Header list of 1j8c.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS 21-MAY-01 1J8C
TITLE SOLUTION STRUCTURE OF THE UBIQUITIN-LIKE DOMAIN OF HPLIC-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-LIKE PROTEIN HPLIC-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-103);
COMPND 5 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_TYPE: PET
KEYWDS UBIQUITIN-LIKE DOMAIN, STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.WALTERS,M.F.KLEIJNEN,A.M.GOH,G.WAGNER,P.M.HOWLEY
REVDAT 3 23-FEB-22 1J8C 1 REMARK
REVDAT 2 24-FEB-09 1J8C 1 VERSN
REVDAT 1 20-MAR-02 1J8C 0
JRNL AUTH K.J.WALTERS,M.F.KLEIJNEN,A.M.GOH,G.WAGNER,P.M.HOWLEY
JRNL TITL STRUCTURAL STUDIES OF THE INTERACTION BETWEEN UBIQUITIN
JRNL TITL 2 FAMILY PROTEINS AND PROTEASOME SUBUNIT S5A.
JRNL REF BIOCHEMISTRY V. 41 1767 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11827521
JRNL DOI 10.1021/BI011892Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 983 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS, 44 DIHEDRAL ANGLE RESTRAINTS, 23
REMARK 3 HYDROGEN BONDS
REMARK 4
REMARK 4 1J8C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013486.
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 : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED BY USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR 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 ARG A 104
REMARK 465 ASP A 105
REMARK 465 PRO A 106
REMARK 465 ASN A 107
REMARK 465 SER A 108
REMARK 465 SER A 109
REMARK 465 SER A 110
REMARK 465 VAL A 111
REMARK 465 ASP A 112
REMARK 465 LYS A 113
REMARK 465 TYR A 114
REMARK 465 ALA A 115
REMARK 465 ALA A 116
REMARK 465 ALA A 117
REMARK 465 LEU A 118
REMARK 465 GLU A 119
REMARK 465 HIS A 120
REMARK 465 HIS A 121
REMARK 465 HIS A 122
REMARK 465 HIS A 123
REMARK 465 HIS A 124
REMARK 465 HIS A 125
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: 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 2 -44.77 -147.96
REMARK 500 1 GLU A 3 -175.74 52.11
REMARK 500 1 PRO A 13 -169.44 -73.60
REMARK 500 1 SER A 14 94.12 -166.77
REMARK 500 1 GLN A 21 -174.79 52.29
REMARK 500 1 SER A 23 66.91 -119.80
REMARK 500 1 ALA A 24 82.56 -167.40
REMARK 500 1 ALA A 25 83.22 52.59
REMARK 500 1 ALA A 28 26.86 -155.63
REMARK 500 1 GLU A 29 81.04 51.77
REMARK 500 1 PRO A 30 38.75 -81.97
REMARK 500 1 ILE A 32 99.88 -58.04
REMARK 500 1 LYS A 41 -46.53 -174.67
REMARK 500 1 GLU A 42 -179.20 -173.60
REMARK 500 1 ASN A 51 63.42 -115.01
REMARK 500 1 LYS A 66 81.30 68.72
REMARK 500 1 SER A 67 -65.40 -152.98
REMARK 500 1 THR A 69 -63.91 -145.95
REMARK 500 1 LYS A 79 -178.46 -59.80
REMARK 500 1 LEU A 81 81.45 -65.07
REMARK 500 1 LYS A 82 -155.42 -137.98
REMARK 500 1 HIS A 90 -41.55 -173.35
REMARK 500 1 ASP A 94 31.69 -179.97
