Header list of 1tr6.pdb file
Complete list - 17 20 Bytes
HEADER TOXIN 21-JUN-04 1TR6
TITLE NMR SOLUTION STRUCTURE OF OMEGA-CONOTOXIN [K10]GVIA, A CYCLIC CYSTEINE
TITLE 2 KNOT PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN GVIA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GVIA, GVIB, GVIC;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS GEOGRAPHUS;
SOURCE 3 ORGANISM_COMMON: GEOGRAPHY CONE;
SOURCE 4 ORGANISM_TAXID: 6491
KEYWDS CYSTEINE KNOT, FOUR-LOOP FRAME WORK, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.MOULD,T.YASUDA,C.I.SCHROEDER,A.M.BEEDLE,C.J.DOERING,G.W.ZAMPONI,
AUTHOR 2 D.J.ADAMS,R.J.LEWIS
REVDAT 5 17-SEP-14 1TR6 1 JRNL
REVDAT 4 05-OCT-11 1TR6 1 LINK SSBOND VERSN
REVDAT 3 24-FEB-09 1TR6 1 VERSN
REVDAT 2 12-OCT-04 1TR6 1 JRNL AUTHOR
REVDAT 1 13-JUL-04 1TR6 0
JRNL AUTH J.MOULD,T.YASUDA,C.I.SCHROEDER,A.M.BEEDLE,C.J.DOERING,
JRNL AUTH 2 G.W.ZAMPONI,D.J.ADAMS,R.J.LEWIS
JRNL TITL THE ALPHA2DELTA AUXILIARY SUBUNIT REDUCES AFFINITY OF
JRNL TITL 2 OMEGA-CONOTOXINS FOR RECOMBINANT N-TYPE (CAV2.2) CALCIUM
JRNL TITL 3 CHANNELS
JRNL REF J.BIOL.CHEM. V. 279 34705 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15166237
JRNL DOI 10.1074/JBC.M310848200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 467 NOE DISTANCE RESTRAINTS
REMARK 3 (INCLUDING H-BONDS) AND 22 DIHEDRAL ANGLE RESTRAINTS (16 PHI AND
REMARK 3 6 CHI) WERE USED DURING STRUCTURE CALCULATIONS.
REMARK 4
REMARK 4 1TR6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB022862.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275; 293
REMARK 210 PH : 3.5; 3.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM [K10]GVIA, DSS; 2 MM [K10]
REMARK 210 GVIA, DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; E-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : ARX; DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, X-PLOR 3.851
REMARK 210 METHOD USED : THE STRUCTURES WERE CALCULATED
REMARK 210 USING TORSION ANGLE DYNAMICS/
REMARK 210 SIMULATED ANNEALING PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 1 CYS A 15 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 1 CYS A 26 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 CYS A 8 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 CYS A 26 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 CYS A 15 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 3 CYS A 26 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 CYS A 8 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 5 CYS A 15 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 5 CYS A 26 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 7 CYS A 15 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 7 CYS A 26 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 8 CYS A 16 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 9 CYS A 26 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 12 CYS A 15 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 12 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 12 CYS A 26 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 14 CYS A 15 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 14 CYS A 26 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 15 CYS A 15 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 15 CYS A 26 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 16 CYS A 8 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 17 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.1 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 HYP A 4 40.43 -78.47
