Header list of 1x5b.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 15-MAY-05 1X5B
TITLE THE SOLUTION STRUCTURE OF THE VHS DOMAIN OF HUMAN SIGNAL TRANSDUCING
TITLE 2 ADAPTOR MOLECULE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIGNAL TRANSDUCING ADAPTOR MOLECULE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: VHS 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: STAM2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040607-06;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS VHS DOMAIN, UBIQUITIN BINDING, STAM2, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN
KEYWDS 4 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5B 1 VERSN
REVDAT 1 15-NOV-05 1X5B 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE VHS DOMAIN OF HUMAN SIGNAL
JRNL TITL 2 TRANSDUCING ADAPTOR MOLECULE 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 1X5B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM VHS DOMAIN U-15N,13C; 20MM
REMARK 210 D-TRIS HCL; 100MM NACL; 5MM D-
REMARK 210 DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.926, 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 : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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 PRO A 9 99.33 -69.74
REMARK 500 1 LEU A 10 81.04 -68.84
REMARK 500 1 VAL A 80 -28.62 -37.05
REMARK 500 1 LYS A 107 50.26 34.59
REMARK 500 1 LYS A 117 -73.50 -47.80
REMARK 500 1 PHE A 127 39.89 -97.37
REMARK 500 1 LYS A 129 39.38 -87.21
REMARK 500 1 PRO A 152 -163.68 -69.78
REMARK 500 1 GLN A 156 98.32 -47.45
REMARK 500 2 LEU A 10 85.21 -66.72
REMARK 500 2 ILE A 39 -66.01 -94.40
REMARK 500 2 VAL A 80 -26.40 -38.33
REMARK 500 2 PHE A 96 -63.23 -92.78
REMARK 500 2 LYS A 107 51.98 36.26
REMARK 500 2 PHE A 127 45.85 -103.98
REMARK 500 2 THR A 139 -24.75 -39.97
REMARK 500 2 PRO A 160 2.78 -69.77
REMARK 500 3 SER A 2 119.53 -168.58
REMARK 500 3 ASP A 32 58.70 -91.59
REMARK 500 3 ASP A 38 -35.21 -35.96
REMARK 500 3 VAL A 80 -28.09 -37.37
REMARK 500 3 LYS A 107 51.09 35.14
REMARK 500 3 PHE A 127 57.12 -98.63
REMARK 500 3 THR A 149 -177.02 -65.31
REMARK 500 4 LEU A 10 45.56 -82.16
REMARK 500 4 GLU A 26 33.57 -84.42
REMARK 500 4 ASP A 32 44.86 -100.61
REMARK 500 4 VAL A 80 -25.91 -38.76
REMARK 500 4 LEU A 89 -36.39 -38.07
REMARK 500 4 CYS A 92 32.88 -90.93
REMARK 500 4 ALA A 97 -36.40 -37.70
REMARK 500 4 PHE A 127 49.48 -109.96
REMARK 500 4 SER A 134 -35.67 -37.20
REMARK 500 4 SER A 155 153.89 -47.41
REMARK 500 4 GLN A 156 60.76 -102.62
REMARK 500 5 GLU A 17 -31.43 -37.98
REMARK 500 5 VAL A 80 -26.08 -39.56
REMARK 500 5 LEU A 89 -38.89 -38.13
REMARK 500 5 CYS A 92 33.90 -86.35
REMARK 500 5 LEU A 116 -70.03 -55.30
REMARK 500 5 PHE A 127 61.46 -109.45
REMARK 500 5 SER A 155 171.40 -46.54
REMARK 500 5 THR A 157 48.14 34.13
REMARK 500 5 SER A 162 -50.55 -131.68
REMARK 500 6 GLU A 26 -19.75 -48.71
REMARK 500 6 ASP A 32 54.03 70.46
REMARK 500 6 LEU A 89 -30.64 -38.25
REMARK 500 6 CYS A 92 35.33 -89.48
REMARK 500 6 LYS A 107 38.51 34.49
REMARK 500 6 PHE A 127 70.60 -117.67
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000649.1 RELATED DB: TARGETDB
DBREF 1X5B A 8 157 UNP O75886 STAM2_HUMAN 1 150
SEQADV 1X5B GLY A 1 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 2 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 3 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B GLY A 4 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 5 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 6 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B GLY A 7 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 158 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B GLY A 159 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B PRO A 160 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 161 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B SER A 162 UNP O75886 CLONING ARTIFACT
SEQADV 1X5B GLY A 163 UNP O75886 CLONING ARTIFACT
SEQRES 1 A 163 GLY SER SER GLY SER SER GLY MET PRO LEU PHE THR ALA
SEQRES 2 A 163 ASN PRO PHE GLU GLN ASP VAL GLU LYS ALA THR ASN GLU
SEQRES 3 A 163 TYR ASN THR THR GLU ASP TRP SER LEU ILE MET ASP ILE
SEQRES 4 A 163 CYS ASP LYS VAL GLY SER THR PRO ASN GLY ALA LYS ASP
SEQRES 5 A 163 CYS LEU LYS ALA ILE MET LYS ARG VAL ASN HIS LYS VAL
SEQRES 6 A 163 PRO HIS VAL ALA LEU GLN ALA LEU THR LEU LEU GLY ALA
SEQRES 7 A 163 CYS VAL ALA ASN CYS GLY LYS ILE PHE HIS LEU GLU VAL
SEQRES 8 A 163 CYS SER ARG ASP PHE ALA THR GLU VAL ARG ALA VAL ILE
SEQRES 9 A 163 LYS ASN LYS ALA HIS PRO LYS VAL CYS GLU LYS LEU LYS
SEQRES 10 A 163 SER LEU MET VAL GLU TRP SER GLU GLU PHE GLN LYS ASP
SEQRES 11 A 163 PRO GLN PHE SER LEU ILE SER ALA THR ILE LYS SER MET
SEQRES 12 A 163 LYS GLU GLU GLY ILE THR PHE PRO PRO ALA GLY SER GLN
SEQRES 13 A 163 THR SER GLY PRO SER SER GLY
HELIX 1 1 PHE A 16 THR A 24 1 9
HELIX 2 2 ASP A 32 THR A 46 1 15
HELIX 3 3 ASN A 48 ASN A 62 1 15
HELIX 4 4 VAL A 65 CYS A 83 1 19
HELIX 5 5 GLY A 84 CYS A 92 1 9
HELIX 6 6 SER A 93 ASN A 106 1 14
HELIX 7 7 HIS A 109 PHE A 127 1 19
HELIX 8 8 PHE A 133 GLU A 145 1 13
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