Header list of 2daz.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 14-DEC-05 2DAZ
TITLE SOLUTION STRUCTURE OF THE 7TH PDZ DOMAIN OF INAD-LIKE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INAD-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: INADL PROTEIN, HINADL, PALS1-ASSOCIATED TIGHT JUNCTION
COMPND 6 PROTEIN, PROTEIN ASSOCIATED TO TIGHT JUNCTIONS;
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: INADL, PATJ;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-33;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, INAD-LIKE PROTEIN, INADL PROTEIN, HINADL, PALS1-
KEYWDS 2 ASSOCIATED TIGHT JUNCTION PROTEIN, PROTEIN ASSOCIATED TO TIGHT
KEYWDS 3 JUNCTIONS, INADL, PATJ, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 4 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,T.NAGASHIMA,K.IZUMI,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAZ 1 REMARK SEQADV SHEET
REVDAT 2 24-FEB-09 2DAZ 1 VERSN
REVDAT 1 14-JUN-06 2DAZ 0
JRNL AUTH K.INOUE,T.NAGASHIMA,K.IZUMI,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 7TH PDZ DOMAIN OF INAD-LIKE
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 : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DAZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025200.
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 : 1.28MM U-15N,13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.93191, 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 : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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 ASP A 8 40.20 -89.16
REMARK 500 1 LYS A 35 -34.18 -34.24
REMARK 500 1 LEU A 38 86.14 -69.27
REMARK 500 1 SER A 52 129.92 -175.02
REMARK 500 1 ASN A 59 120.64 -37.71
REMARK 500 1 TYR A 85 109.09 -42.86
REMARK 500 1 MET A 117 165.93 -42.68
REMARK 500 2 SER A 2 149.72 -39.65
REMARK 500 2 ASP A 8 39.53 -91.95
REMARK 500 2 LYS A 35 -37.29 -34.39
REMARK 500 2 SER A 49 -39.75 -35.27
REMARK 500 2 ASN A 59 118.83 -34.92
REMARK 500 2 ARG A 69 -52.01 -121.76
REMARK 500 2 TYR A 85 98.85 -35.79
REMARK 500 2 SER A 119 38.76 74.64
REMARK 500 2 SER A 123 138.58 -172.54
REMARK 500 3 SER A 3 154.70 -37.30
REMARK 500 3 SER A 6 78.10 -69.26
REMARK 500 3 ASN A 45 149.63 -34.87
REMARK 500 3 ASN A 80 50.03 35.10
REMARK 500 3 TYR A 85 100.04 -36.12
REMARK 500 3 MET A 117 152.46 -46.64
REMARK 500 4 ASP A 8 30.69 -87.50
REMARK 500 4 LYS A 33 122.63 -35.05
REMARK 500 4 LYS A 35 -32.18 -36.49
REMARK 500 4 LEU A 38 85.08 -69.35
REMARK 500 4 SER A 49 -38.54 -37.30
REMARK 500 4 TYR A 85 94.14 -40.14
REMARK 500 4 PRO A 121 2.41 -69.76
REMARK 500 4 SER A 122 37.64 -99.83
REMARK 500 5 ASP A 8 36.56 -94.91
REMARK 500 5 ASN A 45 137.45 -34.45
REMARK 500 5 ASN A 81 44.88 74.81
REMARK 500 5 TYR A 85 94.84 -41.95
REMARK 500 5 PRO A 121 2.80 -69.76
REMARK 500 6 LYS A 35 -28.71 -37.53
REMARK 500 6 SER A 49 -37.95 -36.44
REMARK 500 6 TYR A 85 99.04 -40.81
REMARK 500 6 ALA A 118 -38.77 -39.73
REMARK 500 6 PRO A 121 91.79 -69.78
REMARK 500 7 LYS A 33 132.17 -39.16
REMARK 500 7 LYS A 35 -39.68 -34.25
REMARK 500 7 SER A 49 -33.83 -35.47
REMARK 500 7 ASN A 59 119.00 -39.19
REMARK 500 7 ASN A 80 47.08 37.28
REMARK 500 7 SER A 122 157.58 -48.96
REMARK 500 8 LYS A 35 -38.27 -36.94
REMARK 500 8 TYR A 85 92.94 -42.92
REMARK 500 8 PRO A 121 2.70 -69.78
REMARK 500 9 SER A 6 152.88 -46.21
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003006830.2 RELATED DB: TARGETDB
DBREF 2DAZ A 8 118 UNP Q8NI35 INADL_HUMAN 1219 1329
SEQADV 2DAZ GLY A 1 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 2 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 3 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ GLY A 4 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 5 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 6 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ GLY A 7 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 119 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ GLY A 120 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ PRO A 121 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 122 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ SER A 123 UNP Q8NI35 CLONING ARTIFACT
SEQADV 2DAZ GLY A 124 UNP Q8NI35 CLONING ARTIFACT
SEQRES 1 A 124 GLY SER SER GLY SER SER GLY ASP ALA PHE THR ASP GLN
SEQRES 2 A 124 LYS ILE ARG GLN ARG TYR ALA ASP LEU PRO GLY GLU LEU
SEQRES 3 A 124 HIS ILE ILE GLU LEU GLU LYS ASP LYS ASN GLY LEU GLY
SEQRES 4 A 124 LEU SER LEU ALA GLY ASN LYS ASP ARG SER ARG MET SER
SEQRES 5 A 124 ILE PHE VAL VAL GLY ILE ASN PRO GLU GLY PRO ALA ALA
SEQRES 6 A 124 ALA ASP GLY ARG MET ARG ILE GLY ASP GLU LEU LEU GLU
SEQRES 7 A 124 ILE ASN ASN GLN ILE LEU TYR GLY ARG SER HIS GLN ASN
SEQRES 8 A 124 ALA SER ALA ILE ILE LYS THR ALA PRO SER LYS VAL LYS
SEQRES 9 A 124 LEU VAL PHE ILE ARG ASN GLU ASP ALA VAL ASN GLN MET
SEQRES 10 A 124 ALA SER GLY PRO SER SER GLY
HELIX 1 1 THR A 11 TYR A 19 1 9
HELIX 2 2 GLY A 62 GLY A 68 1 7
HELIX 3 3 SER A 88 ALA A 99 1 12
HELIX 4 4 ASP A 112 MET A 117 1 6
SHEET 1 A 3 GLU A 25 GLU A 32 0
SHEET 2 A 3 LYS A 102 ARG A 109 -1 O PHE A 107 N HIS A 27
SHEET 3 A 3 GLU A 75 ILE A 79 -1 N GLU A 78 O VAL A 106
SHEET 1 B 2 LEU A 40 ALA A 43 0
SHEET 2 B 2 ILE A 53 ILE A 58 -1 O GLY A 57 N SER A 41
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 9 2 Bytes