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HEADER MEMBRANE PROTEIN 01-MAR-21 7E8E
TITLE CRYOEM STRUCTURE OF HUMAN KV4.2-DPP6S-KCHIP1 COMPLEX, TRANSMEMBRANE
TITLE 2 AND INTRACELLULAR REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KV CHANNEL-INTERACTING PROTEIN 1;
COMPND 3 CHAIN: G, E;
COMPND 4 SYNONYM: KCHIP1,A-TYPE POTASSIUM CHANNEL MODULATORY PROTEIN 1,
COMPND 5 POTASSIUM CHANNEL-INTERACTING PROTEIN 1,VESICLE APC-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;
COMPND 9 CHAIN: C, D, A, B;
COMPND 10 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 14 CHAIN: K, I;
COMPND 15 SYNONYM: DPPX,DIPEPTIDYL AMINOPEPTIDASE-RELATED PROTEIN,DIPEPTIDYL
COMPND 16 PEPTIDASE 6,DIPEPTIDYL PEPTIDASE IV-LIKE PROTEIN,DIPEPTIDYL PEPTIDASE
COMPND 17 VI,DPP VI;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: KV CHANNEL-INTERACTING PROTEIN 1;
COMPND 21 CHAIN: H, F;
COMPND 22 SYNONYM: KCHIP1,A-TYPE POTASSIUM CHANNEL MODULATORY PROTEIN 1,
COMPND 23 POTASSIUM CHANNEL-INTERACTING PROTEIN 1,VESICLE APC-BINDING PROTEIN;
COMPND 24 ENGINEERED: YES;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 27 CHAIN: L, J;
COMPND 28 SYNONYM: DPPX,DIPEPTIDYL AMINOPEPTIDASE-RELATED PROTEIN,DIPEPTIDYL
COMPND 29 PEPTIDASE 6,DIPEPTIDYL PEPTIDASE IV-LIKE PROTEIN,DIPEPTIDYL PEPTIDASE
COMPND 30 VI,DPP VI;
COMPND 31 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: KCNIP1, KCHIP1, VABP;
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;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 GENE: KCNIP1, KCHIP1, VABP;
SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 29 MOL_ID: 5;
SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 31 ORGANISM_COMMON: HUMAN;
SOURCE 32 ORGANISM_TAXID: 9606;
SOURCE 33 GENE: DPP6;
SOURCE 34 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.KISE,O.NUREKI
REVDAT 1 13-OCT-21 7E8E 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. 3.90 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) : 3.900
REMARK 3 NUMBER OF PARTICLES : 139524
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 7E8E 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_1300020964.
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-KCHIP1
REMARK 245 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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, C, K, H, D, L, E, A, I, F,
REMARK 350 AND CHAINS: B, J
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 ASP G 187
REMARK 465 GLY G 188
REMARK 465 ILE G 189
REMARK 465 VAL G 190
REMARK 465 GLY C 158
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 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 GLY C 451
REMARK 465 LEU C 452
REMARK 465 LEU C 453
REMARK 465 SER C 454
REMARK 465 ASN C 455
REMARK 465 GLN C 456
REMARK 465 LEU C 457
REMARK 465 GLN C 458
REMARK 465 SER C 459
REMARK 465 SER C 460
REMARK 465 GLU C 461
REMARK 465 ASP C 462
REMARK 465 GLU C 463
REMARK 465 GLN C 464
REMARK 465 ALA C 465
REMARK 465 PHE C 466
REMARK 465 VAL C 467
REMARK 465 SER C 468
REMARK 465 LYS C 469
REMARK 465 SER C 470
REMARK 465 GLY C 471
REMARK 465 ASP H 187
REMARK 465 GLY H 188
REMARK 465 ILE H 189
REMARK 465 VAL H 190
REMARK 465 GLY D 158
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 THR D 164
REMARK 465 MET D 165
REMARK 465 THR D 166
REMARK 465 LEU D 219
REMARK 465 PRO D 220
REMARK 465 CYS D 221
REMARK 465 GLY D 222
REMARK 465 GLU D 223
REMARK 465 GLY D 451
REMARK 465 LEU D 452
REMARK 465 LEU D 453
REMARK 465 SER D 454
REMARK 465 ASN D 455
REMARK 465 GLN D 456
REMARK 465 LEU D 457
REMARK 465 GLN D 458
REMARK 465 SER D 459
REMARK 465 SER D 460
REMARK 465 GLU D 461
REMARK 465 ASP D 462
REMARK 465 GLU D 463
REMARK 465 GLN D 464
REMARK 465 ALA D 465
REMARK 465 PHE D 466
REMARK 465 VAL D 467
REMARK 465 SER D 468
REMARK 465 LYS D 469
REMARK 465 SER D 470
REMARK 465 GLY D 471
REMARK 465 ASP E 187
