HEADER OXIDOREDUCTASE 05-APR-06 2GLX
TITLE CRYSTAL STRUCTURE ANALYSIS OF BACTERIAL 1,5-AF REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,5-ANHYDRO-D-FRUCTOSE REDUCTASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: 1,5-AF-REDUCTASE;
COMPND 5 EC: 1.1.1.263;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENSIFER ADHAERENS;
SOURCE 3 ORGANISM_TAXID: 106592;
SOURCE 4 STRAIN: S-30.7.5;
SOURCE 5 GENE: AFR;
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: PET24A
KEYWDS NADP(H) DEPENDENT REDUCTASE, ROSSMANN-FOLD, BACTERIAL 1, 5-ANHYDRO-D-
KEYWDS 2 FRUCTOSE REDUCTASE, SUGAR METABOLISM, 1, 5-ANHYDRO-D-FRUCTOSE, 5-
KEYWDS 3 ANHYDRO-D-MANNITOL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.DAMBE,A.J.SCHEIDIG
REVDAT 4 13-MAR-24 2GLX 1 REMARK SEQADV
REVDAT 3 18-OCT-17 2GLX 1 REMARK
REVDAT 2 24-FEB-09 2GLX 1 VERSN
REVDAT 1 29-AUG-06 2GLX 0
JRNL AUTH T.R.DAMBE,A.M.KUEHN,T.BROSSETTE,F.GIFFHORN,A.J.SCHEIDIG
JRNL TITL CRYSTAL STRUCTURE OF NADP(H)-DEPENDENT
JRNL TITL 2 1,5-ANHYDRO-D-FRUCTOSE REDUCTASE FROM SINORHIZOBIUM
JRNL TITL 3 MORELENSE AT 2.2 A RESOLUTION: CONSTRUCTION OF A
JRNL TITL 4 NADH-ACCEPTING MUTANT AND ITS APPLICATION IN RARE SUGAR
JRNL TITL 5 SYNTHESIS
JRNL REF BIOCHEMISTRY V. 45 10030 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16906761
JRNL DOI 10.1021/BI052589Q
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.KUEHN,S.YU,F.GIFFHORN
REMARK 1 TITL CATABOLISM OF 1,5-ANHYDRO-D-FRUCTOSE IN SINORHIZOBIUM
REMARK 1 TITL 2 MORELENSE S-30.7.5: DISCOVERY, CHARACTERIZATION, AND
REMARK 1 TITL 3 OVEREXPRESSION OF A NEW 1,5-ANHYDRO-D-FRUCTOSE REDUCTASE AND
REMARK 1 TITL 4 ITS APPLICATION IN SUGAR ANALYSIS AND RARE SUGAR SYNTHESIS
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 72 1248 2006
REMARK 1 REFN ISSN 0099-2240
REMARK 1 PMID 16461673
REMARK 1 DOI 10.1128/AEM.72.2.1248-1257.2006
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 123085
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6155
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) : 8581
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 452
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 312
REMARK 3 SOLVENT ATOMS : 1304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.06000
REMARK 3 B22 (A**2) : 2.47000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.240
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.210
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.687
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15324 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20868 ; 1.615 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1986 ; 8.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 648 ;37.406 ;23.611
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2334 ;21.099 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;23.088 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2394 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11622 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7665 ; 0.269 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10312 ; 0.324 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1328 ; 0.230 ; 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): 182 ; 0.223 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 43 ; 0.189 ; 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): 10017 ; 2.854 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15594 ; 3.690 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5898 ; 5.979 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5274 ; 7.942 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2GLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-04; 14-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SLS; ESRF
