HEADER HYDROLASE 23-AUG-00 1E6Z
TITLE CHITINASE B FROM SERRATIA MARCESCENS WILDTYPE IN COMPLEX WITH
TITLE 2 CATALYTIC INTERMEDIATE
CAVEAT 1E6Z THR A 79 HAS WRONG CHIRALITY AT ATOM CB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1,4-BETA-POLY-N-ACETYLGLUCOSAMINIDASE, CHITODEXTRINASE,
COMPND 5 POLY-BETA-GLUCOSAMINIDASE, POLY(1,4-(N-ACETYL-BETA-D-GLUCOSAMINIDE))
COMPND 6 GLYCANOHYDROLASE;
COMPND 7 EC: 3.2.1.14;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 ORGANISM_TAXID: 615;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, CHITIN DEGRADATION, CATALYTIC INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOMANDER,B.SYNSTAD,V.G.H.EIJSINK,D.M.F.VAN AALTEN
REVDAT 9 13-DEC-23 1E6Z 1 REMARK HETSYN
REVDAT 8 29-JUL-20 1E6Z 1 COMPND REMARK HETNAM LINK
REVDAT 8 2 1 SITE ATOM
REVDAT 7 24-JUL-19 1E6Z 1 REMARK
REVDAT 6 12-JUL-17 1E6Z 1
REVDAT 5 31-AUG-11 1E6Z 1 REMARK DBREF HET HETNAM
REVDAT 5 2 1 HETSYN FORMUL LINK SITE
REVDAT 5 3 1 ATOM TER HETATM VERSN
REVDAT 4 24-FEB-09 1E6Z 1 VERSN
REVDAT 3 07-APR-05 1E6Z 1 REMARK ATOM
REVDAT 2 17-MAR-05 1E6Z 1 COMPND JRNL SEQRES
REVDAT 1 22-JUN-01 1E6Z 0
JRNL AUTH D.M.F.VAN AALTEN,D.KOMANDER,B.SYNSTAD,S.GSEIDNES,M.G.PETER,
JRNL AUTH 2 V.G.H.EIJSINK
JRNL TITL STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM OF A FAMILY
JRNL TITL 2 18 EXO-CHITINASE
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 8979 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11481469
JRNL DOI 10.1073/PNAS.151103798
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2794364.830
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 70231
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1442
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9537
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 214
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7819
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 933
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.33000
REMARK 3 B22 (A**2) : 2.27000
REMARK 3 B33 (A**2) : -4.60000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.260 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.870 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 47.90
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1290005306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 197360
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1E15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 20% GLYCEROL,
REMARK 280 HEPES PH 7.0, PH 7.00
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 27.90050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.17950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.90550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.17950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.90050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.90550
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
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, 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: 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 400
REMARK 400 COMPOUND
REMARK 400 REACTION TYPE: O-GLYCOSYL BOND HYDROLYSIS (ENDOHYDROLYSIS)
REMARK 400 CHITIN + H2O = OLIGOMERS OF N-ACETYLGLUCOSAMINE
REMARK 400 (RANDOM HYDROLYSIS OF N-ACETYL-BETA-D-GLUCOSAMINIDE
REMARK 400 1,4-LINKAGES IN CHITIN AND CHITODEXTRINS)
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 ALA A 499 CA C O CB
REMARK 470 LYS B 222 CG CD CE NZ
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 LYS A 222 CD CE NZ
REMARK 480 GLU A 329 CD OE1 OE2
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 NE2 GLN B 350 O HOH B 601 2.16
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 THR A 79 CB THR A 79 OG1 -0.122
REMARK 500 ARG A 129 CZ ARG A 129 NH2 0.557
REMARK 500 ARG A 129 CZ ARG A 129 NH2 0.507
REMARK 500 ASP A 142 CG ASP A 142 OD1 1.607
REMARK 500 ASP A 142 CG ASP A 142 OD1 1.937
REMARK 500 ASP A 142 CG ASP A 142 OD2 1.260
REMARK 500 ASP A 142 CG ASP A 142 OD2 0.726
REMARK 500 LYS B 42 CE LYS B 42 NZ 0.171
REMARK 500 LYS B 42 CE LYS B 42 NZ 0.168
REMARK 500 ASP B 142 CG ASP B 142 OD2 1.417
REMARK 500 ASP B 142 CG ASP B 142 OD2 1.312
