HEADER SIGNALING PROTEIN, PROTEIN FIBRIL 12-DEC-18 6NCV
TITLE CRYO-EM STRUCTURE OF NLRP6 PYD FILAMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 6;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, V;
COMPND 4 FRAGMENT: PYD DOMAIN (UNP RESIDUES 1-106);
COMPND 5 SYNONYM: ANGIOTENSIN II/VASOPRESSIN RECEPTOR,PYRIN-CONTAINING APAF1-
COMPND 6 LIKE PROTEIN 5, NLRP6;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NLRP6, NALP6, PYPAF5;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS DEATH DOMAIN FOLD, HELICAL ASSEMBLY, INFLAMMASOME, SIGNALING PROTEIN,
KEYWDS 2 PROTEIN FIBRIL
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.SHEN,T.M.FU,H.WU
REVDAT 5 20-MAR-24 6NCV 1 REMARK
REVDAT 4 11-DEC-19 6NCV 1 REMARK
REVDAT 3 20-FEB-19 6NCV 1 JRNL
REVDAT 2 06-FEB-19 6NCV 1 JRNL
REVDAT 1 23-JAN-19 6NCV 0
JRNL AUTH C.SHEN,A.LU,W.J.XIE,J.RUAN,R.NEGRO,E.H.EGELMAN,T.M.FU,H.WU
JRNL TITL MOLECULAR MECHANISM FOR NLRP6 INFLAMMASOME ASSEMBLY AND
JRNL TITL 2 ACTIVATION.
JRNL REF PROC. NATL. ACAD. SCI. V. 116 2052 2019
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30674671
JRNL DOI 10.1073/PNAS.1817221116
REMARK 2
REMARK 2 RESOLUTION. 3.70 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) : 3.700
REMARK 3 NUMBER OF PARTICLES : 181477
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 6NCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1000238604.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : FILAMENT
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : NLRP6 PYD
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.50
REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
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 K2 SUMMIT (4K X 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) : 5000.00
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS:
REMARK 300 ROTATION PER SUBUNIT (TWIST) = 56.80 DEGREES
REMARK 300 RISE PER SUBUNIT (HEIGHT) = 13.80 ANGSTROMS
REMARK 300 IN ADDITION, THERE IS 3-FOLD CIRCULAR
REMARK 300 SYMMETRY AROUND THE HELIX AXIS
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: 21-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, V
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 CYS A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 PRO A 13
REMARK 465 LEU A 105
REMARK 465 GLY A 106
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 ALA B 6
REMARK 465 PRO B 7
REMARK 465 CYS B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 GLY B 12
REMARK 465 PRO B 13
REMARK 465 LEU B 105
REMARK 465 GLY B 106
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 PRO C 4
REMARK 465 GLU C 5
REMARK 465 ALA C 6
REMARK 465 PRO C 7
REMARK 465 CYS C 8
REMARK 465 SER C 9
REMARK 465 SER C 10
REMARK 465 THR C 11
REMARK 465 GLY C 12
REMARK 465 PRO C 13
REMARK 465 LEU C 105
REMARK 465 GLY C 106
REMARK 465 MET D 1
REMARK 465 ASP D 2
REMARK 465 GLN D 3
REMARK 465 PRO D 4
REMARK 465 GLU D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 CYS D 8
REMARK 465 SER D 9
REMARK 465 SER D 10
REMARK 465 THR D 11
REMARK 465 GLY D 12
REMARK 465 PRO D 13
REMARK 465 LEU D 105
REMARK 465 GLY D 106
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 GLN E 3
REMARK 465 PRO E 4
REMARK 465 GLU E 5
REMARK 465 ALA E 6
REMARK 465 PRO E 7
REMARK 465 CYS E 8
REMARK 465 SER E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 PRO E 13
REMARK 465 LEU E 105
REMARK 465 GLY E 106
REMARK 465 MET F 1
REMARK 465 ASP F 2
REMARK 465 GLN F 3
REMARK 465 PRO F 4
REMARK 465 GLU F 5
REMARK 465 ALA F 6
REMARK 465 PRO F 7
REMARK 465 CYS F 8
REMARK 465 SER F 9
REMARK 465 SER F 10
REMARK 465 THR F 11
REMARK 465 GLY F 12
REMARK 465 PRO F 13
REMARK 465 LEU F 105
