Header list of 1p6q.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 30-APR-03 1P6Q TITLE NMR STRUCTURE OF THE RESPONSE REGULATOR CHEY2 FROM SINORHIZOBIUM TITLE 2 MELILOTI, COMPLEXED WITH MG++ COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHEY2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI; SOURCE 3 ORGANISM_TAXID: 382; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ER2566; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTYB1 KEYWDS CHEY2, CHEMOTAXIS, SINORHIZOBIUM MELILOTI, SIGNAL TRANSDUCTION, KEYWDS 2 RESPONSE REGULATOR, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, KEYWDS 3 STRUCTURAL GENOMICS, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR H.RIEPL,B.SCHARF,T.MAURER,R.SCHMITT,H.R.KALBITZER,STRUCTURAL AUTHOR 2 PROTEOMICS IN EUROPE (SPINE) REVDAT 3 23-FEB-22 1P6Q 1 REMARK REVDAT 2 24-FEB-09 1P6Q 1 VERSN REVDAT 1 15-JUN-04 1P6Q 0 JRNL AUTH H.RIEPL,B.SCHARF,R.SCHMITT,H.R.KALBITZER,T.MAURER JRNL TITL SOLUTION STRUCTURES OF THE INACTIVE AND BEF3-ACTIVATED JRNL TITL 2 RESPONSE REGULATOR CHEY2. JRNL REF J.MOL.BIOL. V. 338 287 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15066432 JRNL DOI 10.1016/J.JMB.2004.02.054 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, DYANA 1.5 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1P6Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-03. REMARK 100 THE DEPOSITION ID IS D_1000019076. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.83 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM CHEY2, 1MM TRIS-HCL, 5MM REMARK 210 MGCL2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNCA; HNCO; REMARK 210 HN(CO)CA; CBCA(CO)CA; HBHA(CO)NH; REMARK 210 HCCH-TOCSY; CC(CO)NH REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 2.7.9, DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 250 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: TOTAL NUMBER OF NOES USED FOR THE CALCULATION: 1598, REMARK 210 NUMBER OF INTRA-RESIDUE NOES USED FOR THE CALCULATION: 796, REMARK 210 NUMBER OF SEQUENTIAL NOES USED FOR THE CALCULATION: 437, REMARK 210 NUMBER OF MEDIUM RANGE NOES USED FOR THE CALCULATION: 179, REMARK 210 NUMBER OF LONG RANGE (I,J, J > I+4) NOES USED FOR THE CALCULATION: REMARK 210 186, REMARK 210 NUMBER OF DIHEDRAL ANGLES RESTRAINTS USED FOR THE CALCULATION: 52, REMARK 210 NUMBER OF HYDROGEN BOND RESTRAINTS USED FOR THE CALCULATION: 5, REMARK 210 REMARK 210 MINIMAL TARGET FUNCTION WAS 2.80, REMARK 210 MEAN TARGET FUNCTION OF 16 STRUCTURES WAS 3.00 (+-0.4), REMARK 210 THE NUMBER OF NOE VIOLATIONS > 0.02 NM WAS 3 (+-1), REMARK 210 THE NUMBER OF NOE VIOLATIONS > 0.03 NM WAS 0, REMARK 210 THE NUMBER OF DIHEDRAL ANGLES VIOLATIONS > 10 DEGREES WAS 0, REMARK 210 RMSDS BACK BONE (6-124): 0.042 (+-0.015) NM, REMARK 210 RMSDS ALL HEAVY ATOMS (6-124): 0.098 (+-0.016)NM 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 HE2 HIS A 52 HG1 THR A 79 0.80 REMARK 500 O ASP A 39 H GLY A 43 1.38 REMARK 500 O LYS A 8 H HIS A 53 1.43 REMARK 500 HE2 HIS A 52 OG1 THR A 79 1.44 REMARK 500 O VAL A 55 H ILE A 85 1.49 REMARK 500 O LEU A 21 H ALA A 25 1.58 REMARK 500 O VAL A 16 H LEU A 20 1.59 REMARK 500 O VAL A 9 O GLN A 33 2.18 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 LYS A 6 27.24 