HEADER NEUROPEPTIDE 19-FEB-02 1IU2
TITLE THE FIRST PDZ DOMAIN OF PSD-95
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PSD-95;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ1 DOMAIN;
COMPND 5 SYNONYM: PRESYNAPTIC DENSITY PROTEIN 95;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PSD-95, PDZ DOMAIN, POST SYNAPTIC DENSITY, NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR J.-F.LONG,H.TOCHIO,P.WANG,C.SALA,M.NIETHAMMER,M.SHENG,M.ZHANG
REVDAT 4 27-DEC-23 1IU2 1 REMARK
REVDAT 3 23-FEB-22 1IU2 1 REMARK
REVDAT 2 24-FEB-09 1IU2 1 VERSN
REVDAT 1 11-MAR-03 1IU2 0
JRNL AUTH J.-F.LONG,H.TOCHIO,P.WANG,J.-S.FAN,C.SALA,M.NIETHAMMER,
JRNL AUTH 2 M.SHENG,M.ZHANG
JRNL TITL SUPRAMODULAR STRUCTURE AND SYNERGISTIC TARGET BINDING OF THE
JRNL TITL 2 N-TERMINAL TANDEM PDZ DOMAINS OF PSD-95
JRNL REF J.MOL.BIOL. V. 327 203 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12614619
JRNL DOI 10.1016/S0022-2836(03)00113-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8, CNS 1.1
REMARK 3 AUTHORS : DELAGRIO (NMRPIPE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IU2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000005275.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20MM KPI, 100MM KCL; 20MM KPI,
REMARK 210 100MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 H ARG A 10 O SER A 82 1.54
REMARK 500 H LEU A 58 O TYR A 87 1.57
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 ARG A 10 89.25 -49.35
REMARK 500 1 PRO A 26 64.13 -67.67
REMARK 500 1 ILE A 28 -152.29 -88.45
REMARK 500 1 ASP A 30 43.36 76.54
REMARK 500 1 VAL A 53 157.78 -49.14
REMARK 500 1 ASN A 61 -66.83 70.42
REMARK 500 1 GLU A 62 29.75 -163.39
REMARK 500 1 GLU A 67 44.62 -145.97
REMARK 500 1 SER A 82 -91.31 -130.45
REMARK 500 2 ARG A 10 88.89 -50.78
REMARK 500 2 PRO A 26 63.07 -65.96
REMARK 500 2 ILE A 28 -151.75 -93.73
REMARK 500 2 ASP A 30 45.38 76.88
REMARK 500 2 LYS A 38 134.24 -172.41
REMARK 500 2 ASN A 54 -2.01 76.60
REMARK 500 2 GLU A 62 33.43 78.86
REMARK 500 2 GLU A 67 76.27 -150.80
REMARK 500 2 SER A 82 -90.25 -142.19
REMARK 500 3 ARG A 10 88.92 -51.40
REMARK 500 3 PRO A 26 64.53 -67.27
REMARK 500 3 ILE A 28 -155.77 -83.13
REMARK 500 3 ASP A 30 42.12 -179.34
REMARK 500 3 LYS A 38 141.23 -170.29
REMARK 500 3 VAL A 53 157.51 -49.08
REMARK 500 3 ASN A 54 -2.31 77.03
REMARK 500 3 PHE A 59 143.90 -171.61
REMARK 500 3 GLU A 62 32.29 78.73
REMARK 500 3 GLU A 67 45.38 -140.56
REMARK 500 3 SER A 82 -90.05 -142.84
REMARK 500 4 ARG A 10 92.13 -44.76
REMARK 500 4 ASN A 12 -74.42 64.65
REMARK 500 4 PRO A 26 60.82 -67.93
REMARK 500 4 ILE A 28 -154.04 -90.39
REMARK 500 4 ASP A 30 40.09 172.80
REMARK 500 4 LYS A 38 136.06 -171.55
REMARK 500 4 VAL A 53 157.57 -49.17
REMARK 500 4 ASN A 54 -3.02 77.40
REMARK 500 4 GLU A 62 34.00 79.55
REMARK 500 4 VAL A 65 40.83 -95.97
REMARK 500 4 SER A 82 -89.38 -120.68
REMARK 500 5 ARG A 10 88.20 -47.83
REMARK 500 5 PRO A 26 62.17 -66.72
REMARK 500 5 ILE A 28 -151.40 -93.25
REMARK 500 5 ASP A 30 45.88 77.23
REMARK 500 5 LYS A 38 134.59 -172.52
REMARK 500 5 ASN A 54 -1.54 75.29
REMARK 500 5 ASN A 61 -67.56 67.82
REMARK 500 5 GLU A 62 32.27 -156.41
REMARK 500 5 VAL A 65 40.07 -92.82
REMARK 500 5 GLU A 67 70.64 -152.87
REMARK 500
REMARK 500 THIS ENTRY HAS 526 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IU0 RELATED DB: PDB
REMARK 900 1IU0 IS ENERGY MINIMIZED AVERAGE COORDINATE
DBREF 1IU2 A 1 91 UNP P31016 DLG4_RAT 61 151
SEQRES 1 A 91 MET GLU TYR GLU GLU ILE THR LEU GLU ARG GLY ASN SER
SEQRES 2 A 91 GLY LEU GLY PHE SER ILE ALA GLY GLY THR ASP ASN PRO
SEQRES 3 A 91 HIS ILE GLY ASP ASP PRO SER ILE PHE ILE THR LYS ILE
SEQRES 4 A 91 ILE PRO GLY GLY ALA ALA ALA GLN ASP GLY ARG LEU ARG
SEQRES 5 A 91 VAL ASN ASP SER ILE LEU PHE VAL ASN GLU VAL ASP VAL
SEQRES 6 A 91 ARG GLU VAL THR HIS SER ALA ALA VAL GLU ALA LEU LYS
SEQRES 7 A 91 GLU ALA GLY SER ILE VAL ARG LEU TYR VAL MET ARG ARG
HELIX 1 1 GLY A 43 GLY A 49 1 7
HELIX 2 2 ARG A 66 VAL A 68 5 3
HELIX 3 3 THR A 69 ALA A 80 1 12
SHEET 1 A 4 GLU A 2 GLU A 9 0
SHEET 2 A 4 ILE A 83 ARG A 90 -1 O LEU A 86 N ILE A 6
SHEET 3 A 4 PHE A 59 VAL A 60 -1 N PHE A 59 O TYR A 87
SHEET 4 A 4 VAL A 63 ASP A 64 -1 O VAL A 63 N VAL A 60
SHEET 1 B 3 PHE A 17 ALA A 20 0
SHEET 2 B 3 ILE A 34 ILE A 39 -1 O LYS A 38 N SER A 18
SHEET 3 B 3 SER A 56 ILE A 57 -1 O ILE A 57 N ILE 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