REMARK 465 GLY E 188
REMARK 465 ILE E 189
REMARK 465 VAL E 190
REMARK 465 GLY A 158
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 THR A 164
REMARK 465 MET A 165
REMARK 465 THR A 166
REMARK 465 PRO A 220
REMARK 465 CYS A 221
REMARK 465 GLY A 222
REMARK 465 GLU A 223
REMARK 465 GLY A 451
REMARK 465 LEU A 452
REMARK 465 LEU A 453
REMARK 465 SER A 454
REMARK 465 ASN A 455
REMARK 465 GLN A 456
REMARK 465 LEU A 457
REMARK 465 GLN A 458
REMARK 465 SER A 459
REMARK 465 SER A 460
REMARK 465 GLU A 461
REMARK 465 ASP A 462
REMARK 465 GLU A 463
REMARK 465 GLN A 464
REMARK 465 ALA A 465
REMARK 465 PHE A 466
REMARK 465 VAL A 467
REMARK 465 SER A 468
REMARK 465 LYS A 469
REMARK 465 SER A 470
REMARK 465 GLY A 471
REMARK 465 ASP F 187
REMARK 465 GLY F 188
REMARK 465 ILE F 189
REMARK 465 VAL F 190
REMARK 465 GLY B 158
REMARK 465 GLU B 159
REMARK 465 SER B 160
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 LEU B 219
REMARK 465 PRO B 220
REMARK 465 CYS B 221
REMARK 465 GLY B 222
REMARK 465 GLU B 223
REMARK 465 GLY B 451
REMARK 465 LEU B 452
REMARK 465 LEU B 453
REMARK 465 SER B 454
REMARK 465 ASN B 455
REMARK 465 GLN B 456
REMARK 465 LEU B 457
REMARK 465 GLN B 458
REMARK 465 SER B 459
REMARK 465 SER B 460
REMARK 465 GLU B 461
REMARK 465 ASP B 462
REMARK 465 GLU B 463
REMARK 465 GLN B 464
REMARK 465 ALA B 465
REMARK 465 PHE B 466
REMARK 465 VAL B 467
REMARK 465 SER B 468
REMARK 465 LYS B 469
REMARK 465 SER B 470
REMARK 465 GLY B 471
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 OG1 THR B 65 OH TYR B 99 2.14
REMARK 500 OG1 THR D 65 OH TYR D 99 2.14
REMARK 500 O MET B 238 OG1 THR B 241 2.15
REMARK 500 O MET D 238 OG1 THR D 241 2.15
REMARK 500 OE1 GLU D 346 OG1 THR D 380 2.18
REMARK 500 OE1 GLU B 346 OG1 THR B 380 2.18
REMARK 500 NE ARG C 100 O ASP D 86 2.19
REMARK 500 NE ARG A 100 O ASP B 86 2.19
REMARK 500 OG SER C 69 OE1 GLU C 71 2.19
REMARK 500 OG SER A 69 OE1 GLU A 71 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 GLN G 41 56.62 -96.47
REMARK 500 GLN G 45 -7.94 74.14
REMARK 500 PRO G 83 1.74 -68.18
REMARK 500 LYS G 138 -73.78 71.18
REMARK 500 LYS G 144 -2.36 69.88
REMARK 500 TYR G 161 34.95 -97.45
REMARK 500 MET C 27 75.91 54.12
REMARK 500 PRO C 28 5.45 -63.31
REMARK 500 ALA C 29 160.38 72.54
REMARK 500 ARG C 32 -179.63 57.10
REMARK 500 LYS C 36 50.02 -92.85
REMARK 500 SER C 69 -147.28 60.49
REMARK 500 GLU C 71 2.91 -67.35
REMARK 500 HIS C 109 31.65 -140.21
REMARK 500 ASP C 131 14.49 50.76
REMARK 500 THR C 154 46.51 37.38
REMARK 500 SER C 181 -95.51 57.83
REMARK 500 SER C 212 162.18 178.84
REMARK 500 PRO C 213 75.67 -69.38
REMARK 500 ARG C 259 1.61 -65.77
REMARK 500 PHE C 303 1.79 -63.93
REMARK 500 CYS C 320 52.20 -90.68
REMARK 500 ASN C 490 47.53 36.44
REMARK 500 PRO H 83 46.70 -81.76
REMARK 500 SER H 105 117.74 -164.91
REMARK 500 ARG H 120 31.52 -140.89
REMARK 500 ASN H 137 -161.61 -109.33
REMARK 500 LYS H 138 41.49 -108.84
REMARK 500 VAL H 165 80.39 59.90
REMARK 500 MET D 27 76.48 54.29
REMARK 500 PRO D 28 -5.60 -56.74
REMARK 500 ALA D 29 150.05 68.61
REMARK 500 SER D 69 -164.20 58.18
REMARK 500 ASP D 86 36.26 -98.10
REMARK 500 SER D 211 45.72 -140.21
REMARK 500 PRO D 213 75.92 -69.70
REMARK 500 ARG D 296 20.45 -76.14
REMARK 500 CYS D 320 51.70 -93.98
REMARK 500 LEU D 371 -66.05 -93.87
REMARK 500 GLN E 41 56.59 -96.46
REMARK 500 GLN E 45 -7.93 74.14
REMARK 500 PRO E 83 1.80 -68.21
REMARK 500 LYS E 138 -73.88 71.19
REMARK 500 LYS E 144 -2.31 69.88
REMARK 500 TYR E 161 34.88 -97.38
REMARK 500 MET A 27 75.86 54.18
REMARK 500 PRO A 28 5.40 -63.31
REMARK 500 ALA A 29 160.41 72.54
REMARK 500 ARG A 32 -179.68 57.05
REMARK 500 LYS A 36 50.02 -92.83
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-31016 RELATED DB: EMDB
REMARK 900 MEMBRANE PROTEIN
DBREF 7E8E G 36 216 UNP Q9NZI2 KCIP1_HUMAN 47 227
DBREF 7E8E C 2 495 UNP Q9NZV8 KCND2_HUMAN 2 495
