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HEADER MEMBRANE PROTEIN 01-MAR-21 7E8B
TITLE CRYOEM STRUCTURE OF HUMAN KV4.2-DPP6S COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 3 CHAIN: L, K, J, I;
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;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;
COMPND 15 CHAIN: A, C;
COMPND 16 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;
COMPND 17 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;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: KCND2, KIAA1044;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: KCND2, KIAA1044;
SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.KISE,O.NUREKI
REVDAT 1 13-OCT-21 7E8B 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. 4.20 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 : REAL
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) : 4.200
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 7E8B 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_1300020962.
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, K, B, A, J, I, D, C
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 ALA B 161
REMARK 465 LEU B 162
REMARK 465 PRO B 163
REMARK 465 THR B 164
REMARK 465 MET B 165
REMARK 465 THR B 166
REMARK 465 PRO B 220
REMARK 465 CYS B 221
REMARK 465 GLY B 222
REMARK 465 GLU B 223
REMARK 465 GLU A 159
REMARK 465 SER A 160
REMARK 465 ALA A 161
REMARK 465 LEU A 162
REMARK 465 PRO A 163
REMARK 465 PRO A 220
REMARK 465 CYS A 221
REMARK 465 GLY A 222
REMARK 465 GLU A 223
REMARK 465 ALA D 161
REMARK 465 LEU D 162
REMARK 465 PRO D 163
REMARK 465 THR D 164
REMARK 465 MET D 165
REMARK 465 THR D 166
REMARK 465 PRO D 220
REMARK 465 CYS D 221
REMARK 465 GLY D 222
REMARK 465 GLU D 223
REMARK 465 GLU C 159
REMARK 465 SER C 160
REMARK 465 ALA C 161
REMARK 465 LEU C 162
REMARK 465 PRO C 163
REMARK 465 PRO C 220
REMARK 465 CYS C 221
REMARK 465 GLY C 222
REMARK 465 GLU C 223
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 OE2 GLU C 346 OG1 THR C 380 2.12
REMARK 500 OE2 GLU A 346 OG1 THR A 380 2.12
REMARK 500 OD1 ASP D 116 OH TYR D 137 2.16
REMARK 500 OD1 ASP B 116 OH TYR B 137 2.16
REMARK 500 OH TYR I 96 OE1 GLN I 99 2.19
REMARK 500 OH TYR K 96 OE1 GLN K 99 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS L 468 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 CYS J 468 CA - CB - SG ANGL. DEV. = 8.1 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 LYS L 32 -9.61 70.10
REMARK 500 ALA L 58 -61.32 -92.46
REMARK 500 SER L 62 -125.27 58.83
REMARK 500 GLN L 65 148.14 68.54
REMARK 500 LYS L 100 45.61 -141.37
REMARK 500 ASN L 111 48.45 36.37
REMARK 500 SER L 124 51.32 -91.52
REMARK 500 SER L 152 45.75 -141.14
REMARK 500 HIS L 164 173.16 179.30
REMARK 500 SER L 176 -166.66 -79.53
REMARK 500 MET L 316 19.53 -140.23
REMARK 500 MET L 323 148.20 -170.77
REMARK 500 ARG L 382 -166.68 -77.38
REMARK 500 LYS L 434 57.57 -93.50
REMARK 500 SER L 467 -64.07 -92.49
REMARK 500 THR L 475 8.41 57.90
REMARK 500 ASP L 540 -126.01 57.03
REMARK 500 ALA L 552 -5.18 72.10
REMARK 500 PHE L 605 -4.64 68.83
REMARK 500 ASP L 650 -122.08 50.46
REMARK 500 ARG L 703 -4.85 70.05
REMARK 500 THR L 708 31.85 -98.88
REMARK 500 ALA L 716 -71.98 -63.18
REMARK 500 LEU L 717 51.61 31.62
REMARK 500 ARG K 97 -175.33 -68.98
REMARK 500 GLN K 99 -60.11 -93.50
REMARK 500 LYS K 100 44.28 -141.37
REMARK 500 ASN K 111 56.18 37.47
REMARK 500 HIS K 164 142.45 -170.97
REMARK 500 SER K 176 -167.05 -78.43
REMARK 500 GLU K 197 54.08 37.70
REMARK 500 VAL K 221 -51.96 -121.52
REMARK 500 ILE K 235 -60.39 -122.15
REMARK 500 ARG K 315 33.03 -97.00
REMARK 500 ALA K 366 -62.18 -96.47
REMARK 500 THR K 443 31.64 -98.58
REMARK 500 ASP K 469 148.17 77.47
REMARK 500 GLU K 493 29.21 47.30
REMARK 500 ASP K 540 -117.76 58.12
REMARK 500 GLN K 606 29.48 -141.00
REMARK 500 ARG K 616 19.47 56.48
REMARK 500 ASP K 650 -132.23 53.02
REMARK 500 LEU K 660 62.59 -114.55
REMARK 500 GLN K 667 55.89 -91.45
REMARK 500 LEU K 717 59.66 38.62
REMARK 500 ALA K 729 36.64 -99.51
REMARK 500 PRO B 89 43.71 -86.48
REMARK 500 CYS B 111 -165.81 51.76
REMARK 500 THR B 156 -115.45 51.99
REMARK 500 SER B 211 -168.87 -127.78
REMARK 500
REMARK 500 THIS ENTRY HAS 132 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-31013 RELATED DB: EMDB
REMARK 900 MEMBRANE PROTEIN
DBREF 7E8B L 31 787 UNP P42658 DPP6_HUMAN 93 849
DBREF 7E8B K 31 787 UNP P42658 DPP6_HUMAN 93 849
DBREF 7E8B B 40 437 UNP Q9NZV8 KCND2_HUMAN 40 437
DBREF 7E8B A 40 436 UNP Q9NZV8 KCND2_HUMAN 40 436
DBREF 7E8B J 31 787 UNP P42658 DPP6_HUMAN 93 849
DBREF 7E8B I 31 787 UNP P42658 DPP6_HUMAN 93 849
DBREF 7E8B D 40 437 UNP Q9NZV8 KCND2_HUMAN 40 437
DBREF 7E8B C 40 436 UNP Q9NZV8 KCND2_HUMAN 40 436
SEQRES 1 L 757 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 L 757 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 L 757 PRO ALA GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL
SEQRES 4 L 757 THR VAL GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS
SEQRES 5 L 757 ASP PRO GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE
SEQRES 6 L 757 TYR ARG GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL
SEQRES 7 L 757 GLU THR ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS
SEQRES 8 L 757 ILE GLU SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO
SEQRES 9 L 757 ASP ARG GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO
SEQRES 10 L 757 ILE TYR GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER
SEQRES 11 L 757 LYS ILE PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO
SEQRES 12 L 757 GLU VAL SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY
