HEADER HYDROLASE 07-DEC-09 2X09
TITLE INHIBITION OF THE EXO-BETA-D-GLUCOSAMINIDASE CSXA BY A GLUCOSAMINE-
TITLE 2 CONFIGURED CASTANOSPERMINE AND AN AMINO-AUSTRALINE ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXO-BETA-D-GLUCOSAMINIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-1032;
COMPND 5 EC: 3.2.1.165;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS ORIENTALIS;
SOURCE 3 ORGANISM_TAXID: 31958;
SOURCE 4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 457428;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TK24;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PFD666
KEYWDS EXO-BETA-D-GLUCOSAMINIDASE, GLYCOSIDE HYDROLASE, GH2, CSXA,
KEYWDS 2 HYDROLASE, GLYCOSIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.PLUVINAGE,M.G.GHINET,R.BRZEZINSKI,A.B.BORASTON,K.A.STUBBS
REVDAT 2 20-DEC-23 2X09 1 REMARK LINK
REVDAT 1 09-FEB-10 2X09 0
JRNL AUTH B.PLUVINAGE,M.G.GHINET,R.BRZEZINSKI,A.B.BORASTON,K.A.STUBBS
JRNL TITL INHIBITION OF THE EXO-BETA-D-GLUCOSAMINIDASE CSXA BY A
JRNL TITL 2 GLUCOSAMINE-CONFIGURED CASTANOSPERMINE AND AN
JRNL TITL 3 AMINO-AUSTRALINE ANALOGUE.
JRNL REF ORG.BIOMOL.CHEM. V. 7 4169 2009
JRNL REFN ISSN 1477-0520
JRNL PMID 19795054
JRNL DOI 10.1039/B913235J
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 72891
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3652
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4876
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 262
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13024
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 1441
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.507
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.273
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.182
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.659
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.871
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13363 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18244 ; 1.352 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1700 ; 6.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 578 ;34.992 ;24.325
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2037 ;15.618 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;18.028 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2011 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10305 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 8450 ; 0.482 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13601 ; 0.891 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4913 ; 1.497 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4642 ; 2.327 ; 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. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 2X09 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1290041802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 SCALE, MERGE INTENSITIES
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72891
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2VZS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 60.97500
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 VAL A 1
REMARK 465 SER A 2
REMARK 465 PHE A 3
REMARK 465 ARG A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 THR A 8
REMARK 465 ARG A 9
REMARK 465 ILE A 10
REMARK 465 PRO A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 MET A 15
REMARK 465 THR A 16
REMARK 465 VAL A 17
REMARK 465 THR A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 VAL A 24
REMARK 465 CYS A 25
REMARK 465 GLY A 26
REMARK 465 VAL A 27
REMARK 465 THR A 28
REMARK 465 THR A 29
REMARK 465 ALA A 30
REMARK 465 PRO A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 THR A 34
REMARK 465 GLY A 35
REMARK 465 ALA A 36
REMARK 465 GLU A 37
REMARK 465 VAL A 38
REMARK 465 ALA A 39
REMARK 465 VAL A 40
REMARK 465 PRO A 41
REMARK 465 LEU A 42
REMARK 465 SER A 43
REMARK 465 VAL A 44
REMARK 465 GLY A 45
REMARK 465 ALA A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 GLY A 900
REMARK 465 SER A 901
REMARK 465 GLY A 902
REMARK 465 PRO A 903
REMARK 465 GLY A 904
REMARK 465 PRO A 905
REMARK 465 SER A 906
REMARK 465 ASP A 907
REMARK 465 PRO A 908
REMARK 465 VAL A 909
REMARK 465 ASP A 910
REMARK 465 TYR A 911
REMARK 465 GLN A 912
REMARK 465 ALA A 913
REMARK 465 GLU A 914
REMARK 465 ASP A 915
REMARK 465 ALA A 916
REMARK 465 THR A 917
REMARK 465 ILE A 918
REMARK 465 VAL A 919
REMARK 465 GLN A 920
REMARK 465 GLY A 921
REMARK 465 ALA A 922
REMARK 465 VAL A 923
REMARK 465 GLU A 924
REMARK 465 SER A 925
