HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JAN-13 4IWV
TITLE CRYSTALS STRUCTURE OF HUMAN GLUCOKINASE IN COMPLEX WITH SMALL MOLECULE
TITLE 2 ACTIVATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOKINASE ISOFORM 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLUCOKINASE;
COMPND 5 SYNONYM: HEXOKINASE TYPE IV, HK IV, HEXOKINASE-4, HK4, HEXOKINASE-D;
COMPND 6 EC: 2.7.1.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: GCK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALLOSTERIC SITE, CATALYSIS, ENZYME ACTIVATION, GENE EXPRESSION
KEYWDS 2 REGULATION, GLUCOKINASE, GLUCOSE, HOMEOSTASIS, HUMANS, HYPOGLYCEMIA,
KEYWDS 3 KINETICS, BIOLOGICAL, MODELS, MOLECULAR, MUTATION, PROTEIN
KEYWDS 4 CONFORMATION, SCATTERING, RADIATION, X-RAYS, TRANSFERASE-TRANSFERASE
KEYWDS 5 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.OGG,D.HARGREAVES,S.GERHARDT,L.FLAVELL,M.MCALISTER
REVDAT 3 20-SEP-23 4IWV 1 HETSYN
REVDAT 2 29-JUL-20 4IWV 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 24-APR-13 4IWV 0
JRNL AUTH M.J.WARING,S.N.BENNETT,S.BOYD,L.CAMPBELL,R.D.M.DAVIES,
JRNL AUTH 2 D.J.OGG,D.HARGREAVES,N.G.MARTIN,G.ROBB,S.WILKINSON,
JRNL AUTH 3 P.MACPAUL,J.M.WOOD
JRNL TITL OPTIMISING PHARMACOKINETICS OF GLUCOKINASE ACTIVATORS WITH
JRNL TITL 2 MATCHED TRIPLICATE DESIGN SETS THE DISCOVERY OF AZD3651 AND
JRNL TITL 3 AZD9485
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 37.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 26853
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1450
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) : 1503
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3457
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08000
REMARK 3 B22 (A**2) : -1.08000
REMARK 3 B33 (A**2) : 2.16000
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): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3593 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3355 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4830 ; 1.854 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7716 ; 0.888 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 440 ; 6.787 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;38.703 ;23.855
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 647 ;16.662 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;21.455 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 529 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4127 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 799 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 459
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8241 24.3921 -0.0188
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: 0.0252
REMARK 3 T33: 0.0495 T12: -0.0070
REMARK 3 T13: 0.0158 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.9171 L22: 0.4236
REMARK 3 L33: 0.1685 L12: -0.5735
REMARK 3 L13: -0.0930 L23: 0.1569
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.0831 S13: 0.1469
REMARK 3 S21: 0.0322 S22: 0.0618 S23: -0.1137
REMARK 3 S31: 0.0307 S32: 0.0016 S33: -0.0325
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4IWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077310.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 7.0-8.5
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 FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRADED, MULTILAYER CONFOCAL
REMARK 200 MIRRORS
REMARK 200 OPTICS : OSMIC VARIMAX HF MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 2.430
