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HEADER MEMBRANE PROTEIN 01-MAR-21 7E87
TITLE CRYOEM STRUCTURE OF THE HUMAN KV4.2-DPP6S COMPLEX, TRANSMEMBRANE AND
TITLE 2 INTRACELLULAR REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;
COMPND 3 CHAIN: B, C;
COMPND 4 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;
COMPND 8 CHAIN: A, D;
COMPND 9 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 13 CHAIN: J, I, E, F;
COMPND 14 SYNONYM: DPPX,DIPEPTIDYL AMINOPEPTIDASE-RELATED PROTEIN,DIPEPTIDYL
COMPND 15 PEPTIDASE 6,DIPEPTIDYL PEPTIDASE IV-LIKE PROTEIN,DIPEPTIDYL PEPTIDASE
COMPND 16 VI,DPP VI;
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: KCND2, KIAA1044;
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: DPP6;
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 7E87 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. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.400
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 7E87 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_1300020957.
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: B, A, J, I, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 C 161
REMARK 465 LEU C 162
REMARK 465 PRO C 163
REMARK 465 THR C 164
REMARK 465 MET C 165
REMARK 465 THR C 166
REMARK 465 PRO C 220
REMARK 465 CYS C 221
REMARK 465 GLY C 222
REMARK 465 GLU C 223
REMARK 465 GLU D 159
REMARK 465 SER D 160
REMARK 465 ALA D 161
REMARK 465 LEU D 162
REMARK 465 PRO D 163
REMARK 465 PRO D 220
REMARK 465 CYS D 221
REMARK 465 GLY D 222
REMARK 465 GLU D 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 OG SER A 69 OE1 GLU A 71 2.11
REMARK 500 OG SER D 69 OE1 GLU D 71 2.11
REMARK 500 OD1 ASN B 97 NH1 ARG B 100 2.15
REMARK 500 OD1 ASN C 97 NH1 ARG C 100 2.15
REMARK 500 O MET A 238 OG1 THR A 241 2.17
REMARK 500 O MET D 238 OG1 THR D 241 2.18
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 PRO B 89 41.93 -86.42
REMARK 500 CYS B 111 -164.43 51.80
REMARK 500 THR B 156 -121.24 57.79
REMARK 500 PRO B 208 -7.63 -58.79
REMARK 500 ASN B 282 57.42 -92.47
REMARK 500 GLU B 283 -134.85 59.21
REMARK 500 PHE B 303 1.13 -69.21
REMARK 500 HIS B 306 49.60 -85.33
REMARK 500 GLU A 127 30.87 -93.35
REMARK 500 ALA A 167 -168.61 -167.64
REMARK 500 PRO A 178 46.56 -83.97
REMARK 500 HIS A 179 10.83 -142.08
REMARK 500 GLU A 205 7.19 -66.71
REMARK 500 PRO A 208 43.51 -81.34
REMARK 500 ALA A 228 -7.97 -56.61
REMARK 500 ASN A 282 40.07 -104.35
REMARK 500 GLU A 283 172.93 68.32
REMARK 500 ALA A 288 -7.08 -56.67
REMARK 500 HIS A 306 48.94 -91.14
REMARK 500 LEU A 371 -60.52 -93.30
REMARK 500 LYS J 32 -5.44 72.22
REMARK 500 PRO C 89 41.94 -86.37
REMARK 500 CYS C 111 -164.41 51.71
REMARK 500 THR C 156 -121.22 57.87
REMARK 500 PRO C 208 -7.50 -58.90
REMARK 500 ASN C 282 57.43 -92.51
REMARK 500 GLU C 283 -134.88 59.24
REMARK 500 PHE C 303 1.04 -69.13
REMARK 500 HIS C 306 49.68 -85.38
REMARK 500 GLU D 127 30.93 -93.34
REMARK 500 ALA D 167 -168.56 -167.64
REMARK 500 PRO D 178 46.63 -84.03
REMARK 500 HIS D 179 10.78 -142.09
REMARK 500 GLU D 205 7.18 -66.64
REMARK 500 PRO D 208 43.50 -81.34
REMARK 500 ALA D 228 -8.00 -56.54
REMARK 500 ASN D 282 40.09 -104.39
REMARK 500 GLU D 283 172.90 68.35
REMARK 500 ALA D 288 -7.15 -56.63
REMARK 500 HIS D 306 48.96 -91.20
REMARK 500 LEU D 371 -60.54 -93.30
REMARK 500 LYS E 32 -5.45 72.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-31011 RELATED DB: EMDB
REMARK 900 TRANSMEMBRANE PROTEIN
DBREF 7E87 B 40 437 UNP Q9NZV8 KCND2_HUMAN 40 437
DBREF 7E87 A 40 436 UNP Q9NZV8 KCND2_HUMAN 40 436
DBREF 7E87 J 31 58 UNP P42658 DPP6_HUMAN 93 120
DBREF 7E87 I 31 58 UNP P42658 DPP6_HUMAN 93 120
DBREF 7E87 C 40 437 UNP Q9NZV8 KCND2_HUMAN 40 437
DBREF 7E87 D 40 436 UNP Q9NZV8 KCND2_HUMAN 40 436
DBREF 7E87 E 31 58 UNP P42658 DPP6_HUMAN 93 120
DBREF 7E87 F 31 58 UNP P42658 DPP6_HUMAN 93 120
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 28 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 J 28 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 J 28 PRO ALA
