Header list of 1wxt.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 01-FEB-05 1WXT
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF HUMAN HYPOTHETICAL PROTEIN
TITLE 2 FLJ21522
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN FLJ21522;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 8-LIKE
COMPND 6 PROTEIN 3 ISOFORM C;
COMPND 7 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: HUMAN CDNA COL05884;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040517-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, EPS8-RELATED PROTEIN 3, PROTEIN-PROTEIN INTERACTION,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 4 FUNCTIONAL ANALYSES, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,K.SAITO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WXT 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WXT 1 VERSN
REVDAT 2 17-JAN-06 1WXT 1 JRNL TITLE
REVDAT 1 01-AUG-05 1WXT 0
JRNL AUTH M.YONEYAMA,K.SAITO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF HUMAN HYPOTHETICAL
JRNL TITL 2 PROTEIN FLJ21522
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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WXT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024129.
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 : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.33MM SH3 DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL; 100MM 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 : 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 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 SER A 3 96.15 -47.49
REMARK 500 1 LEU A 35 -52.86 -123.31
REMARK 500 1 HIS A 37 42.44 -107.22
REMARK 500 1 SER A 38 -62.32 -101.17
REMARK 500 1 PRO A 61 85.45 -69.78
REMARK 500 1 LEU A 62 97.64 -35.02
REMARK 500 1 SER A 67 173.59 -55.51
REMARK 500 2 HIS A 37 69.58 -104.99
REMARK 500 2 SER A 38 -61.28 -122.99
REMARK 500 2 PRO A 61 94.81 -69.74
REMARK 500 3 LEU A 35 -57.84 -120.00
REMARK 500 3 PRO A 61 88.48 -69.78
REMARK 500 3 LEU A 62 -73.91 -64.81
REMARK 500 4 HIS A 37 47.77 -107.56
REMARK 500 4 ALA A 48 -36.67 -39.20
REMARK 500 4 PRO A 61 92.50 -69.73
REMARK 500 5 GLU A 15 140.08 -36.88
REMARK 500 5 LEU A 35 -63.68 -108.30
REMARK 500 5 HIS A 37 46.03 -102.45
REMARK 500 5 SER A 38 -67.56 -109.31
REMARK 500 5 PRO A 61 79.75 -69.72
REMARK 500 5 LEU A 62 134.26 -38.29
REMARK 500 5 SER A 67 153.73 -43.29
REMARK 500 6 GLU A 17 93.02 -68.07
REMARK 500 6 LEU A 35 -55.90 -126.28
REMARK 500 6 PRO A 61 96.80 -69.76
REMARK 500 7 SER A 5 100.18 -59.35
REMARK 500 7 LEU A 35 -61.47 -127.03
REMARK 500 7 HIS A 37 40.88 -104.10
REMARK 500 7 PRO A 61 85.37 -69.74
REMARK 500 8 HIS A 37 41.91 -105.81
REMARK 500 8 SER A 38 -65.35 -104.31
REMARK 500 8 ILE A 58 32.54 -91.05
REMARK 500 8 PRO A 61 95.11 -69.78
REMARK 500 8 SER A 63 147.18 -172.67
REMARK 500 9 PRO A 21 1.48 -69.73
REMARK 500 9 HIS A 37 35.03 -98.09
REMARK 500 9 SER A 38 -72.31 -99.84
REMARK 500 9 LEU A 62 -175.08 -65.74
REMARK 500 9 SER A 66 109.63 -169.92
REMARK 500 9 SER A 67 144.78 -38.15
REMARK 500 10 LEU A 35 -56.52 -122.03
REMARK 500 10 HIS A 37 43.06 -104.98
REMARK 500 10 ILE A 58 31.32 -98.05
REMARK 500 10 PRO A 61 84.37 -69.82
REMARK 500 10 SER A 67 99.00 -49.07
REMARK 500 11 SER A 5 95.97 -62.93
REMARK 500 11 ALA A 18 151.05 -45.06
REMARK 500 11 LEU A 35 -51.36 -123.18
REMARK 500 11 SER A 38 -70.80 -93.98
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001086.1 RELATED DB: TARGETDB
DBREF 1WXT A 8 62 UNP Q5T8Q6 Q5T8Q6_HUMAN 423 477
SEQADV 1WXT GLY A 1 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 2 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 3 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT GLY A 4 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 5 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 6 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT GLY A 7 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 63 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT GLY A 64 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT PRO A 65 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 66 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT SER A 67 UNP Q5T8Q6 CLONING ARTIFACT
SEQADV 1WXT GLY A 68 UNP Q5T8Q6 CLONING ARTIFACT
SEQRES 1 A 68 GLY SER SER GLY SER SER GLY LEU LYS MET GLN VAL LEU
SEQRES 2 A 68 TYR GLU PHE GLU ALA ARG ASN PRO ARG GLU LEU THR VAL
SEQRES 3 A 68 VAL GLN GLY GLU LYS LEU GLU VAL LEU ASP HIS SER LYS
SEQRES 4 A 68 ARG TRP TRP LEU VAL LYS ASN GLU ALA GLY ARG SER GLY
SEQRES 5 A 68 TYR ILE PRO SER ASN ILE LEU GLU PRO LEU SER GLY PRO
SEQRES 6 A 68 SER SER GLY
SHEET 1 A 5 SER A 51 PRO A 55 0
SHEET 2 A 5 TRP A 41 LYS A 45 -1 N TRP A 42 O ILE A 54
SHEET 3 A 5 LYS A 31 ASP A 36 -1 N LEU A 35 O LEU A 43
SHEET 4 A 5 LEU A 8 VAL A 12 -1 N MET A 10 O LEU A 32
SHEET 5 A 5 LEU A 59 GLU A 60 -1 O GLU A 60 N GLN A 11
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