HEADER TRANSFERASE 29-FEB-08 2ZJ4
TITLE ISOMERASE DOMAIN OF HUMAN GLUCOSE:FRUCTOSE-6-PHOSPHATE
TITLE 2 AMIDOTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE
COMPND 3 AMINOTRANSFERASE [ISOMERIZING] 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SIS(SUGAR ISOMERASE) DOMAINS, UNP RESIDUES 332-
COMPND 6 699;
COMPND 7 SYNONYM: GLUTAMINE:FRUCTOSE 6 PHOSPHATE AMIDOTRANSFERASE 1,
COMPND 8 HEXOSEPHOSPHATE AMINOTRANSFERASE 1, D-FRUCTOSE-6-PHOSPHATE
COMPND 9 AMIDOTRANSFERASE 1, GFAT 1, GFAT1;
COMPND 10 EC: 2.6.1.16;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23
KEYWDS GLUCOSAMINE-6-PHOSPHATE SYNTHASE, ALDOSE/KETOSE ISOMERASE,
KEYWDS 2 CRYSTAL STRUCTURE, ROSSMANN-LIKE FOLD, TRANSFERASE,
KEYWDS 3 ALTERNATIVE SPLICING, AMINOTRANSFERASE, GLUTAMINE
KEYWDS 4 AMIDOTRANSFERASE, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKAISHI,M.BANDO,K.KONDO,H.TSUGE
REVDAT 1 13-JAN-09 2ZJ4 0
JRNL AUTH Y.NAKAISHI,M.BANDO,H.SHIMIZU,K.WATANABE,F.GOTO,
JRNL AUTH 2 H.TSUGE,K.KONDO,M.KOMATSU
JRNL TITL STRUCTURAL ANALYSIS OF HUMAN
JRNL TITL 2 GLUTAMINE:FRUCTOSE-6-PHOSPHATE AMIDOTRANSFERASE, A
JRNL TITL 3 KEY REGULATOR IN TYPE 2 DIABETES
JRNL REF FEBS LETT. V. 583 163 2009
JRNL REFN ISSN 0014-5793
JRNL PMID 19059404
JRNL DOI 10.1016/J.FEBSLET.2008.11.041
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 21357
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1144
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1560
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.1460
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2863
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 267
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
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): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2920 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2003 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3937 ; 1.778 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4906 ; 1.454 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 364 ; 6.404 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;32.790 ;23.871
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 555 ;15.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.724 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 464 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3173 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 562 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 584 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1997 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1380 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1404 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 178 ; 0.185 ; 0.200
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): 15 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.289 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.240 ; 0.200
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): 2368 ; 1.437 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 742 ; 0.238 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2940 ; 1.612 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1246 ; 3.106 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 997 ; 4.334 ; 4.500
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 : NULL
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2ZJ4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB028036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL32B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 39.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2ZJ3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% ISOPORPANOL, 0.04M TRIS, 0.08M
REMARK 280 AMMONIUM ACETATE, 12% GLYCEROL 10-FOLD EXCESS OF 2-DEOXY-2-
REMARK 280 AMINOGLUCITOL-6-PHOSPHATE, PH 8.50, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -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 39.46350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 39.46350
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 138.66150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.33075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.46350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 207.99225
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 207.99225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.46350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.33075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 39.46350
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 138.66150
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 39.46350
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 138.66150
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 39.46350
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 207.99225
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 69.33075
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 39.46350
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 69.33075
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 207.99225
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 39.46350
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 39.46350
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 138.66150
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: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 78.92700
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 78.92700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 883 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 887 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 929 LIES ON A SPECIAL POSITION.
