Header list of 1jjj.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 06-JUL-01 1JJJ TITLE SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID TITLE 2 BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FABP5; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS BETA BARREL, FATTY ACID CARRIER, HOLO FORM, NMR SPECTROSCOPY, 15N KEYWDS 2 ISOTOPE ENRICHMENT, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.H.GUTIERREZ-GONZALEZ,C.LUDWIG,C.HOHOFF,M.RADEMACHER,T.HANHOFF, AUTHOR 2 H.RUETERJANS,F.SPENER,C.LUECKE REVDAT 5 23-FEB-22 1JJJ 1 REMARK REVDAT 4 24-FEB-09 1JJJ 1 VERSN REVDAT 3 12-AUG-03 1JJJ 1 DBREF REVDAT 2 03-JUL-02 1JJJ 1 AUTHOR REVDAT 1 19-JUN-02 1JJJ 0 JRNL AUTH L.H.GUTIERREZ-GONZALEZ,C.LUDWIG,C.HOHOFF,M.RADEMACHER, JRNL AUTH 2 T.HANHOFF,H.RUETERJANS,F.SPENER,C.LUECKE JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN JRNL TITL 2 EPIDERMAL-TYPE FATTY ACID-BINDING PROTEIN (E-FABP) JRNL REF BIOCHEM.J. V. 364 725 2002 JRNL REFN ISSN 0264-6021 JRNL PMID 12049637 JRNL DOI 10.1042/BJ20020039 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.HOHOFF,T.BOERCHERS,B.RUESTOW,F.SPENER,H.VAN TILBEURGH REMARK 1 TITL EXPRESSION, PURIFICATION, AND CRYSTAL STRUCTURE REMARK 1 TITL 2 DETERMINATION OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID REMARK 1 TITL 3 BINDING PROTEIN REMARK 1 REF BIOCHEMISTRY V. 38 12229 1999 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI990305U REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 97 REMARK 3 AUTHORS : MSI REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2008 NOE-DERIVED DISTANCE RESTRAINTS REMARK 4 REMARK 4 1JJJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-01. REMARK 100 THE DEPOSITION ID IS D_1000013846. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.00 REMARK 210 PH : 5.60 REMARK 210 IONIC STRENGTH : 20 MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5-2 MM E-FABP PHOSPHATE REMARK 210 BUFFER; 0.05% SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_TOCSY; 2D_NOESY; 2D_15N-HSQC; REMARK 210 2D_15N-HTQC; 3D_15N-TOCSY-HSQC; REMARK 210 3D_15N-NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 1.3, AURELIA 2.5.9, REMARK 210 DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS COMBINED REMARK 210 WITH SIMULATED ANNEALING REMARK 210 FOLLOWED BY ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 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 OE1 GLU A 75 HG1 THR A 83 1.47 REMARK 500 HG SER A 58 O LYS A 61 1.50 REMARK 500 HZ3 LYS A 55 OE2 GLU A 57 1.52 REMARK 500 HZ1 LYS A 110 OE1 GLU A 119 1.53 REMARK 500 OD2 ASP A 15 HZ3 LYS A 17 1.54 REMARK 500 HE2 HIS A 97 OE1 GLU A 104 1.56 REMARK 500 OD2 ASP A 113 HZ3 LYS A 115 1.57 REMARK 500 HH11 ARG A 12 OE2 GLU A 132 1.57 REMARK 500 HZ3 LYS A 112 OE2 GLU A 119 1.58 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 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 2 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 2 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES REMARK 500 2 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 2 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 3 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 3 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 3 