HEADER SIGNALING PROTEIN 14-FEB-07 2ED0
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF ABL INTERACTOR 2 (ABELSON
TITLE 2 INTERACTOR 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABL INTERACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: ABELSON INTERACTOR 2, ABI-2, ABL-BINDING PROTEIN 3, ABLBP3,
COMPND 6 ARG-BINDING PROTEIN 1, ARGBP1;
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: ABI2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050704-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS COILED COIL, CYTOSKELETON, NUCLEAR PROTEIN, PHOSPHORYLATION, SH3
KEYWDS 2 DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.ABE,N.TOCHIO,K.MIYAMOTO,K.SAITO,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2ED0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ED0 1 VERSN
REVDAT 1 26-FEB-08 2ED0 0
JRNL AUTH H.ABE,N.TOCHIO,K.MIYAMOTO,K.SAITO,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF ABL INTERACTOR 2
JRNL TITL 2 (ABELSON INTERACTOR 2)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ED0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026513.
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 : 0.73MM PROTEIN; 20MM D-TRIS-HCL;
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C
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 20031121, NMNMRVIEW
REMARK 210 5.0.4, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, 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 GLU A 38 96.84 -51.62
REMARK 500 1 ASN A 67 -37.97 -130.42
REMARK 500 2 ASP A 8 154.22 -48.27
REMARK 500 2 ASP A 32 38.54 -90.94
REMARK 500 3 ASP A 32 54.38 -95.94
REMARK 500 3 ASN A 48 38.81 -83.55
REMARK 500 3 ASP A 49 32.08 36.67
REMARK 500 3 TRP A 52 106.97 -162.87
REMARK 500 3 PRO A 75 1.58 -69.80
REMARK 500 3 SER A 77 116.16 -37.04
REMARK 500 4 LEU A 17 -71.68 -57.14
REMARK 500 4 LYS A 28 128.99 -36.15
REMARK 500 4 GLU A 38 152.35 -46.42
REMARK 500 5 ASP A 32 47.35 -93.45
REMARK 500 5 GLU A 38 108.29 -52.64
REMARK 500 5 ASN A 58 38.07 39.97
REMARK 500 5 TYR A 68 -31.71 -38.52
REMARK 500 6 SER A 6 -44.93 -130.17
REMARK 500 6 LYS A 28 122.27 -36.84
REMARK 500 6 ASP A 50 40.39 -99.45
REMARK 500 6 ASN A 58 37.79 35.78
REMARK 500 7 SER A 5 104.48 -35.06
REMARK 500 7 LYS A 28 133.18 -35.57
REMARK 500 7 ASP A 32 49.10 -76.20
REMARK 500 7 GLU A 38 110.57 -39.62
REMARK 500 7 TRP A 52 137.96 -34.46
REMARK 500 8 ASP A 49 48.36 -76.38
REMARK 500 9 GLU A 38 109.07 -52.81
REMARK 500 9 TYR A 68 35.32 -97.83
REMARK 500 10 GLU A 31 36.64 -83.33
REMARK 500 10 SER A 77 100.68 -55.18
REMARK 500 11 SER A 2 42.43 -89.55
REMARK 500 11 SER A 5 177.20 -51.84
REMARK 500 11 PRO A 10 2.87 -69.73
REMARK 500 11 VAL A 44 95.39 -64.25
REMARK 500 11 TYR A 68 32.60 -94.59
REMARK 500 11 PRO A 75 1.21 -69.66
REMARK 500 11 SER A 77 87.50 -69.22
REMARK 500 12 SER A 6 165.56 -47.66
REMARK 500 12 GLU A 38 106.23 -51.83
REMARK 500 12 TRP A 52 115.16 -162.33
REMARK 500 12 TYR A 68 -33.99 -36.37
REMARK 500 13 SER A 5 -51.90 -131.72
REMARK 500 13 LYS A 28 157.70 -43.67
REMARK 500 13 GLU A 38 104.35 -36.69
REMARK 500 13 ASP A 49 -39.28 -38.34
REMARK 500 14 LYS A 28 150.28 -43.94
REMARK 500 14 ASP A 32 43.23 -89.21
REMARK 500 14 PRO A 75 99.14 -69.73
REMARK 500 15 ARG A 14 36.05 -87.06
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002003990.1 RELATED DB: TARGETDB
DBREF 2ED0 A 8 72 UNP Q9NYB9 ABI2_HUMAN 444 508
SEQADV 2ED0 GLY A 1 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 2 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 3 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 GLY A 4 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 5 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 6 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 GLY A 7 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 73 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 GLY A 74 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 PRO A 75 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 76 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 SER A 77 UNP Q9NYB9 EXPRESSION TAG
SEQADV 2ED0 GLY A 78 UNP Q9NYB9 EXPRESSION TAG
SEQRES 1 A 78 GLY SER SER GLY SER SER GLY ASP PRO PRO TRP ALA PRO
SEQRES 2 A 78 ARG SER TYR LEU GLU LYS VAL VAL ALA ILE TYR ASP TYR
SEQRES 3 A 78 THR LYS ASP LYS GLU ASP GLU LEU SER PHE GLN GLU GLY
SEQRES 4 A 78 ALA ILE ILE TYR VAL ILE LYS LYS ASN ASP ASP GLY TRP
SEQRES 5 A 78 TYR GLU GLY VAL MET ASN GLY VAL THR GLY LEU PHE PRO
SEQRES 6 A 78 GLY ASN TYR VAL GLU SER ILE SER GLY PRO SER SER GLY
SHEET 1 A 5 VAL A 60 PRO A 65 0
SHEET 2 A 5 TRP A 52 MET A 57 -1 N MET A 57 O VAL A 60
SHEET 3 A 5 ILE A 41 LYS A 47 -1 N ILE A 45 O GLU A 54
SHEET 4 A 5 GLU A 18 ALA A 22 -1 N VAL A 20 O ILE A 42
SHEET 5 A 5 VAL A 69 SER A 71 -1 O GLU A 70 N VAL A 21
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
