Header list of 1omc.pdb file
Complete list - 29 20 Bytes
HEADER PRESYNAPTIC NEUROTOXIN 28-APR-93 1OMC
TITLE SOLUTION STRUCTURE OF OMEGA-CONOTOXIN GVIA USING 2-D NMR SPECTROSCOPY
TITLE 2 AND RELAXATION MATRIX ANALYSIS
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
KEYWDS PRESYNAPTIC NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR J.H.DAVIS,E.K.BRADLEY,G.P.MILJANICH,L.NADASDI,J.RAMACHANDRAN,
AUTHOR 2 V.J.BASUS
REVDAT 4 29-NOV-17 1OMC 1 REMARK HELIX
REVDAT 3 24-FEB-09 1OMC 1 VERSN
REVDAT 2 03-SEP-97 1OMC 1 COMPND
REVDAT 1 31-JAN-94 1OMC 0
JRNL AUTH J.H.DAVIS,E.K.BRADLEY,G.P.MILJANICH,L.NADASDI,
JRNL AUTH 2 J.RAMACHANDRAN,V.J.BASUS
JRNL TITL SOLUTION STRUCTURE OF OMEGA-CONOTOXIN GVIA USING 2-D NMR
JRNL TITL 2 SPECTROSCOPY AND RELAXATION MATRIX ANALYSIS.
JRNL REF BIOCHEMISTRY V. 32 7396 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8338837
JRNL DOI 10.1021/BI00080A009
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.RIVIER,R.GALYEAN,W.R.GRAY,A.AZIMI-ZONOOZ,J.M.MCINTOSH,
REMARK 1 AUTH 2 L.J.CRUZ,B.M.OLIVERA
REMARK 1 TITL NEURONAL CALCIUM CHANNEL INHIBITORS
REMARK 1 REF J.BIOL.CHEM. V. 262 1194 1987
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.M.OLIVERA,J.M.MCINTOSH,L.J.CRUZ,F.A.LUQUE,W.R.GRAY
REMARK 1 TITL PURIFICATION AND SEQUENCE OF A PRESYNAPTIC PEPTIDE TOXIN
REMARK 1 TITL 2 FROM CONUS GEOGRAPHUS VENOM
REMARK 1 REF BIOCHEMISTRY V. 23 5087 1984
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OMC 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_1000175470.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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
REMARK 500 REMARK: NULL
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. = 3.5 DEGREES
REMARK 500 1 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 TYR A 22 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 TYR A 22 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 3 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 4 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 6 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 TYR A 27 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 7 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 TYR A 13 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 15 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 15 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 15 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 16 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 17 TYR A 27 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 19 TYR A 22 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 19 TYR A 27 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 21 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.4 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 ASN A 14 42.40 -81.50
REMARK 500 1 SER A 18 149.63 -36.70
REMARK 500 2 ASN A 14 37.64 -74.13
REMARK 500 2 SER A 18 152.58 -22.17
REMARK 500 3 ASN A 14 35.36 -78.11
REMARK 500 3 SER A 18 144.80 -8.69
REMARK 500 4 TYR A 13 37.95 -90.92
REMARK 500 4 ASN A 14 39.73 -87.57
REMARK 500 4 SER A 18 151.55 -1.77
REMARK 500 5 TYR A 13 49.25 -75.36
REMARK 500 5 ASN A 14 44.50 -96.00
REMARK 500 5 SER A 18 139.85 21.75
REMARK 500 6 TYR A 13 39.54 -75.88
REMARK 500 7 LYS A 2 -9.70 -53.76
REMARK 500 7 SER A 3 140.68 63.83
REMARK 500 7 TYR A 13 25.93 -67.94
REMARK 500 7 ASN A 14 43.66 -91.60
REMARK 500 8 SER A 3 144.08 -39.85
REMARK 500 8 SER A 12 85.38 -152.67
REMARK 500 8 SER A 18 163.65 65.74
REMARK 500 9 ASN A 14 36.36 -82.05
REMARK 500 9 SER A 18 148.58 16.67
REMARK 500 10 SER A 3 143.76 -28.26
REMARK 500 10 TYR A 13 46.06 -79.82
REMARK 500 10 ASN A 14 35.44 -87.03
REMARK 500 10 SER A 18 154.62 -8.90
