Header list of 1lvz.pdb file
Complete list - 27 20 Bytes
HEADER PEPTIDE BINDING PROTEIN 30-MAY-02 1LVZ TITLE METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA- TITLE 2 SUBUNIT OF TRANSDUCIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(T), ALPHA-1 SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: S2 PEPTIDE, RESIDUES 339-349; COMPND 5 SYNONYM: TRANSDUCIN ALPHA-1 CHAIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: GNAT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: GEV-S2 KEYWDS ALPHA HELIX, RHODOPSIN-TRANSDUCIN COMPLEX, PEPTIDE BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.W.KOENIG,G.KONTAXIS,D.C.MITCHELL,J.M.LOUIS,B.J.LITMAN,A.BAX REVDAT 3 27-OCT-21 1LVZ 1 REMARK SEQADV REVDAT 2 24-FEB-09 1LVZ 1 VERSN REVDAT 1 11-SEP-02 1LVZ 0 JRNL AUTH B.W.KOENIG,G.KONTAXIS,D.C.MITCHELL,J.M.LOUIS,B.J.LITMAN, JRNL AUTH 2 A.BAX JRNL TITL STRUCTURE AND ORIENTATION OF A G PROTEIN FRAGMENT IN THE JRNL TITL 2 RECEPTOR BOUND STATE FROM RESIDUAL DIPOLAR COUPLINGS. JRNL REF J.MOL.BIOL. V. 322 441 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 12217702 JRNL DOI 10.1016/S0022-2836(02)00745-3 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1, X-PLOR NIH REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), A.T. BRUNGER, N. TJANDRA, C.D. REMARK 3 SCHWIETERS, J. KUSZEWSKI, G.M. CLORE (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 121 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 12 NOE-DERIVED DIHEDRAL ANGLE RESTRAINTS, REMARK 3 AND 38 RESIDUAL DIPOLAR COUPLINGS REMARK 4 REMARK 4 1LVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016329. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 6.6 REMARK 210 IONIC STRENGTH : 10 MM HEPES, 20 MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.6MM S2 PEPTIDE U-15N, 0.063MM REMARK 210 RHODOPSIN AS PART OF INTACT DISK REMARK 210 MEMBRANES FROM BOVINE RETINA; REMARK 210 BUFFER: 10 MM HEPES, 20MM KCL, REMARK 210 0.05MM DTPA; 2.6MM S2 PEPTIDE U- REMARK 210 15N, 13C, 0.063MM RHODOPSIN AS REMARK 210 PART OF INTACT DISK MEMBRANES REMARK 210 FROM BOVINE RETINA; BUFFER: 10 REMARK 210 MM HEPES, 20MM KCL, 0.05MM DTPA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D 1H-15N HSQC (W/O 1H REMARK 210 DECOUPLING); 2D 1H-13C CT-HSQC REMARK 210 (W/O 1H DECOUPLING) REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR NIH REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: SAMPLE WAS STUDIED IN DARK ADAPTED STATE AND AFTER PHOTO REMARK 210 ACTIVATION OF RHODOPSIN BY ILLUMINATING THE SAMPLE FOR 60S WITH REMARK 210 A FOCUSSED MICROSCOPE LIGHT, CHEMICAL SHIFTS OF S2 PEPTIDE ARE REMARK 210 IDENTICAL IN BOTH STATES, TRNOES AND TRDCS ARE DIFFERENCE VALUES REMARK 210 BETWEEN THE DARK AND LIGHT-ACTIVATED STATES. ORIENTATION OF THE REMARK 210 BOUND PEPTIDE RELATIVE TO THE MEMBRANE NORMAL WAS DETERMINED REMARK 210 FROM RESIDUAL DIPOLAR COUPLINGS. THE MEMBRANE NORMAL THAT REMARK 210 BELONGS TO MODEL 1 RUNS PARALLEL TO THE Y-AXIS OF THE COORDINATE REMARK 210 FRAME IN WHICH THE DEPOSITED S2 PEPTIDE COORDINATES ARE REMARK 210 SPECIFIED. 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: 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 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5376 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT VALUES OF THE SAME TRANSDUCIN PEPTIDE DBREF 1LVZ A 1 11 UNP P04695 GNAT1_BOVIN 339 349 SEQADV 1LVZ ARG A 2 UNP P04695 LYS 340 ENGINEERED MUTATION SEQADV 1LVZ SER A 8 UNP P04695 CYS 346 ENGINEERED MUTATION SEQRES 1 A 11 ILE ARG GLU ASN LEU LYS ASP SER GLY LEU PHE HELIX 1 1 ILE A 1 SER A 8 1 8 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 - 27 20 Bytes