Header list of 1kd6.pdb file
Complete list - b 23 2 Bytes
HEADER MEMBRANE PROTEIN 12-NOV-01 1KD6
TITLE SOLUTION STRUCTURE OF THE EUKARYOTIC PORE-FORMING CYTOLYSIN
TITLE 2 EQUINATOXIN II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EQUINATOXIN II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EQTII, TENEBROSIN C;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINIA EQUINA;
SOURCE 3 ORGANISM_TAXID: 6106;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAG2.1
KEYWDS CYTOLYSIN, PORE FORMATION, BETA SANDWICH, TOXIN, SEA ANEMONE,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.G.HINDS,W.ZHANG,G.ANDERLUH,P.E.HANSEN,R.S.NORTON
REVDAT 4 23-FEB-22 1KD6 1 REMARK
REVDAT 3 24-FEB-09 1KD6 1 VERSN
REVDAT 2 27-FEB-02 1KD6 1 TITLE
REVDAT 1 13-FEB-02 1KD6 0
JRNL AUTH M.G.HINDS,W.ZHANG,G.ANDERLUH,P.E.HANSEN,R.S.NORTON
JRNL TITL SOLUTION STRUCTURE OF THE EUKARYOTIC PORE-FORMING CYTOLYSIN
JRNL TITL 2 EQUINATOXIN II: IMPLICATIONS FOR PORE FORMATION.
JRNL REF J.MOL.BIOL. V. 315 1219 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11827489
JRNL DOI 10.1006/JMBI.2001.5321
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.ZHANG,M.G.HINDS,G.ANDERLUH,P.E.HANSEN,R.S.NORTON
REMARK 1 TITL SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS OF THE POTENT
REMARK 1 TITL 2 CYTOLYSIN EQUINATOXIN II
REMARK 1 REF J.BIOMOL.NMR V. 18 281 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1026793926271
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6, CNS 1.0
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), BRUNGER, A.T., ADAMS,
REMARK 3 P.D., CLORE, G.M., DELANO, W.L., GROS, P., GROSSE-
REMARK 3 KUNSTLEVE, R.W., JIANG, J.S., KUSZEWSKI, J.,
REMARK 3 NILGES, M., PANNU, N.S, READ, R.J., RICE, L.M.,
REMARK 3 SIMONSON, T., WARREN, G.L. ACTA CRYSTALLOGR. D
REMARK 3 BIOL. CRYSTALLOGR. 1998, 54, 905-921. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 3161 TOTAL
REMARK 3 RESTRAINTS INCLUDING 167 ANGLE CONSTRAINTS, 42 HYDROGEN BONDS,
REMARK 3 534 SEQUENTIAL, 972 SHORT RANGE AND 1346 LONG RANGE DISTANCE
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1KD6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014831.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 13C, 15N EQUINATOXIN II PH
REMARK 210 3.9; 1MM 15N EQUINATOXIN II PH
REMARK 210 3.9; 1MM UNLABELLED EQUINATOXIN
REMARK 210 II PH 3.9
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3.13, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS DISTANCE
REMARK 210 GEOMETRY SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 250
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE
REMARK 210 SPECTROSCOPY
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
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 2 -56.61 -146.51
REMARK 500 1 ALA A 5 44.86 -109.02
REMARK 500 1 ALA A 7 44.87 -97.04
REMARK 500 1 ALA A 12 -32.95 -154.66
REMARK 500 1 ALA A 25 34.41 -90.18
REMARK 500 1 ASN A 28 43.66 -78.44
REMARK 500 1 SER A 54 -70.89 -133.98
REMARK 500 1 THR A 56 -167.46 -165.61
REMARK 500 1 SER A 57 -53.53 -159.96
REMARK 500 1 HIS A 63 51.29 -119.48
REMARK 500 1 GLN A 76 46.60 -145.19
REMARK 500 1 LYS A 77 175.81 52.64
REMARK 500 1 ARG A 79 -46.93 72.86
REMARK 500 1 PRO A 81 -142.10 -71.53
REMARK 500 1 SER A 95 -100.34 -167.35
