Header list of 2ax5.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 03-SEP-05 2AX5
TITLE SOLUTION STRUCTURE OF URM1 FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL 11.0 KDA PROTEIN IN FAA3-MAS3 INTERGENIC
COMPND 3 REGION;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: UBIQUITIN-RELATED MODIFIER-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YIL008W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS BETA GRASP FOLD, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.XU,H.HUANG,J.ZHANG,J.WU,Y.SHI
REVDAT 3 09-MAR-22 2AX5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2AX5 1 VERSN
REVDAT 1 27-JUN-06 2AX5 0
JRNL AUTH J.XU,J.ZHANG,L.WANG,J.ZHOU,H.HUANG,J.WU,Y.ZHONG,Y.SHI
JRNL TITL SOLUTION STRUCTURE OF URM1 AND ITS IMPLICATIONS FOR THE
JRNL TITL 2 ORIGIN OF PROTEIN MODIFIERS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 11625 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16864801
JRNL DOI 10.1073/PNAS.0604876103
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),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS SOLVED USING A TOTAL
REMARK 3 OF 1655 DISTANCE RESTRAINTS AND 79 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 2AX5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034419.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM [15N, 13C] LABELED URM1
REMARK 210 PROTEIN, 50MM PHOSPHATE BUFFER
REMARK 210 (PH6.5), 50MM SODIUM CHLORIDE,
REMARK 210 90% H2O, 10% D2O; 0.8MM [15N,
REMARK 210 13C] LABELED URM1 PROTEIN, 50MM
REMARK 210 PHOSPHATE BUFFER (PH6.5), 50MM
REMARK 210 SODIUM CHLORIDE, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3, CNS 1.1, CSI 1.0,
REMARK 210 MOLMOL 2K.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 100
REMARK 465 GLU A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
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 LYS A 28 -69.33 -149.37
REMARK 500 1 SER A 43 -77.52 -99.33
REMARK 500 1 ASN A 47 74.05 -157.15
REMARK 500 1 ASN A 50 -44.93 -171.86
REMARK 500 1 GLU A 77 -72.20 -76.15
REMARK 500 1 GLU A 79 -83.98 56.71
REMARK 500 1 ASP A 81 31.09 -91.56
REMARK 500 1 GLU A 85 101.06 -167.64
REMARK 500 1 THR A 95 53.99 -94.43
REMARK 500 2 LYS A 28 -50.49 -156.09
REMARK 500 2 SER A 43 -78.79 -81.87
REMARK 500 2 PRO A 49 77.56 -63.52
REMARK 500 2 ASN A 50 -54.32 -162.26
REMARK 500 2 GLU A 85 102.08 -165.42
REMARK 500 2 SER A 94 82.18 -155.34
REMARK 500 3 PHE A 16 -75.19 -67.38
REMARK 500 3 LYS A 28 -49.35 -155.49
REMARK 500 3 SER A 43 -74.83 -92.67
REMARK 500 3 ASN A 47 74.96 -162.24
REMARK 500 3 PRO A 49 79.53 -61.67
REMARK 500 3 ASN A 50 -51.33 -172.88
REMARK 500 3 GLU A 57 -162.97 -71.85
REMARK 500 3 ASP A 58 86.93 -64.43
REMARK 500 3 GLU A 77 -50.90 -120.96
REMARK 500 3 GLU A 85 100.96 -165.88
REMARK 500 4 PHE A 16 -70.40 -58.61
REMARK 500 4 ASP A 27 48.52 -91.93
REMARK 500 4 SER A 43 -64.59 -95.33
REMARK 500 4 ASN A 47 72.51 -173.87
REMARK 500 4 ASN A 50 -49.00 -158.85
REMARK 500 4 GLU A 77 -58.53 -137.31
REMARK 500 4 GLU A 79 -71.42 -49.61
REMARK 500 4 GLU A 85 99.71 -162.74
REMARK 500 4 ASP A 86 105.05 -43.50
REMARK 500 4 HIS A 97 114.27 73.08
REMARK 500 5 PHE A 16 -70.44 -69.65
REMARK 500 5 ASP A 27 76.13 56.59
REMARK 500 5 LYS A 28 -67.57 -136.67
REMARK 500 5 SER A 43 -68.81 -92.70
REMARK 500 5 ASN A 47 51.41 -143.91
REMARK 500 5 PRO A 49 74.41 -63.32
REMARK 500 5 ASN A 50 -58.35 -167.63
REMARK 500 5 GLU A 79 -78.50 61.76
REMARK 500 5 ASP A 81 47.52 -93.52
REMARK 500 5 LEU A 84 173.78 -59.75
REMARK 500 5 GLU A 85 100.50 -161.65
REMARK 500 5 ASP A 86 105.03 -43.07
REMARK 500 5 LEU A 96 102.19 61.49
REMARK 500 6 LYS A 28 -53.41 -166.29
REMARK 500 6 GLU A 29 -166.59 -174.07
REMARK 500
REMARK 500 THIS ENTRY HAS 209 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AX5 A 1 99 UNP P40554 URM1_YEAST 1 99
SEQADV 2AX5 LEU A 100 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 GLU A 101 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 102 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 103 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 104 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 105 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 106 UNP P40554 EXPRESSION TAG
SEQADV 2AX5 HIS A 107 UNP P40554 EXPRESSION TAG
SEQRES 1 A 107 MET VAL ASN VAL LYS VAL GLU PHE LEU GLY GLY LEU ASP
SEQRES 2 A 107 ALA ILE PHE GLY LYS GLN ARG VAL HIS LYS ILE LYS MET
SEQRES 3 A 107 ASP LYS GLU ASP PRO VAL THR VAL GLY ASP LEU ILE ASP
SEQRES 4 A 107 HIS ILE VAL SER THR MET ILE ASN ASN PRO ASN ASP VAL
SEQRES 5 A 107 SER ILE PHE ILE GLU ASP ASP SER ILE ARG PRO GLY ILE
SEQRES 6 A 107 ILE THR LEU ILE ASN ASP THR ASP TRP GLU LEU GLU GLY
SEQRES 7 A 107 GLU LYS ASP TYR ILE LEU GLU ASP GLY ASP ILE ILE SER
SEQRES 8 A 107 PHE THR SER THR LEU HIS GLY GLY LEU GLU HIS HIS HIS
SEQRES 9 A 107 HIS HIS HIS
HELIX 1 1 LEU A 12 GLY A 17 1 6
HELIX 2 2 THR A 33 THR A 44 1 12
HELIX 3 3 ASP A 51 ILE A 56 1 6
HELIX 4 4 ASP A 73 GLY A 78 1 6
SHEET 1 A 4 HIS A 22 ILE A 24 0
SHEET 2 A 4 VAL A 4 PHE A 8 -1 N VAL A 6 O HIS A 22
SHEET 3 A 4 ASP A 88 SER A 94 1 O PHE A 92 N GLU A 7
SHEET 4 A 4 ILE A 65 ILE A 69 -1 N ILE A 66 O THR A 93
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 9 2 Bytes