Header list of 1zl8.pdb file
Complete list - r 25 2 Bytes
HEADER PROTEIN BINDING 05-MAY-05 1ZL8
TITLE NMR STRUCTURE OF L27 HETERODIMER FROM C. ELEGANS LIN-7 AND H. SAPIENS
TITLE 2 LIN-2 SCAFFOLD PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIN-7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: L27 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PERIPHERAL PLASMA MEMBRANE PROTEIN CASK;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: L27 DOMAIN;
COMPND 10 SYNONYM: HCASK, CALCIUM/CALMODULIN-DEPENDENT SERINE PROTEIN KINASE,
COMPND 11 LIN-2 HOMOLOG;
COMPND 12 EC: 2.7.1.-;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: LIN7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET19B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: CASK, LIN2;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS HETERODIMER, L27, ALPHA HELIX, SCAFFOLD, ASSEMBLY, SPECIFICITY,
KEYWDS 2 SIGNALING, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.Y.PETROSKY,H.D.OU,F.LOHR,V.DOTSCH,W.A.LIM
REVDAT 4 20-OCT-10 1ZL8 1 REMARK
REVDAT 3 24-FEB-09 1ZL8 1 VERSN
REVDAT 2 14-MAR-06 1ZL8 1 JRNL
REVDAT 1 13-SEP-05 1ZL8 0
JRNL AUTH K.Y.PETROSKY,H.D.OU,F.LOHR,V.DOTSCH,W.A.LIM
JRNL TITL A GENERAL MODEL FOR PREFERENTIAL HETERO-OLIGOMERIZATION OF
JRNL TITL 2 LIN-2/7 DOMAINS: MECHANISM UNDERLYING DIRECTED ASSEMBLY OF
JRNL TITL 3 SUPRAMOLECULAR SIGNALING COMPLEXES
JRNL REF J.BIOL.CHEM. V. 280 38528 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16147993
JRNL DOI 10.1074/JBC.M506536200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1544 NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS AND 204 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1ZL8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032848.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM LIN-7/LIN-2C; 20MM HEPES,
REMARK 210 5MM TCEP, 0.05% DSS, 0.05% SODIUM
REMARK 210 AZIDE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 4.5, XEASY 1.3, DYANA
REMARK 210 1.5, TALOS 98.040.21.02
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASN A 27 H ALA A 31 1.48
REMARK 500 O GLN A 34 H GLN A 38 1.50
REMARK 500 O SER A 32 HE ARG B 111 1.50
REMARK 500 O ALA A 31 HE21 GLN A 35 1.51
REMARK 500 O ARG B 133 HG1 THR B 136 1.57
REMARK 500 O VAL B 149 HD1 HIS B 152 1.57
REMARK 500 O ASN A 4 H ASP A 8 1.58
REMARK 500 O GLU B 130 H ILE B 134 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 VAL A 25 43.88 -170.14
REMARK 500 1 ASN A 26 108.77 -0.16
REMARK 500 1 PHE B 140 -72.31 -78.24
REMARK 500 1 SER B 156 120.49 -35.29
REMARK 500 2 LEU A 3 97.65 -58.77
REMARK 500 2 VAL A 25 44.25 -161.92
REMARK 500 2 ASN A 26 109.66 -0.14
REMARK 500 2 PHE B 140 -70.81 -77.47
REMARK 500 2 ASP B 157 106.74 -43.07
REMARK 500 3 VAL A 25 51.90 -153.91
REMARK 500 3 ASN A 26 102.66 -3.74
REMARK 500 3 PHE B 140 -70.85 -76.81
