HEADER CELL ADHESION 19-MAY-03 1UEN
TITLE SOLUTION STRUCTURE OF THE THIRD FIBRONECTIN 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: P021007-38;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS IMMUNOGLOBULIN-LIKE BETA-SANDWICH FOLD, FIBRONECTIN TYPE III, NG-CAM
KEYWDS 2 RELATED CELL ADHESION MOLECULE, STRUCTURAL GENOMICS, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,T.KIGAWA,F.HAYASHI,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 27-DEC-23 1UEN 1 REMARK
REVDAT 3 02-MAR-22 1UEN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UEN 1 VERSN
REVDAT 1 19-NOV-03 1UEN 0
JRNL AUTH K.MIYAMOTO,T.KIGAWA,F.HAYASHI,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD FIBRONECTIN III DOMAIN OF
JRNL TITL 2 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 : VNMR 6.1C, OPALP
REMARK 3 AUTHORS : VARIAN (VNMR), R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3 (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UEN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005738.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
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 PHOSPHATE
REMARK 210 BUFFER NA, 100MM NACL, 1MM D-DTT,
REMARK 210 0.02% NAN3
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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.816, 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, 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: 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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 5 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 18 VAL A 38 CA - CB - CG2 ANGL. DEV. = 16.1 DEGREES
REMARK 500 19 VAL A 38 CA - CB - CG1 ANGL. DEV. = 14.0 DEGREES
REMARK 500 20 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
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 2 -71.48 -153.65
REMARK 500 1 SER A 3 96.95 48.37
REMARK 500 1 SER A 5 176.68 60.42
REMARK 500 1 SER A 6 137.18 62.14
REMARK 500 1 GLU A 11 77.82 73.96
REMARK 500 1 LEU A 13 144.65 38.19
REMARK 500 1 MET A 15 -40.53 -132.91
REMARK 500 1 ASN A 20 66.00 23.65
REMARK 500 1 VAL A 26 -64.70 -99.32
REMARK 500 1 ARG A 44 80.44 50.01
REMARK 500 1 SER A 60 78.94 53.05
REMARK 500 1 SER A 61 -60.48 -18.33
REMARK 500 1 LYS A 62 125.26 67.83
REMARK 500 1 ARG A 63 -89.26 53.69
REMARK 500 1 ARG A 66 106.26 -49.58
REMARK 500 1 SER A 78 44.37 -87.55
REMARK 500 1 LEU A 87 -166.41 -105.02
REMARK 500 1 PRO A 117 -73.49 -64.16
REMARK 500 1 GLU A 118 -41.31 -154.00
REMARK 500 1 SER A 120 135.28 172.71
REMARK 500 1 PRO A 122 46.29 -79.49
REMARK 500 1 SER A 124 -50.26 -151.94
REMARK 500 2 SER A 5 -40.40 -143.81
REMARK 500 2 SER A 6 -177.01 59.21
REMARK 500 2 SER A 9 171.86 62.60
REMARK 500 2 GLU A 11 -83.45 -69.70
REMARK 500 2 MET A 15 -59.37 -126.51
REMARK 500 2 ASN A 20 103.99 -36.09
REMARK 500 2 ARG A 44 -2.09 54.72
REMARK 500 2 LYS A 62 97.79 -48.97
REMARK 500 2 ARG A 65 74.00 57.67
REMARK 500 2 SER A 124 47.20 125.63
REMARK 500 3 SER A 5 157.60 127.16
REMARK 500 3 SER A 9 -40.67 -168.94
REMARK 500 3 LEU A 13 141.18 33.90
REMARK 500 3 ASN A 20 94.55 -21.30
REMARK 500 3 SER A 28 0.93 -64.16
REMARK 500 3 GLN A 58 76.76 51.92
REMARK 500 3 SER A 59 -75.41 -133.96
REMARK 500 3 ARG A 63 67.64 38.40
REMARK 500 3 ARG A 65 177.76 67.61
REMARK 500 3 ARG A 66 57.38 -151.01
REMARK 500 3 SER A 78 34.76 -79.50
REMARK 500 3 LYS A 103 -31.79 -162.78
REMARK 500 4 SER A 5 45.19 -148.51
REMARK 500 4 HIS A 8 -70.53 -133.10
REMARK 500 4 ASN A 20 56.25 30.43
REMARK 500 4 VAL A 26 -78.17 -117.03
REMARK 500 4 ARG A 65 175.16 68.86
REMARK 500 4 ARG A 66 -179.41 53.13
REMARK 500
REMARK 500 THIS ENTRY HAS 224 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 124 GLY A 125 3 143.34