REMARK 465 ASN A 926
REMARK 465 HIS A 927
REMARK 465 ALA A 928
REMARK 465 GLY A 929
REMARK 465 TYR A 930
REMARK 465 THR A 931
REMARK 465 GLY A 932
REMARK 465 THR A 933
REMARK 465 GLY A 934
REMARK 465 PHE A 935
REMARK 465 VAL A 936
REMARK 465 ASN A 937
REMARK 465 TYR A 938
REMARK 465 ASP A 939
REMARK 465 ASN A 940
REMARK 465 VAL A 941
REMARK 465 ALA A 942
REMARK 465 GLY A 943
REMARK 465 SER A 944
REMARK 465 SER A 945
REMARK 465 VAL A 946
REMARK 465 GLU A 947
REMARK 465 TRP A 948
REMARK 465 THR A 949
REMARK 465 VAL A 950
REMARK 465 THR A 951
REMARK 465 VAL A 952
REMARK 465 PRO A 953
REMARK 465 SER A 954
REMARK 465 ALA A 955
REMARK 465 GLY A 956
REMARK 465 THR A 957
REMARK 465 TYR A 958
REMARK 465 ASP A 959
REMARK 465 VAL A 960
REMARK 465 VAL A 961
REMARK 465 VAL A 962
REMARK 465 ARG A 963
REMARK 465 TYR A 964
REMARK 465 ALA A 965
REMARK 465 ASN A 966
REMARK 465 GLY A 967
REMARK 465 THR A 968
REMARK 465 THR A 969
REMARK 465 THR A 970
REMARK 465 SER A 971
REMARK 465 ARG A 972
REMARK 465 PRO A 973
REMARK 465 LEU A 974
REMARK 465 ASP A 975
REMARK 465 PHE A 976
REMARK 465 SER A 977
REMARK 465 VAL A 978
REMARK 465 ASN A 979
REMARK 465 GLY A 980
REMARK 465 SER A 981
REMARK 465 ILE A 982
REMARK 465 SER A 983
REMARK 465 ALA A 984
REMARK 465 SER A 985
REMARK 465 GLY A 986
REMARK 465 VAL A 987
REMARK 465 ALA A 988
REMARK 465 PHE A 989
REMARK 465 GLY A 990
REMARK 465 SER A 991
REMARK 465 THR A 992
REMARK 465 GLY A 993
REMARK 465 THR A 994
REMARK 465 TRP A 995
REMARK 465 PRO A 996
REMARK 465 ALA A 997
REMARK 465 TRP A 998
REMARK 465 THR A 999
REMARK 465 THR A 1000
REMARK 465 LYS A 1001
REMARK 465 THR A 1002
REMARK 465 VAL A 1003
REMARK 465 ARG A 1004
REMARK 465 VAL A 1005
REMARK 465 THR A 1006
REMARK 465 LEU A 1007
REMARK 465 ALA A 1008
REMARK 465 ALA A 1009
REMARK 465 GLY A 1010
REMARK 465 VAL A 1011
REMARK 465 ASN A 1012
REMARK 465 LYS A 1013
REMARK 465 ILE A 1014
REMARK 465 LYS A 1015
REMARK 465 ALA A 1016
REMARK 465 VAL A 1017
REMARK 465 ALA A 1018
REMARK 465 THR A 1019
REMARK 465 THR A 1020
REMARK 465 ALA A 1021
REMARK 465 ASN A 1022
REMARK 465 GLY A 1023
REMARK 465 GLY A 1024
REMARK 465 PRO A 1025
REMARK 465 ASN A 1026
REMARK 465 VAL A 1027
REMARK 465 ASP A 1028
REMARK 465 LYS A 1029
REMARK 465 ILE A 1030
REMARK 465 THR A 1031
REMARK 465 LEU A 1032
REMARK 465 VAL B 1
REMARK 465 SER B 2
REMARK 465 PHE B 3
REMARK 465 ARG B 4
REMARK 465 GLN B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 THR B 8
REMARK 465 ARG B 9
REMARK 465 ILE B 10
REMARK 465 PRO B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 ALA B 14
REMARK 465 MET B 15
REMARK 465 THR B 16
REMARK 465 VAL B 17
REMARK 465 THR B 18
REMARK 465 ALA B 19
REMARK 465 LEU B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 VAL B 24
REMARK 465 CYS B 25
REMARK 465 GLY B 26
REMARK 465 VAL B 27
REMARK 465 THR B 28
REMARK 465 THR B 29
REMARK 465 ALA B 30
REMARK 465 PRO B 31
REMARK 465 ALA B 32
REMARK 465 ALA B 33
REMARK 465 THR B 34
REMARK 465 GLY B 35
REMARK 465 ALA B 36
REMARK 465 GLU B 37
REMARK 465 VAL B 38
REMARK 465 ALA B 39
REMARK 465 VAL B 40
REMARK 465 PRO B 41
REMARK 465 LEU B 42
REMARK 465 SER B 43
REMARK 465 VAL B 44
REMARK 465 GLY B 45
REMARK 465 ALA B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 GLY B 900
REMARK 465 SER B 901
REMARK 465 GLY B 902
REMARK 465 PRO B 903
REMARK 465 GLY B 904
REMARK 465 PRO B 905
REMARK 465 SER B 906
REMARK 465 ASP B 907
REMARK 465 PRO B 908
REMARK 465 VAL B 909
REMARK 465 ASP B 910
REMARK 465 TYR B 911
REMARK 465 GLN B 912
REMARK 465 ALA B 913
REMARK 465 GLU B 914
REMARK 465 ASP B 915
REMARK 465 ALA B 916
REMARK 465 THR B 917
REMARK 465 ILE B 918
REMARK 465 VAL B 919
REMARK 465 GLN B 920
REMARK 465 GLY B 921
REMARK 465 ALA B 922
REMARK 465 VAL B 923
REMARK 465 GLU B 924
REMARK 465 SER B 925
REMARK 465 ASN B 926
REMARK 465 HIS B 927
REMARK 465 ALA B 928
REMARK 465 GLY B 929
REMARK 465 TYR B 930
REMARK 465 THR B 931
REMARK 465 GLY B 932
REMARK 465 THR B 933
REMARK 465 GLY B 934
REMARK 465 PHE B 935
REMARK 465 VAL B 936
REMARK 465 ASN B 937
REMARK 465 TYR B 938
REMARK 465 ASP B 939
REMARK 465 ASN B 940
REMARK 465 VAL B 941
REMARK 465 ALA B 942
REMARK 465 GLY B 943
REMARK 465 SER B 944
REMARK 465 SER B 945
REMARK 465 VAL B 946
REMARK 465 GLU B 947
REMARK 465 TRP B 948
REMARK 465 THR B 949
REMARK 465 VAL B 950
REMARK 465 THR B 951
REMARK 465 VAL B 952
REMARK 465 PRO B 953
REMARK 465 SER B 954
REMARK 465 ALA B 955
REMARK 465 GLY B 956
REMARK 465 THR B 957
REMARK 465 TYR B 958
REMARK 465 ASP B 959
REMARK 465 VAL B 960
REMARK 465 VAL B 961
