HEADER OXIDOREDUCTASE 19-JAN-09 2ZYD
TITLE DIMERIC 6-PHOSPHOGLUCONATE DEHYDROGENASE COMPLEXED WITH GLUCOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.44;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: GND;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS NADP, PENTOSE PHOSPHATE PATHWAY, OXIDOREDUCTASE, 6-PHOSPHOGLUCONATE
KEYWDS 2 DEHYDROGENASE, 6-PHOSPHOGLUCONATE, GLUCONATE UTILIZATION, PENTOSE
KEYWDS 3 SHUNT
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-Y.CHEN,T.-P.KO,L.-P.LO,C.-H.LIN,A.H.-J.WANG
REVDAT 7 01-NOV-23 2ZYD 1 REMARK
REVDAT 6 10-NOV-21 2ZYD 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 2ZYD 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 SITE
REVDAT 4 11-OCT-17 2ZYD 1 REMARK
REVDAT 3 22-JAN-14 2ZYD 1 JRNL
REVDAT 2 13-JUL-11 2ZYD 1 VERSN
REVDAT 1 01-SEP-09 2ZYD 0
JRNL AUTH Y.-Y.CHEN,T.-P.KO,W.-H.CHEN,L.-P.LO,C.-H.LIN,A.H.-J.WANG
JRNL TITL CONFORMATIONAL CHANGES ASSOCIATED WITH COFACTOR/SUBSTRATE
JRNL TITL 2 BINDING OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM ESCHERICHIA
JRNL TITL 3 COLI AND KLEBSIELLA PNEUMONIAE: IMPLICATIONS FOR ENZYME
JRNL TITL 4 MECHANISM
JRNL REF J.STRUCT.BIOL. V. 169 25 2010
JRNL REFN ISSN 1047-8477
JRNL PMID 19686854
JRNL DOI 10.1016/J.JSB.2009.08.006
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 137750
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) : 0.165
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7306
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.64
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2546
REMARK 3 BIN FREE R VALUE : 0.2608
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 495
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7206
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 1814
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.862
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000028580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150258
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 55.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1PGP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE DIHRDRATE, 0.5M
REMARK 280 AMMONIUM ACETATE, 6-7% PEG 3350, 17-18% PEG 4000, 30% D(+)-
REMARK 280 GLUCOSE, PH 5.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 34.22600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.99800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.30450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.99800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.22600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.30450
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: 10850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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 -11
REMARK 465 GLY A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LEU A 467
REMARK 465 ASP A 468
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASP B 468
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 O1 GLO A 3929 O HOH A 796 1.65
REMARK 500 O5 GLO A 3929 O HOH A 1761 1.70
REMARK 500 O HOH A 682 O HOH A 1785 1.71
REMARK 500 O HOH A 1110 O HOH A 1535 1.75
REMARK 500 O HOH A 558 O HOH A 1805 1.79
