Header list of 1wkt.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 08-MAY-96 1WKT
TITLE WILLIOPSIS MRAKII KILLER TOXIN, NMR SOLUTION STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YEAST KILLER TOXIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: WILLIOPSIS SATURNUS VAR. MRAKII;
SOURCE 3 ORGANISM_TAXID: 4963;
SOURCE 4 STRAIN: VAR. MRAKII
KEYWDS YEAST KILLER TOXIN, WILLIOPSIS MRAKII, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.ANTUCH,P.GUNTERT,K.WUTHRICH
REVDAT 3 02-MAR-22 1WKT 1 REMARK
REVDAT 2 24-FEB-09 1WKT 1 VERSN
REVDAT 1 08-NOV-96 1WKT 0
JRNL AUTH W.ANTUCH,P.GUNTERT,K.WUTHRICH
JRNL TITL ANCESTRAL BETA GAMMA-CRYSTALLIN PRECURSOR STRUCTURE IN A
JRNL TITL 2 YEAST KILLER TOXIN.
JRNL REF NAT.STRUCT.BIOL. V. 3 662 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8756320
JRNL DOI 10.1038/NSB0896-662
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, OPAL
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 LUGINBUHL,GUNTERT,BILLETER,WUTHRICH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WKT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177215.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 309
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 88 O
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 13 VAL A 87 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 15 CYS A 8 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 15 CYS A 18 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 16 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 18 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 20 SER A 42 N - CA - CB ANGL. DEV. = -9.4 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 ASP A 2 126.62 69.12
REMARK 500 1 ASN A 10 -166.00 -126.07
REMARK 500 1 TRP A 20 59.84 -111.99
REMARK 500 1 ALA A 32 80.54 67.77
REMARK 500 1 HIS A 35 25.75 -146.37
REMARK 500 1 ASP A 44 104.65 -19.62
REMARK 500 1 GLN A 47 157.61 -46.94
REMARK 500 1 THR A 77 -169.72 -126.48
REMARK 500 1 ARG A 82 -66.75 -134.14
REMARK 500 1 VAL A 87 -32.87 -139.64
REMARK 500 2 ASP A 2 -59.10 68.21
REMARK 500 2 TRP A 20 42.70 -84.51
REMARK 500 2 TRP A 24 94.13 -58.78
REMARK 500 2 ALA A 32 72.81 61.01
REMARK 500 2 HIS A 35 34.38 -146.35
REMARK 500 2 LYS A 46 137.04 61.93
REMARK 500 2 ASN A 70 62.72 83.11
REMARK 500 2 ASN A 76 66.95 -150.47
REMARK 500 3 TRP A 20 54.87 -151.50
REMARK 500 3 ASN A 23 -23.45 -146.50
REMARK 500 3 ASN A 25 43.84 -141.72
REMARK 500 3 THR A 26 177.02 89.98
REMARK 500 3 CYS A 27 109.89 -47.44
REMARK 500 3 ALA A 32 89.45 48.72
REMARK 500 3 HIS A 35 25.80 -146.53
REMARK 500 3 THR A 43 -86.93 -163.44
REMARK 500 3 ASN A 76 112.82 141.66
REMARK 500 4 ASP A 2 -71.66 63.83
REMARK 500 4 THR A 15 29.50 -142.37
REMARK 500 4 TRP A 20 56.45 -103.71
REMARK 500 4 ASN A 23 -8.17 -143.52
REMARK 500 4 CYS A 27 66.79 -151.52
REMARK 500 4 ALA A 32 99.38 67.99
REMARK 500 4 HIS A 35 28.96 -143.25
REMARK 500 4 SER A 42 -96.14 -107.06
REMARK 500 4 THR A 43 -63.13 -156.85
REMARK 500 4 LYS A 46 163.33 60.81
REMARK 500 4 SER A 56 108.87 -49.71
REMARK 500 4 CYS A 58 55.10 163.03
REMARK 500 4 ARG A 82 -85.78 -136.25
REMARK 500 5 ASP A 2 109.95 64.05
REMARK 500 5 SER A 17 122.05 94.22
REMARK 500 5 ALA A 32 74.05 70.23
REMARK 500 5 HIS A 35 39.90 -145.80
REMARK 500 5 ASP A 44 72.88 -59.97
REMARK 500 5 THR A 64 88.33 -67.80