REMARK 465 VAL B 962
REMARK 465 ARG B 963
REMARK 465 TYR B 964
REMARK 465 ALA B 965
REMARK 465 ASN B 966
REMARK 465 GLY B 967
REMARK 465 THR B 968
REMARK 465 THR B 969
REMARK 465 THR B 970
REMARK 465 SER B 971
REMARK 465 ARG B 972
REMARK 465 PRO B 973
REMARK 465 LEU B 974
REMARK 465 ASP B 975
REMARK 465 PHE B 976
REMARK 465 SER B 977
REMARK 465 VAL B 978
REMARK 465 ASN B 979
REMARK 465 GLY B 980
REMARK 465 SER B 981
REMARK 465 ILE B 982
REMARK 465 SER B 983
REMARK 465 ALA B 984
REMARK 465 SER B 985
REMARK 465 GLY B 986
REMARK 465 VAL B 987
REMARK 465 ALA B 988
REMARK 465 PHE B 989
REMARK 465 GLY B 990
REMARK 465 SER B 991
REMARK 465 THR B 992
REMARK 465 GLY B 993
REMARK 465 THR B 994
REMARK 465 TRP B 995
REMARK 465 PRO B 996
REMARK 465 ALA B 997
REMARK 465 TRP B 998
REMARK 465 THR B 999
REMARK 465 THR B 1000
REMARK 465 LYS B 1001
REMARK 465 THR B 1002
REMARK 465 VAL B 1003
REMARK 465 ARG B 1004
REMARK 465 VAL B 1005
REMARK 465 THR B 1006
REMARK 465 LEU B 1007
REMARK 465 ALA B 1008
REMARK 465 ALA B 1009
REMARK 465 GLY B 1010
REMARK 465 VAL B 1011
REMARK 465 ASN B 1012
REMARK 465 LYS B 1013
REMARK 465 ILE B 1014
REMARK 465 LYS B 1015
REMARK 465 ALA B 1016
REMARK 465 VAL B 1017
REMARK 465 ALA B 1018
REMARK 465 THR B 1019
REMARK 465 THR B 1020
REMARK 465 ALA B 1021
REMARK 465 ASN B 1022
REMARK 465 GLY B 1023
REMARK 465 GLY B 1024
REMARK 465 PRO B 1025
REMARK 465 ASN B 1026
REMARK 465 VAL B 1027
REMARK 465 ASP B 1028
REMARK 465 LYS B 1029
REMARK 465 ILE B 1030
REMARK 465 THR B 1031
REMARK 465 LEU B 1032
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 179 CB OG1 CG2
REMARK 470 ASP A 899 CA C O CB CG OD1 OD2
REMARK 470 THR B 179 CB OG1 CG2
REMARK 470 ASP B 899 CA C O CB CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 127 CD1 CD2
REMARK 480 GLU A 430 CG CD OE1 OE2
REMARK 480 LYS A 432 CD CE NZ
REMARK 480 LYS A 573 CD CE NZ
REMARK 480 LYS A 758 NZ
REMARK 480 LYS A 770 NZ
REMARK 480 ALA A 898 CB
REMARK 480 ARG B 297 NE CZ NH1 NH2
REMARK 480 LYS B 530 CE NZ
REMARK 480 LYS B 573 NZ
REMARK 480 LYS B 758 CE NZ
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 CA THR B 179 O HOH B 2149 2.14
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 OD1 ASP B 246 CD CD A 1902 2557 1.94
REMARK 500 NE2 HIS B 244 CD CD A 1902 2557 2.10
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 LEU A 127 CG LEU A 127 CD1 -0.579
REMARK 500 LEU A 127 CG LEU A 127 CD2 0.287
REMARK 500 LYS A 432 CG LYS A 432 CD -0.358
REMARK 500 ALA A 898 CA ALA A 898 CB -0.201
REMARK 500 ARG B 297 CD ARG B 297 NE -0.586
REMARK 500 LYS B 530 CD LYS B 530 CE 0.616
REMARK 500 LYS B 573 CE LYS B 573 NZ -0.415
REMARK 500 LYS B 758 CD LYS B 758 CE -0.552
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 127 CB - CG - CD1 ANGL. DEV. = 39.4 DEGREES
REMARK 500 LEU A 127 CB - CG - CD2 ANGL. DEV. = -24.2 DEGREES
REMARK 500 LEU A 144 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG A 335 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LYS A 573 CB - CG - CD ANGL. DEV. = -23.9 DEGREES
REMARK 500 LYS A 758 CD - CE - NZ ANGL. DEV. = -14.2 DEGREES
REMARK 500 ALA A 898 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU B 144 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG B 297 CG - CD - NE ANGL. DEV. = 49.1 DEGREES
REMARK 500 ARG B 297 CD - NE - CZ ANGL. DEV. = 20.7 DEGREES
REMARK 500 ARG B 335 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LYS B 530 CG - CD - CE ANGL. DEV. = -32.4 DEGREES
REMARK 500 LYS B 573 CD - CE - NZ ANGL. DEV. = 26.9 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 SER A 106 -135.22 45.82
REMARK 500 LYS A 146 157.41 179.31
REMARK 500 ALA A 157 144.91 -170.91
REMARK 500 SER A 198 -131.91 -137.38
REMARK 500 ILE A 202 -119.79 54.20
REMARK 500 ALA A 205 -125.59 -147.34
REMARK 500 SER A 224 165.90 177.84
REMARK 500 ASP A 421 -157.26 -157.73
REMARK 500 SER A 468 -78.13 -117.91
REMARK 500 ILE A 504 -63.62 -99.65
REMARK 500 SER A 537 -151.54 58.19
REMARK 500 GLU A 541 96.99 174.39
REMARK 500 ARG A 577 -92.66 -88.11
REMARK 500 ASN A 602 -179.93 -174.87
REMARK 500 ASN A 663 -165.20 -111.58
REMARK 500 ASP A 780 -165.75 -118.09
REMARK 500 SER A 801 -154.69 -118.97
REMARK 500 SER B 106 -132.97 49.16
REMARK 500 PRO B 190 151.17 -49.85
REMARK 500 SER B 198 -135.40 -136.31
REMARK 500 ILE B 202 -119.00 46.81
REMARK 500 ALA B 205 -125.44 -148.08
REMARK 500 ASN B 352 45.45 39.41
REMARK 500 PRO B 399 171.07 -58.01
REMARK 500 ASP B 421 -154.15 -161.52
REMARK 500 SER B 468 -83.23 -114.39
REMARK 500 ILE B 504 -61.29 -93.63