REMARK 500 N GLN A 309 OD1 ASN A 414 1.81
REMARK 500 O HOH B 626 O HOH B 884 1.81
REMARK 500 ND2 ASN A 259 O HOH A 1741 1.84
REMARK 500 O HOH B 711 O HOH B 1795 1.85
REMARK 500 O HOH A 1331 O HOH A 1783 1.85
REMARK 500 O HOH B 1592 O HOH B 1593 1.86
REMARK 500 O HOH A 1000 O HOH A 1744 1.89
REMARK 500 O HOH A 601 O HOH A 806 1.90
REMARK 500 O HOH B 620 O HOH B 1689 1.91
REMARK 500 O HOH A 1348 O HOH A 1786 1.91
REMARK 500 O HOH B 552 O HOH B 1255 1.91
REMARK 500 O HOH A 971 O HOH B 1499 1.92
REMARK 500 O HOH B 826 O HOH B 1674 1.92
REMARK 500 O HOH A 693 O HOH A 831 1.93
REMARK 500 O HOH A 493 O HOH A 674 1.93
REMARK 500 O TYR A 410 ND2 ASN A 414 1.94
REMARK 500 O HOH A 749 O HOH A 1466 1.94
REMARK 500 O HOH A 627 O HOH A 1752 1.94
REMARK 500 O HOH B 1329 O HOH B 1639 1.94
REMARK 500 O HOH B 986 O HOH B 1754 1.94
REMARK 500 O HOH B 489 O HOH B 1554 1.95
REMARK 500 O HOH A 1031 O HOH A 1423 1.95
REMARK 500 O HOH A 1311 O HOH A 1312 1.95
REMARK 500 O HOH B 884 O HOH B 1770 1.96
REMARK 500 O HOH A 558 O HOH A 792 1.98
REMARK 500 O HOH A 611 O HOH B 1810 1.99
REMARK 500 O HOH A 1608 O HOH A 1609 2.00
REMARK 500 O HOH B 1563 O HOH B 1567 2.00
REMARK 500 O HOH A 1374 O HOH A 1802 2.01
REMARK 500 O HOH B 859 O HOH B 1126 2.01
REMARK 500 O HOH A 1346 O HOH A 1788 2.01
REMARK 500 O HOH B 1084 O HOH B 1791 2.01
REMARK 500 O HOH A 985 O HOH A 1464 2.02
REMARK 500 O HOH B 688 O HOH B 1171 2.03
REMARK 500 O HOH A 628 O HOH A 863 2.04
REMARK 500 O HOH B 1694 O HOH B 1768 2.04
REMARK 500 O HOH A 1500 O HOH A 1501 2.04
REMARK 500 O HOH A 1057 O HOH A 1058 2.05
REMARK 500 O HOH A 1091 O HOH A 1502 2.05
REMARK 500 O HOH A 1420 O HOH A 1532 2.05
REMARK 500 O HOH A 711 O HOH B 473 2.06
REMARK 500 O HOH A 1809 O HOH B 546 2.06
REMARK 500 O HOH A 818 O HOH A 819 2.06
REMARK 500 O HOH A 1741 O HOH B 1447 2.06
REMARK 500 O HOH A 900 O HOH A 1290 2.07
REMARK 500
REMARK 500 THIS ENTRY HAS 103 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
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 1803 O HOH B 1382 1655 1.97
REMARK 500 O HOH A 819 O HOH B 1184 1655 2.06
REMARK 500 O HOH A 1808 O HOH B 483 1655 2.07
REMARK 500 O HOH A 809 O HOH B 1184 1655 2.12
REMARK 500 O HOH B 637 O HOH B 1792 4456 2.19
REMARK 500 O HOH A 956 O HOH B 1226 2564 2.19
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 GLY B 263 C GLY B 263 O 0.110
REMARK 500 SER B 422 CA SER B 422 CB 0.103
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 MET B 141 CG - SD - CE ANGL. DEV. = -20.2 DEGREES
REMARK 500 GLY B 261 N - CA - C ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU B 279 CB - CG - CD2 ANGL. DEV. = -15.4 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 ALA A 12 -175.93 -67.64
REMARK 500 ASP A 176 -114.95 40.19
REMARK 500 SER A 228 120.01 -39.20
REMARK 500 GLU A 244 0.56 -46.12
REMARK 500 ASN A 259 -30.09 -169.78
REMARK 500 LYS A 260 23.40 83.12
REMARK 500 LEU A 292 49.89 -97.96
REMARK 500 THR A 452 161.88 71.66
REMARK 500 CYS B 169 49.62 -87.77
REMARK 500 ASP B 176 -115.07 40.11
REMARK 500 LEU B 292 51.33 -102.26
REMARK 500 THR B 452 157.79 73.83
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 TYR B 353 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZYA RELATED DB: PDB
