Header list of 1idz.pdb file
Complete list - v 3 2 Bytes
HEADER DNA BINDING PROTEIN 15-AUG-96 1IDZ TITLE STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PAR2156NCOI; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRP3 KEYWDS PROTOONCOGENE PRODUCT, DNA-BINDING PROTEIN, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.FURUKAWA,M.ODA,H.NAKAMURA REVDAT 3 03-NOV-21 1IDZ 1 KEYWDS REMARK SEQADV REVDAT 2 24-FEB-09 1IDZ 1 VERSN REVDAT 1 23-DEC-96 1IDZ 0 JRNL AUTH K.FURUKAWA,M.ODA,H.NAKAMURA JRNL TITL A SMALL ENGINEERED PROTEIN LACKS STRUCTURAL UNIQUENESS BY JRNL TITL 2 INCREASING THE SIDE-CHAIN CONFORMATIONAL ENTROPY. JRNL REF PROC.NATL.ACAD.SCI.USA V. 93 13583 1996 JRNL REFN ISSN 0027-8424 JRNL PMID 8942977 JRNL DOI 10.1073/PNAS.93.24.13583 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.OGATA,S.MORIKAWA,H.NAKAMURA,H.HOJO,S.YOSHIMURA,R.ZHANG, REMARK 1 AUTH 2 S.AIMOTO,Y.AMETANI,Z.HIRATA,A.SARAI,ET AL. REMARK 1 TITL COMPARISON OF THE FREE AND DNA-COMPLEXED FORMS OF THE REMARK 1 TITL 2 DNA-BINDING DOMAIN FROM C-MYB REMARK 1 REF NAT.STRUCT.BIOL. V. 2 309 1995 REMARK 1 REFN ISSN 1072-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.OGATA,S.MORIKAWA,H.NAKAMURA,A.SEKIKAWA,T.INOUE,H.KANAI, REMARK 1 AUTH 2 A.SARAI,S.ISHII,Y.NISHIMURA REMARK 1 TITL SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB REMARK 1 TITL 2 DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 79 639 1994 REMARK 1 REFN ISSN 0092-8674 REMARK 1 REFERENCE 3 REMARK 1 AUTH K.OGATA,H.HOJO,S.AIMOTO,T.NAKAI,H.NAKAMURA,A.SARAI,S.ISHII, REMARK 1 AUTH 2 Y.NISHIMURA REMARK 1 TITL SOLUTION STRUCTURE OF A DNA-BINDING UNIT OF MYB: A REMARK 1 TITL 2 HELIX-TURN-HELIX-RELATED MOTIF WITH CONSERVED TRYPTOPHANS REMARK 1 TITL 3 FORMING A HYDROPHOBIC CORE REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6428 1992 REMARK 1 REFN ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : MORIKAMI,NAKAI,KIDERA,SAITO,NAKAMURA REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IDZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174119. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600.13 MHZ REMARK 210 SPECTROMETER MODEL : AMX-600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : EMBOSS REMARK 210 METHOD USED : SIMULATED ANNEALING IN 4D REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 120 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : 0.1 ANGSTROM MAXIMUM DISTANCE REMARK 210 VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 GLU A 141 47.52 -156.17 REMARK 500 1 LYS A 143 -69.78 69.57 REMARK 500 1 ASN A 164 22.33 -160.76 REMARK 500 1 LYS A 192 90.39 67.03 REMARK 500 2 LYS A 143 -43.54 -177.90 REMARK 500 2 ASN A 164 30.91 -83.19 REMARK 500 3 VAL A 142 -124.85 36.95 REMARK 500 3 LYS A 143 59.97 28.75 REMARK 500 3 SER A 146 119.09 73.25 REMARK 500 3 ASN A 164 22.30 -160.57 REMARK 500 3 LYS A 192 105.47 59.75 REMARK 500 4 LYS A 143 -23.77 -140.28 REMARK 500 4 SER A 146 35.81 -150.73 REMARK 500 4 ASN A 164 45.07 -81.56 REMARK 500 4 ARG A 165 69.97 -102.27 REMARK 500 4 THR A 188 -61.06 -104.99 REMARK 500 5 VAL A 142 -41.81 -137.98 REMARK 500 5 LYS A 143 102.60 -164.22 REMARK 500 5 SER A 146 65.83 -162.30 REMARK 500 5 ALA A 167 -71.66 -50.74 REMARK 500 5 THR A 188 -69.84 -104.09 REMARK 500 6 VAL A 142 -177.13 48.12 REMARK 500 6 LYS A 143 -160.51 51.06 REMARK 500 6 LYS A 144 32.50 -91.06 REMARK 500 6 THR A 188 -39.36 -157.33 REMARK 500 6 ARG A 190 100.77 62.27 REMARK 500 7 GLU A 141 92.41 62.36 REMARK 500 7 LYS A 143 51.86 38.55 REMARK 500 7 ASN A 164 25.05 -160.35 REMARK 500 7 ARG A 176 -176.90 57.32 REMARK 500 7 THR A 188 -77.46 -79.24 REMARK 500 7 LYS A 192 82.91 56.54 REMARK 500 8 VAL A 142 46.42 39.14 REMARK 500 8 LYS A 143 41.18 39.75 REMARK 500 8 THR A 188 -70.67 -82.36 REMARK 500 9 LYS A 143 -70.35 -84.02 REMARK 500 9 LYS A 144 52.94 -90.10 REMARK 500 9 ASN A 164 28.05 -79.95 REMARK 500 9 SER A 187 -82.39 -79.29 REMARK 500 9 MET A 189 -40.27 -172.78 REMARK 500 10 GLU A 141 -72.75 66.76 REMARK 500 10 VAL A 142 175.92 62.98 REMARK 500 10 LYS A 143 -31.43 85.32 REMARK 500 10 SER A 146 -75.37 -66.35 REMARK 500 10 TRP A 166 35.93 -77.39 REMARK 500 10 SER A 187 35.89 -84.54 REMARK 500 10 THR A 188 -33.43 -160.38 REMARK 500 10 ARG A 191 -176.07 63.62 REMARK 500 11 THR A 145 88.83 -66.20 REMARK 500 11 ASP A 152 -51.39 -124.38 REMARK 500 REMARK 500 THIS ENTRY HAS 103 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 12 ARG A 153 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IDY RELATED DB: PDB REMARK 900 REPRESENTATIVE STRUCTURE DBREF 1IDZ A 141 193 UNP P06876 MYB_MOUSE 141 193 SEQADV 1IDZ LEU A 155 UNP P06876 ILE 155 ENGINEERED MUTATION SEQRES 1 A 54 MET GLU VAL LYS LYS THR SER TRP THR GLU GLU GLU ASP SEQRES 2 A 54 ARG ILE LEU TYR GLN ALA HIS LYS ARG LEU GLY ASN ARG SEQRES 3 A 54 TRP ALA GLU ILE ALA LYS LEU LEU PRO GLY ARG THR ASP SEQRES 4 A 54 ASN ALA ILE LYS ASN HIS TRP ASN SER THR MET ARG ARG SEQRES 5 A 54 LYS VAL HELIX 1 1 GLU A 149 LEU A 162 1 14 HELIX 2 2 TRP A 166 LEU A 172 1 7 HELIX 3 3 ASP A 178 SER A 187 1 10 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 - v 3 2 Bytes