Header list of 1fu6.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 14-SEP-00 1FU6 TITLE NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 321 TO 431 OF P85, N-SH2 (SRC HOMOLOGY 2) DOMAIN; COMPND 5 SYNONYM: N-SH2 (SRC HOMOLOGY 2) DOMAIN OF P85 SUBUNIT OF P13-KINASE COMPND 6 (PHOSPHOINOSITOL 3-KINASE), PI3-KINASE P85-ALPHA SUBUNIT, PTDINS-3- COMPND 7 KINASE P85-ALPHA, PI3K; COMPND 8 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 KEYWDS CENTRAL BETA-SHEET WITH TWO FLANKING ALPHA-HELICES, PROTEIN BINDING EXPDTA SOLUTION NMR AUTHOR T.WEBER,B.SCHAFFHAUSEN,Y.LIU,U.L.GUENTHER REVDAT 4 23-FEB-22 1FU6 1 REMARK SEQADV REVDAT 3 24-FEB-09 1FU6 1 VERSN REVDAT 2 01-APR-03 1FU6 1 JRNL REVDAT 1 21-FEB-01 1FU6 0 JRNL AUTH T.WEBER,B.SCHAFFHAUSEN,Y.LIU,U.L.GUNTHER JRNL TITL NMR STRUCTURE OF THE N-SH2 OF THE P85 SUBUNIT OF JRNL TITL 2 PHOSPHOINOSITIDE 3-KINASE COMPLEXED TO A DOUBLY JRNL TITL 3 PHOSPHORYLATED PEPTIDE REVEALS A SECOND PHOSPHOTYROSINE JRNL TITL 4 BINDING SITE. JRNL REF BIOCHEMISTRY V. 39 15860 2000 JRNL REFN ISSN 0006-2960 JRNL PMID 11123912 JRNL DOI 10.1021/BI001474D REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRLAB, DISCOVER REMARK 3 AUTHORS : ULRICH GUENTHER, CHRISTIAN LUDWIG AND HEINZ REMARK 3 RUETERJANS (NMRLAB), MSI (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WITH THE LOWEST ENERGY IS REMARK 3 PRESENTED. REMARK 4 REMARK 4 1FU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-00. REMARK 100 THE DEPOSITION ID IS D_1000011904. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 0.1MM REMARK 210 PRESSURE : 1 BAR REMARK 210 SAMPLE CONTENTS : 1.5MM N-SH2 15N, 13C; 0.1MM KCL; REMARK 210 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PRONTO, NMR2ST, DYANA REMARK 210 METHOD USED : THE STRUCTURES WERE ENERGY REMARK 210 MINIMIZED WITH MSI DISCOVER. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 110 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NOESY ASSIGNMENTS WERE OBTAINED BY A SEMI-AUTOMATIC REMARK 210 PROCEDURE EMPLOYING A PROGRAM FROM PRISTOVSEK [PRISTOVSEK, P. & REMARK 210 KIDRIC, J. (1997) BIOPOL. 42, 671-679)]. 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: 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 HG1 THR A 42 OD1 ASP A 47 1.34 REMARK 500 OD2 ASP A 29 HH TYR A 106 1.38 REMARK 500 HG SER A 92 OD1 ASP A 101 1.38 REMARK 500 OD2 ASP A 47 HH TYR A 48 1.42 REMARK 500 OE2 GLU A 22 HZ2 LYS A 110 1.51 REMARK 500 O ASP A 39 HG1 THR A 49 1.52 REMARK 500 OD2 ASP A 67 HZ2 LYS A 69 1.55 REMARK 500 O GLU A 12 HG SER A 109 1.56 REMARK 500 O ALA A 40 HG SER A 41 1.57 REMARK 500 HG1 THR A 34 O TYR A 106 1.