HEADER HEXOKINASE 04-JUN-98 1BG3
TITLE RAT BRAIN HEXOKINASE TYPE I COMPLEX WITH GLUCOSE AND INHIBITOR
TITLE 2 GLUCOSE-6-PHOSPHATE
CAVEAT 1BG3 G6P A 1002 HAS WRONG CHIRALITY AT ATOM C1 G6P A 1004 HAS
CAVEAT 2 1BG3 WRONG CHIRALITY AT ATOM C1 G6P B 1002 HAS WRONG CHIRALITY
CAVEAT 3 1BG3 AT ATOM C1 G6P B 1004 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATP-D-HEXOSE-6-PHOSPHOTRANSFERASE;
COMPND 5 EC: 2.7.1.1;
COMPND 6 OTHER_DETAILS: BOTH MONOMERS HAVE TWO SMALL BREAKS AT KNOWN OR LIKELY
COMPND 7 TRYPSIN CLEAVAGE SITES. ALTHOUGH ENZYME IS ACTIVE AS A MONOMER,
COMPND 8 DIMERIZATION OCCURS AT HIGH PROTEIN CONCENTRATION, PARTICULARLY IN
COMPND 9 THE PRESENCE OF THE INHIBITOR G6P
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 TISSUE: BRAIN
KEYWDS HEXOKINASE, PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.MULICHAK,R.M.GARAVITO
REVDAT 6 03-APR-24 1BG3 1 REMARK
REVDAT 5 07-FEB-24 1BG3 1 HETSYN
REVDAT 4 29-JUL-20 1BG3 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 SITE
REVDAT 3 04-AUG-09 1BG3 1 ATOM COMPND CONECT HET
REVDAT 3 2 1 HETATM HETNAM LINK SITE
REVDAT 2 24-FEB-09 1BG3 1 VERSN
REVDAT 1 08-JUN-99 1BG3 0
JRNL AUTH A.M.MULICHAK,J.E.WILSON,K.PADMANABHAN,R.M.GARAVITO
JRNL TITL THE STRUCTURE OF MAMMALIAN HEXOKINASE-1.
JRNL REF NAT.STRUCT.BIOL. V. 5 555 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9665168
JRNL DOI 10.1038/811
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 71.0
REMARK 3 NUMBER OF REFLECTIONS : 46567
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2404
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 37.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1227
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
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 : 13615
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 113
REMARK 3 SOLVENT ATOMS : 234
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.00
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.770
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.320
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171713.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-97
REMARK 200 TEMPERATURE (KELVIN) : 153
REMARK 200 PH : 7.0
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MSC FOCUSSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54454
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
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) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: HEXOKINASE FROM SCHISTOSOMA MANSONI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
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 38.55000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: ALTHOUGH ENZYME IS ACTIVE AS A MONOMER, DIMERIZATION OCCURS
REMARK 300 AT HIGH PROTEIN CONCENTRATION, PARTICULARLY IN THE
REMARK 300 PRESENCE OF THE INHIBITOR G6P
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 BOTH MONOMERS HAVE TWO SMALL BREAKS AT KNOWN OR LIKELY
REMARK 400 TRYPSIN CLEAVAGE SITES.
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 ASN A 98
REMARK 465 HIS A 99
REMARK 465 GLU A 100
REMARK 465 LYS A 101
REMARK 465 ASN A 102
REMARK 465 GLN A 103
REMARK 465 GLY A 548
REMARK 465 LYS A 549
REMARK 465 LYS A 550
REMARK 465 ARG A 912
REMARK 465 GLY A 913
REMARK 465 ASP A 914
REMARK 465 PRO A 915
REMARK 465 SER A 916
REMARK 465 ILE A 917
REMARK 465 ALA A 918
REMARK 465 ASN B 98