REMARK 500 ALA B 535 81.93 -65.71
REMARK 500 SER B 537 -159.35 62.79
REMARK 500 GLU B 541 107.53 -178.38
REMARK 500 PRO B 549 -175.49 -68.17
REMARK 500 ARG B 577 -97.23 -92.16
REMARK 500 ASN B 602 -179.14 -174.33
REMARK 500 ASN B 663 -156.23 -117.81
REMARK 500 ARG B 685 16.70 56.62
REMARK 500 SER B 801 -164.78 -116.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2056 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A2070 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A2115 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A2130 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B2079 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B2144 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B2309 DISTANCE = 6.08 ANGSTROMS
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 CD A1901 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 244 NE2
REMARK 620 2 ASP A 246 OD1 100.1
REMARK 620 3 HOH A2212 O 101.9 110.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1902 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 296 OD2
REMARK 620 2 ASP A 296 OD1 56.9
REMARK 620 3 HOH A2261 O 101.2 104.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1901 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 428 OD1
REMARK 620 2 GLY B 429 O 101.5
REMARK 620 3 GLU B 431 O 91.0 95.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X09 A 1900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X09 B 1900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X05 RELATED DB: PDB
REMARK 900 INHIBITION OF THE EXO-BETA-D-GLUCOSAMINIDASE CSXA BY A GLUCOSAMINE-
REMARK 900 CONFIGURED CASTANOSPERMINE AND AN AMINO-AUSTRALINE ANALOGUE
REMARK 900 RELATED ID: 2VZR RELATED DB: PDB
REMARK 900 C-TERMINAL CBM35 FROM AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA
REMARK 900 IN COMPLEX WITH GLUCURONIC ACID
REMARK 900 RELATED ID: 2VZU RELATED DB: PDB
REMARK 900 COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO- CHITOSANASE CSXA D469A
REMARK 900 WITH PNP-BETA-D- GLUCOSAMINE
REMARK 900 RELATED ID: 2VZS RELATED DB: PDB
REMARK 900 CHITOSAN PRODUCT COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-
REMARK 900 CHITOSANASE CSXA
REMARK 900 RELATED ID: 2VZT RELATED DB: PDB
REMARK 900 COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO- CHITOSANASE CSXA E541A
REMARK 900 WITH PNP-BETA-D- GLUCOSAMINE
REMARK 900 RELATED ID: 2VZO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA
REMARK 900 RELATED ID: 2VZQ RELATED DB: PDB
REMARK 900 C-TERMINAL CBM35 FROM AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA
REMARK 900 IN COMPLEX WITH DIGALACTURONIC ACID
REMARK 900 RELATED ID: 2VZP RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF THE C- TERMINAL CBM35 FROM
REMARK 900 AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA
REMARK 900 RELATED ID: 2VZV RELATED DB: PDB
REMARK 900 SUBSTRATE COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA
REMARK 900 E541A WITH CHITOSAN
DBREF 2X09 A 1 1 PDB 2X09 2X09 1 1
DBREF 2X09 A 2 1032 UNP Q56F26 Q56F26_AMYOR 2 1032
DBREF 2X09 B 1 1 PDB 2X09 2X09 1 1
DBREF 2X09 B 2 1032 UNP Q56F26 Q56F26_AMYOR 2 1032
SEQADV 2X09 ASN A 750 UNP Q56F26 TRP 750 CONFLICT
SEQADV 2X09 ASN B 750 UNP Q56F26 TRP 750 CONFLICT
SEQRES 1 A 1032 VAL SER PHE ARG GLN LYS ARG THR ARG ILE PRO LEU LEU
SEQRES 2 A 1032 ALA MET THR VAL THR ALA LEU ALA ALA ALA VAL CYS GLY
SEQRES 3 A 1032 VAL THR THR ALA PRO ALA ALA THR GLY ALA GLU VAL ALA
SEQRES 4 A 1032 VAL PRO LEU SER VAL GLY ALA ALA ALA GLY ASN ALA THR
SEQRES 5 A 1032 PRO ILE PRO GLY TYR VAL ILE GLN SER SER ALA GLN VAL
SEQRES 6 A 1032 SER ASP ASP SER ALA VAL SER LYS PRO GLY PHE PRO THR
SEQRES 7 A 1032 SER GLY TRP TYR PRO VAL SER SER ARG SER THR VAL TYR
SEQRES 8 A 1032 ALA GLY LEU LEU GLN ASN GLY LYS TYR ALA ASP PRO PHE
SEQRES 9 A 1032 TYR SER THR ASN MET GLN ASN VAL PRO ALA ALA GLN PHE
SEQRES 10 A 1032 SER VAL PRO TRP TRP TYR ARG THR ASP LEU ASN VAL ASP
SEQRES 11 A 1032 ASP THR SER SER ARG THR TYR LEU ASP PHE SER GLY VAL
SEQRES 12 A 1032 LEU SER LYS ALA ASP VAL TRP VAL ASN GLY THR LYS VAL
SEQRES 13 A 1032 ALA THR LYS ASP GLN VAL ASN GLY ALA TYR THR ARG HIS
SEQRES 14 A 1032 ASP LEU ASP ILE THR ALA GLN VAL HIS THR GLY VAL ASN
SEQRES 15 A 1032 SER VAL ALA PHE LYS VAL TYR PRO ASN ASP PRO ASN ARG
SEQRES 16 A 1032 ASP LEU SER MET GLY TRP ILE ASP TRP ALA GLN THR PRO
SEQRES 17 A 1032 PRO ASP GLN ASN MET GLY ILE VAL ARG ASP VAL LEU VAL
SEQRES 18 A 1032 ARG ARG SER GLY ALA VAL ALA LEU ARG SER ALA HIS VAL
SEQRES 19 A 1032 ILE GLN LYS LEU ASN SER ALA LEU ASP HIS ALA ASP LEU