REMARK 900 RELATED ID: 3FWN RELATED DB: PDB
REMARK 900 RELATED ID: 2ZYG RELATED DB: PDB
DBREF 2ZYD A 1 468 UNP P00350 6PGD_ECOLI 1 468
DBREF 2ZYD B 1 468 UNP P00350 6PGD_ECOLI 1 468
SEQADV 2ZYD MET A -11 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD GLY A -10 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -9 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -8 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -7 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -6 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -5 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -4 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -3 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -2 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A -1 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS A 0 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD CYS A 378 UNP P00350 TYR 378 ENGINEERED MUTATION
SEQADV 2ZYD MET B -11 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD GLY B -10 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -9 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -8 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -7 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -6 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -5 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -4 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -3 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -2 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B -1 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD HIS B 0 UNP P00350 EXPRESSION TAG
SEQADV 2ZYD CYS B 378 UNP P00350 TYR 378 ENGINEERED MUTATION
SEQRES 1 A 480 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 480 SER LYS GLN GLN ILE GLY VAL VAL GLY MET ALA VAL MET
SEQRES 3 A 480 GLY ARG ASN LEU ALA LEU ASN ILE GLU SER ARG GLY TYR
SEQRES 4 A 480 THR VAL SER ILE PHE ASN ARG SER ARG GLU LYS THR GLU
SEQRES 5 A 480 GLU VAL ILE ALA GLU ASN PRO GLY LYS LYS LEU VAL PRO
SEQRES 6 A 480 TYR TYR THR VAL LYS GLU PHE VAL GLU SER LEU GLU THR
SEQRES 7 A 480 PRO ARG ARG ILE LEU LEU MET VAL LYS ALA GLY ALA GLY
SEQRES 8 A 480 THR ASP ALA ALA ILE ASP SER LEU LYS PRO TYR LEU ASP
SEQRES 9 A 480 LYS GLY ASP ILE ILE ILE ASP GLY GLY ASN THR PHE PHE
SEQRES 10 A 480 GLN ASP THR ILE ARG ARG ASN ARG GLU LEU SER ALA GLU
SEQRES 11 A 480 GLY PHE ASN PHE ILE GLY THR GLY VAL SER GLY GLY GLU
SEQRES 12 A 480 GLU GLY ALA LEU LYS GLY PRO SER ILE MET PRO GLY GLY
SEQRES 13 A 480 GLN LYS GLU ALA TYR GLU LEU VAL ALA PRO ILE LEU THR
SEQRES 14 A 480 LYS ILE ALA ALA VAL ALA GLU ASP GLY GLU PRO CYS VAL
SEQRES 15 A 480 THR TYR ILE GLY ALA ASP GLY ALA GLY HIS TYR VAL LYS
SEQRES 16 A 480 MET VAL HIS ASN GLY ILE GLU TYR GLY ASP MET GLN LEU
SEQRES 17 A 480 ILE ALA GLU ALA TYR SER LEU LEU LYS GLY GLY LEU ASN
SEQRES 18 A 480 LEU THR ASN GLU GLU LEU ALA GLN THR PHE THR GLU TRP
SEQRES 19 A 480 ASN ASN GLY GLU LEU SER SER TYR LEU ILE ASP ILE THR
SEQRES 20 A 480 LYS ASP ILE PHE THR LYS LYS ASP GLU ASP GLY ASN TYR
SEQRES 21 A 480 LEU VAL ASP VAL ILE LEU ASP GLU ALA ALA ASN LYS GLY
