HEADER SIGNALING PROTEIN 07-NOV-15 5EMZ
TITLE CRYSTAL STRUCTURE OF K48-LINKED DIUBIQUITIN WITH F45W MUTATION IN THE
TITLE 2 PROXIMAL UNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYUBIQUITIN-B;
COMPND 3 CHAIN: A, C, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: POLYUBIQUITIN-B;
COMPND 7 CHAIN: B, D, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: UBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: UBB;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN SIGNALING, MULTIDOMAIN SYSTEM, FLUORESCENCE ASSAY,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.NAKASONE,P.J.PAUKSTELIS,D.FUSHMAN
REVDAT 2 27-SEP-23 5EMZ 1 REMARK
REVDAT 1 16-NOV-16 5EMZ 0
JRNL AUTH M.A.NAKASONE,C.GENG,M.CHOJNACKI,M.GLICKMAN,P.J.PAUKSTELIS,
JRNL AUTH 2 D.FUSHMAN
JRNL TITL STRUCTURAL CHARACTERIZATION AND PRACTICAL FLUORESCENCE
JRNL TITL 2 APPLICATIONS OF THE F45W UBIQUITIN MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 46956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2332
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.6912 - 4.2671 0.99 2777 141 0.1445 0.1483
REMARK 3 2 4.2671 - 3.3873 0.99 2732 136 0.1345 0.1731
REMARK 3 3 3.3873 - 2.9593 0.99 2715 133 0.1588 0.1866
REMARK 3 4 2.9593 - 2.6887 0.98 2677 140 0.1699 0.2194
REMARK 3 5 2.6887 - 2.4961 0.98 2683 148 0.1756 0.2424
REMARK 3 6 2.4961 - 2.3489 0.98 2661 140 0.1742 0.2036
REMARK 3 7 2.3489 - 2.2313 0.98 2687 141 0.1730 0.2341
REMARK 3 8 2.2313 - 2.1341 0.97 2659 131 0.1732 0.2157
REMARK 3 9 2.1341 - 2.0520 0.97 2626 159 0.1763 0.2173
REMARK 3 10 2.0520 - 1.9812 0.97 2673 125 0.1848 0.2401
REMARK 3 11 1.9812 - 1.9192 0.97 2650 147 0.1855 0.2270
REMARK 3 12 1.9192 - 1.8644 0.97 2635 146 0.1958 0.2403
REMARK 3 13 1.8644 - 1.8153 0.96 2602 156 0.2087 0.3006
REMARK 3 14 1.8153 - 1.7710 0.97 2637 142 0.2294 0.2793
REMARK 3 15 1.7710 - 1.7307 0.96 2580 157 0.2431 0.2565
REMARK 3 16 1.7307 - 1.6939 0.91 2485 120 0.2593 0.2964
REMARK 3 17 1.6939 - 1.6600 0.76 2145 70 0.2777 0.3073
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 3652
REMARK 3 ANGLE : 0.923 4956
REMARK 3 CHIRALITY : 0.032 601
REMARK 3 PLANARITY : 0.004 634
REMARK 3 DIHEDRAL : 14.128 1428
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46959
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 43.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3M3J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LISO TRIS PEG-3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 29.43500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.46000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 29.43500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.46000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 D 281 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 278 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 287 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 300 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH F 192 LIES ON A SPECIAL POSITION.