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES REMARK 500 3 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 4 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 4 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 4 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 4 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 4 ARG A 81 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 4 TRP A 100 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 5 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 5 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 5 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 5 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 6 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 6 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES REMARK 500 6 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 6 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 6 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 6 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 6 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 7 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 7 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 7 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 7 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 7 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 7 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 7 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 7 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 8 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 134 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 SER A 16 59.30 -152.16 REMARK 500 1 LYS A 40 67.40 60.65 REMARK 500 1 THR A 59 49.24 -78.08 REMARK 500 1 LEU A 60 -61.50 179.72 REMARK 500 1 GLU A 71 160.82 179.48 REMARK 500 1 ASP A 91 70.80 25.40 REMARK 500 1 ASN A 123 -73.48 -143.67 REMARK 500 2 VAL A 14 -72.22 -110.73 REMARK 500 2 LYS A 40 77.05 -114.82 REMARK 500 2 ASP A 48 -116.72 -101.37 REMARK 500 2 THR A 59 49.80 -76.86 REMARK 500 2 LEU A 60 -52.01 -150.48 REMARK 500 2 ASP A 91 -82.96 66.90 REMARK 500 2 MET A 122 -76.73 -89.58 REMARK 500 2 ASN A 123 -62.93 -140.11 REMARK 500 3 VAL A 4 39.44 -77.88 REMARK 500 3 ASP A 91 -86.72 71.74 REMARK 500 3 LYS A 112 -113.75 -106.16 REMARK 500 3 MET A 122 -102.47 -102.81 REMARK 500 3 ASN A 124 -43.19 75.60 REMARK 500 4 VAL A 14 -55.51 -120.45 REMARK 500 4 LYS A 40 74.77 -109.42 REMARK 500 4 MET A 122 -79.42 -81.08 REMARK 500 4 ASN A 123 -60.73 -122.10 REMARK 500 5 VAL A 4 -48.71 63.31 REMARK 500 5 SER A 16 59.22 -144.47 REMARK 500 5 MET A 122 -60.12 -97.71 REMARK 500 5 ASN A 123 -92.99 -139.65 REMARK 500 6 VAL A 14 -60.01 -126.86 REMARK 500 6 ASP A 91 70.45 45.34 REMARK 500 6 LYS A 112 -126.72 -103.24 REMARK 500 6 MET A 122 -77.35 -98.25 REMARK 500 6 ASN A 123 -70.89 -123.48 REMARK 500 7 VAL A 4 -44.37 64.79 REMARK 500 7 SER A 16 84.38 -153.62 REMARK 500 7 LYS A 61 103.84 -161.34 REMARK 500 7 ASP A 91 -73.56 68.60 REMARK 500 7 LYS A 112 -130.92 -134.85 REMARK 500 7 MET A 122 -94.16 -118.24 REMARK 500 8 THR A 59 42.32 -75.78 REMARK 500 8 LEU A 60 -54.64 -152.91 REMARK 500 8 ASN A 123 -93.57 66.57 REMARK 500 9 SER A 16 65.56 -154.28 REMARK 500 9 LYS A 40 66.42 63.32 