REMARK 500 SER A 124 GLY A 125 4 146.17
REMARK 500 ARG A 63 ASN A 64 5 146.62
REMARK 500 GLY A 19 ASN A 20 6 -147.92
REMARK 500 SER A 109 PRO A 110 6 145.99
REMARK 500 SER A 109 PRO A 110 7 149.98
REMARK 500 SER A 124 GLY A 125 7 -139.24
REMARK 500 SER A 91 HIS A 92 9 148.13
REMARK 500 SER A 124 GLY A 125 11 -140.41
REMARK 500 ARG A 65 ARG A 66 13 149.27
REMARK 500 SER A 2 SER A 3 15 147.75
REMARK 500 SER A 124 GLY A 125 15 -143.80
REMARK 500 SER A 124 GLY A 125 16 140.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 44 0.07 SIDE CHAIN
REMARK 500 1 ARG A 112 0.09 SIDE CHAIN
REMARK 500 2 ARG A 112 0.12 SIDE CHAIN
REMARK 500 3 TYR A 53 0.09 SIDE CHAIN
REMARK 500 4 ARG A 51 0.09 SIDE CHAIN
REMARK 500 6 ARG A 22 0.09 SIDE CHAIN
REMARK 500 6 PHE A 114 0.08 SIDE CHAIN
REMARK 500 7 ARG A 51 0.11 SIDE CHAIN
REMARK 500 8 ARG A 98 0.09 SIDE CHAIN
REMARK 500 9 TYR A 53 0.09 SIDE CHAIN
REMARK 500 9 ARG A 98 0.08 SIDE CHAIN
REMARK 500 10 ARG A 22 0.12 SIDE CHAIN
REMARK 500 11 TYR A 53 0.08 SIDE CHAIN
REMARK 500 12 ARG A 44 0.12 SIDE CHAIN
REMARK 500 13 TYR A 50 0.07 SIDE CHAIN
REMARK 500 13 ARG A 98 0.08 SIDE CHAIN
REMARK 500 14 ARG A 51 0.11 SIDE CHAIN
REMARK 500 14 PHE A 75 0.09 SIDE CHAIN
REMARK 500 15 TYR A 53 0.11 SIDE CHAIN
REMARK 500 15 ARG A 112 0.11 SIDE CHAIN
REMARK 500 16 ARG A 63 0.08 SIDE CHAIN
REMARK 500 16 ARG A 66 0.12 SIDE CHAIN
REMARK 500 17 ARG A 63 0.10 SIDE CHAIN
REMARK 500 17 ARG A 66 0.10 SIDE CHAIN
REMARK 500 17 ARG A 98 0.09 SIDE CHAIN
REMARK 500 19 TYR A 50 0.07 SIDE CHAIN
REMARK 500 19 ARG A 63 0.10 SIDE CHAIN
REMARK 500 19 ARG A 66 0.10 SIDE CHAIN
REMARK 500 20 ARG A 44 0.16 SIDE CHAIN
REMARK 500 20 ARG A 98 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000335.2 RELATED DB: TARGETDB
DBREF 1UEN A 8 119 UNP Q92823 NRCAM_HUMAN 820 931
SEQADV 1UEN GLY A 1 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 2 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 3 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN GLY A 4 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 5 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 6 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN GLY A 7 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 120 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN GLY A 121 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN PRO A 122 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 123 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN SER A 124 UNP Q92823 CLONING ARTIFACT
SEQADV 1UEN GLY A 125 UNP Q92823 CLONING ARTIFACT
SEQRES 1 A 125 GLY SER SER GLY SER SER GLY HIS SER GLY GLU ASP LEU
SEQRES 2 A 125 PRO MET VAL ALA PRO GLY ASN VAL ARG VAL ASN VAL VAL
SEQRES 3 A 125 ASN SER THR LEU ALA GLU VAL HIS TRP ASP PRO VAL PRO
SEQRES 4 A 125 LEU LYS SER ILE ARG GLY HIS LEU GLN GLY TYR ARG ILE
SEQRES 5 A 125 TYR TYR TRP LYS THR GLN SER SER SER LYS ARG ASN ARG
SEQRES 6 A 125 ARG HIS ILE GLU LYS LYS ILE LEU THR PHE GLN GLY SER
SEQRES 7 A 125 LYS THR HIS GLY MET LEU PRO GLY LEU GLU PRO PHE SER
SEQRES 8 A 125 HIS TYR THR LEU ASN VAL ARG VAL VAL ASN GLY LYS GLY
SEQRES 9 A 125 GLU GLY PRO ALA SER PRO ASP ARG VAL PHE ASN THR PRO
SEQRES 10 A 125 GLU GLY SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 40 ILE A 43 1 4
SHEET 1 A 3 ARG A 22 ASN A 27 0
SHEET 2 A 3 LEU A 30 HIS A 34 -1 O LEU A 30 N ASN A 27
SHEET 3 A 3 LEU A 47 THR A 57 -1 O GLY A 82 N VAL A 33
SHEET 1 B 5 LYS A 70 GLN A 76 0
SHEET 2 B 5 HIS A 81 PRO A 85 -1 N TYR A 50 O PHE A 75
SHEET 3 B 5 HIS A 92 ASN A 101 -1 O HIS A 92 N THR A 57
SHEET 4 B 5 GLU A 105 ALA A 108 -1 N GLY A 106 O VAL A 99
SHEET 5 B 5 ARG A 112 ASN A 115 -1 N ARG A 112 O LEU A 95
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
