Header list of 1ure.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 17-JUN-96 1URE TITLE NMR STRUCTURE OF INTESTINAL FATTY ACID-BINDING PROTEIN COMPLEXED WITH TITLE 2 PALMITATE, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTESTINAL FATTY ACID-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IFABP, I-FABP; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: COMPLEXED WITH PALMITATE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 CELL: SMALL INTESTINAL ENTEROCYTE; SOURCE 6 GENE: POTENTIAL; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511145; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: MG1655; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMON5840-I-FABP; SOURCE 11 OTHER_DETAILS: SEE REMARK 1, REFERENCE 1 KEYWDS LIPID-BINDING, LIPID TRANSPORT, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.E.HODSDON,J.W.PONDER,D.P.CISTOLA REVDAT 3 02-MAR-22 1URE 1 REMARK REVDAT 2 24-FEB-09 1URE 1 VERSN REVDAT 1 12-MAR-97 1URE 0 JRNL AUTH M.E.HODSDON,J.W.PONDER,D.P.CISTOLA JRNL TITL THE NMR SOLUTION STRUCTURE OF INTESTINAL FATTY ACID-BINDING JRNL TITL 2 PROTEIN COMPLEXED WITH PALMITATE: APPLICATION OF A NOVEL JRNL TITL 3 DISTANCE GEOMETRY ALGORITHM. JRNL REF J.MOL.BIOL. V. 264 585 1996 JRNL REFN ISSN 0022-2836 JRNL PMID 8969307 JRNL DOI 10.1006/JMBI.1996.0663 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.E.HODSDON,J.J.TONER,D.P.CISTOLA REMARK 1 TITL 1H, 13C AND 15N ASSIGNMENTS AND CHEMICAL SHIFT-DERIVED REMARK 1 TITL 2 SECONDARY STRUCTURE OF INTESTINAL FATTY ACID-BINDING PROTEIN REMARK 1 REF J.BIOMOL.NMR V. 6 198 1995 REMARK 1 REFN ISSN 0925-2738 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.BANASZAK,N.WINTER,Z.XU,D.A.BERNLOHR,S.COWAN,T.A.JONES REMARK 1 TITL LIPID-BINDING PROTEINS: A FAMILY OF FATTY ACID AND RETINOID REMARK 1 TITL 2 TRANSPORT PROTEINS REMARK 1 REF ADV.PROTEIN CHEM. V. 45 89 1994 REMARK 1 REFN ISSN 0065-3233 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.C.SACCHETTINI,J.I.GORDON REMARK 1 TITL RAT INTESTINAL FATTY ACID BINDING PROTEIN. A MODEL SYSTEM REMARK 1 TITL 2 FOR ANALYZING THE FORCES THAT CAN BIND FATTY ACIDS TO REMARK 1 TITL 3 PROTEIN REMARK 1 REF J.BIOL.CHEM. V. 268 18399 1993 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 4 REMARK 1 AUTH J.C.SACCHETTINI,J.I.GORDON,L.J.BANASZAK REMARK 1 TITL CRYSTAL STRUCTURE OF RAT INTESTINAL FATTY-ACID-BINDING REMARK 1 TITL 2 PROTEIN. REFINEMENT AND ANALYSIS OF THE ESCHERICHIA REMARK 1 TITL 3 COLI-DERIVED PROTEIN WITH BOUND PALMITATE REMARK 1 REF J.MOL.BIOL. V. 208 327 1989 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TINKER REMARK 3 AUTHORS : PONDER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1URE 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_1000176976. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3-D 13C-RESOLVED NOESY; 3-D 15N REMARK 210 -RESOLVED NOESY; 2-D 1H- REMARK 210 HOMONUCLEAR NOESY; 2-D 13C- REMARK 210 EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : TINKER REMARK 210 METHOD USED : DISTANCE GEOMETRY WITH SIMULATED REMARK 210 ANNEALING REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 26 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : FINAL PENALTY FUNCTION VALUES REMARK 210 LESS THAN 10.0 REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: LIMITS ON SECONDARY STRUCTURE ELEMENTS WERE DEFINED BY THE REMARK 210 PROTON-CARBON CONSENSUS CHEMICAL SHIFT INDEX. 