HEADER LIGASE 14-OCT-07 2RJ2
TITLE CRYSTAL STRUCTURE OF THE SUGAR RECOGNIZING SCF UBIQUITIN LIGASE AT 1.7
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-BOX ONLY PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SBD DOMAIN. UNP RESIDUES 117-297;
COMPND 5 EC: 6.3.2.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: FBXO2, FBX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(RIL);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS UBIQUITIN, SCF, UBIQUITIN LIGASE, LECTIN, UBL CONJUGATION PATHWAY,
KEYWDS 2 LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VAIJAYANTHIMALA,D.VELMURUGAN,T.MIZUSHIMA,T.YAMANE,Y.YOSHIDA,
AUTHOR 2 K.TANAKA
REVDAT 4 08-NOV-23 2RJ2 1 REMARK
REVDAT 3 25-JAN-23 2RJ2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2RJ2 1 VERSN
REVDAT 1 14-OCT-08 2RJ2 0
JRNL AUTH S.VAIJAYANTHIMALA,D.VELMURUGAN,T.MIZUSHIMA,T.YAMANE,
JRNL AUTH 2 Y.YOSHIDA,K.TANAKA
JRNL TITL CRYSTAL STRUCTURE OF THE SUGAR RECOGNIZING SCF UBIQUITIN
JRNL TITL 2 LIGASE AT 1.7 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.MIZUSHIMA,T.HIRAO,Y.YOSHIDA,S.J.LEE,T.CHIBA,K.IWAI,
REMARK 1 AUTH 2 Y.YAMAGUCHI,K.KATO,T.TSUKIHARA,K.TANAKA
REMARK 1 TITL STRUCTURAL BASIS OF SUGAR-RECOGNIZING UBIQUITIN LIGASE
REMARK 1 REF NAT.STRUCT.MOL.BIOL. V. 11 365 2004
REMARK 1 REFN ISSN 1545-9993
REMARK 1 PMID 14990996
REMARK 1 DOI 10.1038/NSMB732
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 24567
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2749
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1874
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1497
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
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): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.810
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1536 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2083 ; 1.304 ; 1.919
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 184 ; 7.504 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;35.236 ;23.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 238 ;12.081 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.015 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 208 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1210 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 732 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1033 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.232 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.037 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 49 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 42 ; 0.195 ; 0.200
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): 924 ; 0.866 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1452 ; 1.361 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 723 ; 1.986 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 631 ; 3.012 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044918.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU ULTRAX 18
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NICKEL FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27682
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24100
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1UMH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.1%(V/V) PEG 400, 0.01M
REMARK 280 NICKEL CHLORIDE, 1.7M AMMONIUM SULFATE, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 76.66667
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 38.33333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 38.33333
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 76.66667
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 544 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 156 C - N - CD ANGL. DEV. = -18.2 DEGREES
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 SER A 114 -8.98 -167.20
REMARK 500 ASP A 136 -121.15 56.56
REMARK 500 HIS A 145 74.80 -107.24
REMARK 500 LEU A 155 -167.09 -47.29
REMARK 500 PRO A 156 63.63 -9.65
REMARK 500 ASP A 158 -170.00 89.84
REMARK 500 VAL A 161 90.70 44.43
REMARK 500 PHE A 163 76.52 -23.09
REMARK 500 GLN A 165 50.42 29.64
REMARK 500 ASP A 166 99.39 166.34
REMARK 500 SER A 176 -147.67 -120.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 156 GLY A 157 142.15
REMARK 500 GLU A 162 PHE A 163 -145.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 113 N
REMARK 620 2 SER A 114 N 81.5
REMARK 620 3 HIS A 115 N 167.0 85.5
REMARK 620 4 HIS A 115 ND1 97.1 177.5 95.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UMH RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UBIQUITIN LIGASE AT 2.0 RESOLUTION
REMARK 900 RELATED ID: 1UMI RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UBIQUITIN LIGASE COMPLEXED WITH SUGAR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE DIFFERENCES BETWEEN THE REPORTED SEQRES AND THE
REMARK 999 DATABASE SEQUENCE.
REMARK 999 THE DEPOSITORS BELIEVE THAT THESE RESIDUES ARE VALIANTS AT
REMARK 999 THE POSITIONS.
