Header list of 1mph.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNAL TRANSDUCTION 23-APR-97 1MPH TITLE PLECKSTRIN HOMOLOGY DOMAIN FROM MOUSE BETA-SPECTRIN, NMR, 50 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA SPECTRIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY; COMPND 5 SYNONYM: PH DOMAIN; COMPND 6 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 CELL_LINE: BL21; SOURCE 6 ORGAN: BRAIN; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21D KEYWDS SIGNAL TRANSDUCTION, INOSITOL PHOSPHATES EXPDTA SOLUTION NMR NUMMDL 50 AUTHOR M.NILGES,M.J.MACIAS,S.I.O'DONOGHUE,H.OSCHKINAT REVDAT 4 23-FEB-22 1MPH 1 REMARK REVDAT 3 24-FEB-09 1MPH 1 VERSN REVDAT 2 01-APR-03 1MPH 1 JRNL REVDAT 1 16-JUN-97 1MPH 0 JRNL AUTH M.NILGES,M.J.MACIAS,S.I.O'DONOGHUE,H.OSCHKINAT JRNL TITL AUTOMATED NOESY INTERPRETATION WITH AMBIGUOUS DISTANCE JRNL TITL 2 RESTRAINTS: THE REFINED NMR SOLUTION STRUCTURE OF THE JRNL TITL 3 PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN. JRNL REF J.MOL.BIOL. V. 269 408 1997 JRNL REFN ISSN 0022-2836 JRNL PMID 9199409 JRNL DOI 10.1006/JMBI.1997.1044 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.WILMANNS,M.NILGES REMARK 1 TITL MOLECULAR REPLACEMENT WITH NMR MODELS USING DISTANCE-DERIVED REMARK 1 TITL 2 PSEUDO B FACTORS REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 973 1996 REMARK 1 REFN ISSN 0907-4449 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.HYVONEN,M.J.MACIAS,M.NILGES,H.OSCHKINAT,M.SARASTE, REMARK 1 AUTH 2 M.WILMANNS REMARK 1 TITL STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A REMARK 1 TITL 2 PH DOMAIN REMARK 1 REF EMBO J. V. 14 4676 1995 REMARK 1 REFN ISSN 0261-4189 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.J.MACIAS,A.MUSACCHIO,H.PONSTINGL,M.NILGES,M.SARASTE, REMARK 1 AUTH 2 H.OSCHKINAT REMARK 1 TITL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM REMARK 1 TITL 2 BETA-SPECTRIN REMARK 1 REF NATURE V. 369 675 1994 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED WITH A REMARK 3 MODIFIED VERSION OF X-PLOR (SEE JRNL REFERENCE FOR DETAILS) WITH REMARK 3 A SIMULATED ANNEALING PROTOCOL. AN AUTOMATED PROCEDURE (ARIA) REMARK 3 WAS USED TO AUTOMATICALLY ASSIGN AND AUGMENT AN INITIAL LIST OF REMARK 3 568 MANUALLY SELECTED RESTRAINTS, FROM PEAK LISTS FROM TWO H2O REMARK 3 NOESY SPECTRA (30 AND 80 MS). 20 STRUCTURES WERE ITERATIVELY REMARK 3 REFINED, AND THE NOE DATA RE-ASSIGNED ON THE BASIS OF THE 7 REMARK 3 LOWEST ENERGY STRUCTURES IN EACH ITERATION. EIGHT REFINEMENT/ REMARK 3 ASSIGNMENT CYCLES WERE RUN, PLUS TWO IN AN EXPLICIT SHELL OF REMARK 3 WATER. THE FINAL LIST OF RESTRAINTS CONTAINED 1328 UNAMBIGUOUS REMARK 3 RESTRAINTS AND 486 AMBIGUOUS RESTRAINTS WITH MAXIMALLY 5 REMARK 3 ASSIGNMENT POSSIBILITIES. REMARK 4 REMARK 4 1MPH 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_1000175113. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; 3D TOCSY-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR, ARIA REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY 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 DBREF 1MPH A 1 106 UNP Q62261 SPTB2_MOUSE 2199 2304 SEQRES 1 A 106 MET GLU GLY PHE LEU ASN ARG LYS HIS GLU TRP GLU ALA SEQRES 2 A 106 HIS ASN LYS LYS ALA SER SER ARG SER TRP HIS ASN VAL SEQRES 3 A 106 TYR CYS VAL ILE ASN ASN GLN GLU MET GLY PHE TYR LYS SEQRES 4 A 106 ASP ALA LYS SER ALA ALA SER GLY ILE PRO TYR HIS SER SEQRES 5 A 106 GLU VAL PRO VAL SER LEU LYS GLU ALA ILE CYS GLU VAL SEQRES 6 A 106 ALA LEU ASP TYR LYS LYS LYS LYS HIS VAL PHE LYS LEU SEQRES 7 A 106 ARG LEU SER ASP GLY ASN GLU TYR LEU PHE GLN ALA LYS SEQRES 8 A 106 ASP ASP GLU GLU MET ASN THR TRP ILE GLN ALA ILE SER SEQRES 9 A 106 SER ALA HELIX 1 1 ALA A 41 SER A 46 1 6 HELIX 2 2 ASP A 93 SER A 104 1 12 SHEET 1 A 7 PRO A 55 SER A 57 0 SHEET 2 A 7 GLU A 34 TYR A 38 -1 N MET A 35 O VAL A 56 SHEET 3 A 7 TRP A 23 ASN A 31 -1 N ASN A 31 O GLU A 34 SHEET 4 A 7 GLU A 2 TRP A 11 -1 N ARG A 7 O HIS A 24 SHEET 5 A 7 GLU A 85 GLN A 89 -1 N GLN A 89 O ASN A 6 SHEET 6 A 7 VAL A 75 ARG A 79 -1 N LEU A 78 O TYR A 86 SHEET 7 A 7 ILE A 62 ALA A 66 -1 N ALA A 66 O VAL A 75 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 - b 23 2 Bytes