Header list of 1yz2.pdb file
Complete list - 6 20 Bytes
HEADER TOXIN 26-FEB-05 1YZ2
TITLE SOLUTION STRUCTURE OF AM2766
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-CONOTOXIN AM 2766;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS AMADIS;
SOURCE 3 ORGANISM_TAXID: 198732;
SOURCE 4 SECRETION: VENOM
KEYWDS DELTA CONOTOXIN, MOLLUSCIVOROUS SNAIL, INHIBITORY CYSTEINE KNOT
KEYWDS 2 MOTIF, 15 STRUCTURES, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.P.SARMA,G.S.KUMAR,S.SUDARSLAL,P.IENGAR,S.K.SIKDAR,K.S.KRISHNAN,
AUTHOR 2 P.BALARAM
REVDAT 3 06-NOV-19 1YZ2 1 REMARK SEQADV SSBOND LINK
REVDAT 3 2 1 SITE
REVDAT 2 24-FEB-09 1YZ2 1 VERSN
REVDAT 1 07-FEB-06 1YZ2 0
JRNL AUTH S.P.SARMA,G.S.KUMAR,S.SUDARSLAL,P.IENGAR,P.RAMASAMY,
JRNL AUTH 2 S.K.SIKDAR,K.S.KRISHNAN,P.BALARAM
JRNL TITL SOLUTION STRUCTURE OF DELTA-AM2766: A HIGHLY HYDROPHOBIC
JRNL TITL 2 DELTA-CONOTOXIN FROM CONUS AMADIS THAT INHIBITS INACTIVATION
JRNL TITL 3 OF NEURONAL VOLTAGE-GATED SODIUM CHANNELS
JRNL REF CHEM.BIODIVERS. V. 2 535 2005
JRNL REFN ISSN 1612-1872
JRNL DOI 10.1002/CBDV.200590035
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1A, X-PLOR-NIH 2.9.1
REMARK 3 AUTHORS : VARIAN (VNMR), SCHWIETERS (X-PLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YZ2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032091.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2-3MM DELTA AM2766; 2-3MM DELTA
REMARK 210 AM2766
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; 2D TOCSY; 2D
REMARK 210 ROESY; 2D 1H-13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE VERSION
REMARK 210 2.3, ANSIG 3.3, X-PLOR-NIH 2.9.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
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 HG2 GLU A 26 HN1 NH2 A 27 0.54
REMARK 500 HZ1 LYS A 2 OD1 ASN A 14 1.35
REMARK 500 HZ2 LYS A 2 OE1 GLU A 6 1.50
REMARK 500 CG GLU A 26 HN1 NH2 A 27 1.53
REMARK 500 HG2 GLU A 26 N NH2 A 27 1.54
REMARK 500 O ILE A 10 HE21 GLN A 13 1.56
REMARK 500 OD2 ASP A 9 HG SER A 12 1.57
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 21 -59.38 -25.40
REMARK 500 1 ILE A 23 146.17 -170.36
REMARK 500 2 ILE A 10 -70.21 -83.84
REMARK 500 2 VAL A 17 48.84 -141.42
REMARK 500 2 ALA A 21 -63.29 -19.19
REMARK 500 3 SER A 7 144.61 -173.15
REMARK 500 3 VAL A 17 50.85 -141.57
REMARK 500 3 ALA A 21 -62.27 -21.42
REMARK 500 3 ILE A 23 147.80 -170.86
REMARK 500 4 LYS A 2 -173.80 -174.95
REMARK 500 4 CYS A 8 156.25 176.85
REMARK 500 4 ALA A 21 -58.10 -24.37
REMARK 500 5 SER A 7 149.91 176.16
REMARK 500 5 CYS A 20 27.06 -150.45
REMARK 500 5 ALA A 21 -58.33 -25.36
REMARK 500 5 PHE A 22 17.22 -140.28
REMARK 500 5 ILE A 23 149.38 -175.00
REMARK 500 6 SER A 7 157.22 178.39
REMARK 500 6 CYS A 8 143.61 -179.28
REMARK 500 6 VAL A 17 51.95 -140.87
REMARK 500 6 CYS A 20 28.36 -140.56
REMARK 500 6 ALA A 21 -60.18 -23.60
REMARK 500 7 CYS A 8 138.61 -178.44
REMARK 500 7 ALA A 21 -61.77 -21.25
REMARK 500 8 VAL A 17 52.17 -141.34
REMARK 500 8 ALA A 21 -59.80 -22.83
REMARK 500 8 PHE A 22 14.95 -140.61
REMARK 500 8 ILE A 23 140.70 -170.57
REMARK 500 9 GLU A 6 -74.55 -67.16
REMARK 500 9 CYS A 8 153.22 179.73
REMARK 500 9 ALA A 21 -63.32 -20.02
REMARK 500 10 CYS A 8 148.35 -170.19
REMARK 500 10 ILE A 10 -71.86 -78.12
REMARK 500 10 CYS A 20 24.61 -142.73
REMARK 500 10 ALA A 21 -58.15 -25.39
REMARK 500 10 ILE A 23 147.68 -173.77
REMARK 500 11 CYS A 8 145.80 -178.62
REMARK 500 11 ILE A 10 -70.03 -81.22
REMARK 500 11 VAL A 17 47.49 -144.27
REMARK 500 11 CYS A 20 25.26 -147.30
REMARK 500 11 ALA A 21 -59.86 -26.71
REMARK 500 11 ILE A 23 144.27 -171.55
REMARK 500 11 ILE A 25 58.58 -114.01
REMARK 500 12 CYS A 8 148.09 -173.74
REMARK 500 12 CYS A 20 19.17 -142.30
REMARK 500 12 ALA A 21 -60.58 -24.13
REMARK 500 12 ILE A 23 149.59 -173.39
REMARK 500 13 SER A 7 146.10 -171.90
REMARK 500 13 VAL A 17 49.16 -156.25
REMARK 500 13 ALA A 21 -63.53 -20.08
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YZ2 A 1 26 UNP P60179 CXD6_CONAA 1 26
SEQADV 1YZ2 NH2 A 27 UNP P60179 AMIDATION
SEQRES 1 A 27 CYS LYS GLN ALA GLY GLU SER CYS ASP ILE PHE SER GLN
SEQRES 2 A 27 ASN CYS CYS VAL GLY THR CYS ALA PHE ILE CYS ILE GLU
SEQRES 3 A 27 NH2
HET NH2 A 27 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.01
SSBOND 3 CYS A 15 CYS A 24 1555 1555 2.02
LINK C GLU A 26 N NH2 A 27 1555 1555 1.38
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 - 6 20 Bytes