Header list of 1p1e.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 12-APR-03 1P1E
TITLE STRUCTURAL INSIGHTS INTO THE INTER-DOMAIN CHAPERONING OF TANDEM PDZ
TITLE 2 DOMAINS IN GLUTAMATE RECEPTOR INTERACTING PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR INTERACTING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 18-118;
COMPND 5 SYNONYM: PDZ4;
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;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS PDZ DOMAIN, GLUTAMATE RECEPTOR, CHAPERONING DOMAIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR W.FENG,Y.SHI,M.LI,M.ZHANG
REVDAT 3 23-FEB-22 1P1E 1 REMARK
REVDAT 2 24-FEB-09 1P1E 1 VERSN
REVDAT 1 11-NOV-03 1P1E 0
JRNL AUTH W.FENG,Y.SHI,M.LI,M.ZHANG
JRNL TITL TANDEM PDZ REPEATS IN GLUTAMATE RECEPTOR-INTERACTING
JRNL TITL 2 PROTEINS HAVE A NOVEL MODE OF PDZ DOMAIN-MEDIATED TARGET
JRNL TITL 3 BINDING
JRNL REF NAT.STRUCT.BIOL. V. 10 972 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 14555997
JRNL DOI 10.1038/NSB992
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,
REMARK 3 WARREN (CNS), BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P1E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018894.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM UNIFORMLY 15N LABELLED
REMARK 210 PDZ4; 100MM PHOSPHATE BUFFER;
REMARK 210 1.5MM UNIFORMLY 15N/13C LABELLED
REMARK 210 PDZ4; 100MM PHOSPHATE BUFFER;
REMARK 210 1.5MM UNIFORMLY 15N/13C LABELLED
REMARK 210 PDZ4; 100MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNCACB,
REMARK 210 CBCA(CO)NH, HNCO
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 : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13
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 THR A 22 102.69 174.77
REMARK 500 1 VAL A 34 -67.05 -98.81
REMARK 500 1 VAL A 45 -39.95 -155.30
REMARK 500 1 THR A 50 164.72 58.14
REMARK 500 1 SER A 58 41.78 -164.34
REMARK 500 1 TYR A 59 123.19 -176.32
REMARK 500 1 ALA A 62 43.25 -81.15
REMARK 500 1 ASP A 63 31.20 168.18
REMARK 500 1 VAL A 71 34.52 -170.97
REMARK 500 1 MET A 79 27.48 -141.14
REMARK 500 1 ALA A 80 61.83 -178.86
REMARK 500 1 THR A 86 150.29 61.68
REMARK 500 1 ASP A 88 -81.23 61.94
REMARK 500 1 SER A 89 114.82 -161.02
REMARK 500 1 SER A 105 -4.54 78.97
REMARK 500 1 ALA A 116 46.19 -140.65
REMARK 500 1 GLU A 117 53.70 -179.82
REMARK 500 2 VAL A 19 77.84 -100.74
REMARK 500 2 THR A 22 132.18 167.55
REMARK 500 2 VAL A 34 -68.90 -155.42
REMARK 500 2 PHE A 46 44.46 173.38
REMARK 500 2 ALA A 47 114.83 -175.57
REMARK 500 2 THR A 50 -170.88 46.29
REMARK 500 2 LEU A 51 133.93 -177.52
REMARK 500 2 SER A 58 50.17 -175.40
REMARK 500 2 TYR A 59 134.15 -173.79
REMARK 500 2 ALA A 62 41.00 -89.87
REMARK 500 2 ASP A 63 33.30 171.82
REMARK 500 2 VAL A 71 -58.97 -137.29
REMARK 500 2 MET A 79 29.23 -170.29
REMARK 500 2 ALA A 80 46.40 -176.18
REMARK 500 2 THR A 86 107.24 58.55
REMARK 500 2 ASP A 88 78.37 -65.91
REMARK 500 2 SER A 89 -49.73 -151.94
REMARK 500 2 SER A 105 -5.02 79.35
REMARK 500 2 ALA A 116 48.03 -174.51
REMARK 500 2 GLU A 117 48.70 -174.04
REMARK 500 3 VAL A 19 75.09 -109.18
REMARK 500 3 THR A 22 105.79 167.13
REMARK 500 3 THR A 35 -66.54 -133.91
REMARK 500 3 PHE A 46 132.66 -171.60
REMARK 500 3 ALA A 47 110.12 59.24
REMARK 500 3 SER A 52 22.82 -154.78
REMARK 500 3 ALA A 62 38.34 -86.87
REMARK 500 3 ASP A 63 26.11 -179.72
REMARK 500 3 VAL A 71 -52.90 -145.03
REMARK 500 3 MET A 79 -65.36 -134.98
REMARK 500 3 THR A 86 142.32 63.45
REMARK 500 3 ASP A 88 -79.99 62.95
REMARK 500 3 SER A 89 106.78 -179.80
REMARK 500
REMARK 500 THIS ENTRY HAS 367 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P1D RELATED DB: PDB
REMARK 900 1P1D CONTAINS 196 RESIDUES PER 1 MODEL
DBREF 1P1E A 18 118 UNP P97879 GRIP1_RAT 463 563
SEQRES 1 A 101 GLN VAL VAL HIS THR GLU THR THR GLU VAL VAL LEU THR
SEQRES 2 A 101 ALA ASP PRO VAL THR GLY PHE GLY ILE GLN LEU GLN GLY
SEQRES 3 A 101 SER VAL PHE ALA THR GLU THR LEU SER SER PRO PRO LEU
SEQRES 4 A 101 ILE SER TYR ILE GLU ALA ASP SER PRO ALA GLU ARG CYS
SEQRES 5 A 101 GLY VAL LEU GLN ILE GLY ASP ARG VAL MET ALA ILE ASN
SEQRES 6 A 101 GLY ILE PRO THR GLU ASP SER THR PHE GLU GLU ALA ASN
SEQRES 7 A 101 GLN LEU LEU ARG ASP SER SER ILE THR SER LYS VAL THR
SEQRES 8 A 101 LEU GLU ILE GLU PHE ASP VAL ALA GLU SER
HELIX 1 1 SER A 64 CYS A 69 1 6
HELIX 2 2 THR A 90 ASP A 100 1 11
HELIX 3 3 SER A 101 THR A 104 5 4
SHEET 1 A 3 GLU A 23 THR A 30 0
SHEET 2 A 3 LYS A 106 PHE A 113 -1 O PHE A 113 N GLU A 23
SHEET 3 A 3 ARG A 77 ILE A 81 -1 N ARG A 77 O GLU A 112
SHEET 1 B 2 LEU A 41 GLN A 42 0
SHEET 2 B 2 LEU A 56 ILE A 57 -1 O LEU A 56 N GLN A 42
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 - b 23 2 Bytes