Header list of 1z1z.pdb file
Complete list - 2 20 Bytes
HEADER VIRAL PROTEIN 07-MAR-05 1Z1Z TITLE NMR STRUCTURE OF THE GPU TAIL PROTEIN FROM LAMBDA BACTERIOPHAGE COMPND MOL_ID: 1; COMPND 2 MOLECULE: MINOR TAIL PROTEIN U; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA; SOURCE 3 ORGANISM_TAXID: 10710; SOURCE 4 GENE: GPU; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B; SOURCE 10 OTHER_DETAILS: THE FULL GPU GENE WAS INSERTED INTO THE NDEI AND SOURCE 11 BAMHI SITES OF PET15B RESULTING IN AN AMINO TERMINALLY HEXAHISTIDINE SOURCE 12 TAGGED FUSION PROTEIN WITH AN INTERVENING THROMBIN PROTEASE CLEAVAGE SOURCE 13 SITE KEYWDS MIXED ALPHA-BETA, TAIL PROTEIN, BACTERIOPHAGE, VIRAL PROTEIN EXPDTA SOLUTION NMR AUTHOR L.EDMONDS,K.MAXWELL,A.DAVIDSON,L.W.DONALDSON REVDAT 4 02-MAR-22 1Z1Z 1 REMARK REVDAT 3 24-FEB-09 1Z1Z 1 VERSN REVDAT 2 08-JUL-08 1Z1Z 1 JRNL REVDAT 1 18-APR-06 1Z1Z 0 JRNL AUTH L.EDMONDS,A.LIU,J.J.KWAN,A.AVANESSY,M.CARACOGLIA,I.YANG, JRNL AUTH 2 K.L.MAXWELL,J.RUBENSTEIN,A.R.DAVIDSON,L.W.DONALDSON JRNL TITL THE NMR STRUCTURE OF THE GPU TAIL-TERMINATOR PROTEIN FROM JRNL TITL 2 BACTERIOPHAGE LAMBDA: IDENTIFICATION OF SITES CONTRIBUTING JRNL TITL 3 TO MG(II)-MEDIATED OLIGOMERIZATION AND BIOLOGICAL FUNCTION. JRNL REF J.MOL.BIOL. V. 365 175 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17056065 JRNL DOI 10.1016/J.JMB.2006.09.068 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.EDMONDS,R.T.THIRUMOORTHY,A.LIU,A.DAVIDSON,L.W.DONALDSON REMARK 1 TITL NMR ASSIGNMENT OF THE GPU TAIL PROTEIN FROM LAMBDA REMARK 1 TITL 2 BACTERIOPHAGE REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, XPLOR-NIH 2.9.9 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE REMARK 3 (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1180 NOE DISTANCE RESTRAINTS (876 REMARK 3 INTRAMOLECULAR, 505 SHORT-RANGE, 128 MEDIUM RANGE, 371 LONG- REMARK 3 RANGE), 42 PAIRS OF HYDROGEN BOND DISTANCE RESTRAINTS, 106 PAIRS REMARK 3 OF PHI/PSI DIHEDRAL ANGLE RESTRAINTS AND 41 AMIDE RESIDUAL REMARK 3 DIPOLAR COUPLING RESTRAINTS WERE INCORPORATED INTO THE STRUCTURE REMARK 3 CALCULATION. NOE CALIBRATION WAS PERFORMED WITH CANDID MODULE OF REMARK 3 CYANA. INITIALLY, 200 STRUCTURES WERE CALCUATED WITH XPLOR-NIH. REMARK 3 FROM THIS ENSEMBLE, 50 LOW-ENERGY STRUCTURE WERE REFINED IN REMARK 3 WATER USING THE XPLOR-NIH PROTOCOL BY C. SPRONK. THE TOP 20 REMARK 3 STRUCTURES BY ENERGY HAD A BACKBONE RMSD OF 0.96 +/- 0.16 A ON REMARK 3 THE SECONDARY STRUCTURE ELEMENTS. IN ADDITION TO RESIDUES 1-3 REMARK 3 AND 128-131 AT THE TERMINI, A LARGE LOOP SPANNING RESIDUES 45-60 REMARK 3 IS DISORDERED. REMARK 4 REMARK 4 1Z1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032196. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.8 REMARK 210 IONIC STRENGTH : 50 MM KCL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.9 MM GPU, U-15N,13C, 10 MM REMARK 210 TRIS-D11, PH 7.8, 50 MM REMARK 210 POTASSIUM CHLORIDE, 0.02% SODIUM REMARK 210 AZIDE, 10% D2O, 90% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED-AROMATIC_NOESY; 2D- REMARK 210 IPAP-15N_HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.2, CYANA 2.1.3 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HETERONUCLEAR TECHNIQUES 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 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 MET A 1 REMARK 465 MET A 131 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 ALA A 29 38.07 -94.94 REMARK 500 VAL A 30 -169.02 -106.56 REMARK 500 GLU A 51 97.51 48.83 REMARK 500 ASP A 112 18.65 -145.58 REMARK 500 ASP A 114 -74.00 -97.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IN0 RELATED DB: PDB REMARK 900 HOMOLOGOUS TERTIARY STRUCTURE DBREF 1Z1Z A 1 131 UNP P03732 VMTU_LAMBD 1 131 SEQRES 1 A 131 MET LYS HIS THR GLU LEU ARG ALA ALA VAL LEU ASP ALA SEQRES 2 A 131 LEU GLU LYS HIS ASP THR GLY ALA THR PHE PHE ASP GLY SEQRES 3 A 131 ARG PRO ALA VAL PHE ASP GLU ALA ASP PHE PRO ALA VAL SEQRES 4 A 131 ALA VAL TYR LEU THR GLY ALA GLU TYR THR GLY GLU GLU SEQRES 5 A 131 LEU ASP SER ASP THR TRP GLN ALA GLU LEU HIS ILE GLU SEQRES 6 A 131 VAL PHE LEU PRO ALA GLN VAL PRO ASP SER GLU LEU ASP SEQRES 7 A 131 ALA TRP MET GLU SER ARG ILE TYR PRO VAL MET SER ASP SEQRES 8 A 131 ILE PRO ALA LEU SER ASP LEU ILE THR SER MET VAL ALA SEQRES 9 A 131 SER GLY TYR ASP TYR ARG ARG ASP ASP ASP ALA GLY LEU SEQRES 10 A 131 TRP SER SER ALA ASP LEU THR TYR VAL ILE THR TYR GLU SEQRES 11 A 131 MET HELIX 1 1 THR A 4 ASP A 18 1 15 HELIX 2 2 ASP A 32 PHE A 36 5 5 HELIX 3 3 PRO A 73 ILE A 92 1 20 HELIX 4 4 ILE A 92 ILE A 99 1 8 SHEET 1 A 5 PHE A 23 PHE A 24 0 SHEET 2 A 5 ALA A 38 LEU A 43 1 O VAL A 41 N PHE A 24 SHEET 3 A 5 GLU A 61 LEU A 68 -1 O PHE A 67 N ALA A 38 SHEET 4 A 5 SER A 119 VAL A 126 -1 O SER A 119 N LEU A 68 SHEET 5 A 5 TYR A 107 ARG A 110 -1 N ASP A 108 O ASP A 122 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 - 2 20 Bytes