Header list of 1guw.pdb file
Complete list - n 17 2 Bytes
HEADER CHROMATIN-BINDING 01-FEB-02 1GUW TITLE STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1BETA IN COMPLEX WITH THE TITLE 2 LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHROMOBOX PROTEIN HOMOLOG 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CHROMODOMAIN, RESIDUES 8 - 80; COMPND 5 SYNONYM: HETEROCHROMATIN PROTEIN 1 HOMOLOG BETA, HP1 BETA, MODIFIER 1 COMPND 6 PROTEIN, M31; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HISTONE H3.1; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: N-TERMINAL TAIL, RESIDUES 1-18; COMPND 12 SYNONYM: HISTONE H3, NUCLEAR PROTEIN, CHROMOSOMAL PROTEIN, DNA- COMPND 13 BINDING, NUCLEOSOME CORE, MULTIGENE FAMILY, METHYLATION; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: LYSINES 4 AND 9 HAVE BEEN MODIFIED TO N (EPSILON)- COMPND 16 DIMETHYL-LYSINE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 OTHER_DETAILS: BOTH CHEMICALLY SYTHESIZED PEPTIDE AND PEPTIDE SOURCE 15 OBTAINED FROM EXPRESSION IN BACTERIA WERE USED. KEYWDS CHROMATIN-BINDING, LYSINE METHYLATION, HETEROCHROMATIN, HISTONE KEYWDS 2 MODIFICATION EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR P.R.NIELSEN,D.NIETLISPACH,H.R.MOTT,J.M.CALLAGHAN,A.BANNISTER, AUTHOR 2 T.KOUZARIDES,A.G.MURZIN,N.V.MURZINA,E.D.LAUE REVDAT 4 17-JAN-18 1GUW 1 JRNL REVDAT 3 24-FEB-09 1GUW 1 VERSN REVDAT 2 16-MAR-05 1GUW 1 JRNL REVDAT 1 12-MAR-02 1GUW 0 JRNL AUTH P.R.NIELSEN,D.NIETLISPACH,H.R.MOTT,J.M.CALLAGHAN, JRNL AUTH 2 A.BANNISTER,T.KOUZARIDES,A.G.MURZIN,N.V.MURZINA,E.D.LAUE JRNL TITL STRUCTURE OF THE HP1 CHROMODOMAIN BOUND TO HISTONE H3 JRNL TITL 2 METHYLATED AT LYSINE 9 JRNL REF NATURE V. 416 103 2002 JRNL REFN ISSN 0028-0836 JRNL PMID 11882902 JRNL DOI 10.1038/NATURE722 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.J.BALL,N.V.MURZINA,R.W.BROADHURST,A.R.RAINE,S.J.ARCHER, REMARK 1 AUTH 2 F.J.STOTT,A.G.MURZIN,P.B.SINGH,P.J.DOMAILLE,E.D.LAUE REMARK 1 TITL STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM REMARK 1 TITL 2 MOUSE MODIFIER PROTEIN 1 REMARK 1 REF EMBO J. V. 16 2437 1997 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 9171360 REMARK 1 DOI 10.1093/EMBOJ/16.9.2473 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA1.0 REMARK 3 AUTHORS : J.P.LINGE,S.I.O'DONOGHUE,M.NILGES REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GUW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-02. REMARK 100 THE DEPOSITION ID IS D_1290009379. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 150 MM NACL, 20 MM PHOSPHATE REMARK 210 BUFFER, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D; 3D 1H; 15N; 13C REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AZARA, ANZIG, ARIA1.0, CNS1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY OF 75 CONVERGED REMARK 210 STRUCTURES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE 2D AND REMARK 210 3D NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. FOR PROTEIN REMARK 210 ASSIGMENTS THE SAMPLE CONTAINED AN EXCESS OF 1.2 FOLD OF REMARK 210 UNLABELLED PEPTIDE. THE PEPTIDE WAS ASSIGNED USING 13C, 15N REMARK 210 REJECTED NOESY AND TOCSY EXPERIMENTS ON A SAMPLE OF EXCESS 13C, REMARK 210 15N LABELLED PROTEIN TO UNLABELLED PEPTIDE. THE METHYL GROUP REMARK 210 RESONANCES OF LYSINE 4 AND 9 OF THE PEPTIDE WERE CONFIRMED WITH REMARK 210 THE HELP OF A 13C METHYL-SELECTIVELY LABELLED SAMPLE MIXED WITH REMARK 210 UNLABELLED PROTEIN. INTERMOLECULAR CONTACTS WERE OBTAINED FROM A REMARK 210 13C/15N X-FILTERED NOESY SPECTRUM AND A 3D J(CH,NH)- SEPARATED REMARK 