Header list of 2ezw.pdb file
Complete list - n 24 2 Bytes
HEADER TRANSFERASE 10-NOV-05 2EZW TITLE SOLUTION STRUCTURE OF THE DOCKING AND DIMERIZATION DOMAIN OF THE TYPE TITLE 2 I ALPHA REGULATORY SUBUNIT OF PROTEIN KINASE A (RIALPHA D/D) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY COMPND 3 SUBUNIT; COMPND 4 CHAIN: A, B; COMPND 5 FRAGMENT: DIMERIZATION-ANCHORING DOMAIN (RESIDUES 12-61); COMPND 6 EC: 2.7.1.37; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: PRKAR1A (AMINO ACIDS:12 - 61); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ECORI; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETC KEYWDS REGULATORY SUBUNIT, ANCHORING, FOUR-HELIX BUNDLE, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR P.BANKY REVDAT 3 24-JAN-18 2EZW 1 JRNL REMARK REVDAT 2 24-FEB-09 2EZW 1 VERSN REVDAT 1 14-FEB-06 2EZW 0 JRNL AUTH P.BANKY,M.ROY,M.G.NEWLON,D.MORIKIS,N.M.HASTE,S.S.TAYLOR, JRNL AUTH 2 P.A.JENNINGS JRNL TITL RELATED PROTEIN-PROTEIN INTERACTION MODULES PRESENT JRNL TITL 2 DRASTICALLY DIFFERENT SURFACE TOPOGRAPHIES DESPITE A JRNL TITL 3 CONSERVED HELICAL PLATFORM JRNL REF J.MOL.BIOL. V. 330 1117 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12860132 JRNL DOI 10.1016/S0022-2836(03)00552-7 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.BANKY,M.G.NEWLON,M.ROY,S.GARROD,S.S.TAYLOR,P.A.JENNINGS REMARK 1 TITL ISOFORM-SPECIFIC DIFFERENCES BETWEEN THE TYPE IA AND IIA REMARK 1 TITL 2 CYCLIC-DEPENDENT PROTEIN KINASE ANCHORING DOMAINS REVEALED REMARK 1 TITL 3 BY SOLUTION NMR REMARK 1 REF J.BIOL.CHEM. V. 275 35146 2000 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 95.0, X-PLOR 3.851 REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (FELIX), BRUNGER, A.T. REMARK 3 (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 435 NOE-DERIVED DISTANCE, 139 BACKBONE DIHEDRAL AND 13 HYDROGEN REMARK 3 BOND RESTRAINTS PER MONOMER REMARK 4 REMARK 4 2EZW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-05. REMARK 100 THE DEPOSITION ID IS D_1000035281. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 4. REMARK 210 IONIC STRENGTH : 50MM SODIUM ACETATE, 150MM REMARK 210 SODIUM CHLORIDE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : R1A(12-61) AT 1.2-1.6 MM DIMER, REMARK 210 50MM SODIUM ACETATE, 150MM REMARK 210 SODIUM CHLORIDE, PH 4.0, 90% H2O, REMARK 210 10% D2O; 15N-ENRICHED R1A(12-61) REMARK 210 , 5% H2O, 95% D2O; 15N-ENRICHED REMARK 210 R1A(12-61), 90% H2O, 10% D2O; REMARK 210 13C/15N-ENRICHED R1A(12-61), 5% REMARK 210 H2O, 95% D2O; ASYMMETRICALLY REMARK 210 ENRICHED 13C/15N-12C/14N R1A(12- REMARK 210 61), 