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PDBsum entry 2e5k

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Protein binding PDB id
2e5k
Jmol
Contents
Protein chain
94 a.a.
HEADER    PROTEIN BINDING                         21-DEC-06   2E5K
TITLE     SOLUTION STRUCTURE OF SH3 DOMAIN IN SUPPRESSOR OF T-CELL
TITLE    2 RECEPTOR SIGNALING 1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SUPPRESSOR OF T-CELL RECEPTOR SIGNALING 1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: SH3 DOMAIN;
COMPND   5 SYNONYM: STS-1, CBL-INTERACTING PROTEIN P70;
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: STS1;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P050704-22;
SOURCE   8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS    SH3 DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS   2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS   3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN
KEYWDS   4 BINDING
EXPDTA    SOLUTION NMR
NUMMDL    20
AUTHOR    S.SUKEGAWA,K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,
AUTHOR   2 M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR   3 INITIATIVE (RSGI)
REVDAT   2   24-FEB-09 2E5K    1       VERSN
REVDAT   1   26-JUN-07 2E5K    0
JRNL        AUTH   S.SUKEGAWA,K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,
JRNL        AUTH 2 T.TERADA,M.SHIROUZU,S.YOKOYAMA
JRNL        TITL   SOLUTION STRUCTURE OF SH3 DOMAIN IN SUPPRESSOR OF
JRNL        TITL 2 T-CELL RECEPTOR SIGNALING 1
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CYANA 2.0.17
REMARK   3   AUTHORS     : GUNTERT, P.
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2E5K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB026252.
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                : 1.18MM 13C-15N PROTEIN, 20MM
REMARK 210                                   D-TRIS-HCL(PH7.0), 100MM NACL,
REMARK 210                                   1MM D-DTT, 0.02% NAN3, 90%
REMARK 210                                   H2O, 10% D2O
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY, 3D_
REMARK 210                                   15N-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                 : XWINNMR 3.5, NMRPIPE
REMARK 210                                   20060702, NMRVIEW 5.0.4,
REMARK 210                                   KUJIRA 0.9820, 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,
REMARK 210                                   STRUCTURES WITH THE LOWEST
REMARK 210                                   ENERGY, TARGET 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 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 245      176.70    -56.29
REMARK 500  1 ASN A 255       46.12   -106.03
REMARK 500  1 ASP A 271      -38.72    -37.70
REMARK 500  1 ILE A 324      -31.26   -130.09
REMARK 500  1 SER A 328      141.87   -174.13
REMARK 500  1 PRO A 331       91.93    -69.76
REMARK 500  1 SER A 332       41.77     37.27
REMARK 500  2 ARG A 252       44.85     38.33
REMARK 500  2 ASN A 255       47.28    -77.96
REMARK 500  2 GLN A 288       87.08    -69.27
REMARK 500  2 SER A 290       26.33     48.09
REMARK 500  2 SER A 292      -36.17    -35.36
REMARK 500  2 ALA A 317       92.06    -69.54
REMARK 500  2 THR A 322     -176.91    -66.60
REMARK 500  2 PHE A 325      143.89    -34.32
REMARK 500  2 SER A 329       43.84     37.58
REMARK 500  3 ASP A 250      143.21   -172.56
REMARK 500  3 ARG A 252       44.58     39.30
REMARK 500  3 PHE A 253       47.41     35.69
REMARK 500  3 ASN A 255      -53.60   -132.54
REMARK 500  3 ASP A 271      -38.47    -35.67
REMARK 500  3 SER A 292      -34.33    -34.06
REMARK 500  3 ALA A 317       89.35    -55.21
REMARK 500  3 ILE A 324      -55.97   -125.36
