HEADER NEUROPEPTIDE/MEMBRANE PROTEIN 09-DEC-03 1RSO
TITLE HETERO-TETRAMERIC L27 (LIN-2, LIN-7) DOMAIN COMPLEXES AS ORGANIZATION
TITLE 2 PLATFORMS OF SUPRA-MOLECULAR ASSEMBLIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESYNAPTIC PROTEIN SAP97;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: L27 DOMAIN;
COMPND 5 SYNONYM: SAP97;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PERIPHERAL PLASMA MEMBRANE PROTEIN CASK;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: L27N DOMAIN;
COMPND 11 SYNONYM: MLIN-2/CASK;
COMPND 12 EC: 2.7.1.-;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: 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: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: NORWAY RAT;
SOURCE 12 ORGANISM_TAXID: 10116;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS L27 DOMAIN, SCAFFOLD PROTEIN, PROTEIN ASSEMBLY, CELL POLARITY,
KEYWDS 2 NEUROPEPTIDE-MEMBRANE PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR W.FENG,J.-F.LONG,J.-S.FAN,T.SUETAKE,M.ZHANG
REVDAT 3 10-NOV-21 1RSO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RSO 1 VERSN
REVDAT 1 04-MAY-04 1RSO 0
JRNL AUTH W.FENG,J.-F.LONG,J.-S.FAN,T.SUETAKE,M.ZHANG
JRNL TITL THE TETRAMERIC L27 DOMAIN COMPLEX AS AN ORGANIZATION
JRNL TITL 2 PLATFORM FOR SUPRAMOLECULAR ASSEMBLIES
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 475 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15048107
JRNL DOI 10.1038/NSMB751
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, A.T. (CNS), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021014.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM UNLABELLED L27S/L27N
REMARK 210 COMPLEX IN 99.9% D2O; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 UNIFORMLY 15N LABELLED L27S/L27N
REMARK 210 COMPLEX IN 90% H2O/10% D2O;
REMARK 210 100MM POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 UNIFORMLY 15N/13C LABELLED L27S/
REMARK 210 L27N COMPLEX IN 90% H2O/10% D2O;
REMARK 210 100MM POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 UNIFORMLY 15N/13C LABELLED L27S/
REMARK 210 L27N COMPLEX IN 99.9% D2O; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 1.5MM 10%
REMARK 210 13C LABELLED L27S/L27N COMPLEX
REMARK 210 IN 90% H2O/10% D2O; 100MM
REMARK 210 POTASSIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNCO, HNCA,
REMARK 210 HN(CO)CA, HNCACB, CBCA(CO)NH; 3D_
REMARK 210 13C-SEPARATED_NOESY; 13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 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 : 11
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 LEU B 83 H ARG B 87 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 LEU A 25 -66.87 -92.36
REMARK 500 1 SER A 26 -157.48 -60.45
REMARK 500 1 THR A 28 -63.75 -147.87
REMARK 500 1 GLU A 29 27.87 -170.40
REMARK 500 1 ASP A 30 53.11 -146.73
REMARK 500 1 PHE A 58 44.57 -156.24
REMARK 500 1 GLU A 60 93.21 -53.72
REMARK 500 1 THR B 103 -31.12 -145.02
REMARK 500 1 SER B 106 121.82 80.96
REMARK 500 1 LEU C 25 -67.76 -94.44
REMARK 500 1 SER C 26 -160.06 -59.79
REMARK 500 1 THR C 28 -59.30 -152.14
REMARK 500 1 GLU C 29 28.36 -176.67
REMARK 500 1 ASP C 30 49.41 -145.52
REMARK 500 1 PHE C 58 31.58 -156.64
REMARK 500 1 GLU C 60 100.45 -57.73
REMARK 500 1 ASP C 65 -40.45 -142.90
REMARK 500 1 THR D 103 -33.24 -147.33
