Header list of 1mzt.pdb file
Complete list - 23 202 Bytes
HEADER VIRAL PROTEIN 09-OCT-02 1MZT
TITLE NMR STRUCTURE OF THE FD BACTERIOPHAGE PVIII COAT PROTEIN IN LIPID
TITLE 2 BILAYER MEMBRANES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR COAT PROTEIN PVIII;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FILAMENTOUS PHAGE CLONING VECTOR FD-TET
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE FD;
SOURCE 3 ORGANISM_TAXID: 10864
KEYWDS FD COAT PROTEIN, MEMBRANE-BOUND, PVIII, VIRAL PROTEIN
EXPDTA SOLID-STATE NMR
AUTHOR F.M.MARASSI,S.J.OPELLA
REVDAT 4 23-FEB-22 1MZT 1 REMARK
REVDAT 3 24-FEB-09 1MZT 1 VERSN
REVDAT 2 01-MAR-05 1MZT 1 JRNL
REVDAT 1 27-NOV-02 1MZT 0
JRNL AUTH F.M.MARASSI,S.J.OPELLA
JRNL TITL SIMULTANEOUS ASSIGNMENT AND STRUCTURE DETERMINATION OF A
JRNL TITL 2 MEMBRANE PROTEIN FROM NMR ORIENTATIONAL RESTRAINTS
JRNL REF PROTEIN SCI. V. 12 403 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 12592011
JRNL DOI 10.1110/PS.0211503
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.M.MARASSI,S.J.OPELLA
REMARK 1 TITL USING PISA PIES TO RESOLVE AMBIGUITIES IN ANGULAR
REMARK 1 TITL 2 CONSTRAINTS FROM PISEMA SPECTRA OF ALIGNED PROTEINS
REMARK 1 REF J.BIOMOL.NMR V. 23 239 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1019887612018
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CMXW 95, BACKTOR 2
REMARK 3 AUTHORS : CHEMAGNETICS (CMXW), MARASSI, OPELLA (BACKTOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATED FROM 40 CHEMICAL
REMARK 3 SHIFT AND 40 DIPOLAR COUPLING RESTRAINTS
REMARK 4
REMARK 4 1MZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017341.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 8 MG 15N-LABELED FD COAT
REMARK 210 PROTEIN, 64 MG POPC, 16 MG POPG,
REMARK 210 LIPID BILAYERS ORIENTED ON GLASS
REMARK 210 SLIDES
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H/15N PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : CMX
REMARK 210 SPECTROMETER MANUFACTURER : CHEMAGNETICS
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, BACKTOR 2
REMARK 210 METHOD USED : CALCULATION OF BOND ORIENTATIONS
REMARK 210 AND DIHEDRAL ANGLES FROM SOLID-
REMARK 210 STATE NMR RESTRAINTS, FOLLOWED
REMARK 210 BY BACK-CALCULATION OF NMR DATA
REMARK 210 FROM ORIENTED STRUCTURE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 6
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED FROM ONE UNIFORMLY AND FOUR
REMARK 210 SELECTIVELY 15N-LABELED SAMPLES.
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 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 PRO A 6
REMARK 465 THR A 46
REMARK 465 SER A 47
REMARK 465 LYS A 48
REMARK 465 ALA A 49
REMARK 465 SER A 50
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 VAL A 33 H ILE A 37 1.43
REMARK 500 O ALA A 25 H VAL A 29 1.48
REMARK 500 O GLY A 34 H GLY A 38 1.49
REMARK 500 O VAL A 30 H GLY A 34 1.50
REMARK 500 O SER A 17 CA TYR A 24 2.01
REMARK 500 O THR A 36 N LEU A 41 2.12
REMARK 500 O ILE A 37 CA LEU A 41 2.13
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 THR A 19 -81.76 -93.08
REMARK 500 GLU A 20 132.45 -37.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FDM RELATED DB: PDB
REMARK 900 FD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR PROVIDED COORDINATES FOR THE PROTEIN BACKBONE ONLY.
DBREF 1MZT 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 ALA A 7 THR A 19 1 13
HELIX 2 2 GLU A 20 PHE A 45 1 26
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
Complete list - 23 202 Bytes