HEADER TRANSCRIPTION 25-FEB-05 1WZ6
TITLE SOLUTION STRUCTURE OF THE HMG_BOX DOMAIN OF MURINE BOBBY SOX HOMOLOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HMG-BOX TRANSCRIPTION FACTOR BBX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HMG_BOX DOMAIN;
COMPND 5 SYNONYM: BOBBY SOX HOMOLOG;
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 GENE: BBX;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040719-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BOBBY SOX HOMOLOG, TRANSCRIPTION FACTOR, HMG_BOX DOMAIN, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 3 RSGI, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 4 ANALYSES, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WZ6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WZ6 1 VERSN
REVDAT 1 25-AUG-05 1WZ6 0
JRNL AUTH H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE HMG_BOX DOMAIN OF MURINE BOBBY SOX
JRNL TITL 2 HOMOLOG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WZ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.55MM HMG_BOX DOMAIN U-13C,
REMARK 210 15N; 20MM D-TRIS-HCL(PH7.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.913, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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: 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: 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 PRO A 51 H GLN A 55 1.52
REMARK 500 O LYS A 54 H THR A 58 1.52
REMARK 500 O ALA A 43 H ALA A 47 1.53
REMARK 500 O ASN A 35 HG1 THR A 39 1.58
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 SER A 5 140.83 178.76
REMARK 500 1 ARG A 9 126.70 174.23
REMARK 500 1 PRO A 11 -89.22 -74.99
REMARK 500 1 ARG A 27 -38.82 -38.45
REMARK 500 1 HIS A 30 80.09 -159.07
REMARK 500 1 LEU A 33 165.42 -43.69
REMARK 500 1 VAL A 48 51.22 -109.77
REMARK 500 1 MET A 69 109.76 -45.91
REMARK 500 1 LYS A 70 -68.44 -143.66
REMARK 500 1 SER A 77 98.94 179.86
REMARK 500 1 SER A 80 -50.11 -157.54
REMARK 500 2 SER A 5 -58.76 -136.84
REMARK 500 2 SER A 6 -59.29 -168.66
REMARK 500 2 ALA A 8 -65.09 -129.01
REMARK 500 2 ARG A 27 -38.47 -38.67
REMARK 500 2 LEU A 33 157.81 -40.54
REMARK 500 2 VAL A 48 53.57 -113.25
REMARK 500 2 GLN A 55 -70.91 -57.69
REMARK 500 2 MET A 69 104.13 -38.21
REMARK 500 2 LYS A 70 -63.67 -155.56
REMARK 500 2 ALA A 71 71.04 -109.21
REMARK 500 2 ARG A 76 -69.45 -136.65
REMARK 500 2 SER A 77 82.28 -175.77
REMARK 500 3 SER A 3 117.77 -178.81
REMARK 500 3 ARG A 9 147.98 174.73
REMARK 500 3 ARG A 10 163.26 64.74
REMARK 500 3 LEU A 25 -70.49 -46.62
REMARK 500 3 ASP A 34 -81.79 -90.06
REMARK 500 3 ASN A 35 -57.80 -145.96
REMARK 500 3 GLN A 55 -72.40 -52.57
REMARK 500 3 LYS A 70 -76.76 -107.28
REMARK 500 3 ASN A 72 104.91 -45.01
REMARK 500 3 ARG A 76 145.39 62.37
REMARK 500 3 SER A 77 -64.32 -104.24
REMARK 500 3 SER A 80 132.17 -172.02
REMARK 500 3 SER A 81 128.68 -39.76
REMARK 500 4 SER A 3 -58.73 -132.82
REMARK 500 4 ARG A 9 85.17 54.30
REMARK 500 4 ARG A 10 165.62 179.52
REMARK 500 4 PRO A 11 -167.78 -74.97
REMARK 500 4 LEU A 25 -70.88 -42.04
REMARK 500 4 ASP A 34 51.52 -110.16
REMARK 500 4 ASN A 35 -65.94 69.00
REMARK 500 4 VAL A 48 60.55 -119.85
REMARK 500 4 GLN A 55 -73.78 -61.46
REMARK 500 4 MET A 69 95.21 -62.49
REMARK 500 4 LYS A 70 -61.98 -127.00
REMARK 500 4 ASN A 72 95.84 -161.92
REMARK 500 4 TYR A 75 -86.70 54.35
REMARK 500 4 ARG A 76 -68.83 70.15
REMARK 500
REMARK 500 THIS ENTRY HAS 243 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: MMT008001260.1 RELATED DB: TARGETDB
DBREF 1WZ6 A 8 76 UNP Q8CDV1 Q8CDV1_MOUSE 80 148
SEQADV 1WZ6 GLY A 1 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 2 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 3 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 GLY A 4 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 5 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 6 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 GLY A 7 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 77 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 GLY A 78 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 PRO A 79 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 80 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 SER A 81 UNP Q8CDV1 CLONING ARTIFACT
SEQADV 1WZ6 GLY A 82 UNP Q8CDV1 CLONING ARTIFACT
SEQRES 1 A 82 GLY SER SER GLY SER SER GLY ALA ARG ARG PRO MET ASN
SEQRES 2 A 82 ALA PHE LEU LEU PHE CYS LYS ARG HIS ARG SER LEU VAL
SEQRES 3 A 82 ARG GLN GLU HIS PRO ARG LEU ASP ASN ARG GLY ALA THR
SEQRES 4 A 82 LYS ILE LEU ALA ASP TRP TRP ALA VAL LEU ASP PRO LYS
SEQRES 5 A 82 GLU LYS GLN LYS TYR THR ASP MET ALA LYS GLU TYR LYS
SEQRES 6 A 82 ASP ALA PHE MET LYS ALA ASN PRO GLY TYR ARG SER GLY
SEQRES 7 A 82 PRO SER SER GLY
HELIX 1 1 ALA A 14 GLU A 29 1 16
HELIX 2 2 ARG A 36 ALA A 47 1 12
HELIX 3 3 PRO A 51 PHE A 68 1 18
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
(ATOM LINES ARE NOT SHOWN.)
END
