Header list of 1c99.pdb file
Complete list - 27 20 Bytes
HEADER PROTON TRANSPORT, HYDROLASE 30-APR-99 1C99
TITLE ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF
TITLE 2 ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEOLIPID F1FO OF ATP SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBUNIT C;
COMPND 5 SYNONYM: PROTEOLIPID, DCCD-BINDING PROTEIN;
COMPND 6 EC: 3.6.1.34;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: ER;
SOURCE 5 CELLULAR_LOCATION: MEMBRANE;
SOURCE 6 GENE: UNCE;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ER
KEYWDS PROTEOLIPID F1FO, ATP SYNTHASE, PROTON TRANSLOCATION, PROTON
KEYWDS 2 TRANSPORT, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR V.K.RASTOGI,M.E.GIRVIN
REVDAT 4 27-NOV-19 1C99 1 JRNL REMARK
REVDAT 3 24-FEB-09 1C99 1 VERSN
REVDAT 2 26-SEP-01 1C99 3 ATOM
REVDAT 1 19-NOV-99 1C99 0
JRNL AUTH V.K.RASTOGI,M.E.GIRVIN
JRNL TITL STRUCTURAL CHANGES LINKED TO PROTON TRANSLOCATION BY SUBUNIT
JRNL TITL 2 C OF THE ATP SYNTHASE.
JRNL REF NATURE V. 402 263 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10580496
JRNL DOI 10.1038/46224
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.K.RASTOGI,M.E.GIRVIN
REMARK 1 TITL 1H, 13C, AND 15N ASSIGNMENTS AND SECONDARY STRUCTURE OF THE
REMARK 1 TITL 2 HIGH PH FORM OF SUBUNIT C OF THE F1F0 ATP SYNTHASE.
REMARK 1 REF J.BIOMOL.NMR V. 13 91 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 10070750
REMARK 1 DOI 10.1023/A:1008379624478
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.E.GIRVIN,V.K.RASTOGI,F.ABILDGAARD,J.L.MARKLEY,
REMARK 1 AUTH 2 R.H.FILLINGAME
REMARK 1 TITL SOLUTION STRUCTURE OF THE TRANSMEMBRANE H+-TRANSPORTING
REMARK 1 TITL 2 SUBUNIT C OF THE F1F0 ATP SYNTHASE.
REMARK 1 REF BIOCHEMISTRY V. 37 8817 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9636021
REMARK 1 DOI 10.1021/BI980511M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.854, CNS 0.3
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C99 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000000981.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; TOCSY-HSQC; NOESY-HSQC;
REMARK 210 HNCO; HNHA; HN(CO)CA; HNCACB;
REMARK 210 H(CCO)NH; C(CO)NH; HCACO; HCCH-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C,
REMARK 210 15N-LABELED SUBUNIT C
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: 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 LEU A 48 H GLN A 52 1.51
REMARK 500 O PRO A 47 HG1 THR A 51 1.54
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 ILE A 30 -71.53 -59.73
REMARK 500 1 MET A 75 -76.04 -75.03
REMARK 500 2 PRO A 43 -25.74 -38.38
REMARK 500 3 GLN A 42 -177.01 -61.21
REMARK 500 3 PRO A 43 -71.58 -48.81
REMARK 500 3 ASP A 44 46.94 -146.09
REMARK 500 3 MET A 75 -74.57 -70.07
REMARK 500 4 ILE A 30 -72.54 -61.88
REMARK 500 4 PRO A 43 -33.21 -32.78
REMARK 500 4 ASP A 44 29.30 -141.02
REMARK 500 4 MET A 75 -74.99 -82.14
REMARK 500 5 ILE A 30 -72.30 -60.39
REMARK 500 5 PRO A 43 -7.44 -56.05
REMARK 500 5 MET A 75 -70.04 -82.34
REMARK 500 6 ILE A 30 -72.94 -57.92
REMARK 500 6 PRO A 43 -25.20 -38.06
REMARK 500 6 ILE A 63 -70.39 -58.15
REMARK 500 6 MET A 75 -74.97 -75.44
REMARK 500 7 ILE A 30 -70.90 -55.03
REMARK 500 7 PRO A 43 1.71 -61.12
REMARK 500 7 MET A 75 -74.71 -78.04
REMARK 500 8 ILE A 30 -74.22 -56.45
REMARK 500 8 ASP A 44 -83.87 -125.22
REMARK 500 8 LEU A 45 -51.53 69.87
REMARK 500 8 LEU A 49 -73.49 -48.61
REMARK 500 8 ALA A 77 -62.15 -98.59
REMARK 500 9 ILE A 30 -77.49 -58.17
REMARK 500 9 GLN A 42 -108.57 -71.85
REMARK 500 9 PRO A 43 -68.37 -101.48
REMARK 500 9 ASP A 44 36.36 -158.95
REMARK 500 9 MET A 75 -76.13 -73.21
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C99 A 1 79 UNP P68699 ATPL_ECOLI 1 79
SEQRES 1 A 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 A 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 A 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 A 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 A 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 A 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 A 79 ALA
HELIX 1 1 GLU A 2 ALA A 40 1 39
HELIX 2 2 PRO A 47 VAL A 74 1 28
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 - 27 20 Bytes