HEADER HYDROLASE 28-JUL-04 1U60
TITLE MCSG APC5046 PROBABLE GLUTAMINASE YBAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE GLUTAMINASE YBAS;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.5.1.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YBAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, APC5046, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,M.E.CUFF,A.JOACHIMIAK,A.SAVCHENKO,A.EDWARDS,T.SKARINA,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 8 14-FEB-24 1U60 1 REMARK
REVDAT 7 26-SEP-12 1U60 1 AUTHOR
REVDAT 6 13-JUL-11 1U60 1 VERSN
REVDAT 5 24-FEB-09 1U60 1 VERSN
REVDAT 4 03-JUN-08 1U60 1 JRNL
REVDAT 3 20-MAY-08 1U60 1 JRNL
REVDAT 2 18-JAN-05 1U60 1 AUTHOR KEYWDS REMARK
REVDAT 1 07-SEP-04 1U60 0
JRNL AUTH G.BROWN,A.SINGER,M.PROUDFOOT,T.SKARINA,Y.KIM,C.CHANG,
JRNL AUTH 2 I.DEMENTIEVA,E.KUZNETSOVA,C.F.GONZALEZ,A.JOACHIMIAK,
JRNL AUTH 3 A.SAVCHENKO,A.F.YAKUNIN
JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF FOUR
JRNL TITL 2 GLUTAMINASES FROM ESCHERICHIA COLI AND BACILLUS SUBTILIS.
JRNL REF BIOCHEMISTRY V. 47 5724 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18459799
JRNL DOI 10.1021/BI800097H
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.7
REMARK 3 NUMBER OF REFLECTIONS : 125216
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6641
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2786
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 1150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71000
REMARK 3 B22 (A**2) : -1.68000
REMARK 3 B33 (A**2) : 2.38000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.856
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9490 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 8541 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12897 ; 1.599 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19874 ; 0.925 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1252 ; 6.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1476 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10818 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1766 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2117 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10300 ; 0.248 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 5389 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 813 ; 0.210 ; 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): 35 ; 0.250 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 124 ; 0.314 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.248 ; 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): 6156 ; 0.877 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9790 ; 1.507 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3334 ; 2.902 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3097 ; 4.556 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0920 55.4400 50.1810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0359 T22: 0.0502
REMARK 3 T33: 0.0174 T12: 0.0056
REMARK 3 T13: -0.0016 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.3584 L22: 0.3768
REMARK 3 L33: 0.1469 L12: 0.0532
REMARK 3 L13: 0.1149 L23: 0.0248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: -0.0056 S13: 0.0006
REMARK 3 S21: -0.0231 S22: -0.0242 S23: 0.0091
REMARK 3 S31: 0.0000 S32: -0.0076 S33: 0.0229
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 310
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3180 60.0600 79.1900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: 0.0460
REMARK 3 T33: 0.0085 T12: 0.0011
REMARK 3 T13: -0.0114 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.3782 L22: 0.2681
REMARK 3 L33: 0.2313 L12: -0.1147
