Header list of 1wxa.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 20-JAN-05 1WXA
TITLE SOLUTION STRUCTURE OF RAS-BINDING DOMAIN IN MOUSE AF-6 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AFADIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RAS-BINDING DOMAIN;
COMPND 5 SYNONYM: AF-6 PROTEIN;
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 4932441D06;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040719-08;
SOURCE 8 OTHER_DETAILS: CELL-FREE SYNTHESIS
KEYWDS RAS-BINDING DOMAIN, UBIQUITIN-LIKE FOLD, AF-6 PROTEIN, STRUCTURAL
KEYWDS 2 GENOMICS, AFADIN, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ZHAO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WXA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WXA 1 VERSN
REVDAT 1 20-JUL-05 1WXA 0
JRNL AUTH C.ZHAO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RAS-BINDING DOMAIN IN MOUSE AF-6
JRNL TITL 2 PROTEIN
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 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WXA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024110.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.28MM PROTEIN U-15N, 13C; 20MM
REMARK 210 D-TRIS-HCL (PH7.0); 100MM NACL;
REMARK 210 1MM D-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 : 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 0.921, CYANA 1.0.8
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: 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 HE1 TRP A 94 O GLY A 99 1.50
REMARK 500 H VAL A 62 O VAL A 102 1.54
REMARK 500 O ALA A 36 H VAL A 40 1.59
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 5 89.24 55.10
REMARK 500 1 SER A 8 -54.81 -135.55
REMARK 500 1 SER A 18 -61.05 173.29
REMARK 500 1 PRO A 24 -82.09 -74.94
REMARK 500 1 THR A 33 -41.99 -165.47
REMARK 500 1 ASP A 34 162.27 -41.81
REMARK 500 1 LEU A 49 54.24 -109.61
REMARK 500 1 GLU A 50 47.29 -85.26
REMARK 500 1 LYS A 51 -45.64 -156.18
REMARK 500 1 GLU A 52 165.98 -48.19
REMARK 500 1 GLN A 69 71.89 -177.95
REMARK 500 1 HIS A 70 -54.18 -164.49
REMARK 500 1 GLU A 73 28.75 48.27
REMARK 500 1 ARG A 74 106.15 -49.64
REMARK 500 1 ASP A 82 -79.12 -49.10
REMARK 500 1 ASP A 83 -36.34 170.22
REMARK 500 1 GLU A 93 52.12 -115.29
REMARK 500 1 SER A 111 92.98 -163.60
REMARK 500 1 SER A 114 104.34 56.23
REMARK 500 2 SER A 2 -58.47 -179.24
REMARK 500 2 SER A 3 93.63 58.21
REMARK 500 2 SER A 18 -55.45 175.41
REMARK 500 2 PRO A 24 -88.26 -74.99
REMARK 500 2 THR A 32 33.39 -92.86
REMARK 500 2 THR A 33 -45.61 -138.22
REMARK 500 2 ASP A 34 174.96 -52.80
REMARK 500 2 THR A 35 -167.64 -128.76
REMARK 500 2 GLU A 50 48.21 -89.31
REMARK 500 2 LYS A 51 -45.66 -155.77
REMARK 500 2 GLU A 52 -176.07 -51.53
REMARK 500 2 ASP A 72 -39.47 174.46
REMARK 500 2 GLU A 73 -86.65 57.36
REMARK 500 2 ARG A 74 78.52 61.35
REMARK 500 2 ASP A 83 -34.58 156.13
REMARK 500 2 GLU A 93 44.44 -103.93
REMARK 500 2 SER A 111 75.62 61.96
REMARK 500 3 SER A 5 -58.63 -135.94
REMARK 500 3 SER A 8 99.30 57.84
REMARK 500 3 ASP A 17 69.32 -68.16
REMARK 500 3 SER A 18 -72.01 170.61
REMARK 500 3 ASN A 22 -72.69 -62.39
REMARK 500 3 THR A 33 -38.86 -174.99
REMARK 500 3 ASP A 34 158.03 -39.92
REMARK 500 3 GLU A 50 46.51 -86.88
REMARK 500 3 LYS A 51 -46.15 -156.17
REMARK 500 3 GLU A 52 165.68 -44.33
REMARK 500 3 GLN A 69 54.04 -145.67
REMARK 500 3 ASP A 72 136.89 178.40
REMARK 500 3 ASP A 82 -161.83 -65.53
REMARK 500 3 ASP A 84 30.38 -162.29
REMARK 500
REMARK 500 THIS ENTRY HAS 357 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007011839.3 RELATED DB: TARGETDB
DBREF 1WXA A 8 110 UNP Q9QZQ1 AFAD_MOUSE 246 348
SEQADV 1WXA GLY A 1 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 2 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 3 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA GLY A 4 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 5 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 6 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA GLY A 7 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 111 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA GLY A 112 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA PRO A 113 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 114 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA SER A 115 UNP Q9QZQ1 CLONING ARTIFACT
SEQADV 1WXA GLY A 116 UNP Q9QZQ1 CLONING ARTIFACT
SEQRES 1 A 116 GLY SER SER GLY SER SER GLY SER GLY GLY THR LEU ARG
SEQRES 2 A 116 ILE TYR ALA ASP SER LEU LYS PRO ASN ILE PRO TYR LYS
SEQRES 3 A 116 THR ILE LEU LEU SER THR THR ASP THR ALA ASP PHE ALA
SEQRES 4 A 116 VAL ALA GLU SER LEU GLU LYS TYR GLY LEU GLU LYS GLU
SEQRES 5 A 116 ASN PRO LYS ASP TYR CYS ILE ALA ARG VAL MET LEU PRO
SEQRES 6 A 116 PRO GLY ALA GLN HIS SER ASP GLU ARG GLY ALA LYS GLU
SEQRES 7 A 116 ILE ILE LEU ASP ASP ASP GLU CYS PRO LEU GLN ILE PHE
SEQRES 8 A 116 ARG GLU TRP PRO SER ASP LYS GLY ILE LEU VAL PHE GLN
SEQRES 9 A 116 LEU LYS ARG ARG PRO PRO SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 36 TYR A 47 1 12
HELIX 2 2 PRO A 87 ARG A 92 1 6
HELIX 3 3 SER A 96 LYS A 98 5 3
SHEET 1 A 2 THR A 11 ILE A 14 0
SHEET 2 A 2 LYS A 26 LEU A 29 -1 O LYS A 26 N ILE A 14
SHEET 1 B 3 LYS A 77 ILE A 79 0
SHEET 2 B 3 TYR A 57 MET A 63 -1 N ARG A 61 O ILE A 79
SHEET 3 B 3 LEU A 101 ARG A 107 -1 O VAL A 102 N VAL A 62
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