Header list of 1exe.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION 02-MAY-00 1EXE
TITLE SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PHAGE SPO1;
SOURCE 3 ORGANISM_TAXID: 10685;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PBTF1X
KEYWDS BETA RIBBON ARMS, DNA-BINDING, DNA-BENDING PROTEIN, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR W.LIU,H.M.VU,E.P.GEIDUSCHEK,D.R.KEARNS
REVDAT 3 03-NOV-21 1EXE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1EXE 1 VERSN
REVDAT 1 18-OCT-00 1EXE 0
JRNL AUTH W.LIU,H.M.VU,E.P.GEIDUSCHEK,D.R.KEARNS
JRNL TITL SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1:
JRNL TITL 2 IMPLICATIONS FOR ENHANCED DNA BINDING.
JRNL REF J.MOL.BIOL. V. 302 821 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10993726
JRNL DOI 10.1006/JMBI.2000.4084
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.M.VU,W.LIU,A.GROVE,E.P.GEIDUSCHEK,D.R.KEARNS
REMARK 1 TITL MECHANISMS FOR THE ENHANCED THERMAL STABILITY OF A MUTANT OF
REMARK 1 TITL 2 TRANSCRIPTION FACTOR 1 AS EXPLAINED BY 1H, 15N AND 13C NMR
REMARK 1 TITL 3 CHEMICAL SHIFTS AND SECONDARY STRUCTURE ANALYSIS.
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1478 113 2000
REMARK 1 REFN ISSN 0006-3002
REMARK 1 DOI 10.1016/S0167-4838(99)00252-6
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.JIA,A.GROVE,M.IVANCIC,V.L.HSU,E.P.GEIDUSCHEK,D.R.KEARNS
REMARK 1 TITL STRUCTURE OF THE BACILLUS SUBTILIS PHAGE SPO1-ENCODED TYPE
REMARK 1 TITL 2 II DNA-BINDING PROTEIN TF1 IN SOLUTION.
REMARK 1 REF J.MOL.BIOL. V. 263 259 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1996.0573
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, X-PLOR 3
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE BASED ON A TOTAL OF
REMARK 3 2008 NOE-DERIVED DISTANCE CONSTRAINTS, 288 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND 116 H-BOND CONSTRAINTS.
REMARK 4
REMARK 4 1EXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000010994.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308; 308
REMARK 210 PH : 6.7; 6.7; 6.7
REMARK 210 IONIC STRENGTH : 400 MM NACL; 400 MM NACL; 400 MM
REMARK 210 NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM TF1-G15/I32, 100 MM
REMARK 210 PHOSPHATE BUFFER; 2 MM TF1-G15/
REMARK 210 I32, U-15N, 100 MM PHOSPHATE
REMARK 210 BUFFER; 2 MM TF1-G15/I32, U-15N,
REMARK 210 13C, 100 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97, X-PLOR 3
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 H PHE A 61 H ALA A 68 1.02
REMARK 500 O LYS B 30 HB2 GLU B 34 1.35
REMARK 500 O SER A 20 H LYS A 23 1.35
REMARK 500 N PHE A 61 H ALA A 68 1.46
REMARK 500 O GLU A 83 H LYS A 87 1.46
REMARK 500 O SER B 20 H LYS B 23 1.48
REMARK 500 O ILE A 31 H THR A 35 1.49
REMARK 500 O ILE A 7 H ALA A 11 1.53
REMARK 500 O PHE B 28 H ILE B 32 1.53
REMARK 500 O LYS A 30 HB2 GLU A 34 1.57
REMARK 500 O SER B 20 H MET B 24 1.59
REMARK 500 OD1 ASN B 2 H GLU B 5 1.60
REMARK 500 O GLY A 60 O PHE A 61 1.71
REMARK 500 O SER A 20 N SER A 22 1.85
REMARK 500 O ILE A 10 OG1 THR A 14 1.98
REMARK 500 O SER B 20 N LYS B 23 1.99