DBREF 7E8E K 32 58 UNP P42658 DPP6_HUMAN 94 120
DBREF 7E8E H 37 216 UNP Q9NZI2 KCIP1_HUMAN 48 227
DBREF 7E8E D 2 495 UNP Q9NZV8 KCND2_HUMAN 2 495
DBREF 7E8E L 32 58 UNP P42658 DPP6_HUMAN 94 120
DBREF 7E8E E 36 216 UNP Q9NZI2 KCIP1_HUMAN 47 227
DBREF 7E8E A 2 495 UNP Q9NZV8 KCND2_HUMAN 2 495
DBREF 7E8E I 32 58 UNP P42658 DPP6_HUMAN 94 120
DBREF 7E8E F 37 216 UNP Q9NZI2 KCIP1_HUMAN 48 227
DBREF 7E8E B 2 495 UNP Q9NZV8 KCND2_HUMAN 2 495
DBREF 7E8E J 32 58 UNP P42658 DPP6_HUMAN 94 120
SEQADV 7E8E SER C 450 UNP Q9NZV8 ASN 450 CONFLICT
SEQADV 7E8E ALA K 28 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA K 29 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA K 30 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA K 31 UNP P42658 EXPRESSION TAG
SEQADV 7E8E SER D 450 UNP Q9NZV8 ASN 450 CONFLICT
SEQADV 7E8E ALA L 31 UNP P42658 EXPRESSION TAG
SEQADV 7E8E SER A 450 UNP Q9NZV8 ASN 450 CONFLICT
SEQADV 7E8E ALA I 28 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA I 29 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA I 30 UNP P42658 EXPRESSION TAG
SEQADV 7E8E ALA I 31 UNP P42658 EXPRESSION TAG
SEQADV 7E8E SER B 450 UNP Q9NZV8 ASN 450 CONFLICT
SEQADV 7E8E ALA J 31 UNP P42658 EXPRESSION TAG
SEQRES 1 G 181 PRO GLU GLY LEU GLU GLN LEU GLU ALA GLN THR ASN PHE
SEQRES 2 G 181 THR LYS ARG GLU LEU GLN VAL LEU TYR ARG GLY PHE LYS
SEQRES 3 G 181 ASN GLU CYS PRO SER GLY VAL VAL ASN GLU ASP THR PHE
SEQRES 4 G 181 LYS GLN ILE TYR ALA GLN PHE PHE PRO HIS GLY ASP ALA
SEQRES 5 G 181 SER THR TYR ALA HIS TYR LEU PHE ASN ALA PHE ASP THR
SEQRES 6 G 181 THR GLN THR GLY SER VAL LYS PHE GLU ASP PHE VAL THR
SEQRES 7 G 181 ALA LEU SER ILE LEU LEU ARG GLY THR VAL HIS GLU LYS
SEQRES 8 G 181 LEU ARG TRP THR PHE ASN LEU TYR ASP ILE ASN LYS ASP
SEQRES 9 G 181 GLY TYR ILE ASN LYS GLU GLU MET MET ASP ILE VAL LYS
SEQRES 10 G 181 ALA ILE TYR ASP MET MET GLY LYS TYR THR TYR PRO VAL
SEQRES 11 G 181 LEU LYS GLU ASP THR PRO ARG GLN HIS VAL ASP VAL PHE
SEQRES 12 G 181 PHE GLN LYS MET ASP LYS ASN LYS ASP GLY ILE VAL THR
SEQRES 13 G 181 LEU ASP GLU PHE LEU GLU SER CYS GLN GLU ASP ASP ASN
SEQRES 14 G 181 ILE MET ARG SER LEU GLN LEU PHE GLN ASN VAL MET
SEQRES 1 C 494 ALA ALA GLY VAL ALA ALA TRP LEU PRO PHE ALA ARG ALA
SEQRES 2 C 494 ALA ALA ILE GLY TRP MET PRO VAL ALA SER GLY PRO MET
SEQRES 3 C 494 PRO ALA PRO PRO ARG GLN GLU ARG LYS ARG THR GLN ASP
SEQRES 4 C 494 ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE GLN
SEQRES 5 C 494 THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR LEU
SEQRES 6 C 494 LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO GLU
SEQRES 7 C 494 THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE PHE
SEQRES 8 C 494 ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU HIS
SEQRES 9 C 494 TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU GLU
SEQRES 10 C 494 LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY ASP
SEQRES 11 C 494 CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU ASN
SEQRES 12 C 494 ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR ALA
SEQRES 13 C 494 GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN ARG
SEQRES 14 C 494 VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR MET
SEQRES 15 C 494 ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE ALA
SEQRES 16 C 494 VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO CYS
SEQRES 17 C 494 GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS GLY
SEQRES 18 C 494 GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR ALA
SEQRES 19 C 494 CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG LEU
SEQRES 20 C 494 ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER VAL
SEQRES 21 C 494 MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR TYR
SEQRES 22 C 494 ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER GLY
SEQRES 23 C 494 ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG ILE
