER SER LEU LYS GLN HIS LEU
SEQRES 56 A 729 TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS PHE ARG
SEQRES 57 A 729 ILE
SEQRES 1 B 729 GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL THR VAL
SEQRES 2 B 729 GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS ASP PRO
SEQRES 3 B 729 GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE TYR ARG
SEQRES 4 B 729 GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL GLU THR
SEQRES 5 B 729 ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS ILE GLU
SEQRES 6 B 729 SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO ASP ARG
SEQRES 7 B 729 GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO ILE TYR
SEQRES 8 B 729 GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER LYS ILE
SEQRES 9 B 729 PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO GLU VAL
SEQRES 10 B 729 SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY PRO LYS
SEQRES 11 B 729 GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN ILE TYR
SEQRES 12 B 729 TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG VAL VAL
SEQRES 13 B 729 SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY LEU SER
SEQRES 14 B 729 ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR HIS ILE
SEQRES 15 B 729 ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU ALA TYR
SEQRES 16 B 729 ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET GLU LEU
SEQRES 17 B 729 PRO THR TYR THR GLY SER ILE TYR PRO THR VAL LYS PRO
SEQRES 18 B 729 TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO SER ILE
SEQRES 19 B 729 SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR HIS ASP
SEQRES 20 B 729 LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET ARG GLU
SEQRES 21 B 729 TYR TYR ILE THR MET VAL LYS TRP ALA THR SER THR LYS
SEQRES 22 B 729 VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN VAL SER
SEQRES 23 B 729 ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL CYS THR
SEQRES 24 B 729 LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU HIS ARG
SEQRES 25 B 729 GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY ARG LYS
SEQRES 26 B 729 PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY ARG GLY
SEQRES 27 B 729 LYS PHE TYR HIS ILE THR VAL SER SER SER GLN PRO ASN
SEQRES 28 B 729 SER SER ASN ASP ASN ILE GLN SER ILE THR SER GLY ASP
SEQRES 29 B 729 TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU LYS GLY
SEQRES 30 B 729 ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU PRO ARG
SEQRES 31 B 729 ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY ASN PHE
SEQRES 32 B 729 ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU ASN CYS
SEQRES 33 B 729 THR TYR PHE SER ALA SER PHE SER HIS SER MET ASP PHE
SEQRES 34 B 729 PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO MET VAL
