Header list of 3ifb.pdb file
Complete list - v 29 2 Bytes
HEADER LIPID BINDING PROTEIN 16-OCT-98 3IFB
TITLE NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTESTINAL FATTY ACID BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: I-FABP;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PH 6.5, 310K, HOLO PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21 (DE3);
SOURCE 6 ORGAN: INTESTINE;
SOURCE 7 TISSUE: PROXIMAL SMALL INTESTINE;
SOURCE 8 CELL: EPITHELIAL CELLS;
SOURCE 9 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 GENE: FABP2;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 14 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS FATTY ACID BINDING PROTEIN, INTRACELLULAR LIPID BINDING PROTEIN,
KEYWDS 2 FATTY ACID BINDING, SINGLE BASE POLYMORPHISM, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR F.ZHANG,C.LUECKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON
REVDAT 5 29-NOV-17 3IFB 1 REMARK HELIX
REVDAT 4 24-FEB-09 3IFB 1 VERSN
REVDAT 3 01-APR-03 3IFB 1 JRNL
REVDAT 2 22-DEC-99 3IFB 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 21-OCT-98 3IFB 0
JRNL AUTH F.ZHANG,C.LUCKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON
JRNL TITL SOLUTION STRUCTURE OF HUMAN INTESTINAL FATTY ACID BINDING
JRNL TITL 2 PROTEIN: IMPLICATIONS FOR LIGAND ENTRY AND EXIT.
JRNL REF J.BIOMOL.NMR V. 9 213 1997
JRNL REFN ISSN 0925-2738
JRNL PMID 9204553
JRNL DOI 10.1023/A:1018666522787
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.J.BAIER,C.BOGARDUS,J.C.SACCHETTINI
REMARK 1 TITL A POLYMORPHISM IN THE HUMAN INTESTINAL FATTY ACID BINDING
REMARK 1 TITL 2 PROTEIN ALTERS FATTY ACID TRANSPORT ACROSS CACO-2 CELLS
REMARK 1 REF J.BIOL.CHEM. V. 271 10892 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.J.BAIER,J.C.SACCHETTINI,W.C.KNOWLER,J.EADS,G.PAOLISSO,
REMARK 1 AUTH 2 P.A.TATARANNI,H.MOCHIZUKI,P.H.BENNET,C.BOGARDUS,M.PROCHAZKA
REMARK 1 TITL AN AMINO ACID SUBSTITUTION IN THE HUMAN INTESTINAL FATTY
REMARK 1 TITL 2 ACID BINDING PROTEIN IS ASSOCIATED WITH INCREASED FATTY ACID
REMARK 1 TITL 3 BINDING, INCREASED FAT OXIDATION, AND INSULIN RESISTANCE
REMARK 1 REF J.CLIN.INVEST. V. 95 1281 1995
REMARK 1 REFN ISSN 0021-9738
REMARK 1 REFERENCE 3
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-ANGSTROMS 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 : SYBYL 6.2
REMARK 3 AUTHORS : TRIPOS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMULATED ANNEALING AND
REMARK 3 ENERGY MINIMIZATION
REMARK 4
REMARK 4 3IFB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008055.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC
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 : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: SET OF 10 ENERGY-MINIMIZED NMR STRUCTURES 20MM PHOSPHATE
REMARK 210 BUFFER
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
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 1 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 2 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 3 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 4 ASP A 131 C ASP A 131 OXT 0.152
REMARK 500 5 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 6 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 7 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 8 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 9 ASP A 131 C ASP A 131 OXT 0.151
REMARK 500 10 ASP A 131 C ASP A 131 OXT 0.151
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 TRP A 6 CB - CG - CD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 1 TRP A 6 CB - CG - CD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 1 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 HIS A 33 CG - CD2 - NE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 1 LEU A 64 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 126 CB - CA - C ANGL. DEV. = 19.9 DEGREES
REMARK 500 1 ARG A 126 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 2 TRP A 6 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 TRP A 6 CB - CG - CD2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 3 TRP A 6 CB - CG - CD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 3 TRP A 6 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ALA A 31 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 3 LEU A 38 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 4 TRP A 6 CB - CG - CD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 4 LEU A 38 CB - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 4 LEU A 38 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 4 LEU A 78 N - CA - CB ANGL. DEV. = 14.1 DEGREES
REMARK 500 4 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 LEU A 84 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 4 LEU A 84 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 4 LEU A 84 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 4 ARG A 106 N - CA - CB ANGL. DEV. = 13.7 DEGREES
REMARK 500 4 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 4 ARG A 126 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 4 ARG A 126 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 5 TRP A 6 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 5 TRP A 6 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 5 SER A 52 N - CA - CB ANGL. DEV. = -9.9 DEGREES
REMARK 500 5 LEU A 78 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 5 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 6 TRP A 6 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 LEU A 36 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500 6 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 LEU A 84 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 6 LEU A 89 CB - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 6 PHE A 93 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 6 PHE A 93 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 6 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 ARG A 106 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 6 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 85 ANGLE DEVIATIONS.