SEQRES 20 A 1032 THR VAL LYS ALA ASP VAL ARG ASN ASP SER ALA ASN ALA
SEQRES 21 A 1032 VAL GLN THR THR VAL ALA GLY THR VAL ALA GLY LYS PRO
SEQRES 22 A 1032 ILE SER GLN THR VAL SER LEU ALA ALA LYS GLU ARG LYS
SEQRES 23 A 1032 THR VAL THR PHE PRO LEU VAL GLY LEU ASP ARG PRO ASN
SEQRES 24 A 1032 VAL TRP TRP PRO ALA GLY MET GLY GLY GLN HIS ARG TYR
SEQRES 25 A 1032 ASP LEU ASP LEU THR ALA SER VAL GLY GLY THR PRO SER
SEQRES 26 A 1032 ASP ALA ALA LYS SER LYS PHE GLY VAL ARG ASP VAL LYS
SEQRES 27 A 1032 ALA THR LEU ASN SER SER GLY GLY ARG GLN TYR SER VAL
SEQRES 28 A 1032 ASN GLY LYS PRO LEU LEU ILE ARG GLY GLY GLY TYR THR
SEQRES 29 A 1032 PRO ASP LEU PHE LEU ARG TRP ASN GLU THR ALA ALA ALA
SEQRES 30 A 1032 ASP LYS LEU LYS TYR VAL LEU ASN LEU GLY LEU ASN THR
SEQRES 31 A 1032 VAL ARG LEU GLU GLY HIS ILE GLU PRO ASP GLU PHE PHE
SEQRES 32 A 1032 ASP ILE ALA ASP ASP LEU GLY VAL LEU THR MET PRO GLY
SEQRES 33 A 1032 TRP GLU CYS CYS ASP LYS TRP GLU GLY GLN VAL ASN GLY
SEQRES 34 A 1032 GLU GLU LYS GLY GLU PRO TRP VAL GLU SER ASP TYR PRO
SEQRES 35 A 1032 ILE ALA LYS ALA SER MET PHE SER GLU ALA GLU ARG LEU
SEQRES 36 A 1032 ARG ASP HIS PRO SER VAL ILE SER PHE HIS ILE GLY SER
SEQRES 37 A 1032 ASP PHE ALA PRO ASP ARG ARG ILE GLU GLN GLY TYR LEU
SEQRES 38 A 1032 ASP ALA MET LYS ALA ALA ASP PHE LEU LEU PRO VAL ILE
SEQRES 39 A 1032 PRO ALA ALA SER ALA ARG PRO SER PRO ILE THR GLY ALA
SEQRES 40 A 1032 SER GLY MET LYS MET ASN GLY PRO TYR ASP TYR VAL PRO
SEQRES 41 A 1032 PRO VAL TYR TRP TYR ASP LYS SER GLN LYS ASP ARG GLY
SEQRES 42 A 1032 GLY ALA TRP SER PHE ASN SER GLU THR SER ALA GLY VAL
SEQRES 43 A 1032 ASP ILE PRO THR MET ASP THR LEU LYS ARG MET MET SER
SEQRES 44 A 1032 ALA SER GLU LEU ASP THR MET TRP LYS ASN PRO SER ALA
SEQRES 45 A 1032 LYS GLN TYR HIS ARG SER SER SER ASP THR PHE GLY ASN
SEQRES 46 A 1032 LEU LYS LEU PHE GLY ASP ALA LEU THR LYS ARG TYR GLY
SEQRES 47 A 1032 ALA SER ALA ASN LEU ASN ASP PHE VAL ARG LYS ALA GLN
SEQRES 48 A 1032 LEU SER GLN TYR GLU ASN VAL ARG ALA GLU PHE GLU SER
SEQRES 49 A 1032 HIS SER ARG ASN TYR THR ASP SER THR ASN PRO SER THR
SEQRES 50 A 1032 GLY LEU ILE TYR TRP MET LEU ASN SER PRO TRP THR SER
SEQRES 51 A 1032 LEU HIS TRP GLN LEU PHE ASP ALA TYR MET ASP GLN ASN
SEQRES 52 A 1032 GLY ALA TYR TYR GLY ALA LYS LYS ALA ASN GLU PRO LEU
SEQRES 53 A 1032 HIS ILE GLN TYR SER HIS ASP ASN ARG SER VAL VAL VAL
SEQRES 54 A 1032 ILE ASN GLN THR SER ASN ALA VAL SER GLY LEU THR ALA
SEQRES 55 A 1032 THR THR LYS LEU TYR ASN LEU ASP GLY THR GLU LYS TYR
SEQRES 56 A 1032 SER ASN THR LYS THR GLY LEU SER VAL GLY ALA LEU GLY
SEQRES 57 A 1032 ALA LYS ALA THR ALA VAL THR VAL PRO ALA VAL SER GLY
SEQRES 58 A 1032 LEU SER THR THR TYR LEU ALA LYS ASN VAL LEU THR ASP
SEQRES 59 A 1032 SER SER GLY LYS GLU VAL SER ARG ASN VAL TYR TRP LEU
SEQRES 60 A 1032 SER THR LYS ALA ASP THR LEU ASN TRP GLY GLY SER ASP
SEQRES 61 A 1032 TRP TYR TYR THR PRO GLN SER ALA PHE ALA ASP LEU SER
SEQRES 62 A 1032 GLY LEU ASN ASN LEU GLY GLN SER ALA VAL GLY ALA THR
SEQRES 63 A 1032 ALA ASN SER VAL ALA GLY ALA ASP GLY THR THR THR THR
SEQRES 64 A 1032 THR VAL THR LEU LYS ASN THR SER GLY GLY ARG LEU PRO
SEQRES 65 A 1032 ALA PHE TYR VAL ASP SER LYS VAL VAL ASP SER ALA GLY
SEQRES 66 A 1032 LYS PRO VAL LEU PRO VAL GLU TRP ASN ASP ASN ALA VAL
SEQRES 67 A 1032 SER LEU TRP PRO GLY GLU THR THR THR LEU THR ALA LYS
SEQRES 68 A 1032 TYR ARG THR ALA ASP LEU LYS GLY SER LYS PRO SER VAL
SEQRES 69 A 1032 ARG ILE SER GLY TRP ASN THR GLY THR GLN THR VAL PRO
SEQRES 70 A 1032 ALA ASP GLY SER GLY PRO GLY PRO SER ASP PRO VAL ASP
SEQRES 71 A 1032 TYR GLN ALA GLU ASP ALA THR ILE VAL GLN GLY ALA VAL
SEQRES 72 A 1032 GLU SER ASN HIS ALA GLY TYR THR GLY THR GLY PHE VAL
SEQRES 73 A 1032 ASN TYR ASP ASN VAL ALA GLY SER SER VAL GLU TRP THR
SEQRES 74 A 1032 VAL THR VAL PRO SER ALA GLY THR TYR ASP VAL VAL VAL
SEQRES 75 A 1032 ARG TYR ALA ASN GLY THR THR THR SER ARG PRO LEU ASP
SEQRES 76 A 1032 PHE SER VAL ASN GLY SER ILE SER ALA SER GLY VAL ALA
SEQRES 77 A 1032 PHE GLY SER THR GLY THR TRP PRO ALA TRP THR THR LYS
SEQRES 78 A 1032 THR VAL ARG VAL THR LEU ALA ALA GLY VAL ASN LYS ILE
SEQRES 79 A 1032 LYS ALA VAL ALA THR THR ALA ASN GLY GLY PRO ASN VAL
SEQRES 80 A 1032 ASP LYS ILE THR LEU
SEQRES 1 B 1032 VAL SER PHE ARG GLN LYS ARG THR ARG ILE PRO LEU LEU
SEQRES 2 B 1032 ALA MET THR VAL THR ALA LEU ALA ALA ALA VAL CYS GLY
SEQRES 3 B 1032 VAL THR THR ALA PRO ALA ALA THR GLY ALA GLU VAL ALA
SEQRES 4 B 1032 VAL PRO LEU SER VAL GLY ALA ALA ALA GLY ASN ALA THR
SEQRES 5 B 1032 PRO ILE PRO GLY TYR VAL ILE GLN SER SER ALA GLN VAL
