Header list of 1bsh.pdb file
Complete list - l 7 2 Bytes
HEADER HYDROLASE 27-AUG-98 1BSH
TITLE SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM
TITLE 2 ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA
TITLE 3 SUBUNITS OF THE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (EPSILON SUBUNIT);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.34;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: UNCC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K38, 594, DL39, 435;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PES2;
SOURCE 10 EXPRESSION_SYSTEM_GENE: UNCC
KEYWDS ATPSYNTHASE, F1-ATPASE, EPSILON SUBUNIT, NMR SPECTROSCOPY, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.WILKENS,R.A.CAPALDI
REVDAT 4 07-JUL-21 1BSH 1 REMARK
REVDAT 3 24-FEB-09 1BSH 1 VERSN
REVDAT 2 29-DEC-99 1BSH 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 02-SEP-98 1BSH 0
JRNL AUTH S.WILKENS,R.A.CAPALDI
JRNL TITL SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPASE
JRNL TITL 2 FROM ESCHERICHIA COLI AND INTERACTIONS OF THIS SUBUNIT WITH
JRNL TITL 3 BETA SUBUNITS IN THE COMPLEX.
JRNL REF J.BIOL.CHEM. V. 273 26645 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9756905
JRNL DOI 10.1074/JBC.273.41.26645
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.WILKENS,F.W.DAHLQUIST,L.P.MCINTOSH,L.W.DONALDSON,
REMARK 1 AUTH 2 R.A.CAPALDI
REMARK 1 TITL STRUCTURAL FEATURES OF THE EPSILON SUBUNIT OF THE
REMARK 1 TITL 2 ESCHERICHIA COLI ATP SYNTHASE DETERMINED BY NMR SPECTROSCOPY
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 961 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING AND MOLECULAR
REMARK 3 DYNAMICS
REMARK 4
REMARK 4 1BSH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008223.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.03
REMARK 210 PRESSURE : 10000 PA
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-HSMQC; 3D TOCSY-HSMQC;
REMARK 210 3D C(CO)NH; 3D H(CCO)NH;
REMARK 210 SIMULTANEOUS 13C/ 15N RESOLVED
REMARK 210 NOESY; VARIOUS 2D EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : GN; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : GE; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE OF THE E. COLI ATPASE EPSILON SUBUNIT WAS
REMARK 210 DETERMINED USING TRIPLE-RESONANCE NMR EXPERIMENTS WITH 15N AND
REMARK 210 13C/15N LABELED PROTEIN.
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: 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 MET A 2 36.38 -148.85
REMARK 500 1 ALA A 11 101.15 61.82
REMARK 500 1 VAL A 20 116.93 -168.44
