Header list of 1y74.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 08-DEC-04 1Y74
TITLE SOLUTION STRUCTURE OF MLIN-2/MLIN-7 L27 DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIN 7 HOMOLOG B;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: L27 DOMAIN;
COMPND 5 SYNONYM: MLIN-7/VELIS/MALS;
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: L27C DOMAIN;
COMPND 11 SYNONYM: MLIN-2/CASK;
COMPND 12 EC: 2.7.1.-;
COMPND 13 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS L27 DOMAIN, SCAFFOLD PROTEIN, PROTEIN ASSEMBLY, CELL POLARITY,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR W.FENG,J.-F.LONG,M.ZHANG
REVDAT 4 02-MAR-22 1Y74 1 REMARK
REVDAT 3 24-FEB-09 1Y74 1 VERSN
REVDAT 2 31-MAY-05 1Y74 1 JRNL
REVDAT 1 19-APR-05 1Y74 0
JRNL AUTH W.FENG,J.F.LONG,M.ZHANG
JRNL TITL A UNIFIED ASSEMBLY MODE REVEALED BY THE STRUCTURES OF
JRNL TITL 2 TETRAMERIC L27 DOMAIN COMPLEXES FORMED BY MLIN-2/MLIN-7 AND
JRNL TITL 3 PATJ/PALS1 SCAFFOLD PROTEINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 6861 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15863617
JRNL DOI 10.1073/PNAS.0409346102
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 1Y74 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031199.
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 L27M/L27C
REMARK 210 COMPLEX IN 99.9% D2O; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 UNIFORMLY 15N LABELLED L27M/L27C
REMARK 210 COMPLEX IN 90% H2O, 10% D2O;
REMARK 210 100MM POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 UNIFORMLY 15N/13C LABELLED L27M/
REMARK 210 L27C COMPLEX IN 90% H2O, 10% D2O;
REMARK 210 100MM POTASSIUM PHOSPHATE;
REMARK 210 1.5MM UNIFORMLY 15N/13C LABELLED
REMARK 210 L27M/L27C COMPLEX IN 99.9% D2O;
REMARK 210 100MM POTASSIUM PHOSPHATE; 1.5MM
REMARK 210 10% 13C LABELLED L27M/L27C
REMARK 210 COMPLEX IN 90% H2O, 10% D2O;
REMARK 210 100MM 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: 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 PRO A 40 102.74 -45.19
REMARK 500 1 TYR B 130 56.54 -170.46
REMARK 500 1 PRO C 40 104.12 -46.98
REMARK 500 1 SER D 131 -70.01 -138.40
REMARK 500 2 PRO A 40 101.41 -42.49
REMARK 500 2 TYR B 130 57.23 -171.81
REMARK 500 2 SER C 53 152.17 -49.71
REMARK 500 2 ILE C 72 -72.94 -75.55
REMARK 500 2 GLN D 112 109.70 -51.55
REMARK 500 2 TYR D 130 66.82 -153.38
REMARK 500 2 SER D 131 -75.44 -169.80
REMARK 500 3 PRO A 40 105.66 -50.98
REMARK 500 3 GLN B 112 108.96 -48.50
REMARK 500 3 TYR B 130 61.39 -172.20
REMARK 500 3 PRO C 40 104.04 -52.18
REMARK 500 3 GLN D 112 108.42 -49.58
REMARK 500 3 PRO D 113 -36.54 -38.95
REMARK 500 3 SER D 131 -56.55 -125.82
REMARK 500 4 PRO A 40 108.49 -48.61
REMARK 500 4 ILE A 72 -70.15 -75.53
REMARK 500 4 SER B 131 -68.42 -151.01
REMARK 500 4 PRO C 40 107.34 -50.80
REMARK 500 4 TYR D 130 57.40 -167.90
REMARK 500 5 PRO A 40 104.24 -48.72