REMARK 465 HIS B 99
REMARK 465 GLU B 100
REMARK 465 LYS B 101
REMARK 465 ASN B 102
REMARK 465 GLN B 103
REMARK 465 LYS B 141
REMARK 465 LYS B 142
REMARK 465 ILE B 143
REMARK 465 ARG B 912
REMARK 465 GLY B 913
REMARK 465 ASP B 914
REMARK 465 PRO B 915
REMARK 465 SER B 916
REMARK 465 ILE B 917
REMARK 465 ALA B 918
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 MET A 1 CG SD CE
REMARK 470 ILE A 2 CG1 CG2 CD1
REMARK 470 GLN A 5 CG CD OE1 NE2
REMARK 470 TYR A 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 17 CG OD1 OD2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 24 CG CD CE NZ
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLN A 96 CG CD OE1 NE2
REMARK 470 ASN A 104 CG OD1 ND2
REMARK 470 SER A 106 OG
REMARK 470 GLU A 108 CG CD OE1 OE2
REMARK 470 SER A 109 OG
REMARK 470 ASP A 132 CG OD1 OD2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 LYS A 146 CG CD CE NZ
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 LYS A 346 CG CD CE NZ
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 GLU A 446 CG CD OE1 OE2
REMARK 470 SER A 480 OG
REMARK 470 GLN A 482 CD OE1 NE2
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 ARG A 500 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 501 CG CD CE NZ
REMARK 470 SER A 505 OG
REMARK 470 LYS A 506 CG CD CE NZ
REMARK 470 SER A 547 OG
REMARK 470 GLU A 565 CG CD OE1 OE2
REMARK 470 ARG A 595 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 642 CG CD CE NZ
REMARK 470 GLU A 645 CG CD OE1 OE2
REMARK 470 GLU A 646 CG CD OE1 OE2
REMARK 470 LYS A 691 CG CD CE NZ
REMARK 470 GLU A 697 CG CD OE1 OE2
REMARK 470 LYS A 727 CG CD CE NZ
REMARK 470 GLU A 731 CG CD OE1 OE2
REMARK 470 ARG A 769 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 771 CG CD OE1 NE2
REMARK 470 LYS A 777 CG CD CE NZ
REMARK 470 ARG A 794 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 798 CG CD1 CD2
REMARK 470 GLN A 806 CD OE1 NE2
REMARK 470 ASN A 810 CG OD1 ND2
REMARK 470 ASP A 852 CG OD1 OD2
REMARK 470 GLN A 877 CG CD OE1 NE2
REMARK 470 LYS A 885 CG CD CE NZ
REMARK 470 VAL A 907 CG1 CG2
REMARK 470 LEU A 911 CG CD1 CD2
REMARK 470 MET B 1 CG SD CE
REMARK 470 ILE B 2 CG1 CG2 CD1
REMARK 470 GLN B 5 CG CD OE1 NE2
REMARK 470 TYR B 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 17 CG OD1 OD2
REMARK 470 LYS B 20 CG CD CE NZ
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 TYR B 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 48 CD CE NZ
REMARK 470 ARG B 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 ASN B 104 CG OD1 ND2
REMARK 470 SER B 106 OG
REMARK 470 GLU B 108 CG CD OE1 OE2
REMARK 470 SER B 109 OG
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 SER B 122 OG
REMARK 470 GLU B 139 CG CD OE1 OE2
REMARK 470 LYS B 144 CG CD CE NZ
REMARK 470 LYS B 146 CG CD CE NZ
REMARK 470 LYS B 147 CG CD CE NZ
REMARK 470 ARG B 159 CG CD NE CZ NH1 NH2
REMARK 470 SER B 161 OG
REMARK 470 LYS B 162 CG CD CE NZ
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 194 CG CD CE NZ
REMARK 470 ARG B 196 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 222 CG CD OE1 NE2
REMARK 470 ARG B 243 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 252 CG CD OE1 OE2
REMARK 470 LYS B 290 CG CD CE NZ
REMARK 470 GLU B 321 CG CD OE1 OE2
REMARK 470 GLU B 347 CG CD OE1 OE2
REMARK 470 LYS B 353 CG CD CE NZ
REMARK 470 SER B 447 OG
REMARK 470 ARG B 462 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 489 CG CD CE NZ
