Header list of 1wqu.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 02-OCT-04 1WQU TITLE SOLUTION STRUCTURE OF THE HUMAN FES SH2 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FES/FPS; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH2 DOMAIN; COMPND 5 SYNONYM: C-FES; COMPND 6 EC: 2.7.1.112; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P040524-01; SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS SH2 DOMAIN, FES, FELINE SARCOMA ONCOGENE, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.SCOTT,D.PANTOJA-UCEDA,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA, AUTHOR 2 M.SHIROUZU,A.TANAKA,S.SUGANO,S.YOKOYAMA,P.GUNTERT,RIKEN STRUCTURAL AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WQU 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WQU 1 VERSN REVDAT 1 14-JUN-05 1WQU 0 JRNL AUTH A.SCOTT,D.PANTOJA-UCEDA,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA, JRNL AUTH 2 M.SHIROUZU,A.TANAKA,S.SUGANO,S.YOKOYAMA,P.GUNTERT JRNL TITL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN FROM THE JRNL TITL 2 HUMAN FELINE SARCOMA ONCOGENE FES JRNL REF J.BIOMOL.NMR V. 31 357 2005 JRNL REFN ISSN 0925-2738 JRNL PMID 15929003 JRNL DOI 10.1007/S10858-005-0946-6 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.SCOTT,D.PANTOJA-UCEDA,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA, REMARK 1 AUTH 2 M.SHIROUZU,A.TANAKA,S.SUGANO,S.YOKOYAMA,P.GUNTERT REMARK 1 TITL NMR ASSIGNMENT OF THE SH2 DOMAIN FROM THE HUMAN FELINE REMARK 1 TITL 2 SARCOMA ONCOGENE FES REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1, OPALP 1.3 REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), KORADI, R., BILLETER, M., REMARK 3 GUNTERT, P. (OPALP) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WQU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000023891. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2MM UNIFORMLY 13C AND 15N REMARK 210 LABELED PROTEIN; 20MM TRIS-HCL REMARK 210 BUFFER; 100MM NACL; 1MM REMARK 210 DITHIOTHREITOL; 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, CYANA 2.0.32 REMARK 210 METHOD USED : AUTOMATED NOESY ASSIGNMENT, REMARK 210 TORSION ANGLE DYNAMICS, ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT 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: 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 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 4 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.2 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 1 ALA A 22 26.89 -74.92 REMARK 500 1 ASP A 56 8.02 56.07 REMARK 500 1 LEU A 67 -61.05 -153.89 REMARK 500 1 ASP A 68 30.65 -78.23 REMARK 500 1 LEU A 73 -33.13 -142.71 REMARK 500 1 GLU A 74 -31.20 -156.93 REMARK 500 1 SER A 99 -39.44 -134.53 REMARK 500 2 VAL A 33 -31.59 -131.12 REMARK 500 2 GLN A 47 37.41 -75.97 REMARK 500 2 ILE A 63 97.02 -67.98 REMARK 500 2 ILE A 64 108.68 -56.38 REMARK 500 2 GLU A 74 -56.48 -155.57 REMARK 500 3 HIS A 14 0.53 -65.60 REMARK 500 3 ALA A 22 25.30 -76.75 REMARK 500 3 GLN A 47 12.70 57.85 REMARK 500 3 ASP A 56 18.72 49.24 REMARK 500 3 ASN A 69 -5.03 70.73 REMARK 500 3 LEU A 73 -36.28 -131.27 REMARK 500 3 GLU A 74 -20.35 -159.69 REMARK 500 4 LEU A 73 -49.39 -142.80 REMARK 500 5 ALA A 22 43.03 -71.82 REMARK 500 5 TRP A 55 -85.89 -152.56 REMARK 500 5 ASP A 56 23.85 -79.24 REMARK 500 5 PRO A 59 92.66 -68.62 REMARK 500 5 LEU A 67 -81.06 -130.09 REMARK 500 5 ASP A 68 37.69 -75.73 