Header list of 1a9v.pdb file
Complete list - b 16 2 Bytes
HEADER ALLERGEN 10-APR-98 1A9V
TITLE TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR,
TITLE 2 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITE ALLERGEN DER P 2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: D1S MUTANT MADE TO ENHANCE N-TERMINAL MET REMOVAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DERMATOPHAGOIDES PTERONYSSINUS;
SOURCE 3 ORGANISM_COMMON: EUROPEAN HOUSE DUST MITE;
SOURCE 4 ORGANISM_TAXID: 6956;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (PLYSE);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21A
KEYWDS ALLERGEN, IMMUNOGLOBULIN FOLD
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.A.MUELLER,D.C.BENJAMIN,G.S.RULE
REVDAT 3 16-FEB-22 1A9V 1 REMARK
REVDAT 2 24-FEB-09 1A9V 1 VERSN
REVDAT 1 14-OCT-98 1A9V 0
JRNL AUTH G.A.MUELLER,D.C.BENJAMIN,G.S.RULE
JRNL TITL TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER
JRNL TITL 2 P 2: SEQUENTIAL AND STRUCTURAL HOMOLOGIES.
JRNL REF BIOCHEMISTRY V. 37 12707 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9737847
JRNL DOI 10.1021/BI980578+
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.A.MUELLER,A.M.SMITH,D.C.WILLIAMS JUNIOR,G.A.HAKKAART,
REMARK 1 AUTH 2 R.C.AALBERSE,M.D.CHAPMAN,G.S.RULE,D.C.BENJAMIN
REMARK 1 TITL EXPRESSION AND SECONDARY STRUCTURE DETERMINATION BY NMR
REMARK 1 TITL 2 METHODS OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2
REMARK 1 REF J.BIOL.CHEM. V. 272 26893 1997
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CONVENTIONAL
REMARK 4
REMARK 4 1A9V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170573.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM NACL 100 MM K2SO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90 H2O/10 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; CA(CO)HN; HN(CA)HA;
REMARK 210 HA(CACO)NH; HNCACB; CBCA(CO)NH;
REMARK 210 HNCO; CBACOHA; HBHA(CACO)NH;
REMARK 210 HCCH-TOCSY; HSQC-NOESY; CHH-
REMARK 210 NOESY; HCH-NOESY; NHNH-NOESY; CN-
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, X-PLOR 3.821
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEAL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING DOUBLE LABELED MATERIAL AND
REMARK 210 TRIPLE RESONANCE METHODS
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HB2 LYS A 109 HB2 CYS A 119 1.26
REMARK 500 H ASP A 59 O ASN A 103 1.50
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 1 VAL A 5 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 1 GLU A 62 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 1 ASP A 64 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 1 GLU A 102 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 1 ASN A 103 N - CA - CB ANGL. DEV. = -18.4 DEGREES
REMARK 500 2 VAL A 5 N - CA - CB ANGL. DEV. = -15.7 DEGREES
REMARK 500 2 GLU A 62 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 2 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 2 GLU A 102 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 2 ASN A 103 N - CA - CB ANGL. DEV. = -18.4 DEGREES
REMARK 500 3 VAL A 5 N - CA - CB ANGL. DEV. = -15.7 DEGREES
REMARK 500 3 GLU A 62 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 3 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 3 GLU A 102 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 3 ASN A 103 N - CA - CB ANGL. DEV. = -18.3 DEGREES