REMARK 500 11 ASN A 14 39.07 -85.12
REMARK 500 11 SER A 18 167.22 66.70
REMARK 500 12 SER A 3 132.31 -35.85
REMARK 500 12 HYP A 10 -9.33 -58.12
REMARK 500 12 TYR A 13 48.56 -81.35
REMARK 500 12 ASN A 14 46.70 -90.53
REMARK 500 12 SER A 18 148.55 -18.29
REMARK 500 13 SER A 12 73.27 -117.51
REMARK 500 13 TYR A 13 37.01 -72.92
REMARK 500 13 ASN A 14 37.33 -97.71
REMARK 500 13 SER A 18 177.41 67.62
REMARK 500 14 HYP A 10 -3.16 -56.47
REMARK 500 14 ASN A 14 42.35 -84.14
REMARK 500 14 SER A 18 154.21 -10.57
REMARK 500 15 TYR A 13 41.05 -69.14
REMARK 500 15 ASN A 14 36.21 -81.74
REMARK 500 15 SER A 18 169.59 67.65
REMARK 500 16 ASN A 14 42.99 -89.20
REMARK 500 16 SER A 18 171.53 61.52
REMARK 500 17 TYR A 13 36.32 33.55
REMARK 500 17 ASN A 14 30.79 -76.00
REMARK 500 17 SER A 18 154.25 -15.29
REMARK 500 18 SER A 12 67.75 -102.57
REMARK 500 18 TYR A 13 43.92 -75.71
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 TYR A 22 0.14 SIDE CHAIN
REMARK 500 2 TYR A 13 0.10 SIDE CHAIN
REMARK 500 2 TYR A 22 0.12 SIDE CHAIN
REMARK 500 2 ARG A 25 0.10 SIDE CHAIN
REMARK 500 2 TYR A 27 0.08 SIDE CHAIN
REMARK 500 3 TYR A 13 0.19 SIDE CHAIN
REMARK 500 3 TYR A 27 0.13 SIDE CHAIN
REMARK 500 4 TYR A 13 0.07 SIDE CHAIN
REMARK 500 4 TYR A 27 0.09 SIDE CHAIN
REMARK 500 5 TYR A 22 0.11 SIDE CHAIN
REMARK 500 6 TYR A 13 0.09 SIDE CHAIN
REMARK 500 6 TYR A 27 0.12 SIDE CHAIN
REMARK 500 7 TYR A 27 0.09 SIDE CHAIN
REMARK 500 8 TYR A 13 0.13 SIDE CHAIN
REMARK 500 8 TYR A 27 0.10 SIDE CHAIN
REMARK 500 9 ARG A 17 0.10 SIDE CHAIN
REMARK 500 10 TYR A 13 0.14 SIDE CHAIN
REMARK 500 10 ARG A 25 0.08 SIDE CHAIN
REMARK 500 11 ARG A 17 0.11 SIDE CHAIN
REMARK 500 12 TYR A 13 0.11 SIDE CHAIN
REMARK 500 13 TYR A 13 0.09 SIDE CHAIN
REMARK 500 14 TYR A 13 0.10 SIDE CHAIN
REMARK 500 14 TYR A 22 0.07 SIDE CHAIN
REMARK 500 14 TYR A 27 0.10 SIDE CHAIN
REMARK 500 15 TYR A 13 0.09 SIDE CHAIN
REMARK 500 15 ARG A 17 0.08 SIDE CHAIN
REMARK 500 15 TYR A 27 0.10 SIDE CHAIN
REMARK 500 16 TYR A 22 0.11 SIDE CHAIN
REMARK 500 17 TYR A 22 0.07 SIDE CHAIN
REMARK 500 19 TYR A 22 0.10 SIDE CHAIN
REMARK 500 20 TYR A 22 0.13 SIDE CHAIN
REMARK 500 20 TYR A 27 0.08 SIDE CHAIN
REMARK 500 21 TYR A 22 0.11 SIDE CHAIN
REMARK 500 21 TYR A 27 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 HYP A 10 -10.33
REMARK 500 1 SER A 18 -10.02
REMARK 500 3 HYP A 21 -11.13
REMARK 500 4 ARG A 17 11.04
REMARK 500 5 ARG A 17 12.19
REMARK 500 5 HYP A 21 -10.23
REMARK 500 9 TYR A 13 -10.09
REMARK 500 9 ARG A 17 16.09
REMARK 500 11 TYR A 13 -10.39
REMARK 500 14 HYP A 21 -10.37
REMARK 500 15 SER A 6 -10.06
REMARK 500 16 TYR A 13 -12.25
REMARK 500 17 TYR A 13 -12.18
REMARK 500 19 TYR A 13 -12.05
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 1OMC A 1 27 UNP P01522 CXO6_CONGE 46 72
SEQADV 1OMC HYP A 4 UNP P01522 PRO 49 CONFLICT
SEQADV 1OMC HYP A 10 UNP P01522 PRO 55 CONFLICT
SEQADV 1OMC HYP A 21 UNP P01522 PRO 66 CONFLICT
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 1OMC HYP A 4 PRO 4-HYDROXYPROLINE
MODRES 1OMC HYP A 10 PRO 4-HYDROXYPROLINE
MODRES 1OMC 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 S1 3 SER A 6 CYS A 8 0
SHEET 2 S1 3 LYS A 24 TYR A 27 -1 N CYS A 26 O SER A 6
SHEET 3 S1 3 SER A 18 HYP A 21 -1 N ASN A 20 O ARG A 25
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.04
SSBOND 2 CYS A 8 CYS A 19 1555 1555 2.04
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.03
LINK C SER A 3 N HYP A 4 1555 1555 1.34
LINK C HYP A 4 N GLY A 5 1555 1555 1.33
LINK C TYR A 27 N NH2 A 28 1555 1555 1.36
LINK C SER A 9 N HYP A 10 1555 1555 1.34
LINK C HYP A 10 N THR A 11 1555 1555 1.34
LINK C ASN A 20 N HYP A 21 1555 1555 1.34
LINK C HYP A 21 N TYR A 22 1555 1555 1.34
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 - 29 20 Bytes