Header list of 1wiz.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 28-MAY-04 1WIZ
TITLE SOLUTION STRUCTURE OF THE FIRST CUT DOMAIN OF KIAA1034 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN SATB2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CUT DOMAIN;
COMPND 5 SYNONYM: KIAA1034 PROTEIN, SATB2 PROTEIN, SPECIAL AT-RICH SEQUENCE-
COMPND 6 BINDING PROTEIN 2;
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: KAZUSA CDNA FH00753;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-63;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS HELIX BUNDLE, SATB2, KIAA1034 PROTEIN, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,S.NAMEKI,F.HAYASHI,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WIZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WIZ 1 VERSN
REVDAT 1 28-NOV-04 1WIZ 0
JRNL AUTH K.INOUE,S.NAMEKI,F.HAYASHI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST CUT DOMAIN OF KIAA1034
JRNL TITL 2 PROTEIN
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 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WIZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023629.
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 : 1.20MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 2MM
REMARK 210 D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.8992, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 GLU A 86 H ILE A 90 1.51
REMARK 500 O GLN A 49 H SER A 53 1.52
REMARK 500 O GLN A 67 H VAL A 71 1.56
REMARK 500 O GLN A 25 H GLU A 29 1.60
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 2 168.68 67.82
REMARK 500 1 SER A 3 145.00 69.14
REMARK 500 1 SER A 5 130.57 -172.77
REMARK 500 1 LYS A 8 95.79 61.91
REMARK 500 1 PRO A 9 -169.01 -75.06
REMARK 500 1 THR A 12 99.83 -164.39
REMARK 500 1 SER A 15 79.57 39.71
REMARK 500 1 GLN A 37 -30.69 -39.84
REMARK 500 1 PHE A 45 24.57 -148.68
REMARK 500 1 THR A 48 -157.91 -107.04
REMARK 500 1 GLU A 60 104.57 -46.80
REMARK 500 1 LEU A 82 163.90 -47.68
REMARK 500 1 SER A 96 77.95 53.96
REMARK 500 1 SER A 99 74.31 43.43
REMARK 500 1 SER A 100 145.84 -39.84
REMARK 500 2 SER A 2 144.94 68.19
REMARK 500 2 SER A 3 134.51 -171.19
REMARK 500 2 PRO A 9 -167.58 -75.05
REMARK 500 2 GLU A 10 91.85 179.73
REMARK 500 2 SER A 15 90.67 41.89
REMARK 500 2 PHE A 45 24.98 -148.40
REMARK 500 2 THR A 48 -157.93 -101.13
REMARK 500 2 GLU A 60 104.87 -47.05
REMARK 500 2 ALA A 65 153.94 -40.22
REMARK 500 2 LEU A 82 164.71 -45.66
REMARK 500 2 SER A 96 111.40 60.05
REMARK 500 3 SER A 3 167.74 175.84
REMARK 500 3 SER A 5 145.91 -170.13
REMARK 500 3 SER A 6 160.00 176.06
REMARK 500 3 LYS A 8 113.47 -172.85
REMARK 500 3 PRO A 11 -165.49 -74.97
REMARK 500 3 ASN A 13 152.09 175.03
REMARK 500 3 SER A 14 75.37 166.87
REMARK 500 3 SER A 15 77.17 39.85
REMARK 500 3 PHE A 45 26.57 -149.73
REMARK 500 3 THR A 48 -145.23 -107.99
REMARK 500 3 GLU A 60 104.90 -46.73
REMARK 500 3 LEU A 82 162.53 -48.65
REMARK 500 4 SER A 2 -60.93 -172.51
REMARK 500 4 SER A 3 166.07 179.41
REMARK 500 4 SER A 5 86.25 61.81
REMARK 500 4 SER A 6 127.41 179.29
REMARK 500 4 SER A 14 -166.85 -108.67
REMARK 500 4 VAL A 16 138.58 62.28
REMARK 500 4 ALA A 41 -33.63 -39.32
REMARK 500 4 PHE A 45 25.23 -149.55
REMARK 500 4 THR A 48 -166.28 -101.15
REMARK 500 4 GLU A 60 104.89 -46.85
REMARK 500 4 ALA A 65 140.08 -39.65
REMARK 500 4 SER A 96 97.23 -54.67
REMARK 500
REMARK 500 THIS ENTRY HAS 239 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001010.2 RELATED DB: TARGETDB
DBREF 1WIZ A 8 95 UNP Q9UPW6 SATB2_HUMAN 350 437
SEQADV 1WIZ GLY A 1 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 2 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 3 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ GLY A 4 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 5 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 6 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ GLY A 7 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 96 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ GLY A 97 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ PRO A 98 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 99 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ SER A 100 UNP Q9UPW6 CLONING ARTIFACT
SEQADV 1WIZ GLY A 101 UNP Q9UPW6 CLONING ARTIFACT
SEQRES 1 A 101 GLY SER SER GLY SER SER GLY LYS PRO GLU PRO THR ASN
SEQRES 2 A 101 SER SER VAL GLU VAL SER PRO ASP ILE TYR GLN GLN VAL
SEQRES 3 A 101 ARG ASP GLU LEU LYS ARG ALA SER VAL SER GLN ALA VAL
SEQRES 4 A 101 PHE ALA ARG VAL ALA PHE ASN ARG THR GLN GLY LEU LEU
SEQRES 5 A 101 SER GLU ILE LEU ARG LYS GLU GLU ASP PRO ARG THR ALA
SEQRES 6 A 101 SER GLN SER LEU LEU VAL ASN LEU ARG ALA MET GLN ASN
SEQRES 7 A 101 PHE LEU ASN LEU PRO GLU VAL GLU ARG ASP ARG ILE TYR
SEQRES 8 A 101 GLN ASP GLU ARG SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 21 SER A 34 1 14
HELIX 2 2 SER A 36 ASN A 46 1 11
HELIX 3 3 THR A 48 LYS A 58 1 11
HELIX 4 4 SER A 66 LEU A 80 1 15
HELIX 5 5 PRO A 83 SER A 96 1 14
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