Header list of 1wxu.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 01-FEB-05 1WXU
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF MOUSE PEROXISOMAL BIOGENESIS
TITLE 2 FACTOR 13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOMAL BIOGENESIS FACTOR 13;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 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: PEX13;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040802-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, PEX13, PROTEIN-PROTEIN INTERACTION, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA,
KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 4 PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WXU 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WXU 1 VERSN
REVDAT 2 17-JAN-06 1WXU 1 JRNL TITLE
REVDAT 1 01-AUG-05 1WXU 0
JRNL AUTH M.YONEYAMA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF MOUSE PEROXISOMAL
JRNL TITL 2 BIOGENESIS FACTOR 13
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), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WXU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024130.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 220
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.09MM SH3 DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL; 200MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 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 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
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 THR A 8 87.12 -57.35
REMARK 500 1 GLN A 50 144.21 -35.30
REMARK 500 1 PRO A 51 -175.20 -69.77
REMARK 500 1 ALA A 71 -60.40 -98.88
REMARK 500 2 ALA A 38 100.69 -45.45
REMARK 500 2 GLN A 50 145.21 -39.71
REMARK 500 2 PRO A 51 -172.40 -69.70
REMARK 500 2 VAL A 53 136.34 -33.67
REMARK 500 2 GLN A 64 -60.18 -106.37
REMARK 500 2 LYS A 79 136.43 -35.81
REMARK 500 2 ILE A 86 106.95 -54.22
REMARK 500 3 ALA A 38 103.78 -48.53
REMARK 500 3 LYS A 47 -34.00 -34.66
REMARK 500 3 PRO A 51 -174.43 -69.75
REMARK 500 3 ALA A 71 -60.49 -104.46
REMARK 500 4 GLU A 32 -36.29 -37.13
REMARK 500 4 ALA A 38 105.27 -49.83
REMARK 500 4 LYS A 47 -37.43 -35.85
REMARK 500 4 PRO A 51 -167.53 -69.73
REMARK 500 5 SER A 6 113.54 -36.89
REMARK 500 5 ALA A 38 101.67 -48.61
REMARK 500 5 LYS A 47 -32.67 -35.86
REMARK 500 5 GLN A 50 154.81 -39.94
REMARK 500 5 PRO A 51 -165.36 -69.72
REMARK 500 5 GLN A 64 -60.36 -95.67
REMARK 500 5 LYS A 79 143.65 -38.81
REMARK 500 5 GLU A 87 115.20 -162.35
REMARK 500 5 PRO A 90 99.97 -69.76
REMARK 500 6 SER A 2 102.30 -42.60
REMARK 500 6 ALA A 38 101.03 -44.68
REMARK 500 6 GLN A 50 143.78 -37.10
REMARK 500 6 PRO A 51 -168.70 -69.68
REMARK 500 6 SER A 91 43.36 35.96
REMARK 500 7 ALA A 38 102.45 -54.61
REMARK 500 7 LEU A 46 157.04 -46.90
REMARK 500 7 GLN A 50 144.10 -38.78
REMARK 500 7 PRO A 51 -174.82 -69.74
REMARK 500 8 SER A 5 116.45 -172.94
REMARK 500 8 ALA A 38 104.74 -52.97
REMARK 500 8 ALA A 45 -174.98 -53.32
REMARK 500 8 GLN A 50 146.56 -37.99
REMARK 500 8 PRO A 51 -163.82 -69.73
REMARK 500 9 SER A 3 46.21 -106.18
REMARK 500 9 ALA A 38 101.60 -57.62
REMARK 500 9 PRO A 51 -169.43 -69.71
REMARK 500 9 ILE A 86 106.37 -34.72
REMARK 500 9 SER A 88 -66.04 -92.20
REMARK 500 9 PRO A 90 98.99 -69.79
REMARK 500 9 SER A 92 99.30 -60.75
REMARK 500 10 ALA A 28 154.05 -46.54
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT008001098.1 RELATED DB: TARGETDB
DBREF 1WXU A 8 87 UNP Q8CCJ5 Q8CCJ5_MOUSE 267 346
SEQADV 1WXU GLY A 1 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 2 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 3 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU GLY A 4 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 5 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 6 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU GLY A 7 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 88 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU GLY A 89 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU PRO A 90 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 91 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU SER A 92 UNP Q8CCJ5 CLONING ARTIFACT
SEQADV 1WXU GLY A 93 UNP Q8CCJ5 CLONING ARTIFACT
SEQRES 1 A 93 GLY SER SER GLY SER SER GLY THR ASN TRP ALA SER GLY
SEQRES 2 A 93 GLU ASP ASP HIS VAL VAL ALA ARG ALA GLU TYR ASP PHE
SEQRES 3 A 93 VAL ALA VAL SER ASP GLU GLU ILE SER PHE ARG ALA GLY
SEQRES 4 A 93 ASP MET LEU ASN LEU ALA LEU LYS GLU GLN GLN PRO LYS
SEQRES 5 A 93 VAL ARG GLY TRP LEU LEU ALA SER LEU ASP GLY GLN THR
SEQRES 6 A 93 THR GLY LEU ILE PRO ALA ASN TYR VAL LYS ILE LEU GLY
SEQRES 7 A 93 LYS ARG ARG GLY ARG LYS THR ILE GLU SER GLY PRO SER
SEQRES 8 A 93 SER GLY
SHEET 1 A 2 ALA A 20 ALA A 22 0
SHEET 2 A 2 VAL A 74 ILE A 76 -1 O LYS A 75 N ARG A 21
SHEET 1 B 3 ASN A 43 LEU A 44 0
SHEET 2 B 3 LEU A 57 SER A 60 -1 O SER A 60 N ASN A 43
SHEET 3 B 3 GLY A 67 ILE A 69 -1 O GLY A 67 N ALA A 59
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