SEQRES 35 B 729 THR VAL HIS ASN THR THR ASP LYS LYS LYS MET PHE ASP
SEQRES 36 B 729 LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE ASN ASP
SEQRES 37 B 729 ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE GLU ILE
SEQRES 38 B 729 ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS PRO ALA
SEQRES 39 B 729 THR PHE THR ASP THR THR HIS TYR PRO LEU LEU LEU VAL
SEQRES 40 B 729 VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA GLU LYS
SEQRES 41 B 729 PHE GLU VAL SER TRP GLU THR VAL MET VAL SER SER HIS
SEQRES 42 B 729 GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY SER GLY
SEQRES 43 B 729 PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG ARG ARG
SEQRES 44 B 729 LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU ALA VAL
SEQRES 45 B 729 ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG THR ARG
SEQRES 46 B 729 VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR LEU SER
SEQRES 47 B 729 THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN GLY GLN
SEQRES 48 B 729 THR PHE THR CYS GLY SER ALA LEU SER PRO ILE THR ASP
SEQRES 49 B 729 PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG TYR LEU
SEQRES 50 B 729 GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU MET THR
SEQRES 51 B 729 LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU GLN GLN
SEQRES 52 B 729 PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS ILE HIS
SEQRES 53 B 729 PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU ILE ARG
SEQRES 54 B 729 GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO ASP GLU
SEQRES 55 B 729 SER HIS TYR PHE THR SER SER SER LEU LYS GLN HIS LEU
SEQRES 56 B 729 TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS PHE ARG
SEQRES 57 B 729 ILE
HELIX 1 AA1 THR J 70 SER J 76 1 7
HELIX 2 AA2 GLU J 77 LYS J 80 5 4
HELIX 3 AA3 GLU J 118 ILE J 122 5 5
HELIX 4 AA4 TRP J 229 GLU J 234 1 6
HELIX 5 AA5 ASN J 517 ARG J 527 1 11
HELIX 6 AA6 SER J 582 GLY J 592 1 11
HELIX 7 AA7 GLY J 607 GLU J 613 1 7
HELIX 8 AA8 GLY J 619 LEU J 634 1 16
HELIX 9 AA9 ASP J 650 ILE J 659 1 10
HELIX 10 AB1 ASP J 682 TYR J 686 5 5
HELIX 11 AB2 ALA J 687 GLY J 696 1 10
HELIX 12 AB3 HIS J 734 LYS J 749 1 16
HELIX 13 AB4 SER J 766 ARG J 786 1 21
HELIX 14 AB5 THR I 70 SER I 76 5 7
HELIX 15 AB6 ASP I 228 GLU I 234 1 7
HELIX 16 AB7 ASN I 517 ARG I 527 1 11
HELIX 17 AB8 SER I 582 HIS I 591 1 10
HELIX 18 AB9 GLY I 607 GLU I 613 1 7
HELIX 19 AC1 GLY I 619 LYS I 635 1 17
HELIX 20 AC2 ASP I 650 ILE I 659 1 10
HELIX 21 AC3 ALA I 687 GLY I 696 1 10
HELIX 22 AC4 VAL I 710 SER I 715 1 6
HELIX 23 AC5 HIS I 734 LYS I 749 1 16
HELIX 24 AC6 SER I 766 PHE I 785 1 20
HELIX 25 AC7 THR A 70 SER A 76 1 7
HELIX 26 AC8 GLU A 77 LYS A 80 5 4
HELIX 27 AC9 GLU A 118 ILE A 122 5 5