5% H2O,95% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D 1H-15N HSQC, AMIDE REMARK 210 PROTON EXCHANGE; 3D 1H-15N HSQC REMARK 210 NOESY; 3D HNHA; 3D 13C-EDITED REMARK 210 HMQC-NOESY; 3D 13C-EDITED(W2) REMARK 210 12C-FILTERED(W1) 13C-FILTERED(W3) REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 GLN A 21 -132.49 -90.44 REMARK 500 1 ASN A 24 -70.53 -114.72 REMARK 500 1 ARG A 40 49.33 -143.75 REMARK 500 1 ARG A 43 87.14 -164.37 REMARK 500 1 GLU A 59 -174.00 53.03 REMARK 500 1 GLN B 21 -132.48 -90.45 REMARK 500 1 ASN B 24 -70.65 -114.46 REMARK 500 1 ARG B 40 49.13 -144.56 REMARK 500 1 ARG B 43 87.15 -164.24 REMARK 500 1 GLU B 59 -173.96 52.95 REMARK 500 2 TYR A 19 38.87 -90.61 REMARK 500 2 VAL A 20 -124.16 -77.67 REMARK 500 2 HIS A 23 -40.93 -165.80 REMARK 500 2 ASN A 24 -43.57 -143.90 REMARK 500 2 ALA A 39 -164.60 56.51 REMARK 500 2 LYS A 57 42.01 -90.17 REMARK 500 2 GLU A 59 -166.31 53.87 REMARK 500 2 ALA A 60 -44.25 -158.50 REMARK 500 2 TYR B 19 38.83 -90.60 REMARK 500 2 VAL B 20 -124.02 -77.51 REMARK 500 2 HIS B 23 -40.79 -165.73 REMARK 500 2 ASN B 24 -43.63 -143.83 REMARK 500 2 ALA B 39 -164.69 56.53 REMARK 500 2 LYS B 57 41.96 -90.25 REMARK 500 2 GLU B 59 -166.36 53.77 REMARK 500 2 ALA B 60 -44.30 -158.36 REMARK 500 3 GLN A 21 -156.25 -87.19 REMARK 500 3 HIS A 23 -39.64 -167.01 REMARK 500 3 ALA A 27 -72.00 -62.52 REMARK 500 3 ARG A 43 75.41 -111.21 REMARK 500 3 TYR A 51 -64.92 -90.38 REMARK 500 3 GLU A 59 -167.97 -62.64 REMARK 500 3 GLN B 21 -156.25 -87.22 REMARK 500 3 HIS B 23 -39.70 -166.83 REMARK 500 3 ALA B 27 -71.91 -62.50 REMARK 500 3 ARG B 43 75.49 -111.39 REMARK 500 3 TYR B 51 -64.86 -90.10 REMARK 500 3 GLU B 59 -168.01 -62.59 REMARK 500 4 TYR A 19 39.24 -90.68 REMARK 500 4 VAL A 20 -125.98 -75.39 REMARK 500 4 LYS A 22 64.18 -69.19 REMARK 500 4 HIS A 23 -35.90 -169.19 REMARK 500 4 ASN A 24 -43.40 -151.86 REMARK 500 4 ALA A 39 -165.58 55.47 REMARK 500 4 ARG A 43 99.00 -169.41 REMARK 500 4 LYS A 57 47.50 -90.17 REMARK 500 4 ALA A 60 51.80 -163.71 REMARK 500 4 TYR B 19 39.06 -90.40 REMARK 500 4 VAL B 20 -125.79 -75.47 REMARK 500 4 LYS B 22 64.08 -69.16 REMARK 500 REMARK 500 THIS ENTRY HAS 218 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 14 0.25 SIDE CHAIN REMARK 500 1 ARG A 40 0.32 SIDE CHAIN REMARK 500 1 ARG A 43 0.25 SIDE CHAIN REMARK 500 1 ARG A 49 0.32 SIDE CHAIN REMARK 500 1 ARG B 14 0.25 SIDE CHAIN REMARK 500 1 ARG B 40 0.32 SIDE CHAIN REMARK 500 1 ARG B 43 0.25 SIDE CHAIN REMARK 500 1 ARG B 49 0.32 SIDE CHAIN REMARK 500 2 ARG A 14 0.21 SIDE CHAIN REMARK 500 2 ARG A 40 0.30 SIDE CHAIN REMARK 500 2 ARG A 43 0.27 SIDE CHAIN REMARK 500 2 ARG A 49 