REMARK 500 6 ASP A 2 123.89 72.10
REMARK 500 6 ASN A 10 -166.55 -125.59
REMARK 500 6 ASN A 14 -73.68 -66.61
REMARK 500 6 SER A 17 114.37 71.98
REMARK 500
REMARK 500 THIS ENTRY HAS 204 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 TYR A 4 0.09 SIDE CHAIN
REMARK 500 1 TYR A 84 0.19 SIDE CHAIN
REMARK 500 2 ARG A 61 0.09 SIDE CHAIN
REMARK 500 2 TYR A 80 0.11 SIDE CHAIN
REMARK 500 2 ARG A 85 0.08 SIDE CHAIN
REMARK 500 2 ARG A 86 0.17 SIDE CHAIN
REMARK 500 3 TYR A 4 0.07 SIDE CHAIN
REMARK 500 3 TYR A 84 0.10 SIDE CHAIN
REMARK 500 4 TYR A 80 0.21 SIDE CHAIN
REMARK 500 4 TYR A 84 0.16 SIDE CHAIN
REMARK 500 4 ARG A 85 0.09 SIDE CHAIN
REMARK 500 5 ARG A 61 0.10 SIDE CHAIN
REMARK 500 5 TYR A 80 0.26 SIDE CHAIN
REMARK 500 5 TYR A 84 0.07 SIDE CHAIN
REMARK 500 5 ARG A 85 0.12 SIDE CHAIN
REMARK 500 6 ARG A 61 0.11 SIDE CHAIN
REMARK 500 6 TYR A 80 0.11 SIDE CHAIN
REMARK 500 6 TYR A 84 0.14 SIDE CHAIN
REMARK 500 7 PHE A 79 0.11 SIDE CHAIN
REMARK 500 7 TYR A 80 0.06 SIDE CHAIN
REMARK 500 8 TYR A 4 0.12 SIDE CHAIN
REMARK 500 8 ARG A 61 0.19 SIDE CHAIN
REMARK 500 8 PHE A 79 0.09 SIDE CHAIN
REMARK 500 8 TYR A 80 0.09 SIDE CHAIN
REMARK 500 9 TYR A 4 0.07 SIDE CHAIN
REMARK 500 9 TYR A 80 0.07 SIDE CHAIN
REMARK 500 9 ARG A 85 0.11 SIDE CHAIN
REMARK 500 9 ARG A 86 0.12 SIDE CHAIN
REMARK 500 10 TYR A 80 0.17 SIDE CHAIN
REMARK 500 10 TYR A 84 0.26 SIDE CHAIN
REMARK 500 11 TYR A 80 0.07 SIDE CHAIN
REMARK 500 11 ARG A 82 0.11 SIDE CHAIN
REMARK 500 12 TYR A 80 0.11 SIDE CHAIN
REMARK 500 13 TYR A 80 0.12 SIDE CHAIN
REMARK 500 13 TYR A 84 0.11 SIDE CHAIN
REMARK 500 13 ARG A 86 0.09 SIDE CHAIN
REMARK 500 14 TYR A 84 0.08 SIDE CHAIN
REMARK 500 15 ARG A 61 0.10 SIDE CHAIN
REMARK 500 15 TYR A 84 0.14 SIDE CHAIN
REMARK 500 16 TYR A 4 0.07 SIDE CHAIN
REMARK 500 16 TYR A 84 0.06 SIDE CHAIN
REMARK 500 18 TYR A 4 0.09 SIDE CHAIN
REMARK 500 18 TYR A 80 0.13 SIDE CHAIN
REMARK 500 18 ARG A 82 0.10 SIDE CHAIN
REMARK 500 18 TYR A 84 0.19 SIDE CHAIN
REMARK 500 18 ARG A 86 0.09 SIDE CHAIN
REMARK 500 19 TYR A 80 0.10 SIDE CHAIN
REMARK 500 20 PHE A 79 0.08 SIDE CHAIN
REMARK 500 20 ARG A 86 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WKT A 1 88 UNP P10410 TOXK_WILMR 1 88
SEQRES 1 A 88 GLY ASP GLY TYR LEU ILE MET CYS LYS ASN CYS ASP PRO
SEQRES 2 A 88 ASN THR GLY SER CYS ASP TRP LYS GLN ASN TRP ASN THR
SEQRES 3 A 88 CYS VAL GLY ILE GLY ALA ASN VAL HIS TRP MET VAL THR
SEQRES 4 A 88 GLY GLY SER THR ASP GLY LYS GLN GLY CYS ALA THR ILE
SEQRES 5 A 88 TRP GLU GLY SER GLY CYS VAL GLY ARG SER THR THR MET
SEQRES 6 A 88 CYS CYS PRO ALA ASN THR CYS CYS ASN ILE ASN THR GLY
SEQRES 7 A 88 PHE TYR ILE ARG SER TYR ARG ARG VAL GLU
SHEET 1 S1 4 SER A 17 ASP A 19 0
SHEET 2 S1 4 TYR A 4 LYS A 9 -1 O MET A 7 N ASP A 19
SHEET 3 S1 4 HIS A 35 GLY A 40 -1 O TRP A 36 N CYS A 8
SHEET 4 S1 4 THR A 71 ILE A 75 -1 O CYS A 73 N MET A 37
SHEET 1 S2 4 VAL A 28 ILE A 30 0
SHEET 2 S2 4 ARG A 82 VAL A 87 -1 O ARG A 82 N ILE A 30
SHEET 3 S2 4 GLY A 48 GLU A 54 -1 N TRP A 53 O SER A 83
SHEET 4 S2 4 ARG A 61 CYS A 67 -1 N THR A 63 O ILE A 52
SSBOND 1 CYS A 8 CYS A 18 1555 1555 2.08
SSBOND 2 CYS A 11 CYS A 72 1555 1555 2.08
SSBOND 3 CYS A 27 CYS A 58 1555 1555 2.09
SSBOND 4 CYS A 49 CYS A 66 1555 1555 2.08
SSBOND 5 CYS A 67 CYS A 73 1555 1555 2.07
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