Header list of 1h9c.pdb file
Complete list - n 31 2 Bytes
HEADER TRANSFERASE 07-MAR-01 1H9C
TITLE NMR STRUCTURE OF CYSTEINYL-PHOSPHORYLATED ENZYME IIB OF THE N,N'-
TITLE 2 DIACETYLCHITOBIOSE SPECIFIC PHOSPHOENOLPYRUVATE-DEPENDENT
TITLE 3 PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, CHITOBIOSE-SPECIFIC IIB COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIIB-CEL, EIIB-CHB;
COMPND 5 EC: 2.7.1.69;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PHOSPHORYLATION AT RESIDUE CYS10
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 316407;
SOURCE 4 STRAIN: W3110;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: CHBB [PREV CELA];
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 316407;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: W3110;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PJR-BLIIB
KEYWDS TRANSFERASE, ENZYME IIB-CHITOBIOSE, PHOSPHOTRANSFERASE SYSTEM, SUGAR
KEYWDS 2 TRANSPORT, PHOSPHORYLATION, IIB- CELLOBIOSE
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR E.AB,G.K.SCHUURMAN-WOLTERS,D.NIJLANT,K.DIJKSTRA,M.H.SAIER,
AUTHOR 2 G.T.ROBILLARD,R.M.SCHEEK
REVDAT 3 31-JAN-18 1H9C 1 SOURCE JRNL REMARK
REVDAT 2 24-FEB-09 1H9C 1 VERSN
REVDAT 1 21-MAY-01 1H9C 0
JRNL AUTH E.AB,G.K.SCHUURMAN-WOLTERS,D.NIJLANT,K.DIJKSTRA,M.H.SAIER,
JRNL AUTH 2 G.T.ROBILLARD,R.M.SCHEEK
JRNL TITL NMR STRUCTURE OF CYSTEINYL-PHOSPHORYLATED ENZYME IIB OF THE
JRNL TITL 2 N,N'-DIACETYLCHITOBIOSE SPECIFIC
JRNL TITL 3 PHOSPHOENOLPYRUVATE-DEPENDENTPHOSPHOTRANSFERASE SYSTEM OF
JRNL TITL 4 ESCHERICHIA COLI
JRNL REF J.MOL.BIOL. V. 308 993 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11352587
JRNL DOI 10.1006/JMBI.2001.4623
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.AB,G.SCHUURMAN-WOLTERS,J.REIZER,M.H.SAIER,K.DIJKSTRA,
REMARK 1 AUTH 2 R.M.SCHEEK,G.T.ROBILLARD
REMARK 1 TITL THE NMR SIDE-CHAIN ASSIGNMENTS AND SOLUTION STRUCTURE OF
REMARK 1 TITL 2 ENZYME IIBCELLOBIOSE OF THE PHOSPHOENOLPYRUVATE-DEPENDENT
REMARK 1 TITL 3 PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI
REMARK 1 REF PROTEIN SCI. V. 6 304 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9041631
REMARK 1 DOI 10.1002/PRO.5560060205
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.AB,G.K.SCHUURMAN-WOLTERS,M.H.SAIER,J.REIZER,M.JACUINOD,
REMARK 1 AUTH 2 P.ROEPSTORFF,K.DIJKSTRA,R.M.SCHEEK,G.T.ROBILLARD
REMARK 1 TITL ENZYME IIBCELLOBIOSE OF THE PHOSPHOENOL-PYRUVATE-DEPENDENT
REMARK 1 TITL 2 PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI: BACKBONE
REMARK 1 TITL 3 ASSIGNMENT AND SECONDARY STRUCTURE DETERMINED BY
REMARK 1 TITL 4 THREE-DIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF PROTEIN SCI. V. 3 282 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 8003964
REMARK 1 DOI 10.1002/PRO.5560030212
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.L.PARKER,B.G.HALL
REMARK 1 TITL CHARACTERIZATION AND NUCLEOTIDE SEQUENCE OF THE CRYPTIC CEL
REMARK 1 TITL 2 OPERON OF ESCHERICHIA COLI K12
REMARK 1 REF GENETICS V. 124 455 1990
REMARK 1 REFN ISSN 0016-6731
REMARK 1 PMID 2179047
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.REIZER,A.REIZER,M.H.SAIER JR
REMARK 1 TITL THE CELLOBIOSE PERMEASE OF ESCHERICHIA COLI CONSISTS OF
REMARK 1 TITL 2 THREE PROTEINS AND IS HOMOLOGOUS TO THE LACTOSE PERMEASE OF
REMARK 1 TITL 3 STAPHYLOCOCCUS AUREUS
REMARK 1 REF RES.MICROBIOL. V. 141 1061 1990
REMARK 1 REFN ISSN 0923-2508
REMARK 1 PMID 2092358
REMARK 1 DOI 10.1016/0923-2508(90)90079-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMACS
REMARK 3 AUTHORS : VAN DER SPOEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1H9C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1290005879.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SNARF, DDD, GROMACS
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 33
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET-FUNCTION, R-FACTOR,
REMARK 210 NUMBER OF VIOLATIONS
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: 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 400
REMARK 400 COMPOUND
REMARK 400 COMPONENT OF THE PHOSPHOENOLPYRUVATE-DEPENDENT SUGAR
