Header list of 2f05.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION REPRESSOR 11-NOV-05 2F05 TITLE SOLUTION STRUCTURE OF FREE PAH2 DOMAIN OF MSIN3B COMPND MOL_ID: 1; COMPND 2 MOLECULE: PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PAH2 DOMAIN (RESIDUES 148-252); COMPND 5 SYNONYM: TRANSCRIPTIONAL COREPRESSOR SIN3B, HISTONE DEACETYLASE COMPND 6 COMPLEX SUBUNIT SIN3B; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: SIN3B, KIAA0700; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T KEYWDS 4 HELIX BUNDLE, TRANSCRIPTION REPRESSOR EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR H.VAN INGEN,M.A.BALTUSSEN,J.AELEN,G.W.VUISTER REVDAT 4 09-MAR-22 2F05 1 REMARK REVDAT 3 24-FEB-09 2F05 1 VERSN REVDAT 2 09-MAY-06 2F05 1 JRNL REVDAT 1 28-MAR-06 2F05 0 JRNL AUTH H.VAN INGEN,M.A.BALTUSSEN,J.AELEN,G.W.VUISTER JRNL TITL ROLE OF STRUCTURAL AND DYNAMICAL PLASTICITY IN SIN3: THE JRNL TITL 2 FREE PAH2 DOMAIN IS A FOLDED MODULE IN MSIN3B JRNL REF J.MOL.BIOL. V. 358 485 2006 JRNL REFN ISSN 0022-2836 JRNL PMID 16519900 JRNL DOI 10.1016/J.JMB.2006.01.100 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.05, X-PLOR REMARK 3 AUTHORS : GUENTERT (CYANA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2F05 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000035287. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 150 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.9 MM PAH2 UNIFORM 13C/15N REMARK 210 LABELED, H2O, 100MM KCL, 50 MM REMARK 210 PI BUFFER PH 6.3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING, WITH WATER REMARK 210 -REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 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: NULL 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-30 REMARK 465 RES C SSSEQI REMARK 465 SER A 86 REMARK 465 LEU A 87 REMARK 465 PHE A 88 REMARK 465 THR A 89 REMARK 465 GLY A 90 REMARK 465 ASN A 91 REMARK 465 GLY A 92 REMARK 465 SER A 93 REMARK 465 CYS A 94 REMARK 465 GLU A 95 REMARK 465 MET A 96 REMARK 465 ASN A 97 REMARK 465 SER A 98 REMARK 465 GLY A 99 REMARK 465 GLN A 100 REMARK 465 LYS A 101 REMARK 465 ASN A 102 REMARK 465 GLU A 103 REMARK 465 GLU A 104 REMARK 465 LYS A 105 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 OE2 GLU A 41 HZ2 LYS A 46 1.59 REMARK 500 OE1 GLU A 55 HZ3 LYS A 84 1.59 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 PRO A 49 99.91 -64.97 REMARK 500 1 PRO A 81 94.65 -53.21 REMARK 500 2 SER A 2 -156.26 55.21 REMARK 500 2 HIS A 44 108.38 -49.46 REMARK 500 2 LYS A 46 87.79 -68.08 REMARK 500 2 GLU A 82 54.60 -108.25 REMARK 500 3 PHE A 50 78.07 -158.75 REMARK 500 3 MET A 53 97.86 -40.36 REMARK 500 3 PRO A 81 97.03 -51.75 REMARK 500 4 SER A 4 73.45 62.93 