REMARK 200 BEAMLINE : X06SA; ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788; 0.933
REMARK 200 MONOCHROMATOR : MIRROR; MIRROR
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PRODC
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123108
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 1.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.43700
REMARK 200 R SYM FOR SHELL (I) : 0.44800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NACITRAT, 200MM AMMONIUMACETAT,
REMARK 280 30% MPEG 5000, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 42.45000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 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 2578 O HOH B 2766 2.00
REMARK 500 OD2 ASP B 306 O HOH B 2758 2.04
REMARK 500 N ASN C 2 O HOH C 3692 2.07
REMARK 500 O VAL F 64 NZ LYS F 88 2.08
REMARK 500 OD2 ASP E 134 O HOH E 5614 2.11
REMARK 500 O HOH A 1567 O HOH A 1715 2.12
REMARK 500 O HOH C 3641 O HOH C 3660 2.12
REMARK 500 OD2 ASP F 181 OD1 ASP F 230 2.12
REMARK 500 O HOH A 1668 O HOH A 1848 2.12
REMARK 500 OD1 ASN C 2 O HOH C 3603 2.12
REMARK 500 OE1 GLU B 56 O HOH B 2635 2.12
REMARK 500 OE2 GLU A 15 O HOH A 1712 2.13
REMARK 500 O VAL D 64 NZ LYS D 88 2.13
REMARK 500 O HOH A 1843 O HOH A 1845 2.13
REMARK 500 O HOH A 1842 O HOH A 1843 2.13
REMARK 500 OXT ACT A 1502 O HOH A 1846 2.14
REMARK 500 OE2 GLU E 78 O HOH E 5714 2.15
REMARK 500 ND2 ASN E 2 O HOH E 5509 2.15
REMARK 500 O HOH E 5741 O HOH E 5742 2.15
REMARK 500 N ASN E 2 O HOH E 5723 2.16
REMARK 500 O HOH E 5517 O HOH E 5724 2.16
REMARK 500 OD2 ASP F 306 O HOH F 6601 2.17
REMARK 500 O HOH A 1608 O HOH A 1825 2.17
REMARK 500 O HOH A 1575 O HOH A 1832 2.17
REMARK 500 O HOH A 1615 O HOH A 1641 2.18
REMARK 500 O HOH B 2570 O HOH B 2728 2.19
REMARK 500 O HOH A 1659 O HOH A 1673 2.19
REMARK 500 O HOH E 5515 O HOH E 5717 2.19
REMARK 500 OD1 ASN D 125 OG SER D 301 2.19
REMARK 500 O THR D 24 O HOH D 4604 2.19
REMARK 500 CG2 ILE D 141 O HOH D 4506 2.19
REMARK 500 O ARG F 22 O HOH F 6557 2.19
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 A 32 CA - CB - CG ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG B 143 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO B 279 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG E 140 NE - CZ - NH1 ANGL. DEV. = 3.0 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 TRP A 16 -53.59 -137.06
REMARK 500 THR A 34 -9.12 -50.93
REMARK 500 ALA A 97 -165.60 -162.01
REMARK 500 GLN A 160 48.64 -85.22
REMARK 500 ARG A 166 79.14 54.08
REMARK 500 GLU A 208 -141.63 50.61
REMARK 500 ASP A 278 77.13 -108.01
REMARK 500 TRP B 16 -51.14 -128.03
REMARK 500 HIS B 158 -9.93 -58.86
REMARK 500 ARG B 166 76.82 43.31
REMARK 500 GLU B 168 0.80 -61.47
REMARK 500 GLU B 208 -129.84 50.86
REMARK 500 TRP C 16 -46.20 -142.40
REMARK 500 ALA C 97 -155.27 -146.11
REMARK 500 HIS C 151 43.71 -143.36
REMARK 500 GLN C 160 38.77 -83.59
REMARK 500 ARG C 166 70.87 44.56
REMARK 500 GLU C 208 -125.96 32.63
REMARK 500 ASN C 254 39.64 71.49
REMARK 500 ASP C 278 79.80 -104.71
REMARK 500 ASN C 281 121.79 -38.88
REMARK 500 TRP D 16 -54.27 -130.42
REMARK 500 THR D 44 -72.19 -66.82
REMARK 500 GLU D 45 -29.67 -23.13
REMARK 500 ALA D 97 -168.09 -168.41
REMARK 500 HIS D 151 32.05 -163.61
REMARK 500 HIS D 158 1.99 -57.89
REMARK 500 GLN D 160 41.66 -86.58
REMARK 500 ARG D 166 60.59 66.41
REMARK 500 ASN D 190 59.78 38.36
REMARK 500 ALA D 203 44.60 -107.50
REMARK 500 GLU D 208 -136.26 49.03
REMARK 500 PHE D 241 128.07 -171.94
REMARK 500 ASN D 268 -159.78 -130.86
REMARK 500 HIS D 297 56.61 -110.89
REMARK 500 ALA D 326 138.50 -37.86
REMARK 500 ALA E 86 -3.83 -55.90
REMARK 500 GLN E 160 45.00 -86.87
REMARK 500 ARG E 166 71.70 42.96
REMARK 500 ALA E 203 36.34 -98.70
