HEADER LYASE 03-JUL-16 5GK4
TITLE NATIVE STRUCTURE OF FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM
TITLE 2 ESCHERICHIA COLI AT 2.0 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FBPA,FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE,FRUCTOSE-
COMPND 5 BISPHOSPHATE ALDOLASE CLASS II;
COMPND 6 EC: 4.1.2.13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: FBAA, FBA, FDA, B2925, JW2892;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALDOLASE EC 4.1.2.13 FRUCTOSE 1, 6-BISPHOSPHATE GLYCOLYSIS ANABOLIC
KEYWDS 2 PATHWAYS CATABOLIC PATHWAYS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.H.TRAN,K.H.HUYNH,T.H.HO,L.W.KANG
REVDAT 2 08-NOV-23 5GK4 1 REMARK LINK
REVDAT 1 05-JUL-17 5GK4 0
JRNL AUTH T.H.TRAN,K.H.HUYNH,T.H.HO,L.W.KANG
JRNL TITL APO STRUCTURE OF FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM
JRNL TITL 2 ESCHERICHIA COLI AT 2.0 ANGSTROM RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 47820
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2561
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3409
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.1660
REMARK 3 BIN FREE R VALUE SET COUNT : 189
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5098
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 376
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.16
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) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.972
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5272 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5002 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7146 ; 1.843 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11542 ; 1.078 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 661 ; 6.001 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;35.886 ;25.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 882 ;13.614 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;13.527 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 794 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6009 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1183 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2650 ; 2.287 ; 2.132
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2649 ; 2.285 ; 2.132
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3309 ; 3.016 ; 3.175
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3310 ; 3.016 ; 3.175
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2622 ; 3.495 ; 2.548
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2622 ; 3.495 ; 2.548
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3838 ; 5.289 ; 3.643
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6338 ; 6.907 ;18.076
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6255 ; 6.880 ;17.966
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5GK4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300000925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6-7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DCM SI (111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.13900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1DOS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 5% FRUCTOSE 1,6
