Header list of 1dz1.pdb file
Complete list - r 7 2 Bytes
HEADER CHROMATIN STRUCTURE 11-FEB-00 1DZ1
TITLE MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MODIFIER 1 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SHADOW CHROMO DOMAIN, RESIDUES 104-171;
COMPND 5 SYNONYM: M31, HP1 BETA, MOMOD1, HETEROCHROMATIN PROTEIN 1;
COMPND 6 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS CHROMATIN STRUCTURE, CHROMO DOMAIN, HETEROCHROMATIN PROTEIN PROTEIN
KEYWDS 2 INTERACTION, DIMERIC
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR S.V.BRASHER,B.O.SMITH,R.H.FOGH,D.NIETLISPACH,A.THIRU,P.R.NIELSEN,
AUTHOR 2 R.W.BROADHURST,L.J.BALL,N.MURZINA,E.D.LAUE
REVDAT 4 07-MAR-18 1DZ1 1 SOURCE
REVDAT 3 24-FEB-09 1DZ1 1 VERSN
REVDAT 2 19-JUL-00 1DZ1 1 DBREF
REVDAT 1 09-APR-00 1DZ1 0
JRNL AUTH S.V.BRASHER,B.O.SMITH,R.H.FOGH,D.NIETLISPACH,A.THIRU,
JRNL AUTH 2 P.R.NIELSEN,R.W.BROADHURST,L.J.BALL,N.MURZINA,E.D.LAUE
JRNL TITL THE STRUCTURE OF MOUSE HP1 SUGGESTS A UNIQUE MODE OF SINGLE
JRNL TITL 2 PEPTIDE RECOGNITION BY THE SHADOW CHROMO DOMAIN DIMER
JRNL REF EMBO J. V. 19 1587 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10747027
JRNL DOI 10.1093/EMBOJ/19.7.1587
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. STRUCTURE WAS GENERATED FROM EXPERIMENTS
REMARK 3 CARRIED OUT AT 303-308K WITH PH 7.5-8.0
REMARK 4
REMARK 4 1DZ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1290004588.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.6-1.4 MM MOUSE HP1 C-TERMINAL
REMARK 210 DOMAIN (AS MONOMER), 10 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 10 MM
REMARK 210 PERDEUTERATED DTT, 0.05% SODIUM
REMARK 210 AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA, ANSIG, CNS, ARIA
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST NOE VIOLATION ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. DOUBLE-HALF FILTERED
REMARK 210 2D NOESY AND HALF-FILTERED HSQC-NOESY ON A MIXED LABELED/
REMARK 210 UNLABELED SAMPLE WERE USED TO DISTINGUISH INTRA- AND INTER-
REMARK 210 MONOMER NOES. RESIDUES 102-109 AND 171 ARE INSUFFICIENTLY
REMARK 210 CONSTRAINED BY THE INPUT DATA AND SHOULD BE CONSIDERED OF
REMARK 210 UNKNOWN STRUCTURE. THUS THE STRUCTURE IS ONLY DEFINED FOR
REMARK 210 RESIDUES 110 - 170.
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 LYS A 104 53.70 -172.14
REMARK 500 1 GLU A 106 -101.87 -63.09
REMARK 500 1 SER A 107 -31.73 71.84
REMARK 500 1 GLU A 108 -34.04 -163.97
REMARK 500 1 ARG A 121 132.07 -170.55
REMARK 500 1 THR A 126 -140.93 -161.52
REMARK 500 1 ASP A 127 133.23 -176.60
REMARK 500 1 SER A 129 32.96 -166.00
REMARK 500 1 ALA A 144 -153.36 -89.08
REMARK 500 1 ASP A 145 135.45 -177.44
REMARK 500 1 ASN A 153 43.28 -77.53
REMARK 500 1 VAL A 154 -45.44 -165.65
REMARK 500 1 CYS A 156 58.28 -140.12
REMARK 500 1 ARG A 167 40.62 -90.50
REMARK 500 1 LEU A 168 -165.82 -74.94
REMARK 500 1 THR A 169 47.38 177.60
REMARK 500 1 TRP A 170 48.45 -80.74
REMARK 500 1 LYS B 104 53.66 -172.09
REMARK 500 1 GLU B 106 -101.79 -63.07
REMARK 500 1 SER B 107 -31.64 71.70