REMARK 500 GLU E 208 -123.34 34.69
REMARK 500 PRO E 260 47.85 -69.00
REMARK 500 PRO E 279 47.27 -92.75
REMARK 500 TRP F 16 -48.28 -133.55
REMARK 500 ALA F 97 -163.38 -163.32
REMARK 500 ARG F 124 1.75 -59.97
REMARK 500 GLN F 160 49.38 -77.28
REMARK 500 ARG F 166 91.23 39.89
REMARK 500 ASN F 190 63.62 36.63
REMARK 500 ALA F 194 -31.56 -131.16
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
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 ACT A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 3502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 4502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 5502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 6502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 3500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 4500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP E 5500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP F 6500
DBREF 2GLX A 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
DBREF 2GLX B 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
DBREF 2GLX C 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
DBREF 2GLX D 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
DBREF 2GLX E 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
DBREF 2GLX F 2 333 UNP Q2I8V6 Q2I8V6_9RHIZ 2 333
SEQADV 2GLX VAL A 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU A 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQADV 2GLX VAL B 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU B 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQADV 2GLX VAL C 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU C 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQADV 2GLX VAL D 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU D 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQADV 2GLX VAL E 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU E 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQADV 2GLX VAL F 217 UNP Q2I8V6 GLY 217 CONFLICT
SEQADV 2GLX LEU F 218 UNP Q2I8V6 VAL 218 CONFLICT
SEQRES 1 A 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 A 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 A 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 A 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 A 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 A 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 A 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 A 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 A 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 A 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 A 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 A 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 A 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 A 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 A 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 A 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 A 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 A 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 A 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 A 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 A 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 A 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 A 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 A 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 A 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 A 332 ALA GLU ILE GLU THR GLY LEU
