Header list of 1nvl.pdb file
Complete list - r 25 2 Bytes
HEADER LIGAND BINDING PROTEIN 04-FEB-03 1NVL TITLE RDC-REFINED NMR STRUCTURE OF BOVINE ACYL-COENZYME A BINDING PROTEIN, TITLE 2 ACBP, IN COMPLEX WITH PALMITOYL-COENZYME A CAVEAT 1NVL THERE IS A CHIRALITY ERROR INVOLVING COA 87. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACYL-COA-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ACBP, DIAZEPAM BINDING INHIBITOR, DBI, ENDOZEPINE, EP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: ACBP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3A KEYWDS 4-ALPHA-HELIX BUNDLE, PROTEIN-LIGAND COMPLEX, PALMITOYL-COENZYME A, KEYWDS 2 LIGAND BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.H.LERCHE,B.B.KRAGELUND,C.REDFIELD,F.M.POULSEN REVDAT 3 28-SEP-11 1NVL 1 LINK CAVEAT VERSN REVDAT 2 24-FEB-09 1NVL 1 VERSN REVDAT 1 11-MAY-04 1NVL 0 JRNL AUTH M.H.LERCHE,B.B.KRAGELUND,C.REDFIELD,F.M.POULSEN JRNL TITL RDC-REFINED NMR STRUCTURE OF BOVINE ACYL-COENZYME A BINDING JRNL TITL 2 PROTEIN, ACBP, IN COMPLEX WITH PALMITOYL-COENZYME A JRNL REF TO BE PUBLISHED 2003 JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.B.KRAGELUND,K.V.ANDERSEN,J.C.MADSEN,J.KNUDSEN,F.M.POULSEN REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN REMARK 1 TITL 2 ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A. REMARK 1 REF J.MOL.BIOL. V. 230 1260 1993 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1993.1240 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.V.ANDERSEN,F.M.POULSEN REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING REMARK 1 TITL 2 PROTEIN FROM BOVINE LIVER: STRUCTURAL REFINEMENT USING REMARK 1 TITL 3 HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY. REMARK 1 REF J.BIOMOL.NMR V. 3 271 1993 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR MODIFIED 3.8 REMARK 3 AUTHORS : BRNGER, A. T. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NVL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-03. REMARK 100 THE RCSB ID CODE IS RCSB018252. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 298 REMARK 210 PH : 6.5; 6.5 REMARK 210 IONIC STRENGTH : NO SALT ADDED; NO SALT ADDED REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM ACBP, PH 6.5, 0.5 MM REMARK 210 PALMITOYL-COENZYME A, 5% (3:1) REMARK 210 [DMPC:DHPC], 90% H2O, 10% D2O; REMARK 210 0.5 MM ACBP, PH 6.5, 0.5 MM REMARK 210 PALMITOYL-COENZYME A, 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; S3E-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX; HOME BUILT REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; HOME BUILT REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PRONTO 20000515, FELIX, MNMR REMARK 210 METHOD USED : SIMULATED ANNEALING FOLLOWED BY REMARK 210 RESTRAINED MOLECULAR DYNAMICS IN REMARK 210 FULL CHARMM FORCE FIELD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 REMARK 210 REMARK 210 REMARK: REFINEMENT OF EARLIER PDB DEPOSIT, 1ACA, SEE ENTRY FOR REMARK 210 DETAILS. NOE AND DIHEDRAL ANGLE CONSTRAINTS OBTAINED AND MODIFIED REMARK 210 FROM THIS ENTRY. RESIDUAL DIPOLAR COUPLINGS ADDED AS ADDITIONAL REMARK 210 RESTRAINTS. 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: 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 3 HIS A 14 CG HIS A 14 ND1 -0.091 REMARK 500 5 HIS A 14 CG HIS A 14 ND1 -0.094 REMARK 500 15 HIS A 14 CG HIS A 14 ND1 -0.093 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 55 CG - CD1 - NE1 ANGL. DEV. = -8.1 DEGREES REMARK 500 1 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 1 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES REMARK 500 1 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES REMARK 500 1 TRP A 58 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 