HEADER TRANSFERASE 17-APR-01 1IG8
TITLE CRYSTAL STRUCTURE OF YEAST HEXOKINASE PII WITH THE CORRECT
TITLE 2 AMINO ACID SEQUENCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE PII;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEXOKINASE B;
COMPND 5 EC: 2.7.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS MIXED ALPHA BETA, TWO DOMAINS, CLEFT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.R.KUSER,S.KRAUCHENCO,O.A.ANTUNES,I.POLIKARPOV
REVDAT 2 24-FEB-09 1IG8 1 VERSN
REVDAT 1 02-MAY-01 1IG8 0
JRNL AUTH P.R.KUSER,S.KRAUCHENCO,O.A.ANTUNES,I.POLIKARPOV
JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF YEAST
JRNL TITL 2 HEXOKINASE PII WITH THE CORRECT PRIMARY SEQUENCE
JRNL TITL 3 PROVIDES NEW INSIGHTS INTO ITS MECHANISM OF ACTION.
JRNL REF J.BIOL.CHEM. V. 275 20814 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10749890
JRNL DOI 10.1074/JBC.M910412199
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.KUSER,A.M.GOLUBEV,I.POLIKARPOV
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTAL ANALYSIS
REMARK 1 TITL 2 OF YEAST HEXOKINASE PI AND PII
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 2047 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444999012263
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 30146
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1368
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3671
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 441
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.40
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.141
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.011 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.033 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.036 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IG8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-01.
REMARK 100 THE RCSB ID CODE IS RCSB013246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-98
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : D03B-MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.38
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60395
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 13.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 2.120
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.82
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
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: AMORE
REMARK 200 STARTING MODEL: P152K MUTANT OF YEAST HEXOKINASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3-3.2M AMMONIUM SULPHATE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 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 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 71.40450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.40450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.23100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 71.40450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.40450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.23100
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 71.40450
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 71.40450
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 29.23100
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 71.40450
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 71.40450
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 29.23100
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 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 1
REMARK 465 VAL A 2
REMARK 465 HIS 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 GLN A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 GLY A 14
REMARK 465 SER A 15
REMARK 465 MET A 16
REMARK 465 ALA A 17
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 571 O HOH A 630 8454 2.18
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 ASP A 86 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 199 CD - NE - CZ ANGL. DEV. = 18.4 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLU A 204 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 VAL A 206 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 GLU A 225 OE1 - CD - OE2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 VAL A 278 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 GLU A 359 OE1 - CD - OE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP A 362 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 382 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 383 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 383 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 423 CD - NE - CZ ANGL. DEV. = 23.2 DEGREES
REMARK 500 ARG A 423 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 474 CD - NE - CZ ANGL. DEV. = 18.4 DEGREES
REMARK 500 ARG A 474 NE - CZ - NH2 ANGL. DEV. = -7.2 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 VAL A 19 119.87 -37.14
