Header list of 1tfs.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 26-JAN-95 1TFS TITLE NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE THREE-DIMENSIONAL TITLE 2 SOLUTION STRUCTURE OF TOXIN FS2, A SPECIFIC BLOCKER OF THE L-TYPE TITLE 3 CALCIUM CHANNEL, ISOLATED FROM BLACK MAMBA VENOM COMPND MOL_ID: 1; COMPND 2 MOLECULE: TOXIN FS2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENDROASPIS POLYLEPIS POLYLEPIS; SOURCE 3 ORGANISM_COMMON: BLACK MAMBA; SOURCE 4 ORGANISM_TAXID: 8620; SOURCE 5 STRAIN: POLYLEPIS KEYWDS TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.-P.ALBRAND,M.J.BLACKLEDGE,F.PASCAUD,M.HOLLECKER,D.MARION REVDAT 3 02-MAR-22 1TFS 1 REMARK SEQADV REVDAT 2 24-FEB-09 1TFS 1 VERSN REVDAT 1 31-MAR-95 1TFS 0 JRNL AUTH J.P.ALBRAND,M.J.BLACKLEDGE,F.PASCAUD,M.HOLLECKER,D.MARION JRNL TITL NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE JRNL TITL 2 THREE-DIMENSIONAL SOLUTION STRUCTURE OF TOXIN FS2, A JRNL TITL 3 SPECIFIC BLOCKER OF THE L-TYPE CALCIUM CHANNEL, ISOLATED JRNL TITL 4 FROM BLACK MAMBA VENOM. JRNL REF BIOCHEMISTRY V. 34 5923 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 7727450 JRNL DOI 10.1021/BI00017A022 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TFS 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_1000176661. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 1 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 1 CYS A 41 CB - CA - C ANGL. DEV. = 8.3 DEGREES REMARK 500 1 CYS A 41 CA - CB - SG ANGL. DEV. = 11.5 DEGREES REMARK 500 1 PRO A 42 C - N - CA ANGL. DEV. = 10.6 DEGREES REMARK 500 3 CYS A 41 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 3 PRO A 42 C - N - CA ANGL. DEV. = 11.4 DEGREES REMARK 500 3 PRO A 42 C - N - CD ANGL. DEV. = -13.5 DEGREES REMARK 500 3 PRO A 42 CA - N - CD ANGL. DEV. = -11.2 DEGREES REMARK 500 8 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 9 CYS A 41 CA - CB - SG ANGL. DEV. = 12.2 DEGREES REMARK 500 9 PRO A 42 C - N - CA ANGL. DEV. = 11.4 DEGREES REMARK 500 11 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 17 CYS A 41 CB - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 17 CYS A 41 CA - CB - SG ANGL. DEV. = 12.5 DEGREES REMARK 500 17 PRO A 42 C - N - CA ANGL. DEV. = 9.1 DEGREES REMARK 500 19 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 19 CYS A 41 CB - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 19 CYS A 41 CA - CB - SG ANGL. DEV. = 13.9 DEGREES REMARK 500 19 PRO A 42 C - N - CA ANGL. DEV. = 12.0 DEGREES REMARK 500 20 