Header list of 1v5m.pdb file
Complete list - v 10 2 Bytes
HEADER PROTEIN BINDING 25-NOV-03 1V5M
TITLE SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF MOUSE APS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH2 AND PH DOMAIN-CONTAINING ADAPTER PROTEIN APS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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: RIKEN CDNA 5730427K19;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030212-26;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ADAPTOR PROTEIN, PLECKSTRIN HOMOLOGY DOMAIN, CELLULAR SIGNALING,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 10-NOV-21 1V5M 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V5M 1 VERSN
REVDAT 1 25-MAY-04 1V5M 0
JRNL AUTH H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 MOUSE APS
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 1V5M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006235.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.23MM PLECKSTRIN HOMOLOGY
REMARK 210 DOMAIN U-13C, 15N; 20MM D-TRIS-
REMARK 210 HCL(7.5); 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 90% H2O, 10% 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 5.0.4,
REMARK 210 KUJIRA 0.854, 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 14 44.92 -102.49
REMARK 500 1 ALA A 33 44.07 -80.53
REMARK 500 1 SER A 34 44.59 -87.79
REMARK 500 1 TRP A 42 124.24 -39.73
REMARK 500 1 ALA A 54 42.50 73.64
REMARK 500 1 GLU A 56 134.48 -36.38
REMARK 500 1 VAL A 73 59.73 -116.72
REMARK 500 1 PRO A 88 -163.59 -69.76
REMARK 500 1 PRO A 92 5.92 -69.77
REMARK 500 1 ILE A 113 -71.51 -49.22
REMARK 500 2 VAL A 16 145.57 -176.90
REMARK 500 2 ILE A 18 109.67 -59.38
REMARK 500 2 GLN A 41 -35.76 -37.02
REMARK 500 2 TRP A 42 128.01 -34.88
REMARK 500 2 ARG A 57 -71.97 -80.23
REMARK 500 2 PHE A 62 79.43 -107.26
REMARK 500 2 PRO A 66 3.26 -69.84
REMARK 500 2 PRO A 88 -165.25 -69.80
REMARK 500 2 PRO A 92 3.47 -69.76
REMARK 500 2 ASP A 130 134.79 -176.47
REMARK 500 2 SER A 134 155.53 -39.77
REMARK 500 3 SER A 6 139.51 -38.93
REMARK 500 3 GLU A 56 155.85 -40.99
REMARK 500 3 ARG A 57 -70.90 -73.18
REMARK 500 3 PRO A 66 3.60 -69.80
REMARK 500 3 PRO A 88 -163.81 -69.67
REMARK 500 3 LEU A 89 47.95 -79.37
REMARK 500 3 PRO A 92 19.78 -69.70
REMARK 500 3 ASP A 95 39.54 -95.14
REMARK 500 3 VAL A 129 -32.31 -34.63
REMARK 500 3 ASP A 130 132.85 -175.25
REMARK 500 3 SER A 131 95.84 -31.79
REMARK 500 4 LYS A 12 44.41 -99.31
REMARK 500 4 ILE A 18 102.59 -57.78
REMARK 500 4 ALA A 32 -59.08 -131.65
REMARK 500 4 PRO A 36 89.83 -69.75
REMARK 500 4 ALA A 54 52.40 37.54
REMARK 500 4 PRO A 66 1.51 -69.80
REMARK 500 4 VAL A 73 63.06 -119.43
REMARK 500 4 THR A 85 37.25 -86.61
REMARK 500 4 PRO A 88 -163.12 -69.70
REMARK 500 4 PRO A 92 20.72 -69.78
REMARK 500 4 ASP A 95 54.96 38.03
REMARK 500 4 PHE A 98 144.05 -170.06
REMARK 500 4 ASN A 104 37.54 -89.13
REMARK 500 4 ILE A 113 -75.40 -42.46
REMARK 500 4 SER A 115 -32.74 -39.82
REMARK 500 4 SER A 131 -74.27 -131.54
