Header list of 1wj5.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WJ5
TITLE SOLUTION STRUCTURE OF THE HYPOTHETICAL DOMAIN OF RIKEN CDNA 0610009H20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN (RIKEN CDNA 0610009H20);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HYPOTHETICAL DOMAIN;
COMPND 5 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: FANTOM 2 CDNA 0610009H20;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030811-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS WINGED HELIX, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.HATTA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WJ5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WJ5 1 VERSN
REVDAT 1 28-NOV-04 1WJ5 0
JRNL AUTH R.HATTA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE HYPOTHETICAL DOMAIN OF RIKEN CDNA
JRNL TITL 2 0610009H20
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.7
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJ5 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_1000023635.
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 : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.05MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 DTT; 0.02% 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 : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20031121, NMR
REMARK 210 VEIW 5.0.4, KUJIRA 0.872, CYANA
REMARK 210 1.0.7
REMARK 210 METHOD USED : NULL
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 ASP A 13 H LEU A 17 1.53
REMARK 500 O LEU A 48 H LEU A 51 1.54
REMARK 500 O LEU A 92 H THR A 107 1.58
REMARK 500 O GLU A 46 H SER A 50 1.59
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 2 170.42 64.51
REMARK 500 1 SER A 5 -59.64 -149.75
REMARK 500 1 SER A 6 106.12 69.14
REMARK 500 1 ASN A 8 -58.65 -160.06
REMARK 500 1 LYS A 9 77.61 -151.01
REMARK 500 1 LEU A 12 177.31 51.76
REMARK 500 1 SER A 19 -38.14 -37.83
REMARK 500 1 PHE A 37 -176.67 -175.76
REMARK 500 1 ARG A 54 158.91 -44.95
REMARK 500 1 VAL A 56 -142.13 -153.43
REMARK 500 1 THR A 57 46.09 -108.76
REMARK 500 1 SER A 59 57.08 -175.23
REMARK 500 1 SER A 62 -179.28 54.75
REMARK 500 1 LYS A 68 73.54 -114.14
REMARK 500 1 ASP A 69 -165.48 -179.16
REMARK 500 1 SER A 70 -74.39 -142.94
REMARK 500 1 SER A 73 -54.82 -175.62
REMARK 500 1 THR A 108 45.41 36.02
REMARK 500 1 LYS A 109 84.25 42.51
REMARK 500 1 ASP A 110 164.24 179.77
REMARK 500 1 LYS A 111 163.45 -45.10
REMARK 500 1 SER A 118 114.07 60.01
REMARK 500 2 SER A 6 -60.37 -178.28
REMARK 500 2 ASN A 8 123.26 175.18
REMARK 500 2 LYS A 9 60.27 -118.85
REMARK 500 2 ASP A 10 114.23 -161.77
REMARK 500 2 SER A 19 -39.72 -36.90
REMARK 500 2 ARG A 54 158.34 -47.32
REMARK 500 2 VAL A 56 -142.43 -151.74
REMARK 500 2 SER A 59 -51.14 -168.23
REMARK 500 2 LEU A 67 137.90 66.23
REMARK 500 2 LYS A 68 -66.78 163.72
REMARK 500 2 ASP A 97 -24.71 155.63
REMARK 500 2 SER A 98 147.81 63.66
REMARK 500 2 THR A 107 -165.40 -103.93
REMARK 500 2 THR A 108 -156.92 37.99
REMARK 500 2 ASP A 110 91.68 58.52
REMARK 500 2 LYS A 111 72.61 31.19
REMARK 500 2 LEU A 113 155.86 -45.74
REMARK 500 2 GLN A 114 -174.44 -174.12
REMARK 500 2 SER A 115 75.71 -101.39
REMARK 500 2 SER A 119 -59.29 -176.51
REMARK 500 3 SER A 5 97.59 -163.27
REMARK 500 3 SER A 6 171.77 59.43
REMARK 500 3 ASN A 8 105.58 60.80
REMARK 500 3 LYS A 9 105.68 65.87
REMARK 500 3 SER A 19 -33.09 -36.80
REMARK 500 3 SER A 47 -31.70 -38.09
REMARK 500 3 ARG A 54 158.35 -44.98
REMARK 500 3 VAL A 56 150.81 166.77
REMARK 500
REMARK 500 THIS ENTRY HAS 459 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007119179.1 RELATED DB: TARGETDB
DBREF 1WJ5 A 8 114 UNP Q8K2X3 OBFC1_MOUSE 205 311
SEQADV 1WJ5 GLY A 1 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 2 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 3 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 GLY A 4 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 5 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 6 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 GLY A 7 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 115 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 GLY A 116 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 PRO A 117 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 118 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 SER A 119 UNP Q8K2X3 CLONING ARTIFACT
SEQADV 1WJ5 GLY A 120 UNP Q8K2X3 CLONING ARTIFACT
SEQRES 1 A 120 GLY SER SER GLY SER SER GLY ASN LYS ASP ASN LEU ASP
SEQRES 2 A 120 LEU ALA GLY LEU THR SER LEU LEU SER GLU LYS ILE LYS
SEQRES 3 A 120 GLU PHE LEU GLN GLU LYS LYS MET GLN SER PHE TYR GLN
SEQRES 4 A 120 GLN GLU LEU GLU THR VAL GLU SER LEU GLN SER LEU ALA
SEQRES 5 A 120 SER ARG PRO VAL THR HIS SER THR GLY SER ASP GLN VAL
SEQRES 6 A 120 GLU LEU LYS ASP SER GLY THR SER GLY VAL ALA GLN ARG
SEQRES 7 A 120 VAL PHE LYS ASN ALA LEU GLN LEU LEU GLN GLU LYS GLY
SEQRES 8 A 120 LEU VAL PHE GLN ARG ASP SER GLY SER ASP LYS LEU TYR
SEQRES 9 A 120 TYR VAL THR THR LYS ASP LYS ASP LEU GLN SER GLY PRO
SEQRES 10 A 120 SER SER GLY
HELIX 1 1 ASP A 13 LYS A 33 1 21
HELIX 2 2 TYR A 38 THR A 44 1 7
HELIX 3 3 VAL A 45 SER A 53 1 9
HELIX 4 4 SER A 73 GLY A 91 1 19
SHEET 1 A 3 SER A 36 PHE A 37 0
SHEET 2 A 3 TYR A 105 VAL A 106 -1 O TYR A 104 N PHE A 37
SHEET 3 A 3 VAL A 93 PHE A 94 -1 O TYR A 105 N PHE A 94
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