40.17 REMARK 500 1 PHE A 31 -100.55 -19.10 REMARK 500 1 LYS A 32 -56.49 -162.22 REMARK 500 1 HIS A 53 14.34 -147.20 REMARK 500 1 ASN A 60 -81.67 -57.33 REMARK 500 1 MET A 61 49.81 -159.96 REMARK 500 1 ALA A 89 38.59 -78.72 REMARK 500 1 GLN A 90 -59.18 -125.10 REMARK 500 1 ASN A 106 126.46 -171.21 REMARK 500 1 ALA A 127 66.96 32.89 REMARK 500 2 LYS A 6 29.16 38.68 REMARK 500 2 PHE A 31 -93.79 -21.52 REMARK 500 2 LYS A 32 -57.40 -158.66 REMARK 500 2 HIS A 53 15.27 -147.40 REMARK 500 2 ASN A 60 -81.63 -59.08 REMARK 500 2 MET A 61 49.28 -157.85 REMARK 500 2 ALA A 89 38.61 -78.44 REMARK 500 2 GLN A 90 -60.20 -124.88 REMARK 500 2 ASN A 106 125.66 -171.29 REMARK 500 2 ALA A 127 61.52 33.23 REMARK 500 3 LYS A 6 23.98 43.34 REMARK 500 3 PHE A 31 -103.58 -20.08 REMARK 500 3 LYS A 32 -54.35 -163.37 REMARK 500 3 HIS A 53 12.75 -146.31 REMARK 500 3 ASN A 60 -81.72 -57.36 REMARK 500 3 MET A 61 49.73 -159.46 REMARK 500 3 ALA A 89 38.24 -78.84 REMARK 500 3 GLN A 90 -59.10 -125.42 REMARK 500 3 ALA A 104 152.74 -48.51 REMARK 500 3 LYS A 110 77.31 -112.49 REMARK 500 3 ALA A 127 66.46 33.36 REMARK 500 4 SER A 2 -44.76 -145.92 REMARK 500 4 LYS A 6 22.61 43.57 REMARK 500 4 PHE A 31 -102.27 -18.97 REMARK 500 4 LYS A 32 -55.35 -162.92 REMARK 500 4 HIS A 53 14.04 -147.45 REMARK 500 4 ASN A 60 -80.30 -57.48 REMARK 500 4 MET A 61 48.14 -156.63 REMARK 500 4 ALA A 89 38.27 -77.80 REMARK 500 4 GLN A 90 -59.69 -126.14 REMARK 500 4 ASN A 106 127.02 -170.84 REMARK 500 4 ALA A 127 67.38 33.36 REMARK 500 5 LYS A 6 30.45 38.20 REMARK 500 5 PHE A 31 -101.28 -19.73 REMARK 500 5 LYS A 32 -56.63 -162.40 REMARK 500 5 HIS A 53 15.36 -146.90 REMARK 500 5 ASN A 60 -80.44 -58.50 REMARK 500 5 MET A 61 48.76 -160.03 REMARK 500 5 ALA A 89 38.16 -78.79 REMARK 500 5 GLN A 90 -59.28 -124.51 REMARK 500 REMARK 500 THIS ENTRY HAS 171 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1P6U RELATED DB: PDB REMARK 900 BEF3-ACTIVATED STRUCTURE OF THE RESPONSE REGULATOR CHEY2 FROM REMARK 900 SINORHIZOBIUM MELILOTI REMARK 900 RELATED ID: 1 RELATED DB: TARGETDB DBREF 1P6Q A 1 129 UNP Q52884 Q52884_RHIME 1 129 SEQRES 1 A 129 MET SER LEU ALA GLU LYS ILE LYS VAL LEU ILE VAL ASP SEQRES 2 A 129 ASP GLN VAL THR SER ARG LEU LEU LEU GLY ASP ALA LEU SEQRES 3 A 129 GLN GLN LEU GLY PHE LYS GLN ILE THR ALA ALA GLY ASP SEQRES 4 A 129 GLY GLU GLN GLY MET LYS ILE MET ALA GLN ASN PRO HIS SEQRES 5 A 129 HIS LEU VAL ILE SER ASP PHE ASN MET PRO LYS MET ASP SEQRES 6 A 129 GLY LEU GLY LEU LEU GLN ALA VAL ARG ALA ASN PRO ALA SEQRES 7 A 129 THR LYS LYS ALA ALA PHE ILE ILE LEU THR ALA GLN GLY SEQRES 8 A 129 ASP ARG ALA LEU VAL GLN LYS ALA ALA ALA LEU GLY ALA SEQRES 9 A 129 ASN ASN VAL LEU ALA LYS PRO PHE THR ILE GLU LYS MET SEQRES 10 A 129 LYS ALA ALA ILE GLU ALA VAL PHE GLY ALA LEU LYS HELIX 1 1 GLN A 15 GLN A 28 1 14 HELIX 2 2 ASP A 39 GLN A 49 1 11 HELIX 3 3 ASP A 65 ARG A 74 1 10 HELIX 4 4 ASP A 92 GLY A 103 1 12 HELIX 5 5 THR A 113 ALA A 127 1 15 SHEET 1 A 5 ILE A 34 THR A 35 0 SHEET 2 A 5 VAL A 9 VAL A 12 1 N VAL A 9 O THR A 35 SHEET 3 A 5 LEU A 54 SER A 57 1 O ILE A 56 N LEU A 10 SHEET 4 A 5 ALA A 83 ILE A 86 1 O ILE A 85 N VAL A 55 SHEET 5 A 5 VAL A 107 LEU A 108 1 O LEU A 108 N PHE A 84 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 - b 23 2 Bytes