Header list of 2a7u.pdb file
Complete list - 25 20 Bytes
HEADER HYDROLASE 06-JUL-05 2A7U
TITLE NMR SOLUTION STRUCTURE OF THE E.COLI F-ATPASE DELTA SUBUNIT N-TERMINAL
TITLE 2 DOMAIN IN COMPLEX WITH ALPHA SUBUNIT N-TERMINAL 22 RESIDUES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, (RESIDUES 1-22);
COMPND 5 SYNONYM: F-ATPASE ALPHA CHAIN;
COMPND 6 EC: 3.6.3.14;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: REGULATORY UNIT;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ATP SYNTHASE DELTA CHAIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: N-TERMINAL DOMAIN, (RESIDUES 2-135);
COMPND 13 SYNONYM: F-ATPASE DELTA CHAIN;
COMPND 14 EC: 3.6.3.14;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE OCCURS NATURALLY IN E.COLI, GENES ATPA,
SOURCE 4 PAPA, UNCA;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 83334;
SOURCE 8 STRAIN: O157:H7;
SOURCE 9 GENE: ATPH, PAPE, UNCH;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: 594;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA HELIX BUNDLE, HYDROLASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR S.WILKENS,D.BORCHARDT,J.WEBER,A.E.SENIOR
REVDAT 3 13-JUL-11 2A7U 1 VERSN
REVDAT 2 24-FEB-09 2A7U 1 VERSN
REVDAT 1 11-OCT-05 2A7U 0
JRNL AUTH S.WILKENS,D.BORCHARDT,J.WEBER,A.E.SENIOR
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE INTERACTION OF THE DELTA
JRNL TITL 2 AND ALPHA SUBUNITS OF THE ESCHERICHIA COLI F(1)F(0)-ATP
JRNL TITL 3 SYNTHASE BY NMR SPECTROSCOPY
JRNL REF BIOCHEMISTRY V. 44 11786 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16128580
JRNL DOI 10.1021/BI0510678
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : AT BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMS DIFFERENCE OF NON-H ATOMS 1.114,
REMARK 3 FOR THE BACKBONE ATOMS 0.6174
REMARK 4
REMARK 4 2A7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-05.
REMARK 100 THE RCSB ID CODE IS RCSB033596.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM DELTA SUBUNIT N-TERMINAL
REMARK 210 DOMAIN U-13C,15N; 0.9 MM ALPHA
REMARK 210 SUBUNIT N-TERMINAL PEPTIDE; 10 MM
REMARK 210 NA,K PHOSPHATE, PH 7.2, 3MM NAN3,
REMARK 210 0.1 MM EDTA; 93% H20, 7% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 13C/12C
REMARK 210 FILTERED 2-D NOESY; 12C/12C
REMARK 210 FILTERED 2-D NOESY; 14N/12C
REMARK 210 FILTERED 2-D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.8, FELIX 98
REMARK 210 METHOD USED : DISTANCE GEOMETRY; SIMULATED
REMARK 210 ANNEALING; MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGED MINIMIZED STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ALA B 106
REMARK 465 GLU B 107
REMARK 465 VAL B 108
REMARK 465 ASP B 109
REMARK 465 VAL B 110
REMARK 465 ILE B 111
REMARK 465 SER B 112
REMARK 465 ALA B 113
REMARK 465 ALA B 114
REMARK 465 ALA B 115
REMARK 465 LEU B 116
REMARK 465 SER B 117
REMARK 465 GLU B 118
REMARK 465 GLN B 119
REMARK 465 GLN B 120
REMARK 465 LEU B 121
REMARK 465 ALA B 122
REMARK 465 LYS B 123
REMARK 465 ILE B 124
REMARK 465 SER B 125
REMARK 465 ALA B 126
REMARK 465 ALA B 127
REMARK 465 MET B 128
REMARK 465 GLU B 129
REMARK 465 LYS B 130
REMARK 465 ARG B 131
REMARK 465 LEU B 132
REMARK 465 SER B 133
REMARK 465 ARG B 134
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 HH21 ARG B 99 OE1 GLU B 103 1.51
REMARK 500 O ILE A 12 H ILE A 16 1.52
REMARK 500 O SER B 23 H TRP B 27 1.60
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 LEU A 3 -34.64 178.92
REMARK 500 ASN A 20 45.60 -84.21
REMARK 500 VAL A 21 41.06 -140.83
REMARK 500 LYS B 39 37.29 -94.46
REMARK 500 GLU B 41 -64.21 -29.47
REMARK 500 GLU B 66 21.48 48.51
REMARK 500 GLN B 67 45.34 -93.06
REMARK 500 ARG B 84 33.08 -160.24
REMARK 500 ALA B 87 40.69 -85.59
REMARK 500 GLU B 103 37.28 -89.57
REMARK 500 ALA B 104 -28.35 -142.48
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 ARG A 15 0.31 SIDE CHAIN
REMARK 500 ARG B 8 0.30 SIDE CHAIN
REMARK 500 ARG B 26 0.31 SIDE CHAIN
REMARK 500 ARG B 77 0.29 SIDE CHAIN
REMARK 500 ARG B 84 0.31 SIDE CHAIN
REMARK 500 ARG B 99 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ABV RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE
REMARK 900 E.COLI F-ATPASE DELTA SUBUNIT
DBREF 2A7U A 1 22 UNP P00822 ATPA_ECOLI 1 22
DBREF 2A7U B 1 134 UNP P0ABA4 ATPD_ECOLI 2 135
SEQRES 1 A 22 MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES 2 A 22 GLN ARG ILE ALA GLN PHE ASN VAL VAL
SEQRES 1 B 134 SER GLU PHE ILE THR VAL ALA ARG PRO TYR ALA LYS ALA
SEQRES 2 B 134 ALA PHE ASP PHE ALA VAL GLU HIS GLN SER VAL GLU ARG
SEQRES 3 B 134 TRP GLN ASP MET LEU ALA PHE ALA ALA GLU VAL THR LYS
SEQRES 4 B 134 ASN GLU GLN MET ALA GLU LEU LEU SER GLY ALA LEU ALA
SEQRES 5 B 134 PRO GLU THR LEU ALA GLU SER PHE ILE ALA VAL CYS GLY
SEQRES 6 B 134 GLU GLN LEU ASP GLU ASN GLY GLN ASN LEU ILE ARG VAL
SEQRES 7 B 134 MET ALA GLU ASN GLY ARG LEU ASN ALA LEU PRO ASP VAL
SEQRES 8 B 134 LEU GLU GLN PHE ILE HIS LEU ARG ALA VAL SER GLU ALA
SEQRES 9 B 134 THR ALA GLU VAL ASP VAL ILE SER ALA ALA ALA LEU SER
SEQRES 10 B 134 GLU GLN GLN LEU ALA LYS ILE SER ALA ALA MET GLU LYS
SEQRES 11 B 134 ARG LEU SER ARG
HELIX 1 1 ASN A 4 GLU A 7 5 4
HELIX 2 2 ILE A 8 PHE A 19 1 12
HELIX 3 3 PHE B 3 THR B 5 5 3
HELIX 4 4 VAL B 6 HIS B 21 1 16
HELIX 5 5 SER B 23 LYS B 39 1 17
HELIX 6 6 ASN B 40 SER B 48 1 9
HELIX 7 7 ALA B 52 CYS B 64 1 13
HELIX 8 8 ASP B 69 ASN B 82 1 14
HELIX 9 9 ALA B 87 GLU B 103 1 17
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
Complete list - 25 20 Bytes