DBREF 2RJ2 A 117 297 UNP Q80UW2 FBX2_MOUSE 117 297
SEQADV 2RJ2 GLY A 113 UNP Q80UW2 EXPRESSION TAG
SEQADV 2RJ2 SER A 114 UNP Q80UW2 EXPRESSION TAG
SEQADV 2RJ2 HIS A 115 UNP Q80UW2 EXPRESSION TAG
SEQADV 2RJ2 MET A 116 UNP Q80UW2 EXPRESSION TAG
SEQADV 2RJ2 LYS A 151 UNP Q80UW2 ARG 151 SEE REMARK 999
SEQADV 2RJ2 GLY A 159 UNP Q80UW2 ASN 159 SEE REMARK 999
SEQADV 2RJ2 ASN A 160 UNP Q80UW2 GLY 160 SEE REMARK 999
SEQRES 1 A 185 GLY SER HIS MET PHE TYR PHE LEU SER LYS ARG ARG ARG
SEQRES 2 A 185 ASN LEU LEU ARG ASN PRO CYS GLY GLU GLU ASP LEU GLU
SEQRES 3 A 185 GLY TRP SER ASP VAL GLU HIS GLY GLY ASP GLY TRP LYS
SEQRES 4 A 185 VAL GLU GLU LEU PRO GLY ASP GLY ASN VAL GLU PHE THR
SEQRES 5 A 185 GLN ASP ASP SER VAL LYS LYS TYR PHE ALA SER SER PHE
SEQRES 6 A 185 GLU TRP CYS ARG LYS ALA GLN VAL ILE ASP LEU GLN ALA
SEQRES 7 A 185 GLU GLY TYR TRP GLU GLU LEU LEU ASP THR THR GLN PRO
SEQRES 8 A 185 ALA ILE VAL VAL LYS ASP TRP TYR SER GLY ARG THR ASP
SEQRES 9 A 185 ALA GLY SER LEU TYR GLU LEU THR VAL ARG LEU LEU SER
SEQRES 10 A 185 GLU ASN GLU ASP VAL LEU ALA GLU PHE ALA THR GLY GLN
SEQRES 11 A 185 VAL ALA VAL PRO GLU ASP GLY SER TRP MET GLU ILE SER
SEQRES 12 A 185 HIS THR PHE ILE ASP TYR GLY PRO GLY VAL ARG PHE VAL
SEQRES 13 A 185 ARG PHE GLU HIS GLY GLY GLN ASP SER VAL TYR TRP LYS
SEQRES 14 A 185 GLY TRP PHE GLY ALA ARG VAL THR ASN SER SER VAL TRP
SEQRES 15 A 185 VAL GLU PRO
HET NI A 501 1
HET CL A 1 1
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
FORMUL 2 NI NI 2+
FORMUL 3 CL CL 1-
FORMUL 4 HOH *256(H2 O)
HELIX 1 1 HIS A 115 ARG A 124 1 10
HELIX 2 2 TRP A 194 THR A 201 1 8
SHEET 1 A 5 SER A 141 HIS A 145 0
SHEET 2 A 5 CYS A 180 ASP A 187 -1 O ALA A 183 N SER A 141
SHEET 3 A 5 VAL A 265 ASP A 276 -1 O VAL A 268 N ILE A 186
SHEET 4 A 5 SER A 219 SER A 229 -1 N LEU A 228 O ARG A 266
SHEET 5 A 5 VAL A 234 ALA A 239 -1 O PHE A 238 N VAL A 225
SHEET 1 B 5 SER A 141 HIS A 145 0
SHEET 2 B 5 CYS A 180 ASP A 187 -1 O ALA A 183 N SER A 141
SHEET 3 B 5 VAL A 265 ASP A 276 -1 O VAL A 268 N ILE A 186
SHEET 4 B 5 SER A 219 SER A 229 -1 N LEU A 228 O ARG A 266
SHEET 5 B 5 VAL A 243 ALA A 244 -1 O VAL A 243 N TYR A 221
SHEET 1 C 5 LYS A 151 GLU A 154 0
SHEET 2 C 5 LYS A 171 ALA A 174 -1 O ALA A 174 N LYS A 151
SHEET 3 C 5 ARG A 287 GLU A 296 -1 O VAL A 288 N PHE A 173
SHEET 4 C 5 ALA A 204 SER A 212 -1 N SER A 212 O ARG A 287
SHEET 5 C 5 MET A 252 PHE A 258 -1 O HIS A 256 N VAL A 207
LINK N GLY A 113 NI NI A 501 1555 1555 2.06
LINK N SER A 114 NI NI A 501 1555 1555 1.90
LINK N HIS A 115 NI NI A 501 1555 1555 1.96
LINK ND1 HIS A 115 NI NI A 501 1555 1555 1.95
SITE 1 AC1 4 GLY A 113 SER A 114 HIS A 115 TYR A 118
SITE 1 AC2 1 ASN A 126
CRYST1 61.760 61.760 115.000 90.00 90.00 120.00 P 32 2 1 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 0.016192 0.009348 0.000000 0.00000
SCALE2 0.000000 0.018697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008696 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
