Header list of 1eci.pdb file
Complete list - b 16 2 Bytes
HEADER TOXIN 16-AUG-95 1ECI
TITLE ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTATOMIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ECTATOMIN;
COMPND 6 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECTATOMMA TUBERCULATUM;
SOURCE 3 ORGANISM_TAXID: 39300;
SOURCE 4 TISSUE: VENOM;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ECTATOMMA TUBERCULATUM;
SOURCE 7 ORGANISM_TAXID: 39300;
SOURCE 8 TISSUE: VENOM
KEYWDS PORE-FORMING TOXINS, ANT VENOMS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.E.NOLDE,A.G.SOBOL,K.A.PLUZHNIKOV,A.S.ARSENIEV,E.V.GRISHIN
REVDAT 3 16-FEB-22 1ECI 1 REMARK
REVDAT 2 24-FEB-09 1ECI 1 VERSN
REVDAT 1 07-DEC-95 1ECI 0
JRNL AUTH D.E.NOLDE,A.G.SOBOL,K.A.PLUZHNIKOV,E.V.GRISHIN,A.S.ARSENIEV
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF ECTATOMIN FROM ECTATOMMA
JRNL TITL 2 TUBERCULATUM ANT VENOM.
JRNL REF J.BIOMOL.NMR V. 5 1 1995
JRNL REFN ISSN 0925-2738
JRNL PMID 7881269
JRNL DOI 10.1007/BF00227465
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.S.ARSENIEV,K.A.PLUZHNIKOV,D.E.NOLDE,A.G.SOBOL,M.YU.TORGOV,
REMARK 1 AUTH 2 S.V.SUKHANOV,E.V.GRISHIN
REMARK 1 TITL TOXIC PRINCIPLE OF SELVA ANT VENOM IS A PORE-FORMING PROTEIN
REMARK 1 TITL 2 TRANSFORMER
REMARK 1 REF FEBS LETT. V. 347 112 1994
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CHARMM
REMARK 3 AUTHORS : BROOKS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ECI 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_1000173007.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 CYS A 12 -63.67 -21.75
REMARK 500 1 LYS A 21 47.58 -82.77
REMARK 500 1 SER B 23 43.74 -165.13
REMARK 500 2 CYS A 12 -62.38 -23.84
REMARK 500 2 SER B 23 44.97 -165.25
REMARK 500 2 CYS B 32 -71.50 -66.41
REMARK 500 2 ASP B 33 64.03 -166.42
REMARK 500 3 CYS A 12 -62.64 -23.41
REMARK 500 3 SER B 23 43.13 -165.02
REMARK 500 3 ASP B 33 66.69 -163.90
REMARK 500 4 THR A 14 -72.82 -60.04
REMARK 500 4 VAL A 15 38.71 -84.39
REMARK 500 4 LYS A 21 44.77 -83.42
REMARK 500 4 SER B 23 36.83 -168.38
REMARK 500 5 CYS A 12 -59.02 -29.97
REMARK 500 5 LYS A 36 108.99 -57.46
REMARK 500 5 SER B 23 45.86 -163.45
REMARK 500 5 ASP B 33 92.64 -167.00
REMARK 500 6 CYS A 12 -61.60 -29.14
REMARK 500 6 LYS B 19 47.80 -94.71
REMARK 500 6 GLU B 21 -176.73 -67.98
REMARK 500 6 CYS B 32 -177.74 -65.09
REMARK 500 7 CYS A 12 -64.35 -20.27
REMARK 500 7 LYS A 36 86.41 -69.24
REMARK 500 7 SER B 23 40.98 -151.71
REMARK 500 8 SER B 23 41.90 -164.76
REMARK 500 8 ASP B 33 76.27 -168.07
REMARK 500 9 CYS A 12 -64.96 -21.97
REMARK 500 9 SER B 23 41.67 -149.29
REMARK 500 10 SER B 23 38.86 -163.50
REMARK 500 11 CYS A 12 -64.31 -20.86
REMARK 500 11 SER B 2 -175.20 -69.47
REMARK 500 11 LYS B 19 59.07 -140.38
REMARK 500 11 SER B 23 40.88 -150.19
REMARK 500 12 LYS B 19 52.64 -113.10
REMARK 500 12 SER B 23 38.35 -83.72
REMARK 500 12 CYS B 32 -168.56 -67.07
REMARK 500 13 VAL A 15 36.14 -88.09
REMARK 500 13 LYS A 36 87.20 -69.96
REMARK 500 13 LYS B 19 60.05 -109.97
REMARK 500 13 SER B 23 40.72 -155.31
REMARK 500 14 SER B 23 34.18 -150.84
REMARK 500 15 CYS A 12 -62.30 -26.07
REMARK 500 15 GLU B 21 -173.01 -69.64
REMARK 500 15 SER B 23 42.50 -143.24
REMARK 500 16 LYS A 21 49.31 -85.94
REMARK 500 16 SER B 2 -174.95 -68.73
REMARK 500 16 SER B 23 40.52 -163.37
REMARK 500 17 LYS A 21 41.33 -81.57
REMARK 500 17 LYS B 19 31.05 -86.16
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ECI A 1 37 UNP P49343 ECAA_ECTTU 1 37
DBREF 1ECI B 1 34 UNP P49344 ECAB_ECTTU 1 34
SEQRES 1 A 37 GLY VAL ILE PRO LYS LYS ILE TRP GLU THR VAL CYS PRO
SEQRES 2 A 37 THR VAL GLU PRO TRP ALA LYS LYS CYS SER GLY ASP ILE
SEQRES 3 A 37 ALA THR TYR ILE LYS ARG GLU CYS GLY LYS LEU
SEQRES 1 B 34 TRP SER THR ILE VAL LYS LEU THR ILE CYS PRO THR LEU
SEQRES 2 B 34 LYS SER MET ALA LYS LYS CYS GLU GLY SER ILE ALA THR
SEQRES 3 B 34 MET ILE LYS LYS LYS CYS ASP LYS
HELIX 1 A1 LYS A 5 LYS A 20 1KINKS AT PRO 13 AND PRO 17 16
HELIX 2 A2 ASP A 25 GLY A 35 1 11
HELIX 3 B1 THR B 3 LYS B 18 1KINK AT PRO 11 16
HELIX 4 B2 SER B 23 CYS B 32 1 10
SSBOND 1 CYS A 12 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 22 CYS B 20 1555 1555 2.02
SSBOND 3 CYS B 10 CYS B 32 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 16 2 Bytes