HEADER CELL ADHESION 26-MAY-04 1WFN
TITLE THE FOURTH FN3 DOMAIN OF HUMAN SIDEKICK-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIDEKICK 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FN3 DOMAIN;
COMPND 5 SYNONYM: DROSOPHILA SIDEKICK-LIKE, CHICKEN SIDEKICK 2-LIKE;
COMPND 6 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 FH00815;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-46;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SIDEKICK-2, FN3, CELL ADHESION, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WFN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WFN 1 VERSN
REVDAT 1 07-JUN-05 1WFN 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL THE FOURTH FN3 DOMAIN OF HUMAN SIDEKICK-2
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 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023526.
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 : 1.21MM 13C/15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS, 100MM NACL, 1MM D-
REMARK 210 DTT, 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 : 900 MHZ; 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 0.8992, CYANA 1.0.7
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: 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 GLU A 56 H THR A 88 1.47
REMARK 500 O TYR A 87 H ILE A 107 1.50
REMARK 500 O GLY A 50 H MET A 94 1.50
REMARK 500 O THR A 82 HG SER A 109 1.53
REMARK 500 H THR A 49 O MET A 94 1.54
REMARK 500 O LEU A 34 H VAL A 78 1.54
REMARK 500 O ARG A 52 H ALA A 92 1.55
REMARK 500 O SER A 25 H SER A 37 1.57
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 5 107.64 -178.97
REMARK 500 1 SER A 6 162.16 60.40
REMARK 500 1 GLN A 9 71.42 -116.15
REMARK 500 1 THR A 13 -168.20 46.08
REMARK 500 1 VAL A 17 164.87 -42.70
REMARK 500 1 VAL A 21 171.37 -56.47
REMARK 500 1 LEU A 30 -138.93 -132.67
REMARK 500 1 THR A 32 28.53 -150.17
REMARK 500 1 LYS A 44 -35.98 -39.97
REMARK 500 1 ASN A 45 54.19 39.45
REMARK 500 1 GLU A 57 -179.58 -50.12
REMARK 500 1 LEU A 81 -157.99 -93.22
REMARK 500 1 THR A 95 -168.41 -119.63
REMARK 500 1 GLN A 101 169.41 -45.15
REMARK 500 1 SER A 109 146.86 -35.22
REMARK 500 1 SER A 114 77.28 38.77
REMARK 500 1 SER A 117 -63.63 71.21
REMARK 500 1 SER A 118 -58.07 -171.56
REMARK 500 2 SER A 5 164.46 57.99
REMARK 500 2 GLN A 9 94.37 52.85
REMARK 500 2 ARG A 12 148.49 -39.55
REMARK 500 2 HIS A 14 85.13 -164.49
REMARK 500 2 GLU A 28 48.74 39.72
REMARK 500 2 LEU A 30 -142.11 -120.26
REMARK 500 2 THR A 32 26.54 -150.69
REMARK 500 2 GLU A 57 174.26 -48.12
REMARK 500 2 ARG A 60 84.93 -152.81
REMARK 500 2 LEU A 81 -147.78 -92.94
REMARK 500 2 LEU A 84 60.55 37.94
REMARK 500 2 THR A 95 -167.65 -120.22
REMARK 500 2 GLN A 101 176.42 -49.07
REMARK 500 2 SER A 109 -131.42 19.88
REMARK 500 2 VAL A 111 140.77 -179.21
REMARK 500 2 SER A 118 138.99 63.52
REMARK 500 3 GLU A 15 149.27 -173.50
REMARK 500 3 VAL A 17 165.32 -43.48
REMARK 500 3 VAL A 21 -173.20 -56.22
REMARK 500 3 GLU A 28 56.06 39.74
REMARK 500 3 LEU A 30 -121.94 -115.00
REMARK 500 3 THR A 32 17.61 -145.65
REMARK 500 3 LYS A 44 -34.74 -39.94
REMARK 500 3 ASN A 45 43.23 39.60
REMARK 500 3 GLU A 57 173.62 -46.47
REMARK 500 3 LEU A 81 -140.54 -82.32
REMARK 500 3 THR A 95 -162.94 -120.88
REMARK 500 3 GLN A 101 176.83 -48.40
REMARK 500 3 SER A 109 146.23 -38.54
REMARK 500 3 VAL A 111 141.87 -176.47
REMARK 500 3 SER A 114 74.78 39.39
REMARK 500 4 SER A 6 154.89 66.91
REMARK 500
REMARK 500 THIS ENTRY HAS 357 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101486.1 RELATED DB: TARGETDB
DBREF 1WFN A 8 113 UNP Q58EX2 Q58EX2_HUMAN 509 614
SEQADV 1WFN GLY A 1 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 2 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 3 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN GLY A 4 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 5 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 6 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN GLY A 7 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 114 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN GLY A 115 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN PRO A 116 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 117 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN SER A 118 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFN GLY A 119 UNP Q58EX2 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY PRO GLN LEU VAL ARG THR
SEQRES 2 A 119 HIS GLU ASP VAL PRO GLY PRO VAL GLY HIS LEU SER PHE
SEQRES 3 A 119 SER GLU ILE LEU ASP THR SER LEU LYS VAL SER TRP GLN
SEQRES 4 A 119 GLU PRO GLY GLU LYS ASN GLY ILE LEU THR GLY TYR ARG
SEQRES 5 A 119 ILE SER TRP GLU GLU TYR ASN ARG THR ASN THR ARG VAL
SEQRES 6 A 119 THR HIS TYR LEU PRO ASN VAL THR LEU GLU TYR ARG VAL
SEQRES 7 A 119 THR GLY LEU THR ALA LEU THR THR TYR THR ILE GLU VAL
SEQRES 8 A 119 ALA ALA MET THR SER LYS GLY GLN GLY GLN VAL SER ALA
SEQRES 9 A 119 SER THR ILE SER SER GLY VAL PRO PRO SER GLY PRO SER
SEQRES 10 A 119 SER GLY
HELIX 1 1 ARG A 60 ARG A 64 5 5
SHEET 1 A 3 SER A 25 SER A 27 0
SHEET 2 A 3 SER A 33 SER A 37 -1 O SER A 37 N SER A 25
SHEET 3 A 3 GLU A 75 THR A 79 -1 O VAL A 78 N LEU A 34
SHEET 1 B 4 HIS A 67 LEU A 69 0
SHEET 2 B 4 GLY A 50 GLU A 57 -1 N TYR A 51 O LEU A 69
SHEET 3 B 4 THR A 86 MET A 94 -1 O THR A 88 N GLU A 56
SHEET 4 B 4 GLN A 99 SER A 108 -1 O ILE A 107 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
