Header list of 1bv2.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID BINDING PROTEIN 21-SEP-98 1BV2 TITLE LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: NONSPECIFIC LIPID TRANSFER PROTEIN; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA; SOURCE 3 ORGANISM_COMMON: RICE; SOURCE 4 ORGANISM_TAXID: 4530; SOURCE 5 ORGAN: SEEDS KEYWDS LIPID-BINDING PROTEIN, LIPID TRANSFER PROTEIN, RICE, MOLECULAR KEYWDS 2 MODELING, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 14 AUTHOR J.POZNANSKI,P.SODANO,S.W.SUH,J.Y.LEE,M.PTAK,F.VOVELLE REVDAT 3 16-FEB-22 1BV2 1 KEYWDS REMARK REVDAT 2 24-FEB-09 1BV2 1 VERSN REVDAT 1 18-MAY-99 1BV2 0 JRNL AUTH J.POZNANSKI,P.SODANO,S.W.SUH,J.Y.LEE,M.PTAK,F.VOVELLE JRNL TITL SOLUTION STRUCTURE OF A LIPID TRANSFER PROTEIN EXTRACTED JRNL TITL 2 FROM RICE SEEDS. COMPARISON WITH HOMOLOGOUS PROTEINS. JRNL REF EUR.J.BIOCHEM. V. 259 692 1999 JRNL REFN ISSN 0014-2956 JRNL PMID 10092854 JRNL DOI 10.1046/J.1432-1327.1999.00093.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BV2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000172105. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% H2O AND 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY TOCSY P-COSY 2Q-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX-500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY, DIANA, X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND REMARK 210 ANALYSIS OF THE RAMACHANDRAN REMARK 210 MAPS AND ENERGETIC CRITERIA REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES REMARK 500 3 ARG A 45 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES REMARK 500 4 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 6 CYS A 73 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 9 CYS A 13 CA - CB - SG ANGL. DEV. = 6.8 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 ALA A 55 28.42 -71.19 REMARK 500 1 LYS A 59 34.23 -97.41 REMARK 500 1 SER A 76 91.75 117.23 REMARK 500 1 ILE A 81 66.47 31.28 REMARK 500 1 ILE A 85 78.24 -18.66 REMARK 500 1 ASP A 86 37.68 -94.26 REMARK 500 1 CYS A 87 -126.65 28.70 REMARK 500 1 SER A 88 26.77 44.45 REMARK 500 2 THR A 2 -167.35 -114.17 REMARK 500 2 SER A 76 89.37 -31.89 REMARK 500 2 SER A 84 54.61 -110.79 REMARK 500 2 SER A 88 -54.00 93.40 REMARK 500 2 ARG A 89 59.89 -94.43 REMARK 500 3 ALA A 55 10.58 -56.86 REMARK 500 3 LYS A 59 82.85 -10.40 REMARK 500 3 VAL A 75 62.76 -116.74 REMARK 500 3 SER A 76 95.07 -33.98 REMARK 500 3 ILE A 81 52.70 32.04 REMARK 500 3 SER A 88 -42.39 122.99 REMARK 500 3 ARG A 89 44.16 -99.19 REMARK 500 4 ALA A 55 35.79 -74.58 REMARK 500 4 ILE A 58 55.74 -107.84 REMARK 500 4 LYS A 59 76.23 -20.81 REMARK 500 4 ASN A 65 -49.75 -131.23 REMARK 500 4 SER A 76 86.94 30.74 REMARK 500 4 TYR A 79 156.52 165.46 REMARK 500 4 SER A 84 50.52 -143.15 REMARK 500 4 ARG A 89 73.97 43.37 REMARK 500 4 VAL A 90 40.38 -80.73 REMARK 500 5 ALA A 55 -2.50 -57.21 REMARK 500 5 ARG A 56 57.28 -95.19 REMARK 500 5 ILE A 58 74.08 -108.31 REMARK 500 5 LYS A 59 60.93 11.65 REMARK 500 5 ASN A 65 -43.20 -131.43 REMARK 500 5 VAL A 75 63.18 -117.04 REMARK 500 5 SER A 76 87.38 -33.09 REMARK 500 5 THR A 80 -156.26 -145.95 REMARK 500 5 SER A 88 -37.28 114.55 REMARK 500 5 ARG A 89 47.05 -93.59 REMARK 500 5 VAL A 90 -59.91 -124.28 REMARK 500 6 VAL A 10 24.17 -79.53 REMARK 500 6 ALA A 38 46.37 -88.55 REMARK 500 6 ALA A 55 36.74 -78.97 REMARK 500 6 ILE A 58 54.07 -108.21 REMARK 500 6 LYS A 59 70.73 -8.77 REMARK 500 6 VAL A 75 68.70 -111.40 REMARK 500 6 SER A 76 96.14 -33.58 REMARK 500 6 ILE A 81 62.61 32.57 REMARK 500 6 ASP A 86 -80.39 -130.72 REMARK 500 