HEADER ANTITUMOR PROTEIN 28-MAY-04 1WHL
TITLE SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN HUMAN CYLINDROMATOSIS
TITLE 2 TUMOR SUPPRESSOR CYLD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYLINDROMATOSIS TUMOR SUPPRESSOR CYLD;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CAP-GLY DOMAIN;
COMPND 5 SYNONYM: KIAA0849 PROTEIN;
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 FH04363;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031006-33;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TUMOR SUPPRESSOR, DEUBIQUITINATING ENZYME, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, ANTITUMOR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WHL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WHL 1 VERSN
REVDAT 1 28-NOV-04 1WHL 0
JRNL AUTH K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN HUMAN
JRNL TITL 2 CYLINDROMATOSIS TUMOR SUPPRESSOR CYLD
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, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WHL 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_1000023588.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN, 20MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, 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 20020425, NMRVIEW 5, CNS
REMARK 210 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 5 -67.06 -127.06
REMARK 500 1 SER A 6 -172.89 60.17
REMARK 500 1 GLU A 23 126.87 -176.62
REMARK 500 1 PRO A 34 -173.16 -56.67
REMARK 500 1 LEU A 35 -61.29 -148.57
REMARK 500 1 THR A 40 -61.49 -141.09
REMARK 500 1 GLN A 57 33.25 -140.89
REMARK 500 1 ASP A 73 -179.98 -68.78
REMARK 500 1 CYS A 76 -46.75 -130.10
REMARK 500 1 SER A 90 35.45 -98.40
REMARK 500 2 SER A 6 -77.62 -79.33
REMARK 500 2 PRO A 34 -176.98 -53.72
REMARK 500 2 LEU A 35 -63.58 -95.73
REMARK 500 2 SER A 90 96.38 56.28
REMARK 500 3 GLU A 22 -58.16 -120.45
REMARK 500 3 LEU A 35 -66.52 -124.10
REMARK 500 3 GLU A 38 -70.28 -137.03
REMARK 500 3 ARG A 39 -46.83 -145.45
REMARK 500 3 THR A 40 35.42 -161.07
REMARK 500 3 CYS A 76 -58.34 -129.93
REMARK 500 3 SER A 93 172.63 59.61
REMARK 500 4 SER A 2 126.94 -170.36
REMARK 500 4 SER A 6 -45.89 -155.27
REMARK 500 4 LEU A 35 -55.41 -121.02
REMARK 500 4 ALA A 37 33.03 -143.62
REMARK 500 4 SER A 42 -48.15 -146.25
REMARK 500 4 CYS A 76 -51.79 -130.06
REMARK 500 5 ALA A 37 48.02 -146.26
REMARK 500 5 GLU A 38 -40.59 -177.68
REMARK 500 5 THR A 40 -78.95 62.87
REMARK 500 5 SER A 42 109.75 -168.73
REMARK 500 6 PRO A 34 -177.95 -69.04
REMARK 500 6 ALA A 37 79.01 60.66
REMARK 500 6 GLN A 57 33.39 -143.40
REMARK 500 6 CYS A 76 -63.93 -130.07
REMARK 500 6 SER A 90 49.31 -161.01
REMARK 500 7 SER A 5 -45.61 -163.28
REMARK 500 7 THR A 40 97.65 57.06
REMARK 500 7 SER A 42 35.18 -167.88
REMARK 500 7 GLN A 57 31.36 -141.47
REMARK 500 8 SER A 2 153.77 61.26
REMARK 500 8 SER A 3 179.60 58.18
REMARK 500 8 ARG A 19 -174.78 -61.80
REMARK 500 8 SER A 20 48.37 -93.00
REMARK 500 8 GLU A 22 -51.93 -121.43
REMARK 500 8 CYS A 76 -49.28 -130.04
REMARK 500 9 SER A 2 95.45 60.43
REMARK 500 9 SER A 5 31.50 -98.82
REMARK 500 9 SER A 20 48.26 -100.04
REMARK 500 9 GLU A 22 -60.45 -128.95
REMARK 500
REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK001000012.1 RELATED DB: TARGETDB
DBREF 1WHL A 8 89 UNP Q9NQC7 CYLD_HUMAN 132 213
SEQADV 1WHL GLY A 1 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 2 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 3 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL GLY A 4 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 5 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 6 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL GLY A 7 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 90 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL GLY A 91 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL PRO A 92 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 93 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL SER A 94 UNP Q9NQC7 CLONING ARTIFACT
SEQADV 1WHL GLY A 95 UNP Q9NQC7 CLONING ARTIFACT
SEQRES 1 A 95 GLY SER SER GLY SER SER GLY ILE ASP VAL GLY CYS PRO
SEQRES 2 A 95 VAL LYS VAL GLN LEU ARG SER GLY GLU GLU LYS PHE PRO
SEQRES 3 A 95 GLY VAL VAL ARG PHE ARG GLY PRO LEU LEU ALA GLU ARG
SEQRES 4 A 95 THR VAL SER GLY ILE PHE PHE GLY VAL GLU LEU LEU GLU
SEQRES 5 A 95 GLU GLY ARG GLY GLN GLY PHE THR ASP GLY VAL TYR GLN
SEQRES 6 A 95 GLY LYS GLN LEU PHE GLN CYS ASP GLU ASP CYS GLY VAL
SEQRES 7 A 95 PHE VAL ALA LEU ASP LYS LEU GLU LEU ILE GLU SER GLY
SEQRES 8 A 95 PRO SER SER GLY
HELIX 1 1 ALA A 81 ASP A 83 5 3
SHEET 1 A 5 GLY A 77 VAL A 80 0
SHEET 2 A 5 PHE A 46 LEU A 50 -1 N VAL A 48 O VAL A 78
SHEET 3 A 5 LYS A 24 ARG A 32 -1 N ARG A 30 O GLY A 47
SHEET 4 A 5 PRO A 13 GLN A 17 -1 N VAL A 16 O PHE A 25
SHEET 5 A 5 LEU A 85 LEU A 87 -1 O GLU A 86 N LYS A 15
SHEET 1 B 2 VAL A 63 TYR A 64 0
SHEET 2 B 2 LYS A 67 GLN A 68 -1 O LYS A 67 N TYR A 64
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
(ATOM LINES ARE NOT SHOWN.)
END