REMARK 500 O ILE B 10 OG1 THR B 14 2.06
REMARK 500 O SER A 20 N LYS A 23 2.08
REMARK 500 O LYS B 30 CB GLU B 34 2.09
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 5 ALA B 98 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 6 ALA A 98 N - CA - CB ANGL. DEV. = -8.7 DEGREES
REMARK 500 12 ALA B 72 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 19 ALA A 98 N - CA - CB ANGL. DEV. = -8.4 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 ASN A 2 -167.55 -174.12
REMARK 500 1 THR A 14 -76.12 -93.00
REMARK 500 1 THR A 17 0.74 -150.70
REMARK 500 1 VAL A 19 -95.80 -4.98
REMARK 500 1 VAL A 21 -40.86 -4.29
REMARK 500 1 THR A 45 -95.54 33.20
REMARK 500 1 ARG A 55 -151.18 -141.21
REMARK 500 1 GLN A 56 -175.33 -177.43
REMARK 500 1 ALA A 57 148.98 -172.90
REMARK 500 1 ARG A 58 147.30 -176.17
REMARK 500 1 LYS A 59 39.16 135.26
REMARK 500 1 PHE A 61 -155.70 -11.71
REMARK 500 1 ASN A 62 -56.94 170.57
REMARK 500 1 GLN A 64 -111.55 -116.22
REMARK 500 1 GLN A 66 118.80 58.23
REMARK 500 1 GLU A 67 41.81 137.17
REMARK 500 1 ALA A 68 96.67 163.06
REMARK 500 1 LEU A 69 -148.76 -152.18
REMARK 500 1 GLU A 70 67.75 -177.19
REMARK 500 1 ILE A 71 -152.38 -115.41
REMARK 500 1 ALA A 72 56.33 -179.94
REMARK 500 1 SER A 74 95.87 -161.89
REMARK 500 1 SER A 78 -166.41 -58.87
REMARK 500 1 PRO A 81 74.30 -106.32
REMARK 500 1 LYS A 93 44.02 157.06
REMARK 500 1 ASN B 2 -174.02 -176.47
REMARK 500 1 LYS B 3 -16.37 -49.53
REMARK 500 1 THR B 14 -85.76 -113.54
REMARK 500 1 LEU B 16 -66.00 -13.93
REMARK 500 1 VAL B 19 -96.24 -4.94
REMARK 500 1 VAL B 21 -40.52 -24.42
REMARK 500 1 THR B 45 -89.83 33.07
REMARK 500 1 ARG B 55 17.62 -158.57
REMARK 500 1 GLN B 56 147.02 -173.50
REMARK 500 1 ALA B 57 21.80 -165.81
REMARK 500 1 LYS B 59 36.62 -174.57
REMARK 500 1 ASN B 62 -171.19 -56.22
REMARK 500 1 GLN B 64 -94.05 -135.47
REMARK 500 1 THR B 65 -30.88 -174.92
REMARK 500 1 GLU B 67 47.39 -89.37
REMARK 500 1 ALA B 68 152.77 -47.92
REMARK 500 1 LEU B 69 -162.83 -127.48
REMARK 500 1 GLU B 70 79.87 173.96
REMARK 500 1 ALA B 72 124.09 135.78
REMARK 500 1 VAL B 75 145.23 -19.41
REMARK 500 1 VAL B 79 172.99 -46.90
REMARK 500 1 LYS B 80 175.74 178.15
REMARK 500 1 LEU B 92 -71.67 -113.03
REMARK 500 2 ASN A 2 -158.30 -166.93
REMARK 500 2 LYS A 3 -8.04 -56.02
REMARK 500
REMARK 500 THIS ENTRY HAS 1093 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 55 0.24 SIDE CHAIN
REMARK 500 1 ARG A 58 0.25 SIDE CHAIN
REMARK 500 1 ARG B 55 0.24 SIDE CHAIN
REMARK 500 1 ARG B 58 0.24 SIDE CHAIN
REMARK 500 2 ARG A 55 0.26 SIDE CHAIN
REMARK 500 2 ARG A 58 0.31 SIDE CHAIN
REMARK 500 2 ARG B 55 0.32 SIDE CHAIN
REMARK 500 2 ARG B 58 0.31 SIDE CHAIN
REMARK 500 3 ARG A 55 0.29 SIDE CHAIN
REMARK 500 3 ARG A 58 0.21 SIDE CHAIN
REMARK 500 3 ARG B 55 0.25 SIDE CHAIN
REMARK 500 3 ARG B 58 0.30 SIDE CHAIN
REMARK 500 4 ARG A 55 0.31 SIDE CHAIN
REMARK 500 4 ARG A 58 0.32 SIDE CHAIN
REMARK 500 4 ARG B 55 0.32 SIDE CHAIN
REMARK 500 4 ARG B 58 0.22 SIDE CHAIN
REMARK 500 5 ARG A 55 0.31 SIDE CHAIN
REMARK 500 5 ARG A 58 0.23 SIDE CHAIN
REMARK 500 5 ARG B 55 0.26 SIDE CHAIN
