Header list of 1y76.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 08-DEC-04 1Y76 TITLE SOLUTION STRUCTURE OF PATJ/PALS1 L27 DOMAIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN ASSOCIATED TO TIGHT JUNCTIONS; COMPND 3 CHAIN: A, C; COMPND 4 FRAGMENT: L27 DOMAIN; COMPND 5 SYNONYM: PATJ; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MAGUK P55 SUBFAMILY MEMBER 5; COMPND 9 CHAIN: B, D; COMPND 10 FRAGMENT: L27 DOMAIN; COMPND 11 SYNONYM: PALS1; COMPND 12 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: PET32A; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: 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 1Y76 1 REMARK REVDAT 3 24-FEB-09 1Y76 1 VERSN REVDAT 2 31-MAY-05 1Y76 1 JRNL REVDAT 1 19-APR-05 1Y76 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 1Y76 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-04. REMARK 100 THE DEPOSITION ID IS D_1000031201. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM UNLABELLED L27P/L27NP REMARK 210 COMPLEX IN 99.9% D2O; 100MM REMARK 210 POTASSIUM PHOSPHATE; 1.5MM REMARK 210 UNIFORMLY 15N LABELLED L27P/ REMARK 210 L27NP COMPLEX IN 90% H2O/10% D2O; REMARK 210 100MM POTASSIUM PHOSPHATE; REMARK 210 1.5MM UNIFORMLY 15N/13C LABELLED REMARK 210 L27P/L27NP COMPLEX IN 90% H2O, REMARK 210 10% D2O; 100MM POTASSIUM REMARK 210 PHOSPHATE; 1.5MM UNIFORMLY 15N/ REMARK 210 13C LABELLED L27P/L27NP COMPLEX REMARK 210 IN 99.9% D2O; 100MM POTASSIUM REMARK 210 PHOSPHATE; 1.5MM 10% 13C REMARK 210 LABELLED L27P/L27NP COMPLEX IN REMARK 210 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 : 10 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 ASP A 28 77.69 -114.76 REMARK 500 1 THR A 29 36.17 -93.25 REMARK 500 1 VAL B 81 -66.17 -179.08 REMARK 500 1 LYS B 82 118.90 61.21 REMARK 500 1 ILE B 83 -159.30 -90.20 REMARK 500 1 LEU B 84 -37.34 -154.99 REMARK 500 1 GLU B 85 107.20 61.74 REMARK 500 1 SER B 103 -72.52 65.69 REMARK 500 1 LYS B 137 -75.10 -70.63 REMARK 500 1 VAL D 81 33.11 -170.23 REMARK 500 1 ILE D 83 -162.80 44.68 REMARK 500 1 LEU D 84 -40.98 -153.59 REMARK 500 1 GLU D 85 104.94 65.54 REMARK 500 1 VAL D 101 36.31 -97.27 REMARK 500 1 SER D 103 -67.60 69.28 REMARK 500 1 ALA D 138 -168.74 57.97 REMARK 500 2 VAL B 81 85.43 41.20 REMARK 500 2 LEU B 84 -52.53 70.21 REMARK 500 2 GLU B 85 115.63 62.01 REMARK 500 2 SER B 103 -73.58 65.99 REMARK 500 2 ALA B 138 -177.51 60.71 REMARK 500 2 VAL D 81 39.53 177.89 REMARK 500 2 LEU D 84 -0.99 -157.92 REMARK 500 2 GLU D 85 143.15 58.75 REMARK 500 2 VAL D 101 36.18 -95.04 REMARK 500 2 SER D 103 -68.34 69.28 REMARK 500 2 ALA D 138 114.20 61.34 REMARK 500 3 VAL B 81 49.23 -172.54 REMARK 500 3 GLU B 85 126.12 -37.39 REMARK 500 3 SER B 103 -72.42 66.51 REMARK 500 3 ALA B 138 105.67 61.83 REMARK 