Header list of 1se7.pdb file
Complete list - 2 20 Bytes
HEADER TRANSFERASE 16-FEB-04 1SE7 TITLE SOLUTION STRUCTURE OF THE E. COLI BACTERIOPHAGE P1 ENCODED HOT TITLE 2 PROTEIN: A HOMOLOGUE OF THE THETA SUBUNIT OF E. COLI DNA POLYMERASE TITLE 3 III COMPND MOL_ID: 1; COMPND 2 MOLECULE: HOMOLOGUE OF THE THETA SUBUNIT OF DNA POLYMERASE III; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HOT; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P1; SOURCE 3 ORGANISM_TAXID: 10678; SOURCE 4 GENE: HOT; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLR(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30HOT KEYWDS E. COLI BACTERIOPHAGE P1, HOMOLOGUE OF THETA, HOT, E. COLI DNA KEYWDS 2 POLYMERASE III, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 7 AUTHOR E.F.DEROSE,T.W.KIRBY,G.A.MUELLER,A.K.CHIKOVA,R.M.SCHAAPER,R.E.LONDON REVDAT 3 02-MAR-22 1SE7 1 REMARK REVDAT 2 24-FEB-09 1SE7 1 VERSN REVDAT 1 14-DEC-04 1SE7 0 JRNL AUTH E.F.DEROSE,T.W.KIRBY,G.A.MUELLER,A.K.CHIKOVA,R.M.SCHAAPER, JRNL AUTH 2 R.E.LONDON JRNL TITL PHAGE LIKE IT HOT: SOLUTION STRUCTURE OF THE BACTERIOPHAGE JRNL TITL 2 P1-ENCODED HOT PROTEIN, A HOMOLOG OF THE THETA SUBUNIT OF E. JRNL TITL 3 COLI DNA POLYMERASE III JRNL REF STRUCTURE V. 12 2221 2004 JRNL REFN ISSN 0969-2126 JRNL PMID 15576035 JRNL DOI 10.1016/J.STR.2004.09.019 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1 REV 2002.044.17.08, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE COMPUTED USING REMARK 3 DEFAULT ARIA PARAMETERS, WITH QRELAX SET TO FALSE. 430 MANUALLY REMARK 3 ASSIGNED NOE DISTANCE RESTRAINTS WERE INCLUDED, AND QSHIFT AND REMARK 3 QEXCLUDE WERE SET TO FALSE FOR THE MANUALLY ASSIGNED NOES. ARIA REMARK 3 ASSIGNED 1140 UNAMBIGUOUS AND 435 AMBIGUOUS NOE DISTANCE REMARK 3 RESTRAINTS. 51 DIHEDRAL RESTRAINTS, 46 HYDROGEN BOND RESTRAINTS, REMARK 3 AND 36 BACKBONE AMIDE RESIDUAL DIPOLAR COUPLINGS WERE ALSO USED REMARK 3 IN THE CALCULATION. REMARK 4 REMARK 4 1SE7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000021633. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.3MM U-[13C,15N] PROTEIN, 5MM REMARK 210 TRIS, 100MM NACL, 5MM NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, ARIA 1.2, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7 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: THE 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 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 TYR A 2 -163.78 56.65 REMARK 500 1 TRP A 4 -21.79 -148.86 REMARK 500 1 ASN A 5 38.06 -88.10 REMARK 500 1 LEU A 32 -86.70 -78.57 REMARK 500 1 ASN A 33 20.20 178.24 REMARK 500 1 LEU A 67 170.02 -44.29 REMARK 500 1 PRO A 68 -156.49 -58.84 REMARK 500 1 LYS A 69 163.69 -45.62 REMARK 500 1 SER A 71 79.97 -178.60 REMARK 500 1 ASP A 78 8.38 58.99 REMARK 500 1 ASP A 79 18.28 59.07 REMARK 500 1 ALA A 80 -64.83 -94.73 REMARK 500 2 TYR A 2 -170.71 57.67 REMARK 500 2 TRP A 4 -12.24 -160.12 REMARK 500 2 ASN A 5 38.75 -81.88 REMARK 500 2 LYS A 9 -50.70 -120.74 REMARK 500 2 LEU A 32 -140.17 73.36 REMARK 500 2 GLU A 44 -69.71 -121.21 REMARK 500 2 ASN A 48 -6.74 -58.01 REMARK 500 2 LEU A 67 165.47 -43.62 REMARK 500 2 PRO A 68 -100.62 -69.00 REMARK 500 2 SER A 71 -145.56 -128.77 REMARK 500 2 ALA A 74 37.35 -90.53 REMARK 500 2 ASP A 79 -27.12 -143.39 REMARK 500 2 VAL A 81 74.06 47.55 REMARK 500 3 TRP A 4 -7.79 -151.34 REMARK 500 3 ASN A 5 33.63 -90.47 REMARK 500 3 ALA A 7 30.56 -94.52 REMARK 500 3 SER A 10 -162.66 -68.69 REMARK 500 3 GLN A 11 -63.92 -100.84 REMARK 500 3 GLU A 30 9.21 -65.25 REMARK 500 3 ARG A 31 -61.69 -123.05 REMARK 500 3 LEU A 32 -141.80 -103.03 REMARK 500 3 ASN A 33 74.50 -111.42 REMARK 500 3 GLN A 45 76.68 52.78 REMARK 500 3 LEU A 67 171.45 -49.20 REMARK 500 3 LYS A 69 132.74 57.86 REMARK 500 3 ASP A 79 -72.53 -120.86 REMARK 500 3 ALA A 80 76.43 -172.49 REMARK 500 4 TRP A 4 151.90 173.61 REMARK 500 4 GLU A 30 7.37 -66.36 REMARK 500 4 ARG A 31 -63.75 -122.18 REMARK 500 4 LEU A 32 -132.08 -91.68 REMARK 500 4 GLU A 44 -69.18 -120.98 REMARK 500 4 PRO A 68 -165.55 -64.76 REMARK 500 4 LYS A 69 -113.76 56.60 REMARK 500 4 GLN A 76 170.59 -54.99 REMARK 500 4 ASP A 79 -70.02 -66.74 REMARK 500 4 ALA A 80 -19.50 -172.72 REMARK 500 5 TRP A 4 -19.87 -150.87 REMARK 500 REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1SE7 A 1 83 UNP Q71T70 Q71T70_BPP1 5 87 SEQRES 1 A 83 MET TYR ASP TRP ASN ILE ALA ALA LYS SER GLN GLU GLU SEQRES 2 A 83 ARG ASP LYS VAL ASN VAL ASP LEU ALA ALA SER GLY VAL SEQRES 3 A 83 ALA TYR LYS GLU ARG LEU ASN ILE PRO VAL ILE ALA GLU SEQRES 4 A 83 GLN VAL ALA ARG GLU GLN PRO GLU ASN LEU ARG THR TYR SEQRES 5 A 83 PHE MET GLU ARG LEU ARG HIS TYR ARG GLN LEU SER LEU SEQRES 6 A 83 GLN LEU PRO LYS GLY SER ASP PRO ALA TYR GLN LYS ASP SEQRES 7 A 83 ASP ALA VAL LYS LYS HELIX 1 1 SER A 10 LEU A 32 1 23 HELIX 2 2 ILE A 37 ARG A 43 1 7 HELIX 3 3 PRO A 46 ASN A 48 5 3 HELIX 4 4 LEU A 49 LEU A 67 1 19 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 - 2 20 Bytes