REMARK 500  3 PHE A 325      139.22    -34.36
REMARK 500  4 SER A 300      174.14    -50.08
REMARK 500  4 ILE A 324      -53.52   -129.96
REMARK 500  4 PHE A 325      133.01    -34.90
REMARK 500  4 SER A 333      174.28    -52.60
REMARK 500  5 GLU A 319       45.70     34.62
REMARK 500  5 CYS A 320       51.04     34.26
REMARK 500  5 SER A 321      -75.06    -82.41
REMARK 500  5 THR A 322      145.34    -34.60
REMARK 500  6 HIS A 256      142.83   -172.85
REMARK 500  6 SER A 290       25.08     41.79
REMARK 500  6 CYS A 320      161.76    -44.13
REMARK 500  6 ILE A 324      -51.14   -126.89
REMARK 500  6 PHE A 325      156.65    -41.49
REMARK 500  7 ARG A 252       35.06    -94.96
REMARK 500  7 GLN A 288       52.95    -96.94
REMARK 500  7 ILE A 324      -64.92   -125.58
REMARK 500  7 PHE A 325      140.37    -34.24
REMARK 500  7 PRO A 331        2.16    -69.75
REMARK 500  7 SER A 332      115.68    -34.75
REMARK 500  8 ARG A 252      -51.34   -123.76
REMARK 500  8 HIS A 256      131.43    -38.52
REMARK 500  8 ASP A 271      -39.54    -35.57
REMARK 500  8 SER A 292      -32.30    -37.85
REMARK 500  8 THR A 322      140.28    -34.02
REMARK 500  8 ILE A 324      -70.24   -119.54
REMARK 500  8 PHE A 325      119.10    -33.76
REMARK 500  9 SER A 248      107.10    -38.55
REMARK 500  9 ARG A 252       35.71     39.20
REMARK 500  9 SER A 290       29.46     48.47
REMARK 500  9 SER A 292      -38.07    -39.90
REMARK 500  9 ALA A 317       94.59    -59.51
REMARK 500  9 ILE A 324      -67.12   -121.92
REMARK 500  9 PHE A 325      148.17    -36.67
REMARK 500 10 SER A 243      103.03    -36.39
REMARK 500 10 ARG A 252       52.62    -99.43
REMARK 500 10 HIS A 256      140.25    -35.36
REMARK 500 10 ASP A 271      -39.49    -36.38
REMARK 500 10 ILE A 296      119.36   -160.02
REMARK 500 10 ALA A 317       92.64    -66.60
REMARK 500 10 PHE A 325      135.96    -34.61
REMARK 500 10 SER A 333      100.95    -57.06
REMARK 500 11 SER A 245      156.07    -49.56
REMARK 500 11 ARG A 252       32.38    -89.70
REMARK 500 11 PHE A 253       39.98     71.20
REMARK 500 11 ALA A 254     -178.27    -64.03
REMARK 500 11 HIS A 256      131.13    -35.82
REMARK 500 11 GLN A 288       92.54    -67.38
REMARK 500 11 SER A 292      -37.96    -34.41
REMARK 500 11 ALA A 317       93.13    -54.23
REMARK 500 11 GLU A 319      101.51    -48.75
REMARK 500 11 TRP A 323      -33.99   -130.49
REMARK 500 11 SER A 332      102.14    -37.57
REMARK 500 11 SER A 333       42.21    -86.65
REMARK 500 12 PRO A 285        0.51    -69.76
REMARK 500 12 ALA A 317       95.02    -66.20
REMARK 500 12 ILE A 324      -54.85   -133.84
REMARK 500 12 PHE A 325      135.61    -35.18
REMARK 500 13 SER A 246       86.72    -69.52
REMARK 500 13 TYR A 265      118.69   -171.77
REMARK 500 13 GLN A 288       85.63    -67.98
REMARK 500 13 ASP A 318      -53.75   -120.59
REMARK 500 13 CYS A 320      176.01    -51.87
REMARK 500 13 THR A 322     -179.12    -67.00
REMARK 500 13 SER A 329      172.92    -55.17
REMARK 500 13 SER A 332       42.19     37.60
REMARK 500 14 ALA A 254      -70.40    -88.31
REMARK 500 14 SER A 290       25.06     45.48
REMARK 500 14 SER A 292      -38.50    -36.20
REMARK 500 14 ALA A 317       96.68    -60.89
REMARK 500 14 ILE A 324      -72.82   -121.81
REMARK 500 14 PHE A 325      123.23    -33.99
REMARK 500 15 SER A 248      -44.05   -130.14
REMARK 500 15 SER A 290       25.41     48.49
REMARK 500 15 ALA A 317       95.44    -52.40
REMARK 500 15 GLU A 319       91.77    -67.96
REMARK 500 15 SER A 321      179.63    -50.62
REMARK 500 15 ILE A 324      -67.44   -132.26
REMARK 500 15 PHE A 325      136.63    -34.06
REMARK 500 15 SER A 328      148.83   -173.70
REMARK 500 16 SER A 242      -47.03   -132.12
REMARK 500 16 ARG A 252      -63.35   -123.66
