Header list of 1eal.pdb file
Complete list - 16 20 Bytes
HEADER FATTY ACID BINDING PROTEIN 28-AUG-96 1EAL
TITLE NMR STUDY OF ILEAL LIPID BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ILEAL LIPID BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GASTROTROPIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PH 5.0, 310K, APO FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: INTESTINE;
SOURCE 7 TISSUE: ILEAL EPITHELIUM;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS INTRACELLULAR LIPID BINDING PROTEIN, BILE ACID BINDING, ILEAL
KEYWDS 2 EPITHELIUM, FATTY ACID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR C.LUECKE,F.ZHANG,H.RUETERJANS,J.A.HAMILTON,J.C.SACCHETTINI
REVDAT 4 16-FEB-22 1EAL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EAL 1 VERSN
REVDAT 2 01-APR-03 1EAL 1 JRNL
REVDAT 1 22-JAN-97 1EAL 0
JRNL AUTH C.LUCKE,F.ZHANG,H.RUTERJANS,J.A.HAMILTON,J.C.SACCHETTINI
JRNL TITL FLEXIBILITY IS A LIKELY DETERMINANT OF BINDING SPECIFICITY
JRNL TITL 2 IN THE CASE OF ILEAL LIPID BINDING PROTEIN.
JRNL REF STRUCTURE V. 4 785 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8805562
JRNL DOI 10.1016/S0969-2126(96)00086-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LASSEN,C.LUCKE,M.KVEDER,A.MESGARZADEH,J.M.SCHMIDT,
REMARK 1 AUTH 2 B.SPECHT,A.LEZIUS,F.SPENER,H.RUTERJANS
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF BOVINE HEART
REMARK 1 TITL 2 FATTY-ACID-BINDING PROTEIN WITH BOUND PALMITIC ACID,
REMARK 1 TITL 3 DETERMINED BY MULTIDIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF EUR.J.BIOCHEM. V. 230 266 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.C.SACCHETTINI,S.M.HAUFT,S.L.VAN CAMP,D.P.CISTOLA,
REMARK 1 AUTH 2 J.I.GORDON
REMARK 1 TITL DEVELOPMENTAL AND STRUCTURAL STUDIES OF AN INTRACELLULAR
REMARK 1 TITL 2 LIPID BINDING PROTEIN EXPRESSED IN THE ILEAL EPITHELIUM
REMARK 1 REF J.BIOL.CHEM. V. 265 19199 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SYBYL 5.2
REMARK 3 AUTHORS : TRIPOS ASSOCIATES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EAL 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_1000172986.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, SYBYL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST VIOLATION OF EXPERIMENTAL
REMARK 210 DISTANCE CONSTRAINTS
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 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 4 HIS A 98 CE1 HIS A 98 NE2 -0.067
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 2 ALA A 127 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 3 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.0 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 PHE A 2 -86.58 -85.23
REMARK 500 1 ASN A 13 61.41 110.83
REMARK 500 1 ALA A 22 67.47 100.17
REMARK 500 1 ARG A 32 -49.76 -22.61
REMARK 500 1 ASN A 33 48.54 -155.94
REMARK 500 1 ASP A 43 -112.83 -100.29
REMARK 500 1 LYS A 67 -126.15 55.34
REMARK 500 1 THR A 73 -71.20 -68.77
REMARK 500 1 ASN A 96 52.70 -145.85
REMARK 500 1 TYR A 97 71.11 -171.01
REMARK 500 1 LEU A 126 51.29 -155.94