REMARK 500 1 TYR A 108 40.12 -84.26
REMARK 500 1 ASN A 111 -131.61 -160.76
REMARK 500 1 ARG A 126 129.32 69.99
REMARK 500 1 ASP A 129 -159.42 -161.19
REMARK 500 1 GLU A 135 -56.51 56.80
REMARK 500 1 TYR A 137 40.46 -78.34
REMARK 500 1 SER A 141 76.94 -153.38
REMARK 500 1 ASN A 147 92.17 -47.19
REMARK 500 1 ARG A 152 144.16 -171.50
REMARK 500 1 PHE A 163 -174.58 -175.15
REMARK 500 1 SER A 166 -121.50 -82.36
REMARK 500 1 GLU A 173 75.85 -116.40
REMARK 500 2 ALA A 5 131.72 70.00
REMARK 500 2 ALA A 12 -38.75 -154.87
REMARK 500 2 LEU A 26 44.90 -80.78
REMARK 500 2 ASN A 28 -45.84 -135.09
REMARK 500 2 SER A 41 -76.93 -92.52
REMARK 500 2 LEU A 48 -57.73 -120.45
REMARK 500 2 THR A 56 143.18 -171.06
REMARK 500 2 ASP A 58 37.27 -176.84
REMARK 500 2 ILE A 59 -65.92 60.99
REMARK 500 2 LYS A 77 -155.20 -80.36
REMARK 500 2 ASP A 78 119.15 68.05
REMARK 500 2 ARG A 79 -40.84 -170.42
REMARK 500 2 ALA A 83 41.59 -143.49
REMARK 500 2 ALA A 86 105.06 -165.83
REMARK 500 2 MET A 94 -93.20 -81.81
REMARK 500 2 SER A 95 -45.74 -151.17
REMARK 500 2 ASP A 96 33.25 -89.68
REMARK 500 2 ASP A 109 145.49 69.60
REMARK 500 2 TYR A 110 42.03 -84.23
REMARK 500 2 ASN A 111 -114.60 -80.18
REMARK 500 2 TRP A 112 37.97 -153.49
REMARK 500 2 LYS A 123 46.84 -82.18
REMARK 500 2 ARG A 126 123.14 72.39
REMARK 500
REMARK 500 THIS ENTRY HAS 517 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE THERE ARE TWO NATURALLY OCCURING SEQUENCE VARIANTS
REMARK 999 P116D AND T212S FOR EQUINATOXIN II P116D VARIANT OCCURS IN 50%
REMARK 999 OF MOLECULES FROM ACTINIA EQUINA AND THE T212S VARIANT IN ACTINA
REMARK 999 TENEBROSA.
DBREF 1KD6 A 1 179 UNP P61914 EQT2_ACTEQ 36 214
SEQADV 1KD6 THR A 177 UNP P61914 SER 212 SEE REMARK 999
SEQRES 1 A 179 SER ALA ASP VAL ALA GLY ALA VAL ILE ASP GLY ALA SER
SEQRES 2 A 179 LEU SER PHE ASP ILE LEU LYS THR VAL LEU GLU ALA LEU
SEQRES 3 A 179 GLY ASN VAL LYS ARG LYS ILE ALA VAL GLY VAL ASP ASN
SEQRES 4 A 179 GLU SER GLY LYS THR TRP THR ALA LEU ASN THR TYR PHE
SEQRES 5 A 179 ARG SER GLY THR SER ASP ILE VAL LEU PRO HIS LYS VAL
SEQRES 6 A 179 PRO HIS GLY LYS ALA LEU LEU TYR ASN GLY GLN LYS ASP
SEQRES 7 A 179 ARG GLY PRO VAL ALA THR GLY ALA VAL GLY VAL LEU ALA
SEQRES 8 A 179 TYR LEU MET SER ASP GLY ASN THR LEU ALA VAL LEU PHE
SEQRES 9 A 179 SER VAL PRO TYR ASP TYR ASN TRP TYR SER ASN TRP TRP
SEQRES 10 A 179 ASN VAL ARG ILE TYR LYS GLY LYS ARG ARG ALA ASP GLN
SEQRES 11 A 179 ARG MET TYR GLU GLU LEU TYR TYR ASN LEU SER PRO PHE
SEQRES 12 A 179 ARG GLY ASP ASN GLY TRP HIS THR ARG ASN LEU GLY TYR
SEQRES 13 A 179 GLY LEU LYS SER ARG GLY PHE MET ASN SER SER GLY HIS
SEQRES 14 A 179 ALA ILE LEU GLU ILE HIS VAL THR LYS ALA
HELIX 1 1 SER A 15 ALA A 25 1 11
HELIX 2 2 ASP A 129 GLU A 134 1 6
SHEET 1 A 5 LYS A 69 GLY A 75 0
SHEET 2 A 5 ILE A 33 ASN A 39 -1 N VAL A 35 O TYR A 73
SHEET 3 A 5 ALA A 170 THR A 177 1 O ALA A 170 N ALA A 34
SHEET 4 A 5 LYS A 159 ASN A 165 -1 N LYS A 159 O THR A 177
SHEET 5 A 5 HIS A 150 ASN A 153 -1 N ARG A 152 O SER A 160
SHEET 1 B 5 THR A 46 PHE A 52 0
SHEET 2 B 5 GLY A 88 LEU A 93 -1 O LEU A 93 N THR A 46
SHEET 3 B 5 ASN A 98 SER A 105 -1 O PHE A 104 N GLY A 88
SHEET 4 B 5 TRP A 116 LYS A 123 -1 O TYR A 122 N THR A 99
SHEET 5 B 5 PHE A 143 ARG A 144 -1 O PHE A 143 N TRP A 117
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