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 9 -64.85 -104.66
REMARK 500 1 ASN A 13 44.00 33.93
REMARK 500 1 VAL A 23 -153.53 -83.56
REMARK 500 1 ALA A 32 -47.15 -23.69
REMARK 500 1 ASN A 35 178.56 79.16
REMARK 500 1 THR A 41 92.16 -160.12
REMARK 500 1 ARG A 56 147.79 -173.23
REMARK 500 1 LEU A 64 113.53 149.38
REMARK 500 1 ASP A 97 -68.23 -140.85
REMARK 500 1 GLU A 120 6.08 48.36
REMARK 500 2 ASP A 3 82.34 61.39
REMARK 500 2 VAL A 8 151.19 -36.92
REMARK 500 2 ASP A 9 -62.12 -132.63
REMARK 500 2 ASN A 13 38.73 37.70
REMARK 500 2 ASN A 35 71.91 67.96
REMARK 500 2 GLU A 63 -72.93 -121.70
REMARK 500 2 TYR A 70 114.80 -160.09
REMARK 500 2 GLU A 107 134.75 -172.01
REMARK 500 2 LYS A 130 151.05 -48.52
REMARK 500 3 PHE A 2 -92.03 -96.01
REMARK 500 3 ASN A 13 41.33 22.34
REMARK 500 3 GLU A 19 -37.08 -35.97
REMARK 500 3 VAL A 23 133.93 -30.60
REMARK 500 3 HIS A 33 52.93 -117.00
REMARK 500 3 ASP A 34 -64.48 -108.88
REMARK 500 3 ASN A 35 81.63 77.58
REMARK 500 3 ARG A 56 148.09 -174.59
REMARK 500 3 GLU A 63 71.62 -158.22
REMARK 500 3 LYS A 88 160.41 63.51
REMARK 500 3 ASN A 98 -40.09 177.53
REMARK 500 3 ASN A 100 76.61 -105.12
REMARK 500 3 GLU A 101 154.15 -15.11
REMARK 500 3 GLU A 120 -5.61 -57.99
REMARK 500 3 LYS A 130 81.06 -63.79
REMARK 500 4 PHE A 2 51.09 -143.89
REMARK 500 4 SER A 4 118.07 -176.97
REMARK 500 4 VAL A 23 -149.99 -78.02
REMARK 500 4 ASN A 35 -67.02 -1.86
REMARK 500 4 LEU A 36 98.82 -172.93
REMARK 500 4 THR A 41 83.74 -150.89
REMARK 500 4 GLU A 43 -158.83 -150.63
REMARK 500 4 LEU A 64 91.56 62.93
REMARK 500 4 ASN A 69 119.08 -160.34
REMARK 500 4 ARG A 79 -165.21 -105.81
REMARK 500 4 ASN A 98 -56.76 -169.67
REMARK 500 4 GLU A 107 94.19 -174.49
REMARK 500 4 GLU A 120 18.34 37.63
REMARK 500 4 LYS A 130 160.72 -44.00
REMARK 500 5 PHE A 2 171.07 58.30
REMARK 500 5 ASP A 3 114.38 58.82
REMARK 500
REMARK 500 THIS ENTRY HAS 134 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 LEU A 38 THR A 39 1 138.43
REMARK 500 LYS A 130 ASP A 131 1 -148.69
REMARK 500 LYS A 88 LEU A 89 3 -139.77
REMARK 500 ARG A 106 GLU A 107 4 -144.85
REMARK 500 ASN A 35 LEU A 36 5 -139.46
REMARK 500 GLY A 22 VAL A 23 6 -148.82
REMARK 500 GLY A 22 VAL A 23 8 -147.92
REMARK 500 ASN A 100 GLU A 101 8 129.56
REMARK 500 LYS A 130 ASP A 131 8 147.38
REMARK 500 GLY A 22 VAL A 23 9 -149.10
REMARK 500 ASN A 100 GLU A 101 9 -143.22
REMARK 500 LYS A 130 ASP A 131 9 140.50
REMARK 500 GLY A 22 VAL A 23 10 123.12
REMARK 500 LYS A 130 ASP A 131 10 -145.88
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 PHE A 47 0.10 SIDE CHAIN
REMARK 500 1 PHE A 62 0.08 SIDE CHAIN
REMARK 500 1 PHE A 93 0.09 SIDE CHAIN
REMARK 500 1 PHE A 128 0.09 SIDE CHAIN