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 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 GLN A 313
REMARK 465 GLN A 314
REMARK 465 ILE A 315
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 722 O HOH A 844 2.08
REMARK 500 O HOH A 877 O HOH A 922 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 396 CG MET A 396 SD 0.165
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 502 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 502 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 594 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 663 NE - CZ - NH1 ANGL. DEV. = -4.0 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 ASN A 319 -25.38 108.30
REMARK 500 ARG A 342 -50.53 -129.43
REMARK 500 SER A 420 117.54 -161.55
REMARK 500 THR A 474 -82.58 -132.69
REMARK 500 ASP A 595 -164.96 -127.48
REMARK 500 GLN A 612 4.82 80.74
REMARK 500 VAL A 679 -78.63 -112.08
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 HIS A 547 0.06 SIDE_CHAIN
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 845 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH A 910 DISTANCE = 5.41 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGP A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZJ3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ALPHA-D-GLUCOSE-6-PHOSPHATE
DBREF 2ZJ4 A 313 680 UNP Q06210 GFPT1_HUMAN 332 699
SEQADV 2ZJ4 MET A 306 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 307 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 308 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 309 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 310 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 311 UNP Q06210 EXPRESSION TAG
SEQADV 2ZJ4 HIS A 312 UNP Q06210 EXPRESSION TAG
SEQRES 1 A 375 MET HIS HIS HIS HIS HIS HIS GLN GLN ILE MET LYS GLY
SEQRES 2 A 375 ASN PHE SER SER PHE MET GLN LYS GLU ILE PHE GLU GLN
SEQRES 3 A 375 PRO GLU SER VAL VAL ASN THR MET ARG GLY ARG VAL ASN
SEQRES 4 A 375 PHE ASP ASP TYR THR VAL ASN LEU GLY GLY LEU LYS ASP
SEQRES 5 A 375 HIS ILE LYS GLU ILE GLN ARG CYS ARG ARG LEU ILE LEU
SEQRES 6 A 375 ILE ALA CYS GLY THR SER TYR HIS ALA GLY VAL ALA THR
SEQRES 7 A 375 ARG GLN VAL LEU GLU GLU LEU THR GLU LEU PRO VAL MET
SEQRES 8 A 375 VAL GLU LEU ALA SER ASP PHE LEU ASP ARG ASN THR PRO
SEQRES 9 A 375 VAL PHE ARG ASP ASP VAL CYS PHE PHE LEU SER GLN SER
SEQRES 10 A 375 GLY GLU THR ALA ASP THR LEU MET GLY LEU ARG TYR CYS
SEQRES 11 A 375 LYS GLU ARG GLY ALA LEU THR VAL GLY ILE THR ASN THR
SEQRES 12 A 375 VAL GLY SER SER ILE SER ARG GLU THR ASP CYS GLY VAL
SEQRES 13 A 375 HIS ILE ASN ALA GLY PRO GLU ILE GLY VAL ALA SER THR
SEQRES 14 A 375 LYS ALA TYR THR SER GLN PHE VAL SER LEU VAL MET PHE
SEQRES 15 A 375 ALA LEU MET MET CYS ASP ASP ARG ILE SER MET GLN GLU
SEQRES 16 A 375 ARG ARG LYS GLU ILE MET LEU GLY LEU LYS ARG LEU PRO