HELIX 28 AD1 TRP A 229 GLU A 234 1 6
HELIX 29 AD2 ASN A 517 ARG A 527 1 11
HELIX 30 AD3 SER A 582 GLY A 592 1 11
HELIX 31 AD4 GLY A 607 GLU A 613 1 7
HELIX 32 AD5 GLY A 619 LEU A 634 1 16
HELIX 33 AD6 ASP A 650 ILE A 659 1 10
HELIX 34 AD7 ASP A 682 TYR A 686 5 5
HELIX 35 AD8 ALA A 687 GLY A 696 1 10
HELIX 36 AD9 HIS A 734 LYS A 749 1 16
HELIX 37 AE1 SER A 766 ARG A 786 1 21
HELIX 38 AE2 THR B 70 SER B 76 5 7
HELIX 39 AE3 ASP B 228 GLU B 234 1 7
HELIX 40 AE4 ASN B 517 ARG B 527 1 11
HELIX 41 AE5 SER B 582 HIS B 591 1 10
HELIX 42 AE6 GLY B 607 GLU B 613 1 7
HELIX 43 AE7 GLY B 619 LYS B 635 1 17
HELIX 44 AE8 ASP B 650 ILE B 659 1 10
HELIX 45 AE9 ALA B 687 GLY B 696 1 10
HELIX 46 AF1 VAL B 710 SER B 715 1 6
HELIX 47 AF2 HIS B 734 LYS B 749 1 16
HELIX 48 AF3 SER B 766 PHE B 785 1 20
SHEET 1 AA1 4 TRP J 88 SER J 90 0
SHEET 2 AA1 4 GLU J 93 PHE J 94 -1 O GLU J 93 N SER J 90
SHEET 3 AA1 4 VAL J 103 ASN J 107 -1 O TRP J 106 N PHE J 94
SHEET 4 AA1 4 THR J 112 ILE J 117 -1 O THR J 114 N LEU J 105
SHEET 1 AA2 4 ARG J 129 ILE J 132 0
SHEET 2 AA2 4 TYR J 138 TYR J 143 -1 O LEU J 140 N GLU J 131
SHEET 3 AA2 4 TYR J 156 LYS J 161 -1 O VAL J 158 N PHE J 141
SHEET 4 AA2 4 GLN J 168 SER J 169 -1 O GLN J 168 N LEU J 159
SHEET 1 AA3 3 LEU J 192 PHE J 196 0
SHEET 2 AA3 3 ASN J 199 CYS J 203 -1 O CYS J 203 N LEU J 192
SHEET 3 AA3 3 ILE J 211 VAL J 214 -1 O VAL J 214 N ILE J 200
SHEET 1 AA4 3 ILE J 222 ASN J 224 0
SHEET 2 AA4 3 ARG J 250 ASN J 257 -1 O ILE J 256 N TYR J 223
SHEET 3 AA4 3 HIS J 242 TRP J 244 -1 N TRP J 243 O ALA J 252
SHEET 1 AA5 4 ILE J 222 ASN J 224 0
SHEET 2 AA5 4 ARG J 250 ASN J 257 -1 O ILE J 256 N TYR J 223
SHEET 3 AA5 4 SER J 291 GLY J 298 -1 O HIS J 295 N TYR J 253
SHEET 4 AA5 4 LEU J 306 GLU J 307 -1 O LEU J 306 N VAL J 296
SHEET 1 AA6 2 MET J 264 LEU J 266 0
SHEET 2 AA6 2 LYS J 278 TYR J 280 -1 O TYR J 280 N MET J 264
SHEET 1 AA7 4 TYR J 319 TRP J 326 0
SHEET 2 AA7 4 LYS J 331 ASN J 338 -1 O THR J 335 N MET J 323
SHEET 3 AA7 4 VAL J 343 ASP J 350 -1 O ILE J 345 N TRP J 336
SHEET 4 AA7 4 VAL J 355 GLU J 363 -1 O THR J 357 N LEU J 348
SHEET 1 AA8 2 PHE J 384 ALA J 389 0
SHEET 2 AA8 2 TYR J 399 SER J 404 -1 O THR J 402 N PHE J 386
SHEET 1 AA9 3 VAL J 425 ASP J 432 0
SHEET 2 AA9 3 LYS J 437 SER J 442 -1 O LEU J 441 N LYS J 427
SHEET 3 AA9 3 GLN J 451 ALA J 455 -1 O GLN J 451 N SER J 442
SHEET 1 AB1 4 SER J 478 PHE J 481 0
SHEET 2 AB1 4 PHE J 487 LYS J 491 -1 O LEU J 489 N SER J 480
SHEET 3 AB1 4 VAL J 500 ASN J 504 -1 O THR J 501 N LEU J 490
SHEET 4 AB1 4 ASP J 513 GLU J 515 -1 O GLU J 515 N VAL J 500
SHEET 1 AB2 7 LYS J 531 TYR J 534 0
SHEET 2 AB2 7 MET J 546 LYS J 550 -1 O LYS J 550 N LYS J 531
SHEET 3 AB2 7 VAL J 594 CYS J 598 -1 O LYS J 597 N GLN J 547
SHEET 4 AB2 7 TYR J 560 VAL J 565 1 N LEU J 563 O VAL J 594
