Header list of 1pux.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 25-JUN-03 1PUX TITLE NMR SOLUTION STRUCTURE OF BEF3-ACTIVATED SPO0F, 20 CONFORMERS COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPORULATION INITIATION PHOSPHOTRANSFERASE F; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: STAGE 0 SPORULATION PROTEIN F; COMPND 5 EC: 2.7.-.-; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 GENE: SPO0F; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) WITH PACYC; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A (NOVAGEN) KEYWDS SPORULATION, (BETA/ALPHA)5 BARREL, RESPONSE REGULATOR, PHOSPHORELAY, KEYWDS 2 BERYLLOFLUORIDE, TWO-COMPONENT SYSTEMS, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.K.GARDINO,B.F.VOLKMAN,H.S.CHO,S.Y.LEE,D.E.WEMMER,D.KERN REVDAT 3 02-MAR-22 1PUX 1 REMARK REVDAT 2 24-FEB-09 1PUX 1 VERSN REVDAT 1 19-AUG-03 1PUX 0 JRNL AUTH A.K.GARDINO,B.F.VOLKMAN,H.S.CHO,S.Y.LEE,D.E.WEMMER,D.KERN JRNL TITL THE NMR SOLUTION STRUCTURE OF BEF(3)(-)-ACTIVATED SPO0F JRNL TITL 2 REVEALS THE CONFORMATIONAL SWITCH IN A PHOSPHORELAY SYSTEM. JRNL REF J.MOL.BIOL. V. 331 245 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12875849 JRNL DOI 10.1016/S0022-2836(03)00733-2 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUNTERT, P (DYANA), GUNTERT, P (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE BASED ON A TOTAL OF 1,835 REMARK 3 DISTANCE CONSTRAINTS (OBTAINED FROM 4,221 NOE CROSSPEAKS), REMARK 3 INCLUDING 602 INTRARESIDUAL, 504 SHORT-RANGE, 310 MEDIUM-RANGE, REMARK 3 AND 383 LONG-RANGE CONSTRAINTS AS WELL AS 165 DIHEDRAL ANGLE REMARK 3 RESTRAINTS FOR A TOTAL OF 2,000 RESTRAINTS. DYANA 1.5 ANNEAL REMARK 3 COMMAND (20000) STEPS WAS USED TO GENERATE 60 CONFORMERS. 20 REMARK 3 LOWEST TARGET FUNCTION STRUCTURES WERE ANALYZED. REMARK 4 REMARK 4 1PUX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000019588. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.85 REMARK 210 IONIC STRENGTH : 50 MM MGCL2, 6 MM BECL2, 60 MM REMARK 210 NAF REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : UNIFORM LABELING WITH 15N AND REMARK 210 13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.12 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 O ASP A 49 HE ARG A 77 1.46 REMARK 500 O ASN A 20 H ASN A 24 1.50 REMARK 500 O GLU A 64 H ARG A 68 1.55 REMARK 500 O VAL A 115 H LEU A 119 1.57 REMARK 500 O LEU A 87 H GLN A 91 1.58 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 MET A 2 -167.84 -128.51 REMARK 500 1 GLU A 4 140.70 -179.28 REMARK 500 1 ASP A 10 178.72 49.64 REMARK 500 1 TYR A 13 28.55 -153.47 REMARK 500 1 ASN A 35 -176.37 164.89 REMARK 500 1 ARG A 47 61.77 23.83 REMARK 500 1 LYS A 56 106.01 -44.05 REMARK 500 1 MET A 60 90.74 73.80 REMARK 500 1 ASP A 61 170.70 -49.09 REMARK 500 1 THR A 82 149.84 -177.80 REMARK 500 1 TYR A 84 