Header list of 2mst.pdb file
Complete list - r 16 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-99 2MST
TITLE MUSASHI1 RBD2, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (MUSASHI1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA-BINDING DOMAIN;
COMPND 5 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELL: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET3A;
SOURCE 10 EXPRESSION_SYSTEM_GENE: PET3A;
SOURCE 11 OTHER_DETAILS: PCR
KEYWDS RNA-BINDING DOMAIN, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGATA,R.KANNO,Y.KURIHARA,S.UESUGI,T.IMAI,S.SAKAKIBARA,H.OKANO,
AUTHOR 2 M.KATAHIRA
REVDAT 3 16-MAR-22 2MST 1 REMARK
REVDAT 2 24-FEB-09 2MST 1 VERSN
REVDAT 1 19-MAY-00 2MST 0
JRNL AUTH T.NAGATA,R.KANNO,Y.KURIHARA,S.UESUGI,T.IMAI,S.SAKAKIBARA,
JRNL AUTH 2 H.OKANO,M.KATAHIRA
JRNL TITL STRUCTURE, BACKBONE DYNAMICS AND INTERACTIONS WITH RNA OF
JRNL TITL 2 THE C-TERMINAL RNA-BINDING DOMAIN OF A MOUSE NEURAL
JRNL TITL 3 RNA-BINDING PROTEIN, MUSASHI1.
JRNL REF J.MOL.BIOL. V. 287 315 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10080895
JRNL DOI 10.1006/JMBI.1999.2596
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.KURIHARA,T.NAGATA,T.IMAI,A.HIWATASHI,M.HORIUCHI,
REMARK 1 AUTH 2 S.SAKAKIBARA,M.KATAHIRA,H.OKANO,S.UESUGI
REMARK 1 TITL STRUCTURAL PROPERTIES AND RNA-BINDING ACTIVITIES OF TWO RNA
REMARK 1 TITL 2 RECOGNITION MOTIFS OF A MOUSE NEURAL RNA-BINDING PROTEIN,
REMARK 1 TITL 3 MOUSE-MUSASHI-1
REMARK 1 REF GENE V. 186 21 1997
REMARK 1 REFN ISSN 0378-1119
REMARK 1 DOI 10.1016/S0378-1119(96)00673-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MST COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001089.
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 : 0 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; 1H-15N
REMARK 210 2D HSQC; 15N-EDITED NOESY-HSQC;
REMARK 210 15N-EDITED TOCSY-HSQC; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1, X-PLOR 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWER ENERGIES
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: 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 THR A 121 H ASP A 124 1.50
REMARK 500 O VAL A 118 H THR A 120 1.52
REMARK 500 O ILE A 174 H ASN A 176 1.53
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 116 97.93 -47.63
REMARK 500 1 SER A 117 -168.19 -57.52
REMARK 500 1 ASN A 119 -35.28 62.26
REMARK 500 1 VAL A 135 90.31 55.34
REMARK 500 1 PHE A 142 -133.22 -111.91
REMARK 500 1 THR A 146 53.33 -150.00
REMARK 500 1 HIS A 149 -174.62 -67.65
REMARK 500 1 THR A 156 104.74 -164.81
REMARK 500 1 GLU A 158 -26.58 -39.31
REMARK 500 1 SER A 159 81.14 -56.48
REMARK 500 1 PHE A 171 59.79 -177.98
REMARK 500 1 HIS A 172 -159.61 -58.18
REMARK 500 1 ASN A 175 -53.13 64.47
REMARK 500 1 MET A 178 57.69 -113.05
REMARK 500 1 VAL A 179 -166.79 -56.88
REMARK 500 2 SER A 117 -169.40 -52.91
REMARK 500 2 VAL A 118 -153.72 -78.28
REMARK 500 2 ASN A 119 -17.34 64.65
REMARK 500 2 VAL A 135 92.27 44.59
REMARK 500 2 ASP A 143 -162.40 59.31
REMARK 500 2 LYS A 144 -83.21 56.50
REMARK 500 2 THR A 145 15.61 -151.12
REMARK 500 2 HIS A 149 -76.99 -71.30
REMARK 500 2 THR A 156 107.28 -161.94
REMARK 500 2 GLU A 158 -27.69 -39.33
