Header list of 1xo3.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 05-OCT-04 1XO3
TITLE SOLUTION STRUCTURE OF UBIQUITIN LIKE PROTEIN FROM MUS MUSCULUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIKEN CDNA 2900073H19;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UBIQUITIN-LIKE PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, CENTER FOR
KEYWDS 2 EUKARYOTIC STRUCTURAL GENOMICS, PSI, CESG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SINGH,M.TONELLI,R.C.TYLER,A.BAHRAMI,M.S.LEE,J.L.MARKLEY,CENTER FOR
AUTHOR 2 EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 6 02-MAR-22 1XO3 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1XO3 1 VERSN
REVDAT 4 12-FEB-08 1XO3 1 REMARK
REVDAT 3 31-JAN-06 1XO3 1 AUTHOR JRNL
REVDAT 2 01-FEB-05 1XO3 1 AUTHOR KEYWDS REMARK
REVDAT 1 19-OCT-04 1XO3 0
JRNL AUTH S.SINGH,M.TONELLI,R.C.TYLER,A.BAHRAMI,M.S.LEE,J.L.MARKLEY
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE AAH26994.1 PROTEIN FROM
JRNL TITL 2 MUS MUSCULUS, A PUTATIVE EUKARYOTIC URM1.
JRNL REF PROTEIN SCI. V. 14 2095 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16046629
JRNL DOI 10.1110/PS.051577605
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.1
REMARK 3 AUTHORS : F. DELAGLIO (NMRPIPE), AXEL BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2166 NOE DERIVED CONSTRAINTS, 46 H-BOND
REMARK 3 CONSTRAINTS, 96 DIHEDRAL ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1XO3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030567.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM BIS-TRIS, 50MM NACL, 93%
REMARK 210 H2O, 7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, NMRVIEW 5.1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE,
REMARK 210 CARTESIAN COORDINATE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 HA ASN A 72 H SER A 91 1.21
REMARK 500 H GLN A 87 OD2 ASP A 90 1.58
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 PRO A 4 -73.96 -70.33
REMARK 500 1 ASP A 20 -16.86 82.32
REMARK 500 1 LYS A 23 -61.04 -98.64
REMARK 500 1 GLN A 32 -75.81 -158.21
REMARK 500 1 GLU A 34 82.29 54.49
REMARK 500 1 TRP A 36 35.79 -94.88
REMARK 500 1 ASP A 61 -38.11 -163.87
REMARK 500 1 SER A 62 -79.37 -154.11
REMARK 500 1 ASN A 72 -47.59 67.05
REMARK 500 1 ASP A 73 24.13 175.46
REMARK 500 1 GLU A 81 -116.94 40.15
REMARK 500 1 LEU A 86 151.81 61.45
REMARK 500 2 ASP A 20 64.76 65.95
REMARK 500 2 LYS A 23 -67.81 -121.10
REMARK 500 2 GLN A 32 116.95 -161.43
REMARK 500 2 GLU A 33 -39.89 68.37
REMARK 500 2 GLU A 34 87.87 61.05
REMARK 500 2 GLU A 52 -158.25 -96.05
REMARK 500 2 ASP A 61 -68.08 -144.36
REMARK 500 2 SER A 62 -67.61 -138.12
REMARK 500 2 ASN A 72 -48.44 68.19
REMARK 500 2 ASP A 73 36.03 178.22
REMARK 500 2 GLU A 81 -128.06 41.21
REMARK 500 2 ASP A 83 73.05 -100.77
REMARK 500 2 LEU A 86 151.63 65.10
REMARK 500 3 PRO A 4 -78.79 -53.38
REMARK 500 3 LYS A 23 -82.20 -117.98
REMARK 500 3 GLN A 32 -85.55 -125.46
REMARK 500 3 GLU A 34 94.51 -32.48
REMARK 500 3 ASP A 61 -63.98 -142.68
REMARK 500 3 SER A 62 -68.67 -140.13
REMARK 500 3 ASN A 72 -59.14 77.08
REMARK 500 3 ASP A 73 23.59 179.81
REMARK 500 3 GLU A 81 -148.32 61.68
REMARK 500 3 GLN A 85 20.45 -79.46
REMARK 500 3 LEU A 86 151.88 56.99
REMARK 500 3 GLN A 87 -74.94 -113.06
REMARK 500 3 ASP A 88 129.07 172.00
REMARK 500 4 PRO A 4 -76.55 -81.87
REMARK 500 4 LYS A 23 -73.77 -119.24
REMARK 500 4 TRP A 36 34.71 -96.37
REMARK 500 4 ASN A 48 -54.27 -121.27
REMARK 500 4 ASP A 61 -62.04 -146.97
REMARK 500 4 SER A 62 -72.06 -131.20
REMARK 500 4 ASN A 72 -63.38 76.82
REMARK 500 4 ASP A 73 24.24 -173.33
REMARK 500 4 GLU A 81 -127.06 41.77
REMARK 500 4 LEU A 86 145.52 60.01
REMARK 500 4 ASP A 88 127.29 174.97
REMARK 500 5 PRO A 4 -62.73 -91.29
REMARK 500
REMARK 500 THIS ENTRY HAS 261 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6337 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ENTRY
REMARK 900 RELATED ID: GO.34198 RELATED DB: TARGETDB
DBREF 1XO3 A 2 101 UNP Q9D2P4 Q9D2P4_MOUSE 2 101
SEQADV 1XO3 SER A 1 UNP Q9D2P4 CLONING ARTIFACT
SEQRES 1 A 101 SER ALA ALA PRO LEU CYS VAL LYS VAL GLU PHE GLY GLY
SEQRES 2 A 101 GLY ALA GLU LEU LEU PHE ASP GLY VAL LYS LYS HIS GLN
SEQRES 3 A 101 VAL ALA LEU PRO GLY GLN GLU GLU PRO TRP ASP ILE ARG
SEQRES 4 A 101 ASN LEU LEU VAL TRP ILE LYS LYS ASN LEU LEU LYS GLU
SEQRES 5 A 101 ARG PRO GLU LEU PHE ILE GLN GLY ASP SER VAL ARG PRO
SEQRES 6 A 101 GLY ILE LEU VAL LEU ILE ASN ASP ALA ASP TRP GLU LEU
SEQRES 7 A 101 LEU GLY GLU LEU ASP TYR GLN LEU GLN ASP GLN ASP SER
SEQRES 8 A 101 ILE LEU PHE ILE SER THR LEU HIS GLY GLY
HELIX 1 1 GLY A 14 ASP A 20 5 7
HELIX 2 2 ASP A 37 LEU A 50 1 14
HELIX 3 3 ARG A 53 PHE A 57 5 5
HELIX 4 4 TRP A 76 GLY A 80 1 5
SHEET 1 A 5 HIS A 25 ALA A 28 0
SHEET 2 A 5 CYS A 6 PHE A 11 -1 N VAL A 9 O HIS A 25
SHEET 3 A 5 SER A 91 SER A 96 1 O ILE A 92 N LYS A 8
SHEET 4 A 5 ILE A 67 ILE A 71 -1 N LEU A 68 O ILE A 95
SHEET 5 A 5 ALA A 74 ASP A 75 -1 O ALA A 74 N ILE A 71
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