Header list of 1s5q.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 21-JAN-04 1S5Q TITLE SOLUTION STRUCTURE OF MAD1 SID-MSIN3A PAH2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAD PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SIN3 INTERACTION DOMAIN (SID), RESIDUES 6 TO 21; COMPND 5 SYNONYM: MAX DIMERIZER; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SIN3A PROTEIN; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: PAIRED AMPHIPATHIC HELIX 2, (PAH2 REPEAT), RESIDUES 295 TO COMPND 11 383; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE SEQUENCE WAS SYNTHESIZED USING AUTOMATED SOURCE 4 METHODS. THE SEQUENCE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 GENE: SIN3A; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24 KEYWDS PROTEIN-PEPTIDE COMPLEX, AMPHIPATHIC HELIX MOTIF, FOUR-HELIX BUNDLE, KEYWDS 2 REPRESSOR-COREPRESSOR COMPLEX, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.A.SWANSON,P.S.KNOEPFLER,K.HUANG,R.S.KANG,S.M.COWLEY,C.D.LAHERTY, AUTHOR 2 R.N.EISENMAN,I.RADHAKRISHNAN REVDAT 4 02-MAR-22 1S5Q 1 REMARK REVDAT 3 24-FEB-09 1S5Q 1 VERSN REVDAT 2 03-AUG-04 1S5Q 1 JRNL REVDAT 1 06-JUL-04 1S5Q 0 JRNL AUTH K.A.SWANSON,P.S.KNOEPFLER,K.HUANG,R.S.KANG,S.M.COWLEY, JRNL AUTH 2 C.D.LAHERTY,R.N.EISENMAN,I.RADHAKRISHNAN JRNL TITL HBP1 AND MAD1 REPRESSORS BIND THE SIN3 COREPRESSOR PAH2 JRNL TITL 2 DOMAIN WITH OPPOSITE HELICAL ORIENTATIONS. JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 738 2004 JRNL REFN ISSN 1545-9993 JRNL PMID 15235594 JRNL DOI 10.1038/NSMB798 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.BRUBAKER,S.M.COWLEY,K.HUANG,L.LOO,G.S.YOCHUM,D.E.AYER, REMARK 1 AUTH 2 R.N.EISENMAN,I.RADHAKRISHNAN REMARK 1 TITL SOLUTION STRUCTURE OF THE INTERACTING DOMAINS OF THE REMARK 1 TITL 2 MAD-SIN3 COMPLEX: IMPLICATIONS FOR RECRUITMENT OF A REMARK 1 TITL 3 CHROMATIN-MODIFYING COMPLEX REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 103 655 2000 REMARK 1 REFN ISSN 0092-8674 REMARK 1 PMID 11106735 REMARK 1 DOI 10.1016/S0092-8674(00)00168-9 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, ARIA 1.2, CNS 1.1 REMARK 3 AUTHORS : VARIAN NMR INC (VNMR), LINGE, NILGES (ARIA), REMARK 3 BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1S5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1000021400. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE, PH 6, REMARK 210 0.2% NAN3 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0 MM 1:1 SID UNLABELED, PAH2 U REMARK 210 -15N; 1.6 MM 1:1 SID UNLABELED, REMARK 210 PAH2 U-15N,U-13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; REMARK 210 2D_DOUBLE_HALF-FILTERED_NOESY; REMARK 210 3D_13C-SEPARATED_NOESY; 3D_13C- REMARK 210 FILTERED,13C-EDITED_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 : FELIX 98.