SEQRES 22 A 480 THR GLY LYS TRP THR SER GLN SER ALA LEU ASP LEU GLY
SEQRES 23 A 480 GLU PRO LEU SER LEU ILE THR GLU SER VAL PHE ALA ARG
SEQRES 24 A 480 TYR ILE SER SER LEU LYS ASP GLN ARG VAL ALA ALA SER
SEQRES 25 A 480 LYS VAL LEU SER GLY PRO GLN ALA GLN PRO ALA GLY ASP
SEQRES 26 A 480 LYS ALA GLU PHE ILE GLU LYS VAL ARG ARG ALA LEU TYR
SEQRES 27 A 480 LEU GLY LYS ILE VAL SER TYR ALA GLN GLY PHE SER GLN
SEQRES 28 A 480 LEU ARG ALA ALA SER GLU GLU TYR ASN TRP ASP LEU ASN
SEQRES 29 A 480 TYR GLY GLU ILE ALA LYS ILE PHE ARG ALA GLY CYS ILE
SEQRES 30 A 480 ILE ARG ALA GLN PHE LEU GLN LYS ILE THR ASP ALA CYS
SEQRES 31 A 480 ALA GLU ASN PRO GLN ILE ALA ASN LEU LEU LEU ALA PRO
SEQRES 32 A 480 TYR PHE LYS GLN ILE ALA ASP ASP TYR GLN GLN ALA LEU
SEQRES 33 A 480 ARG ASP VAL VAL ALA TYR ALA VAL GLN ASN GLY ILE PRO
SEQRES 34 A 480 VAL PRO THR PHE SER ALA ALA VAL ALA TYR TYR ASP SER
SEQRES 35 A 480 TYR ARG ALA ALA VAL LEU PRO ALA ASN LEU ILE GLN ALA
SEQRES 36 A 480 GLN ARG ASP TYR PHE GLY ALA HIS THR TYR LYS ARG ILE
SEQRES 37 A 480 ASP LYS GLU GLY VAL PHE HIS THR GLU TRP LEU ASP
SEQRES 1 B 480 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 480 SER LYS GLN GLN ILE GLY VAL VAL GLY MET ALA VAL MET
SEQRES 3 B 480 GLY ARG ASN LEU ALA LEU ASN ILE GLU SER ARG GLY TYR
SEQRES 4 B 480 THR VAL SER ILE PHE ASN ARG SER ARG GLU LYS THR GLU
SEQRES 5 B 480 GLU VAL ILE ALA GLU ASN PRO GLY LYS LYS LEU VAL PRO
SEQRES 6 B 480 TYR TYR THR VAL LYS GLU PHE VAL GLU SER LEU GLU THR
SEQRES 7 B 480 PRO ARG ARG ILE LEU LEU MET VAL LYS ALA GLY ALA GLY
SEQRES 8 B 480 THR ASP ALA ALA ILE ASP SER LEU LYS PRO TYR LEU ASP
SEQRES 9 B 480 LYS GLY ASP ILE ILE ILE ASP GLY GLY ASN THR PHE PHE
SEQRES 10 B 480 GLN ASP THR ILE ARG ARG ASN ARG GLU LEU SER ALA GLU
SEQRES 11 B 480 GLY PHE ASN PHE ILE GLY THR GLY VAL SER GLY GLY GLU
SEQRES 12 B 480 GLU GLY ALA LEU LYS GLY PRO SER ILE MET PRO GLY GLY
SEQRES 13 B 480 GLN LYS GLU ALA TYR GLU LEU VAL ALA PRO ILE LEU THR
SEQRES 14 B 480 LYS ILE ALA ALA VAL ALA GLU ASP GLY GLU PRO CYS VAL
SEQRES 15 B 480 THR TYR ILE GLY ALA ASP GLY ALA GLY HIS TYR VAL LYS
SEQRES 16 B 480 MET VAL HIS ASN GLY ILE GLU TYR GLY ASP MET GLN LEU
SEQRES 17 B 480 ILE ALA GLU ALA TYR SER LEU LEU LYS GLY GLY LEU ASN
SEQRES 18 B 480 LEU THR ASN GLU GLU LEU ALA GLN THR PHE THR GLU TRP
SEQRES 19 B 480 ASN ASN GLY GLU LEU SER SER TYR LEU ILE ASP ILE THR
SEQRES 20 B 480 LYS ASP ILE PHE THR LYS LYS ASP GLU ASP GLY ASN TYR
SEQRES 21 B 480 LEU VAL ASP VAL ILE LEU ASP GLU ALA ALA ASN LYS GLY
SEQRES 22 B 480 THR GLY LYS TRP THR SER GLN SER ALA LEU ASP LEU GLY
SEQRES 23 B 480 GLU PRO LEU SER LEU ILE THR GLU SER VAL PHE ALA ARG
SEQRES 24 B 480 TYR ILE SER SER LEU LYS ASP GLN ARG VAL ALA ALA SER
SEQRES 25 B 480 LYS VAL LEU SER GLY PRO GLN ALA GLN PRO ALA GLY ASP
SEQRES 26 B 480 LYS ALA GLU PHE ILE GLU LYS VAL ARG ARG ALA LEU TYR
SEQRES 27 B 480 LEU GLY LYS ILE VAL SER TYR ALA GLN GLY PHE SER GLN
SEQRES 28 B 480 LEU ARG ALA ALA SER GLU GLU TYR ASN TRP ASP LEU ASN
SEQRES 29 B 480 TYR GLY GLU ILE ALA LYS ILE PHE ARG ALA GLY CYS ILE
SEQRES 30 B 480 ILE ARG ALA GLN PHE LEU GLN LYS ILE THR ASP ALA CYS
SEQRES 31 B 480 ALA GLU ASN PRO GLN ILE ALA ASN LEU LEU LEU ALA PRO