1 TRP A 58 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 1 TRP A 58 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ASP A 68 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 GLU A 23 OE1 - CD - OE2 ANGL. DEV. = 8.6 DEGREES REMARK 500 2 HIS A 30 CA - CB - CG ANGL. DEV. = -11.4 DEGREES REMARK 500 2 ASP A 38 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES REMARK 500 2 THR A 41 OG1 - CB - CG2 ANGL. DEV. = -14.7 DEGREES REMARK 500 2 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 2 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 2 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES REMARK 500 2 TRP A 55 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES REMARK 500 2 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -7.7 DEGREES REMARK 500 2 TRP A 58 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 2 GLU A 79 OE1 - CD - OE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 3 HIS A 30 CA - CB - CG ANGL. DEV. = -12.9 DEGREES REMARK 500 3 ASP A 38 CB - CG - OD2 ANGL. DEV. = -9.0 DEGREES REMARK 500 3 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -8.7 DEGREES REMARK 500 3 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 9.2 DEGREES REMARK 500 3 ASP A 56 N - CA - CB ANGL. DEV. = -11.6 DEGREES REMARK 500 3 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 3 TRP A 58 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES REMARK 500 3 TRP A 58 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES REMARK 500 3 ASP A 68 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 3 ALA A 72 N - CA - CB ANGL. DEV. = -10.3 DEGREES REMARK 500 4 ASP A 38 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 4 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 4 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -8.1 DEGREES REMARK 500 4 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 4 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES REMARK 500 4 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 4 TRP A 58 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES REMARK 500 5 HIS A 30 CA - CB - CG ANGL. DEV. = -11.4 DEGREES REMARK 500 5 ASP A 38 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES REMARK 500 5 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 5 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 5 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 5 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES REMARK 500 5 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 5 TRP A 58 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 6 HIS A 30 CA - CB - CG ANGL. DEV. = -10.9 DEGREES REMARK 500 6 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES REMARK 500 6 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 6 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES REMARK 500 6 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 8.3 DEGREES REMARK 500 6 TRP A 58 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 170 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 ALA A 3 -39.42 -16.10 REMARK 500 1 LYS A 16 -1.65 -48.14 REMARK 500 1 PRO A 19 174.03 -45.26 REMARK 500 1 ALA A 34 -30.44 -38.59 REMARK 500 1 ASP A 38 94.84 -38.83 REMARK 500 1 ASP A 48 -70.72 -98.88 REMARK 500 1 LYS A 62 -37.77 -29.87 REMARK 500 1 LYS A 66 -70.59 -24.05 REMARK 500 2 LEU A 15 102.64 -37.38 REMARK 500 2 LYS A 16 -4.45 -53.11 REMARK 500 2 LYS A 18 98.72 -16.05 REMARK 500 2 ARG A 43 98.79 -34.89 REMARK 500 2 PRO A 44 139.95 -38.64 REMARK 500 2 ASP A 48 -74.49 -111.01 REMARK 500 2 TYR A 84 -83.15 -83.67 REMARK 500 3 GLN A 2 100.33 -162.06 REMARK 500 3 ALA A 3 -39.10 -23.83 REMARK 500 3 PRO A 19 -177.77 -55.61 REMARK 500 3 GLU A 42 