Header list of 1ahl.pdb file
Complete list - v 29 2 Bytes
HEADER NEUROTOXIN 28-OCT-94 1AHL TITLE ANTHOPLEURIN-A,NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTHOPLEURIN-A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: AP-A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANTHOPLEURA XANTHOGRAMMICA; SOURCE 3 ORGANISM_COMMON: GIANT GREEN SEA ANEMONE; SOURCE 4 ORGANISM_TAXID: 6112 KEYWDS NEUROTOXIN, CARDIAC STIMULANT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.K.PALLAGHY,M.J.SCANLON,S.A.MONKS,R.S.NORTON REVDAT 4 29-NOV-17 1AHL 1 HELIX REVDAT 3 24-NOV-10 1AHL 1 SOURCE REVDAT 2 24-FEB-09 1AHL 1 VERSN REVDAT 1 14-NOV-95 1AHL 0 JRNL AUTH P.K.PALLAGHY,M.J.SCANLON,S.A.MONKS,R.S.NORTON JRNL TITL THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE POLYPEPTIDE JRNL TITL 2 CARDIAC STIMULANT ANTHOPLEURIN-A. JRNL REF BIOCHEMISTRY V. 34 3782 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 7893675 JRNL DOI 10.1021/BI00011A036 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.S.NORTON REMARK 1 TITL STRUCTURE AND STRUCTURE-FUNCTION RELATIONSHIPS OF SEA REMARK 1 TITL 2 ANEMONE PROTEINS THAT INTERACT WITH THE SODIUM CHANNEL REMARK 1 REF TOXICON V. 29 1051 1991 REMARK 1 REFN ISSN 0041-0101 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.E.TORDA,B.C.MABBUTT,W.F.VAN GUNSTEREN,R.S.NORTON REMARK 1 TITL BACKBONE FOLDING OF THE POLYPEPTIDE CARDIAC STIMULANT REMARK 1 TITL 2 ANTHOPLEURIN-A DETERMINED BY NUCLEAR MAGNETIC RESONANCE, REMARK 1 TITL 3 DISTANCE GEOMETRY AND MOLECULAR DYNAMICS REMARK 1 REF FEBS LETT. V. 239 266 1988 REMARK 1 REFN ISSN 0014-5793 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.TANAKA,M.HANIU,M.YASUNOBU,T.R.NORTON REMARK 1 TITL AMINO ACID SEQUENCE OF THE ANTHOPLEURA XANTHOGRAMMICA HEART REMARK 1 TITL 2 STIMULANT ANTHOPLEURIN-A REMARK 1 REF BIOCHEMISTRY V. 16 204 1977 REMARK 1 REFN ISSN 0006-2960 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: NULL REMARK 4 REMARK 4 1AHL 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_1000170825. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 4.8 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 CYS A 4 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 1 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 TRP A 23 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 TRP A 23 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES REMARK 500 1 TRP A 23 NE1 - CE2 - CZ2 ANGL. DEV. = 7.2 DEGREES REMARK 500 1 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -7.7 DEGREES REMARK 500 1 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 1 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES REMARK 500 1 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 1 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 1 TRP A 45 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 1 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES REMARK 500 2 TRP A 23 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 2 TRP A 23 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 2 TRP A 23 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES REMARK 500 2 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -7.9 DEGREES REMARK 500 2 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 2 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES REMARK 500 2 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 2 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 2 TRP A 45 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 2 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 3 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES REMARK 500 3 TRP A 23 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 3 TRP A 23 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 3 TRP A 23 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES REMARK 500 3 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 3 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 3 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES REMARK 500 3 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 3 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 3 TRP A 45 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 3 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 7.2 DEGREES REMARK 500 4 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES REMARK 500 4 TRP A 23 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 4 TRP A 23 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 4 TRP A 23 NE1 - CE2 - CZ2 ANGL. DEV. = 7.2 DEGREES REMARK 500 4 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 4 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 4 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES REMARK 500 4 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 4 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 4 TRP A 45 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 4 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 6.6 DEGREES REMARK 500 5 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES REMARK 500 5 TRP A 23 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 5 TRP A 23 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 5 TRP A 23 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES REMARK 500 5 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 5 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 217 ANGLE DEVIATIONS. 