SEQRES 32 B 480 TYR PHE LYS GLN ILE ALA ASP ASP TYR GLN GLN ALA LEU
SEQRES 33 B 480 ARG ASP VAL VAL ALA TYR ALA VAL GLN ASN GLY ILE PRO
SEQRES 34 B 480 VAL PRO THR PHE SER ALA ALA VAL ALA TYR TYR ASP SER
SEQRES 35 B 480 TYR ARG ALA ALA VAL LEU PRO ALA ASN LEU ILE GLN ALA
SEQRES 36 B 480 GLN ARG ASP TYR PHE GLY ALA HIS THR TYR LYS ARG ILE
SEQRES 37 B 480 ASP LYS GLU GLY VAL PHE HIS THR GLU TRP LEU ASP
HET GLO A3929 12
HETNAM GLO D-GLUCOSE
HETSYN GLO D-GLUCOSE IN LINEAR FORM
FORMUL 3 GLO C6 H12 O6
FORMUL 4 HOH *1814(H2 O)
HELIX 1 1 ALA A 12 SER A 24 1 13
HELIX 2 2 SER A 35 ASN A 46 1 12
HELIX 3 3 THR A 56 SER A 63 1 8
HELIX 4 4 ALA A 78 LYS A 88 1 11
HELIX 5 5 PRO A 89 LEU A 91 5 3
HELIX 6 6 PHE A 104 GLU A 118 1 15
HELIX 7 7 GLY A 129 GLY A 137 1 9
HELIX 8 8 GLN A 145 ALA A 160 1 16
HELIX 9 9 GLY A 177 ASN A 209 1 33
HELIX 10 10 THR A 211 GLY A 225 1 15
HELIX 11 11 SER A 229 LYS A 241 1 13
HELIX 12 12 TYR A 248 ILE A 253 5 6
HELIX 13 13 LYS A 264 GLY A 274 1 11
HELIX 14 14 LEU A 277 SER A 291 1 15
HELIX 15 15 LEU A 292 LYS A 301 1 10
HELIX 16 16 ASP A 313 ASN A 348 1 36
HELIX 17 17 ASN A 352 PHE A 360 1 9
HELIX 18 18 GLN A 369 ASN A 381 1 13
HELIX 19 19 ASN A 386 LEU A 389 5 4
HELIX 20 20 ALA A 390 GLY A 415 1 26
HELIX 21 21 VAL A 418 ARG A 432 1 15
HELIX 22 22 PRO A 437 ALA A 450 1 14
HELIX 23 23 ALA B 12 ARG B 25 1 14
HELIX 24 24 SER B 35 ASN B 46 1 12
HELIX 25 25 THR B 56 SER B 63 1 8
HELIX 26 26 GLY B 77 LYS B 88 1 12
HELIX 27 27 PRO B 89 LEU B 91 5 3
HELIX 28 28 PHE B 104 GLU B 118 1 15
HELIX 29 29 GLY B 129 GLY B 137 1 9
HELIX 30 30 GLN B 145 ALA B 160 1 16
HELIX 31 31 GLY B 177 ASN B 209 1 33
HELIX 32 32 THR B 211 ASN B 224 1 14
HELIX 33 33 SER B 229 PHE B 239 1 11
HELIX 34 34 TYR B 248 ILE B 253 1 6
HELIX 35 35 GLY B 261 GLY B 274 1 14
HELIX 36 36 LEU B 277 SER B 291 1 15
HELIX 37 37 LEU B 292 LYS B 301 1 10
HELIX 38 38 ASP B 313 ASN B 348 1 36
HELIX 39 39 ASN B 352 PHE B 360 1 9
HELIX 40 40 GLN B 369 ASN B 381 1 13
HELIX 41 41 ASN B 386 LEU B 389 5 4
HELIX 42 42 ALA B 390 GLY B 415 1 26
HELIX 43 43 VAL B 418 ARG B 432 1 15
HELIX 44 44 PRO B 437 ALA B 450 1 14
SHEET 1 A 7 LEU A 51 PRO A 53 0
SHEET 2 A 7 VAL A 29 PHE A 32 1 N ILE A 31 O VAL A 52
SHEET 3 A 7 ILE A 6 VAL A 9 1 N VAL A 8 O SER A 30
SHEET 4 A 7 ARG A 69 LEU A 72 1 O LEU A 71 N GLY A 7
SHEET 5 A 7 ILE A 96 ASP A 99 1 O ILE A 98 N LEU A 72
SHEET 6 A 7 ASN A 121 SER A 128 1 O THR A 125 N ASP A 99
SHEET 7 A 7 SER A 139 GLY A 143 -1 O SER A 139 N SER A 128
SHEET 1 B 7 LEU B 51 PRO B 53 0
SHEET 2 B 7 VAL B 29 PHE B 32 1 N VAL B 29 O VAL B 52
SHEET 3 B 7 ILE B 6 VAL B 9 1 N VAL B 8 O SER B 30
SHEET 4 B 7 ARG B 69 LEU B 72 1 O LEU B 71 N GLY B 7
SHEET 5 B 7 ILE B 96 ASP B 99 1 O ILE B 98 N LEU B 72
SHEET 6 B 7 ASN B 121 SER B 128 1 O ILE B 123 N ASP B 99
SHEET 7 B 7 SER B 139 GLY B 144 -1 O SER B 139 N SER B 128
SHEET 1 C 2 TYR B 453 LYS B 454 0
SHEET 2 C 2 VAL B 461 PHE B 462 -1 O PHE B 462 N TYR B 453
CISPEP 1 THR A 66 PRO A 67 0 -0.52
CISPEP 2 THR B 66 PRO B 67 0 -0.67
CRYST1 68.452 118.609 119.996 90.00 90.00 90.00 P 21 21 21 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 0.014609 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
