Header list of 2prf.pdb file
Complete list - v 29 2 Bytes
HEADER ACTIN-BINDING 12-JAN-94 2PRF
TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROFILIN IA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACANTHAMOEBA SP.;
SOURCE 3 ORGANISM_TAXID: 5756
KEYWDS ACTIN-BINDING
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR S.J.ARCHER,V.K.VINSON,T.D.POLLARD,E.E.LATTMAN,D.A.TORCHIA
REVDAT 4 29-NOV-17 2PRF 1 REMARK HELIX
REVDAT 3 24-FEB-09 2PRF 1 VERSN
REVDAT 2 01-APR-03 2PRF 1 JRNL
REVDAT 1 31-MAY-94 2PRF 0
JRNL AUTH V.K.VINSON,S.J.ARCHER,E.E.LATTMAN,T.D.POLLARD,D.A.TORCHIA
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA
JRNL TITL 2 PROFILIN-I.
JRNL REF J.CELL BIOL. V. 122 1277 1993
JRNL REFN ISSN 0021-9525
JRNL PMID 8397216
JRNL DOI 10.1083/JCB.122.6.1277
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.ARCHER,V.K.VINSON,T.D.POLLARD,D.A.TORCHIA
REMARK 1 TITL SECONDARY STRUCTURE AND TOPOLOGY OF ACANTHAMOEBA PROFILIN I
REMARK 1 TITL 2 AS DETERMINED BY HETERONUCLEAR NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 32 6680 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 2PRF 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_1000178496.
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 : 19
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 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 ASP A 7 48.29 -90.46
REMARK 500 1 THR A 8 -96.67 -165.85
REMARK 500 1 ASN A 9 -68.97 -101.46
REMARK 500 1 LEU A 10 -43.37 -23.05
REMARK 500 1 THR A 13 41.28 163.62
REMARK 500 1 ALA A 15 -34.10 153.97
REMARK 500 1 LEU A 24 121.00 60.78
REMARK 500 1 ASP A 25 39.30 -78.03
REMARK 500 1 ASN A 27 -172.82 162.79
REMARK 500 1 TRP A 29 -54.67 -142.80
REMARK 500 1 ALA A 30 134.87 -177.00
REMARK 500 1 ALA A 33 -164.40 -169.81
REMARK 500 1 ASN A 50 -69.51 -101.10
REMARK 500 1 ALA A 52 22.42 49.06
REMARK 500 1 SER A 58 -42.72 82.52
REMARK 500 1 LEU A 62 -147.20 -137.00
REMARK 500 1 THR A 69 109.08 63.85
REMARK 500 1 ASP A 73 -31.65 178.08
REMARK 500 1 ASP A 74 -93.23 -66.25
REMARK 500 1 ARG A 75 -53.86 -138.56
REMARK 500 1 ILE A 77 84.14 -152.90
REMARK 500 1 SER A 83 -60.41 -125.94
REMARK 500 1 THR A 91 -92.51 -147.09
REMARK 500 1 ASN A 101 -166.51 -102.81
REMARK 500 1 ASP A 118 -29.64 -38.52
REMARK 500 2 GLN A 3 -82.21 -32.57
REMARK 500 2 ASP A 7 53.57 -91.37
REMARK 500 2 THR A 8 -92.69 -171.11
REMARK 500 2 ASN A 9 -88.34 -101.21
REMARK 500 2 LEU A 10 -44.26 -21.13
REMARK 500 2 THR A 13 37.87 157.83
REMARK 500 2 ALA A 15 -25.63 158.92
REMARK 500 2 ALA A 19 166.48 179.54
REMARK 500 2 ASN A 27 -45.70 -171.69
REMARK 500 2 ALA A 33 -16.64 87.12
REMARK 500 2 PHE A 35 126.15 61.49
REMARK 500 2 PRO A 39 -73.96 -54.91
REMARK 500 2 ALA A 40 81.17 -154.00
REMARK 500 2 PRO A 54 -74.05 -68.45
REMARK 500 2 ALA A 57 -91.83 -86.18
REMARK 500 2 SER A 58 -76.57 -43.41
REMARK 500 2 LEU A 62 57.35 -107.59
REMARK 500 2 ASP A 73 -41.63 178.02
REMARK 500 2 ASP A 74 -81.33 -59.43
REMARK 500 2 ARG A 75 -48.81 -144.69
REMARK 500 2 ILE A 77 63.95 -163.13
REMARK 500 2 THR A 91 -60.19 -103.25
REMARK 500 2 SER A 92 -66.34 -168.47
REMARK 500 2 GLU A 102 31.40 39.06
REMARK 500 2 GLN A 123 -75.40 -92.77
REMARK 500
REMARK 500 THIS ENTRY HAS 490 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2PRF A 1 125 UNP P07763 PRO1_ACACA 1 125
SEQRES 1 A 125 SER TRP GLN THR TYR VAL ASP THR ASN LEU VAL GLY THR
SEQRES 2 A 125 GLY ALA VAL THR GLN ALA ALA ILE LEU GLY LEU ASP GLY
SEQRES 3 A 125 ASN THR TRP ALA THR SER ALA GLY PHE ALA VAL THR PRO
SEQRES 4 A 125 ALA GLN GLY GLN THR LEU ALA SER ALA PHE ASN ASN ALA
SEQRES 5 A 125 ASP PRO ILE ARG ALA SER GLY PHE ASP LEU ALA GLY VAL
SEQRES 6 A 125 HIS TYR VAL THR LEU ARG ALA ASP ASP ARG SER ILE TYR
SEQRES 7 A 125 GLY LYS LYS GLY SER ALA GLY VAL ILE THR VAL LYS THR
SEQRES 8 A 125 SER LYS SER ILE LEU VAL GLY VAL TYR ASN GLU LYS ILE
SEQRES 9 A 125 GLN PRO GLY THR ALA ALA ASN VAL VAL GLU LYS LEU ALA
SEQRES 10 A 125 ASP TYR LEU ILE GLY GLN GLY PHE
HELIX 1 H1 GLN A 3 ASP A 7 1THIS HELIX MAY INCLUDE T8-V11 5
HELIX 2 H2 ALA A 40 PHE A 49 1D53-R56 FORM A HELICAL TURN 10
HELIX 3 H3 ALA A 109 ILE A 121 1 13
SHEET 1 S1 5 ALA A 30 ALA A 33 0
SHEET 2 S1 5 GLN A 18 LEU A 22 -1 O ALA A 19 N SER A 32
SHEET 3 S1 5 SER A 94 ASN A 101 -1 O VAL A 97 N ALA A 20
SHEET 4 S1 5 ALA A 84 THR A 91 -1 O ILE A 87 N GLY A 98
SHEET 5 S1 5 SER A 76 LYS A 81 -1 O GLY A 79 N VAL A 86
SHEET 1 S2 2 PHE A 60 LEU A 62 0
SHEET 2 S2 2 VAL A 65 VAL A 68 -1 N TYR A 67 O PHE A 60
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 - v 29 2 Bytes