Header list of 2da2.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 13-DEC-05 2DA2
TITLE SOLUTION STRUCTURE OF THE SECOND HOMEOBOX DOMAIN OF AT-BINDING
TITLE 2 TRANSCRIPTION FACTOR 1 (ATBF1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-FETOPROTEIN ENHANCER BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE SECOND HOMEOBOX DOMAIN;
COMPND 5 SYNONYM: AT MOTIF-BINDING FACTOR, AT-BINDING TRANSCRIPTION FACTOR 1,
COMPND 6 ATBF1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ATBF1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050620-20;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS HOMEOBOX DOMAIN, THREE HELICES WITH THE DNA BINDING HELIX-TURN-HELIX
KEYWDS 2 MOTIF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OHNISHI,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DA2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DA2 1 VERSN
REVDAT 1 13-JUN-06 2DA2 0
JRNL AUTH S.OHNISHI,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND HOMEOBOX DOMAIN OF
JRNL TITL 2 AT-BINDING TRANSCRIPTION FACTOR 1 (ATBF1)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DA2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025173.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM PROTEIN U-15N,13C; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR 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 LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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: 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 9 43.53 34.43
REMARK 500 1 PRO A 67 1.71 -69.79
REMARK 500 2 SER A 6 169.63 -48.38
REMARK 500 2 SER A 65 143.47 -175.01
REMARK 500 2 PRO A 67 93.41 -69.76
REMARK 500 2 SER A 69 109.31 -44.51
REMARK 500 3 SER A 6 172.48 -56.58
REMARK 500 3 SER A 10 116.17 -165.34
REMARK 500 3 ARG A 63 129.58 -34.48
REMARK 500 3 SER A 69 134.32 -35.45
REMARK 500 4 SER A 9 42.48 39.73
REMARK 500 4 THR A 12 87.68 -69.73
REMARK 500 4 PRO A 67 89.81 -69.80
REMARK 500 4 SER A 69 115.24 -162.27
REMARK 500 5 SER A 2 46.24 -80.50
REMARK 500 5 SER A 5 42.27 39.97
REMARK 500 5 LYS A 64 158.98 -39.14
REMARK 500 5 SER A 65 45.22 -79.03
REMARK 500 5 PRO A 67 2.56 -69.70
REMARK 500 6 ARG A 63 126.26 -34.70
REMARK 500 6 SER A 65 -60.83 -103.25
REMARK 500 7 SER A 5 172.49 -46.07
REMARK 500 7 SER A 9 112.47 -171.53
REMARK 500 7 PRO A 67 2.33 -69.78
REMARK 500 7 SER A 69 123.90 -173.35
REMARK 500 8 SER A 10 129.84 -38.82
REMARK 500 8 PRO A 67 2.75 -69.70
REMARK 500 8 SER A 68 92.36 -50.03
REMARK 500 9 SER A 6 42.16 -95.29
REMARK 500 9 SER A 9 44.51 35.36
REMARK 500 10 LYS A 64 90.61 -68.19
REMARK 500 11 SER A 5 -60.78 -133.86
REMARK 500 11 SER A 6 42.17 39.07
REMARK 500 11 SER A 10 42.50 39.30
REMARK 500 11 PRO A 67 87.23 -69.71
REMARK 500 12 SER A 3 42.28 -97.51
REMARK 500 12 ARG A 8 91.19 -56.41
REMARK 500 12 THR A 12 41.76 -81.24
REMARK 500 12 ARG A 63 123.08 -34.52
REMARK 500 13 ARG A 63 -177.55 -57.49
REMARK 500 13 PRO A 67 2.78 -69.76
REMARK 500 13 SER A 68 82.19 -59.63
REMARK 500 14 ARG A 13 52.73 71.62
REMARK 500 14 LYS A 64 93.67 -59.23
REMARK 500 15 SER A 6 82.25 -65.13
REMARK 500 15 ARG A 63 119.38 -36.25
REMARK 500 15 SER A 68 41.23 -108.39
REMARK 500 16 SER A 2 127.06 -35.27
REMARK 500 17 SER A 5 42.22 -105.93
REMARK 500 18 PRO A 67 2.76 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000131.3 RELATED DB: TARGETDB
DBREF 2DA2 A 8 64 UNP Q15911 ATBF1_HUMAN 2243 2299
SEQADV 2DA2 GLY A 1 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 2 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 3 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 GLY A 4 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 5 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 6 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 GLY A 7 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 65 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 GLY A 66 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 PRO A 67 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 68 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 SER A 69 UNP Q15911 CLONING ARTIFACT
SEQADV 2DA2 GLY A 70 UNP Q15911 CLONING ARTIFACT
SEQRES 1 A 70 GLY SER SER GLY SER SER GLY ARG SER SER ARG THR ARG
SEQRES 2 A 70 PHE THR ASP TYR GLN LEU ARG VAL LEU GLN ASP PHE PHE
SEQRES 3 A 70 ASP ALA ASN ALA TYR PRO LYS ASP ASP GLU PHE GLU GLN
SEQRES 4 A 70 LEU SER ASN LEU LEU ASN LEU PRO THR ARG VAL ILE VAL
SEQRES 5 A 70 VAL TRP PHE GLN ASN ALA ARG GLN LYS ALA ARG LYS SER
SEQRES 6 A 70 GLY PRO SER SER GLY
HELIX 1 1 THR A 15 ASN A 29 1 15
HELIX 2 2 LYS A 33 LEU A 44 1 12
HELIX 3 3 PRO A 47 ARG A 63 1 17
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 9 2 Bytes