REMARK 500 4 SER A 134 98.36 -63.99
REMARK 500 5 SER A 5 -62.63 -124.87
REMARK 500
REMARK 500 THIS ENTRY HAS 263 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007005031.1 RELATED DB: TARGETDB
DBREF 1V5M A 8 130 UNP Q9JID9 APS_MOUSE 177 299
SEQADV 1V5M GLY A 1 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 2 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 3 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M GLY A 4 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 5 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 6 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M GLY A 7 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M ASN A 8 UNP Q9JID9 THR 177 ENGINEERED MUTATION
SEQADV 1V5M SER A 131 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M GLY A 132 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M PRO A 133 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 134 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M SER A 135 UNP Q9JID9 CLONING ARTIFACT
SEQADV 1V5M GLY A 136 UNP Q9JID9 CLONING ARTIFACT
SEQRES 1 A 136 GLY SER SER GLY SER SER GLY ASN LEU ALA ALA LYS VAL
SEQRES 2 A 136 GLU LEU VAL ASP ILE GLN ARG GLU GLY ALA LEU ARG PHE
SEQRES 3 A 136 MET VAL ALA ASP ASP ALA ALA SER GLY PRO GLY GLY THR
SEQRES 4 A 136 ALA GLN TRP GLN LYS CYS ARG LEU LEU LEU ARG ARG ALA
SEQRES 5 A 136 VAL ALA GLY GLU ARG PHE ARG LEU GLU PHE PHE VAL PRO
SEQRES 6 A 136 PRO LYS ALA SER ARG PRO LYS VAL SER ILE PRO LEU SER
SEQRES 7 A 136 ALA ILE ILE GLU VAL ARG THR THR MET PRO LEU GLU MET
SEQRES 8 A 136 PRO GLU LYS ASP ASN THR PHE VAL LEU LYS VAL GLU ASN
SEQRES 9 A 136 GLY ALA GLU TYR ILE LEU GLU THR ILE ASP SER LEU GLN
SEQRES 10 A 136 LYS HIS SER TRP VAL ALA ASP ILE GLN GLY CYS VAL ASP
SEQRES 11 A 136 SER GLY PRO SER SER GLY
HELIX 1 1 SER A 115 ASP A 130 1 16
SHEET 1 A 7 ARG A 20 VAL A 28 0
SHEET 2 A 7 GLN A 43 ARG A 51 -1 N LEU A 60 O ILE A 75
SHEET 3 A 7 PHE A 58 PHE A 63 -1 N ARG A 46 O PHE A 63
SHEET 4 A 7 ILE A 75 PRO A 76 -1 N ARG A 20 O LEU A 49
SHEET 5 A 7 ILE A 80 ARG A 84 -1 O ILE A 109 N MET A 27
SHEET 6 A 7 THR A 97 VAL A 102 -1 N PHE A 98 O LEU A 110
SHEET 7 A 7 TYR A 108 GLU A 111 0
CISPEP 1 VAL A 64 PRO A 65 1 -0.03
CISPEP 2 VAL A 64 PRO A 65 2 -0.08
CISPEP 3 VAL A 64 PRO A 65 3 -0.03
CISPEP 4 VAL A 64 PRO A 65 4 -0.03
CISPEP 5 VAL A 64 PRO A 65 5 -0.14
CISPEP 6 VAL A 64 PRO A 65 6 -0.03
CISPEP 7 VAL A 64 PRO A 65 7 0.02
CISPEP 8 VAL A 64 PRO A 65 8 -0.08
CISPEP 9 VAL A 64 PRO A 65 9 0.07
CISPEP 10 VAL A 64 PRO A 65 10 -0.05
CISPEP 11 VAL A 64 PRO A 65 11 -0.06
CISPEP 12 VAL A 64 PRO A 65 12 -0.04
CISPEP 13 VAL A 64 PRO A 65 13 -0.02
CISPEP 14 VAL A 64 PRO A 65 14 0.03
CISPEP 15 VAL A 64 PRO A 65 15 -0.03
CISPEP 16 VAL A 64 PRO A 65 16 -0.04
CISPEP 17 VAL A 64 PRO A 65 17 -0.08
CISPEP 18 VAL A 64 PRO A 65 18 -0.05
CISPEP 19 VAL A 64 PRO A 65 19 -0.08
CISPEP 20 VAL A 64 PRO A 65 20 -0.15
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 - v 10 2 Bytes