Header list of 1wjr.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 29-MAY-04 1WJR
TITLE SOLUTION STRUCTURE OF THE 2ND MBT DOMAIN FROM HUMAN KIAA1617 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1617 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MBT DOMAIN;
COMPND 5 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 FJ13890;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040119-21;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS MBT DOMAIN, KIAA1617 PROTEIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WJR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WJR 1 VERSN
REVDAT 1 29-NOV-04 1WJR 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 2ND MBT DOMAIN FROM HUMAN KIAA1617
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 : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023651.
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 : 1.14MM MBT DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
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 : 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 0.901, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 : 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 2 121.40 -174.56
REMARK 500 1 VAL A 14 131.13 -35.65
REMARK 500 1 TYR A 46 121.11 -37.36
REMARK 500 1 TYR A 55 42.67 -88.64
REMARK 500 1 LEU A 62 34.58 -91.61
REMARK 500 1 LEU A 66 109.50 -57.41
REMARK 500 1 ARG A 78 109.16 -174.55
REMARK 500 1 ALA A 91 -38.08 -38.02
REMARK 500 1 PHE A 115 47.73 -100.52
REMARK 500 1 ASP A 120 113.74 -37.89
REMARK 500 2 SER A 6 96.58 -54.06
REMARK 500 2 VAL A 14 132.88 -34.54
REMARK 500 2 ASN A 25 108.24 -54.15
REMARK 500 2 PHE A 27 46.11 -92.68
REMARK 500 2 TYR A 55 43.70 -86.94
REMARK 500 2 ASP A 63 147.06 -34.60
REMARK 500 2 ARG A 65 -38.20 -34.50
REMARK 500 2 LEU A 66 95.29 -59.42
REMARK 500 2 LYS A 76 37.58 36.09
REMARK 500 2 TYR A 77 -174.67 -62.32
REMARK 500 2 MET A 79 79.62 -114.10
REMARK 500 2 CYS A 96 -70.40 -59.07
REMARK 500 2 PHE A 115 47.83 -90.03
REMARK 500 2 ASP A 120 29.64 48.00
REMARK 500 3 SER A 6 150.66 -46.35
REMARK 500 3 VAL A 14 132.37 -34.03
REMARK 500 3 TYR A 55 43.30 -86.67
REMARK 500 3 LEU A 62 33.57 -85.05
REMARK 500 3 LEU A 66 95.45 -60.00
REMARK 500 3 GLU A 74 179.90 -52.91
REMARK 500 3 ASN A 75 37.25 -88.36
REMARK 500 3 PRO A 82 -170.61 -69.80
REMARK 500 3 MET A 112 -36.98 -37.08
REMARK 500 3 PHE A 115 43.89 -94.04
REMARK 500 3 SER A 125 119.89 -161.95
REMARK 500 4 SER A 2 111.07 -171.31
REMARK 500 4 VAL A 14 132.90 -34.26
REMARK 500 4 GLN A 24 -62.95 -130.49
REMARK 500 4 ASN A 25 106.29 -49.72
REMARK 500 4 PHE A 27 47.68 -100.55
REMARK 500 4 GLU A 53 53.28 -116.57
REMARK 500 4 SER A 54 -32.73 -132.16
REMARK 500 4 TYR A 55 41.27 -92.98
REMARK 500 4 TYR A 61 -28.78 -37.26
REMARK 500 4 LEU A 62 38.64 -83.70
REMARK 500 4 CYS A 72 43.58 -82.12
REMARK 500 4 GLU A 74 -179.31 -56.79
REMARK 500 4 MET A 79 37.35 -97.32
REMARK 500 4 PRO A 87 11.01 -69.76
REMARK 500 4 ALA A 91 -31.92 -38.16
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001589.1 RELATED DB: TARGETDB
DBREF 1WJR A 8 121 UNP Q5VUG0 SMBT2_HUMAN 192 305
SEQADV 1WJR GLY A 1 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 2 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 3 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR GLY A 4 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 5 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 6 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR GLY A 7 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 122 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR GLY A 123 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR PRO A 124 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 125 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR SER A 126 UNP Q5VUG0 CLONING ARTIFACT
SEQADV 1WJR GLY A 127 UNP Q5VUG0 CLONING ARTIFACT
SEQRES 1 A 127 GLY SER SER GLY SER SER GLY PRO ILE ASP LEU ILE THR
SEQRES 2 A 127 VAL GLY SER LEU ILE GLU LEU GLN ASP SER GLN ASN PRO
SEQRES 3 A 127 PHE GLN TYR TRP ILE VAL SER VAL ILE GLU ASN VAL GLY
SEQRES 4 A 127 GLY ARG LEU ARG LEU ARG TYR VAL GLY LEU GLU ASP THR
SEQRES 5 A 127 GLU SER TYR ASP GLN TRP LEU PHE TYR LEU ASP TYR ARG
SEQRES 6 A 127 LEU ARG PRO VAL GLY TRP CYS GLN GLU ASN LYS TYR ARG
SEQRES 7 A 127 MET ASP PRO PRO SER GLU ILE TYR PRO LEU LYS MET ALA
SEQRES 8 A 127 SER GLU TRP LYS CYS THR LEU GLU LYS SER LEU ILE ASP
SEQRES 9 A 127 ALA ALA LYS PHE PRO LEU PRO MET GLU VAL PHE LYS ASP
SEQRES 10 A 127 HIS ALA ASP LEU SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 7 ILE A 12 1 6
HELIX 2 2 TRP A 71 LYS A 76 1 6
HELIX 3 3 MET A 90 PHE A 108 1 19
HELIX 4 4 PRO A 111 LYS A 116 5 6
SHEET 1 A 2 LEU A 17 GLN A 21 0
SHEET 2 A 2 TYR A 29 SER A 33 -1 O VAL A 32 N ILE A 18
SHEET 1 B 3 ASN A 37 VAL A 38 0
SHEET 2 B 3 ARG A 41 LEU A 44 -1 O ARG A 41 N VAL A 38
SHEET 3 B 3 GLN A 57 PHE A 60 -1 O LEU A 59 N LEU A 42
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