Header list of 1p8b.pdb file
Complete list - 3 20 Bytes
HEADER PLANT PROTEIN 06-MAY-03 1P8B
TITLE SOLUTION STRUCTURE OF PA1B, A 37-AMINO ACID INSECTICIDAL PROTEIN
TITLE 2 EXTRACTED FROM PEA SEEDS (PISUM SATIVUM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEA ALBUMIN 1, SUBUNIT B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PA1B, ALBUMIN A1B, LEGINSULIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;
SOURCE 3 ORGANISM_COMMON: PEA;
SOURCE 4 ORGANISM_TAXID: 3888;
SOURCE 5 STRAIN: CV. FRILENE;
SOURCE 6 OTHER_DETAILS: ISOLATED FROM PEA SEEDS
KEYWDS INHIBITOR CYSTINE-KNOT, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR L.JOUVENSAL,L.QUILLIEN,E.FERRASSON,Y.RAHBE,J.GUEGUEN,F.VOVELLE
REVDAT 4 03-FEB-21 1P8B 1 JRNL REMARK
REVDAT 3 24-FEB-09 1P8B 1 VERSN
REVDAT 2 02-DEC-03 1P8B 1 JRNL
REVDAT 1 25-NOV-03 1P8B 0
JRNL AUTH L.JOUVENSAL,L.QUILLIEN,E.FERRASSON,Y.RAHBE,J.GUEGUEN,
JRNL AUTH 2 F.VOVELLE
JRNL TITL PA1B, AN INSECTICIDAL PROTEIN EXTRACTED FROM PEA SEEDS
JRNL TITL 2 (PISUM SATIVUM): 1H-2-D NMR STUDY AND MOLECULAR MODELING
JRNL REF BIOCHEMISTRY V. 42 11915 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14556622
JRNL DOI 10.1021/BI034803L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.GRESSENT,I.RAHIOUI,Y.RAHBE
REMARK 1 TITL CHARACTERIZATION OF A HIGH AFFINITY BINDING SITE FOR THE PEA
REMARK 1 TITL 2 ALBUMIN 1B ENTOMOTOXIN IN THE WEEVIL SITOPHILUS
REMARK 1 REF EUR.J.BIOCHEM. V. 270 2429 2003
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1033.2003.03611.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.DELOBEL,A.M.GRENIER,J.GUEGUEN,E.FERRASSON,M.MBAIGUINAM
REMARK 1 TITL USE OF A POLYPEPTIDE DERIVED FROM A PA1B LEGUME ALBUMEN AS
REMARK 1 TITL 2 INSECTICIDE
REMARK 1 REF PATENT 1999
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, ARIA 1.1
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 858 NOE-DERIVED DISTANCE RESTRAINTS,
REMARK 3 15 DIHEDRAL ANGLE RESTRAINTS
REMARK 3 AND 7 HYDROGEN BOND RESTRAINTS
REMARK 4
REMARK 4 1P8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019133.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.1MM PA1B; 0.02% NAN3; 50% H2O,
REMARK 210 50% TFE-D2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 6001, CNS 1.1, ARIA 1.1
REMARK 210 METHOD USED : TORSION ANGLE SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS IN
REMARK 210 EXPLICIT SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 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: 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 ASN A 4 134.36 -173.47
REMARK 500 1 VAL A 25 44.79 -84.34
REMARK 500 1 PRO A 35 32.58 -76.19
REMARK 500 2 ASN A 4 132.02 -170.31