REMARK 500 2 ALA A 22 59.91 92.05
REMARK 500 2 PRO A 24 -76.37 -61.07
REMARK 500 2 SER A 25 -59.39 -161.60
REMARK 500 2 ASP A 43 -138.72 -141.39
REMARK 500 2 GLN A 45 34.84 38.83
REMARK 500 2 THR A 73 -62.68 -130.75
REMARK 500 2 ILE A 74 -46.57 173.82
REMARK 500 2 LYS A 78 108.15 -167.15
REMARK 500 2 ASN A 93 66.63 -153.05
REMARK 500 2 ASP A 105 -88.74 52.73
REMARK 500 3 THR A 3 68.42 39.63
REMARK 500 3 SER A 10 71.95 -176.14
REMARK 500 3 ALA A 22 -92.86 108.87
REMARK 500 3 LEU A 23 156.73 59.32
REMARK 500 3 ASN A 33 -51.85 82.16
REMARK 500 3 SER A 58 93.78 -170.11
REMARK 500 3 THR A 73 -175.26 56.98
REMARK 500 3 ILE A 74 -78.51 65.14
REMARK 500 3 GLU A 86 55.79 -154.72
REMARK 500 3 TYR A 97 62.82 -176.06
REMARK 500 3 ASP A 105 47.19 37.04
REMARK 500 3 VAL A 114 51.40 -147.00
REMARK 500 4 THR A 3 73.02 46.02
REMARK 500 4 ALA A 22 57.31 76.06
REMARK 500 4 PRO A 54 89.35 -36.44
REMARK 500 4 HIS A 57 79.72 -104.73
REMARK 500 4 GLU A 68 84.50 121.20
REMARK 500 4 ILE A 74 87.69 44.92
REMARK 500 4 THR A 82 81.90 -67.19
REMARK 500 4 ASN A 96 54.98 -147.39
REMARK 500 4 TYR A 97 67.15 167.08
REMARK 500 4 VAL A 114 56.98 -148.02
REMARK 500 5 PHE A 2 -72.03 74.61
REMARK 500 5 THR A 3 132.46 -35.26
REMARK 500 5 GLU A 11 138.85 -175.96
REMARK 500 5 LYS A 12 51.01 -140.33
REMARK 500 5 ASN A 13 35.68 -152.34
REMARK 500 5 ILE A 59 64.39 -115.46
REMARK 500 5 LYS A 77 155.11 54.08
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 1 TYR A 14 0.07 SIDE CHAIN
REMARK 500 1 TYR A 119 0.12 SIDE CHAIN
REMARK 500 2 TYR A 53 0.11 SIDE CHAIN
REMARK 500 3 TYR A 14 0.12 SIDE CHAIN
REMARK 500 4 TYR A 14 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EAL A 1 127 UNP P10289 ILBP_PIG 1 127
SEQADV 1EAL SER A 118 UNP P10289 THR 118 CONFLICT
SEQRES 1 A 127 ALA PHE THR GLY LYS TYR GLU ILE GLU SER GLU LYS ASN
SEQRES 2 A 127 TYR ASP GLU PHE MET LYS ARG LEU ALA LEU PRO SER ASP
SEQRES 3 A 127 ALA ILE ASP LYS ALA ARG ASN LEU LYS ILE ILE SER GLU
SEQRES 4 A 127 VAL LYS GLN ASP GLY GLN ASN PHE THR TRP SER GLN GLN
SEQRES 5 A 127 TYR PRO GLY GLY HIS SER ILE THR ASN THR PHE THR ILE
SEQRES 6 A 127 GLY LYS GLU CYS ASP ILE GLU THR ILE GLY GLY LYS LYS
SEQRES 7 A 127 PHE LYS ALA THR VAL GLN MET GLU GLY GLY LYS VAL VAL
SEQRES 8 A 127 VAL ASN SER PRO ASN TYR HIS HIS THR ALA GLU ILE VAL
SEQRES 9 A 127 ASP GLY LYS LEU VAL GLU VAL SER THR VAL GLY GLY VAL
SEQRES 10 A 127 SER TYR GLU ARG VAL SER LYS LYS LEU ALA
HELIX 1 1 ASN A 13 LEU A 21 1 9
HELIX 2 2 SER A 25 ARG A 32 1 8
SHEET 1 A 8 SER A 58 THR A 64 0
SHEET 2 A 8 PHE A 47 GLN A 52 -1 N GLN A 51 O ILE A 59
SHEET 3 A 8 ILE A 37 GLN A 42 -1 N LYS A 41 O THR A 48
SHEET 4 A 8 GLY A 4 LYS A 12 -1 N TYR A 6 O SER A 38
SHEET 5 A 8 SER A 118 LYS A 125 -1 N LYS A 124 O GLU A 7
SHEET 6 A 8 LEU A 108 THR A 113 -1 N GLU A 110 O ARG A 121
SHEET 7 A 8 HIS A 98 ILE A 103 -1 N GLU A 102 O VAL A 109
SHEET 8 A 8 VAL A 90 ASN A 93 -1 N VAL A 92 O HIS A 99
SHEET 1 B 2 CYS A 69 GLU A 72 0
SHEET 2 B 2 LYS A 78 MET A 85 -1 N ALA A 81 O CYS A 69
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 - 16 20 Bytes