Header list of 3eza.pdb file
Complete list - 16 20 Bytes
HEADER COMPLEX (TRANSFERASE/PHOSPHOCARRIER) 03-NOV-98 3EZA
TITLE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-
TITLE 2 CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR,
TITLE 3 RESTRAINED REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOTRANSFERASE SYSTEM, ENZYME I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN RESIDUES 1 - 249;
COMPND 5 EC: 2.7.3.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: GI698;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLP2;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 562;
SOURCE 11 STRAIN: GI698;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PSP100
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT, COMPLEX
KEYWDS 2 (TRANSFERASE-PHOSPHOCARRIER), COMPLEX (TRANSFERASE-PHOSPHOCARRIER)
KEYWDS 3 COMPLEX
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,D.S.GARRETT,A.M.GRONENBORN
REVDAT 3 16-MAR-22 3EZA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 3EZA 1 VERSN
REVDAT 1 25-MAY-99 3EZA 0
JRNL AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,A.M.GRONENBORN,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE 40,000 MR PHOSPHORYL TRANSFER
JRNL TITL 2 COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF ENZYME I AND HPR.
JRNL REF NAT.STRUCT.BIOL. V. 6 166 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10048929
JRNL DOI 10.1038/5854
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL TAUTOMERIC STATE AND PKA OF THE PHOSPHORYLATED ACTIVE SITE
REMARK 1 TITL 2 HISTIDINE IN THE N-TERMINAL DOMAIN OF ENZYME I OF THE
REMARK 1 TITL 3 ESCHERICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR
REMARK 1 TITL 4 PHOSPHOTRANSFERASE SYSTEM
REMARK 1 REF PROTEIN SCI. V. 7 789 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,D.I.LIAO,A.PETERKOFSKY,A.M.GRONENBORN,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL SOLUTION STRUCTURE OF THE 30 KDA N-TERMINAL DOMAIN OF ENZYME
REMARK 1 TITL 2 I OF THE ESCHERICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR
REMARK 1 TITL 3 PHOSPHOTRANSFERASE SYSTEM BY MULTIDIMENSIONAL NMR
REMARK 1 REF BIOCHEMISTRY V. 36 2517 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL IDENTIFICATION BY NMR OF THE BINDING SURFACE FOR THE
REMARK 1 TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR ON THE
REMARK 1 TITL 3 N-TERMINAL DOMAIN OF ENZYME I OF THE ESCHERICHIA COLI
REMARK 1 TITL 4 PHOSPHOTRANSFERASE SYSTEM
REMARK 1 REF BIOCHEMISTRY V. 36 4393 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
REMARK 3 129-136 USING THE PROGRAM CNS MODIFIED TO INCORPORATE
REMARK 3 COUPLING CONSTANT RESTRAINTS (GARRETT ET AL. (1984) J. MAGN.
REMARK 3 RESON. SERIES B 104, 99-103), CARBON CHEMICAL SHIFT
REMARK 3 RESTRAINTS, (KUSZEWSKI ET AL. (1995) J. MAGN. RESON.
REMARK 3 SERIES B 106, 92-96) RESTRAINTS, AND RESIDUAL DIPOLAR
REMARK 3 COUPLING RESTRAINTS (CLORE ET AL. J. MAGN. RESON 131,
REMARK 3 159-162 (1998); J. MAGN 133, 216-221(1998)).
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST
REMARK 3 COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO MEANING.
REMARK 3 FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT
REMARK 3 BEST TO RESIDUES 1 - 250 (RESIDUES 251 - 249 ARE DISORDERED
REMARK 3 IN SOLUTION) OF ENZYME I AND RESIDUES 1-85 OF HPR.
REMARK 3 RESIDUES 251-249 ARE OMITTED FROM THE MEAN STRUCTURE.