REMARK 465 GLY F 106
REMARK 465 MET G 1
REMARK 465 ASP G 2
REMARK 465 GLN G 3
REMARK 465 PRO G 4
REMARK 465 GLU G 5
REMARK 465 ALA G 6
REMARK 465 PRO G 7
REMARK 465 CYS G 8
REMARK 465 SER G 9
REMARK 465 SER G 10
REMARK 465 THR G 11
REMARK 465 GLY G 12
REMARK 465 PRO G 13
REMARK 465 LEU G 105
REMARK 465 GLY G 106
REMARK 465 MET H 1
REMARK 465 ASP H 2
REMARK 465 GLN H 3
REMARK 465 PRO H 4
REMARK 465 GLU H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 CYS H 8
REMARK 465 SER H 9
REMARK 465 SER H 10
REMARK 465 THR H 11
REMARK 465 GLY H 12
REMARK 465 PRO H 13
REMARK 465 LEU H 105
REMARK 465 GLY H 106
REMARK 465 MET I 1
REMARK 465 ASP I 2
REMARK 465 GLN I 3
REMARK 465 PRO I 4
REMARK 465 GLU I 5
REMARK 465 ALA I 6
REMARK 465 PRO I 7
REMARK 465 CYS I 8
REMARK 465 SER I 9
REMARK 465 SER I 10
REMARK 465 THR I 11
REMARK 465 GLY I 12
REMARK 465 PRO I 13
REMARK 465 LEU I 105
REMARK 465 GLY I 106
REMARK 465 MET J 1
REMARK 465 ASP J 2
REMARK 465 GLN J 3
REMARK 465 PRO J 4
REMARK 465 GLU J 5
REMARK 465 ALA J 6
REMARK 465 PRO J 7
REMARK 465 CYS J 8
REMARK 465 SER J 9
REMARK 465 SER J 10
REMARK 465 THR J 11
REMARK 465 GLY J 12
REMARK 465 PRO J 13
REMARK 465 LEU J 105
REMARK 465 GLY J 106
REMARK 465 MET K 1
REMARK 465 ASP K 2
REMARK 465 GLN K 3
REMARK 465 PRO K 4
REMARK 465 GLU K 5
REMARK 465 ALA K 6
REMARK 465 PRO K 7
REMARK 465 CYS K 8
REMARK 465 SER K 9
REMARK 465 SER K 10
REMARK 465 THR K 11
REMARK 465 GLY K 12
REMARK 465 PRO K 13
REMARK 465 LEU K 105
REMARK 465 GLY K 106
REMARK 465 MET L 1
REMARK 465 ASP L 2
REMARK 465 GLN L 3
REMARK 465 PRO L 4
REMARK 465 GLU L 5
REMARK 465 ALA L 6
REMARK 465 PRO L 7
REMARK 465 CYS L 8
REMARK 465 SER L 9
REMARK 465 SER L 10
REMARK 465 THR L 11
REMARK 465 GLY L 12
REMARK 465 PRO L 13
REMARK 465 LEU L 105
REMARK 465 GLY L 106
REMARK 465 MET M 1
REMARK 465 ASP M 2
REMARK 465 GLN M 3
REMARK 465 PRO M 4
REMARK 465 GLU M 5
REMARK 465 ALA M 6
REMARK 465 PRO M 7
REMARK 465 CYS M 8
REMARK 465 SER M 9
REMARK 465 SER M 10
REMARK 465 THR M 11
REMARK 465 GLY M 12
REMARK 465 PRO M 13
REMARK 465 LEU M 105
REMARK 465 GLY M 106
REMARK 465 MET N 1
REMARK 465 ASP N 2
REMARK 465 GLN N 3
REMARK 465 PRO N 4
REMARK 465 GLU N 5
REMARK 465 ALA N 6
REMARK 465 PRO N 7
REMARK 465 CYS N 8
REMARK 465 SER N 9
REMARK 465 SER N 10
REMARK 465 THR N 11
REMARK 465 GLY N 12
REMARK 465 PRO N 13
REMARK 465 LEU N 105
REMARK 465 GLY N 106
REMARK 465 MET O 1
REMARK 465 ASP O 2
REMARK 465 GLN O 3
REMARK 465 PRO O 4
REMARK 465 GLU O 5
REMARK 465 ALA O 6
REMARK 465 PRO O 7
REMARK 465 CYS O 8
REMARK 465 SER O 9
REMARK 465 SER O 10
REMARK 465 THR O 11
REMARK 465 GLY O 12
REMARK 465 PRO O 13
REMARK 465 LEU O 105
REMARK 465 GLY O 106
REMARK 465 MET P 1
REMARK 465 ASP P 2
REMARK 465 GLN P 3
REMARK 465 PRO P 4
REMARK 465 GLU P 5
REMARK 465 ALA P 6
REMARK 465 PRO P 7
REMARK 465 CYS P 8
REMARK 465 SER P 9
REMARK 465 SER P 10
REMARK 465 THR P 11
REMARK 465 GLY P 12
REMARK 465 PRO P 13
REMARK 465 LEU P 105
REMARK 465 GLY P 106
REMARK 465 MET Q 1
REMARK 465 ASP Q 2
REMARK 465 GLN Q 3
REMARK 465 PRO Q 4
REMARK 465 GLU Q 5
REMARK 465 ALA Q 6
REMARK 465 PRO Q 7
REMARK 465 CYS Q 8
REMARK 465 SER Q 9
REMARK 465 SER Q 10
REMARK 465 THR Q 11
REMARK 465 GLY Q 12
REMARK 465 PRO Q 13
REMARK 465 LEU Q 105
REMARK 465 GLY Q 106
REMARK 465 MET R 1
REMARK 465 ASP R 2
REMARK 465 GLN R 3
REMARK 465 PRO R 4
REMARK 465 GLU R 5
REMARK 465 ALA R 6
REMARK 465 PRO R 7
REMARK 465 CYS R 8
REMARK 465 SER R 9
REMARK 465 SER R 10
REMARK 465 THR R 11
REMARK 465 GLY R 12
REMARK 465 PRO R 13
REMARK 465 LEU R 105
REMARK 465 GLY R 106
REMARK 465 MET S 1
REMARK 465 ASP S 2
REMARK 465 GLN S 3
REMARK 465 PRO S 4
REMARK 465 GLU S 5