REMARK 500 2 VAL A 25 39.24 -86.88
REMARK 500 2 PRO A 35 30.96 -70.41
REMARK 500 3 PRO A 14 -74.04 -58.00
REMARK 500 3 VAL A 25 36.74 -83.77
REMARK 500 3 SER A 36 -41.94 -151.06
REMARK 500 4 ASN A 4 134.32 -173.26
REMARK 500 5 ASN A 4 126.86 -174.61
REMARK 500 5 THR A 17 139.38 -179.95
REMARK 500 5 VAL A 25 38.32 -85.07
REMARK 500 5 PRO A 35 33.51 -75.65
REMARK 500 6 CYS A 7 -155.85 -140.36
REMARK 500 6 CYS A 15 -39.03 78.32
REMARK 500 6 VAL A 25 36.29 -84.71
REMARK 500 6 PRO A 35 23.64 -67.57
REMARK 500 7 SER A 2 73.92 -67.80
REMARK 500 7 SER A 18 -42.42 72.83
REMARK 500 7 PRO A 35 37.80 -81.14
REMARK 500 8 VAL A 25 32.53 -81.57
REMARK 500 8 SER A 36 49.01 -151.85
REMARK 500 9 ASN A 4 117.76 179.69
REMARK 500 9 VAL A 25 36.68 -85.72
REMARK 500 9 SER A 36 -69.61 -92.39
REMARK 500 10 SER A 2 58.36 -158.84
REMARK 500 10 PRO A 14 -80.99 -50.98
REMARK 500 10 VAL A 25 36.61 -80.92
REMARK 500 11 THR A 17 -39.77 -143.84
REMARK 500 11 SER A 18 -39.14 72.03
REMARK 500 12 PRO A 35 30.29 -68.16
REMARK 500 13 ASN A 4 135.85 -171.64
REMARK 500 13 CYS A 15 13.19 59.35
REMARK 500 13 THR A 17 -31.06 -141.89
REMARK 500 13 SER A 18 -41.03 70.07
REMARK 500 13 VAL A 25 38.10 -82.59
REMARK 500 13 PRO A 35 1.98 -68.31
REMARK 500 14 ASN A 4 148.79 -173.77
REMARK 500 14 THR A 17 140.84 -172.05
REMARK 500 15 ASN A 4 38.96 -175.53
REMARK 500 15 PRO A 35 41.90 -73.23
REMARK 500 15 SER A 36 27.72 -150.79
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P8B A 1 37 UNP P62927 ALB1B_PEA 27 63
SEQADV 1P8B ILE A 29 UNP P62927 VAL 55 SEE REMARK 999
SEQRES 1 A 37 ALA SER CYS ASN GLY VAL CYS SER PRO PHE GLU MET PRO
SEQRES 2 A 37 PRO CYS GLY THR SER ALA CYS ARG CYS ILE PRO VAL GLY
SEQRES 3 A 37 LEU VAL ILE GLY TYR CYS ARG ASN PRO SER GLY
HELIX 1 1 PRO A 13 THR A 17 5 5
SHEET 1 A 3 ASN A 4 CYS A 7 0
SHEET 2 A 3 GLY A 30 ARG A 33 -1 O GLY A 30 N CYS A 7
SHEET 3 A 3 ARG A 21 ILE A 23 -1 N ILE A 23 O TYR A 31
SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.02
SSBOND 2 CYS A 7 CYS A 22 1555 1555 2.03
SSBOND 3 CYS A 15 CYS A 32 1555 1555 2.03
CISPEP 1 MET A 12 PRO A 13 1 -0.23
CISPEP 2 MET A 12 PRO A 13 2 -0.34
CISPEP 3 MET A 12 PRO A 13 3 -0.39
CISPEP 4 MET A 12 PRO A 13 4 -0.22
CISPEP 5 MET A 12 PRO A 13 5 -0.31
CISPEP 6 MET A 12 PRO A 13 6 -0.39
CISPEP 7 MET A 12 PRO A 13 7 -0.14
CISPEP 8 MET A 12 PRO A 13 8 -0.18
CISPEP 9 MET A 12 PRO A 13 9 -0.23
CISPEP 10 MET A 12 PRO A 13 10 -0.28
CISPEP 11 MET A 12 PRO A 13 11 -0.37
CISPEP 12 MET A 12 PRO A 13 12 -0.28
CISPEP 13 MET A 12 PRO A 13 13 0.08
CISPEP 14 MET A 12 PRO A 13 14 -0.16
CISPEP 15 MET A 12 PRO A 13 15 -0.20
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 - 3 20 Bytes