Header list of 1t8v.pdb file
Complete list - t 27 2 Bytes
HEADER LIPID BINDING PROTEIN 13-MAY-04 1T8V
TITLE THE NMR STRUCTURE OF D34A I-FABP: IMPLICATIONS FOR THE DETERMINANTS OF
TITLE 2 LIGAND BINDING STOICHIOMETRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, INTESTINAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: I-FABP, D34A I-FABP, FABPI;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FATTY ACID, STOICHIOMETRY, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.OGBAY,D.P.CISTOLA
REVDAT 3 27-OCT-21 1T8V 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1T8V 1 VERSN
REVDAT 1 04-OCT-05 1T8V 0
JRNL AUTH B.OGBAY,D.P.CISTOLA
JRNL TITL THE NMR STRUCTURE OF D34A I-FABP: IMPLICATIONS FOR THE
JRNL TITL 2 DETERMINANTS OF LIGAND BINDING STOICHIOMETRY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.P.CISTOLA,B.OGBAY,G.T.DEKOSTER
REMARK 1 TITL THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-B-SHEET
REMARK 1 TITL 2 VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN
REMARK 1 REF PROTEIN SCI. V. 13 1227 2004
REMARK 1 REFN ISSN 0961-8368
REMARK 1 DOI 10.1110/PS.03546204
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, ARIA 1.2
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), LINGE, O'DONOGHUE,
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3471 NOE-DERIVED RESTRAINTS AND 80 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1T8V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022457.
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 : 50MM KCL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 20 MM POTASSIUM PHOSPHATE, 50 MM
REMARK 210 KCL, 0.5% NAN3, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C_
REMARK 210 AROMATIC_NOESY; 3D_15N-15N_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2001, CNS 1.1, ARIA 1.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 HG13 VAL A 105 H THR A 116 1.17
REMARK 500 HD22 ASN A 11 HD2 LYS A 16 1.23
REMARK 500 HB VAL A 61 HZ PHE A 68 1.30
REMARK 500 HG2 LYS A 46 HG23 THR A 48 1.32
REMARK 500 HB2 LYS A 16 HD1 PHE A 17 1.32
REMARK 500 HG2 ARG A 10 HH21 ARG A 126 1.33
REMARK 500 H TYR A 14 HA3 GLY A 31 1.34
REMARK 500 H LEU A 89 HB2 ARG A 106 1.35
REMARK 500 H LEU A 78 HG23 VAL A 96 1.35
REMARK 500 OE1 GLU A 107 HZ3 LYS A 129 1.48
REMARK 500 O GLU A 15 H GLU A 19 1.52
REMARK 500 HZ1 LYS A 50 OD1 ASP A 59 1.55
REMARK 500 O TYR A 119 H GLY A 121 1.56
REMARK 500 HB THR A 39 O VAL A 49 1.58
REMARK 500 OE1 GLU A 77 HH12 ARG A 95 1.59
REMARK 500
REMARK 500 REMARK: NULL
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 6 GLY A 80 N GLY A 80 CA -0.092
REMARK 500 7 GLY A 80 N GLY A 80 CA -0.097
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 -50.56 -138.14
REMARK 500 1 VAL A 8 -60.99 -171.81
REMARK 500 1 ASP A 9 -166.94 -125.77
REMARK 500 1 ARG A 10 -173.14 -170.94
REMARK 500 1 LYS A 20 -43.92 -140.21
REMARK 500 1 ILE A 23 -71.46 65.38
REMARK 500 1 ASN A 24 -140.07 44.80
REMARK 500 1 ARG A 28 30.16 -87.46
REMARK 500 1 HIS A 33 39.41 169.57
REMARK 500 1 ALA A 34 139.61 -173.69
REMARK 500 1 ILE A 40 109.00 -164.27
REMARK 500 1 GLN A 42 -77.31 -175.99
REMARK 500 1 ASN A 45 82.15 -175.47
REMARK 500 1 PHE A 47 97.85 -163.45
REMARK 500 1 THR A 48 101.28 -168.32
REMARK 500 1 VAL A 49 103.98 -169.61
REMARK 500 1 LYS A 50 101.52 -168.05
REMARK 500 1 PHE A 55 -45.22 -146.68
REMARK 500 1 ILE A 58 126.18 -174.39
REMARK 500 1 VAL A 61 114.17 -168.41
REMARK 500 1 ALA A 73 51.71 -161.97
REMARK 500 1 ASP A 74 -140.43 -168.83
REMARK 500 1 THR A 76 117.02 -163.15
REMARK 500 1 GLU A 77 94.81 -163.82
REMARK 500 1 TRP A 82 105.43 -161.16
REMARK 500 1 ASN A 87 -25.99 165.22
REMARK 500 1 VAL A 90 101.97 -167.70
