Header list of 1sa8.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 07-FEB-04 1SA8
TITLE THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-BETA-SHEET VARIANT OF
TITLE 2 INTESTINAL FATTY ACID-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, INTESTINAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: D27-GG;
COMPND 5 SYNONYM: I-FABP, FABPI;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: FABP2;
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_CELL: SMALL INTESTINAL ENTEROCYTE;
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMON5840-IFABP(DELTA17SG)
KEYWDS INTESTINAL FATTY ACID-BINDING PROTEIN, PROTEIN STABILITY, PROTEIN
KEYWDS 2 STRUCTURE, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.OGBAY,G.T.DEKOSTER,D.P.CISTOLA
REVDAT 3 02-MAR-22 1SA8 1 REMARK
REVDAT 2 24-FEB-09 1SA8 1 VERSN
REVDAT 1 08-JUN-04 1SA8 0
JRNL AUTH B.OGBAY,G.T.DEKOSTER,D.P.CISTOLA
JRNL TITL THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-BETA-SHEET
JRNL TITL 2 VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN.
JRNL REF PROTEIN SCI. V. 13 1227 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15096629
JRNL DOI 10.1110/PS.03546204
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : NILGES, M. AND O'DONOGHUE, S. (1998) PROG. NMR
REMARK 3 SPECTROSCOPY 32, 107-139.2. LINGE, J. AND NILGES,
REMARK 3 M. (1999) JOURNAL OF BIOMOLECULAR NMR 13, 51-59.
REMARK 3 (CNS), NILGES, M. AND O'DONOGHUE, S. (1998) PROG.
REMARK 3 NMR SPECTROSCOPY 32, 107-139.2. LINGE, J. AND
REMARK 3 NILGES, M. (1999) JOURNAL OF BIOMOLECULAR NMR 13,
REMARK 3 51-59. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2173 DISTANCE CONSTRAINTS AND 176 CSI-DERIVED DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1SA8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021561.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 20 MM POTASSIUM PHOSPHATE, 135
REMARK 210 MM KCL, 10 MM NACL, 0.5% NAN3
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 1.8 MM PROTEIN, 20 MM POTASSIUM
REMARK 210 PHOSPHATE, 135 MM KCL, 10 MM
REMARK 210 NACL, 0.5% NAN3,95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C-EDITED NOESY-HSQC; 15N
REMARK 210 -EDITED NOESY-HSQC; 3D 15N-15N
REMARK 210 EDITED NOESY; AROMATIC13C-NOESY-
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2001, VNMR 6.1
REMARK 210 METHOD USED : ARIA1.1.2/CNS1.1
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 HZ3 LYS A 7 OE1 GLU A 26 1.56
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 ASP A 3 81.22 -60.34
REMARK 500 1 LYS A 21 103.84 -167.70
REMARK 500 1 ASN A 29 -72.22 67.23
REMARK 500 1 PHE A 30 47.66 -171.75
REMARK 500 1 ASP A 72 40.80 -79.38
REMARK 500 1 ASN A 73 -62.44 -171.38
REMARK 500 1 LYS A 75 21.39 43.02
REMARK 500 1 GLU A 76 104.30 -164.81
REMARK 500 1 GLU A 95 -69.40 66.77
REMARK 500 2 PHE A 2 -105.21 -74.44
REMARK 500 2 LYS A 21 103.20 -171.70
REMARK 500 2 ASN A 29 -68.79 65.02
REMARK 500 2 PHE A 30 56.68 -162.75
REMARK 500 2 ASN A 62 43.89 -108.44
REMARK 500 2 LYS A 75 -26.68 -168.29
REMARK 500 2 GLU A 87 141.48 -170.53
REMARK 500 2 GLU A 95 -62.77 65.60
REMARK 500 3 PHE A 2 -114.04 -88.74
REMARK 500 3 GLU A 18 -134.81 -85.44
REMARK 500 3 ASN A 20 96.67 -163.17
REMARK 500 3 LYS A 21 105.55 -169.89
REMARK 500 3 ASN A 29 -54.46 67.11
REMARK 500 3 PHE A 30 49.36 -158.03