REMARK 470 ARG B 490 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 502 CD OE1 OE2
REMARK 470 LYS B 506 CG CD CE NZ
REMARK 470 LYS B 549 CG CD CE NZ
REMARK 470 LYS B 550 CG CD CE NZ
REMARK 470 ARG B 551 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 565 CG CD OE1 OE2
REMARK 470 GLU B 645 CG CD OE1 OE2
REMARK 470 ASP B 648 CG OD1 OD2
REMARK 470 ASP B 650 CG OD1 OD2
REMARK 470 LYS B 691 CG CD CE NZ
REMARK 470 GLU B 697 CG CD OE1 OE2
REMARK 470 GLN B 700 CG CD OE1 NE2
REMARK 470 LYS B 738 CG CD CE NZ
REMARK 470 LYS B 763 CG CD CE NZ
REMARK 470 ARG B 769 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 771 CG CD OE1 NE2
REMARK 470 LYS B 785 CG CD CE NZ
REMARK 470 ARG B 794 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 806 CG CD OE1 NE2
REMARK 470 SER B 811 OG
REMARK 470 GLN B 877 CG CD OE1 NE2
REMARK 470 LYS B 885 CD CE NZ
REMARK 470 ARG B 910 CG CD NE CZ NH1 NH2
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 254 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 279 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 279 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 279 NE - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 381 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 381 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 381 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 425 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 425 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 425 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG A 490 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 SER A 514 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO A 884 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG B 254 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 254 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 279 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 279 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG B 279 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG B 381 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 381 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG B 425 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 425 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 SER B 514 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO B 884 C - N - CA ANGL. DEV. = 10.8 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 ILE A 2 -9.89 -55.18
REMARK 500 ALA A 3 -71.90 -76.55
REMARK 500 LEU A 26 42.87 -104.08
REMARK 500 PRO A 115 162.87 -48.90
REMARK 500 GLU A 116 46.08 -73.17
REMARK 500 ASN A 117 -31.57 -143.91
REMARK 500 SER A 155 46.66 -71.33
REMARK 500 ALA A 166 74.83 -161.60
REMARK 500 LYS A 173 -111.28 63.70
REMARK 500 LYS A 176 74.67 -168.43
REMARK 500 GLN A 222 5.19 -68.90
REMARK 500 GLN A 291 38.48 39.69
REMARK 500 SER A 298 150.47 -48.07
REMARK 500 ASP A 345 -78.16 -46.29
REMARK 500 ASP A 439 66.80 -106.19
REMARK 500 LYS A 501 -72.54 -34.68
REMARK 500 PHE A 515 40.69 -77.10
REMARK 500 PRO A 520 123.79 -35.36
REMARK 500 THR A 552 138.18 -173.88
REMARK 500 ASP A 612 0.42 -68.45
REMARK 500 SER A 618 140.77 -175.19
REMARK 500 LYS A 621 -142.16 61.57
REMARK 500 LYS A 624 42.21 -152.27
REMARK 500 LYS A 642 -70.15 -61.56
REMARK 500 ASP A 719 1.20 -67.78
REMARK 500 ILE A 745 -41.94 -138.33
REMARK 500 PHE A 871 -70.64 -21.68
REMARK 500 LEU B 26 42.64 -104.46
