Header list of 1bo9.pdb file
Complete list - b 16 2 Bytes
HEADER METAL TRANSPORT 10-AUG-98 1BO9
TITLE NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ANNEXIN I);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN 1;
COMPND 5 SYNONYM: LIPOCORTIN I, CALPACTIN II, CHROMOBINDIN 9, P35,
COMPND 6 PHOSPHOLIPASE A2 INHIBITORY PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-17
KEYWDS DOMAIN 1, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR J.GAO,H.YAN LI
REVDAT 4 16-FEB-22 1BO9 1 REMARK
REVDAT 3 24-FEB-09 1BO9 1 VERSN
REVDAT 2 22-DEC-99 1BO9 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 19-AUG-98 1BO9 0
JRNL AUTH J.GAO,Y.LI,H.YAN
JRNL TITL NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I SHOWS
JRNL TITL 2 AN AUTONOMOUS FOLDING UNIT.
JRNL REF J.BIOL.CHEM. V. 274 2971 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 9915835
JRNL DOI 10.1074/JBC.274.5.2971
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: DG/SA
REMARK 4
REMARK 4 1BO9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008122.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C,
REMARK 210 15N-LABELED PROTEIN.
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 PHE A 2 113.74 59.00
REMARK 500 1 SER A 5 -56.30 168.31
REMARK 500 1 VAL A 20 131.08 61.78
REMARK 500 1 ALA A 23 29.30 -165.88
REMARK 500 1 THR A 24 -47.57 -142.69
REMARK 500 1 ASN A 33 -164.51 -66.10
REMARK 500 1 GLU A 47 -80.57 -94.35
REMARK 500 1 VAL A 68 -47.04 -136.55
REMARK 500 1 LEU A 71 36.41 -97.58
REMARK 500 1 LEU A 72 33.61 -145.92
REMARK 500 2 ASN A 3 106.18 -168.18
REMARK 500 2 SER A 5 -57.66 -179.23
REMARK 500 2 VAL A 20 115.51 58.82
REMARK 500 2 ALA A 23 30.90 -167.48
REMARK 500 2 THR A 24 -47.47 -143.19
REMARK 500 2 ASN A 33 -178.37 -53.71
REMARK 500 2 GLU A 47 -79.02 -62.77
REMARK 500 3 SER A 5 -59.42 177.62
REMARK 500 3 MET A 16 34.42 -92.12
REMARK 500 3 VAL A 20 121.23 63.52
REMARK 500 3 ALA A 23 27.45 -161.32
REMARK 500 3 THR A 24 -47.81 -139.17
REMARK 500 3 GLU A 47 -79.18 -94.97
REMARK 500 3 LEU A 71 43.71 -94.35
REMARK 500 3 LEU A 72 26.93 -145.48
REMARK 500 4 PHE A 2 160.65 -49.13
REMARK 500 4 ASN A 3 93.37 -168.35
REMARK 500 4 SER A 5 -58.55 168.67
REMARK 500 4 MET A 16 47.21 -91.29
REMARK 500 4 VAL A 20 109.98 82.41
REMARK 500 4 ASP A 21 93.54 -62.07
REMARK 500 4 ALA A 23 19.35 -144.90
REMARK 500 4 THR A 24 -45.70 -139.54
REMARK 500 4 ASN A 33 -167.88 -59.23
REMARK 500 4 GLU A 47 -80.81 -85.58
REMARK 500 5 PHE A 2 108.88 58.51
REMARK 500 5 PRO A 4 48.82 -83.06
REMARK 500 5 SER A 5 -36.89 178.04
REMARK 500 5 VAL A 17 -72.37 -57.61
REMARK 500 5 LYS A 18 39.08 -161.33
REMARK 500 5 ALA A 23 31.09 -167.84
REMARK 500 5 THR A 24 -46.90 -144.96