REMARK 500 4 LYS A 46 170.30 74.15 REMARK 500 4 PHE A 50 100.94 -47.50 REMARK 500 4 MET A 53 100.03 -53.49 REMARK 500 5 HIS A 44 78.96 59.99 REMARK 500 5 LYS A 46 88.47 60.72 REMARK 500 5 ARG A 51 133.13 72.06 REMARK 500 5 PHE A 66 39.25 -96.23 REMARK 500 5 ARG A 67 104.84 -59.93 REMARK 500 6 SER A 2 87.82 58.48 REMARK 500 6 SER A 4 67.24 -114.36 REMARK 500 6 PRO A 49 104.89 -56.85 REMARK 500 6 ARG A 51 42.23 -144.06 REMARK 500 6 PHE A 66 49.75 -99.85 REMARK 500 6 PRO A 81 10.73 -62.11 REMARK 500 6 GLU A 82 -82.91 -83.53 REMARK 500 7 THR A 45 81.13 -162.07 REMARK 500 7 LYS A 46 -165.64 52.83 REMARK 500 7 PHE A 50 154.24 75.22 REMARK 500 7 PHE A 66 49.82 -103.62 REMARK 500 7 ARG A 67 96.02 -67.94 REMARK 500 7 GLU A 82 63.13 -119.42 REMARK 500 8 ASP A 3 162.59 176.17 REMARK 500 8 LYS A 46 -175.53 58.32 REMARK 500 9 THR A 45 100.00 -160.51 REMARK 500 9 LYS A 46 -74.83 -57.92 REMARK 500 9 PRO A 49 99.72 -62.24 REMARK 500 10 SER A 2 -167.66 62.63 REMARK 500 10 HIS A 44 -55.43 -138.15 REMARK 500 10 THR A 45 -95.30 63.43 REMARK 500 10 LYS A 46 144.46 -179.45 REMARK 500 10 ARG A 51 68.94 -159.00 REMARK 500 10 PHE A 66 49.05 -100.51 REMARK 500 11 SER A 2 -164.98 -161.35 REMARK 500 11 MET A 53 109.86 -58.76 REMARK 500 11 PHE A 66 55.66 -108.31 REMARK 500 11 PRO A 81 54.30 -66.74 REMARK 500 12 LEU A 43 -80.02 -73.07 REMARK 500 12 HIS A 44 101.88 177.79 REMARK 500 12 LYS A 46 155.29 75.89 REMARK 500 12 PRO A 49 109.57 -52.90 REMARK 500 REMARK 500 THIS ENTRY HAS 125 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 5 ARG A 67 0.07 SIDE CHAIN REMARK 500 11 ARG A 51 0.09 SIDE CHAIN REMARK 500 25 ARG A 85 0.08 SIDE CHAIN REMARK 500 30 ARG A 51 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7315 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS AND RELAXATIOND DATA REMARK 900 RELATED ID: 1PD7 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF MAD1-COMPLEX DBREF 2F05 A 1 105 UNP Q62141 SIN3B_MOUSE 148 252 SEQRES 1 A 105 GLU SER ASP SER VAL GLU PHE ASN ASN ALA ILE SER TYR SEQRES 2 A 105 VAL ASN LYS ILE LYS THR ARG PHE LEU ASP HIS PRO GLU SEQRES 3 A 105 ILE TYR ARG SER PHE LEU GLU ILE LEU HIS THR TYR GLN SEQRES 4 A 105 LYS GLU GLN LEU HIS THR LYS GLY ARG PRO PHE ARG GLY SEQRES 5 A 105 MET SER GLU GLU GLU VAL PHE THR GLU VAL ALA ASN LEU SEQRES 6 A 105 PHE ARG GLY GLN GLU ASP LEU LEU SER GLU PHE GLY GLN SEQRES 7 A 105 PHE LEU PRO GLU ALA LYS ARG SER LEU PHE THR GLY ASN SEQRES 8 A 105 GLY SER CYS GLU MET ASN SER GLY GLN LYS ASN GLU GLU SEQRES 9 A 105 LYS HELIX 1 1 SER A 4 PHE A 21 1 18 HELIX 2 2 HIS A 24 LEU A 43 1 20 HELIX 3 3 SER A 54 PHE A 66 1 13 HELIX 4 4 GLN A 69 LEU A 80 1 12 HELIX 5 5 PRO A 81 ARG A 85 5 5 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