HEADER TRANSFERASE 19-JUL-10 3O08
TITLE CRYSTAL STRUCTURE OF DIMERIC KLHXK1 IN CRYSTAL FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 28985;
SOURCE 5 STRAIN: CBS2359/152;
SOURCE 6 GENE: KLLA0D11352G, RAG5;
SOURCE 7 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 28985;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JA6-DELTA-RAG5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PTS32X;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTSRAG5
KEYWDS RNASEH-LIKE FOLD, HEXOKINASE, GLYCOLYSIS, GLUCOSE REPRESSION, ATP
KEYWDS 2 BINDING, MIG1 BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.KUETTNER,K.KETTNER,A.KEIM,T.M.KRIEGEL,N.STRATER
REVDAT 2 29-DEC-10 3O08 1 JRNL
REVDAT 1 13-OCT-10 3O08 0
JRNL AUTH E.B.KUETTNER,K.KETTNER,A.KEIM,D.I.SVERGUN,D.VOLKE,D.SINGER,
JRNL AUTH 2 R.HOFFMANN,E.C.MULLER,A.OTTO,T.M.KRIEGEL,N.STRATER
JRNL TITL CRYSTAL STRUCTURE OF HEXOKINASE KLHXK1 OF KLUYVEROMYCES
JRNL TITL 2 LACTIS: A MOLECULAR BASIS FOR UNDERSTANDING THE CONTROL OF
JRNL TITL 3 YEAST HEXOKINASE FUNCTIONS VIA COVALENT MODIFICATION AND
JRNL TITL 4 OLIGOMERIZATION.
JRNL REF J.BIOL.CHEM. V. 285 41019 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20943665
JRNL DOI 10.1074/JBC.M110.185850
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.B.KUETTNER,T.M.KRIEGEL,A.KEIM,M.NAUMANN,STRATER N.
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 HEXOKINASE KLHXK1 FROM KLUYVEROMYCES LACTIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 430 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 DOI 17565189
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 68555
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1033
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4944
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 1.58000
REMARK 3 B33 (A**2) : -1.65000
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): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.753
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7654 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10378 ; 2.017 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 948 ; 6.493 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 327 ;37.912 ;25.229
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1336 ;16.828 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;23.938 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1149 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5655 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4715 ; 2.333 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7621 ; 3.109 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2939 ; 5.200 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2757 ; 6.974 ; 9.000
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 76
REMARK 3 RESIDUE RANGE : A 210 A 456
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9471 24.8589 57.9714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: 0.0242
REMARK 3 T33: 0.1046 T12: -0.0142
REMARK 3 T13: 0.0055 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.0344 L22: 1.9617
REMARK 3 L33: 2.2760 L12: -0.0902
REMARK 3 L13: 0.2457 L23: 1.3829
REMARK 3 S TENSOR
REMARK 3 S11: -0.0684 S12: 0.0177 S13: 0.0927
REMARK 3 S21: 0.1717 S22: -0.0537 S23: 0.0353
REMARK 3 S31: -0.1171 S32: -0.1211 S33: 0.1222
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 77 A 209
REMARK 3 RESIDUE RANGE : A 457 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): 74.3352 14.7016 39.3399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0758 T22: 0.1010
REMARK 3 T33: 0.0971 T12: 0.0267
REMARK 3 T13: 0.0098 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 3.5423 L22: 1.2064
REMARK 3 L33: 3.7181 L12: 1.2142
REMARK 3 L13: 0.9808 L23: 0.8381