REMARK 500 1 SER A 7 91.14 -65.32
REMARK 500 1 CYS A 8 -152.69 -89.60
REMARK 500 1 SER A 9 -120.00 -162.16
REMARK 500 1 ASN A 14 21.11 -77.94
REMARK 500 1 ARG A 17 -85.53 -89.35
REMARK 500 2 SER A 7 93.89 -57.25
REMARK 500 2 SER A 9 171.75 -59.85
REMARK 500 2 SER A 12 25.92 -143.19
REMARK 500 2 TYR A 13 94.59 -55.62
REMARK 500 2 ARG A 17 -83.75 -108.65
REMARK 500 2 SER A 18 -175.18 -175.63
REMARK 500 2 THR A 23 -7.62 -144.05
REMARK 500 3 HYP A 4 84.34 -65.67
REMARK 500 3 SER A 9 -76.29 -98.21
REMARK 500 3 LYS A 10 -54.66 -143.40
REMARK 500 3 ARG A 17 -83.69 -89.24
REMARK 500 3 THR A 23 -20.96 -150.11
REMARK 500 4 SER A 7 98.48 -63.85
REMARK 500 4 SER A 9 -152.32 -80.86
REMARK 500 4 ARG A 17 -121.99 -89.59
REMARK 500 4 THR A 23 -17.33 -150.14
REMARK 500 5 THR A 11 -139.31 -88.62
REMARK 500 5 SER A 12 73.59 49.97
REMARK 500 5 TYR A 13 40.51 -81.88
REMARK 500 5 ARG A 17 -85.53 -103.82
REMARK 500 5 SER A 18 166.32 179.28
REMARK 500 5 THR A 23 -16.33 -150.72
REMARK 500 6 SER A 7 95.07 -59.94
REMARK 500 6 SER A 9 54.85 -145.01
REMARK 500 6 THR A 11 26.71 -140.42
REMARK 500 6 SER A 12 -52.53 -152.80
REMARK 500 6 TYR A 13 12.44 57.58
REMARK 500 6 ARG A 17 -91.72 -89.79
REMARK 500 7 LYS A 10 -70.14 63.53
REMARK 500 7 ARG A 17 -94.08 -90.58
REMARK 500 7 LYS A 24 30.93 35.13
REMARK 500 7 ARG A 25 -168.02 -127.32
REMARK 500 8 SER A 7 91.79 -55.18
REMARK 500 8 SER A 9 -50.71 -143.22
REMARK 500 8 LYS A 10 -47.76 -167.55
REMARK 500 8 SER A 12 39.46 -88.77
REMARK 500 8 ARG A 17 -111.81 -89.44
REMARK 500 8 SER A 18 -156.35 -163.79
REMARK 500 8 LYS A 24 29.21 49.34
REMARK 500 9 SER A 7 96.41 -50.64
REMARK 500 9 SER A 9 -65.03 -151.80
REMARK 500 9 LYS A 10 19.75 -148.43
REMARK 500 9 TYR A 13 21.98 -67.42
REMARK 500 9 ASN A 14 115.51 68.17
REMARK 500
REMARK 500 THIS ENTRY HAS 117 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 28
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OMC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CONOTOXIN GVIA USING 2-D NMR
REMARK 900 SPECTROSCOPY AND RELAXATION MATRIX ANALYSIS.
REMARK 900 RELATED ID: 2CCO RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CALCIUM CHANNEL BLOCKER CONOTOXIN GVIA,
REMARK 900 NMR, 20 STRUCTURES
DBREF 1TR6 A 1 27 UNP P01522 CXO6_CONGE 46 72
SEQADV 1TR6 LYS A 10 UNP P01522 PRO 55 ENGINEERED MUTATION
SEQRES 1 A 28 CYS LYS SER HYP GLY SER SER CYS SER LYS THR SER TYR
SEQRES 2 A 28 ASN CYS CYS ARG SER CYS ASN HYP TYR THR LYS ARG CYS
SEQRES 3 A 28 TYR NH2
MODRES 1TR6 HYP A 4 PRO 4-HYDROXYPROLINE
MODRES 1TR6 HYP A 21 PRO 4-HYDROXYPROLINE
HET HYP A 4 15
HET HYP A 21 15
HET NH2 A 28 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP 2(C5 H9 N O3)
FORMUL 1 NH2 H2 N
SHEET 1 A 2 CYS A 19 ASN A 20 0
SHEET 2 A 2 ARG A 25 CYS A 26 -1 O ARG A 25 N ASN A 20
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.01
SSBOND 2 CYS A 8 CYS A 19 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.02
LINK C SER A 3 N HYP A 4 1555 1555 1.32
LINK C HYP A 4 N GLY A 5 1555 1555 1.30
LINK C TYR A 27 N NH2 A 28 1555 1555 1.30
LINK C ASN A 20 N HYP A 21 1555 1555 1.32
LINK C HYP A 21 N TYR A 22 1555 1555 1.31
SITE 1 AC1 1 TYR A 27
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 - 17 20 Bytes