SEQRES 6 B 1032 SER ASP ASP SER ALA VAL SER LYS PRO GLY PHE PRO THR
SEQRES 7 B 1032 SER GLY TRP TYR PRO VAL SER SER ARG SER THR VAL TYR
SEQRES 8 B 1032 ALA GLY LEU LEU GLN ASN GLY LYS TYR ALA ASP PRO PHE
SEQRES 9 B 1032 TYR SER THR ASN MET GLN ASN VAL PRO ALA ALA GLN PHE
SEQRES 10 B 1032 SER VAL PRO TRP TRP TYR ARG THR ASP LEU ASN VAL ASP
SEQRES 11 B 1032 ASP THR SER SER ARG THR TYR LEU ASP PHE SER GLY VAL
SEQRES 12 B 1032 LEU SER LYS ALA ASP VAL TRP VAL ASN GLY THR LYS VAL
SEQRES 13 B 1032 ALA THR LYS ASP GLN VAL ASN GLY ALA TYR THR ARG HIS
SEQRES 14 B 1032 ASP LEU ASP ILE THR ALA GLN VAL HIS THR GLY VAL ASN
SEQRES 15 B 1032 SER VAL ALA PHE LYS VAL TYR PRO ASN ASP PRO ASN ARG
SEQRES 16 B 1032 ASP LEU SER MET GLY TRP ILE ASP TRP ALA GLN THR PRO
SEQRES 17 B 1032 PRO ASP GLN ASN MET GLY ILE VAL ARG ASP VAL LEU VAL
SEQRES 18 B 1032 ARG ARG SER GLY ALA VAL ALA LEU ARG SER ALA HIS VAL
SEQRES 19 B 1032 ILE GLN LYS LEU ASN SER ALA LEU ASP HIS ALA ASP LEU
SEQRES 20 B 1032 THR VAL LYS ALA ASP VAL ARG ASN ASP SER ALA ASN ALA
SEQRES 21 B 1032 VAL GLN THR THR VAL ALA GLY THR VAL ALA GLY LYS PRO
SEQRES 22 B 1032 ILE SER GLN THR VAL SER LEU ALA ALA LYS GLU ARG LYS
SEQRES 23 B 1032 THR VAL THR PHE PRO LEU VAL GLY LEU ASP ARG PRO ASN
SEQRES 24 B 1032 VAL TRP TRP PRO ALA GLY MET GLY GLY GLN HIS ARG TYR
SEQRES 25 B 1032 ASP LEU ASP LEU THR ALA SER VAL GLY GLY THR PRO SER
SEQRES 26 B 1032 ASP ALA ALA LYS SER LYS PHE GLY VAL ARG ASP VAL LYS
SEQRES 27 B 1032 ALA THR LEU ASN SER SER GLY GLY ARG GLN TYR SER VAL
SEQRES 28 B 1032 ASN GLY LYS PRO LEU LEU ILE ARG GLY GLY GLY TYR THR
SEQRES 29 B 1032 PRO ASP LEU PHE LEU ARG TRP ASN GLU THR ALA ALA ALA
SEQRES 30 B 1032 ASP LYS LEU LYS TYR VAL LEU ASN LEU GLY LEU ASN THR
SEQRES 31 B 1032 VAL ARG LEU GLU GLY HIS ILE GLU PRO ASP GLU PHE PHE
SEQRES 32 B 1032 ASP ILE ALA ASP ASP LEU GLY VAL LEU THR MET PRO GLY
SEQRES 33 B 1032 TRP GLU CYS CYS ASP LYS TRP GLU GLY GLN VAL ASN GLY
SEQRES 34 B 1032 GLU GLU LYS GLY GLU PRO TRP VAL GLU SER ASP TYR PRO
SEQRES 35 B 1032 ILE ALA LYS ALA SER MET PHE SER GLU ALA GLU ARG LEU
SEQRES 36 B 1032 ARG ASP HIS PRO SER VAL ILE SER PHE HIS ILE GLY SER
SEQRES 37 B 1032 ASP PHE ALA PRO ASP ARG ARG ILE GLU GLN GLY TYR LEU
SEQRES 38 B 1032 ASP ALA MET LYS ALA ALA ASP PHE LEU LEU PRO VAL ILE
SEQRES 39 B 1032 PRO ALA ALA SER ALA ARG PRO SER PRO ILE THR GLY ALA
SEQRES 40 B 1032 SER GLY MET LYS MET ASN GLY PRO TYR ASP TYR VAL PRO
SEQRES 41 B 1032 PRO VAL TYR TRP TYR ASP LYS SER GLN LYS ASP ARG GLY
SEQRES 42 B 1032 GLY ALA TRP SER PHE ASN SER GLU THR SER ALA GLY VAL
SEQRES 43 B 1032 ASP ILE PRO THR MET ASP THR LEU LYS ARG MET MET SER
SEQRES 44 B 1032 ALA SER GLU LEU ASP THR MET TRP LYS ASN PRO SER ALA
SEQRES 45 B 1032 LYS GLN TYR HIS ARG SER SER SER ASP THR PHE GLY ASN
SEQRES 46 B 1032 LEU LYS LEU PHE GLY ASP ALA LEU THR LYS ARG TYR GLY
SEQRES 47 B 1032 ALA SER ALA ASN LEU ASN ASP PHE VAL ARG LYS ALA GLN
SEQRES 48 B 1032 LEU SER GLN TYR GLU ASN VAL ARG ALA GLU PHE GLU SER
SEQRES 49 B 1032 HIS SER ARG ASN TYR THR ASP SER THR ASN PRO SER THR
SEQRES 50 B 1032 GLY LEU ILE TYR TRP MET LEU ASN SER PRO TRP THR SER
SEQRES 51 B 1032 LEU HIS TRP GLN LEU PHE ASP ALA TYR MET ASP GLN ASN
SEQRES 52 B 1032 GLY ALA TYR TYR GLY ALA LYS LYS ALA ASN GLU PRO LEU
SEQRES 53 B 1032 HIS ILE GLN TYR SER HIS ASP ASN ARG SER VAL VAL VAL
SEQRES 54 B 1032 ILE ASN GLN THR SER ASN ALA VAL SER GLY LEU THR ALA
SEQRES 55 B 1032 THR THR LYS LEU TYR ASN LEU ASP GLY THR GLU LYS TYR
SEQRES 56 B 1032 SER ASN THR LYS THR GLY LEU SER VAL GLY ALA LEU GLY
SEQRES 57 B 1032 ALA LYS ALA THR ALA VAL THR VAL PRO ALA VAL SER GLY
SEQRES 58 B 1032 LEU SER THR THR TYR LEU ALA LYS ASN VAL LEU THR ASP
SEQRES 59 B 1032 SER SER GLY LYS GLU VAL SER ARG ASN VAL TYR TRP LEU
SEQRES 60 B 1032 SER THR LYS ALA ASP THR LEU ASN TRP GLY GLY SER ASP
SEQRES 61 B 1032 TRP TYR TYR THR PRO GLN SER ALA PHE ALA ASP LEU SER
SEQRES 62 B 1032 GLY LEU ASN ASN LEU GLY GLN SER ALA VAL GLY ALA THR
SEQRES 63 B 1032 ALA ASN SER VAL ALA GLY ALA ASP GLY THR THR THR THR
SEQRES 64 B 1032 THR VAL THR LEU LYS ASN THR SER GLY GLY ARG LEU PRO
SEQRES 65 B 1032 ALA PHE TYR VAL ASP SER LYS VAL VAL ASP SER ALA GLY
SEQRES 66 B 1032 LYS PRO VAL LEU PRO VAL GLU TRP ASN ASP ASN ALA VAL
SEQRES 67 B 1032 SER LEU TRP PRO GLY GLU THR THR THR LEU THR ALA LYS
SEQRES 68 B 1032 TYR ARG THR ALA ASP LEU LYS GLY SER LYS PRO SER VAL
SEQRES 69 B 1032 ARG ILE SER GLY TRP ASN THR GLY THR GLN THR VAL PRO
SEQRES 70 B 1032 ALA ASP GLY SER GLY PRO GLY PRO SER ASP PRO VAL ASP