SHEET 5 AB2 7 ILE J 639 PHE J 647 1 O ALA J 645 N LEU J 562
SHEET 6 AB2 7 CYS J 673 GLY J 674 1 N CYS J 673 O VAL J 644
SHEET 7 AB2 7 GLN J 721 PHE J 722 1 O GLN J 721 N GLY J 674
SHEET 1 AB3 2 ILE J 537 ILE J 539 0
SHEET 2 AB3 2 TYR J 542 LEU J 544 -1 O LEU J 544 N ILE J 537
SHEET 1 AB4 2 ILE J 725 PRO J 727 0
SHEET 2 AB4 2 GLN J 755 TYR J 757 1 O GLN J 755 N HIS J 726
SHEET 1 AB5 2 TRP I 88 SER I 90 0
SHEET 2 AB5 2 GLU I 93 PHE I 94 -1 O GLU I 93 N SER I 90
SHEET 1 AB6 2 VAL I 103 ASN I 107 0
SHEET 2 AB6 2 THR I 112 ILE I 117 -1 O THR I 112 N ASN I 107
SHEET 1 AB7 3 ARG I 129 ILE I 132 0
SHEET 2 AB7 3 TYR I 138 TYR I 143 -1 O LEU I 140 N GLU I 131
SHEET 3 AB7 3 TYR I 156 LYS I 161 -1 O VAL I 158 N PHE I 141
SHEET 1 AB8 3 LEU I 192 ILE I 195 0
SHEET 2 AB8 3 ILE I 200 CYS I 203 -1 O CYS I 203 N LEU I 192
SHEET 3 AB8 3 ILE I 211 VAL I 214 -1 O VAL I 214 N ILE I 200
SHEET 1 AB9 3 ILE I 222 ASN I 224 0
SHEET 2 AB9 3 ARG I 250 ASN I 257 -1 O ILE I 256 N TYR I 223
SHEET 3 AB9 3 HIS I 242 TRP I 244 -1 N TRP I 243 O ALA I 252
SHEET 1 AC1 4 ILE I 222 ASN I 224 0
SHEET 2 AC1 4 ARG I 250 ASN I 257 -1 O ILE I 256 N TYR I 223
SHEET 3 AC1 4 SER I 291 GLY I 298 -1 O SER I 291 N ASN I 257
SHEET 4 AC1 4 LEU I 306 GLU I 307 -1 O LEU I 306 N VAL I 296
SHEET 1 AC2 2 ILE I 263 LEU I 266 0
SHEET 2 AC2 2 LYS I 278 HIS I 281 -1 O TYR I 280 N MET I 264
SHEET 1 AC3 4 TYR I 319 TRP I 326 0
SHEET 2 AC3 4 LYS I 331 ASN I 338 -1 O THR I 335 N MET I 323
SHEET 3 AC3 4 VAL I 343 ASP I 350 -1 O THR I 347 N VAL I 334
SHEET 4 AC3 4 CYS I 356 GLU I 363 -1 O THR I 357 N LEU I 348
SHEET 1 AC4 2 PHE I 384 ALA I 389 0
SHEET 2 AC4 2 TYR I 399 SER I 404 -1 O SER I 404 N PHE I 384
SHEET 1 AC5 4 VAL I 425 ASP I 432 0
SHEET 2 AC5 4 LYS I 437 SER I 442 -1 O TYR I 439 N ALA I 430
SHEET 3 AC5 4 GLN I 451 ALA I 455 -1 O GLN I 451 N SER I 442
SHEET 4 AC5 4 GLN I 464 CYS I 465 -1 O GLN I 464 N SER I 454
SHEET 1 AC6 4 SER I 478 PHE I 481 0
SHEET 2 AC6 4 PHE I 487 LYS I 491 -1 O LYS I 491 N SER I 478
SHEET 3 AC6 4 VAL I 500 ASN I 504 -1 O HIS I 503 N PHE I 488
SHEET 4 AC6 4 ASP I 513 GLU I 515 -1 O GLU I 515 N VAL I 500
SHEET 1 AC7 5 LYS I 531 VAL I 532 0
SHEET 2 AC7 5 MET I 546 LYS I 550 -1 O LYS I 550 N LYS I 531
SHEET 3 AC7 5 VAL I 594 CYS I 598 -1 O VAL I 595 N LEU I 549
SHEET 4 AC7 5 TYR I 560 VAL I 565 1 N VAL I 565 O VAL I 596
SHEET 5 AC7 5 ILE I 639 PHE I 647 1 O ALA I 645 N LEU I 562
SHEET 1 AC8 2 ILE I 537 ILE I 539 0
SHEET 2 AC8 2 TYR I 542 LEU I 544 -1 O LEU I 544 N ILE I 537
SHEET 1 AC9 2 PHE I 722 PRO I 727 0
SHEET 2 AC9 2 TYR I 752 TYR I 757 1 O GLN I 755 N ILE I 724
SHEET 1 AD1 4 TRP A 88 SER A 90 0
SHEET 2 AD1 4 GLU A 93 PHE A 94 -1 O GLU A 93 N ILE A 89
SHEET 3 AD1 4 VAL A 103 ASN A 107 -1 O TRP A 106 N PHE A 94
