HEADER TRANSFERASE 07-JUL-15 5CEM
TITLE PSEUDOKINASE AND C-TERMINAL EXTENSION OF HUMAN TRIBBLES HOMOLOG 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIBBLES HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 83-371;
COMPND 5 SYNONYM: TRB-1,G-PROTEIN-COUPLED RECEPTOR-INDUCED GENE 2 PROTEIN,GIG-
COMPND 6 2,SKIP1;
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 GENE: TRIB1, C8FW, GIG2, TRB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS KINASE, KINASE-LIKE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.MACE,Y.NAKATANI
REVDAT 4 06-MAR-24 5CEM 1 REMARK
REVDAT 3 01-NOV-17 5CEM 1 JRNL REMARK
REVDAT 2 18-NOV-15 5CEM 1 JRNL
REVDAT 1 11-NOV-15 5CEM 0
JRNL AUTH J.M.MURPHY,Y.NAKATANI,S.A.JAMIESON,W.DAI,I.S.LUCET,P.D.MACE
JRNL TITL MOLECULAR MECHANISM OF CCAAT-ENHANCER BINDING PROTEIN
JRNL TITL 2 RECRUITMENT BY THE TRIB1 PSEUDOKINASE.
JRNL REF STRUCTURE V. 23 2111 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26455797
JRNL DOI 10.1016/J.STR.2015.08.017
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17853
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1031
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1330
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2043
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : -0.23000
REMARK 3 B12 (A**2) : 0.04000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.605
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2127 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2062 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2878 ; 1.385 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4743 ; 0.923 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 254 ; 6.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;31.260 ;21.735
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 379 ;12.584 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;18.435 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 321 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2310 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 498 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1010 ; 4.209 ; 2.639
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1009 ; 4.210 ; 2.638
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 5.953 ; 3.916
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1258 ; 5.951 ; 3.919
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1117 ; 5.255 ; 3.160
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1099 ; 5.166 ; 3.105
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1594 ; 7.394 ; 4.462
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2366 ; 9.980 ;21.329
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2324 ; 9.731 ;20.973
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 364
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2040 46.8060 0.6000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0200 T22: 0.0352
REMARK 3 T33: 0.0889 T12: -0.0033
REMARK 3 T13: -0.0050 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 3.2207 L22: 0.3961
REMARK 3 L33: 0.6085 L12: -0.3044
REMARK 3 L13: -0.7409 L23: 0.0798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: 0.1903 S13: -0.0983
REMARK 3 S21: -0.0436 S22: 0.0227 S23: -0.0176
REMARK 3 S31: 0.0146 S32: 0.0423 S33: 0.0432
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5CEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18911
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 42.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 (PH 5.5), 1% W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.94150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.94150
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.94150
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: AUTHORS HAVE USED SAXS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 81
REMARK 465 PRO A 82
REMARK 465 GLY A 83
REMARK 465 SER A 84
REMARK 465 ALA A 85
REMARK 465 PRO A 86
REMARK 465 GLY A 87
REMARK 465 HIS A 140
REMARK 465 SER A 141
REMARK 465 THR A 229
REMARK 465 HIS A 230
REMARK 465 ILE A 231
REMARK 465 MET A 232
REMARK 465 LYS A 233
REMARK 465 GLY A 234
REMARK 465 GLU A 235
REMARK 465 ASP A 236
REMARK 465 ASP A 237
