Header list of 1f22.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 23-MAY-00 1F22
TITLE A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM
TITLE 2 DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE REDUCED AND THE
TITLE 3 OXIDIZED FORMS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C7;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFUROMONAS ACETOXIDANS;
SOURCE 3 ORGANISM_TAXID: 891
KEYWDS TRIHEME, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR M.ASSFALG,L.BANCI,I.BERTINI,M.BRUSCHI,M.T.GIUDICI-ORTICONI
REVDAT 4 16-FEB-22 1F22 1 REMARK LINK
REVDAT 3 24-FEB-09 1F22 1 VERSN
REVDAT 2 06-SEP-05 1F22 1 JRNL REMARK LINK HETATM
REVDAT 1 21-JUN-00 1F22 0
JRNL AUTH M.ASSFALG,L.BANCI,I.BERTINI,M.BRUSCHI,M.T.GIUDICI-ORTICONI
JRNL TITL A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME
JRNL TITL 2 C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE
JRNL TITL 3 REDUCED AND THE OXIDIZED FORMS.
JRNL REF EUR.J.BIOCHEM. V. 266 634 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10561607
JRNL DOI 10.1046/J.1432-1327.1999.00904.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F22 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011148.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 292
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.1 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2-3MM CYTOCHROME C7; 10MM
REMARK 210 PHOSPHATE BUFFER; CATALYTIC
REMARK 210 AMOUNTS OF D. VULGARIS
REMARK 210 HYDROGENASE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING AND ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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
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 HIS A 30 CB - CG - CD2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 26 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 33 ASP A 40 CB - CG - OD2 ANGL. DEV. = -6.3 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 12 121.94 -38.26
REMARK 500 1 ASP A 16 131.12 -37.10
REMARK 500 1 HIS A 17 -63.99 -120.60
REMARK 500 1 CYS A 26 -50.85 177.09
REMARK 500 1 ALA A 35 -33.37 -172.35
REMARK 500 1 LYS A 36 175.07 161.53
REMARK 500 1 ILE A 37 -62.20 -133.95
REMARK 500 1 ALA A 38 82.14 72.96
REMARK 500 1 LYS A 42 -83.17 -45.35
REMARK 500 1 LYS A 46 -70.18 -99.56
REMARK 500 1 ALA A 48 -89.64 -98.82
REMARK 500 1 HIS A 53 43.69 -73.98
REMARK 500 1 ASN A 57 -175.75 60.49
REMARK 500 1 THR A 60 39.78 -157.22
REMARK 500 1 LYS A 61 -73.88 55.62
REMARK 500 1 CYS A 62 -151.91 -121.39
REMARK 500 1 CYS A 65 -52.43 -133.28
REMARK 500 2 ASP A 2 -11.32 -144.48
REMARK 500 2 GLU A 7 131.35 74.53
REMARK 500 2 ASN A 12 -168.17 57.64
REMARK 500 2 HIS A 17 -71.36 -109.78
REMARK 500 2 CYS A 26 -50.59 174.76
REMARK 500 2 GLU A 31 -114.62 -85.34
REMARK 500 2 ALA A 35 44.41 38.22
REMARK 500 2 LYS A 36 125.94 59.64
REMARK 500 2 ILE A 37 -133.59 -87.85
REMARK 500 2 ALA A 38 50.36 164.28