REMARK 500 2 ASN A 4 89.77 -161.80
REMARK 500 2 GLU A 6 88.36 -165.54
REMARK 500 2 SER A 8 -164.56 -118.00
REMARK 500 2 ALA A 19 -42.82 -132.69
REMARK 500 2 ALA A 20 50.51 -90.16
REMARK 500 2 GLN A 21 47.51 -168.87
REMARK 500 2 ALA A 26 62.56 -169.16
REMARK 500 2 GLU A 29 79.37 -151.95
REMARK 500 2 PRO A 30 43.00 -78.77
REMARK 500 2 LYS A 41 -42.00 -175.61
REMARK 500 2 LYS A 66 81.69 69.33
REMARK 500 2 SER A 67 -75.00 -155.04
REMARK 500 2 THR A 69 -62.01 -139.99
REMARK 500 2 LEU A 81 83.33 -66.43
REMARK 500 2 LYS A 82 -147.07 -148.96
REMARK 500 2 HIS A 90 -30.78 176.54
REMARK 500 2 ASP A 94 35.13 179.71
REMARK 500 3 ALA A 2 44.78 -156.30
REMARK 500 3 SER A 8 -171.41 52.51
REMARK 500 3 PRO A 13 -82.24 -73.26
REMARK 500 3 SER A 14 -71.29 -141.01
REMARK 500 3 GLN A 21 -176.11 -58.82
REMARK 500 3 ALA A 25 -174.37 51.71
REMARK 500 3 ALA A 28 -54.39 -166.23
REMARK 500 3 GLU A 29 71.11 52.67
REMARK 500 3 LYS A 31 67.25 -69.46
REMARK 500 3 LYS A 41 -46.86 -174.70
REMARK 500
REMARK 500 THIS ENTRY HAS 397 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 12 0.25 SIDE CHAIN
REMARK 500 1 ARG A 15 0.23 SIDE CHAIN
REMARK 500 1 ARG A 64 0.22 SIDE CHAIN
REMARK 500 2 ARG A 12 0.31 SIDE CHAIN
REMARK 500 2 ARG A 15 0.27 SIDE CHAIN
REMARK 500 2 ARG A 64 0.21 SIDE CHAIN
REMARK 500 3 ARG A 12 0.23 SIDE CHAIN
REMARK 500 3 ARG A 15 0.28 SIDE CHAIN
REMARK 500 3 ARG A 64 0.27 SIDE CHAIN
REMARK 500 4 ARG A 12 0.31 SIDE CHAIN
REMARK 500 4 ARG A 15 0.25 SIDE CHAIN
REMARK 500 4 ARG A 64 0.31 SIDE CHAIN
REMARK 500 5 ARG A 12 0.21 SIDE CHAIN
REMARK 500 5 ARG A 15 0.21 SIDE CHAIN
REMARK 500 5 ARG A 64 0.23 SIDE CHAIN
REMARK 500 6 ARG A 12 0.32 SIDE CHAIN
REMARK 500 6 ARG A 15 0.23 SIDE CHAIN
REMARK 500 6 ARG A 64 0.32 SIDE CHAIN
REMARK 500 7 ARG A 12 0.22 SIDE CHAIN
REMARK 500 7 ARG A 15 0.25 SIDE CHAIN
REMARK 500 7 ARG A 64 0.31 SIDE CHAIN
REMARK 500 8 ARG A 12 0.27 SIDE CHAIN
REMARK 500 8 ARG A 15 0.32 SIDE CHAIN
REMARK 500 8 ARG A 64 0.23 SIDE CHAIN
REMARK 500 9 ARG A 12 0.22 SIDE CHAIN
REMARK 500 9 ARG A 15 0.29 SIDE CHAIN
REMARK 500 9 ARG A 64 0.32 SIDE CHAIN
REMARK 500 10 ARG A 12 0.28 SIDE CHAIN
REMARK 500 10 ARG A 15 0.26 SIDE CHAIN
REMARK 500 10 ARG A 64 0.23 SIDE CHAIN
REMARK 500 11 ARG A 12 0.21 SIDE CHAIN
REMARK 500 11 ARG A 15 0.30 SIDE CHAIN
REMARK 500 11 ARG A 64 0.31 SIDE CHAIN
REMARK 500 12 ARG A 12 0.32 SIDE CHAIN
REMARK 500 12 ARG A 15 0.26 SIDE CHAIN
REMARK 500 12 ARG A 64 0.31 SIDE CHAIN
REMARK 500 13 ARG A 12 0.31 SIDE CHAIN
REMARK 500 13 ARG A 15 0.22 SIDE CHAIN
REMARK 500 13 ARG A 64 0.32 SIDE CHAIN
REMARK 500 14 ARG A 12 0.31 SIDE CHAIN
REMARK 500 14 ARG A 15 0.21 SIDE CHAIN
REMARK 500 14 ARG A 64 0.29 SIDE CHAIN
REMARK 500 15 ARG A 12 0.32 SIDE CHAIN
REMARK 500 15 ARG A 15 0.26 SIDE CHAIN
REMARK 500 15 ARG A 64 0.21 SIDE CHAIN
