Header list of 1v28.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 09-OCT-03 1V28
TITLE SOLUTION STRUCTURE OF PARALYTIC PEPTIDE OF THE WILD SILKMOTH,
TITLE 2 ANTHERAEA YAMAMAI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARALYTIC PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC CONSTRUCT
KEYWDS PARALYTIC PEPTIDE, ANTHERAEA YAMAMAI, SINGLE BETA SHEET, ENF FAMILY,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.KAWAGUCHI,A.YING,K.SUZUKI,Y.KUMAKI,M.DEMURA,K.NITTA
REVDAT 3 02-MAR-22 1V28 1 REMARK
REVDAT 2 24-FEB-09 1V28 1 VERSN
REVDAT 1 26-OCT-04 1V28 0
JRNL AUTH K.KAWAGUCHI,A.YING,K.SUZUKI,Y.KUMAKI,M.DEMURA,K.NITTA
JRNL TITL STRUCTURAL CHARACTERIZATION OF PARALYTIC PEPTIDE OF THE WILD
JRNL TITL 2 SILKMOTH ANTHERAEA YAMAMAI BY NMR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : MICHAEL NILGES, JOHN KUSZEWSKI, AXEL T. BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 189 RESTRAINTS, 165 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 12
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 12 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1V28 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000006114.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM PARALYTIC PEPTIDE; PH 4.4(PH
REMARK 210 WAS ADJUSTED BY HCL AND NAOH);
REMARK 210 90% H2O, 10% D2O; 3MM PARALYTIC
REMARK 210 PEPTIDE; PH 4.4(PH WAS ADJUSTED
REMARK 210 BY HCL AND NAOH); 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; ALPHA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O THR A 14 H GLY A 17 1.49
REMARK 500 H MET A 12 O LYS A 20 1.53
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 ASN A 2 106.69 -179.45
REMARK 500 1 PHE A 3 117.11 -162.90
REMARK 500 1 THR A 9 -98.08 -41.24
REMARK 500 2 ASN A 2 163.47 55.28
REMARK 500 2 PHE A 3 64.46 64.99
REMARK 500 2 ALA A 4 61.29 179.82
REMARK 500 2 THR A 9 -97.69 -39.67
REMARK 500 3 THR A 9 -98.24 -39.85
REMARK 500 3 THR A 22 -82.20 -62.50
REMARK 500 4 ASN A 2 73.35 49.20
REMARK 500 4 THR A 9 -97.14 -41.41
REMARK 500 4 THR A 22 -92.33 -60.52
REMARK 500 5 ASN A 2 142.12 63.86
REMARK 500 5 ALA A 4 51.91 -142.63
REMARK 500 5 ALA A 8 -168.48 -75.99
REMARK 500 5 THR A 9 -95.43 -39.64
REMARK 500 6 ASN A 2 67.35 -68.65
REMARK 500 6 ALA A 4 98.47 48.87
REMARK 500 6 THR A 9 -98.29 -42.20
REMARK 500 6 THR A 22 42.05 -83.19
REMARK 500 7 ASN A 2 69.20 -113.98
REMARK 500 7 PHE A 3 169.17 59.66
REMARK 500 7 ALA A 4 155.73 65.81
REMARK 500 7 CYS A 7 -159.48 -146.08
REMARK 500 7 THR A 9 -96.68 -39.91
REMARK 500 8 ASN A 2 135.38 65.04
REMARK 500 8 THR A 9 -97.01 -40.04
REMARK 500 9 PHE A 3 61.25 -160.38
REMARK 500 9 THR A 9 -96.99 -40.00
REMARK 500 10 ASN A 2 134.48 174.91
REMARK 500 10 ALA A 4 46.39 175.99
REMARK 500 10 THR A 9 -96.21 -39.64
REMARK 500 11 PHE A 3 70.19 43.05
REMARK 500 11 ALA A 4 -163.19 -116.50
