Header list of 2crj.pdb file
Complete list - r 9 2 Bytes
HEADER GENE REGULATION 20-MAY-05 2CRJ
TITLE SOLUTION STRUCTURE OF THE HMG DOMAIN OF MOUSE HMG DOMAIN PROTEIN HMGX2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR
COMPND 3 OF CHROMATIN SUBFAMILY E MEMBER 1-RELATED;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: HMG-BOX (RESIDUES 1-92);
COMPND 6 SYNONYM: SMARCE1-RELATED PROTEIN, HMG DOMAIN PROTEIN HMG20B,
COMPND 7 STRUCTURAL DNA-BINDING PROTEIN BRAF35, BRCA2- ASSOCIATED FACTOR 35;
COMPND 8 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: HMG20B, BRAF35, HMGX2, SMARCE1R;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041206-05;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL DNA-BINDING PROTEIN BRAF35, DNA-BENDING, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CRJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CRJ 1 VERSN
REVDAT 1 20-NOV-05 2CRJ 0
JRNL AUTH H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE HMG DOMAIN OF MOUSE HMG DOMAIN
JRNL TITL 2 PROTEIN HMGX2
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 2CRJ 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_1000024545.
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 : 120 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.03MM 13C,15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 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 SER A 6 50.19 39.06
REMARK 500 1 THR A 13 175.88 -58.98
REMARK 500 1 HIS A 30 77.05 -108.12
REMARK 500 1 PRO A 34 -163.35 -69.82
REMARK 500 1 PRO A 36 19.47 -69.74
REMARK 500 1 PRO A 51 0.34 -69.75
REMARK 500 1 GLU A 62 -60.26 -99.48
REMARK 500 1 THR A 85 40.52 -81.86
REMARK 500 1 SER A 91 46.12 37.46
REMARK 500 2 ARG A 27 -33.70 -36.40
REMARK 500 2 HIS A 30 72.98 -107.12
REMARK 500 2 PRO A 34 -163.26 -69.79
REMARK 500 2 PRO A 36 19.50 -69.69
REMARK 500 2 PRO A 51 2.76 -69.71
REMARK 500 2 GLN A 66 -34.74 -34.26
REMARK 500 2 CYS A 84 173.79 -47.56
REMARK 500 2 SER A 87 165.04 -47.96
REMARK 500 3 HIS A 30 75.16 -109.26
REMARK 500 3 PRO A 34 -163.21 -69.70
REMARK 500 3 PRO A 36 19.53 -69.78
REMARK 500 3 PRO A 51 0.91 -69.75
REMARK 500 3 GLN A 67 -35.70 -37.54
REMARK 500 3 LEU A 72 -75.46 -32.16
REMARK 500 3 ALA A 74 -33.69 -34.17
REMARK 500 3 CYS A 84 94.14 -69.23
REMARK 500 4 ALA A 10 105.43 -41.09
REMARK 500 4 PRO A 34 -163.15 -69.79
REMARK 500 4 PRO A 36 19.55 -69.78
REMARK 500 4 PRO A 51 3.24 -69.81
REMARK 500 5 PRO A 11 -163.78 -69.74
REMARK 500 5 HIS A 30 75.45 -108.01
REMARK 500 5 PRO A 34 -163.19 -69.75
REMARK 500 5 PRO A 36 19.44 -69.75
REMARK 500 5 PRO A 51 2.19 -69.73
REMARK 500 5 SER A 78 129.06 -38.23
REMARK 500 5 VAL A 83 35.81 34.75
REMARK 500 5 PRO A 89 -171.95 -69.72
REMARK 500 6 ARG A 17 -36.62 -38.03
REMARK 500 6 ASN A 20 -74.74 -64.06
REMARK 500 6 ARG A 23 -30.59 -36.43
REMARK 500 6 HIS A 30 75.06 -107.19
REMARK 500 6 PRO A 34 -163.16 -69.75
REMARK 500 6 PRO A 36 19.53 -69.76
REMARK 500 6 PRO A 51 1.68 -69.76
REMARK 500 6 LEU A 72 -75.71 -31.53
REMARK 500 6 ALA A 74 -35.03 -32.90
REMARK 500 6 GLN A 76 -32.01 -39.69
REMARK 500 6 GLN A 77 48.57 -102.26
REMARK 500 6 SER A 91 104.05 -46.82
REMARK 500 7 ALA A 10 105.93 -47.54
REMARK 500
REMARK 500 THIS ENTRY HAS 152 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMI002018633.1 RELATED DB: TARGETDB
DBREF 2CRJ A 8 86 UNP Q9Z104 HM20B_MOUSE 70 148
SEQADV 2CRJ GLY A 1 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 2 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 3 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ GLY A 4 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 5 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 6 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ GLY A 7 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 87 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ GLY A 88 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ PRO A 89 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 90 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ SER A 91 UNP Q9Z104 CLONING ARTIFACT
SEQADV 2CRJ GLY A 92 UNP Q9Z104 CLONING ARTIFACT
SEQRES 1 A 92 GLY SER SER GLY SER SER GLY PRO LYS ALA PRO VAL THR
SEQRES 2 A 92 GLY TYR VAL ARG PHE LEU ASN GLU ARG ARG GLU GLN ILE
SEQRES 3 A 92 ARG THR ARG HIS PRO ASP LEU PRO PHE PRO GLU ILE THR
SEQRES 4 A 92 LYS MET LEU GLY ALA GLU TRP SER LYS LEU GLN PRO ALA
SEQRES 5 A 92 GLU LYS GLN ARG TYR LEU ASP GLU ALA GLU LYS GLU LYS
SEQRES 6 A 92 GLN GLN TYR LEU LYS GLU LEU TRP ALA TYR GLN GLN SER
SEQRES 7 A 92 GLU ALA TYR LYS VAL CYS THR GLU SER GLY PRO SER SER
SEQRES 8 A 92 GLY
HELIX 1 1 THR A 13 HIS A 30 1 18
HELIX 2 2 PRO A 34 LYS A 48 1 15
HELIX 3 3 ALA A 52 GLN A 77 1 26
HELIX 4 4 SER A 78 VAL A 83 1 6
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