REMARK 3 S TENSOR
REMARK 3 S11: -0.1386 S12: 0.0674 S13: 0.1617
REMARK 3 S21: -0.0576 S22: 0.0315 S23: -0.0840
REMARK 3 S31: -0.1878 S32: 0.2885 S33: 0.1071
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 76
REMARK 3 RESIDUE RANGE : B 210 B 456
REMARK 3 ORIGIN FOR THE GROUP (A): 84.2382 7.2424 80.5412
REMARK 3 T TENSOR
REMARK 3 T11: 0.0189 T22: 0.1254
REMARK 3 T33: 0.1286 T12: -0.0136
REMARK 3 T13: -0.0019 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.4581 L22: 0.9217
REMARK 3 L33: 5.6224 L12: 0.3809
REMARK 3 L13: -1.2909 L23: -1.5041
REMARK 3 S TENSOR
REMARK 3 S11: -0.1627 S12: 0.1613 S13: -0.0311
REMARK 3 S21: -0.0543 S22: -0.2185 S23: -0.0620
REMARK 3 S31: 0.1560 S32: 0.4944 S33: 0.3812
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 209
REMARK 3 RESIDUE RANGE : B 457 B 485
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8740 19.4260 99.0166
REMARK 3 T TENSOR
REMARK 3 T11: 0.2212 T22: 0.1557
REMARK 3 T33: 0.1667 T12: 0.0966
REMARK 3 T13: -0.0300 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.7320 L22: 3.7748
REMARK 3 L33: 5.9963 L12: -0.6360
REMARK 3 L13: 0.6181 L23: -2.4709
REMARK 3 S TENSOR
REMARK 3 S11: -0.1756 S12: 0.0984 S13: 0.1915
REMARK 3 S21: 0.3915 S22: 0.0077 S23: -0.0053
REMARK 3 S31: -0.9914 S32: -0.3116 S33: 0.1678
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 : 1.40
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. FULL B FACTORS AND ANISO RECORDS WERE COMPUTED BY CCP4
REMARK 3 PROGRAMM TLSANL.
REMARK 4
REMARK 4 3O08 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8940
REMARK 200 MONOCHROMATOR : SI - 111 TRIANGULAR CRYSTAL
REMARK 200 OPTICS : SI, COATED WITH 200 LAYERS OF
REMARK 200 MO/SI
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69639
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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 1IG8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1MICROL RESERVOIR + 1MICROL PROTEIN;
REMARK 280 RESERVOIR: 2.5M AMMONIA SULFATE, 0.1M CHES PH 9.4, PROTEIN: 10MG/
REMARK 280 ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT, 0.5MM PMSF, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 49.34600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.60950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.34600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.60950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -274.0 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 GLY A 14
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 GLY B 5
REMARK 465 PRO B 6
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 VAL A 216 CB VAL A 216 CG1 0.126
REMARK 500 VAL A 399 CB VAL A 399 CG1 0.132
REMARK 500 TYR A 426 CD1 TYR A 426 CE1 0.098
REMARK 500 TYR B 240 CE2 TYR B 240 CD2 0.094
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 ARG A 172 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 186 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 42 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU B 363 CB - CG - CD2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG B 406 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP B 416 CB - CG - OD1 ANGL. DEV. = 6.9 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 157 50.57 -93.01
REMARK 500 ALA A 160 136.65 -171.73
REMARK 500 ASN A 166 52.21 -93.14
REMARK 500 ASP A 178 68.94 -166.22
REMARK 500 PRO A 201 60.77 -68.74
REMARK 500 VAL A 278 -32.04 -140.21
REMARK 500 ALA A 411 142.75 -170.58
REMARK 500 PRO B 10 150.06 -43.44
REMARK 500 ASN B 102 55.51 -141.59
REMARK 500 PRO B 149 137.00 -30.40
REMARK 500 ASN B 166 42.47 -98.20
REMARK 500 THR B 174 -169.67 -117.59
REMARK 500 ASP B 178 24.70 -144.72
REMARK 500 ALA B 411 147.92 -171.85
