Header list of 1hvw.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 08-JAN-01 1HVW
TITLE HAIRPINLESS MUTANT OF OMEGA-ATRACOTOXIN-HV1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-ATRACOTOXIN-HV1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMEGA-ACTX-HV1A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE NATIVE
SOURCE 4 PEPTIDE IS NATURALLY FOUND IN HADRONYCHE VERSUTA (BLUE MOUNTAIN
SOURCE 5 FUNNEL-WEB SPIDER).THE MUTANT HAIRPINLESS TOXIN WAS SYNTHESIZED BY
SOURCE 6 SOLID-PHASE PEPTIDE SYNTHESIS, OXIDIZED/FOLDED IN A GLUTATHIONE
SOURCE 7 REDOX BUFFER, THEN PURIFIED USING REVERSE-PHASE HPLC.
KEYWDS CYSTINE KNOT, BETA-HAIRPIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.I.FLETCHER,G.F.KING
REVDAT 4 23-FEB-22 1HVW 1 REMARK
REVDAT 3 24-FEB-09 1HVW 1 VERSN
REVDAT 2 27-JAN-04 1HVW 1 JRNL REMARK
REVDAT 1 17-JAN-01 1HVW 0
JRNL AUTH H.W.TEDFORD,J.I.FLETCHER,G.F.KING
JRNL TITL FUNCTIONAL SIGNIFICANCE OF THE BETA HAIRPIN IN THE
JRNL TITL 2 INSECTICIDAL NEUROTOXIN OMEGA-ATRACOTOXIN-HV1A.
JRNL REF J.BIOL.CHEM. V. 276 26568 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11313356
JRNL DOI 10.1074/JBC.M102199200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.I.FLETCHER,R.SMITH,S.I.O'DONOGHUE,M.NILGES,M.CONNOR,
REMARK 1 AUTH 2 M.E.HOWDEN,M.J.CHRISTIE,G.F.KING
REMARK 1 TITL THE STRUCTURE OF A NOVEL INSECTICIDAL NEUROTOXIN,
REMARK 1 TITL 2 OMEGA-ATRACOTOXIN-HV1, FROM THE VENOM OF AN AUSTRALIAN
REMARK 1 TITL 3 FUNNEL WEB SPIDER
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 559 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.WANG,R.SMITH,J.I.FLETCHER,H.WILSON,C.J.WOOD,M.E.HOWDEN,
REMARK 1 AUTH 2 G.F.KING
REMARK 1 TITL STRUCTURE-FUNCTION STUDIES OF OMEGA-ATRACOTOXIN, A POTENT
REMARK 1 TITL 2 ANTAGONIST OF INSECT VOLTAGE-GATED CALCIUM CHANNELS
REMARK 1 REF EUR.J.BIOCHEM. V. 264 488 1999
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1327.1999.00646.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), AXEL BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 231 NOE-DERIVED DISTANCE RESTRAINTS, 19 DIHEDRAL-ANGLE
REMARK 3 RESTRAINTS, AND 16 RESTRAINTS DEFINING 8 HYDROGEN BONDS.