SEQRES 24 C 494 PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE LEU
SEQRES 25 C 494 GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY PHE
SEQRES 26 C 494 LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE ALA
SEQRES 27 C 494 THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA SER
SEQRES 28 C 494 LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR ILE
SEQRES 29 C 494 VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL PRO
SEQRES 30 C 494 LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS SER
SEQRES 31 C 494 LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO VAL
SEQRES 32 C 494 ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN GLN
SEQRES 33 C 494 ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG LEU
SEQRES 34 C 494 ALA ARG ILE ARG ALA ALA LYS SER GLY SER ALA ASN ALA
SEQRES 35 C 494 TYR MET GLN SER LYS ARG SER GLY LEU LEU SER ASN GLN
SEQRES 36 C 494 LEU GLN SER SER GLU ASP GLU GLN ALA PHE VAL SER LYS
SEQRES 37 C 494 SER GLY SER SER PHE GLU THR GLN HIS HIS HIS LEU LEU
SEQRES 38 C 494 HIS CYS LEU GLU LYS THR THR ASN HIS GLU PHE VAL ASP
SEQRES 1 K 31 ALA ALA ALA ALA LYS GLY ILE ALA ILE ALA LEU LEU VAL
SEQRES 2 K 31 ILE LEU VAL ILE CYS SER LEU ILE VAL THR SER VAL ILE
SEQRES 3 K 31 LEU LEU THR PRO ALA
SEQRES 1 H 180 GLU GLY LEU GLU GLN LEU GLU ALA GLN THR ASN PHE THR
SEQRES 2 H 180 LYS ARG GLU LEU GLN VAL LEU TYR ARG GLY PHE LYS ASN
SEQRES 3 H 180 GLU CYS PRO SER GLY VAL VAL ASN GLU ASP THR PHE LYS
SEQRES 4 H 180 GLN ILE TYR ALA GLN PHE PHE PRO HIS GLY ASP ALA SER
SEQRES 5 H 180 THR TYR ALA HIS TYR LEU PHE ASN ALA PHE ASP THR THR
SEQRES 6 H 180 GLN THR GLY SER VAL LYS PHE GLU ASP PHE VAL THR ALA
SEQRES 7 H 180 LEU SER ILE LEU LEU ARG GLY THR VAL HIS GLU LYS LEU
SEQRES 8 H 180 ARG TRP THR PHE ASN LEU TYR ASP ILE ASN LYS ASP GLY
SEQRES 9 H 180 TYR ILE ASN LYS GLU GLU MET MET ASP ILE VAL LYS ALA
SEQRES 10 H 180 ILE TYR ASP MET MET GLY LYS TYR THR TYR PRO VAL LEU
SEQRES 11 H 180 LYS GLU ASP THR PRO ARG GLN HIS VAL ASP VAL PHE PHE
SEQRES 12 H 180 GLN LYS MET ASP LYS ASN LYS ASP GLY ILE VAL THR LEU
SEQRES 13 H 180 ASP GLU PHE LEU GLU SER CYS GLN GLU ASP ASP ASN ILE
SEQRES 14 H 180 MET ARG SER LEU GLN LEU PHE GLN ASN VAL MET
SEQRES 1 D 494 ALA ALA GLY VAL ALA ALA TRP LEU PRO PHE ALA ARG ALA
SEQRES 2 D 494 ALA ALA ILE GLY TRP MET PRO VAL ALA SER GLY PRO MET
SEQRES 3 D 494 PRO ALA PRO PRO ARG GLN GLU ARG LYS ARG THR GLN ASP
SEQRES 4 D 494 ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE GLN
SEQRES 5 D 494 THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR LEU
SEQRES 6 D 494 LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO GLU
SEQRES 7 D 494 THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE PHE
SEQRES 8 D 494 ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU HIS
SEQRES 9 D 494 TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU GLU
SEQRES 10 D 494 LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY ASP
SEQRES 11 D 494 CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU ASN
SEQRES 12 D 494 ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR ALA
SEQRES 13 D 494 GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN ARG
SEQRES 14 D 494 VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR MET
SEQRES 15 D 494 ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE ALA
SEQRES 16 D 494 VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO CYS
SEQRES 17 D 494 GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS GLY
SEQRES 18 D 494 GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR ALA
SEQRES 19 D 494 CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG LEU
SEQRES 20 D 494 ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER VAL
SEQRES 21 D 494 MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR TYR
SEQRES 22 D 494 ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER GLY