SEQRES 71 B 1032 TYR GLN ALA GLU ASP ALA THR ILE VAL GLN GLY ALA VAL
SEQRES 72 B 1032 GLU SER ASN HIS ALA GLY TYR THR GLY THR GLY PHE VAL
SEQRES 73 B 1032 ASN TYR ASP ASN VAL ALA GLY SER SER VAL GLU TRP THR
SEQRES 74 B 1032 VAL THR VAL PRO SER ALA GLY THR TYR ASP VAL VAL VAL
SEQRES 75 B 1032 ARG TYR ALA ASN GLY THR THR THR SER ARG PRO LEU ASP
SEQRES 76 B 1032 PHE SER VAL ASN GLY SER ILE SER ALA SER GLY VAL ALA
SEQRES 77 B 1032 PHE GLY SER THR GLY THR TRP PRO ALA TRP THR THR LYS
SEQRES 78 B 1032 THR VAL ARG VAL THR LEU ALA ALA GLY VAL ASN LYS ILE
SEQRES 79 B 1032 LYS ALA VAL ALA THR THR ALA ASN GLY GLY PRO ASN VAL
SEQRES 80 B 1032 ASP LYS ILE THR LEU
HET X09 A1900 13
HET CD A1901 1
HET CD A1902 1
HET X09 B1900 13
HET CD B1901 1
HETNAM X09 AMINO-AUSTRALINE
HETNAM CD CADMIUM ION
HETSYN X09 (1R,2R,3R,7S,7AR)-3-(AMINOMETHYL)HEXAHYDRO-1H-
HETSYN 2 X09 PYRROLIZINE-1,2,7-TRIOL
FORMUL 3 X09 2(C8 H16 N2 O3)
FORMUL 4 CD 3(CD 2+)
FORMUL 8 HOH *1441(H2 O)
HELIX 1 1 ALA A 63 VAL A 65 5 3
HELIX 2 2 ASP A 67 VAL A 71 5 5
HELIX 3 3 THR A 89 ASN A 97 1 9
HELIX 4 4 THR A 107 VAL A 112 5 6
HELIX 5 5 ALA A 114 SER A 118 5 5
HELIX 6 6 ASN A 372 LEU A 386 1 15
HELIX 7 7 PRO A 399 GLY A 410 1 12
HELIX 8 8 ASP A 421 GLY A 425 5 5
HELIX 9 9 SER A 439 ARG A 456 1 18
HELIX 10 10 ASP A 473 ALA A 487 1 15
HELIX 11 11 PRO A 520 ASP A 526 5 7
HELIX 12 12 THR A 550 MET A 558 1 9
HELIX 13 13 SER A 559 ASN A 569 1 11
HELIX 14 14 LEU A 586 GLY A 598 1 13
HELIX 15 15 ASN A 602 ASN A 628 1 27
HELIX 16 16 TYR A 629 ASP A 631 5 3
HELIX 17 17 ASN A 663 ASN A 673 1 11
HELIX 18 18 TRP A 776 SER A 779 5 4
HELIX 19 19 LEU A 792 LEU A 798 5 7
HELIX 20 20 ALA A 875 LYS A 878 5 4
HELIX 21 21 ASP B 67 VAL B 71 5 5
HELIX 22 22 THR B 89 ASN B 97 1 9
HELIX 23 23 THR B 107 VAL B 112 5 6
HELIX 24 24 ALA B 114 SER B 118 5 5
HELIX 25 25 ASN B 372 GLY B 387 1 16
HELIX 26 26 PRO B 399 GLY B 410 1 12
HELIX 27 27 ASP B 421 GLY B 425 5 5
HELIX 28 28 SER B 439 ARG B 456 1 18
HELIX 29 29 ASP B 473 ALA B 487 1 15
HELIX 30 30 PRO B 520 ASP B 526 5 7
HELIX 31 31 THR B 550 MET B 558 1 9
HELIX 32 32 SER B 559 ASN B 569 1 11
HELIX 33 33 LEU B 586 GLY B 598 1 13
HELIX 34 34 ASN B 602 ASN B 628 1 27
HELIX 35 35 TYR B 629 ASP B 631 5 3
HELIX 36 36 ASN B 663 ASN B 673 1 11
HELIX 37 37 TRP B 776 SER B 779 5 4
HELIX 38 38 LEU B 792 LEU B 798 5 7
HELIX 39 39 ALA B 875 LYS B 878 5 4
SHEET 1 AA 4 ALA A 51 PRO A 53 0
SHEET 2 AA 4 VAL A 219 SER A 224 -1 O VAL A 221 N THR A 52
SHEET 3 AA 4 ARG A 135 PHE A 140 -1 O ARG A 135 N SER A 224
SHEET 4 AA 4 HIS A 169 ASP A 172 -1 O HIS A 169 N PHE A 140
SHEET 1 AB 6 TYR A 82 SER A 85 0
SHEET 2 AB 6 GLY A 56 SER A 61 -1 O TYR A 57 N VAL A 84
SHEET 3 AB 6 TRP A 121 VAL A 129 -1 O TRP A 122 N GLN A 60
SHEET 4 AB 6 GLY A 180 VAL A 188 -1 O GLY A 180 N VAL A 129
SHEET 5 AB 6 ALA A 147 VAL A 151 -1 O ASP A 148 N LYS A 187
SHEET 6 AB 6 THR A 154 ALA A 157 -1 O THR A 154 N VAL A 151
SHEET 1 AC 2 VAL A 143 LEU A 144 0
SHEET 2 AC 2 GLY A 214 ILE A 215 -1 O GLY A 214 N LEU A 144
SHEET 1 AD 2 VAL A 227 LEU A 238 0
SHEET 2 AD 2 HIS A 244 ASN A 255 -1 O ASP A 246 N LYS A 237
SHEET 1 AE 2 ARG A 285 THR A 289 0
SHEET 2 AE 2 HIS A 244 ASN A 255 1 O ALA A 251 N VAL A 288
SHEET 1 AF 2 VAL A 293 ASP A 296 0
SHEET 2 AF 2 HIS A 244 ASN A 255 -1 O ALA A 245 N LEU A 295
SHEET 1 AG 4 LYS A 272 LEU A 280 0
SHEET 2 AG 4 VAL A 261 VAL A 269 -1 O VAL A 261 N LEU A 280
SHEET 3 AG 4 TYR A 312 SER A 319 -1 O ASP A 315 N THR A 268
SHEET 4 AG 4 PRO A 324 PHE A 332 -1 N SER A 325 O ALA A 318
SHEET 1 AH 3 VAL A 337 LEU A 341 0
SHEET 2 AH 3 ARG A 347 VAL A 351 -1 O GLN A 348 N THR A 340
SHEET 3 AH 3 LYS A 354 LEU A 356 -1 O LYS A 354 N VAL A 351
SHEET 1 AI 5 LEU A 412 MET A 414 0
SHEET 2 AI 5 THR A 390 LEU A 393 1 O VAL A 391 N MET A 414
SHEET 3 AI 5 ILE A 358 TYR A 363 1 O GLY A 361 N ARG A 392
SHEET 4 AI 5 SER A 636 TYR A 641 1 O THR A 637 N ILE A 358
SHEET 5 AI 5 SER A 537 THR A 542 1 O SER A 537 N THR A 637
SHEET 1 AJ 2 PHE A 464 HIS A 465 0
SHEET 2 AJ 2 VAL A 493 ILE A 494 1 N ILE A 494 O PHE A 464
SHEET 1 AK 3 LEU A 676 TYR A 680 0
SHEET 2 AK 3 SER A 686 ASN A 691 -1 O VAL A 688 N GLN A 679
SHEET 3 AK 3 ALA A 729 THR A 735 -1 O ALA A 729 N ASN A 691
SHEET 1 AL 4 GLU A 713 VAL A 724 0
SHEET 2 AL 4 VAL A 697 ASN A 708 -1 O VAL A 697 N VAL A 724
SHEET 3 AL 4 THR A 745 THR A 753 -1 O LEU A 747 N TYR A 707
SHEET 4 AL 4 GLU A 759 SER A 768 -1 N VAL A 760 O LEU A 752
SHEET 1 AM 2 THR A 773 LEU A 774 0
SHEET 2 AM 2 GLN A 786 ALA A 788 -1 N SER A 787 O THR A 773
SHEET 1 AN 4 VAL A 803 ALA A 811 0
SHEET 2 AN 4 THR A 816 ASN A 825 -1 O THR A 818 N VAL A 810
