Header list of 1i02.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 28-JAN-01 1I02
TITLE NMR STRUCTURE OF CTX A3 AT NEUTRAL PH (20 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARDIOTOXIN-3;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NAJA ATRA;
SOURCE 3 ORGANISM_COMMON: CHINESE COBRA;
SOURCE 4 ORGANISM_TAXID: 8656
KEYWDS CARDIOTOXIN, CTX, CYTOTOXIN, HEMOLYSIS, MEMBRANE BINDING PROTEIN, GAG
KEYWDS 2 BINDING PROTEIN, BOUND WATER, THREE-FINGER TYPE, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.-C.SUE,J.HAROLD,W.-G.WU
REVDAT 6 23-FEB-22 1I02 1 REMARK
REVDAT 5 24-FEB-09 1I02 1 VERSN
REVDAT 4 01-APR-03 1I02 1 JRNL
REVDAT 3 31-DEC-02 1I02 1 REMARK
REVDAT 2 07-NOV-01 1I02 1 JRNL
REVDAT 1 14-FEB-01 1I02 0
JRNL AUTH S.C.SUE,H.C.JARRELL,J.R.BRISSON,W.G.WU
JRNL TITL DYNAMIC CHARACTERIZATION OF THE WATER BINDING LOOP IN THE
JRNL TITL 2 P-TYPE CARDIOTOXIN: IMPLICATION FOR THE ROLE OF THE BOUND
JRNL TITL 3 WATER MOLECULE.
JRNL REF BIOCHEMISTRY V. 40 12782 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11669614
JRNL DOI 10.1021/BI010848F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE NMR STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 680 NOE RESTRAINTS, 40 DIHEDRAL ANGLE RESTRAINTS, 19 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS AND 4 DISULFIDE BOND LINKAGES.
REMARK 4
REMARK 4 1I02 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012737.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 283
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 5MM CARDIOTOXIN A3; 10MM
REMARK 210 PHOSPHATE BUFFER; 5 MM
REMARK 210 CARDIOTOXIN A3; 10MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED STRUCTURES ARE THE
REMARK 210 20 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: 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 MET A 26 H THR A 29 1.51
REMARK 500 O LEU A 20 H ILE A 39 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 LEU A 6 -37.23 -36.72
REMARK 500 1 PRO A 8 47.86 -70.45
REMARK 500 1 LEU A 9 -45.34 -136.30
REMARK 500 1 VAL A 27 -35.32 -31.26
REMARK 500 1 PRO A 43 -159.77 -61.22
REMARK 500 1 SER A 46 -157.43 -143.05
REMARK 500 1 ARG A 58 73.05 54.73
REMARK 500 2 PRO A 8 24.52 -70.40
REMARK 500 2 PRO A 15 -179.54 -62.77
REMARK 500 2 PRO A 43 -152.85 -64.75
REMARK 500 2 LEU A 48 -61.95 -132.14
REMARK 500 3 LEU A 6 -33.05 -32.30
REMARK 500 3 PRO A 8 55.34 -69.41
REMARK 500 3 LEU A 9 -40.24 -144.68
REMARK 500 3 ASN A 19 -3.41 -150.05
REMARK 500 3 VAL A 27 -24.96 -38.35
REMARK 500 3 PRO A 30 0.06 -68.68
REMARK 500 3 PRO A 43 178.48 -58.79
REMARK 500 3 SER A 46 -150.85 -127.91
REMARK 500 3 ARG A 58 61.05 80.75
REMARK 500 4 PRO A 8 57.24 -66.95
REMARK 500 4 LEU A 9 -47.48 -148.49
REMARK 500 4 PRO A 15 172.12 -56.32
REMARK 500 4 VAL A 27 -43.31 -22.82
REMARK 500 4 LYS A 31 20.71 -79.70
REMARK 500 4 SER A 46 -141.13 -144.92
REMARK 500 4 LEU A 47 -88.25 -44.72
REMARK 500 5 PRO A 8 4.59 -68.88
REMARK 500 5 MET A 26 32.55 -91.23
REMARK 500 5 VAL A 27 -40.18 63.43
REMARK 500 5 PRO A 43 -176.94 -54.91
REMARK 500 5 SER A 46 -146.52 -110.16
REMARK 500 5 ARG A 58 74.99 77.20
REMARK 500 6 PRO A 8 54.78 -68.05
REMARK 500 6 LEU A 9 -45.18 -148.71
REMARK 500 6 PRO A 30 39.87 -67.94
REMARK 500 6 SER A 46 -141.71 -97.69
REMARK 500 6 LEU A 48 24.15 -144.76
REMARK 500 7 ASN A 4 164.37 -45.27
REMARK 500 7 PRO A 8 21.37 -71.35
REMARK 500 7 VAL A 27 -28.21 -38.79