REMARK 3 L13: 0.0545 L23: 0.0760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0329 S12: -0.0041 S13: 0.0023
REMARK 3 S21: 0.0466 S22: 0.0086 S23: 0.0082
REMARK 3 S31: 0.0009 S32: 0.0298 S33: 0.0243
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 310
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4930 23.5700 5.2440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: 0.0357
REMARK 3 T33: 0.0051 T12: -0.0056
REMARK 3 T13: -0.0042 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.4433 L22: 0.4415
REMARK 3 L33: 0.0791 L12: 0.1407
REMARK 3 L13: -0.0528 L23: 0.1494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0751 S12: -0.0361 S13: 0.0074
REMARK 3 S21: -0.1024 S22: 0.0339 S23: 0.0090
REMARK 3 S31: -0.0270 S32: 0.0166 S33: 0.0412
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 310
REMARK 3 ORIGIN FOR THE GROUP (A): 36.4420 24.9010 34.6090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0302 T22: 0.0529
REMARK 3 T33: 0.0241 T12: 0.0031
REMARK 3 T13: -0.0043 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.3206 L22: 0.3790
REMARK 3 L33: 0.1867 L12: -0.0972
REMARK 3 L13: -0.1215 L23: 0.0902
REMARK 3 S TENSOR
REMARK 3 S11: -0.0210 S12: 0.0238 S13: -0.0071
REMARK 3 S21: 0.0283 S22: -0.0406 S23: 0.0250
REMARK 3 S31: 0.0086 S32: -0.0266 S33: 0.0616
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1U60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131904
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
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 (%) : 77.9
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) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 23.0
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION SOLUTION: 0.1M HEPES,
REMARK 280 10% ISOPROPANOL, 20% PEG 4000. CRYOPROTECTANT: CRYSTALLIZATION
REMARK 280 SOLUTION PLUS 12% ETHYLENE GLYCOL, PH 7.5
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 25.25450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.08550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.94550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.08550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.25450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.94550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 5150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 50.50900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 77.94550
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 82.08550
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -50.50900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
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 1284 O HOH B 1469 1.74
REMARK 500 O HOH A 1496 O HOH A 1519 1.86
REMARK 500 CB VAL B 231 O HOH B 1455 1.86
REMARK 500 NH1 ARG D 61 O HOH D 1339 1.90
REMARK 500 O HOH C 1253 O HOH C 1464 1.96
REMARK 500 O HOH A 1352 O HOH B 1353 1.99
REMARK 500 O HOH C 1346 O HOH C 1452 1.99
REMARK 500 O HOH D 1467 O HOH D 1501 2.02
REMARK 500 O HOH C 1364 O HOH C 1453 2.06
REMARK 500 O HOH B 1397 O HOH B 1499 2.08
REMARK 500 O HOH D 1319 O HOH D 1335 2.13
REMARK 500 O HOH A 1463 O HOH A 1471 2.13
REMARK 500 C GLY B 310 O HOH B 1441 2.16
REMARK 500 N LEU B 2 O HOH B 1464 2.16
REMARK 500 O2 EDO A 1217 O HOH A 1374 2.17
REMARK 500 O HOH A 1407 O HOH D 1263 2.17
REMARK 500 O HOH B 1329 O HOH B 1469 2.18
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 C 1444 O HOH C 1466 4455 1.98
REMARK 500 O HOH C 1467 O HOH C 1486 4455 2.11
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 GLU C 105 CD GLU C 105 OE2 0.086