500 3 ASP C 28 79.82 -108.05 REMARK 500 3 GLN C 63 -80.05 -120.03 REMARK 500 3 LEU C 64 -87.38 52.37 REMARK 500 3 LEU D 84 -39.56 -157.68 REMARK 500 3 GLU D 85 100.77 63.26 REMARK 500 3 SER D 103 -71.71 65.80 REMARK 500 3 ALA D 138 -179.67 59.63 REMARK 500 4 GLN A 63 20.84 -143.84 REMARK 500 4 LEU A 64 45.88 -100.66 REMARK 500 4 VAL B 81 39.81 -155.31 REMARK 500 4 ILE B 83 -61.42 -92.21 REMARK 500 4 VAL B 101 37.08 -96.90 REMARK 500 4 SER B 103 -68.31 68.99 REMARK 500 4 LYS B 137 -75.73 -71.29 REMARK 500 4 ALA B 138 102.91 62.00 REMARK 500 4 LEU C 64 -99.85 -58.06 REMARK 500 4 VAL D 81 32.93 -143.08 REMARK 500 4 ILE D 83 -95.95 -107.91 REMARK 500 4 LEU D 84 -39.65 166.92 REMARK 500 REMARK 500 THIS ENTRY HAS 248 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Y74 RELATED DB: PDB REMARK 900 MLIN-2/MLIN-7 L27 DOMAIN COMPLEX DBREF 1Y76 A 4 65 UNP O55164 MPDZ_RAT 4 65 DBREF 1Y76 C 4 65 UNP O55164 MPDZ_RAT 4 65 DBREF 1Y76 B 80 139 UNP Q8N3R9 MPP5_HUMAN 118 177 DBREF 1Y76 D 80 139 UNP Q8N3R9 MPP5_HUMAN 118 177 SEQRES 1 A 62 ASN PRO ALA ALA GLU LYS MET GLN VAL LEU GLN VAL LEU SEQRES 2 A 62 ASP ARG LEU ARG GLY LYS LEU GLN GLU LYS GLY ASP THR SEQRES 3 A 62 THR GLN ASN GLU LYS LEU SER ALA PHE TYR GLU THR LEU SEQRES 4 A 62 LYS SER PRO LEU PHE ASN GLN ILE LEU THR LEU GLN GLN SEQRES 5 A 62 SER ILE LYS GLN LEU LYS GLY GLN LEU SER SEQRES 1 B 60 ALA VAL LYS ILE LEU GLU ILE GLU ASP LEU PHE SER SER SEQRES 2 B 60 LEU LYS HIS ILE GLN HIS THR LEU VAL ASP SER GLN SER SEQRES 3 B 60 GLN GLU ASP ILE SER LEU LEU LEU GLN LEU VAL GLN ASN SEQRES 4 B 60 LYS ASP PHE GLN ASN ALA PHE LYS ILE HIS ASN ALA ILE SEQRES 5 B 60 THR VAL HIS MET ASN LYS ALA SER SEQRES 1 C 62 ASN PRO ALA ALA GLU LYS MET GLN VAL LEU GLN VAL LEU SEQRES 2 C 62 ASP ARG LEU ARG GLY LYS LEU GLN GLU LYS GLY ASP THR SEQRES 3 C 62 THR GLN ASN GLU LYS LEU SER ALA PHE TYR GLU THR LEU SEQRES 4 C 62 LYS SER PRO LEU PHE ASN GLN ILE LEU THR LEU GLN GLN SEQRES 5 C 62 SER ILE LYS GLN LEU LYS GLY GLN LEU SER SEQRES 1 D 60 ALA VAL LYS ILE LEU GLU ILE GLU ASP LEU PHE SER SER SEQRES 2 D 60 LEU LYS HIS ILE GLN HIS THR LEU VAL ASP SER GLN SER SEQRES 3 D 60 GLN GLU ASP ILE SER LEU LEU LEU GLN LEU VAL GLN ASN SEQRES 4 D 60 LYS ASP PHE GLN ASN ALA PHE LYS ILE HIS ASN ALA ILE SEQRES 5 D 60 THR VAL HIS MET ASN LYS ALA SER HELIX 1 1 ASN A 4 GLY A 27 1 24 HELIX 2 2 GLN A 31 SER A 44 1 14 HELIX 3 3 SER A 44 LEU A 64 1 21 HELIX 4 4 GLU B 85 VAL B 101 1 17 HELIX 5 5 SER B 103 ASN B 118 1 16 HELIX 6 6 ASN B 118 ALA B 138 1 21 HELIX 7 7 PRO C 5 GLY C 27 1 23 HELIX 8 8 GLN C 31 SER C 44 1 14 HELIX 9 9 SER C 44 LEU C 64 1 21 HELIX 10 10 GLU D 85 LEU D 100 1 16 HELIX 11 11 SER D 103 ASN D 118 1 16 HELIX 12 12 ASN D 118 ALA D 138 1 21 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