SEQRES 1 I 28 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 I 28 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 I 28 PRO ALA
SEQRES 1 C 398 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 C 398 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 C 398 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 C 398 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 C 398 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 C 398 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 C 398 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 C 398 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 C 398 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 C 398 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 C 398 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 C 398 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 C 398 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 C 398 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 C 398 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 C 398 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 C 398 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 C 398 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 C 398 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 C 398 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 C 398 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 C 398 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 C 398 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 C 398 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 C 398 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 C 398 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 C 398 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 C 398 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 C 398 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 C 398 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 C 398 LEU ALA ARG ILE ARG ALA ALA LYS
SEQRES 1 D 397 ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE
SEQRES 2 D 397 GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR
SEQRES 3 D 397 LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO
SEQRES 4 D 397 GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE
SEQRES 5 D 397 PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU
SEQRES 6 D 397 HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU
SEQRES 7 D 397 GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY
SEQRES 8 D 397 ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU
SEQRES 9 D 397 ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR
SEQRES 10 D 397 ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN
SEQRES 11 D 397 ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR
SEQRES 12 D 397 MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE
SEQRES 13 D 397 ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO
SEQRES 14 D 397 CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS
SEQRES 15 D 397 GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR
SEQRES 16 D 397 ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG
SEQRES 17 D 397 LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER
SEQRES 18 D 397 VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR
SEQRES 19 D 397 TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER
SEQRES 20 D 397 GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG
SEQRES 21 D 397 ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE
SEQRES 22 D 397 LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY
SEQRES 23 D 397 PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE
SEQRES 24 D 397 ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA
SEQRES 25 D 397 SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR
SEQRES 26 D 397 ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL
SEQRES 27 D 397 PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS
SEQRES 28 D 397 SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO
SEQRES 29 D 397 VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN
SEQRES 30 D 397 GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG
