Header list of 1a5j.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 16-FEB-98 1A5J
TITLE CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: B-MYB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN, REPEAT 2 AND REPEAT 3;
COMPND 5 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: HB101;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS DNA-BINDING PROTEIN, PROTOONCOGENE PRODUCT, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR P.B.MCINTOSH,M.D.CARR,U.WOLLBORN,T.A.FRENKIEL,J.FEENEY,J.E.MCCORMICK,
AUTHOR 2 K.H.KLEMPNAUER
REVDAT 3 16-FEB-22 1A5J 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1A5J 1 VERSN
REVDAT 1 01-JUL-98 1A5J 0
JRNL AUTH P.B.MCINTOSH,T.A.FRENKIEL,U.WOLLBORN,J.E.MCCORMICK,
JRNL AUTH 2 K.H.KLEMPNAUER,J.FEENEY,M.D.CARR
JRNL TITL SOLUTION STRUCTURE OF THE B-MYB DNA-BINDING DOMAIN: A
JRNL TITL 2 POSSIBLE ROLE FOR CONFORMATIONAL INSTABILITY OF THE PROTEIN
JRNL TITL 3 IN DNA BINDING AND CONTROL OF GENE EXPRESSION.
JRNL REF BIOCHEMISTRY V. 37 9619 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9657674
JRNL DOI 10.1021/BI972861Z
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.D.CARR,U.WOLLBORN,P.B.MCINTOSH,T.A.FRENKIEL,J.E.MCCORMICK,
REMARK 1 AUTH 2 C.J.BAUER,K.H.KLEMPNAUER,J.FEENEY
REMARK 1 TITL STRUCTURE OF THE B-MYB DNA-BINDING DOMAIN IN SOLUTION AND
REMARK 1 TITL 2 EVIDENCE FOR MULTIPLE CONFORMATIONS IN THE REGION OF
REMARK 1 TITL 3 REPEAT-2 INVOLVED IN DNA BINDING. IMPLICATIONS FOR
REMARK 1 TITL 4 SEQUENCE-SPECIFIC DNA BINDING BY MYB PROTEINS
REMARK 1 REF EUR.J.BIOCHEM. V. 235 721 1996
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A5J 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_1000170418.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D DQF-COSY; TOCSY; NOESY; 2D
REMARK 210 1H/13C HMQC; 2D F2 12C-FILTERED
REMARK 210 TOCSY; 3D 1H/13C HMQC-NOESY;
REMARK 210 HCCH-COSY; HCCH-TOCSY; 3D 1H/15N
REMARK 210 NOESY-HSQC; NOESY-HMQC; HNHA;
REMARK 210 HNHB; HMQC-NOESY-HMQC; ROESY-
REMARK 210 HMQC; TOCSY-HMQC; 3D-1H/15N/13C
REMARK 210 CBCANH; CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE CONSTRAINT ORVAN DER
REMARK 210 WAALS VIOLATIONS >0.5A,NO
REMARK 210 DIHEDRAL ANGLE CONSTRAINT
REMARK 210 VIOLATIONS >6 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING DOUBLE AND TRIPLE
REMARK 210 RESONANCE NMR SPECTROSCOPY ON 13C/15N AND 15N LABELED B-MYB.
