Header list of 1mvi.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN 02-AUG-96 1MVI
TITLE N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MVIIA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMEGA-CONOTOXIN MVIIA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS MAGUS;
SOURCE 3 ORGANISM_COMMON: MAGUS CONE;
SOURCE 4 ORGANISM_TAXID: 6492
KEYWDS CONUS MAGUS PEPTIDE SPECIFIC TO N-TYPE VOLTAGE SENSITIVE CALCIUM
KEYWDS 2 CHANNEL, NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.J.NIELSEN,L.THOMAS,R.J.LEWIS,P.F.ALEWOOD,D.J.CRAIK
REVDAT 3 29-NOV-17 1MVI 1 REMARK HELIX
REVDAT 2 24-FEB-09 1MVI 1 VERSN
REVDAT 1 12-AUG-97 1MVI 0
JRNL AUTH K.J.NIELSEN,L.THOMAS,R.J.LEWIS,P.F.ALEWOOD,D.J.CRAIK
JRNL TITL A CONSENSUS STRUCTURE FOR OMEGA-CONOTOXINS WITH DIFFERENT
JRNL TITL 2 SELECTIVITIES FOR VOLTAGE-SENSITIVE CALCIUM CHANNEL
JRNL TITL 3 SUBTYPES: COMPARISON OF MVIIA, SVIB AND SNX-202.
JRNL REF J.MOL.BIOL. V. 263 297 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8913308
JRNL DOI 10.1006/JMBI.1996.0576
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: A TOTAL OF 50 INITIAL STRUCTURES WERE
REMARK 3 CALCULATED USING A SIMULATED ANNEALING PROGRAM AS SUPPLIED WITH
REMARK 3 X-PLOR 3.1. THE FINAL 20 STRUCTURES WITH THE LOWEST OVERALL
REMARK 3 ENERGIES AND FEWEST VIOLATIONS OF NOE AND DIHEDRAL RESTRAINTS
REMARK 3 WERE ENERGY MINIMIZED IN X-PLOR USING THE CHARMM FORCEFIELD
REMARK 3 [BROOKS ET AL. (1983) J. COMPUT. CHEM., VOL. 4 187-217.]
REMARK 4
REMARK 4 1MVI 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_1000175176.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 3.
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : MD/SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW E AND FEW VIOLATIONS OF
REMARK 210 EXPERIMENTAL RESTRAINTS
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 4 93.76 -65.97
REMARK 500 1 CYS A 8 -157.96 -80.23
REMARK 500 1 ARG A 21 70.62 -118.93
REMARK 500 1 SER A 22 29.05 49.68
REMARK 500 2 CYS A 20 120.51 -26.63
REMARK 500 3 CYS A 20 120.51 -26.63
REMARK 500 4 CYS A 8 -159.94 -79.91
REMARK 500 4 CYS A 20 130.01 -31.86
REMARK 500 5 LYS A 7 91.07 -65.74
REMARK 500 5 CYS A 20 133.04 -28.58
REMARK 500 6 MET A 12 42.37 -144.36
REMARK 500 6 TYR A 13 66.94 -8.35
REMARK 500 6 CYS A 20 125.56 -21.10
REMARK 500 6 ARG A 21 66.72 -113.85
REMARK 500 7 MET A 12 38.42 -163.74
REMARK 500 7 TYR A 13 63.88 -4.74
REMARK 500 7 CYS A 20 120.62 -35.40
REMARK 500 7 ARG A 21 65.89 -117.02
REMARK 500 8 CYS A 20 130.42 -28.68
REMARK 500 9 LYS A 7 90.79 -63.87
REMARK 500 9 MET A 12 38.57 -156.87
REMARK 500 9 TYR A 13 64.39 -5.35
REMARK 500 9 CYS A 20 113.29 -25.08
REMARK 500 9 ARG A 21 67.77 -111.42
REMARK 500 10 CYS A 8 -157.69 -81.22
REMARK 500 10 CYS A 20 122.55 -33.17
REMARK 500 10 ARG A 21 66.10 -117.27
REMARK 500 11 LYS A 4 93.76 -65.97
REMARK 500 11 CYS A 8 -157.96 -80.23
REMARK 500 11 ARG A 21 70.62 -118.93
REMARK 500 11 SER A 22 29.05 49.68
REMARK 500 12 LYS A 7 94.17 -64.28
REMARK 500 12 MET A 12 50.89 -164.52
REMARK 500 12 TYR A 13 66.28 -7.33
REMARK 500 12 CYS A 20 120.96 -31.03
REMARK 500 12 ARG A 21 69.83 -119.09
REMARK 500 13 CYS A 8 -161.53 -102.26
REMARK 500 13 CYS A 20 121.32 -26.87
REMARK 500 13 ARG A 21 65.31 -119.59
REMARK 500 13 SER A 22 27.75 49.93
REMARK 500 14 CYS A 8 -157.79 -81.29
REMARK 500 14 CYS A 20 132.87 -35.83
REMARK 500 15 CYS A 8 -159.78 -79.79
REMARK 500 15 CYS A 20 120.58 -28.25
REMARK 500 15 ARG A 21 67.66 -116.35
REMARK 500 15 SER A 22 28.88 49.81
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 1MVI 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
SHEET 1 S1 3 CYS A 20 ARG A 21 0
SHEET 2 S1 3 GLY A 23 CYS A 25 -1 O LYS A 24 N ARG A 21
SHEET 3 S1 3 ALA A 6 CYS A 8 -1 N CYS A 8 O GLY A 23
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 N NH2 A 26 C CYS A 25 1555 1555 1.30
SITE 1 AC1 2 SER A 19 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 - 29 20 Bytes