SHEET 4 AD1 4 THR A 112 ILE A 117 -1 O THR A 114 N LEU A 105
SHEET 1 AD2 4 ARG A 129 ILE A 132 0
SHEET 2 AD2 4 TYR A 138 TYR A 143 -1 O LEU A 140 N GLU A 131
SHEET 3 AD2 4 TYR A 156 LYS A 161 -1 O VAL A 158 N PHE A 141
SHEET 4 AD2 4 GLN A 168 SER A 169 -1 O GLN A 168 N LEU A 159
SHEET 1 AD3 3 LEU A 192 PHE A 196 0
SHEET 2 AD3 3 ASN A 199 CYS A 203 -1 O CYS A 203 N LEU A 192
SHEET 3 AD3 3 ILE A 211 VAL A 214 -1 O VAL A 214 N ILE A 200
SHEET 1 AD4 3 ILE A 222 ASN A 224 0
SHEET 2 AD4 3 ARG A 250 ASN A 257 -1 O ILE A 256 N TYR A 223
SHEET 3 AD4 3 HIS A 242 TRP A 244 -1 N TRP A 243 O ALA A 252
SHEET 1 AD5 4 ILE A 222 ASN A 224 0
SHEET 2 AD5 4 ARG A 250 ASN A 257 -1 O ILE A 256 N TYR A 223
SHEET 3 AD5 4 SER A 291 GLY A 298 -1 O HIS A 295 N TYR A 253
SHEET 4 AD5 4 LEU A 306 GLU A 307 -1 O LEU A 306 N VAL A 296
SHEET 1 AD6 2 MET A 264 LEU A 266 0
SHEET 2 AD6 2 LYS A 278 TYR A 280 -1 O TYR A 280 N MET A 264
SHEET 1 AD7 4 TYR A 319 TRP A 326 0
SHEET 2 AD7 4 LYS A 331 ASN A 338 -1 O THR A 335 N MET A 323
SHEET 3 AD7 4 VAL A 343 ASP A 350 -1 O ILE A 345 N TRP A 336
SHEET 4 AD7 4 VAL A 355 GLU A 363 -1 O THR A 357 N LEU A 348
SHEET 1 AD8 2 PHE A 384 ALA A 389 0
SHEET 2 AD8 2 TYR A 399 SER A 404 -1 O THR A 402 N PHE A 386
SHEET 1 AD9 3 VAL A 425 ASP A 432 0
SHEET 2 AD9 3 LYS A 437 SER A 442 -1 O LEU A 441 N LYS A 427
SHEET 3 AD9 3 GLN A 451 ALA A 455 -1 O GLN A 451 N SER A 442
SHEET 1 AE1 4 SER A 478 PHE A 481 0
SHEET 2 AE1 4 PHE A 487 LYS A 491 -1 O LEU A 489 N SER A 480
SHEET 3 AE1 4 VAL A 500 ASN A 504 -1 O THR A 501 N LEU A 490
SHEET 4 AE1 4 ASP A 513 GLU A 515 -1 O GLU A 515 N VAL A 500
SHEET 1 AE2 7 LYS A 531 TYR A 534 0
SHEET 2 AE2 7 MET A 546 LYS A 550 -1 O LYS A 550 N LYS A 531
SHEET 3 AE2 7 VAL A 594 CYS A 598 -1 O LYS A 597 N GLN A 547
SHEET 4 AE2 7 TYR A 560 VAL A 565 1 N LEU A 563 O VAL A 594
SHEET 5 AE2 7 ILE A 639 PHE A 647 1 O ALA A 645 N LEU A 562
SHEET 6 AE2 7 CYS A 673 GLY A 674 1 N CYS A 673 O VAL A 644
SHEET 7 AE2 7 GLN A 721 PHE A 722 1 O GLN A 721 N GLY A 674
SHEET 1 AE3 2 ILE A 537 ILE A 539 0
SHEET 2 AE3 2 TYR A 542 LEU A 544 -1 O LEU A 544 N ILE A 537
SHEET 1 AE4 2 ILE A 725 PRO A 727 0
SHEET 2 AE4 2 GLN A 755 TYR A 757 1 O GLN A 755 N HIS A 726
SHEET 1 AE5 2 TRP B 88 SER B 90 0
SHEET 2 AE5 2 GLU B 93 PHE B 94 -1 O GLU B 93 N SER B 90
SHEET 1 AE6 2 VAL B 103 ASN B 107 0
SHEET 2 AE6 2 THR B 112 ILE B 117 -1 O THR B 112 N ASN B 107
SHEET 1 AE7 3 ARG B 129 ILE B 132 0
SHEET 2 AE7 3 TYR B 138 TYR B 143 -1 O LEU B 140 N GLU B 131
SHEET 3 AE7 3 TYR B 156 LYS B 161 -1 O VAL B 158 N PHE B 141
SHEET 1 AE8 3 LEU B 192 ILE B 195 0
SHEET 2 AE8 3 ILE B 200 CYS B 203 -1 O CYS B 203 N LEU B 192
SHEET 3 AE8 3 ILE B 211 VAL B 214 -1 O VAL B 214 N ILE B 200
SHEET 1 AE9 3 ILE B 222 ASN B 224 0