REMARK 280 -BISPHOSPHATASE, 0.1M TRIS PH 7.0, AND 15% PEG 4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 36.44650
REMARK 290 SMTRY3 2 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: 5980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 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 0
REMARK 465 GLY A 176
REMARK 465 CYS A 177
REMARK 465 THR A 178
REMARK 465 GLY A 179
REMARK 465 GLY A 180
REMARK 465 GLU A 181
REMARK 465 GLU A 182
REMARK 465 ASP A 183
REMARK 465 GLY A 184
REMARK 465 VAL A 185
REMARK 465 ASP A 186
REMARK 465 ASN A 187
REMARK 465 SER A 188
REMARK 465 HIS A 189
REMARK 465 MET A 190
REMARK 465 ASP A 191
REMARK 465 ALA A 192
REMARK 465 SER A 193
REMARK 465 ALA A 194
REMARK 465 LEU A 195
REMARK 465 VAL A 225
REMARK 465 HIS A 226
REMARK 465 GLY A 227
REMARK 465 VAL A 228
REMARK 465 TYR A 229
REMARK 465 LYS A 230
REMARK 465 PRO A 231
REMARK 465 GLY A 232
REMARK 465 ASN A 233
REMARK 465 MET B 0
REMARK 465 CYS B 177
REMARK 465 THR B 178
REMARK 465 GLY B 179
REMARK 465 GLY B 180
REMARK 465 GLU B 181
REMARK 465 GLU B 182
REMARK 465 ASP B 183
REMARK 465 GLY B 184
REMARK 465 VAL B 185
REMARK 465 ASP B 186
REMARK 465 ASN B 187
REMARK 465 SER B 188
REMARK 465 HIS B 189
REMARK 465 MET B 190
REMARK 465 ASP B 191
REMARK 465 ALA B 192
REMARK 465 SER B 193
REMARK 465 ALA B 194
REMARK 465 LEU B 195
REMARK 465 HIS B 226
REMARK 465 GLY B 227
REMARK 465 VAL B 228
REMARK 465 TYR B 229
REMARK 465 LYS B 230
REMARK 465 PRO B 231
REMARK 465 GLY B 232
REMARK 465 ASN B 233
REMARK 465 VAL B 234
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 B 673 O HOH B 697 2.02
REMARK 500 O HOH A 658 O HOH A 671 2.05
REMARK 500 ND2 ASN A 28 O HOH A 501 2.12
REMARK 500 ND1 HIS A 91 O4 PEG A 405 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 LEU A 171 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 ASP B 15 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LEU B 241 CB - CG - CD1 ANGL. DEV. = 11.4 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 LYS A 53 69.21 64.55
REMARK 500 LYS A 74 66.37 -116.42
REMARK 500 HIS A 110 110.23 -21.59
REMARK 500 HIS A 110 112.98 -24.29
REMARK 500 ASP A 288 -64.80 -145.75
REMARK 500 LYS B 53 70.85 67.91
REMARK 500 HIS B 110 112.72 -19.74
REMARK 500 HIS B 110 114.76 -23.85
REMARK 500 ASP B 288 -67.33 -148.50
REMARK 500 ALA B 354 69.02 -100.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 110 NE2
REMARK 620 2 GLU A 174 OE1 110.7
REMARK 620 3 GLU A 174 OE2 165.8 56.2
REMARK 620 4 HIS A 264 ND1 79.4 112.3 109.7
REMARK 620 5 HOH A 629 O 114.6 130.2 76.1 95.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 110 NE2
REMARK 620 2 HIS A 264 ND1 89.2
REMARK 620 3 HOH A 560 O 97.4 86.9
REMARK 620 4 HOH A 652 O 168.9 94.0 72.2
REMARK 620 5 HOH A 656 O 99.4 170.5 95.9 78.3
REMARK 620 6 HOH A 658 O 95.2 106.2 162.0 94.1 69.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 110 NE2
REMARK 620 2 GLU B 174 OE1 103.8
