Header list of 1wik.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 28-MAY-04 1WIK
TITLE SOLUTION STRUCTURE OF THE PICOT HOMOLOGY 2 DOMAIN OF THE MOUSE PKC-
TITLE 2 INTERACTING COUSIN OF THIOREDOXIN PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN-LIKE PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PICOT HOMOLOGY 2 DOMAIN;
COMPND 5 SYNONYM: PKC-INTERACTING COUSIN OF THIOREDOXIN, PKC-THETA-INTERACTING
COMPND 6 PROTEIN, PKCQ-INTERACTING PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 2410003E11;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030421-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PICOT HOMOLOGY 2 DOMAIN, PICOT PROTEIN, THIOREDOXIN LIKE 2,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WIK 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WIK 1 VERSN
REVDAT 1 28-NOV-04 1WIK 0
JRNL AUTH K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PICOT HOMOLOGY 2 DOMAIN OF THE
JRNL TITL 2 MOUSE PKC-INTERACTING COUSIN OF THIOREDOXIN PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WIK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023619.
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 : 0.65MM PICOT HOMOLOGY 2 DOMAIN U
REMARK 210 -13C,15N; 20MM D-TRIS-HCL(PH6.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 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 0.8996, 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, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, 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 38 H SER A 42 1.53
REMARK 500 O LEU A 62 H SER A 66 1.54
REMARK 500 O ILE A 36 H LEU A 40 1.54
REMARK 500 O LYS A 88 H ASP 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 2 98.01 -65.35
REMARK 500 1 SER A 5 86.33 60.91
REMARK 500 1 ASN A 24 171.40 56.00
REMARK 500 1 LYS A 25 -30.79 -38.99
REMARK 500 1 CYS A 30 -42.91 167.20
REMARK 500 1 PHE A 32 -65.16 67.71
REMARK 500 1 GLN A 35 -73.83 -48.18
REMARK 500 1 GLU A 38 -38.91 -38.69
REMARK 500 1 ASN A 67 33.76 74.22
REMARK 500 1 ARG A 77 -70.07 67.05
REMARK 500 1 GLU A 95 49.89 -141.30
REMARK 500 1 SER A 104 145.91 -170.48
REMARK 500 2 SER A 2 97.69 -172.89
REMARK 500 2 SER A 5 -57.61 -169.39
REMARK 500 2 LEU A 8 -65.06 -90.47
REMARK 500 2 ASN A 24 164.82 56.68
REMARK 500 2 CYS A 30 82.56 87.29
REMARK 500 2 PHE A 32 -49.09 -134.54
REMARK 500 2 GLN A 35 -71.92 -44.55
REMARK 500 2 LEU A 53 -68.41 -90.26
REMARK 500 2 ASN A 67 36.84 79.48
REMARK 500 2 THR A 70 98.72 -40.77
REMARK 500 2 GLU A 95 52.07 -142.95
REMARK 500 2 LYS A 101 -86.33 -40.93
REMARK 500 2 SER A 104 78.05 178.82
REMARK 500 3 SER A 2 107.49 61.20
REMARK 500 3 ASN A 24 160.68 59.18
REMARK 500 3 GLU A 27 114.77 -163.48
REMARK 500 3 THR A 43 -39.26 -39.58
REMARK 500 3 VAL A 45 -171.74 -66.28
REMARK 500 3 ARG A 59 -70.10 -61.14
REMARK 500 3 ASN A 67 33.81 73.51
REMARK 500 3 THR A 70 97.82 -49.37
REMARK 500 3 ARG A 77 -39.27 -38.18
REMARK 500 3 LEU A 80 103.31 -47.31
REMARK 500 3 LYS A 101 -75.65 -40.17
REMARK 500 3 SER A 104 87.34 44.71
REMARK 500 3 SER A 107 127.21 -175.59