136.19 -38.43 REMARK 500 3 PRO A 44 168.38 -43.89 REMARK 500 3 ASP A 48 -71.89 -112.14 REMARK 500 3 LYS A 71 -72.12 -46.56 REMARK 500 4 LYS A 16 -1.32 -58.06 REMARK 500 4 LYS A 18 84.09 -16.35 REMARK 500 4 PRO A 19 163.40 -48.95 REMARK 500 4 ASN A 40 40.39 -95.63 REMARK 500 4 PRO A 44 -31.30 -23.89 REMARK 500 4 ASP A 48 -77.92 -106.87 REMARK 500 4 ALA A 53 -71.56 -39.47 REMARK 500 4 LYS A 54 -7.96 -55.20 REMARK 500 4 LYS A 66 -55.48 -25.54 REMARK 500 5 GLN A 2 72.36 1.82 REMARK 500 5 ALA A 3 -45.19 -18.90 REMARK 500 5 GLU A 4 -31.99 -38.82 REMARK 500 5 LEU A 15 133.04 -36.80 REMARK 500 5 LYS A 16 -2.96 -57.05 REMARK 500 5 PRO A 19 -178.38 -64.17 REMARK 500 5 PRO A 44 162.25 -42.96 REMARK 500 5 MET A 46 -78.51 -19.69 REMARK 500 5 ASP A 48 -79.68 -21.07 REMARK 500 5 LYS A 50 -2.85 -52.91 REMARK 500 5 LYS A 62 -37.30 -17.50 REMARK 500 5 ASP A 75 -70.01 -64.89 REMARK 500 6 GLN A 2 103.45 107.61 REMARK 500 6 ALA A 3 -32.43 -29.73 REMARK 500 6 PRO A 19 -174.84 -58.11 REMARK 500 6 ASP A 38 84.12 -56.15 REMARK 500 6 ILE A 39 100.89 -14.07 REMARK 500 6 ASP A 48 -70.06 143.32 REMARK 500 6 PHE A 49 -91.38 -55.28 REMARK 500 REMARK 500 THIS ENTRY HAS 199 RAMACHANDRAN OUTLIERS. 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 43 0.30 SIDE CHAIN REMARK 500 2 ARG A 43 0.30 SIDE CHAIN REMARK 500 3 ARG A 43 0.19 SIDE CHAIN REMARK 500 4 ARG A 43 0.18 SIDE CHAIN REMARK 500 5 ARG A 43 0.20 SIDE CHAIN REMARK 500 6 ARG A 43 0.18 SIDE CHAIN REMARK 500 7 ARG A 43 0.20 SIDE CHAIN REMARK 500 8 ARG A 43 0.27 SIDE CHAIN REMARK 500 9 ARG A 43 0.30 SIDE CHAIN REMARK 500 10 ARG A 43 0.31 SIDE CHAIN REMARK 500 11 ARG A 43 0.31 SIDE CHAIN REMARK 500 12 ARG A 43 0.16 SIDE CHAIN REMARK 500 14 ARG A 43 0.16 SIDE CHAIN REMARK 500 15 ARG A 43 0.30 SIDE CHAIN REMARK 500 16 ARG A 43 0.30 SIDE CHAIN REMARK 500 17 ARG A 43 0.14 SIDE CHAIN REMARK 500 18 ARG A 43 0.16 SIDE CHAIN REMARK 500 19 ARG A 43 0.31 SIDE CHAIN REMARK 500 20 ARG A 43 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 4 ASP A 56 45.5 L L OUTSIDE RANGE REMARK 500 10 PHE A 5 45.1 L L OUTSIDE RANGE REMARK 500 12 ASP A 56 46.2 L L OUTSIDE RANGE REMARK 500 20 ASP A 56 45.5 L L OUTSIDE RANGE 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 COA A 87 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 88 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NTI RELATED DB: PDB REMARK 900 RDC REFINED STRUCTURE OF APO-ACBP REMARK 900 RELATED ID: 1ACA RELATED DB: PDB REMARK 900 ORIGINAL NMR STRUCTURE OF HOLO-ACBP REMARK 900 RELATED ID: 2ABD RELATED DB: PDB REMARK 900 ORIGINAL NMR STRUCTURE OF APO-ACBP DBREF 1NVL A 1 86 UNP P07107 ACBP_BOVIN 1 86 SEQRES 1 A 86 SER GLN ALA GLU PHE ASP LYS ALA ALA GLU GLU VAL LYS SEQRES 2 A 86 HIS LEU LYS THR LYS PRO ALA ASP GLU GLU MET LEU PHE SEQRES 3 A 86 ILE TYR SER HIS TYR LYS GLN ALA THR VAL GLY ASP ILE SEQRES 4 A 86 ASN THR GLU ARG PRO GLY MET LEU ASP PHE LYS GLY LYS SEQRES 5 A 86 ALA LYS TRP ASP ALA TRP ASN GLU LEU LYS GLY THR SER SEQRES 6 A 86 LYS GLU ASP ALA MET LYS ALA TYR ILE ASP LYS VAL GLU SEQRES 7 A 86 GLU LEU LYS LYS LYS TYR GLY ILE HET COA A 87 79 HET PLM A 88 48 HETNAM COA COENZYME A HETNAM PLM PALMITIC ACID FORMUL 2 COA C21 H36 N7 O16 P3 S FORMUL 3 PLM C16 H32 O2 HELIX 1 1 ALA A 3 HIS A 14 1 12 HELIX 2 2 ALA A 20 VAL A 36 1 17 HELIX 3 3 GLY A 51 GLU A 60 1 10 HELIX 4 4 SER A 65 GLY A 85 1 21 LINK S1P COA A 87 C1 PLM A 88 1555 1555 1.82 SITE 1 AC1 11 ALA A 9 VAL A 12 LYS A 13 LEU A 15 SITE 2 AC1 11 LYS A 18 TYR A 28 TYR A 31 LYS A 32 SITE 3 AC1 11 LYS A 54 TYR A 73 PLM A 88 SITE 1 AC2 9 VAL A 12 LEU A 15 THR A 17 PRO A 19 SITE 2 AC2 9 MET A 24 LEU A 25 ILE A 27 PHE A 49 SITE 3 AC2 9 COA A 87 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 25 2 Bytes