REMARK 620 3 GLU B 174 OE2 159.5 56.2
REMARK 620 4 HIS B 264 ND1 79.7 105.2 107.9
REMARK 620 5 HOH B 534 O 89.8 74.3 81.1 169.1
REMARK 620 6 HOH B 606 O 122.3 131.8 76.4 96.8 91.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 110 NE2
REMARK 620 2 HIS B 110 NE2 18.9
REMARK 620 3 HIS B 264 ND1 89.5 81.7
REMARK 620 4 HOH B 550 O 97.6 114.7 90.8
REMARK 620 5 HOH B 673 O 99.7 108.9 168.9 81.9
REMARK 620 6 HOH B 674 O 171.0 167.9 97.9 77.4 72.4
REMARK 620 7 HOH B 682 O 94.5 79.9 104.5 160.6 81.2 88.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GK8 RELATED DB: PDB
REMARK 900 RELATED ID: 5GK7 RELATED DB: PDB
REMARK 900 RELATED ID: 5GK6 RELATED DB: PDB
REMARK 900 RELATED ID: 5GK5 RELATED DB: PDB
REMARK 900 RELATED ID: 5GK3 RELATED DB: PDB
DBREF 5GK4 A 0 358 UNP P0AB71 ALF_ECOLI 1 359
DBREF 5GK4 B 0 358 UNP P0AB71 ALF_ECOLI 1 359
SEQRES 1 A 359 MET SER LYS ILE PHE ASP PHE VAL LYS PRO GLY VAL ILE
SEQRES 2 A 359 THR GLY ASP ASP VAL GLN LYS VAL PHE GLN VAL ALA LYS
SEQRES 3 A 359 GLU ASN ASN PHE ALA LEU PRO ALA VAL ASN CYS VAL GLY
SEQRES 4 A 359 THR ASP SER ILE ASN ALA VAL LEU GLU THR ALA ALA LYS
SEQRES 5 A 359 VAL LYS ALA PRO VAL ILE VAL GLN PHE SER ASN GLY GLY
SEQRES 6 A 359 ALA SER PHE ILE ALA GLY LYS GLY VAL LYS SER ASP VAL
SEQRES 7 A 359 PRO GLN GLY ALA ALA ILE LEU GLY ALA ILE SER GLY ALA
SEQRES 8 A 359 HIS HIS VAL HIS GLN MET ALA GLU HIS TYR GLY VAL PRO
SEQRES 9 A 359 VAL ILE LEU HIS THR ASP HIS CYS ALA LYS LYS LEU LEU
SEQRES 10 A 359 PRO TRP ILE ASP GLY LEU LEU ASP ALA GLY GLU LYS HIS
SEQRES 11 A 359 PHE ALA ALA THR GLY LYS PRO LEU PHE SER SER HIS MET
SEQRES 12 A 359 ILE ASP LEU SER GLU GLU SER LEU GLN GLU ASN ILE GLU
SEQRES 13 A 359 ILE CYS SER LYS TYR LEU GLU ARG MET SER LYS ILE GLY
SEQRES 14 A 359 MET THR LEU GLU ILE GLU LEU GLY CYS THR GLY GLY GLU
SEQRES 15 A 359 GLU ASP GLY VAL ASP ASN SER HIS MET ASP ALA SER ALA
SEQRES 16 A 359 LEU TYR THR GLN PRO GLU ASP VAL ASP TYR ALA TYR THR
SEQRES 17 A 359 GLU LEU SER LYS ILE SER PRO ARG PHE THR ILE ALA ALA
SEQRES 18 A 359 SER PHE GLY ASN VAL HIS GLY VAL TYR LYS PRO GLY ASN
SEQRES 19 A 359 VAL VAL LEU THR PRO THR ILE LEU ARG ASP SER GLN GLU
SEQRES 20 A 359 TYR VAL SER LYS LYS HIS ASN LEU PRO HIS ASN SER LEU
SEQRES 21 A 359 ASN PHE VAL PHE HIS GLY GLY SER GLY SER THR ALA GLN
SEQRES 22 A 359 GLU ILE LYS ASP SER VAL SER TYR GLY VAL VAL LYS MET
SEQRES 23 A 359 ASN ILE ASP THR ASP THR GLN TRP ALA THR TRP GLU GLY
SEQRES 24 A 359 VAL LEU ASN TYR TYR LYS ALA ASN GLU ALA TYR LEU GLN
SEQRES 25 A 359 GLY GLN LEU GLY ASN PRO LYS GLY GLU ASP GLN PRO ASN
SEQRES 26 A 359 LYS LYS TYR TYR ASP PRO ARG VAL TRP LEU ARG ALA GLY
SEQRES 27 A 359 GLN THR SER MET ILE ALA ARG LEU GLU LYS ALA PHE GLN
SEQRES 28 A 359 GLU LEU ASN ALA ILE ASP VAL LEU
SEQRES 1 B 359 MET SER LYS ILE PHE ASP PHE VAL LYS PRO GLY VAL ILE
SEQRES 2 B 359 THR GLY ASP ASP VAL GLN LYS VAL PHE GLN VAL ALA LYS
SEQRES 3 B 359 GLU ASN ASN PHE ALA LEU PRO ALA VAL ASN CYS VAL GLY
SEQRES 4 B 359 THR ASP SER ILE ASN ALA VAL LEU GLU THR ALA ALA LYS
SEQRES 5 B 359 VAL LYS ALA PRO VAL ILE VAL GLN PHE SER ASN GLY GLY
