Header list of 1r9i.pdb file
Complete list - 25 20 Bytes
HEADER TOXIN 30-OCT-03 1R9I
TITLE NMR SOLUTION STRUCTURE OF PIIIA TOXIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MU-CONOTOXIN PIIIA;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS PURPURASCENS;
SOURCE 3 ORGANISM_TAXID: 41690
KEYWDS CONOTOXIN, CYSTEINE KNOT, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.NIELSEN,M.WATSON,D.J.ADAMS,A.K.HAMMARSTROM,P.W.GAGE,J.M.HILL,
AUTHOR 2 D.J.CRAIK,L.THOMAS,D.ADAMS,P.F.ALEWOOD,R.J.LEWIS
REVDAT 3 25-DEC-19 1R9I 1 REMARK SEQADV SEQRES LINK
REVDAT 2 24-FEB-09 1R9I 1 VERSN
REVDAT 1 18-NOV-03 1R9I 0
JRNL AUTH K.J.NIELSEN,M.WATSON,D.J.ADAMS,A.K.HAMMARSTROM,P.W.GAGE,
JRNL AUTH 2 J.M.HILL,D.J.CRAIK,L.THOMAS,D.ADAMS,P.F.ALEWOOD,R.J.LEWIS
JRNL TITL SOLUTION STRUCTURE OF MU-CONOTOXIN PIIIA, A PREFERENTIAL
JRNL TITL 2 INHIBITOR OF PERSISTENT TETRODOTOXIN-SENSITIVE SODIUM
JRNL TITL 3 CHANNELS
JRNL REF J.BIOL.CHEM. V. 277 27247 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12006587
JRNL DOI 10.1074/JBC.M201611200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR, X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020604.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 3.0; 5.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : NULL; NULL
REMARK 210 SAMPLE CONTENTS : 2MM PIIIA, 95% H2O, 5% D2O; 2MM
REMARK 210 PIIIA, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA, UXNMR, X-PLOR 3.8
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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. = 8.6 DEGREES
REMARK 500 1 CYS A 16 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 CYS A 21 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 CYS A 4 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 CYS A 21 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 3 CYS A 4 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 4 CYS A 11 CA - CB - SG ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 CYS A 11 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 7 CYS A 11 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 8 CYS A 11 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 8 CYS A 21 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 9 CYS A 4 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 9 CYS A 16 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 10 CYS A 11 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 11 CYS A 4 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 11 CYS A 11 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 11 CYS A 16 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 12 CYS A 4 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 12 CYS A 11 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 13 CYS A 4 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 14 CYS A 11 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 14 CYS A 21 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 15 CYS A 4 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 15 CYS A 16 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 15 CYS A 21 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 16 CYS A 4 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 16 CYS A 11 CA - CB - SG ANGL. DEV. = 9.4 DEGREES
REMARK 500 17 CYS A 4 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 17 CYS A 11 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 18 CYS A 11 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 18 CYS A 21 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 19 CYS A 4 CA - CB - SG ANGL. DEV. = 9.3 DEGREES
REMARK 500 19 CYS A 16 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 20 CYS A 4 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 20 CYS A 5 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 20 CYS A 11 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 20 CYS A 21 CA - CB - SG ANGL. DEV. = 10.5 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 ARG A 2 46.20 -86.56
REMARK 500 1 LEU A 3 -132.12 -60.77
REMARK 500 2 LEU A 3 -72.56 -56.08
REMARK 500 2 CYS A 5 53.26 -90.79
REMARK 500 3 HYP A 18 1.50 -67.51
REMARK 500 6 LEU A 3 -117.02 -76.11
REMARK 500 6 CYS A 11 -30.55 -37.51
REMARK 500 7 ARG A 2 41.21 -104.86
REMARK 500 8 CYS A 11 -33.33 -35.40
REMARK 500 8 HYP A 18 1.36 -67.09
REMARK 500 9 ARG A 2 64.23 -108.96
REMARK 500 9 LEU A 3 -76.64 -92.20
REMARK 500 10 ARG A 2 59.29 -90.45
REMARK 500 10 LEU A 3 -88.69 -64.58
REMARK 500 10 CYS A 11 -30.86 -39.23
REMARK 500 11 LEU A 3 -70.44 -81.74
REMARK 500 13 LEU A 3 -121.06 -82.74
REMARK 500 13 CYS A 5 46.69 -88.13
REMARK 500 14 LEU A 3 -157.67 -68.76
REMARK 500 14 CYS A 11 -26.07 -37.30
REMARK 500 15 ARG A 2 50.29 -119.51
REMARK 500 15 LEU A 3 -112.84 -89.94
REMARK 500 15 CYS A 11 -5.60 -57.35
REMARK 500 15 HYP A 18 15.79 -65.75
REMARK 500 16 LEU A 3 -107.13 -78.53
REMARK 500 17 ARG A 2 40.77 -94.85
REMARK 500 17 LEU A 3 -147.25 -91.62
REMARK 500 17 CYS A 5 44.50 -87.52
REMARK 500 18 CYS A 11 -35.92 -39.17
REMARK 500 19 LEU A 3 -118.03 -95.27
REMARK 500 19 CYS A 11 -7.16 -59.92
REMARK 500 20 LEU A 3 -105.89 -77.61
REMARK 500 20 CYS A 11 -27.93 -34.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R9I A 1 22 UNP P58925 CXM3A_CONPU 4 25
SEQADV 1R9I HYP A 8 UNP P58925 PRO 11 MODIFIED RESIDUE
SEQADV 1R9I HYP A 18 UNP P58925 PRO 21 MODIFIED RESIDUE
SEQADV 1R9I CY3 A 22 UNP P58925 CYS 25 MODIFIED RESIDUE
SEQRES 1 A 22 PCA ARG LEU CYS CYS GLY PHE HYP LYS SER CYS ARG SER
SEQRES 2 A 22 ARG GLN CYS LYS HYP HIS ARG CYS CY3
MODRES 1R9I PCA A 1 GLN PYROGLUTAMIC ACID
MODRES 1R9I HYP A 8 PRO 4-HYDROXYPROLINE
MODRES 1R9I HYP A 18 PRO 4-HYDROXYPROLINE
MODRES 1R9I CY3 A 22 CYS 2-AMINO-3-MERCAPTO-PROPIONAMIDE
HET PCA A 1 14
HET HYP A 8 15
HET HYP A 18 15
HET CY3 A 22 13
HETNAM PCA PYROGLUTAMIC ACID
HETNAM HYP 4-HYDROXYPROLINE
HETNAM CY3 2-AMINO-3-MERCAPTO-PROPIONAMIDE
HETSYN HYP HYDROXYPROLINE
FORMUL 1 PCA C5 H7 N O3
FORMUL 1 HYP 2(C5 H9 N O3)
FORMUL 1 CY3 C3 H8 N2 O S
HELIX 1 1 LYS A 9 SER A 13 5 5
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.01
SSBOND 2 CYS A 5 CYS A 21 1555 1555 2.02
LINK C PCA A 1 N ARG A 2 1555 1555 1.31
LINK C PHE A 7 N HYP A 8 1555 1555 1.32
LINK C HYP A 8 N LYS A 9 1555 1555 1.31
LINK SG CYS A 11 SG CY3 A 22 1555 1555 2.02
LINK C CYS A 21 N CY3 A 22 1555 1555 1.31
LINK C LYS A 17 N HYP A 18 1555 1555 1.32
LINK C HYP A 18 N HIS A 19 1555 1555 1.31
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 - 25 20 Bytes