Header list of 1dw5.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 24-JAN-00 1DW5
TITLE NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE
TITLE 2 BRIDGES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE NATURALLY OCCURS IN CONUS MAGUS (MAGUS CONE)
KEYWDS CONOTOXIN, CALCIUM CHANNEL, CONFORMATIONAL EXCHANGE, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR R.A.ATKINSON,B.KIEFFER,A.DEJAEGERE,F.SIROCKIN,J.-F.LEFEVRE
REVDAT 6 16-FEB-22 1DW5 1 REMARK LINK
REVDAT 5 24-FEB-09 1DW5 1 VERSN
REVDAT 4 01-APR-03 1DW5 1 JRNL
REVDAT 3 28-JUN-00 1DW5 1 SOURCE
REVDAT 2 10-MAY-00 1DW5 1 JRNL ATOM COMPND SSBOND
REVDAT 2 2 1 SEQRES SEQADV
REVDAT 1 01-MAR-00 1DW5 0
JRNL AUTH R.A.ATKINSON,B.KIEFFER,A.DEJAEGERE,F.SIROCKIN,J.F.LEFEVRE
JRNL TITL STRUCTURAL AND DYNAMIC CHARACTERIZATION OF OMEGA-CONOTOXIN
JRNL TITL 2 MVIIA: THE BINDING LOOP EXHIBITS SLOW CONFORMATIONAL
JRNL TITL 3 EXCHANGE.
JRNL REF BIOCHEMISTRY V. 39 3908 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10747778
JRNL DOI 10.1021/BI992651H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.2, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SUBSTRUCTURE EMBEDDING BY DISTANCE
REMARK 3 GEOMETRY, SIMULATED ANNEALING REGULARISATION OF FULL STRUCTURE,
REMARK 3 SIMULATED ANNEALING REFINEMENT
REMARK 4
REMARK 4 1DW5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010429.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283.00
REMARK 210 PH : 3.50
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D COSY; 2D HOHAHA; 2D
REMARK 210 13C-1H HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.10, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: TEMPERATURE DEPENDENCE OF CHEMICAL SHIFTS, NH EXCHANGE
REMARK 210 INTO D2O, RELAXATION MEASUREMENTS AT 500 AND 600 MHZ
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 LYS A 2 H CYS A 16 1.55
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 LYS A 4 159.81 -43.56
REMARK 500 1 LYS A 7 154.98 56.33
REMARK 500 1 CYS A 8 -147.33 178.37
REMARK 500 1 SER A 9 -142.52 -137.28
REMARK 500 1 LEU A 11 77.28 83.96
REMARK 500 1 TYR A 13 52.51 70.69
REMARK 500 1 THR A 17 75.55 -154.34
REMARK 500 1 SER A 19 -164.55 -127.37
REMARK 500 2 LYS A 4 157.88 -49.46
REMARK 500 2 LYS A 7 156.17 55.41
REMARK 500 2 CYS A 8 -165.57 177.47
REMARK 500 2 SER A 9 -145.14 -101.53
REMARK 500 2 LEU A 11 -105.91 -133.08
REMARK 500 2 MET A 12 -58.16 67.41
REMARK 500 2 TYR A 13 45.49 71.02
REMARK 500 2 SER A 19 -158.96 -137.09
REMARK 500 2 SER A 22 13.49 59.84
REMARK 500 3 LYS A 7 155.32 55.79
REMARK 500 3 CYS A 8 -175.17 178.84
REMARK 500 3 SER A 9 -142.01 -98.68
REMARK 500 3 ARG A 10 -62.45 -92.34
REMARK 500 4 LYS A 7 145.09 -22.51
REMARK 500 4 SER A 9 -122.87 -93.92
REMARK 500 4 TYR A 13 38.13 70.29
REMARK 500 4 THR A 17 -144.57 -99.42
REMARK 500 4 SER A 22 24.64 47.43
REMARK 500 5 LYS A 2 -167.11 -113.21
REMARK 500 5 ALA A 6 73.89 -69.42
REMARK 500 5 LYS A 7 150.30 -31.59
REMARK 500 5 SER A 9 -125.75 -94.99
REMARK 500 5 TYR A 13 80.57 53.28
REMARK 500 5 ASP A 14 -38.25 -136.35
REMARK 500 5 SER A 22 22.62 48.19
REMARK 500 6 LYS A 4 156.53 -45.30
REMARK 500 6 LYS A 7 151.33 56.41
REMARK 500 6 CYS A 8 -151.06 177.73
REMARK 500 6 SER A 9 -123.48 -115.27
REMARK 500 6 LEU A 11 70.33 -150.58
REMARK 500 6 SER A 22 23.55 47.72
REMARK 500 7 ALA A 6 26.68 -80.00
REMARK 500 7 LYS A 7 155.55 55.43
REMARK 500 7 CYS A 8 -158.67 -179.20
REMARK 500 7 SER A 9 -102.37 -106.96
REMARK 500 7 ARG A 10 -44.36 -140.23
REMARK 500 7 LEU A 11 39.01 -140.22
REMARK 500 7 TYR A 13 73.14 60.85
REMARK 500 7 THR A 17 72.04 -153.18
REMARK 500 8 LYS A 2 -166.75 -107.48
REMARK 500 8 LYS A 7 149.14 -28.44
REMARK 500 8 SER A 9 -101.20 -94.07
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
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 1DW5 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 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 - 16 20 Bytes