Header list of 1av3.pdb file
Complete list - 16 20 Bytes
HEADER POTASSIUM CHANNEL BLOCKER 24-SEP-97 1AV3
TITLE POTASSIUM CHANNEL BLOCKER KAPPA CONOTOXIN PVIIA FROM C. PURPURASCENS,
TITLE 2 NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAPPA-CONOTOXIN PVIIA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CGX-1051,FIN-POPPING PEPTIDE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: CONUS PURPURASCENS;
SOURCE 4 ORGANISM_COMMON: PURPLE CONE;
SOURCE 5 ORGANISM_TAXID: 41690
KEYWDS KAPPA-CONOTOXIN, POTASSIUM CHANNEL BLOCKER, CYSTINE KNOT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.SCANLON,D.NARANJO,L.THOMAS,P.F.ALEWOOD,R.J.LEWIS,D.J.CRAIK
REVDAT 4 16-DEC-20 1AV3 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQADV HET HETNAM FORMUL
REVDAT 4 3 1 LINK
REVDAT 3 24-FEB-09 1AV3 1 VERSN
REVDAT 2 18-NOV-98 1AV3 2 COMPND REMARK TITLE JRNL
REVDAT 2 2 2 HEADER MODRES CONECT
REVDAT 1 14-OCT-98 1AV3 0
JRNL AUTH M.J.SCANLON,D.NARANJO,L.THOMAS,P.F.ALEWOOD,R.J.LEWIS,
JRNL AUTH 2 D.J.CRAIK
JRNL TITL SOLUTION STRUCTURE AND PROPOSED BINDING MECHANISM OF A NOVEL
JRNL TITL 2 POTASSIUM CHANNEL TOXIN KAPPA-CONOTOXIN PVIIA.
JRNL REF STRUCTURE V. 5 1585 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9438859
JRNL DOI 10.1016/S0969-2126(97)00307-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.TERLAU,K.-J.SHON,M.GRILLEY,M.STOCKER,W.STUHMER,B.M.OLIVERA
REMARK 1 TITL STRATEGY FOR RAPID IMMOBILISATION OF PREY BY A FISH HUNTING
REMARK 1 TITL 2 MARINE SNAIL
REMARK 1 REF NATURE V. 381 148 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1AV3 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_1000171294.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; ECOSY; TOCSY (50 AND 80
REMARK 210 MS) AND NOESY (80; 150; 250 MS)
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX 750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND AGREEMENT WITH
REMARK 210 EXPERIMENTAL RESTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H NMR SPECTROSCOPY ON
REMARK 210 SYNTHETIC PVIIA
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 5 CYS A 1 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 6 CYS A 1 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 7 CYS A 1 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 8 CYS A 1 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 9 CYS A 1 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 10 CYS A 1 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 14 CYS A 1 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 17 CYS A 1 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 20 CYS A 1 CA - CB - SG ANGL. DEV. = 6.7 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 ASN A 5 10.76 48.89
REMARK 500 1 LYS A 7 103.46 -47.73
REMARK 500 1 ASP A 13 93.82 -68.42
REMARK 500 2 ASN A 5 7.96 52.39
REMARK 500 2 LEU A 12 70.92 -113.87
REMARK 500 3 ASN A 5 -7.80 58.96
REMARK 500 3 LYS A 7 107.28 -51.79
REMARK 500 3 ARG A 18 27.77 43.87
REMARK 500 3 ASN A 21 -172.42 -67.97
REMARK 500 4 HYP A 4 153.93 -45.06
REMARK 500 4 ASN A 5 -7.89 64.36
REMARK 500 4 LYS A 7 103.44 -47.61
REMARK 500 4 LEU A 12 47.93 -90.93
REMARK 500 5 HYP A 4 158.14 -48.53
REMARK 500 5 ASN A 5 -2.72 60.07
REMARK 500 5 LYS A 7 103.10 -47.21
REMARK 500 6 ASN A 5 26.39 46.24
REMARK 500 6 LYS A 7 99.10 -49.64
REMARK 500 6 ASN A 21 -178.92 -68.60
REMARK 500 7 ASN A 5 -10.39 68.19
REMARK 500 7 LYS A 7 106.37 -54.92
REMARK 500 7 ASN A 21 -176.96 -66.48
REMARK 500 8 HYP A 4 158.09 -46.85
REMARK 500 8 ASN A 5 1.67 52.83
REMARK 500 8 LEU A 12 70.37 -111.97