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 ILE A 33 H LEU A 37 1.48
REMARK 500 O VAL A 22 H GLY A 26 1.55
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 ILE A 2 71.79 65.11
REMARK 500 1 PRO A 3 -163.30 -75.05
REMARK 500 1 LYS A 7 20.07 -78.52
REMARK 500 1 GLU A 13 -75.62 -51.62
REMARK 500 1 THR A 27 55.38 71.62
REMARK 500 1 LYS A 43 -138.83 -80.83
REMARK 500 1 GLN A 44 66.09 35.55
REMARK 500 1 CYS A 45 -44.06 -166.27
REMARK 500 1 ARG A 46 -35.17 -36.79
REMARK 500 1 ARG A 48 -41.18 -174.65
REMARK 500 1 ASN A 51 75.62 -110.05
REMARK 500 1 HIS A 52 -63.78 -160.41
REMARK 500 1 LEU A 53 123.41 -39.93
REMARK 500 1 ASN A 54 65.45 178.23
REMARK 500 1 PRO A 55 -157.74 -74.95
REMARK 500 1 LYS A 58 35.40 -176.15
REMARK 500 1 LYS A 59 110.31 56.42
REMARK 500 1 SER A 60 -43.46 85.28
REMARK 500 1 SER A 61 -154.17 -58.27
REMARK 500 1 THR A 63 -158.30 -124.27
REMARK 500 1 GLU A 64 -82.04 -80.85
REMARK 500 1 LEU A 77 -73.23 -123.95
REMARK 500 1 THR A 92 -169.80 -107.20
REMARK 500 1 SER A 102 -77.22 -73.46
REMARK 500 1 LYS A 107 86.06 -64.49
REMARK 500 1 VAL A 108 -46.79 -155.99
REMARK 500 1 ASP A 109 33.52 -92.31
REMARK 500 2 LEU A 5 95.55 37.97
REMARK 500 2 VAL A 6 -144.05 -128.81
REMARK 500 2 LYS A 7 28.54 38.56
REMARK 500 2 PRO A 9 -168.89 -74.97
REMARK 500 2 LYS A 12 -32.11 -38.15
REMARK 500 2 ILE A 19 -72.60 -63.07
REMARK 500 2 LEU A 21 -77.07 -81.25
REMARK 500 2 THR A 27 -71.19 160.60
REMARK 500 2 LYS A 28 64.47 166.25
REMARK 500 2 LYS A 43 -51.38 -144.02
REMARK 500 2 CYS A 45 -65.10 -162.48
REMARK 500 2 ARG A 46 46.12 -82.91
REMARK 500 2 ASN A 51 48.77 -90.38
REMARK 500 2 HIS A 52 -66.85 -101.63
REMARK 500 2 LEU A 53 105.50 -40.39
REMARK 500 2 PRO A 55 -89.71 -75.00
REMARK 500 2 GLU A 56 165.53 54.22
REMARK 500 2 LYS A 58 92.15 88.78
REMARK 500 2 LYS A 59 -165.17 43.77
REMARK 500 2 SER A 61 -150.82 -172.14
REMARK 500 2 THR A 63 -156.82 -124.60
REMARK 500 2 GLU A 64 -81.59 -82.06
REMARK 500 2 ILE A 69 -70.95 -38.74
REMARK 500
REMARK 500 THIS ENTRY HAS 981 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A5J A 3 110 UNP Q03237 MYBB_CHICK 79 186
SEQRES 1 A 110 GLY ILE PRO ASP LEU VAL LYS GLY PRO TRP THR LYS GLU
SEQRES 2 A 110 GLU ASP GLN LYS VAL ILE GLU LEU VAL LYS LYS TYR GLY
SEQRES 3 A 110 THR LYS GLN TRP THR LEU ILE ALA LYS HIS LEU LYS GLY
SEQRES 4 A 110 ARG LEU GLY LYS GLN CYS ARG GLU ARG TRP HIS ASN HIS
SEQRES 5 A 110 LEU ASN PRO GLU VAL LYS LYS SER SER TRP THR GLU GLU
SEQRES 6 A 110 GLU ASP ARG ILE ILE PHE GLU ALA HIS LYS VAL LEU GLY
SEQRES 7 A 110 ASN ARG TRP ALA GLU ILE ALA LYS LEU LEU PRO GLY ARG
SEQRES 8 A 110 THR ASP ASN ALA VAL LYS ASN HIS TRP ASN SER THR ILE
SEQRES 9 A 110 LYS ARG LYS VAL ASP THR
HELIX 1 1 LYS A 12 TYR A 25 1 14
HELIX 2 2 TRP A 30 HIS A 36 1 7
HELIX 3 3 ARG A 46 TRP A 49 1 4
HELIX 4 4 GLU A 64 GLU A 72 1 9
HELIX 5 5 TRP A 81 LEU A 87 1 7
HELIX 6 6 ASP A 93 SER A 102 1 10
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