Header list of 1ael.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID BINDING PROTEIN 30-JUL-96 1AEL
TITLE NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IFABP, I-FABP;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: INTESTINAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 CELL: SMALL INTESTINAL ENTEROCYTE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511145;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: MG1655;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMON5840-I-FABP
KEYWDS FATTY ACID-BINDING PROTEIN, LIPID TRANSPORT, I-FABP, LIPID-BINDING
KEYWDS 2 PROTEIN, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.E.HODSDON,D.P.CISTOLA
REVDAT 3 16-FEB-22 1AEL 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1AEL 1 VERSN
REVDAT 1 01-APR-97 1AEL 0
JRNL AUTH M.E.HODSDON,D.P.CISTOLA
JRNL TITL LIGAND BINDING ALTERS THE BACKBONE MOBILITY OF INTESTINAL
JRNL TITL 2 FATTY ACID-BINDING PROTEIN AS MONITORED BY 15N NMR
JRNL TITL 3 RELAXATION AND 1H EXCHANGE.
JRNL REF BIOCHEMISTRY V. 36 2278 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9047330
JRNL DOI 10.1021/BI962018L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.HODSDON,J.W.PONDER,D.P.CISTOLA
REMARK 1 TITL THE NMR SOLUTION STRUCTURE OF INTESTINAL FATTY ACID-BINDING
REMARK 1 TITL 2 PROTEIN COMPLEXED WITH PALMITATE: APPLICATION OF A NOVEL
REMARK 1 TITL 3 DISTANCE GEOMETRY ALGORITHM
REMARK 1 REF J.MOL.BIOL. V. 264 585 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.BANASZAK,N.WINTER,Z.XU,D.A.BERNLOHR,S.COWAN,T.A.JONES
REMARK 1 TITL LIPID BINDING PROTEINS: A FAMILY OF FATTY ACID AND RETINOID
REMARK 1 TITL 2 TRANSPORT PROTEINS
REMARK 1 REF ADV.PROTEIN CHEM. V. 268 18399 1993
REMARK 1 REFN ISSN 0065-3233
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.C.SACCHETTINI,J.I.GORDON
REMARK 1 TITL RAT INTESTINAL FATTY ACID BINDING PROTEIN. A MODEL SYSTEM
REMARK 1 TITL 2 FOR ANALYZING THE FORCES THAT CAN BIND FATTY ACIDS TO
REMARK 1 TITL 3 PROTEINS
REMARK 1 REF J.BIOL.CHEM. V. 268 18399 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.SCAPIN,J.I.GORDON,J.C.SACCHETTINI
REMARK 1 TITL REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL
REMARK 1 TITL 2 FATTY ACID-BINDING APOPROTEIN AT 1.2-A RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 267 4253 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TINKER
REMARK 3 AUTHORS : PONDER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AEL 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_1000170720.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2-D 1H-HOMONUCLEAR NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TINKER
REMARK 210 METHOD USED : SIMULATED ANNEALING REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 21
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : FINAL PENALTY FUNCTION VALUES
REMARK 210 LESS THAN 10.0
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: LIMITS ON SECONDARY STRUCTURE ELEMENTS WERE DEFINED BY THE
REMARK 210 PROTON-CARBON CONSENSUS CHEMICAL SHIFT INDEX.
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
DBREF 1AEL A 1 131 UNP P02693 FABPI_RAT 1 131
SEQRES 1 A 131 ALA PHE ASP GLY THR TRP LYS VAL ASP ARG ASN GLU ASN
SEQRES 2 A 131 TYR GLU LYS PHE MET GLU LYS MET GLY ILE ASN VAL VAL
SEQRES 3 A 131 LYS ARG LYS LEU GLY ALA HIS ASP ASN LEU LYS LEU THR
SEQRES 4 A 131 ILE THR GLN GLU GLY ASN LYS PHE THR VAL LYS GLU SER
SEQRES 5 A 131 SER ASN PHE ARG ASN ILE ASP VAL VAL PHE GLU LEU GLY
SEQRES 6 A 131 VAL ASP PHE ALA TYR SER LEU ALA ASP GLY THR GLU LEU
SEQRES 7 A 131 THR GLY THR TRP THR MET GLU GLY ASN LYS LEU VAL GLY
SEQRES 8 A 131 LYS PHE LYS ARG VAL ASP ASN GLY LYS GLU LEU ILE ALA
SEQRES 9 A 131 VAL ARG GLU ILE SER GLY ASN GLU LEU ILE GLN THR TYR
SEQRES 10 A 131 THR TYR GLU GLY VAL GLU ALA LYS ARG ILE PHE LYS LYS
SEQRES 11 A 131 GLU
HELIX 1 A1 GLU A 15 MET A 21 1 7
HELIX 2 A2 VAL A 25 ARG A 28 1 4
SHEET 1 A 6 GLY A 4 GLU A 12 0
SHEET 2 A 6 LYS A 37 GLU A 43 -1 N ILE A 40 O GLY A 4
SHEET 3 A 6 LYS A 46 SER A 53 -1 N THR A 48 O THR A 41
SHEET 4 A 6 ASN A 57 GLU A 63 -1 N VAL A 60 O VAL A 49
SHEET 5 A 6 VAL A 66 SER A 71 -1
SHEET 6 A 6 LEU A 78 GLY A 80 -1 N LEU A 78 O TYR A 70
SHEET 1 B 5 THR A 81 GLU A 85 0
SHEET 2 B 5 LYS A 88 PHE A 93 -1 N VAL A 90 O THR A 83
SHEET 3 B 5 GLU A 101 SER A 109 -1 N ALA A 104 O GLY A 91
SHEET 4 B 5 GLU A 112 TYR A 119 -1 N THR A 116 O VAL A 105
SHEET 5 B 5 VAL A 122 LYS A 129 -1 N ARG A 126 O GLN A 115
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