REMARK 4
REMARK 4 1HVW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012614.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : 0.005
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3 MM HAIRPINLESS PEPTIDE, 0.1 MM
REMARK 210 TSP, 25 MICROMOLAR
REMARK 210 CHLORAMPHENICOL; 3 MM
REMARK 210 HAIRPINLESS PEPTIDE, 0.1 MM TSP,
REMARK 210 25 MICROMOLAR CHLORAMPHENICOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 2D_TOCSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 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 GLU A 12 35.24 -173.48
REMARK 500 1 ASN A 13 30.32 -149.62
REMARK 500 2 GLU A 12 33.27 -169.71
REMARK 500 2 ASN A 13 29.79 -150.25
REMARK 500 3 GLU A 12 30.14 -163.30
REMARK 500 4 GLU A 12 32.80 -168.12
REMARK 500 4 ASN A 13 30.68 -143.88
REMARK 500 5 GLU A 12 34.50 -171.61
REMARK 500 5 ASN A 13 29.94 -145.74
REMARK 500 6 GLU A 12 29.08 -145.05
REMARK 500 6 SER A 18 62.09 -107.05
REMARK 500 7 GLU A 12 34.64 -171.82
REMARK 500 7 ASN A 13 33.99 -148.52
REMARK 500 8 PRO A 9 -74.25 -84.45
REMARK 500 8 ASN A 11 49.15 -92.36
REMARK 500 8 GLU A 12 31.81 -154.77
REMARK 500 8 SER A 18 62.00 -102.89
REMARK 500 9 ASN A 11 40.49 -104.13
REMARK 500 9 GLU A 12 28.30 -148.00
REMARK 500 9 SER A 18 61.76 -108.72
REMARK 500 10 PRO A 9 -73.59 -84.86
REMARK 500 10 ASN A 11 36.02 -99.53
REMARK 500 10 GLU A 12 32.39 -147.63
REMARK 500 10 SER A 18 62.19 -110.06
REMARK 500 11 PRO A 9 -74.11 -84.35
REMARK 500 11 ASN A 11 40.27 -106.35
REMARK 500 11 GLU A 12 32.43 -148.41
REMARK 500 12 GLU A 12 33.44 -168.78
REMARK 500 12 ASN A 13 36.24 -142.32
REMARK 500 13 GLU A 12 29.22 -144.50
REMARK 500 13 SER A 18 60.34 -107.62
REMARK 500 14 PRO A 9 -74.78 -84.49
REMARK 500 14 GLU A 12 29.80 -146.39
REMARK 500 14 SER A 18 62.04 -109.65
REMARK 500 15 PRO A 9 -76.80 -84.59
REMARK 500 15 GLU A 12 35.80 -174.59
REMARK 500 15 ASN A 13 26.00 -149.91
REMARK 500 15 SER A 18 61.93 -105.20
REMARK 500 16 PRO A 9 -75.01 -84.59
REMARK 500 16 ASN A 11 42.15 -109.63
REMARK 500 16 GLU A 12 27.66 -149.91
REMARK 500 16 SER A 18 61.56 -109.22
REMARK 500 17 PRO A 9 -76.05 -84.04
REMARK 500 17 GLU A 12 36.43 -176.23
REMARK 500 17 ASN A 13 27.06 -146.43
REMARK 500 17 SER A 18 60.11 -107.29
REMARK 500 18 ASN A 11 41.90 -98.43
REMARK 500 18 GLU A 12 30.27 -155.31
REMARK 500 18 SER A 18 66.88 -106.17
REMARK 500 19 ASN A 11 48.84 -106.73
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AXH RELATED DB: PDB
REMARK 900 NATIVE OMEGA-ATRACOTOXIN-HV1A
DBREF 1HVW A 1 25 UNP P56207 TOT1A_HADVE 4 37
SEQADV 1HVW A UNP P56207 PHE 24 SEE REMARK 999
SEQADV 1HVW A UNP P56207 LYS 25 SEE REMARK 999
SEQADV 1HVW A UNP P56207 GLU 26 SEE REMARK 999
SEQADV 1HVW A UNP P56207 ASN 27 SEE REMARK 999
SEQADV 1HVW A UNP P56207 GLU 28 SEE REMARK 999
SEQADV 1HVW A UNP P56207 ASN 29 SEE REMARK 999
SEQADV 1HVW A UNP P56207 GLY 30 SEE REMARK 999
SEQADV 1HVW A UNP P56207 ASN 31 SEE REMARK 999
SEQADV 1HVW A UNP P56207 THR 32 SEE REMARK 999
SEQADV 1HVW A UNP P56207 VAL 33 SEE REMARK 999
SEQADV 1HVW GLY A 22 UNP P56207 LYS 34 SEE REMARK 999
SEQRES 1 A 25 CYS ILE PRO SER GLY GLN PRO CYS PRO TYR ASN GLU ASN
SEQRES 2 A 25 CYS CYS SER GLN SER CYS THR GLY GLY ARG CYS ASP
SHEET 1 A 2 CYS A 19 THR A 20 0
SHEET 2 A 2 ARG A 23 CYS A 24 -1 O ARG A 23 N THR A 20
SSBOND 1 CYS A 1 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 19 1555 1555 2.02
SSBOND 3 CYS A 14 CYS A 24 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 - 23 20 Bytes