REMARK 500 9 ASP A 101 58.16 34.31 REMARK 500 9 MET A 122 -88.44 -98.21 REMARK 500 9 ASN A 124 -26.53 69.40 REMARK 500 10 VAL A 4 -58.86 -154.63 REMARK 500 10 VAL A 14 -73.32 -116.68 REMARK 500 10 SER A 16 51.96 -148.02 REMARK 500 REMARK 500 THIS ENTRY HAS 97 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 THR A 90 ASP A 91 9 148.72 REMARK 500 GLN A 84 THR A 85 15 -148.09 REMARK 500 VAL A 125 THR A 126 17 -144.56 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 33 0.15 SIDE CHAIN REMARK 500 1 ARG A 81 0.08 SIDE CHAIN REMARK 500 1 TYR A 131 0.07 SIDE CHAIN REMARK 500 2 ARG A 10 0.08 SIDE CHAIN REMARK 500 2 PHE A 73 0.10 SIDE CHAIN REMARK 500 2 ARG A 81 0.11 SIDE CHAIN REMARK 500 2 TYR A 131 0.09 SIDE CHAIN REMARK 500 4 ARG A 12 0.08 SIDE CHAIN REMARK 500 5 ARG A 12 0.10 SIDE CHAIN REMARK 500 5 ARG A 81 0.10 SIDE CHAIN REMARK 500 5 ARG A 129 0.07 SIDE CHAIN REMARK 500 7 TYR A 131 0.09 SIDE CHAIN REMARK 500 8 ARG A 81 0.09 SIDE CHAIN REMARK 500 8 TYR A 131 0.07 SIDE CHAIN REMARK 500 10 ARG A 10 0.07 SIDE CHAIN REMARK 500 10 ARG A 81 0.11 SIDE CHAIN REMARK 500 11 ARG A 81 0.10 SIDE CHAIN REMARK 500 11 TYR A 131 0.06 SIDE CHAIN REMARK 500 13 ARG A 10 0.08 SIDE CHAIN REMARK 500 13 ARG A 81 0.08 SIDE CHAIN REMARK 500 13 TYR A 131 0.06 SIDE CHAIN REMARK 500 14 ARG A 12 0.09 SIDE CHAIN REMARK 500 14 TYR A 22 0.07 SIDE CHAIN REMARK 500 14 TYR A 131 0.07 SIDE CHAIN REMARK 500 16 ARG A 81 0.12 SIDE CHAIN REMARK 500 16 TYR A 131 0.06 SIDE CHAIN REMARK 500 17 ARG A 12 0.08 SIDE CHAIN REMARK 500 17 ARG A 81 0.12 SIDE CHAIN REMARK 500 17 TYR A 131 0.06 SIDE CHAIN REMARK 500 19 ARG A 10 0.08 SIDE CHAIN REMARK 500 19 ARG A 81 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1B56 RELATED DB: PDB REMARK 900 X-RAY STRUCTURE DBREF 1JJJ A 1 135 UNP Q01469 FABPE_HUMAN 1 135 SEQRES 1 A 135 MET ALA THR VAL GLN GLN LEU GLU GLY ARG TRP ARG LEU SEQRES 2 A 135 VAL ASP SER LYS GLY PHE ASP GLU TYR MET LYS GLU LEU SEQRES 3 A 135 GLY VAL GLY ILE ALA LEU ARG LYS MET GLY ALA MET ALA SEQRES 4 A 135 LYS PRO ASP CYS ILE ILE THR CYS ASP GLY LYS ASN LEU SEQRES 5 A 135 THR ILE LYS THR GLU SER THR LEU LYS THR THR GLN PHE SEQRES 6 A 135 SER CYS THR LEU GLY GLU LYS PHE GLU GLU THR THR ALA SEQRES 7 A 135 ASP GLY ARG LYS THR GLN THR VAL CYS ASN PHE THR ASP SEQRES 8 A 135 GLY ALA LEU VAL GLN HIS GLN GLU TRP ASP GLY LYS GLU SEQRES 9 A 135 SER THR ILE THR ARG LYS LEU LYS ASP GLY LYS LEU VAL SEQRES 10 A 135 VAL GLU CYS VAL MET ASN ASN VAL THR CYS THR ARG ILE SEQRES 11 A 135 TYR GLU LYS VAL GLU HELIX 1 1 THR A 3 GLU A 8 5 6 HELIX 2 2 GLY A 18 GLY A 27 1 10 HELIX 3 3 GLY A 29 ALA A 39 1 11 SHEET 1 A10 THR A 62 THR A 68 0 SHEET 2 A10 ASN A 51 GLU A 57 -1 N THR A 56 O THR A 63 SHEET 3 A10 ASP A 42 CYS A 47 -1 N ILE A 44 O LYS A 55 SHEET 4 A10 GLY A 9 LYS A 17 -1 N TRP A 11 O CYS A 43 SHEET 5 A10 THR A 126 LYS A 133 -1 O GLU A 132 N ARG A 12 SHEET 6 A10 LYS A 115 VAL A 121 -1 N VAL A 118 O ARG A 129 SHEET 7 A10 LYS A 103 LYS A 112 -1 N LYS A 112 O LYS A 115 SHEET 8 A10 ALA A 93 TRP A 100 -1 N GLN A 98 O SER A 105 SHEET 9 A10 LYS A 82 THR A 90 -1 N GLN A 84 O GLU A 99 SHEET 10 A10 LYS A 72 THR A 76 -1 N PHE A 73 O THR A 85 SSBOND 1 CYS A 120 CYS A 127 1555 1555 2.63 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 23 2 Bytes