REMARK 500 5 SER B 131 -77.40 -141.76
REMARK 500 5 PRO C 40 103.90 -51.44
REMARK 500 5 TYR D 130 57.87 177.46
REMARK 500 6 PRO A 40 104.98 -50.06
REMARK 500 6 TYR B 130 58.46 -166.14
REMARK 500 6 PRO C 40 104.53 -47.80
REMARK 500 6 GLN D 112 106.73 -48.82
REMARK 500 6 PRO D 113 -35.88 -38.45
REMARK 500 6 SER D 131 32.49 -155.70
REMARK 500 7 PRO A 40 101.97 -43.15
REMARK 500 7 GLN B 112 108.81 -47.56
REMARK 500 7 PRO B 113 -38.62 -39.50
REMARK 500 7 TYR B 130 62.36 -172.00
REMARK 500 7 PRO C 40 104.05 -47.51
REMARK 500 7 TYR D 130 -87.86 -112.87
REMARK 500 7 SER D 131 33.00 38.87
REMARK 500 8 PRO A 40 101.68 -46.87
REMARK 500 8 ILE A 72 -72.51 -76.09
REMARK 500 8 GLN B 112 108.00 -49.85
REMARK 500 8 TYR B 130 30.79 -173.76
REMARK 500 8 PRO C 40 101.01 -46.89
REMARK 500 8 TYR D 130 59.61 -174.95
REMARK 500 9 PRO A 40 106.26 -52.08
REMARK 500 9 TYR B 130 -88.00 -118.61
REMARK 500 9 SER B 131 28.74 41.82
REMARK 500 9 SER C 53 156.18 -48.15
REMARK 500
REMARK 500 THIS ENTRY HAS 123 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y76 RELATED DB: PDB
REMARK 900 PATJ/PALS1 L27 DOMAIN COMPLEX
DBREF 1Y74 A 17 73 UNP O88951 LIN7B_MOUSE 8 64
DBREF 1Y74 C 17 73 UNP O88951 LIN7B_MOUSE 8 64
DBREF 1Y74 B 83 132 UNP O70589 CSKP_MOUSE 405 454
DBREF 1Y74 D 83 132 UNP O70589 CSKP_MOUSE 405 454
SEQRES 1 A 57 LEU GLY LEU GLU ARG ASP VAL SER ARG ALA VAL GLU LEU
SEQRES 2 A 57 LEU GLU ARG LEU GLN ARG SER GLY GLU LEU PRO PRO GLN
SEQRES 3 A 57 LYS LEU GLN ALA LEU GLN ARG VAL LEU GLN SER ARG PHE
SEQRES 4 A 57 CYS SER ALA ILE ARG GLU VAL TYR GLU GLN LEU TYR ASP
SEQRES 5 A 57 THR LEU ASP ILE THR
SEQRES 1 B 50 ALA VAL GLN ARG ALA LYS GLU VAL LEU GLU GLU ILE SER
SEQRES 2 B 50 CYS TYR PRO GLU ASN ASN ASP ALA LYS GLU LEU LYS ARG
SEQRES 3 B 50 ILE LEU THR GLN PRO HIS PHE MET ALA LEU LEU GLN THR
SEQRES 4 B 50 HIS ASP VAL VAL ALA HIS GLU VAL TYR SER ASP
SEQRES 1 C 57 LEU GLY LEU GLU ARG ASP VAL SER ARG ALA VAL GLU LEU
SEQRES 2 C 57 LEU GLU ARG LEU GLN ARG SER GLY GLU LEU PRO PRO GLN
SEQRES 3 C 57 LYS LEU GLN ALA LEU GLN ARG VAL LEU GLN SER ARG PHE
SEQRES 4 C 57 CYS SER ALA ILE ARG GLU VAL TYR GLU GLN LEU TYR ASP
SEQRES 5 C 57 THR LEU ASP ILE THR
SEQRES 1 D 50 ALA VAL GLN ARG ALA LYS GLU VAL LEU GLU GLU ILE SER
SEQRES 2 D 50 CYS TYR PRO GLU ASN ASN ASP ALA LYS GLU LEU LYS ARG
SEQRES 3 D 50 ILE LEU THR GLN PRO HIS PHE MET ALA LEU LEU GLN THR
SEQRES 4 D 50 HIS ASP VAL VAL ALA HIS GLU VAL TYR SER ASP
HELIX 1 1 GLY A 18 GLY A 37 1 20
HELIX 2 2 PRO A 40 SER A 53 1 14
HELIX 3 3 SER A 53 THR A 73 1 21
HELIX 4 4 ALA B 83 CYS B 96 1 14
HELIX 5 5 ASN B 100 GLN B 112 1 13
HELIX 6 6 GLN B 112 SER B 131 1 20
HELIX 7 7 GLY C 18 GLY C 37 1 20
HELIX 8 8 PRO C 40 SER C 53 1 14
HELIX 9 9 SER C 53 THR C 73 1 21
HELIX 10 10 ALA D 83 CYS D 96 1 14
HELIX 11 11 ASN D 100 GLN D 112 1 13
HELIX 12 12 GLN D 112 TYR D 130 1 19
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 2 2 Bytes