SEQRES 13 L 757 PRO LYS GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN
SEQRES 14 L 757 ILE TYR TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG
SEQRES 15 L 757 VAL VAL SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY
SEQRES 16 L 757 LEU SER ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR
SEQRES 17 L 757 HIS ILE ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU
SEQRES 18 L 757 ALA TYR ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET
SEQRES 19 L 757 GLU LEU PRO THR TYR THR GLY SER ILE TYR PRO THR VAL
SEQRES 20 L 757 LYS PRO TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO
SEQRES 21 L 757 SER ILE SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR
SEQRES 22 L 757 HIS ASP LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET
SEQRES 23 L 757 ARG GLU TYR TYR ILE THR MET VAL LYS TRP ALA THR SER
SEQRES 24 L 757 THR LYS VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN
SEQRES 25 L 757 VAL SER ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL
SEQRES 26 L 757 CYS THR LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU
SEQRES 27 L 757 HIS ARG GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY
SEQRES 28 L 757 ARG LYS PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY
SEQRES 29 L 757 ARG GLY LYS PHE TYR HIS ILE THR VAL SER SER SER GLN
SEQRES 30 L 757 PRO ASN SER SER ASN ASP ASN ILE GLN SER ILE THR SER
SEQRES 31 L 757 GLY ASP TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU
SEQRES 32 L 757 LYS GLY ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU
SEQRES 33 L 757 PRO ARG ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY
SEQRES 34 L 757 ASN PHE ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU
SEQRES 35 L 757 ASN CYS THR TYR PHE SER ALA SER PHE SER HIS SER MET
SEQRES 36 L 757 ASP PHE PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO
SEQRES 37 L 757 MET VAL THR VAL HIS ASN THR THR ASP LYS LYS LYS MET
SEQRES 38 L 757 PHE ASP LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE
SEQRES 39 L 757 ASN ASP ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE
SEQRES 40 L 757 GLU ILE ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS
SEQRES 41 L 757 PRO ALA THR PHE THR ASP THR THR HIS TYR PRO LEU LEU
SEQRES 42 L 757 LEU VAL VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA
SEQRES 43 L 757 GLU LYS PHE GLU VAL SER TRP GLU THR VAL MET VAL SER
SEQRES 44 L 757 SER HIS GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY
SEQRES 45 L 757 SER GLY PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG
SEQRES 46 L 757 ARG ARG LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU
SEQRES 47 L 757 ALA VAL ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG
SEQRES 48 L 757 THR ARG VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR
SEQRES 49 L 757 LEU SER THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN
SEQRES 50 L 757 GLY GLN THR PHE THR CYS GLY SER ALA LEU SER PRO ILE
SEQRES 51 L 757 THR ASP PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG
SEQRES 52 L 757 TYR LEU GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU
SEQRES 53 L 757 MET THR LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU
SEQRES 54 L 757 GLN GLN PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS
SEQRES 55 L 757 ILE HIS PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU
SEQRES 56 L 757 ILE ARG GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO
SEQRES 57 L 757 ASP GLU SER HIS TYR PHE THR SER SER SER LEU LYS GLN
SEQRES 58 L 757 HIS LEU TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS
SEQRES 59 L 757 PHE ARG ILE
SEQRES 1 K 757 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 K 757 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 K 757 PRO ALA GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL
SEQRES 4 K 757 THR VAL GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS
SEQRES 5 K 757 ASP PRO GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE
SEQRES 6 K 757 TYR ARG GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL
SEQRES 7 K 757 GLU THR ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS
SEQRES 8 K 757 ILE GLU SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO
SEQRES 9 K 757 ASP ARG GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO
SEQRES 10 K 757 ILE TYR GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER
SEQRES 11 K 757 LYS ILE PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO
SEQRES 12 K 757 GLU VAL SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY
SEQRES 13 K 757 PRO LYS GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN
SEQRES 14 K 757 ILE TYR TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG
SEQRES 15 K 757 VAL VAL SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY
SEQRES 16 K 757 LEU SER ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR
SEQRES 17 K 757 HIS ILE ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU
SEQRES 18 K 757 ALA TYR ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET
SEQRES 19 K 757 GLU LEU PRO THR TYR THR GLY SER ILE TYR PRO THR VAL
SEQRES 20 K 757 LYS PRO TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO
SEQRES 21 K 757 SER ILE SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR
SEQRES 22 K 757 HIS ASP LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET
SEQRES 23 K 757 ARG GLU TYR TYR ILE THR MET VAL LYS TRP ALA THR SER
SEQRES 24 K 757 THR LYS VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN
SEQRES 25 K 757 VAL SER ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL
SEQRES 26 K 757 CYS THR LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU
SEQRES 27 K 757 HIS ARG GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY
SEQRES 28 K 757 ARG LYS PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY
SEQRES 29 K 757 ARG GLY LYS PHE TYR HIS ILE THR VAL SER SER SER GLN
SEQRES 30 K 757 PRO ASN SER SER ASN ASP ASN ILE GLN SER ILE THR SER
SEQRES 31 K 757 GLY ASP TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU
SEQRES 32 K 757 LYS GLY ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU
SEQRES 33 K 757 PRO ARG ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY
SEQRES 34 K 757 ASN PHE ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU
SEQRES 35 K 757 ASN CYS THR TYR PHE SER ALA SER PHE SER HIS SER MET
SEQRES 36 K 757 ASP PHE PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO
SEQRES 37 K 757 MET VAL THR VAL HIS ASN THR THR ASP LYS LYS LYS MET
SEQRES 38 K 757 PHE ASP LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE
SEQRES 39 K 757 ASN ASP ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE
SEQRES 40 K 757 GLU ILE ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS
SEQRES 41 K 757 PRO ALA THR PHE THR ASP THR THR HIS TYR PRO LEU LEU
SEQRES 42 K 757 LEU VAL VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA
SEQRES 43 K 757 GLU LYS PHE GLU VAL SER TRP GLU THR VAL MET VAL SER
SEQRES 44 K 757 SER HIS GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY
SEQRES 45 K 757 SER GLY PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG
SEQRES 46 K 757 ARG ARG LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU
SEQRES 47 K 757 ALA VAL ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG
SEQRES 48 K 757 THR ARG VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR
SEQRES 49 K 757 LEU SER THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN
SEQRES 50 K 757 GLY GLN THR PHE THR CYS GLY SER ALA LEU SER PRO ILE
SEQRES 51 K 757 THR ASP PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG
SEQRES 52 K 757 TYR LEU GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU
SEQRES 53 K 757 MET THR LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU
SEQRES 54 K 757 GLN GLN PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS
SEQRES 55 K 757 ILE HIS PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU
SEQRES 56 K 757 ILE ARG GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO
SEQRES 57 K 757 ASP GLU SER HIS TYR PHE THR SER SER SER LEU LYS GLN
SEQRES 58 K 757 HIS LEU TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS
SEQRES 59 K 757 PHE ARG ILE
SEQRES 1 B 398 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 B 398 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 B 398 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 B 398 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 B 398 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 B 398 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 B 398 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 B 398 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 B 398 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 B 398 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 B 398 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 B 398 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 B 398 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 B 398 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 B 398 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 B 398 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 B 398 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 B 398 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 B 398 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 B 398 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 B 398 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 B 398 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 B 398 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 B 398 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 B 398 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 B 398 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 B 398 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 B 398 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 B 398 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 B 398 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 B 398 LEU ALA ARG ILE ARG ALA ALA LYS
SEQRES 1 A 397 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 A 397 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 A 397 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 A 397 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 A 397 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 A 397 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 A 397 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 A 397 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 A 397 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 A 397 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 A 397 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 A 397 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 A 397 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 A 397 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 A 397 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 A 397 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 A 397 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 A 397 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 A 397 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 A 397 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 A 397 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 A 397 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 A 397 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 A 397 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 A 397 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 A 397 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 A 397 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 A 397 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 A 397 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 A 397 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 A 397 LEU ALA ARG ILE ARG ALA ALA