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 GLU A 15 CD GLU A 15 OE2 0.078 REMARK 500 1 GLU A 77 CD GLU A 77 OE2 0.074 REMARK 500 1 GLU A 85 CD GLU A 85 OE2 0.070 REMARK 500 1 GLU A 107 CD GLU A 107 OE2 0.068 REMARK 500 1 GLU A 123 CD GLU A 123 OE2 0.082 REMARK 500 2 GLU A 12 CD GLU A 12 OE2 0.079 REMARK 500 2 GLU A 15 CD GLU A 15 OE2 0.070 REMARK 500 2 GLU A 63 CD GLU A 63 OE2 0.070 REMARK 500 2 GLU A 85 CD GLU A 85 OE2 0.073 REMARK 500 2 GLU A 107 CD GLU A 107 OE1 0.072 REMARK 500 2 GLU A 123 CD GLU A 123 OE2 0.069 REMARK 500 2 GLU A 131 CD GLU A 131 OE1 0.077 REMARK 500 3 GLU A 12 CD GLU A 12 OE1 0.070 REMARK 500 3 GLU A 15 CD GLU A 15 OE1 0.073 REMARK 500 3 GLU A 77 CD GLU A 77 OE2 0.074 REMARK 500 3 GLU A 101 CD GLU A 101 OE2 0.075 REMARK 500 3 GLU A 123 CD GLU A 123 OE2 0.081 REMARK 500 3 GLU A 131 CD GLU A 131 OE2 0.077 REMARK 500 4 GLU A 15 CD GLU A 15 OE1 0.067 REMARK 500 4 GLU A 63 CD GLU A 63 OE2 0.067 REMARK 500 4 GLU A 85 CD GLU A 85 OE2 0.073 REMARK 500 4 GLU A 112 CD GLU A 112 OE2 0.067 REMARK 500 4 GLU A 123 CD GLU A 123 OE2 0.078 REMARK 500 5 GLU A 12 CD GLU A 12 OE1 0.070 REMARK 500 5 GLU A 15 CD GLU A 15 OE2 0.070 REMARK 500 5 GLU A 77 CD GLU A 77 OE2 0.079 REMARK 500 5 GLU A 85 CD GLU A 85 OE1 0.070 REMARK 500 5 GLU A 101 CD GLU A 101 OE2 0.072 REMARK 500 5 GLU A 123 CD GLU A 123 OE2 0.076 REMARK 500 5 GLU A 131 CD GLU A 131 OE2 0.077 REMARK 500 6 GLU A 12 CD GLU A 12 OE1 0.079 REMARK 500 6 GLU A 15 CD GLU A 15 OE2 0.070 REMARK 500 6 GLU A 19 CD GLU A 19 OE2 0.075 REMARK 500 6 GLU A 77 CD GLU A 77 OE2 0.070 REMARK 500 6 GLU A 120 CD GLU A 120 OE2 0.073 REMARK 500 6 GLU A 123 CD GLU A 123 OE2 0.074 REMARK 500 6 GLU A 131 CD GLU A 131 OE1 0.074 REMARK 500 7 GLU A 15 CD GLU A 15 OE1 0.072 REMARK 500 7 GLU A 19 CD GLU A 19 OE2 0.071 REMARK 500 7 GLU A 85 CD GLU A 85 OE2 0.071 REMARK 500 8 GLU A 15 CD GLU A 15 OE2 0.081 REMARK 500 8 GLU A 77 CD GLU A 77 OE2 0.075 REMARK 500 8 GLU A 123 CD GLU A 123 OE1 0.072 REMARK 500 9 GLU A 15 CD GLU A 15 OE2 0.077 REMARK 500 9 GLU A 77 CD GLU A 77 OE1 0.076 REMARK 500 9 GLU A 85 CD GLU A 85 OE2 0.071 REMARK 500 9 GLU A 101 CD GLU A 101 OE2 0.071 REMARK 500 9 GLU A 107 CD GLU A 107 OE2 0.069 REMARK 500 9 GLU A 120 CD GLU A 120 OE2 0.069 REMARK 500 9 GLU A 123 CD GLU A 123 OE2 0.077 REMARK 500 REMARK 500 THIS ENTRY HAS 100 BOND DEVIATIONS. 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 THR A 5 N - CA - CB ANGL. DEV. = 12.2 DEGREES REMARK 500 1 ASP A 9 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES REMARK 500 1 ASP A 9 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES REMARK 500 1 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES REMARK 500 1 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES REMARK 500 1 SER A 52 N - CA - CB ANGL. DEV. = -9.2 DEGREES REMARK 500 1 ARG A 56 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES REMARK 500 1 ARG A 56 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES REMARK 500 1 ASP A 59 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 1 ASP A 59 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 1 ASP A 67 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 74 CB - CG - OD2 ANGL. DEV. = -9.3 DEGREES REMARK 500 1 LYS A 88 CB - CA - C ANGL. DEV. = -13.4 DEGREES REMARK 500 1 ARG A 95 N - CA - CB ANGL. DEV. = -10.8 DEGREES REMARK 500 1 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 ASP A 97 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES REMARK 500 1 ASP A 97 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES REMARK 500 1 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 126 NE - CZ - NH2 ANGL. DEV. = 9.3 DEGREES REMARK 500 1 GLU A 131 N - CA - CB ANGL. DEV. = 12.1 DEGREES REMARK 500 2 ASP A 3 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES REMARK 500 2 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 2 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 2 TYR A 14 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 2 TYR A 14 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES REMARK 500 2 TYR A 14 CG - CD2 - CE2 ANGL. DEV. = -5.0 DEGREES REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES REMARK 500 2 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 2 THR A 48 N - CA - CB ANGL. DEV. = 11.8 DEGREES REMARK 500 2 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES REMARK 500 2 