REMARK 500 PHE B 67 40.77 -109.15
REMARK 500 SER B 155 48.31 -74.38
REMARK 500 ASP B 164 31.80 -97.95
REMARK 500 ALA B 166 75.80 -165.17
REMARK 500 LYS B 173 -112.63 61.64
REMARK 500 LYS B 176 71.96 -167.28
REMARK 500 GLN B 222 -6.86 -59.77
REMARK 500 ASP B 251 -87.33 -136.82
REMARK 500 SER B 298 150.37 -47.44
REMARK 500 ASP B 345 -84.96 -43.19
REMARK 500 ASP B 439 64.27 -105.40
REMARK 500 SER B 447 5.00 -67.30
REMARK 500 PHE B 515 40.83 -80.08
REMARK 500 PRO B 520 126.13 -33.95
REMARK 500 LYS B 550 -131.42 -108.38
REMARK 500 ARG B 551 149.66 174.62
REMARK 500 LYS B 621 -141.60 61.30
REMARK 500 LYS B 624 43.36 -154.77
REMARK 500 VAL B 651 83.23 -65.25
REMARK 500 ASP B 719 0.23 -68.09
REMARK 500 ILE B 745 -40.84 -138.81
REMARK 500 PHE B 782 76.74 -101.71
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 490 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BG3 A 1 918 UNP P05708 HXK1_RAT 1 918
DBREF 1BG3 B 1 918 UNP P05708 HXK1_RAT 1 918
SEQRES 1 A 918 MET ILE ALA ALA GLN LEU LEU ALA TYR TYR PHE THR GLU
SEQRES 2 A 918 LEU LYS ASP ASP GLN VAL LYS LYS ILE ASP LYS TYR LEU
SEQRES 3 A 918 TYR ALA MET ARG LEU SER ASP GLU ILE LEU ILE ASP ILE
SEQRES 4 A 918 LEU THR ARG PHE LYS LYS GLU MET LYS ASN GLY LEU SER
SEQRES 5 A 918 ARG ASP TYR ASN PRO THR ALA SER VAL LYS MET LEU PRO
SEQRES 6 A 918 THR PHE VAL ARG SER ILE PRO ASP GLY SER GLU LYS GLY
SEQRES 7 A 918 ASP PHE ILE ALA LEU ASP LEU GLY GLY SER SER PHE ARG
SEQRES 8 A 918 ILE LEU ARG VAL GLN VAL ASN HIS GLU LYS ASN GLN ASN
SEQRES 9 A 918 VAL SER MET GLU SER GLU ILE TYR ASP THR PRO GLU ASN
SEQRES 10 A 918 ILE VAL HIS GLY SER GLY THR GLN LEU PHE ASP HIS VAL
SEQRES 11 A 918 ALA ASP CYS LEU GLY ASP PHE MET GLU LYS LYS LYS ILE
SEQRES 12 A 918 LYS ASP LYS LYS LEU PRO VAL GLY PHE THR PHE SER PHE
SEQRES 13 A 918 PRO CYS ARG GLN SER LYS ILE ASP GLU ALA VAL LEU ILE
SEQRES 14 A 918 THR TRP THR LYS ARG PHE LYS ALA SER GLY VAL GLU GLY
SEQRES 15 A 918 ALA ASP VAL VAL LYS LEU LEU ASN LYS ALA ILE LYS LYS
SEQRES 16 A 918 ARG GLY ASP TYR ASP ALA ASN ILE VAL ALA VAL VAL ASN
SEQRES 17 A 918 ASP THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP
SEQRES 18 A 918 GLN GLN CYS GLU VAL GLY LEU ILE ILE GLY THR GLY THR
SEQRES 19 A 918 ASN ALA CYS TYR MET GLU GLU LEU ARG HIS ILE ASP LEU
SEQRES 20 A 918 VAL GLU GLY ASP GLU GLY ARG MET CYS ILE ASN THR GLU
SEQRES 21 A 918 TRP GLY ALA PHE GLY ASP ASP GLY SER LEU GLU ASP ILE
SEQRES 22 A 918 ARG THR GLU PHE ASP ARG GLU LEU ASP ARG GLY SER LEU
SEQRES 23 A 918 ASN PRO GLY LYS GLN LEU PHE GLU LYS MET VAL SER GLY
SEQRES 24 A 918 MET TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS
SEQRES 25 A 918 MET ALA LYS GLU GLY LEU LEU PHE GLU GLY ARG ILE THR
SEQRES 26 A 918 PRO GLU LEU LEU THR ARG GLY LYS PHE ASN THR SER ASP
SEQRES 27 A 918 VAL SER ALA ILE GLU LYS ASP LYS GLU GLY ILE GLN ASN
SEQRES 28 A 918 ALA LYS GLU ILE LEU THR ARG LEU GLY VAL GLU PRO SER
SEQRES 29 A 918 ASP VAL ASP CYS VAL SER VAL GLN HIS ILE CYS THR ILE
SEQRES 30 A 918 VAL SER PHE ARG SER ALA ASN LEU VAL ALA ALA THR LEU
SEQRES 31 A 918 GLY ALA ILE LEU ASN ARG LEU ARG ASP ASN LYS GLY THR
SEQRES 32 A 918 PRO ARG LEU ARG THR THR VAL GLY VAL ASP GLY SER LEU
SEQRES 33 A 918 TYR LYS MET HIS PRO GLN TYR SER ARG ARG PHE HIS LYS
SEQRES 34 A 918 THR LEU ARG ARG LEU VAL PRO ASP SER ASP VAL ARG PHE
SEQRES 35 A 918 LEU LEU SER GLU SER GLY THR GLY LYS GLY ALA ALA MET
SEQRES 36 A 918 VAL THR ALA VAL ALA TYR ARG LEU ALA GLU GLN HIS ARG
