Header list of 1m2c.pdb file
Complete list - 23 20 Bytes
HEADER NEUROTOXIN 15-SEP-97 1M2C
TITLE THREE-DIMENSIONAL STRUCTURE OF ALPHA-CONOTOXIN MII, NMR, 14 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN MII;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS MAGUS;
SOURCE 3 ORGANISM_COMMON: MAGUS CONE;
SOURCE 4 ORGANISM_TAXID: 6492
KEYWDS NEUROTOXIN, NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR INHIBITOR,
KEYWDS 2 SUBTYPE SPECIFIC LIGAND, PRESYNAPTIC NICOTINIC ACETYLCHOLINE
KEYWDS 3 RECEPTOR BLOCKER, CHOLINERGIC MODULATION, DOPAMINE RELEASE
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR K.J.SHON,S.C.KOERBER,J.E.RIVIER,B.M.OLIVERA,J.M.MCINTOSH
REVDAT 5 23-FEB-22 1M2C 1 REMARK LINK
REVDAT 4 24-FEB-09 1M2C 1 VERSN
REVDAT 3 01-APR-03 1M2C 1 JRNL
REVDAT 2 13-JAN-99 1M2C 3 COMPND REMARK TITLE HETATM
REVDAT 2 2 3 HEADER TER SOURCE SEQRES
REVDAT 2 3 3 FORMUL JRNL KEYWDS CONECT
REVDAT 1 09-DEC-98 1M2C 0
JRNL AUTH G.E.CARTIER,D.YOSHIKAMI,W.R.GRAY,S.LUO,B.M.OLIVERA,
JRNL AUTH 2 J.M.MCINTOSH
JRNL TITL A NEW ALPHA-CONOTOXIN WHICH TARGETS ALPHA3BETA2 NICOTINIC
JRNL TITL 2 ACETYLCHOLINE RECEPTORS.
JRNL REF J.BIOL.CHEM. V. 271 7522 1996
JRNL REFN ISSN 0021-9258
JRNL PMID 8631783
JRNL DOI 10.1074/JBC.271.13.7522
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INSIGHT II II
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M2C 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_1000174892.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : 5MM SODIUM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O / 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; PE-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VARIAN VNMR VNMR, MSI FELIX
REMARK 210 FELIX, INSIGHT II II, DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY, ITERATIVE
REMARK 210 RELAXATION MATRIX APPROACH,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2-D HOMONUCLEAR 1H NMR
REMARK 210 EXPERIMENTS. THESE ARE A SET OF NOESY, TOCSY, DQF-COSY, AND PE-
REMARK 210 COSY.
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 11 CD GLU A 11 OE2 0.111
REMARK 500 1 HIS A 12 CG HIS A 12 CD2 0.056
REMARK 500 2 GLU A 11 CD GLU A 11 OE2 0.107
REMARK 500 2 HIS A 12 CG HIS A 12 CD2 0.056
REMARK 500 3 GLU A 11 CD GLU A 11 OE2 0.109
REMARK 500 3 HIS A 12 CG HIS A 12 CD2 0.056
REMARK 500 4 GLU A 11 CD GLU A 11 OE2 0.106
REMARK 500 4 HIS A 12 CG HIS A 12 CD2 0.058
REMARK 500 5 GLU A 11 CD GLU A 11 OE2 0.106
REMARK 500 5 HIS A 12 CG HIS A 12 CD2 0.057
REMARK 500 6 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 6 HIS A 12 CG HIS A 12 CD2 0.054
REMARK 500 7 GLU A 11 CD GLU A 11 OE2 0.106
REMARK 500 7 HIS A 12 CG HIS A 12 CD2 0.059
REMARK 500 8 GLU A 11 CD GLU A 11 OE2 0.107
REMARK 500 9 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 9 HIS A 12 CG HIS A 12 CD2 0.058
REMARK 500 10 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 10 HIS A 12 CG HIS A 12 CD2 0.056
REMARK 500 11 GLU A 11 CD GLU A 11 OE2 0.108
REMARK 500 12 GLU A 11 CD GLU A 11 OE2 0.111
REMARK 500 12 HIS A 12 CG HIS A 12 CD2 0.060
REMARK 500 13 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 13 HIS A 12 CG HIS A 12 CD2 0.055
REMARK 500 14 GLU A 11 CD GLU A 11 OE2 0.106
REMARK 500 14 HIS A 12 CG HIS A 12 CD2 0.060
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 HIS A 9 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 2 HIS A 9 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 3 HIS A 9 CA - CB - CG ANGL. DEV. = 20.3 DEGREES
REMARK 500 3 LEU A 15 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 4 HIS A 9 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 5 HIS A 9 CA - CB - CG ANGL. DEV. = 22.6 DEGREES
REMARK 500 6 HIS A 9 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 6 GLU A 11 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 6 HIS A 12 CA - CB - CG ANGL. DEV. = 10.9 DEGREES
