Header list of 1z99.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 01-APR-05 1Z99
TITLE SOLUTION STRUCTURE OF CROTAMINE, A MYOTOXIN FROM CROTALUS DURISSUS
TITLE 2 TERRIFICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CROTAMINE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CRT, MYOTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CROTALUS DURISSUS TERRIFICUS;
SOURCE 3 ORGANISM_COMMON: TROPICAL RATTLESNAKE;
SOURCE 4 ORGANISM_TAXID: 8732;
SOURCE 5 STRAIN: TERRIFICUS
KEYWDS BETA-DEFENSIN-FOLD, MYOTOXIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.FADEL,P.BETTENDORFF,T.HERRMANN,W.F.DE AZEVEDO,E.B.OLIVEIRA,
AUTHOR 2 T.YAMANE,K.WUTHRICH
REVDAT 3 02-MAR-22 1Z99 1 REMARK
REVDAT 2 24-FEB-09 1Z99 1 VERSN
REVDAT 1 14-MAR-06 1Z99 0
JRNL AUTH V.FADEL,P.BETTENDORFF,T.HERRMANN,W.F.DE AZEVEDO,
JRNL AUTH 2 E.B.OLIVEIRA,T.YAMANE,K.WUTHRICH
JRNL TITL AUTOMATED NMR STRUCTURE DETERMINATION AND DISULFIDE BOND
JRNL TITL 2 IDENTIFICATION OF THE MYOTOXIN CROTAMINE FROM CROTALUS
JRNL TITL 3 DURISSUS TERRIFICUS.
JRNL REF TOXICON V. 46 759 2005
JRNL REFN ISSN 0041-0101
JRNL PMID 16185738
JRNL DOI 10.1016/J.TOXICON.2005.07.018
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 6.02, RADAR 0.9B
REMARK 3 AUTHORS : GÜNTERT P., HERRMANN, T. (DYANA), HERRMANN,
REMARK 3 T. (RADAR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED ENERGY-MINIMIZED IN A WATER
REMARK 3 SHELL USING AMBER FORCE FIELD
REMARK 4
REMARK 4 1Z99 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032458.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293.4; 313.4
REMARK 210 PH : 5.8; 5.8
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM CROTAMINE, 1UM NAN3, H2O
REMARK 210 95%, D2O 5%; 0.9 MM CROTAMINE,
REMARK 210 1UM NAN3, D2O 100 %
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : RADAR 0.9B, CARA 1.0, XWINNMR
REMARK 210 3.5
REMARK 210 METHOD USED : OPALP
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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 PHE A 25 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 CYS A 37 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 12 CYS A 4 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 15 CYS A 4 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 20 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.0 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 11 113.25 95.89
REMARK 500 1 ILE A 17 98.14 46.08
REMARK 500 1 PRO A 21 -163.30 -74.97
REMARK 500 1 SER A 22 -56.60 79.58
REMARK 500 1 PHE A 25 -62.77 24.25
REMARK 500 1 MET A 28 -70.97 -112.68
REMARK 500 1 ASP A 29 20.86 -156.60
REMARK 500 1 ARG A 33 -37.16 148.79
REMARK 500 1 LYS A 39 82.41 -51.50
REMARK 500 1 SER A 41 -40.80 -150.65
REMARK 500 2 CYS A 11 103.36 154.61
REMARK 500 2 ILE A 17 95.07 41.26
REMARK 500 2 SER A 22 -50.40 -149.62
REMARK 500 2 ASP A 24 65.76 -101.24
REMARK 500 2 MET A 28 -118.41 -123.49
REMARK 500 2 ASP A 29 1.92 -68.66
REMARK 500 2 LYS A 38 -86.97 -51.72
REMARK 500 2 SER A 41 -64.49 -147.02
REMARK 500 3 HIS A 10 -88.24 -91.31
REMARK 500 3 CYS A 11 116.30 166.08
REMARK 500 3 ILE A 17 95.70 43.67
