Header list of 1st7.pdb file
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HEADER TRANSPORT PROTEIN 25-MAR-04 1ST7 TITLE SOLUTION STRUCTURE OF ACYL COENZYME A BINDING PROTEIN FROM YEAST COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACYL-COA-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ACBP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: ACB1, ACB, YGR037C; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETACBP KEYWDS FOUR HELIX BUNDLE, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.TEILUM,T.THORMANN,N.R.CATERER,H.I.POULSEN,P.H.JENSEN,J.KNUDSEN, AUTHOR 2 B.B.KRAGELUND,F.M.POULSEN REVDAT 3 02-MAR-22 1ST7 1 REMARK REVDAT 2 24-FEB-09 1ST7 1 VERSN REVDAT 1 01-MAR-05 1ST7 0 JRNL AUTH K.TEILUM,T.THORMANN,N.R.CATERER,H.I.POULSEN,P.H.JENSEN, JRNL AUTH 2 J.KNUDSEN,B.B.KRAGELUND,F.M.POULSEN JRNL TITL DIFFERENT SECONDARY STRUCTURE ELEMENTS AS SCAFFOLDS FOR JRNL TITL 2 PROTEIN FOLDING TRANSITION STATES OF TWO HOMOLOGOUS JRNL TITL 3 FOUR-HELIX BUNDLES JRNL REF PROTEINS V. 59 80 2005 JRNL REFN ISSN 0887-3585 JRNL PMID 15690348 JRNL DOI 10.1002/PROT.20340 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8, X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 1040 NOE REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 133 DIHEDRAL ANGLE CONSTRAINTS, REMARK 3 13 DISTANCE CONSTRAINTS FROM HYDROGEN BONDS REMARK 4 REMARK 4 1ST7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000021982. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.75 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2.5 MM U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING AND CHARMM22 REMARK 210 WATER REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS,STRUCTURES WITH THE REMARK 210 LOWEST 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: 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 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 LEU A 25 N - CA - CB ANGL. DEV. = -13.0 DEGREES REMARK 500 5 TYR A 84 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES REMARK 500 6 TYR A 84 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 6 TYR A 84 CB - CG - CD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 10 TYR A 84 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES REMARK 500 11 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 11 TYR A 84 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES REMARK 500 12 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 12 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 12 TYR A 84 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 16 TYR A 84 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES REMARK 500 16 TYR A 84 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES REMARK 500 19 TYR A 53 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 19 TYR A 53 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES REMARK 500 19 TYR A 73 CB - CG - CD1 ANGL. DEV. = -4.8 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 GLU A 14 25.08 -142.86 REMARK 500 1 THR A 17 74.74 -102.46 REMARK 500 1 ASP A 40 -75.33 -109.96 REMARK 500 1 LYS A 43 84.94 -160.15 REMARK 500 1 LYS A 62 -36.10 -31.09 REMARK 500 1 SER A 65 -59.79 -26.78 REMARK 500 2 THR A 17 79.18 -106.10 REMARK 500 2 ASN A 39 107.69 -55.80 REMARK 500 2 GLU A 42 29.08 -146.08 REMARK 500 2 ILE A 46 -64.72 -104.12 REMARK 500 2 LYS A 62 -26.43 -29.74 REMARK 500 2 SER A 65 35.71 -86.44 REMARK 500 3 THR A 17 77.96 -102.40 REMARK 500 3 GLU A 42 48.10 -84.29 REMARK 500 3 LYS A 43 89.89 -153.86 REMARK 500 3 MET A 49 -64.75 -126.18 REMARK 500 3 LYS A 62 -34.00 -26.44 REMARK 500 3 SER A 65 46.14 -87.56 REMARK 500 4 GLU A 14 29.60 -144.89 REMARK 500 4 ASN A 39 84.27 -59.18 REMARK 500 4 LYS A 43 87.26 -153.97 REMARK 500 4 LYS A 62 -46.68 -25.61 REMARK 500 5 GLU A 14 21.31 -140.62 REMARK 500 5 ASP A 40 -73.63 -76.40 REMARK 500 5 GLU A 42 43.52 -77.03 REMARK 500 5 LYS A 43 82.19 -160.11 REMARK 500 5 LYS A 62 -39.77 -26.61 REMARK 500 5 SER A 65 34.82 -73.15 REMARK 500 6 ASP A 40 -80.00 -101.02 REMARK 500 6 LYS A 43 76.36 -160.37 REMARK 500 7 THR A 17 77.79 -105.27 REMARK 500 7 ASP A 40 -86.19 -113.35 REMARK 500 7 LYS A 43 77.42 -159.89 REMARK 500 8 GLU A 14 36.57 -144.55 REMARK 500 8 THR A 17 75.52 -106.79 REMARK 500 8 ASP A 40 -81.27 -93.18 REMARK 500 8 GLU A 42 48.89 -78.80 REMARK 500 8 LYS A 43 86.80 -160.31 REMARK 500 8 LYS A 62 -32.93 -27.69 REMARK 500 8 LYS A 64 -61.48 -109.85 REMARK 500 8 SER A 65 43.36 -87.52 REMARK 500 9 GLU A 14 47.74 -155.78 REMARK 500 9 THR A 17 77.48 -115.68 REMARK 500 9 ASN A 39 92.68 -61.41 REMARK 500 9 GLU A 42 21.51 -72.38 REMARK 500 10 ASN A 39 79.59 -67.78 REMARK 500 10 LYS A 43 84.36 -155.65 REMARK 500 10 LYS A 62 -35.39 -27.74 REMARK 500 10 SER A 65 -63.30 -26.30 REMARK 500 11 ASN A 39 103.61 -48.32 REMARK 500 REMARK 500 THIS ENTRY HAS 101 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 ASP A 38 ASN A 39 6 145.34 REMARK 500 LYS A 83 TYR A 84 14 -149.61 REMARK 500 ASP A 38 ASN A 39 15 146.50 REMARK 500 ASP A 38 ASN A 39 16 149.51 REMARK 500 ASP A 38 ASN A 39 19 147.59 REMARK 500 LYS A 43 PRO A 44 19 146.12 REMARK 500 LYS A 64 SER A 65 20 -136.41 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 2 ARG A 52 0.08 SIDE CHAIN REMARK 500 6 TYR A 28 0.08 SIDE CHAIN REMARK 500 6 TYR A 31 0.08 SIDE CHAIN REMARK 500 9 ARG A 52 0.11 SIDE CHAIN REMARK 500 10 PHE A 5 0.10 SIDE CHAIN REMARK 500 11 TYR A 31 0.07 SIDE CHAIN REMARK 500 12 TYR A 31 0.07 SIDE CHAIN REMARK 500 14 TYR A 28 0.09 SIDE CHAIN REMARK 500 16 PHE A 5 0.08 SIDE CHAIN REMARK 500 18 ARG A 52 0.08 SIDE CHAIN REMARK 500 19 TYR A 31 0.07 SIDE CHAIN REMARK 500 19 ARG A 52 0.10 SIDE CHAIN REMARK 500 19 TYR A 84 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NTI RELATED DB: PDB REMARK 900 HOMOLOGOUE, BOVINE ACBP REMARK 900 RELATED ID: 1ACA RELATED DB: PDB REMARK 900 BOVINE ACBP COMPLEXED WITH PALMITOYL-COENZYME A REMARK 900 RELATED ID: 2ABD RELATED DB: PDB REMARK 900 BOVINE ACBP, EARLIER RELEASE REMARK 900 RELATED ID: 1HBK RELATED DB: PDB REMARK 900 PLASMODIUM FALCIPARUM ACBP DBREF 1ST7 A 1 86 UNP P31787 ACBP_YEAST 1 86 SEQRES 1 A 86 VAL SER GLN LEU PHE GLU GLU LYS ALA LYS ALA VAL ASN SEQRES 2 A 86 GLU LEU PRO THR LYS PRO SER THR ASP GLU LEU LEU GLU SEQRES 3 A 86 LEU TYR ALA LEU TYR LYS GLN ALA THR VAL GLY ASP ASN SEQRES 4 A 86 ASP LYS GLU LYS PRO GLY ILE PHE ASN MET LYS ASP ARG SEQRES 5 A 86 TYR LYS TRP GLU ALA TRP GLU ASN LEU LYS GLY LYS SER SEQRES 6 A 86 GLN GLU ASP ALA GLU LYS GLU TYR ILE ALA LEU VAL ASP SEQRES 7 A 86 GLN LEU ILE ALA LYS TYR SER SER HELIX 1 1 GLN A 3 GLU A 14 1 12 HELIX 2 2 THR A 21 VAL A 36 1 16 HELIX 3 3 MET A 49 ASN A 60 1 12 HELIX 4 4 GLN A 66 TYR A 84 1 19 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