SHEET 3 AN 4 THR A 865 ARG A 873 -1 O THR A 866 N LEU A 823
SHEET 4 AN 4 GLU A 852 TRP A 853 -1 O GLU A 852 N LYS A 871
SHEET 1 AO 4 VAL A 858 LEU A 860 0
SHEET 2 AO 4 ALA A 833 VAL A 841 -1 O ALA A 833 N LEU A 860
SHEET 3 AO 4 SER A 883 GLY A 888 -1 O SER A 883 N VAL A 841
SHEET 4 AO 4 GLY A 892 PRO A 897 -1 O GLY A 892 N GLY A 888
SHEET 1 BA 4 ASN B 50 PRO B 53 0
SHEET 2 BA 4 VAL B 219 SER B 224 -1 O VAL B 221 N THR B 52
SHEET 3 BA 4 ARG B 135 PHE B 140 -1 O ARG B 135 N SER B 224
SHEET 4 BA 4 HIS B 169 ASP B 172 -1 O HIS B 169 N PHE B 140
SHEET 1 BB 6 TYR B 82 SER B 85 0
SHEET 2 BB 6 GLY B 56 SER B 61 -1 O TYR B 57 N VAL B 84
SHEET 3 BB 6 TRP B 121 VAL B 129 -1 O TRP B 122 N GLN B 60
SHEET 4 BB 6 GLY B 180 VAL B 188 -1 O GLY B 180 N VAL B 129
SHEET 5 BB 6 LYS B 146 VAL B 151 -1 O ASP B 148 N LYS B 187
SHEET 6 BB 6 THR B 154 ASN B 163 -1 O THR B 154 N VAL B 151
SHEET 1 BC 2 VAL B 143 LEU B 144 0
SHEET 2 BC 2 GLY B 214 ILE B 215 -1 O GLY B 214 N LEU B 144
SHEET 1 BD 2 VAL B 227 LEU B 238 0
SHEET 2 BD 2 HIS B 244 ASN B 255 -1 O ASP B 246 N LYS B 237
SHEET 1 BE 2 ARG B 285 THR B 289 0
SHEET 2 BE 2 HIS B 244 ASN B 255 1 O ALA B 251 N VAL B 288
SHEET 1 BF 2 VAL B 293 ASP B 296 0
SHEET 2 BF 2 HIS B 244 ASN B 255 -1 O ALA B 245 N LEU B 295
SHEET 1 BG 4 LYS B 272 LEU B 280 0
SHEET 2 BG 4 VAL B 261 VAL B 269 -1 O VAL B 261 N LEU B 280
SHEET 3 BG 4 TYR B 312 VAL B 320 -1 O ASP B 315 N THR B 268
SHEET 4 BG 4 THR B 323 PHE B 332 -1 O THR B 323 N VAL B 320
SHEET 1 BH 3 VAL B 337 LEU B 341 0
SHEET 2 BH 3 ARG B 347 VAL B 351 -1 O GLN B 348 N THR B 340
SHEET 3 BH 3 LYS B 354 PRO B 355 -1 O LYS B 354 N VAL B 351
SHEET 1 BI 5 LEU B 412 GLY B 416 0
SHEET 2 BI 5 THR B 390 GLU B 394 1 O VAL B 391 N MET B 414
SHEET 3 BI 5 ILE B 358 TYR B 363 1 O GLY B 361 N ARG B 392
SHEET 4 BI 5 SER B 636 TYR B 641 1 O THR B 637 N ILE B 358
SHEET 5 BI 5 SER B 537 THR B 542 1 O SER B 537 N THR B 637
SHEET 1 BJ 2 PHE B 464 HIS B 465 0
SHEET 2 BJ 2 VAL B 493 ILE B 494 1 N ILE B 494 O PHE B 464
SHEET 1 BK 3 LEU B 676 TYR B 680 0
SHEET 2 BK 3 SER B 686 ASN B 691 -1 O VAL B 688 N GLN B 679
SHEET 3 BK 3 ALA B 729 THR B 735 -1 O ALA B 729 N ASN B 691
SHEET 1 BL 4 GLU B 713 VAL B 724 0
SHEET 2 BL 4 VAL B 697 ASN B 708 -1 O VAL B 697 N VAL B 724
SHEET 3 BL 4 THR B 745 THR B 753 -1 O LEU B 747 N TYR B 707
SHEET 4 BL 4 GLU B 759 SER B 768 -1 N VAL B 760 O LEU B 752
SHEET 1 BM 2 THR B 773 LEU B 774 0
SHEET 2 BM 2 GLN B 786 ALA B 788 -1 N SER B 787 O THR B 773
SHEET 1 BN 4 VAL B 803 ALA B 811 0
SHEET 2 BN 4 THR B 816 ASN B 825 -1 O THR B 818 N VAL B 810
SHEET 3 BN 4 THR B 865 ARG B 873 -1 O THR B 866 N LEU B 823
SHEET 4 BN 4 GLU B 852 TRP B 853 -1 O GLU B 852 N LYS B 871
SHEET 1 BO 4 VAL B 858 LEU B 860 0
SHEET 2 BO 4 ALA B 833 VAL B 841 -1 O ALA B 833 N LEU B 860
SHEET 3 BO 4 SER B 883 GLY B 888 -1 O SER B 883 N VAL B 841
SHEET 4 BO 4 GLY B 892 PRO B 897 -1 O GLY B 892 N GLY B 888
SSBOND 1 CYS A 419 CYS A 420 1555 1555 2.05
SSBOND 2 CYS B 419 CYS B 420 1555 1555 2.05
LINK NE2 HIS A 244 CD CD A1901 1555 1555 2.19
LINK OD1 ASP A 246 CD CD A1901 1555 1555 1.90
LINK OD2 ASP A 296 CD CD A1902 1555 1555 2.12
LINK OD1 ASP A 296 CD CD A1902 1555 1555 2.42
LINK CD CD A1901 O HOH A2212 1555 1555 2.29
LINK CD CD A1902 O HOH A2261 1555 1555 2.48
LINK OD1 ASN B 428 CD CD B1901 1555 1555 2.61
LINK O GLY B 429 CD CD B1901 1555 1555 2.62
LINK O GLU B 431 CD CD B1901 1555 1555 2.47
CISPEP 1 LEU A 144 SER A 145 0 2.21
CISPEP 2 GLY A 514 PRO A 515 0 5.18
CISPEP 3 TRP A 642 MET A 643 0 -0.23
CISPEP 4 VAL A 803 GLY A 804 0 6.75
CISPEP 5 LEU A 849 PRO A 850 0 2.47
CISPEP 6 LEU B 144 SER B 145 0 3.38
CISPEP 7 GLY B 514 PRO B 515 0 1.67
CISPEP 8 TRP B 642 MET B 643 0 4.99
CISPEP 9 LEU B 849 PRO B 850 0 -4.53
SITE 1 AC1 12 ILE A 202 ASP A 203 TRP A 204 GLU A 394
SITE 2 AC1 12 CYS A 419 SER A 468 ASP A 469 TYR A 516
SITE 3 AC1 12 GLU A 541 TRP A 642 TRP A 653 HOH A2437
SITE 1 AC2 14 ILE B 202 ASP B 203 TRP B 204 GLU B 394
SITE 2 AC2 14 CYS B 419 SER B 468 ASP B 469 TYR B 516
SITE 3 AC2 14 GLU B 541 TRP B 642 TRP B 653 TRP B 781
SITE 4 AC2 14 HOH B2415 HOH B2708
SITE 1 AC3 3 HIS A 244 ASP A 246 HOH A2212
SITE 1 AC4 2 ASP A 296 HOH A2261
SITE 1 AC5 5 ASN B 428 GLY B 429 GLU B 431 GLY B 433
SITE 2 AC5 5 HOH B2371
CRYST1 86.750 121.950 92.050 90.00 90.65 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 0.011527 0.000000 0.000131 0.00000
SCALE2 0.000000 0.008200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010864 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