REMARK 4
REMARK 4 3EZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178956.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS (SEE ABOVE) ABOVE)
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE 3D STRUCTURE OF THE EIN-HPR COMPLEX WAS SOLVED
REMARK 210 BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED
REMARK 210 ON 5475 EXPERIMENTAL NMR RESTRAINTS:'
REMARK 210
REMARK 210 INTRAMOLECULAR EIN NOES: 746 SEQUENTIAL (|I-J|1), 517
REMARK 210 MEDIUM RANGE (1 < |I-J <= 5), 436 LONG RANGE (|I-J|>5)
REMARK 210 INTERRESIDUE NOES AND 486 INTRARESIDUE NOES.
REMARK 210
REMARK 210 INTRAMOLECULAR HPR NOES: 247 SEQUENTIAL (|I-J|1), 167
REMARK 210 MEDIUM RANGE (1 < |I-J <= 5), 246 LONG RANGE (|I-J|>5)
REMARK 210 INTERRESIDUE NOES AND 202 INTRARESIDUE NOES.
REMARK 210
REMARK 210 INTERMOLECULAR NOES BETWEEN EIN AND HPR: 117 TORSION ANGLE
REMARK 210 RESTRAINTS 768 FOR EIN AND 170 FOR HPR.
REMARK 210
REMARK 210 3JHNA COUPLING CONSTANT RESTRAINTS: 34 FOR HPR
REMARK 210
REMARK 210 13CALPHA AND 13CBETA CHEMICAL SHIFT RESTRAINTS: 503 FOR
REMARK 210 EIN, 162 FOR HPR.
REMARK 210
REMARK 210 ONE-BOND N-H DIPOLAR COUPLING CONSTANT RESTRAINTS: 165 FOR
REMARK 210 EIN AND 79 FOR HPR
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 O ALA A 91 H ASP A 95 1.49
REMARK 500 O LEU B 50 H LEU B 53 1.50
REMARK 500 O GLU A 41 H SER A 45 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 97 CB HIS A 97 CG 0.125
REMARK 500 HIS A 97 CG HIS A 97 CD2 0.137
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 HIS A 97 CB - CG - CD2 ANGL. DEV. = 15.3 DEGREES
REMARK 500 HIS A 97 ND1 - CG - CD2 ANGL. DEV. = -77.0 DEGREES
REMARK 500 HIS A 97 CG - ND1 - CE1 ANGL. DEV. = -69.0 DEGREES
REMARK 500 HIS A 97 ND1 - CE1 - NE2 ANGL. DEV. = -74.5 DEGREES
REMARK 500 HIS A 97 CE1 - NE2 - CD2 ANGL. DEV. = -65.6 DEGREES
REMARK 500 HIS A 97 CG - CD2 - NE2 ANGL. DEV. = -67.3 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 LEU A 6 103.92 53.36
REMARK 500 LYS A 49 -73.01 -63.80
REMARK 500 ALA A 50 -33.72 -38.50
REMARK 500 ASP A 119 40.60 -98.53
REMARK 500 ASP A 148 113.62 61.63
REMARK 500 ASP A 162 146.57 -170.37
REMARK 500 PRO A 165 -36.48 -39.80
REMARK 500 GLN A 170 36.95 -84.49
REMARK 500 ALA A 183 -163.67 -55.31
REMARK 500 THR A 187 2.99 -65.10
REMARK 500 SER A 207 40.56 -160.78
REMARK 500 ALA A 222 14.44 49.80
REMARK 500 ASN B 38 64.33 39.77
REMARK 500 GLN B 51 -18.24 -41.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZB RELATED DB: PDB
REMARK 900 RELATED ID: 3EZE RELATED DB: PDB
DBREF 3EZA A 1 249 UNP P08839 PT1_ECOLI 1 249
DBREF 3EZA B 1 85 UNP P0AA04 PTHP_ECOLI 1 85
SEQADV 3EZA ILE B 63 UNP P0AA04 LEU 63 CONFLICT
