Header list of 1iba.pdb file
Complete list - v 29 2 Bytes
HEADER PHOSPHOTRANSFERASE 23-MAR-96 1IBA
TITLE GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE PERMEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN IIB;
COMPND 5 EC: 2.7.1.69;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: K-12, W3110;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQBH;
SOURCE 8 EXPRESSION_SYSTEM_GENE: PTSG
KEYWDS PHOSPHOTRANSFERASE SYSTEM, SUGAR TRANSPORT, TRANSFERASE,
KEYWDS 2 PHOSPHORYLATION, TRANSMEMBRANE, INNER MEMBRANE, PHOSPHOTRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR M.EBERSTADT,S.G.GRDADOLNIK,G.GEMMECKER,H.KESSLER,A.BUHR,B.ERNI
REVDAT 3 29-NOV-17 1IBA 1 REMARK HELIX
REVDAT 2 24-FEB-09 1IBA 1 VERSN
REVDAT 1 14-OCT-96 1IBA 0
JRNL AUTH M.EBERSTADT,S.G.GRDADOLNIK,G.GEMMECKER,H.KESSLER,A.BUHR,
JRNL AUTH 2 B.ERNI
JRNL TITL SOLUTION STRUCTURE OF THE IIB DOMAIN OF THE GLUCOSE
JRNL TITL 2 TRANSPORTER OF ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 35 11286 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8784182
JRNL DOI 10.1021/BI960492L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.GOLIC GRDADOLNIK,M.EBERSTADT,G.GEMMECKER,H.KESSLER,A.BUHR,
REMARK 1 AUTH 2 B.ERNI
REMARK 1 TITL THE GLUCOSE TRANSPORTER OF ESCHERICHIA COLI. ASSIGNMENT OF
REMARK 1 TITL 2 THE 1H, 13C AND 15N RESONANCES AND IDENTIFICATION OF THE
REMARK 1 TITL 3 SECONDARY STRUCTURE OF THE SOLUBLE IIB DOMAIN
REMARK 1 REF EUR.J.BIOCHEM. V. 219 945 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.BUHR,K.FLUKIGER,B.ERNI
REMARK 1 TITL THE GLUCOSE TRANSPORTER OF ESCHERICHIA COLI
REMARK 1 REF J.BIOL.CHEM. V. 269 23437 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.MEINS,P.JENO,D.MULLER,W.J.RICHTER,J.P.ROSENBUSCH,B.ERNI
REMARK 1 TITL CYSTEINE PHOSPHORYLATION OF THE GLUCOSE TRANSPORTER OF
REMARK 1 TITL 2 ESCHERICHIA COLI
REMARK 1 REF J.BIOL.CHEM. V. 268 11604 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.ERNI,B.ZANOLARI
REMARK 1 TITL GLUCOSE-PERMEASE OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM.
REMARK 1 TITL 2 GENE CLONING, OVERPRODUCTION, AND AMINO ACID SEQUENCE OF
REMARK 1 TITL 3 ENZYME IIGLC
REMARK 1 REF J.BIOL.CHEM. V. 261 16398 1986
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 2.8
REMARK 3 AUTHORS : GUNTERT, BRAUN, WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IBA 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_1000174094.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-11
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PHE A 2
REMARK 465 LYS A 3
REMARK 465 ASN A 4
REMARK 465 GLU A 5
REMARK 465 ASP A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 THR A 10
REMARK 465 GLY A 11
REMARK 465 THR A 12
REMARK 465 SER A 13
REMARK 465 GLU A 14
REMARK 465 SER A 93
REMARK 465 ARG A 94
REMARK 465 SER A 95
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
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 1 LEU A 39 CB - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 2 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 PHE A 23 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 4 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 LEU A 39 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 5 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 7 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 8 PHE A 23 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 8 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 9 PHE A 23 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 9 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 9 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 10 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 40 CB - CG - CD ANGL. DEV. = 16.9 DEGREES
