Header list of 1ufx.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 10-JUN-03 1UFX
TITLE SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF HUMAN KIAA1526 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1526 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ 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 FJ04743;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-48;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,N.KOBAYASHI,S.KOSHIBA,T.KIGAWA,M.INOUE,M.SHIROUZU,T.TERADA,
AUTHOR 2 T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA,A.TANAKA,
AUTHOR 3 T.OSANAI,Y.MATSUO,O.OHARA,T.NAGASE,R.KIKUNO,M.NAKAYAMA,S.YOKOYAMA,
AUTHOR 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UFX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UFX 1 VERSN
REVDAT 1 10-DEC-03 1UFX 0
JRNL AUTH N.TOCHIO,N.KOBAYASHI,S.KOSHIBA,T.KIGAWA,M.INOUE,M.SHIROUZU,
JRNL AUTH 2 T.TERADA,T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,
JRNL AUTH 3 M.YOSHIDA,A.TANAKA,T.OSANAI,Y.MATSUO,O.OHARA,T.NAGASE,
JRNL AUTH 4 R.KIKUNO,M.NAKAYAMA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF HUMAN KIAA1526
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 2.0.14
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UFX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000005784.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM PDZ 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_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 : NMRPIPE 200204025, NMRVIEW
REMARK 210 5.0.4, KUJIRA 0.816, CYANA 2.0.14
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: 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 2 173.19 -53.83
REMARK 500 1 THR A 83 157.63 -39.71
REMARK 500 1 PHE A 96 145.26 -37.68
REMARK 500 1 SER A 102 -64.41 -105.38
REMARK 500 2 ALA A 16 -177.29 -67.36
REMARK 500 2 TYR A 88 -179.11 -173.73
REMARK 500 2 GLU A 95 81.27 -61.59
REMARK 500 2 PHE A 96 94.22 -57.79
REMARK 500 3 SER A 2 41.19 38.73
REMARK 500 3 LYS A 14 49.83 -76.61
REMARK 500 3 LEU A 19 -71.39 -55.23
REMARK 500 3 THR A 83 149.63 -38.67
REMARK 500 3 ASP A 87 38.29 -87.03
REMARK 500 3 TYR A 88 -179.53 -170.33
REMARK 500 3 GLU A 95 91.41 -60.70
REMARK 500 4 THR A 83 149.01 -36.62
REMARK 500 4 ASP A 87 39.57 -83.26
REMARK 500 4 PHE A 96 139.60 -37.66
REMARK 500 5 ASN A 28 40.21 -90.26
REMARK 500 5 ARG A 30 -35.24 -37.45
REMARK 500 5 THR A 83 145.34 -38.74
REMARK 500 5 GLU A 95 80.43 -62.52
REMARK 500 5 PHE A 96 90.06 -59.08
REMARK 500 5 ASN A 97 115.33 -38.79
REMARK 500 5 SER A 98 136.28 -174.51
REMARK 500 6 LYS A 14 83.60 -68.98
REMARK 500 6 ALA A 27 -38.02 -39.87
REMARK 500 6 THR A 29 174.46 -56.26
REMARK 500 6 THR A 83 145.15 -36.97
REMARK 500 6 ASP A 87 41.02 -84.08
REMARK 500 6 PHE A 96 125.85 -36.33
REMARK 500 6 PRO A 100 90.99 -69.71
REMARK 500 7 SER A 5 98.21 -69.36
REMARK 500 7 LYS A 14 49.24 -78.20
REMARK 500 7 THR A 83 143.60 -36.56
REMARK 500 7 SER A 98 166.90 -45.41
REMARK 500 8 GLU A 95 83.19 -61.15
REMARK 500 9 LYS A 14 86.52 -67.27
REMARK 500 9 HIS A 55 175.02 -59.79
REMARK 500 9 GLU A 95 81.89 -61.17
REMARK 500 10 SER A 2 103.23 -43.83
REMARK 500 10 SER A 3 150.57 -43.49
REMARK 500 10 SER A 5 162.68 -43.78
REMARK 500 10 LYS A 14 75.66 -60.86
REMARK 500 10 GLU A 95 89.58 -64.31
REMARK 500 10 ASN A 97 121.54 -39.68
REMARK 500 10 SER A 102 128.59 -35.88
REMARK 500 11 ARG A 30 -35.31 -36.49
REMARK 500 11 THR A 83 152.48 -35.80
REMARK 500 11 ASP A 87 40.30 -104.53
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001498.3 RELATED DB: TARGETDB
DBREF 1UFX A 8 97 UNP Q9P202 WHRN_HUMAN 871 960
SEQADV 1UFX GLY A 1 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 2 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 3 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX GLY A 4 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 5 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 6 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX GLY A 7 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 98 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX GLY A 99 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX PRO A 100 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 101 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX SER A 102 UNP Q9P202 CLONING ARTIFACT
SEQADV 1UFX GLY A 103 UNP Q9P202 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY THR LEU VAL ARG VAL LYS
SEQRES 2 A 103 LYS SER ALA ALA THR LEU GLY ILE ALA ILE GLU GLY GLY
SEQRES 3 A 103 ALA ASN THR ARG GLN PRO LEU PRO ARG ILE VAL THR ILE
SEQRES 4 A 103 GLN ARG GLY GLY SER ALA HIS ASN CYS GLY GLN LEU LYS
SEQRES 5 A 103 VAL GLY HIS VAL ILE LEU GLU VAL ASN GLY LEU THR LEU
SEQRES 6 A 103 ARG GLY LYS GLU HIS ARG GLU ALA ALA ARG ILE ILE ALA
SEQRES 7 A 103 GLU ALA PHE LYS THR LYS ASP ARG ASP TYR ILE ASP PHE
SEQRES 8 A 103 LEU VAL THR GLU PHE ASN SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 43 GLY A 49 1 7
HELIX 2 2 GLU A 69 THR A 83 1 15
SHEET 1 A 2 THR A 8 LYS A 13 0
SHEET 2 A 2 TYR A 88 VAL A 93 -1 O VAL A 93 N THR A 8
SHEET 1 B 2 ILE A 21 GLU A 24 0
SHEET 2 B 2 ARG A 35 ILE A 39 -1 O THR A 38 N ALA A 22
SHEET 1 C 2 GLU A 59 VAL A 60 0
SHEET 2 C 2 LEU A 63 THR A 64 -1 O LEU A 63 N VAL A 60
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