REMARK 500 7 PRO A 43 -168.02 -62.13
REMARK 500 7 SER A 46 -157.77 -132.43
REMARK 500 7 LEU A 48 30.63 -140.06
REMARK 500 7 ARG A 58 66.46 62.53
REMARK 500 8 PRO A 8 7.39 -68.36
REMARK 500 8 PRO A 15 -171.37 -64.85
REMARK 500 8 VAL A 27 -33.41 -32.67
REMARK 500 8 PRO A 30 31.45 -75.36
REMARK 500 8 PRO A 43 -160.52 -55.94
REMARK 500
REMARK 500 THIS ENTRY HAS 130 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 36 0.32 SIDE CHAIN
REMARK 500 1 ARG A 58 0.09 SIDE CHAIN
REMARK 500 2 ARG A 36 0.16 SIDE CHAIN
REMARK 500 2 ARG A 58 0.19 SIDE CHAIN
REMARK 500 3 ARG A 36 0.32 SIDE CHAIN
REMARK 500 3 ARG A 58 0.14 SIDE CHAIN
REMARK 500 4 ARG A 58 0.31 SIDE CHAIN
REMARK 500 5 ARG A 36 0.28 SIDE CHAIN
REMARK 500 5 ARG A 58 0.16 SIDE CHAIN
REMARK 500 6 ARG A 36 0.24 SIDE CHAIN
REMARK 500 6 ARG A 58 0.15 SIDE CHAIN
REMARK 500 7 ARG A 36 0.27 SIDE CHAIN
REMARK 500 7 ARG A 58 0.30 SIDE CHAIN
REMARK 500 8 ARG A 36 0.31 SIDE CHAIN
REMARK 500 8 ARG A 58 0.31 SIDE CHAIN
REMARK 500 9 ARG A 36 0.25 SIDE CHAIN
REMARK 500 9 ARG A 58 0.10 SIDE CHAIN
REMARK 500 10 ARG A 36 0.18 SIDE CHAIN
REMARK 500 10 ARG A 58 0.21 SIDE CHAIN
REMARK 500 11 ARG A 58 0.31 SIDE CHAIN
REMARK 500 12 ARG A 36 0.20 SIDE CHAIN
REMARK 500 12 ARG A 58 0.19 SIDE CHAIN
REMARK 500 13 ARG A 36 0.18 SIDE CHAIN
REMARK 500 13 ARG A 58 0.29 SIDE CHAIN
REMARK 500 14 ARG A 36 0.25 SIDE CHAIN
REMARK 500 14 ARG A 58 0.32 SIDE CHAIN
REMARK 500 15 ARG A 36 0.23 SIDE CHAIN
REMARK 500 15 ARG A 58 0.32 SIDE CHAIN
REMARK 500 16 ARG A 36 0.29 SIDE CHAIN
REMARK 500 16 ARG A 58 0.18 SIDE CHAIN
REMARK 500 17 ARG A 36 0.16 SIDE CHAIN
REMARK 500 17 ARG A 58 0.08 SIDE CHAIN
REMARK 500 18 ARG A 36 0.28 SIDE CHAIN
REMARK 500 18 ARG A 58 0.31 SIDE CHAIN
REMARK 500 19 ARG A 36 0.25 SIDE CHAIN
REMARK 500 19 ARG A 58 0.21 SIDE CHAIN
REMARK 500 20 ARG A 36 0.31 SIDE CHAIN
REMARK 500 20 ARG A 58 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CB9 RELATED DB: PDB
REMARK 900 1CB9 CONTAINS CYTOTOXIN II (CARDIOTOXIN) FROM NAJA NAJA OXIANA IN
REMARK 900 AQUEOUS SOLUTION (MAJOR FORM)
REMARK 900 RELATED ID: 1CDT RELATED DB: PDB
REMARK 900 1CDT CONTAINS CARDIOTOXIN V4II (TOXIN III)
REMARK 900 RELATED ID: 2CDX RELATED DB: PDB
REMARK 900 2CDX CONTAINS CARDIOTOXIN A1 FROM TAIWAN COBRA (NAJA NAJA ATRA)
REMARK 900 RELATED ID: 2CRT RELATED DB: PDB
REMARK 900 2CRT CONTAINS CARDIOTOXIN A3 FROM TAIWAN COBRA (NAJA NAJA ATRA)
REMARK 900 RELATED ID: 1KXI RELATED DB: PDB
REMARK 900 1KXI CONTAINS CYTOTOXIN HOMOLOG PRECURSOR
REMARK 900 RELATED ID: 1TGX RELATED DB: PDB
REMARK 900 1TGX CONTAINS TOXIN GAMMA (CARDIOTOXIN)
DBREF 1I02 A 1 60 UNP P60301 CTX3_NAJAT 22 81
SEQRES 1 A 60 LEU LYS CYS ASN LYS LEU VAL PRO LEU PHE TYR LYS THR
SEQRES 2 A 60 CYS PRO ALA GLY LYS ASN LEU CYS TYR LYS MET PHE MET
SEQRES 3 A 60 VAL ALA THR PRO LYS VAL PRO VAL LYS ARG GLY CYS ILE
SEQRES 4 A 60 ASP VAL CYS PRO LYS SER SER LEU LEU VAL LYS TYR VAL
SEQRES 5 A 60 CYS CYS ASN THR ASP ARG CYS ASN
SHEET 1 A 2 LYS A 2 ASN A 4 0
SHEET 2 A 2 TYR A 11 THR A 13 -1 O LYS A 12 N CYS A 3
SHEET 1 B 3 LYS A 35 ILE A 39 0
SHEET 2 B 3 LEU A 20 PHE A 25 -1 O LEU A 20 N ILE A 39
SHEET 3 B 3 LYS A 50 ASN A 55 -1 O LYS A 50 N PHE A 25
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.02
SSBOND 2 CYS A 14 CYS A 38 1555 1555 2.02
SSBOND 3 CYS A 42 CYS A 53 1555 1555 2.02
SSBOND 4 CYS A 54 CYS A 59 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 - b 23 2 Bytes