SEQRES 37 A 918 GLN ILE GLU GLU THR LEU ALA HIS PHE ARG LEU SER LYS
SEQRES 38 A 918 GLN THR LEU MET GLU VAL LYS LYS ARG LEU ARG THR GLU
SEQRES 39 A 918 MET GLU MET GLY LEU ARG LYS GLU THR ASN SER LYS ALA
SEQRES 40 A 918 THR VAL LYS MET LEU PRO SER PHE VAL ARG SER ILE PRO
SEQRES 41 A 918 ASP GLY THR GLU HIS GLY ASP PHE LEU ALA LEU ASP LEU
SEQRES 42 A 918 GLY GLY THR ASN PHE ARG VAL LEU LEU VAL LYS ILE ARG
SEQRES 43 A 918 SER GLY LYS LYS ARG THR VAL GLU MET HIS ASN LYS ILE
SEQRES 44 A 918 TYR SER ILE PRO LEU GLU ILE MET GLN GLY THR GLY ASP
SEQRES 45 A 918 GLU LEU PHE ASP HIS ILE VAL SER CYS ILE SER ASP PHE
SEQRES 46 A 918 LEU ASP TYR MET GLY ILE LYS GLY PRO ARG MET PRO LEU
SEQRES 47 A 918 GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR ASN LEU
SEQRES 48 A 918 ASP CYS GLY ILE LEU ILE SER TRP THR LYS GLY PHE LYS
SEQRES 49 A 918 ALA THR ASP CYS GLU GLY HIS ASP VAL ALA SER LEU LEU
SEQRES 50 A 918 ARG ASP ALA VAL LYS ARG ARG GLU GLU PHE ASP LEU ASP
SEQRES 51 A 918 VAL VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET
SEQRES 52 A 918 THR CYS ALA TYR GLU GLU PRO THR CYS GLU ILE GLY LEU
SEQRES 53 A 918 ILE VAL GLY THR GLY THR ASN ALA CYS TYR MET GLU GLU
SEQRES 54 A 918 MET LYS ASN VAL GLU MET VAL GLU GLY ASN GLN GLY GLN
SEQRES 55 A 918 MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASN
SEQRES 56 A 918 GLY CYS LEU ASP ASP ILE ARG THR ASP PHE ASP LYS VAL
SEQRES 57 A 918 VAL ASP GLU TYR SER LEU ASN SER GLY LYS GLN ARG PHE
SEQRES 58 A 918 GLU LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL
SEQRES 59 A 918 ARG ASN ILE LEU ILE ASP PHE THR LYS LYS GLY PHE LEU
SEQRES 60 A 918 PHE ARG GLY GLN ILE SER GLU PRO LEU LYS THR ARG GLY
SEQRES 61 A 918 ILE PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP
SEQRES 62 A 918 ARG LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN GLN
SEQRES 63 A 918 LEU GLY LEU ASN SER THR CYS ASP ASP SER ILE LEU VAL
SEQRES 64 A 918 LYS THR VAL CYS GLY VAL VAL SER LYS ARG ALA ALA GLN
SEQRES 65 A 918 LEU CYS GLY ALA GLY MET ALA ALA VAL VAL GLU LYS ILE
SEQRES 66 A 918 ARG GLU ASN ARG GLY LEU ASP HIS LEU ASN VAL THR VAL
SEQRES 67 A 918 GLY VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE
SEQRES 68 A 918 SER ARG ILE MET HIS GLN THR VAL LYS GLU LEU SER PRO
SEQRES 69 A 918 LYS CYS THR VAL SER PHE LEU LEU SER GLU ASP GLY SER
SEQRES 70 A 918 GLY LYS GLY ALA ALA LEU ILE THR ALA VAL GLY VAL ARG
SEQRES 71 A 918 LEU ARG GLY ASP PRO SER ILE ALA
SEQRES 1 B 918 MET ILE ALA ALA GLN LEU LEU ALA TYR TYR PHE THR GLU
SEQRES 2 B 918 LEU LYS ASP ASP GLN VAL LYS LYS ILE ASP LYS TYR LEU
SEQRES 3 B 918 TYR ALA MET ARG LEU SER ASP GLU ILE LEU ILE ASP ILE
SEQRES 4 B 918 LEU THR ARG PHE LYS LYS GLU MET LYS ASN GLY LEU SER
SEQRES 5 B 918 ARG ASP TYR ASN PRO THR ALA SER VAL LYS MET LEU PRO
SEQRES 6 B 918 THR PHE VAL ARG SER ILE PRO ASP GLY SER GLU LYS GLY
SEQRES 7 B 918 ASP PHE ILE ALA LEU ASP LEU GLY GLY SER SER PHE ARG
SEQRES 8 B 918 ILE LEU ARG VAL GLN VAL ASN HIS GLU LYS ASN GLN ASN
SEQRES 9 B 918 VAL SER MET GLU SER GLU ILE TYR ASP THR PRO GLU ASN
SEQRES 10 B 918 ILE VAL HIS GLY SER GLY THR GLN LEU PHE ASP HIS VAL
SEQRES 11 B 918 ALA ASP CYS LEU GLY ASP PHE MET GLU LYS LYS LYS ILE
SEQRES 12 B 918 LYS ASP LYS LYS LEU PRO VAL GLY PHE THR PHE SER PHE
SEQRES 13 B 918 PRO CYS ARG GLN SER LYS ILE ASP GLU ALA VAL LEU ILE
SEQRES 14 B 918 THR TRP THR LYS ARG PHE LYS ALA SER GLY VAL GLU GLY
