HEADER PROTEIN BINDING, LIGASE 16-JUN-09 3HVE
TITLE STRUCTURES OF SPOP-SUBSTRATE COMPLEXES: INSIGHTS INTO MOLECULAR
TITLE 2 ARCHITECTURES OF BTB-CUL3 UBIQUITIN LIGASES: GIGAXONINBTB/3-BOX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GIGAXONIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-254;
COMPND 5 SYNONYM: KELCH-LIKE PROTEIN 16;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GIGAXONIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 1-254;
COMPND 11 SYNONYM: KELCH-LIKE PROTEIN 16;
COMPND 12 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: GAN, GAN1, KLHL16;
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: GAN, GAN1, KLHL16;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN, GIGAXONIN, CYTOPLASM, CYTOSKELETON, DISEASE MUTATION,
KEYWDS 2 KELCH REPEAT, NEURODEGENERATION, PHOSPHOPROTEIN, POLYMORPHISM, UBL
KEYWDS 3 CONJUGATION, UBL CONJUGATION PATHWAY, PROTEIN BINDING, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHUANG,B.A.SCHULMAN
REVDAT 2 27-JUN-18 3HVE 1 REMARK
REVDAT 1 27-OCT-09 3HVE 0
JRNL AUTH M.ZHUANG,M.F.CALABRESE,J.LIU,M.B.WADDELL,A.NOURSE,M.HAMMEL,
JRNL AUTH 2 D.J.MILLER,H.WALDEN,D.M.DUDA,S.N.SEYEDIN,T.HOGGARD,
JRNL AUTH 3 J.W.HARPER,K.P.WHITE,B.A.SCHULMAN
JRNL TITL STRUCTURES OF SPOP-SUBSTRATE COMPLEXES: INSIGHTS INTO
JRNL TITL 2 MOLECULAR ARCHITECTURES OF BTB-CUL3 UBIQUITIN LIGASES.
JRNL REF MOL.CELL V. 36 39 2009
JRNL REFN ISSN 1097-2765
JRNL PMID 19818708
JRNL DOI 10.1016/J.MOLCEL.2009.09.022
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 13573
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.303
REMARK 3 FREE R VALUE : 0.333
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 615
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15314
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 27.80000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 ALA A 6
REMARK 465 VAL A 7
REMARK 465 GLU A 26
REMARK 465 SER A 27
REMARK 465 ASN A 60
REMARK 465 TYR A 61
REMARK 465 ASN A 62
REMARK 465 PRO A 63
REMARK 465 PRO A 64
REMARK 465 LYS A 65
REMARK 465 ASP A 66
REMARK 465 ASP A 67
REMARK 465 GLY A 68
REMARK 465 SER A 69
REMARK 465 THR A 70
REMARK 465 GLU A 99
REMARK 465 LYS A 186
REMARK 465 LEU A 187
REMARK 465 ASN A 188
REMARK 465 VAL A 189
REMARK 465 GLY A 190
REMARK 465 ASN A 191
REMARK 465 GLU A 192
REMARK 465 ASP A 206
REMARK 465 THR A 207
REMARK 465 SER A 228
REMARK 465 CYS A 248
REMARK 465 SER A 249
REMARK 465 ASN A 250
REMARK 465 ILE A 251
REMARK 465 PRO A 252
REMARK 465 LEU A 253
REMARK 465 SER A 254
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 ALA B 6
REMARK 465 VAL B 7
REMARK 465 SER B 8
REMARK 465 GLU B 26
REMARK 465 SER B 27
REMARK 465 LEU B 37
REMARK 465 ASP B 38
REMARK 465 GLY B 39
REMARK 465 GLU B 40A
REMARK 465 ILE B 40B
REMARK 465 ASN B 60
REMARK 465 TYR B 61
REMARK 465 ASN B 62
REMARK 465 PRO B 63
REMARK 465 PRO B 64
REMARK 465 LYS B 65
REMARK 465 ASP B 66
REMARK 465 ASP B 67
REMARK 465 GLY B 68
REMARK 465 SER B 69
REMARK 465 THR B 70
REMARK 465 ASN B 98
REMARK 465 THR B 101
REMARK 465 ALA B 131
REMARK 465 GLU B 132
REMARK 465 HIS B 147
REMARK 465 UNK B 186
