Header list of 1ap0.pdb file
Complete list - b 16 2 Bytes
HEADER CHROMATIN-BINDING 22-JUL-97 1AP0
TITLE STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER
TITLE 2 PROTEIN 1, NMR, 26 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MODIFIER PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHROMATIN-BINDING (CHROMO), RESIDUES 10 - 80;
COMPND 5 SYNONYM: MOMOD1, HETEROCHROMATIN PROTEIN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21;
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: PET16B
KEYWDS CHROMATIN-BINDING, PROTEIN INTERACTION MOTIF, ALPHA+BETA
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR L.J.BALL,N.V.MURZINA,R.W.BROADHURST,A.R.C.RAINE,S.J.ARCHER,F.J.STOTT,
AUTHOR 2 A.G.MURZIN,P.B.SINGH,P.J.DOMAILLE,E.D.LAUE
REVDAT 3 16-FEB-22 1AP0 1 REMARK
REVDAT 2 24-FEB-09 1AP0 1 VERSN
REVDAT 1 22-JUL-98 1AP0 0
JRNL AUTH L.J.BALL,N.V.MURZINA,R.W.BROADHURST,A.R.RAINE,S.J.ARCHER,
JRNL AUTH 2 F.J.STOTT,A.G.MURZIN,P.B.SINGH,P.J.DOMAILLE,E.D.LAUE
JRNL TITL STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM
JRNL TITL 2 MOUSE MODIFIER PROTEIN 1.
JRNL REF EMBO J. V. 16 2473 1997
JRNL REFN ISSN 0261-4189
JRNL PMID 9171360
JRNL DOI 10.1093/EMBOJ/16.9.2473
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AP0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171081.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2; 3 AND 4D 1H; 15N AND 13C
REMARK 210 SPECTRA: CBCA(CO)NNH; CBCANNH;
REMARK 210 15N-TOCSY-HMQC; HNHB; 13C/15N-
REMARK 210 HCC(CO)NNH; 13C/15N-HCCNNH; 13C-
REMARK 210 HCCH-TOCSY; CBHD; CBHE; DQF-COSY;
REMARK 210 NOESY; 13C AND 15N -NOESY-HMQC;
REMARK 210 15N-1H-COSY; 1H-15N-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SA FROM RANDOM COORDINATES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : 0 VIOLATIONS > 0.5 A
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 24
REMARK 210
REMARK 210 REMARK: TRIPLE-RESONANCE EXPERIMENTS ON 13C/15N DOUBLE-LABELLED
REMARK 210 MATERIAL
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 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 13 49.90 -151.48
REMARK 500 1 GLU A 17 -76.55 -53.33
REMARK 500 1 LYS A 25 177.37 169.59
REMARK 500 1 ASP A 28 -165.61 -168.71
REMARK 500 1 LYS A 33 -19.10 157.53
REMARK 500 1 PHE A 45 -85.38 -133.83
REMARK 500 1 SER A 46 -42.99 -138.62
REMARK 500 1 ASP A 47 -42.15 178.48
REMARK 500 1 GLU A 48 62.47 -151.38
REMARK 500 1 ASP A 49 52.58 -90.45
REMARK 500 1 ASN A 57 -39.41 -143.37
REMARK 500 1 THR A 73 111.46 175.15
REMARK 500 1 ALA A 74 -40.42 -154.43
REMARK 500 1 THR A 77 -78.79 -117.21
REMARK 500 1 ASP A 78 169.76 71.13
REMARK 500 2 MET A 9 97.51 -167.45
REMARK 500 2 GLU A 11 83.41 48.02
REMARK 500 2 GLU A 12 -152.51 63.50
REMARK 500 2 GLU A 15 -86.90 66.35
REMARK 500 2 GLU A 16 112.16 75.97
REMARK 500 2 GLU A 17 -81.53 -102.25
REMARK 500 2 GLU A 18 -67.38 -99.41
REMARK 500 2 GLU A 19 101.81 52.34
REMARK 500 2 LYS A 25 -178.04 162.75
REMARK 500 2 VAL A 32 47.56 -101.14
REMARK 500 2 PHE A 45 45.20 -160.44
REMARK 500 2 ASP A 49 35.67 -93.90
REMARK 500 2 ASN A 50 95.27 -43.54
REMARK 500 2 ASN A 57 10.37 -141.23
REMARK 500 2 ASP A 59 22.95 -140.56