REMARK 500 VAL B 480 29.38 -140.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 494
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 494
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 495
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 496
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 499
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O1B RELATED DB: PDB
REMARK 900 CRYSTAL FORM II OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O1W RELATED DB: PDB
REMARK 900 CRYSTAL FORM III OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O4W RELATED DB: PDB
REMARK 900 CRYSTAL FORM IV OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O5B RELATED DB: PDB
REMARK 900 CRYSTAL FORM VII OF KLHXK1 (DIMER) WITH GLUCOSE BOUND
REMARK 900 RELATED ID: 3O6W RELATED DB: PDB
REMARK 900 CRYSTAL FORM VIII OF KLHXK1 (MONOMER)
REMARK 900 RELATED ID: 3O8M RELATED DB: PDB
REMARK 900 CRYSTAL FORM XI OF KLHXK1 (MONONER) WITH GLUCOSE BOUND
DBREF 3O08 A 1 485 UNP P33284 HXK_KLULA 1 485
DBREF 3O08 B 1 485 UNP P33284 HXK_KLULA 1 485
SEQRES 1 A 485 MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS
SEQRES 2 A 485 GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN
SEQRES 3 A 485 ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU
SEQRES 4 A 485 LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU
SEQRES 5 A 485 ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 A 485 ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU
SEQRES 7 A 485 THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN
SEQRES 8 A 485 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP
SEQRES 9 A 485 PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS
SEQRES 10 A 485 LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE
SEQRES 11 A 485 ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO
SEQRES 12 A 485 ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE
SEQRES 13 A 485 SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL
SEQRES 14 A 485 LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL
SEQRES 15 A 485 GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE
SEQRES 16 A 485 GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE
SEQRES 17 A 485 ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR
SEQRES 18 A 485 ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY
SEQRES 19 A 485 VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU
SEQRES 20 A 485 LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP
SEQRES 21 A 485 SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP
SEQRES 22 A 485 ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL
SEQRES 23 A 485 ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA
SEQRES 24 A 485 PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE
SEQRES 25 A 485 MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE
SEQRES 26 A 485 ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA
SEQRES 27 A 485 TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP
SEQRES 28 A 485 ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE
SEQRES 29 A 485 LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG
SEQRES 30 A 485 LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG
SEQRES 31 A 485 ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS
SEQRES 32 A 485 ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP
SEQRES 33 A 485 GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS
SEQRES 34 A 485 ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL
SEQRES 35 A 485 GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA
SEQRES 36 A 485 GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS
SEQRES 37 A 485 LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY
SEQRES 38 A 485 ILE LYS GLY GLU
