HEADER CELL ADHESION 22-MAY-03 1UEY
TITLE SOLUTION STRUCTURE OF THE FIRST FIBRONECTIN TYPE III DOMAIN OF HUMAN
TITLE 2 KIAA0343 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA0343 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIBRONECTIN TYPE III 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 HG01457;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021007-30;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS IMMUNOGLOBULIN-LIKE BETA-SANDWICH FOLD, NG-CAM RELATED CELL ADHESION
KEYWDS 2 MOLECULE, FIBRONECTIN TYPE III DOMAIN, STRUCTURAL GENOMICS, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ZHAO,T.KIGAWA,Y.MUTO,S.KOSHIBA,N.TOCHIO,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 27-DEC-23 1UEY 1 REMARK
REVDAT 3 02-MAR-22 1UEY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UEY 1 VERSN
REVDAT 1 22-NOV-03 1UEY 0
JRNL AUTH C.ZHAO,T.KIGAWA,Y.MUTO,S.KOSHIBA,N.TOCHIO,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST FIBRONECTIN TYPE III DOMAIN
JRNL TITL 2 OF HUMAN KIAA0343 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 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UEY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005749.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM FIBRONECTIN TYPE III
REMARK 210 DOMAIN U-15N, 13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA (PH6.0);
REMARK 210 100MM NACL; 0.02% NAN3; 90% H2O,
REMARK 210 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 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.811, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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, STRUCTURES
REMARK 210 WITH THE LOWEST TARGET 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: 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 O VAL A 33 H LEU A 79 1.54
REMARK 500 O ASN A 43 H SER A 45 1.55
REMARK 500 O ILE A 51 H MET A 92 1.56
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 6 167.04 63.97
REMARK 500 1 THR A 9 123.94 -175.30
REMARK 500 1 TYR A 14 -165.62 -117.42
REMARK 500 1 ASP A 15 54.01 157.24
REMARK 500 1 VAL A 16 161.80 49.68
REMARK 500 1 ASN A 18 160.80 -45.99
REMARK 500 1 GLN A 28 40.99 175.15
REMARK 500 1 LEU A 29 -75.59 -110.61
REMARK 500 1 ASP A 30 -71.40 171.47
REMARK 500 1 LYS A 31 56.25 -119.43
REMARK 500 1 SER A 32 105.22 -178.15
REMARK 500 1 ASN A 43 67.97 61.00
REMARK 500 1 ASN A 44 -61.61 66.86
REMARK 500 1 HIS A 59 -68.12 -127.46
REMARK 500 1 GLN A 67 -77.87 -93.89
REMARK 500 1 THR A 75 14.76 -142.37
REMARK 500 1 TYR A 87 170.97 178.25
REMARK 500 1 ILE A 97 -77.33 -63.71
REMARK 500 1 SER A 103 152.74 -49.56
REMARK 500 1 GLU A 104 -78.06 -35.53
REMARK 500 1 ALA A 105 104.67 161.87
REMARK 500 1 SER A 114 45.36 -85.80
REMARK 500 1 GLU A 115 139.73 175.81
REMARK 500 1 PRO A 116 -164.26 -75.01
REMARK 500 1 ASP A 117 130.17 73.34
REMARK 500 1 LYS A 118 -91.42 -43.72
REMARK 500 1 SER A 126 87.39 61.13
REMARK 500 2 SER A 5 99.73 -167.65
REMARK 500 2 PRO A 12 -167.10 -75.01
REMARK 500 2 ASP A 15 51.88 158.37
REMARK 500 2 VAL A 16 162.19 49.96
REMARK 500 2 ASN A 18 164.46 -45.73
REMARK 500 2 GLN A 28 -46.79 -145.12
REMARK 500 2 LYS A 31 -52.45 173.00
REMARK 500 2 ASN A 43 68.41 60.79
REMARK 500 2 ASN A 44 -62.19 66.66
REMARK 500 2 HIS A 59 -74.96 -129.83
REMARK 500 2 GLN A 67 -73.34 -104.35
REMARK 500 2 TYR A 84 50.24 71.95
REMARK 500 2 ILE A 97 -82.69 -58.20
REMARK 500 2 GLU A 104 -76.81 -37.06
REMARK 500 2 ALA A 105 101.40 161.77
REMARK 500 2 GLU A 107 150.25 -49.67
REMARK 500 2 ASP A 117 163.25 -42.49
REMARK 500 2 ASN A 119 107.56 72.36
REMARK 500 2 SER A 126 90.35 54.65
REMARK 500 3 PRO A 12 -168.64 -75.00
REMARK 500 3 ASP A 15 52.77 161.37
REMARK 500 3 VAL A 16 162.08 50.03
REMARK 500 3 ASN A 18 163.27 -44.78
REMARK 500
REMARK 500 THIS ENTRY HAS 509 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000335.1 RELATED DB: TARGETDB
DBREF 1UEY A 8 121 UNP Q92823 NRCAM_HUMAN 619 732
SEQADV 1UEY GLY A 1 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 2 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 3 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY GLY A 4 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 5 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 6 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY GLY A 7 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 122 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY GLY A 123 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY PRO A 124 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 125 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY SER A 126 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEY GLY A 127 UNP Q92823 CLONING ARTIFACT
SEQRES 1 A 127 GLY SER SER GLY SER SER GLY PRO THR PRO ALA PRO VAL
SEQRES 2 A 127 TYR ASP VAL PRO ASN PRO PRO PHE ASP LEU GLU LEU THR
SEQRES 3 A 127 ASP GLN LEU ASP LYS SER VAL GLN LEU SER TRP THR PRO
SEQRES 4 A 127 GLY ASP ASP ASN ASN SER PRO ILE THR LYS PHE ILE ILE
SEQRES 5 A 127 GLU TYR GLU ASP ALA MET HIS LYS PRO GLY LEU TRP HIS
SEQRES 6 A 127 HIS GLN THR GLU VAL SER GLY THR GLN THR THR ALA GLN
SEQRES 7 A 127 LEU ASN LEU SER PRO TYR VAL ASN TYR SER PHE ARG VAL
SEQRES 8 A 127 MET ALA VAL ASN SER ILE GLY LYS SER LEU PRO SER GLU
SEQRES 9 A 127 ALA SER GLU GLN TYR LEU THR LYS ALA SER GLU PRO ASP
SEQRES 10 A 127 LYS ASN PRO THR SER GLY PRO SER SER GLY
SHEET 1 A 3 PHE A 21 THR A 26 0
SHEET 2 A 3 VAL A 33 THR A 38 -1 O SER A 36 N GLU A 24
SHEET 3 A 3 THR A 76 LEU A 79 -1 O LEU A 79 N VAL A 33
SHEET 1 B 3 TRP A 64 SER A 71 0
SHEET 2 B 3 ILE A 47 GLU A 55 -1 N PHE A 50 O VAL A 70
SHEET 3 B 3 SER A 88 ASN A 95 -1 O MET A 92 N ILE A 51
SHEET 1 C 2 ASN A 86 TYR A 87 0
SHEET 2 C 2 TYR A 109 LEU A 110 -1 O TYR A 109 N TYR A 87
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
(ATOM LINES ARE NOT SHOWN.)
END
