Header list of 1fdm.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 28-MAY-97 1FDM
TITLE FD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FD MAJOR COAT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FD COAT PROTEIN;
COMPND 5 OTHER_DETAILS: IN SDS MICELLES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE FD;
SOURCE 3 ORGANISM_TAXID: 10864
KEYWDS FD COAT PROTEIN, MEMBRANE PROTEIN, MICELLES, COAT PROTEIN, VIRAL
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.C.L.ALMEIDA,S.J.OPELLA
REVDAT 3 23-FEB-22 1FDM 1 REMARK
REVDAT 2 24-FEB-09 1FDM 1 VERSN
REVDAT 1 17-SEP-97 1FDM 0
JRNL AUTH F.C.ALMEIDA,S.J.OPELLA
JRNL TITL FD COAT PROTEIN STRUCTURE IN MEMBRANE ENVIRONMENTS:
JRNL TITL 2 STRUCTURAL DYNAMICS OF THE LOOP BETWEEN THE HYDROPHOBIC
JRNL TITL 3 TRANS-MEMBRANE HELIX AND THE AMPHIPATHIC IN-PLANE HELIX.
JRNL REF J.MOL.BIOL. V. 270 481 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9237913
JRNL DOI 10.1006/JMBI.1997.1114
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 PAPER CITED ON JRNL RECORDS ABOVE.
REMARK 4
REMARK 4 1FDM 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_1000173247.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-TOCSY-HNHA-D2O EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 220
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 10 LOWEST ENERGY FOR EACH FAMILY
REMARK 210 OF STRUCTURE
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 5 153.49 59.13
REMARK 500 1 SER A 13 -74.83 -80.17
REMARK 500 1 ALA A 16 -82.94 -50.52
REMARK 500 1 ALA A 18 -92.47 -125.90
REMARK 500 1 THR A 19 -58.49 -176.31
REMARK 500 1 GLU A 20 -104.10 -52.06
REMARK 500 1 TYR A 24 38.10 178.08
REMARK 500 1 TRP A 26 -30.28 -35.84
REMARK 500 1 ALA A 27 -68.60 -130.83
REMARK 500 1 LYS A 40 -76.98 -73.90
REMARK 500 1 PHE A 45 32.45 -175.51
REMARK 500 1 SER A 47 -89.63 161.00
REMARK 500 1 ALA A 49 27.22 -168.48
REMARK 500 2 PRO A 6 -77.16 -78.66
REMARK 500 2 SER A 13 -77.04 -74.91
REMARK 500 2 ALA A 16 -88.02 -46.42
REMARK 500 2 ALA A 18 -90.12 -111.81
REMARK 500 2 THR A 19 -55.22 176.43
REMARK 500 2 GLU A 20 -108.43 -57.40
REMARK 500 2 ALA A 25 -35.28 -131.07
REMARK 500 2 SER A 47 -153.85 -97.79
REMARK 500 3 PRO A 6 41.22 -80.37
REMARK 500 3 ALA A 7 -69.40 -153.40
REMARK 500 3 ALA A 9 -80.22 -55.29
REMARK 500 3 SER A 13 -76.68 -69.34
REMARK 500 3 SER A 17 45.07 -83.01
REMARK 500 3 ALA A 18 34.86 37.55
REMARK 500 3 GLU A 20 -64.46 -176.89
REMARK 500 3 TYR A 24 39.36 32.28
REMARK 500 3 ALA A 27 -64.23 -133.63
REMARK 500 3 LYS A 40 -70.66 -79.10
REMARK 500 3 SER A 47 -60.55 -109.87
REMARK 500 4 GLU A 2 -179.36 57.40
REMARK 500 4 ASP A 4 84.01 -166.75
REMARK 500 4 SER A 13 -76.19 -76.27
REMARK 500 4 ALA A 16 -82.49 -48.93
REMARK 500 4 ALA A 18 -90.80 -107.42
REMARK 500 4 THR A 19 -53.20 175.34
REMARK 500 4 GLU A 20 -100.47 -49.56
REMARK 500 4 TYR A 24 51.02 37.25
REMARK 500 4 TRP A 26 -27.90 -37.35
REMARK 500 4 ALA A 27 -65.92 -129.49
REMARK 500 4 THR A 46 40.59 178.09
REMARK 500 4 SER A 47 -72.32 -166.71
REMARK 500 4 ALA A 49 -75.59 -126.50
REMARK 500 5 GLU A 2 -164.65 59.92
REMARK 500 5 ASP A 4 96.01 50.91
REMARK 500 5 ASP A 5 100.82 -160.29
REMARK 500 5 ALA A 7 -26.48 172.38
REMARK 500 5 LYS A 8 -33.07 -39.64
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FDM A 1 50 UNP P69539 COATB_BPFD 24 73
SEQRES 1 A 50 ALA GLU GLY ASP ASP PRO ALA LYS ALA ALA PHE ASP SER
SEQRES 2 A 50 LEU GLN ALA SER ALA THR GLU TYR ILE GLY TYR ALA TRP
SEQRES 3 A 50 ALA MET VAL VAL VAL ILE VAL GLY ALA THR ILE GLY ILE
SEQRES 4 A 50 LYS LEU PHE LYS LYS PHE THR SER LYS ALA SER
HELIX 1 1 LYS A 8 ALA A 16 1 9
HELIX 2 2 MET A 28 LYS A 43 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
MODEL 1
Complete list - b 23 2 Bytes