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 B 75
REMARK 465 GLY B 76
REMARK 465 ARG D 74
REMARK 465 GLY D 75
REMARK 465 GLY D 76
REMARK 465 ARG F 74
REMARK 465 GLY F 75
REMARK 465 GLY F 76
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 6 CG CD CE NZ
REMARK 470 GLU A 16 CD OE1 OE2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 LYS C 6 CG CD CE NZ
REMARK 470 ARG C 48 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 73 CG CD1 CD2
REMARK 470 ARG C 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 11 CG CD CE NZ
REMARK 470 GLU E 51 CD OE1 OE2
REMARK 470 ARG E 72 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 72 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O HOH B 274 O HOH B 289 1.91
REMARK 500 O HOH D 202 O HOH D 219 1.92
REMARK 500 OE1 GLU B 64 O HOH B 201 1.95
REMARK 500 O GLY C 76 NZ LYS D 48 1.96
REMARK 500 O HOH B 205 O HOH B 245 1.96
REMARK 500 O HOH E 204 O HOH E 208 1.97
REMARK 500 O HOH A 148 O HOH A 186 1.99
REMARK 500 NH2 ARG B 74 O HOH B 202 2.02
REMARK 500 O HOH A 108 O HOH A 180 2.04
REMARK 500 NZ LYS A 27 O HOH A 101 2.06
REMARK 500 O HOH D 263 O HOH D 265 2.06
REMARK 500 O GLY A 76 NZ LYS B 48 2.10
REMARK 500 O LYS C 33 O HOH C 101 2.12
REMARK 500 OD1 ASN E 60 O HOH E 201 2.16
REMARK 500 CA GLY A 76 NZ LYS B 48 2.16
REMARK 500 O GLY E 76 NZ LYS F 48 2.16
REMARK 500 O HOH D 274 O HOH F 189 2.17
REMARK 500 NH1 ARG B 54 O HOH B 203 2.17
REMARK 500 O HOH C 158 O HOH C 170 2.18
REMARK 500 O HOH B 285 O HOH D 202 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 199 O HOH D 275 2657 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 296 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH D 285 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH F 192 DISTANCE = 5.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS D 48 and GLY C
REMARK 800 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS F 48 and GLY E
REMARK 800 76
DBREF 5EMZ A 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EMZ B 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EMZ C 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EMZ D 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EMZ E 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EMZ F 1 76 UNP P0CG47 UBB_HUMAN 1 76
SEQADV 5EMZ ARG A 48 UNP P0CG47 LYS 48 CONFLICT
SEQADV 5EMZ TRP B 45 UNP P0CG47 PHE 45 ENGINEERED MUTATION
SEQADV 5EMZ ARG C 48 UNP P0CG47 LYS 48 CONFLICT
SEQADV 5EMZ TRP D 45 UNP P0CG47 PHE 45 ENGINEERED MUTATION
SEQADV 5EMZ ARG E 48 UNP P0CG47 LYS 48 CONFLICT
SEQADV 5EMZ TRP F 45 UNP P0CG47 PHE 45 ENGINEERED MUTATION
SEQRES 1 A 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 A 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 A 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 A 76 GLN GLN ARG LEU ILE PHE ALA GLY ARG GLN LEU GLU ASP
SEQRES 5 A 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 A 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 76 GLN GLN ARG LEU ILE TRP ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 C 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 C 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 C 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 C 76 GLN GLN ARG LEU ILE PHE ALA GLY ARG GLN LEU GLU ASP
SEQRES 5 C 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 C 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 76 GLN GLN ARG LEU ILE TRP ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 E 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 E 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 E 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 E 76 GLN GLN ARG LEU ILE PHE ALA GLY ARG GLN LEU GLU ASP