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 49 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP B 57 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 92 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP C 57 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP C 184 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP D 184 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 65 -128.70 47.86
REMARK 500 ILE A 89 -60.45 -126.11
REMARK 500 LEU A 112 -47.74 67.84
REMARK 500 ASN A 165 36.48 -92.13
REMARK 500 GLU A 241 -1.76 -146.14
REMARK 500 TYR A 244 -133.87 64.03
REMARK 500 VAL A 273 -57.97 -130.25
REMARK 500 GLU B 65 -132.90 52.79
REMARK 500 ILE B 89 -63.14 -123.30
REMARK 500 LEU B 112 -45.97 78.42
REMARK 500 ALA B 129 141.25 -170.40
REMARK 500 ASN B 165 36.61 -94.68
REMARK 500 GLU B 241 -0.26 -143.51
REMARK 500 TYR B 244 -132.67 58.84
REMARK 500 VAL B 273 -53.59 -128.45
REMARK 500 GLU C 65 -134.63 50.04
REMARK 500 ILE C 89 -58.98 -124.75
REMARK 500 LEU C 112 -44.65 77.42
REMARK 500 ASN C 165 35.30 -91.22
REMARK 500 GLU C 241 -1.33 -144.37
REMARK 500 TYR C 244 -133.37 60.51
REMARK 500 VAL C 273 -55.61 -128.05
REMARK 500 GLU D 65 -128.80 49.72
REMARK 500 ILE D 89 -60.92 -123.49
REMARK 500 ILE D 89 -59.50 -124.20
REMARK 500 LEU D 112 -45.37 70.18
REMARK 500 ASN D 165 38.23 -93.56
REMARK 500 TYR D 244 -133.27 64.37
REMARK 500 VAL D 273 -59.38 -132.17
REMARK 500 ASN D 306 122.30 -172.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1225
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 1226
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 1215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC5046 RELATED DB: TARGETDB
DBREF 1U60 A 1 310 UNP P77454 GLSA1_ECOLI 1 310
DBREF 1U60 B 1 310 UNP P77454 GLSA1_ECOLI 1 310
DBREF 1U60 C 1 310 UNP P77454 GLSA1_ECOLI 1 310
DBREF 1U60 D 1 310 UNP P77454 GLSA1_ECOLI 1 310
SEQRES 1 A 310 MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN
SEQRES 2 A 310 ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN
SEQRES 3 A 310 ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN
SEQRES 4 A 310 LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL
SEQRES 5 A 310 TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU
SEQRES 6 A 310 SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU
SEQRES 7 A 310 ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA
SEQRES 8 A 310 ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU
SEQRES 9 A 310 GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN
SEQRES 10 A 310 ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU
SEQRES 11 A 310 ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN
SEQRES 12 A 310 GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU
SEQRES 13 A 310 VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG
SEQRES 14 A 310 ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR
SEQRES 15 A 310 CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN
SEQRES 16 A 310 CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU
SEQRES 17 A 310 GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR
SEQRES 18 A 310 HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE
SEQRES 19 A 310 LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER
SEQRES 20 A 310 GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER
SEQRES 21 A 310 GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL
SEQRES 22 A 310 MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP
SEQRES 23 A 310 GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL
SEQRES 24 A 310 ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY
SEQRES 1 B 310 MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN
SEQRES 2 B 310 ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN
SEQRES 3 B 310 ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN
SEQRES 4 B 310 LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL
SEQRES 5 B 310 TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU
SEQRES 6 B 310 SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU
SEQRES 7 B 310 ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA
SEQRES 8 B 310 ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU
SEQRES 9 B 310 GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN
SEQRES 10 B 310 ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU
SEQRES 11 B 310 ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN
SEQRES 12 B 310 GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU
SEQRES 13 B 310 VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG
SEQRES 14 B 310 ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR
SEQRES 15 B 310 CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN
SEQRES 16 B 310 CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU
SEQRES 17 B 310 GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR
SEQRES 18 B 310 HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE
SEQRES 19 B 310 LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER
SEQRES 20 B 310 GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER
SEQRES 21 B 310 GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL
SEQRES 22 B 310 MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP
SEQRES 23 B 310 GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL
SEQRES 24 B 310 ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY
SEQRES 1 C 310 MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN
SEQRES 2 C 310 ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN
SEQRES 3 C 310 ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN
SEQRES 4 C 310 LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL
SEQRES 5 C 310 TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU
SEQRES 6 C 310 SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU
SEQRES 7 C 310 ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA
SEQRES 8 C 310 ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU
SEQRES 9 C 310 GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN
SEQRES 10 C 310 ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU
SEQRES 11 C 310 ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN
SEQRES 12 C 310 GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU
SEQRES 13 C 310 VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG
SEQRES 14 C 310 ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR
SEQRES 15 C 310 CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN
SEQRES 16 C 310 CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU
SEQRES 17 C 310 GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR
SEQRES 18 C 310 HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE
SEQRES 19 C 310 LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER
SEQRES 20 C 310 GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER
SEQRES 21 C 310 GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL
SEQRES 22 C 310 MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP
SEQRES 23 C 310 GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL
SEQRES 24 C 310 ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY
SEQRES 1 D 310 MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN
SEQRES 2 D 310 ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN
SEQRES 3 D 310 ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN
SEQRES 4 D 310 LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL
SEQRES 5 D 310 TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU
SEQRES 6 D 310 SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU
SEQRES 7 D 310 ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA
SEQRES 8 D 310 ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU
SEQRES 9 D 310 GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN
SEQRES 10 D 310 ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU
SEQRES 11 D 310 ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN
SEQRES 12 D 310 GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU
SEQRES 13 D 310 VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG
SEQRES 14 D 310 ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR
SEQRES 15 D 310 CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN
SEQRES 16 D 310 CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU
SEQRES 17 D 310 GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR
SEQRES 18 D 310 HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE
SEQRES 19 D 310 LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER
SEQRES 20 D 310 GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER
SEQRES 21 D 310 GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL
SEQRES 22 D 310 MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP
SEQRES 23 D 310 GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL
SEQRES 24 D 310 ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY
HET EDO A1203 4
HET EDO A1204 4
HET EDO A1205 4
HET EDO A1211 4
HET EDO A1217 4
HET EDO A1219 4
HET FMT A1212 3
HET FMT A1218 3
HET EDO B1210 4
HET EDO B1224 4
HET FMT B1206 3
HET FMT B1207 3
HET FMT B1209 3
HET FMT B1225 3
HET EDO C1208 4
HET FMT C1222 3
HET FMT C1226 3
HET EDO D1213 4
HET EDO D1214 4
HET EDO D1216 4
HET FMT D1215 3
HETNAM EDO 1,2-ETHANEDIOL
HETNAM FMT FORMIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 12(C2 H6 O2)
FORMUL 11 FMT 9(C H2 O2)
FORMUL 26 HOH *1150(H2 O)
HELIX 1 1 ASP A 3 HIS A 19 1 17
HELIX 2 2 ILE A 30 ASN A 35 1 6
HELIX 3 3 ILE A 67 GLY A 81 1 15
HELIX 4 4 GLY A 81 ILE A 89 1 9
HELIX 5 5 SER A 100 HIS A 107 1 8
HELIX 6 6 VAL A 116 ILE A 127 1 12
HELIX 7 7 ASN A 131 GLY A 148 1 18
HELIX 8 8 SER A 154 THR A 163 1 10
HELIX 9 9 ASN A 165 GLY A 179 1 15
HELIX 10 10 ASP A 184 CYS A 196 1 13
HELIX 11 11 ASN A 201 ALA A 214 1 14
HELIX 12 12 GLN A 227 ASP A 229 5 3
HELIX 13 13 ASN A 230 GLY A 242 1 13
HELIX 14 14 LEU A 243 GLY A 245 5 3
HELIX 15 15 ARG A 246 VAL A 254 1 9
HELIX 16 16 SER A 289 GLY A 304 1 16
HELIX 17 17 ASP B 3 HIS B 19 1 17
HELIX 18 18 ILE B 30 ASN B 35 1 6
HELIX 19 19 ILE B 67 GLY B 81 1 15
HELIX 20 20 GLY B 81 ILE B 89 1 9
HELIX 21 21 SER B 100 LEU B 106 1 7
HELIX 22 22 VAL B 116 ILE B 127 1 12
HELIX 23 23 ASN B 131 GLY B 148 1 18
HELIX 24 24 SER B 154 THR B 163 1 10
HELIX 25 25 ASN B 165 GLY B 179 1 15
HELIX 26 26 ASP B 184 CYS B 196 1 13
HELIX 27 27 ASN B 201 ALA B 214 1 14
HELIX 28 28 GLN B 227 ASP B 229 5 3
HELIX 29 29 ASN B 230 GLY B 242 1 13
HELIX 30 30 LEU B 243 GLY B 245 5 3
HELIX 31 31 ARG B 246 VAL B 254 1 9
HELIX 32 32 SER B 289 GLY B 304 1 16
HELIX 33 33 ASP C 3 HIS C 19 1 17
HELIX 34 34 ILE C 30 ASN C 35 1 6
HELIX 35 35 ILE C 67 GLY C 81 1 15
HELIX 36 36 GLY C 81 ILE C 89 1 9
HELIX 37 37 SER C 100 LEU C 106 1 7
HELIX 38 38 VAL C 116 ILE C 127 1 12
HELIX 39 39 ASN C 131 GLY C 148 1 18
HELIX 40 40 SER C 154 THR C 163 1 10
HELIX 41 41 ASN C 165 GLY C 179 1 15
HELIX 42 42 ASP C 184 SER C 197 1 14
HELIX 43 43 ASN C 201 ALA C 214 1 14
HELIX 44 44 GLN C 227 ASP C 229 5 3
HELIX 45 45 ASN C 230 GLY C 242 1 13
HELIX 46 46 LEU C 243 GLY C 245 5 3
HELIX 47 47 ARG C 246 VAL C 254 1 9
HELIX 48 48 SER C 289 GLY C 304 1 16
HELIX 49 49 ASP D 3 HIS D 19 1 17
HELIX 50 50 ILE D 30 ASN D 35 1 6
HELIX 51 51 ILE D 67 GLY D 81 1 15
HELIX 52 52 GLY D 81 ILE D 89 1 9
HELIX 53 53 SER D 100 HIS D 107 1 8
HELIX 54 54 VAL D 116 ILE D 127 1 12
HELIX 55 55 ASN D 131 GLY D 148 1 18
HELIX 56 56 SER D 154 THR D 163 1 10
HELIX 57 57 ASN D 165 GLY D 179 1 15