REMARK 500 10 ARG A 40 CG - CD - NE ANGL. DEV. = 13.8 DEGREES
REMARK 500 10 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 10 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 PHE A 23 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 11 PHE A 23 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 11 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 4.9 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 VAL A 20 -36.99 -38.31
REMARK 500 1 ALA A 22 -19.70 -48.15
REMARK 500 1 PHE A 23 -53.86 -140.14
REMARK 500 1 ILE A 29 135.94 -32.05
REMARK 500 1 ASP A 33 65.74 -111.92
REMARK 500 1 ILE A 36 -63.23 -25.03
REMARK 500 1 LYS A 48 26.58 -150.74
REMARK 500 1 ALA A 59 -160.00 -112.81
REMARK 500 1 SER A 67 -33.59 127.07
REMARK 500 1 THR A 75 -74.59 53.62
REMARK 500 1 LYS A 76 54.75 -105.10
REMARK 500 2 ALA A 22 -16.66 -49.03
REMARK 500 2 PHE A 23 -52.78 -142.28
REMARK 500 2 LYS A 26 55.97 -95.18
REMARK 500 2 ILE A 29 152.18 -44.00
REMARK 500 2 ILE A 36 -94.70 -4.18
REMARK 500 2 ALA A 44 74.36 -104.87
REMARK 500 2 LYS A 48 -64.80 -164.59
REMARK 500 2 VAL A 49 177.31 42.63
REMARK 500 2 ALA A 59 -166.00 -110.56
REMARK 500 2 SER A 67 -39.46 130.74
REMARK 500 2 SER A 77 -34.08 -37.72
REMARK 500 3 PHE A 23 -52.84 -128.66
REMARK 500 3 ILE A 29 159.25 -20.67
REMARK 500 3 ILE A 36 -71.75 -30.43
REMARK 500 3 ASP A 45 76.03 -59.15
REMARK 500 3 LYS A 48 13.01 -140.35
REMARK 500 3 VAL A 49 132.75 -38.25
REMARK 500 3 ALA A 59 -162.17 -119.19
REMARK 500 3 ALA A 60 56.23 -151.08
REMARK 500 3 SER A 67 -29.14 120.82
REMARK 500 3 SER A 77 -39.91 -32.98
REMARK 500 4 ALA A 22 -13.83 -49.91
REMARK 500 4 PHE A 23 -48.17 -145.85
REMARK 500 4 ILE A 29 155.15 -13.98
REMARK 500 4 ILE A 36 -66.27 -24.99
REMARK 500 4 SER A 42 98.06 -69.10
REMARK 500 4 LYS A 48 26.01 -150.31
REMARK 500 4 ASP A 50 64.21 -102.89
REMARK 500 4 ALA A 59 -151.69 -105.48
REMARK 500 4 SER A 67 -24.28 117.35
REMARK 500 4 PHE A 73 50.04 -116.04
REMARK 500 4 THR A 75 -42.66 82.74
REMARK 500 4 LYS A 76 55.25 -148.78
REMARK 500 5 PHE A 23 -49.15 -132.29
REMARK 500 5 LYS A 26 57.42 -98.31
REMARK 500 5 ASN A 28 -9.47 -55.93
REMARK 500 5 ILE A 29 153.67 -44.79
REMARK 500 5 THR A 37 42.69 -144.21
REMARK 500 5 ASP A 45 -101.45 -21.12
REMARK 500
REMARK 500 THIS ENTRY HAS 128 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 2 PHE A 73 0.10 SIDE CHAIN
REMARK 500 7 TYR A 87 0.10 SIDE CHAIN
REMARK 500 8 PHE A 73 0.07 SIDE CHAIN
REMARK 500 11 PHE A 73 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHORYLATION SITE CYS 35.
DBREF 1IBA A 5 90 UNP P69786 PTGCB_ECOLI 391 476
SEQRES 1 A 101 MET PHE LYS ASN GLU ASP ALA LYS ALA THR GLY THR SER
SEQRES 2 A 101 GLU MET ALA PRO ALA LEU VAL ALA ALA PHE GLY GLY LYS
SEQRES 3 A 101 GLU ASN ILE THR ASN LEU ASP ALA CYS ILE THR ARG LEU
SEQRES 4 A 101 ARG VAL SER VAL ALA ASP VAL SER LYS VAL ASP GLN ALA
SEQRES 5 A 101 GLY LEU LYS LYS LEU GLY ALA ALA GLY VAL VAL VAL ALA
SEQRES 6 A 101 GLY SER GLY VAL GLN ALA ILE PHE GLY THR LYS SER ASP
SEQRES 7 A 101 ASN LEU LYS THR GLU MET ASP GLU TYR ILE ARG ASN PHE
SEQRES 8 A 101 GLY SER ARG SER HIS HIS HIS HIS HIS HIS
HELIX 1 H1 ALA A 18 PHE A 23 1 6
HELIX 2 H2 ALA A 52 LEU A 57 1 6
HELIX 3 H3 LYS A 76 ASN A 90 1 15
SHEET 1 B1 4 THR A 30 CYS A 35 0
SHEET 2 B1 4 ARG A 38 VAL A 43 -1 O SER A 42 N ASN A 31
SHEET 3 B1 4 GLY A 68 PHE A 73 -1 O VAL A 69 N VAL A 41
SHEET 4 B1 4 GLY A 61 ALA A 65 -1 O VAL A 63 N GLN A 70
SITE 1 S1 1 CYS A 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
MODEL 1
Complete list - v 29 2 Bytes