SEQRES 6 B 359 ALA SER PHE ILE ALA GLY LYS GLY VAL LYS SER ASP VAL
SEQRES 7 B 359 PRO GLN GLY ALA ALA ILE LEU GLY ALA ILE SER GLY ALA
SEQRES 8 B 359 HIS HIS VAL HIS GLN MET ALA GLU HIS TYR GLY VAL PRO
SEQRES 9 B 359 VAL ILE LEU HIS THR ASP HIS CYS ALA LYS LYS LEU LEU
SEQRES 10 B 359 PRO TRP ILE ASP GLY LEU LEU ASP ALA GLY GLU LYS HIS
SEQRES 11 B 359 PHE ALA ALA THR GLY LYS PRO LEU PHE SER SER HIS MET
SEQRES 12 B 359 ILE ASP LEU SER GLU GLU SER LEU GLN GLU ASN ILE GLU
SEQRES 13 B 359 ILE CYS SER LYS TYR LEU GLU ARG MET SER LYS ILE GLY
SEQRES 14 B 359 MET THR LEU GLU ILE GLU LEU GLY CYS THR GLY GLY GLU
SEQRES 15 B 359 GLU ASP GLY VAL ASP ASN SER HIS MET ASP ALA SER ALA
SEQRES 16 B 359 LEU TYR THR GLN PRO GLU ASP VAL ASP TYR ALA TYR THR
SEQRES 17 B 359 GLU LEU SER LYS ILE SER PRO ARG PHE THR ILE ALA ALA
SEQRES 18 B 359 SER PHE GLY ASN VAL HIS GLY VAL TYR LYS PRO GLY ASN
SEQRES 19 B 359 VAL VAL LEU THR PRO THR ILE LEU ARG ASP SER GLN GLU
SEQRES 20 B 359 TYR VAL SER LYS LYS HIS ASN LEU PRO HIS ASN SER LEU
SEQRES 21 B 359 ASN PHE VAL PHE HIS GLY GLY SER GLY SER THR ALA GLN
SEQRES 22 B 359 GLU ILE LYS ASP SER VAL SER TYR GLY VAL VAL LYS MET
SEQRES 23 B 359 ASN ILE ASP THR ASP THR GLN TRP ALA THR TRP GLU GLY
SEQRES 24 B 359 VAL LEU ASN TYR TYR LYS ALA ASN GLU ALA TYR LEU GLN
SEQRES 25 B 359 GLY GLN LEU GLY ASN PRO LYS GLY GLU ASP GLN PRO ASN
SEQRES 26 B 359 LYS LYS TYR TYR ASP PRO ARG VAL TRP LEU ARG ALA GLY
SEQRES 27 B 359 GLN THR SER MET ILE ALA ARG LEU GLU LYS ALA PHE GLN
SEQRES 28 B 359 GLU LEU ASN ALA ILE ASP VAL LEU
HET GOL A 401 6
HET GOL A 402 6
HET ZN A 403 1
HET ZN A 404 1
HET PEG A 405 7
HET ZN B 401 1
HET ZN B 402 1
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 ZN 4(ZN 2+)
FORMUL 7 PEG C4 H10 O3
FORMUL 10 HOH *376(H2 O)
HELIX 1 AA1 LYS A 2 PHE A 6 5 5
HELIX 2 AA2 GLY A 14 ASN A 27 1 14
HELIX 3 AA3 GLY A 38 LYS A 53 1 16
HELIX 4 AA4 SER A 61 GLY A 70 1 10
HELIX 5 AA5 GLN A 79 ALA A 97 1 19
HELIX 6 AA6 GLU A 98 GLY A 101 5 4
HELIX 7 AA7 ALA A 112 LYS A 114 5 3
HELIX 8 AA8 LEU A 115 GLY A 134 1 20
HELIX 9 AA9 SER A 149 LYS A 166 1 18
HELIX 10 AB1 GLN A 198 LYS A 211 1 14
HELIX 11 AB2 PRO A 238 HIS A 252 1 15
HELIX 12 AB3 THR A 270 TYR A 280 1 11
HELIX 13 AB4 ASP A 288 ASN A 306 1 19
HELIX 14 AB5 GLU A 307 LEU A 310 5 4
HELIX 15 AB6 ASN A 324 ASP A 329 1 6
HELIX 16 AB7 ASP A 329 LEU A 352 1 24
HELIX 17 AB8 LYS B 2 PHE B 6 5 5
HELIX 18 AB9 GLY B 14 ASN B 27 1 14
HELIX 19 AC1 GLY B 38 LYS B 53 1 16
HELIX 20 AC2 SER B 61 GLY B 70 1 10
HELIX 21 AC3 GLN B 79 ALA B 97 1 19
HELIX 22 AC4 GLU B 98 GLY B 101 5 4
HELIX 23 AC5 ALA B 112 LYS B 114 5 3
HELIX 24 AC6 LEU B 115 GLY B 134 1 20
HELIX 25 AC7 SER B 149 LYS B 166 1 18
HELIX 26 AC8 GLN B 198 LYS B 211 1 14
HELIX 27 AC9 PRO B 238 ASN B 253 1 16
HELIX 28 AD1 THR B 270 TYR B 280 1 11
HELIX 29 AD2 ASP B 288 GLU B 307 1 20
HELIX 30 AD3 ALA B 308 LEU B 310 5 3
HELIX 31 AD4 ASN B 324 ASP B 329 1 6
HELIX 32 AD5 ASP B 329 LEU B 352 1 24
SHEET 1 AA110 GLY A 10 VAL A 11 0
SHEET 2 AA110 PRO A 103 THR A 108 1 O VAL A 104 N GLY A 10
SHEET 3 AA110 SER A 140 ILE A 143 1 N SER A 140 O LEU A 106
