Header list of 1l6h.pdb file
Complete list - 23 202 Bytes
HEADER LIPID TRANSPORT 11-MAR-02 1L6H
TITLE SOLUTION STRUCTURE OF PLANT NSLTP2 PURIFIED FROM RICE (ORYZA SATIVA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-SPECIFIC LIPID TRANSFER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LTP2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 4530
KEYWDS NSLTP2, PLANT LTP, LIPID TRANSFER, LIPID TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR D.SAMUEL,P.-C.LYU
REVDAT 5 23-FEB-22 1L6H 1 REMARK
REVDAT 4 24-FEB-09 1L6H 1 VERSN
REVDAT 3 01-APR-03 1L6H 1 JRNL
REVDAT 2 04-FEB-03 1L6H 1 REMARK
REVDAT 1 02-OCT-02 1L6H 0
JRNL AUTH D.SAMUEL,Y.J.LIU,C.S.CHENG,P.C.LYU
JRNL TITL SOLUTION STRUCTURE OF PLANT NONSPECIFIC LIPID TRANSFER
JRNL TITL 2 PROTEIN-2 FROM RICE (ORYZA SATIVA).
JRNL REF J.BIOL.CHEM. V. 277 35267 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12011089
JRNL DOI 10.1074/JBC.M203113200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.-J.LIU,D.SAMUEL,C.-H.LIN,P.-C.LYU
REMARK 1 TITL PURIFICATION AND CHARACTERIZATION OF A NOVEL 7-KDA
REMARK 1 TITL 2 NON-SPECIFIC LIPID TRANSFER PROTEIN-2 FROM RICE (ORYZA
REMARK 1 TITL 3 SATIVA)
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 294 535 2002
REMARK 1 REFN ISSN 0006-291X
REMARK 1 DOI 10.1016/S0006-291X(02)00509-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUGNER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS BASED ON A TOTAL OF
REMARK 3 862 DISTANCE CONSTRAINTS, 813 ARE NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINS, 30 DIESTANCE RESTRAINTS FROM HYDROGEN BONDS, 19
REMARK 3 DIHEDRAL ANGLE RESTRAINS.
REMARK 4
REMARK 4 1L6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015685.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, X-PLOR 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 CYS A 11 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 ALA A 40 CB - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 CYS A 61 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 CYS A 68 CA - CB - SG ANGL. DEV. = 15.4 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 CYS A 3 35.73 -163.55
REMARK 500 THR A 9 -37.90 -36.42
REMARK 500 CYS A 11 14.04 -67.26
REMARK 500 ALA A 19 94.35 -63.01
REMARK 500 ARG A 44 -3.09 -145.01
REMARK 500 TYR A 48 -75.93 -86.66
REMARK 500 SER A 51 -82.36 -147.50
REMARK 500 ASN A 53 -33.43 -135.15
REMARK 500 ALA A 57 70.28 -159.86
REMARK 500 SER A 59 -112.44 112.04
REMARK 500 SER A 60 55.66 99.27
REMARK 500 ALA A 64 -24.02 143.56
REMARK 500 LEU A 65 67.46 76.66
REMARK 500 PRO A 66 29.87 -68.27
REMARK 500 CYS A 68 41.68 -85.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 50 SER A 51 128.89
REMARK 500 SER A 51 PRO A 52 -136.39
REMARK 500 SER A 59 SER A 60 -136.52
REMARK 500 ILE A 63 ALA A 64 122.14
REMARK 500 ALA A 64 LEU A 65 -147.28
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 PHE A 39 0.08 SIDE CHAIN
REMARK 500 TYR A 45 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1L6H A 1 69 UNP P83210 NLTPX_ORYSA 1 69
SEQRES 1 A 69 ALA GLY CYS ASN ALA GLY GLN LEU THR VAL CYS THR GLY
SEQRES 2 A 69 ALA ILE ALA GLY GLY ALA ARG PRO THR ALA ALA CYS CYS
SEQRES 3 A 69 SER SER LEU ARG ALA GLN GLN GLY CYS PHE CYS GLN PHE
SEQRES 4 A 69 ALA LYS ASP PRO ARG TYR GLY ARG TYR VAL ASN SER PRO
SEQRES 5 A 69 ASN ALA ARG LYS ALA VAL SER SER CYS GLY ILE ALA LEU
SEQRES 6 A 69 PRO THR CYS HIS
HELIX 1 1 GLN A 7 ALA A 16 1 10
HELIX 2 2 THR A 22 ALA A 40 1 19
HELIX 3 3 ARG A 44 VAL A 49 1 6
HELIX 4 4 ASN A 53 ALA A 57 5 5
SSBOND 1 CYS A 3 CYS A 35 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 25 1555 1555 2.04
SSBOND 3 CYS A 26 CYS A 61 1555 1555 2.04
SSBOND 4 CYS A 37 CYS A 68 1555 1555 2.05
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
Complete list - 23 202 Bytes