210 NOESY SPECTRUM 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 VAL A 10 -147.27 -145.14 REMARK 500 1 LEU A 14 46.69 -176.07 REMARK 500 1 GLU A 15 140.64 -176.58 REMARK 500 1 GLU A 16 135.59 66.44 REMARK 500 1 GLU A 17 42.17 -170.15 REMARK 500 1 LYS A 25 142.64 177.87 REMARK 500 1 ASP A 28 -146.25 -153.67 REMARK 500 1 LYS A 33 -37.15 76.05 REMARK 500 1 LYS A 35 -157.58 -79.74 REMARK 500 1 ASP A 49 41.66 -76.42 REMARK 500 1 ASP A 59 50.00 -110.90 REMARK 500 1 CYS A 60 62.32 -152.40 REMARK 500 1 LYS A 72 -143.28 -65.95 REMARK 500 1 ALA A 74 -26.02 176.87 REMARK 500 1 GLU A 76 -29.93 70.52 REMARK 500 1 ASP A 78 -133.18 -154.01 REMARK 500 1 LYS A 79 -140.97 -68.57 REMARK 500 2 MET A 9 -133.82 56.22 REMARK 500 2 VAL A 10 -40.62 -167.59 REMARK 500 2 GLU A 11 134.10 64.45 REMARK 500 2 GLU A 12 37.56 -174.31 REMARK 500 2 GLU A 15 146.92 65.36 REMARK 500 2 GLU A 16 -39.20 -148.61 REMARK 500 2 LYS A 25 146.04 -172.62 REMARK 500 2 ASP A 28 -149.35 179.95 REMARK 500 2 ASP A 59 44.65 -107.54 REMARK 500 2 GLN A 71 29.05 -76.25 REMARK 500 2 HIS A 75 -37.74 72.49 REMARK 500 2 THR A 77 43.23 -145.52 REMARK 500 2 LYS A 79 47.36 -172.17 REMARK 500 2 SER B 10 136.23 -179.96 REMARK 500 2 LYS B 14 47.22 -164.53 REMARK 500 3 GLU A 11 120.51 -170.58 REMARK 500 3 GLU A 12 -37.83 179.85 REMARK 500 3 VAL A 13 126.30 68.75 REMARK 500 3 LEU A 14 52.24 -175.13 REMARK 500 3 GLU A 16 -146.53 54.39 REMARK 500 3 GLU A 17 -144.12 -86.84 REMARK 500 3 LYS A 25 138.38 -175.47 REMARK 500 3 ASP A 28 -157.89 -175.76 REMARK 500 3 LYS A 33 -15.52 -170.62 REMARK 500 3 LYS A 35 -159.96 -88.49 REMARK 500 3 LYS A 72 125.75 -179.47 REMARK 500 3 ALA A 74 -43.57 178.35 REMARK 500 3 HIS A 75 -129.03 57.45 REMARK 500 3 GLU A 76 -44.96 -164.39 REMARK 500 3 ASP A 78 -133.38 55.55 REMARK 500 3 LYS A 79 -47.71 -174.80 REMARK 500 3 MLY B 4 -130.05 -85.70 REMARK 500 3 MLY B 9 44.73 -82.82 REMARK 500 REMARK 500 THIS ENTRY HAS 532 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AP0 RELATED DB: PDB REMARK 900 STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE REMARK 900 MODIFIER PROTEIN 1, NMR, 26 STRUCTURES REMARK 900 RELATED ID: 1DZ1 RELATED DB: PDB REMARK 900 MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN DBREF 1GUW A 8 9 PDB 1GUW 1GUW 8 9 DBREF 1GUW A 10 80 UNP P23197 CBX1_HUMAN 10 80 DBREF 1GUW B 1 16 UNP P16106 H31_HUMAN 1 16 DBREF 1GUW B 17 18 PDB 1GUW 1GUW 17 18 SEQRES 1 A 73 HIS MET VAL GLU GLU VAL LEU GLU GLU GLU GLU GLU GLU SEQRES 2 A 73 TYR VAL VAL GLU LYS VAL LEU ASP ARG ARG VAL VAL LYS SEQRES 3 A 73 GLY LYS VAL GLU TYR LEU LEU LYS TRP LYS GLY PHE SER SEQRES 4 A 73 ASP GLU ASP ASN THR TRP GLU PRO GLU GLU ASN LEU ASP SEQRES 5 A 73 CYS PRO ASP LEU ILE ALA GLU PHE LEU GLN SER GLN LYS SEQRES 6 A 73 THR ALA HIS GLU THR ASP LYS SER SEQRES 1 B 18 ALA ARG THR MLY GLN THR ALA ARG MLY SER THR GLY GLY SEQRES 2 B 18 LYS ALA PRO GLY GLY MODRES 1GUW MLY B 4 LYS N-DIMETHYL-LYSINE MODRES 1GUW MLY B 9 LYS N-DIMETHYL-LYSINE HET MLY B 4 28 HET MLY B 9 28 HETNAM MLY N-DIMETHYL-LYSINE FORMUL 2 MLY 2(C8 H18 N2 O2) HELIX 1 1 CYS A 60 LYS A 72 1 13 SHEET 1 AA 2 VAL A 23 VAL A 26 0 SHEET 2 AA 2 LEU A 40 TRP A 42 -1 O LYS A 41 N GLU A 24 SHEET 1 AB 2 GLU A 37 TYR A 38 0 SHEET 2 AB 2 GLU A 53 PRO A 54 -1 O GLU A 53 N TYR A 38 SHEET 1 AC 2 LEU A 58 ASP A 59 0 SHEET 2 AC 2 THR B 6 ALA B 7 -1 O THR B 6 N ASP A 59 LINK C THR B 3 N MLY B 4 1555 1555 1.33 LINK C MLY B 4 N GLN B 5 1555 1555 1.33 LINK C ARG B 8 N MLY B 9 1555 1555 1.33 LINK C MLY B 9 N SER B 10 1555 1555 1.33 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 17 2 Bytes