Header list of 1t12.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID TRANSPORT 15-APR-04 1T12
TITLE SOLUTION STRUCTURE OF A NEW LTP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSPECIFIC LIPID-TRANSFER PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 24-114;
COMPND 5 SYNONYM: LTP 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA TABACUM;
SOURCE 3 ORGANISM_COMMON: COMMON TOBACCO;
SOURCE 4 ORGANISM_TAXID: 4097;
SOURCE 5 GENE: LTP1;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS CYSTEIN RICH PROTEIN; LIPID TRANSFER PROTEIN, LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.DA SILVA,C.LANDON,B.INDUSTRI,M.PONCHET,F.VOVELLE
REVDAT 3 02-MAR-22 1T12 1 REMARK
REVDAT 2 24-FEB-09 1T12 1 VERSN
REVDAT 1 05-APR-05 1T12 0
JRNL AUTH P.DA SILVA,C.LANDON,B.INDUSTRI,A.MARAIS,D.MARION,M.PONCHET,
JRNL AUTH 2 F.VOVELLE
JRNL TITL SOLUTION STRUCTURE OF A TOBACCO LIPID TRANSFER PROTEIN
JRNL TITL 2 EXHIBITING NEW BIOPHYSICAL AND BIOLOGICAL FEATURES
JRNL REF PROTEINS V. 59 356 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15726627
JRNL DOI 10.1002/PROT.20405
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRDRAW, ARIA
REMARK 3 AUTHORS : DELAGLIO (NMRDRAW), BRUNGER, LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON A TOTAL OF
REMARK 3 1526 RESTRAINTS AND 47 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1T12 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022179.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8MM TOBACCO LTP1 15N, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY; HNHA
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 : NMRVIEW, ARIA
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 RESTRAINT ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR AND 3D
REMARK 210 HETERONUCLEAR NMR TECHNIQUES AND MOLECULAR MODELLING
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: 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 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 4 ARG A 44 CG - CD - NE ANGL. DEV. = 13.2 DEGREES
REMARK 500 4 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 5 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 6 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.6 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 1 THR A 21 -51.18 -140.90
REMARK 500 1 SER A 37 33.63 -84.31
REMARK 500 1 ALA A 38 33.16 -145.13
REMARK 500 1 THR A 40 47.31 -77.85
REMARK 500 1 THR A 41 -62.30 62.84
REMARK 500 1 SER A 59 -74.55 -74.79
REMARK 500 1 SER A 84 -58.65 -159.28
REMARK 500 2 THR A 21 -47.51 -140.78
REMARK 500 2 SER A 37 50.18 -105.15
REMARK 500 2 ALA A 38 38.82 -151.92
REMARK 500 2 THR A 40 45.31 -107.58
REMARK 500 2 THR A 41 -68.34 66.80
REMARK 500 2 ALA A 57 -49.52 179.80
REMARK 500 2 VAL A 75 -159.12 -105.42
REMARK 500 2 ASN A 76 67.10 -112.35
REMARK 500 2 SER A 84 -53.43 -165.42
REMARK 500 2 THR A 85 105.36 -37.52
REMARK 500 3 ILE A 2 150.71 -39.60
REMARK 500 3 ASN A 20 59.15 83.31
REMARK 500 3 THR A 21 -67.90 -148.34
REMARK 500 3 PRO A 23 -168.57 -71.74
REMARK 500 3 ALA A 38 -57.40 -154.93
REMARK 500 3 ARG A 39 66.69 -66.94
REMARK 500 3 THR A 40 40.99 -140.32
REMARK 500 3 THR A 41 -66.26 62.99
REMARK 500 3 ALA A 57 -53.85 -172.52
REMARK 500 3 SER A 84 -53.71 -170.76
REMARK 500 3 THR A 85 116.80 -37.19
REMARK 500 3 CYS A 87 39.75 -143.18
REMARK 500 3 LYS A 89 55.30 -152.05
REMARK 500 4 ASN A 20 29.70 39.82
REMARK 500 4 ALA A 38 -54.13 -172.24
REMARK 500 4 THR A 40 39.87 -147.08
REMARK 500 4 THR A 41 -75.01 52.98
REMARK 500 4 TYR A 79 146.48 -179.38
REMARK 500 4 LYS A 80 50.27 -112.17
REMARK 500 4 ILE A 81 59.55 29.75
REMARK 500 4 PRO A 83 11.97 -65.02
REMARK 500 4 SER A 84 26.91 -140.95
REMARK 500 5 THR A 21 -49.98 -159.87
REMARK 500 5 ARG A 26 31.24 -91.25
REMARK 500 5 SER A 37 47.94 -91.47
REMARK 500 5 ALA A 38 48.44 -158.89
REMARK 500 5 ARG A 39 -41.36 -148.85
REMARK 500 5 THR A 40 46.31 -59.81
REMARK 500 5 THR A 41 -57.34 67.46
REMARK 500 5 SER A 84 -53.14 -177.84
REMARK 500 6 ILE A 2 150.94 -48.28
REMARK 500 6 THR A 21 -46.89 -160.19
REMARK 500 6 SER A 37 38.68 -92.74
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
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 4 TYR A 17 0.08 SIDE CHAIN
REMARK 500 4 TYR A 79 0.08 SIDE CHAIN
REMARK 500 5 TYR A 17 0.07 SIDE CHAIN
REMARK 500 8 TYR A 17 0.09 SIDE CHAIN
REMARK 500 9 TYR A 17 0.07 SIDE CHAIN
REMARK 500 9 TYR A 79 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GH1 RELATED DB: PDB
DBREF 1T12 A 1 91 UNP Q42952 NLTP1_TOBAC 24 114
SEQRES 1 A 91 ALA ILE THR CYS GLY GLN VAL THR SER ASN LEU ALA PRO
SEQRES 2 A 91 CYS LEU ALA TYR LEU ARG ASN THR GLY PRO LEU GLY ARG
SEQRES 3 A 91 CYS CYS GLY GLY VAL LYS ALA LEU VAL ASN SER ALA ARG
SEQRES 4 A 91 THR THR GLU ASP ARG GLN ILE ALA CYS THR CYS LEU LYS
SEQRES 5 A 91 SER ALA ALA GLY ALA ILE SER GLY ILE ASN LEU GLY LYS
SEQRES 6 A 91 ALA ALA GLY LEU PRO SER THR CYS GLY VAL ASN ILE PRO
SEQRES 7 A 91 TYR LYS ILE SER PRO SER THR ASP CYS SER LYS VAL GLN
HELIX 1 1 THR A 3 LEU A 11 1 9
HELIX 2 2 LEU A 11 ARG A 19 1 9
HELIX 3 3 ARG A 26 SER A 37 1 12
HELIX 4 4 THR A 41 ILE A 58 1 18
HELIX 5 5 ASN A 62 CYS A 73 1 12
SSBOND 1 CYS A 4 CYS A 50 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.03
SSBOND 4 CYS A 48 CYS A 87 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
MODEL 1
Complete list - r 2 2 Bytes