Header list of 1srb.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 06-SEP-94 1SRB
TITLE CONFORMATIONAL STUDIES ON SRTB, A NON-SELECTIVE ENDOTHELIN RECEPTOR
TITLE 2 AGONIST, AND ON IRL 1620, AN ETB RECEPTOR SPECIFIC AGONIST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARAFOTOXINS PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ATRACTASPIS MICROLEPIDOTA ANDERSONI;
SOURCE 3 ORGANISM_TAXID: 8600;
SOURCE 4 STRAIN: ANDERSONI
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR R.SMITH,A.R.ATKINS
REVDAT 3 02-MAR-22 1SRB 1 REMARK
REVDAT 2 24-FEB-09 1SRB 1 VERSN
REVDAT 1 01-NOV-94 1SRB 0
JRNL AUTH A.R.ATKINS,R.C.MARTIN,R.SMITH
JRNL TITL 1H NMR STUDIES OF SARAFOTOXIN SRTB, A NONSELECTIVE
JRNL TITL 2 ENDOTHELIN RECEPTOR AGONIST, AND IRL 1620, AN ETB
JRNL TITL 3 RECEPTOR-SPECIFIC AGONIST.
JRNL REF BIOCHEMISTRY V. 34 2026 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7849060
JRNL DOI 10.1021/BI00006A024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.G.MILLS,A.R.ATKINS,T.HARVEY,F.K.JUNIUS,R.SMITH,G.F.KING
REMARK 1 TITL CONFORMATION OF SARAFOTOXIN-6B IN AQUEOUS SOLUTION
REMARK 1 TITL 2 DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY
REMARK 1 REF FEBS LETT. V. 282 247 1991
REMARK 1 REFN ISSN 0014-5793
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 1SRB 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_1000176474.
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 : 10
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 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 2 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 3 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 4 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 5 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 5 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 5 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 6 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 6 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 6 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 7 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 7 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 8 TRP A 21 CB - CG - CD1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 8 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 8 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 9 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 9 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 9 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 10 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 10 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 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 ASP A 5 21.64 100.80
REMARK 500 1 THR A 7 -145.40 -110.72
REMARK 500 1 TYR A 13 -3.91 -58.13
REMARK 500 1 HIS A 16 40.08 -102.74
REMARK 500 1 ASP A 18 70.22 -107.02
REMARK 500 2 SER A 2 83.75 14.97
REMARK 500 2 GLN A 17 67.92 69.92
REMARK 500 2 ASP A 18 73.25 -106.14
REMARK 500 3 LYS A 4 126.16 -24.50
REMARK 500 3 ASP A 5 35.00 33.69
REMARK 500 3 THR A 7 -159.14 -110.61
REMARK 500 3 ASP A 8 -61.46 -103.20
REMARK 500 3 LYS A 9 -36.46 -37.25
REMARK 500 3 CYS A 15 -63.05 -99.91
REMARK 500 3 GLN A 17 51.22 -118.59
REMARK 500 4 ASP A 5 37.53 90.34
REMARK 500 4 THR A 7 -114.86 -107.50
REMARK 500 4 ASP A 8 -64.83 -130.18
REMARK 500 4 TYR A 13 -18.70 -45.77
REMARK 500 4 ASP A 18 -73.51 -125.26
REMARK 500 5 CYS A 3 58.96 -104.08
REMARK 500 5 THR A 7 -157.07 -108.89
REMARK 500 5 ASP A 8 -67.74 -105.47
REMARK 500 5 HIS A 16 -47.22 -133.95
REMARK 500 6 ASP A 5 35.18 29.44
REMARK 500 6 THR A 7 -136.87 -112.83
REMARK 500 6 TYR A 13 -27.54 -37.12
REMARK 500 6 ASP A 18 -82.10 -119.78
REMARK 500 7 CYS A 3 -48.42 -130.92
REMARK 500 7 LYS A 4 58.11 9.61
REMARK 500 7 ASP A 5 -44.49 166.54
REMARK 500 7 THR A 7 -94.20 -94.39
REMARK 500 7 ASP A 8 -60.05 -145.02
REMARK 500 7 TYR A 13 -34.76 -38.71
REMARK 500 8 LYS A 4 82.80 54.40
REMARK 500 8 THR A 7 -153.18 -100.65
REMARK 500 8 ASP A 8 -61.96 -108.57
REMARK 500 8 HIS A 16 -66.05 -90.40
REMARK 500 8 ASP A 18 -67.00 -25.35
REMARK 500 9 CYS A 3 69.56 -114.28
REMARK 500 9 ASP A 8 -66.20 76.60
REMARK 500 9 HIS A 16 36.90 -94.29
REMARK 500 10 THR A 7 -154.40 -111.99
REMARK 500 10 ASP A 8 -75.27 -98.42
REMARK 500 10 GLN A 17 54.26 -112.32
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SRB A 1 21 UNP P13208 SRTX_ATREN 430 450
SEQRES 1 A 21 CYS SER CYS LYS ASP MET THR ASP LYS GLU CYS LEU TYR
SEQRES 2 A 21 PHE CYS HIS GLN ASP VAL ILE TRP
HELIX 1 1 ASP A 8 HIS A 16 1 9
SSBOND 1 CYS A 1 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 3 CYS A 11 1555 1555 2.02
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 - 2 20 Bytes