Header list of 1msz.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 20-SEP-02 1MSZ TITLE SOLUTION STRUCTURE OF THE R3H DOMAIN FROM HUMAN SMUBP-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA-BINDING PROTEIN SMUBP-2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: R3H DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SMUBP-2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE60 KEYWDS R3H FOLD, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR E.LIEPINSH,A.LEONCHIKS,A.SHARIPO,L.GUIGNARD,G.OTTING REVDAT 5 23-FEB-22 1MSZ 1 REMARK SEQADV REVDAT 4 24-FEB-09 1MSZ 1 VERSN REVDAT 3 18-OCT-05 1MSZ 1 JRNL REVDAT 2 30-OCT-02 1MSZ 1 SEQRES DBREF SEQADV REMARK REVDAT 1 09-OCT-02 1MSZ 0 JRNL AUTH E.LIEPINSH,A.LEONCHIKS,A.SHARIPO,L.GUIGNARD,G.OTTING JRNL TITL SOLUTION STRUCTURE OF THE R3H DOMAIN FROM HUMAN SMUBP-2 JRNL REF J.MOL.BIOL. V. 326 217 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12547203 JRNL DOI 10.1016/S0022-2836(02)01381-5 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, OPAL 2.6 REMARK 3 AUTHORS : GUENTERT (DYANA), LUGINBUEHL (OPAL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURE BASED ON 663 NON-REDUNDANT NOES, 123 COUPLING CONSTANTS, REMARK 3 AND 170 DIHEDRAL-ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS, REMARK 3 NOE DATA AND PRELIMINARY STRUCTURE CALCULATIONS. REMARK 3 THE NUMBER OF MISSING RESIDUES WAS SO MUCH THAT REMARK 465 REMARK 3 FOR THE MISSING RESIDUES LIST WERE REMOVED. REMARK 4 REMARK 4 1MSZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1000017158. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.9 REMARK 210 IONIC STRENGTH : NO BUFFER ADDED REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4MM R3H DOMAIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: DISTANCE RESTRAINTS COLLECTED FROM A NOESY SPECTRUM WITH REMARK 210 40 MS MIXING TIME. 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 4 ARG A 768 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 16 ARG A 755 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES 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 LYS A 741 -81.69 -60.22 REMARK 500 1 MET A 742 -66.32 -162.63 REMARK 500 1 SER A 749 -8.63 -56.39 REMARK 500 1 ASN A 751 -71.72 -59.19 REMARK 500 1 SER A 752 -65.87 -146.84 REMARK 500 1 HIS A 765 -148.48 -85.25 REMARK 500 1 GLU A 774 -66.39 -91.59 REMARK 500 1 LYS A 776 23.50 -73.01 REMARK 500 2 LYS A 741 -81.89 -67.43 REMARK 500 2 MET A 742 -65.85 -158.39 REMARK 500 2 ASN A 751 -71.87 -62.56 REMARK 500 2 SER A 752 -66.14 -146.76 REMARK 500 2 HIS A 765 -148.63 -81.43 REMARK 500 2 GLU A 774 -65.33 -96.11 REMARK 500 2 LYS A 776 23.63 -73.02 REMARK 500 3 LYS A 741 -77.97 -53.96 REMARK 500 3 MET A 742 -66.14 -166.41 REMARK 500 3 ASN A 751 -70.96 -65.40 REMARK 500 3 SER A 752 -66.37 -146.11 REMARK 500 3 HIS A 765 -148.51 -91.89 REMARK 500 3 LYS A 776 23.92 -68.28 REMARK 500 4 LYS A 741 -81.86 -59.40 