SEQRES 1 J 757 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 J 757 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 J 757 PRO ALA GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL
SEQRES 4 J 757 THR VAL GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS
SEQRES 5 J 757 ASP PRO GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE
SEQRES 6 J 757 TYR ARG GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL
SEQRES 7 J 757 GLU THR ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS
SEQRES 8 J 757 ILE GLU SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO
SEQRES 9 J 757 ASP ARG GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO
SEQRES 10 J 757 ILE TYR GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER
SEQRES 11 J 757 LYS ILE PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO
SEQRES 12 J 757 GLU VAL SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY
SEQRES 13 J 757 PRO LYS GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN
SEQRES 14 J 757 ILE TYR TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG
SEQRES 15 J 757 VAL VAL SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY
SEQRES 16 J 757 LEU SER ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR
SEQRES 17 J 757 HIS ILE ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU
SEQRES 18 J 757 ALA TYR ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET
SEQRES 19 J 757 GLU LEU PRO THR TYR THR GLY SER ILE TYR PRO THR VAL
SEQRES 20 J 757 LYS PRO TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO
SEQRES 21 J 757 SER ILE SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR
SEQRES 22 J 757 HIS ASP LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET
SEQRES 23 J 757 ARG GLU TYR TYR ILE THR MET VAL LYS TRP ALA THR SER
SEQRES 24 J 757 THR LYS VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN
SEQRES 25 J 757 VAL SER ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL
SEQRES 26 J 757 CYS THR LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU
SEQRES 27 J 757 HIS ARG GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY
SEQRES 28 J 757 ARG LYS PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY
SEQRES 29 J 757 ARG GLY LYS PHE TYR HIS ILE THR VAL SER SER SER GLN
SEQRES 30 J 757 PRO ASN SER SER ASN ASP ASN ILE GLN SER ILE THR SER
SEQRES 31 J 757 GLY ASP TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU
SEQRES 32 J 757 LYS GLY ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU
SEQRES 33 J 757 PRO ARG ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY
SEQRES 34 J 757 ASN PHE ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU
SEQRES 35 J 757 ASN CYS THR TYR PHE SER ALA SER PHE SER HIS SER MET
SEQRES 36 J 757 ASP PHE PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO
SEQRES 37 J 757 MET VAL THR VAL HIS ASN THR THR ASP LYS LYS LYS MET
SEQRES 38 J 757 PHE ASP LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE
SEQRES 39 J 757 ASN ASP ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE
SEQRES 40 J 757 GLU ILE ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS
SEQRES 41 J 757 PRO ALA THR PHE THR ASP THR THR HIS TYR PRO LEU LEU
SEQRES 42 J 757 LEU VAL VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA
SEQRES 43 J 757 GLU LYS PHE GLU VAL SER TRP GLU THR VAL MET VAL SER
SEQRES 44 J 757 SER HIS GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY
SEQRES 45 J 757 SER GLY PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG
SEQRES 46 J 757 ARG ARG LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU
SEQRES 47 J 757 ALA VAL ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG
SEQRES 48 J 757 THR ARG VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR
SEQRES 49 J 757 LEU SER THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN
SEQRES 50 J 757 GLY GLN THR PHE THR CYS GLY SER ALA LEU SER PRO ILE
SEQRES 51 J 757 THR ASP PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG
SEQRES 52 J 757 TYR LEU GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU
SEQRES 53 J 757 MET THR LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU
SEQRES 54 J 757 GLN GLN PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS
SEQRES 55 J 757 ILE HIS PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU
SEQRES 56 J 757 ILE ARG GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO
SEQRES 57 J 757 ASP GLU SER HIS TYR PHE THR SER SER SER LEU LYS GLN
SEQRES 58 J 757 HIS LEU TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS
SEQRES 59 J 757 PHE ARG ILE
SEQRES 1 I 757 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 I 757 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 I 757 PRO ALA GLU ASP ASN SER LEU SER GLN LYS LYS LYS VAL
SEQRES 4 I 757 THR VAL GLU ASP LEU PHE SER GLU ASP PHE LYS ILE HIS
SEQRES 5 I 757 ASP PRO GLU ALA LYS TRP ILE SER ASP THR GLU PHE ILE
SEQRES 6 I 757 TYR ARG GLU GLN LYS GLY THR VAL ARG LEU TRP ASN VAL
SEQRES 7 I 757 GLU THR ASN THR SER THR VAL LEU ILE GLU GLY LYS LYS
SEQRES 8 I 757 ILE GLU SER LEU ARG ALA ILE ARG TYR GLU ILE SER PRO
SEQRES 9 I 757 ASP ARG GLU TYR ALA LEU PHE SER TYR ASN VAL GLU PRO