SHEET 4 AA110 THR A 170 LEU A 175 1 O GLU A 172 N ILE A 143
SHEET 5 AA110 PHE A 216 SER A 221 1 O ALA A 219 N ILE A 173
SHEET 6 AA110 PHE A 261 PHE A 263 1 O VAL A 262 N ILE A 218
SHEET 7 AA110 VAL A 282 ILE A 287 1 O LYS A 284 N PHE A 263
SHEET 8 AA110 LEU A 31 ASN A 35 1 N LEU A 31 O VAL A 283
SHEET 9 AA110 VAL A 56 PHE A 60 1 O ILE A 57 N VAL A 34
SHEET 10 AA110 PRO A 103 THR A 108 1 O HIS A 107 N VAL A 58
SHEET 1 AA2 2 LEU A 314 ASN A 316 0
SHEET 2 AA2 2 GLY A 319 PRO A 323 -1 O GLN A 322 N GLY A 315
SHEET 1 AA310 GLY B 10 VAL B 11 0
SHEET 2 AA310 PRO B 103 THR B 108 1 O VAL B 104 N GLY B 10
SHEET 3 AA310 SER B 140 MET B 142 1 N SER B 140 O LEU B 106
SHEET 4 AA310 THR B 170 GLU B 174 1 O GLU B 172 N HIS B 141
SHEET 5 AA310 PHE B 216 ALA B 219 1 O ALA B 219 N ILE B 173
SHEET 6 AA310 PHE B 261 PHE B 263 1 O VAL B 262 N ILE B 218
SHEET 7 AA310 VAL B 282 ILE B 287 1 O VAL B 283 N PHE B 261
SHEET 8 AA310 LEU B 31 ASN B 35 1 N ALA B 33 O ILE B 287
SHEET 9 AA310 VAL B 56 PHE B 60 1 O ILE B 57 N PRO B 32
SHEET 10 AA310 PRO B 103 THR B 108 1 O HIS B 107 N VAL B 58
SHEET 1 AA4 2 LEU B 314 ASN B 316 0
SHEET 2 AA4 2 GLY B 319 PRO B 323 -1 O GLN B 322 N GLY B 315
LINK NE2BHIS A 110 ZN ZN A 403 1555 1555 2.38
LINK NE2AHIS A 110 ZN ZN A 404 1555 1555 2.15
LINK OE1 GLU A 174 ZN ZN A 403 1555 1555 1.70
LINK OE2 GLU A 174 ZN ZN A 403 1555 1555 2.47
LINK ND1BHIS A 264 ZN ZN A 403 1555 1555 2.48
LINK ND1AHIS A 264 ZN ZN A 404 1555 1555 2.24
LINK ZN ZN A 403 O HOH A 629 1555 1555 2.27
LINK ZN ZN A 404 O HOH A 560 1555 1555 2.22
LINK ZN ZN A 404 O HOH A 652 1555 1555 2.12
LINK ZN ZN A 404 O HOH A 656 1555 1555 2.15
LINK ZN ZN A 404 O HOH A 658 1555 1555 2.40
LINK NE2BHIS B 110 ZN ZN B 401 1555 1555 2.31
LINK NE2AHIS B 110 ZN ZN B 402 1555 1555 2.00
LINK NE2BHIS B 110 ZN ZN B 402 1555 1555 2.66
LINK OE1 GLU B 174 ZN ZN B 401 1555 1555 2.05
LINK OE2 GLU B 174 ZN ZN B 401 1555 1555 2.38
LINK ND1BHIS B 264 ZN ZN B 401 1555 1555 2.46
LINK ND1AHIS B 264 ZN ZN B 402 1555 1555 2.15
LINK ZN ZN B 401 O HOH B 534 1555 1555 2.67
LINK ZN ZN B 401 O HOH B 606 1555 1555 2.15
LINK ZN ZN B 402 O HOH B 550 1555 1555 2.32
LINK ZN ZN B 402 O HOH B 673 1555 1555 2.16
LINK ZN ZN B 402 O HOH B 674 1555 1555 2.07
LINK ZN ZN B 402 O HOH B 682 1555 1555 2.63
SITE 1 AC1 10 GLN A 18 TYR A 206 PRO A 214 PHE A 216
SITE 2 AC1 10 SER A 258 LEU A 259 ASN A 260 HOH A 526
SITE 3 AC1 10 HOH A 574 HOH A 599
SITE 1 AC2 1 TYR A 160
SITE 1 AC3 5 HIS A 110 GLU A 174 HIS A 264 HOH A 534
SITE 2 AC3 5 HOH A 629
SITE 1 AC4 6 HIS A 110 HIS A 264 HOH A 560 HOH A 652
SITE 2 AC4 6 HOH A 656 HOH A 658
SITE 1 AC5 8 SER A 88 HIS A 91 HIS A 92 GLN A 95
SITE 2 AC5 8 SER B 88 HIS B 91 HIS B 92 GLN B 95
SITE 1 AC6 6 HIS B 110 GLU B 174 HIS B 264 HOH B 534
SITE 2 AC6 6 HOH B 606 HOH B 682
SITE 1 AC7 6 HIS B 110 HIS B 264 HOH B 550 HOH B 673
SITE 2 AC7 6 HOH B 674 HOH B 682
CRYST1 73.126 72.893 72.455 90.00 103.20 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 0.013675 0.000000 0.003206 0.00000
SCALE2 0.000000 0.013719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