REMARK 500 6 SER A 3 -151.60 -108.46 REMARK 500 6 ALA A 22 18.91 38.89 REMARK 500 6 ASP A 56 2.00 55.70 REMARK 500 6 ASP A 68 22.96 49.95 REMARK 500 6 LEU A 73 -78.70 -125.26 REMARK 500 6 THR A 96 141.89 -177.53 REMARK 500 7 VAL A 33 -35.88 -136.21 REMARK 500 7 GLN A 44 107.51 -41.77 REMARK 500 7 TRP A 55 -63.35 -149.20 REMARK 500 7 ASP A 56 42.53 -107.24 REMARK 500 7 LEU A 67 -5.09 -150.28 REMARK 500 7 LEU A 73 -32.59 -150.90 REMARK 500 7 GLU A 74 -71.81 -113.20 REMARK 500 7 SER A 113 102.72 -55.04 REMARK 500 8 SER A 3 -169.58 -75.45 REMARK 500 8 ALA A 22 26.68 -66.91 REMARK 500 8 ASP A 68 18.00 56.63 REMARK 500 8 ASN A 69 2.99 91.90 REMARK 500 8 LEU A 73 -83.90 -127.20 REMARK 500 8 PRO A 111 38.43 -68.26 REMARK 500 9 SER A 2 4.27 -61.04 REMARK 500 9 ALA A 22 11.40 46.66 REMARK 500 9 LYS A 46 24.23 -65.45 REMARK 500 9 TRP A 55 -97.88 -145.30 REMARK 500 REMARK 500 THIS ENTRY HAS 132 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 2 TYR A 19 0.08 SIDE CHAIN REMARK 500 2 ARG A 72 0.09 SIDE CHAIN REMARK 500 2 ARG A 105 0.09 SIDE CHAIN REMARK 500 3 ARG A 72 0.12 SIDE CHAIN REMARK 500 5 TYR A 19 0.09 SIDE CHAIN REMARK 500 5 ARG A 60 0.09 SIDE CHAIN REMARK 500 7 ARG A 105 0.08 SIDE CHAIN REMARK 500 12 ARG A 41 0.08 SIDE CHAIN REMARK 500 15 ARG A 25 0.09 SIDE CHAIN REMARK 500 15 ARG A 105 0.10 SIDE CHAIN REMARK 500 18 ARG A 41 0.09 SIDE CHAIN REMARK 500 20 ARG A 41 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001002011.2 RELATED DB: TARGETDB DBREF 1WQU A 8 108 UNP P07332 FES_HUMAN 450 550 SEQADV 1WQU GLY A 1 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 2 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 3 UNP P07332 CLONING ARTIFACT SEQADV 1WQU GLY A 4 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 5 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 6 UNP P07332 CLONING ARTIFACT SEQADV 1WQU GLY A 7 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 109 UNP P07332 CLONING ARTIFACT SEQADV 1WQU GLY A 110 UNP P07332 CLONING ARTIFACT SEQADV 1WQU PRO A 111 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 112 UNP P07332 CLONING ARTIFACT SEQADV 1WQU SER A 113 UNP P07332 CLONING ARTIFACT SEQADV 1WQU GLY A 114 UNP P07332 CLONING ARTIFACT SEQRES 1 A 114 GLY SER SER GLY SER SER GLY GLU VAL GLN LYS PRO LEU SEQRES 2 A 114 HIS GLU GLN LEU TRP TYR HIS GLY ALA ILE PRO ARG ALA SEQRES 3 A 114 GLU VAL ALA GLU LEU LEU VAL HIS SER GLY ASP PHE LEU SEQRES 4 A 114 VAL ARG GLU SER GLN GLY LYS GLN GLU TYR VAL LEU SER SEQRES 5 A 114 VAL LEU TRP ASP GLY LEU PRO ARG HIS PHE ILE ILE GLN SEQRES 6 A 114 SER LEU ASP ASN LEU TYR ARG LEU GLU GLY GLU GLY PHE SEQRES 7 A 114 PRO SER ILE PRO LEU LEU ILE ASP HIS LEU LEU SER THR SEQRES 8 A 114 GLN GLN PRO LEU THR LYS LYS SER GLY VAL VAL LEU HIS SEQRES 9 A 114 ARG ALA VAL PRO SER GLY PRO SER SER GLY HELIX 1 1 GLY A 7 LYS A 11 5 5 HELIX 2 2 PRO A 12 GLN A 16 5 5 HELIX 3 3 PRO A 24 GLU A 30 1 7 HELIX 4 4 SER A 80 GLN A 92 1 13 SHEET 1 A 4 TYR A 19 GLY A 21 0 SHEET 2 A 4 ASP A 37 GLU A 42 1 O GLU A 42 N GLY A 21 SHEET 3 A 4 TYR A 49 TRP A 55 -1 O SER A 52 N LEU A 39 SHEET 4 A 4 LEU A 58 ILE A 63 -1 O PHE A 62 N LEU A 51 SHEET 1 B 3 TYR A 19 GLY A 21 0 SHEET 2 B 3 ASP A 37 GLU A 42 1 O GLU A 42 N GLY A 21 SHEET 3 B 3 ARG A 105 ALA A 106 1 O ARG A 105 N PHE A 38 SHEET 1 C 2 GLN A 65 SER A 66 0 SHEET 2 C 2 TYR A 71 ARG A 72 -1 O ARG A 72 N GLN A 65 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