Header list of 1aty.pdb file
Complete list - 16 20 Bytes
HEADER MEMBRANE PROTEIN 05-OCT-94 1ATY
TITLE DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE 2D
TITLE 2 NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C OF THE F1FO ATP
TITLE 3 SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F1F0 ATP SYNTHASE (SUBUNIT C);
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: UNCE;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PCP35 (PBR322 DERIVATIV
KEYWDS MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR M.E.GIRVIN,R.H.FILLINGAME
REVDAT 3 16-FEB-22 1ATY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ATY 1 VERSN
REVDAT 1 20-DEC-94 1ATY 0
JRNL AUTH M.E.GIRVIN,R.H.FILLINGAME
JRNL TITL DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL
JRNL TITL 2 DIFFERENCE 2D NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C
JRNL TITL 3 OF THE F1F0 ATP SYNTHASE.
JRNL REF BIOCHEMISTRY V. 34 1635 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7849023
JRNL DOI 10.1021/BI00005A020
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.GIRVIN,R.H.FILLINGAME
REMARK 1 TITL HAIRPIN FOLDING OF SUBUNIT C OF F1FO ATP SYNTHASE: 1H
REMARK 1 TITL 2 DISTANCE MEASUREMENTS TO NITROXIDE-DERIVATIZED ASPARTYL-61
REMARK 1 REF BIOCHEMISTRY V. 33 665 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.E.GIRVIN,R.H.FILLINGAME
REMARK 1 TITL HELICAL STRUCTURE AND FOLDING OF SUBUNIT C OF F1FO ATP
REMARK 1 TITL 2 SYNTHASE: 1H NMR RESONANCE ASSIGNMENTS AND NOE ANALYSIS
REMARK 1 REF BIOCHEMISTRY V. 32 12167 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ATY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171254.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 MODELS 1-9
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 LEU A 4
REMARK 465 ASN A 5
REMARK 465 MET A 6
REMARK 465 ASP A 7
REMARK 465 LEU A 8
REMARK 465 GLY A 27
REMARK 465 ILE A 28
REMARK 465 GLY A 29
REMARK 465 ILE A 30
REMARK 465 LEU A 31
REMARK 465 GLY A 32
REMARK 465 GLY A 33
REMARK 465 LYS A 34
REMARK 465 PHE A 35
REMARK 465 LEU A 36
REMARK 465 GLU A 37
REMARK 465 GLY A 38
REMARK 465 ALA A 39
REMARK 465 ALA A 40
REMARK 465 ARG A 41
REMARK 465 GLN A 42
REMARK 465 PRO A 43
REMARK 465 ASP A 44
REMARK 465 LEU A 45
REMARK 465 ILE A 46
REMARK 465 PRO A 47
REMARK 465 LEU A 48
REMARK 465 LEU A 49
REMARK 465 ARG A 50
REMARK 465 THR A 51
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 72 N MET A 75 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 TYR A 10 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 TYR A 10 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 5 TYR A 10 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 6 GLY A 69 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 8 TYR A 10 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 9 GLY A 69 N - CA - C ANGL. DEV. = -15.4 DEGREES
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 TYR A 10 20.75 -70.96
REMARK 500 1 MET A 16 -85.46 -33.50
REMARK 500 1 MET A 17 -73.59 -76.04
REMARK 500 1 LEU A 19 -71.53 -61.61
REMARK 500 1 ALA A 24 -79.75 -82.84
REMARK 500 1 ILE A 55 -20.98 171.01
REMARK 500 1 ASP A 61 16.11 105.05
REMARK 500 1 ILE A 63 -56.03 -21.06
REMARK 500 1 PRO A 64 -76.68 -70.86
REMARK 500 1 MET A 65 -73.08 -3.15
REMARK 500 1 MET A 75 -37.04 -32.03
REMARK 500 1 ALA A 77 40.45 -85.33
REMARK 500 1 VAL A 78 37.78 -94.85
REMARK 500 2 TYR A 10 23.57 -72.86
REMARK 500 2 MET A 16 -86.37 -51.49
REMARK 500 2 ALA A 24 -73.68 -83.93
REMARK 500 2 PHE A 53 54.87 27.55
REMARK 500 2 PHE A 54 -46.35 84.19
REMARK 500 2 VAL A 60 -77.31 -99.44
REMARK 500 2 ASP A 61 -104.52 -166.17
REMARK 500 2 ILE A 63 -63.28 -131.74
REMARK 500 2 MET A 75 -36.75 -31.60
REMARK 500 2 ALA A 77 46.16 -86.90
REMARK 500 3 TYR A 10 28.38 -77.76
REMARK 500 3 MET A 11 -63.79 -91.66
REMARK 500 3 MET A 16 -87.69 -27.29
REMARK 500 3 MET A 17 -71.01 -79.41
REMARK 500 3 LEU A 19 -71.47 -64.15
REMARK 500 3 ALA A 24 -92.21 -107.68
REMARK 500 3 PHE A 53 53.46 28.41
REMARK 500 3 PHE A 54 -45.73 83.74
REMARK 500 3 LEU A 59 -63.10 -174.18
REMARK 500 3 VAL A 60 -44.48 172.38
REMARK 500 3 ASP A 61 -111.24 -159.29
REMARK 500 3 ALA A 62 -53.73 89.15
REMARK 500 3 ILE A 63 -55.96 -18.36
REMARK 500 3 MET A 65 -56.03 -18.02
REMARK 500 3 ILE A 66 -73.36 -59.91
REMARK 500 3 LEU A 72 -64.11 -109.97
REMARK 500 3 MET A 75 -36.26 -32.72
REMARK 500 3 ALA A 77 45.49 -86.24
REMARK 500 3 VAL A 78 52.52 -95.63
REMARK 500 4 TYR A 10 7.24 -60.36
REMARK 500 4 MET A 16 -91.90 -46.28
REMARK 500 4 ALA A 25 39.14 -164.06
REMARK 500 4 PHE A 53 -132.95 -61.87
REMARK 500 4 PHE A 54 25.47 47.69
REMARK 500 4 ILE A 55 41.91 87.64
REMARK 500 4 VAL A 60 -81.39 -101.00
REMARK 500 4 ASP A 61 -140.04 -158.23
REMARK 500
REMARK 500 THIS ENTRY HAS 120 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 4 TYR A 10 0.08 SIDE CHAIN
REMARK 500 5 TYR A 10 0.06 SIDE CHAIN
REMARK 500 9 TYR A 10 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ATY A 1 79 UNP P68699 ATPL_ECOLI 1 79
SEQADV 1ATY CYS A 67 UNP P68699 ALA 67 CONFLICT
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 CYS VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 A 79 ALA
HELIX 1 1 MET A 11 ALA A 25 1 15
HELIX 2 2 VAL A 56 ASP A 61 1 6
HELIX 3 3 ASP A 61 ALA A 77 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
MODEL 1
Complete list - 16 20 Bytes