Header list of 1ub1.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 27-MAR-03 1UB1
TITLE SOLUTION STRUCTURE OF THE MATRIX ATTACHMENT REGION-BINDING DOMAIN OF
TITLE 2 CHICKEN MECP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATTACHMENT REGION BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MATRIX ATTACHMENT REGION-BINDING DOMAIN;
COMPND 5 SYNONYM: MECP2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-CARBP-EX4.2
KEYWDS CHICKEN METHYL-CPG-BINDING PROTEIN 2 (CMECP2), MAR-BINDING PROTEIN
KEYWDS 2 (ARBP), NMR SPECTROSCOPY, PROTEIN-DNA INTERACTION, STRUCTURAL
KEYWDS 3 PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.HEITMANN,T.MAURER,J.M.WEITZEL,W.H.STRATLING,H.R.KALBITZER,
AUTHOR 2 E.BRUNNER,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1UB1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UB1 1 VERSN
REVDAT 1 05-AUG-03 1UB1 0
JRNL AUTH B.HEITMANN,T.MAURER,J.M.WEITZEL,W.H.STRATLING,H.R.KALBITZER,
JRNL AUTH 2 E.BRUNNER
JRNL TITL SOLUTION STRUCTURE OF THE MATRIX ATTACHMENT REGION-BINDING
JRNL TITL 2 DOMAIN OF CHICKEN MECP2
JRNL REF EUR.J.BIOCHEM. V. 270 3263 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 12869202
JRNL DOI 10.1046/J.1432-1033.2003.03714.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : BRUKER, KARLSRUHE, GERMANY (XWINNMR), GUENTERT, P.
REMARK 3 (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UB1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000005636.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 154MM NACL, 10MM SODIUM
REMARK 210 PHOSPHATE
REMARK 210 PRESSURE : 1 BAR
REMARK 210 SAMPLE CONTENTS : 1-2MM CMECP2 MAR-BD, U-15N, 13C:
REMARK 210 154MM NACL, 10MM SODIUM
REMARK 210 PHOSPHATE; 1-2MM CMECP2 MAR-BD,
REMARK 210 U-15N, 13C: 154MM NACL, 10MM
REMARK 210 SODIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
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 : AURELIA, AUREMOL 1.0, TALOS
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 240
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 64
REMARK 465 GLY A 65
REMARK 465 HIS A 66
REMARK 465 HIS A 67
REMARK 465 HIS A 68
REMARK 465 HIS A 69
REMARK 465 HIS A 70
REMARK 465 HIS A 71
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 O ILE A 140 H GLU A 144 1.34
REMARK 500 H LYS A 108 O TYR A 124 1.41
REMARK 500 O LYS A 108 H TYR A 124 1.47
REMARK 500 O LEU A 139 H PHE A 143 1.50
REMARK 500 H ASN A 127 O LYS A 131 1.56
REMARK 500 O LYS A 108 N TYR A 124 2.17
REMARK 500 O ILE A 140 N GLU A 144 2.19
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 75 140.46 -171.65
REMARK 500 1 GLU A 77 -179.07 72.36
REMARK 500 1 SER A 79 88.12 -169.93
REMARK 500 1 SER A 81 74.35 37.80
REMARK 500 1 LYS A 83 152.63 66.24
REMARK 500 1 ASP A 91 109.54 -57.95
REMARK 500 1 ARG A 92 55.55 39.27
REMARK 500 1 TYR A 96 -166.27 -70.26
REMARK 500 1 ASP A 97 -153.73 -69.49
REMARK 500 1 ASP A 98 -52.19 163.59
REMARK 500 1 THR A 100 -136.35 -121.72
REMARK 500 1 GLU A 103 -49.25 177.07
REMARK 500 1 TRP A 105 125.19 63.96
