Header list of 1g1z.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 16-OCT-00 1G1Z
TITLE NMR SOLUTION STRUCTURES OF DELTA-CONOTOXIN EVIA FROM CONUS ERMINEUS
TITLE 2 THAT SELECTIVELY ACTS ON VERTEBRATE NEURONAL NA+ CHANNELS, LEU12-
TITLE 3 PRO13 CIS ISOMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONOTOXIN EVIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: THIS STRUCTURE IS IN EQUILIBRIUM WITH THE LEU12-PRO13
COMPND 6 TRANS ISOMER (1G1P).
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SOLID PHASE SYNTHESIS OF CONOTOXIN EVIA WAS
SOURCE 4 CARRIED OUT USING THE F-MOC CHEMISTRY. THE SEQUENCE OF THE PEPTIDE
SOURCE 5 IS NATURALLY FOUND IN CONUS ERMINEUS (ATLANTIC FISH-HUNTING CONE).
KEYWDS THREE DISULFIDE LINKAGES, CIS/TRANS ISOMERISM OF LEU12-PRO13 PEPTIDE
KEYWDS 2 BOND, HYDROXYPROLINE, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR L.VOLPON,H.LAMTHANH,F.LE GALL,A.MENEZ,J.M.LANCELIN
REVDAT 5 23-FEB-22 1G1Z 1 REMARK LINK
REVDAT 4 24-FEB-09 1G1Z 1 VERSN
REVDAT 3 18-MAY-04 1G1Z 1 JRNL
REVDAT 2 13-JAN-04 1G1Z 1 JRNL REMARK
REVDAT 1 01-NOV-00 1G1Z 0
JRNL AUTH L.VOLPON,H.LAMTHANH,J.BARBIER,N.GILLES,J.M.LANCELIN
JRNL TITL NMR SOLUTION STRUCTURES OF DELTA-CONOTOXIN EVIA FROM CONUS
JRNL TITL 2 ERMINEUS THAT SELECTIVELY ACTS ON VERTEBRATE NEURONAL NA+
JRNL TITL 3 CHANNELS.
JRNL REF J.BIOL.CHEM. V. 279 21356 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14976206
JRNL DOI 10.1074/JBC.M309594200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.BARBIER,H.LAMTHANH,F.LE GALL,P.FAVREAU,E.BENOIT,H.CHEN,
REMARK 1 AUTH 2 N.GILLES,N.ILAN,S.F.HEINEMANN,D.GORDON,A.MENEZ,J.MOLGO
REMARK 1 TITL CONOTOXIN EVIA, A NOVEL PEPTIDE FROM CONUS ERMINEUS VENOM
REMARK 1 TITL 2 THAT PREFERENTIALLY ACTS ON NEURONAL VOLTAGE-DEPENDENT
REMARK 1 TITL 3 SODIUM CHANNELS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851, CHARMM 22
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR), BROOKS
REMARK 3 (CHARMM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 257 RESTRAINTS, 211 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 24
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 22 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1G1Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012133.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM CONOTOXIN EVIA; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.22
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 DYNAMICAL SIMULATED ANNEALING
REMARK 210 WITH THE ALLHDG FORCE FIELD AND
REMARK 210 SIMULATED ANNEALING WITH THE
REMARK 210 CHARMM22 FORCE FIELD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 2 LEU A 32 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 3 LEU A 32 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 4 SER A 11 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 5 GLY A 18 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 8 LEU A 32 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 9 LEU A 32 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 10 LEU A 12 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 10 GLY A 18 N - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 13 ILE A 14 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 13 GLY A 18 N - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 13 LEU A 32 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 14 LEU A 12 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 14 GLY A 18 N - CA - C ANGL. DEV. = -16.0 DEGREES
REMARK 500 14 LEU A 32 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 15 LEU A 32 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 17 LYS A 16 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 18 VAL A 26 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 18 LEU A 32 N - CA - C ANGL. DEV. = -17.8 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 ASP A 2 -170.68 -172.67