REMARK 500 4 MET A 742 -66.27 -156.08 REMARK 500 4 SER A 752 -66.28 -146.37 REMARK 500 4 HIS A 765 -148.81 -97.30 REMARK 500 4 GLU A 774 -65.46 -126.20 REMARK 500 4 LYS A 776 36.29 -72.80 REMARK 500 5 LYS A 741 -81.85 -67.25 REMARK 500 5 MET A 742 -58.32 -157.48 REMARK 500 5 SER A 749 -11.58 -47.11 REMARK 500 5 SER A 752 -52.97 -146.48 REMARK 500 5 HIS A 765 -154.32 -83.15 REMARK 500 6 ASP A 727 -66.06 -109.74 REMARK 500 6 LYS A 741 -81.59 -65.05 REMARK 500 6 MET A 742 -66.36 -164.41 REMARK 500 6 ASN A 751 -71.46 -79.29 REMARK 500 6 SER A 752 -65.91 -146.05 REMARK 500 6 HIS A 765 -148.60 -82.67 REMARK 500 6 GLU A 774 -66.89 -126.99 REMARK 500 7 LYS A 741 -81.30 -54.29 REMARK 500 7 MET A 742 -66.43 -166.79 REMARK 500 7 ASN A 751 -70.74 -61.76 REMARK 500 7 SER A 752 -66.19 -146.06 REMARK 500 7 HIS A 765 -148.40 -78.10 REMARK 500 7 GLU A 774 -58.29 -126.50 REMARK 500 7 LYS A 776 43.16 -107.68 REMARK 500 8 LYS A 741 -81.86 -54.15 REMARK 500 8 MET A 742 -66.27 -166.72 REMARK 500 8 ASN A 751 -71.70 -72.71 REMARK 500 8 SER A 752 -55.22 -146.72 REMARK 500 REMARK 500 THIS ENTRY HAS 135 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 2 ARG A 757 0.09 SIDE CHAIN REMARK 500 8 ARG A 730 0.08 SIDE CHAIN REMARK 500 11 ARG A 785 0.08 SIDE CHAIN REMARK 500 12 ARG A 730 0.08 SIDE CHAIN REMARK 500 13 ARG A 730 0.08 SIDE CHAIN REMARK 500 14 ARG A 730 0.09 SIDE CHAIN REMARK 500 15 ARG A 768 0.12 SIDE CHAIN REMARK 500 16 ARG A 755 0.08 SIDE CHAIN REMARK 500 16 ARG A 777 0.09 SIDE CHAIN REMARK 500 16 ARG A 785 0.13 SIDE CHAIN REMARK 500 17 ARG A 757 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1MSZ A 711 786 UNP P38935 SMBP2_HUMAN 711 786 SEQADV 1MSZ MET A 709 UNP P38935 CLONING ARTIFACT SEQADV 1MSZ GLY A 710 UNP P38935 CLONING ARTIFACT SEQADV 1MSZ GLY A 787 UNP P38935 EXPRESSION TAG SEQADV 1MSZ SER A 788 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 789 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 790 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 791 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 792 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 793 UNP P38935 EXPRESSION TAG SEQADV 1MSZ HIS A 794 UNP P38935 EXPRESSION TAG SEQRES 1 A 86 MET GLY SER LEU ASN GLY GLY SER PRO GLU GLY VAL GLU SEQRES 2 A 86 SER GLN ASP GLY VAL ASP HIS PHE ARG ALA MET ILE VAL SEQRES 3 A 86 GLU PHE MET ALA SER LYS LYS MET GLN LEU GLU PHE PRO SEQRES 4 A 86 PRO SER LEU ASN SER HIS ASP ARG LEU ARG VAL HIS GLN SEQRES 5 A 86 ILE ALA GLU GLU HIS GLY LEU ARG HIS ASP SER SER GLY SEQRES 6 A 86 GLU GLY LYS ARG ARG PHE ILE THR VAL SER LYS ARG ALA SEQRES 7 A 86 GLY SER HIS HIS HIS HIS HIS HIS HELIX 1 1 VAL A 726 LYS A 740 1 15 HELIX 2 2 SER A 752 HIS A 765 1 14 SHEET 1 A 3 GLN A 743 PHE A 746 0 SHEET 2 A 3 PHE A 779 LYS A 784 -1 O ILE A 780 N PHE A 746 SHEET 3 A 3 LEU A 767 SER A 772 -1 N ASP A 770 O THR A 781 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