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 THR A 17 175.37 105.16 REMARK 500 1 TRP A 33 -154.04 -109.51 REMARK 500 1 HIS A 34 -65.57 -137.55 REMARK 500 1 ASN A 35 147.45 137.42 REMARK 500 1 CYS A 36 -1.33 -150.74 REMARK 500 1 HIS A 39 -112.79 -140.12 REMARK 500 1 ILE A 43 -75.61 -132.25 REMARK 500 2 VAL A 13 -156.90 -87.69 REMARK 500 2 CYS A 29 106.54 -45.78 REMARK 500 2 TRP A 33 -167.97 -105.69 REMARK 500 2 HIS A 34 -114.22 -135.50 REMARK 500 2 ASN A 35 134.99 -174.92 REMARK 500 2 CYS A 36 -52.35 -141.47 REMARK 500 3 ASP A 7 -2.98 -54.05 REMARK 500 3 VAL A 13 171.14 179.06 REMARK 500 3 THR A 17 128.23 90.91 REMARK 500 3 CYS A 29 108.97 -43.82 REMARK 500 3 SER A 31 101.87 -45.92 REMARK 500 3 TRP A 33 -168.54 -105.53 REMARK 500 3 HIS A 34 -70.61 -140.16 REMARK 500 3 ASN A 35 140.78 155.91 REMARK 500 3 CYS A 36 -7.65 -140.82 REMARK 500 3 ALA A 38 31.31 -77.79 REMARK 500 3 HIS A 39 -145.99 -132.58 REMARK 500 3 PRO A 41 -165.59 -79.13 REMARK 500 4 ASP A 7 15.32 -65.79 REMARK 500 4 VAL A 13 -132.91 45.46 REMARK 500 4 TRP A 33 -167.35 -116.65 REMARK 500 4 HIS A 34 -73.38 -127.34 REMARK 500 4 ASN A 35 150.77 143.06 REMARK 500 4 CYS A 36 -53.16 -151.46 REMARK 500 5 THR A 17 36.48 -156.53 REMARK 500 5 TRP A 33 -164.85 -116.49 REMARK 500 5 HIS A 34 -87.93 -126.39 REMARK 500 5 ASN A 35 149.76 149.90 REMARK 500 5 CYS A 36 -46.78 -150.78 REMARK 500 5 ALA A 38 49.82 -80.60 REMARK 500 5 HIS A 39 -52.26 -146.81 REMARK 500 5 THR A 42 33.38 -72.53 REMARK 500 5 ILE A 43 -41.94 -140.98 REMARK 500 6 ARG A 14 165.06 85.47 REMARK 500 6 TRP A 33 -162.56 -117.26 REMARK 500 6 HIS A 34 -114.82 -133.50 REMARK 500 6 ASN A 35 136.50 177.93 REMARK 500 6 CYS A 36 -46.63 -145.62 REMARK 500 6 ALA A 38 5.76 -66.12 REMARK 500 6 PRO A 41 -171.30 -68.15 REMARK 500 6 ILE A 43 -57.52 -123.84 REMARK 500 7 ASP A 7 -14.19 -49.29 REMARK 500 7 ARG A 14 135.81 83.14 REMARK 500 REMARK 500 THIS ENTRY HAS 163 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY A 40 PRO A 41 13 33.66 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 14 0.31 SIDE CHAIN REMARK 500 2 ARG A 14 0.32 SIDE CHAIN REMARK 500 3 ARG A 14 0.30 SIDE CHAIN REMARK 500 4 ARG A 14 0.26 SIDE CHAIN REMARK 500 5 ARG A 14 0.32 SIDE CHAIN REMARK 500 6 ARG A 14 0.29 SIDE CHAIN REMARK 500 7 ARG A 14 0.30 SIDE CHAIN REMARK 500 8 ARG A 14 0.30 SIDE CHAIN REMARK 500 9 ARG A 14 0.28 SIDE CHAIN REMARK 500 10 ARG A 14 0.32 SIDE CHAIN REMARK 500 11 ARG A 14 0.29 SIDE CHAIN REMARK 500 12 ARG A 14 0.32 SIDE CHAIN REMARK 500 13 ARG A 14 0.32 SIDE CHAIN REMARK 500 14 ARG A 14 0.32 SIDE CHAIN REMARK 500 15 ARG A 14 0.32 SIDE CHAIN REMARK 500 16 ARG A 14 0.32 SIDE CHAIN REMARK 500 17 ARG A 14 0.32 SIDE CHAIN REMARK 500 18 ARG A 14 0.27 SIDE CHAIN REMARK 500 19 ARG A 14 0.31 SIDE CHAIN REMARK 500 20 ARG A 14 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1AHL A 1 49 UNP P01530 TXAA_ANTXA 1 49 SEQRES 1 A 49 GLY VAL SER CYS LEU CYS ASP SER ASP GLY PRO SER VAL SEQRES 2 A 49 ARG GLY ASN THR LEU SER GLY THR LEU TRP LEU TYR PRO SEQRES 3 A 49 SER GLY CYS PRO SER GLY TRP HIS ASN CYS LYS ALA HIS SEQRES 4 A 49 GLY PRO THR ILE GLY TRP CYS CYS LYS GLN SHEET 1 A 4 VAL A 2 CYS A 4 0 SHEET 2 A 4 GLY A 20 TRP A 23 -1 O LEU A 22 N VAL A 2 SHEET 3 A 4 TRP A 45 LYS A 48 -1 N TRP A 45 O TRP A 23 SHEET 4 A 4 HIS A 34 LYS A 37 -1 N CYS A 36 O CYS A 46 SSBOND 1 CYS A 4 CYS A 46 1555 1555 2.02 SSBOND 2 CYS A 6 CYS A 36 1555 1555 2.02 SSBOND 3 CYS A 29 CYS A 47 1555 1555 2.02 CISPEP 1 GLY A 40 PRO A 41 1 6.72 CISPEP 2 GLY A 40 PRO A 41 2 25.44 CISPEP 3 GLY A 40 PRO A 41 3 1.51 CISPEP 4 GLY A 40 PRO A 41 4 4.61 CISPEP 5 GLY A 40 PRO A 41 5 8.04 CISPEP 6 GLY A 40 PRO A 41 6 4.57 CISPEP 7 GLY A 40 PRO A 41 7 8.97 CISPEP 8 GLY A 40 PRO A 41 8 25.46 CISPEP 9 GLY A 40 PRO A 41 9 -6.25 CISPEP 10 GLY A 40 PRO A 41 10 -7.94 CISPEP 11 GLY A 40 PRO A 41 11 16.75 CISPEP 12 GLY A 40 PRO A 41 12 -8.25 CISPEP 13 GLY A 40 PRO A 41 14 29.61 CISPEP 14 GLY A 40 PRO A 41 15 4.31 CISPEP 15 GLY A 40 PRO A 41 16 -4.99 CISPEP 16 GLY A 40 PRO A 41 17 -6.09 CISPEP 17 GLY A 40 PRO A 41 18 11.90 CISPEP 18 GLY A 40 PRO A 41 19 -5.27 CISPEP 19 GLY A 40 PRO A 41 20 8.00 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 29 2 Bytes