Header list of 2bo5.pdb file
Complete list - y 9 2 Bytes
HEADER HYDROLASE 07-APR-05 2BO5 TITLE BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ATP SYNTHASE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 24-143; COMPND 5 SYNONYM: OSCP; COMPND 6 EC: 3.6.3.14; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 ORGAN: HEART; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-10, PET-11; SOURCE 10 OTHER_DETAILS: MITOCHONDRIAL KEYWDS ATP SYNTHASE, PERIPHERAL STALK, OSCP, ALPHA-SUBUNIT, BETA-SUBUNIT, KEYWDS 2 PROTEIN-PROTEIN INTERACTIONS, CHEMICAL SHIFT PERTURBATIONS, CHEMICAL KEYWDS 3 SHIFT MAPPING, TITRATION, BINDING INTERFACE, CF(1), HYDROGEN ION KEYWDS 4 TRANSPORT, HYDROLASE, ION TRANSPORT, MITOCHONDRION, TRANSIT PEPTIDE, KEYWDS 5 TRANSPORT EXPDTA SOLUTION NMR NUMMDL 44 AUTHOR R.J.CARBAJO,F.A.KELLAS,M.J.RUNSWICK,M.G.MONTGOMERY,J.E.WALKER, AUTHOR 2 D.NEUHAUS REVDAT 3 09-MAY-18 2BO5 1 JRNL REMARK REVDAT 2 24-FEB-09 2BO5 1 VERSN REVDAT 1 17-AUG-05 2BO5 0 JRNL AUTH R.J.CARBAJO,F.A.KELLAS,M.J.RUNSWICK,M.G.MONTGOMERY, JRNL AUTH 2 J.E.WALKER,D.NEUHAUS JRNL TITL STRUCTURE OF THE F1-BINDING DOMAIN OF THE STATOR OF BOVINE JRNL TITL 2 F1FO-ATPASE AND HOW IT BINDS AN ALPHA-SUBUNIT. JRNL REF J. MOL. BIOL. V. 351 824 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 16045926 JRNL DOI 10.1016/J.JMB.2005.06.012 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 2BO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-APR-05. REMARK 100 THE DEPOSITION ID IS D_1290023559. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300.0 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 0.5M NACL, 20MM SODIUM PHOSPHATE REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 7% D2O, 93%H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; HNCA; REMARK 210 CBCACONH; HCCH-COSY; 15N NOESY- REMARK 210 HSQC; 13C NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 44 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW NOE ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED OSCP-NT 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 400 REMARK 400 COMPOUND REMARK 400 FUNCTION: PART OF THE STALK THAT LINKS CF(0) TO CF(1) 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 O ALA A 26 H ASN A 30 1.56 REMARK 500 O TYR A 23 H SER A 27 1.56 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 LYS A 3 -74.58 -60.65 REMARK 500 1 LEU A 4 156.02 61.05 REMARK 500 1 ARG A 6 76.30 60.24 REMARK 500 1 GLN A 10 -41.13 -174.55 REMARK 500 1 TYR A 12 -67.99 -148.00 REMARK 500 1 ASN A 30 31.72 105.72 REMARK 500 1 VAL A 60 -88.79 -63.06 REMARK 500 1 LYS A 61 -166.69 170.72 REMARK 500 1 LYS A 77 -36.53 168.20 REMARK 500 1 PHE A 78 -174.38 -55.03 REMARK 500 1 SER A 79 -45.14 131.62 REMARK 500 1 PRO A 80 -75.01 -99.94 REMARK 500 1 SER A 83 31.74 -93.75 REMARK 500 1 ASN A 84 -45.56 -146.48 REMARK 500 1 ARG A 94 32.47 -97.48 REMARK 500 1 LEU A 95 35.04 -97.90 REMARK 500 1 PRO A 117 90.47 -52.04 REMARK 500 2 ALA A 2 -71.74 67.38 REMARK 500 2 LYS A 3 135.24 -171.05 REMARK 500 2 LEU A 4 -176.40 -59.88 REMARK 500 2 VAL A 5 28.58 -143.04 REMARK 500 2 VAL A 9 -50.26 -130.89 REMARK 500 2 GLN A 10 -80.34 84.10 REMARK 500 2 TYR A 12 44.51 -146.31 REMARK 500 2 ASN A 30 32.01 100.06 REMARK 500 2 LYS A 61 160.83 62.58 REMARK 500 2 ARG A 62 38.79 -97.36 REMARK 500 2 SER A 63 -42.57 -169.92 REMARK 500 2 GLU A 76 -52.83 -122.33 REMARK 500 2 LYS A 77 -35.53 166.76 REMARK 500 2 PHE A 78 174.39 -50.10 REMARK 500 2 SER A 79 -46.26 144.03 REMARK 500 2 PRO A 80 -74.24 -99.53 REMARK 500 2 ASN A 84 -46.25 -143.83 REMARK 500 2 LEU A 95 -179.75 -54.26 REMARK 500 2 THR A 96 -51.81 82.98 REMARK 500 2 GLU A 115 46.35 -94.09 REMARK 500 2 CYS A 118 168.61 60.64 REMARK 500 3 ALA A 2 154.53 61.21 REMARK 500 3 VAL A 5 75.25 -67.39 REMARK 500 3 VAL A 9 78.73 -107.09 REMARK 500 3 TYR A 12 -57.96 -145.16 REMARK 500 3 ASN A 30 33.66 87.54 REMARK 500 3 GLU A 48 109.86 -56.62 REMARK 500 3 LYS A 61 -176.17 -57.77 REMARK 500 3 GLU A 76 -57.63 -128.51 REMARK 500 3 LYS A 77 -39.90 168.50 REMARK 500 3 PHE A 78 162.47 -43.47 REMARK 500 3 SER A 79 -53.11 157.91 REMARK 500 3 PRO A 80 -67.42 -99.71 REMARK 500 REMARK 500 THIS ENTRY HAS 729 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6564 RELATED DB: BMRB DBREF 2BO5 A 1 120 UNP P13621 ATPO_BOVIN 24 143 SEQRES 1 A 120 PHE ALA LYS LEU VAL ARG PRO PRO VAL GLN ILE TYR GLY SEQRES 2 A 120 ILE GLU GLY ARG TYR ALA THR ALA LEU TYR SER ALA ALA SEQRES 3 A 120 SER LYS GLN ASN LYS LEU GLU GLN VAL GLU LYS GLU LEU SEQRES 4 A 120 LEU ARG VAL GLY GLN ILE LEU LYS GLU PRO LYS MET ALA SEQRES 5 A 120 ALA SER LEU LEU ASN PRO TYR VAL LYS ARG SER VAL LYS SEQRES 6 A 120 VAL LYS SER LEU SER ASP MET THR ALA LYS GLU LYS PHE SEQRES 7 A 120 SER PRO LEU THR SER ASN LEU ILE ASN LEU LEU ALA GLU SEQRES 8 A 120 ASN GLY ARG LEU THR ASN THR PRO ALA VAL ILE SER ALA SEQRES 9 A 120 PHE SER THR MET MET SER VAL HIS ARG GLY GLU VAL PRO SEQRES 10 A 120 CYS THR VAL HELIX 1 1 GLY A 13 ASN A 30 1 18 HELIX 2 2 LYS A 31 GLU A 48 1 18 HELIX 3 3 GLU A 48 ALA A 53 1 6 HELIX 4 4 VAL A 64 ALA A 74 1 11 HELIX 5 5 ASN A 84 ALA A 90 1 7 HELIX 6 6 THR A 98 GLU A 115 1 18 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 - y 9 2 Bytes