REMARK 500 2 THR A 73 -136.51 -119.80
REMARK 500 2 HIS A 75 79.68 -168.70
REMARK 500 2 GLU A 76 -71.95 176.18
REMARK 500 3 GLU A 12 -175.58 50.17
REMARK 500 3 GLU A 16 -148.98 -68.42
REMARK 500 3 GLU A 20 154.54 67.87
REMARK 500 3 TYR A 21 -73.78 -106.01
REMARK 500 3 LYS A 25 166.80 165.71
REMARK 500 3 LYS A 33 -55.00 162.85
REMARK 500 3 VAL A 36 107.78 55.88
REMARK 500 3 SER A 46 -172.40 175.54
REMARK 500 3 GLU A 48 80.70 167.34
REMARK 500 3 ASN A 50 112.53 57.74
REMARK 500 3 ASN A 57 -41.80 -137.69
REMARK 500 3 SER A 70 -74.21 -51.30
REMARK 500 3 THR A 77 22.15 -142.25
REMARK 500 4 MET A 9 97.65 -167.44
REMARK 500 4 GLU A 11 83.35 47.90
REMARK 500 4 GLU A 12 -152.52 63.68
REMARK 500 4 GLU A 15 -86.99 66.39
REMARK 500
REMARK 500 THIS ENTRY HAS 424 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 29 0.32 SIDE CHAIN
REMARK 500 1 ARG A 30 0.31 SIDE CHAIN
REMARK 500 2 ARG A 29 0.31 SIDE CHAIN
REMARK 500 2 ARG A 30 0.14 SIDE CHAIN
REMARK 500 3 ARG A 29 0.14 SIDE CHAIN
REMARK 500 3 ARG A 30 0.27 SIDE CHAIN
REMARK 500 4 ARG A 29 0.31 SIDE CHAIN
REMARK 500 4 ARG A 30 0.14 SIDE CHAIN
REMARK 500 5 ARG A 29 0.28 SIDE CHAIN
REMARK 500 5 ARG A 30 0.31 SIDE CHAIN
REMARK 500 6 ARG A 29 0.09 SIDE CHAIN
REMARK 500 6 ARG A 30 0.32 SIDE CHAIN
REMARK 500 7 ARG A 29 0.22 SIDE CHAIN
REMARK 500 7 ARG A 30 0.11 SIDE CHAIN
REMARK 500 8 ARG A 29 0.23 SIDE CHAIN
REMARK 500 8 ARG A 30 0.21 SIDE CHAIN
REMARK 500 9 ARG A 29 0.21 SIDE CHAIN
REMARK 500 9 ARG A 30 0.23 SIDE CHAIN
REMARK 500 10 ARG A 29 0.31 SIDE CHAIN
REMARK 500 10 ARG A 30 0.29 SIDE CHAIN
REMARK 500 11 ARG A 29 0.18 SIDE CHAIN
REMARK 500 11 ARG A 30 0.31 SIDE CHAIN
REMARK 500 12 ARG A 29 0.30 SIDE CHAIN
REMARK 500 12 ARG A 30 0.15 SIDE CHAIN
REMARK 500 13 ARG A 29 0.17 SIDE CHAIN
REMARK 500 13 ARG A 30 0.21 SIDE CHAIN
REMARK 500 14 ARG A 29 0.16 SIDE CHAIN
REMARK 500 15 ARG A 29 0.12 SIDE CHAIN
REMARK 500 15 ARG A 30 0.15 SIDE CHAIN
REMARK 500 16 ARG A 29 0.30 SIDE CHAIN
REMARK 500 16 ARG A 30 0.30 SIDE CHAIN
REMARK 500 17 ARG A 29 0.25 SIDE CHAIN
REMARK 500 17 ARG A 30 0.30 SIDE CHAIN
REMARK 500 18 ARG A 29 0.32 SIDE CHAIN
REMARK 500 18 ARG A 30 0.12 SIDE CHAIN
REMARK 500 19 ARG A 29 0.22 SIDE CHAIN
REMARK 500 19 ARG A 30 0.28 SIDE CHAIN
REMARK 500 20 ARG A 29 0.32 SIDE CHAIN
REMARK 500 20 ARG A 30 0.28 SIDE CHAIN
REMARK 500 21 ARG A 29 0.20 SIDE CHAIN
REMARK 500 21 ARG A 30 0.30 SIDE CHAIN
REMARK 500 22 ARG A 30 0.25 SIDE CHAIN
REMARK 500 23 ARG A 29 0.22 SIDE CHAIN
REMARK 500 23 ARG A 30 0.31 SIDE CHAIN
REMARK 500 24 ARG A 29 0.30 SIDE CHAIN
REMARK 500 24 ARG A 30 0.29 SIDE CHAIN
REMARK 500 25 ARG A 29 0.31 SIDE CHAIN
REMARK 500 25 ARG A 30 0.12 SIDE CHAIN
REMARK 500 26 ARG A 29 0.11 SIDE CHAIN
REMARK 500 26 ARG A 30 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AP0 A 10 80 UNP P83917 CBX1_MOUSE 10 80
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
HELIX 1 1 PRO A 61 PHE A 67 1 7
SHEET 1 A 3 THR A 51 PRO A 54 0
SHEET 2 A 3 VAL A 36 LEU A 40 -1 N LEU A 40 O THR A 51
SHEET 3 A 3 VAL A 26 VAL A 31 -1 N ARG A 30 O GLU A 37
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 - b 16 2 Bytes