SEQRES 1 B 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 B 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 B 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 B 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 B 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 B 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 B 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 B 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 B 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 B 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 B 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 B 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 B 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 B 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 B 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 B 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 B 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 B 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 B 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 B 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 B 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 B 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 B 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 B 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 B 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 B 332 ALA GLU ILE GLU THR GLY LEU
SEQRES 1 C 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 C 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 C 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 C 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 C 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 C 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 C 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 C 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 C 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 C 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 C 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 C 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 C 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 C 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 C 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 C 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 C 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 C 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 C 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 C 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 C 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 C 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 C 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 C 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 C 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 C 332 ALA GLU ILE GLU THR GLY LEU
SEQRES 1 D 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 D 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 D 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 D 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 D 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 D 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 D 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 D 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 D 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 D 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 D 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 D 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 D 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 D 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 D 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 D 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 D 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 D 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 D 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 D 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 D 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 D 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 D 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 D 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 D 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 D 332 ALA GLU ILE GLU THR GLY LEU
SEQRES 1 E 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 E 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 E 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 E 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 E 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 E 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 E 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 E 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 E 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 E 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 E 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 E 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 E 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 E 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 E 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 E 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 E 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 E 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 E 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 E 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 E 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 E 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 E 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 E 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 E 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 E 332 ALA GLU ILE GLU THR GLY LEU
SEQRES 1 F 332 ASN ARG TRP GLY LEU ILE GLY ALA SER THR ILE ALA ARG
SEQRES 2 F 332 GLU TRP VAL ILE GLY ALA ILE ARG ALA THR GLY GLY GLU
SEQRES 3 F 332 VAL VAL SER MET MET SER THR SER ALA GLU ARG GLY ALA
SEQRES 4 F 332 ALA TYR ALA THR GLU ASN GLY ILE GLY LYS SER VAL THR
SEQRES 5 F 332 SER VAL GLU GLU LEU VAL GLY ASP PRO ASP VAL ASP ALA
SEQRES 6 F 332 VAL TYR VAL SER THR THR ASN GLU LEU HIS ARG GLU GLN
SEQRES 7 F 332 THR LEU ALA ALA ILE ARG ALA GLY LYS HIS VAL LEU CYS
SEQRES 8 F 332 GLU LYS PRO LEU ALA MET THR LEU GLU ASP ALA ARG GLU
SEQRES 9 F 332 MET VAL VAL ALA ALA ARG GLU ALA GLY VAL VAL LEU GLY
SEQRES 10 F 332 THR ASN HIS HIS LEU ARG ASN ALA ALA ALA HIS ARG ALA
SEQRES 11 F 332 MET ARG ASP ALA ILE ALA GLU GLY ARG ILE GLY ARG PRO
SEQRES 12 F 332 ILE ALA ALA ARG VAL PHE HIS ALA VAL TYR LEU PRO PRO
SEQRES 13 F 332 HIS LEU GLN GLY TRP ARG LEU GLU ARG PRO GLU ALA GLY
SEQRES 14 F 332 GLY GLY VAL ILE LEU ASP ILE THR VAL HIS ASP ALA ASP
SEQRES 15 F 332 THR LEU ARG PHE VAL LEU ASN ASP ASP PRO ALA GLU ALA
SEQRES 16 F 332 VAL ALA ILE SER HIS SER ALA GLY MET GLY LYS GLU GLY
SEQRES 17 F 332 VAL GLU ASP GLY VAL MET GLY VAL LEU ARG PHE GLN SER
SEQRES 18 F 332 GLY VAL ILE ALA GLN PHE HIS ASP ALA PHE THR THR LYS
SEQRES 19 F 332 PHE ALA GLU THR GLY PHE GLU VAL HIS GLY THR GLU GLY
SEQRES 20 F 332 SER LEU ILE GLY ARG ASN VAL MET THR GLN LYS PRO VAL
SEQRES 21 F 332 GLY THR VAL THR LEU ARG ASN ALA GLU GLY GLU SER GLN
SEQRES 22 F 332 LEU PRO LEU ASP PRO ALA ASN LEU TYR GLU THR ALA LEU
SEQRES 23 F 332 ALA ALA PHE HIS SER ALA ILE GLU GLY HIS GLY GLN PRO
SEQRES 24 F 332 SER ALA THR GLY GLU ASP GLY VAL TRP SER LEU ALA THR
SEQRES 25 F 332 GLY LEU ALA VAL VAL LYS ALA ALA ALA THR GLY GLN ALA
SEQRES 26 F 332 ALA GLU ILE GLU THR GLY LEU
HET ACT A1502 4
HET NDP A1500 48
HET ACT B2502 4
HET NDP B2500 48
HET ACT C3502 4
HET NDP C3500 48
HET ACT D4502 4
HET NDP D4500 48
HET ACT E5502 4
HET NDP E5500 48
HET ACT F6502 4
HET NDP F6500 48