REMARK 500 THR A 121 158.59 -45.65
REMARK 500 SER A 158 42.75 -91.12
REMARK 500 ASP A 179 78.54 -164.27
REMARK 500 ASP A 242 -155.92 -99.87
REMARK 500 VAL A 279 -40.55 -132.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR A 121 -12.63
REMARK 500 THR A 213 -10.31
REMARK 500 VAL A 279 11.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 934 DISTANCE = 6.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YHX RELATED DB: PDB
DBREF 1IG8 A 1 486 UNP P04807 HXKB_YEAST 1 486
SEQRES 1 A 486 MET VAL HIS LEU GLY PRO LYS LYS PRO GLN ALA ARG LYS
SEQRES 2 A 486 GLY SER MET ALA ASP VAL PRO LYS GLU LEU MET GLN GLN
SEQRES 3 A 486 ILE GLU ASN PHE GLU LYS ILE PHE THR VAL PRO THR GLU
SEQRES 4 A 486 THR LEU GLN ALA VAL THR LYS HIS PHE ILE SER GLU LEU
SEQRES 5 A 486 GLU LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 A 486 ILE PRO GLY TRP VAL MET ASP PHE PRO THR GLY LYS GLU
SEQRES 7 A 486 SER GLY ASP PHE LEU ALA ILE ASP LEU GLY GLY THR ASN
SEQRES 8 A 486 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASP ARG THR
SEQRES 9 A 486 PHE ASP THR THR GLN SER LYS TYR ARG LEU PRO ASP ALA
SEQRES 10 A 486 MET ARG THR THR GLN ASN PRO ASP GLU LEU TRP GLU PHE
SEQRES 11 A 486 ILE ALA ASP SER LEU LYS ALA PHE ILE ASP GLU GLN PHE
SEQRES 12 A 486 PRO GLN GLY ILE SER GLU PRO ILE PRO LEU GLY PHE THR
SEQRES 13 A 486 PHE SER PHE PRO ALA SER GLN ASN LYS ILE ASN GLU GLY
SEQRES 14 A 486 ILE LEU GLN ARG TRP THR LYS GLY PHE ASP ILE PRO ASN
SEQRES 15 A 486 ILE GLU ASN HIS ASP VAL VAL PRO MET LEU GLN LYS GLN
SEQRES 16 A 486 ILE THR LYS ARG ASN ILE PRO ILE GLU VAL VAL ALA LEU
SEQRES 17 A 486 ILE ASN ASP THR THR GLY THR LEU VAL ALA SER TYR TYR
SEQRES 18 A 486 THR ASP PRO GLU THR LYS MET GLY VAL ILE PHE GLY THR
SEQRES 19 A 486 GLY VAL ASN GLY ALA TYR TYR ASP VAL CYS SER ASP ILE
SEQRES 20 A 486 GLU LYS LEU GLN GLY LYS LEU SER ASP ASP ILE PRO PRO
SEQRES 21 A 486 SER ALA PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE
SEQRES 22 A 486 ASP ASN GLU HIS VAL VAL LEU PRO ARG THR LYS TYR ASP
SEQRES 23 A 486 ILE THR ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN
SEQRES 24 A 486 THR PHE GLU LYS MET SER SER GLY TYR TYR LEU GLY GLU
SEQRES 25 A 486 ILE LEU ARG LEU ALA LEU MET ASP MET TYR LYS GLN GLY
SEQRES 26 A 486 PHE ILE PHE LYS ASN GLN ASP LEU SER LYS PHE ASP LYS
SEQRES 27 A 486 PRO PHE VAL MET ASP THR SER TYR PRO ALA ARG ILE GLU
SEQRES 28 A 486 GLU ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU
SEQRES 29 A 486 PHE GLN ASN GLU PHE GLY ILE ASN THR THR VAL GLN GLU
SEQRES 30 A 486 ARG LYS LEU ILE ARG ARG LEU SER GLU LEU ILE GLY ALA
SEQRES 31 A 486 ARG ALA ALA ARG LEU SER VAL CYS GLY ILE ALA ALA ILE
SEQRES 32 A 486 CYS GLN LYS ARG GLY TYR LYS THR GLY HIS ILE ALA ALA
SEQRES 33 A 486 ASP GLY SER VAL TYR ASN ARG TYR PRO GLY PHE LYS GLU
SEQRES 34 A 486 LYS ALA ALA ASN ALA LEU LYS ASP ILE TYR GLY TRP THR
SEQRES 35 A 486 GLN THR SER LEU ASP ASP TYR PRO ILE LYS ILE VAL PRO
SEQRES 36 A 486 ALA GLU ASP GLY SER GLY ALA GLY ALA ALA VAL ILE ALA
SEQRES 37 A 486 ALA LEU ALA GLN LYS ARG ILE ALA GLU GLY LYS SER VAL
SEQRES 38 A 486 GLY ILE ILE GLY ALA
HET SO4 A 501 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *441(H2 O)
HELIX 1 1 PRO A 20 THR A 35 1 16
HELIX 2 2 PRO A 37 SER A 57 1 21
HELIX 3 3 ALA A 117 THR A 121 5 5
HELIX 4 4 ASP A 125 PHE A 143 1 19
HELIX 5 5 ASP A 187 ARG A 199 1 13
HELIX 6 6 ASN A 210 ASP A 223 1 14
HELIX 7 7 SER A 245 GLN A 251 5 7
HELIX 8 8 GLU A 269 PHE A 273 5 5
HELIX 9 9 THR A 283 SER A 293 1 11
HELIX 10 10 GLN A 299 SER A 306 1 8
HELIX 11 11 TYR A 309 GLN A 324 1 16
HELIX 12 12 THR A 344 ASP A 353 1 10
HELIX 13 13 LEU A 358 GLY A 370 1 13
HELIX 14 14 THR A 374 VAL A 397 1 24
HELIX 15 15 VAL A 397 GLY A 408 1 12
HELIX 16 16 GLY A 418 TYR A 424 1 7
HELIX 17 17 GLY A 426 GLY A 440 1 15
HELIX 18 18 SER A 445 TYR A 449 5 5
HELIX 19 19 GLY A 461 GLU A 477 1 17
SHEET 1 A 6 ILE A 66 PRO A 67 0
SHEET 2 A 6 PRO A 263 ASN A 267 -1 N ASN A 267 O ILE A 66
SHEET 3 A 6 VAL A 236 VAL A 243 -1 O TYR A 240 N ILE A 266
SHEET 4 A 6 THR A 226 PHE A 232 -1 N GLY A 229 O ALA A 239
SHEET 5 A 6 GLY A 412 ASP A 417 1 O HIS A 413 N LYS A 227
SHEET 6 A 6 ILE A 451 PRO A 455 1 O LYS A 452 N ILE A 414
SHEET 1 B 5 PHE A 105 ARG A 113 0
SHEET 2 B 5 ASN A 91 GLY A 100 -1 O LEU A 92 N TYR A 112
SHEET 3 B 5 SER A 79 LEU A 87 -1 O GLY A 80 N LEU A 99
SHEET 4 B 5 ILE A 151 THR A 156 1 O PRO A 152 N LEU A 83
SHEET 5 B 5 ILE A 203 ILE A 209 1 O GLU A 204 N LEU A 153
SHEET 1 C 2 ALA A 161 SER A 162 0
SHEET 2 C 2 ILE A 170 LEU A 171 -1 N ILE A 170 O SER A 162
SITE 1 AC1 5 THR A 234 GLY A 418 SER A 419 HOH A 650
SITE 2 AC1 5 HOH A 874
CRYST1 142.809 142.809 58.462 90.00 90.00 90.00 I 4 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 0.007000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017110 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
