Header list of 1wwn.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 10-JAN-05 1WWN
TITLE NMR SOLUTION STRUCTURE OF BMK-BETAIT, AN EXCITATORY SCORPION TOXIN
TITLE 2 FROM BUTHUS MARTENSI KARSCH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXCITATORY INSECT SELECTIVE TOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BMK IT1, BMKIT1, BMK IT, BMKIT, BM32-VI, NEUROTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MESOBUTHUS MARTENSII;
SOURCE 3 ORGANISM_COMMON: CHINESE SCORPION;
SOURCE 4 ORGANISM_TAXID: 34649
KEYWDS AN EXCITATORY SCORPION TOXIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.WU,X.TONG,X.CHEN,Q.ZHANG,X.ZHENG,N.ZHANG,G.WU
REVDAT 4 02-MAR-22 1WWN 1 REMARK
REVDAT 3 24-FEB-09 1WWN 1 VERSN
REVDAT 2 10-OCT-06 1WWN 1 JRNL
REVDAT 1 17-JAN-06 1WWN 0
JRNL AUTH X.TONG,J.YAO,F.HE,X.CHEN,X.ZHENG,C.XIE,G.WU,N.ZHANG,J.DING,
JRNL AUTH 2 H.WU
JRNL TITL NMR SOLUTION STRUCTURE OF BMK-BETAIT, AN EXCITATORY SCORPION
JRNL TITL 2 BETA-TOXIN WITHOUT A 'HOT SPOT' AT THE RELEVANT POSITION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 349 890 2006
JRNL REFN ISSN 0006-291X
JRNL PMID 16970911
JRNL DOI 10.1016/J.BBRC.2006.08.131
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, AMBER 5.0
REMARK 3 AUTHORS : MIKE CARLISLE, DAN STEELE, AND MIKE MILLER (VNMR),
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WWN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024088.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.80
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0MM; 2.0MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 2D TOCSY, DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY 1994, DYANA 1.5
REMARK 210 METHOD USED : THE STRUCTURE ARE BASED ON A
REMARK 210 TOTAL OF 884 CONSTRAINTS, 814
REMARK 210 ARE NOE-DERIVED DISTANCE
REMARK 210 CONSTRAINTS,26 DIHEDRAL ANGLE
REMARK 210 CONSTRAINTS,44 DISTANCE
REMARK 210 CONSTRAINTS FROM SIXTEEN
REMARK 210 HYDROGEN BONDS AND FOUR
REMARK 210 DISULFIDE BONDS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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: 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 TYR A 43 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 TYR A 5 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 CYS A 44 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 3 CYS A 44 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 3 LEU A 47 CB - CG - CD2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 6 CYS A 44 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 9 CYS A 44 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 12 CYS A 16 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 15 LYS A 61 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 16 TYR A 5 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 16 CYS A 44 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 17 TYR A 5 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 20 LEU A 47 CB - CG - CD1 ANGL. DEV. = 12.2 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 LYS A 2 -158.89 -130.28
