Header list of 1vzs.pdb file
Complete list - n 24 2 Bytes
HEADER SYNTHASE 25-MAY-04 1VZS
TITLE SOLUTION STRUCTURE OF SUBUNIT F6 FROM THE PERIPHERAL STALK REGION OF
TITLE 2 ATP SYNTHASE FROM BOVINE HEART MITOCHONDRIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: F6;
COMPND 5 EC: 3.6.3.14;
COMPND 6 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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS SYNTHASE, ATP SYNTHASE, PERIPHERAL STALK, F6 SUBUNIT, HYDROGEN ION
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 34
AUTHOR R.J.CARBAJO,J.A.SILVESTER,M.J.RUNSWICK,J.E.WALKER,D.NEUHAUS
REVDAT 4 24-JAN-18 1VZS 1 SOURCE
REVDAT 3 24-MAR-09 1VZS 1 REMARK MASTER
REVDAT 2 24-FEB-09 1VZS 1 VERSN
REVDAT 1 02-SEP-04 1VZS 0
JRNL AUTH R.J.CARBAJO,J.A.SILVESTER,M.J.RUNSWICK,J.E.WALKER,D.NEUHAUS
JRNL TITL SOLUTION STRUCTURE OF SUBUNIT F(6) FROM THE PERIPHERAL STALK
JRNL TITL 2 REGION OF ATP SYNTHASE FROM BOVINE HEART MITOCHONDRIA
JRNL REF J.MOL.BIOL. V. 342 593 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15327958
JRNL DOI 10.1016/J.JMB.2004.07.013
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: NULL
REMARK 4
REMARK 4 1VZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1290015321.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 95% H2O, 5% D2O, 50MM NACL, 20
REMARK 210 MM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HSQC; NOESY-HSQC;
REMARK 210 TOCSY-HSQC; HCCH-COSY; HNCA;
REMARK 210 CBCACONH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, SPARKY
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 34
REMARK 210 CONFORMERS, SELECTION CRITERIA : JUMP IN TOTAL ENERGIES
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 400
REMARK 400 COMPOUND
REMARK 400 THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT
REMARK 400 (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX.
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 TYR A 35 H ASP A 38 1.40
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 2 -74.04 -68.63
REMARK 500 1 GLU A 3 33.72 -158.47
REMARK 500 1 LEU A 4 104.05 178.32
REMARK 500 1 VAL A 7 -44.96 177.20
REMARK 500 1 THR A 24 -86.21 52.86
REMARK 500 1 SER A 25 38.28 -168.55
REMARK 500 1 VAL A 29 160.98 51.38
REMARK 500 1 ASN A 60 46.54 178.61
REMARK 500 1 PHE A 61 87.35 45.32
REMARK 500 1 THR A 62 -79.89 -95.73
REMARK 500 1 GLU A 64 -37.89 -177.35
REMARK 500 1 ASP A 65 157.99 -47.43
REMARK 500 1 GLU A 69 87.97 -57.97
REMARK 500 1 VAL A 70 -44.96 -135.31
REMARK 500 1 VAL A 71 55.77 -147.15
REMARK 500 1 LYS A 73 -53.76 177.31
REMARK 500 2 LYS A 2 -40.88 -175.75
REMARK 500 2 GLU A 3 81.68 62.29
REMARK 500 2 LEU A 4 -82.79 -148.20
REMARK 500 2 VAL A 7 -46.61 178.59
REMARK 500 2 GLN A 23 41.45 -102.68
REMARK 500 2 GLU A 34 26.81 -152.09
REMARK 500 2 ALA A 53 -66.80 -123.56
REMARK 500 2 ASP A 54 -36.32 -179.71
REMARK 500 2 ASN A 56 31.16 -155.72
REMARK 500 2 THR A 57 -51.43 -154.98
REMARK 500 2 PHE A 61 83.80 -179.67
REMARK 500 2 THR A 62 -44.86 -167.30
REMARK 500 2 GLU A 69 -47.05 -172.95
REMARK 500 2 GLU A 72 -69.13 68.35
REMARK 500 2 GLN A 75 -68.55 -160.43
REMARK 500 3 LYS A 2 -69.76 68.18
REMARK 500 3 ASP A 5 159.63 173.69
REMARK 500 3 VAL A 7 -43.55 179.22
REMARK 500 3 GLN A 23 40.59 -96.95
REMARK 500 3 SER A 25 149.99 -176.81
REMARK 500 3 LYS A 52 18.87 -145.90
REMARK 500 3 ASP A 54 86.37 59.49
REMARK 500 3 THR A 57 -47.36 -134.92
REMARK 500 3 PRO A 59 46.82 -78.01
REMARK 500 3 PHE A 61 98.44 60.33
REMARK 500 3 THR A 62 31.67 -150.10
REMARK 500 3 LYS A 67 -21.04 87.35
REMARK 500 3 LYS A 73 54.09 -153.45
REMARK 500 3 GLN A 75 98.10 60.45
REMARK 500 4 GLU A 3 -57.97 -155.43
REMARK 500 4 LEU A 4 -58.82 -134.65
REMARK 500 4 ASP A 5 169.50 167.70
REMARK 500 4 VAL A 7 -47.02 -178.28
REMARK 500 4 THR A 24 37.49 -169.93
REMARK 500
REMARK 500 THIS ENTRY HAS 646 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VZS A 1 76 UNP P02721 ATPR_BOVIN 33 108
SEQRES 1 A 76 ASN LYS GLU LEU ASP PRO VAL GLN LYS LEU PHE VAL ASP
SEQRES 2 A 76 LYS ILE ARG GLU TYR ARG THR LYS ARG GLN THR SER GLY
SEQRES 3 A 76 GLY PRO VAL ASP ALA GLY PRO GLU TYR GLN GLN ASP LEU
SEQRES 4 A 76 ASP ARG GLU LEU PHE LYS LEU LYS GLN MET TYR GLY LYS
SEQRES 5 A 76 ALA ASP MET ASN THR PHE PRO ASN PHE THR PHE GLU ASP
SEQRES 6 A 76 PRO LYS PHE GLU VAL VAL GLU LYS PRO GLN SER
HELIX 1 1 VAL A 7 THR A 24 1 18
HELIX 2 2 TYR A 35 ASP A 54 1 20
HELIX 3 3 ASP A 65 GLU A 69 5 5
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 - n 24 2 Bytes