REMARK 500 3 ASN A 62 40.32 -107.34
REMARK 500 3 ASN A 73 -39.15 -171.06
REMARK 500 3 LYS A 75 -43.59 73.84
REMARK 500 3 GLU A 87 148.92 -170.21
REMARK 500 3 GLU A 95 -62.83 67.91
REMARK 500 4 ASN A 20 97.52 -162.11
REMARK 500 4 LYS A 21 104.82 -169.55
REMARK 500 4 ASN A 29 -77.46 65.21
REMARK 500 4 PHE A 30 58.50 -171.71
REMARK 500 4 ASN A 62 41.12 -144.50
REMARK 500 4 LYS A 67 117.70 -166.05
REMARK 500 4 ASP A 72 36.56 -80.31
REMARK 500 4 ASN A 73 -43.13 -166.16
REMARK 500 4 LYS A 75 -28.12 -170.62
REMARK 500 5 PHE A 2 -105.39 -103.89
REMARK 500 5 LYS A 21 105.21 -169.80
REMARK 500 5 ASN A 29 -64.42 68.40
REMARK 500 5 PHE A 30 56.35 -170.70
REMARK 500 5 LYS A 67 116.49 -160.75
REMARK 500 5 LYS A 75 -30.61 -152.85
REMARK 500 5 GLU A 95 -72.06 64.32
REMARK 500 6 PHE A 2 -111.55 -73.06
REMARK 500 6 LYS A 21 106.53 -169.40
REMARK 500 6 ASN A 29 -72.09 163.56
REMARK 500 6 PHE A 30 -57.98 -125.92
REMARK 500 6 ARG A 31 99.92 -170.41
REMARK 500 6 ASN A 32 108.66 -170.84
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
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 GLY A 19 ASN A 20 8 -146.65
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 6 ASN A 29 -11.66
REMARK 500 7 GLY A 4 -11.93
REMARK 500 8 GLY A 19 14.66
REMARK 500 8 GLY A 85 10.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A57 RELATED DB: PDB
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF A HELIX-LESS VARIANT OF
REMARK 900 INTESTINAL FATTY ACID BINDING PROTEIN, NMR
REMARK 900 RELATED ID: 1AEL RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN
REMARK 900 RELATED ID: 1URE RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF INTESTINAL FATTY ACID-BINDING PROTEIN COMPLEXED
REMARK 900 WITH PALMITATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN IS A DELETION MUTANT WHERE 27 CONSECUTIVE
REMARK 999 RESIDUES WERE DELETED FOR WILD-TYPE INTESTINAL
REMARK 999 FATTY-ACID BINDING PROTEIN (I-FABP), AND REPLACED BY
REMARK 999 A GLY-GLY LINKER (GLY 9A - GLY 10A).
DBREF 1SA8 A 1 8 UNP P02693 FABPI_RAT 1 8
DBREF 1SA8 A 11 106 UNP P02693 FABPI_RAT 36 131
SEQADV 1SA8 GLY A 9 UNP P02693 SEE REMARK 999
SEQADV 1SA8 GLY A 10 UNP P02693 SEE REMARK 999
SEQRES 1 A 106 ALA PHE ASP GLY THR TRP LYS VAL GLY GLY LEU LYS LEU
SEQRES 2 A 106 THR ILE THR GLN GLU GLY ASN LYS PHE THR VAL LYS GLU
SEQRES 3 A 106 SER SER ASN PHE ARG ASN ILE ASP VAL VAL PHE GLU LEU
SEQRES 4 A 106 GLY VAL ASP PHE ALA TYR SER LEU ALA ASP GLY THR GLU
SEQRES 5 A 106 LEU THR GLY THR TRP THR MET GLU GLY ASN LYS LEU VAL
SEQRES 6 A 106 GLY LYS PHE LYS ARG VAL ASP ASN GLY LYS GLU LEU ILE
SEQRES 7 A 106 ALA VAL ARG GLU ILE SER GLY ASN GLU LEU ILE GLN THR
SEQRES 8 A 106 TYR THR TYR GLU GLY VAL GLU ALA LYS ARG ILE PHE LYS
SEQRES 9 A 106 LYS GLU
SHEET 1 A 4 GLY A 4 THR A 5 0
SHEET 2 A 4 LYS A 12 GLN A 17 -1 O ILE A 15 N GLY A 4
SHEET 3 A 4 PHE A 22 SER A 28 -1 O SER A 27 N LYS A 12
SHEET 4 A 4 ARG A 31 PHE A 37 -1 O PHE A 37 N PHE A 22
SHEET 1 B 4 VAL A 41 LEU A 47 0
SHEET 2 B 4 THR A 51 GLU A 60 -1 O THR A 51 N LEU A 47
SHEET 3 B 4 LYS A 63 ARG A 70 -1 O VAL A 65 N THR A 58
SHEET 4 B 4 ARG A 81 GLU A 82 -1 O ARG A 81 N LEU A 64
SHEET 1 C 3 LEU A 77 ALA A 79 0
SHEET 2 C 3 GLU A 87 TYR A 94 -1 O THR A 93 N ILE A 78
SHEET 3 C 3 VAL A 97 LYS A 104 -1 O ALA A 99 N TYR A 92
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 - r 2 2 Bytes