Header list of 1omg.pdb file
Complete list - 23 20 Bytes
HEADER PRESYNAPTIC NEUROTOXIN 26-APR-95 1OMG
TITLE NMR STUDY OF OMEGA-CONOTOXIN MVIIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIA;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS MAGUS;
SOURCE 3 ORGANISM_COMMON: MAGUS CONE;
SOURCE 4 ORGANISM_TAXID: 6492
KEYWDS PRESYNAPTIC NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR T.KOHNO,J.-I.KIM,K.KOBAYASHI,Y.KODERA,T.MAEDA,K.SATO
REVDAT 4 23-FEB-22 1OMG 1 REMARK LINK
REVDAT 3 24-FEB-09 1OMG 1 VERSN
REVDAT 2 01-APR-03 1OMG 1 JRNL
REVDAT 1 03-APR-96 1OMG 0
JRNL AUTH T.KOHNO,J.I.KIM,K.KOBAYASHI,Y.KODERA,T.MAEDA,K.SATO
JRNL TITL THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE CALCIUM
JRNL TITL 2 CHANNEL BLOCKER OMEGA-CONOTOXIN MVIIA.
JRNL REF BIOCHEMISTRY V. 34 10256 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7640281
JRNL DOI 10.1021/BI00032A020
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.M.OLIVERA,L.J.CRUZ,V.DE SANTOS,G.W.LECHEMINANT,D.GRIFFIN,
REMARK 1 AUTH 2 R.ZEIKUS,J.M.MCINTSH,R.GALYEAN,J.VARGA,W.R.GRAY,J.RIVIER
REMARK 1 TITL NEURAL CALCIUM CHANNEL ANTAGONISTS. DISCRIMINATION BETWEEN
REMARK 1 TITL 2 CALCIUM CHANNEL SUBTYPES USING OMEGA-CONOTOXIN FROM CONUS
REMARK 1 TITL 3 MAGUS VENOM
REMARK 1 REF BIOCHEMISTRY V. 26 2086 1987
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 1OMG 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_1000175474.
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 : 13
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: 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 LYS A 2 -150.26 -118.41
REMARK 500 1 MET A 12 52.61 -101.13
REMARK 500 1 CYS A 20 98.71 -171.27
REMARK 500 2 LYS A 2 -128.02 -114.21
REMARK 500 2 LYS A 4 135.42 -37.65
REMARK 500 2 MET A 12 50.68 -112.06
REMARK 500 2 SER A 19 -158.06 -115.70
REMARK 500 2 CYS A 20 93.59 -161.79
REMARK 500 3 LYS A 2 -126.50 -122.73
REMARK 500 3 LYS A 4 154.27 -37.67
REMARK 500 3 SER A 19 -158.87 -139.29
REMARK 500 3 CYS A 20 93.35 -167.14
REMARK 500 3 SER A 22 -1.35 77.16
REMARK 500 4 LYS A 2 -129.21 -113.94
REMARK 500 4 LYS A 4 145.49 -37.56
REMARK 500 4 MET A 12 54.85 -117.96
REMARK 500 4 SER A 19 -154.27 -150.98
REMARK 500 4 CYS A 20 101.26 -161.44
REMARK 500 5 ARG A 10 -27.60 -37.83
REMARK 500 5 TYR A 13 127.51 64.30
REMARK 500 5 CYS A 20 87.91 -176.64
REMARK 500 6 MET A 12 48.19 -100.06
REMARK 500 7 LYS A 2 -126.16 -121.35
REMARK 500 7 LYS A 4 152.43 -37.50
REMARK 500 7 ARG A 10 -27.95 -37.20
REMARK 500 7 TYR A 13 114.29 60.56
REMARK 500 7 ASP A 14 28.56 -141.27
REMARK 500 7 THR A 17 51.98 -149.51
REMARK 500 7 CYS A 20 98.02 -169.99
REMARK 500 7 SER A 22 -1.65 78.07
REMARK 500 8 MET A 12 49.17 -103.58
REMARK 500 8 THR A 17 65.42 -151.48
REMARK 500 8 SER A 19 -156.28 -150.49
REMARK 500 8 CYS A 20 99.85 -171.78
REMARK 500 9 LYS A 2 -159.96 -135.69
REMARK 500 9 MET A 12 45.78 -107.24
REMARK 500 9 SER A 19 -158.66 -117.77
REMARK 500 9 CYS A 20 92.06 -174.54
REMARK 500 10 LYS A 2 -147.30 -124.98
REMARK 500 10 TYR A 13 135.28 59.84
REMARK 500 10 ASP A 14 21.41 -147.57
REMARK 500 10 SER A 19 -157.20 -150.72
REMARK 500 11 LYS A 2 -156.12 -133.79
REMARK 500 11 MET A 12 47.89 -101.31
REMARK 500 11 THR A 17 53.96 -148.46
REMARK 500 11 SER A 19 -158.76 -127.94
REMARK 500 11 CYS A 20 99.77 -174.53
REMARK 500 11 SER A 22 -4.36 79.10
REMARK 500 12 TYR A 13 127.33 56.27
REMARK 500 12 CYS A 20 98.96 -170.62
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 10 0.26 SIDE CHAIN
REMARK 500 2 ARG A 10 0.08 SIDE CHAIN
REMARK 500 2 ARG A 21 0.32 SIDE CHAIN
REMARK 500 3 ARG A 10 0.25 SIDE CHAIN
REMARK 500 3 ARG A 21 0.22 SIDE CHAIN
REMARK 500 4 ARG A 10 0.32 SIDE CHAIN
REMARK 500 4 ARG A 21 0.32 SIDE CHAIN
REMARK 500 5 ARG A 10 0.15 SIDE CHAIN
REMARK 500 5 ARG A 21 0.24 SIDE CHAIN
REMARK 500 6 ARG A 10 0.23 SIDE CHAIN
REMARK 500 6 ARG A 21 0.19 SIDE CHAIN
REMARK 500 7 ARG A 10 0.12 SIDE CHAIN
REMARK 500 7 ARG A 21 0.22 SIDE CHAIN
REMARK 500 8 ARG A 10 0.22 SIDE CHAIN
REMARK 500 8 ARG A 21 0.22 SIDE CHAIN
REMARK 500 9 ARG A 10 0.24 SIDE CHAIN
REMARK 500 9 ARG A 21 0.24 SIDE CHAIN
REMARK 500 10 ARG A 10 0.22 SIDE CHAIN
REMARK 500 10 ARG A 21 0.32 SIDE CHAIN
REMARK 500 11 ARG A 10 0.32 SIDE CHAIN
REMARK 500 11 ARG A 21 0.27 SIDE CHAIN
REMARK 500 12 ARG A 10 0.18 SIDE CHAIN
REMARK 500 12 ARG A 21 0.28 SIDE CHAIN
REMARK 500 13 ARG A 10 0.32 SIDE CHAIN
REMARK 500 13 ARG A 21 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 26
DBREF 1OMG A 1 25 UNP P05484 CXO7A_CONMA 1 25
SEQRES 1 A 26 CYS LYS GLY LYS GLY ALA LYS CYS SER ARG LEU MET TYR
SEQRES 2 A 26 ASP CYS CYS THR GLY SER CYS ARG SER GLY LYS CYS NH2
HET NH2 A 26 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
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 25 1555 1555 2.02
LINK C CYS A 25 N NH2 A 26 1555 1555 1.30
SITE 1 AC1 3 SER A 19 LYS A 24 CYS A 25
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 - 23 20 Bytes