SEQRES 10 I 757 ILE TYR GLN HIS SER TYR THR GLY TYR TYR VAL LEU SER
SEQRES 11 I 757 LYS ILE PRO HIS GLY ASP PRO GLN SER LEU ASP PRO PRO
SEQRES 12 I 757 GLU VAL SER ASN ALA LYS LEU GLN TYR ALA GLY TRP GLY
SEQRES 13 I 757 PRO LYS GLY GLN GLN LEU ILE PHE ILE PHE GLU ASN ASN
SEQRES 14 I 757 ILE TYR TYR CYS ALA HIS VAL GLY LYS GLN ALA ILE ARG
SEQRES 15 I 757 VAL VAL SER THR GLY LYS GLU GLY VAL ILE TYR ASN GLY
SEQRES 16 I 757 LEU SER ASP TRP LEU TYR GLU GLU GLU ILE LEU LYS THR
SEQRES 17 I 757 HIS ILE ALA HIS TRP TRP SER PRO ASP GLY THR ARG LEU
SEQRES 18 I 757 ALA TYR ALA ALA ILE ASN ASP SER ARG VAL PRO ILE MET
SEQRES 19 I 757 GLU LEU PRO THR TYR THR GLY SER ILE TYR PRO THR VAL
SEQRES 20 I 757 LYS PRO TYR HIS TYR PRO LYS ALA GLY SER GLU ASN PRO
SEQRES 21 I 757 SER ILE SER LEU HIS VAL ILE GLY LEU ASN GLY PRO THR
SEQRES 22 I 757 HIS ASP LEU GLU MET MET PRO PRO ASP ASP PRO ARG MET
SEQRES 23 I 757 ARG GLU TYR TYR ILE THR MET VAL LYS TRP ALA THR SER
SEQRES 24 I 757 THR LYS VAL ALA VAL THR TRP LEU ASN ARG ALA GLN ASN
SEQRES 25 I 757 VAL SER ILE LEU THR LEU CYS ASP ALA THR THR GLY VAL
SEQRES 26 I 757 CYS THR LYS LYS HIS GLU ASP GLU SER GLU ALA TRP LEU
SEQRES 27 I 757 HIS ARG GLN ASN GLU GLU PRO VAL PHE SER LYS ASP GLY
SEQRES 28 I 757 ARG LYS PHE PHE PHE ILE ARG ALA ILE PRO GLN GLY GLY
SEQRES 29 I 757 ARG GLY LYS PHE TYR HIS ILE THR VAL SER SER SER GLN
SEQRES 30 I 757 PRO ASN SER SER ASN ASP ASN ILE GLN SER ILE THR SER
SEQRES 31 I 757 GLY ASP TRP ASP VAL THR LYS ILE LEU ALA TYR ASP GLU
SEQRES 32 I 757 LYS GLY ASN LYS ILE TYR PHE LEU SER THR GLU ASP LEU
SEQRES 33 I 757 PRO ARG ARG ARG GLN LEU TYR SER ALA ASN THR VAL GLY
SEQRES 34 I 757 ASN PHE ASN ARG GLN CYS LEU SER CYS ASP LEU VAL GLU
SEQRES 35 I 757 ASN CYS THR TYR PHE SER ALA SER PHE SER HIS SER MET
SEQRES 36 I 757 ASP PHE PHE LEU LEU LYS CYS GLU GLY PRO GLY VAL PRO
SEQRES 37 I 757 MET VAL THR VAL HIS ASN THR THR ASP LYS LYS LYS MET
SEQRES 38 I 757 PHE ASP LEU GLU THR ASN GLU HIS VAL LYS LYS ALA ILE
SEQRES 39 I 757 ASN ASP ARG GLN MET PRO LYS VAL GLU TYR ARG ASP ILE
SEQRES 40 I 757 GLU ILE ASP ASP TYR ASN LEU PRO MET GLN ILE LEU LYS
SEQRES 41 I 757 PRO ALA THR PHE THR ASP THR THR HIS TYR PRO LEU LEU
SEQRES 42 I 757 LEU VAL VAL ASP GLY THR PRO GLY SER GLN SER VAL ALA
SEQRES 43 I 757 GLU LYS PHE GLU VAL SER TRP GLU THR VAL MET VAL SER
SEQRES 44 I 757 SER HIS GLY ALA VAL VAL VAL LYS CYS ASP GLY ARG GLY
SEQRES 45 I 757 SER GLY PHE GLN GLY THR LYS LEU LEU HIS GLU VAL ARG
SEQRES 46 I 757 ARG ARG LEU GLY LEU LEU GLU GLU LYS ASP GLN MET GLU
SEQRES 47 I 757 ALA VAL ARG THR MET LEU LYS GLU GLN TYR ILE ASP ARG
SEQRES 48 I 757 THR ARG VAL ALA VAL PHE GLY LYS ASP TYR GLY GLY TYR
SEQRES 49 I 757 LEU SER THR TYR ILE LEU PRO ALA LYS GLY GLU ASN GLN
SEQRES 50 I 757 GLY GLN THR PHE THR CYS GLY SER ALA LEU SER PRO ILE
SEQRES 51 I 757 THR ASP PHE LYS LEU TYR ALA SER ALA PHE SER GLU ARG
SEQRES 52 I 757 TYR LEU GLY LEU HIS GLY LEU ASP ASN ARG ALA TYR GLU
SEQRES 53 I 757 MET THR LYS VAL ALA HIS ARG VAL SER ALA LEU GLU GLU
SEQRES 54 I 757 GLN GLN PHE LEU ILE ILE HIS PRO THR ALA ASP GLU LYS
SEQRES 55 I 757 ILE HIS PHE GLN HIS THR ALA GLU LEU ILE THR GLN LEU
SEQRES 56 I 757 ILE ARG GLY LYS ALA ASN TYR SER LEU GLN ILE TYR PRO
SEQRES 57 I 757 ASP GLU SER HIS TYR PHE THR SER SER SER LEU LYS GLN
SEQRES 58 I 757 HIS LEU TYR ARG SER ILE ILE ASN PHE PHE VAL GLU CYS
SEQRES 59 I 757 PHE ARG ILE
SEQRES 1 D 398 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 D 398 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 D 398 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 D 398 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 D 398 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 D 398 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 D 398 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 D 398 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 D 398 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 D 398 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 D 398 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 D 398 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 D 398 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 D 398 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 D 398 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 D 398 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 D 398 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 D 398 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 D 398 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 D 398 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 D 398 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 D 398 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 D 398 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 D 398 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 D 398 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 D 398 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 D 398 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 D 398 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 D 398 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 D 398 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 D 398 LEU ALA ARG ILE ARG ALA ALA LYS