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.27500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1V4S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% GLUCOSE, 10-18% PEG8000, 200MM
REMARK 280 SODIUM ACETATE, MMT 100MM PH7.0-8.5, PH 7.4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 42.67500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.33750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 64.01250
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 GLY A 10
REMARK 465 GLY A 94
REMARK 465 GLU A 95
REMARK 465 GLU A 96
REMARK 465 GLY A 97
REMARK 465 ASP A 341
REMARK 465 THR A 342
REMARK 465 ALA A 460
REMARK 465 CYS A 461
REMARK 465 MET A 462
REMARK 465 LEU A 463
REMARK 465 GLY A 464
REMARK 465 GLN A 465
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 196 CD GLU A 196 OE1 -0.066
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 77 CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 397 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 397 NE - CZ - NH2 ANGL. DEV. = -3.1 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 MET A 139 22.63 -140.54
REMARK 500 SER A 151 57.91 -91.40
REMARK 500 ALA A 173 132.47 -38.59
REMARK 500 ILE A 293 -50.50 -123.26
REMARK 500 HIS A 317 41.78 28.26
REMARK 500 SER A 321 -176.00 -67.91
REMARK 500 SER A 353 -65.71 -25.05
REMARK 500 LEU A 355 4.95 -66.11
REMARK 500 SER A 360 173.45 -55.64
REMARK 500 ARG A 397 -163.97 -121.69
REMARK 500 GLU A 443 36.48 -152.63
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 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 238 O
REMARK 620 2 VAL A 241 O 89.9
REMARK 620 3 VAL A 244 O 149.4 81.1
REMARK 620 4 GLY A 246 O 82.0 171.1 104.0
REMARK 620 5 HOH A 696 O 103.0 99.2 107.4 86.2
REMARK 620 N 1 2 3 4
DBREF 4IWV A 13 465 UNP P35557 HXK4_HUMAN 13 465
SEQADV 4IWV GLY A 10 UNP P35557 EXPRESSION TAG
SEQADV 4IWV SER A 11 UNP P35557 EXPRESSION TAG
SEQADV 4IWV SER A 12 UNP P35557 EXPRESSION TAG
SEQADV 4IWV ALA A 27 UNP P35557 GLU 27 ENGINEERED MUTATION
SEQADV 4IWV ALA A 28 UNP P35557 GLU 28 ENGINEERED MUTATION
SEQADV 4IWV ALA A 51 UNP P35557 GLU 51 ENGINEERED MUTATION
SEQADV 4IWV ALA A 52 UNP P35557 GLU 52 ENGINEERED MUTATION
SEQRES 1 A 456 GLY SER SER ASN SER GLN VAL GLU GLN ILE LEU ALA GLU
SEQRES 2 A 456 PHE GLN LEU GLN ALA ALA ASP LEU LYS LYS VAL MET ARG
SEQRES 3 A 456 ARG MET GLN LYS GLU MET ASP ARG GLY LEU ARG LEU GLU
SEQRES 4 A 456 THR HIS ALA ALA ALA SER VAL LYS MET LEU PRO THR TYR
SEQRES 5 A 456 VAL ARG SER THR PRO GLU GLY SER GLU VAL GLY ASP PHE
SEQRES 6 A 456 LEU SER LEU ASP LEU GLY GLY THR ASN PHE ARG VAL MET
SEQRES 7 A 456 LEU VAL LYS VAL GLY GLU GLY GLU GLU GLY GLN TRP SER
SEQRES 8 A 456 VAL LYS THR LYS HIS GLN MET TYR SER ILE PRO GLU ASP
SEQRES 9 A 456 ALA MET THR GLY THR ALA GLU MET LEU PHE ASP TYR ILE
SEQRES 10 A 456 SER GLU CYS ILE SER ASP PHE LEU ASP LYS HIS GLN MET
SEQRES 11 A 456 LYS HIS LYS LYS LEU PRO LEU GLY PHE THR PHE SER PHE
SEQRES 12 A 456 PRO VAL ARG HIS GLU ASP ILE ASP LYS GLY ILE LEU LEU
SEQRES 13 A 456 ASN TRP THR LYS GLY PHE LYS ALA SER GLY ALA GLU GLY
SEQRES 14 A 456 ASN ASN VAL VAL GLY LEU LEU ARG ASP ALA ILE LYS ARG
SEQRES 15 A 456 ARG GLY ASP PHE GLU MET ASP VAL VAL ALA MET VAL ASN
SEQRES 16 A 456 ASP THR VAL ALA THR MET ILE SER CYS TYR TYR GLU ASP
SEQRES 17 A 456 HIS GLN CYS GLU VAL GLY MET ILE VAL GLY THR GLY CYS
SEQRES 18 A 456 ASN ALA CYS TYR MET GLU GLU MET GLN ASN VAL GLU LEU
