Header list of 2cco.pdb file
Complete list - 9 20 Bytes
HEADER TOXIN 13-FEB-98 2CCO
TITLE STRUCTURE OF THE CALCIUM CHANNEL BLOCKER OMEGA CONOTOXIN GVIA, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN GVIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS GEOGRAPHUS;
SOURCE 3 ORGANISM_COMMON: GEOGRAPHY CONE;
SOURCE 4 ORGANISM_TAXID: 6491;
SOURCE 5 ORGAN: VENOM GLAND
KEYWDS CONOTOXIN, CYSTINE KNOT, INHIBITOR CYSTINE KNOT MOTIF, CALCIUM
KEYWDS 2 CHANNEL BLOCKER, CONE-SHELL, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.K.PALLAGHY,R.S.NORTON
REVDAT 4 09-MAR-22 2CCO 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2CCO 1 VERSN
REVDAT 2 01-APR-03 2CCO 1 JRNL
REVDAT 1 15-JUL-98 2CCO 0
SPRSDE 15-JUL-98 2CCO 1CCO
JRNL AUTH P.K.PALLAGHY,R.S.NORTON
JRNL TITL REFINED SOLUTION STRUCTURE OF OMEGA-CONOTOXIN GVIA:
JRNL TITL 2 IMPLICATIONS FOR CALCIUM CHANNEL BINDING
JRNL REF J.PEPT.RES. V. 53 343 1999
JRNL REFN ISSN 1397-002X
JRNL PMID 10231724
JRNL DOI 10.1034/J.1399-3011.1999.00040.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMULATED ANNEALING OF DIANA
REMARK 3 STRUCTURES
REMARK 4
REMARK 4 2CCO 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_1000177903.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 3.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY; DQF; AMIDE
REMARK 210 EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA/X-PLOR
REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL, NOE & DIHEDRAL 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 ARG A 17 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 SER A 9 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 3 ARG A 17 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 6 ARG A 17 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 6 ARG A 25 NH1 - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 6 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 7 SER A 9 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 7 ARG A 25 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 11 ARG A 25 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 12 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 13 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 14 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 14 ARG A 25 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 15 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 16 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 19 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 20 ARG A 17 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 20 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -4.0 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 SER A 18 -174.13 157.62
REMARK 500 1 HYP A 21 -4.04 -40.77
REMARK 500 1 THR A 23 -44.58 -144.35
REMARK 500 1 LYS A 24 43.74 84.35
REMARK 500 2 ARG A 17 -59.97 -122.05
REMARK 500 2 SER A 18 -178.35 176.45
REMARK 500 2 HYP A 21 -13.30 -36.33
REMARK 500 2 THR A 23 -38.59 -141.94
REMARK 500 2 LYS A 24 44.08 75.32
REMARK 500 3 THR A 11 52.08 -118.67
REMARK 500 3 ARG A 17 -51.18 -122.56
REMARK 500 3 SER A 18 -175.25 161.44
REMARK 500 3 HYP A 21 2.94 -52.80
REMARK 500 3 THR A 23 -41.19 -141.63
REMARK 500 3 LYS A 24 43.27 85.65
REMARK 500 4 CYS A 8 -161.25 -122.84
REMARK 500 4 CYS A 16 29.22 -75.80
REMARK 500 4 ARG A 17 -37.36 -146.39
REMARK 500 4 SER A 18 -176.26 134.91
REMARK 500 4 HYP A 21 1.51 -45.80
REMARK 500 4 THR A 23 -36.51 -133.48
REMARK 500 4 LYS A 24 37.25 82.55
REMARK 500 5 HYP A 4 145.18 -36.14
REMARK 500 5 CYS A 8 -166.83 -121.65
REMARK 500 5 CYS A 16 28.84 -74.19
REMARK 500 5 ARG A 17 -44.99 -144.31
REMARK 500 5 SER A 18 -174.12 140.67
REMARK 500 5 HYP A 21 2.48 -51.00