REMARK 500 2 PHE A 93 0.10 SIDE CHAIN
REMARK 500 2 TYR A 119 0.07 SIDE CHAIN
REMARK 500 3 TYR A 14 0.09 SIDE CHAIN
REMARK 500 3 PHE A 17 0.12 SIDE CHAIN
REMARK 500 3 PHE A 93 0.09 SIDE CHAIN
REMARK 500 3 TYR A 119 0.07 SIDE CHAIN
REMARK 500 3 PHE A 128 0.09 SIDE CHAIN
REMARK 500 4 TYR A 14 0.08 SIDE CHAIN
REMARK 500 4 PHE A 68 0.08 SIDE CHAIN
REMARK 500 4 TYR A 70 0.12 SIDE CHAIN
REMARK 500 4 PHE A 93 0.14 SIDE CHAIN
REMARK 500 4 TYR A 117 0.12 SIDE CHAIN
REMARK 500 5 TYR A 14 0.18 SIDE CHAIN
REMARK 500 5 PHE A 17 0.12 SIDE CHAIN
REMARK 500 5 ARG A 28 0.08 SIDE CHAIN
REMARK 500 5 TYR A 70 0.07 SIDE CHAIN
REMARK 500 5 PHE A 93 0.07 SIDE CHAIN
REMARK 500 5 TYR A 117 0.13 SIDE CHAIN
REMARK 500 5 TYR A 119 0.12 SIDE CHAIN
REMARK 500 6 PHE A 55 0.10 SIDE CHAIN
REMARK 500 6 TYR A 70 0.08 SIDE CHAIN
REMARK 500 6 PHE A 93 0.07 SIDE CHAIN
REMARK 500 6 TYR A 119 0.09 SIDE CHAIN
REMARK 500 7 PHE A 55 0.09 SIDE CHAIN
REMARK 500 7 TYR A 117 0.09 SIDE CHAIN
REMARK 500 8 TYR A 14 0.11 SIDE CHAIN
REMARK 500 8 PHE A 47 0.14 SIDE CHAIN
REMARK 500 8 PHE A 55 0.08 SIDE CHAIN
REMARK 500 8 PHE A 128 0.15 SIDE CHAIN
REMARK 500 9 TYR A 14 0.17 SIDE CHAIN
REMARK 500 9 PHE A 47 0.10 SIDE CHAIN
REMARK 500 10 PHE A 17 0.10 SIDE CHAIN
REMARK 500 10 PHE A 68 0.10 SIDE CHAIN
REMARK 500 10 PHE A 93 0.08 SIDE CHAIN
REMARK 500 10 TYR A 119 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3IFB A 1 131 UNP P12104 FABPI_HUMAN 2 132
SEQRES 1 A 131 ALA PHE ASP SER THR TRP LYS VAL ASP ARG SER GLU ASN
SEQRES 2 A 131 TYR ASP LYS PHE MET GLU LYS MET GLY VAL ASN ILE VAL
SEQRES 3 A 131 LYS ARG LYS LEU ALA 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 ALA PHE ARG ASN ILE GLU VAL VAL PHE GLU LEU GLY
SEQRES 6 A 131 VAL THR PHE ASN TYR ASN LEU ALA ASP GLY THR GLU LEU
SEQRES 7 A 131 ARG GLY THR TRP SER LEU GLU GLY ASN LYS LEU ILE GLY
SEQRES 8 A 131 LYS PHE LYS ARG THR ASP ASN GLY ASN GLU LEU ASN THR
SEQRES 9 A 131 VAL ARG GLU ILE ILE GLY ASP GLU LEU VAL GLN THR TYR
SEQRES 10 A 131 VAL TYR GLU GLY VAL GLU ALA LYS ARG ILE PHE LYS LYS
SEQRES 11 A 131 ASP
HELIX 1 1 TYR A 14 GLY A 22 1 9
HELIX 2 2 ILE A 25 HIS A 33 1 9
SHEET 1 A 4 PHE A 2 GLU A 12 0
SHEET 2 A 4 LEU A 36 GLU A 43 -1 N LEU A 38 O TRP A 6
SHEET 3 A 4 LYS A 46 SER A 53 -1 N LYS A 50 O THR A 39
SHEET 4 A 4 ARG A 56 GLU A 63 -1 N VAL A 60 O VAL A 49
SHEET 1 B 6 VAL A 66 LEU A 72 0
SHEET 2 B 6 THR A 76 GLU A 85 -1 N LEU A 78 O TYR A 70
SHEET 3 B 6 LYS A 88 ARG A 95 -1 N LYS A 92 O THR A 81
SHEET 4 B 6 ASN A 100 ILE A 109 -1 N THR A 104 O GLY A 91
SHEET 5 B 6 GLU A 112 TYR A 119 -1 N THR A 116 O VAL A 105
SHEET 6 B 6 VAL A 122 LYS A 130 -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 - v 29 2 Bytes