REMARK 500 1 GLU B 108 -33.98 -164.02
REMARK 500 1 ARG B 121 132.03 -170.62
REMARK 500 1 THR B 126 -140.92 -161.50
REMARK 500 1 ASP B 127 133.20 -176.63
REMARK 500 1 SER B 129 33.26 -165.93
REMARK 500 1 ALA B 144 -153.14 -89.64
REMARK 500 1 ASP B 145 135.39 -177.48
REMARK 500 1 ASN B 153 43.27 -77.54
REMARK 500 1 VAL B 154 -45.35 -165.66
REMARK 500 1 CYS B 156 58.32 -140.06
REMARK 500 1 ARG B 167 40.62 -90.52
REMARK 500 1 LEU B 168 -165.86 -74.91
REMARK 500 1 THR B 169 47.34 177.68
REMARK 500 1 TRP B 170 48.40 -80.71
REMARK 500 2 GLU A 106 -121.62 -72.43
REMARK 500 2 LYS A 109 128.17 64.90
REMARK 500 2 ARG A 121 128.42 -171.14
REMARK 500 2 ASP A 127 48.39 -89.25
REMARK 500 2 SER A 129 -44.71 74.48
REMARK 500 2 TRP A 138 140.82 71.59
REMARK 500 2 ASP A 142 -44.05 75.78
REMARK 500 2 GLU A 143 -150.32 -71.80
REMARK 500 2 ALA A 144 147.46 -175.16
REMARK 500 2 CYS A 156 69.83 -151.90
REMARK 500 2 ARG A 167 -55.77 -133.53
REMARK 500 2 LEU A 168 -153.17 56.48
REMARK 500 2 THR A 169 -60.39 177.97
REMARK 500 2 GLU B 106 -121.61 -72.47
REMARK 500 2 LYS B 109 127.93 64.97
REMARK 500 2 ARG B 121 128.40 -171.15
REMARK 500
REMARK 500 THIS ENTRY HAS 503 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 999
REMARK 999 SEQUENCE
REMARK 999 HIS A 102 CLONING ARTIFACT MUTATION ARISING FROM VECTOR
REMARK 999 MET A 103 CLONING ARTIFACT MUTATION ARISING FROM VECTOR
REMARK 999 HIS B 102 CLONING ARTIFACT MUTATION ARISING FROM VECTOR
REMARK 999 MET B 103 CLONING ARTIFACT MUTATION ARISING FROM VECTOR
DBREF 1DZ1 A 102 103 PDB 1DZ1 1DZ1 102 103
DBREF 1DZ1 A 104 171 UNP P83917 CBX1_MOUSE 104 171
DBREF 1DZ1 B 102 103 PDB 1DZ1 1DZ1 102 103
DBREF 1DZ1 B 104 171 UNP P83917 CBX1_MOUSE 104 171
SEQRES 1 A 70 HIS MET LYS GLU GLU SER GLU LYS PRO ARG GLY PHE ALA
SEQRES 2 A 70 ARG GLY LEU GLU PRO GLU ARG ILE ILE GLY ALA THR ASP
SEQRES 3 A 70 SER SER GLY GLU LEU MET PHE LEU MET LYS TRP LYS ASN
SEQRES 4 A 70 SER ASP GLU ALA ASP LEU VAL PRO ALA LYS GLU ALA ASN
SEQRES 5 A 70 VAL LYS CYS PRO GLN VAL VAL ILE SER PHE TYR GLU GLU
SEQRES 6 A 70 ARG LEU THR TRP HIS
SEQRES 1 B 70 HIS MET LYS GLU GLU SER GLU LYS PRO ARG GLY PHE ALA
SEQRES 2 B 70 ARG GLY LEU GLU PRO GLU ARG ILE ILE GLY ALA THR ASP
SEQRES 3 B 70 SER SER GLY GLU LEU MET PHE LEU MET LYS TRP LYS ASN
SEQRES 4 B 70 SER ASP GLU ALA ASP LEU VAL PRO ALA LYS GLU ALA ASN
SEQRES 5 B 70 VAL LYS CYS PRO GLN VAL VAL ILE SER PHE TYR GLU GLU
SEQRES 6 B 70 ARG LEU THR TRP HIS
HELIX 1 1 GLY A 112 ARG A 115 5 4
HELIX 2 2 ALA A 149 LYS A 155 1 7
HELIX 3 3 PRO A 157 GLU A 166 1 10
HELIX 4 4 GLY B 112 ARG B 115 5 4
HELIX 5 5 ALA B 149 LYS B 155 1 7
HELIX 6 6 PRO B 157 GLU B 166 1 10
SHEET 1 1 3 PRO A 119 ASP A 127 0
SHEET 2 1 3 LEU A 132 TRP A 138 -1 O LYS A 137 N GLU A 120
SHEET 3 1 3 ASP A 145 PRO A 148 -1 N VAL A 147 O PHE A 134
SHEET 1 2 3 PRO B 119 ASP B 127 0
SHEET 2 2 3 LEU B 132 TRP B 138 -1 O LYS B 137 N GLU B 120
SHEET 3 2 3 ASP B 145 PRO B 148 -1 N VAL B 147 O PHE B 134
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 7 2 Bytes