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 65 CG HIS A 65 CD2 0.055 REMARK 500 TYR A 111 C TYR A 111 OXT 0.138 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 HIS A 65 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES REMARK 500 HIS A 87 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 TYR A 106 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES 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 GLN A 9 -28.46 -144.17 REMARK 500 ASP A 10 70.04 -162.19 REMARK 500 GLU A 12 36.56 -70.08 REMARK 500 TRP A 13 -58.23 -166.12 REMARK 500 TRP A 15 -56.56 -123.26 REMARK 500 ILE A 18 -159.85 -131.33 REMARK 500 SER A 19 -157.37 -120.52 REMARK 500 ARG A 28 -79.64 -104.07 REMARK 500 LEU A 36 -51.89 -152.16 REMARK 500 VAL A 37 95.00 99.21 REMARK 500 ASP A 39 -141.63 -91.95 REMARK 500 SER A 41 55.07 -156.97 REMARK 500 LYS A 43 -60.58 -157.24 REMARK 500 MET A 44 -84.33 -91.03 REMARK 500 ASP A 47 -68.56 -97.44 REMARK 500 SER A 60 96.80 -60.50 REMARK 500 ILE A 61 75.43 -106.32 REMARK 500 ARG A 66 -91.11 59.55 REMARK 500 LYS A 69 -152.90 -92.44 REMARK 500 PHE A 72 -65.26 -95.28 REMARK 500 SER A 80 114.45 -161.36 REMARK 500 LEU A 84 42.67 -75.52 REMARK 500 ILE A 85 -48.48 -167.39 REMARK 500 ASN A 90 30.45 -90.30 REMARK 500 GLU A 91 -77.57 -157.21 REMARK 500 SER A 92 142.53 -175.38 REMARK 500 TYR A 96 -70.46 -66.84 REMARK 500 LEU A 100 -32.96 -155.74 REMARK 500 ASP A 101 75.66 -4.49 REMARK 500 VAL A 102 -152.38 -86.45 REMARK 500 LYS A 103 54.83 -171.25 REMARK 500 LEU A 104 36.84 39.52 REMARK 500 TYR A 106 60.63 -151.00 REMARK 500 SER A 109 77.96 -170.22 REMARK 500 LYS A 110 -63.37 71.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR A 48 THR A 49 -145.89 REMARK 500 ASP A 101 VAL A 102 146.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR A 48 0.19 SIDE CHAIN REMARK 500 ARG A 66 0.16 SIDE CHAIN REMARK 500 TYR A 70 0.07 SIDE CHAIN REMARK 500 TYR A 96 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FU5 RELATED DB: PDB REMARK 900 1FU5 IS NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3- REMARK 900 KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM REMARK 900 POLYOMAVIRUS MIDDLE T ANTIGEN DBREF 1FU6 A 1 111 UNP Q63787 P85A_RAT 321 431 SEQADV 1FU6 SER A 60 UNP Q63787 LEU 380 CONFLICT SEQRES 1 A 111 GLY MET ASN ASN ASN MET SER LEU GLN ASP ALA GLU TRP SEQRES 2 A 111 TYR TRP GLY ASP ILE SER ARG GLU GLU VAL ASN GLU LYS SEQRES 3 A 111 LEU ARG ASP THR ALA ASP GLY THR PHE LEU VAL ARG ASP SEQRES 4 A 111 ALA SER THR LYS MET HIS GLY ASP TYR THR LEU THR LEU SEQRES 5 A 111 ARG LYS GLY GLY ASN ASN LYS SER ILE LYS ILE PHE HIS SEQRES 6 A 111 ARG ASP GLY LYS TYR GLY PHE SER ASP PRO LEU THR PHE SEQRES 7 A 111 ASN SER VAL VAL GLU LEU ILE ASN HIS TYR ARG ASN GLU SEQRES 8 A 111 SER LEU ALA GLN TYR ASN PRO LYS LEU ASP VAL LYS LEU SEQRES 9 A 111 LEU TYR PRO VAL SER LYS TYR HELIX 1 1 ARG A 20 LEU A 27 1 8 HELIX 2 2 VAL A 82 ASN A 90 1 9 SHEET 1 A 2 THR A 51 LYS A 54 0 SHEET 2 A 2 ASN A 57 SER A 60 -1 O ASN A 57 N LYS A 54 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
Complete list - 23 20 Bytes