SEQRES 5 E 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 E 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 F 76 GLN GLN ARG LEU ILE TRP ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HET SO4 B 101 5
HET SO4 D 101 5
HET SO4 E 101 5
HET SO4 E 102 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 4(O4 S 2-)
FORMUL 11 HOH *561(H2 O)
HELIX 1 AA1 THR A 22 GLY A 35 1 14
HELIX 2 AA2 PRO A 37 ASP A 39 5 3
HELIX 3 AA3 THR B 22 GLY B 35 1 14
HELIX 4 AA4 PRO B 37 ASP B 39 5 3
HELIX 5 AA5 LEU B 56 ASN B 60 5 5
HELIX 6 AA6 THR C 22 GLY C 35 1 14
HELIX 7 AA7 PRO C 37 ASP C 39 5 3
HELIX 8 AA8 LEU C 56 ASN C 60 5 5
HELIX 9 AA9 THR D 22 GLY D 35 1 14
HELIX 10 AB1 PRO D 37 ASP D 39 5 3
HELIX 11 AB2 THR E 22 GLY E 35 1 14
HELIX 12 AB3 PRO E 37 ASP E 39 5 3
HELIX 13 AB4 LEU E 56 ASN E 60 5 5
HELIX 14 AB5 THR F 22 GLY F 35 1 14
HELIX 15 AB6 PRO F 37 ASP F 39 5 3
HELIX 16 AB7 THR F 55 ASN F 60 1 6
SHEET 1 AA1 5 THR A 12 GLU A 16 0
SHEET 2 AA1 5 GLN A 2 THR A 7 -1 N VAL A 5 O ILE A 13
SHEET 3 AA1 5 THR A 66 LEU A 71 1 O LEU A 67 N PHE A 4
SHEET 4 AA1 5 GLN A 41 PHE A 45 -1 N ARG A 42 O VAL A 70
SHEET 5 AA1 5 ARG A 48 GLN A 49 -1 O ARG A 48 N PHE A 45
SHEET 1 AA2 5 THR B 12 GLU B 16 0
SHEET 2 AA2 5 GLN B 2 THR B 7 -1 N ILE B 3 O LEU B 15
SHEET 3 AA2 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4
SHEET 4 AA2 5 GLN B 41 TRP B 45 -1 N ILE B 44 O HIS B 68
SHEET 5 AA2 5 LYS B 48 GLN B 49 -1 O LYS B 48 N TRP B 45
SHEET 1 AA3 5 THR C 12 GLU C 16 0
SHEET 2 AA3 5 GLN C 2 THR C 7 -1 N VAL C 5 O ILE C 13
SHEET 3 AA3 5 THR C 66 LEU C 71 1 O LEU C 67 N LYS C 6
SHEET 4 AA3 5 GLN C 41 PHE C 45 -1 N ILE C 44 O HIS C 68
SHEET 5 AA3 5 ARG C 48 GLN C 49 -1 O ARG C 48 N PHE C 45
SHEET 1 AA4 5 THR D 12 GLU D 16 0
SHEET 2 AA4 5 GLN D 2 THR D 7 -1 N ILE D 3 O LEU D 15
SHEET 3 AA4 5 THR D 66 LEU D 71 1 O LEU D 67 N PHE D 4
SHEET 4 AA4 5 GLN D 41 TRP D 45 -1 N ILE D 44 O HIS D 68
SHEET 5 AA4 5 LYS D 48 GLN D 49 -1 O LYS D 48 N TRP D 45
SHEET 1 AA5 5 THR E 12 GLU E 16 0
SHEET 2 AA5 5 GLN E 2 THR E 7 -1 N VAL E 5 O ILE E 13
SHEET 3 AA5 5 THR E 66 LEU E 71 1 O LEU E 67 N PHE E 4
SHEET 4 AA5 5 GLN E 41 PHE E 45 -1 N ILE E 44 O HIS E 68
SHEET 5 AA5 5 ARG E 48 GLN E 49 -1 O ARG E 48 N PHE E 45
SHEET 1 AA6 5 THR F 12 GLU F 16 0
SHEET 2 AA6 5 GLN F 2 THR F 7 -1 N VAL F 5 O ILE F 13
SHEET 3 AA6 5 THR F 66 LEU F 71 1 O LEU F 67 N PHE F 4
SHEET 4 AA6 5 GLN F 41 TRP F 45 -1 N ILE F 44 O HIS F 68
SHEET 5 AA6 5 LYS F 48 GLN F 49 -1 O LYS F 48 N TRP F 45
LINK C GLY A 76 NZ LYS B 48 1555 1555 1.21
LINK C GLY C 76 NZ LYS D 48 1555 1555 1.49
LINK C GLY E 76 NZ LYS F 48 1555 1555 1.30
SITE 1 AC1 7 ARG A 42 GLN A 49 ARG A 72 ARG B 42
SITE 2 AC1 7 GLN B 49 ARG B 72 HOH B 246
SITE 1 AC2 6 ARG C 42 GLN C 49 ARG C 72 ARG D 42
SITE 2 AC2 6 GLN D 49 ARG D 72
SITE 1 AC3 5 ARG E 42 GLN E 49 HOH E 205 ARG F 42
SITE 2 AC3 5 GLN F 49
SITE 1 AC4 2 HOH E 208 HOH E 209
SITE 1 AC5 19 ILE C 44 PHE C 45 ALA C 46 GLY C 47
SITE 2 AC5 19 GLN C 49 LEU C 50 LEU C 71 LEU C 73
SITE 3 AC5 19 ARG C 74 GLY C 75 ILE D 44 TRP D 45
SITE 4 AC5 19 ALA D 46 GLY D 47 GLN D 49 LEU D 50
SITE 5 AC5 19 LEU D 71 HOH D 212 HOH D 226
SITE 1 AC6 24 LEU A 71 ALA B 46 ILE E 44 PHE E 45
SITE 2 AC6 24 ALA E 46 GLY E 47 GLN E 49 LEU E 50
SITE 3 AC6 24 LEU E 71 LEU E 73 ARG E 74 GLY E 75
SITE 4 AC6 24 HOH E 203 HOH E 207 HOH E 212 HOH E 227
SITE 5 AC6 24 ILE F 44 TRP F 45 ALA F 46 GLY F 47
SITE 6 AC6 24 GLN F 49 LEU F 50 LEU F 71 LEU F 73
CRYST1 58.870 78.920 91.510 90.00 97.93 90.00 C 1 2 1 12
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 0.016987 0.000000 0.002366 0.00000
SCALE2 0.000000 0.012671 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011033 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
