Header list of 1w1n.pdb file
Complete list - 2 20 Bytes
HEADER TRANSFERASE 23-JUN-04 1W1N TITLE THE SOLUTION STRUCTURE OF THE FATC DOMAIN OF THE PROTEIN KINASE TOR1 TITLE 2 FROM YEAST COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE TOR1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FATC, RESIDUES 2438-2470; COMPND 5 SYNONYM: PI3-KINASE RELATED, PTDINS-3-KINASE RELATED, PI3K RELATED; COMPND 6 EC: 2.7.1.137; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: DISULFIDE BOND BETWEEN RESIDUES C2460 (23) AND C2467 COMPND 9 (30) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA; SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEV2 KEYWDS TOR, TARGET OF RAPAMYCIN, SER/THR KINASE, REDOX-REGULATION, DISULFIDE KEYWDS 2 BOND, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.A.DAMES,J.M.MULET,K.RATHGEB-SZABO,M.N.HALL,S.GRZESIEK REVDAT 6 02-MAY-18 1W1N 1 SOURCE JRNL REMARK REVDAT 5 24-FEB-09 1W1N 1 VERSN REVDAT 4 19-SEP-06 1W1N 1 SEQRES REVDAT 3 25-MAY-05 1W1N 1 JRNL REVDAT 2 01-APR-05 1W1N 1 ATOM REVDAT 1 16-MAR-05 1W1N 0 JRNL AUTH S.A.DAMES,J.M.MULET,K.RATHGEB-SZABO,M.N.HALL,S.GRZESIEK JRNL TITL THE SOLUTION STRUCTURE OF THE FATC DOMAIN OF THE PROTEIN JRNL TITL 2 KINASE TARGET OF RAPAMYCIN SUGGESTS A ROLE FOR JRNL TITL 3 REDOX-DEPENDENT STRUCTURAL AND CELLULAR STABILITY. JRNL REF J. BIOL. CHEM. V. 280 20558 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15772072 JRNL DOI 10.1074/JBC.M501116200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH REMARK 3 AUTHORS : BRUNGER, SCHWIETERS REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SHIFTS HAVE BEEN DEPOSITED AT BMRB REMARK 3 UNDER ACCESSION NUMBER 6228 REMARK 4 REMARK 4 1W1N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1290020211. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 298.0 REMARK 210 PH : 6.0; 6.0; 6.0 REMARK 210 IONIC STRENGTH : 10; 10; 10 REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM; 1.0 ATM REMARK 210 SAMPLE CONTENTS : NULL; NULL; NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC; 3D-CBCANH; 3D REMARK 210 CBCA(CO)NH; 3D-HBHACBCACONH; 3D- REMARK 210 CCONH-TOCSY; 3D HNCO; 3D HNHA; REMARK 210 3D-15N-NOESY; 3D-15N- ROESY; REMARK 210 13CO-13CG -HSQC; 15N- 13CG-HSQC; REMARK 210 15N-T1; 15N-T2; 1H- 15N-NOE; 13- REMARK 210 HSQC; 3D-13C- NOESY; 3D HCCH- REMARK 210 TOCSY; 3D- HACAHB-COSY; 15N-IPAP- REMARK 210 HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XPLOR-NIH, NMRVIEW REMARK 210 METHOD USED : RESTRAINED TORSION ANGLE REMARK 210 MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND LEAST REMARK 210 RESTRAINED VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING MULTINUCLEAR NMR REMARK 210 EXPERIMENTS ON 15- OR 15N-13C-LABELED YEAST TOR1 FATC. 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 400 REMARK 400 COMPOUND REMARK 400 PHOSPHATIDYLINOSITOL 3-KINASE HOMOLOG REQUIRED FOR G1 REMARK 400 PROGRESSION. TARGET OF THE ANTIBIOTIC RAPAMYCIN. 