REMARK 500 5 THR A 23 -41.48 -137.86
REMARK 500 5 LYS A 24 44.61 86.85
REMARK 500 6 ARG A 17 -53.80 -126.13
REMARK 500 6 SER A 18 179.73 175.22
REMARK 500 6 HYP A 21 -1.09 -48.62
REMARK 500 6 THR A 23 -40.02 -136.60
REMARK 500 6 LYS A 24 43.89 80.06
REMARK 500 7 HYP A 4 139.54 -39.71
REMARK 500 7 TYR A 13 21.47 84.87
REMARK 500 7 ARG A 17 -57.45 -127.31
REMARK 500 7 HYP A 21 -1.85 -44.34
REMARK 500 7 THR A 23 -40.52 -142.05
REMARK 500 7 LYS A 24 37.50 77.44
REMARK 500 8 HYP A 4 150.00 -41.78
REMARK 500 8 ARG A 17 -59.75 -126.58
REMARK 500 8 SER A 18 -179.54 178.56
REMARK 500 8 HYP A 21 -4.94 -37.12
REMARK 500 8 THR A 23 -34.58 -136.13
REMARK 500 8 LYS A 24 43.23 78.61
REMARK 500 9 CYS A 8 -156.26 -128.85
REMARK 500 9 HYP A 10 -37.55 -39.51
REMARK 500 9 ARG A 17 -52.24 -124.89
REMARK 500
REMARK 500 THIS ENTRY HAS 118 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 17 0.31 SIDE CHAIN
REMARK 500 1 ARG A 25 0.32 SIDE CHAIN
REMARK 500 2 ARG A 17 0.31 SIDE CHAIN
REMARK 500 2 ARG A 25 0.30 SIDE CHAIN
REMARK 500 3 ARG A 17 0.31 SIDE CHAIN
REMARK 500 3 ARG A 25 0.23 SIDE CHAIN
REMARK 500 4 ARG A 17 0.32 SIDE CHAIN
REMARK 500 4 ARG A 25 0.21 SIDE CHAIN
REMARK 500 5 ARG A 17 0.18 SIDE CHAIN
REMARK 500 5 ARG A 25 0.25 SIDE CHAIN
REMARK 500 6 ARG A 17 0.31 SIDE CHAIN
REMARK 500 6 ARG A 25 0.32 SIDE CHAIN
REMARK 500 7 ARG A 17 0.31 SIDE CHAIN
REMARK 500 7 ARG A 25 0.31 SIDE CHAIN
REMARK 500 8 ARG A 17 0.31 SIDE CHAIN
REMARK 500 8 ARG A 25 0.32 SIDE CHAIN
REMARK 500 9 ARG A 17 0.29 SIDE CHAIN
REMARK 500 9 ARG A 25 0.12 SIDE CHAIN
REMARK 500 10 ARG A 17 0.23 SIDE CHAIN
REMARK 500 10 ARG A 25 0.32 SIDE CHAIN
REMARK 500 11 ARG A 17 0.29 SIDE CHAIN
REMARK 500 11 ARG A 25 0.31 SIDE CHAIN
REMARK 500 12 ARG A 17 0.24 SIDE CHAIN
REMARK 500 12 ARG A 25 0.29 SIDE CHAIN
REMARK 500 13 ARG A 17 0.31 SIDE CHAIN
REMARK 500 13 ARG A 25 0.13 SIDE CHAIN
REMARK 500 14 ARG A 17 0.10 SIDE CHAIN
REMARK 500 14 ARG A 25 0.32 SIDE CHAIN
REMARK 500 15 ARG A 17 0.30 SIDE CHAIN
REMARK 500 15 ARG A 25 0.30 SIDE CHAIN
REMARK 500 16 ARG A 17 0.29 SIDE CHAIN
REMARK 500 16 ARG A 25 0.20 SIDE CHAIN
REMARK 500 17 ARG A 17 0.25 SIDE CHAIN
REMARK 500 17 ARG A 25 0.22 SIDE CHAIN
REMARK 500 18 ARG A 17 0.31 SIDE CHAIN
REMARK 500 18 ARG A 25 0.30 SIDE CHAIN
REMARK 500 19 ARG A 17 0.27 SIDE CHAIN
REMARK 500 19 ARG A 25 0.11 SIDE CHAIN
REMARK 500 20 ARG A 17 0.29 SIDE CHAIN
REMARK 500 20 ARG A 25 0.28 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 28
DBREF 2CCO A 1 27 UNP P01522 CXO6_CONGE 46 72
SEQADV 2CCO HYP A 4 UNP P01522 PRO 49 MODIFIED RESIDUE
SEQADV 2CCO HYP A 10 UNP P01522 PRO 55 MODIFIED RESIDUE
SEQADV 2CCO HYP A 21 UNP P01522 PRO 66 MODIFIED RESIDUE
SEQRES 1 A 28 CYS LYS SER HYP GLY SER SER CYS SER HYP 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 2CCO HYP A 4 PRO 4-HYDROXYPROLINE
MODRES 2CCO HYP A 10 PRO 4-HYDROXYPROLINE
MODRES 2CCO HYP A 21 PRO 4-HYDROXYPROLINE
HET HYP A 4 15
HET HYP A 10 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 3(C5 H9 N O3)
FORMUL 1 NH2 H2 N
SHEET 1 1 3 SER A 6 CYS A 8 0
SHEET 2 1 3 LYS A 24 TYR A 27 -1 O LYS A 24 N CYS A 8
SHEET 3 1 3 SER A 18 ASN A 20 -1 O ASN A 20 N ARG A 25
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 19 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.03
LINK C SER A 3 N HYP A 4 1555 1555 1.30
LINK C HYP A 4 N GLY A 5 1555 1555 1.30
LINK C SER A 9 N HYP A 10 1555 1555 1.32
LINK C HYP A 10 N THR A 11 1555 1555 1.30
LINK C ASN A 20 N HYP A 21 1555 1555 1.31
LINK C HYP A 21 N TYR A 22 1555 1555 1.32
LINK C TYR A 27 N NH2 A 28 1555 1555 1.30
SITE 1 AC1 3 HYP A 4 CYS A 26 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 - 9 20 Bytes