57.46 -68.69 REMARK 500 1 GLU A 86 45.31 -105.54 REMARK 500 1 THR A 100 -165.97 -172.98 REMARK 500 1 LYS A 104 -61.14 -22.42 REMARK 500 2 MET A 2 -165.47 -111.87 REMARK 500 2 ASN A 3 101.81 -169.27 REMARK 500 2 GLU A 4 141.19 -179.23 REMARK 500 2 ASP A 10 -177.17 48.34 REMARK 500 2 TYR A 13 28.05 -158.44 REMARK 500 2 ASN A 35 -176.90 160.13 REMARK 500 2 ARG A 47 60.38 24.93 REMARK 500 2 MET A 60 122.47 69.81 REMARK 500 2 THR A 82 143.57 -171.16 REMARK 500 2 GLU A 86 47.43 -98.68 REMARK 500 2 THR A 100 -164.21 -167.34 REMARK 500 2 LYS A 104 -58.80 -29.95 REMARK 500 2 LYS A 122 99.50 -41.48 REMARK 500 3 MET A 2 -152.46 175.79 REMARK 500 3 ASN A 3 147.82 84.08 REMARK 500 3 GLU A 4 156.71 170.39 REMARK 500 3 ASP A 10 -168.05 43.45 REMARK 500 3 TYR A 13 27.86 -158.69 REMARK 500 3 ASN A 35 -174.08 159.94 REMARK 500 3 ARG A 47 60.50 25.78 REMARK 500 3 LYS A 56 105.12 -53.57 REMARK 500 3 MET A 60 95.53 49.40 REMARK 500 3 ASP A 61 173.97 -49.20 REMARK 500 3 THR A 82 143.51 -175.28 REMARK 500 3 TYR A 84 49.32 -78.07 REMARK 500 3 LYS A 104 -59.61 -25.20 REMARK 500 4 GLU A 4 156.71 166.92 REMARK 500 4 ASP A 10 -164.63 42.12 REMARK 500 4 TYR A 13 28.73 -162.72 REMARK 500 4 ASN A 35 -175.89 170.13 REMARK 500 4 ARG A 47 60.20 25.90 REMARK 500 4 LEU A 50 118.63 -168.46 REMARK 500 4 MET A 60 112.98 68.75 REMARK 500 4 THR A 82 148.46 -178.26 REMARK 500 4 TYR A 84 39.32 -83.11 REMARK 500 4 GLU A 86 53.15 -103.81 REMARK 500 REMARK 500 THIS ENTRY HAS 246 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FSP RELATED DB: PDB REMARK 900 INACTIVE SPO0F, 20 CONFORMERS REMARK 900 RELATED ID: 2FSP RELATED DB: PDB REMARK 900 INACTIVE SPO0F, MINIMIZED MEAN DBREF 1PUX A 1 124 UNP P06628 SP0F_BACSU 1 124 SEQRES 1 A 124 MET MET ASN GLU LYS ILE LEU ILE VAL ASP ASP GLN TYR SEQRES 2 A 124 GLY ILE ARG ILE LEU LEU ASN GLU VAL PHE ASN LYS GLU SEQRES 3 A 124 GLY TYR GLN THR PHE GLN ALA ALA ASN GLY LEU GLN ALA SEQRES 4 A 124 LEU ASP ILE VAL THR LYS GLU ARG PRO ASP LEU VAL LEU SEQRES 5 A 124 LEU ASP MET LYS ILE PRO GLY MET ASP GLY ILE GLU ILE SEQRES 6 A 124 LEU LYS ARG MET LYS VAL ILE ASP GLU ASN ILE ARG VAL SEQRES 7 A 124 ILE ILE MET THR ALA TYR GLY GLU LEU ASP MET ILE GLN SEQRES 8 A 124 GLU SER LYS GLU LEU GLY ALA LEU THR HIS PHE ALA LYS SEQRES 9 A 124 PRO PHE ASP ILE ASP GLU ILE ARG ASP ALA VAL LYS LYS SEQRES 10 A 124 TYR LEU PRO LEU LYS SER ASN HELIX 1 1 ILE A 15 GLU A 26 1 12 HELIX 2 2 GLY A 36 ARG A 47 1 12 HELIX 3 3 GLY A 62 ILE A 72 1 11 HELIX 4 4 LEU A 87 LEU A 96 1 10 HELIX 5 5 ILE A 108 TYR A 118 1 11 SHEET 1 A 5 GLN A 29 ALA A 33 0 SHEET 2 A 5 LYS A 5 VAL A 9 1 N ILE A 8 O PHE A 31 SHEET 3 A 5 LEU A 50 LEU A 53 1 O LEU A 50 N LEU A 7 SHEET 4 A 5 ARG A 77 MET A 81 1 O ILE A 79 N LEU A 53 SHEET 5 A 5 THR A 100 PHE A 102 1 N PHE A 102 O ILE A 80 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 - r 2 2 Bytes