SEQRES 15 B 918 ALA ASP VAL VAL LYS LEU LEU ASN LYS ALA ILE LYS LYS
SEQRES 16 B 918 ARG GLY ASP TYR ASP ALA ASN ILE VAL ALA VAL VAL ASN
SEQRES 17 B 918 ASP THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP
SEQRES 18 B 918 GLN GLN CYS GLU VAL GLY LEU ILE ILE GLY THR GLY THR
SEQRES 19 B 918 ASN ALA CYS TYR MET GLU GLU LEU ARG HIS ILE ASP LEU
SEQRES 20 B 918 VAL GLU GLY ASP GLU GLY ARG MET CYS ILE ASN THR GLU
SEQRES 21 B 918 TRP GLY ALA PHE GLY ASP ASP GLY SER LEU GLU ASP ILE
SEQRES 22 B 918 ARG THR GLU PHE ASP ARG GLU LEU ASP ARG GLY SER LEU
SEQRES 23 B 918 ASN PRO GLY LYS GLN LEU PHE GLU LYS MET VAL SER GLY
SEQRES 24 B 918 MET TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS
SEQRES 25 B 918 MET ALA LYS GLU GLY LEU LEU PHE GLU GLY ARG ILE THR
SEQRES 26 B 918 PRO GLU LEU LEU THR ARG GLY LYS PHE ASN THR SER ASP
SEQRES 27 B 918 VAL SER ALA ILE GLU LYS ASP LYS GLU GLY ILE GLN ASN
SEQRES 28 B 918 ALA LYS GLU ILE LEU THR ARG LEU GLY VAL GLU PRO SER
SEQRES 29 B 918 ASP VAL ASP CYS VAL SER VAL GLN HIS ILE CYS THR ILE
SEQRES 30 B 918 VAL SER PHE ARG SER ALA ASN LEU VAL ALA ALA THR LEU
SEQRES 31 B 918 GLY ALA ILE LEU ASN ARG LEU ARG ASP ASN LYS GLY THR
SEQRES 32 B 918 PRO ARG LEU ARG THR THR VAL GLY VAL ASP GLY SER LEU
SEQRES 33 B 918 TYR LYS MET HIS PRO GLN TYR SER ARG ARG PHE HIS LYS
SEQRES 34 B 918 THR LEU ARG ARG LEU VAL PRO ASP SER ASP VAL ARG PHE
SEQRES 35 B 918 LEU LEU SER GLU SER GLY THR GLY LYS GLY ALA ALA MET
SEQRES 36 B 918 VAL THR ALA VAL ALA TYR ARG LEU ALA GLU GLN HIS ARG
SEQRES 37 B 918 GLN ILE GLU GLU THR LEU ALA HIS PHE ARG LEU SER LYS
SEQRES 38 B 918 GLN THR LEU MET GLU VAL LYS LYS ARG LEU ARG THR GLU
SEQRES 39 B 918 MET GLU MET GLY LEU ARG LYS GLU THR ASN SER LYS ALA
SEQRES 40 B 918 THR VAL LYS MET LEU PRO SER PHE VAL ARG SER ILE PRO
SEQRES 41 B 918 ASP GLY THR GLU HIS GLY ASP PHE LEU ALA LEU ASP LEU
SEQRES 42 B 918 GLY GLY THR ASN PHE ARG VAL LEU LEU VAL LYS ILE ARG
SEQRES 43 B 918 SER GLY LYS LYS ARG THR VAL GLU MET HIS ASN LYS ILE
SEQRES 44 B 918 TYR SER ILE PRO LEU GLU ILE MET GLN GLY THR GLY ASP
SEQRES 45 B 918 GLU LEU PHE ASP HIS ILE VAL SER CYS ILE SER ASP PHE
SEQRES 46 B 918 LEU ASP TYR MET GLY ILE LYS GLY PRO ARG MET PRO LEU
SEQRES 47 B 918 GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR ASN LEU
SEQRES 48 B 918 ASP CYS GLY ILE LEU ILE SER TRP THR LYS GLY PHE LYS
SEQRES 49 B 918 ALA THR ASP CYS GLU GLY HIS ASP VAL ALA SER LEU LEU
SEQRES 50 B 918 ARG ASP ALA VAL LYS ARG ARG GLU GLU PHE ASP LEU ASP
SEQRES 51 B 918 VAL VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET
SEQRES 52 B 918 THR CYS ALA TYR GLU GLU PRO THR CYS GLU ILE GLY LEU
SEQRES 53 B 918 ILE VAL GLY THR GLY THR ASN ALA CYS TYR MET GLU GLU
SEQRES 54 B 918 MET LYS ASN VAL GLU MET VAL GLU GLY ASN GLN GLY GLN
SEQRES 55 B 918 MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASN
SEQRES 56 B 918 GLY CYS LEU ASP ASP ILE ARG THR ASP PHE ASP LYS VAL
SEQRES 57 B 918 VAL ASP GLU TYR SER LEU ASN SER GLY LYS GLN ARG PHE
SEQRES 58 B 918 GLU LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL
SEQRES 59 B 918 ARG ASN ILE LEU ILE ASP PHE THR LYS LYS GLY PHE LEU
SEQRES 60 B 918 PHE ARG GLY GLN ILE SER GLU PRO LEU LYS THR ARG GLY
SEQRES 61 B 918 ILE PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP
SEQRES 62 B 918 ARG LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN GLN
SEQRES 63 B 918 LEU GLY LEU ASN SER THR CYS ASP ASP SER ILE LEU VAL