REMARK 500 2 SER A 159 85.91 -55.58
REMARK 500 2 PHE A 171 76.72 -61.16
REMARK 500 2 ASN A 175 -55.32 65.73
REMARK 500 2 ASN A 176 18.74 -158.19
REMARK 500 2 VAL A 179 159.35 -37.96
REMARK 500 3 LEU A 116 97.46 -44.81
REMARK 500 3 SER A 117 171.64 -45.66
REMARK 500 3 ASN A 119 -42.24 65.08
REMARK 500 3 THR A 120 120.91 -38.76
REMARK 500 3 LYS A 134 -38.85 -39.22
REMARK 500 3 VAL A 135 91.55 45.24
REMARK 500 3 ARG A 148 -68.84 -106.38
REMARK 500 3 THR A 156 109.82 -161.26
REMARK 500 3 GLU A 158 -27.91 -39.70
REMARK 500 3 SER A 159 85.95 -55.29
REMARK 500 3 ILE A 169 -29.44 175.08
REMARK 500 3 PHE A 171 57.34 175.89
REMARK 500 3 HIS A 172 -145.84 -61.72
REMARK 500 3 ASN A 175 -55.91 66.56
REMARK 500 3 ASN A 176 21.49 -164.86
REMARK 500 3 MET A 178 43.20 -96.58
REMARK 500 3 VAL A 179 -174.29 -53.98
REMARK 500 4 SER A 117 -170.09 -53.41
REMARK 500 4 VAL A 118 -154.35 -81.28
REMARK 500 4 ASN A 119 -17.96 64.45
REMARK 500
REMARK 500 THIS ENTRY HAS 344 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 1 ARG A 148 0.29 SIDE CHAIN
REMARK 500 1 ARG A 150 0.31 SIDE CHAIN
REMARK 500 2 ARG A 148 0.29 SIDE CHAIN
REMARK 500 2 ARG A 150 0.29 SIDE CHAIN
REMARK 500 3 ARG A 148 0.21 SIDE CHAIN
REMARK 500 3 ARG A 150 0.30 SIDE CHAIN
REMARK 500 4 ARG A 148 0.26 SIDE CHAIN
REMARK 500 4 ARG A 150 0.31 SIDE CHAIN
REMARK 500 5 ARG A 148 0.32 SIDE CHAIN
REMARK 500 5 ARG A 150 0.24 SIDE CHAIN
REMARK 500 6 ARG A 148 0.32 SIDE CHAIN
REMARK 500 6 ARG A 150 0.19 SIDE CHAIN
REMARK 500 7 ARG A 148 0.20 SIDE CHAIN
REMARK 500 7 ARG A 150 0.18 SIDE CHAIN
REMARK 500 8 ARG A 148 0.29 SIDE CHAIN
REMARK 500 8 ARG A 150 0.21 SIDE CHAIN
REMARK 500 9 ARG A 150 0.13 SIDE CHAIN
REMARK 500 10 ARG A 148 0.31 SIDE CHAIN
REMARK 500 10 ARG A 150 0.27 SIDE CHAIN
REMARK 500 11 ARG A 148 0.32 SIDE CHAIN
REMARK 500 11 ARG A 150 0.31 SIDE CHAIN
REMARK 500 12 ARG A 150 0.30 SIDE CHAIN
REMARK 500 13 ARG A 148 0.31 SIDE CHAIN
REMARK 500 13 ARG A 150 0.20 SIDE CHAIN
REMARK 500 14 ARG A 148 0.31 SIDE CHAIN
REMARK 500 14 ARG A 150 0.25 SIDE CHAIN
REMARK 500 15 ARG A 148 0.25 SIDE CHAIN
REMARK 500 16 ARG A 148 0.22 SIDE CHAIN
REMARK 500 16 ARG A 150 0.28 SIDE CHAIN
REMARK 500 17 ARG A 148 0.10 SIDE CHAIN
REMARK 500 17 ARG A 150 0.28 SIDE CHAIN
REMARK 500 18 ARG A 148 0.26 SIDE CHAIN
REMARK 500 18 ARG A 150 0.18 SIDE CHAIN
REMARK 500 19 ARG A 148 0.12 SIDE CHAIN
REMARK 500 19 ARG A 150 0.20 SIDE CHAIN
REMARK 500 20 ARG A 148 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2MSS RELATED DB: PDB
DBREF 2MST A 110 184 UNP Q61474 MSI1H_MOUSE 110 184
SEQRES 1 A 75 LYS ILE PHE VAL GLY GLY LEU SER VAL ASN THR THR VAL
SEQRES 2 A 75 GLU ASP VAL LYS HIS TYR PHE GLU GLN PHE GLY LYS VAL
SEQRES 3 A 75 ASP ASP ALA MET LEU MET PHE ASP LYS THR THR ASN ARG
SEQRES 4 A 75 HIS ARG GLY PHE GLY PHE VAL THR PHE GLU SER GLU ASP
SEQRES 5 A 75 ILE VAL GLU LYS VAL CYS GLU ILE HIS PHE HIS GLU ILE
SEQRES 6 A 75 ASN ASN LYS MET VAL GLU CYS LYS LYS ALA
HELIX 1 H1 VAL A 122 PHE A 132 5 11
HELIX 2 H2 GLU A 160 CYS A 167 5 8
SHEET 1 S1 1 LYS A 110 GLY A 114 0
SHEET 1 S2 1 VAL A 135 MET A 141 0
SHEET 1 S3 1 PHE A 152 PHE A 157 0
SHEET 1 S4 1 GLU A 180 ALA A 184 0
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 16 2 Bytes