Header list of 2fr9.pdb file
Complete list - 9 20 Bytes
HEADER TOXIN 19-JAN-06 2FR9
TITLE NMR STRUCTURE OF THE ALPHA-CONOTOXIN GI (SER12)-BENZOYLPHENYLALANINE
TITLE 2 DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN GI;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: CONUS GEOGRAPHUS;
SOURCE 4 ORGANISM_COMMON: CONUS GEOGRAPHUS;
SOURCE 5 ORGANISM_TAXID: 6491;
SOURCE 6 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED.
KEYWDS ALPHA-CONOTOXIN GI, BENZOPHENONE ANALOGS, NICOTINIC ACETYLCHOLINE
KEYWDS 2 RECEPTOR ANTAGONIST, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR V.S.PASHKOV,I.V.MASLENNIKOV,I.E.KASHEVEROV,M.N.ZHMAK,Y.N.UTKIN,
AUTHOR 2 V.I.TSETLIN,A.S.ARSENIEV
REVDAT 3 09-MAR-22 2FR9 1 SOURCE REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2FR9 1 VERSN
REVDAT 1 30-MAY-06 2FR9 0
JRNL AUTH I.E.KASHEVEROV,D.C.CHIARA,M.N.ZHMAK,I.V.MASLENNIKOV,
JRNL AUTH 2 V.S.PASHKOV,A.S.ARSENIEV,Y.N.UTKIN,J.B.COHEN,V.I.TSETLIN
JRNL TITL ALPHA-CONOTOXIN GI BENZOYLPHENYLALANINE DERIVATIVES.
JRNL TITL 2 (1)H-NMR STRUCTURES AND PHOTOAFFINITY LABELING OF THE
JRNL TITL 3 TORPEDO CALIFORNICA NICOTINIC ACETYLCHOLINE RECEPTOR.
JRNL REF FEBS J. V. 273 1373 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16689926
JRNL DOI 10.1111/J.1742-4658.2006.05161.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, BRAUN AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FR9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036216.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313.0
REMARK 210 PH : 3.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 10 MM PBF12-GI, 85% H2O/15% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-NMR SPECTROSCOPY ON
REMARK 210 SYNTHETIC (PFB12)-GI ANALOGUE.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO A 5 H GLY A 8 1.51
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 CYS A 2 87.19 -162.22
REMARK 500 1 HIS A 10 30.40 -95.13
REMARK 500 1 PBF A 12 115.32 -160.80
REMARK 500 2 CYS A 2 87.29 -162.25
REMARK 500 2 HIS A 10 30.33 -95.26
REMARK 500 2 PBF A 12 111.64 -160.83
REMARK 500 3 CYS A 2 87.28 -162.24
REMARK 500 3 HIS A 10 40.67 -95.25
REMARK 500 4 CYS A 2 97.67 -162.26
REMARK 500 4 HIS A 10 35.54 -95.20
REMARK 500 5 CYS A 2 94.77 -162.27
REMARK 500 5 HIS A 10 41.56 -95.05
REMARK 500 6 CYS A 2 89.75 -162.23
REMARK 500 6 HIS A 10 45.52 -95.32
REMARK 500 6 PBF A 12 102.65 -160.86
REMARK 500 7 CYS A 2 96.73 -162.31
REMARK 500 7 HIS A 10 45.04 -95.28
REMARK 500 7 PBF A 12 113.24 -160.84
REMARK 500 8 CYS A 2 87.08 -162.21
REMARK 500 8 HIS A 10 49.37 -95.25
REMARK 500 8 PBF A 12 115.63 -160.77
REMARK 500 9 CYS A 2 95.79 -162.29
REMARK 500 9 HIS A 10 46.76 -95.24
REMARK 500 10 CYS A 2 87.52 -162.26
REMARK 500 10 HIS A 10 35.75 -95.17
REMARK 500 11 CYS A 2 91.19 -162.31
REMARK 500 11 HIS A 10 46.63 -95.20
REMARK 500 12 CYS A 2 87.87 -162.30
REMARK 500 12 HIS A 10 40.63 -95.27
REMARK 500 13 CYS A 2 94.34 -162.29
REMARK 500 13 HIS A 10 46.75 -95.18
REMARK 500 13 PBF A 12 115.58 -160.74
REMARK 500 14 CYS A 2 87.35 -162.20
REMARK 500 14 HIS A 10 36.14 -95.22
REMARK 500 15 CYS A 2 91.02 -162.21
REMARK 500 15 HIS A 10 46.84 -95.19
REMARK 500 15 PBF A 12 109.01 -160.71
REMARK 500 16 CYS A 2 87.34 -162.22
REMARK 500 16 HIS A 10 46.94 -95.18
REMARK 500 17 CYS A 2 96.59 -162.30
REMARK 500 17 HIS A 10 40.36 -95.19
REMARK 500 18 CYS A 2 95.47 -162.08
REMARK 500 18 HIS A 10 53.71 -95.27
REMARK 500 18 PBF A 12 118.65 -160.81
REMARK 500 19 CYS A 2 97.02 -162.04
REMARK 500 19 HIS A 10 46.37 -95.21
REMARK 500 20 CYS A 2 87.37 -162.26
REMARK 500 20 HIS A 10 30.48 -95.19
REMARK 500 21 CYS A 2 87.19 -162.21
REMARK 500 21 HIS A 10 55.21 -95.25
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FR9 A 1 13 UNP P01519 CXAA_CONGE 1 13
SEQADV 2FR9 PBF A 12 UNP P01519 SER 12 MODIFIED RESIDUE
SEQRES 1 A 13 GLU CYS CYS ASN PRO ALA CYS GLY ARG HIS TYR PBF CYS
MODRES 2FR9 PBF A 12 PHE PARA-(BENZOYL)-PHENYLALANINE
HET PBF A 12 32
HETNAM PBF PARA-(BENZOYL)-PHENYLALANINE
FORMUL 1 PBF C16 H15 N O3
HELIX 1 1 ASN A 4 TYR A 11 5 8
SSBOND 1 CYS A 2 CYS A 7 1555 1555 1.96
SSBOND 2 CYS A 3 CYS A 13 1555 1555 2.28
LINK C TYR A 11 N PBF A 12 1555 1555 1.35
LINK C PBF A 12 N CYS A 13 1555 1555 1.32
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 - 9 20 Bytes