REMARK 465 ALA S 6
REMARK 465 PRO S 7
REMARK 465 CYS S 8
REMARK 465 SER S 9
REMARK 465 SER S 10
REMARK 465 THR S 11
REMARK 465 GLY S 12
REMARK 465 PRO S 13
REMARK 465 LEU S 105
REMARK 465 GLY S 106
REMARK 465 MET T 1
REMARK 465 ASP T 2
REMARK 465 GLN T 3
REMARK 465 PRO T 4
REMARK 465 GLU T 5
REMARK 465 ALA T 6
REMARK 465 PRO T 7
REMARK 465 CYS T 8
REMARK 465 SER T 9
REMARK 465 SER T 10
REMARK 465 THR T 11
REMARK 465 GLY T 12
REMARK 465 PRO T 13
REMARK 465 LEU T 105
REMARK 465 GLY T 106
REMARK 465 MET V 1
REMARK 465 ASP V 2
REMARK 465 GLN V 3
REMARK 465 PRO V 4
REMARK 465 GLU V 5
REMARK 465 ALA V 6
REMARK 465 PRO V 7
REMARK 465 CYS V 8
REMARK 465 SER V 9
REMARK 465 SER V 10
REMARK 465 THR V 11
REMARK 465 GLY V 12
REMARK 465 PRO V 13
REMARK 465 LEU V 105
REMARK 465 GLY V 106
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 A 40 48.20 -93.66
REMARK 500 GLN A 103 53.08 -94.15
REMARK 500 LYS B 40 48.19 -93.60
REMARK 500 GLN B 103 53.08 -94.22
REMARK 500 LYS C 40 48.25 -93.70
REMARK 500 GLN C 103 53.03 -94.13
REMARK 500 LYS D 40 48.25 -93.64
REMARK 500 GLN D 103 53.10 -94.20
REMARK 500 LYS E 40 48.18 -93.68
REMARK 500 GLN E 103 53.02 -94.15
REMARK 500 LYS F 40 48.24 -93.64
REMARK 500 GLN F 103 53.08 -94.15
REMARK 500 LYS G 40 48.26 -93.63
REMARK 500 GLN G 103 53.01 -94.07
REMARK 500 LYS H 40 48.17 -93.68
REMARK 500 GLN H 103 53.09 -94.12
REMARK 500 LYS I 40 48.15 -93.66
REMARK 500 GLN I 103 53.05 -94.11
REMARK 500 LYS J 40 48.22 -93.68
REMARK 500 GLN J 103 53.08 -94.15
REMARK 500 LYS K 40 48.23 -93.64
REMARK 500 GLN K 103 53.03 -94.11
REMARK 500 LYS L 40 48.17 -93.62
REMARK 500 GLN L 103 53.07 -94.17
REMARK 500 LYS M 40 48.23 -93.70
REMARK 500 GLN M 103 53.03 -94.08
REMARK 500 LYS N 40 48.27 -93.67
REMARK 500 GLN N 103 53.14 -94.17
REMARK 500 LYS O 40 48.16 -93.59
REMARK 500 GLN O 103 53.07 -94.13
REMARK 500 LYS P 40 48.27 -93.67
REMARK 500 GLN P 103 53.09 -94.13
REMARK 500 LYS Q 40 48.17 -93.66
REMARK 500 GLN Q 103 53.04 -94.13
REMARK 500 LYS R 40 48.16 -93.58
REMARK 500 GLN R 103 53.04 -94.10
REMARK 500 LYS S 40 48.16 -93.69
REMARK 500 GLN S 103 53.04 -94.15
REMARK 500 LYS T 40 48.17 -93.64
REMARK 500 GLN T 103 53.06 -94.16
REMARK 500 LYS V 40 48.16 -93.61
REMARK 500 GLN V 103 53.06 -94.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-0438 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF NLRP6 PYD FILAMENT
DBREF 6NCV A 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV B 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV C 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV D 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV E 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV F 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV G 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV H 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV I 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV J 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV K 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV L 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV M 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV N 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV O 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV P 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV Q 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV R 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV S 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV T 1 106 UNP P59044 NLRP6_HUMAN 1 106
DBREF 6NCV V 1 106 UNP P59044 NLRP6_HUMAN 1 106