REMARK 500 6 LEU A 15 N - CA - CB ANGL. DEV. = -16.1 DEGREES
REMARK 500 7 HIS A 9 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 8 CYS A 2 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 8 CYS A 2 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 8 CYS A 3 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 8 HIS A 9 CA - CB - CG ANGL. DEV. = 20.7 DEGREES
REMARK 500 9 CYS A 3 N - CA - CB ANGL. DEV. = -14.3 DEGREES
REMARK 500 9 HIS A 9 CA - CB - CG ANGL. DEV. = 12.3 DEGREES
REMARK 500 9 CYS A 16 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 10 CYS A 3 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 10 HIS A 9 CA - CB - CG ANGL. DEV. = 22.1 DEGREES
REMARK 500 11 HIS A 9 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 12 CYS A 3 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 12 HIS A 9 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 12 LEU A 15 N - CA - CB ANGL. DEV. = -19.3 DEGREES
REMARK 500 13 HIS A 9 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 14 HIS A 9 CA - CB - CG ANGL. DEV. = 22.2 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 GLU A 11 -38.96 -38.09
REMARK 500 4 GLU A 11 -34.93 -31.94
REMARK 500 5 GLU A 11 -37.41 -36.64
REMARK 500 6 VAL A 7 -62.22 -105.73
REMARK 500 6 GLU A 11 -38.81 -36.52
REMARK 500 9 GLU A 11 -35.55 -30.19
REMARK 500 10 GLU A 11 -39.40 -31.75
REMARK 500 11 GLU A 11 -49.36 -14.57
REMARK 500 12 GLU A 11 -39.10 -30.85
REMARK 500 12 SER A 13 14.74 -28.44
REMARK 500 13 CYS A 3 -39.47 -35.67
REMARK 500 13 GLU A 11 -38.28 -38.20
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 SER A 13 ASN A 14 1 148.28
REMARK 500 LEU A 10 GLU A 11 2 146.94
REMARK 500 SER A 13 ASN A 14 2 148.66
REMARK 500 LEU A 15 CYS A 16 2 148.37
REMARK 500 CYS A 8 HIS A 9 3 146.37
REMARK 500 LEU A 10 GLU A 11 3 142.93
REMARK 500 LEU A 10 GLU A 11 4 139.29
REMARK 500 SER A 4 ASN A 5 5 147.80
REMARK 500 LEU A 10 GLU A 11 5 145.17
REMARK 500 LEU A 10 GLU A 11 6 145.37
REMARK 500 SER A 13 ASN A 14 6 144.79
REMARK 500 LEU A 15 CYS A 16 7 136.67
REMARK 500 VAL A 7 CYS A 8 8 143.76
REMARK 500 CYS A 2 CYS A 3 9 148.34
REMARK 500 LEU A 10 GLU A 11 9 142.65
REMARK 500 SER A 4 ASN A 5 10 147.73
REMARK 500 LEU A 10 GLU A 11 10 135.48
REMARK 500 LEU A 10 GLU A 11 11 132.41
REMARK 500 LEU A 15 CYS A 16 11 146.16
REMARK 500 LEU A 10 GLU A 11 12 145.26
REMARK 500 HIS A 12 SER A 13 12 -122.09
REMARK 500 SER A 13 ASN A 14 12 146.21
REMARK 500 SER A 13 ASN A 14 13 146.30
REMARK 500 LEU A 15 CYS A 16 13 146.47
REMARK 500 LEU A 10 GLU A 11 14 143.40
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 HIS A 9 0.11 SIDE CHAIN
REMARK 500 3 HIS A 9 0.20 SIDE CHAIN
REMARK 500 4 HIS A 9 0.10 SIDE CHAIN
REMARK 500 4 HIS A 12 0.12 SIDE CHAIN
REMARK 500 5 HIS A 9 0.15 SIDE CHAIN
REMARK 500 6 HIS A 9 0.14 SIDE CHAIN
REMARK 500 7 HIS A 9 0.16 SIDE CHAIN
REMARK 500 8 HIS A 9 0.15 SIDE CHAIN
REMARK 500 8 HIS A 12 0.19 SIDE CHAIN
REMARK 500 9 HIS A 9 0.11 SIDE CHAIN
REMARK 500 9 HIS A 12 0.12 SIDE CHAIN
REMARK 500 10 HIS A 9 0.15 SIDE CHAIN
REMARK 500 11 HIS A 12 0.18 SIDE CHAIN
REMARK 500 12 HIS A 9 0.11 SIDE CHAIN
REMARK 500 12 HIS A 12 0.10 SIDE CHAIN
REMARK 500 13 HIS A 9 0.13 SIDE CHAIN
REMARK 500 14 HIS A 9 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M2C A 1 16 UNP P56636 CXA2_CONMA 1 16
SEQRES 1 A 17 GLY CYS CYS SER ASN PRO VAL CYS HIS LEU GLU HIS SER
SEQRES 2 A 17 ASN LEU CYS NH2
HET NH2 A 17H 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 CYS A 8 GLU A 11 1 4
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.02
SSBOND 2 CYS A 3 CYS A 16 1555 1555 2.01
LINK C CYS A 16 N NH2 A 17H 1555 1555 1.32
CISPEP 1 GLY A 1 CYS A 2 1 -6.64
CISPEP 2 GLY A 1 CYS A 2 4 -3.04
CISPEP 3 GLY A 1 CYS A 2 5 -0.91
CISPEP 4 GLY A 1 CYS A 2 10 0.14
CISPEP 5 GLY A 1 CYS A 2 11 -6.04
CISPEP 6 GLY A 1 CYS A 2 13 -6.10
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