HETNAM ACT ACETATE ION
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 7 ACT 6(C2 H3 O2 1-)
FORMUL 8 NDP 6(C21 H30 N7 O17 P3)
FORMUL 19 HOH *1304(H2 O)
HELIX 1 1 SER A 10 TRP A 16 1 7
HELIX 2 2 TRP A 16 THR A 24 1 9
HELIX 3 3 SER A 35 ASN A 46 1 12
HELIX 4 4 SER A 54 GLY A 60 1 7
HELIX 5 5 THR A 72 GLU A 74 5 3
HELIX 6 6 LEU A 75 ALA A 86 1 12
HELIX 7 7 THR A 99 GLY A 114 1 16
HELIX 8 8 HIS A 122 ASN A 125 5 4
HELIX 9 9 ALA A 126 GLU A 138 1 13
HELIX 10 10 PRO A 156 GLN A 160 5 5
HELIX 11 11 GLY A 161 GLU A 165 5 5
HELIX 12 12 GLY A 172 ILE A 177 1 6
HELIX 13 13 ILE A 177 ASN A 190 1 14
HELIX 14 14 ASN A 281 GLU A 295 1 15
HELIX 15 15 THR A 303 GLY A 324 1 22
HELIX 16 16 SER B 10 TRP B 16 1 7
HELIX 17 17 TRP B 16 THR B 24 1 9
HELIX 18 18 SER B 35 ASN B 46 1 12
HELIX 19 19 SER B 54 GLY B 60 1 7
HELIX 20 20 THR B 72 GLU B 74 5 3
HELIX 21 21 LEU B 75 ALA B 86 1 12
HELIX 22 22 THR B 99 GLY B 114 1 16
HELIX 23 23 HIS B 122 ASN B 125 5 4
HELIX 24 24 ALA B 126 GLU B 138 1 13
HELIX 25 25 PRO B 156 GLN B 160 5 5
HELIX 26 26 GLY B 161 GLU B 165 5 5
HELIX 27 27 ARG B 166 GLY B 170 5 5
HELIX 28 28 GLY B 172 ILE B 177 1 6
HELIX 29 29 ILE B 177 ASN B 190 1 14
HELIX 30 30 ASN B 281 GLU B 295 1 15
HELIX 31 31 THR B 303 GLY B 324 1 22
HELIX 32 32 SER C 10 TRP C 16 1 7
HELIX 33 33 TRP C 16 THR C 24 1 9
HELIX 34 34 SER C 35 GLY C 47 1 13
HELIX 35 35 SER C 54 ASP C 61 1 8
HELIX 36 36 THR C 72 GLU C 74 5 3
HELIX 37 37 LEU C 75 ALA C 86 1 12
HELIX 38 38 THR C 99 GLY C 114 1 16
HELIX 39 39 HIS C 122 ASN C 125 5 4
HELIX 40 40 ALA C 126 GLU C 138 1 13
HELIX 41 41 PRO C 156 GLN C 160 5 5
HELIX 42 42 GLY C 161 GLU C 165 5 5
HELIX 43 43 ARG C 166 GLY C 170 5 5
HELIX 44 44 GLY C 172 ILE C 177 1 6
HELIX 45 45 ILE C 177 ASN C 190 1 14
HELIX 46 46 ASN C 281 GLU C 295 1 15
HELIX 47 47 THR C 303 GLY C 324 1 22
HELIX 48 48 SER D 10 TRP D 16 1 7
HELIX 49 49 TRP D 16 ALA D 23 1 8
HELIX 50 50 SER D 35 ASN D 46 1 12
HELIX 51 51 SER D 54 GLY D 60 1 7
HELIX 52 52 THR D 72 GLU D 74 5 3
HELIX 53 53 LEU D 75 ALA D 86 1 12
HELIX 54 54 THR D 99 ALA D 113 1 15
HELIX 55 55 HIS D 122 ASN D 125 5 4
HELIX 56 56 ALA D 126 GLU D 138 1 13
HELIX 57 57 PRO D 156 GLN D 160 5 5
HELIX 58 58 GLY D 161 GLU D 165 5 5
HELIX 59 59 ARG D 166 GLY D 170 5 5
HELIX 60 60 GLY D 172 ILE D 177 1 6
HELIX 61 61 ILE D 177 LEU D 189 1 13
HELIX 62 62 ASN D 281 GLY D 296 1 16
HELIX 63 63 THR D 303 GLY D 324 1 22
HELIX 64 64 SER E 10 TRP E 16 1 7
HELIX 65 65 TRP E 16 THR E 24 1 9
HELIX 66 66 SER E 35 ASN E 46 1 12
HELIX 67 67 SER E 54 GLY E 60 1 7
HELIX 68 68 LEU E 75 ALA E 86 1 12
HELIX 69 69 THR E 99 ALA E 113 1 15
HELIX 70 70 HIS E 122 ASN E 125 5 4
HELIX 71 71 ALA E 126 GLU E 138 1 13
HELIX 72 72 PRO E 156 GLN E 160 5 5
HELIX 73 73 GLY E 161 GLU E 165 5 5
HELIX 74 74 ARG E 166 GLY E 170 5 5
HELIX 75 75 GLY E 172 ASN E 190 1 19
HELIX 76 76 ASN E 281 GLU E 295 1 15
HELIX 77 77 THR E 303 GLY E 324 1 22
HELIX 78 78 SER F 10 TRP F 16 1 7
HELIX 79 79 TRP F 16 ALA F 23 1 8
HELIX 80 80 SER F 35 ASN F 46 1 12
HELIX 81 81 SER F 54 GLY F 60 1 7
HELIX 82 82 THR F 72 GLU F 74 5 3
HELIX 83 83 LEU F 75 ALA F 86 1 12
HELIX 84 84 THR F 99 GLY F 114 1 16
HELIX 85 85 HIS F 122 ASN F 125 5 4
HELIX 86 86 ALA F 126 GLU F 138 1 13
HELIX 87 87 PRO F 156 GLN F 160 5 5
HELIX 88 88 GLY F 161 GLU F 165 5 5
HELIX 89 89 GLY F 172 LEU F 189 1 18
HELIX 90 90 ASN F 281 GLU F 295 1 15
HELIX 91 91 THR F 303 GLY F 324 1 22
SHEET 1 A 5 GLU A 27 MET A 32 0
SHEET 2 A 5 ARG A 3 ILE A 7 1 N TRP A 4 O GLU A 27
SHEET 3 A 5 ALA A 66 VAL A 69 1 O TYR A 68 N ILE A 7
SHEET 4 A 5 HIS A 89 CYS A 92 1 O HIS A 89 N VAL A 67
SHEET 5 A 5 LEU A 117 THR A 119 1 O GLY A 118 N CYS A 92
SHEET 1 B 9 GLY A 271 GLN A 274 0
SHEET 2 B 9 THR A 263 ASN A 268 -1 N LEU A 266 O SER A 273