REMARK 500 9 ASN A 5 10.78 48.61
REMARK 500 9 LYS A 7 98.05 -44.00
REMARK 500 9 LEU A 12 68.18 -102.18
REMARK 500 9 CYS A 15 156.35 -47.51
REMARK 500 10 HYP A 4 151.90 -47.30
REMARK 500 10 ASN A 5 -0.80 60.04
REMARK 500 10 LYS A 7 105.20 -48.66
REMARK 500 10 ASP A 13 97.80 -69.02
REMARK 500 10 ARG A 18 29.62 44.10
REMARK 500 11 ASN A 5 11.13 47.10
REMARK 500 11 LYS A 7 104.96 -50.84
REMARK 500 12 ASN A 5 -10.46 74.27
REMARK 500 12 LYS A 7 103.53 -53.31
REMARK 500 12 LEU A 12 58.19 -92.02
REMARK 500 12 ASN A 21 -175.40 -62.79
REMARK 500 13 HYP A 4 156.34 -48.30
REMARK 500 13 ASN A 5 -13.45 64.82
REMARK 500 13 CYS A 8 -159.02 -141.77
REMARK 500 13 ASN A 21 -173.68 -65.26
REMARK 500 14 ASN A 5 -10.66 63.71
REMARK 500 14 LYS A 7 105.43 -51.68
REMARK 500 14 LEU A 12 55.81 -91.17
REMARK 500 14 ASN A 21 -173.98 -60.42
REMARK 500 15 ASN A 5 0.21 59.37
REMARK 500 15 LYS A 7 99.57 -45.82
REMARK 500
REMARK 500 THIS ENTRY HAS 68 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 ARG A 2 0.29 SIDE CHAIN
REMARK 500 1 ARG A 18 0.32 SIDE CHAIN
REMARK 500 1 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 2 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.30 SIDE CHAIN
REMARK 500 2 ARG A 22 0.29 SIDE CHAIN
REMARK 500 3 ARG A 2 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.31 SIDE CHAIN
REMARK 500 3 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 2 0.26 SIDE CHAIN
REMARK 500 4 ARG A 18 0.26 SIDE CHAIN
REMARK 500 4 ARG A 22 0.30 SIDE CHAIN
REMARK 500 5 ARG A 2 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.32 SIDE CHAIN
REMARK 500 5 ARG A 22 0.32 SIDE CHAIN
REMARK 500 6 ARG A 2 0.30 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 22 0.31 SIDE CHAIN
REMARK 500 7 ARG A 2 0.20 SIDE CHAIN
REMARK 500 7 ARG A 18 0.26 SIDE CHAIN
REMARK 500 7 ARG A 22 0.32 SIDE CHAIN
REMARK 500 8 ARG A 2 0.28 SIDE CHAIN
REMARK 500 8 ARG A 18 0.30 SIDE CHAIN
REMARK 500 8 ARG A 22 0.31 SIDE CHAIN
REMARK 500 9 ARG A 2 0.28 SIDE CHAIN
REMARK 500 9 ARG A 18 0.31 SIDE CHAIN
REMARK 500 9 ARG A 22 0.31 SIDE CHAIN
REMARK 500 10 ARG A 2 0.31 SIDE CHAIN
REMARK 500 10 ARG A 18 0.32 SIDE CHAIN
REMARK 500 10 ARG A 22 0.32 SIDE CHAIN
REMARK 500 11 ARG A 2 0.31 SIDE CHAIN
REMARK 500 11 ARG A 18 0.30 SIDE CHAIN
REMARK 500 11 ARG A 22 0.32 SIDE CHAIN
REMARK 500 12 ARG A 2 0.31 SIDE CHAIN
REMARK 500 12 ARG A 18 0.32 SIDE CHAIN
REMARK 500 12 ARG A 22 0.32 SIDE CHAIN
REMARK 500 13 ARG A 2 0.31 SIDE CHAIN
REMARK 500 13 ARG A 18 0.26 SIDE CHAIN
REMARK 500 13 ARG A 22 0.31 SIDE CHAIN
REMARK 500 14 ARG A 2 0.32 SIDE CHAIN
REMARK 500 14 ARG A 18 0.31 SIDE CHAIN
REMARK 500 14 ARG A 22 0.31 SIDE CHAIN
REMARK 500 15 ARG A 2 0.31 SIDE CHAIN
REMARK 500 15 ARG A 18 0.30 SIDE CHAIN
REMARK 500 15 ARG A 22 0.31 SIDE CHAIN
REMARK 500 16 ARG A 2 0.32 SIDE CHAIN
REMARK 500 16 ARG A 18 0.22 SIDE CHAIN
REMARK 500 16 ARG A 22 0.32 SIDE CHAIN
REMARK 500 17 ARG A 2 0.30 SIDE CHAIN
REMARK 500 17 ARG A 18 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AV3 A 1 27 UNP P56633 O17A_CONPU 46 72
SEQRES 1 A 27 CYS ARG ILE HYP ASN GLN LYS CYS PHE GLN HIS LEU ASP
SEQRES 2 A 27 ASP CYS CYS SER ARG LYS CYS ASN ARG PHE ASN LYS CYS
SEQRES 3 A 27 VAL
MODRES 1AV3 HYP A 4 PRO MODIFIED RESIDUE
HET HYP A 4 15
HETNAM HYP 4-HYDROXYPROLINE
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP C5 H9 N O3
HELIX 1 1 GLN A 10 LEU A 12 5 3
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.02
LINK C ILE A 3 N HYP A 4 1555 1555 1.32
LINK C HYP A 4 N ASN A 5 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 - 16 20 Bytes