REMARK 500 1 ARG A 112 40.92 -93.67
REMARK 500 1 LYS A 113 165.58 -43.90
REMARK 500 1 SER A 114 46.83 86.00
REMARK 500 1 ARG A 116 -73.85 65.52
REMARK 500 1 ALA A 118 -154.81 39.63
REMARK 500 1 TYR A 121 -159.96 -70.07
REMARK 500 1 GLN A 129 -38.32 -169.86
REMARK 500 1 LYS A 145 57.35 177.61
REMARK 500 1 ASP A 148 161.57 58.51
REMARK 500 1 THR A 149 -69.94 -106.23
REMARK 500 1 SER A 150 51.12 -169.16
REMARK 500 1 ASP A 155 50.78 -153.55
REMARK 500 1 PHE A 156 -177.14 -48.87
REMARK 500 1 THR A 159 -85.31 -110.51
REMARK 500 1 SER A 167 -70.80 -45.87
REMARK 500 1 ARG A 168 -160.62 -169.62
REMARK 500 1 ARG A 169 179.40 178.23
REMARK 500 1 GLU A 170 120.15 75.40
REMARK 500 1 PRO A 174 -162.24 -75.04
REMARK 500 1 LYS A 175 92.15 -167.36
REMARK 500 1 SER A 179 115.11 -172.10
REMARK 500 1 SER A 182 95.07 -179.00
REMARK 500 1 SER A 185 87.81 84.73
REMARK 500 2 ALA A 74 115.73 -163.68
REMARK 500 2 VAL A 75 115.73 -164.51
REMARK 500 2 GLU A 77 78.08 47.59
REMARK 500 2 SER A 79 82.34 -165.18
REMARK 500 2 GLN A 84 154.16 58.95
REMARK 500 2 ILE A 88 -74.20 -130.95
REMARK 500 2 ARG A 90 -58.81 -143.78
REMARK 500 2 TYR A 96 30.66 -143.48
REMARK 500 2 ASP A 98 73.86 38.98
REMARK 500 2 THR A 100 110.23 179.21
REMARK 500 2 LEU A 101 60.89 29.20
REMARK 500 2 GLU A 103 -36.88 169.24
REMARK 500 2 TRP A 105 124.76 164.66
REMARK 500 2 LYS A 113 -78.33 -41.60
REMARK 500
REMARK 500 THIS ENTRY HAS 341 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3 RELATED DB: TARGETDB
DBREF 1UB1 A 72 196 UNP O42403 O42403_CHICK 72 196
SEQADV 1UB1 MET A 64 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 GLY A 65 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 66 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 67 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 68 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 69 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 70 UNP O42403 EXPRESSION TAG
SEQADV 1UB1 HIS A 71 UNP O42403 EXPRESSION TAG
SEQRES 1 A 133 MET GLY HIS HIS HIS HIS HIS HIS ALA PRO ALA VAL PRO
SEQRES 2 A 133 GLU ALA SER ALA SER PRO LYS GLN ARG ARG SER ILE ILE
SEQRES 3 A 133 ARG ASP ARG GLY PRO MET TYR ASP ASP PRO THR LEU PRO
SEQRES 4 A 133 GLU GLY TRP THR ARG LYS LEU LYS GLN ARG LYS SER GLY
SEQRES 5 A 133 ARG SER ALA GLY LYS TYR ASP VAL TYR LEU ILE ASN PRO
SEQRES 6 A 133 GLN GLY LYS ALA PHE ARG SER LYS VAL GLU LEU ILE ALA
SEQRES 7 A 133 TYR PHE GLU LYS VAL GLY ASP THR SER LEU ASP PRO ASN
SEQRES 8 A 133 ASP PHE ASP PHE THR VAL THR GLY ARG GLY SER PRO SER
SEQRES 9 A 133 ARG ARG GLU GLN ARG PRO PRO LYS LYS ALA LYS SER PRO
SEQRES 10 A 133 LYS SER PRO GLY SER GLY ARG GLY ARG GLY ARG PRO LYS
SEQRES 11 A 133 GLY SER GLY
HELIX 1 1 SER A 135 GLU A 144 1 10
HELIX 2 2 PRO A 153 ASP A 155 5 3
HELIX 3 3 THR A 159 ARG A 163 3 5
SHEET 1 A 3 THR A 106 GLN A 111 0
SHEET 2 A 3 TYR A 121 ILE A 126 -1 O TYR A 124 N LYS A 108
SHEET 3 A 3 ALA A 132 PHE A 133 -1 O PHE A 133 N LEU A 125
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