REMARK 500 16 ARG A 12 0.31 SIDE CHAIN
REMARK 500 16 ARG A 15 0.27 SIDE CHAIN
REMARK 500 16 ARG A 64 0.30 SIDE CHAIN
REMARK 500 17 ARG A 12 0.26 SIDE CHAIN
REMARK 500 17 ARG A 15 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE C-TERMINUS RESIDUES 104-125 WERE ADDED AS LINKER AND
REMARK 999 HIS TAG FOR EASE OF PURIFICATION.
DBREF 1J8C A 1 103 UNP Q9UHD9 UBQL2_HUMAN 1 103
SEQADV 1J8C ARG A 104 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ASP A 105 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C PRO A 106 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ASN A 107 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C SER A 108 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C SER A 109 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C SER A 110 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C VAL A 111 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ASP A 112 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C LYS A 113 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C TYR A 114 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ALA A 115 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ALA A 116 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C ALA A 117 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C LEU A 118 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C GLU A 119 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 120 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 121 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 122 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 123 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 124 UNP Q9UHD9 SEE REMARK 999
SEQADV 1J8C HIS A 125 UNP Q9UHD9 SEE REMARK 999
SEQRES 1 A 125 MET ALA GLU ASN GLY GLU SER SER GLY PRO PRO ARG PRO
SEQRES 2 A 125 SER ARG GLY PRO ALA ALA ALA GLN GLY SER ALA ALA ALA
SEQRES 3 A 125 PRO ALA GLU PRO LYS ILE ILE LYS VAL THR VAL LYS THR
SEQRES 4 A 125 PRO LYS GLU LYS GLU GLU PHE ALA VAL PRO GLU ASN SER
SEQRES 5 A 125 SER VAL GLN GLN PHE LYS GLU ALA ILE SER LYS ARG PHE
SEQRES 6 A 125 LYS SER GLN THR ASP GLN LEU VAL LEU ILE PHE ALA GLY
SEQRES 7 A 125 LYS ILE LEU LYS ASP GLN ASP THR LEU ILE GLN HIS GLY
SEQRES 8 A 125 ILE HIS ASP GLY LEU THR VAL HIS LEU VAL ILE LYS ARG
SEQRES 9 A 125 ASP PRO ASN SER SER SER VAL ASP LYS TYR ALA ALA ALA
SEQRES 10 A 125 LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 SER A 53 LYS A 66 1 14
SHEET 1 A 5 LYS A 43 VAL A 48 0
SHEET 2 A 5 ILE A 33 LYS A 38 -1 N VAL A 35 O PHE A 46
SHEET 3 A 5 LEU A 96 ILE A 102 1 O LEU A 96 N THR A 36
SHEET 4 A 5 LEU A 72 PHE A 76 -1 N ILE A 75 O HIS A 99
SHEET 5 A 5 LYS A 79 LEU A 81 -1 O LEU A 81 N LEU A 74
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 23 2 Bytes