Header list of 1ul7.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 10-SEP-03 1UL7 TITLE SOLUTION STRUCTURE OF KINASE ASSOCIATED DOMAIN 1 OF MOUSE TITLE 2 MAP/MICROTUBULE AFFINITY-REGULATING KINASE 3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAP/MICROTUBULE AFFINITY-REGULATING KINASE 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: KINASE ASSOCIATED DOMAIN 1; COMPND 5 SYNONYM: MPK-10, ELKL MOTIF KINASE 2; COMPND 6 EC: 2.7.11.1; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 1600015G02, MARK3, EMK2, MPK10; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021202-01; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS KA1 DOMAIN, ELKL MOTIF, MARK3, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.TOCHIO,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 5 02-MAR-22 1UL7 1 REMARK SEQADV REVDAT 4 24-FEB-09 1UL7 1 VERSN REVDAT 3 28-NOV-06 1UL7 1 JRNL REVDAT 2 29-AUG-06 1UL7 1 COMPND DBREF SEQADV REMARK REVDAT 2 2 1 AUTHOR KEYWDS REVDAT 1 10-MAR-04 1UL7 0 JRNL AUTH N.TOCHIO,S.KOSHIBA,N.KOBAYASHI,M.INOUE,T.YABUKI,M.AOKI, JRNL AUTH 2 E.SEKI,T.MATSUDA,Y.TOMO,Y.MOTODA,A.KOBAYASHI,A.TANAKA, JRNL AUTH 3 Y.HAYASHIZAKI,T.TERADA,M.SHIROUZU,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE KINASE-ASSOCIATED DOMAIN 1 OF JRNL TITL 2 MOUSE MICROTUBULE-ASSOCIATED PROTEIN/MICROTUBULE JRNL TITL 3 AFFINITY-REGULATING KINASE 3 JRNL REF PROTEIN SCI. V. 15 2534 2006 JRNL REFN ISSN 0961-8368 JRNL PMID 17075132 JRNL DOI 10.1110/PS.062391106 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), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UL7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000005950. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0MM KA1 DOMAIN U-15N, 13C; REMARK 210 20MM PHOSPHATE BUFFER NA; 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N 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 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.853, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS 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, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, TARGET REMARK 210 FUNCTION 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 THR A 10 132.95 -174.05 REMARK 500 1 ASN A 35 44.69 -85.43 REMARK 500 1 ASN A 36 47.17 35.11 REMARK 500 1 SER A 73 51.70 -112.62 REMARK 500 1 ALA A 97 -26.50 -39.65 REMARK 500 1 ASN A 98 -63.68 -97.52 REMARK 500 1 LEU A 100 93.19 -40.59 REMARK 500 2 ARG A 42 -71.75 -89.05 REMARK 500 2 LEU A 69 144.06 -34.41 REMARK 500 2 SER A 73 37.59 -85.22 REMARK 500 2 ILE A 82 -58.73 -125.96 REMARK 500 2 ASN A 98 -72.65 -72.58 REMARK 500 2 GLU A 99 -35.91 -38.18 REMARK 500 3 SER A 6 98.69 -59.40 REMARK 500 3 LYS A 14 -59.14 -133.37 REMARK 500 3 ASP A 20 152.42 -46.97 REMARK 500 3 ASN A 35 40.15 -88.53 REMARK 500 3 ASN A 36 40.94 34.80 REMARK 500 3 ARG A 42 -71.92 -90.19 REMARK 500 3 ASP A 53 58.32 -102.39 REMARK 500 3 SER A 73 48.16 -100.90 REMARK 500 3 ILE A 82 -51.18 -132.64 REMARK 500 3 LEU A 100 100.98 -39.85 REMARK 500 4 SER A 2 42.45 -96.11 REMARK 500 4 MET A 19 149.90 -37.39 REMARK 500 4 ILE A 28 -27.92 -37.57 REMARK 500 4 ARG A 42 -74.99 -82.66 REMARK 500 4 LEU A 100 98.28 -35.95 REMARK 500 4 LYS A 101 48.17 -76.30 REMARK 500 5 TRP A 11 56.92 -101.07 REMARK 500 5 ASN A 35 41.81 -88.21 REMARK 500 5 ASN A 36 26.25 41.03 REMARK 500 5 ASP A 53 53.50 -96.63 REMARK 500 5 SER A 73 39.76 -96.53 REMARK 500 5 LEU A 100 122.75 -38.79 REMARK 500 5 LYS A 101 70.44 -100.63 REMARK 500 6 SER A 5 150.93 -37.07 REMARK 500 6 LYS A 14 52.73 -90.33 REMARK 500 6 SER A 18 53.94 -105.04 REMARK 500 6 LYS A 30 -31.60 -39.82 REMARK 500 6 ARG A 42 -74.15 -96.95 REMARK 500 6 THR A 85 -179.08 -56.72 REMARK 500 6 ASN A 98 -73.20 -80.19 REMARK 500 6 LEU A 100 93.47 -38.57 REMARK 500 7 THR A 10 -175.30 -60.16 REMARK 500 7 SER A 12 127.82 -174.10 REMARK 500 7 ASN A 35 31.35 -90.18 REMARK 500 7 ASN A 36 50.94 39.63 REMARK 500 7 ARG A 42 -71.85 -117.95 REMARK 500 7 LEU A 74 -176.51 -52.83 REMARK 500 REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007019316.1 RELATED DB: TARGETDB DBREF 1UL7 A 8 102 UNP Q03141 MARK3_MOUSE 659 753 SEQADV 1UL7 GLY A 1 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 SER A 2 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 SER A 3 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 GLY A 4 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 SER A 5 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 SER A 6 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 GLY A 7 UNP Q03141 CLONING ARTIFACT SEQADV 1UL7 GLY A 33 UNP Q03141 ASP 684 CONFLICT SEQRES 1 A 102 GLY SER SER GLY SER SER GLY ARG PHE THR TRP SER MET SEQRES 2 A 102 LYS THR THR SER SER MET ASP PRO SER ASP MET MET ARG SEQRES 3 A 102 GLU ILE ARG LYS VAL LEU GLY ALA ASN ASN CYS ASP TYR SEQRES 4 A 102 GLU GLN ARG GLU ARG PHE LEU LEU PHE CYS VAL HIS GLY SEQRES 5 A 102 ASP GLY HIS ALA GLU ASN LEU VAL GLN TRP GLU MET GLU SEQRES 6 A 102 VAL CYS LYS LEU PRO ARG LEU SER LEU ASN GLY VAL ARG SEQRES 7 A 102 PHE LYS ARG ILE SER GLY THR SER ILE ALA PHE LYS ASN SEQRES 8 A 102 ILE ALA SER LYS ILE ALA ASN GLU LEU LYS LEU HELIX 1 1 ASP A 20 ASN A 35 1 16 HELIX 2 2 HIS A 55 LEU A 59 5 5 HELIX 3 3 THR A 85 LEU A 100 1 16 SHEET 1 A 5 THR A 16 SER A 17 0 SHEET 2 A 5 ASP A 38 GLN A 41 0 SHEET 3 A 5 LEU A 47 HIS A 51 -1 O PHE A 48 N GLU A 40 SHEET 4 A 5 VAL A 60 LYS A 68 -1 O VAL A 60 N HIS A 51 SHEET 5 A 5 ASN A 75 SER A 83 -1 O ILE A 82 N GLN A 61 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