SEQRES 23 D 494 ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG ILE
SEQRES 24 D 494 PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE LEU
SEQRES 25 D 494 GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY PHE
SEQRES 26 D 494 LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE ALA
SEQRES 27 D 494 THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA SER
SEQRES 28 D 494 LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR ILE
SEQRES 29 D 494 VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL PRO
SEQRES 30 D 494 LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS SER
SEQRES 31 D 494 LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO VAL
SEQRES 32 D 494 ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN GLN
SEQRES 33 D 494 ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG LEU
SEQRES 34 D 494 ALA ARG ILE ARG ALA ALA LYS SER GLY SER ALA ASN ALA
SEQRES 35 D 494 TYR MET GLN SER LYS ARG SER GLY LEU LEU SER ASN GLN
SEQRES 36 D 494 LEU GLN SER SER GLU ASP GLU GLN ALA PHE VAL SER LYS
SEQRES 37 D 494 SER GLY SER SER PHE GLU THR GLN HIS HIS HIS LEU LEU
SEQRES 38 D 494 HIS CYS LEU GLU LYS THR THR ASN HIS GLU PHE VAL ASP
SEQRES 1 L 28 ALA LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL
SEQRES 2 L 28 ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR
SEQRES 3 L 28 PRO ALA
SEQRES 1 E 181 PRO GLU GLY LEU GLU GLN LEU GLU ALA GLN THR ASN PHE
SEQRES 2 E 181 THR LYS ARG GLU LEU GLN VAL LEU TYR ARG GLY PHE LYS
SEQRES 3 E 181 ASN GLU CYS PRO SER GLY VAL VAL ASN GLU ASP THR PHE
SEQRES 4 E 181 LYS GLN ILE TYR ALA GLN PHE PHE PRO HIS GLY ASP ALA
SEQRES 5 E 181 SER THR TYR ALA HIS TYR LEU PHE ASN ALA PHE ASP THR
SEQRES 6 E 181 THR GLN THR GLY SER VAL LYS PHE GLU ASP PHE VAL THR
SEQRES 7 E 181 ALA LEU SER ILE LEU LEU ARG GLY THR VAL HIS GLU LYS
SEQRES 8 E 181 LEU ARG TRP THR PHE ASN LEU TYR ASP ILE ASN LYS ASP
SEQRES 9 E 181 GLY TYR ILE ASN LYS GLU GLU MET MET ASP ILE VAL LYS
SEQRES 10 E 181 ALA ILE TYR ASP MET MET GLY LYS TYR THR TYR PRO VAL
SEQRES 11 E 181 LEU LYS GLU ASP THR PRO ARG GLN HIS VAL ASP VAL PHE
SEQRES 12 E 181 PHE GLN LYS MET ASP LYS ASN LYS ASP GLY ILE VAL THR
SEQRES 13 E 181 LEU ASP GLU PHE LEU GLU SER CYS GLN GLU ASP ASP ASN
SEQRES 14 E 181 ILE MET ARG SER LEU GLN LEU PHE GLN ASN VAL MET
SEQRES 1 A 494 ALA ALA GLY VAL ALA ALA TRP LEU PRO PHE ALA ARG ALA
SEQRES 2 A 494 ALA ALA ILE GLY TRP MET PRO VAL ALA SER GLY PRO MET
SEQRES 3 A 494 PRO ALA PRO PRO ARG GLN GLU ARG LYS ARG THR GLN ASP
SEQRES 4 A 494 ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE GLN
SEQRES 5 A 494 THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR LEU
SEQRES 6 A 494 LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO GLU
SEQRES 7 A 494 THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE PHE
SEQRES 8 A 494 ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU HIS
SEQRES 9 A 494 TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU GLU
SEQRES 10 A 494 LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY ASP
SEQRES 11 A 494 CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU ASN
SEQRES 12 A 494 ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR ALA
SEQRES 13 A 494 GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN ARG
SEQRES 14 A 494 VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR MET
SEQRES 15 A 494 ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE ALA
SEQRES 16 A 494 VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO CYS
SEQRES 17 A 494 GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS GLY
SEQRES 18 A 494 GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR ALA
SEQRES 19 A 494 CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG LEU
SEQRES 20 A 494 ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER VAL
SEQRES 21 A 494 MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR TYR
