Header list of 1wi4.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 28-MAY-04 1WI4
TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF SYNTAXIN BINDING PROTEIN 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNTAXIN BINDING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: SYNIP;
COMPND 6 ENGINEERED: 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 2700027C09;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030203-50;
SOURCE 8 OTHER_DETAILS: CELL FREE SYNTHESIS
KEYWDS SYNTAXIN4-INTERACTING PROTEIN, SYNIP, STXBP4 PROTEIN, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.ENDO,T.TOMIZAWA,T.KIGAWA,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WI4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WI4 1 VERSN
REVDAT 1 07-JUN-05 1WI4 0
JRNL AUTH H.ENDO,T.TOMIZAWA,T.KIGAWA,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PDZ DOMAIN OF SYNTAXIN BINDING
JRNL TITL 2 PROTEIN 4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.1
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WI4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023603.
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 : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 200MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM PHOSPHATE BUFFER; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 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 : XWINNMR 2.6, NMRPIPE 20020405,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.899,
REMARK 210 CYANA 2.0.1
REMARK 210 METHOD USED : NULL
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 SER A 5 -178.98 49.41
REMARK 500 1 SER A 6 -70.12 70.55
REMARK 500 1 ASP A 11 104.22 -179.63
REMARK 500 1 GLU A 24 -53.26 -128.40
REMARK 500 1 LEU A 27 -70.86 -50.79
REMARK 500 1 GLU A 47 140.37 -172.60
REMARK 500 1 ARG A 59 -37.48 -38.23
REMARK 500 1 VAL A 67 -46.45 -140.18
REMARK 500 1 ASN A 70 -66.76 71.68
REMARK 500 1 LYS A 71 30.27 -179.03
REMARK 500 1 LEU A 91 143.91 65.14
REMARK 500 1 SER A 93 -158.75 -112.87
REMARK 500 1 PRO A 96 -172.29 -69.80
REMARK 500 1 SER A 104 120.77 -176.53
REMARK 500 1 SER A 108 158.99 58.29
REMARK 500 2 ASP A 11 124.13 -178.93
REMARK 500 2 ILE A 35 -30.50 -37.63
REMARK 500 2 ILE A 45 104.74 -43.76
REMARK 500 2 GLU A 47 128.44 179.92
REMARK 500 2 LYS A 61 160.64 178.01
REMARK 500 2 VAL A 67 -34.54 -139.32
REMARK 500 2 SER A 68 144.39 177.64
REMARK 500 2 ASN A 70 -67.63 70.52
REMARK 500 2 LYS A 71 38.23 -176.25
REMARK 500 2 ALA A 89 167.65 -43.50
REMARK 500 2 LEU A 91 173.73 58.68
REMARK 500 2 ARG A 92 90.17 33.57
REMARK 500 2 SER A 95 131.03 -36.11
REMARK 500 2 PRO A 96 -175.38 -69.70
REMARK 500 2 SER A 104 38.28 -82.13
REMARK 500 2 PRO A 106 -176.73 -69.71
REMARK 500 2 SER A 107 176.94 55.96
REMARK 500 3 ASP A 11 177.08 56.61
REMARK 500 3 ARG A 12 156.49 -41.91
REMARK 500 3 GLU A 24 -51.27 -152.85
REMARK 500 3 GLU A 47 139.24 -172.88
REMARK 500 3 VAL A 67 -50.26 -136.85
REMARK 500 3 ASN A 70 -66.17 71.84
REMARK 500 3 LYS A 71 36.56 -173.57
REMARK 500 3 ALA A 89 -150.15 35.23
REMARK 500 3 LYS A 90 -31.27 -138.86
REMARK 500 3 LEU A 91 36.27 32.03
REMARK 500 3 ARG A 92 40.85 -145.22
REMARK 500 4 SER A 6 -57.93 -178.38
REMARK 500 4 SER A 8 86.41 -161.12
REMARK 500 4 ASP A 11 170.05 -49.68
REMARK 500 4 ARG A 12 156.44 -46.50
REMARK 500 4 THR A 22 103.78 -57.88
REMARK 500 4 GLU A 24 -44.79 -144.46
REMARK 500 4 ILE A 35 -34.42 -37.24
REMARK 500
REMARK 500 THIS ENTRY HAS 311 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007008668 RELATED DB: TARGETDB
DBREF 1WI4 A 8 103 UNP Q9WV89 STXB4_MOUSE 12 107
SEQADV 1WI4 GLY A 1 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 2 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 3 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 GLY A 4 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 5 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 6 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 GLY A 7 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 104 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 GLY A 105 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 PRO A 106 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 107 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 SER A 108 UNP Q9WV89 CLONING ARTIFACT
SEQADV 1WI4 GLY A 109 UNP Q9WV89 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY SER PRO LEU ASP ARG ASP
SEQRES 2 A 109 PRO ALA PHE ARG VAL ILE THR VAL THR LYS GLU THR GLY
SEQRES 3 A 109 LEU GLY LEU LYS ILE LEU GLY GLY ILE ASN ARG ASN GLU
SEQRES 4 A 109 GLY PRO LEU VAL TYR ILE HIS GLU VAL ILE PRO GLY GLY
SEQRES 5 A 109 ASP CYS TYR LYS ASP GLY ARG LEU LYS PRO GLY ASP GLN
SEQRES 6 A 109 LEU VAL SER ILE ASN LYS GLU SER MET ILE GLY VAL SER
SEQRES 7 A 109 PHE GLU GLU ALA LYS SER ILE ILE THR ARG ALA LYS LEU
SEQRES 8 A 109 ARG SER GLU SER PRO TRP GLU ILE ALA PHE ILE ARG SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 GLY A 52 GLY A 58 1 7
HELIX 2 2 SER A 78 ALA A 89 1 12
SHEET 1 A 3 PHE A 16 VAL A 21 0
SHEET 2 A 3 TRP A 97 ILE A 102 -1 O PHE A 101 N ARG A 17
SHEET 3 A 3 LEU A 66 ILE A 69 -1 N VAL A 67 O ALA A 100
SHEET 1 B 2 LEU A 29 GLY A 33 0
SHEET 2 B 2 VAL A 43 VAL A 48 -1 O TYR A 44 N LEU A 32
CISPEP 1 GLY A 40 PRO A 41 1 0.01
CISPEP 2 GLY A 40 PRO A 41 2 0.07
CISPEP 3 GLY A 40 PRO A 41 3 0.08
CISPEP 4 GLY A 40 PRO A 41 4 0.07
CISPEP 5 GLY A 40 PRO A 41 5 0.12
CISPEP 6 GLY A 40 PRO A 41 6 -0.01
CISPEP 7 GLY A 40 PRO A 41 7 0.05
CISPEP 8 GLY A 40 PRO A 41 8 0.01
CISPEP 9 GLY A 40 PRO A 41 9 0.01
CISPEP 10 GLY A 40 PRO A 41 10 0.05
CISPEP 11 GLY A 40 PRO A 41 11 0.07
CISPEP 12 GLY A 40 PRO A 41 12 0.03
CISPEP 13 GLY A 40 PRO A 41 13 0.08
CISPEP 14 GLY A 40 PRO A 41 14 0.06
CISPEP 15 GLY A 40 PRO A 41 15 0.02
CISPEP 16 GLY A 40 PRO A 41 16 0.08
CISPEP 17 GLY A 40 PRO A 41 17 -0.03
CISPEP 18 GLY A 40 PRO A 41 18 0.09
CISPEP 19 GLY A 40 PRO A 41 19 0.06
CISPEP 20 GLY A 40 PRO A 41 20 0.07
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