Header list of 1siy.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 02-MAR-04 1SIY
TITLE NMR STRUCTURE OF MUNG BEAN NON-SPECIFIC LIPID TRANSFER PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSPECIFIC LIPID-TRANSFER PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LTP 1, NS-LTP1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIGNA RADIATA VAR. RADIATA;
SOURCE 3 ORGANISM_COMMON: MUNG BEAN;
SOURCE 4 ORGANISM_TAXID: 3916;
SOURCE 5 STRAIN: VAR. RADIATA
KEYWDS ALPHA HELIX, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.F.LIN,Y.N.LIU,S.T.D.HSU,D.SAMUEL,C.S.CHENG,A.M.J.J.BONVIN,P.C.LYU
REVDAT 6 02-MAR-22 1SIY 1 REMARK
REVDAT 5 21-APR-09 1SIY 1 REMARK REVDAT
REVDAT 4 24-FEB-09 1SIY 1 VERSN
REVDAT 3 19-APR-05 1SIY 1 JRNL
REVDAT 2 12-APR-05 1SIY 1 DBREF
REVDAT 1 05-APR-05 1SIY 0
JRNL AUTH K.F.LIN,Y.N.LIU,S.T.D.HSU,D.SAMUEL,C.S.CHENG,A.M.J.J.BONVIN,
JRNL AUTH 2 P.C.LYU
JRNL TITL CHARACTERIZATION AND STRUCTURAL ANALYSES OF NONSPECIFIC
JRNL TITL 2 LIPID TRANSFER PROTEIN 1 FROM MUNG BEAN
JRNL REF BIOCHEMISTRY V. 44 5703 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15823028
JRNL DOI 10.1021/BI047608V
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, ARIA 2.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE CALCULATED FROM 1675
REMARK 3 ASSIGNED NOE. 4 DISULFIDE BONDS ARE SHOWN
REMARK 4
REMARK 4 1SIY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021743.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 20MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM LTP1; 20MM PHOSPHATE BUFFER
REMARK 210 NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D 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 : X-PLOR 3.8, ARIA 2.0, SPARKY 3.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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 PHE A 16 -43.91 -146.71
REMARK 500 1 PRO A 25 4.95 -69.30
REMARK 500 1 ARG A 39 -58.41 79.47
REMARK 500 1 VAL A 58 98.64 -56.30
REMARK 500 1 ASN A 86 109.02 65.45
REMARK 500 2 CYS A 3 -24.06 73.33
REMARK 500 2 GLN A 18 -76.85 -70.32
REMARK 500 2 LYS A 19 84.09 -150.81
REMARK 500 2 ASN A 62 116.41 65.15
REMARK 500 2 ASN A 76 71.02 48.51
REMARK 500 2 SER A 89 -78.32 -118.09
REMARK 500 2 ILE A 90 -135.31 36.71
REMARK 500 3 CYS A 3 -23.65 71.35
REMARK 500 3 LEU A 35 -72.76 -81.40
REMARK 500 3 ARG A 39 -64.99 88.54
REMARK 500 3 ASN A 76 95.26 50.74
REMARK 500 3 PRO A 78 -159.16 -73.21
REMARK 500 3 TYR A 79 -164.94 47.91
REMARK 500 3 SER A 89 -73.50 -117.62
REMARK 500 3 ILE A 90 -119.37 35.25
REMARK 500 4 CYS A 3 3.53 -69.31
REMARK 500 4 PHE A 16 -42.70 -157.65
REMARK 500 4 LYS A 19 -79.02 -84.43
REMARK 500 4 ASN A 36 -47.75 -139.36
REMARK 500 4 SER A 38 96.87 -61.88
REMARK 500 4 ARG A 39 -71.27 -55.20
REMARK 500 4 ARG A 45 32.20 -79.91
REMARK 500 4 ALA A 46 -43.87 -137.03
REMARK 500 4 ASN A 62 98.62 40.38
REMARK 500 4 VAL A 75 72.29 -112.52
REMARK 500 5 ASN A 36 -54.43 -167.95
REMARK 500 5 ARG A 39 -80.35 -77.56
REMARK 500 5 ARG A 44 -47.38 -131.27
REMARK 500 5 VAL A 75 -56.82 -123.18
REMARK 500 5 ASN A 76 111.56 65.04
REMARK 500 5 ASN A 86 43.08 -77.13
REMARK 500 5 SER A 89 -75.15 -122.10
REMARK 500 5 ILE A 90 -134.45 35.44
REMARK 500 6 CYS A 3 7.90 -68.71
REMARK 500 6 VAL A 22 126.25 62.82
REMARK 500 6 LEU A 35 -62.63 -93.46
REMARK 500 6 ASN A 62 97.48 55.76
REMARK 500 6 SER A 89 -89.18 -134.22
REMARK 500 6 ILE A 90 -159.08 39.37
REMARK 500 7 LEU A 35 -70.97 -92.52
REMARK 500 7 THR A 40 -173.83 -174.76
REMARK 500 7 ILE A 61 -81.62 -89.14
REMARK 500 7 ASN A 62 106.21 99.30
REMARK 500 7 VAL A 75 -88.69 -123.89
REMARK 500 7 ASN A 76 134.45 68.80
REMARK 500
REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6089 RELATED DB: BMRB
REMARK 900 RELEASED CHEMICAL SHIFT OF THE SAME PROTEIN
DBREF 1SIY A 1 91 UNP P83434 NLTP1_PHAAU 1 91
SEQRES 1 A 91 MET THR CYS GLY GLN VAL GLN GLY ASN LEU ALA GLN CYS
SEQRES 2 A 91 ILE GLY PHE LEU GLN LYS GLY GLY VAL VAL PRO PRO SER
SEQRES 3 A 91 CYS CYS THR GLY VAL LYS ASN ILE LEU ASN SER SER ARG
SEQRES 4 A 91 THR THR ALA ASP ARG ARG ALA VAL CYS SER CYS LEU LYS
SEQRES 5 A 91 ALA ALA ALA GLY ALA VAL ARG GLY ILE ASN PRO ASN ASN
SEQRES 6 A 91 ALA GLU ALA LEU PRO GLY LYS CYS GLY VAL ASN ILE PRO
SEQRES 7 A 91 TYR LYS ILE SER THR SER THR ASN CYS ASN SER ILE ASN
HELIX 1 1 VAL A 6 GLN A 18 1 13
HELIX 2 2 PRO A 24 ASN A 36 1 13
HELIX 3 3 THR A 41 ALA A 55 1 15
HELIX 4 4 ASN A 62 GLY A 74 1 13
SSBOND 1 CYS A 3 CYS A 50 1555 1555 2.03
SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.04
SSBOND 4 CYS A 48 CYS A 87 1555 1555 2.03
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 - r 2 2 Bytes