Header list of 2csf.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 21-MAY-05 2CSF
TITLE SOLUTION STRUCTURE OF THE SECOND CUT DOMAIN OF HUMAN SATB2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN SATB2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CUT DOMAIN;
COMPND 5 SYNONYM: SPECIAL AT-RICH SEQUENCE-BINDING PROTEIN 2;
COMPND 6 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: KAZUSA CDNA FH00753;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CUT DOMAIN, DNA-BINDING PROTEIN SATB2, SPECIAL AT-RICH SEQUENCE-
KEYWDS 2 BINDING PROTEIN 2, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CSF 1 VERSN
REVDAT 1 21-NOV-05 2CSF 0
JRNL AUTH K.INOUE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND CUT DOMAIN OF HUMAN SATB2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024571.
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 : 1.23MM U-15N, 13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
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 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 ILE A 9 109.88 -53.51
REMARK 500 1 LYS A 10 151.29 -44.10
REMARK 500 1 ALA A 44 -64.93 -90.94
REMARK 500 1 SER A 99 108.41 -50.56
REMARK 500 1 SER A 100 138.63 -170.59
REMARK 500 2 SER A 6 122.52 -171.70
REMARK 500 2 ALA A 44 -61.00 -102.27
REMARK 500 2 SER A 100 176.41 -52.48
REMARK 500 3 SER A 3 116.51 -39.60
REMARK 500 3 ILE A 22 -38.21 -39.54
REMARK 500 3 GLU A 94 -70.28 -62.64
REMARK 500 4 ASP A 12 124.18 -172.29
REMARK 500 4 ALA A 14 82.35 -67.05
REMARK 500 4 LYS A 34 44.39 70.68
REMARK 500 4 ALA A 44 -64.95 -91.58
REMARK 500 4 GLU A 60 173.01 -50.46
REMARK 500 4 PRO A 64 1.02 -69.80
REMARK 500 4 GLU A 94 -70.31 -70.82
REMARK 500 4 PRO A 98 -174.41 -69.72
REMARK 500 5 ILE A 16 131.17 -34.35
REMARK 500 5 ILE A 22 -38.27 -39.48
REMARK 500 5 SER A 99 149.50 -175.01
REMARK 500 6 SER A 3 95.51 -52.64
REMARK 500 6 ALA A 14 159.56 -46.31
REMARK 500 6 LYS A 34 49.18 70.59
REMARK 500 6 ALA A 44 -63.37 -97.94
REMARK 500 6 PRO A 64 0.27 -69.81
REMARK 500 7 VAL A 11 125.98 -172.02
REMARK 500 7 ILE A 22 -38.80 -39.45
REMARK 500 7 LYS A 34 46.19 70.97
REMARK 500 7 ALA A 44 -60.93 -94.78
REMARK 500 8 ILE A 16 127.67 -34.30
REMARK 500 8 ALA A 44 -60.61 -102.54
REMARK 500 8 GLU A 60 170.38 -44.77
REMARK 500 8 PRO A 64 0.22 -69.80
REMARK 500 8 GLU A 94 -71.02 -62.81
REMARK 500 8 SER A 96 42.02 -86.74
REMARK 500 8 SER A 99 155.32 -47.31
REMARK 500 9 ILE A 9 87.53 -68.94
REMARK 500 9 LYS A 34 51.91 70.26
REMARK 500 9 GLN A 37 -33.11 -39.99
REMARK 500 9 ALA A 44 -63.62 -92.60
REMARK 500 9 GLU A 60 -174.68 -51.58
REMARK 500 9 PRO A 64 0.28 -69.73
REMARK 500 9 ARG A 67 -70.17 -70.73
REMARK 500 10 ILE A 16 128.47 -37.27
REMARK 500 10 PRO A 64 0.18 -69.74
REMARK 500 10 GLU A 94 -70.66 -66.58
REMARK 500 11 SER A 3 111.51 -36.77
REMARK 500 11 SER A 5 92.13 -69.43
REMARK 500
REMARK 500 THIS ENTRY HAS 101 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001010.3 RELATED DB: TARGETDB
DBREF 2CSF A 8 95 UNP Q9UPW6 SATB2_HUMAN 473 560
SEQADV 2CSF GLY A 1 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 2 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 3 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF GLY A 4 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 5 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 6 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF GLY A 7 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 96 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF GLY A 97 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF PRO A 98 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 99 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF SER A 100 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 2CSF GLY A 101 UNP Q9UPW6 CLONING ARTIFACT
SEQRES 1 A 101 GLY SER SER GLY SER SER GLY PRO ILE LYS VAL ASP GLY
SEQRES 2 A 101 ALA ASN ILE ASN ILE THR ALA ALA ILE TYR ASP GLU ILE
SEQRES 3 A 101 GLN GLN GLU MET LYS ARG ALA LYS VAL SER GLN ALA LEU
SEQRES 4 A 101 PHE ALA LYS VAL ALA ALA ASN LYS SER GLN GLY TRP LEU
SEQRES 5 A 101 CYS GLU LEU LEU ARG TRP LYS GLU ASN PRO SER PRO GLU
SEQRES 6 A 101 ASN ARG THR LEU TRP GLU ASN LEU CYS THR ILE ARG ARG
SEQRES 7 A 101 PHE LEU ASN LEU PRO GLN HIS GLU ARG ASP VAL ILE TYR
SEQRES 8 A 101 GLU GLU GLU SER SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 20 LYS A 34 1 15
HELIX 2 2 SER A 36 ALA A 44 1 9
HELIX 3 3 SER A 48 LYS A 59 1 12
HELIX 4 4 ASN A 66 ASN A 81 1 16
HELIX 5 5 PRO A 83 SER A 95 1 13
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