REMARK 500 1 LYS A 22 144.44 -172.95
REMARK 500 1 ILE A 23 -145.69 -98.26
REMARK 500 1 GLN A 24 127.27 -174.12
REMARK 500 1 GLU A 31 26.72 -152.13
REMARK 500 1 ALA A 39 158.32 58.99
REMARK 500 1 LEU A 42 57.20 -171.16
REMARK 500 1 THR A 43 -136.90 -114.62
REMARK 500 1 LYS A 46 158.33 55.54
REMARK 500 1 HIS A 58 -77.05 -84.82
REMARK 500 1 GLU A 59 139.99 -179.59
REMARK 500 1 ILE A 62 -146.81 -100.46
REMARK 500 1 TYR A 63 132.40 -175.51
REMARK 500 1 SER A 65 -64.78 -139.79
REMARK 500 1 GLU A 70 111.65 -163.72
REMARK 500 1 GLN A 87 -72.92 162.32
REMARK 500 1 LEU A 89 -93.72 43.17
REMARK 500 1 ASP A 90 159.64 -49.48
REMARK 500 1 GLU A 91 -56.68 -141.26
REMARK 500 1 HIS A 109 21.76 -146.57
REMARK 500 1 ASP A 113 -99.13 -67.81
REMARK 500 2 TYR A 4 -144.86 -142.22
REMARK 500 2 ALA A 11 -89.83 53.71
REMARK 500 2 LYS A 22 110.68 -160.77
REMARK 500 2 SER A 28 -81.00 -128.83
REMARK 500 2 GLU A 29 -87.11 -68.53
REMARK 500 2 GLU A 31 32.47 -156.54
REMARK 500 2 PRO A 36 31.15 -81.11
REMARK 500 2 ALA A 39 168.24 77.05
REMARK 500 2 THR A 43 -156.69 -100.67
REMARK 500 2 GLN A 55 -93.69 43.22
REMARK 500 2 HIS A 56 66.98 -152.19
REMARK 500 2 HIS A 58 -165.74 -69.28
REMARK 500 2 VAL A 78 127.36 -178.97
REMARK 500 2 ARG A 85 126.18 61.32
REMARK 500 2 LEU A 89 -88.29 56.58
REMARK 500 2 SER A 106 78.88 -105.83
REMARK 500 2 SER A 108 -152.22 64.85
REMARK 500 2 HIS A 109 101.14 174.34
REMARK 500 2 ASP A 113 -96.41 -68.96
REMARK 500 2 LYS A 136 50.42 -110.07
REMARK 500 3 TYR A 4 -142.28 -143.55
REMARK 500 3 SER A 10 -159.68 -128.80
REMARK 500 3 ALA A 11 -74.26 -44.93
REMARK 500 3 GLN A 13 109.92 -161.77
REMARK 500 3 GLU A 21 -63.63 -144.94
REMARK 500 3 SER A 28 -40.10 -138.30
REMARK 500 3 GLU A 29 -91.53 -75.05
REMARK 500
REMARK 500 THIS ENTRY HAS 768 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 85 0.29 SIDE CHAIN
REMARK 500 1 ARG A 93 0.12 SIDE CHAIN
REMARK 500 1 ARG A 99 0.28 SIDE CHAIN
REMARK 500 1 ARG A 129 0.20 SIDE CHAIN
REMARK 500 2 ARG A 51 0.27 SIDE CHAIN
REMARK 500 2 ARG A 85 0.18 SIDE CHAIN
REMARK 500 2 ARG A 93 0.31 SIDE CHAIN
REMARK 500 2 ARG A 99 0.31 SIDE CHAIN
REMARK 500 2 ARG A 129 0.32 SIDE CHAIN
REMARK 500 3 ARG A 51 0.19 SIDE CHAIN
REMARK 500 3 ARG A 85 0.32 SIDE CHAIN
REMARK 500 3 ARG A 93 0.18 SIDE CHAIN
REMARK 500 3 ARG A 99 0.32 SIDE CHAIN
REMARK 500 3 ARG A 129 0.10 SIDE CHAIN
REMARK 500 4 ARG A 51 0.31 SIDE CHAIN
REMARK 500 4 ARG A 85 0.30 SIDE CHAIN
REMARK 500 4 ARG A 93 0.31 SIDE CHAIN
REMARK 500 4 ARG A 99 0.32 SIDE CHAIN
REMARK 500 4 ARG A 129 0.25 SIDE CHAIN
REMARK 500 5 ARG A 51 0.31 SIDE CHAIN