REMARK 500 4 VAL A 5 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 4 GLU A 62 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 4 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 4 GLU A 102 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 4 ASN A 103 N - CA - CB ANGL. DEV. = -18.1 DEGREES
REMARK 500 5 VAL A 5 N - CA - CB ANGL. DEV. = -15.4 DEGREES
REMARK 500 5 GLU A 62 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 5 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 5 GLU A 102 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 5 ASN A 103 N - CA - CB ANGL. DEV. = -18.1 DEGREES
REMARK 500 6 VAL A 5 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 6 GLU A 62 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 6 ASP A 64 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 6 GLU A 102 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 6 ASN A 103 N - CA - CB ANGL. DEV. = -18.2 DEGREES
REMARK 500 7 VAL A 5 N - CA - CB ANGL. DEV. = -15.6 DEGREES
REMARK 500 7 GLU A 62 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 7 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 7 GLU A 102 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 7 ASN A 103 N - CA - CB ANGL. DEV. = -18.1 DEGREES
REMARK 500 8 VAL A 5 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 8 GLU A 62 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 8 ASP A 64 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 8 GLU A 102 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 8 ASN A 103 N - CA - CB ANGL. DEV. = -18.1 DEGREES
REMARK 500 9 VAL A 5 N - CA - CB ANGL. DEV. = -15.6 DEGREES
REMARK 500 9 GLU A 62 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 9 ASP A 64 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 9 GLU A 102 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 9 ASN A 103 N - CA - CB ANGL. DEV. = -18.2 DEGREES
REMARK 500 10 VAL A 5 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 10 GLU A 62 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 10 ASP A 64 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 10 GLU A 102 CB - CA - C ANGL. DEV. = -13.4 DEGREES
REMARK 500 10 ASN A 103 N - CA - CB ANGL. DEV. = -18.4 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 1 GLN A 2 157.02 64.00
REMARK 500 1 VAL A 5 -50.77 -161.30
REMARK 500 1 LYS A 6 139.46 84.86
REMARK 500 1 ALA A 9 -85.81 -124.43
REMARK 500 1 ASN A 10 65.04 -159.96
REMARK 500 1 HIS A 11 32.00 33.30
REMARK 500 1 ILE A 13 -165.24 -117.14
REMARK 500 1 LYS A 14 -48.03 -162.31
REMARK 500 1 ILE A 28 -166.03 -79.37
REMARK 500 1 HIS A 30 33.19 -70.36
REMARK 500 1 ARG A 31 170.39 58.10
REMARK 500 1 ASN A 44 50.51 -117.32
REMARK 500 1 GLN A 45 -159.44 166.87
REMARK 500 1 ASP A 59 62.35 35.84
REMARK 500 1 LEU A 61 57.02 -108.13
REMARK 500 1 ILE A 68 -163.56 174.30
REMARK 500 1 LYS A 77 95.51 -12.08
REMARK 500 1 PRO A 95 150.16 -37.03
REMARK 500 1 SER A 101 99.62 -42.96
REMARK 500 1 GLU A 102 -51.45 -163.67
REMARK 500 1 ASN A 103 79.22 -159.30
REMARK 500 1 VAL A 116 152.36 136.21
REMARK 500 1 LEU A 117 -59.51 -162.22
REMARK 500 1 THR A 123 -87.31 -148.70
REMARK 500 1 HIS A 124 82.69 8.68
REMARK 500 1 ALA A 125 79.20 -173.51
REMARK 500 1 LYS A 126 -155.81 -130.63