REMARK 500 3 ASP B 157 106.08 -45.38
REMARK 500 4 VAL A 25 46.37 -154.25
REMARK 500 4 ASN A 26 104.78 -2.69
REMARK 500 4 SER B 156 118.92 -35.14
REMARK 500 5 VAL A 25 59.98 -171.13
REMARK 500 5 ASN A 26 115.31 -6.23
REMARK 500 5 SER B 156 117.11 -36.21
REMARK 500 6 LEU A 3 87.55 -57.95
REMARK 500 6 VAL A 25 60.03 -156.69
REMARK 500 6 ASN A 26 101.00 -16.37
REMARK 500 6 PHE B 140 -70.46 -78.05
REMARK 500 6 ASP B 157 107.45 -44.36
REMARK 500 7 LEU A 3 107.72 -59.21
REMARK 500 7 VAL A 25 52.18 -172.86
REMARK 500 7 ASN A 26 104.93 -0.86
REMARK 500 7 ASP B 157 107.89 -43.88
REMARK 500 8 LEU A 3 78.54 -67.89
REMARK 500 8 ASN A 4 -41.84 -135.05
REMARK 500 8 VAL A 25 56.94 -170.95
REMARK 500 8 ASN A 26 102.71 -1.56
REMARK 500 8 PHE B 140 -74.31 -77.73
REMARK 500 8 ASP B 157 107.02 -44.07
REMARK 500 9 VAL A 25 49.06 -157.18
REMARK 500 9 ASN A 26 107.65 -9.46
REMARK 500 9 PHE B 140 -72.45 -77.38
REMARK 500 9 ASP B 157 107.54 -43.69
REMARK 500 10 LEU A 3 90.00 -59.35
REMARK 500 10 VAL A 25 57.90 -171.67
REMARK 500 10 ASN A 26 106.13 -3.43
REMARK 500 10 PHE B 140 -71.78 -78.41
REMARK 500 10 ASP B 157 107.67 -43.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RSO RELATED DB: PDB
REMARK 900 HETERO-TETRAMERIC L27 (LIN-2, LIN-7) DOMAIN COMPLEXES AS
REMARK 900 ORGANIZATION PLATFORMS OF SUPRA-MOLECULAR ASSEMBLIES
REMARK 900 RELATED ID: 1VF6 RELATED DB: PDB
REMARK 900 2.1 ANGSTROM CRYSTAL STRUCTURE OF THE PALS-1-L27N AND PATJ
REMARK 900 L27 HETERODIMER COMPLEX
REMARK 900 RELATED ID: 1Y74 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF MLIN-2/MLIN-7 L27 DOMAIN COMPLEX
REMARK 900 RELATED ID: 1Y76 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PATJ/PALS1 L27 DOMAIN COMPLEX
DBREF 1ZL8 A 4 53 GB 1685067 AAB36684 116 165
DBREF 1ZL8 B 106 159 UNP O14936 CSKP_HUMAN 403 456
SEQADV 1ZL8 GLY A 1 GB 1685067 CLONING ARTIFACT
SEQADV 1ZL8 SER A 2 GB 1685067 CLONING ARTIFACT
SEQADV 1ZL8 LEU A 3 GB 1685067 CLONING ARTIFACT
SEQRES 1 A 53 GLY SER LEU ASN LEU GLU ARG ASP VAL GLN ARG ILE LEU
SEQRES 2 A 53 GLU LEU MET GLU HIS VAL GLN LYS THR GLY GLU VAL ASN
SEQRES 3 A 53 ASN ALA LYS LEU ALA SER LEU GLN GLN VAL LEU GLN SER
SEQRES 4 A 53 GLU PHE PHE GLY ALA VAL ARG GLU VAL TYR GLU THR VAL
SEQRES 5 A 53 TYR
SEQRES 1 B 54 SER ASP ALA VAL GLN ARG ALA LYS GLU VAL LEU GLU GLU
SEQRES 2 B 54 ILE SER CYS TYR PRO GLU ASN ASN ASP ALA LYS GLU LEU
SEQRES 3 B 54 LYS ARG ILE LEU THR GLN PRO HIS PHE MET ALA LEU LEU
SEQRES 4 B 54 GLN THR HIS ASP VAL VAL ALA HIS GLU VAL TYR SER ASP
SEQRES 5 B 54 GLU ALA
HELIX 1 1 LEU A 3 GLN A 20 1 18
HELIX 2 2 LYS A 21 GLY A 23 5 3
HELIX 3 3 ASN A 26 GLN A 38 1 13
HELIX 4 4 GLU A 40 TYR A 53 1 14
HELIX 5 5 SER B 106 SER B 120 1 15
HELIX 6 6 ASN B 125 LEU B 135 1 11
HELIX 7 7 HIS B 139 VAL B 154 1 16
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 - r 25 2 Bytes