SEQRES 1 B 485 MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS
SEQRES 2 B 485 GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN
SEQRES 3 B 485 ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU
SEQRES 4 B 485 LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU
SEQRES 5 B 485 ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 B 485 ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU
SEQRES 7 B 485 THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN
SEQRES 8 B 485 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP
SEQRES 9 B 485 PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS
SEQRES 10 B 485 LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE
SEQRES 11 B 485 ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO
SEQRES 12 B 485 ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE
SEQRES 13 B 485 SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL
SEQRES 14 B 485 LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL
SEQRES 15 B 485 GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE
SEQRES 16 B 485 GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE
SEQRES 17 B 485 ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR
SEQRES 18 B 485 ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY
SEQRES 19 B 485 VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU
SEQRES 20 B 485 LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP
SEQRES 21 B 485 SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP
SEQRES 22 B 485 ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL
SEQRES 23 B 485 ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA
SEQRES 24 B 485 PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE
SEQRES 25 B 485 MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE
SEQRES 26 B 485 ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA
SEQRES 27 B 485 TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP
SEQRES 28 B 485 ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE
SEQRES 29 B 485 LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG
SEQRES 30 B 485 LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG
SEQRES 31 B 485 ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS
SEQRES 32 B 485 ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP
SEQRES 33 B 485 GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS
SEQRES 34 B 485 ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL
SEQRES 35 B 485 GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA
SEQRES 36 B 485 GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS
SEQRES 37 B 485 LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY
SEQRES 38 B 485 ILE LYS GLY GLU
HET SO4 A 486 5
HET SO4 A 487 5
HET SO4 A 488 5
HET SO4 A 489 5
HET SO4 A 490 5
HET SO4 A 491 5
HET SO4 A 492 5
HET SO4 A 493 5
HET SO4 A 494 5
HET NHE B 486 26
HET SO4 B 487 5
HET SO4 B 488 5
HET SO4 B 489 5
HET SO4 B 490 5
HET SO4 B 491 5
HET SO4 B 492 5
HET SO4 B 493 5
HET SO4 B 494 5
HET SO4 B 495 5
HET SO4 B 496 5
HET SO4 B 497 5
HET SO4 B 498 5
HET SO4 B 499 5
HETNAM SO4 SULFATE ION
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 3 SO4 22(O4 S 2-)
FORMUL 12 NHE C8 H17 N O3 S
FORMUL 26 HOH *400(H2 O)
HELIX 1 1 PRO A 20 THR A 35 1 16
HELIX 2 2 SER A 37 SER A 57 1 21
HELIX 3 3 PRO A 115 ARG A 119 5 5
HELIX 4 4 THR A 122 TYR A 142 1 21
HELIX 5 5 ASP A 186 LEU A 198 1 13
HELIX 6 6 ASN A 209 ASP A 222 1 14
HELIX 7 7 SER A 244 GLU A 250 5 7
HELIX 8 8 GLU A 268 PHE A 272 5 5
HELIX 9 9 THR A 282 SER A 292 1 11
HELIX 10 10 GLN A 298 SER A 305 1 8
HELIX 11 11 TYR A 308 SER A 323 1 16
HELIX 12 12 THR A 343 ASP A 352 1 10
HELIX 13 13 LEU A 357 ASN A 369 1 13
HELIX 14 14 THR A 373 GLY A 407 1 35
HELIX 15 15 GLY A 417 TYR A 423 1 7