SEQRES 1 A 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 A 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 A 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 A 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 A 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 A 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 A 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 A 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 A 106 LEU GLY
SEQRES 1 B 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 B 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 B 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 B 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 B 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 B 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 B 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 B 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 B 106 LEU GLY
SEQRES 1 C 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 C 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 C 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 C 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 C 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 C 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 C 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 C 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 C 106 LEU GLY
SEQRES 1 D 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 D 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 D 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 D 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 D 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 D 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 D 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 D 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 D 106 LEU GLY
SEQRES 1 E 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 E 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 E 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 E 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 E 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 E 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 E 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 E 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 E 106 LEU GLY
SEQRES 1 F 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 F 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 F 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 F 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 F 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 F 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 F 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 F 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 F 106 LEU GLY
SEQRES 1 G 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 G 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 G 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 G 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 G 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 G 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 G 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 G 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 G 106 LEU GLY
SEQRES 1 H 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 H 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 H 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 H 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 H 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 H 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 H 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 H 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 H 106 LEU GLY
SEQRES 1 I 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 I 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 I 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 I 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 I 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 I 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 I 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 I 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 I 106 LEU GLY
SEQRES 1 J 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 J 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 J 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 J 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 J 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 J 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 J 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 J 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 J 106 LEU GLY
SEQRES 1 K 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 K 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 K 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 K 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 K 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 K 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 K 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 K 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 K 106 LEU GLY
SEQRES 1 L 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 L 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 L 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 L 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 L 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 L 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 L 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 L 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 L 106 LEU GLY
SEQRES 1 M 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 M 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 M 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 M 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 M 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 M 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 M 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 M 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 M 106 LEU GLY
SEQRES 1 N 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 N 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 N 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 N 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 N 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 N 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 N 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 N 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 N 106 LEU GLY
SEQRES 1 O 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 O 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 O 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 O 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 O 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 O 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 O 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 O 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 O 106 LEU GLY
SEQRES 1 P 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 P 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 P 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 P 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 P 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 P 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 P 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 P 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 P 106 LEU GLY