SEQRES 1 C 397 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 C 397 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 C 397 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 C 397 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 C 397 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 C 397 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 C 397 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 C 397 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 C 397 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 C 397 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 C 397 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 C 397 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 C 397 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 C 397 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 C 397 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 C 397 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 C 397 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 C 397 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 C 397 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 C 397 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 C 397 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 C 397 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 C 397 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 C 397 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 C 397 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 C 397 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 C 397 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 C 397 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 C 397 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 C 397 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 C 397 LEU ALA ARG ILE ARG ALA ALA
HELIX 1 AA1 LYS L 32 THR L 56 1 25
HELIX 2 AA2 THR L 70 PHE L 75 1 6
HELIX 3 AA3 SER L 76 LYS L 80 5 5
HELIX 4 AA4 GLU L 118 ILE L 122 5 5
HELIX 5 AA5 ASP L 228 GLU L 234 1 7
HELIX 6 AA6 ASN L 517 ARG L 527 1 11
HELIX 7 AA7 SER L 582 HIS L 591 1 10
HELIX 8 AA8 THR L 608 GLU L 613 1 6
HELIX 9 AA9 GLY L 619 THR L 632 1 14
HELIX 10 AB1 TYR L 651 ILE L 659 1 9
HELIX 11 AB2 ASP L 682 TYR L 686 5 5
HELIX 12 AB3 ALA L 687 GLY L 696 1 10
HELIX 13 AB4 PHE L 735 LYS L 749 1 15
HELIX 14 AB5 SER L 766 ARG L 786 1 21
HELIX 15 AB6 LYS K 32 THR K 56 1 25
HELIX 16 AB7 VAL K 71 LYS K 80 5 10
HELIX 17 AB8 ASP K 228 GLU K 234 1 7
HELIX 18 AB9 ASN K 517 ARG K 527 1 11
HELIX 19 AC1 SER K 582 GLY K 592 1 11
HELIX 20 AC2 GLY K 607 HIS K 612 1 6
HELIX 21 AC3 GLY K 619 LYS K 635 1 17
HELIX 22 AC4 TYR K 651 ILE K 659 1 9
HELIX 23 AC5 ALA K 687 GLY K 696 1 10
HELIX 24 AC6 LYS K 709 ARG K 713 5 5
HELIX 25 AC7 HIS K 734 LYS K 749 1 16
HELIX 26 AC8 SER K 766 ARG K 786 1 21
HELIX 27 AC9 GLN B 56 GLU B 60 1 5
HELIX 28 AD1 GLU B 71 PHE B 75 1 5
HELIX 29 AD2 ASP B 90 GLY B 102 1 13
HELIX 30 AD3 ALA B 114 PHE B 122 1 9
HELIX 31 AD4 ASP B 131 GLU B 146 1 16
HELIX 32 AD5 ASP B 151 THR B 156 5 6
HELIX 33 AD6 ARG B 168 ASN B 177 1 10
HELIX 34 AD7 SER B 181 GLU B 205 1 25
HELIX 35 AD8 ALA B 228 ALA B 251 1 24
HELIX 36 AD9 SER B 253 SER B 260 1 8
HELIX 37 AE1 SER B 260 ASN B 282 1 23
HELIX 38 AE2 GLY B 287 ARG B 296 1 10
HELIX 39 AE3 VAL B 297 ARG B 305 5 9
HELIX 40 AE4 GLN B 308 CYS B 320 1 13
HELIX 41 AE5 CYS B 320 LYS B 347 1 28
HELIX 42 AE6 SER B 356 THR B 369 1 14
HELIX 43 AE7 THR B 380 LEU B 400 1 21
HELIX 44 AE8 PRO B 401 ARG B 434 1 34
HELIX 45 AE9 TRP A 55 ARG A 61 1 7
HELIX 46 AF1 SER A 70 PHE A 75 1 6
HELIX 47 AF2 ASP A 88 THR A 101 1 14
HELIX 48 AF3 CYS A 111 PHE A 122 1 12
HELIX 49 AF4 ILE A 125 ILE A 129 5 5
HELIX 50 AF5 ASP A 131 ASP A 150 1 20
HELIX 51 AF6 ASP A 151 ASP A 153 5 3
HELIX 52 AF7 ALA A 167 ASN A 177 1 11
HELIX 53 AF8 SER A 181 GLU A 205 1 25
HELIX 54 AF9 VAL A 227 ALA A 250 1 24
HELIX 55 AG1 SER A 253 SER A 260 1 8
HELIX 56 AG2 SER A 260 ASN A 282 1 23
HELIX 57 AG3 GLY A 287 ARG A 299 1 13
HELIX 58 AG4 ILE A 300 ARG A 305 5 6
HELIX 59 AG5 GLN A 308 CYS A 320 1 13
HELIX 60 AG6 CYS A 320 ALA A 345 1 26
HELIX 61 AG7 SER A 356 THR A 369 1 14
HELIX 62 AG8 THR A 380 LEU A 400 1 21
HELIX 63 AG9 PRO A 401 ALA A 436 1 36
HELIX 64 AH1 LYS J 32 THR J 56 1 25
HELIX 65 AH2 THR J 70 PHE J 75 1 6
HELIX 66 AH3 SER J 76 LYS J 80 5 5
HELIX 67 AH4 GLU J 118 ILE J 122 5 5
HELIX 68 AH5 ASP J 228 GLU J 234 1 7
HELIX 69 AH6 ASN J 517 ARG J 527 1 11
HELIX 70 AH7 SER J 582 HIS J 591 1 10
HELIX 71 AH8 THR J 608 GLU J 613 1 6
HELIX 72 AH9 GLY J 619 THR J 632 1 14
HELIX 73 AI1 TYR J 651 ILE J 659 1 9
HELIX 74 AI2 ASP J 682 TYR J 686 5 5
HELIX 75 AI3 ALA J 687 GLY J 696 1 10
HELIX 76 AI4 PHE J 735 LYS J 749 1 15
HELIX 77 AI5 SER J 766 ARG J 786 1 21
HELIX 78 AI6 LYS I 32 THR I 56 1 25
HELIX 79 AI7 VAL I 71 LYS I 80 5 10
HELIX 80 AI8 ASP I 228 GLU I 234 1 7
HELIX 81 AI9 ASN I 517 ARG I 527 1 11
HELIX 82 AJ1 SER I 582 GLY I 592 1 11
HELIX 83 AJ2 GLY I 607 HIS I 612 1 6
HELIX 84 AJ3 GLY I 619 LYS I 635 1 17
HELIX 85 AJ4 TYR I 651 ILE I 659 1 9
HELIX 86 AJ5 ALA I 687 GLY I 696 1 10
HELIX 87 AJ6 LYS I 709 ARG I 713 5 5
HELIX 88 AJ7 HIS I 734 LYS I 749 1 16
HELIX 89 AJ8 SER I 766 ARG I 786 1 21
HELIX 90 AJ9 GLN D 56 GLU D 60 1 5
HELIX 91 AK1 GLU D 71 PHE D 75 1 5
HELIX 92 AK2 ASP D 90 GLY D 102 1 13
HELIX 93 AK3 ALA D 114 PHE D 122 1 9
HELIX 94 AK4 ASP D 131 GLU D 146 1 16
HELIX 95 AK5 ASP D 151 THR D 156 5 6
HELIX 96 AK6 ARG D 168 ASN D 177 1 10
HELIX 97 AK7 SER D 181 GLU D 205 1 25
HELIX 98 AK8 ALA D 228 ALA D 251 1 24
HELIX 99 AK9 SER D 253 SER D 260 1 8
HELIX 100 AL1 SER D 260 ASN D 282 1 23
HELIX 101 AL2 GLY D 287 ARG D 296 1 10
HELIX 102 AL3 VAL D 297 ARG D 305 5 9
HELIX 103 AL4 GLN D 308 CYS D 320 1 13
HELIX 104 AL5 CYS D 320 LYS D 347 1 28
HELIX 105 AL6 SER D 356 THR D 369 1 14
HELIX 106 AL7 THR D 380 LEU D 400 1 21
HELIX 107 AL8 PRO D 401 ARG D 434 1 34
HELIX 108 AL9 TRP C 55 ARG C 61 1 7
HELIX 109 AM1 SER C 70 PHE C 75 1 6
HELIX 110 AM2 ASP C 88 THR C 101 1 14
HELIX 111 AM3 CYS C 111 PHE C 122 1 12
HELIX 112 AM4 ILE C 125 ILE C 129 5 5
HELIX 113 AM5 ASP C 131 ASP C 150 1 20
