Header list of 2czy.pdb file
Complete list - r 9 2 Bytes
HEADER GENE REGULATION 20-JUL-05 2CZY
TITLE SOLUTION STRUCTURE OF THE NRSF/REST-MSIN3B PAH1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAH1 DOMAIN (RESIDUES 31-107);
COMPND 5 SYNONYM: SIN3B, TRANSCRIPTIONAL COREPRESSOR SIN3B, HISTONE
COMPND 6 DEACETYLASE COMPLEX SUBUNIT SIN3B;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRANSCRIPTION FACTOR REST (VERSION 3);
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SIN3 INTERACTION DOMAIN (RESIDUES 43-57);
COMPND 12 SYNONYM: NRSF/REST;
COMPND 13 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;
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: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS NRSF, SIN3, PAH1, TRANSCRIPTIONAL REPRESSOR, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.NOMURA,H.UDA-TOCHIO,K.MURAI,N.MORI,Y.NISHIMURA
REVDAT 3 09-MAR-22 2CZY 1 REMARK
REVDAT 2 24-FEB-09 2CZY 1 VERSN
REVDAT 1 20-DEC-05 2CZY 0
JRNL AUTH M.NOMURA,H.UDA-TOCHIO,K.MURAI,N.MORI,Y.NISHIMURA
JRNL TITL THE NEURAL REPRESSOR NRSF/REST BINDS THE PAH1 DOMAIN OF THE
JRNL TITL 2 SIN3 COREPRESSOR BY USING ITS DISTINCT SHORT HYDROPHOBIC
JRNL TITL 3 HELIX
JRNL REF J.MOL.BIOL. V. 354 903 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16288918
JRNL DOI 10.1016/J.JMB.2005.10.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CZY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000024815.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5-0.8MM PAH1 U-15N,13C; 0.5
REMARK 210 -0.8MM SID; 20MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER; 0.5-0.8MM PAH1
REMARK 210 U-15N,13C; 0.5-0.8MM SID; 20MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D_X
REMARK 210 -FILTERED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_13C-FILTERED_
REMARK 210 13C-EDITED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2004, NMRVIEW 5.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 VAL A 32 83.88 -67.62
REMARK 500 1 GLN A 68 39.51 71.38
REMARK 500 1 PHE A 83 51.11 -107.03
REMARK 500 1 THR B 55 78.47 -169.98
REMARK 500 2 HIS A 33 -161.58 -106.34
REMARK 500 2 GLN A 68 40.57 70.90
REMARK 500 2 PHE A 83 61.05 -106.55
REMARK 500 2 THR B 55 93.61 -171.90
REMARK 500 3 VAL A 32 83.12 -63.10
REMARK 500 3 GLN A 68 45.06 74.83
REMARK 500 3 THR B 55 93.25 -171.83
REMARK 500 4 PHE A 83 58.79 -116.31
REMARK 500 4 THR B 55 93.82 -172.40
REMARK 500 5 VAL A 32 77.55 -65.71
REMARK 500 5 HIS A 33 -169.76 -123.47
REMARK 500 5 PHE A 83 54.02 -111.78
REMARK 500 5 THR B 55 71.00 -167.65
REMARK 500 6 VAL A 32 86.45 -70.00
REMARK 500 6 GLN A 68 43.84 75.26
REMARK 500 6 TYR A 101 68.77 -104.34
REMARK 500 6 ILE A 105 84.28 -154.68
REMARK 500 6 THR B 55 70.04 -170.85
REMARK 500 7 VAL A 32 91.37 -63.20
REMARK 500 7 GLN A 68 39.82 70.04
REMARK 500 7 PHE A 83 52.67 -112.67
REMARK 500 7 THR B 55 84.69 -167.89
REMARK 500 8 VAL A 32 -81.40 -60.22
REMARK 500 8 GLN A 68 41.05 73.87
REMARK 500 8 PHE A 83 53.47 -106.87
REMARK 500 8 PHE A 96 30.32 -100.00
REMARK 500 8 PRO A 98 176.96 -53.38
REMARK 500 8 THR B 55 70.23 -172.51
REMARK 500 9 HIS A 33 -161.71 -125.98
REMARK 500 9 SER A 50 42.31 -107.90
REMARK 500 9 PHE A 83 50.03 -119.92
REMARK 500 9 PRO A 98 177.03 -53.63
REMARK 500 9 TYR A 101 75.13 -102.55
REMARK 500 9 THR B 55 79.27 -170.36
REMARK 500 10 VAL A 32 82.12 -62.80
REMARK 500 10 HIS A 33 -164.51 -115.81
REMARK 500 10 GLN A 68 53.76 71.93
REMARK 500 10 PHE A 83 55.81 -114.62
REMARK 500 10 ILE A 105 80.11 -162.07
REMARK 500 10 THR B 55 84.10 -171.06
REMARK 500 11 THR B 55 78.11 -171.41
REMARK 500 12 VAL A 32 75.69 -66.93
REMARK 500 12 HIS A 33 -165.70 -119.20
REMARK 500 12 GLN A 68 49.38 71.02
REMARK 500 12 PHE A 83 61.67 -107.26
REMARK 500 12 PHE A 96 30.03 -99.79
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
DBREF 2CZY A 31 107 UNP Q62141 SIN3B_MOUSE 31 107
DBREF 2CZY B 43 57 UNP Q13127 Q13127_HUMAN 43 57
SEQRES 1 A 77 PRO VAL HIS VAL GLU ASP ALA LEU THR TYR LEU ASP GLN
SEQRES 2 A 77 VAL LYS ILE ARG PHE GLY SER ASP PRO ALA THR TYR ASN
SEQRES 3 A 77 GLY PHE LEU GLU ILE MET LYS GLU PHE LYS SER GLN SER
SEQRES 4 A 77 ILE ASP THR PRO GLY VAL ILE ARG ARG VAL SER GLN LEU
SEQRES 5 A 77 PHE HIS GLU HIS PRO ASP LEU ILE VAL GLY PHE ASN ALA
SEQRES 6 A 77 PHE LEU PRO LEU GLY TYR ARG ILE ASP ILE PRO LYS
SEQRES 1 B 15 ALA PRO GLN LEU ILE MET LEU ALA ASN VAL ALA LEU THR
SEQRES 2 B 15 GLY GLU
HELIX 1 1 VAL A 34 ARG A 47 1 14
HELIX 2 2 PRO A 52 LYS A 66 1 15
HELIX 3 3 THR A 72 LEU A 82 1 11
HELIX 4 4 PRO A 87 ASN A 94 1 8
HELIX 5 5 PRO B 44 LEU B 54 1 11
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