Header list of 2b5q.pdb file
Complete list - 9 20 Bytes
HEADER TOXIN 29-SEP-05 2B5Q
TITLE SOLUTION STRUCTURE OF GLOBULAR CONFORMATION OF CMRVIA LAMBDA CONOTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMBDA-CONOTOXIN CMRVIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED USING FMOC-CHEMISTRY SOLID
SOURCE 4 PHASE PEPTIDE SYNTHESIS. THE SEQUENCE OF THE PEPTIDE IS NATURALLY
SOURCE 5 FOUND IN CONUS MARMOREUS (MARBLE CONE).
KEYWDS CONOTOXIN, DISULFIDE LINKAGE, RIBBON CONFORMATION, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 15
MDLTYP MINIMIZED AVERAGE
AUTHOR T.S.KANG,S.D.S.JOIS,R.M.KINI
REVDAT 3 09-MAR-22 2B5Q 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2B5Q 1 VERSN
REVDAT 1 29-AUG-06 2B5Q 0
JRNL AUTH T.S.KANG,S.D.S.JOIS,R.M.KINI
JRNL TITL SOLUTION STRUCTURES OF TWO STRUCTURAL ISOFORMS OF CMRVIA
JRNL TITL 2 CHI/LAMBDA-CONOTOXIN
JRNL REF BIOMACROMOLECULES V. 7 2337 2006
JRNL REFN ISSN 1525-7797
JRNL PMID 16903680
JRNL DOI 10.1021/BM060269W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, INSIGHT II
REMARK 3 AUTHORS : ACCELRYS (INSIGHT II)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034707.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 3MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM PEPTIDE SAMPLE; 10% D20, 90%
REMARK 210 H20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; DQF-COSY; 2D ROESY
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 : MESTRE-C 4.5.9, INSIGHT II
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 211
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 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 CYS A 11 C CYS A 11 OXT 0.136
REMARK 500 2 CYS A 11 C CYS A 11 OXT 0.142
REMARK 500 3 CYS A 11 C CYS A 11 OXT 0.138
REMARK 500 4 CYS A 11 C CYS A 11 OXT 0.137
REMARK 500 5 CYS A 11 C CYS A 11 OXT 0.136
REMARK 500 6 CYS A 11 C CYS A 11 OXT 0.136
REMARK 500 7 CYS A 11 C CYS A 11 OXT 0.133
REMARK 500 8 CYS A 11 C CYS A 11 OXT 0.133
REMARK 500 9 CYS A 11 C CYS A 11 OXT 0.135
REMARK 500 10 CYS A 11 C CYS A 11 OXT 0.136
REMARK 500 11 CYS A 11 C CYS A 11 OXT 0.132
REMARK 500 12 CYS A 11 C CYS A 11 OXT 0.134
REMARK 500 13 CYS A 11 C CYS A 11 OXT 0.134
REMARK 500 14 CYS A 11 C CYS A 11 OXT 0.134
REMARK 500 15 CYS A 11 C CYS A 11 OXT 0.135
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 CYS A 2 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 1 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 3 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 4 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 5 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 6 CYS A 2 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 6 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 7 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 8 CYS A 2 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 8 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 9 CYS A 2 CB - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 9 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 10 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 11 CYS A 2 CB - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 11 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 12 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 13 CYS A 2 CB - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 13 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 14 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 15 HIS A 9 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 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 CYS A 2 -99.03 -106.87
REMARK 500 1 TYR A 5 -140.24 -107.79
REMARK 500 1 LYS A 6 35.51 -82.31
REMARK 500 2 CYS A 2 -72.17 -96.72
REMARK 500 2 TYR A 5 -144.82 -100.67
REMARK 500 2 LYS A 6 48.65 -85.07
REMARK 500 3 CYS A 2 -67.29 -91.29
REMARK 500 3 TYR A 5 -151.33 -92.68
REMARK 500 3 LYS A 6 49.45 -85.53
REMARK 500 4 CYS A 2 -61.88 -93.44
REMARK 500 4 TYR A 5 -127.09 -113.06
REMARK 500 5 CYS A 2 -80.98 -79.80
REMARK 500 5 TYR A 5 -109.96 -124.45
REMARK 500 6 CYS A 2 -94.85 -122.69
REMARK 500 6 TYR A 5 -120.55 -119.54
REMARK 500 7 CYS A 2 -109.80 -135.28
REMARK 500 7 TYR A 5 -99.67 -107.06
REMARK 500 8 CYS A 2 -118.15 -127.31
REMARK 500 8 TYR A 5 -102.43 -93.21
REMARK 500 9 CYS A 2 -106.08 -138.35
REMARK 500 9 TYR A 5 -90.39 -114.84
REMARK 500 10 CYS A 2 -114.64 -133.24
REMARK 500 10 TYR A 5 -84.97 -126.49
REMARK 500 11 CYS A 2 -104.30 -107.52
REMARK 500 11 TYR A 5 -112.26 -96.11
REMARK 500 11 CYS A 8 43.92 -79.30
REMARK 500 12 CYS A 2 -85.98 -143.06
REMARK 500 12 TYR A 5 -108.12 -119.09
REMARK 500 13 CYS A 2 -128.07 -125.56
REMARK 500 13 TYR A 5 -90.62 -123.25
REMARK 500 14 CYS A 2 -81.50 -122.74
REMARK 500 14 TYR A 5 -113.10 -104.11
REMARK 500 15 CYS A 2 -63.18 -101.07
REMARK 500 15 TYR A 5 -142.12 -109.62
REMARK 500 15 LYS A 6 45.61 -82.47
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 5 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IE0 RELATED DB: PDB
REMARK 900 AMIDATED ANALOGUE OF MRIB CONOTOXIN, ANOTHER MEMBER OF LAMBDA
REMARK 900 CONOTOXIN FAMILY
REMARK 900 RELATED ID: 2B5P RELATED DB: PDB
REMARK 900 NATIVE CONFORMATION OF CMRVIA CONOTOXIN
DBREF 2B5Q A 1 11 UNP P58807 CXL1_CONMR 1 11
SEQADV 2B5Q HYP A 10 UNP P58807 PRO 10 MODIFIED RESIDUE
SEQRES 1 A 11 VAL CYS CYS GLY TYR LYS LEU CYS HIS HYP CYS
MODRES 2B5Q HYP A 10 PRO 4-HYDROXYPROLINE
HET HYP A 10 15
HETNAM HYP 4-HYDROXYPROLINE
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP C5 H9 N O3
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.01
SSBOND 2 CYS A 3 CYS A 11 1555 1555 2.00
LINK C HIS A 9 N HYP A 10 1555 1555 1.37
LINK C HYP A 10 N CYS A 11 1555 1555 1.34
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