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMERS ARE THE REMARK 210 20 STRUCTURES WITH THE LOWEST REMARK 210 RESTRAINT ENERGIES, RESTRAINT REMARK 210 VIOLATIONS, AND RMS DEVIATIONS REMARK 210 FROM IDEAL COVALENT GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15 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: 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: 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 ASN A 8 -48.64 -169.96 REMARK 500 1 LEU B 296 -169.94 55.28 REMARK 500 1 GLN B 297 -23.62 -143.39 REMARK 500 1 ASN B 299 11.95 -141.96 REMARK 500 1 TYR B 349 143.54 -173.78 REMARK 500 1 PRO B 381 -173.72 -69.92 REMARK 500 2 MET A 7 40.16 -96.22 REMARK 500 2 ASN A 8 -73.63 -139.01 REMARK 500 2 GLN B 300 90.70 58.64 REMARK 500 2 PRO B 301 48.07 -80.97 REMARK 500 2 PHE B 318 31.80 -83.92 REMARK 500 2 TYR B 349 104.62 64.03 REMARK 500 2 THR B 354 -169.37 -103.50 REMARK 500 2 PHE B 366 71.31 -110.65 REMARK 500 3 ASN A 8 -39.92 -173.58 REMARK 500 3 ILE A 9 -32.86 -145.19 REMARK 500 3 GLN B 300 146.22 64.49 REMARK 500 3 PHE B 318 46.64 -103.65 REMARK 500 3 TYR B 349 -28.41 -160.74 REMARK 500 3 THR B 350 90.17 34.99 REMARK 500 3 PRO B 381 -166.29 -62.95 REMARK 500 4 MET A 7 -3.89 -143.18 REMARK 500 4 LEU B 296 100.77 60.83 REMARK 500 4 ASN B 299 -71.25 -83.18 REMARK 500 4 PHE B 318 37.85 -91.06 REMARK 500 4 PHE B 366 39.04 -92.26 REMARK 500 4 PRO B 381 -163.62 -62.19 REMARK 500 5 ASN A 8 -61.95 -129.73 REMARK 500 5 LEU B 296 110.42 62.00 REMARK 500 5 ASN B 299 -68.33 -158.68 REMARK 500 5 GLN B 300 64.34 -157.18 REMARK 500 5 PHE B 318 30.18 -86.06 REMARK 500 5 THR B 354 -169.29 -125.61 REMARK 500 6 MET A 7 -162.42 -124.95 REMARK 500 6 ASN A 8 -83.37 64.26 REMARK 500 6 TYR B 349 -35.76 -155.23 REMARK 500 6 THR B 350 85.76 36.19 REMARK 500 6 PRO B 351 -167.47 -64.80 REMARK 500 6 PHE B 366 43.90 -105.72 REMARK 500 6 ASP B 382 14.53 59.82 REMARK 500 7 ASN A 8 -73.64 -89.30 REMARK 500 7 LEU B 296 121.13 63.62 REMARK 500 7 ASN B 299 4.94 -156.05 REMARK 500 7 PHE B 318 38.23 -90.16 REMARK 500 7 GLN B 369 56.10 -104.72 REMARK 500 7 ASP B 382 18.38 59.22 REMARK 500 8 ASN A 8 -76.02 69.10 REMARK 500 8 ASN B 348 101.89 59.86 REMARK 500 8 PRO B 381 -171.65 -61.46 REMARK 500 9 ASN A 8 -34.86 -165.71 REMARK 500 REMARK 500 THIS ENTRY HAS 116 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1G1E RELATED DB: PDB REMARK 900 RELATED ID: 1S5R RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF HBP1 SID-MSIN3A PAH2 COMPLEX DBREF 1S5Q A 6 21 UNP Q05195 MAD_HUMAN 6 21 DBREF 1S5Q B 295 383 UNP Q60520 SIN3A_MOUSE 295 383 SEQRES 1 A 16 ARG MET ASN ILE GLN MET LEU LEU GLU ALA ALA ASP TYR SEQRES 2 A 16 LEU GLU ARG SEQRES 1 B 89 SER LEU GLN ASN ASN GLN PRO VAL GLU PHE ASN HIS ALA SEQRES 2 B 89 ILE ASN TYR VAL ASN LYS ILE LYS ASN ARG PHE GLN GLY SEQRES 3 B 89 GLN PRO ASP ILE TYR LYS ALA PHE LEU GLU ILE LEU HIS SEQRES 4 B 89 THR TYR GLN LYS GLU GLN ARG ASN ALA LYS GLU ALA GLY SEQRES 5 B 89 GLY ASN TYR THR PRO ALA LEU THR GLU GLN GLU VAL TYR SEQRES 6 B 89 ALA GLN VAL ALA ARG LEU PHE LYS ASN GLN GLU ASP LEU SEQRES 7 B 89 LEU SER GLU PHE GLY GLN PHE LEU PRO ASP ALA HELIX 1 1 ILE A 9 GLU A 20 1 12 HELIX 2 2 VAL B 302 ARG B 317 1 16 HELIX 3 3 PRO B 322 ALA B 345 1 24 HELIX 4 4 GLU B 355 LEU B 365 1 11 HELIX 5 5 GLU B 370 PHE B 379 1 10 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 2 2 Bytes