REMARK 465 UNK B 187
REMARK 465 UNK B 188
REMARK 465 UNK B 189
REMARK 465 UNK B 190
REMARK 465 UNK B 191
REMARK 465 UNK B 206
REMARK 465 UNK B 207
REMARK 465 UNK B 208
REMARK 465 UNK B 209
REMARK 465 UNK B 210
REMARK 465 LEU B 226
REMARK 465 ASP B 227
REMARK 465 LEU B 240
REMARK 465 VAL B 241
REMARK 465 ARG B 242
REMARK 465 GLU B 243
REMARK 465 ILE B 244
REMARK 465 VAL B 245
REMARK 465 LYS B 246
REMARK 465 GLU B 247
REMARK 465 CYS B 248
REMARK 465 SER B 249
REMARK 465 ASN B 250
REMARK 465 ILE B 251
REMARK 465 PRO B 252
REMARK 465 LEU B 253
REMARK 465 SER B 254
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 SER A 8 OG
REMARK 470 VAL A 43 CG1 CG2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 ASN A 98 CG OD1 ND2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 163 CG OD1 OD2
REMARK 470 GLU A 168 CG CD OE1 OE2
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 GLN A 176 CG CD OE1 NE2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 GLU A 185 CG CD OE1 OE2
REMARK 470 ARG A 193 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 194 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 HIS A 205 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 208 CG CD OE1 OE2
REMARK 470 ILE A 209 CG1 CG2 CD1
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 VAL A 212 CG1 CG2
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 ASP A 216 CG OD1 OD2
REMARK 470 LEU A 226 CG CD1 CD2
REMARK 470 ASP A 227 CG OD1 OD2
REMARK 470 SER A 229 OG
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 LEU A 240 CG CD1 CD2
REMARK 470 ARG A 242 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 243 CG CD OE1 OE2
REMARK 470 ILE A 244 CG1 CG2 CD1
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 GLU A 247 CG CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 GLU B 99 CG CD OE1 OE2
REMARK 470 ASP B 100 CG OD1 OD2
REMARK 470 ASP B 139 OD1 OD2
REMARK 470 ARG B 162 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 163 CG OD1 OD2
REMARK 470 LYS B 211 CG CD CE NZ
REMARK 470 VAL B 212 CG1 CG2
REMARK 470 LYS B 215 CG CD CE NZ
REMARK 470 TYR B 230 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 233 CG CD OE1 OE2
REMARK 470 GLN B 234 CG CD OE1 NE2
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 B 239 C - N - CD ANGL. DEV. = -19.5 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 ASP A 9 88.72 -165.32
REMARK 500 PHE A 23 42.74 -90.30
REMARK 500 ASP A 37 -114.46 53.39
REMARK 500 LYS A 58 22.41 -76.81
REMARK 500 LEU A 114 78.17 -107.94
REMARK 500 ASN A 133 42.81 -86.98
REMARK 500 HIS A 147 -71.74 -47.67
REMARK 500 SER A 166 33.26 -95.28
REMARK 500 ALA A 198 -30.83 -135.99
REMARK 500 MSE A 214 -18.98 -48.22
REMARK 500 LEU A 236 3.95 -57.50
REMARK 500 PRO A 239 18.46 -61.70
REMARK 500 PRO B 10 -14.65 -48.30
REMARK 500 GLN B 11 38.43 -83.64
REMARK 500 HIS B 12 -77.00 -110.52
REMARK 500 GLN B 103 -15.20 -46.43
REMARK 500 GLU B 126 -35.90 -39.05
REMARK 500 PHE B 161 -15.93 -45.50
REMARK 500 UNK B 203 99.83 -68.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HQI RELATED DB: PDB
REMARK 900 RELATED ID: 3HQL RELATED DB: PDB