SEQRES 1 A 249 MET ILE SER GLY ILE LEU ALA SER PRO GLY ILE ALA PHE
SEQRES 2 A 249 GLY LYS ALA LEU LEU LEU LYS GLU ASP GLU ILE VAL ILE
SEQRES 3 A 249 ASP ARG LYS LYS ILE SER ALA ASP GLN VAL ASP GLN GLU
SEQRES 4 A 249 VAL GLU ARG PHE LEU SER GLY ARG ALA LYS ALA SER ALA
SEQRES 5 A 249 GLN LEU GLU THR ILE LYS THR LYS ALA GLY GLU THR PHE
SEQRES 6 A 249 GLY GLU GLU LYS GLU ALA ILE PHE GLU GLY HIS ILE MET
SEQRES 7 A 249 LEU LEU GLU ASP GLU GLU LEU GLU GLN GLU ILE ILE ALA
SEQRES 8 A 249 LEU ILE LYS ASP LYS HIS MET THR ALA ASP ALA ALA ALA
SEQRES 9 A 249 HIS GLU VAL ILE GLU GLY GLN ALA SER ALA LEU GLU GLU
SEQRES 10 A 249 LEU ASP ASP GLU TYR LEU LYS GLU ARG ALA ALA ASP VAL
SEQRES 11 A 249 ARG ASP ILE GLY LYS ARG LEU LEU ARG ASN ILE LEU GLY
SEQRES 12 A 249 LEU LYS ILE ILE ASP LEU SER ALA ILE GLN ASP GLU VAL
SEQRES 13 A 249 ILE LEU VAL ALA ALA ASP LEU THR PRO SER GLU THR ALA
SEQRES 14 A 249 GLN LEU ASN LEU LYS LYS VAL LEU GLY PHE ILE THR ASP
SEQRES 15 A 249 ALA GLY GLY ARG THR SER HIS THR SER ILE MET ALA ARG
SEQRES 16 A 249 SER LEU GLU LEU PRO ALA ILE VAL GLY THR GLY SER VAL
SEQRES 17 A 249 THR SER GLN VAL LYS ASN ASP ASP TYR LEU ILE LEU ASP
SEQRES 18 A 249 ALA VAL ASN ASN GLN VAL TYR VAL ASN PRO THR ASN GLU
SEQRES 19 A 249 VAL ILE ASP LYS MET ARG ALA VAL GLN GLU GLN VAL ALA
SEQRES 20 A 249 SER GLU
SEQRES 1 B 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 B 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 B 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 B 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 B 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 B 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 B 85 LYS LEU MET ALA GLU LEU GLU
HELIX 1 1 ALA A 33 THR A 64 1 32
HELIX 2 2 GLU A 67 LEU A 80 1 14
HELIX 3 3 GLU A 83 LYS A 96 1 14
HELIX 4 4 ALA A 100 GLU A 116 1 17
HELIX 5 5 GLU A 121 LEU A 142 1 22
HELIX 6 6 PRO A 165 ALA A 169 1 5
HELIX 7 7 HIS A 189 LEU A 197 1 9
HELIX 8 8 ASN A 233 ALA A 247 1 15
HELIX 9 9 THR B 16 GLY B 28 1 13
HELIX 10 10 LEU B 47 THR B 52 1 6
HELIX 11 11 GLU B 70 GLU B 83 1 14
SHEET 1 A 5 PHE A 179 THR A 181 0
SHEET 2 A 5 ILE A 157 ALA A 160 1 N LEU A 158 O ILE A 180
SHEET 3 A 5 ALA A 12 LEU A 18 1 N LEU A 17 O ILE A 157
SHEET 4 A 5 ASP A 216 LEU A 220 -1 N LEU A 220 O ALA A 12
SHEET 5 A 5 VAL A 227 VAL A 229 -1 N TYR A 228 O ILE A 219
SHEET 1 B 4 PHE B 2 THR B 7 0
SHEET 2 B 4 VAL B 60 GLU B 66 -1 N ALA B 65 O PHE B 2
SHEET 3 B 4 GLU B 32 SER B 37 -1 N THR B 36 O THR B 62
SHEET 4 B 4 LYS B 40 SER B 43 -1 N ALA B 42 O VAL B 35
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
Complete list - 16 20 Bytes