HEADER SIGNALING PROTEIN 11-AUG-03 1UJV
TITLE SOLUTION STRUCTURE OF THE SECOND PDZ DOMAIN OF HUMAN MEMBRANE
TITLE 2 ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: KIAA0705 PROTEIN;
COMPND 6 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: KAZUSA CDNA HG03359;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-28;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ATROPHIN-1 INTERACTING PROTEIN 1, PDZ DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 KIAA0705 PROTEIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 3 RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.NAMEKI,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 27-DEC-23 1UJV 1 REMARK
REVDAT 3 02-MAR-22 1UJV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UJV 1 VERSN
REVDAT 1 11-FEB-04 1UJV 0
JRNL AUTH N.NAMEKI,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND PDZ DOMAIN OF HUMAN
JRNL TITL 2 MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2)
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, OPALP
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R., BILLETER, M.,
REMARK 3 GUENTERT, P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UJV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005907.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM PDZ DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 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 0.811, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR 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 HG SER A 30 O GLY A 33 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 9 LEU A 48 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES
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 -56.49 -123.19
REMARK 500 1 SER A 3 -141.79 44.30
REMARK 500 1 ALA A 20 -62.41 -157.64
REMARK 500 1 GLN A 21 6.40 -65.10
REMARK 500 1 PHE A 23 173.06 63.54
REMARK 500 1 CYS A 45 57.99 -150.23
REMARK 500 1 GLU A 50 152.30 66.20
REMARK 500 1 VAL A 55 -51.60 -124.78
REMARK 500 1 SER A 94 118.23 -166.82
REMARK 500 2 SER A 5 117.68 66.19
REMARK 500 2 ALA A 9 -8.71 -152.24
REMARK 500 2 GLU A 10 109.34 -59.46
REMARK 500 2 ALA A 20 -166.92 54.27
REMARK 500 2 GLN A 21 9.70 40.47
REMARK 500 2 PHE A 23 174.61 63.75
REMARK 500 2 ASP A 52 -173.32 -58.48
REMARK 500 2 VAL A 55 -58.08 -124.28
REMARK 500 2 SER A 94 -63.17 -147.89
REMARK 500 3 SER A 2 97.82 -61.82
REMARK 500 3 SER A 5 -81.39 72.77
REMARK 500 3 SER A 6 150.30 62.52
REMARK 500 3 ALA A 20 -62.44 -157.32
REMARK 500 3 PHE A 23 -11.46 84.90
REMARK 500 3 PHE A 25 151.05 -49.40
REMARK 500 3 ASN A 58 54.42 32.28
REMARK 500 3 GLN A 59 4.49 47.78
REMARK 500 3 ASN A 61 126.42 65.88
REMARK 500 3 ARG A 89 -45.76 -141.61
REMARK 500 3 SER A 91 -41.10 175.51
REMARK 500 3 SER A 94 102.11 84.34
REMARK 500 4 SER A 6 -171.00 53.70
REMARK 500 4 ALA A 20 -58.11 -160.34
REMARK 500 4 PHE A 23 -71.53 69.69
REMARK 500 4 VAL A 55 -52.24 -130.46
REMARK 500 4 GLN A 59 -1.42 72.77
REMARK 500 4 ARG A 89 113.94 -160.67
REMARK 500 4 SER A 91 152.31 74.17
REMARK 500 4 SER A 94 107.57 132.94
REMARK 500 4 SER A 95 142.57 80.40
REMARK 500 5 SER A 3 73.45 51.87
REMARK 500 5 SER A 5 117.64 54.32
REMARK 500 5 SER A 6 85.53 -154.49
REMARK 500 5 ALA A 9 86.08 50.59
REMARK 500 5 LEU A 11 167.80 51.05
REMARK 500 5 PHE A 23 168.08 77.00
REMARK 500 5 PRO A 31 11.33 -69.89
REMARK 500 5 ASP A 52 -174.99 -57.15
REMARK 500 5 GLN A 59 -24.11 65.64
REMARK 500 5 ARG A 89 87.41 -160.35
REMARK 500 6 SER A 2 93.43 73.11
REMARK 500
REMARK 500 THIS ENTRY HAS 171 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 1 SER A 2 14 -138.91
REMARK 500 VAL A 17 LYS A 18 14 -145.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 ARG A 89 0.08 SIDE CHAIN
REMARK 500 9 PHE A 25 0.08 SIDE CHAIN
REMARK 500 10 ARG A 35 0.09 SIDE CHAIN
REMARK 500 16 ARG A 35 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000688.3 RELATED DB: TARGETDB
DBREF 1UJV A 8 90 UNP Q86UL8 AIP1_HUMAN 642 724
SEQADV 1UJV GLY A 1 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 2 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 3 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV GLY A 4 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 5 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 6 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV GLY A 7 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 91 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV GLY A 92 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV PRO A 93 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 94 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV SER A 95 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UJV GLY A 96 UNP Q86UL8 CLONING ARTIFACT
SEQRES 1 A 96 GLY SER SER GLY SER SER GLY GLN ALA GLU LEU MET THR
SEQRES 2 A 96 LEU THR ILE VAL LYS GLY ALA GLN GLY PHE GLY PHE THR
SEQRES 3 A 96 ILE ALA ASP SER PRO THR GLY GLN ARG VAL LYS GLN ILE
SEQRES 4 A 96 LEU ASP ILE GLN GLY CYS PRO GLY LEU CYS GLU GLY ASP
SEQRES 5 A 96 LEU ILE VAL GLU ILE ASN GLN GLN ASN VAL GLN ASN LEU
SEQRES 6 A 96 SER HIS THR GLU VAL VAL ASP ILE LEU LYS ASP CYS PRO
SEQRES 7 A 96 ILE GLY SER GLU THR SER LEU ILE ILE HIS ARG GLY SER
SEQRES 8 A 96 GLY PRO SER SER GLY
HELIX 1 1 HIS A 67 ASP A 76 1 10
SHEET 1 A 4 MET A 12 VAL A 17 0
SHEET 2 A 4 GLU A 82 HIS A 88 -1 O LEU A 85 N LEU A 14
SHEET 3 A 4 LEU A 53 ILE A 57 -1 N GLU A 56 O ILE A 86
SHEET 4 A 4 GLN A 60 ASN A 61 -1 O GLN A 60 N ILE A 57
SHEET 1 B 2 PHE A 25 SER A 30 0
SHEET 2 B 2 GLY A 33 ILE A 39 -1 O GLN A 38 N THR A 26
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