SEQRES 22 A 494 ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER GLY
SEQRES 23 A 494 ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG ILE
SEQRES 24 A 494 PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE LEU
SEQRES 25 A 494 GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY PHE
SEQRES 26 A 494 LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE ALA
SEQRES 27 A 494 THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA SER
SEQRES 28 A 494 LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR ILE
SEQRES 29 A 494 VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL PRO
SEQRES 30 A 494 LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS SER
SEQRES 31 A 494 LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO VAL
SEQRES 32 A 494 ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN GLN
SEQRES 33 A 494 ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG LEU
SEQRES 34 A 494 ALA ARG ILE ARG ALA ALA LYS SER GLY SER ALA ASN ALA
SEQRES 35 A 494 TYR MET GLN SER LYS ARG SER GLY LEU LEU SER ASN GLN
SEQRES 36 A 494 LEU GLN SER SER GLU ASP GLU GLN ALA PHE VAL SER LYS
SEQRES 37 A 494 SER GLY SER SER PHE GLU THR GLN HIS HIS HIS LEU LEU
SEQRES 38 A 494 HIS CYS LEU GLU LYS THR THR ASN HIS GLU PHE VAL ASP
SEQRES 1 I 31 ALA ALA ALA ALA LYS GLY ILE ALA ILE ALA LEU LEU VAL
SEQRES 2 I 31 ILE LEU VAL ILE CYS SER LEU ILE VAL THR SER VAL ILE
SEQRES 3 I 31 LEU LEU THR PRO ALA
SEQRES 1 F 180 GLU GLY LEU GLU GLN LEU GLU ALA GLN THR ASN PHE THR
SEQRES 2 F 180 LYS ARG GLU LEU GLN VAL LEU TYR ARG GLY PHE LYS ASN
SEQRES 3 F 180 GLU CYS PRO SER GLY VAL VAL ASN GLU ASP THR PHE LYS
SEQRES 4 F 180 GLN ILE TYR ALA GLN PHE PHE PRO HIS GLY ASP ALA SER
SEQRES 5 F 180 THR TYR ALA HIS TYR LEU PHE ASN ALA PHE ASP THR THR
SEQRES 6 F 180 GLN THR GLY SER VAL LYS PHE GLU ASP PHE VAL THR ALA
SEQRES 7 F 180 LEU SER ILE LEU LEU ARG GLY THR VAL HIS GLU LYS LEU
SEQRES 8 F 180 ARG TRP THR PHE ASN LEU TYR ASP ILE ASN LYS ASP GLY
SEQRES 9 F 180 TYR ILE ASN LYS GLU GLU MET MET ASP ILE VAL LYS ALA
SEQRES 10 F 180 ILE TYR ASP MET MET GLY LYS TYR THR TYR PRO VAL LEU
SEQRES 11 F 180 LYS GLU ASP THR PRO ARG GLN HIS VAL ASP VAL PHE PHE
SEQRES 12 F 180 GLN LYS MET ASP LYS ASN LYS ASP GLY ILE VAL THR LEU
SEQRES 13 F 180 ASP GLU PHE LEU GLU SER CYS GLN GLU ASP ASP ASN ILE
SEQRES 14 F 180 MET ARG SER LEU GLN LEU PHE GLN ASN VAL MET
SEQRES 1 B 494 ALA ALA GLY VAL ALA ALA TRP LEU PRO PHE ALA ARG ALA
SEQRES 2 B 494 ALA ALA ILE GLY TRP MET PRO VAL ALA SER GLY PRO MET
SEQRES 3 B 494 PRO ALA PRO PRO ARG GLN GLU ARG LYS ARG THR GLN ASP
SEQRES 4 B 494 ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE GLN
SEQRES 5 B 494 THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR LEU
SEQRES 6 B 494 LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO GLU
SEQRES 7 B 494 THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE PHE
SEQRES 8 B 494 ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU HIS
SEQRES 9 B 494 TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU GLU
SEQRES 10 B 494 LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY ASP
SEQRES 11 B 494 CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU ASN
SEQRES 12 B 494 ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR ALA
SEQRES 13 B 494 GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN ARG
SEQRES 14 B 494 VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR MET
SEQRES 15 B 494 ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE ALA
SEQRES 16 B 494 VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO CYS
SEQRES 17 B 494 GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS GLY
SEQRES 18 B 494 GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR ALA
SEQRES 19 B 494 CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG LEU
SEQRES 20 B 494 ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER VAL