SEQRES 31 D 397 LEU ALA ARG ILE ARG ALA ALA
SEQRES 1 E 28 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 E 28 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 E 28 PRO ALA
SEQRES 1 F 28 TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 F 28 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 F 28 PRO ALA
HELIX 1 AA1 GLN B 56 GLU B 60 1 5
HELIX 2 AA2 SER B 70 TYR B 76 1 7
HELIX 3 AA3 ASP B 90 GLY B 102 1 13
HELIX 4 AA4 ALA B 114 PHE B 122 1 9
HELIX 5 AA5 ASP B 131 ARG B 147 1 17
HELIX 6 AA6 GLN B 149 THR B 154 1 6
HELIX 7 AA7 ARG B 168 ASN B 177 1 10
HELIX 8 AA8 SER B 181 GLU B 205 1 25
HELIX 9 AA9 ALA B 228 ALA B 250 1 23
HELIX 10 AB1 SER B 253 ARG B 259 1 7
HELIX 11 AB2 SER B 260 ASN B 282 1 23
HELIX 12 AB3 ALA B 288 ARG B 296 1 9
HELIX 13 AB4 VAL B 297 ARG B 305 5 9
HELIX 14 AB5 GLN B 308 SER B 319 1 12
HELIX 15 AB6 CYS B 320 LYS B 347 1 28
HELIX 16 AB7 SER B 356 THR B 369 1 14
HELIX 17 AB8 THR B 380 LEU B 400 1 21
HELIX 18 AB9 PRO B 401 ARG B 434 1 34
HELIX 19 AC1 TRP A 55 ARG A 61 1 7
HELIX 20 AC2 SER A 70 PHE A 75 1 6
HELIX 21 AC3 ASP A 88 THR A 101 1 14
HELIX 22 AC4 CYS A 111 GLY A 123 1 13
HELIX 23 AC5 ILE A 125 ILE A 129 5 5
HELIX 24 AC6 ASP A 131 ASP A 150 1 20
HELIX 25 AC7 ASP A 151 ASP A 153 5 3
HELIX 26 AC8 ALA A 167 ASN A 177 1 11
HELIX 27 AC9 SER A 181 GLU A 205 1 25
HELIX 28 AD1 ALA A 228 ALA A 250 1 23
HELIX 29 AD2 SER A 253 SER A 260 1 8
HELIX 30 AD3 SER A 260 ASN A 282 1 23
HELIX 31 AD4 ALA A 288 PHE A 295 1 8
HELIX 32 AD5 ARG A 296 ARG A 305 5 10
HELIX 33 AD6 GLN A 308 CYS A 320 1 13
HELIX 34 AD7 CYS A 320 GLU A 346 1 27
HELIX 35 AD8 SER A 356 THR A 369 1 14
HELIX 36 AD9 THR A 380 LEU A 400 1 21
HELIX 37 AE1 PRO A 401 ARG A 434 1 34
HELIX 38 AE2 LYS J 32 THR J 56 1 25
HELIX 39 AE3 LYS I 32 THR I 56 1 25
HELIX 40 AE4 GLN C 56 GLU C 60 1 5
HELIX 41 AE5 SER C 70 TYR C 76 1 7
HELIX 42 AE6 ASP C 90 GLY C 102 1 13
HELIX 43 AE7 ALA C 114 PHE C 122 1 9
HELIX 44 AE8 ASP C 131 ARG C 147 1 17
HELIX 45 AE9 GLN C 149 THR C 154 1 6
HELIX 46 AF1 ARG C 168 ASN C 177 1 10
HELIX 47 AF2 SER C 181 GLU C 205 1 25
HELIX 48 AF3 ALA C 228 ALA C 250 1 23
HELIX 49 AF4 SER C 253 ARG C 259 1 7
HELIX 50 AF5 SER C 260 ASN C 282 1 23
HELIX 51 AF6 ALA C 288 ARG C 296 1 9
HELIX 52 AF7 VAL C 297 ARG C 305 5 9
HELIX 53 AF8 GLN C 308 SER C 319 1 12
HELIX 54 AF9 CYS C 320 LYS C 347 1 28
HELIX 55 AG1 SER C 356 THR C 369 1 14
HELIX 56 AG2 THR C 380 LEU C 400 1 21
HELIX 57 AG3 PRO C 401 ARG C 434 1 34
HELIX 58 AG4 TRP D 55 ARG D 61 1 7
HELIX 59 AG5 SER D 70 PHE D 75 1 6
HELIX 60 AG6 ASP D 88 THR D 101 1 14
HELIX 61 AG7 CYS D 111 GLY D 123 1 13
HELIX 62 AG8 ILE D 125 ILE D 129 5 5
HELIX 63 AG9 ASP D 131 ASP D 150 1 20
HELIX 64 AH1 ASP D 151 ASP D 153 5 3
HELIX 65 AH2 ALA D 167 ASN D 177 1 11
HELIX 66 AH3 SER D 181 GLU D 205 1 25
HELIX 67 AH4 ALA D 228 ALA D 250 1 23
HELIX 68 AH5 SER D 253 SER D 260 1 8
HELIX 69 AH6 SER D 260 ASN D 282 1 23
HELIX 70 AH7 ALA D 288 PHE D 295 1 8
HELIX 71 AH8 ARG D 296 ARG D 305 5 10
HELIX 72 AH9 GLN D 308 CYS D 320 1 13
HELIX 73 AI1 CYS D 320 GLU D 346 1 27
HELIX 74 AI2 SER D 356 THR D 369 1 14
HELIX 75 AI3 THR D 380 LEU D 400 1 21
HELIX 76 AI4 PRO D 401 ARG D 434 1 34
HELIX 77 AI5 LYS E 32 THR E 56 1 25
HELIX 78 AI6 LYS F 32 THR F 56 1 25
SHEET 1 AA1 3 ARG B 51 TRP B 55 0
SHEET 2 AA1 3 LEU B 42 ASN B 46 -1 N ILE B 43 O THR B 54
SHEET 3 AA1 3 TYR B 83 PHE B 84 1 O TYR B 83 N ASN B 46
SHEET 1 AA2 3 ARG A 51 THR A 54 0
SHEET 2 AA2 3 ILE A 43 ASN A 46 -1 N LEU A 45 O PHE A 52
SHEET 3 AA2 3 TYR A 83 PHE A 84 1 O TYR A 83 N ASN A 46
SHEET 1 AA3 3 ARG C 51 TRP C 55 0
SHEET 2 AA3 3 LEU C 42 ASN C 46 -1 N ILE C 43 O THR C 54
SHEET 3 AA3 3 TYR C 83 PHE C 84 1 O TYR C 83 N ASN C 46
SHEET 1 AA4 3 ARG D 51 THR D 54 0
SHEET 2 AA4 3 ILE D 43 ASN D 46 -1 N LEU D 45 O PHE D 52
SHEET 3 AA4 3 TYR D 83 PHE D 84 1 O TYR D 83 N ASN D 46
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 3123 LYS B 437
TER 6244 ALA A 436
TER 6450 ALA J 58
TER 6656 ALA I 58
TER 9779 LYS C 437
TER 12900 ALA D 436
TER 13106 ALA E 58
TER 13312 ALA F 58
MASTER 217 0 0 78 12 0 0 613304 8 0 136
END |