REMARK 500 1 ARG A 95 -174.38 -58.51
REMARK 500 1 ASN A 98 -67.14 -157.88
REMARK 500 1 LEU A 102 122.41 -172.35
REMARK 500 1 ILE A 103 121.82 -175.14
REMARK 500 1 ALA A 104 102.09 -169.35
REMARK 500 1 SER A 109 102.34 -169.27
REMARK 500 1 GLU A 112 131.48 -171.06
REMARK 500 1 TYR A 119 101.51 -171.90
REMARK 500 1 GLU A 120 -58.91 67.45
REMARK 500 1 VAL A 122 110.28 -163.43
REMARK 500 1 ARG A 126 111.30 -165.47
REMARK 500 1 LYS A 130 130.57 62.51
REMARK 500 2 ASP A 3 23.55 -165.32
REMARK 500 2 LYS A 7 114.87 -168.35
REMARK 500 2 VAL A 8 -63.61 -163.50
REMARK 500 2 LYS A 20 -47.20 -150.79
REMARK 500 2 MET A 21 -70.71 -47.39
REMARK 500 2 ILE A 23 -50.10 69.50
REMARK 500 2 ASN A 24 -141.09 44.56
REMARK 500 2 VAL A 26 -26.37 71.94
REMARK 500 2 LYS A 27 -92.69 47.78
REMARK 500 2 LYS A 29 95.25 -61.93
REMARK 500 2 ALA A 32 -96.09 -87.15
REMARK 500
REMARK 500 THIS ENTRY HAS 420 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 44 ASN A 45 1 149.38
REMARK 500 GLY A 80 THR A 81 1 148.80
REMARK 500 GLY A 80 THR A 81 2 147.16
REMARK 500 GLY A 44 ASN A 45 4 148.14
REMARK 500 GLY A 86 ASN A 87 5 148.62
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 ARG A 106 0.11 SIDE CHAIN
REMARK 500 2 ARG A 126 0.08 SIDE CHAIN
REMARK 500 3 ARG A 106 0.10 SIDE CHAIN
REMARK 500 5 ARG A 106 0.16 SIDE CHAIN
REMARK 500 6 ARG A 106 0.09 SIDE CHAIN
REMARK 500 9 ARG A 106 0.09 SIDE CHAIN
REMARK 500 10 ARG A 106 0.10 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 THR A 5 10.48
REMARK 500 1 TRP A 6 10.29
REMARK 500 1 VAL A 8 10.49
REMARK 500 1 GLU A 12 -11.81
REMARK 500 1 GLY A 44 -15.56
REMARK 500 1 GLY A 80 -16.39
REMARK 500 1 VAL A 105 -10.37
REMARK 500 1 GLY A 110 -12.86
REMARK 500 2 GLU A 12 -10.30
REMARK 500 2 GLY A 44 -15.40
REMARK 500 2 THR A 79 -10.66
REMARK 500 2 GLY A 80 -15.46
REMARK 500 2 VAL A 105 -10.29
REMARK 500 2 GLY A 110 -12.11
REMARK 500 3 VAL A 8 11.89
REMARK 500 3 GLU A 12 -10.81
REMARK 500 3 GLY A 44 -14.29
REMARK 500 3 LYS A 46 -10.20
REMARK 500 3 THR A 79 -11.89
REMARK 500 3 GLY A 80 -14.03
REMARK 500 3 VAL A 105 -10.59
REMARK 500 3 GLY A 110 -12.63
REMARK 500 3 ILE A 127 -10.34
REMARK 500 4 LYS A 7 -11.49
REMARK 500 4 VAL A 8 10.84
REMARK 500 4 GLU A 12 -10.09
REMARK 500 4 GLU A 19 10.28
REMARK 500 4 GLY A 44 -16.07
REMARK 500 4 THR A 79 -13.78
REMARK 500 4 MET A 84 -10.82
REMARK 500 4 GLY A 110 -13.47
REMARK 500 4 PHE A 128 13.42
REMARK 500 5 THR A 5 10.13
REMARK 500 5 TRP A 6 11.87
REMARK 500 5 GLU A 12 -12.81
REMARK 500 5 GLY A 44 -14.53
REMARK 500 5 LYS A 46 -13.55
REMARK 500 5 THR A 79 -13.00
REMARK 500 5 GLY A 86 -14.07
REMARK 500 5 ARG A 106 -10.60
REMARK 500 5 GLY A 110 -12.21
REMARK 500 5 LYS A 125 10.37
REMARK 500 5 PHE A 128 10.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AEL RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN
REMARK 900 RELATED ID: 1IFC RELATED DB: PDB
REMARK 900 INTESTINAL FATTY ACID BINDING PROTEIN
REMARK 900 RELATED ID: 1IFB RELATED DB: PDB
REMARK 900 INTESTINAL FATTY ACID BINDING PROTEIN (APO FORM 1) (I-FABP)
REMARK 900 RELATED ID: 2IFB RELATED DB: PDB
REMARK 900 INTESTINAL FATTY ACID BINDING PROTEIN (HOLO FORM) (I-FABP)
DBREF 1T8V A 1 131 UNP P02693 FABPI_RAT 1 131
SEQADV 1T8V ALA A 34 UNP P02693 ASP 34 ENGINEERED MUTATION
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 ALA 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 1 GLU A 15 MET A 21 1 7
SHEET 1 A 5 GLY A 4 GLU A 12 0
SHEET 2 A 5 LYS A 37 GLN A 42 -1 N LEU A 38 O TRP A 6
SHEET 3 A 5 LYS A 46 SER A 53 -1 N LYS A 50 O THR A 39
SHEET 4 A 5 ASN A 57 GLU A 63 -1 N VAL A 60 O VAL A 49
SHEET 5 A 5 VAL A 66 SER A 71 -1
SHEET 1 B 5 LEU A 78 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 - t 27 2 Bytes