REMARK 500 11 THR A 9 -97.49 -40.41
REMARK 500 12 PHE A 3 177.02 51.63
REMARK 500 12 ALA A 8 -169.27 -75.76
REMARK 500 12 THR A 9 -98.04 -39.54
REMARK 500 13 PHE A 3 161.49 59.17
REMARK 500 13 ALA A 4 143.94 -175.69
REMARK 500 13 THR A 9 -98.63 -41.19
REMARK 500 14 THR A 9 -95.70 -39.63
REMARK 500 15 ALA A 4 95.66 -55.34
REMARK 500 15 THR A 9 -97.37 -41.78
REMARK 500 16 THR A 9 -99.95 -40.26
REMARK 500 17 THR A 9 -99.46 -41.73
REMARK 500 18 ASN A 2 74.35 -153.29
REMARK 500 18 THR A 9 -98.03 -40.11
REMARK 500 19 ALA A 4 -92.86 -172.06
REMARK 500 19 THR A 9 -97.03 -39.74
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
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 ARG A 13 0.29 SIDE CHAIN
REMARK 500 1 ARG A 18 0.23 SIDE CHAIN
REMARK 500 2 ARG A 13 0.31 SIDE CHAIN
REMARK 500 2 ARG A 18 0.27 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.32 SIDE CHAIN
REMARK 500 4 ARG A 13 0.26 SIDE CHAIN
REMARK 500 4 ARG A 18 0.31 SIDE CHAIN
REMARK 500 5 ARG A 13 0.29 SIDE CHAIN
REMARK 500 5 ARG A 18 0.32 SIDE CHAIN
REMARK 500 6 ARG A 13 0.27 SIDE CHAIN
REMARK 500 6 ARG A 18 0.19 SIDE CHAIN
REMARK 500 7 ARG A 13 0.27 SIDE CHAIN
REMARK 500 7 ARG A 18 0.15 SIDE CHAIN
REMARK 500 8 ARG A 13 0.17 SIDE CHAIN
REMARK 500 8 ARG A 18 0.29 SIDE CHAIN
REMARK 500 9 ARG A 13 0.32 SIDE CHAIN
REMARK 500 9 ARG A 18 0.20 SIDE CHAIN
REMARK 500 10 ARG A 13 0.32 SIDE CHAIN
REMARK 500 10 ARG A 18 0.28 SIDE CHAIN
REMARK 500 11 ARG A 13 0.25 SIDE CHAIN
REMARK 500 11 ARG A 18 0.31 SIDE CHAIN
REMARK 500 12 ARG A 13 0.32 SIDE CHAIN
REMARK 500 12 ARG A 18 0.31 SIDE CHAIN
REMARK 500 13 ARG A 13 0.17 SIDE CHAIN
REMARK 500 13 ARG A 18 0.18 SIDE CHAIN
REMARK 500 14 ARG A 13 0.31 SIDE CHAIN
REMARK 500 14 ARG A 18 0.19 SIDE CHAIN
REMARK 500 15 ARG A 13 0.28 SIDE CHAIN
REMARK 500 15 ARG A 18 0.31 SIDE CHAIN
REMARK 500 16 ARG A 13 0.28 SIDE CHAIN
REMARK 500 16 ARG A 18 0.12 SIDE CHAIN
REMARK 500 17 ARG A 13 0.31 SIDE CHAIN
REMARK 500 17 ARG A 18 0.30 SIDE CHAIN
REMARK 500 18 ARG A 18 0.27 SIDE CHAIN
REMARK 500 19 ARG A 13 0.31 SIDE CHAIN
REMARK 500 19 ARG A 18 0.32 SIDE CHAIN
REMARK 500 20 ARG A 13 0.25 SIDE CHAIN
REMARK 500 20 ARG A 18 0.20 SIDE CHAIN
REMARK 500 22 ARG A 13 0.31 SIDE CHAIN
REMARK 500 22 ARG A 18 0.18 SIDE CHAIN
REMARK 500 23 ARG A 13 0.27 SIDE CHAIN
REMARK 500 23 ARG A 18 0.26 SIDE CHAIN
REMARK 500 24 ARG A 13 0.31 SIDE CHAIN
REMARK 500 24 ARG A 18 0.28 SIDE CHAIN
REMARK 500 25 ARG A 13 0.28 SIDE CHAIN
REMARK 500 25 ARG A 18 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V28 A 1 23 PDB 1V28 1V28 1 23
SEQRES 1 A 23 GLU ASN PHE ALA GLY GLY CYS ALA THR GLY PHE MET ARG
SEQRES 2 A 23 THR ALA ASP GLY ARG CYS LYS PRO THR PHE
SHEET 1 A 2 PHE A 11 THR A 14 0
SHEET 2 A 2 ARG A 18 PRO A 21 -1 O LYS A 20 N MET A 12
SSBOND 1 CYS A 7 CYS A 19 1555 1555 2.02
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 - 2 20 Bytes