REMARK 500 16 PHE A 253       44.00   -104.91
REMARK 500 16 HIS A 256      134.29    -37.91
REMARK 500 16 GLN A 288       85.62    -58.80
REMARK 500 16 SER A 292      -39.57    -39.80
REMARK 500 16 ALA A 317       94.03    -61.79
REMARK 500 16 ILE A 324      -52.99   -127.21
REMARK 500 16 PHE A 325      130.46    -34.80
REMARK 500 16 SER A 328       52.29   -111.59
REMARK 500 16 SER A 332      132.90    -35.85
REMARK 500 17 ARG A 252       41.82    -81.47
REMARK 500 17 ASN A 255       44.18    -82.41
REMARK 500 17 ASP A 271      -39.80    -35.10
REMARK 500 17 SER A 290       31.22     39.45
REMARK 500 17 THR A 303      -65.70   -102.12
REMARK 500 17 ALA A 317       92.56    -54.91
REMARK 500 17 GLU A 319       43.22    -80.81
REMARK 500 17 TRP A 323      -41.52   -131.96
REMARK 500 17 PHE A 325      141.58    -34.23
REMARK 500 18 ARG A 252       47.51    -97.84
REMARK 500 18 ASN A 255       44.07    -84.01
REMARK 500 18 ASP A 271      -39.93    -37.34
REMARK 500 18 ALA A 317       46.71    -77.32
REMARK 500 18 TRP A 323      -45.51   -133.66
REMARK 500 18 PHE A 325      138.39    -34.20
REMARK 500 18 SER A 333       42.10   -103.85
REMARK 500 19 SER A 248      136.02    -35.15
REMARK 500 19 ASN A 255       43.96   -108.81
REMARK 500 19 SER A 292      -37.03    -36.35
REMARK 500 19 ALA A 317       95.64    -66.07
REMARK 500 19 ILE A 324      -53.64   -130.00
REMARK 500 19 PHE A 325      146.11    -36.23
REMARK 500 19 PRO A 331       85.44    -69.74
REMARK 500 20 ASN A 255       40.48    -99.59
REMARK 500 20 THR A 303      -63.73   -100.04
REMARK 500 20 ALA A 317       86.55    -64.39
REMARK 500 20 THR A 322      161.50    -48.89
REMARK 500 20 ILE A 324      -46.57   -130.16
REMARK 500 20 PHE A 325      126.57    -34.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001926.1   RELATED DB: TARGETDB
DBREF  2E5K A  248   328  UNP    Q8TF42   STS1_HUMAN     248    328
SEQADV 2E5K GLY A  241  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  242  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  243  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K GLY A  244  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  245  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  246  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K GLY A  247  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  329  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K GLY A  330  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K PRO A  331  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  332  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K SER A  333  UNP  Q8TF42              CLONING ARTIFACT
SEQADV 2E5K GLY A  334  UNP  Q8TF42              CLONING ARTIFACT
SEQRES   1 A   94  GLY SER SER GLY SER SER GLY SER ARG ASP ILE ARG PHE
SEQRES   2 A   94  ALA ASN HIS GLU THR LEU GLN VAL ILE TYR PRO TYR THR
SEQRES   3 A   94  PRO GLN ASN ASP ASP GLU LEU GLU LEU VAL PRO GLY ASP
SEQRES   4 A   94  PHE ILE PHE MET SER PRO MET GLU GLN THR SER THR SER
SEQRES   5 A   94  GLU GLY TRP ILE TYR GLY THR SER LEU THR THR GLY CYS
SEQRES   6 A   94  SER GLY LEU LEU PRO GLU ASN TYR ILE THR LYS ALA ASP
SEQRES   7 A   94  GLU CYS SER THR TRP ILE PHE HIS GLY SER SER GLY PRO
SEQRES   8 A   94  SER SER GLY
HELIX    1   1 PRO A  285  GLN A  288  5                                   4
SHEET    1   A 5 SER A 306  PRO A 310  0
SHEET    2   A 5 TRP A 295  SER A 300 -1  N  GLY A 298   O  GLY A 307
SHEET    3   A 5 PHE A 280  MET A 283 -1  N  PHE A 282   O  THR A 299
SHEET    4   A 5 GLU A 257  VAL A 261 -1  N  GLU A 257   O  MET A 283
SHEET    5   A 5 ILE A 314  LYS A 316 -1  O  THR A 315   N  GLN A 260
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
      
PROCHECK
Go to PROCHECK summary
 References