HEADER TRANSFERASE/TRANSFERASE ACTIVATOR 16-JAN-13 4ISG
TITLE HUMAN GLUCOKINASE IN COMPLEX WITH NOVEL ACTIVATOR (2S)-3-CYCLOHEXYL-2-
TITLE 2 [4-(METHYLSULFONYL)-2-OXOPIPERAZIN-1-YL]-N-(1,3-THIAZOL-2-YL)
TITLE 3 PROPANAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 16-465;
COMPND 5 SYNONYM: HEXOKINASE TYPE IV, HK IV, HEXOKINASE-4, HK4, HEXOKINASE-D;
COMPND 6 EC: 2.7.1.2;
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: GCK, HXK4 ISOFORM II;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFLAG-CTC
KEYWDS TRANSFERASE/ACTIVATOR ACTIVITY, GLUCOSE CONVERSION TO G6P,
KEYWDS 2 PHOSPHORYLATION, TRANSFERASE-TRANSFERASE ACTIVATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HOSFIELD,R.J.SKENE
REVDAT 4 28-FEB-24 4ISG 1 HETSYN
REVDAT 3 29-JUL-20 4ISG 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 SITE
REVDAT 2 03-APR-13 4ISG 1 JRNL
REVDAT 1 20-MAR-13 4ISG 0
JRNL AUTH Z.S.CHERUVALLATH,S.L.GWALTNEY,M.SABAT,M.TANG,J.FENG,H.WANG,
JRNL AUTH 2 J.MIURA,P.GUNTUPALLI,A.JENNINGS,D.HOSFIELD,B.LEE,Y.WU
JRNL TITL DESIGN, SYNTHESIS AND SAR OF NOVEL GLUCOKINASE ACTIVATORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 2166 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23434031
JRNL DOI 10.1016/J.BMCL.2013.01.093
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 13423
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 711
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 956
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3279
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.12000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.396
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.257
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.032
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.865
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3398 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3268 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4565 ; 1.174 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7533 ; 0.721 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 413 ; 5.275 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;39.621 ;23.827
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 638 ;16.444 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;21.382 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 513 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3779 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 756 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 465
REMARK 3 RESIDUE RANGE : A 500 A 502
REMARK 3 RESIDUE RANGE : A 601 A 732
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7217 -7.4532 -21.0503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0142 T22: 0.0195
REMARK 3 T33: 0.0148 T12: -0.0027
REMARK 3 T13: 0.0094 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.4660 L22: 0.5643
REMARK 3 L33: 0.6634 L12: 0.0454
REMARK 3 L13: 0.3499 L23: 0.2217
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0346 S13: 0.0520
REMARK 3 S21: -0.0149 S22: -0.0374 S23: 0.0166
REMARK 3 S31: -0.0158 S32: 0.0352 S33: 0.0354
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4ISG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000077151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : CHANNEL CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13423