SEQRES 19 A 456 VAL GLU GLY ASP GLU GLY ARG MET CYS VAL ASN THR GLU
SEQRES 20 A 456 TRP GLY ALA PHE GLY ASP SER GLY GLU LEU ASP GLU PHE
SEQRES 21 A 456 LEU LEU GLU TYR ASP ARG LEU VAL ASP GLU SER SER ALA
SEQRES 22 A 456 ASN PRO GLY GLN GLN LEU TYR GLU LYS LEU ILE GLY GLY
SEQRES 23 A 456 LYS TYR MET GLY GLU LEU VAL ARG LEU VAL LEU LEU ARG
SEQRES 24 A 456 LEU VAL ASP GLU ASN LEU LEU PHE HIS GLY GLU ALA SER
SEQRES 25 A 456 GLU GLN LEU ARG THR ARG GLY ALA PHE GLU THR ARG PHE
SEQRES 26 A 456 VAL SER GLN VAL GLU SER ASP THR GLY ASP ARG LYS GLN
SEQRES 27 A 456 ILE TYR ASN ILE LEU SER THR LEU GLY LEU ARG PRO SER
SEQRES 28 A 456 THR THR ASP CYS ASP ILE VAL ARG ARG ALA CYS GLU SER
SEQRES 29 A 456 VAL SER THR ARG ALA ALA HIS MET CYS SER ALA GLY LEU
SEQRES 30 A 456 ALA GLY VAL ILE ASN ARG MET ARG GLU SER ARG SER GLU
SEQRES 31 A 456 ASP VAL MET ARG ILE THR VAL GLY VAL ASP GLY SER VAL
SEQRES 32 A 456 TYR LYS LEU HIS PRO SER PHE LYS GLU ARG PHE HIS ALA
SEQRES 33 A 456 SER VAL ARG ARG LEU THR PRO SER CYS GLU ILE THR PHE
SEQRES 34 A 456 ILE GLU SER GLU GLU GLY SER GLY ARG GLY ALA ALA LEU
SEQRES 35 A 456 VAL SER ALA VAL ALA CYS LYS LYS ALA CYS MET LEU GLY
SEQRES 36 A 456 GLN
HET NA A 501 1
HET GLC A 502 12
HET 1J9 A 503 66
HETNAM NA SODIUM ION
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM 1J9 (2S)-2-{[1-(2-CHLOROPHENYL)-1H-PYRAZOLO[3,4-
HETNAM 2 1J9 D]PYRIMIDIN-4-YL]OXY}-N-(5-CHLOROPYRIDIN-2-YL)-3-(2-
HETNAM 3 1J9 HYDROXYETHOXY)PROPANAMIDE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 NA NA 1+
FORMUL 3 GLC C6 H12 O6
FORMUL 4 1J9 C21 H18 CL2 N6 O4
FORMUL 5 HOH *151(H2 O)
HELIX 1 1 SER A 11 ALA A 21 1 11
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 ALA A 51 1 6
HELIX 5 5 PRO A 111 THR A 116 1 6
HELIX 6 6 THR A 118 HIS A 137 1 20
HELIX 7 7 ASN A 180 GLY A 193 1 14
HELIX 8 8 ASN A 204 ASP A 217 1 14
HELIX 9 9 GLN A 239 VAL A 241 5 3
HELIX 10 10 GLU A 256 PHE A 260 5 5
HELIX 11 11 LEU A 266 LEU A 270 5 5
HELIX 12 12 LEU A 271 SER A 280 1 10
HELIX 13 13 GLN A 287 GLY A 294 1 8
HELIX 14 14 GLY A 294 ASP A 311 1 18
HELIX 15 15 LEU A 315 GLU A 319 5 5
HELIX 16 16 GLU A 331 GLU A 339 1 9
HELIX 17 17 ARG A 345 SER A 353 1 9
HELIX 18 18 SER A 360 SER A 396 1 37
HELIX 19 19 GLY A 410 HIS A 416 1 7
HELIX 20 20 SER A 418 THR A 431 1 14
HELIX 21 21 GLU A 443 LYS A 459 1 17
SHEET 1 A 6 LEU A 58 ARG A 63 0
SHEET 2 A 6 ARG A 250 ASN A 254 -1 O CYS A 252 N VAL A 62
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 MET A 402 ASP A 409 1 O GLY A 407 N MET A 224
SHEET 6 A 6 CYS A 434 GLU A 440 1 O ILE A 439 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 PHE A 84 O TYR A 108
SHEET 3 B 5 GLY A 72 LEU A 79 -1 N PHE A 74 O VAL A 89
SHEET 4 B 5 LEU A 144 PHE A 150 1 O THR A 149 N LEU A 77
SHEET 5 B 5 MET A 197 VAL A 203 1 O VAL A 203 N PHE A 150
SHEET 1 C 2 VAL A 154 ASP A 158 0
SHEET 2 C 2 LYS A 161 LEU A 164 -1 O LYS A 161 N GLU A 157
SSBOND 1 CYS A 213 CYS A 220 1555 1555 2.02
LINK O MET A 238 NA NA A 501 1555 1555 2.33
LINK O VAL A 241 NA NA A 501 1555 1555 2.26
LINK O VAL A 244 NA NA A 501 1555 1555 2.21
LINK O GLY A 246 NA NA A 501 1555 1555 2.62
LINK NA NA A 501 O HOH A 696 1555 1555 2.54
CRYST1 77.938 77.938 85.350 90.00 90.00 90.00 P 41 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 0.012831 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012831 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011716 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
