Header list of 1abv.pdb file
Complete list - 27 20 Bytes
HEADER ATP SYNTHESIS 29-JAN-97 1ABV
TITLE N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM
TITLE 2 ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1 - 134;
COMPND 5 EC: 3.6.1.34;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: MM294 AND 594;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJC1;
SOURCE 9 EXPRESSION_SYSTEM_GENE: UNCH
KEYWDS ATP SYNTHESIS, ATP SYNTHASE, F1-ATPASE, DELTA SUBUNIT, NMR
KEYWDS 2 SPECTROSCOPY
EXPDTA SOLUTION NMR
AUTHOR S.WILKENS,S.D.DUNN,J.CHANDLER,F.W.DAHLQUIST,R.A.CAPALDI
REVDAT 4 27-OCT-21 1ABV 1 REMARK
REVDAT 3 19-MAY-09 1ABV 1 REMARK
REVDAT 2 24-FEB-09 1ABV 1 VERSN
REVDAT 1 07-JUL-97 1ABV 0
JRNL AUTH S.WILKENS,S.D.DUNN,J.CHANDLER,F.W.DAHLQUIST,R.A.CAPALDI
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE DELTA
JRNL TITL 2 SUBUNIT OF THE E. COLI ATPSYNTHASE.
JRNL REF NAT.STRUCT.BIOL. V. 4 198 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9164460
JRNL DOI 10.1038/NSB0397-198
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. THIS ENTRY CONTAINS THE MINIMIZED AVERAGE
REMARK 3 OVER 30 FILES. THE AVERAGE RMS DIFFERENCE TO THE MEAN STRUCTURE
REMARK 3 FOR NON-HYDROGEN ATOMS IS 1.25067. THE AVERAGE RMS DIFFERENCE TO
REMARK 3 THE MEAN STRUCTURE FOR THE BACKBONE IS 0.795004. THE B VALUE
REMARK 3 FIELD (COLUMNS 61 =66) CONTAINS THE RMS DIFFERENCE FROM THE MEAN.
REMARK 4
REMARK 4 1ABV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170633.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
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 : DG, SA, MD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL
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 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 A 106
REMARK 465 GLU A 107
REMARK 465 VAL A 108
REMARK 465 ASP A 109
REMARK 465 VAL A 110
REMARK 465 ILE A 111
REMARK 465 SER A 112
REMARK 465 ALA A 113
REMARK 465 ALA A 114
REMARK 465 ALA A 115
REMARK 465 LEU A 116
REMARK 465 SER A 117
REMARK 465 GLU A 118
REMARK 465 GLN A 119
REMARK 465 GLN A 120
REMARK 465 LEU A 121
REMARK 465 ALA A 122
REMARK 465 LYS A 123
REMARK 465 ILE A 124
REMARK 465 SER A 125
REMARK 465 ALA A 126
REMARK 465 ALA A 127
REMARK 465 MET A 128
REMARK 465 GLU A 129
REMARK 465 LYS A 130
REMARK 465 ARG A 131
REMARK 465 LEU A 132
REMARK 465 SER A 133
REMARK 465 ARG A 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 OE2 GLU A 36 HZ2 LYS A 39 1.40
REMARK 500 O SER A 23 H TRP A 27 1.49
REMARK 500 HZ1 LYS A 12 OD1 ASP A 16 1.55
REMARK 500 O ARG A 77 H GLU A 81 1.58
REMARK 500 O VAL A 101 H THR A 105 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 ALA A 87 37.02 -81.00
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 8 0.30 SIDE CHAIN
REMARK 500 ARG A 26 0.28 SIDE CHAIN
REMARK 500 ARG A 77 0.32 SIDE CHAIN
REMARK 500 ARG A 84 0.31 SIDE CHAIN
REMARK 500 ARG A 99 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ABV A 1 134 UNP P0ABA4 ATPD_ECOLI 2 135
SEQRES 1 A 134 SER GLU PHE ILE THR VAL ALA ARG PRO TYR ALA LYS ALA
SEQRES 2 A 134 ALA PHE ASP PHE ALA VAL GLU HIS GLN SER VAL GLU ARG
SEQRES 3 A 134 TRP GLN ASP MET LEU ALA PHE ALA ALA GLU VAL THR LYS
SEQRES 4 A 134 ASN GLU GLN MET ALA GLU LEU LEU SER GLY ALA LEU ALA
SEQRES 5 A 134 PRO GLU THR LEU ALA GLU SER PHE ILE ALA VAL CYS GLY
SEQRES 6 A 134 GLU GLN LEU ASP GLU ASN GLY GLN ASN LEU ILE ARG VAL
SEQRES 7 A 134 MET ALA GLU ASN GLY ARG LEU ASN ALA LEU PRO ASP VAL
SEQRES 8 A 134 LEU GLU GLN PHE ILE HIS LEU ARG ALA VAL SER GLU ALA
SEQRES 9 A 134 THR ALA GLU VAL ASP VAL ILE SER ALA ALA ALA LEU SER
SEQRES 10 A 134 GLU GLN GLN LEU ALA LYS ILE SER ALA ALA MET GLU LYS
SEQRES 11 A 134 ARG LEU SER ARG
HELIX 1 1 ILE A 4 GLU A 20 1 17
HELIX 2 2 VAL A 24 THR A 38 1 15
HELIX 3 3 GLU A 41 LEU A 47 1 7
HELIX 4 4 PRO A 53 CYS A 64 1 12
HELIX 5 5 GLU A 70 GLU A 81 1 12
HELIX 6 6 LEU A 88 GLU A 103 1 16
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 - 27 20 Bytes