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.645
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 200 MM AMMONIUM IODIDE,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.62800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.13050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.13000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.13050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.62800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.13000
REMARK 290 SMTRY3 4 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: 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 MET A 8
REMARK 465 GLY A 94
REMARK 465 GLU A 95
REMARK 465 GLU A 96
REMARK 465 GLY A 97
REMARK 465 SER A 151
REMARK 465 PHE A 152
REMARK 465 PRO A 153
REMARK 465 VAL A 154
REMARK 465 ARG A 155
REMARK 465 HIS A 156
REMARK 465 GLU A 157
REMARK 465 ASP A 158
REMARK 465 ILE A 159
REMARK 465 ASP A 160
REMARK 465 LYS A 161
REMARK 465 GLY A 162
REMARK 465 ILE A 163
REMARK 465 LEU A 164
REMARK 465 LEU A 165
REMARK 465 ASN A 166
REMARK 465 TRP A 167
REMARK 465 THR A 168
REMARK 465 LYS A 169
REMARK 465 GLY A 170
REMARK 465 PHE A 171
REMARK 465 LYS A 172
REMARK 465 ALA A 173
REMARK 465 SER A 174
REMARK 465 GLY A 175
REMARK 465 ALA A 176
REMARK 465 GLU A 177
REMARK 465 GLY A 178
REMARK 465 ASN A 179
REMARK 465 SER A 398
REMARK 465 GLU A 399
REMARK 465 ASP A 400
REMARK 465 VAL A 401
REMARK 465 GLU A 443
REMARK 465 GLY A 444
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 ARG A 358 74.61 -118.76
REMARK 500 SER A 396 13.11 -69.82
REMARK 500 PRO A 417 -58.62 -29.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ISE RELATED DB: PDB
REMARK 900 RELATED ID: 4ISF RELATED DB: PDB
DBREF 4ISG A 16 465 UNP P35557 HXK4_HUMAN 16 465
SEQADV 4ISG MET A 8 UNP P35557 EXPRESSION TAG
SEQADV 4ISG LYS A 9 UNP P35557 EXPRESSION TAG
SEQADV 4ISG PRO A 10 UNP P35557 EXPRESSION TAG
SEQADV 4ISG MET A 11 UNP P35557 EXPRESSION TAG
SEQADV 4ISG PRO A 12 UNP P35557 EXPRESSION TAG
SEQADV 4ISG LEU A 13 UNP P35557 EXPRESSION TAG
SEQADV 4ISG THR A 14 UNP P35557 EXPRESSION TAG
SEQADV 4ISG LEU A 15 UNP P35557 EXPRESSION TAG
SEQRES 1 A 458 MET LYS PRO MET PRO LEU THR LEU VAL GLU GLN ILE LEU
SEQRES 2 A 458 ALA GLU PHE GLN LEU GLN GLU GLU ASP LEU LYS LYS VAL
SEQRES 3 A 458 MET ARG ARG MET GLN LYS GLU MET ASP ARG GLY LEU ARG
SEQRES 4 A 458 LEU GLU THR HIS GLU GLU ALA SER VAL LYS MET LEU PRO
SEQRES 5 A 458 THR TYR VAL ARG SER THR PRO GLU GLY SER GLU VAL GLY
SEQRES 6 A 458 ASP PHE LEU SER LEU ASP LEU GLY GLY THR ASN PHE ARG
SEQRES 7 A 458 VAL MET LEU VAL LYS VAL GLY GLU GLY GLU GLU GLY GLN
SEQRES 8 A 458 TRP SER VAL LYS THR LYS HIS GLN MET TYR SER ILE PRO
SEQRES 9 A 458 GLU ASP ALA MET THR GLY THR ALA GLU MET LEU PHE ASP
SEQRES 10 A 458 TYR ILE SER GLU CYS ILE SER ASP PHE LEU ASP LYS HIS
SEQRES 11 A 458 GLN MET LYS HIS LYS LYS LEU PRO LEU GLY PHE THR PHE
SEQRES 12 A 458 SER PHE PRO VAL ARG HIS GLU ASP ILE ASP LYS GLY ILE
SEQRES 13 A 458 LEU LEU ASN TRP THR LYS GLY PHE LYS ALA SER GLY ALA
SEQRES 14 A 458 GLU GLY ASN ASN VAL VAL GLY LEU LEU ARG ASP ALA ILE
SEQRES 15 A 458 LYS ARG ARG GLY ASP PHE GLU MET ASP VAL VAL ALA MET