REMARK 500 5 ARG A 85 0.32 SIDE CHAIN
REMARK 500 5 ARG A 93 0.29 SIDE CHAIN
REMARK 500 5 ARG A 129 0.32 SIDE CHAIN
REMARK 500 6 ARG A 51 0.17 SIDE CHAIN
REMARK 500 6 ARG A 85 0.31 SIDE CHAIN
REMARK 500 6 ARG A 93 0.10 SIDE CHAIN
REMARK 500 6 ARG A 99 0.32 SIDE CHAIN
REMARK 500 6 ARG A 129 0.30 SIDE CHAIN
REMARK 500 7 ARG A 51 0.20 SIDE CHAIN
REMARK 500 7 ARG A 85 0.30 SIDE CHAIN
REMARK 500 7 ARG A 93 0.16 SIDE CHAIN
REMARK 500 7 ARG A 129 0.08 SIDE CHAIN
REMARK 500 8 ARG A 51 0.20 SIDE CHAIN
REMARK 500 8 ARG A 85 0.24 SIDE CHAIN
REMARK 500 8 ARG A 93 0.32 SIDE CHAIN
REMARK 500 8 ARG A 99 0.32 SIDE CHAIN
REMARK 500 8 ARG A 129 0.29 SIDE CHAIN
REMARK 500 9 ARG A 85 0.32 SIDE CHAIN
REMARK 500 9 ARG A 93 0.31 SIDE CHAIN
REMARK 500 9 ARG A 99 0.25 SIDE CHAIN
REMARK 500 9 ARG A 129 0.23 SIDE CHAIN
REMARK 500 10 ARG A 51 0.31 SIDE CHAIN
REMARK 500 10 ARG A 85 0.21 SIDE CHAIN
REMARK 500 10 ARG A 93 0.26 SIDE CHAIN
REMARK 500 10 ARG A 99 0.29 SIDE CHAIN
REMARK 500 10 ARG A 129 0.32 SIDE CHAIN
REMARK 500 11 ARG A 51 0.29 SIDE CHAIN
REMARK 500 11 ARG A 85 0.31 SIDE CHAIN
REMARK 500 11 ARG A 93 0.25 SIDE CHAIN
REMARK 500 11 ARG A 99 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 141 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BSN RELATED DB: PDB
REMARK 900 REPRESENTATIVE STRUCTURE
DBREF 1BSH A 1 138 UNP P0A6E6 ATPE_ECOLI 1 138
SEQRES 1 A 138 ALA MET THR TYR HIS LEU ASP VAL VAL SER ALA GLU GLN
SEQRES 2 A 138 GLN MET PHE SER GLY LEU VAL GLU LYS ILE GLN VAL THR
SEQRES 3 A 138 GLY SER GLU GLY GLU LEU GLY ILE TYR PRO GLY HIS ALA
SEQRES 4 A 138 PRO LEU LEU THR ALA ILE LYS PRO GLY MET ILE ARG ILE
SEQRES 5 A 138 VAL LYS GLN HIS GLY HIS GLU GLU PHE ILE TYR LEU SER
SEQRES 6 A 138 GLY GLY ILE LEU GLU VAL GLN PRO GLY ASN VAL THR VAL
SEQRES 7 A 138 LEU ALA ASP THR ALA ILE ARG GLY GLN ASP LEU ASP GLU
SEQRES 8 A 138 ALA ARG ALA MET GLU ALA LYS ARG LYS ALA GLU GLU HIS
SEQRES 9 A 138 ILE SER SER SER HIS GLY ASP VAL ASP TYR ALA GLN ALA
SEQRES 10 A 138 SER ALA GLU LEU ALA LYS ALA ILE ALA GLN LEU ARG VAL
SEQRES 11 A 138 ILE GLU LEU THR LYS LYS ALA MET
HELIX 1 1 ALA A 97 LYS A 100 1 4
HELIX 2 2 GLU A 102 ILE A 105 1 4
HELIX 3 3 ASP A 113 ALA A 122 1 10
HELIX 4 4 ALA A 126 LYS A 136 1 11
SHEET 1 A 2 TYR A 4 VAL A 8 0
SHEET 2 A 2 PHE A 16 VAL A 20 -1 N VAL A 20 O TYR A 4
SHEET 1 B 2 GLY A 48 ILE A 52 0
SHEET 2 B 2 GLU A 60 LEU A 64 -1 N LEU A 64 O GLY A 48
SHEET 1 C 2 GLY A 67 VAL A 71 0
SHEET 2 C 2 VAL A 76 ALA A 80 -1 N LEU A 79 O ILE A 68
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 - l 7 2 Bytes