HELIX 114 AM6 ASP C 151 ASP C 153 5 3
HELIX 115 AM7 ALA C 167 ASN C 177 1 11
HELIX 116 AM8 SER C 181 GLU C 205 1 25
HELIX 117 AM9 VAL C 227 ALA C 250 1 24
HELIX 118 AN1 SER C 253 SER C 260 1 8
HELIX 119 AN2 SER C 260 ASN C 282 1 23
HELIX 120 AN3 GLY C 287 ARG C 299 1 13
HELIX 121 AN4 ILE C 300 ARG C 305 5 6
HELIX 122 AN5 GLN C 308 CYS C 320 1 13
HELIX 123 AN6 CYS C 320 ALA C 345 1 26
HELIX 124 AN7 SER C 356 THR C 369 1 14
HELIX 125 AN8 THR C 380 LEU C 400 1 21
HELIX 126 AN9 PRO C 401 ALA C 436 1 36
SHEET 1 AA1 2 TRP L 88 SER L 90 0
SHEET 2 AA1 2 GLU L 93 PHE L 94 -1 O GLU L 93 N SER L 90
SHEET 1 AA2 2 VAL L 103 ASN L 107 0
SHEET 2 AA2 2 THR L 112 ILE L 117 -1 O THR L 114 N LEU L 105
SHEET 1 AA3 4 ARG L 129 ILE L 132 0
SHEET 2 AA3 4 TYR L 138 TYR L 143 -1 O SER L 142 N ARG L 129
SHEET 3 AA3 4 TYR L 156 LYS L 161 -1 O TYR L 156 N TYR L 143
SHEET 4 AA3 4 GLN L 168 SER L 169 -1 O GLN L 168 N LEU L 159
SHEET 1 AA4 3 LEU L 192 PHE L 196 0
SHEET 2 AA4 3 ASN L 199 CYS L 203 -1 O CYS L 203 N LEU L 192
SHEET 3 AA4 3 ILE L 211 ARG L 212 -1 O ILE L 211 N TYR L 202
SHEET 1 AA5 4 HIS L 242 TRP L 244 0
SHEET 2 AA5 4 ARG L 250 ASN L 257 -1 O ALA L 252 N TRP L 243
SHEET 3 AA5 4 SER L 291 GLY L 298 -1 O SER L 293 N ALA L 255
SHEET 4 AA5 4 LEU L 306 GLU L 307 -1 O LEU L 306 N VAL L 296
SHEET 1 AA6 2 ILE L 263 LEU L 266 0
SHEET 2 AA6 2 LYS L 278 HIS L 281 -1 O TYR L 280 N MET L 264
SHEET 1 AA7 4 TYR L 319 TRP L 326 0
SHEET 2 AA7 4 LYS L 331 ASN L 338 -1 O ALA L 333 N LYS L 325
SHEET 3 AA7 4 VAL L 343 ASP L 350 -1 O VAL L 343 N ASN L 338
SHEET 4 AA7 4 CYS L 356 GLU L 363 -1 O THR L 357 N LEU L 348
SHEET 1 AA8 2 PHE L 384 ALA L 389 0
SHEET 2 AA8 2 TYR L 399 SER L 404 -1 O HIS L 400 N ARG L 388
SHEET 1 AA9 3 VAL L 425 ASP L 432 0
SHEET 2 AA9 3 LYS L 437 SER L 442 -1 O TYR L 439 N ALA L 430
SHEET 3 AA9 3 GLN L 451 ALA L 455 -1 O GLN L 451 N SER L 442
SHEET 1 AB1 4 SER L 478 SER L 480 0
SHEET 2 AB1 4 PHE L 487 LYS L 491 -1 O LEU L 489 N SER L 480
SHEET 3 AB1 4 VAL L 500 ASN L 504 -1 O THR L 501 N LEU L 490
SHEET 4 AB1 4 ASP L 513 GLU L 515 -1 O GLU L 515 N VAL L 500
SHEET 1 AB2 8 LYS L 531 TYR L 534 0
SHEET 2 AB2 8 MET L 546 LYS L 550 -1 O ILE L 548 N GLU L 533
SHEET 3 AB2 8 VAL L 594 CYS L 598 -1 O LYS L 597 N GLN L 547
SHEET 4 AB2 8 TYR L 560 VAL L 565 1 N LEU L 563 O VAL L 596
SHEET 5 AB2 8 ILE L 639 PHE L 647 1 O ALA L 645 N LEU L 562
SHEET 6 AB2 8 CYS L 673 LEU L 677 1 O SER L 675 N VAL L 646
SHEET 7 AB2 8 PHE L 722 PRO L 727 1 O ILE L 725 N ALA L 676
SHEET 8 AB2 8 GLN L 755 TYR L 757 1 O GLN L 755 N ILE L 724
SHEET 1 AB3 2 ILE L 537 ILE L 539 0
SHEET 2 AB3 2 TYR L 542 LEU L 544 -1 O LEU L 544 N ILE L 537
SHEET 1 AB4 2 TRP K 88 SER K 90 0
SHEET 2 AB4 2 GLU K 93 PHE K 94 -1 O GLU K 93 N SER K 90
SHEET 1 AB5 2 VAL K 103 ASN K 107 0
SHEET 2 AB5 2 THR K 112 ILE K 117 -1 O THR K 112 N ASN K 107
SHEET 1 AB6 4 ARG K 129 ILE K 132 0
SHEET 2 AB6 4 TYR K 138 SER K 142 -1 O SER K 142 N ARG K 129
SHEET 3 AB6 4 VAL K 158 LYS K 161 -1 O SER K 160 N ALA K 139
SHEET 4 AB6 4 GLN K 168 SER K 169 -1 O GLN K 168 N LEU K 159
SHEET 1 AB7 3 LEU K 192 ILE K 195 0
SHEET 2 AB7 3 ILE K 200 CYS K 203 -1 O TYR K 201 N PHE K 194
SHEET 3 AB7 3 ILE K 211 VAL K 214 -1 O ILE K 211 N TYR K 202
SHEET 1 AB8 3 ILE K 222 ASN K 224 0
SHEET 2 AB8 3 ARG K 250 ASN K 257 -1 O ILE K 256 N TYR K 223
SHEET 3 AB8 3 HIS K 242 TRP K 244 -1 N TRP K 243 O ALA K 252
SHEET 1 AB9 4 ILE K 222 ASN K 224 0
SHEET 2 AB9 4 ARG K 250 ASN K 257 -1 O ILE K 256 N TYR K 223
SHEET 3 AB9 4 SER K 291 GLY K 298 -1 O SER K 293 N ALA K 255
SHEET 4 AB9 4 LEU K 306 GLU K 307 -1 O LEU K 306 N VAL K 296
SHEET 1 AC1 2 ILE K 263 LEU K 266 0
SHEET 2 AC1 2 LYS K 278 HIS K 281 -1 O TYR K 280 N MET K 264
SHEET 1 AC2 4 TYR K 319 LYS K 325 0
SHEET 2 AC2 4 LYS K 331 ASN K 338 -1 O THR K 335 N MET K 323
SHEET 3 AC2 4 VAL K 343 ASP K 350 -1 O THR K 347 N VAL K 334
SHEET 4 AC2 4 CYS K 356 GLU K 363 -1 O ASP K 362 N SER K 344
SHEET 1 AC3 2 PHE K 384 ALA K 389 0
SHEET 2 AC3 2 TYR K 399 SER K 404 -1 O SER K 404 N PHE K 384
SHEET 1 AC4 4 VAL K 425 TYR K 431 0
SHEET 2 AC4 4 ILE K 438 LEU K 446 -1 O LEU K 441 N LYS K 427
SHEET 3 AC4 4 ARG K 449 ALA K 455 -1 O GLN K 451 N SER K 442
SHEET 4 AC4 4 GLN K 464 CYS K 465 -1 O GLN K 464 N SER K 454
SHEET 1 AC5 4 SER K 478 PHE K 481 0
SHEET 2 AC5 4 PHE K 487 LYS K 491 -1 O LYS K 491 N SER K 478
SHEET 3 AC5 4 VAL K 500 ASN K 504 -1 O THR K 501 N LEU K 490
SHEET 4 AC5 4 ASP K 513 GLU K 515 -1 O GLU K 515 N VAL K 500
SHEET 1 AC6 6 LYS K 531 GLU K 533 0
SHEET 2 AC6 6 MET K 546 LYS K 550 -1 O ILE K 548 N GLU K 533
SHEET 3 AC6 6 VAL K 594 CYS K 598 -1 O LYS K 597 N GLN K 547
SHEET 4 AC6 6 TYR K 560 VAL K 566 1 N LEU K 563 O VAL K 594
SHEET 5 AC6 6 ILE K 639 GLY K 648 1 O PHE K 647 N VAL K 566
SHEET 6 AC6 6 CYS K 673 GLY K 674 1 O CYS K 673 N VAL K 646
SHEET 1 AC7 2 ILE K 537 ILE K 539 0
SHEET 2 AC7 2 TYR K 542 LEU K 544 -1 O TYR K 542 N ILE K 539
SHEET 1 AC8 3 ALA K 676 LEU K 677 0
SHEET 2 AC8 3 PHE K 722 PRO K 727 1 O ILE K 725 N ALA K 676
SHEET 3 AC8 3 TYR K 752 TYR K 757 1 O GLN K 755 N HIS K 726
SHEET 1 AC9 4 ARG B 51 TRP B 55 0
SHEET 2 AC9 4 LEU B 42 ASN B 46 -1 N ILE B 43 O THR B 54
SHEET 3 AC9 4 GLN B 82 PHE B 84 1 O TYR B 83 N ASN B 46
SHEET 4 AC9 4 TYR B 76 HIS B 77 -1 N HIS B 77 O GLN B 82
SHEET 1 AD1 2 LEU A 45 ASN A 46 0
SHEET 2 AD1 2 ARG A 51 PHE A 52 -1 O PHE A 52 N LEU A 45
SHEET 1 AD2 2 TRP J 88 SER J 90 0
SHEET 2 AD2 2 GLU J 93 PHE J 94 -1 O GLU J 93 N SER J 90
SHEET 1 AD3 2 VAL J 103 ASN J 107 0
SHEET 2 AD3 2 THR J 112 ILE J 117 -1 O THR J 114 N LEU J 105
SHEET 1 AD4 4 ARG J 129 ILE J 132 0
SHEET 2 AD4 4 TYR J 138 TYR J 143 -1 O SER J 142 N ARG J 129