SEQRES 16 A 458 VAL ASN ASP THR VAL ALA THR MET ILE SER CYS TYR TYR
SEQRES 17 A 458 GLU ASP HIS GLN CYS GLU VAL GLY MET ILE VAL GLY THR
SEQRES 18 A 458 GLY CYS ASN ALA CYS TYR MET GLU GLU MET GLN ASN VAL
SEQRES 19 A 458 GLU LEU VAL GLU GLY ASP GLU GLY ARG MET CYS VAL ASN
SEQRES 20 A 458 THR GLU TRP GLY ALA PHE GLY ASP SER GLY GLU LEU ASP
SEQRES 21 A 458 GLU PHE LEU LEU GLU TYR ASP ARG LEU VAL ASP GLU SER
SEQRES 22 A 458 SER ALA ASN PRO GLY GLN GLN LEU TYR GLU LYS LEU ILE
SEQRES 23 A 458 GLY GLY LYS TYR MET GLY GLU LEU VAL ARG LEU VAL LEU
SEQRES 24 A 458 LEU ARG LEU VAL ASP GLU ASN LEU LEU PHE HIS GLY GLU
SEQRES 25 A 458 ALA SER GLU GLN LEU ARG THR ARG GLY ALA PHE GLU THR
SEQRES 26 A 458 ARG PHE VAL SER GLN VAL GLU SER ASP THR GLY ASP ARG
SEQRES 27 A 458 LYS GLN ILE TYR ASN ILE LEU SER THR LEU GLY LEU ARG
SEQRES 28 A 458 PRO SER THR THR ASP CYS ASP ILE VAL ARG ARG ALA CYS
SEQRES 29 A 458 GLU SER VAL SER THR ARG ALA ALA HIS MET CYS SER ALA
SEQRES 30 A 458 GLY LEU ALA GLY VAL ILE ASN ARG MET ARG GLU SER ARG
SEQRES 31 A 458 SER GLU ASP VAL MET ARG ILE THR VAL GLY VAL ASP GLY
SEQRES 32 A 458 SER VAL TYR LYS LEU HIS PRO SER PHE LYS GLU ARG PHE
SEQRES 33 A 458 HIS ALA SER VAL ARG ARG LEU THR PRO SER CYS GLU ILE
SEQRES 34 A 458 THR PHE ILE GLU SER GLU GLU GLY SER GLY ARG GLY ALA
SEQRES 35 A 458 ALA LEU VAL SER ALA VAL ALA CYS LYS LYS ALA CYS MET
SEQRES 36 A 458 LEU GLY GLN
HET GLC A 500 12
HET 1FY A 501 27
HET IOD A 502 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM 1FY (2S)-3-CYCLOHEXYL-2-[4-(METHYLSULFONYL)-2-OXOPIPERAZIN-
HETNAM 2 1FY 1-YL]-N-(1,3-THIAZOL-2-YL)PROPANAMIDE
HETNAM IOD IODIDE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 GLC C6 H12 O6
FORMUL 3 1FY C17 H26 N4 O4 S2
FORMUL 4 IOD I 1-
FORMUL 5 HOH *132(H2 O)
HELIX 1 1 LEU A 13 ALA A 21 1 9
HELIX 2 2 GLU A 22 GLN A 24 5 3
HELIX 3 3 GLN A 26 ARG A 46 1 21
HELIX 4 4 ARG A 46 GLU A 51 1 6
HELIX 5 5 PRO A 111 GLY A 117 1 7
HELIX 6 6 THR A 118 HIS A 137 1 20
HELIX 7 7 VAL A 181 GLY A 193 1 13
HELIX 8 8 ASN A 204 ASP A 217 1 14
HELIX 9 9 GLU A 256 PHE A 260 5 5
HELIX 10 10 LEU A 266 LEU A 270 5 5
HELIX 11 11 LEU A 271 SER A 281 1 11
HELIX 12 12 GLN A 287 GLY A 294 1 8
HELIX 13 13 GLY A 294 GLU A 312 1 19
HELIX 14 14 LEU A 315 GLU A 319 5 5
HELIX 15 15 GLU A 331 ASP A 341 1 11
HELIX 16 16 ARG A 345 LEU A 355 1 11
HELIX 17 17 SER A 360 SER A 396 1 37
HELIX 18 18 GLY A 410 HIS A 416 1 7
HELIX 19 19 SER A 418 THR A 431 1 14
HELIX 20 20 GLY A 446 LEU A 463 1 18
SHEET 1 A 6 LEU A 58 ARG A 63 0
SHEET 2 A 6 ARG A 250 ASN A 254 -1 O ASN A 254 N LEU A 58
SHEET 3 A 6 CYS A 230 GLU A 237 -1 N GLU A 236 O MET A 251
SHEET 4 A 6 CYS A 220 VAL A 226 -1 N GLY A 223 O CYS A 233
SHEET 5 A 6 ARG A 403 ASP A 409 1 O GLY A 407 N VAL A 222
SHEET 6 A 6 GLU A 435 GLU A 440 1 O THR A 437 N VAL A 406
SHEET 1 B 5 SER A 100 SER A 109 0
SHEET 2 B 5 ASN A 83 GLY A 92 -1 N LYS A 90 O LYS A 102
SHEET 3 B 5 ASP A 73 LEU A 79 -1 N SER A 76 O MET A 87
SHEET 4 B 5 PRO A 145 THR A 149 1 O PRO A 145 N LEU A 75
SHEET 5 B 5 ASP A 198 VAL A 199 1 O ASP A 198 N LEU A 146
CRYST1 49.256 78.260 120.261 90.00 90.00 90.00 P 21 21 21 4
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 0.020302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