SEQRES 64 B 918 LYS THR VAL CYS GLY VAL VAL SER LYS ARG ALA ALA GLN
SEQRES 65 B 918 LEU CYS GLY ALA GLY MET ALA ALA VAL VAL GLU LYS ILE
SEQRES 66 B 918 ARG GLU ASN ARG GLY LEU ASP HIS LEU ASN VAL THR VAL
SEQRES 67 B 918 GLY VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE
SEQRES 68 B 918 SER ARG ILE MET HIS GLN THR VAL LYS GLU LEU SER PRO
SEQRES 69 B 918 LYS CYS THR VAL SER PHE LEU LEU SER GLU ASP GLY SER
SEQRES 70 B 918 GLY LYS GLY ALA ALA LEU ILE THR ALA VAL GLY VAL ARG
SEQRES 71 B 918 LEU ARG GLY ASP PRO SER ILE ALA
HET BGC A1001 12
HET G6P A1002 16
HET BGC A1003 12
HET G6P A1004 16
HET CA A1005 1
HET BGC B1001 12
HET G6P B1002 16
HET BGC B1003 12
HET G6P B1004 16
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM G6P 6-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN G6P ALPHA-D-GLUCOSE-6-PHOSPHATE; 6-O-PHOSPHONO-ALPHA-D-
HETSYN 2 G6P GLUCOSE; 6-O-PHOSPHONO-D-GLUCOSE; 6-O-PHOSPHONO-
HETSYN 3 G6P GLUCOSE
FORMUL 3 BGC 4(C6 H12 O6)
FORMUL 4 G6P 4(C6 H13 O9 P)
FORMUL 7 CA CA 2+
FORMUL 12 HOH *234(H2 O)
HELIX 1 1 ILE A 2 TYR A 25 1 24
HELIX 2 2 TYR A 27 MET A 29 5 3
HELIX 3 3 ASP A 33 LEU A 51 1 19
HELIX 4 4 ARG A 53 THR A 58 1 6
HELIX 5 5 GLY A 123 LYS A 141 1 19
HELIX 6 6 VAL A 185 ARG A 196 1 12
HELIX 7 7 ASP A 209 ASP A 220 1 12
HELIX 8 8 LEU A 242 HIS A 244 5 3
HELIX 9 9 TRP A 261 ALA A 263 5 3
HELIX 10 10 GLU A 276 ARG A 283 1 8
HELIX 11 11 GLU A 294 VAL A 297 1 4
HELIX 12 12 MET A 302 LYS A 315 1 14
HELIX 13 13 PRO A 326 LEU A 329 1 4
HELIX 14 14 THR A 336 ILE A 342 1 7
HELIX 15 15 GLY A 348 ARG A 358 1 11
HELIX 16 16 ASP A 365 LYS A 401 1 37
HELIX 17 17 SER A 415 MET A 419 1 5
HELIX 18 18 TYR A 423 LEU A 434 1 12
HELIX 19 19 GLY A 450 PHE A 477 1 28
HELIX 20 20 LYS A 481 LEU A 499 1 19
HELIX 21 21 LYS A 501 LYS A 506 1 6
HELIX 22 22 LEU A 564 MET A 567 1 4
HELIX 23 23 GLY A 571 MET A 589 1 19
HELIX 24 24 VAL A 633 ARG A 644 1 12
HELIX 25 25 ASP A 657 ALA A 666 1 10
HELIX 26 26 MET A 690 ASN A 692 5 3
HELIX 27 27 TRP A 709 ALA A 711 5 3
HELIX 28 28 ASP A 724 GLU A 731 1 8
HELIX 29 29 ARG A 740 MET A 744 1 5
HELIX 30 30 LEU A 750 LYS A 763 1 14
HELIX 31 31 GLU A 774 LYS A 777 1 4
HELIX 32 32 THR A 784 ILE A 790 1 7
HELIX 33 33 LEU A 797 GLN A 806 1 10
HELIX 34 34 CYS A 813 ASN A 848 1 36
HELIX 35 35 THR A 863 LEU A 867 1 5
HELIX 36 36 PHE A 871 LEU A 882 1 12
HELIX 37 37 GLY A 896 VAL A 909 1 14
HELIX 38 38 ILE B 2 TYR B 25 1 24
HELIX 39 39 TYR B 27 MET B 29 5 3
HELIX 40 40 ASP B 33 LEU B 51 1 19
HELIX 41 41 ARG B 53 THR B 58 1 6
HELIX 42 42 GLU B 116 VAL B 119 1 4
HELIX 43 43 GLY B 123 GLU B 139 1 17
HELIX 44 44 VAL B 185 ARG B 196 1 12
HELIX 45 45 ASP B 209 ASP B 220 1 12
HELIX 46 46 LEU B 242 HIS B 244 5 3
HELIX 47 47 TRP B 261 ALA B 263 5 3
HELIX 48 48 GLU B 276 GLY B 284 1 9
HELIX 49 49 GLU B 294 VAL B 297 1 4
HELIX 50 50 MET B 302 GLU B 316 1 15
HELIX 51 51 PRO B 326 LEU B 329 1 4
HELIX 52 52 THR B 336 ILE B 342 1 7
HELIX 53 53 GLU B 347 ARG B 358 5 12
HELIX 54 54 ASP B 365 LYS B 401 1 37
HELIX 55 55 SER B 415 MET B 419 1 5
HELIX 56 56 TYR B 423 LEU B 434 1 12
HELIX 57 57 GLY B 450 PHE B 477 1 28
HELIX 58 58 LYS B 481 LEU B 499 1 19
HELIX 59 59 LYS B 501 ASN B 504 1 4
HELIX 60 60 LEU B 564 MET B 567 1 4
HELIX 61 61 GLY B 571 MET B 589 1 19
HELIX 62 62 VAL B 633 ARG B 644 1 12
HELIX 63 63 ASP B 657 GLU B 668 1 12
HELIX 64 64 TRP B 709 ALA B 711 5 3
HELIX 65 65 ASP B 724 GLU B 731 1 8
