Header list of 1wjl.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 29-MAY-04 1WJL
TITLE SOLUTION STRUCTURE OF PDZ DOMAIN OF MOUSE CYPHER PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYPHER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ 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: RIKEN CDNA 1110032B18;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031104-22;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, SIGNAL TRANSDUCTION, A STRIATED MUSCLE-SPECIFIC PDZLIM
KEYWDS 2 DOMAIN, LIM DOMAIN BINDING 3, ZASP, Z-BAND ALTERNATIVELY SPLICED
KEYWDS 3 PDZ-MOTIF PROTEIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WJL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WJL 1 VERSN
REVDAT 1 29-NOV-04 1WJL 0
JRNL AUTH M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF PDZ DOMAIN OF MOUSE CYPHER PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJL 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_1000023645.
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 : 1.1MM PDZ DOMAIN U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL;
REMARK 210 1MM D-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 : 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, 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 GLY A 27 H MET A 32 1.53
REMARK 500 O ALA A 58 H THR A 86 1.55
REMARK 500 H ILE A 59 O VAL A 62 1.56
REMARK 500 H SER A 51 OD2 ASP A 54 1.57
REMARK 500 H VAL A 57 O THR A 86 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 3 123.03 178.74
REMARK 500 1 MET A 8 104.93 -179.55
REMARK 500 1 SER A 37 -71.91 -49.22
REMARK 500 1 SER A 48 -120.75 -125.03
REMARK 500 1 ASP A 54 156.18 -39.92
REMARK 500 1 ASN A 63 158.51 -46.19
REMARK 500 1 ALA A 79 153.38 -43.74
REMARK 500 1 SER A 80 -89.74 -140.40
REMARK 500 2 SER A 2 104.01 59.65
REMARK 500 2 MET A 8 109.66 -174.24
REMARK 500 2 ILE A 36 96.93 -65.83
REMARK 500 2 SER A 37 -71.04 -48.14
REMARK 500 2 SER A 43 173.26 -48.51
REMARK 500 2 SER A 48 -134.37 -120.67
REMARK 500 2 ASP A 54 157.14 -39.20
REMARK 500 2 ASN A 63 157.00 -42.35
REMARK 500 2 SER A 80 -55.79 -130.99
REMARK 500 3 MET A 8 111.90 -171.17
REMARK 500 3 ILE A 36 89.50 -68.01
REMARK 500 3 SER A 48 -87.39 -116.60
REMARK 500 3 GLN A 49 -37.88 -166.29
REMARK 500 3 ASP A 54 157.02 -39.65
REMARK 500 3 ASN A 63 160.93 -41.50
REMARK 500 3 ALA A 79 154.04 -42.92
REMARK 500 3 SER A 80 -91.22 -135.32
REMARK 500 4 SER A 5 -64.29 -176.24
REMARK 500 4 SER A 6 -166.47 -116.86
REMARK 500 4 MET A 8 117.38 -170.15
REMARK 500 4 LEU A 34 103.27 -59.39
REMARK 500 4 SER A 37 -76.86 -54.58
REMARK 500 4 SER A 48 -106.01 -135.53
REMARK 500 4 GLN A 49 13.94 -142.15
REMARK 500 4 ASP A 54 155.72 -39.77
REMARK 500 4 ASN A 63 156.81 -42.83
REMARK 500 4 THR A 68 -166.09 -77.14
REMARK 500 4 ALA A 79 161.66 -47.88
REMARK 500 4 SER A 80 -80.17 -138.83
REMARK 500 5 SER A 2 113.48 59.96
REMARK 500 5 MET A 8 102.46 -175.50
REMARK 500 5 ILE A 36 98.42 -64.08
REMARK 500 5 SER A 37 -74.87 -51.42
REMARK 500 5 SER A 48 -124.17 -119.20
REMARK 500 5 ASP A 54 156.62 -39.18