SHEET 2 AE9 3 ARG B 250 ASN B 257 -1 O ILE B 256 N TYR B 223
SHEET 3 AE9 3 HIS B 242 TRP B 244 -1 N TRP B 243 O ALA B 252
SHEET 1 AF1 4 ILE B 222 ASN B 224 0
SHEET 2 AF1 4 ARG B 250 ASN B 257 -1 O ILE B 256 N TYR B 223
SHEET 3 AF1 4 SER B 291 GLY B 298 -1 O SER B 291 N ASN B 257
SHEET 4 AF1 4 LEU B 306 GLU B 307 -1 O LEU B 306 N VAL B 296
SHEET 1 AF2 2 ILE B 263 LEU B 266 0
SHEET 2 AF2 2 LYS B 278 HIS B 281 -1 O TYR B 280 N MET B 264
SHEET 1 AF3 4 TYR B 319 TRP B 326 0
SHEET 2 AF3 4 LYS B 331 ASN B 338 -1 O THR B 335 N MET B 323
SHEET 3 AF3 4 VAL B 343 ASP B 350 -1 O THR B 347 N VAL B 334
SHEET 4 AF3 4 CYS B 356 GLU B 363 -1 O THR B 357 N LEU B 348
SHEET 1 AF4 2 PHE B 384 ALA B 389 0
SHEET 2 AF4 2 TYR B 399 SER B 404 -1 O SER B 404 N PHE B 384
SHEET 1 AF5 4 VAL B 425 ASP B 432 0
SHEET 2 AF5 4 LYS B 437 SER B 442 -1 O TYR B 439 N ALA B 430
SHEET 3 AF5 4 GLN B 451 ALA B 455 -1 O GLN B 451 N SER B 442
SHEET 4 AF5 4 GLN B 464 CYS B 465 -1 O GLN B 464 N SER B 454
SHEET 1 AF6 4 SER B 478 PHE B 481 0
SHEET 2 AF6 4 PHE B 487 LYS B 491 -1 O LYS B 491 N SER B 478
SHEET 3 AF6 4 VAL B 500 ASN B 504 -1 O HIS B 503 N PHE B 488
SHEET 4 AF6 4 ASP B 513 GLU B 515 -1 O GLU B 515 N VAL B 500
SHEET 1 AF7 5 LYS B 531 VAL B 532 0
SHEET 2 AF7 5 ILE B 548 LYS B 550 -1 O LYS B 550 N LYS B 531
SHEET 3 AF7 5 VAL B 594 VAL B 596 -1 O VAL B 595 N LEU B 549
SHEET 4 AF7 5 TYR B 560 VAL B 565 1 N VAL B 565 O VAL B 596
SHEET 5 AF7 5 ILE B 639 PHE B 647 1 O ALA B 645 N LEU B 562
SHEET 1 AF8 2 ILE B 537 ILE B 539 0
SHEET 2 AF8 2 TYR B 542 LEU B 544 -1 O LEU B 544 N ILE B 537
SHEET 1 AF9 2 PHE B 722 PRO B 727 0
SHEET 2 AF9 2 TYR B 752 TYR B 757 1 O GLN B 755 N ILE B 724
SSBOND 1 CYS J 349 CYS J 356 1555 1555 2.03
SSBOND 2 CYS J 465 CYS J 468 1555 1555 2.03
SSBOND 3 CYS J 474 CYS J 492 1555 1555 2.03
SSBOND 4 CYS J 673 CYS J 784 1555 1555 2.03
SSBOND 5 CYS I 349 CYS I 356 1555 1555 2.03
SSBOND 6 CYS I 465 CYS I 468 1555 1555 2.03
SSBOND 7 CYS I 474 CYS I 492 1555 1555 2.03
SSBOND 8 CYS I 673 CYS I 784 1555 1555 2.03
SSBOND 9 CYS A 349 CYS A 356 1555 1555 2.03
SSBOND 10 CYS A 465 CYS A 468 1555 1555 2.03
SSBOND 11 CYS A 474 CYS A 492 1555 1555 2.03
SSBOND 12 CYS A 673 CYS A 784 1555 1555 2.03
SSBOND 13 CYS B 349 CYS B 356 1555 1555 2.03
SSBOND 14 CYS B 465 CYS B 468 1555 1555 2.03
SSBOND 15 CYS B 474 CYS B 492 1555 1555 2.03
SSBOND 16 CYS B 673 CYS B 784 1555 1555 2.03
CISPEP 1 GLY J 494 PRO J 495 0 -4.69
CISPEP 2 GLY I 494 PRO I 495 0 -4.54
CISPEP 3 GLY A 494 PRO A 495 0 -4.53
CISPEP 4 GLY B 494 PRO B 495 0 -4.53
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 5883 ILE J 787
TER 11766 ILE I 787
TER 17649 ILE A 787
TER 23532 ILE B 787
MASTER 180 0 0 48 172 0 0 623528 4 32 228
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