Header list of 1v89.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 29-DEC-03 1V89
TITLE SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF HUMAN KIAA0053
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN KIAA0053;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY (PH) 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: KAZUSA CDNA HA01417;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030512-36;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PLECKSTRIN HOMOLOGY DOMAIN, PHOSPHATIDYLINOSITOL BINDING, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,H.HIROTA,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V89 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V89 1 VERSN
REVDAT 1 29-JUN-04 1V89 0
JRNL AUTH H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,H.HIROTA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 HUMAN KIAA0053 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DELTA 4.2, CYANA 1.0.7
REMARK 3 AUTHORS : JEOL (DELTA), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V89 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006330.
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 : 1.30MM PLECKSTRIN HOMOLOGY
REMARK 210 DOMAIN U-13C, 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA(6.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O; 1.30MM PLECKSTRIN
REMARK 210 HOMOLOGY DOMAIN U-13C, 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA(6.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 920 MHZ
REMARK 210 SPECTROMETER MODEL : ECA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.854, CYANA 1.0.7
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL A 104 H ARG A 108 1.53
REMARK 500 O ILE A 75 H TYR A 90 1.55
REMARK 500
REMARK 500 REMARK: NULL
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 6 -55.29 172.67
REMARK 500 1 ARG A 18 -173.81 -56.26
REMARK 500 1 LYS A 22 38.86 -98.78
REMARK 500 1 ALA A 33 -142.91 50.60
REMARK 500 1 GLN A 34 56.28 -94.50
REMARK 500 1 GLU A 42 40.69 -98.59
REMARK 500 1 GLU A 43 -54.57 -125.54
REMARK 500 1 GLN A 48 -70.59 -79.85
REMARK 500 1 THR A 63 -127.33 -66.29
REMARK 500 1 PHE A 71 77.29 -110.80
REMARK 500 1 SER A 79 101.26 53.40
REMARK 500 1 TRP A 80 92.58 -161.13
REMARK 500 1 ASP A 81 -47.54 -171.56
REMARK 500 1 GLN A 82 41.82 -100.14
REMARK 500 1 ARG A 84 43.63 -94.98
REMARK 500 1 MET A 85 -74.50 -128.14
REMARK 500 1 GLN A 87 79.49 -166.26
REMARK 500 1 SER A 89 176.58 -57.64
REMARK 500 1 ARG A 109 -71.06 -50.24
REMARK 500 1 SER A 116 110.69 -162.21
REMARK 500 2 SER A 6 109.84 -42.54
REMARK 500 2 PRO A 8 -163.09 -74.95
REMARK 500 2 ILE A 9 -57.80 -129.13
REMARK 500 2 ARG A 18 179.15 -58.42
REMARK 500 2 SER A 19 -90.10 -48.81
REMARK 500 2 GLN A 26 99.13 -67.38
REMARK 500 2 ALA A 33 -144.31 47.13
REMARK 500 2 GLU A 43 -89.84 -77.29
REMARK 500 2 ASP A 44 85.97 39.67
REMARK 500 2 ASN A 64 167.82 62.47
REMARK 500 2 GLU A 66 -77.23 -113.95
REMARK 500 2 GLU A 67 -156.85 59.82
REMARK 500 2 PHE A 71 65.97 -110.14
REMARK 500 2 TRP A 80 48.48 -168.24
REMARK 500 2 ASP A 81 -56.47 -156.96
REMARK 500 2 ASN A 83 -177.96 63.98
REMARK 500 2 ARG A 84 30.90 -95.14
REMARK 500 2 GLN A 87 62.44 39.74
REMARK 500 2 SER A 117 88.52 -165.39
REMARK 500 3 SER A 3 144.51 -178.65
REMARK 500 3 SER A 5 99.40 51.19
REMARK 500 3 SER A 19 -88.02 -39.71
REMARK 500 3 ALA A 33 -143.87 57.64
REMARK 500 3 GLN A 34 49.32 -91.74
REMARK 500 3 GLU A 42 46.37 -101.74
REMARK 500 3 ASN A 64 159.26 -40.42
REMARK 500 3 GLU A 66 31.15 -98.12
REMARK 500 3 ALA A 78 58.50 38.90
REMARK 500 3 SER A 79 88.98 37.80
REMARK 500 3 ASP A 81 99.98 -40.00
REMARK 500
REMARK 500 THIS ENTRY HAS 382 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000050.1 RELATED DB: TARGETDB
DBREF 1V89 A 8 112 UNP P42331 RHG25_HUMAN 40 144
SEQADV 1V89 GLY A 1 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 2 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 3 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 GLY A 4 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 5 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 6 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 GLY A 7 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 113 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 GLY A 114 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 PRO A 115 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 116 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 SER A 117 UNP P42331 CLONING ARTIFACT
SEQADV 1V89 GLY A 118 UNP P42331 CLONING ARTIFACT
SEQRES 1 A 118 GLY SER SER GLY SER SER GLY PRO ILE LYS MET GLY TRP
SEQRES 2 A 118 LEU LYS LYS GLN ARG SER ILE VAL LYS ASN TRP GLN GLN
SEQRES 3 A 118 ARG TYR PHE VAL LEU ARG ALA GLN GLN LEU TYR TYR TYR
SEQRES 4 A 118 LYS ASP GLU GLU ASP THR LYS PRO GLN GLY CYS MET TYR
SEQRES 5 A 118 LEU PRO GLY CYS THR ILE LYS GLU ILE ALA THR ASN PRO
SEQRES 6 A 118 GLU GLU ALA GLY LYS PHE VAL PHE GLU ILE ILE PRO ALA
SEQRES 7 A 118 SER TRP ASP GLN ASN ARG MET GLY GLN ASP SER TYR VAL
SEQRES 8 A 118 LEU MET ALA SER SER GLN ALA GLU MET GLU GLU TRP VAL
SEQRES 9 A 118 LYS PHE LEU ARG ARG VAL ALA GLY SER GLY PRO SER SER
SEQRES 10 A 118 GLY
HELIX 1 1 GLN A 97 ALA A 111 1 15
SHEET 1 A 7 GLY A 49 MET A 51 0
SHEET 2 A 7 GLN A 35 TYR A 39 -1 N LEU A 36 O MET A 51
SHEET 3 A 7 TRP A 24 ARG A 32 -1 N TYR A 28 O TYR A 39
SHEET 4 A 7 LYS A 10 GLN A 17 -1 N LEU A 14 O ARG A 27
SHEET 5 A 7 TYR A 90 MET A 93 -1 O MET A 93 N LYS A 15
SHEET 6 A 7 VAL A 72 PRO A 77 -1 N ILE A 75 O TYR A 90
SHEET 7 A 7 CYS A 56 ILE A 61 -1 N LYS A 59 O GLU A 74
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