SHEET 3 B 9 SER A 249 ARG A 253 -1 N SER A 249 O ARG A 267
SHEET 4 B 9 GLY A 240 GLY A 245 -1 N VAL A 243 O LEU A 250
SHEET 5 B 9 PRO A 144 ALA A 152 -1 N ALA A 146 O HIS A 244
SHEET 6 B 9 ILE A 225 ALA A 231 1 O HIS A 229 N HIS A 151
SHEET 7 B 9 GLY A 213 PHE A 220 -1 N LEU A 218 O ALA A 226
SHEET 8 B 9 PRO A 193 HIS A 201 -1 N ALA A 194 O ARG A 219
SHEET 9 B 9 ALA A 327 GLU A 328 -1 O ALA A 327 N ALA A 196
SHEET 1 C 6 SER B 51 VAL B 52 0
SHEET 2 C 6 GLU B 27 MET B 32 1 N MET B 31 O VAL B 52
SHEET 3 C 6 ARG B 3 ILE B 7 1 N TRP B 4 O GLU B 27
SHEET 4 C 6 ALA B 66 VAL B 69 1 O TYR B 68 N ILE B 7
SHEET 5 C 6 HIS B 89 CYS B 92 1 O HIS B 89 N VAL B 67
SHEET 6 C 6 LEU B 117 THR B 119 1 O GLY B 118 N CYS B 92
SHEET 1 D 9 GLY B 271 GLN B 274 0
SHEET 2 D 9 THR B 263 ASN B 268 -1 N LEU B 266 O SER B 273
SHEET 3 D 9 SER B 249 ARG B 253 -1 N SER B 249 O ARG B 267
SHEET 4 D 9 GLY B 240 GLY B 245 -1 N VAL B 243 O LEU B 250
SHEET 5 D 9 PRO B 144 ALA B 152 -1 N ALA B 146 O HIS B 244
SHEET 6 D 9 ILE B 225 ALA B 231 1 O HIS B 229 N HIS B 151
SHEET 7 D 9 GLY B 213 PHE B 220 -1 N LEU B 218 O ALA B 226
SHEET 8 D 9 PRO B 193 HIS B 201 -1 N ALA B 194 O ARG B 219
SHEET 9 D 9 ALA B 327 GLU B 328 -1 O ALA B 327 N ALA B 196
SHEET 1 E 6 LYS C 50 VAL C 52 0
SHEET 2 E 6 GLU C 27 MET C 32 1 N MET C 31 O VAL C 52
SHEET 3 E 6 ARG C 3 ILE C 7 1 N TRP C 4 O GLU C 27
SHEET 4 E 6 ALA C 66 VAL C 69 1 O TYR C 68 N ILE C 7
SHEET 5 E 6 HIS C 89 CYS C 92 1 O HIS C 89 N VAL C 67
SHEET 6 E 6 LEU C 117 THR C 119 1 O GLY C 118 N CYS C 92
SHEET 1 F 9 GLY C 271 GLN C 274 0
SHEET 2 F 9 THR C 263 ASN C 268 -1 N LEU C 266 O SER C 273
SHEET 3 F 9 GLY C 248 ARG C 253 -1 N SER C 249 O ARG C 267
SHEET 4 F 9 GLY C 240 GLY C 245 -1 N PHE C 241 O GLY C 252
SHEET 5 F 9 PRO C 144 ALA C 152 -1 N ALA C 146 O HIS C 244
SHEET 6 F 9 ILE C 225 ALA C 231 1 O HIS C 229 N HIS C 151
SHEET 7 F 9 GLY C 213 PHE C 220 -1 N LEU C 218 O ALA C 226
SHEET 8 F 9 PRO C 193 HIS C 201 -1 N ALA C 194 O ARG C 219
SHEET 9 F 9 ALA C 327 GLU C 328 -1 O ALA C 327 N ALA C 196
SHEET 1 G 5 GLU D 27 MET D 32 0
SHEET 2 G 5 ARG D 3 ILE D 7 1 N TRP D 4 O GLU D 27
SHEET 3 G 5 ALA D 66 VAL D 69 1 O TYR D 68 N ILE D 7
SHEET 4 G 5 HIS D 89 CYS D 92 1 O HIS D 89 N VAL D 67
SHEET 5 G 5 LEU D 117 THR D 119 1 O GLY D 118 N CYS D 92
SHEET 1 H 9 GLU D 272 GLN D 274 0
SHEET 2 H 9 THR D 263 ARG D 267 -1 N LEU D 266 O SER D 273
SHEET 3 H 9 SER D 249 ARG D 253 -1 N ARG D 253 O THR D 263
SHEET 4 H 9 GLY D 240 GLY D 245 -1 N PHE D 241 O GLY D 252
SHEET 5 H 9 PRO D 144 ALA D 152 -1 N PHE D 150 O GLY D 240
SHEET 6 H 9 ILE D 225 ALA D 231 1 O GLN D 227 N ALA D 147
SHEET 7 H 9 GLY D 213 PHE D 220 -1 N VAL D 214 O ASP D 230
SHEET 8 H 9 PRO D 193 HIS D 201 -1 N HIS D 201 O GLY D 213
SHEET 9 H 9 ALA D 327 GLU D 328 -1 O ALA D 327 N ALA D 196
SHEET 1 I 6 SER E 51 VAL E 52 0
SHEET 2 I 6 GLU E 27 MET E 32 1 N MET E 31 O VAL E 52
SHEET 3 I 6 ARG E 3 ILE E 7 1 N TRP E 4 O GLU E 27
SHEET 4 I 6 ALA E 66 VAL E 69 1 O ALA E 66 N GLY E 5
SHEET 5 I 6 HIS E 89 CYS E 92 1 O LEU E 91 N VAL E 67
SHEET 6 I 6 LEU E 117 THR E 119 1 O GLY E 118 N CYS E 92
SHEET 1 J 9 GLY E 271 LEU E 275 0
SHEET 2 J 9 THR E 263 ASN E 268 -1 N VAL E 264 O LEU E 275
SHEET 3 J 9 GLY E 248 ARG E 253 -1 N SER E 249 O ARG E 267
SHEET 4 J 9 GLY E 240 GLY E 245 -1 N PHE E 241 O GLY E 252
SHEET 5 J 9 PRO E 144 ALA E 152 -1 N ALA E 146 O HIS E 244
SHEET 6 J 9 ILE E 225 ALA E 231 1 O HIS E 229 N HIS E 151
SHEET 7 J 9 GLY E 213 PHE E 220 -1 N LEU E 218 O ALA E 226
SHEET 8 J 9 PRO E 193 HIS E 201 -1 N ALA E 194 O ARG E 219
SHEET 9 J 9 ALA E 327 GLU E 328 -1 O ALA E 327 N ALA E 196
SHEET 1 K 5 GLU F 27 MET F 32 0
SHEET 2 K 5 ARG F 3 ILE F 7 1 N TRP F 4 O GLU F 27
SHEET 3 K 5 ALA F 66 VAL F 69 1 O TYR F 68 N ILE F 7