0.28 SIDE CHAIN REMARK 500 2 ARG B 14 0.21 SIDE CHAIN REMARK 500 2 ARG B 40 0.30 SIDE CHAIN REMARK 500 2 ARG B 43 0.27 SIDE CHAIN REMARK 500 2 ARG B 49 0.28 SIDE CHAIN REMARK 500 3 ARG A 14 0.18 SIDE CHAIN REMARK 500 3 ARG A 40 0.29 SIDE CHAIN REMARK 500 3 ARG A 43 0.27 SIDE CHAIN REMARK 500 3 ARG A 49 0.22 SIDE CHAIN REMARK 500 3 ARG B 14 0.18 SIDE CHAIN REMARK 500 3 ARG B 40 0.29 SIDE CHAIN REMARK 500 3 ARG B 43 0.27 SIDE CHAIN REMARK 500 3 ARG B 49 0.22 SIDE CHAIN REMARK 500 4 ARG A 14 0.27 SIDE CHAIN REMARK 500 4 ARG A 40 0.28 SIDE CHAIN REMARK 500 4 ARG A 43 0.28 SIDE CHAIN REMARK 500 4 ARG A 49 0.27 SIDE CHAIN REMARK 500 4 ARG B 14 0.27 SIDE CHAIN REMARK 500 4 ARG B 40 0.28 SIDE CHAIN REMARK 500 4 ARG B 43 0.28 SIDE CHAIN REMARK 500 4 ARG B 49 0.27 SIDE CHAIN REMARK 500 5 ARG A 14 0.19 SIDE CHAIN REMARK 500 5 ARG A 40 0.31 SIDE CHAIN REMARK 500 5 ARG A 43 0.25 SIDE CHAIN REMARK 500 5 ARG A 49 0.26 SIDE CHAIN REMARK 500 5 ARG B 14 0.19 SIDE CHAIN REMARK 500 5 ARG B 40 0.31 SIDE CHAIN REMARK 500 5 ARG B 43 0.25 SIDE CHAIN REMARK 500 5 ARG B 49 0.26 SIDE CHAIN REMARK 500 6 ARG A 14 0.19 SIDE CHAIN REMARK 500 6 ARG A 40 0.31 SIDE CHAIN REMARK 500 6 ARG A 43 0.25 SIDE CHAIN REMARK 500 6 ARG A 49 0.26 SIDE CHAIN REMARK 500 6 ARG B 14 0.19 SIDE CHAIN REMARK 500 6 ARG B 40 0.31 SIDE CHAIN REMARK 500 6 ARG B 43 0.25 SIDE CHAIN REMARK 500 6 ARG B 49 0.26 SIDE CHAIN REMARK 500 7 ARG A 14 0.32 SIDE CHAIN REMARK 500 7 ARG A 40 0.23 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 144 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1R2A RELATED DB: PDB REMARK 900 THE SAME FAMILY OF THE PROTEIN KINASE A REGULATORY SUBUNITS DBREF 2EZW A 12 61 UNP P00514 KAP0_BOVIN 12 61 DBREF 2EZW B 12 61 UNP P00514 KAP0_BOVIN 12 61 SEQRES 1 A 50 SER LEU ARG GLU CYS GLU LEU TYR VAL GLN LYS HIS ASN SEQRES 2 A 50 ILE GLN ALA LEU LEU LYS ASP SER ILE VAL GLN LEU CYS SEQRES 3 A 50 THR ALA ARG PRO GLU ARG PRO MET ALA PHE LEU ARG GLU SEQRES 4 A 50 TYR PHE GLU LYS LEU GLU LYS GLU GLU ALA LYS SEQRES 1 B 50 SER LEU ARG GLU CYS GLU LEU TYR VAL GLN LYS HIS ASN SEQRES 2 B 50 ILE GLN ALA LEU LEU LYS ASP SER ILE VAL GLN LEU CYS SEQRES 3 B 50 THR ALA ARG PRO GLU ARG PRO MET ALA PHE LEU ARG GLU SEQRES 4 B 50 TYR PHE GLU LYS LEU GLU LYS GLU GLU ALA LYS HELIX 1 1 SER A 12 GLU A 17 1 6 HELIX 2 2 ILE A 25 CYS A 37 1 13 HELIX 3 3 ARG A 43 LYS A 57 1 15 HELIX 4 4 SER B 12 GLU B 17 1 6 HELIX 5 5 ILE B 25 CYS B 37 1 13 HELIX 6 6 ARG B 43 LYS B 57 1 15 SSBOND 1 CYS A 16 CYS B 37 1555 1555 2.02 SSBOND 2 CYS A 37 CYS B 16 1555 1555 2.02 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 - n 24 2 Bytes