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 ILE A 19 H CYS A 23 1.58 REMARK 500 O LYS A 11 H GLN A 15 1.58 REMARK 500 O GLN A 15 HG SER A 18 1.59 REMARK 500 O GLN A 14 H SER A 18 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 PRO A 6 40.67 -71.43 REMARK 500 1 LYS A 11 -33.32 -34.41 REMARK 500 1 SER A 18 -72.45 -43.42 REMARK 500 1 TYR A 26 -148.67 -98.90 REMARK 500 2 GLU A 2 -143.65 37.13 REMARK 500 2 ASP A 4 39.48 -153.04 REMARK 500 2 PRO A 6 29.20 -70.08 REMARK 500 2 LYS A 11 -38.68 -34.82 REMARK 500 2 SER A 18 -72.51 -43.41 REMARK 500 2 PRO A 31 47.10 -77.14 REMARK 500 3 GLU A 2 -147.37 51.35 REMARK 500 3 ASP A 4 57.33 -171.42 REMARK 500 3 PRO A 6 29.73 -70.64 REMARK 500 3 LYS A 11 -39.47 -34.98 REMARK 500 3 SER A 18 -75.12 -45.75 REMARK 500 3 TYR A 26 -138.98 -95.28 REMARK 500 4 GLU A 2 -82.38 -58.54 REMARK 500 4 PRO A 6 21.66 -72.95 REMARK 500 4 ASP A 10 -73.29 -58.04 REMARK 500 4 LYS A 11 -36.44 -34.02 REMARK 500 4 SER A 18 -78.11 -46.69 REMARK 500 4 TYR A 26 -137.66 -96.15 REMARK 500 5 GLU A 2 -147.90 -80.33 REMARK 500 5 ASP A 4 39.30 -173.31 REMARK 500 5 PRO A 6 24.56 -71.99 REMARK 500 5 LYS A 11 -31.68 -34.47 REMARK 500 5 SER A 18 -77.30 -43.93 REMARK 500 5 TRP A 29 65.27 -65.41 REMARK 500 5 PHE A 32 -32.19 -139.04 REMARK 500 6 GLU A 2 -15.55 84.35 REMARK 500 6 ASP A 4 41.33 -154.23 REMARK 500 6 PRO A 6 23.67 -68.24 REMARK 500 6 LYS A 11 -39.77 -34.58 REMARK 500 6 SER A 18 -73.53 -44.79 REMARK 500 6 TYR A 26 -137.58 -89.22 REMARK 500 6 PHE A 32 -35.29 -135.50 REMARK 500 7 ASP A 4 65.19 -173.00 REMARK 500 7 PRO A 6 29.10 -73.04 REMARK 500 7 ASP A 10 -70.52 -59.20 REMARK 500 7 SER A 18 -80.95 -46.49 REMARK 500 7 TYR A 26 -141.74 -95.67 REMARK 500 7 PHE A 32 -37.06 -137.36 REMARK 500 8 GLU A 2 -6.33 84.36 REMARK 500 8 PRO A 6 40.02 -72.19 REMARK 500 8 LYS A 11 -34.71 -34.37 REMARK 500 8 SER A 18 -80.96 -44.22 REMARK 500 8 TRP A 29 61.13 -67.01 REMARK 500 9 GLU A 2 -85.77 53.75 REMARK 500 9 ASP A 4 64.30 -157.78 REMARK 500 9 PRO A 6 32.47 -71.65 REMARK 500 REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS. 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 1 ARG A 21 0.32 SIDE CHAIN REMARK 500 2 ARG A 21 0.09 SIDE CHAIN REMARK 500 3 ARG A 21 0.20 SIDE CHAIN REMARK 500 4 ARG A 21 0.24 SIDE CHAIN REMARK 500 5 ARG A 21 0.29 SIDE CHAIN REMARK 500 7 ARG A 21 0.31 SIDE CHAIN REMARK 500 8 ARG A 21 0.30 SIDE CHAIN REMARK 500 9 ARG A 21 0.29 SIDE CHAIN REMARK 500 10 ARG A 21 0.11 SIDE CHAIN REMARK 500 11 ARG A 21 0.31 SIDE CHAIN REMARK 500 13 ARG A 21 0.26 SIDE CHAIN REMARK 500 14 ARG A 21 0.16 SIDE CHAIN REMARK 500 15 ARG A 21 0.23 SIDE CHAIN REMARK 500 16 ARG A 21 0.32 SIDE CHAIN REMARK 500 17 ARG A 21 0.29 SIDE CHAIN REMARK 500 18 ARG A 21 0.17 SIDE CHAIN REMARK 500 19 ARG A 21 0.18 SIDE CHAIN REMARK 500 20 ARG A 21 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1W1N A 1 33 UNP P35169 TOR1_YEAST 2438 2470 SEQRES 1 A 33 ASN GLU LEU ASP VAL PRO GLU GLN VAL ASP LYS LEU ILE SEQRES 2 A 33 GLN GLN ALA THR SER ILE GLU ARG LEU CYS GLN HIS TYR SEQRES 3 A 33 ILE GLY TRP CYS PRO PHE TRP HELIX 1 1 PRO A 6 GLN A 24 1 19 SSBOND 1 CYS A 23 CYS A 30 1555 1555 2.02 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 - 2 20 Bytes