Header list of 1z4h.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING, DNA BINDING PROTEIN 16-MAR-05 1Z4H TITLE THE RESPONSE REGULATOR TORI BELONGS TO A NEW FAMILY OF ATYPICAL TITLE 2 EXCISIONASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TOR INHIBITION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TORI; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETSI KEYWDS WINGED HELIX, REVERSE TURN, PROTEIN BINDING, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR L.ELANTAK,M.ANSALDI,F.GUERLESQUIN,V.MEJEAN,X.MORELLI REVDAT 5 02-MAR-22 1Z4H 1 REMARK REVDAT 4 24-FEB-09 1Z4H 1 VERSN REVDAT 3 07-MAR-06 1Z4H 1 JRNL REVDAT 2 30-AUG-05 1Z4H 1 JRNL REVDAT 1 09-AUG-05 1Z4H 0 JRNL AUTH L.ELANTAK,M.ANSALDI,F.GUERLESQUIN,V.MEJEAN,X.MORELLI JRNL TITL STRUCTURAL AND GENETIC ANALYSES REVEAL A KEY ROLE IN JRNL TITL 2 PROPHAGE EXCISION FOR THE TORI RESPONSE REGULATOR INHIBITOR JRNL REF J.BIOL.CHEM. V. 280 36802 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 16079126 JRNL DOI 10.1074/JBC.M507409200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, CNS ARIA 1.2 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1341 RESTRAINTS: 1173 DISTANCE REMARK 3 RESTRAINTS + 68 DIHEDRAL ANGLE CONSTRAINTS FROM TALOS + 100 REMARK 3 DIHEDRAL ANGLE CONSTRAINTS FROM CSI AND 3JHNHA. REMARK 4 REMARK 4 1Z4H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032286. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 5.9 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM TORI U-15N,13C, 50MM REMARK 210 PHOSPHATE BUFFER, 90% H20, 10% REMARK 210 D20; 1.5MM TORI UNLABELLED, 50MM REMARK 210 PHOSPHATE BUFFER, 90% H20, 10% REMARK 210 D20; 1.5MM TORI U-15N, 50MM REMARK 210 PHOSPHATE BUFFER, 90% H20, 10% REMARK 210 D20; 1.5MM TORI U-13C, 50MM REMARK 210 PHOSPHATE BUFFER, 90% H20, 10% REMARK 210 D20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D HNCO; REMARK 210 3D HNCA; CBCA(CO)NH; HN(CO)CA; REMARK 210 HCCH-TOCSY; 2D NOESY; 2D TOCSY; REMARK 210 3D_13C-SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2002, CNS ARIA 1.2 REMARK 210 METHOD USED : NON-BONDED INTERACTION FOR REMARK 210 SIMULATED ANNEALING AND REMARK 210 REFINEMENT IN AN EXPLICIT WATER REMARK 210 BOX. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURE CALCULATIONS WERE PERFORMED WITH ARIA 1.2 USING REMARK 210 NOE'S, PHI ANGLE DIHEDRAL RESTRAINTS ESTIMATED FROM 3JHNHA AND REMARK 210 TALOS-DERIVED DIHEDRAL ANGLE CONSTRAINTS. 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 HA HIS A 53 HD2 PHE A 56 1.33 REMARK 500 HG22 VAL A 11 HB3 TRP A 48 1.34 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 ASP A 35 31.39 -159.54 REMARK 500 1 LEU A 36 119.21 63.67 REMARK 500 1 ALA A 39 146.21 -38.50 REMARK 500 1 ALA A 46 -91.47 172.20 REMARK 500 1 ALA A 64 73.35 59.68 REMARK 500 2 GLN A 2 -36.22 172.82 REMARK 500 2 ASP A 35 33.40 -159.04 REMARK 500 2 LEU A 36 106.56 61.44 REMARK 500 2 ALA A 39 157.74 -43.28 REMARK 500 2 ALA A 46 -92.57 -167.77 REMARK 500 2 ARG A 63 -96.95 -94.68 REMARK 500 2 ALA A 64 50.57 -169.13 REMARK 500 3 PRO A 7 -39.09 -37.35 REMARK 500 3 ASP A 35 68.49 -166.73 REMARK 500 3 LEU A 36 84.34 33.76 REMARK 500 3 ALA A 39 148.70 -34.54 REMARK 500 3 HIS A 43 114.07 -167.34 REMARK 500 3 ALA A 46 -84.31 -63.48 REMARK 500 3 ARG A 63 78.81 -117.99 REMARK 500 3 ALA A 64 100.01 -55.88 REMARK 500 4 PRO A 7 -48.75 -28.45 REMARK 500 4 ASP A 35 27.25 -163.54 REMARK 500 4 LEU A 36 106.84 60.59 REMARK 500 4 ALA A 39 158.13 -43.32 REMARK 500 4 ILE A 42 -32.77 -133.32 REMARK 500 4 ALA A 46 -94.98 -169.74 REMARK 500 4 ASN A 65 27.78 -149.41 REMARK 500 5 SER A 9 -167.28 -168.06 REMARK 500 5 ASP A 35 35.49 -168.74 REMARK 500 5 LEU A 36 126.91 66.75 REMARK 500 5 ALA A 39 158.20 -48.65 REMARK 500 5 HIS A 43 59.12 -144.92 REMARK 500 5 ALA A 46 -88.21 175.83 REMARK 500 5 ALA A 64 79.79 52.46 REMARK 500 6 GLN A 2 108.63 -166.56 REMARK 500 6 THR A 20 -62.48 -122.18 REMARK 500 6 ASP A 35 26.67 -158.72 REMARK 500 6 LEU A 36 108.36 62.53 REMARK 500 6 ALA A 39 156.73 -41.98 REMARK 500 6 HIS A 43 65.28 -154.81 REMARK 500 6 ALA A 46 -88.67 -179.26 REMARK 500 6 ALA A 64 92.46 -65.40 REMARK 500 7 PRO A 7 -36.43 -38.07 REMARK 500 7 SER A 9 -173.79 -173.37 REMARK 500 7 ASP A 35 86.94 179.43 REMARK 500 7 LEU A 36 100.25 18.39 REMARK 500 7 ALA A 39 153.62 -41.93 REMARK 500 7 HIS A 43 57.28 -140.61 REMARK 500 7 ARG A 45 -68.28 -144.79 REMARK 500 7 ALA A 46 -93.25 60.42 REMARK 500 REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z4H A 1 66 UNP Q9AZ38 Q9AZ38_BPHK6 1 66 SEQRES 1 A 66 MET GLN HIS GLU LEU GLN PRO ASP SER LEU VAL ASP LEU SEQRES 2 A 66 LYS PHE ILE MET ALA ASP THR GLY PHE GLY LYS THR PHE SEQRES 3 A 66 ILE TYR ASP ARG ILE LYS SER GLY ASP LEU PRO LYS ALA SEQRES 4 A 66 LYS VAL ILE HIS GLY ARG ALA ARG TRP LEU TYR ARG ASP SEQRES 5 A 66 HIS CYS GLU PHE LYS ASN LYS LEU LEU SER ARG ALA ASN SEQRES 6 A 66 GLY HELIX 1 1 ASP A 12 GLY A 21 1 10 HELIX 2 2 GLY A 23 LEU A 36 1 14 HELIX 3 3 TYR A 50 ALA A 64 1 15 SHEET 1 A 3 LEU A 10 VAL A 11 0 SHEET 2 A 3 ALA A 46 LEU A 49 -1 O TRP A 48 N VAL A 11 SHEET 3 A 3 LYS A 40 VAL A 41 -1 N LYS A 40 O ARG A 47 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