Header list of 1wfo.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 26-MAY-04 1WFO
TITLE THE EIGHTH 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: P040223-52;
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 1WFO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WFO 1 VERSN
REVDAT 1 07-JUN-05 1WFO 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL THE EIGHTH 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 1WFO 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_1000023527.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 220MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.00MM 13C/15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS, 200MM 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 : 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 H LEU A 59 O GLN A 105 1.47
REMARK 500 H PHE A 100 O ALA A 116 1.49
REMARK 500 O TYR A 61 H LEU A 80 1.60
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 2 168.51 177.91
REMARK 500 1 SER A 3 170.39 178.28
REMARK 500 1 ASP A 11 166.03 177.23
REMARK 500 1 SER A 13 91.11 -175.26
REMARK 500 1 ASP A 26 147.28 -178.04
REMARK 500 1 ARG A 40 -163.76 -108.34
REMARK 500 1 THR A 41 -77.06 -70.46
REMARK 500 1 SER A 43 113.10 -168.95
REMARK 500 1 ALA A 60 -174.10 174.65
REMARK 500 1 THR A 70 -163.77 -176.46
REMARK 500 1 ALA A 72 -168.37 162.20
REMARK 500 1 THR A 106 -168.28 -123.60
REMARK 500 1 GLU A 112 161.42 -48.90
REMARK 500 1 SER A 128 106.61 55.62
REMARK 500 1 SER A 129 151.08 179.77
REMARK 500 2 SER A 5 134.74 -170.83
REMARK 500 2 SER A 6 145.66 -172.09
REMARK 500 2 ARG A 8 146.31 60.52
REMARK 500 2 SER A 13 77.84 -156.71
REMARK 500 2 ARG A 22 98.36 50.31
REMARK 500 2 ASP A 26 154.28 177.27
REMARK 500 2 VAL A 27 158.23 -40.58
REMARK 500 2 ARG A 40 -164.51 -119.12
REMARK 500 2 THR A 41 -86.28 -70.42
REMARK 500 2 ARG A 45 108.74 -161.37
REMARK 500 2 ALA A 60 -170.73 175.62
REMARK 500 2 LEU A 67 130.37 -38.58
REMARK 500 2 THR A 69 108.64 -176.08
REMARK 500 2 THR A 70 -171.49 -175.71
REMARK 500 2 THR A 106 -168.27 -123.96
REMARK 500 2 ARG A 124 108.17 57.13
REMARK 500 2 SER A 128 95.80 51.58
REMARK 500 3 SER A 2 167.46 179.09
REMARK 500 3 ARG A 8 131.33 -173.45
REMARK 500 3 SER A 15 154.85 63.19
REMARK 500 3 HIS A 16 145.29 -174.18
REMARK 500 3 LEU A 20 110.28 -162.84
REMARK 500 3 ARG A 22 84.85 42.24
REMARK 500 3 VAL A 27 159.49 -43.40
REMARK 500 3 ARG A 40 -165.81 -106.70
REMARK 500 3 THR A 41 -74.94 -78.54
REMARK 500 3 ALA A 60 -170.14 174.51
REMARK 500 3 ASN A 68 -36.19 -39.73
REMARK 500 3 THR A 70 -164.13 -175.85
REMARK 500 3 THR A 106 -168.71 -123.46
REMARK 500 3 GLU A 112 164.39 -47.23
REMARK 500 3 SER A 129 105.82 56.56
REMARK 500 4 SER A 2 94.30 -176.80
REMARK 500 4 SER A 6 92.78 178.92
REMARK 500 4 LEU A 20 110.84 -178.84
REMARK 500
REMARK 500 THIS ENTRY HAS 342 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101486.2 RELATED DB: TARGETDB
DBREF 1WFO A 8 124 UNP Q58EX2 Q58EX2_HUMAN 905 1021
SEQADV 1WFO GLY A 1 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 2 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 3 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO GLY A 4 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 5 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 6 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO GLY A 7 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 125 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO GLY A 126 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO PRO A 127 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 128 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO SER A 129 UNP Q58EX2 CLONING ARTIFACT
SEQADV 1WFO GLY A 130 UNP Q58EX2 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY ARG ILE GLY ASP GLY SER
SEQRES 2 A 130 PRO SER HIS PRO PRO ILE LEU GLU ARG THR LEU ASP ASP
SEQRES 3 A 130 VAL PRO GLY PRO PRO MET GLY ILE LEU PHE PRO GLU VAL
SEQRES 4 A 130 ARG THR THR SER VAL ARG LEU ILE TRP GLN PRO PRO ALA
SEQRES 5 A 130 ALA PRO ASN GLY ILE ILE LEU ALA TYR GLN ILE THR HIS
SEQRES 6 A 130 ARG LEU ASN THR THR THR ALA ASN THR ALA THR VAL GLU
SEQRES 7 A 130 VAL LEU ALA PRO SER ALA ARG GLN TYR THR ALA THR GLY
SEQRES 8 A 130 LEU LYS PRO GLU SER VAL TYR LEU PHE ARG ILE THR ALA
SEQRES 9 A 130 GLN THR ARG LYS GLY TRP GLY GLU ALA ALA GLU ALA LEU
SEQRES 10 A 130 VAL VAL THR THR GLU LYS ARG SER GLY PRO SER SER GLY
SHEET 1 A 3 LEU A 35 VAL A 39 0
SHEET 2 A 3 SER A 43 ILE A 47 -1 O ARG A 45 N GLU A 38
SHEET 3 A 3 GLN A 86 THR A 90 -1 O ALA A 89 N VAL A 44
SHEET 1 B 4 VAL A 77 LEU A 80 0
SHEET 2 B 4 ALA A 60 LEU A 67 -1 N ILE A 63 O GLU A 78
SHEET 3 B 4 VAL A 97 GLN A 105 -1 O GLN A 105 N ALA A 60
SHEET 4 B 4 TRP A 110 VAL A 119 -1 O ALA A 116 N PHE A 100
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