HELIX 66 66 ARG B 740 LYS B 743 1 4
HELIX 67 67 LEU B 750 LYS B 763 1 14
HELIX 68 68 GLU B 774 LYS B 777 1 4
HELIX 69 69 THR B 784 ILE B 790 1 7
HELIX 70 70 LEU B 797 GLN B 806 1 10
HELIX 71 71 CYS B 813 ASN B 848 1 36
HELIX 72 72 THR B 863 LEU B 867 1 5
HELIX 73 73 PHE B 871 LEU B 882 1 12
HELIX 74 74 GLY B 896 GLY B 908 1 13
SHEET 1 A 5 ASN A 202 VAL A 207 0
SHEET 2 A 5 PRO A 149 PHE A 154 1 N VAL A 150 O ASN A 202
SHEET 3 A 5 GLY A 78 LEU A 85 1 N ILE A 81 O GLY A 151
SHEET 4 A 5 ARG A 91 VAL A 97 -1 N VAL A 97 O GLY A 78
SHEET 5 A 5 SER A 106 GLU A 108 -1 N GLU A 108 O ARG A 94
SHEET 1 B 5 ARG A 254 ASN A 258 0
SHEET 2 B 5 THR A 234 GLU A 241 -1 N GLU A 240 O MET A 255
SHEET 3 B 5 CYS A 224 ILE A 230 -1 N ILE A 229 O ASN A 235
SHEET 4 B 5 THR A 409 ASP A 413 1 N THR A 409 O GLU A 225
SHEET 5 B 5 ARG A 441 LEU A 444 1 N ARG A 441 O VAL A 410
SHEET 1 C 6 MET A 511 PRO A 513 0
SHEET 2 C 6 GLN A 702 MET A 707 -1 N ASN A 706 O LEU A 512
SHEET 3 C 6 THR A 682 GLU A 689 -1 N GLU A 688 O MET A 703
SHEET 4 C 6 CYS A 672 VAL A 678 -1 N ILE A 677 O ASN A 683
SHEET 5 C 6 THR A 857 ASP A 861 1 N THR A 857 O GLU A 673
SHEET 6 C 6 SER A 889 LEU A 892 1 N SER A 889 O VAL A 858
SHEET 1 D 5 LEU A 649 VAL A 655 0
SHEET 2 D 5 MET A 596 PHE A 602 1 N MET A 596 O ASP A 650
SHEET 3 D 5 GLY A 526 LEU A 533 1 N LEU A 529 O GLY A 599
SHEET 4 D 5 ARG A 539 ILE A 545 -1 N ILE A 545 O GLY A 526
SHEET 5 D 5 VAL A 553 ILE A 559 -1 N LYS A 558 O VAL A 540
SHEET 1 E 2 PRO A 157 ARG A 159 0
SHEET 2 E 2 VAL A 167 THR A 170 -1 N THR A 170 O PRO A 157
SHEET 1 F 2 PRO A 605 HIS A 607 0
SHEET 2 F 2 ILE A 615 SER A 618 -1 N SER A 618 O PRO A 605
SHEET 1 G 5 ASN B 202 VAL B 207 0
SHEET 2 G 5 PRO B 149 PHE B 154 1 N VAL B 150 O ASN B 202
SHEET 3 G 5 ASP B 79 LEU B 85 1 N ILE B 81 O GLY B 151
SHEET 4 G 5 ARG B 91 GLN B 96 -1 N VAL B 95 O PHE B 80
SHEET 5 G 5 SER B 106 GLU B 108 -1 N GLU B 108 O ARG B 94
SHEET 1 H 5 ARG B 254 ASN B 258 0
SHEET 2 H 5 THR B 234 GLU B 241 -1 N GLU B 240 O MET B 255
SHEET 3 H 5 CYS B 224 ILE B 230 -1 N ILE B 229 O ASN B 235
SHEET 4 H 5 ARG B 407 ASP B 413 1 N THR B 409 O GLU B 225
SHEET 5 H 5 ASP B 439 LEU B 444 1 N ASP B 439 O THR B 408
SHEET 1 I 6 MET B 511 PRO B 513 0
SHEET 2 I 6 GLN B 702 MET B 707 -1 N ASN B 706 O LEU B 512
SHEET 3 I 6 THR B 682 GLU B 689 -1 N GLU B 688 O MET B 703
SHEET 4 I 6 CYS B 672 VAL B 678 -1 N ILE B 677 O ASN B 683
SHEET 5 I 6 LEU B 854 ASP B 861 1 N THR B 857 O GLU B 673
SHEET 6 I 6 CYS B 886 LEU B 892 1 N THR B 887 O LEU B 854
SHEET 1 J 5 LEU B 649 VAL B 655 0
SHEET 2 J 5 MET B 596 PHE B 602 1 N MET B 596 O ASP B 650
SHEET 3 J 5 GLY B 526 LEU B 533 1 N LEU B 529 O GLY B 599
SHEET 4 J 5 ARG B 539 SER B 547 -1 N ILE B 545 O GLY B 526
SHEET 5 J 5 ARG B 551 ILE B 559 -1 N LYS B 558 O VAL B 540
SHEET 1 K 2 PRO B 157 ARG B 159 0
SHEET 2 K 2 VAL B 167 THR B 170 -1 N THR B 170 O PRO B 157
SHEET 1 L 2 PRO B 605 HIS B 607 0
SHEET 2 L 2 ILE B 615 SER B 618 -1 N SER B 618 O PRO B 605
LINK CA CA A1005 OD2 ASP B 365 1555 1555 3.25
CRYST1 132.100 77.100 137.100 90.00 96.00 90.00 P 1 21 1 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 0.007570 0.000000 0.000796 0.00000
SCALE2 0.000000 0.012970 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007334 0.00000
MTRIX1 1 -0.999992 0.001479 -0.003776 2.40960 1
MTRIX2 1 -0.002470 -0.960616 0.277870 -45.78030 1
MTRIX3 1 -0.003216 0.277877 0.960610 6.54780 1
(ATOM LINES ARE NOT SHOWN.)
END