Header list of 1kqi.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 06-JAN-02 1KQI
TITLE NMR SOLUTION STRUCTURE OF THE TRANS PRO30 ISOMER OF ACTX-HI:OB4219
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTX-HI:OB4219;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HADRONYCHE INFENSA;
SOURCE 3 ORGANISM_TAXID: 153481;
SOURCE 4 OTHER_DETAILS: HADRONYCHE INFENSA FOUND AT ORCHID BEACH, FRASER
SOURCE 5 ISLAND, AUSTRALIA
KEYWDS HADRONYCHE INFENSA, FUNNEL WEB, SPIDER VENOM, CIS-TRANS
KEYWDS 2 ISOMERISATION, DISULFIDE RICH, CYSTINE KNOT, SOLUTION STRUCTURE, NMR
KEYWDS 3 SPECTROSCOPY, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,D.WILSON,N.L.DALY,P.F.ALEWOOD,D.J.CRAIK
REVDAT 4 23-FEB-22 1KQI 1 REMARK
REVDAT 3 24-FEB-09 1KQI 1 VERSN
REVDAT 2 16-OCT-02 1KQI 1 JRNL REMARK MASTER
REVDAT 1 06-FEB-02 1KQI 0
JRNL AUTH K.J.ROSENGREN,D.WILSON,N.L.DALY,P.F.ALEWOOD,D.J.CRAIK
JRNL TITL SOLUTION STRUCTURES OF THE CIS- AND TRANS-PRO30 ISOMERS OF A
JRNL TITL 2 NOVEL 38-RESIDUE TOXIN FROM THE VENOM OF HADRONYCHE INFENSA
JRNL TITL 3 SP. THAT CONTAINS A CYSTINE-KNOT MOTIF WITHIN ITS FOUR
JRNL TITL 4 DISULFIDE BONDS
JRNL REF BIOCHEMISTRY V. 41 3294 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11876637
JRNL DOI 10.1021/BI011932Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, ARIA 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE, J.P., O'DONOGHUE, S.I.,
REMARK 3 NILGES, M.N. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 INITIAL STRUCTURES WERE GENERATED BY TORSION ANGLE DYNAMICS.
REMARK 3 THESE WERE THEN REFINED AND MINIMIZED IN A WATER SHELL USING
REMARK 3 CARTESIAN DYNAMICS AND RESTRAINED POWELL MINIMIZATION ACCORDING
REMARK 3 TO ARIA AND CNS PROTOCOLS.
REMARK 4
REMARK 4 1KQI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015233.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 293; 303
REMARK 210 PH : 5.0; 5.0; 5.0
REMARK 210 IONIC STRENGTH : 0 MM; 0 MM; 0 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MG ACTX-HI:OB4219; 3MG ACTX
REMARK 210 -HI:OB4219
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; NOESY; TOCSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.5, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS.
REMARK 210 REFINEMENT AND ENERGY
REMARK 210 MINIMIZATION IN A WATER SHELL
REMARK 210 USING CARTESIAN DYNAMICS AND
REMARK 210 POWELL MINIMIZATION.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST 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: 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 HZ2 LYS A 1 OD1 ASP A 15 1.54
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 ALA A 4 -166.90 -78.90
REMARK 500 1 CYS A 25 52.29 -119.97
REMARK 500 1 CYS A 31 104.35 -49.48
REMARK 500 2 ALA A 4 -162.44 -79.09
REMARK 500 2 PRO A 30 -171.26 -68.59
REMARK 500 3 PRO A 20 52.31 -99.00
REMARK 500 3 ILE A 26 -168.02 -109.59
REMARK 500 3 CYS A 31 102.13 -58.53
REMARK 500 4 TRP A 12 -54.28 -128.41
