Header list of 1ktm.pdb file
Complete list - c 21 2 Bytes
HEADER TRANSFERASE 16-JAN-02 1KTM TITLE SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FAT DOMAIN (RESIDUES 916-1053); COMPND 5 SYNONYM: FADK 1, PP125FAK; COMPND 6 EC: 2.7.1.112; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET28A KEYWDS FOCAL ADHESION KINASE, FAK, FOCAL ADHENSION TARGETING DOMAIN, FAT, KEYWDS 2 HELIX BUNDLE, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR G.LIU,C.GUIBAO,J.ZHENG REVDAT 5 21-DEC-22 1KTM 1 SEQADV REVDAT 4 23-FEB-22 1KTM 1 REMARK REVDAT 3 24-FEB-09 1KTM 1 VERSN REVDAT 2 04-FEB-03 1KTM 1 JRNL REVDAT 1 16-JAN-03 1KTM 0 JRNL AUTH G.LIU,C.GUIBAO,J.ZHENG JRNL TITL STRUCTURAL INSIGHT INTO THE MECHANISMS OF TARGETING AND JRNL TITL 2 SIGNALING OF FOCAL ADHESION KINASE JRNL REF MOL.CELL.BIOL. V. 22 2751 2002 JRNL REFN ISSN 0270-7306 JRNL PMID 11909967 JRNL DOI 10.1128/MCB.22.8.2751-2760.2002 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : VARIAN ASSOC.,INC AND VARIAN, INC. (VNMR), REMARK 3 GUENTERT ET AL. (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KTM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015331. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE BUFFER REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1.5 MM FAT DOMAIN U-15N, 10MM REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10% REMARK 210 D2O; 2.0 MM FAT U-15N, 13C, 10MM REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10% REMARK 210 D2O' REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; REMARK 210 3D_13C-SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; 4D_13C/15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, XEASY 3.1, DYANA 1.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 270 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 O ALA A 1024 H LEU A 1028 1.50 REMARK 500 O LYS A 1033 H ASP A 1037 1.52 REMARK 500 O LEU A 1036 H ASP A 1040 1.53 REMARK 500 O ALA A 935 H MET A 939 1.53 REMARK 500 O LEU A 1004 H TYR A 1008 1.53 REMARK 500 O LEU A 995 H ILE A 999 1.54 REMARK 500 O ALA A 1027 H ASP A 1031 1.54 REMARK 500 O THR A 930 H LYS A 934 1.56 REMARK 500 O VAL A 1030 H ASN A 1034 1.59 REMARK 500 O GLN A 1014 H LYS A 1018 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 LEU A 918 46.30 -88.76 REMARK 500 1 ASP A 919 42.03 -91.75 REMARK 500 1 ARG A 920 -73.20 -87.88 REMARK 500 1 LYS A 934 -31.04 -39.98 REMARK 500 1 VAL A 936 -38.91 -37.98 REMARK 500 1 ALA A 946 122.23 -30.46 REMARK 500 1 SER A 979 -24.13 156.84 REMARK 500 1 HIS A 981 -77.84 -82.36 REMARK 500 1 SER A 993 -70.42 -40.24 REMARK 500 1 TYR A1008 32.60 -88.89 REMARK 500 1 THR A1011 -78.71 -70.56 REMARK 500 1 SER A1012 -34.10 173.98 REMARK 500 1 ILE A1047 -71.71 -44.98 REMARK 500 1 GLN A1049 -65.85 -169.71 REMARK 500 1 SER A1050 90.77 -175.53 REMARK 500 1 PRO A1052 -80.82 -75.00 REMARK 500 2 ASP A 919 -64.60 -99.78 REMARK 500 2 GLU A 938 -38.72 -33.66 REMARK 500 2 ALA A 946 128.33 -32.47 REMARK 500 2 MET A 954 -71.95 -34.08 REMARK 500 2 LYS A 956 -32.11 -38.89 REMARK 500 2 ALA A 978 -173.93 -58.96 REMARK 500 2 SER A 979 -44.21 85.51 REMARK 500 2 HIS A 981 -84.03 -83.97 REMARK 500 2 THR A1011 -83.55 -73.05 REMARK 500 2 SER A1012 -36.83 -178.32 REMARK 500 2 SER A1050 -77.55 173.42 REMARK 500 3 MET A 939 -71.25 -49.79 REMARK 500 3 ALA A 946 133.26 -34.79 REMARK 500 3 LYS A 956 -34.29 -39.24 REMARK 500 3 ALA A 978 173.35 -47.17 REMARK 500 3 SER A 993 -70.82 -43.24 REMARK 500 3 TYR A1008 39.63 -87.65 REMARK 500 3 MET A1010 -32.11 -36.36 REMARK 500 3 GLN A1014 -75.07 -35.90 REMARK 500 3 SER A1048 58.52 -100.38 REMARK 500 3 SER A1050 -68.88 172.31 REMARK 500 4 ASP A 919 -174.82 -56.07 REMARK 500 4 SER A 921 -86.02 -85.48 REMARK 500 4 ILE A 943 -61.85 -96.51 REMARK 500 4 HIS A 981 -110.71 -84.46 REMARK 500 4 MET A1010 -32.64 -36.76 REMARK 500 4 THR A1011 -139.32 -96.96 REMARK 500 4 GLN A1014 -83.28 -36.86 REMARK 500 4 GLN A1015 -32.30 -38.71 REMARK 500 4 GLN A1049 88.79 -162.01 REMARK 500 4 SER A1050 85.83 42.76 REMARK 500 5 ASP A 919 -172.37 -54.73 REMARK 500 5 ARG A 920 36.02 -88.62 REMARK 500 5 ILE A 943 -60.36 -93.89 REMARK 500 REMARK 500 THIS ENTRY HAS 349 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1KTM A 916 1053 UNP Q00944 FAK1_CHICK 916 1053 SEQADV 1KTM MET A 915 UNP Q00944 INITIATING METHIONINE SEQRES 1 A 139 MET ALA ASN LEU ASP ARG SER ASN ASP LYS VAL TYR GLU SEQRES 2 A 139 ASN VAL THR GLY LEU VAL LYS ALA VAL ILE GLU MET SER SEQRES 3 A 139 SER LYS ILE GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO SEQRES 4 A 139 MET VAL LYS GLU VAL GLY LEU ALA LEU ARG THR LEU LEU SEQRES 5 A 139 ALA THR VAL ASP GLU SER LEU PRO VAL LEU PRO ALA SER SEQRES 6 A 139 THR HIS ARG GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SEQRES 7 A 139 SER ASP LEU ALA GLU LEU ILE ASN LYS MET LYS LEU ALA SEQRES 8 A 139 GLN GLN TYR VAL MET THR SER LEU GLN GLN GLU TYR LYS SEQRES 9 A 139 LYS GLN MET LEU THR ALA ALA HIS ALA LEU ALA VAL ASP SEQRES 10 A 139 ALA LYS ASN LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU SEQRES 11 A 139 LYS MET ILE SER GLN SER ARG PRO HIS HELIX 1 1 SER A 921 LYS A 942 1 22 HELIX 2 2 PRO A 947 LEU A 976 1 30 HELIX 3 3 HIS A 981 GLN A 1006 1 26 HELIX 4 4 LEU A 1013 SER A 1048 1 36 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 - c 21 2 Bytes