REMARK 500 1 CYS A 10 -123.31 -111.21
REMARK 500 1 LEU A 15 -63.13 -137.45
REMARK 500 1 ASN A 17 -166.66 -162.05
REMARK 500 1 VAL A 26 60.49 -160.32
REMARK 500 1 ALA A 30 -153.86 -150.37
REMARK 500 2 CYS A 3 -177.88 -176.46
REMARK 500 2 VAL A 26 54.79 -145.03
REMARK 500 2 ALA A 30 -153.26 -129.84
REMARK 500 3 ASP A 2 -71.99 -97.29
REMARK 500 3 ASN A 17 -109.63 -89.57
REMARK 500 3 VAL A 26 48.10 -144.99
REMARK 500 3 ALA A 30 -143.70 -143.94
REMARK 500 4 ILE A 14 -46.04 -150.03
REMARK 500 4 LEU A 15 -151.73 -117.33
REMARK 500 4 LYS A 16 59.96 -91.81
REMARK 500 4 ASN A 17 -122.71 -83.84
REMARK 500 4 VAL A 26 49.07 -150.59
REMARK 500 4 ALA A 30 -162.36 -129.32
REMARK 500 5 PRO A 13 -77.24 -69.72
REMARK 500 5 LEU A 15 -98.19 -140.44
REMARK 500 5 ASN A 17 -173.35 177.19
REMARK 500 5 ALA A 30 -145.25 -142.16
REMARK 500 6 SER A 11 -125.24 -164.09
REMARK 500 6 LEU A 15 -35.47 79.08
REMARK 500 6 ASN A 17 -129.63 -133.85
REMARK 500 6 VAL A 26 56.57 -151.36
REMARK 500 6 ALA A 30 -153.37 -145.12
REMARK 500 7 CYS A 10 -115.00 -109.60
REMARK 500 7 SER A 11 -163.30 -167.15
REMARK 500 7 LEU A 15 -79.08 -124.72
REMARK 500 7 ASN A 17 -50.06 -160.36
REMARK 500 7 VAL A 26 58.65 -160.03
REMARK 500 7 ALA A 30 -150.09 -140.65
REMARK 500 8 ASP A 2 -77.75 -88.79
REMARK 500 8 LEU A 15 -48.58 75.19
REMARK 500 8 ASN A 17 -70.07 -80.50
REMARK 500 8 VAL A 26 -130.39 -115.71
REMARK 500 8 ALA A 30 -154.75 -133.44
REMARK 500 8 ASP A 31 -163.59 -124.88
REMARK 500 9 LEU A 15 -77.09 -137.00
REMARK 500 9 ASN A 17 175.41 176.91
REMARK 500 9 VAL A 26 44.39 -144.53
REMARK 500 9 ALA A 30 -151.87 -152.58
REMARK 500 10 ASP A 2 -103.69 69.66
REMARK 500 10 LEU A 15 -64.00 -108.92
REMARK 500 10 LYS A 16 42.01 -152.24
REMARK 500 10 ASN A 17 -144.37 -90.49
REMARK 500 10 VAL A 26 -132.37 -130.04
REMARK 500 11 ILE A 14 -112.87 42.08
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 1 ASP A 2 15 147.83
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 33
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G1P RELATED DB: PDB
REMARK 900 1G1P REPRESENTS THE CONOTOXIN EVIA WITH THE LEU12-PRO13 TRANS
REMARK 900 PEPTIDE BOND.
DBREF 1G1Z A 1 32 UNP P60513 CXD6A_CONER 1 32
SEQRES 1 A 33 ASP ASP CYS ILE LYS HYP TYR GLY PHE CYS SER LEU PRO
SEQRES 2 A 33 ILE LEU LYS ASN GLY LEU CYS CYS SER GLY ALA CYS VAL
SEQRES 3 A 33 GLY VAL CYS ALA ASP LEU NH2
MODRES 1G1Z HYP A 6 PRO 4-HYDROXYPROLINE
HET HYP A 6 15
HET NH2 A 33 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP C5 H9 N O3
FORMUL 1 NH2 H2 N
SHEET 1 A 2 ALA A 24 CYS A 25 0
SHEET 2 A 2 CYS A 29 ALA A 30 -1 N ALA A 30 O ALA A 24
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 25 1555 1555 2.03
SSBOND 3 CYS A 20 CYS A 29 1555 1555 2.01
LINK C LYS A 5 N HYP A 6 1555 1555 1.33
LINK C HYP A 6 N TYR A 7 1555 1555 1.36
LINK C LEU A 32 N NH2 A 33 1555 1555 1.36
CISPEP 1 LEU A 12 PRO A 13 1 -6.31
CISPEP 2 LEU A 12 PRO A 13 2 -1.15
CISPEP 3 LEU A 12 PRO A 13 3 14.56
CISPEP 4 LEU A 12 PRO A 13 4 -23.72
CISPEP 5 LEU A 12 PRO A 13 5 -2.57
CISPEP 6 LEU A 12 PRO A 13 6 -16.82
CISPEP 7 LEU A 12 PRO A 13 7 -9.27
CISPEP 8 LEU A 12 PRO A 13 8 17.58
CISPEP 9 LEU A 12 PRO A 13 9 5.63
CISPEP 10 LEU A 12 PRO A 13 10 -8.57
CISPEP 11 LEU A 12 PRO A 13 11 -1.54
CISPEP 12 LEU A 12 PRO A 13 12 0.99
CISPEP 13 LEU A 12 PRO A 13 13 -23.29
CISPEP 14 LEU A 12 PRO A 13 14 -19.19
CISPEP 15 LEU A 12 PRO A 13 15 -5.08
CISPEP 16 LEU A 12 PRO A 13 16 -1.20
CISPEP 17 LEU A 12 PRO A 13 17 -10.90
CISPEP 18 LEU A 12 PRO A 13 18 -10.48
SITE 1 AC1 1 LEU A 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 - 23 20 Bytes