SEQRES 17 A 375 ASP LEU ILE LYS GLU VAL LEU SER MET ASP ASP GLU ILE
SEQRES 18 A 375 GLN LYS LEU ALA THR GLU LEU TYR HIS GLN LYS SER VAL
SEQRES 19 A 375 LEU ILE MET GLY ARG GLY TYR HIS TYR ALA THR CYS LEU
SEQRES 20 A 375 GLU GLY ALA LEU LYS ILE LYS GLU ILE THR TYR MET HIS
SEQRES 21 A 375 SER GLU GLY ILE LEU ALA GLY GLU LEU LYS HIS GLY PRO
SEQRES 22 A 375 LEU ALA LEU VAL ASP LYS LEU MET PRO VAL ILE MET ILE
SEQRES 23 A 375 ILE MET ARG ASP HIS THR TYR ALA LYS CYS GLN ASN ALA
SEQRES 24 A 375 LEU GLN GLN VAL VAL ALA ARG GLN GLY ARG PRO VAL VAL
SEQRES 25 A 375 ILE CYS ASP LYS GLU ASP THR GLU THR ILE LYS ASN THR
SEQRES 26 A 375 LYS ARG THR ILE LYS VAL PRO HIS SER VAL ASP CYS LEU
SEQRES 27 A 375 GLN GLY ILE LEU SER VAL ILE PRO LEU GLN LEU LEU ALA
SEQRES 28 A 375 PHE HIS LEU ALA VAL LEU ARG GLY TYR ASP VAL ASP PHE
SEQRES 29 A 375 PRO ARG ASN LEU ALA LYS SER VAL THR VAL GLU
HET AGP A 1 16
HETNAM AGP 2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE
FORMUL 2 AGP C6 H16 N O8 P
FORMUL 3 HOH *267(H2 O)
HELIX 1 1 SER A 322 GLU A 330 1 9
HELIX 2 2 GLU A 330 ARG A 340 1 11
HELIX 3 3 LEU A 352 LYS A 356 5 5
HELIX 4 4 HIS A 358 CYS A 365 1 8
HELIX 5 5 CYS A 373 GLU A 392 1 20
HELIX 6 6 ALA A 400 ARG A 406 1 7
HELIX 7 7 THR A 425 ARG A 438 1 14
HELIX 8 8 SER A 451 THR A 457 1 7
HELIX 9 9 THR A 474 CYS A 492 1 19
HELIX 10 10 ARG A 495 SER A 497 5 3
HELIX 11 11 MET A 498 SER A 521 1 24
HELIX 12 12 MET A 522 TYR A 534 1 13
HELIX 13 13 ARG A 544 TYR A 546 5 3
HELIX 14 14 HIS A 547 TYR A 563 1 17
HELIX 15 15 GLY A 572 VAL A 582 5 11
HELIX 16 16 THR A 597 ARG A 611 1 15
HELIX 17 17 ASP A 623 THR A 630 1 8
HELIX 18 18 LEU A 643 VAL A 649 1 7
HELIX 19 19 VAL A 649 GLY A 664 1 16
SHEET 1 A 2 VAL A 343 ASN A 344 0
SHEET 2 A 2 THR A 349 VAL A 350 -1 O THR A 349 N ASN A 344
SHEET 1 B 5 VAL A 395 LEU A 399 0
SHEET 2 B 5 ARG A 367 ALA A 372 1 N LEU A 370 O MET A 396
SHEET 3 B 5 ASP A 414 SER A 420 1 O PHE A 417 N ILE A 371
SHEET 4 B 5 LEU A 441 THR A 446 1 O ILE A 445 N PHE A 418
SHEET 5 B 5 CYS A 459 HIS A 462 1 O VAL A 461 N GLY A 444
SHEET 1 C 5 HIS A 565 LEU A 570 0
SHEET 2 C 5 SER A 538 GLY A 543 1 N ILE A 541 O ILE A 569
SHEET 3 C 5 VAL A 588 ILE A 591 1 O ILE A 589 N MET A 542
SHEET 4 C 5 VAL A 616 ASP A 620 1 O ILE A 618 N MET A 590
SHEET 5 C 5 THR A 633 VAL A 636 1 O VAL A 636 N CYS A 619
SITE 1 AC1 19 GLY A 374 THR A 375 SER A 376 SER A 420
SITE 2 AC1 19 GLN A 421 SER A 422 THR A 425 VAL A 471
SITE 3 AC1 19 ALA A 472 SER A 473 LYS A 557 GLU A 560
SITE 4 AC1 19 HIS A 576 HOH A 685 HOH A 692 HOH A 696
SITE 5 AC1 19 HOH A 700 HOH A 702 HOH A 728
CRYST1 78.927 78.927 277.323 90.00 90.00 90.00 I 41 2 2 16
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 0.012670 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003606 0.00000
(ATOM LINES ARE NOT SHOWN.)
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