Header list of 1zry.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 23-MAY-05 1ZRY TITLE NMR STRUCTURAL ANALYSIS OF APO CHICKEN LIVER BILE ACID BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, LIVER; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: L-FABP, LIVER BASIC FABP, LB- FABP, LIVER BILE ACID-BINDING COMPND 5 PROTEIN, L-BABP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24D KEYWDS BETA BARREL, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR L.RAGONA,M.CATALANO,M.LUPPI,D.CICERO,T.ELISEO,J.FOOTE,F.FOGOLARI, AUTHOR 2 L.ZETTA,H.MOLINARI REVDAT 4 02-MAR-22 1ZRY 1 REMARK REVDAT 3 24-FEB-09 1ZRY 1 VERSN REVDAT 2 25-APR-06 1ZRY 1 JRNL REVDAT 1 31-JAN-06 1ZRY 0 JRNL AUTH L.RAGONA,M.CATALANO,M.LUPPI,D.CICERO,T.ELISEO,J.FOOTE, JRNL AUTH 2 F.FOGOLARI,L.ZETTA,H.MOLINARI JRNL TITL NMR DYNAMIC STUDIES SUGGEST THAT ALLOSTERIC ACTIVATION JRNL TITL 2 REGULATES LIGAND BINDING IN CHICKEN LIVER BILE ACID-BINDING JRNL TITL 3 PROTEIN JRNL REF J.BIOL.CHEM. V. 281 9697 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16439356 JRNL DOI 10.1074/JBC.M513003200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, DISCOVER 97 REMARK 3 AUTHORS : BRUKER SOFTWARE (XWINNMR), MOLECULAR SIMULATIONS, REMARK 3 SAN DIEGO, CA (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A SET OF REMARK 3 1000 NON REDUNDANT NOES ; 26 DISTANCE RESTRAINTS FOR 13 BACKBONE REMARK 3 HYDROGEN BONDS; 48 PHI ANGLE CONSTRAINTS REMARK 4 REMARK 4 1ZRY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000033048. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298 REMARK 210 PH : 7.0; 5.6 REMARK 210 IONIC STRENGTH : 20MM; 20 MM REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM CHICKEN LIVER BILE ACID REMARK 210 BINDING PROTEIN 15N, 13C, 20 MM REMARK 210 PHOSPHATE BUFFER NA; 1 MM REMARK 210 CHICKEN LIVER BILE ACID BINDING REMARK 210 PROTEIN 15N, 13C, 20 MM REMARK 210 PHOSPHATE BUFFER NA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY, NOESY; 2D 1H-15N HSQC, REMARK 210 3D 1H-15N HSQC-TOCSY,1H-15N HSQC- REMARK 210 NOESY, 3D HNHA; 3D 1H-15N-13C REMARK 210 HNCA, HN(CO)CA,HNCO,CBCANH, REMARK 210 CBCA(CO)NH; 3D 1H-15N-13C NOESY REMARK 210 OPTIMISED FOR AROMATIC AND REMARK 210 ALIPHATIC RESIDUES; 3D HACACO, REMARK 210 (H)CCH-COSY, (H)CCH-TOCSY, H(C) REMARK 210 CH-COSY, H(C)CHTOCSY; 2D TOCSY, REMARK 210 NOESY,2D 1H-15N HSQC, 3D 1H-15N REMARK 210 HSQC-TOCSY,1H-15N HSQC-NOESY, 3D REMARK 210 HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 700 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.2, NMRVIEW 5, DYANA REMARK 210 1.4 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 MINIMIZATION 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: 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 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 5 PHE A 2 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES 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 3 92.36 -60.07 REMARK 500 1 TYR A 9 -5.52 -146.10 REMARK 500 1 ALA A 10 91.24 -166.21 REMARK 500 1 GLU A 12 -76.66 -55.52 REMARK 500 1 ALA A 22 52.04 -95.40 REMARK 500 1 ALA A 31 78.90 -66.42 REMARK 500 1 ARG A 32 -42.14 179.03 REMARK 500 1 ARG A 55 -60.85 -157.88 REMARK 500 1 LYS A 66 -95.67 -155.12 REMARK 500 1 MET A 73 73.78 -154.78 REMARK 500 1 ASP A 74 -61.55 -168.86 REMARK 500 1 CYS A 80 -63.91 -145.37 REMARK 500 1 HIS A 83 -157.07 -164.06 REMARK 500 1 ASN A 86 -80.26 -149.92 REMARK 500 1 LYS A 88 -115.68 -145.70 REMARK 500 1 LYS A 95 -48.11 -157.61 REMARK 500 1 PHE A 96 -75.50 67.55 REMARK 500 1 SER A 97 -53.88 -158.55 REMARK 500 1 HIS A 98 -126.40 -165.17 REMARK 500 1 GLU A 99 -71.28 -124.03 REMARK 500 1 VAL A 108 71.10 -105.38 REMARK 500 1 ILE A 111 -124.24 -108.70 REMARK 500 2 GLN A 7 -131.70 -95.53 REMARK 500 2 VAL A 8 133.69 176.75 REMARK 500 2 TYR A 9 -8.91 -146.17 REMARK 500 2 GLU A 12 -77.96 -90.32 REMARK 500 2 ALA A 22 43.99 -85.03 REMARK 500 2 PRO A 36 -174.47 -57.43 REMARK 500 2 ARG A 55 -55.02 -174.84 REMARK 500 2 LEU A 64 -72.07 -56.03 REMARK 500 2 ALA A 68 85.65 -162.87 REMARK 500 2 THR A 71 -163.48 -107.75 REMARK 500 2 MET A 73 -61.18 -90.38 REMARK 500 2 LYS A 76 -77.06 -141.55 REMARK 500 2 LYS A 79 52.08 -157.28 REMARK 500 2 VAL A 82 -130.81 -123.62 REMARK 500 2 HIS A 83 127.80 -24.00 REMARK 500 2 ALA A 85 -61.86 -106.18 REMARK 500 2 VAL A 90 -86.17 -72.13 REMARK 500 2 LYS A 92 41.45 -104.13 REMARK 500 2 SER A 93 57.40 -151.03 REMARK 500 2 GLU A 99 -73.20 -57.29 REMARK 500 2 GLN A 100 -55.28 -161.06 REMARK 500 3 PHE A 2 -59.12 -132.21 REMARK 500 3 SER A 3 100.20 -57.56 REMARK 500 3 GLU A 12 -106.67 -79.82 REMARK 500 3 ALA A 20 41.25 -82.80 REMARK 500 3 ALA A 22 39.47 -93.47 REMARK 500 3 ARG A 32 -44.81 -175.68 REMARK 500 3 ASP A 33 48.74 -85.83 REMARK 500 REMARK 500 THIS ENTRY HAS 191 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 TYR A 14 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MVG RELATED DB: PDB REMARK 900 APO CHICKEN LIVER BILE ACID BINDING PROTEIN, NMR STRUCTURE REMARK 900 RELATED ID: 1TVQ RELATED DB: PDB REMARK 900 APO CHICKEN LIVER BILE ACID BINDING PROTEIN, X-RAY STRUCTURE REMARK 900 RELATED ID: 1TW4 RELATED DB: PDB REMARK 900 HOLO CHICKEN LIVER BILE ACID BINDING PROTEIN IN COMPLEX WITH REMARK 900 CHOLATE, X-RAY STRUCTURE DBREF 1ZRY A 1 125 UNP P80226 FABPL_CHICK 1 125 SEQRES 1 A 125 ALA PHE SER GLY THR TRP GLN VAL TYR ALA GLN GLU ASN SEQRES 2 A 125 TYR GLU GLU PHE LEU LYS ALA LEU ALA LEU PRO GLU ASP SEQRES 3 A 125 LEU ILE LYS MET ALA ARG ASP ILE LYS PRO ILE VAL GLU SEQRES 4 A 125 ILE GLN GLN LYS GLY ASP ASP PHE VAL VAL THR SER LYS SEQRES 5 A 125 THR PRO ARG GLN THR VAL THR ASN SER PHE THR LEU GLY SEQRES 6 A 125 LYS GLU ALA ASP ILE THR THR MET ASP GLY LYS LYS LEU SEQRES 7 A 125 LYS CYS THR VAL HIS LEU ALA ASN GLY LYS LEU VAL THR SEQRES 8 A 125 LYS SER GLU LYS PHE SER HIS GLU GLN GLU VAL LYS GLY SEQRES 9 A 125 ASN GLU MET VAL GLU THR ILE THR PHE GLY GLY VAL THR SEQRES 10 A 125 LEU ILE ARG ARG SER LYS ARG VAL HELIX 1 1 ASN A 13 LEU A 21 1 9 HELIX 2 2 PRO A 24 ALA A 31 1 8 SHEET 1 A 7 ALA A 68 ASP A 69 0 SHEET 2 A 7 ASN A 60 THR A 63 -1 N SER A 61 O ASP A 69 SHEET 3 A 7 ASP A 46 LYS A 52 -1 N VAL A 49 O ASN A 60 SHEET 4 A 7 ILE A 37 GLN A 42 -1 N GLU A 39 O THR A 50 SHEET 5 A 7 THR A 5 GLN A 11 -1 N TRP A 6 O VAL A 38 SHEET 6 A 7 ARG A 120 LYS A 123 -1 O ARG A 121 N ALA A 10 SHEET 7 A 7 GLU A 106 MET A 107 -1 N MET A 107 O SER A 122 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