REMARK 400 PHOSPHOTRANSFERASE SYSTEM (PTS)
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 TYR A 7 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 TYR A 30 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 TYR A 7 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 3 TYR A 7 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TYR A 7 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 TYR A 7 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 6 TYR A 7 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 7 TYR A 7 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 7 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 9 TYR A 7 CB - CG - CD2 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 GLU A 31 56.92 31.95
REMARK 500 1 ALA A 105 -169.09 -163.27
REMARK 500 2 MET A 14 -71.15 -115.25
REMARK 500 2 GLU A 31 63.19 29.28
REMARK 500 2 ALA A 105 94.92 137.45
REMARK 500 3 GLU A 31 64.85 28.31
REMARK 500 3 VAL A 87 70.22 58.35
REMARK 500 3 ALA A 104 -73.99 -68.05
REMARK 500 3 ALA A 105 87.09 -169.15
REMARK 500 4 LYS A 3 146.98 63.23
REMARK 500 4 ALA A 104 33.39 -91.88
REMARK 500 4 ALA A 105 105.83 59.61
REMARK 500 5 GLU A 31 68.29 22.57
REMARK 500 5 ALA A 105 59.39 -104.19
REMARK 500 6 GLU A 2 126.65 64.20
REMARK 500 6 GLU A 31 58.31 28.07
REMARK 500 6 VAL A 87 59.29 39.14
REMARK 500 6 ALA A 104 -32.61 62.85
REMARK 500 6 ALA A 105 128.82 120.56
REMARK 500 7 MET A 14 -72.36 -106.34
REMARK 500 7 GLU A 31 65.05 32.47
REMARK 500 7 LYS A 101 -41.22 57.24
REMARK 500 7 LYS A 102 84.22 111.77
REMARK 500 7 ALA A 104 76.01 48.37
REMARK 500 7 ALA A 105 76.43 28.39
REMARK 500 8 GLU A 2 78.05 62.41
REMARK 500 8 GLU A 31 69.20 29.53
REMARK 500 8 ALA A 105 98.97 159.92
REMARK 500 9 LYS A 3 147.60 67.53
REMARK 500 9 MET A 14 -71.37 -101.60
REMARK 500 9 GLU A 31 69.76 30.32
REMARK 500 9 LYS A 101 1.09 -61.56
REMARK 500 9 LYS A 102 70.48 75.33
REMARK 500 9 ALA A 105 81.25 28.14
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 ILE A 100 LYS A 101 7 -147.93
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 TYR A 30 0.08 SIDE CHAIN
REMARK 500 1 TYR A 84 0.07 SIDE CHAIN
REMARK 500 2 TYR A 7 0.07 SIDE CHAIN
REMARK 500 3 TYR A 7 0.07 SIDE CHAIN
REMARK 500 3 TYR A 30 0.07 SIDE CHAIN
REMARK 500 4 TYR A 7 0.07 SIDE CHAIN
REMARK 500 5 TYR A 7 0.07 SIDE CHAIN
REMARK 500 7 TYR A 7 0.07 SIDE CHAIN
REMARK 500 8 TYR A 7 0.07 SIDE CHAIN
REMARK 500 9 TYR A 84 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 GLY A 45 -11.12
REMARK 500 5 GLY A 45 -11.68
REMARK 500 6 GLU A 46 -10.61
REMARK 500 7 ARG A 24 -10.30
REMARK 500 7 GLY A 45 -10.52
REMARK 500 7 LYS A 101 12.29
REMARK 500 9 GLY A 45 -11.96
REMARK 500 9 GLU A 46 -10.35
REMARK 500 9 ALA A 104 -11.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1H9C A 1 106 UNP P17409 PTCB_ECOLI 1 106
SEQADV 1H9C CSP A 10 UNP P17409 CYS 10 MODIFIED RESIDUE
SEQRES 1 A 106 MET GLU LYS LYS HIS ILE TYR LEU PHE CSP SER ALA GLY
SEQRES 2 A 106 MET SER THR SER LEU LEU VAL SER LYS MET ARG ALA GLN
SEQRES 3 A 106 ALA GLU LYS TYR GLU VAL PRO VAL ILE ILE GLU ALA PHE
SEQRES 4 A 106 PRO GLU THR LEU ALA GLY GLU LYS GLY GLN ASN ALA ASP
SEQRES 5 A 106 VAL VAL LEU LEU GLY PRO GLN ILE ALA TYR MET LEU PRO
SEQRES 6 A 106 GLU ILE GLN ARG LEU LEU PRO ASN LYS PRO VAL GLU VAL
SEQRES 7 A 106 ILE ASP SER LEU LEU TYR GLY LYS VAL ASP GLY LEU GLY
SEQRES 8 A 106 VAL LEU LYS ALA ALA VAL ALA ALA ILE LYS LYS ALA ALA
SEQRES 9 A 106 ALA ASN
MODRES 1H9C CSP A 10 CYS S-PHOSPHOCYSTEINE
HET CSP A 10 15
HETNAM CSP S-PHOSPHOCYSTEINE
FORMUL 1 CSP C3 H8 N O5 P S
HELIX 1 1 THR A 16 TYR A 30 1 15
HELIX 2 2 LEU A 43 GLN A 49 1 7
HELIX 3 3 PRO A 58 TYR A 62 5 5
HELIX 4 4 MET A 63 LEU A 71 1 9
HELIX 5 5 ASP A 80 VAL A 87 1 8
HELIX 6 6 ASP A 88 ALA A 105 1 18
SHEET 1 AA 4 VAL A 34 PRO A 40 0
SHEET 2 AA 4 LYS A 4 CSP A 10 1 O LYS A 4 N ILE A 35
SHEET 3 AA 4 VAL A 53 LEU A 56 1 O VAL A 53 N TYR A 7
SHEET 4 AA 4 VAL A 76 VAL A 78 1 O GLU A 77 N LEU A 56
LINK C PHE A 9 N CSP A 10 1555 1555 1.33
LINK C CSP A 10 N SER A 11 1555 1555 1.33
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 - n 31 2 Bytes