Header list of 2d85.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN, PROTEIN BINDING 02-DEC-05 2D85 TITLE SOLUTION STRUCTURE OF THE FOURTH CH DOMAIN FROM HUMAN L-PLASTIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: L-PLASTIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CH DOMAIN; COMPND 5 SYNONYM: LYMPHOCYTE CYTOSOLIC PROTEIN 1, LCP-1, LC64P; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: LCP1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050111-01; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS ALL ALPHA, CALPONIN HOMOLOGY DOMAIN, ACTIN BINDING, STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, STRUCTURAL PROTEIN, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2D85 1 REMARK SEQADV REVDAT 2 24-FEB-09 2D85 1 VERSN REVDAT 1 02-JUN-06 2D85 0 JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FOURTH CH DOMAIN FROM HUMAN JRNL TITL 2 L-PLASTIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2D85 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025106. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 220MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.14MM CH DOMAIN U-15N,13C; 20MM REMARK 210 D-TRIS-HCL(PH 7.0); 200MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.932, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINTED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LOWEST ENERGY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 SER A 2 42.50 -81.75 REMARK 500 1 ASN A 8 162.21 -41.42 REMARK 500 1 LEU A 65 176.84 -50.74 REMARK 500 1 ASP A 67 -34.35 -37.61 REMARK 500 1 ASN A 72 -38.23 -39.73 REMARK 500 1 ARG A 87 99.41 -34.50 REMARK 500 1 VAL A 98 51.71 33.77 REMARK 500 1 VAL A 106 -72.62 -66.17 REMARK 500 1 PRO A 121 83.70 -69.74 REMARK 500 2 LYS A 33 40.15 -94.59 REMARK 500 2 ASN A 64 38.21 34.70 REMARK 500 2 LEU A 65 150.85 -41.79 REMARK 500 2 ASP A 67 -34.24 -34.19 REMARK 500 2 ARG A 87 98.04 -57.38 REMARK 500 2 TYR A 89 59.02 -119.34 REMARK 500 2 VAL A 98 54.55 36.64 REMARK 500 2 MET A 115 88.75 -52.18 REMARK 500 2 SER A 119 127.20 -36.00 REMARK 500 2 SER A 122 42.17 35.52 REMARK 500 3 ASN A 8 178.32 -51.11 REMARK 500 3 GLU A 24 43.59 72.43 REMARK 500 3 LYS A 61 -60.63 -93.73 REMARK 500 3 THR A 62 27.25 40.43 REMARK 500 3 LEU A 65 153.34 -45.46 REMARK 500 3 ASP A 67 -33.40 -34.46 REMARK 500 3 LYS A 70 -39.99 -37.77 REMARK 500 3 ALA A 86 130.95 -175.06 REMARK 500 3 TYR A 89 43.85 36.12 REMARK 500 3 GLU A 93 -32.19 -39.43 REMARK 500 3 VAL A 98 48.62 33.93 REMARK 500 4 SER A 6 127.58 -36.65 REMARK 500 4 ASN A 8 62.59 -115.48 REMARK 500 4 THR A 19 -37.62 -39.90 REMARK 500 4 ASP A 67 -31.59 -38.16 REMARK 500 4 ALA A 86 103.60 -34.44 REMARK 500 4 ARG A 87 171.60 -55.81 REMARK 500 5 SER A 5 159.32 -48.63 REMARK 500 5 ASN A 8 -175.05 -61.71 REMARK 500 5 GLU A 24 37.34 74.00 REMARK 500 5 LYS A 33 43.58 -105.94 REMARK 500 5 LYS A 61 -60.72 -104.94 REMARK 500 5 ASN A 64 47.47 36.06 REMARK 500 5 ASP A 67 -32.30 -38.70 REMARK 500 5 ALA A 86 129.63 -173.55 REMARK 500 5 ASN A 99 99.82 -37.93 REMARK 500 6 GLU A 24 42.83 71.46 REMARK 500 6 PHE A 32 -29.04 -38.17 REMARK 500 6 LYS A 33 43.13 -99.04 REMARK 500 6 LYS A 61 -62.14 -91.12 REMARK 500 6 ASN A 64 36.81 35.16 REMARK 500 REMARK 500 THIS ENTRY HAS 205 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001003823.1 RELATED DB: TARGETDB DBREF 2D85 A 8 118 UNP P13796 PLSL_HUMAN 517 627 SEQADV 2D85 GLY A 1 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 2 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 3 UNP P13796 CLONING ARTIFACT SEQADV 2D85 GLY A 4 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 5 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 6 UNP P13796 CLONING ARTIFACT SEQADV 2D85 GLY A 7 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 119 UNP P13796 CLONING ARTIFACT SEQADV 2D85 GLY A 120 UNP P13796 CLONING ARTIFACT SEQADV 2D85 PRO A 121 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 122 UNP P13796 CLONING ARTIFACT SEQADV 2D85 SER A 123 UNP P13796 CLONING ARTIFACT SEQADV 2D85 GLY A 124 UNP P13796 CLONING ARTIFACT SEQRES 1 A 124 GLY SER SER GLY SER SER GLY ASN ASP ASP ILE ILE VAL SEQRES 2 A 124 ASN TRP VAL ASN GLU THR LEU ARG GLU ALA GLU LYS SER SEQRES 3 A 124 SER SER ILE SER SER PHE LYS ASP PRO LYS ILE SER THR SEQRES 4 A 124 SER LEU PRO VAL LEU ASP LEU ILE ASP ALA ILE GLN PRO SEQRES 5 A 124 GLY SER ILE ASN TYR ASP LEU LEU LYS THR GLU ASN LEU SEQRES 6 A 124 ASN ASP ASP GLU LYS LEU ASN ASN ALA LYS TYR ALA ILE SEQRES 7 A 124 SER MET ALA ARG LYS ILE GLY ALA ARG VAL TYR ALA LEU SEQRES 8 A 124 PRO GLU ASP LEU VAL GLU VAL ASN PRO LYS MET VAL MET SEQRES 9 A 124 THR VAL PHE ALA CYS LEU MET GLY LYS GLY MET LYS ARG SEQRES 10 A 124 VAL SER GLY PRO SER SER GLY HELIX 1 1 ASP A 10 GLU A 24 1 15 HELIX 2 2 PRO A 35 THR A 39 5 5 HELIX 3 3 SER A 40 GLN A 51 1 12 HELIX 4 4 ASN A 66 GLY A 85 1 20 HELIX 5 5 LEU A 91 VAL A 96 1 6 HELIX 6 6 ASN A 99 MET A 104 1 6 HELIX 7 7 THR A 105 GLY A 112 1 8 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 9 2 Bytes