SEQRES 1 Q 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 Q 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 Q 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 Q 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 Q 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 Q 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 Q 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 Q 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 Q 106 LEU GLY
SEQRES 1 R 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 R 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 R 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 R 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 R 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 R 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 R 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 R 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 R 106 LEU GLY
SEQRES 1 S 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 S 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 S 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 S 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 S 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 S 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 S 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 S 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 S 106 LEU GLY
SEQRES 1 T 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 T 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 T 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 T 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 T 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 T 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 T 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 T 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 T 106 LEU GLY
SEQRES 1 V 106 MET ASP GLN PRO GLU ALA PRO CYS SER SER THR GLY PRO
SEQRES 2 V 106 ARG LEU ALA VAL ALA ARG GLU LEU LEU LEU ALA ALA LEU
SEQRES 3 V 106 GLU GLU LEU SER GLN GLU GLN LEU LYS ARG PHE ARG HIS
SEQRES 4 V 106 LYS LEU ARG ASP VAL GLY PRO ASP GLY ARG SER ILE PRO
SEQRES 5 V 106 TRP GLY ARG LEU GLU ARG ALA ASP ALA VAL ASP LEU ALA
SEQRES 6 V 106 GLU GLN LEU ALA GLN PHE TYR GLY PRO GLU PRO ALA LEU
SEQRES 7 V 106 GLU VAL ALA ARG LYS THR LEU LYS ARG ALA ASP ALA ARG
SEQRES 8 V 106 ASP VAL ALA ALA GLN LEU GLN GLU ARG ARG LEU GLN ARG
SEQRES 9 V 106 LEU GLY
HELIX 1 AA1 ARG A 14 ALA A 24 1 11
HELIX 2 AA2 SER A 30 LYS A 40 1 11
HELIX 3 AA3 PRO A 52 LEU A 56 5 5
HELIX 4 AA4 ASP A 60 TYR A 72 1 13
HELIX 5 AA5 PRO A 76 LYS A 86 1 11
HELIX 6 AA6 ALA A 90 LEU A 102 1 13
HELIX 7 AA7 LEU B 15 ALA B 24 1 10
HELIX 8 AA8 SER B 30 LYS B 40 1 11
HELIX 9 AA9 PRO B 52 LEU B 56 5 5
HELIX 10 AB1 ASP B 60 TYR B 72 1 13
HELIX 11 AB2 PRO B 76 LYS B 86 1 11
HELIX 12 AB3 ALA B 90 LEU B 102 1 13
HELIX 13 AB4 LEU C 15 ALA C 24 1 10
HELIX 14 AB5 SER C 30 LYS C 40 1 11
HELIX 15 AB6 PRO C 52 LEU C 56 5 5
HELIX 16 AB7 ASP C 60 TYR C 72 1 13
HELIX 17 AB8 PRO C 76 LYS C 86 1 11
HELIX 18 AB9 ALA C 90 LEU C 102 1 13
HELIX 19 AC1 LEU D 15 ALA D 24 1 10
HELIX 20 AC2 SER D 30 LYS D 40 1 11
HELIX 21 AC3 PRO D 52 LEU D 56 5 5
HELIX 22 AC4 ASP D 60 TYR D 72 1 13
HELIX 23 AC5 PRO D 76 LYS D 86 1 11
HELIX 24 AC6 ALA D 90 LEU D 102 1 13
HELIX 25 AC7 LEU E 15 ALA E 24 1 10
HELIX 26 AC8 SER E 30 LYS E 40 1 11
HELIX 27 AC9 PRO E 52 LEU E 56 5 5
HELIX 28 AD1 ASP E 60 TYR E 72 1 13