REMARK 500 2 LYS A 46 -73.52 -80.82
REMARK 500 2 ASP A 47 86.28 -159.79
REMARK 500 2 ALA A 48 -75.52 -147.37
REMARK 500 2 THR A 51 -36.68 -161.12
REMARK 500 2 SER A 55 62.24 -158.22
REMARK 500 2 ASN A 56 -39.47 173.00
REMARK 500 2 THR A 60 -53.70 -145.52
REMARK 500 2 LYS A 61 74.23 -164.44
REMARK 500 2 CYS A 62 -133.91 55.72
REMARK 500 3 ASP A 2 54.16 -44.43
REMARK 500 3 VAL A 3 138.56 172.61
REMARK 500 3 GLU A 7 85.86 58.32
REMARK 500 3 HIS A 17 -65.53 -130.56
REMARK 500 3 CYS A 26 -43.43 172.68
REMARK 500 3 ALA A 28 -51.17 -29.09
REMARK 500 3 ALA A 35 43.79 -178.38
REMARK 500 3 LYS A 36 116.57 62.82
REMARK 500 3 ALA A 38 75.65 60.95
REMARK 500 3 HIS A 45 32.63 -92.73
REMARK 500 3 LYS A 46 -74.21 -133.47
REMARK 500 3 ALA A 48 -80.37 -153.25
REMARK 500 3 HIS A 53 45.02 -74.24
REMARK 500 3 ASN A 57 178.76 60.12
REMARK 500
REMARK 500 THIS ENTRY HAS 608 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 59 THR A 60 2 -140.69
REMARK 500 ALA A 1 ASP A 2 3 140.59
REMARK 500 PRO A 59 THR A 60 4 -137.48
REMARK 500 ASP A 47 ALA A 48 5 -145.61
REMARK 500 ALA A 1 ASP A 2 10 -144.65
REMARK 500 ALA A 1 ASP A 2 11 140.59
REMARK 500 PRO A 59 THR A 60 13 -135.00
REMARK 500 PRO A 59 THR A 60 15 -134.02
REMARK 500 ALA A 1 ASP A 2 16 143.41
REMARK 500 LYS A 61 CYS A 62 17 144.00
REMARK 500 ALA A 1 ASP A 2 18 142.56
REMARK 500 ALA A 1 ASP A 2 20 144.88
REMARK 500 PHE A 15 ASP A 16 25 144.41
REMARK 500 PRO A 59 THR A 60 25 -141.48
REMARK 500 PRO A 59 THR A 60 30 -129.04
REMARK 500 PRO A 59 THR A 60 33 -136.16
REMARK 500 PRO A 59 THR A 60 35 -129.76
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 HIS A 30 0.09 SIDE CHAIN
REMARK 500 2 TYR A 6 0.12 SIDE CHAIN
REMARK 500 2 HIS A 30 0.09 SIDE CHAIN
REMARK 500 4 TYR A 6 0.14 SIDE CHAIN
REMARK 500 5 PHE A 15 0.10 SIDE CHAIN
REMARK 500 5 HIS A 30 0.13 SIDE CHAIN
REMARK 500 6 HIS A 30 0.10 SIDE CHAIN
REMARK 500 7 TYR A 6 0.11 SIDE CHAIN
REMARK 500 8 TYR A 6 0.11 SIDE CHAIN
REMARK 500 9 HIS A 30 0.09 SIDE CHAIN
REMARK 500 10 TYR A 6 0.08 SIDE CHAIN
REMARK 500 10 HIS A 30 0.10 SIDE CHAIN
REMARK 500 11 TYR A 6 0.10 SIDE CHAIN
REMARK 500 11 HIS A 30 0.11 SIDE CHAIN
REMARK 500 13 HIS A 30 0.09 SIDE CHAIN
REMARK 500 14 HIS A 30 0.12 SIDE CHAIN
REMARK 500 15 HIS A 30 0.11 SIDE CHAIN
REMARK 500 18 TYR A 6 0.09 SIDE CHAIN
REMARK 500 18 HIS A 30 0.11 SIDE CHAIN
REMARK 500 19 PHE A 15 0.08 SIDE CHAIN
REMARK 500 20 HIS A 30 0.12 SIDE CHAIN
REMARK 500 21 TYR A 6 0.14 SIDE CHAIN
REMARK 500 22 TYR A 6 0.12 SIDE CHAIN
REMARK 500 23 TYR A 6 0.16 SIDE CHAIN
REMARK 500 24 HIS A 30 0.12 SIDE CHAIN
REMARK 500 26 TYR A 6 0.11 SIDE CHAIN
REMARK 500 26 HIS A 30 0.11 SIDE CHAIN
REMARK 500 28 HIS A 30 0.09 SIDE CHAIN
REMARK 500 29 HIS A 30 0.10 SIDE CHAIN
REMARK 500 30 TYR A 6 0.06 SIDE CHAIN
REMARK 500 33 TYR A 6 0.07 SIDE CHAIN
REMARK 500 34 PHE A 15 0.14 SIDE CHAIN
REMARK 500 35 HIS A 30 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 69 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 17 NE2
