HEADER CONTRACTILE PROTEIN 14-FEB-07 2EDF
TITLE SOLUTION STRUCTURE OF THE SECOND IG-LIKE DOMAIN(2826-2915) FROM HUMAN
TITLE 2 OBSCURIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OBSCURIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IG-LIKE DOMAIN;
COMPND 5 SYNONYM: OBSCURIN-MYOSIN LIGHT CHAIN KINASE, OBSCURIN-MLCK, OBSCURIN-
COMPND 6 RHOGEF;
COMPND 7 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: OBSCN;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P051216-03;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS BETA-SANDWICH, IG-FOLD, OBSCURIN-MYOSIN LIGHT CHAIN KINASE, OBSCURIN-
KEYWDS 2 MLCK, OBSCURIN-RHOGEF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 3 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.WAKABAYASHI,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2EDF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EDF 1 VERSN
REVDAT 1 14-AUG-07 2EDF 0
JRNL AUTH M.WAKABAYASHI,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND IG-LIKE DOMAIN(2826-2915)
JRNL TITL 2 FROM HUMAN OBSCURIN
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 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT.P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EDF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026526.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.14MM 13C, 15N-LAVELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL (PH7.0);100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O, 90% H2O
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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9815, 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 SER A 5 138.67 -38.79
REMARK 500 1 PRO A 8 -178.49 -69.77
REMARK 500 1 LEU A 15 -176.62 -66.99
REMARK 500 1 PRO A 22 85.20 -69.71
REMARK 500 1 THR A 61 42.80 36.99
REMARK 500 1 ILE A 67 74.92 -106.78
REMARK 500 1 GLU A 83 -71.25 -30.97
REMARK 500 2 SER A 3 155.15 -43.92
REMARK 500 2 ALA A 10 164.34 -47.80
REMARK 500 2 PRO A 22 87.62 -69.72
REMARK 500 2 GLN A 52 -36.97 -34.51
REMARK 500 2 PRO A 100 89.01 -69.71
REMARK 500 3 ALA A 9 44.66 -84.38
REMARK 500 3 PRO A 22 87.08 -69.74
REMARK 500 3 ASP A 44 51.73 72.44
REMARK 500 3 GLU A 59 79.93 -108.58
REMARK 500 3 THR A 61 40.70 -105.71
REMARK 500 3 LEU A 72 -38.59 -39.84
REMARK 500 3 GLU A 83 -70.06 -29.30
REMARK 500 3 LYS A 96 129.32 -35.56
REMARK 500 4 PRO A 22 84.65 -69.82
REMARK 500 4 GLU A 83 -67.59 -28.80
REMARK 500 4 LYS A 86 128.24 -170.12
REMARK 500 5 ALA A 10 -179.97 -62.02
REMARK 500 5 PRO A 22 92.18 -69.77
REMARK 500 5 THR A 61 39.80 -97.89
REMARK 500 5 ILE A 67 77.31 -109.29
REMARK 500 5 LEU A 72 -37.73 -38.69
REMARK 500 5 GLU A 83 -71.98 -28.52
REMARK 500 6 PRO A 8 -175.06 -69.75
REMARK 500 6 ALA A 10 154.38 -36.76
REMARK 500 6 PRO A 22 92.24 -69.83
REMARK 500 6 LYS A 50 137.93 -38.74
REMARK 500 6 GLN A 52 -38.98 -35.08
REMARK 500 6 GLU A 59 48.21 -101.21
REMARK 500 6 THR A 61 37.94 -89.52
REMARK 500 6 ILE A 67 76.35 -118.49
REMARK 500 6 ASP A 74 -36.02 -39.23
REMARK 500 6 GLU A 83 -72.05 -29.74
REMARK 500 6 SER A 101 125.65 -35.61
REMARK 500 7 ALA A 10 158.69 -42.70
REMARK 500 7 LEU A 15 -179.48 -66.50
REMARK 500 7 PRO A 22 86.72 -69.72
REMARK 500 7 ALA A 35 39.30 -86.63
REMARK 500 7 THR A 61 42.31 39.54
REMARK 500 7 ILE A 67 77.15 -119.96
REMARK 500 7 LEU A 72 -34.04 -39.52
REMARK 500 7 GLU A 83 -72.04 -28.53
REMARK 500 7 LYS A 86 149.44 -175.69
REMARK 500 8 SER A 5 87.93 -56.88
REMARK 500
REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001528.6 RELATED DB: TARGETDB
DBREF 2EDF A 8 97 UNP Q5VST9 OBSCN_HUMAN 2826 2915
SEQADV 2EDF GLY A 1 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 2 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 3 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF GLY A 4 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 5 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 6 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF GLY A 7 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 98 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF GLY A 99 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF PRO A 100 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 101 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF SER A 102 UNP Q5VST9 CLONING ARTIFACT
SEQADV 2EDF GLY A 103 UNP Q5VST9 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY PRO ALA ALA ILE ILE LYS
SEQRES 2 A 103 PRO LEU GLU ASP GLN TRP VAL ALA PRO GLY GLU ASP VAL
SEQRES 3 A 103 GLU LEU ARG CYS GLU LEU SER ARG ALA GLY THR PRO VAL
SEQRES 4 A 103 HIS TRP LEU LYS ASP ARG LYS ALA ILE ARG LYS SER GLN
SEQRES 5 A 103 LYS TYR ASP VAL VAL CYS GLU GLY THR MET ALA MET LEU
SEQRES 6 A 103 VAL ILE ARG GLY ALA SER LEU LYS ASP ALA GLY GLU TYR
SEQRES 7 A 103 THR CYS GLU VAL GLU ALA SER LYS SER THR ALA SER LEU
SEQRES 8 A 103 HIS VAL GLU GLU LYS ALA SER GLY PRO SER SER GLY
SHEET 1 A 2 ILE A 11 LYS A 13 0
SHEET 2 A 2 GLU A 31 LEU A 32 -1 O GLU A 31 N ILE A 12
SHEET 1 B 4 GLN A 18 VAL A 20 0
SHEET 2 B 4 LYS A 86 VAL A 93 1 O HIS A 92 N GLN A 18
SHEET 3 B 4 GLU A 77 GLU A 81 -1 N CYS A 80 O SER A 87
SHEET 4 B 4 TRP A 41 LYS A 43 -1 N LEU A 42 O THR A 79
SHEET 1 C 3 VAL A 26 LEU A 28 0
SHEET 2 C 3 MET A 62 ILE A 67 -1 O ILE A 67 N VAL A 26
SHEET 3 C 3 TYR A 54 GLU A 59 -1 N GLU A 59 O MET A 62
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
(ATOM LINES ARE NOT SHOWN.)
END