REMARK 500 4 PRO A 20 40.06 -95.45
REMARK 500 4 CYS A 31 106.75 -51.89
REMARK 500 5 ALA A 4 -158.38 -79.27
REMARK 500 5 TRP A 12 -53.22 -137.17
REMARK 500 5 PRO A 30 -175.89 -64.72
REMARK 500 5 CYS A 31 105.60 -52.65
REMARK 500 6 ALA A 4 -164.95 -78.32
REMARK 500 6 ALA A 6 35.52 70.35
REMARK 500 6 CYS A 25 72.93 -100.08
REMARK 500 6 PRO A 30 -165.12 -66.23
REMARK 500 6 CYS A 31 99.17 -62.43
REMARK 500 7 ALA A 4 -166.04 -78.41
REMARK 500 7 PRO A 20 38.67 -98.08
REMARK 500 7 CYS A 31 103.16 -51.31
REMARK 500 8 ALA A 4 -168.62 -78.15
REMARK 500 8 SER A 13 148.57 -173.21
REMARK 500 8 CYS A 25 68.97 -101.79
REMARK 500 8 PRO A 30 -174.59 -65.15
REMARK 500 8 CYS A 31 99.91 -59.38
REMARK 500 9 ALA A 4 -168.56 -78.48
REMARK 500 9 TRP A 12 -34.20 -136.53
REMARK 500 9 SER A 13 44.79 -77.77
REMARK 500 9 CYS A 25 53.92 -143.25
REMARK 500 9 CYS A 31 97.93 -48.64
REMARK 500 10 ALA A 4 -163.41 -78.31
REMARK 500 10 CYS A 25 58.43 -143.30
REMARK 500 10 CYS A 31 99.25 -52.32
REMARK 500 11 SER A 13 148.14 -174.18
REMARK 500 11 CYS A 31 95.52 -57.61
REMARK 500 12 ALA A 4 -162.18 -78.79
REMARK 500 12 SER A 13 149.35 -174.09
REMARK 500 12 PRO A 20 40.98 -104.64
REMARK 500 12 CYS A 25 59.04 -118.99
REMARK 500 12 PHE A 27 -81.62 -67.01
REMARK 500 12 PHE A 28 36.06 -79.86
REMARK 500 13 ALA A 4 -168.09 -78.41
REMARK 500 13 SER A 13 139.09 -175.47
REMARK 500 13 PRO A 20 44.53 -101.00
REMARK 500 13 CYS A 31 108.55 -50.33
REMARK 500 14 ALA A 4 -165.88 -78.01
REMARK 500 14 SER A 13 143.93 -175.36
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KQH RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE CIS PRO30 ISOMER OF ACTX-HI:OB4219
DBREF 1KQI A 1 38 PDB 1KQI 1KQI 1 38
SEQRES 1 A 38 LYS CYS LEU ALA GLU ALA ALA ASP CYS SER PRO TRP SER
SEQRES 2 A 38 GLY ASP SER CYS CYS LYS PRO TYR LEU CYS SER CYS ILE
SEQRES 3 A 38 PHE PHE TYR PRO CYS SER CYS ARG PRO LYS GLY TRP
SHEET 1 A 3 ALA A 7 ASP A 8 0
SHEET 2 A 3 SER A 32 ARG A 34 -1 O CYS A 33 N ALA A 7
SHEET 3 A 3 LEU A 22 SER A 24 -1 N SER A 24 O SER A 32
SSBOND 1 CYS A 2 CYS A 18 1555 1555 2.03
SSBOND 2 CYS A 9 CYS A 23 1555 1555 2.03
SSBOND 3 CYS A 17 CYS A 33 1555 1555 2.03
SSBOND 4 CYS A 25 CYS A 31 1555 1555 2.03
CISPEP 1 LYS A 19 PRO A 20 1 1.06
CISPEP 2 LYS A 19 PRO A 20 2 1.45
CISPEP 3 LYS A 19 PRO A 20 3 1.13
CISPEP 4 LYS A 19 PRO A 20 4 1.46
CISPEP 5 LYS A 19 PRO A 20 5 0.94
CISPEP 6 LYS A 19 PRO A 20 6 1.31
CISPEP 7 LYS A 19 PRO A 20 7 1.25
CISPEP 8 LYS A 19 PRO A 20 8 1.11
CISPEP 9 LYS A 19 PRO A 20 9 1.05
CISPEP 10 LYS A 19 PRO A 20 10 0.94
CISPEP 11 LYS A 19 PRO A 20 11 1.22
CISPEP 12 LYS A 19 PRO A 20 12 1.29
CISPEP 13 LYS A 19 PRO A 20 13 1.49
CISPEP 14 LYS A 19 PRO A 20 14 1.32
CISPEP 15 LYS A 19 PRO A 20 15 1.08
CISPEP 16 LYS A 19 PRO A 20 16 1.38
CISPEP 17 LYS A 19 PRO A 20 17 1.22
CISPEP 18 LYS A 19 PRO A 20 18 1.33
CISPEP 19 LYS A 19 PRO A 20 19 1.19
CISPEP 20 LYS A 19 PRO A 20 20 1.37
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