HELIX 58 58 ASP D 184 SER D 197 1 14
HELIX 59 59 ASN D 201 ALA D 214 1 14
HELIX 60 60 GLN D 227 ASP D 229 5 3
HELIX 61 61 ASN D 230 GLY D 242 1 13
HELIX 62 62 LEU D 243 GLY D 245 5 3
HELIX 63 63 ARG D 246 VAL D 254 1 9
HELIX 64 64 SER D 289 GLY D 304 1 16
SHEET 1 A 5 VAL A 52 GLY A 56 0
SHEET 2 A 5 ALA A 42 THR A 47 -1 N ILE A 45 O TYR A 53
SHEET 3 A 5 MET A 274 PHE A 279 -1 O ALA A 277 N ALA A 44
SHEET 4 A 5 GLY A 265 VAL A 270 -1 N VAL A 270 O MET A 274
SHEET 5 A 5 GLY A 258 SER A 260 -1 N LYS A 259 O LEU A 267
SHEET 1 B 3 PHE A 62 ALA A 63 0
SHEET 2 B 3 THR A 198 LEU A 200 -1 O LEU A 200 N PHE A 62
SHEET 3 B 3 ALA A 152 LEU A 153 -1 N ALA A 152 O LEU A 199
SHEET 1 C 2 VAL A 217 ASN A 218 0
SHEET 2 C 2 LYS A 223 ARG A 224 -1 O LYS A 223 N ASN A 218
SHEET 1 D 5 VAL B 52 GLY B 56 0
SHEET 2 D 5 ALA B 42 THR B 47 -1 N ILE B 45 O TYR B 53
SHEET 3 D 5 MET B 274 PHE B 279 -1 O ALA B 277 N ALA B 44
SHEET 4 D 5 GLY B 265 VAL B 270 -1 N VAL B 270 O MET B 274
SHEET 5 D 5 GLY B 258 SER B 260 -1 N LYS B 259 O LEU B 267
SHEET 1 E 3 PHE B 62 ALA B 63 0
SHEET 2 E 3 THR B 198 LEU B 200 -1 O LEU B 200 N PHE B 62
SHEET 3 E 3 ALA B 152 LEU B 153 -1 N ALA B 152 O LEU B 199
SHEET 1 F 5 VAL C 52 GLY C 56 0
SHEET 2 F 5 ALA C 42 THR C 47 -1 N ILE C 45 O TYR C 53
SHEET 3 F 5 MET C 274 PHE C 279 -1 O ALA C 277 N ALA C 44
SHEET 4 F 5 GLY C 265 VAL C 270 -1 N VAL C 270 O MET C 274
SHEET 5 F 5 GLY C 258 SER C 260 -1 N LYS C 259 O LEU C 267
SHEET 1 G 3 PHE C 62 ALA C 63 0
SHEET 2 G 3 THR C 198 LEU C 200 -1 O LEU C 200 N PHE C 62
SHEET 3 G 3 ALA C 152 LEU C 153 -1 N ALA C 152 O LEU C 199
SHEET 1 H 5 VAL D 52 GLY D 56 0
SHEET 2 H 5 ALA D 42 THR D 47 -1 N ILE D 45 O TYR D 53
SHEET 3 H 5 MET D 274 PHE D 279 -1 O ALA D 277 N ALA D 44
SHEET 4 H 5 GLY D 265 VAL D 270 -1 N ALA D 268 O ILE D 276
SHEET 5 H 5 GLY D 258 SER D 260 -1 N LYS D 259 O LEU D 267
SHEET 1 I 3 PHE D 62 ALA D 63 0
SHEET 2 I 3 THR D 198 LEU D 200 -1 O LEU D 200 N PHE D 62
SHEET 3 I 3 ALA D 152 LEU D 153 -1 N ALA D 152 O LEU D 199
SHEET 1 J 2 VAL D 217 ASN D 218 0
SHEET 2 J 2 LYS D 223 ARG D 224 -1 O LYS D 223 N ASN D 218
SITE 1 AC1 4 LYS A 294 HOH A1377 THR B 16 GLN B 17
SITE 1 AC2 5 LYS A 88 GLY A 179 TYR A 180 EDO A1205
SITE 2 AC2 5 HOH A1527
SITE 1 AC3 3 ASP A 87 LYS A 88 EDO A1204
SITE 1 AC4 5 PHE A 98 GLY A 287 FMT A1212 HOH A1413
SITE 2 AC4 5 HOH A1415
SITE 1 AC5 5 ASP A 59 ASN A 201 HOH A1229 HOH A1285
SITE 2 AC5 5 HOH A1374
SITE 1 AC6 8 PRO A 37 GLN A 39 LEU A 40 HOH A1380
SITE 2 AC6 8 HOH A1462 HOH A1489 HIS D 222 HOH D1312
SITE 1 AC7 2 ASN B 128 ARG B 138
SITE 1 AC8 8 GLU B 65 GLU B 161 ASN B 168 TYR B 192
SITE 2 AC8 8 THR B 193 HOH B1288 HOH B1404 HOH B1413
SITE 1 AC9 7 VAL C 52 ARG C 224 GLN C 227 HOH C1284
SITE 2 AC9 7 HOH C1298 HOH C1316 HOH C1382
SITE 1 BC1 8 GLU D 65 GLU D 161 ASN D 168 THR D 193
SITE 2 BC1 8 CYS D 196 HOH D1249 HOH D1293 HOH D1372
SITE 1 BC2 5 GLY D 287 FMT D1215 HOH D1418 HOH D1436
SITE 2 BC2 5 HOH D1486
SITE 1 BC3 2 GLN D 25 ASN D 26
SITE 1 BC4 4 GLN A 25 ASP A 284 EDO A1211 HOH A1433
SITE 1 BC5 4 LEU A 199 HOH A1278 HOH A1347 HOH A1372
SITE 1 BC6 3 GLN B 39 ALA B 178 FMT B1207
SITE 1 BC7 7 GLN B 39 GLY B 179 TYR B 180 TYR B 182
SITE 2 BC7 7 FMT B1206 HOH B1410 HOH B1444
SITE 1 BC8 6 SER B 100 VAL B 101 ILE B 102 HOH B1460
SITE 2 BC8 6 GLU C 105 HOH C1430
SITE 1 BC9 3 ASN B 22 GLY B 23 GLY B 24
SITE 1 CC1 4 ASN C 51 VAL C 52 GLU C 78 HOH C1427
SITE 1 CC2 3 ASN C 22 GLY C 23 ARG C 291
SITE 1 CC3 7 SER D 66 TYR D 244 VAL D 262 EDO D1214
SITE 2 CC3 7 HOH D1224 HOH D1242 HOH D1361
CRYST1 50.509 155.891 164.171 90.00 90.00 90.00 P 21 21 21 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 0.019798 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END