Header list of 1v5l.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 25-NOV-03 1V5L
TITLE SOLUTION STRUCTURE OF PDZ DOMAIN OF MOUSE ALPHA-ACTININ-2 ASSOCIATED
TITLE 2 LIM PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PDZ AND LIM DOMAIN 3; ACTININ ALPHA 2 ASSOCIATED LIM
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: PDZ DOMAIN;
COMPND 6 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 6720456D19;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030506-95;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, CYTOSKELETON, ACTIN BINDING, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V5L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V5L 1 VERSN
REVDAT 1 25-MAY-04 1V5L 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF PDZ DOMAIN OF MOUSE ALPHA-ACTININ-2
JRNL TITL 2 ASSOCIATED LIM 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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V5L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006234.
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;
REMARK 210 20MM PHOSPHATE BUFFER NA; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 920 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : ECA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : JEOL; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DELTA 4.2, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.853,
REMARK 210 CYANA 2.0.17
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: 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 PRO A 14 -170.78 -69.77
REMARK 500 1 ALA A 42 -71.40 -74.76
REMARK 500 1 THR A 61 44.25 -101.73
REMARK 500 1 ALA A 76 -175.07 -67.96
REMARK 500 1 ALA A 87 76.96 -117.92
REMARK 500 1 THR A 89 39.62 -81.58
REMARK 500 1 ARG A 90 47.56 -77.59
REMARK 500 1 VAL A 96 142.52 -171.78
REMARK 500 1 SER A 97 107.31 -35.24
REMARK 500 1 SER A 101 115.03 -172.95
REMARK 500 2 SER A 2 173.10 -57.35
REMARK 500 2 SER A 5 78.47 -101.24
REMARK 500 2 PRO A 14 -175.31 -69.80
REMARK 500 2 LEU A 31 97.48 -68.39
REMARK 500 2 ALA A 42 -71.99 -74.23
REMARK 500 2 PRO A 49 98.21 -69.70
REMARK 500 2 THR A 61 39.83 -93.06
REMARK 500 2 ALA A 76 -178.69 -53.29
REMARK 500 2 ASP A 85 35.17 -94.90
REMARK 500 2 ARG A 86 32.93 36.23
REMARK 500 2 TRP A 92 107.42 -165.32
REMARK 500 2 PRO A 94 -169.84 -69.68
REMARK 500 2 GLN A 95 50.02 -106.72
REMARK 500 3 SER A 6 129.60 -173.07
REMARK 500 3 PRO A 14 -179.48 -69.77
REMARK 500 3 PRO A 16 -179.88 -69.80
REMARK 500 3 PRO A 38 92.16 -69.76
REMARK 500 3 ALA A 42 -73.14 -74.79
REMARK 500 3 THR A 61 38.41 -87.67
REMARK 500 3 ALA A 76 -176.29 -56.83
REMARK 500 3 TYR A 78 -29.05 -39.31
REMARK 500 3 LEU A 91 -71.55 -112.85
REMARK 500 3 SER A 93 142.56 -174.39
REMARK 500 3 PRO A 94 -165.32 -69.73
REMARK 500 4 PRO A 14 -172.30 -69.81
REMARK 500 4 ALA A 42 -72.92 -82.55
REMARK 500 4 PRO A 49 96.96 -69.75
REMARK 500 4 ASP A 57 32.31 39.77
REMARK 500 4 THR A 61 35.09 -89.20
REMARK 500 4 ALA A 76 -174.62 -54.12
REMARK 500 4 TYR A 78 -27.91 -38.43
REMARK 500 4 ALA A 87 105.43 -48.00
REMARK 500 4 PRO A 94 -168.49 -69.77
REMARK 500 4 SER A 98 52.85 34.37
REMARK 500 4 SER A 101 153.96 -48.96
REMARK 500 5 PRO A 14 -171.98 -69.84
REMARK 500 5 ALA A 42 -73.36 -80.41
REMARK 500 5 PRO A 49 99.18 -69.75
REMARK 500 5 THR A 61 34.95 -83.73
REMARK 500 5 ALA A 76 -179.04 -52.95