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -3.2 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 SER A 5 -92.97 -135.16 REMARK 500 1 HIS A 6 106.47 40.00 REMARK 500 1 LEU A 10 -67.45 -147.09 REMARK 500 1 GLU A 32 48.52 -77.08 REMARK 500 1 TYR A 33 87.75 -160.16 REMARK 500 1 PRO A 42 147.89 -15.60 REMARK 500 1 THR A 43 127.15 176.81 REMARK 500 1 ALA A 44 169.18 179.50 REMARK 500 2 ALA A 8 -164.01 55.89 REMARK 500 2 GLU A 19 131.13 -31.86 REMARK 500 2 SER A 35 -59.97 -123.90 REMARK 500 2 CYS A 41 93.89 -16.19 REMARK 500 2 PRO A 47 59.74 -102.45 REMARK 500 2 LYS A 54 59.71 -143.28 REMARK 500 2 ARG A 57 39.10 35.59 REMARK 500 3 SER A 5 36.25 -149.38 REMARK 500 3 ARG A 12 -96.98 -159.00 REMARK 500 3 CYS A 41 125.08 19.29 REMARK 500 3 PRO A 42 159.21 37.07 REMARK 500 3 THR A 43 -54.57 -172.31 REMARK 500 4 HIS A 6 -146.94 35.53 REMARK 500 4 LYS A 7 -43.51 -163.75 REMARK 500 4 ALA A 8 -145.01 -139.87 REMARK 500 4 TYR A 33 86.05 -160.14 REMARK 500 4 CYS A 41 97.37 -18.53 REMARK 500 4 PRO A 47 50.36 -99.95 REMARK 500 5 SER A 5 -68.84 -127.88 REMARK 500 5 LEU A 10 -60.70 178.72 REMARK 500 5 ARG A 12 -77.26 62.18 REMARK 500 5 GLU A 32 41.12 -78.74 REMARK 500 5 CYS A 41 104.42 -41.68 REMARK 500 6 ALA A 8 38.97 -76.23 REMARK 500 6 SER A 9 35.44 -161.72 REMARK 500 6 HIS A 30 55.15 -163.40 REMARK 500 6 CYS A 41 100.59 -28.57 REMARK 500 7 SER A 5 81.62 -153.83 REMARK 500 7 SER A 9 34.64 -160.11 REMARK 500 7 GLU A 19 138.95 -29.90 REMARK 500 7 CYS A 41 95.84 -15.50 REMARK 500 7 ASP A 56 -149.09 37.90 REMARK 500 7 ARG A 57 39.82 -69.01 REMARK 500 8 SER A 5 -36.32 -145.26 REMARK 500 8 SER A 9 41.14 -79.79 REMARK 500 8 ARG A 12 -117.30 -173.67 REMARK 500 8 THR A 29 -70.64 -72.55 REMARK 500 8 GLU A 32 37.70 -75.81 REMARK 500 8 CYS A 41 100.30 -30.18 REMARK 500 8 PRO A 47 52.10 -101.14 REMARK 500 8 ARG A 57 28.02 40.09 REMARK 500 9 SER A 5 -60.00 -95.36 REMARK 500 REMARK 500 THIS ENTRY HAS 117 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 TYR A 23 0.12 SIDE CHAIN REMARK 500 1 ARG A 31 0.11 SIDE CHAIN REMARK 500 1 TYR A 48 0.14 SIDE CHAIN REMARK 500 2 TYR A 4 0.11 SIDE CHAIN REMARK 500 2 ARG A 12 0.10 SIDE CHAIN REMARK 500 3 TYR A 33 0.07 SIDE CHAIN REMARK 500 4 TYR A 23 0.07 SIDE CHAIN REMARK 500 7 TYR A 23 0.07 SIDE CHAIN REMARK 500 7 TYR A 33 0.07 SIDE CHAIN REMARK 500 8 TYR A 4 0.10 SIDE CHAIN REMARK 500 8 TYR A 23 0.09 SIDE CHAIN REMARK 500 8 ARG A 31 0.12 SIDE CHAIN REMARK 500 8 TYR A 33 0.12 SIDE CHAIN REMARK 500 8 ARG A 37 0.16 SIDE CHAIN REMARK 500 9 