REMARK 500 5 ASN A 33 -167.97 -103.30
REMARK 500 5 GLU A 47 -77.72 -101.19
REMARK 500 5 LEU A 60 -77.12 -98.72
REMARK 500 5 THR A 61 173.91 55.61
REMARK 500 5 HIS A 63 -64.58 -168.29
REMARK 500 5 LEU A 71 34.56 -96.43
REMARK 500 6 ASN A 3 88.61 -154.88
REMARK 500 6 SER A 5 -55.73 169.67
REMARK 500
REMARK 500 THIS ENTRY HAS 211 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 32 0.32 SIDE CHAIN
REMARK 500 1 ARG A 37 0.21 SIDE CHAIN
REMARK 500 2 ARG A 32 0.21 SIDE CHAIN
REMARK 500 2 ARG A 37 0.31 SIDE CHAIN
REMARK 500 3 ARG A 32 0.31 SIDE CHAIN
REMARK 500 3 ARG A 37 0.28 SIDE CHAIN
REMARK 500 4 ARG A 32 0.28 SIDE CHAIN
REMARK 500 4 ARG A 37 0.23 SIDE CHAIN
REMARK 500 5 ARG A 32 0.25 SIDE CHAIN
REMARK 500 5 ARG A 37 0.19 SIDE CHAIN
REMARK 500 6 ARG A 32 0.13 SIDE CHAIN
REMARK 500 6 ARG A 37 0.25 SIDE CHAIN
REMARK 500 7 ARG A 32 0.26 SIDE CHAIN
REMARK 500 7 ARG A 37 0.10 SIDE CHAIN
REMARK 500 8 ARG A 32 0.22 SIDE CHAIN
REMARK 500 8 ARG A 37 0.21 SIDE CHAIN
REMARK 500 9 ARG A 32 0.24 SIDE CHAIN
REMARK 500 9 ARG A 37 0.23 SIDE CHAIN
REMARK 500 10 ARG A 32 0.26 SIDE CHAIN
REMARK 500 10 ARG A 37 0.21 SIDE CHAIN
REMARK 500 11 ARG A 32 0.21 SIDE CHAIN
REMARK 500 11 ARG A 37 0.21 SIDE CHAIN
REMARK 500 12 ARG A 32 0.22 SIDE CHAIN
REMARK 500 12 ARG A 37 0.21 SIDE CHAIN
REMARK 500 13 ARG A 32 0.22 SIDE CHAIN
REMARK 500 13 ARG A 37 0.30 SIDE CHAIN
REMARK 500 14 ARG A 32 0.29 SIDE CHAIN
REMARK 500 14 ARG A 37 0.21 SIDE CHAIN
REMARK 500 15 ARG A 32 0.15 SIDE CHAIN
REMARK 500 15 ARG A 37 0.31 SIDE CHAIN
REMARK 500 16 ARG A 32 0.27 SIDE CHAIN
REMARK 500 16 ARG A 37 0.19 SIDE CHAIN
REMARK 500 17 ARG A 32 0.28 SIDE CHAIN
REMARK 500 17 ARG A 37 0.15 SIDE CHAIN
REMARK 500 18 ARG A 32 0.32 SIDE CHAIN
REMARK 500 18 ARG A 37 0.20 SIDE CHAIN
REMARK 500 19 ARG A 32 0.20 SIDE CHAIN
REMARK 500 19 ARG A 37 0.23 SIDE CHAIN
REMARK 500 20 ARG A 32 0.31 SIDE CHAIN
REMARK 500 20 ARG A 37 0.26 SIDE CHAIN
REMARK 500 21 ARG A 32 0.26 SIDE CHAIN
REMARK 500 21 ARG A 37 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BO9 A 1 73 UNP P04083 ANXA1_HUMAN 41 113
SEQRES 1 A 73 THR PHE ASN PRO SER SER ASP VAL ALA ALA LEU HIS LYS
SEQRES 2 A 73 ALA ILE MET VAL LYS GLY VAL ASP GLU ALA THR ILE ILE
SEQRES 3 A 73 ASP ILE LEU THR LYS ARG ASN ASN ALA GLN ARG GLN GLN
SEQRES 4 A 73 ILE LYS ALA ALA TYR LEU GLN GLU THR GLY LYS PRO LEU
SEQRES 5 A 73 ASP GLU THR LEU LYS LYS ALA LEU THR GLY HIS LEU GLU
SEQRES 6 A 73 GLU VAL VAL LEU ALA LEU LEU LYS
HELIX 1 1 SER A 5 MET A 16 1 12
HELIX 2 2 THR A 24 ARG A 32 1 9
HELIX 3 3 GLN A 36 THR A 48 1 13
HELIX 4 4 ASP A 53 LEU A 60 1 8
HELIX 5 5 GLU A 65 ALA A 70 1 6
HELIX 6 6 LEU A 71 LYS A 73 5 3
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