REMARK 500
REMARK 500 THIS ENTRY HAS 221 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007020726.1 RELATED DB: TARGETDB
DBREF 1V5L A 8 97 GB 7948997 NP_058078 4 93
SEQADV 1V5L GLY A 1 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 2 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 3 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L GLY A 4 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 5 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 6 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L GLY A 7 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 98 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L GLY A 99 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L PRO A 100 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 101 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L SER A 102 GB 7948997 CLONING ARTIFACT
SEQADV 1V5L GLY A 103 GB 7948997 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY ASN VAL VAL LEU PRO GLY
SEQRES 2 A 103 PRO ALA PRO TRP GLY PHE ARG LEU SER GLY GLY ILE ASP
SEQRES 3 A 103 PHE ASN GLN PRO LEU VAL ILE THR ARG ILE THR PRO GLY
SEQRES 4 A 103 SER LYS ALA ALA ALA ALA ASN LEU CYS PRO GLY ASP VAL
SEQRES 5 A 103 ILE LEU ALA ILE ASP GLY PHE GLY THR GLU SER MET THR
SEQRES 6 A 103 HIS ALA ASP ALA GLN ASP ARG ILE LYS ALA ALA SER TYR
SEQRES 7 A 103 GLN LEU CYS LEU LYS ILE ASP ARG ALA GLU THR ARG LEU
SEQRES 8 A 103 TRP SER PRO GLN VAL SER SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 42 ASN A 46 5 5
HELIX 2 2 THR A 65 LYS A 74 1 10
SHEET 1 A 2 VAL A 10 PRO A 12 0
SHEET 2 A 2 GLN A 79 CYS A 81 -1 O LEU A 80 N LEU A 11
SHEET 1 B 2 SER A 22 GLY A 24 0
SHEET 2 B 2 GLN A 29 VAL A 32 -1 O GLN A 29 N GLY A 24
SHEET 1 C 3 PHE A 59 GLY A 60 0
SHEET 2 C 3 ILE A 53 ILE A 56 -1 N ILE A 56 O PHE A 59
SHEET 3 C 3 LYS A 83 ILE A 84 -1 O LYS A 83 N ALA A 55
CISPEP 1 GLY A 13 PRO A 14 1 0.08
CISPEP 2 ALA A 15 PRO A 16 1 0.05
CISPEP 3 GLY A 13 PRO A 14 2 0.05
CISPEP 4 ALA A 15 PRO A 16 2 -0.02
CISPEP 5 GLY A 13 PRO A 14 3 0.04
CISPEP 6 ALA A 15 PRO A 16 3 0.04
CISPEP 7 GLY A 13 PRO A 14 4 0.11
CISPEP 8 ALA A 15 PRO A 16 4 0.04
CISPEP 9 GLY A 13 PRO A 14 5 0.11
CISPEP 10 ALA A 15 PRO A 16 5 0.02
CISPEP 11 GLY A 13 PRO A 14 6 0.07
CISPEP 12 ALA A 15 PRO A 16 6 0.05
CISPEP 13 GLY A 13 PRO A 14 7 0.14
CISPEP 14 ALA A 15 PRO A 16 7 0.01
CISPEP 15 GLY A 13 PRO A 14 8 0.03
CISPEP 16 ALA A 15 PRO A 16 8 0.00
CISPEP 17 GLY A 13 PRO A 14 9 0.06
CISPEP 18 ALA A 15 PRO A 16 9 -0.07
CISPEP 19 GLY A 13 PRO A 14 10 0.02
CISPEP 20 ALA A 15 PRO A 16 10 -0.01
CISPEP 21 GLY A 13 PRO A 14 11 0.04
CISPEP 22 ALA A 15 PRO A 16 11 0.03
CISPEP 23 GLY A 13 PRO A 14 12 0.09
CISPEP 24 ALA A 15 PRO A 16 12 0.00
CISPEP 25 GLY A 13 PRO A 14 13 0.03
CISPEP 26 ALA A 15 PRO A 16 13 0.06
CISPEP 27 GLY A 13 PRO A 14 14 0.09
CISPEP 28 ALA A 15 PRO A 16 14 0.08
CISPEP 29 GLY A 13 PRO A 14 15 0.06
CISPEP 30 ALA A 15 PRO A 16 15 0.04
CISPEP 31 GLY A 13 PRO A 14 16 0.05
CISPEP 32 ALA A 15 PRO A 16 16 -0.01
CISPEP 33 GLY A 13 PRO A 14 17 0.10
CISPEP 34 ALA A 15 PRO A 16 17 0.03
CISPEP 35 GLY A 13 PRO A 14 18 0.04
CISPEP 36 ALA A 15 PRO A 16 18 -0.03
CISPEP 37 GLY A 13 PRO A 14 19 0.07
CISPEP 38 ALA A 15 PRO A 16 19 0.10
CISPEP 39 GLY A 13 PRO A 14 20 0.05
CISPEP 40 ALA A 15 PRO A 16 20 -0.01
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