Header list of 1zn5.pdb file
Complete list - 2 20 Bytes
HEADER VIRUS 11-MAY-05 1ZN5
TITLE SOLID STATE NMR STRUCTURE OF THE LOW-TEMPERATURE FORM OF THE PF1 MAJOR
TITLE 2 COAT PROTEIN IN MAGNETICALLY ALIGNED BACTERIOPHAGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAT PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAJOR COAT PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PHAGE PF1;
SOURCE 3 ORGANISM_TAXID: 10871;
SOURCE 4 OTHER_DETAILS: HOST BACTERIA IS PSEUDOMONAS AERUGINOSA.
KEYWDS ALPHA-HELIX, VIRION, ORIENTATIONAL CONSTRAINTS, HELICAL VIRUS, VIRUS
EXPDTA SOLID-STATE NMR
NUMMDL 27
AUTHOR D.S.THIRIOT,A.A.NEVZOROV,S.J.OPELLA
REVDAT 3 02-MAR-22 1ZN5 1 REMARK
REVDAT 2 24-FEB-09 1ZN5 1 VERSN
REVDAT 1 17-MAY-05 1ZN5 0
JRNL AUTH D.S.THIRIOT,A.A.NEVZOROV,S.J.OPELLA
JRNL TITL STRUCTURAL BASIS OF THE TEMPERATURE TRANSITION OF PF1
JRNL TITL 2 BACTERIOPHAGE.
JRNL REF PROTEIN SCI. V. 14 1064 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15741342
JRNL DOI 10.1110/PS.041220305
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, SCWRL
REMARK 3 AUTHORS : BOWER ET AL. (SCWRL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS IS A BACKBONE ONLY MODEL. CONSTANT PEPTIDE PLANE
REMARK 3 GEOMETRY WAS ASSUMED. TORSION ANGLES PHI AND PSI WERE
REMARK 3 ALLOWED TO VARY WITHIN 10-20 DEGREES RELATIVE TO PHI=-65,
REMARK 3 PSI=-40. RADIAL AND ANGULAR POSITIONING OF SUBUNITS IN A
REMARK 3 MANNER SIMILAR TO AND IN COMPARISON WITH STRUCTURE 1PJF,
REMARK 3 WHICH INVOLVED MINIMIZATION AGAINST PUBLISHED NEUTRON
REMARK 3 DIFFRACTION DISTANCE CONSTRAINTS AND ENERGY MINIMIZATION
REMARK 3 WITH SIDECHAINS USING THE PROGRAM SCWRL.
REMARK 4
REMARK 4 1ZN5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032916.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 273
REMARK 210 PH : 8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : APPROXIMATELY 50 MG/ML PF1
REMARK 210 BACTERIOPHAGE, U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000.1, MATLAB SCRIPTS 1.0
REMARK 210 METHOD USED : DETERMINATION OF TORSION ANGLES
REMARK 210 BETWEEN ADJACENT RESIDUES USING
REMARK 210 SOLID-STATE NMR FREQUENCIES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURAL FITTING OF PISEMA
REMARK 210 SPECTRUM WITH FIXED PEPTIDE
REMARK 210 PLANE GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: MODEL 1 IS THE BASIC SOLID-STATE NMR STRUCTURE (NO
REMARK 210 SIDECHAINS), WHILE MODELS 2-27 ARE IDENTICAL TRANSLATED
REMARK 210 AND ROTATED COPIES OF MODEL 1 INCLUDED TO PRESENT THE
REMARK 210 MODEL OF THE WHOLE BACTERIOPHAGE ASSEMBLY.
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 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 MET A 42 H ALA A 46 1.54
REMARK 500 O ASP A 4 N SER A 6 1.85
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 THR A 5 -47.12 -0.05
REMARK 500 1 SER A 6 -70.01 -59.61
REMARK 500 2 THR A 5 -47.18 -0.02
REMARK 500 2 SER A 6 -70.05 -59.53
REMARK 500 3 THR A 5 -47.12 -0.05
REMARK 500 4 THR A 5 -47.10 -0.07
REMARK 500 4 SER A 6 -70.00 -59.61
REMARK 500 5 THR A 5 -47.15 -0.04
REMARK 500 6 THR A 5 -47.13 -0.03
REMARK 500 7 THR A 5 -47.16 -0.04
REMARK 500 8 THR A 5 -47.09 -0.08
REMARK 500 8 SER A 6 -70.01 -59.62
REMARK 500 9 THR A 5 -47.13 -0.09
REMARK 500 9 SER A 6 -70.03 -59.59
REMARK 500 10 THR A 5 -47.13 -0.02
REMARK 500 11 THR A 5 -47.15 -0.05
REMARK 500 12 THR A 5 -47.17 -0.07
REMARK 500 13 THR A 5 -47.09 -0.11
REMARK 500 14 THR A 5 -47.13 -0.07
REMARK 500 14 SER A 6 -70.02 -59.56
REMARK 500 15 THR A 5 -47.11 -0.11
REMARK 500 15 SER A 6 -70.02 -59.55
REMARK 500 16 THR A 5 -47.12 -0.05
REMARK 500 17 THR A 5 -47.15 -0.04
REMARK 500 17 SER A 6 -70.00 -59.59
REMARK 500 18 THR A 5 -47.18 -0.03
REMARK 500 19 THR A 5 -47.06 -0.11
REMARK 500 20 THR A 5 -47.17 -0.03
REMARK 500 21 THR A 5 -47.18 -0.04
REMARK 500 22 THR A 5 -47.09 -0.09
REMARK 500 23 THR A 5 -47.15 -0.04
REMARK 500 23 SER A 6 -70.05 -59.57
REMARK 500 24 THR A 5 -47.17 -0.09
REMARK 500 24 SER A 6 -70.01 -59.56
REMARK 500 25 THR A 5 -47.14 -0.07
REMARK 500 25 SER A 6 -70.01 -59.56
REMARK 500 26 THR A 5 -47.16 -0.06
REMARK 500 27 THR A 5 -47.08 -0.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PJF RELATED DB: PDB
REMARK 900 SOLID STATE NMR STRUCTURE OF THE HIGH TEMPERATURE (303 K) FORM OF
REMARK 900 THE PF1 MAJOR COAT PROTEIN IN MAGNETICALLY ALIGNED BACTERIOPHAGE
DBREF 1ZN5 A 1 46 UNP P03621 COATB_BPPF1 37 82
SEQRES 1 A 46 GLY VAL ILE ASP THR SER ALA VAL GLU SER ALA ILE THR
SEQRES 2 A 46 ASP GLY GLN GLY ASP MET LYS ALA ILE GLY GLY TYR ILE
SEQRES 3 A 46 VAL GLY ALA LEU VAL ILE LEU ALA VAL ALA GLY LEU ILE
SEQRES 4 A 46 TYR SER MET LEU ARG LYS ALA
HELIX 1 1 ASP A 4 ALA A 46 1 43
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 - 2 20 Bytes