Header list of 1fr0.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 07-SEP-00 1FR0 TITLE SOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN TITLE 2 OF ANAEROBIC SENSOR KINASE ARCB FROM ESCHERICHIA COLI. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARCB; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THE HISTIDINE-CONTAINING PHOSPHOTRANSFER (HPT) DOMAIN; COMPND 5 EC: 2.7.3.-; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PSU2DH KEYWDS FOUR-HELIX BUNDLE MOTIF, ANAEROBIC SENSOR KINASE, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR T.IKEGAMI,T.OKADA,I.OHKI,J.HIRAYAMA,T.MIZUNO,M.SHIRAKAWA REVDAT 4 23-FEB-22 1FR0 1 REMARK REVDAT 3 24-FEB-09 1FR0 1 VERSN REVDAT 2 31-DEC-02 1FR0 1 REMARK REVDAT 1 14-MAR-01 1FR0 0 JRNL AUTH T.IKEGAMI,T.OKADA,I.OHKI,J.HIRAYAMA,T.MIZUNO,M.SHIRAKAWA JRNL TITL SOLUTION STRUCTURE AND DYNAMIC CHARACTER OF THE JRNL TITL 2 HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ANAEROBIC JRNL TITL 3 SENSOR KINASE ARCB FROM ESCHERICHIA COLI. JRNL REF BIOCHEMISTRY V. 40 375 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11148031 JRNL DOI 10.1021/BI001619G REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUENGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1348 RESTRAINTS, 1188 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 83 DIHEDRAL ANGLE RESTRAINTS,77 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1FR0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-SEP-00. REMARK 100 THE DEPOSITION ID IS D_1000011838. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM HPTARCB, 50MM KH2PO4 REMARK 210 -K2HPO4 (PH6.5 AT 37DEG), 50MM REMARK 210 KCL, AND 1MM DITHIOTHREITOL (DTT) REMARK 210 IN 90% H2O/10% D2O; 1.5MM REMARK 210 HPTARCB, 50MM KH2PO4-K2HPO4 REMARK 210 (PH6.5 AT 37DEG), 50MM KCL, AND REMARK 210 1MM DITHIOTHREITOL (DTT) IN 99.8% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; HMQC-J REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XWINNMR 2.0, NMRPIPE REMARK 210 1.7, NMRPIPP 4.2.4, MOLMOL 2.3 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-30 REMARK 470 RES CSSEQI ATOMS REMARK 470 LYS A 778 O 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 SER A 740 H ASP A 742 1.54 REMARK 500 O TRP A 771 H ALA A 775 1.54 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 GLU A 657 -64.45 67.12 REMARK 500 1 SER A 661 57.22 -117.18 REMARK 500 1 GLU A 662 -35.85 -177.73 REMARK 500 1 PRO A 741 55.57 -66.74 REMARK 500 1 GLU A 760 -34.44 -173.80 REMARK 500 1 LYS A 777 -156.18 -112.79 REMARK 500 2 THR A 655 -167.71 61.83 REMARK 500 2 GLU A 657 64.02 -154.66 REMARK 500 2 ASN A 658 70.79 -111.41 REMARK 500 2 LEU A 676 -72.20 -146.89 REMARK 500 2 LYS A 680 -80.17 -66.13 REMARK 500 2 SER A 740 53.18 -115.01 REMARK 500 2 PRO A 741 54.27 -66.50 REMARK 500 2 GLU A 760 -48.89 -165.99 REMARK 500 3 THR A 655 -72.42 -165.64 REMARK 500 3 ASN A 658 -74.31 -146.21 REMARK 500 3 PRO A 741 59.19 -65.19 REMARK 500 3 ASP A 742 -23.61 -143.33 REMARK 500 3 GLU A 760 -45.26 173.27 REMARK 500 3 ALA A 775 -87.90 -49.88 REMARK 500 4 THR A 655 -72.52 -42.79 REMARK 500 4 GLU A 662 -38.26 -132.77 REMARK 500 4 LEU A 676 -71.82 -62.19 REMARK 500 4 ILE A 719 -77.35 -79.50 REMARK 500 4 SER A 740 51.08 -116.83 REMARK 500 4 PRO A 741 53.00 -67.02 REMARK 500 4 GLU A 760 -46.64 -179.16 REMARK 500 4 THR A 776 97.88 -46.95 REMARK 500 5 THR A 655 110.06 58.88 REMARK 500 5 GLU A 656 -72.43 -55.69 REMARK 500 5 GLU A 657 -90.02 53.80 REMARK 500 5 LYS A 710 -70.65 -65.58 REMARK 500 5 SER A 740 52.78 -117.16 REMARK 500 5 PRO A 741 52.74 -67.12 REMARK 500 5 MET A 757 -70.79 -43.91 REMARK 500 5 GLU A 760 -51.58 -177.03 