REMARK 900 RELATED ID: 3HQM RELATED DB: PDB
REMARK 900 RELATED ID: 3HTM RELATED DB: PDB
REMARK 900 RELATED ID: 3HU6 RELATED DB: PDB
REMARK 900 RELATED ID: 3HSV RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS MODELED RESIDUES B165-B210 AS UNK, SINCE THE
REMARK 999 ELECTRON DENSITY IS POOR IN THIS REGION AND THEY DO NOT
REMARK 999 KNOW WHICH AMINO ACIDS THESE CORRESPOND TO IN TERMS OF
REMARK 999 THE SEQUENCE. THE ACTUAL CRYSTALLIZED SEQUENCE IN THIS
REMARK 999 REGION IS SSTEEFLELSPQKLKEVISLEKLNVGNERYVFEAVIRWIAHDTEIR
DBREF 3HVE A 1 254 UNP Q9H2C0 GAN_HUMAN 1 254
DBREF 3HVE B 1 254 UNP Q9H2C0 GAN_HUMAN 1 254
SEQADV 3HVE GLY A -1 UNP Q9H2C0 EXPRESSION TAG
SEQADV 3HVE SER A 0 UNP Q9H2C0 EXPRESSION TAG
SEQADV 3HVE GLY B -1 UNP Q9H2C0 EXPRESSION TAG
SEQADV 3HVE SER B 0 UNP Q9H2C0 EXPRESSION TAG
SEQRES 1 A 256 GLY SER MSE ALA GLU GLY SER ALA VAL SER ASP PRO GLN
SEQRES 2 A 256 HIS ALA ALA ARG LEU LEU ARG ALA LEU SER SER PHE ARG
SEQRES 3 A 256 GLU GLU SER ARG PHE CYS ASP ALA HIS LEU VAL LEU ASP
SEQRES 4 A 256 GLY GLU GLU ILE PRO VAL GLN LYS ASN ILE LEU ALA ALA
SEQRES 5 A 256 ALA SER PRO TYR ILE ARG THR LYS LEU ASN TYR ASN PRO
SEQRES 6 A 256 PRO LYS ASP ASP GLY SER THR TYR LYS ILE GLU LEU GLU
SEQRES 7 A 256 GLY ILE SER VAL MSE VAL MSE ARG GLU ILE LEU ASP TYR
SEQRES 8 A 256 ILE PHE SER GLY GLN ILE ARG LEU ASN GLU ASP THR ILE
SEQRES 9 A 256 GLN ASP VAL VAL GLN ALA ALA ASP LEU LEU LEU LEU THR
SEQRES 10 A 256 ASP LEU LYS THR LEU CYS CYS GLU PHE LEU GLU GLY CYS
SEQRES 11 A 256 ILE ALA ALA GLU ASN CYS ILE GLY ILE ARG ASP PHE ALA
SEQRES 12 A 256 LEU HIS TYR CYS LEU HIS HIS VAL HIS TYR LEU ALA THR
SEQRES 13 A 256 GLU TYR LEU GLU THR HIS PHE ARG ASP VAL SER SER THR
SEQRES 14 A 256 GLU GLU PHE LEU GLU LEU SER PRO GLN LYS LEU LYS GLU
SEQRES 15 A 256 VAL ILE SER LEU GLU LYS LEU ASN VAL GLY ASN GLU ARG
SEQRES 16 A 256 TYR VAL PHE GLU ALA VAL ILE ARG TRP ILE ALA HIS ASP
SEQRES 17 A 256 THR GLU ILE ARG LYS VAL HIS MSE LYS ASP VAL MSE SER
SEQRES 18 A 256 ALA LEU TRP VAL SER GLY LEU ASP SER SER TYR LEU ARG
SEQRES 19 A 256 GLU GLN MSE LEU ASN GLU PRO LEU VAL ARG GLU ILE VAL
SEQRES 20 A 256 LYS GLU CYS SER ASN ILE PRO LEU SER
SEQRES 1 B 256 GLY SER MSE ALA GLU GLY SER ALA VAL SER ASP PRO GLN
SEQRES 2 B 256 HIS ALA ALA ARG LEU LEU ARG ALA LEU SER SER PHE ARG
SEQRES 3 B 256 GLU GLU SER ARG PHE CYS ASP ALA HIS LEU VAL LEU ASP
SEQRES 4 B 256 GLY GLU GLU ILE PRO VAL GLN LYS ASN ILE LEU ALA ALA
SEQRES 5 B 256 ALA SER PRO TYR ILE ARG THR LYS LEU ASN TYR ASN PRO
SEQRES 6 B 256 PRO LYS ASP ASP GLY SER THR TYR LYS ILE GLU LEU GLU
SEQRES 7 B 256 GLY ILE SER VAL MSE VAL MSE ARG GLU ILE LEU ASP TYR
SEQRES 8 B 256 ILE PHE SER GLY GLN ILE ARG LEU ASN GLU ASP THR ILE
SEQRES 9 B 256 GLN ASP VAL VAL GLN ALA ALA ASP LEU LEU LEU LEU THR
SEQRES 10 B 256 ASP LEU LYS THR LEU CYS CYS GLU PHE LEU GLU GLY CYS
SEQRES 11 B 256 ILE ALA ALA GLU ASN CYS ILE GLY ILE ARG ASP PHE ALA
SEQRES 12 B 256 LEU HIS TYR CYS LEU HIS HIS VAL HIS TYR LEU ALA THR
SEQRES 13 B 256 GLU TYR LEU GLU THR HIS PHE ARG ASP VAL UNK UNK UNK