REMARK 500 5 ARG B 58 0.24 SIDE CHAIN
REMARK 500 6 ARG A 55 0.32 SIDE CHAIN
REMARK 500 6 ARG A 58 0.18 SIDE CHAIN
REMARK 500 6 ARG B 55 0.30 SIDE CHAIN
REMARK 500 6 ARG B 58 0.24 SIDE CHAIN
REMARK 500 7 ARG A 55 0.24 SIDE CHAIN
REMARK 500 7 ARG A 58 0.23 SIDE CHAIN
REMARK 500 7 ARG B 55 0.32 SIDE CHAIN
REMARK 500 7 ARG B 58 0.31 SIDE CHAIN
REMARK 500 8 ARG A 55 0.29 SIDE CHAIN
REMARK 500 8 ARG B 55 0.27 SIDE CHAIN
REMARK 500 8 ARG B 58 0.22 SIDE CHAIN
REMARK 500 9 ARG A 55 0.27 SIDE CHAIN
REMARK 500 9 ARG A 58 0.29 SIDE CHAIN
REMARK 500 9 ARG B 55 0.31 SIDE CHAIN
REMARK 500 9 ARG B 58 0.28 SIDE CHAIN
REMARK 500 10 ARG A 55 0.24 SIDE CHAIN
REMARK 500 10 ARG A 58 0.21 SIDE CHAIN
REMARK 500 10 ARG B 55 0.27 SIDE CHAIN
REMARK 500 10 ARG B 58 0.29 SIDE CHAIN
REMARK 500 11 ARG A 55 0.25 SIDE CHAIN
REMARK 500 11 ARG A 58 0.31 SIDE CHAIN
REMARK 500 11 ARG B 55 0.25 SIDE CHAIN
REMARK 500 11 ARG B 58 0.32 SIDE CHAIN
REMARK 500 12 ARG A 55 0.23 SIDE CHAIN
REMARK 500 12 ARG A 58 0.30 SIDE CHAIN
REMARK 500 12 ARG B 55 0.24 SIDE CHAIN
REMARK 500 12 ARG B 58 0.32 SIDE CHAIN
REMARK 500 13 ARG A 55 0.32 SIDE CHAIN
REMARK 500 13 ARG A 58 0.30 SIDE CHAIN
REMARK 500 13 ARG B 55 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 90 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WTU RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF WILD TYPE TRANSCRIPTION FACTOR 1.
DBREF 1EXE A 1 99 UNP P04445 TF1_BPSP1 1 99
DBREF 1EXE B 1 99 UNP P04445 TF1_BPSP1 1 99
SEQADV 1EXE GLY A 15 UNP P04445 GLU 15 ENGINEERED MUTATION
SEQADV 1EXE ILE A 32 UNP P04445 THR 32 ENGINEERED MUTATION
SEQADV 1EXE GLY B 15 UNP P04445 GLU 15 ENGINEERED MUTATION
SEQADV 1EXE ILE B 32 UNP P04445 THR 32 ENGINEERED MUTATION
SEQRES 1 A 99 MET ASN LYS THR GLU LEU ILE LYS ALA ILE ALA GLN ASP
SEQRES 2 A 99 THR GLY LEU THR GLN VAL SER VAL SER LYS MET LEU ALA
SEQRES 3 A 99 SER PHE GLU LYS ILE ILE THR GLU THR VAL ALA LYS GLY
SEQRES 4 A 99 ASP LYS VAL GLN LEU THR GLY PHE LEU ASN ILE LYS PRO
SEQRES 5 A 99 VAL ALA ARG GLN ALA ARG LYS GLY PHE ASN PRO GLN THR
SEQRES 6 A 99 GLN GLU ALA LEU GLU ILE ALA PRO SER VAL GLY VAL SER
SEQRES 7 A 99 VAL LYS PRO GLY GLU SER LEU LYS LYS ALA ALA GLU GLY
SEQRES 8 A 99 LEU LYS TYR GLU ASP PHE ALA LYS
SEQRES 1 B 99 MET ASN LYS THR GLU LEU ILE LYS ALA ILE ALA GLN ASP
SEQRES 2 B 99 THR GLY LEU THR GLN VAL SER VAL SER LYS MET LEU ALA
SEQRES 3 B 99 SER PHE GLU LYS ILE ILE THR GLU THR VAL ALA LYS GLY
SEQRES 4 B 99 ASP LYS VAL GLN LEU THR GLY PHE LEU ASN ILE LYS PRO
SEQRES 5 B 99 VAL ALA ARG GLN ALA ARG LYS GLY PHE ASN PRO GLN THR
SEQRES 6 B 99 GLN GLU ALA LEU GLU ILE ALA PRO SER VAL GLY VAL SER
SEQRES 7 B 99 VAL LYS PRO GLY GLU SER LEU LYS LYS ALA ALA GLU GLY
SEQRES 8 B 99 LEU LYS TYR GLU ASP PHE ALA LYS
HELIX 1 1 THR A 4 GLY A 15 1 12
HELIX 2 2 SER A 20 GLY A 39 1 20
HELIX 3 3 GLY A 82 LYS A 93 1 12
HELIX 4 4 LYS A 93 LYS A 99 1 7
HELIX 5 5 THR B 4 THR B 14 1 11
HELIX 6 6 SER B 20 GLY B 39 1 20
HELIX 7 7 GLY B 82 LEU B 92 1 11
HELIX 8 8 LYS B 93 LYS B 99 1 7
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 - v 3 2 Bytes