REMARK 500 3 SER A 22 -65.89 -141.64
REMARK 500 3 MET A 28 -107.78 -116.79
REMARK 500 3 LYS A 35 -165.41 -128.00
REMARK 500 3 LYS A 39 -69.18 52.48
REMARK 500 3 SER A 41 -65.65 -132.73
REMARK 500 4 LYS A 2 -56.31 -161.95
REMARK 500 4 HIS A 10 -69.21 -135.81
REMARK 500 4 CYS A 11 109.27 153.48
REMARK 500 4 ILE A 17 98.52 44.81
REMARK 500 4 SER A 22 -68.56 96.89
REMARK 500 4 MET A 28 -124.38 -134.00
REMARK 500 4 ASP A 29 30.32 -72.91
REMARK 500 4 LYS A 38 -91.88 -42.82
REMARK 500 4 SER A 41 107.04 153.66
REMARK 500 5 LYS A 2 -75.08 -154.63
REMARK 500 5 HIS A 10 -82.92 -79.90
REMARK 500 5 CYS A 11 110.95 156.32
REMARK 500 5 ILE A 17 86.62 41.74
REMARK 500 5 SER A 22 -53.79 -129.75
REMARK 500 5 LYS A 27 150.57 63.35
REMARK 500 5 MET A 28 -106.73 -133.99
REMARK 500 5 CYS A 37 140.25 -177.23
REMARK 500 6 HIS A 10 -68.65 -96.91
REMARK 500 6 CYS A 11 118.21 154.60
REMARK 500 6 ILE A 17 106.21 52.61
REMARK 500 6 PRO A 21 -165.40 -73.17
REMARK 500 6 SER A 22 -52.86 92.58
REMARK 500 6 ASP A 24 72.08 -102.08
REMARK 500 6 LYS A 27 152.87 63.36
REMARK 500
REMARK 500 THIS ENTRY HAS 186 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 TYR A 1 LYS A 2 3 -148.62
REMARK 500 TYR A 1 LYS A 2 4 145.67
REMARK 500 SER A 41 GLY A 42 10 -140.68
REMARK 500 SER A 41 GLY A 42 11 -147.43
REMARK 500 SER A 41 GLY A 42 13 -143.60
REMARK 500 SER A 41 GLY A 42 14 -118.93
REMARK 500 SER A 41 GLY A 42 17 129.61
REMARK 500 CYS A 30 ARG A 31 18 145.44
REMARK 500 ILE A 17 CYS A 18 19 -136.05
REMARK 500 SER A 41 GLY A 42 19 -145.59
REMARK 500 PHE A 25 GLY A 26 20 144.31
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 4 TYR A 1 0.06 SIDE CHAIN
REMARK 500 7 TYR A 1 0.08 SIDE CHAIN
REMARK 500 9 PHE A 12 0.10 SIDE CHAIN
REMARK 500 10 ARG A 31 0.10 SIDE CHAIN
REMARK 500 11 TYR A 1 0.10 SIDE CHAIN
REMARK 500 11 PHE A 25 0.08 SIDE CHAIN
REMARK 500 15 TYR A 1 0.07 SIDE CHAIN
REMARK 500 19 TYR A 1 0.07 SIDE CHAIN
REMARK 500 19 ARG A 31 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z99 A 1 42 UNP P01475 MYXC_CRODU 1 42
SEQRES 1 A 42 TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO
SEQRES 2 A 42 LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY
SEQRES 3 A 42 LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS
SEQRES 4 A 42 GLY SER GLY
HELIX 1 1 TYR A 1 LYS A 7 1 7
HELIX 2 2 PRO A 13 ILE A 17 5 5
CISPEP 1 LEU A 19 PRO A 20 1 -5.68
CISPEP 2 LEU A 19 PRO A 20 2 -5.91
CISPEP 3 LEU A 19 PRO A 20 3 0.60
CISPEP 4 LEU A 19 PRO A 20 4 -12.75
CISPEP 5 LEU A 19 PRO A 20 5 -9.72
CISPEP 6 LEU A 19 PRO A 20 6 -9.69
CISPEP 7 LEU A 19 PRO A 20 7 -8.67
CISPEP 8 LEU A 19 PRO A 20 8 8.91
CISPEP 9 LEU A 19 PRO A 20 9 -4.05
CISPEP 10 LEU A 19 PRO A 20 10 -5.07
CISPEP 11 LEU A 19 PRO A 20 11 -8.97
CISPEP 12 LEU A 19 PRO A 20 12 7.91
CISPEP 13 LEU A 19 PRO A 20 13 -15.99
CISPEP 14 LEU A 19 PRO A 20 14 -14.20
CISPEP 15 LEU A 19 PRO A 20 15 -6.14
CISPEP 16 LEU A 19 PRO A 20 16 -18.26
CISPEP 17 LEU A 19 PRO A 20 17 -8.35
CISPEP 18 LEU A 19 PRO A 20 18 -3.74
CISPEP 19 LEU A 19 PRO A 20 19 -8.44
CISPEP 20 LEU A 19 PRO A 20 20 -7.72
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