SEQRES 14 B 256 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 15 B 256 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 16 B 256 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 17 B 256 UNK UNK UNK UNK LYS VAL HIS MSE LYS ASP VAL MSE SER
SEQRES 18 B 256 ALA LEU TRP VAL SER GLY LEU ASP SER SER TYR LEU ARG
SEQRES 19 B 256 GLU GLN MSE LEU ASN GLU PRO LEU VAL ARG GLU ILE VAL
SEQRES 20 B 256 LYS GLU CYS SER ASN ILE PRO LEU SER
MODRES 3HVE MSE A 81 MET SELENOMETHIONINE
MODRES 3HVE MSE A 83 MET SELENOMETHIONINE
MODRES 3HVE MSE A 214 MET SELENOMETHIONINE
MODRES 3HVE MSE A 218 MET SELENOMETHIONINE
MODRES 3HVE MSE A 235 MET SELENOMETHIONINE
MODRES 3HVE MSE B 81 MET SELENOMETHIONINE
MODRES 3HVE MSE B 83 MET SELENOMETHIONINE
MODRES 3HVE MSE B 214 MET SELENOMETHIONINE
MODRES 3HVE MSE B 218 MET SELENOMETHIONINE
MODRES 3HVE MSE B 235 MET SELENOMETHIONINE
HET MSE A 81 8
HET MSE A 83 8
HET MSE A 214 8
HET MSE A 218 8
HET MSE A 235 8
HET MSE B 81 8
HET MSE B 83 8
HET MSE B 214 8
HET MSE B 218 8
HET MSE B 235 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
HELIX 1 1 HIS A 12 SER A 22 1 11
HELIX 2 2 GLN A 44 ALA A 50 1 7
HELIX 3 3 SER A 52 LYS A 58 1 7
HELIX 4 4 SER A 79 GLY A 93 1 15
HELIX 5 5 THR A 101 LEU A 113 1 13
HELIX 6 6 LEU A 114 CYS A 128 1 15
HELIX 7 7 CYS A 134 TYR A 144 1 11
HELIX 8 8 LEU A 146 SER A 165 1 20
HELIX 9 9 THR A 167 GLU A 172 1 6
HELIX 10 10 SER A 174 LEU A 184 1 11
HELIX 11 11 VAL A 195 ILE A 200 1 6
HELIX 12 12 HIS A 213 GLY A 225 1 13
HELIX 13 13 TYR A 230 ASN A 237 1 8
HELIX 14 14 LEU A 240 LYS A 246 1 7
HELIX 15 15 HIS B 12 SER B 22 1 11
HELIX 16 16 GLN B 44 SER B 52 1 9
HELIX 17 17 SER B 52 LYS B 58 1 7
HELIX 18 18 SER B 79 GLY B 93 1 15
HELIX 19 19 ASP B 104 LEU B 113 1 10
HELIX 20 20 LEU B 114 GLY B 127 1 14
HELIX 21 21 CYS B 134 TYR B 144 1 11
HELIX 22 26 HIS B 213 GLY B 225 1 13
HELIX 23 27 SER B 228 GLU B 238 1 11
SHEET 1 A 3 GLU A 39 VAL A 43 0
SHEET 2 A 3 ALA A 32 LEU A 36 -1 N LEU A 36 O GLU A 39
SHEET 3 A 3 LYS A 72 GLU A 74 1 O ILE A 73 N HIS A 33
SHEET 1 B 2 HIS B 33 LEU B 34 0
SHEET 2 B 2 LYS B 72 ILE B 73 1 O ILE B 73 N HIS B 33
LINK C VAL A 80 N MSE A 81 1555 1555 1.33
LINK C MSE A 81 N VAL A 82 1555 1555 1.34
LINK C VAL A 82 N MSE A 83 1555 1555 1.33
LINK C MSE A 83 N ARG A 84 1555 1555 1.33
LINK C HIS A 213 N MSE A 214 1555 1555 1.33
LINK C VAL A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N SER A 219 1555 1555 1.32
LINK C GLN A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N LEU A 236 1555 1555 1.33
LINK C VAL B 80 N MSE B 81 1555 1555 1.32
LINK C MSE B 81 N VAL B 82 1555 1555 1.33
LINK C VAL B 82 N MSE B 83 1555 1555 1.33
LINK C MSE B 83 N ARG B 84 1555 1555 1.33
LINK C HIS B 213 N MSE B 214 1555 1555 1.33
LINK C VAL B 217 N MSE B 218 1555 1555 1.33
LINK C MSE B 218 N SER B 219 1555 1555 1.33
LINK C MSE B 235 N LEU B 236 1555 1555 1.33
LINK C MSE A 214 N LYS A 215 1555 1555 1.33
LINK C MSE B 214 N LYS B 215 1555 1555 1.33
LINK C GLN B 234 N MSE B 235 1555 1555 1.33
CRYST1 46.480 55.600 120.600 90.00 91.10 90.00 P 1 21 1 2
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 0.021515 0.000000 0.000413 0.00000
SCALE2 0.000000 0.017986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