REMARK 620 2 HEC A 69 NA 93.5
REMARK 620 3 HEC A 69 NB 90.7 90.2
REMARK 620 4 HEC A 69 NC 85.2 178.2 91.1
REMARK 620 5 HEC A 69 ND 89.7 88.7 178.8 90.1
REMARK 620 6 HIS A 30 NE2 172.9 93.6 89.4 87.8 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 70 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 20 NE2
REMARK 620 2 HEC A 70 NA 91.1
REMARK 620 3 HEC A 70 NB 94.9 90.8
REMARK 620 4 HEC A 70 NC 87.6 178.6 89.7
REMARK 620 5 HEC A 70 ND 86.0 90.5 178.4 88.9
REMARK 620 6 HIS A 53 NE2 175.8 90.7 88.9 90.5 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 71 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 45 NE2
REMARK 620 2 HEC A 71 NA 91.6
REMARK 620 3 HEC A 71 NB 92.2 91.0
REMARK 620 4 HEC A 71 NC 89.9 178.5 88.7
REMARK 620 5 HEC A 71 ND 92.4 91.4 174.7 88.8
REMARK 620 6 HIS A 66 NE2 178.0 89.3 89.6 89.2 85.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 69
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 71
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHJ RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1F22 A 1 68 UNP P00137 CYC3_DESAC 1 68
SEQRES 1 A 68 ALA ASP VAL VAL THR TYR GLU ASN LYS LYS GLY ASN VAL
SEQRES 2 A 68 THR PHE ASP HIS LYS ALA HIS ALA GLU LYS LEU GLY CYS
SEQRES 3 A 68 ASP ALA CYS HIS GLU GLY THR PRO ALA LYS ILE ALA ILE
SEQRES 4 A 68 ASP LYS LYS SER ALA HIS LYS ASP ALA CYS LYS THR CYS
SEQRES 5 A 68 HIS LYS SER ASN ASN GLY PRO THR LYS CYS GLY GLY CYS
SEQRES 6 A 68 HIS ILE LYS
HET HEC A 69 75
HET HEC A 70 75
HET HEC A 71 75
HETNAM HEC HEME C
FORMUL 2 HEC 3(C34 H34 FE N4 O4)
HELIX 1 1 HIS A 17 GLY A 25 1 9
HELIX 2 2 ASP A 40 ASP A 47 1 8
HELIX 3 3 ALA A 48 HIS A 53 1 6
SHEET 1 A 2 VAL A 3 TYR A 6 0
SHEET 2 A 2 VAL A 13 ASP A 16 -1 N VAL A 13 O TYR A 6
LINK SG CYS A 26 CAB HEC A 69 1555 1555 1.82
LINK SG CYS A 29 CAC HEC A 69 1555 1555 1.81
LINK SG CYS A 49 CAB HEC A 70 1555 1555 1.82
LINK SG CYS A 52 CAC HEC A 70 1555 1555 1.81
LINK SG CYS A 62 CAB HEC A 71 1555 1555 1.81
LINK SG CYS A 65 CAC HEC A 71 1555 1555 1.81
LINK NE2 HIS A 17 FE HEC A 69 1555 1555 1.91
LINK NE2 HIS A 20 FE HEC A 70 1555 1555 1.99
LINK NE2 HIS A 30 FE HEC A 69 1555 1555 1.93
LINK NE2 HIS A 45 FE HEC A 71 1555 1555 1.96
LINK NE2 HIS A 53 FE HEC A 70 1555 1555 2.00
LINK NE2 HIS A 66 FE HEC A 71 1555 1555 1.90
SITE 1 AC1 13 ALA A 1 TYR A 6 HIS A 17 HIS A 20
SITE 2 AC1 13 GLY A 25 CYS A 26 CYS A 29 HIS A 30
SITE 3 AC1 13 PRO A 34 ALA A 35 LYS A 36 ILE A 37
SITE 4 AC1 13 ALA A 38
SITE 1 AC2 11 VAL A 13 PHE A 15 ASP A 16 HIS A 20
SITE 2 AC2 11 LYS A 23 LEU A 24 CYS A 49 CYS A 52
SITE 3 AC2 11 HIS A 53 ASN A 57 GLY A 64
SITE 1 AC3 15 TYR A 6 ASN A 8 LYS A 10 VAL A 13
SITE 2 AC3 15 ILE A 39 ASP A 40 LYS A 41 ALA A 44
SITE 3 AC3 15 HIS A 45 CYS A 49 HIS A 53 LYS A 61
SITE 4 AC3 15 CYS A 62 CYS A 65 HIS A 66
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