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 2 ASP A 59 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES REMARK 500 2 ASP A 74 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES REMARK 500 2 ASP A 74 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 2 TRP A 82 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES REMARK 500 2 LYS A 88 CB - CA - C ANGL. DEV. = -14.4 DEGREES REMARK 500 2 ARG A 95 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES REMARK 500 2 ARG A 95 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ASP A 97 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES REMARK 500 2 ASP A 97 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 2 TYR A 117 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES REMARK 500 2 ARG A 126 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES REMARK 500 2 GLU A 131 N - CA - CB ANGL. DEV. = 15.1 DEGREES REMARK 500 3 THR A 5 CA - CB - CG2 ANGL. DEV. = 10.4 DEGREES REMARK 500 3 TRP A 6 CD1 - CG - CD2 ANGL. DEV. = -5.3 DEGREES REMARK 500 3 ASP A 9 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 385 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 PHE A 2 -51.44 73.42 REMARK 500 1 ASP A 3 91.18 -36.74 REMARK 500 1 ASN A 11 -165.76 -121.10 REMARK 500 1 GLU A 12 89.30 -176.35 REMARK 500 1 ASN A 13 -3.60 97.95 REMARK 500 1 ASN A 24 -85.67 -90.76 REMARK 500 1 VAL A 25 -72.41 -117.40 REMARK 500 1 ASP A 34 -36.67 -38.60 REMARK 500 1 LEU A 36 93.47 -37.08 REMARK 500 1 ARG A 56 153.70 179.72 REMARK 500 1 VAL A 61 128.02 74.57 REMARK 500 1 PHE A 62 99.95 -160.11 REMARK 500 1 THR A 76 -169.03 71.96 REMARK 500 1 ASN A 98 -33.99 -168.54 REMARK 500 1 LYS A 100 -112.01 -81.97 REMARK 500 1 GLU A 101 142.40 166.17 REMARK 500 1 TYR A 117 112.10 -165.96 REMARK 500 1 GLU A 120 -84.95 163.52 REMARK 500 1 ALA A 124 97.08 -162.72 REMARK 500 1 LYS A 130 97.53 55.83 REMARK 500 2 VAL A 8 119.19 -34.76 REMARK 500 2 GLU A 12 -90.07 -150.38 REMARK 500 2 ASN A 24 -106.01 76.11 REMARK 500 2 VAL A 25 -55.26 -133.74 REMARK 500 2 ASN A 35 29.13 97.07 REMARK 500 2 LEU A 36 81.80 -65.94 REMARK 500 2 LEU A 38 95.35 -67.78 REMARK 500 2 THR A 48 79.53 -67.38 REMARK 500 2 VAL A 49 75.83 -59.57 REMARK 500 2 SER A 52 44.85 -104.10 REMARK 500 2 VAL A 60 -60.98 -101.89 REMARK 500 2 VAL A 61 109.11 66.14 REMARK 500 2 ASP A 67 113.43 -39.36 REMARK 500 2 PHE A 68 -166.26 -106.80 REMARK 500 2 ASP A 74 -44.75 -153.79 REMARK 500 2 THR A 76 172.30 71.46 REMARK 500 2 GLU A 77 151.99 -35.77 REMARK 500 2 GLU A 85 -143.98 -72.66 REMARK 500 2 ASN A 87 -13.79 96.74 REMARK 500 2 ASN A 98 6.08 -160.02 REMARK 500 2 LYS A 100 -111.37 -113.28 REMARK 500 2 ARG A 106 85.16 -68.18 REMARK 500 2 TYR A 117 -142.76 96.60 REMARK 500 2 GLU A 120 -84.03 -174.74 REMARK 500 2 GLU A 123 -179.67 -59.13 REMARK 500 2 ALA A 124 76.21 -168.08 REMARK 500 2 LYS A 130 89.26 50.37 REMARK 500 3 ASP A 3 93.74 -43.85 REMARK 500 3 TRP A 6 -158.98 -159.75 REMARK 500 3 LYS A 7 -99.64 178.91 REMARK 500 REMARK 500 THIS ENTRY HAS 495 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 132 DBREF 1URE A 1 131 UNP P02693 FABPI_RAT 1 131 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 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 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 HET PLM A 132 49 HETNAM PLM PALMITIC ACID FORMUL 2 PLM C16 H32 O2 HELIX 1 1 TYR A 14 MET A 21 1 8 HELIX 2 2 VAL A 26 ALA A 32 1 7 SHEET 1 A 3 THR A 5 LYS A 7 0 SHEET 2 A 3 LYS A 37 GLN A 42 -1 N LEU A 38 O TRP A 6 SHEET 3 A 3 PHE A 47 GLU A 51 -1 N LYS A 50 O THR A 39 SHEET 1 B 2 THR A 79 MET A 84 0 SHEET 2 B 2 LEU A 89 LYS A 94 -1 N LYS A 94 O THR A 79 SHEET 1 C 2 LEU A 113 GLN A 115 0 SHEET 2 C 2 ARG A 126 PHE A 128 -1 N PHE A 128 O LEU A 113 SITE 1 AC1 11 TYR A 14 ILE A 23 GLU A 51 PHE A 55 SITE 2 AC1 11 PHE A 62 TYR A 70 LEU A 72 ASP A 74 SITE 3 AC1 11 ARG A 106 GLN A 115 TYR A 117 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