REMARK 500 5 LYS A 777 -163.07 56.56 REMARK 500 6 GLU A 656 51.22 -154.40 REMARK 500 6 GLU A 657 99.41 -43.51 REMARK 500 6 ASN A 658 101.13 65.90 REMARK 500 6 LEU A 676 -53.79 -148.90 REMARK 500 6 LYS A 680 -75.63 -72.21 REMARK 500 6 ASP A 684 -71.19 -60.01 REMARK 500 6 SER A 740 50.15 -116.71 REMARK 500 6 PRO A 741 55.79 -66.27 REMARK 500 6 GLU A 760 -48.69 -175.78 REMARK 500 6 GLU A 766 -70.80 -55.68 REMARK 500 7 GLU A 656 17.25 -141.81 REMARK 500 7 LYS A 660 -90.18 -44.84 REMARK 500 7 SER A 661 73.86 -63.99 REMARK 500 REMARK 500 THIS ENTRY HAS 240 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 729 0.20 SIDE CHAIN REMARK 500 1 ARG A 762 0.22 SIDE CHAIN REMARK 500 2 ARG A 729 0.19 SIDE CHAIN REMARK 500 2 ARG A 762 0.24 SIDE CHAIN REMARK 500 3 ARG A 729 0.30 SIDE CHAIN REMARK 500 3 ARG A 762 0.30 SIDE CHAIN REMARK 500 4 ARG A 729 0.17 SIDE CHAIN REMARK 500 4 ARG A 762 0.27 SIDE CHAIN REMARK 500 5 ARG A 729 0.28 SIDE CHAIN REMARK 500 5 ARG A 762 0.21 SIDE CHAIN REMARK 500 6 ARG A 729 0.18 SIDE CHAIN REMARK 500 6 ARG A 762 0.27 SIDE CHAIN REMARK 500 7 ARG A 729 0.29 SIDE CHAIN REMARK 500 7 ARG A 762 0.20 SIDE CHAIN REMARK 500 8 ARG A 729 0.18 SIDE CHAIN REMARK 500 8 ARG A 762 0.18 SIDE CHAIN REMARK 500 9 ARG A 762 0.15 SIDE CHAIN REMARK 500 10 ARG A 729 0.30 SIDE CHAIN REMARK 500 10 ARG A 762 0.19 SIDE CHAIN REMARK 500 11 ARG A 729 0.31 SIDE CHAIN REMARK 500 11 ARG A 762 0.29 SIDE CHAIN REMARK 500 12 ARG A 729 0.22 SIDE CHAIN REMARK 500 12 ARG A 762 0.13 SIDE CHAIN REMARK 500 13 ARG A 729 0.12 SIDE CHAIN REMARK 500 13 ARG A 762 0.30 SIDE CHAIN REMARK 500 14 ARG A 729 0.27 SIDE CHAIN REMARK 500 14 ARG A 762 0.28 SIDE CHAIN REMARK 500 15 ARG A 729 0.30 SIDE CHAIN REMARK 500 15 ARG A 762 0.16 SIDE CHAIN REMARK 500 16 ARG A 729 0.14 SIDE CHAIN REMARK 500 16 ARG A 762 0.24 SIDE CHAIN REMARK 500 17 ARG A 729 0.19 SIDE CHAIN REMARK 500 17 ARG A 762 0.25 SIDE CHAIN REMARK 500 18 ARG A 729 0.18 SIDE CHAIN REMARK 500 18 ARG A 762 0.21 SIDE CHAIN REMARK 500 19 ARG A 729 0.27 SIDE CHAIN REMARK 500 19 ARG A 762 0.17 SIDE CHAIN REMARK 500 20 ARG A 729 0.29 SIDE CHAIN REMARK 500 20 ARG A 762 0.10 SIDE CHAIN REMARK 500 21 ARG A 729 0.23 SIDE CHAIN REMARK 500 21 ARG A 762 0.24 SIDE CHAIN REMARK 500 22 ARG A 729 0.31 SIDE CHAIN REMARK 500 22 ARG A 762 0.14 SIDE CHAIN REMARK 500 23 ARG A 729 0.32 SIDE CHAIN REMARK 500 23 ARG A 762 0.27 SIDE CHAIN REMARK 500 24 ARG A 729 0.31 SIDE CHAIN REMARK 500 25 ARG A 729 0.31 SIDE CHAIN REMARK 500 25 ARG A 762 0.32 SIDE CHAIN REMARK 500 26 ARG A 729 0.15 SIDE CHAIN REMARK 500 26 ARG A 762 0.28 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A0B RELATED DB: PDB REMARK 900 THE X-RAY STRUCTURE OF THE SAME HPT DOMAIN OF ARCB DBREF 1FR0 A 654 778 UNP P22763 ARCB_ECOLI 654 778 SEQRES 1 A 125 THR THR GLU GLU ASN SER LYS SER GLU ALA LEU LEU ASP SEQRES 2 A 125 ILE PRO MET LEU GLU GLN TYR LEU GLU LEU VAL GLY PRO SEQRES 3 A 125 LYS LEU ILE THR ASP GLY LEU ALA VAL PHE GLU LYS MET SEQRES 4 A 125 MET PRO GLY TYR VAL SER VAL LEU GLU SER ASN LEU THR SEQRES 5 A 125 ALA GLN ASP LYS LYS GLY ILE VAL GLU GLU GLY HIS LYS SEQRES 6 A 125 ILE LYS GLY ALA ALA GLY SER VAL GLY LEU ARG HIS LEU SEQRES 7 A 125 GLN GLN LEU GLY GLN GLN ILE GLN SER PRO ASP LEU PRO SEQRES 8 A 125 ALA TRP GLU ASP ASN VAL GLY GLU TRP ILE GLU GLU MET SEQRES 9 A 125 LYS GLU GLU TRP ARG HIS ASP VAL GLU VAL LEU LYS ALA SEQRES 10 A 125 TRP VAL ALA LYS ALA THR LYS LYS HELIX 1 1 ILE A 667 LEU A 676 1 10 HELIX 2 2 PRO A 679 THR A 705 1 27 HELIX 3 3 LYS A 709 SER A 725 1 17 HELIX 4 4 ARG A 729 ILE A 738 1 10 HELIX 5 5 TRP A 746 ALA A 775 1 30 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