REMARK 500 4 SER A 2 90.82 62.64
REMARK 500 4 ASN A 24 -175.34 61.57
REMARK 500 4 GLU A 27 -165.22 -121.29
REMARK 500 4 ALA A 28 -36.95 179.60
REMARK 500 4 LYS A 29 -49.58 81.83
REMARK 500 4 CYS A 30 99.54 93.94
REMARK 500 4 PHE A 32 -48.12 -155.60
REMARK 500 4 GLU A 95 49.41 -145.76
REMARK 500 4 LYS A 101 -80.11 -40.03
REMARK 500 4 SER A 104 107.77 68.03
REMARK 500 4 SER A 107 80.52 -171.15
REMARK 500 4 SER A 108 84.81 61.15
REMARK 500
REMARK 500 THIS ENTRY HAS 267 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK001001569.1 RELATED DB: TARGETDB
DBREF 1WIK A 8 103 UNP Q9CQM9 TXNL2_MOUSE 241 336
SEQADV 1WIK GLY A 1 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 2 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 3 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK GLY A 4 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 5 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 6 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK GLY A 7 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 104 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK GLY A 105 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK PRO A 106 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 107 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK SER A 108 UNP Q9CQM9 CLONING ARTIFACT
SEQADV 1WIK GLY A 109 UNP Q9CQM9 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY LEU LYS VAL LEU THR ASN
SEQRES 2 A 109 LYS ALA SER VAL MET LEU PHE MET LYS GLY ASN LYS GLN
SEQRES 3 A 109 GLU ALA LYS CYS GLY PHE SER LYS GLN ILE LEU GLU ILE
SEQRES 4 A 109 LEU ASN SER THR GLY VAL GLU TYR GLU THR PHE ASP ILE
SEQRES 5 A 109 LEU GLU ASP GLU GLU VAL ARG GLN GLY LEU LYS THR PHE
SEQRES 6 A 109 SER ASN TRP PRO THR TYR PRO GLN LEU TYR VAL ARG GLY
SEQRES 7 A 109 ASP LEU VAL GLY GLY LEU ASP ILE VAL LYS GLU LEU LYS
SEQRES 8 A 109 ASP ASN GLY GLU LEU LEU PRO ILE LEU LYS GLY GLU SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 LEU A 8 THR A 12 1 5
HELIX 2 2 SER A 33 SER A 42 1 10
HELIX 3 3 GLU A 56 SER A 66 1 11
HELIX 4 4 LEU A 84 ASN A 93 1 10
HELIX 5 5 LEU A 97 LYS A 101 1 5
SHEET 1 A 4 TYR A 47 ASP A 51 0
SHEET 2 A 4 VAL A 17 MET A 21 1 N VAL A 17 O GLU A 48
SHEET 3 A 4 GLN A 73 TYR A 75 -1 O GLN A 73 N PHE A 20
SHEET 4 A 4 LEU A 80 GLY A 82 -1 O GLY A 82 N LEU A 74
CISPEP 1 TYR A 71 PRO A 72 1 0.03
CISPEP 2 TYR A 71 PRO A 72 2 0.00
CISPEP 3 TYR A 71 PRO A 72 3 -0.01
CISPEP 4 TYR A 71 PRO A 72 4 -0.02
CISPEP 5 TYR A 71 PRO A 72 5 -0.03
CISPEP 6 TYR A 71 PRO A 72 6 -0.05
CISPEP 7 TYR A 71 PRO A 72 7 -0.05
CISPEP 8 TYR A 71 PRO A 72 8 0.00
CISPEP 9 TYR A 71 PRO A 72 9 0.00
CISPEP 10 TYR A 71 PRO A 72 10 -0.11
CISPEP 11 TYR A 71 PRO A 72 11 0.00
CISPEP 12 TYR A 71 PRO A 72 12 -0.07
CISPEP 13 TYR A 71 PRO A 72 13 0.00
CISPEP 14 TYR A 71 PRO A 72 14 0.03
CISPEP 15 TYR A 71 PRO A 72 15 0.01
CISPEP 16 TYR A 71 PRO A 72 16 0.00
CISPEP 17 TYR A 71 PRO A 72 17 -0.10
CISPEP 18 TYR A 71 PRO A 72 18 -0.07
CISPEP 19 TYR A 71 PRO A 72 19 -0.05
CISPEP 20 TYR A 71 PRO A 72 20 0.04
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