SHEET 3 AD4 4 TYR J 156 LYS J 161 -1 O TYR J 156 N TYR J 143
SHEET 4 AD4 4 GLN J 168 SER J 169 -1 O GLN J 168 N LEU J 159
SHEET 1 AD5 3 LEU J 192 PHE J 196 0
SHEET 2 AD5 3 ASN J 199 CYS J 203 -1 O CYS J 203 N LEU J 192
SHEET 3 AD5 3 ILE J 211 ARG J 212 -1 O ILE J 211 N TYR J 202
SHEET 1 AD6 4 HIS J 242 TRP J 244 0
SHEET 2 AD6 4 ARG J 250 ASN J 257 -1 O ALA J 252 N TRP J 243
SHEET 3 AD6 4 SER J 291 GLY J 298 -1 O SER J 293 N ALA J 255
SHEET 4 AD6 4 LEU J 306 GLU J 307 -1 O LEU J 306 N VAL J 296
SHEET 1 AD7 2 ILE J 263 LEU J 266 0
SHEET 2 AD7 2 LYS J 278 HIS J 281 -1 O TYR J 280 N MET J 264
SHEET 1 AD8 4 TYR J 319 TRP J 326 0
SHEET 2 AD8 4 LYS J 331 ASN J 338 -1 O ALA J 333 N LYS J 325
SHEET 3 AD8 4 VAL J 343 ASP J 350 -1 O VAL J 343 N ASN J 338
SHEET 4 AD8 4 CYS J 356 GLU J 363 -1 O THR J 357 N LEU J 348
SHEET 1 AD9 2 PHE J 384 ALA J 389 0
SHEET 2 AD9 2 TYR J 399 SER J 404 -1 O HIS J 400 N ARG J 388
SHEET 1 AE1 3 VAL J 425 ASP J 432 0
SHEET 2 AE1 3 LYS J 437 SER J 442 -1 O TYR J 439 N ALA J 430
SHEET 3 AE1 3 GLN J 451 ALA J 455 -1 O GLN J 451 N SER J 442
SHEET 1 AE2 4 SER J 478 SER J 480 0
SHEET 2 AE2 4 PHE J 487 LYS J 491 -1 O LEU J 489 N SER J 480
SHEET 3 AE2 4 VAL J 500 ASN J 504 -1 O THR J 501 N LEU J 490
SHEET 4 AE2 4 ASP J 513 GLU J 515 -1 O GLU J 515 N VAL J 500
SHEET 1 AE3 8 LYS J 531 TYR J 534 0
SHEET 2 AE3 8 MET J 546 LYS J 550 -1 O ILE J 548 N GLU J 533
SHEET 3 AE3 8 VAL J 594 CYS J 598 -1 O LYS J 597 N GLN J 547
SHEET 4 AE3 8 TYR J 560 VAL J 565 1 N LEU J 563 O VAL J 596
SHEET 5 AE3 8 ILE J 639 PHE J 647 1 O ALA J 645 N LEU J 562
SHEET 6 AE3 8 CYS J 673 LEU J 677 1 O SER J 675 N VAL J 646
SHEET 7 AE3 8 PHE J 722 PRO J 727 1 O ILE J 725 N ALA J 676
SHEET 8 AE3 8 GLN J 755 TYR J 757 1 O GLN J 755 N ILE J 724
SHEET 1 AE4 2 ILE J 537 ILE J 539 0
SHEET 2 AE4 2 TYR J 542 LEU J 544 -1 O LEU J 544 N ILE J 537
SHEET 1 AE5 2 TRP I 88 SER I 90 0
SHEET 2 AE5 2 GLU I 93 PHE I 94 -1 O GLU I 93 N SER I 90
SHEET 1 AE6 2 VAL I 103 ASN I 107 0
SHEET 2 AE6 2 THR I 112 ILE I 117 -1 O THR I 112 N ASN I 107
SHEET 1 AE7 4 ARG I 129 ILE I 132 0
SHEET 2 AE7 4 TYR I 138 SER I 142 -1 O SER I 142 N ARG I 129
SHEET 3 AE7 4 VAL I 158 LYS I 161 -1 O SER I 160 N ALA I 139
SHEET 4 AE7 4 GLN I 168 SER I 169 -1 O GLN I 168 N LEU I 159
SHEET 1 AE8 3 LEU I 192 ILE I 195 0
SHEET 2 AE8 3 ILE I 200 CYS I 203 -1 O TYR I 201 N PHE I 194
SHEET 3 AE8 3 ILE I 211 VAL I 214 -1 O ILE I 211 N TYR I 202
SHEET 1 AE9 3 ILE I 222 ASN I 224 0
SHEET 2 AE9 3 ARG I 250 ASN I 257 -1 O ILE I 256 N TYR I 223
SHEET 3 AE9 3 HIS I 242 TRP I 244 -1 N TRP I 243 O ALA I 252
SHEET 1 AF1 4 ILE I 222 ASN I 224 0
SHEET 2 AF1 4 ARG I 250 ASN I 257 -1 O ILE I 256 N TYR I 223
SHEET 3 AF1 4 SER I 291 GLY I 298 -1 O SER I 293 N ALA I 255
SHEET 4 AF1 4 LEU I 306 GLU I 307 -1 O LEU I 306 N VAL I 296
SHEET 1 AF2 2 ILE I 263 LEU I 266 0
SHEET 2 AF2 2 LYS I 278 HIS I 281 -1 O TYR I 280 N MET I 264
SHEET 1 AF3 4 TYR I 319 LYS I 325 0
SHEET 2 AF3 4 LYS I 331 ASN I 338 -1 O THR I 335 N MET I 323
SHEET 3 AF3 4 VAL I 343 ASP I 350 -1 O THR I 347 N VAL I 334
SHEET 4 AF3 4 CYS I 356 GLU I 363 -1 O ASP I 362 N SER I 344
SHEET 1 AF4 2 PHE I 384 ALA I 389 0
SHEET 2 AF4 2 TYR I 399 SER I 404 -1 O SER I 404 N PHE I 384
SHEET 1 AF5 4 VAL I 425 TYR I 431 0
SHEET 2 AF5 4 ILE I 438 LEU I 446 -1 O LEU I 441 N LYS I 427
SHEET 3 AF5 4 ARG I 449 ALA I 455 -1 O GLN I 451 N SER I 442
SHEET 4 AF5 4 GLN I 464 CYS I 465 -1 O GLN I 464 N SER I 454
SHEET 1 AF6 4 SER I 478 PHE I 481 0
SHEET 2 AF6 4 PHE I 487 LYS I 491 -1 O LYS I 491 N SER I 478
SHEET 3 AF6 4 VAL I 500 ASN I 504 -1 O THR I 501 N LEU I 490
SHEET 4 AF6 4 ASP I 513 GLU I 515 -1 O GLU I 515 N VAL I 500
SHEET 1 AF7 6 LYS I 531 GLU I 533 0
SHEET 2 AF7 6 MET I 546 LYS I 550 -1 O ILE I 548 N GLU I 533
SHEET 3 AF7 6 VAL I 594 CYS I 598 -1 O LYS I 597 N GLN I 547
SHEET 4 AF7 6 TYR I 560 VAL I 566 1 N LEU I 563 O VAL I 594
SHEET 5 AF7 6 ILE I 639 GLY I 648 1 O ALA I 645 N LEU I 562
SHEET 6 AF7 6 CYS I 673 GLY I 674 1 O CYS I 673 N VAL I 646
SHEET 1 AF8 2 ILE I 537 ILE I 539 0
SHEET 2 AF8 2 TYR I 542 LEU I 544 -1 O TYR I 542 N ILE I 539
SHEET 1 AF9 3 ALA I 676 LEU I 677 0
SHEET 2 AF9 3 PHE I 722 PRO I 727 1 O ILE I 725 N ALA I 676
SHEET 3 AF9 3 TYR I 752 TYR I 757 1 O GLN I 755 N HIS I 726
SHEET 1 AG1 4 ARG D 51 TRP D 55 0
SHEET 2 AG1 4 LEU D 42 ASN D 46 -1 N ILE D 43 O THR D 54
SHEET 3 AG1 4 GLN D 82 PHE D 84 1 O TYR D 83 N ASN D 46
SHEET 4 AG1 4 TYR D 76 HIS D 77 -1 N HIS D 77 O GLN D 82
SHEET 1 AG2 2 LEU C 45 ASN C 46 0
SHEET 2 AG2 2 ARG C 51 PHE C 52 -1 O PHE C 52 N LEU C 45
SSBOND 1 CYS L 349 CYS L 356 1555 1555 2.03
SSBOND 2 CYS L 465 CYS L 468 1555 1555 2.04
SSBOND 3 CYS L 474 CYS L 492 1555 1555 2.04
SSBOND 4 CYS L 673 CYS L 784 1555 1555 2.03
SSBOND 5 CYS K 349 CYS K 356 1555 1555 2.03
SSBOND 6 CYS K 465 CYS K 468 1555 1555 2.03
SSBOND 7 CYS K 474 CYS K 492 1555 1555 2.03
SSBOND 8 CYS K 673 CYS K 784 1555 1555 2.03
SSBOND 9 CYS J 349 CYS J 356 1555 1555 2.03
SSBOND 10 CYS J 465 CYS J 468 1555 1555 2.03
SSBOND 11 CYS J 474 CYS J 492 1555 1555 2.04
SSBOND 12 CYS J 673 CYS J 784 1555 1555 2.03
SSBOND 13 CYS I 349 CYS I 356 1555 1555 2.03
SSBOND 14 CYS I 465 CYS I 468 1555 1555 2.03
SSBOND 15 CYS I 474 CYS I 492 1555 1555 2.03
SSBOND 16 CYS I 673 CYS I 784 1555 1555 2.03
CISPEP 1 GLY L 494 PRO L 495 0 -2.41
CISPEP 2 GLY K 494 PRO K 495 0 -3.80
CISPEP 3 GLY J 494 PRO J 495 0 -2.52
CISPEP 4 GLY I 494 PRO I 495 0 -3.83
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 6088 ILE L 787
TER 12176 ILE K 787
TER 15299 LYS B 437
TER 18420 ALA A 436
TER 24508 ILE J 787
TER 30596 ILE I 787
TER 33719 LYS D 437
TER 36840 ALA C 436
MASTER 247 0 0 126 182 0 0 636832 8 32 360
END |