Header list of 1nh4.pdb file
Complete list - b 23 2 Bytes
HEADER VIRUS 18-DEC-02 1NH4
TITLE STRUCTURE OF THE COAT PROTEIN IN FD FILAMENTOUS BACTERIOPHAGE
TITLE 2 PARTICLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR COAT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE FD;
SOURCE 3 ORGANISM_TAXID: 10864;
SOURCE 4 STRAIN: FD
KEYWDS ALPHA HELIX, HELICAL VIRUS, VIRUS
EXPDTA SOLID-STATE NMR
NUMMDL 20
AUTHOR A.C.ZERI,M.F.MESLEH,A.A.NEVZOROV,S.J.OPELLA
REVDAT 4 23-FEB-22 1NH4 1 REMARK
REVDAT 3 24-FEB-09 1NH4 1 VERSN
REVDAT 2 18-NOV-03 1NH4 1 JRNL
REVDAT 1 06-MAY-03 1NH4 0
JRNL AUTH A.C.ZERI,M.F.MESLEH,A.A.NEVZOROV,S.J.OPELLA
JRNL TITL STRUCTURE OF THE COAT PROTEIN IN FD FILAMENTOUS
JRNL TITL 2 BACTERIOPHAGE PARTICLES DETERMINED BY SOLID-STATE NMR
JRNL TITL 3 SPECTROSCOPY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 6458 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12750469
JRNL DOI 10.1073/PNAS.1132059100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TECMAG LIBRA, SCWRL 2.1
REMARK 3 AUTHORS : TECMAG (TECMAG), DUNBRACK, R. (SCWRL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE FIRST FIVE N-TERMINAL RESIDUES OF THE COAT PROTEIN UNDERGO
REMARK 3 ISOTROPIC MOVEMENTS AT ROOM TEMPERATURE AND STRUCTURAL PARAMETERS
REMARK 3 CANNOT BE RESOLVED.
REMARK 4
REMARK 4 1NH4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017865.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 338
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 15N 50MG/ML VIRUS PARTICLES IN
REMARK 210 SUSPENSION, 5MM SODIUM BORATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 550 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97
REMARK 210 METHOD USED : SOLID-STATE NMR SPECTROSCOPY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THIS STRUCTURE WAS GENERATED FROM THE FIVE-FOLD SYMMETRY OF
REMARK 210 PDB ENTRY 1IFI, WHICH HAS THE SYMMETRY THAT RELATES
REMARK 210 ONE PENTAMER TO THE NEXT. THIS ONE HAS HAD THE SIDECHAINS
REMARK 210 ADDED USING THE PROGRAM SCWRL.
REMARK 210
REMARK 210 THE STRUCTURE WAS DETERMINED BY SOLID STATE NUCLEAR MAGNETIC
REMARK 210 RESONANCE USING THE WHOLE VIRUS IN SUSPENSION. A MODEL OF A
REMARK 210 SECTION OF THE VIRION CAPSID WAS BUILT WITH 20 COPIES OF THE
REMARK 210 PROTEIN ARRANGED IN AGREEMENT WITH PREVIOUS STUDIES BY FIBER
REMARK 210 DIFFRACTION (MARVIN ET AL., J. MOL. BIOL. 235, 260286 (1994)).
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 ASP A 5
REMARK 465 SER A 50
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 PRO A 6 N CB CG CD
REMARK 470 ALA A 49 C O CB
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 ILE A 32 HB THR A 36 1.06
REMARK 500 HG13 VAL A 33 HD12 ILE A 37 1.14
REMARK 500 O VAL A 33 HB ILE A 37 1.19
REMARK 500 O THR A 19 HG22 ILE A 22 1.22
REMARK 500 O VAL A 31 HB3 ALA A 35 1.34
REMARK 500 O ALA A 16 H GLU A 20 1.44
REMARK 500 O LEU A 41 H PHE A 45 1.45
REMARK 500 O LYS A 43 HB3 SER A 47 1.57
REMARK 500 O ALA A 35 HG12 ILE A 39 1.57
REMARK 500 O VAL A 29 H VAL A 33 1.58
REMARK 500 O ALA A 25 H VAL A 29 1.58
REMARK 500 O PHE A 42 HB THR A 46 1.59
REMARK 500 O GLN A 15 OG1 THR A 19 1.80
REMARK 500 O ILE A 32 CB THR A 36 2.00
REMARK 500 O VAL A 31 CB ALA A 35 2.11
REMARK 500 O LYS A 43 CB SER A 47 2.19
REMARK 500 O PHE A 42 CB THR A 46 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IFI RELATED DB: PDB
REMARK 900 FIBER DIFFRACTION STRUCTURE
REMARK 999
REMARK 999 AUTHORS INFORMED THAT THE SEQUENCE OF THEIR PROTEIN
REMARK 999 IS IDENTICAL TO RESIDUES 27-76 OF THE DATABASE REFERENCE
REMARK 999 SEQUENCE PROVIDED IN GENBANK ENTRY 8698956 BUT THAT THE
REMARK 999 SOURCE OF THEIR PROTEIN IS DIFFERENT. RESIDUE 21 WAS
REMARK 999 MUTATED FROM TYR TO MET.
DBREF 1NH4 A 1 50 UNP Q9T0Q9 Q9T0Q9_BPFD 1 50
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 MET 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 PRO A 6 ALA A 49 1 44
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