REMARK 500 1 SER A 9 -12.35 -141.99
REMARK 500 1 SER A 10 52.22 -163.87
REMARK 500 1 GLU A 15 -120.65 46.71
REMARK 500 1 CYS A 16 66.54 111.96
REMARK 500 1 TYR A 31 31.43 74.34
REMARK 500 1 ALA A 32 160.53 -48.41
REMARK 500 1 CYS A 37 92.62 -69.41
REMARK 500 1 LEU A 39 -54.74 -16.21
REMARK 500 1 LEU A 40 24.60 -143.14
REMARK 500 1 CYS A 42 109.79 -59.78
REMARK 500 1 LEU A 47 108.07 -28.86
REMARK 500 1 ALA A 52 56.05 168.45
REMARK 500 1 ASP A 65 -69.28 -96.76
REMARK 500 1 GLN A 67 -61.10 -24.63
REMARK 500 2 LYS A 2 -149.53 -102.19
REMARK 500 2 ASN A 3 152.71 -49.12
REMARK 500 2 ASP A 8 -117.58 -77.76
REMARK 500 2 SER A 10 68.10 85.47
REMARK 500 2 CYS A 16 -179.51 56.91
REMARK 500 2 LEU A 17 -46.53 -130.21
REMARK 500 2 TYR A 31 51.10 83.62
REMARK 500 2 ALA A 32 -167.28 -78.37
REMARK 500 2 SER A 34 -162.73 -114.78
REMARK 500 2 LEU A 39 -57.37 -7.99
REMARK 500 2 LEU A 40 39.83 -152.52
REMARK 500 2 ASP A 48 -71.22 -96.16
REMARK 500 2 ALA A 52 70.83 42.07
REMARK 500 2 GLN A 67 -70.35 -43.42
REMARK 500 2 ILE A 68 -62.20 -93.38
REMARK 500 3 LYS A 2 -155.68 -88.06
REMARK 500 3 SER A 9 -47.01 -162.65
REMARK 500 3 GLU A 15 -84.84 -36.46
REMARK 500 3 CYS A 16 162.50 73.17
REMARK 500 3 ASN A 19 -64.71 -6.77
REMARK 500 3 LEU A 39 -62.37 -5.58
REMARK 500 3 LEU A 40 44.89 -154.29
REMARK 500 3 LEU A 47 75.04 -62.39
REMARK 500 3 ASP A 50 88.66 69.65
REMARK 500 3 ALA A 52 59.74 175.14
REMARK 500 3 ASP A 65 -55.60 -128.88
REMARK 500 3 GLN A 67 -66.76 -19.72
REMARK 500 4 LYS A 2 -84.97 -163.58
REMARK 500 4 ASP A 8 -109.50 -22.18
REMARK 500 4 SER A 10 -66.36 -154.22
REMARK 500 4 LYS A 12 127.88 -24.27
REMARK 500 4 CYS A 16 -178.16 161.03
REMARK 500 4 LEU A 39 -57.93 -13.59
REMARK 500 4 LEU A 40 48.50 -150.76
REMARK 500 4 SER A 41 -169.92 -168.74
REMARK 500
REMARK 500 THIS ENTRY HAS 247 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 GLY A 11 LYS A 12 4 143.45
REMARK 500 ALA A 6 VAL A 7 6 149.50
REMARK 500 TYR A 31 ALA A 32 6 144.44
REMARK 500 GLY A 4 TYR A 5 7 146.63
REMARK 500 TYR A 31 ALA A 32 7 147.76
REMARK 500 ASP A 8 SER A 9 9 149.70
REMARK 500 TYR A 31 ALA A 32 10 139.98
REMARK 500 VAL A 13 SER A 14 12 149.99
REMARK 500 TYR A 31 ALA A 32 13 144.94
REMARK 500 ASP A 48 ASP A 49 13 147.43
REMARK 500 GLY A 11 LYS A 12 14 147.74
REMARK 500 ASP A 48 ASP A 49 14 141.81
REMARK 500 GLY A 11 LYS A 12 15 138.09
REMARK 500 LYS A 1 LYS A 2 17 -146.55
REMARK 500 LYS A 2 ASN A 3 17 147.58
REMARK 500 ASN A 3 GLY A 4 18 -148.91
REMARK 500 VAL A 7 ASP A 8 18 141.65
REMARK 500 ASP A 49 ASP A 50 19 145.81
REMARK 500 LYS A 55 ILE A 56 19 -147.73
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 21 0.14 SIDE CHAIN
REMARK 500 1 TYR A 30 0.11 SIDE CHAIN
REMARK 500 1 TYR A 31 0.19 SIDE CHAIN
REMARK 500 1 TYR A 36 0.07 SIDE CHAIN
REMARK 500 1 TYR A 43 0.10 SIDE CHAIN
REMARK 500 1 PHE A 45 0.08 SIDE CHAIN
REMARK 500 2 TYR A 21 0.07 SIDE CHAIN
REMARK 500 2 TYR A 30 0.17 SIDE CHAIN
REMARK 500 2 TYR A 31 0.19 SIDE CHAIN
