Header list of 2drn.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 11-JUN-06 2DRN TITLE DOCKING AND DIMERIZATION DOMAIN (D/D) OF THE TYPE II-ALPHA REGULATORY TITLE 2 SUBUNITY OF PROTEIN KINASE A (PKA) IN COMPLEX WITH A PEPTIDE FROM AN TITLE 3 A-KINASE ANCHORING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY COMPND 3 SUBUNIT; COMPND 4 CHAIN: A, B; COMPND 5 FRAGMENT: N-TERMINAL DOCKING AND DIMERIZATION DOMAIN, RESIDUES 4-46; COMPND 6 EC: 2.7.1.37; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: 24-RESIDUES PEPTIDE FROM AN A-KINASE ANCHORING PROTEIN; COMPND 10 CHAIN: C; COMPND 11 SYNONYM: FRAGMENT, HUMAN THYROID ANCHORING PROTEIN, HT31(493-515) COMPND 12 PEPTIDE; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: RIIA(1-44); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-16B; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: THE PEPTIDE HAS BEEN GENERATED BY SOLID PHASE PEPTIDE SOURCE 13 SYNTHESIS.; THIS SEQUENCE OCCURS NATURALLY IN HUMANS. KEYWDS AKAP, PKA, SIGNAL TRANSDUCTION, 4-HELIX BUNDLE, HELIX-LOOP-HELIX, KEYWDS 2 PROTEIN-PEPTIDE COMPLEX, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 13 AUTHOR M.G.NEWLON,M.ROY,D.MORIKIS,Z.E.HAUSKEN,V.COGHLAN,J.D.SCOTT, AUTHOR 2 P.A.JENNINGS REVDAT 3 09-MAR-22 2DRN 1 REMARK REVDAT 2 24-FEB-09 2DRN 1 VERSN REVDAT 1 29-AUG-06 2DRN 0 JRNL AUTH M.G.NEWLON,M.ROY,D.MORIKIS,D.W.CARR,R.WESTPHAL,J.D.SCOTT, JRNL AUTH 2 P.A.JENNINGS JRNL TITL A NOVEL MECHANISM OF PKA ANCHORING REVEALED BY SOLUTION JRNL TITL 2 STRUCTURES OF ANCHORING COMPLEXES. JRNL REF EMBO J. V. 20 1651 2001 JRNL REFN ISSN 0261-4189 JRNL PMID 11285229 JRNL DOI 10.1093/EMBOJ/20.7.1651 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1370 RESTRAINTS, 1247 ARE REMARK 3 NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS, 50 DIHEDRAL ANGLE RESTRAINTS,73 DISTANCE RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 2DRN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-06. REMARK 100 THE DEPOSITION ID IS D_1000025761. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM RII-ALPHA(1-44); 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D REMARK 210 HETERONUCLEAR AND HOMONUCLEAR TECHNIQUES. 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 O LEU B 15 H THR B 19 1.56 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 MET A 2 56.59 -95.47 REMARK 500 1 GLN A 6 53.04 -170.12 REMARK 500 1 ILE A 7 66.72 -162.40 REMARK 500 1 PRO A 9 -166.93 -72.46 REMARK 500 1 TYR A 37 -70.14 -61.01 REMARK 500 1 ARG A 45 -65.04 -165.96 REMARK 500 1 MET B 2 97.25 53.51 REMARK 500 1 HIS B 4 -176.44 -173.05 REMARK 500 1 VAL B 20 -73.09 -62.59 REMARK 500 1 ALA C 23 -56.92 -162.50 REMARK 500 2 MET A 2 -38.54 -130.03 REMARK 500 2 GLN A 6 38.56 -141.85 REMARK 500 2 ARG A 45 77.44 52.93 REMARK 500 2 HIS B 4 32.53 -144.64 REMARK 500 2 LEU C 2 -88.99 -155.73 REMARK 500 2 ALA C 21 -77.35 -53.64 REMARK 500 2 ALA C 23 -76.91 -81.79 REMARK 500 3 HIS A 4 -164.90 -109.74 REMARK 500 3 GLN A 6 -157.67 -101.22 REMARK 500 3 VAL A 20 -76.28 -77.81 REMARK 500 3 ARG A 24 -70.04 -98.49 REMARK 500 3 ARG A 45 74.63 -150.46 REMARK 500 3 MET B 2 -167.92 -75.66 REMARK 500 3 VAL B 20 -74.93 -65.87 REMARK 500 3 GLN B 26 96.31 -36.13 REMARK 500 3 ARG B 45 79.63 53.20 REMARK 500 3 ALA C 23 46.42 -169.31 REMARK 500 4 HIS A 4 30.22 -146.06 REMARK 500 4 GLN A 6 98.58 -164.50 REMARK 500 4 ALA A 44 64.48 -105.03 REMARK 500 4 MET B 2 74.30 -109.52 REMARK 500 4 GLN B 6 57.77 -102.51 REMARK 500 4 VAL B 20 -74.17 -61.57 REMARK 500 4 TYR B 37 -71.36 -59.79 REMARK 500 4 ALA B 44 79.11 49.29 REMARK 500 4 ALA C 21 -73.31 -48.88 REMARK 500 4 ALA C 23 43.67 -100.55 REMARK 500 5 MET A 2 -37.88 -174.44 REMARK 500 5 ILE A 5 52.44 -119.70 REMARK 500 5 GLN A 6 -154.45 -123.27 REMARK 500 5 GLN B 6 79.29 -159.10 REMARK 500 5 VAL B 20 -70.81 -65.77 REMARK 500 5 GLN B 25 60.94 -114.06 REMARK 500 5 GLN B 26 96.13 -38.05 REMARK 500 5 ALA B 44 -82.06 -111.27 REMARK 500 5 ALA C 21 -76.51 -53.98 REMARK 500 6 MET A 2 -66.40 -129.79 REMARK 500 6 PRO A 9 -163.02 -75.51 REMARK 500 6 VAL A 20 -74.48 -70.34 REMARK 500 6 ALA A 44 84.17 47.56 REMARK 500 REMARK 500 THIS ENTRY HAS 104 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 24 0.29 SIDE CHAIN REMARK 500 1 ARG A 40 0.19 SIDE CHAIN REMARK 500 1 ARG A 42 0.32 SIDE CHAIN REMARK 500 1 ARG A 45 0.32 SIDE CHAIN REMARK 500 1 ARG A 46 0.20 SIDE CHAIN REMARK 500 1 ARG B 24 0.23 SIDE CHAIN REMARK 500 1 ARG B 40 0.29 SIDE CHAIN REMARK 500 1 ARG B 42 0.20 SIDE CHAIN REMARK 500 1 ARG B 45 0.20 SIDE CHAIN REMARK 500 1 ARG B 46 0.32 SIDE CHAIN REMARK 500 2 ARG A 24 0.30 SIDE CHAIN REMARK 500 2 ARG A 40 0.32 SIDE CHAIN REMARK 500 2 ARG A 42 0.31 SIDE CHAIN REMARK 500 2 ARG A 45 0.21 SIDE CHAIN REMARK 500 2 ARG A 46 0.25 SIDE CHAIN REMARK 500 2 ARG B 24 0.17 SIDE CHAIN REMARK 500 2 ARG B 40 0.19 SIDE CHAIN REMARK 500 2 ARG B 42 0.30 SIDE CHAIN REMARK 500 2 ARG B 45 0.29 SIDE CHAIN REMARK 500 2 ARG B 46 0.28 SIDE CHAIN REMARK 500 3 ARG A 24 0.24 SIDE CHAIN REMARK 500 3 ARG A 40 0.30 SIDE CHAIN REMARK 500 3 ARG A 42 0.32 SIDE CHAIN REMARK 500 3 ARG A 45 0.31 SIDE CHAIN REMARK 500 3 ARG A 46 0.29 SIDE CHAIN REMARK 500 3 ARG B 24 0.27 SIDE CHAIN REMARK 500 3 ARG B 40 0.24 SIDE CHAIN REMARK 500 3 ARG B 42 