SEQRES 21 B 494 MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR TYR
SEQRES 22 B 494 ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER GLY
SEQRES 23 B 494 ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG ILE
SEQRES 24 B 494 PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE LEU
SEQRES 25 B 494 GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY PHE
SEQRES 26 B 494 LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE ALA
SEQRES 27 B 494 THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA SER
SEQRES 28 B 494 LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR ILE
SEQRES 29 B 494 VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL PRO
SEQRES 30 B 494 LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS SER
SEQRES 31 B 494 LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO VAL
SEQRES 32 B 494 ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN GLN
SEQRES 33 B 494 ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG LEU
SEQRES 34 B 494 ALA ARG ILE ARG ALA ALA LYS SER GLY SER ALA ASN ALA
SEQRES 35 B 494 TYR MET GLN SER LYS ARG SER GLY LEU LEU SER ASN GLN
SEQRES 36 B 494 LEU GLN SER SER GLU ASP GLU GLN ALA PHE VAL SER LYS
SEQRES 37 B 494 SER GLY SER SER PHE GLU THR GLN HIS HIS HIS LEU LEU
SEQRES 38 B 494 HIS CYS LEU GLU LYS THR THR ASN HIS GLU PHE VAL ASP
SEQRES 1 J 28 ALA 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
HELIX 1 AA1 THR G 49 ASN G 62 1 14
HELIX 2 AA2 GLU G 71 GLN G 80 1 10
HELIX 3 AA3 ALA G 87 ASP G 99 1 13
HELIX 4 AA4 THR G 100 THR G 103 5 4
HELIX 5 AA5 PHE G 108 ARG G 120 1 13
HELIX 6 AA6 THR G 122 ASP G 135 1 14
HELIX 7 AA7 GLU G 145 ASP G 156 1 12
HELIX 8 AA8 GLU G 168 MET G 182 1 15
HELIX 9 AA9 LEU G 192 CYS G 199 1 8
HELIX 10 AB1 ASP G 202 VAL G 215 1 14
HELIX 11 AB2 ALA C 2 ALA C 7 5 6
HELIX 12 AB3 TRP C 8 TRP C 19 1 12
HELIX 13 AB4 GLN C 56 GLU C 60 1 5
HELIX 14 AB5 ASP C 88 GLY C 102 1 15
HELIX 15 AB6 CYS C 111 PHE C 122 1 12
HELIX 16 AB7 ILE C 125 ILE C 129 5 5
HELIX 17 AB8 CYS C 133 ALA C 152 1 20
HELIX 18 AB9 ARG C 168 ASN C 177 1 10
HELIX 19 AC1 SER C 181 GLU C 205 1 25
HELIX 20 AC2 VAL C 207 SER C 212 1 6
HELIX 21 AC3 ALA C 228 ALA C 251 1 24
HELIX 22 AC4 SER C 260 ALA C 269 1 10
HELIX 23 AC5 ILE C 270 ASP C 281 1 12
HELIX 24 AC6 ALA C 288 PHE C 295 1 8
HELIX 25 AC7 ARG C 296 ARG C 305 5 10
HELIX 26 AC8 SER C 307 LYS C 318 1 12
HELIX 27 AC9 ALA C 321 GLU C 346 1 26
HELIX 28 AD1 SER C 356 THR C 367 1 12
HELIX 29 AD2 THR C 380 LEU C 400 1 21
HELIX 30 AD3 VAL C 402 SER C 450 1 49
HELIX 31 AD4 SER C 473 THR C 489 1 17
HELIX 32 AD5 ALA K 29 THR K 56 1 28
HELIX 33 AD6 THR H 49 CYS H 64 1 16
HELIX 34 AD7 ASN H 70 PHE H 82 1 13
HELIX 35 AD8 ALA H 87 ASP H 99 1 13
HELIX 36 AD9 THR H 100 THR H 103 5 4
HELIX 37 AE1 LYS H 107 ARG H 120 1 14
HELIX 38 AE2 THR H 122 ASP H 135 1 14
HELIX 39 AE3 ASN H 143 ASP H 156 1 14
HELIX 40 AE4 GLU H 168 MET H 182 1 15
HELIX 41 AE5 LEU H 192 GLN H 200 1 9
HELIX 42 AE6 ASP H 202 SER H 208 1 7
HELIX 43 AE7 LEU H 209 ASN H 214 1 6
HELIX 44 AE8 VAL D 5 ALA D 7 5 3
HELIX 45 AE9 TRP D 8 ILE D 17 1 10
HELIX 46 AF1 GLY D 18 MET D 20 5 3
HELIX 47 AF2 TRP D 55 ARG D 61 1 7
HELIX 48 AF3 SER D 70 PHE D 74 5 5
HELIX 49 AF4 ASP D 90 GLY D 102 1 13
HELIX 50 AF5 CYS D 111 PHE D 122 1 12
HELIX 51 AF6 ILE D 125 ILE D 129 5 5
HELIX 52 AF7 GLY D 130 ASP D 153 1 24
HELIX 53 AF8 ARG D 170 ASN D 177 1 8
HELIX 54 AF9 SER D 181 VAL D 207 1 27
HELIX 55 AG1 VAL D 207 SER D 212 1 6
HELIX 56 AG2 ALA D 228 ALA D 250 1 23
HELIX 57 AG3 TYR D 255 SER D 260 1 6
HELIX 58 AG4 SER D 260 GLU D 283 1 24
HELIX 59 AG5 ALA D 288 ARG D 296 1 9
HELIX 60 AG6 PHE D 298 PHE D 303 1 6
HELIX 61 AG7 SER D 307 CYS D 320 1 14
HELIX 62 AG8 CYS D 320 LYS D 347 1 28
HELIX 63 AG9 SER D 356 THR D 369 1 14
HELIX 64 AH1 THR D 380 LEU D 400 1 21
HELIX 65 AH2 PRO D 401 SER D 450 1 50
HELIX 66 AH3 SER D 473 THR D 489 1 17