6 CYS A 87 174.59 75.58 REMARK 500 REMARK 500 THIS ENTRY HAS 120 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 1 ARG A 18 0.31 SIDE CHAIN REMARK 500 1 ARG A 32 0.28 SIDE CHAIN REMARK 500 1 ARG A 44 0.31 SIDE CHAIN REMARK 500 1 ARG A 45 0.27 SIDE CHAIN REMARK 500 1 ARG A 56 0.29 SIDE CHAIN REMARK 500 1 ARG A 89 0.31 SIDE CHAIN REMARK 500 2 ARG A 18 0.31 SIDE CHAIN REMARK 500 2 ARG A 32 0.32 SIDE CHAIN REMARK 500 2 ARG A 44 0.31 SIDE CHAIN REMARK 500 2 ARG A 45 0.21 SIDE CHAIN REMARK 500 2 ARG A 56 0.27 SIDE CHAIN REMARK 500 2 ARG A 89 0.32 SIDE CHAIN REMARK 500 3 ARG A 18 0.24 SIDE CHAIN REMARK 500 3 ARG A 32 0.32 SIDE CHAIN REMARK 500 3 ARG A 44 0.28 SIDE CHAIN REMARK 500 3 ARG A 45 0.29 SIDE CHAIN REMARK 500 3 ARG A 56 0.30 SIDE CHAIN REMARK 500 3 ARG A 89 0.31 SIDE CHAIN REMARK 500 4 ARG A 18 0.29 SIDE CHAIN REMARK 500 4 ARG A 32 0.29 SIDE CHAIN REMARK 500 4 ARG A 44 0.31 SIDE CHAIN REMARK 500 4 ARG A 45 0.27 SIDE CHAIN REMARK 500 4 ARG A 56 0.29 SIDE CHAIN REMARK 500 4 ARG A 89 0.31 SIDE CHAIN REMARK 500 5 ARG A 18 0.26 SIDE CHAIN REMARK 500 5 ARG A 32 0.31 SIDE CHAIN REMARK 500 5 ARG A 44 0.29 SIDE CHAIN REMARK 500 5 ARG A 45 0.32 SIDE CHAIN REMARK 500 5 ARG A 56 0.30 SIDE CHAIN REMARK 500 5 ARG A 89 0.26 SIDE CHAIN REMARK 500 6 ARG A 18 0.28 SIDE CHAIN REMARK 500 6 ARG A 32 0.31 SIDE CHAIN REMARK 500 6 ARG A 44 0.27 SIDE CHAIN REMARK 500 6 ARG A 45 0.22 SIDE CHAIN REMARK 500 6 ARG A 56 0.32 SIDE CHAIN REMARK 500 6 ARG A 89 0.30 SIDE CHAIN REMARK 500 7 ARG A 18 0.31 SIDE CHAIN REMARK 500 7 ARG A 32 0.31 SIDE CHAIN REMARK 500 7 ARG A 44 0.26 SIDE CHAIN REMARK 500 7 ARG A 45 0.30 SIDE CHAIN REMARK 500 7 ARG A 56 0.27 SIDE CHAIN REMARK 500 7 ARG A 89 0.30 SIDE CHAIN REMARK 500 8 ARG A 18 0.21 SIDE CHAIN REMARK 500 8 ARG A 32 0.30 SIDE CHAIN REMARK 500 8 ARG A 44 0.30 SIDE CHAIN REMARK 500 8 ARG A 45 0.31 SIDE CHAIN REMARK 500 8 ARG A 56 0.17 SIDE CHAIN REMARK 500 8 ARG A 89 0.21 SIDE CHAIN REMARK 500 9 ARG A 18 0.28 SIDE CHAIN REMARK 500 9 ARG A 32 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 84 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BV2 A 1 91 UNP P23096 NLTP1_ORYSA 26 116 SEQADV 1BV2 LYS A 35 UNP P23096 PHE 60 SEE REMARK 999 SEQRES 1 A 91 ILE THR CYS GLY GLN VAL ASN SER ALA VAL GLY PRO CYS SEQRES 2 A 91 LEU THR TYR ALA ARG GLY GLY ALA GLY PRO SER ALA ALA SEQRES 3 A 91 CYS CYS SER GLY VAL ARG SER LEU LYS ALA ALA ALA SER SEQRES 4 A 91 THR THR ALA ASP ARG ARG THR ALA CYS ASN CYS LEU LYS SEQRES 5 A 91 ASN ALA ALA ARG GLY ILE LYS GLY LEU ASN ALA GLY ASN SEQRES 6 A 91 ALA ALA SER ILE PRO SER LYS CYS GLY VAL SER VAL PRO SEQRES 7 A 91 TYR THR ILE SER ALA SER ILE ASP CYS SER ARG VAL SER HELIX 1 H1 CYS A 3 ARG A 18 1BENT AT PRO 12 16 HELIX 2 H2 ALA A 25 ALA A 37 1 13 HELIX 3 H3 THR A 41 ALA A 54 1 14 HELIX 4 H4 ALA A 66 CYS A 73 1 8 SSBOND 1 CYS A 3 CYS A 50 1555 1555 2.02 SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.02 SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.02 SSBOND 4 CYS A 48 CYS A 87 1555 1555 2.02 CISPEP 1 GLY A 22 PRO A 23 1 8.00 CISPEP 2 GLY A 22 PRO A 23 2 7.43 CISPEP 3 GLY A 22 PRO A 23 3 -2.27 CISPEP 4 GLY A 22 PRO A 23 4 -7.77 CISPEP 5 GLY A 22 PRO A 23 5 -2.40 CISPEP 6 GLY A 22 PRO A 23 6 -3.15 CISPEP 7 GLY A 22 PRO A 23 7 -2.19 CISPEP 8 GLY A 22 PRO A 23 8 -1.39 CISPEP 9 GLY A 22 PRO A 23 9 -15.98 CISPEP 10 GLY A 22 PRO A 23 10 -1.38 CISPEP 11 GLY A 22 PRO A 23 11 -5.14 CISPEP 12 GLY A 22 PRO A 23 12 -14.38 CISPEP 13 GLY A 22 PRO A 23 13 -4.99 CISPEP 14 GLY A 22 PRO A 23 14 -2.10 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 - b 16 2 Bytes