HELIX 29 AD2 PRO E 76 LYS E 86 1 11
HELIX 30 AD3 ALA E 90 LEU E 102 1 13
HELIX 31 AD4 LEU F 15 ALA F 24 1 10
HELIX 32 AD5 SER F 30 LYS F 40 1 11
HELIX 33 AD6 PRO F 52 LEU F 56 5 5
HELIX 34 AD7 ASP F 60 TYR F 72 1 13
HELIX 35 AD8 PRO F 76 LYS F 86 1 11
HELIX 36 AD9 ALA F 90 LEU F 102 1 13
HELIX 37 AE1 LEU G 15 ALA G 24 1 10
HELIX 38 AE2 SER G 30 LYS G 40 1 11
HELIX 39 AE3 PRO G 52 LEU G 56 5 5
HELIX 40 AE4 ASP G 60 TYR G 72 1 13
HELIX 41 AE5 PRO G 76 LYS G 86 1 11
HELIX 42 AE6 ALA G 90 LEU G 102 1 13
HELIX 43 AE7 LEU H 15 ALA H 24 1 10
HELIX 44 AE8 SER H 30 LYS H 40 1 11
HELIX 45 AE9 PRO H 52 LEU H 56 5 5
HELIX 46 AF1 ASP H 60 TYR H 72 1 13
HELIX 47 AF2 PRO H 76 LYS H 86 1 11
HELIX 48 AF3 ALA H 90 LEU H 102 1 13
HELIX 49 AF4 LEU I 15 ALA I 24 1 10
HELIX 50 AF5 SER I 30 LYS I 40 1 11
HELIX 51 AF6 PRO I 52 LEU I 56 5 5
HELIX 52 AF7 ASP I 60 TYR I 72 1 13
HELIX 53 AF8 PRO I 76 LYS I 86 1 11
HELIX 54 AF9 ALA I 90 LEU I 102 1 13
HELIX 55 AG1 LEU J 15 ALA J 24 1 10
HELIX 56 AG2 SER J 30 LYS J 40 1 11
HELIX 57 AG3 PRO J 52 LEU J 56 5 5
HELIX 58 AG4 ASP J 60 TYR J 72 1 13
HELIX 59 AG5 PRO J 76 LYS J 86 1 11
HELIX 60 AG6 ALA J 90 LEU J 102 1 13
HELIX 61 AG7 LEU K 15 ALA K 24 1 10
HELIX 62 AG8 SER K 30 LYS K 40 1 11
HELIX 63 AG9 PRO K 52 LEU K 56 5 5
HELIX 64 AH1 ASP K 60 TYR K 72 1 13
HELIX 65 AH2 PRO K 76 LYS K 86 1 11
HELIX 66 AH3 ALA K 90 LEU K 102 1 13
HELIX 67 AH4 LEU L 15 ALA L 24 1 10
HELIX 68 AH5 SER L 30 LYS L 40 1 11
HELIX 69 AH6 PRO L 52 LEU L 56 5 5
HELIX 70 AH7 ASP L 60 TYR L 72 1 13
HELIX 71 AH8 PRO L 76 LYS L 86 1 11
HELIX 72 AH9 ALA L 90 LEU L 102 1 13
HELIX 73 AI1 LEU M 15 ALA M 24 1 10
HELIX 74 AI2 SER M 30 LYS M 40 1 11
HELIX 75 AI3 PRO M 52 LEU M 56 5 5
HELIX 76 AI4 ASP M 60 TYR M 72 1 13
HELIX 77 AI5 PRO M 76 LYS M 86 1 11
HELIX 78 AI6 ALA M 90 LEU M 102 1 13
HELIX 79 AI7 LEU N 15 ALA N 24 1 10
HELIX 80 AI8 SER N 30 LYS N 40 1 11
HELIX 81 AI9 PRO N 52 LEU N 56 5 5
HELIX 82 AJ1 ASP N 60 TYR N 72 1 13
HELIX 83 AJ2 PRO N 76 LYS N 86 1 11
HELIX 84 AJ3 ALA N 90 LEU N 102 1 13
HELIX 85 AJ4 LEU O 15 ALA O 24 1 10
HELIX 86 AJ5 SER O 30 LYS O 40 1 11
HELIX 87 AJ6 PRO O 52 LEU O 56 5 5
HELIX 88 AJ7 ASP O 60 TYR O 72 1 13
HELIX 89 AJ8 PRO O 76 LYS O 86 1 11
HELIX 90 AJ9 ALA O 90 LEU O 102 1 13
HELIX 91 AK1 LEU P 15 ALA P 24 1 10
HELIX 92 AK2 SER P 30 LYS P 40 1 11
HELIX 93 AK3 PRO P 52 LEU P 56 5 5
HELIX 94 AK4 ASP P 60 TYR P 72 1 13
HELIX 95 AK5 PRO P 76 LYS P 86 1 11
HELIX 96 AK6 ALA P 90 LEU P 102 1 13
HELIX 97 AK7 LEU Q 15 ALA Q 24 1 10
HELIX 98 AK8 SER Q 30 LYS Q 40 1 11
HELIX 99 AK9 PRO Q 52 LEU Q 56 5 5
HELIX 100 AL1 ASP Q 60 TYR Q 72 1 13
HELIX 101 AL2 PRO Q 76 LYS Q 86 1 11
HELIX 102 AL3 ALA Q 90 LEU Q 102 1 13
HELIX 103 AL4 LEU R 15 ALA R 24 1 10
HELIX 104 AL5 SER R 30 LYS R 40 1 11
HELIX 105 AL6 PRO R 52 LEU R 56 5 5
HELIX 106 AL7 ASP R 60 TYR R 72 1 13
HELIX 107 AL8 PRO R 76 LYS R 86 1 11
HELIX 108 AL9 ALA R 90 LEU R 102 1 13
HELIX 109 AM1 LEU S 15 ALA S 24 1 10
HELIX 110 AM2 SER S 30 LYS S 40 1 11
HELIX 111 AM3 PRO S 52 LEU S 56 5 5
HELIX 112 AM4 ASP S 60 TYR S 72 1 13
HELIX 113 AM5 PRO S 76 LYS S 86 1 11
HELIX 114 AM6 ALA S 90 LEU S 102 1 13
HELIX 115 AM7 LEU T 15 ALA T 24 1 10
HELIX 116 AM8 SER T 30 LYS T 40 1 11
HELIX 117 AM9 PRO T 52 LEU T 56 5 5
HELIX 118 AN1 ASP T 60 TYR T 72 1 13
HELIX 119 AN2 PRO T 76 LYS T 86 1 11
HELIX 120 AN3 ALA T 90 LEU T 102 1 13
HELIX 121 AN4 LEU V 15 ALA V 24 1 10
HELIX 122 AN5 SER V 30 LYS V 40 1 11
HELIX 123 AN6 PRO V 52 LEU V 56 5 5
HELIX 124 AN7 ASP V 60 TYR V 72 1 13
HELIX 125 AN8 PRO V 76 LYS V 86 1 11
HELIX 126 AN9 ALA V 90 LEU V 102 1 13
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
(ATOM LINES ARE NOT SHOWN.)
END