HELIX 67 AH4 LYS L 32 THR L 56 1 25
HELIX 68 AH5 THR E 49 ASN E 62 1 14
HELIX 69 AH6 GLU E 71 GLN E 80 1 10
HELIX 70 AH7 ALA E 87 ASP E 99 1 13
HELIX 71 AH8 THR E 100 THR E 103 5 4
HELIX 72 AH9 PHE E 108 ARG E 120 1 13
HELIX 73 AI1 THR E 122 ASP E 135 1 14
HELIX 74 AI2 GLU E 145 ASP E 156 1 12
HELIX 75 AI3 GLU E 168 MET E 182 1 15
HELIX 76 AI4 LEU E 192 CYS E 199 1 8
HELIX 77 AI5 ASP E 202 VAL E 215 1 14
HELIX 78 AI6 ALA A 2 ALA A 7 5 6
HELIX 79 AI7 TRP A 8 TRP A 19 1 12
HELIX 80 AI8 GLN A 56 GLU A 60 1 5
HELIX 81 AI9 ASP A 88 GLY A 102 1 15
HELIX 82 AJ1 CYS A 111 PHE A 122 1 12
HELIX 83 AJ2 ILE A 125 ILE A 129 5 5
HELIX 84 AJ3 CYS A 133 ALA A 152 1 20
HELIX 85 AJ4 ARG A 168 ASN A 177 1 10
HELIX 86 AJ5 SER A 181 GLU A 205 1 25
HELIX 87 AJ6 VAL A 207 SER A 212 1 6
HELIX 88 AJ7 ALA A 228 ALA A 251 1 24
HELIX 89 AJ8 SER A 260 ALA A 269 1 10
HELIX 90 AJ9 ILE A 270 ASP A 281 1 12
HELIX 91 AK1 ALA A 288 PHE A 295 1 8
HELIX 92 AK2 ARG A 296 ARG A 305 5 10
HELIX 93 AK3 SER A 307 LYS A 318 1 12
HELIX 94 AK4 ALA A 321 GLU A 346 1 26
HELIX 95 AK5 SER A 356 THR A 367 1 12
HELIX 96 AK6 THR A 380 LEU A 400 1 21
HELIX 97 AK7 VAL A 402 SER A 450 1 49
HELIX 98 AK8 SER A 473 THR A 489 1 17
HELIX 99 AK9 ALA I 29 LEU I 55 1 27
HELIX 100 AL1 THR F 49 CYS F 64 1 16
HELIX 101 AL2 ASN F 70 PHE F 82 1 13
HELIX 102 AL3 ALA F 87 ASP F 99 1 13
HELIX 103 AL4 THR F 100 THR F 103 5 4
HELIX 104 AL5 LYS F 107 ARG F 120 1 14
HELIX 105 AL6 THR F 122 ASP F 135 1 14
HELIX 106 AL7 ASN F 143 ASP F 156 1 14
HELIX 107 AL8 GLU F 168 MET F 182 1 15
HELIX 108 AL9 LEU F 192 GLN F 200 1 9
HELIX 109 AM1 ASP F 202 SER F 208 1 7
HELIX 110 AM2 LEU F 209 ASN F 214 1 6
HELIX 111 AM3 VAL B 5 ALA B 7 5 3
HELIX 112 AM4 TRP B 8 ILE B 17 1 10
HELIX 113 AM5 GLY B 18 MET B 20 5 3
HELIX 114 AM6 TRP B 55 ARG B 61 1 7
HELIX 115 AM7 SER B 70 PHE B 74 5 5
HELIX 116 AM8 ASP B 90 GLY B 102 1 13
HELIX 117 AM9 CYS B 111 PHE B 122 1 12
HELIX 118 AN1 ILE B 125 ILE B 129 5 5
HELIX 119 AN2 GLY B 130 ASP B 153 1 24
HELIX 120 AN3 ARG B 170 ASN B 177 1 8
HELIX 121 AN4 SER B 181 VAL B 207 1 27
HELIX 122 AN5 VAL B 207 SER B 212 1 6
HELIX 123 AN6 ALA B 228 ALA B 250 1 23
HELIX 124 AN7 TYR B 255 SER B 260 1 6
HELIX 125 AN8 SER B 260 GLU B 283 1 24
HELIX 126 AN9 ALA B 288 ARG B 296 1 9
HELIX 127 AO1 PHE B 298 PHE B 303 1 6
HELIX 128 AO2 SER B 307 CYS B 320 1 14
HELIX 129 AO3 CYS B 320 LYS B 347 1 28
HELIX 130 AO4 SER B 356 THR B 369 1 14
HELIX 131 AO5 THR B 380 LEU B 400 1 21
HELIX 132 AO6 PRO B 401 SER B 450 1 50
HELIX 133 AO7 SER B 473 THR B 489 1 17
HELIX 134 AO8 LYS J 32 THR J 56 1 25
SHEET 1 AA1 2 VAL G 68 ASN G 70 0
SHEET 2 AA1 2 SER G 105 LYS G 107 -1 O VAL G 106 N VAL G 69
SHEET 1 AA2 3 THR C 50 TRP C 55 0
SHEET 2 AA2 3 LEU C 42 VAL C 47 -1 N LEU C 45 O PHE C 52
SHEET 3 AA2 3 TYR C 83 PHE C 85 1 O TYR C 83 N ASN C 46
SHEET 1 AA3 4 ARG D 51 THR D 54 0
SHEET 2 AA3 4 ILE D 43 VAL D 47 -1 N LEU D 45 O PHE D 52
SHEET 3 AA3 4 GLN D 82 PHE D 85 1 O TYR D 83 N ASN D 46
SHEET 4 AA3 4 TYR D 76 HIS D 77 -1 O HIS D 77 N GLN D 82
SHEET 1 AA4 2 VAL E 68 ASN E 70 0
SHEET 2 AA4 2 SER E 105 LYS E 107 -1 O VAL E 106 N VAL E 69
SHEET 1 AA5 3 THR A 50 TRP A 55 0
SHEET 2 AA5 3 LEU A 42 VAL A 47 -1 N LEU A 45 O PHE A 52
SHEET 3 AA5 3 TYR A 83 PHE A 85 1 O TYR A 83 N ASN A 46
SHEET 1 AA6 4 ARG B 51 THR B 54 0
SHEET 2 AA6 4 ILE B 43 VAL B 47 -1 N LEU B 45 O PHE B 52
SHEET 3 AA6 4 GLN B 82 PHE B 85 1 O TYR B 83 N ASN B 46
SHEET 4 AA6 4 TYR B 76 HIS B 77 -1 O HIS B 77 N GLN B 82
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 1467 MET G 216
TER 5151 ASP C 495
TER 5363 ALA K 58
TER 6823 MET H 216
TER 10499 ASP D 495
TER 10696 ALA L 58
TER 12163 MET E 216
TER 15847 ASP A 495
TER 16059 ALA I 58
TER 17519 MET F 216
TER 21195 ASP B 495
TER 21392 ALA J 58
MASTER 349 0 0 134 18 0 0 621380 12 0 220
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