TYR A 23 0.16 SIDE CHAIN REMARK 500 11 TYR A 4 0.11 SIDE CHAIN REMARK 500 11 TYR A 23 0.07 SIDE CHAIN REMARK 500 11 TYR A 33 0.11 SIDE CHAIN REMARK 500 11 ARG A 37 0.08 SIDE CHAIN REMARK 500 13 TYR A 4 0.08 SIDE CHAIN REMARK 500 13 TYR A 33 0.09 SIDE CHAIN REMARK 500 14 TYR A 23 0.08 SIDE CHAIN REMARK 500 14 TYR A 33 0.12 SIDE CHAIN REMARK 500 15 TYR A 4 0.17 SIDE CHAIN REMARK 500 15 TYR A 33 0.10 SIDE CHAIN REMARK 500 15 TYR A 48 0.07 SIDE CHAIN REMARK 500 16 TYR A 23 0.08 SIDE CHAIN REMARK 500 16 TYR A 33 0.10 SIDE CHAIN REMARK 500 17 TYR A 4 0.10 SIDE CHAIN REMARK 500 17 TYR A 23 0.16 SIDE CHAIN REMARK 500 18 TYR A 23 0.09 SIDE CHAIN REMARK 500 18 ARG A 37 0.14 SIDE CHAIN REMARK 500 19 ARG A 1 0.08 SIDE CHAIN REMARK 500 19 ARG A 12 0.09 SIDE CHAIN REMARK 500 19 TYR A 23 0.15 SIDE CHAIN REMARK 500 20 TYR A 4 0.10 SIDE CHAIN REMARK 500 20 TYR A 23 0.07 SIDE CHAIN REMARK 500 20 ARG A 31 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1TFS A 1 60 UNP P01414 TXFS2_DENPO 1 60 SEQADV 1TFS GLU A 32 UNP P01414 GLN 32 CONFLICT SEQRES 1 A 60 ARG ILE CYS TYR SER HIS LYS ALA SER LEU PRO ARG ALA SEQRES 2 A 60 THR LYS THR CYS VAL GLU ASN THR CYS TYR LYS MET PHE SEQRES 3 A 60 ILE ARG THR HIS ARG GLU TYR ILE SER GLU ARG GLY CYS SEQRES 4 A 60 GLY CYS PRO THR ALA MET TRP PRO TYR GLN THR GLU CYS SEQRES 5 A 60 CYS LYS GLY ASP ARG CYS ASN LYS SHEET 1 A 2 ILE A 2 TYR A 4 0 SHEET 2 A 2 THR A 14 THR A 16 -1 N LYS A 15 O CYS A 3 SHEET 1 B 3 HIS A 30 CYS A 39 0 SHEET 2 B 3 THR A 21 ILE A 27 -1 O TYR A 23 N GLY A 38 SHEET 3 B 3 TYR A 48 LYS A 54 -1 N GLN A 49 O PHE A 26 SSBOND 1 CYS A 3 CYS A 22 1555 1555 2.06 SSBOND 2 CYS A 17 CYS A 39 1555 1555 2.07 SSBOND 3 CYS A 41 CYS A 52 1555 1555 2.08 SSBOND 4 CYS A 53 CYS A 58 1555 1555 2.08 CISPEP 1 TRP A 46 PRO A 47 1 8.18 CISPEP 2 TRP A 46 PRO A 47 2 -2.08 CISPEP 3 TRP A 46 PRO A 47 3 6.99 CISPEP 4 TRP A 46 PRO A 47 4 -1.42 CISPEP 5 TRP A 46 PRO A 47 5 -4.84 CISPEP 6 TRP A 46 PRO A 47 6 8.71 CISPEP 7 TRP A 46 PRO A 47 7 4.53 CISPEP 8 TRP A 46 PRO A 47 8 -0.47 CISPEP 9 TRP A 46 PRO A 47 9 5.02 CISPEP 10 TRP A 46 PRO A 47 10 7.12 CISPEP 11 TRP A 46 PRO A 47 11 1.72 CISPEP 12 TRP A 46 PRO A 47 12 8.65 CISPEP 13 TRP A 46 PRO A 47 13 7.92 CISPEP 14 TRP A 46 PRO A 47 14 -0.04 CISPEP 15 TRP A 46 PRO A 47 15 8.95 CISPEP 16 TRP A 46 PRO A 47 16 4.09 CISPEP 17 TRP A 46 PRO A 47 17 2.30 CISPEP 18 TRP A 46 PRO A 47 18 7.85 CISPEP 19 TRP A 46 PRO A 47 19 8.76 CISPEP 20 TRP A 46 PRO A 47 20 9.99 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