REMARK 500 5 ASN A 63 159.94 -41.23
REMARK 500 5 SER A 80 -74.27 -135.93
REMARK 500 6 SER A 2 -58.87 -158.27
REMARK 500 6 SER A 5 77.19 61.91
REMARK 500 6 MET A 8 104.15 -165.19
REMARK 500 6 LEU A 34 102.56 -59.37
REMARK 500 6 SER A 48 -84.28 -126.40
REMARK 500
REMARK 500 THIS ENTRY HAS 195 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007001185.1 RELATED DB: TARGETDB
DBREF 1WJL A 8 90 UNP Q9D130 Q9D130_MOUSE 1 83
SEQADV 1WJL GLY A 1 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL SER A 2 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL SER A 3 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL GLY A 4 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL SER A 5 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL SER A 6 UNP Q9D130 CLONING ARTIFACT
SEQADV 1WJL GLY A 7 UNP Q9D130 CLONING ARTIFACT
SEQRES 1 A 90 GLY SER SER GLY SER SER GLY MET SER TYR SER VAL THR
SEQRES 2 A 90 LEU THR GLY PRO GLY PRO TRP GLY PHE ARG LEU GLN GLY
SEQRES 3 A 90 GLY LYS ASP PHE ASN MET PRO LEU THR ILE SER ARG ILE
SEQRES 4 A 90 THR PRO GLY SER LYS ALA ALA GLN SER GLN LEU SER GLN
SEQRES 5 A 90 GLY ASP LEU VAL VAL ALA ILE ASP GLY VAL ASN THR ASP
SEQRES 6 A 90 THR MET THR HIS LEU GLU ALA GLN ASN LYS ILE LYS SER
SEQRES 7 A 90 ALA SER TYR ASN LEU SER LEU THR LEU GLN LYS SER
HELIX 1 1 SER A 43 SER A 48 5 6
HELIX 2 2 THR A 68 ALA A 79 1 12
SHEET 1 A 3 SER A 9 THR A 15 0
SHEET 2 A 3 ASN A 82 GLN A 88 -1 O LEU A 83 N LEU A 14
SHEET 3 A 3 LEU A 55 ILE A 59 -1 N ALA A 58 O THR A 86
SHEET 1 B 2 PHE A 22 LEU A 24 0
SHEET 2 B 2 ILE A 36 ILE A 39 -1 O ARG A 38 N ARG A 23
CISPEP 1 GLY A 16 PRO A 17 1 -0.06
CISPEP 2 GLY A 18 PRO A 19 1 0.02
CISPEP 3 GLY A 16 PRO A 17 2 -0.02
CISPEP 4 GLY A 18 PRO A 19 2 -0.03
CISPEP 5 GLY A 16 PRO A 17 3 -0.01
CISPEP 6 GLY A 18 PRO A 19 3 0.03
CISPEP 7 GLY A 16 PRO A 17 4 0.02
CISPEP 8 GLY A 18 PRO A 19 4 -0.02
CISPEP 9 GLY A 16 PRO A 17 5 -0.07
CISPEP 10 GLY A 18 PRO A 19 5 0.02
CISPEP 11 GLY A 16 PRO A 17 6 0.04
CISPEP 12 GLY A 18 PRO A 19 6 0.05
CISPEP 13 GLY A 16 PRO A 17 7 0.02
CISPEP 14 GLY A 18 PRO A 19 7 0.03
CISPEP 15 GLY A 16 PRO A 17 8 0.05
CISPEP 16 GLY A 18 PRO A 19 8 0.01
CISPEP 17 GLY A 16 PRO A 17 9 -0.02
CISPEP 18 GLY A 18 PRO A 19 9 -0.04
CISPEP 19 GLY A 16 PRO A 17 10 -0.01
CISPEP 20 GLY A 18 PRO A 19 10 0.04
CISPEP 21 GLY A 16 PRO A 17 11 0.05
CISPEP 22 GLY A 18 PRO A 19 11 -0.01
CISPEP 23 GLY A 16 PRO A 17 12 -0.01
CISPEP 24 GLY A 18 PRO A 19 12 0.05
CISPEP 25 GLY A 16 PRO A 17 13 0.00
CISPEP 26 GLY A 18 PRO A 19 13 -0.02
CISPEP 27 GLY A 16 PRO A 17 14 0.07
CISPEP 28 GLY A 18 PRO A 19 14 0.03
CISPEP 29 GLY A 16 PRO A 17 15 -0.01
CISPEP 30 GLY A 18 PRO A 19 15 -0.02
CISPEP 31 GLY A 16 PRO A 17 16 0.03
CISPEP 32 GLY A 18 PRO A 19 16 -0.07
CISPEP 33 GLY A 16 PRO A 17 17 -0.01
CISPEP 34 GLY A 18 PRO A 19 17 0.06
CISPEP 35 GLY A 16 PRO A 17 18 0.03
CISPEP 36 GLY A 18 PRO A 19 18 -0.09
CISPEP 37 GLY A 16 PRO A 17 19 0.02
CISPEP 38 GLY A 18 PRO A 19 19 0.00
CISPEP 39 GLY A 16 PRO A 17 20 0.00
CISPEP 40 GLY A 18 PRO A 19 20 0.08
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