SHEET 4 K 5 HIS F 89 CYS F 92 1 O LEU F 91 N VAL F 67
SHEET 5 K 5 LEU F 117 THR F 119 1 O GLY F 118 N VAL F 90
SHEET 1 L 9 GLU F 272 GLN F 274 0
SHEET 2 L 9 THR F 263 ARG F 267 -1 N LEU F 266 O SER F 273
SHEET 3 L 9 SER F 249 ARG F 253 -1 N ILE F 251 O THR F 265
SHEET 4 L 9 GLY F 240 GLY F 245 -1 N VAL F 243 O LEU F 250
SHEET 5 L 9 PRO F 144 ALA F 152 -1 N ILE F 145 O HIS F 244
SHEET 6 L 9 ILE F 225 ALA F 231 1 O HIS F 229 N HIS F 151
SHEET 7 L 9 GLY F 213 PHE F 220 -1 N LEU F 218 O ALA F 226
SHEET 8 L 9 PRO F 193 HIS F 201 -1 N GLU F 195 O ARG F 219
SHEET 9 L 9 ALA F 327 GLU F 328 -1 O ALA F 327 N ALA F 196
CISPEP 1 LYS A 94 PRO A 95 0 -9.18
CISPEP 2 LYS B 94 PRO B 95 0 -14.42
CISPEP 3 LYS C 94 PRO C 95 0 -17.37
CISPEP 4 LYS D 94 PRO D 95 0 -16.35
CISPEP 5 LYS E 94 PRO E 95 0 -14.57
CISPEP 6 LYS F 94 PRO F 95 0 -9.30
SITE 1 AC1 5 LYS A 94 HIS A 180 NDP A1500 HOH A1738
SITE 2 AC1 5 HOH A1846
SITE 1 AC2 6 LYS B 94 ARG B 163 HIS B 180 NDP B2500
SITE 2 AC2 6 HOH B2614 HOH B2624
SITE 1 AC3 7 LYS C 94 HIS C 122 HIS C 180 GLN C 258
SITE 2 AC3 7 NDP C3500 HOH C3573 HOH C3713
SITE 1 AC4 6 LYS D 94 ARG D 163 ASP D 176 HIS D 180
SITE 2 AC4 6 NDP D4500 HOH D4580
SITE 1 AC5 4 LYS E 94 HIS E 180 NDP E5500 HOH E5562
SITE 1 AC6 6 LYS F 94 HIS F 180 GLN F 258 NDP F6500
SITE 2 AC6 6 HOH F6511 HOH F6566
SITE 1 AC7 28 GLY A 8 ALA A 9 SER A 10 THR A 11
SITE 2 AC7 28 ILE A 12 SER A 33 THR A 34 ARG A 38
SITE 3 AC7 28 SER A 70 THR A 71 ASN A 73 HIS A 76
SITE 4 AC7 28 GLU A 93 LYS A 94 ASN A 120 HIS A 122
SITE 5 AC7 28 TRP A 162 ARG A 163 TYR A 283 ACT A1502
SITE 6 AC7 28 HOH A1511 HOH A1545 HOH A1552 HOH A1568
SITE 7 AC7 28 HOH A1602 HOH A1641 HOH A1648 HOH A1757
SITE 1 AC8 29 GLY B 8 ALA B 9 SER B 10 THR B 11
SITE 2 AC8 29 ILE B 12 SER B 33 THR B 34 ARG B 38
SITE 3 AC8 29 SER B 70 THR B 71 THR B 72 ASN B 73
SITE 4 AC8 29 HIS B 76 GLU B 93 LYS B 94 ASN B 120
SITE 5 AC8 29 HIS B 122 LEU B 159 TRP B 162 ARG B 163
SITE 6 AC8 29 TYR B 283 ACT B2502 HOH B2512 HOH B2536
SITE 7 AC8 29 HOH B2537 HOH B2599 HOH B2606 HOH B2668
SITE 8 AC8 29 HOH B2766
SITE 1 AC9 28 GLY C 8 ALA C 9 SER C 10 THR C 11
SITE 2 AC9 28 ILE C 12 SER C 33 THR C 34 ARG C 38
SITE 3 AC9 28 SER C 70 THR C 71 ASN C 73 HIS C 76
SITE 4 AC9 28 GLU C 93 LYS C 94 ASN C 120 HIS C 122
SITE 5 AC9 28 TRP C 162 ARG C 163 GLN C 258 TYR C 283
SITE 6 AC9 28 ACT C3502 HOH C3506 HOH C3518 HOH C3530
SITE 7 AC9 28 HOH C3561 HOH C3602 HOH C3626 HOH C3663
SITE 1 BC1 24 GLY D 8 ALA D 9 SER D 10 THR D 11
SITE 2 BC1 24 ILE D 12 SER D 33 THR D 34 ARG D 38
SITE 3 BC1 24 SER D 70 THR D 71 ASN D 73 HIS D 76
SITE 4 BC1 24 GLU D 93 LYS D 94 ASN D 120 TRP D 162
SITE 5 BC1 24 ARG D 163 ASP D 176 GLN D 258 TYR D 283
SITE 6 BC1 24 ACT D4502 HOH D4510 HOH D4525 HOH D4554
SITE 1 BC2 30 GLY E 8 ALA E 9 SER E 10 THR E 11
SITE 2 BC2 30 ILE E 12 SER E 33 THR E 34 ARG E 38
SITE 3 BC2 30 SER E 70 THR E 71 ASN E 73 HIS E 76
SITE 4 BC2 30 GLU E 93 LYS E 94 ASN E 120 HIS E 122
SITE 5 BC2 30 TRP E 162 ARG E 163 ASP E 176 GLN E 258
SITE 6 BC2 30 TYR E 283 ACT E5502 HOH E5515 HOH E5542
SITE 7 BC2 30 HOH E5544 HOH E5599 HOH E5647 HOH E5694
SITE 8 BC2 30 HOH E5712 HOH E5717
SITE 1 BC3 25 GLY F 8 ALA F 9 SER F 10 THR F 11
SITE 2 BC3 25 ILE F 12 SER F 33 THR F 34 ARG F 38
SITE 3 BC3 25 SER F 70 THR F 71 THR F 72 ASN F 73
SITE 4 BC3 25 HIS F 76 GLU F 93 LYS F 94 ASN F 120
SITE 5 BC3 25 HIS F 122 LEU F 159 TRP F 162 ARG F 163
SITE 6 BC3 25 GLN F 258 TYR F 283 ACT F6502 HOH F6532
SITE 7 BC3 25 HOH F6580
CRYST1 97.190 84.900 150.940 90.00 96.30 90.00 P 1 21 1 12
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 0.010290 0.000000 0.001140 0.00000
SCALE2 0.000000 0.011780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006670 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