HELIX 16 16 GLY A 425 ASN A 439 1 15
HELIX 17 17 LYS A 444 HIS A 448 5 5
HELIX 18 18 GLY A 460 GLY A 477 1 18
HELIX 19 19 PRO B 20 THR B 35 1 16
HELIX 20 20 SER B 37 LEU B 56 1 20
HELIX 21 21 PRO B 115 ARG B 119 5 5
HELIX 22 22 THR B 122 TYR B 142 1 21
HELIX 23 23 ASP B 186 LEU B 198 1 13
HELIX 24 24 ASN B 209 ASP B 222 1 14
HELIX 25 25 SER B 244 GLU B 250 5 7
HELIX 26 26 GLU B 268 PHE B 272 5 5
HELIX 27 27 THR B 282 GLU B 291 1 10
HELIX 28 28 GLN B 298 SER B 305 1 8
HELIX 29 29 TYR B 308 SER B 323 1 16
HELIX 30 30 ILE B 332 GLU B 337 5 6
HELIX 31 31 THR B 343 ASP B 352 1 10
HELIX 32 32 LEU B 357 ASN B 369 1 13
HELIX 33 33 THR B 373 GLY B 407 1 35
HELIX 34 34 GLY B 417 TYR B 423 1 7
HELIX 35 35 GLY B 425 ASN B 439 1 15
HELIX 36 36 LYS B 444 HIS B 448 5 5
HELIX 37 37 GLY B 460 GLY B 477 1 18
SHEET 1 A 6 ILE A 66 PRO A 67 0
SHEET 2 A 6 PRO A 262 ASN A 266 -1 O ASN A 266 N ILE A 66
SHEET 3 A 6 VAL A 235 VAL A 242 -1 N ASP A 241 O MET A 263
SHEET 4 A 6 THR A 225 ILE A 231 -1 N GLY A 228 O ALA A 238
SHEET 5 A 6 ALA A 411 ASP A 416 1 O ASP A 416 N ILE A 231
SHEET 6 A 6 ILE A 450 ALA A 454 1 O VAL A 453 N ALA A 415
SHEET 1 B 5 PHE A 105 ARG A 113 0
SHEET 2 B 5 ASN A 91 GLY A 100 -1 N LEU A 96 O THR A 108
SHEET 3 B 5 THR A 79 LEU A 87 -1 N PHE A 82 O VAL A 97
SHEET 4 B 5 LEU A 150 THR A 155 1 O THR A 155 N LEU A 85
SHEET 5 B 5 ILE A 202 ILE A 208 1 O ALA A 206 N PHE A 154
SHEET 1 C 2 ALA A 160 SER A 161 0
SHEET 2 C 2 VAL A 169 LEU A 170 -1 O VAL A 169 N SER A 161
SHEET 1 D 6 ILE B 66 PRO B 67 0
SHEET 2 D 6 PRO B 262 ASN B 266 -1 O ASN B 266 N ILE B 66
SHEET 3 D 6 VAL B 235 VAL B 242 -1 N TYR B 239 O ILE B 265
SHEET 4 D 6 THR B 225 ILE B 231 -1 N ILE B 230 O ASN B 236
SHEET 5 D 6 ALA B 411 ASP B 416 1 O ASP B 416 N ILE B 231
SHEET 6 D 6 ILE B 450 ALA B 454 1 O VAL B 453 N ALA B 415
SHEET 1 E 5 PHE B 105 ARG B 113 0
SHEET 2 E 5 ASN B 91 GLY B 100 -1 N LEU B 92 O TYR B 112
SHEET 3 E 5 THR B 79 LEU B 87 -1 N GLY B 80 O LEU B 99
SHEET 4 E 5 LEU B 150 PHE B 156 1 O THR B 155 N LEU B 85
SHEET 5 E 5 ILE B 202 ILE B 208 1 O ALA B 206 N PHE B 154
SHEET 1 F 2 ALA B 160 SER B 161 0
SHEET 2 F 2 VAL B 169 LEU B 170 -1 O VAL B 169 N SER B 161
SITE 1 AC1 5 GLY A 232 THR A 233 GLY A 234 GLY A 417
SITE 2 AC1 5 SER A 418
SITE 1 AC2 6 LYS A 40 SER A 128 LYS A 132 VAL A 278
SITE 2 AC2 6 PRO A 280 HOH A 555
SITE 1 AC3 7 PRO A 223 GLN A 224 LYS A 226 GLY A 407
SITE 2 AC3 7 TYR A 408 LYS A 409 THR A 410
SITE 1 AC4 5 PHE A 420 LYS A 427 VAL A 453 ALA A 454
SITE 2 AC4 5 HOH A 640
SITE 1 AC5 4 GLY A 417 SER A 418 ASN A 421 ARG A 422
SITE 1 AC6 2 GLN A 432 LYS A 435
SITE 1 AC7 4 GLY A 88 GLY A 89 THR A 90 ASN A 91
SITE 1 AC8 5 SER A 292 PRO A 293 ARG A 294 GLN A 297
SITE 2 AC8 5 LYS A 302
SITE 1 AC9 3 LYS A 444 MET A 445 HOH A 646
SITE 1 BC1 7 TYR B 73 LYS B 226 TYR B 408 SO4 B 491
SITE 2 BC1 7 HOH B 571 HOH B 614 HOH B 638
SITE 1 BC2 4 GLY B 232 THR B 233 GLY B 417 SER B 418
SITE 1 BC3 4 SER B 37 SER B 38 ARG B 393 HOH B 604
SITE 1 BC4 2 VAL B 242 ARG B 406
SITE 1 BC5 4 GLY B 417 SER B 418 ASN B 421 ARG B 422
SITE 1 BC6 6 LYS B 226 GLY B 407 TYR B 408 LYS B 409
SITE 2 BC6 6 THR B 410 NHE B 486
SITE 1 BC7 2 LYS B 444 MET B 445
SITE 1 BC8 4 PHE B 420 LYS B 427 VAL B 453 ALA B 454
SITE 1 BC9 4 SER B 292 ARG B 294 GLN B 298 LYS B 302
SITE 1 CC1 4 TYR A 112 ASN B 356 VAL B 374 ARG B 377
SITE 1 CC2 2 GLN B 432 LYS B 435
SITE 1 CC3 3 VAL B 340 TYR B 345 ASN B 367
SITE 1 CC4 4 PHE A 354 ASN B 91 HOH B 590 HOH B 648
SITE 1 CC5 4 PRO B 424 GLY B 425 GLU B 428 HOH B 548
CRYST1 98.692 113.219 91.234 90.00 90.00 90.00 P 21 21 2 8
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 0.010133 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010961 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
