HEADER PROTEIN BINDING 25-NOV-03 1V5Q
TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN FROM MOUSE GLUTAMATE RECEPTOR
TITLE 2 INTERACTING PROTEIN 1A-L (GRIP1) HOMOLOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR INTERACTING PROTEIN 1A-L HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: GRIP1 HOMOLOG;
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 4931400F03;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030203-74;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, CELLULAR SIGNALING, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 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 4 27-DEC-23 1V5Q 1 REMARK
REVDAT 3 02-MAR-22 1V5Q 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V5Q 1 VERSN
REVDAT 1 25-MAY-04 1V5Q 0
JRNL AUTH M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PDZ DOMAIN FROM MOUSE GLUTAMATE
JRNL TITL 2 RECEPTOR INTERACTING PROTEIN 1A-L (GRIP1) HOMOLOG
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 1V5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006239.
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 : 0.59MM 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 : 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 0.863, 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 ASP A 92 H ILE A 95 1.55
REMARK 500 H MET A 71 O GLU A 102 1.59
REMARK 500 O GLU A 84 H GLN A 88 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 5 105.31 -44.31
REMARK 500 1 ALA A 23 99.74 -45.27
REMARK 500 1 VAL A 26 -60.57 -141.66
REMARK 500 1 THR A 27 69.22 -103.80
REMARK 500 1 ALA A 39 -169.79 -165.74
REMARK 500 1 GLU A 41 -51.83 -151.02
REMARK 500 1 THR A 42 -133.23 -108.94
REMARK 500 1 SER A 45 151.71 177.61
REMARK 500 1 ILE A 49 99.55 -64.43
REMARK 500 1 GLU A 53 153.31 -49.99
REMARK 500 1 ASP A 68 -176.43 -64.41
REMARK 500 1 THR A 78 84.76 -61.04
REMARK 500 1 GLU A 79 47.20 -171.71
REMARK 500 1 ASP A 80 176.68 172.88
REMARK 500 1 SER A 81 -163.88 70.90
REMARK 500 1 SER A 110 103.24 -59.71
REMARK 500 2 SER A 2 81.93 -153.06
REMARK 500 2 SER A 6 87.96 -66.05
REMARK 500 2 ALA A 23 100.19 -45.05
REMARK 500 2 VAL A 26 -60.03 -141.40
REMARK 500 2 THR A 27 69.63 -104.32
REMARK 500 2 ALA A 39 -163.33 -175.13
REMARK 500 2 THR A 40 -77.66 -127.26
REMARK 500 2 THR A 42 -134.19 -125.95
REMARK 500 2 SER A 44 33.01 38.87
REMARK 500 2 GLU A 53 153.16 -49.99
REMARK 500 2 ASP A 68 -168.67 -56.33
REMARK 500 2 ASN A 74 13.10 82.40
REMARK 500 2 GLU A 79 38.56 178.13
REMARK 500 2 ASP A 80 58.22 -166.83
REMARK 500 2 SER A 81 -171.70 -179.86
REMARK 500 2 SER A 93 -38.36 -39.44
REMARK 500 2 SER A 117 122.67 -174.93
REMARK 500 3 SER A 2 102.44 54.97
REMARK 500 3 SER A 3 95.06 -162.30
REMARK 500 3 ALA A 23 99.39 -42.79
REMARK 500 3 VAL A 26 -60.91 -140.61
REMARK 500 3 THR A 27 69.38 -104.60
REMARK 500 3 ALA A 39 -174.42 169.59
REMARK 500 3 THR A 40 -78.15 -76.40
REMARK 500 3 THR A 42 -135.99 -122.82
REMARK 500 3 SER A 44 38.60 38.72
REMARK 500 3 SER A 45 170.01 173.08
REMARK 500 3 ASP A 55 23.56 49.48
REMARK 500 3 ASP A 68 -175.98 -59.38
REMARK 500 3 VAL A 70 90.22 -58.48
REMARK 500 3 GLU A 79 64.39 -172.85
REMARK 500 3 ASP A 80 -44.84 176.66
REMARK 500 3 ILE A 95 -72.49 -54.70
REMARK 500 3 SER A 110 99.75 -65.85
REMARK 500
REMARK 500 THIS ENTRY HAS 375 RAMACHANDRAN OUTLIERS.
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: MMT007011047.1 RELATED DB: TARGETDB
DBREF 1V5Q A 8 116 GB 26325828 BAC26668 46 154
SEQADV 1V5Q GLY A 1 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 2 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 3 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q GLY A 4 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 5 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 6 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q GLY A 7 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 117 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q GLY A 118 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q PRO A 119 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 120 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q SER A 121 GB 26325828 CLONING ARTIFACT
SEQADV 1V5Q GLY A 122 GB 26325828 CLONING ARTIFACT
SEQRES 1 A 122 GLY SER SER GLY SER SER GLY ALA GLY GLN VAL VAL HIS
SEQRES 2 A 122 THR GLU THR THR GLU VAL VAL LEU THR ALA ASP PRO VAL
SEQRES 3 A 122 THR GLY PHE GLY ILE GLN LEU GLN GLY SER VAL PHE ALA
SEQRES 4 A 122 THR GLU THR LEU SER SER PRO PRO LEU ILE SER TYR ILE
SEQRES 5 A 122 GLU ALA ASP SER PRO ALA GLU ARG CYS GLY VAL LEU GLN
SEQRES 6 A 122 ILE GLY ASP ARG VAL MET ALA ILE ASN GLY ILE PRO THR
SEQRES 7 A 122 GLU ASP SER THR PHE GLU GLU ALA ASN GLN LEU LEU ARG
SEQRES 8 A 122 ASP SER SER ILE THR SER LYS VAL THR LEU GLU ILE GLU
SEQRES 9 A 122 PHE ASP VAL ALA GLU SER VAL ILE PRO SER SER GLY SER
SEQRES 10 A 122 GLY PRO SER SER GLY
HELIX 1 1 PRO A 57 CYS A 61 1 5
HELIX 2 2 THR A 82 SER A 94 1 13
SHEET 1 A 4 THR A 14 LEU A 21 0
SHEET 2 A 4 VAL A 99 ASP A 106 -1 O ILE A 103 N THR A 17
SHEET 3 A 4 VAL A 70 ILE A 73 -1 N ALA A 72 O GLU A 102
SHEET 4 A 4 ILE A 76 PRO A 77 -1 O ILE A 76 N ILE A 73
SHEET 1 B 2 ILE A 31 GLN A 34 0
SHEET 2 B 2 LEU A 48 ILE A 52 -1 O LEU A 48 N GLN A 34
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