REMARK 465 GLU A 343
REMARK 465 PRO A 344
REMARK 465 GLY A 345
REMARK 465 TYR A 346
REMARK 465 ILE A 347
REMARK 465 ASP A 348
REMARK 465 SER A 349
REMARK 465 GLU A 350
REMARK 465 ILE A 351
REMARK 465 GLY A 352
REMARK 465 THR A 353
REMARK 465 SER A 354
REMARK 465 ASP A 355
REMARK 465 GLN A 356
REMARK 465 SER A 365
REMARK 465 ASP A 366
REMARK 465 ILE A 367
REMARK 465 SER A 368
REMARK 465 SER A 369
REMARK 465 PHE A 370
REMARK 465 PHE A 371
REMARK 465 SER A 372
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 ALA A 92 -120.78 47.50
REMARK 500 ARG A 102 68.63 65.20
REMARK 500 GLU A 103 -82.37 -81.23
REMARK 500 LYS A 175 -62.12 79.88
REMARK 500 ASN A 255 -139.46 -105.92
REMARK 500 THR A 256 -139.07 42.91
REMARK 500 THR A 257 36.37 -149.77
REMARK 500 LEU A 319 47.16 -93.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CEK RELATED DB: PDB
DBREF 5CEM A 83 371 UNP Q96RU8 TRIB1_HUMAN 83 371
SEQADV 5CEM GLY A 81 UNP Q96RU8 EXPRESSION TAG
SEQADV 5CEM PRO A 82 UNP Q96RU8 EXPRESSION TAG
SEQADV 5CEM SER A 372 UNP Q96RU8 EXPRESSION TAG
SEQRES 1 A 292 GLY PRO GLY SER ALA PRO GLY PRO SER ARG ILE ALA ASP
SEQRES 2 A 292 TYR LEU LEU LEU PRO LEU ALA GLU ARG GLU HIS VAL SER
SEQRES 3 A 292 ARG ALA LEU CYS ILE HIS THR GLY ARG GLU LEU ARG CYS
SEQRES 4 A 292 LYS VAL PHE PRO ILE LYS HIS TYR GLN ASP LYS ILE ARG
SEQRES 5 A 292 PRO TYR ILE GLN LEU PRO SER HIS SER ASN ILE THR GLY
SEQRES 6 A 292 ILE VAL GLU VAL ILE LEU GLY GLU THR LYS ALA TYR VAL
SEQRES 7 A 292 PHE PHE GLU LYS ASP PHE GLY ASP MET HIS SER TYR VAL
SEQRES 8 A 292 ARG SER ARG LYS ARG LEU ARG GLU GLU GLU ALA ALA ARG
SEQRES 9 A 292 LEU PHE LYS GLN ILE VAL SER ALA VAL ALA HIS CYS HIS
SEQRES 10 A 292 GLN SER ALA ILE VAL LEU GLY ASP LEU LYS LEU ARG LYS
SEQRES 11 A 292 PHE VAL PHE SER THR GLU GLU ARG THR GLN LEU ARG LEU
SEQRES 12 A 292 GLU SER LEU GLU ASP THR HIS ILE MET LYS GLY GLU ASP
SEQRES 13 A 292 ASP ALA LEU SER ASP LYS HIS GLY CYS PRO ALA TYR VAL
SEQRES 14 A 292 SER PRO GLU ILE LEU ASN THR THR GLY THR TYR SER GLY
SEQRES 15 A 292 LYS ALA ALA ASP VAL TRP SER LEU GLY VAL MET LEU TYR
SEQRES 16 A 292 THR LEU LEU VAL GLY ARG TYR PRO PHE HIS ASP SER ASP
SEQRES 17 A 292 PRO SER ALA LEU PHE SER LYS ILE ARG ARG GLY GLN PHE
SEQRES 18 A 292 CYS ILE PRO GLU HIS ILE SER PRO LYS ALA ARG CYS LEU
SEQRES 19 A 292 ILE ARG SER LEU LEU ARG ARG GLU PRO SER GLU ARG LEU
SEQRES 20 A 292 THR ALA PRO GLU ILE LEU LEU HIS PRO TRP PHE GLU SER
SEQRES 21 A 292 VAL LEU GLU PRO GLY TYR ILE ASP SER GLU ILE GLY THR
SEQRES 22 A 292 SER ASP GLN ILE VAL PRO GLU TYR GLN GLU ASP SER ASP
SEQRES 23 A 292 ILE SER SER PHE PHE SER
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 HOH *107(H2 O)
HELIX 1 AA1 ILE A 124 ILE A 131 1 8
HELIX 2 AA2 ILE A 131 GLN A 136 1 6
HELIX 3 AA3 ASP A 166 LYS A 175 1 10
HELIX 4 AA4 ARG A 178 SER A 199 1 22
HELIX 5 AA5 LYS A 207 ARG A 209 5 3
HELIX 6 AA6 SER A 250 ASN A 255 1 6
HELIX 7 AA7 SER A 261 GLY A 280 1 20
HELIX 8 AA8 ASP A 288 ARG A 298 1 11
HELIX 9 AA9 SER A 308 LEU A 319 1 12
HELIX 10 AB1 GLU A 322 ARG A 326 5 5
HELIX 11 AB2 THR A 328 LEU A 333 1 6
HELIX 12 AB3 HIS A 335 LEU A 342 1 8
SHEET 1 AA1 7 ARG A 90 ILE A 91 0
SHEET 2 AA1 7 TYR A 94 PRO A 98 -1 O TYR A 94 N ILE A 91
SHEET 3 AA1 7 VAL A 105 CYS A 110 -1 O ARG A 107 N LEU A 97
SHEET 4 AA1 7 GLU A 116 PRO A 123 -1 O LEU A 117 N ALA A 108
SHEET 5 AA1 7 LYS A 155 PHE A 160 -1 O ALA A 156 N PHE A 122
SHEET 6 AA1 7 ILE A 146 LEU A 151 -1 N ILE A 150 O TYR A 157
SHEET 7 AA1 7 GLU A 360 GLN A 362 1 O TYR A 361 N LEU A 151
SHEET 1 AA2 2 PHE A 211 PHE A 213 0
SHEET 2 AA2 2 LEU A 221 LEU A 223 -1 O ARG A 222 N VAL A 212
SITE 1 AC1 8 HIS A 168 LYS A 207 LEU A 208 ARG A 209
SITE 2 AC1 8 LEU A 239 TYR A 248 TYR A 282 HOH A 568
SITE 1 AC2 5 GLN A 128 ARG A 132 ARG A 178 GLU A 179
SITE 2 AC2 5 HOH A 550
SITE 1 AC3 6 GLN A 300 ILE A 303 ARG A 312 ARG A 316
SITE 2 AC3 6 HOH A 546 HOH A 561
SITE 1 AC4 3 ARG A 320 ARG A 321 HOH A 519
CRYST1 81.384 81.384 85.883 90.00 90.00 120.00 P 63 6
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 0.012287 0.007094 0.000000 0.00000
SCALE2 0.000000 0.014188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011644 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