REMARK 500 1 SER D 105 -77.36 -52.19
REMARK 500 1 SER D 106 106.82 173.55
REMARK 500 2 THR A 28 -57.21 -175.80
REMARK 500 2 GLU A 29 29.33 -173.19
REMARK 500 2 PHE A 58 38.80 -157.52
REMARK 500 2 GLU A 60 90.72 -65.37
REMARK 500 2 ASP A 65 -20.32 -177.69
REMARK 500 2 THR B 103 -35.45 -153.50
REMARK 500 2 SER B 106 127.74 80.03
REMARK 500 2 LEU C 25 -74.22 -61.07
REMARK 500 2 SER C 26 -147.69 -62.21
REMARK 500 2 GLN C 27 27.41 47.96
REMARK 500 2 THR C 28 -49.54 -153.33
REMARK 500 2 GLU C 29 26.73 -177.15
REMARK 500 2 ASP C 30 59.65 -143.90
REMARK 500 2 PHE C 58 32.60 -158.11
REMARK 500 2 THR D 103 -32.86 -149.18
REMARK 500 2 SER D 105 -84.79 -51.00
REMARK 500 2 SER D 106 108.08 164.47
REMARK 500 3 SER A 26 -158.92 -66.28
REMARK 500 3 THR A 28 -59.43 -153.08
REMARK 500 3 GLU A 29 28.28 -173.62
REMARK 500 3 ASP A 30 46.16 -145.84
REMARK 500 3 SER A 46 122.81 -33.86
REMARK 500 3 PHE A 58 25.36 -154.87
REMARK 500 3 THR B 103 -35.37 -150.18
REMARK 500 3 SER B 106 125.78 77.16
REMARK 500 3 LEU C 25 -65.03 -109.56
REMARK 500 3 THR C 28 -51.57 -174.75
REMARK 500 3 GLU C 29 28.58 -175.65
REMARK 500 3 ASP C 30 47.25 -142.07
REMARK 500 3 PHE C 58 28.52 -157.77
REMARK 500
REMARK 500 THIS ENTRY HAS 374 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RSO A 7 66 UNP Q62696 DLG1_RAT 4 63
DBREF 1RSO C 7 66 UNP Q62696 DLG1_RAT 4 63
DBREF 1RSO B 81 136 UNP Q62915 CSKP_RAT 339 394
DBREF 1RSO D 81 136 UNP Q62915 CSKP_RAT 339 394
SEQADV 1RSO SER B 105 UNP Q62915 CYS 363 ENGINEERED MUTATION
SEQADV 1RSO SER D 105 UNP Q62915 CYS 363 ENGINEERED MUTATION
SEQRES 1 A 60 ARG LYS GLN ASP THR GLN ARG ALA LEU HIS LEU LEU GLU
SEQRES 2 A 60 GLU TYR ARG SER LYS LEU SER GLN THR GLU ASP ARG GLN
SEQRES 3 A 60 LEU ARG SER SER ILE GLU ARG VAL ILE SER ILE PHE GLN
SEQRES 4 A 60 SER ASN LEU PHE GLN ALA LEU ILE ASP ILE GLN GLU PHE
SEQRES 5 A 60 TYR GLU VAL THR LEU LEU ASP ASN
SEQRES 1 B 56 GLY LEU LEU ALA ALA GLU ARG ALA VAL SER GLN VAL LEU
SEQRES 2 B 56 ASP SER LEU GLU GLU ILE HIS ALA LEU THR ASP SER SER
SEQRES 3 B 56 GLU LYS ASP LEU ASP PHE LEU HIS SER VAL PHE GLN ASP
SEQRES 4 B 56 GLN HIS LEU HIS THR LEU LEU ASP LEU TYR ASP LYS ILE
SEQRES 5 B 56 ASN THR LYS SER
SEQRES 1 C 60 ARG LYS GLN ASP THR GLN ARG ALA LEU HIS LEU LEU GLU
SEQRES 2 C 60 GLU TYR ARG SER LYS LEU SER GLN THR GLU ASP ARG GLN
SEQRES 3 C 60 LEU ARG SER SER ILE GLU ARG VAL ILE SER ILE PHE GLN
SEQRES 4 C 60 SER ASN LEU PHE GLN ALA LEU ILE ASP ILE GLN GLU PHE
SEQRES 5 C 60 TYR GLU VAL THR LEU LEU ASP ASN
SEQRES 1 D 56 GLY LEU LEU ALA ALA GLU ARG ALA VAL SER GLN VAL LEU
SEQRES 2 D 56 ASP SER LEU GLU GLU ILE HIS ALA LEU THR ASP SER SER
SEQRES 3 D 56 GLU LYS ASP LEU ASP PHE LEU HIS SER VAL PHE GLN ASP
SEQRES 4 D 56 GLN HIS LEU HIS THR LEU LEU ASP LEU TYR ASP LYS ILE
SEQRES 5 D 56 ASN THR LYS SER
HELIX 1 1 ARG A 7 LYS A 24 1 18
HELIX 2 2 ASP A 30 SER A 46 1 17
HELIX 3 3 SER A 46 GLN A 56 1 11
HELIX 4 4 GLU B 86 LEU B 102 1 17
HELIX 5 5 SER B 106 ASP B 119 1 14
HELIX 6 6 ASP B 119 THR B 134 1 16
HELIX 7 7 ARG C 7 LYS C 24 1 18
HELIX 8 8 ASP C 30 SER C 46 1 17
HELIX 9 9 SER C 46 GLU C 57 1 12
HELIX 10 10 LEU D 83 LEU D 102 1 20
HELIX 11 11 SER D 106 ASP D 119 1 14
HELIX 12 12 ASP D 119 SER D 136 1 18
SHEET 1 A 2 TYR A 59 LEU A 63 0
SHEET 2 A 2 TYR C 59 LEU C 63 -1 O THR C 62 N GLU A 60
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
