Header list of 1cnn.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 20-MAY-99 1CNN
TITLE OMEGA-CONOTOXIN MVIIC FROM CONUS MAGUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MVIIC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN THE VENOM DUCT OF CONUS MAGUS
SOURCE 5 (MAGUS CONE).
KEYWDS VOLTAGE-SENSITIVE CALCIUM CHANNEL ANTAGONIST, PEPTIDE HYBRIDS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR K.J.NIELSEN,D.ADAMS,L.THOMAS,T.BOND,P.F.ALEWOOD,D.J.CRAIK,R.J.LEWIS
REVDAT 3 16-FEB-22 1CNN 1 REMARK LINK
REVDAT 2 24-FEB-09 1CNN 1 VERSN
REVDAT 1 31-MAY-00 1CNN 0
JRNL AUTH K.J.NIELSEN,D.ADAMS,L.THOMAS,T.BOND,P.F.ALEWOOD,D.J.CRAIK,
JRNL AUTH 2 R.J.LEWIS
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF OMEGA-CONOTOXINS MVIIA,
JRNL TITL 2 MVIIC AND 14 LOOP SPLICE HYBRIDS AT N AND P/Q-TYPE CALCIUM
JRNL TITL 3 CHANNELS.
JRNL REF J.MOL.BIOL. V. 289 1405 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10373375
JRNL DOI 10.1006/JMBI.1999.2817
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT BASED ON CHARMM PARAMTERS,
REMARK 3 DETAILS IN JRNL CITATION ABOVE
REMARK 4
REMARK 4 1CNN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001093.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293.00
REMARK 210 PH : 3.50
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 95% WATER/ 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : ARX500; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS/ SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY HOMONUCLEAR NMR
REMARK 210 SPECTROSCOPY ON SYNTHETIC MVIIC
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 6 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.2 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 PRO A 7 84.73 -65.33
REMARK 500 1 CYS A 8 -169.09 -107.66
REMARK 500 1 MET A 12 12.22 -143.04
REMARK 500 1 TYR A 13 73.79 50.52
REMARK 500 2 PRO A 7 95.47 -59.82
REMARK 500 2 TYR A 13 73.60 53.34
REMARK 500 2 SER A 19 67.17 -113.94
REMARK 500 3 PRO A 7 92.09 -66.63
REMARK 500 3 THR A 11 -38.96 -32.89
REMARK 500 3 MET A 12 11.64 -147.65
REMARK 500 3 TYR A 13 77.20 53.80
REMARK 500 4 PRO A 7 99.21 -59.33
REMARK 500 4 TYR A 13 76.61 52.26
REMARK 500 5 PRO A 7 88.10 -67.65
REMARK 500 5 THR A 11 -34.46 -30.41
REMARK 500 5 MET A 12 8.05 -150.35
REMARK 500 5 TYR A 13 75.28 53.80
REMARK 500 5 SER A 19 53.00 -109.14
REMARK 500 6 PRO A 7 84.91 -67.82
REMARK 500 6 MET A 12 16.85 -142.42
REMARK 500 6 TYR A 13 74.28 51.45
REMARK 500 7 PRO A 7 90.13 -61.45
REMARK 500 7 THR A 11 -39.25 -35.12
REMARK 500 8 PRO A 7 87.82 -64.05
REMARK 500 9 PRO A 7 88.12 -65.27
REMARK 500 9 THR A 11 -48.58 -24.44
REMARK 500 9 TYR A 13 74.89 54.88
REMARK 500 9 SER A 19 58.91 -141.87
REMARK 500 10 TYR A 13 79.02 55.13
REMARK 500 10 ASP A 14 20.69 -78.07
REMARK 500 11 PRO A 7 89.08 -64.85
REMARK 500 11 SER A 19 59.60 -118.10
REMARK 500 12 PRO A 7 88.88 -66.47
REMARK 500 12 TYR A 13 73.50 53.99
REMARK 500 13 PRO A 7 79.89 -63.96
REMARK 500 13 TYR A 13 75.92 51.97
REMARK 500 13 SER A 19 55.12 -107.02
REMARK 500 14 THR A 11 -36.68 -35.66
REMARK 500 14 MET A 12 9.75 -150.57
REMARK 500 14 TYR A 13 76.98 52.43
REMARK 500 15 PRO A 7 92.14 -63.40
REMARK 500 15 TYR A 13 74.31 52.94
REMARK 500 15 SER A 19 66.70 -108.72
REMARK 500 16 PRO A 7 96.57 -63.40
REMARK 500 16 MET A 12 10.73 -145.73
REMARK 500 16 TYR A 13 77.31 52.26
REMARK 500 17 PRO A 7 88.48 -61.42
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 27
DBREF 1CNN A 1 26 UNP P37300 CXO7C_CONMA 3 28
SEQRES 1 A 27 CYS LYS GLY LYS GLY ALA PRO CYS ARG LYS THR MET TYR
SEQRES 2 A 27 ASP CYS CYS SER GLY SER CYS GLY ARG ARG GLY LYS CYS
SEQRES 3 A 27 NH2
HET NH2 A 27 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.02
LINK C CYS A 26 N NH2 A 27 1555 1555 1.31
SITE 1 AC1 2 SER A 19 CYS A 26
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 - 16 20 Bytes