REMARK 500 2 ALA A 9 -84.54 -125.94
REMARK 500 2 ASN A 10 66.69 -159.46
REMARK 500 2 HIS A 11 33.11 33.57
REMARK 500 2 ILE A 13 -167.39 -121.15
REMARK 500 2 LYS A 14 -45.04 -162.34
REMARK 500 2 PRO A 19 93.83 -67.63
REMARK 500 2 ILE A 28 -146.38 -80.68
REMARK 500 2 HIS A 30 -90.98 -67.05
REMARK 500 2 ASN A 44 51.26 -114.87
REMARK 500 2 GLN A 45 -160.95 167.34
REMARK 500 2 ASP A 59 65.20 34.86
REMARK 500 2 LEU A 61 57.94 -108.30
REMARK 500 2 ILE A 68 -168.85 179.63
REMARK 500 2 PRO A 70 -5.21 -48.39
REMARK 500 2 LYS A 77 95.98 -19.88
REMARK 500 2 PRO A 95 154.07 -37.96
REMARK 500 2 ILE A 97 39.71 -140.27
REMARK 500 2 SER A 101 96.78 -43.43
REMARK 500 2 GLU A 102 -50.77 -163.64
REMARK 500 2 ASN A 103 81.58 -159.07
REMARK 500 2 VAL A 116 145.23 145.41
REMARK 500 2 LEU A 117 -57.43 -162.27
REMARK 500 2 ALA A 118 130.09 -173.81
REMARK 500
REMARK 500 THIS ENTRY HAS 240 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 31 0.31 SIDE CHAIN
REMARK 500 1 ARG A 128 0.29 SIDE CHAIN
REMARK 500 2 ARG A 31 0.32 SIDE CHAIN
REMARK 500 2 ARG A 128 0.17 SIDE CHAIN
REMARK 500 3 ARG A 31 0.28 SIDE CHAIN
REMARK 500 3 ARG A 128 0.30 SIDE CHAIN
REMARK 500 4 ARG A 31 0.31 SIDE CHAIN
REMARK 500 4 ARG A 128 0.31 SIDE CHAIN
REMARK 500 5 ARG A 31 0.31 SIDE CHAIN
REMARK 500 5 ARG A 128 0.24 SIDE CHAIN
REMARK 500 6 ARG A 31 0.25 SIDE CHAIN
REMARK 500 6 ARG A 128 0.31 SIDE CHAIN
REMARK 500 7 ARG A 31 0.25 SIDE CHAIN
REMARK 500 7 ARG A 128 0.31 SIDE CHAIN
REMARK 500 8 ARG A 31 0.32 SIDE CHAIN
REMARK 500 8 ARG A 128 0.32 SIDE CHAIN
REMARK 500 9 ARG A 31 0.26 SIDE CHAIN
REMARK 500 10 ARG A 31 0.31 SIDE CHAIN
REMARK 500 10 ARG A 128 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A9V A 2 129 UNP P49278 ALL2_DERPT 19 146
SEQRES 1 A 129 SER GLN VAL ASP VAL LYS ASP CYS ALA ASN HIS GLU ILE
SEQRES 2 A 129 LYS LYS VAL LEU VAL PRO GLY CYS HIS GLY SER GLU PRO
SEQRES 3 A 129 CYS ILE ILE HIS ARG GLY LYS PRO PHE GLN LEU GLU ALA
SEQRES 4 A 129 VAL PHE GLU ALA ASN GLN ASN THR LYS THR ALA LYS ILE
SEQRES 5 A 129 GLU ILE LYS ALA SER ILE ASP GLY LEU GLU VAL ASP VAL
SEQRES 6 A 129 PRO GLY ILE ASP PRO ASN ALA CYS HIS TYR MET LYS CYS
SEQRES 7 A 129 PRO LEU VAL LYS GLY GLN GLN TYR ASP ILE LYS TYR THR
SEQRES 8 A 129 TRP ASN VAL PRO LYS ILE ALA PRO LYS SER GLU ASN VAL
SEQRES 9 A 129 VAL VAL THR VAL LYS VAL MET GLY ASP ASP GLY VAL LEU
SEQRES 10 A 129 ALA CYS ALA ILE ALA THR HIS ALA LYS ILE ARG ASP
HELIX 1 1 ILE A 58 GLY A 60 5 3
HELIX 2 2 ALA A 72 HIS A 74 5 3
SHEET 1 A 3 LYS A 15 LEU A 17 0
SHEET 2 A 3 LEU A 37 VAL A 40 -1 N VAL A 40 O LYS A 15
SHEET 3 A 3 ASP A 87 TYR A 90 -1 N TYR A 90 O LEU A 37
SHEET 1 B 3 GLU A 53 ALA A 56 0
SHEET 2 B 3 VAL A 106 VAL A 110 -1 N LYS A 109 O GLU A 53
SHEET 3 B 3 ALA A 118 ILE A 121 -1 N ALA A 120 O VAL A 108
SSBOND 1 CYS A 8 CYS A 119 1555 1555 2.03
SSBOND 2 CYS A 21 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 73 CYS A 78 1555 1555 2.02
CISPEP 1 CYS A 78 PRO A 79 1 0.69
CISPEP 2 CYS A 78 PRO A 79 2 0.18
CISPEP 3 CYS A 78 PRO A 79 3 1.30
CISPEP 4 CYS A 78 PRO A 79 4 1.14
CISPEP 5 CYS A 78 PRO A 79 5 0.39
CISPEP 6 CYS A 78 PRO A 79 6 0.04
CISPEP 7 CYS A 78 PRO A 79 7 0.05
CISPEP 8 CYS A 78 PRO A 79 8 0.06
CISPEP 9 CYS A 78 PRO A 79 9 0.66
CISPEP 10 CYS A 78 PRO A 79 10 1.04
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
MODEL 1
Complete list - b 16 2 Bytes