0.30 SIDE CHAIN REMARK 500 3 ARG B 45 0.28 SIDE CHAIN REMARK 500 3 ARG B 46 0.17 SIDE CHAIN REMARK 500 4 ARG A 24 0.31 SIDE CHAIN REMARK 500 4 ARG A 40 0.20 SIDE CHAIN REMARK 500 4 ARG A 42 0.29 SIDE CHAIN REMARK 500 4 ARG A 45 0.30 SIDE CHAIN REMARK 500 4 ARG A 46 0.21 SIDE CHAIN REMARK 500 4 ARG B 24 0.29 SIDE CHAIN REMARK 500 4 ARG B 40 0.29 SIDE CHAIN REMARK 500 4 ARG B 42 0.24 SIDE CHAIN REMARK 500 4 ARG B 45 0.24 SIDE CHAIN REMARK 500 4 ARG B 46 0.30 SIDE CHAIN REMARK 500 5 ARG A 24 0.25 SIDE CHAIN REMARK 500 5 ARG A 40 0.27 SIDE CHAIN REMARK 500 5 ARG A 42 0.29 SIDE CHAIN REMARK 500 5 ARG A 45 0.28 SIDE CHAIN REMARK 500 5 ARG A 46 0.32 SIDE CHAIN REMARK 500 5 ARG B 24 0.16 SIDE CHAIN REMARK 500 5 ARG B 40 0.31 SIDE CHAIN REMARK 500 5 ARG B 42 0.31 SIDE CHAIN REMARK 500 5 ARG B 45 0.27 SIDE CHAIN REMARK 500 5 ARG B 46 0.19 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 130 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2HWN RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN (CHAIN A AND B) REMARK 900 RELATED ID: 2H9R RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH A DIFFERENT FRAGMENT REMARK 900 RELATED ID: 1R2A RELATED DB: PDB REMARK 900 THE SAME PROTEIN OF CHAIN A AND B REMARK 900 RELATED ID: 1L6E RELATED DB: PDB REMARK 900 THE SAME PROTEIN OF CHAIN A AND B DBREF 2DRN A 4 46 UNP P12368 KAP2_RAT 2 44 DBREF 2DRN B 4 46 UNP P12368 KAP2_RAT 2 44 DBREF 2DRN C 1 23 UNP Q14572 Q14572_HUMAN 493 515 SEQADV 2DRN HIS A 1 UNP P12368 SEE REMARK 999 SEQADV 2DRN MET A 2 UNP P12368 SEE REMARK 999 SEQADV 2DRN GLY A 3 UNP P12368 SEE REMARK 999 SEQADV 2DRN HIS B 1 UNP P12368 SEE REMARK 999 SEQADV 2DRN MET B 2 UNP P12368 SEE REMARK 999 SEQADV 2DRN GLY B 3 UNP P12368 SEE REMARK 999 SEQADV 2DRN TYR C 24 UNP Q14572 SEE REMARK 999 SEQRES 1 A 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU SEQRES 2 A 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN SEQRES 3 A 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR SEQRES 4 A 46 ARG LEU ARG GLU ALA ARG ARG SEQRES 1 B 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU SEQRES 2 B 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN SEQRES 3 B 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR SEQRES 4 B 46 ARG LEU ARG GLU ALA ARG ARG SEQRES 1 C 24 ASP LEU ILE GLU GLU ALA ALA SER ARG ILE VAL ASP ALA SEQRES 2 C 24 VAL ILE GLU GLN VAL LYS ALA ALA GLY ALA TYR HELIX 1 1 GLY A 10 GLN A 26 1 17 HELIX 2 2 ASP A 29 ARG A 42 1 14 HELIX 3 3 GLY B 10 GLN B 26 1 17 HELIX 4 4 ASP B 29 ARG B 45 1 17 HELIX 5 5 LEU C 2 LYS C 19 1 18 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 9 2 Bytes