REMARK 500 2 TYR A 36 0.13 SIDE CHAIN
REMARK 500 2 TYR A 43 0.13 SIDE CHAIN
REMARK 500 3 TYR A 5 0.12 SIDE CHAIN
REMARK 500 3 TYR A 36 0.12 SIDE CHAIN
REMARK 500 4 TYR A 5 0.12 SIDE CHAIN
REMARK 500 4 TYR A 31 0.20 SIDE CHAIN
REMARK 500 4 TYR A 36 0.16 SIDE CHAIN
REMARK 500 4 TYR A 43 0.10 SIDE CHAIN
REMARK 500 5 TYR A 5 0.19 SIDE CHAIN
REMARK 500 5 TYR A 31 0.21 SIDE CHAIN
REMARK 500 5 TYR A 36 0.08 SIDE CHAIN
REMARK 500 5 TYR A 63 0.23 SIDE CHAIN
REMARK 500 6 TYR A 5 0.07 SIDE CHAIN
REMARK 500 6 TYR A 30 0.13 SIDE CHAIN
REMARK 500 6 TYR A 31 0.20 SIDE CHAIN
REMARK 500 6 TYR A 36 0.15 SIDE CHAIN
REMARK 500 6 TYR A 43 0.11 SIDE CHAIN
REMARK 500 7 TYR A 5 0.07 SIDE CHAIN
REMARK 500 7 TYR A 21 0.07 SIDE CHAIN
REMARK 500 7 TYR A 36 0.09 SIDE CHAIN
REMARK 500 8 TYR A 5 0.11 SIDE CHAIN
REMARK 500 8 TYR A 30 0.10 SIDE CHAIN
REMARK 500 8 TYR A 31 0.17 SIDE CHAIN
REMARK 500 8 TYR A 36 0.07 SIDE CHAIN
REMARK 500 8 TYR A 43 0.08 SIDE CHAIN
REMARK 500 8 PHE A 45 0.09 SIDE CHAIN
REMARK 500 8 TYR A 63 0.06 SIDE CHAIN
REMARK 500 9 TYR A 5 0.26 SIDE CHAIN
REMARK 500 9 TYR A 30 0.14 SIDE CHAIN
REMARK 500 9 TYR A 31 0.18 SIDE CHAIN
REMARK 500 9 TYR A 36 0.12 SIDE CHAIN
REMARK 500 9 TYR A 43 0.11 SIDE CHAIN
REMARK 500 9 TYR A 63 0.16 SIDE CHAIN
REMARK 500 10 TYR A 21 0.08 SIDE CHAIN
REMARK 500 10 TYR A 31 0.18 SIDE CHAIN
REMARK 500 10 TYR A 36 0.08 SIDE CHAIN
REMARK 500 10 TYR A 43 0.15 SIDE CHAIN
REMARK 500 11 TYR A 5 0.12 SIDE CHAIN
REMARK 500 11 TYR A 30 0.12 SIDE CHAIN
REMARK 500 11 TYR A 31 0.21 SIDE CHAIN
REMARK 500 11 TYR A 36 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 88 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BCG RELATED DB: PDB
REMARK 900 AN EXCITATORY SCORPION TOXIN WITH A DISTINCTIVE FEATURE: AN
REMARK 900 ADDITIONAL ALPHA HELIX AT THE C TERMINUS AND ITS IMPLICATIONS FOR
REMARK 900 INTERACTION WITH INSECT SODIUM CHANNELS
REMARK 900 RELATED ID: 1NPI RELATED DB: PDB
REMARK 900 TITYUS SERRULATUS NEUROTOXIN (TS1) AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1PTX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS
REMARK 900 AUSTRALIS HECTOR REFINED AT 1.3 A RESOLUTION
DBREF 1WWN A 1 69 UNP O61668 SIX1_MESMA 19 87
SEQRES 1 A 69 LYS LYS ASN GLY TYR ALA VAL ASP SER SER GLY LYS VAL
SEQRES 2 A 69 SER GLU CYS LEU LEU ASN ASN TYR CYS ASN ASN ILE CYS
SEQRES 3 A 69 THR LYS VAL TYR TYR ALA THR SER GLY TYR CYS CYS LEU
SEQRES 4 A 69 LEU SER CYS TYR CYS PHE GLY LEU ASP ASP ASP LYS ALA
SEQRES 5 A 69 VAL LEU LYS ILE LYS ASP ALA THR LYS SER TYR CYS ASP
SEQRES 6 A 69 VAL GLN ILE ILE
HELIX 1 1 LEU A 18 VAL A 29 1 12
HELIX 2 2 LYS A 57 CYS A 64 1 8
SHEET 1 A 3 ASN A 3 TYR A 5 0
SHEET 2 A 3 SER A 41 PHE A 45 -1 O CYS A 44 N GLY A 4
SHEET 3 A 3 SER A 34 CYS A 38 -1 N TYR A 36 O TYR A 43
SSBOND 1 CYS A 16 CYS A 37 1555 1555 2.09
SSBOND 2 CYS A 22 CYS A 42 1555 1555 2.07
SSBOND 3 CYS A 26 CYS A 44 1555 1555 2.05
SSBOND 4 CYS A 38 CYS A 64 1555 1555 2.08
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 - r 2 2 Bytes