REMARK 500 ARG B 244 NE ARG B 244 CZ 2.147
REMARK 500 ARG B 244 NE ARG B 244 CZ 2.276
REMARK 500 ARG B 244 CZ ARG B 244 NH1 1.423
REMARK 500 ARG B 244 CZ ARG B 244 NH1 1.285
REMARK 500 ARG B 244 CZ ARG B 244 NH2 3.474
REMARK 500 ARG B 244 CZ ARG B 244 NH2 3.451
REMARK 500 GLU B 315 CG GLU B 315 CD 0.389
REMARK 500 GLU B 315 CD GLU B 315 OE1 2.198
REMARK 500 GLU B 315 CD GLU B 315 OE1 1.089
REMARK 500 GLU B 315 CD GLU B 315 OE2 1.495
REMARK 500 GLU B 315 CD GLU B 315 OE2 2.316
REMARK 500 ARG B 420 CG ARG B 420 CD 0.203
REMARK 500 ARG B 420 CG ARG B 420 CD -0.194
REMARK 500 ARG B 420 CZ ARG B 420 NH1 3.206
REMARK 500 ARG B 420 CZ ARG B 420 NH1 3.722
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 THR A 79 OG1 - CB - CG2 ANGL. DEV. = 101.3 DEGREES
REMARK 500 ARG A 129 NH1 - CZ - NH2 ANGL. DEV. = 33.2 DEGREES
REMARK 500 ARG A 129 NH1 - CZ - NH2 ANGL. DEV. = 32.4 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH2 ANGL. DEV. = -33.6 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH2 ANGL. DEV. = -34.1 DEGREES
REMARK 500 ASP A 142 OD1 - CG - OD2 ANGL. DEV. = -75.7 DEGREES
REMARK 500 ASP A 142 OD1 - CG - OD2 ANGL. DEV. = -80.5 DEGREES
REMARK 500 ASP A 142 CB - CG - OD1 ANGL. DEV. = -61.3 DEGREES
REMARK 500 ASP A 142 CB - CG - OD1 ANGL. DEV. = -72.8 DEGREES
REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -50.0 DEGREES
REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -36.5 DEGREES
REMARK 500 ASP B 142 OD1 - CG - OD2 ANGL. DEV. = 33.0 DEGREES
REMARK 500 ASP B 142 OD1 - CG - OD2 ANGL. DEV. = 19.2 DEGREES
REMARK 500 ASP B 142 CB - CG - OD2 ANGL. DEV. = -59.1 DEGREES
REMARK 500 ASP B 142 CB - CG - OD2 ANGL. DEV. = -55.7 DEGREES
REMARK 500 VAL B 203 CG1 - CB - CG2 ANGL. DEV. = -88.7 DEGREES
REMARK 500 ARG B 244 CD - NE - CZ ANGL. DEV. = -80.3 DEGREES
REMARK 500 ARG B 244 CD - NE - CZ ANGL. DEV. = -75.3 DEGREES
REMARK 500 ARG B 244 NH1 - CZ - NH2 ANGL. DEV. = 103.8 DEGREES
REMARK 500 ARG B 244 NH1 - CZ - NH2 ANGL. DEV. = 107.4 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH1 ANGL. DEV. = -78.7 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH1 ANGL. DEV. = -80.8 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH2 ANGL. DEV. = -93.6 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH2 ANGL. DEV. = -92.8 DEGREES
REMARK 500 GLU B 315 CB - CG - CD ANGL. DEV. = -19.1 DEGREES
REMARK 500 GLU B 315 OE1 - CD - OE2 ANGL. DEV. = -84.1 DEGREES
REMARK 500 GLU B 315 OE1 - CD - OE2 ANGL. DEV. = -86.7 DEGREES
REMARK 500 GLU B 315 CG - CD - OE1 ANGL. DEV. = -85.2 DEGREES
REMARK 500 GLU B 315 CG - CD - OE1 ANGL. DEV. = -51.0 DEGREES
REMARK 500 GLU B 315 CG - CD - OE2 ANGL. DEV. = -57.8 DEGREES
REMARK 500 GLU B 315 CG - CD - OE2 ANGL. DEV. = -79.9 DEGREES
REMARK 500 ARG B 420 CB - CG - CD ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG B 420 NH1 - CZ - NH2 ANGL. DEV. = 20.6 DEGREES
REMARK 500 ARG B 420 NH1 - CZ - NH2 ANGL. DEV. = 42.8 DEGREES
REMARK 500 ARG B 420 NE - CZ - NH1 ANGL. DEV. = -69.2 DEGREES
REMARK 500 ARG B 420 NE - CZ - NH1 ANGL. DEV. = -58.2 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 ASP A 142 66.34 -116.98
REMARK 500 ALA A 228 47.45 -147.51
REMARK 500 TYR A 318 107.85 -51.97
REMARK 500 PRO A 319 39.14 -70.84
REMARK 500 ASP A 336 110.55 -160.76
REMARK 500 SER A 490 0.26 -63.50
REMARK 500 ASP B 25 85.12 -162.90
REMARK 500 ASP B 142 61.96 -119.98
REMARK 500 ALA B 228 47.01 -148.23
REMARK 500 ASP B 336 115.10 -160.19
REMARK 500 PRO B 445 -9.64 -50.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASP A 142 0.46 SIDE CHAIN
REMARK 500 ASP B 142 0.20 SIDE CHAIN
REMARK 500 ARG B 244 0.09 SIDE CHAIN
REMARK 500 GLU B 315 0.26 SIDE CHAIN
REMARK 500 ARG B 420 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E15 RELATED DB: PDB
REMARK 900 CHITINASE B FROM SERRATIA MARCESCENS
REMARK 900 RELATED ID: 1E6N RELATED DB: PDB
REMARK 900 CHITINASE B FROM SERRATIA MARCESCENS INACTIVE MUTANT E144Q IN
REMARK 900 COMPLEX WITH N-ACETYLGLUCOSAMINE-PENTAMER
REMARK 900 RELATED ID: 1E6P RELATED DB: PDB
REMARK 900 CHITINASE B FROM SERRATIA MARCESCENS INACTIVE MUTANT E144Q
REMARK 900 RELATED ID: 1E6R RELATED DB: PDB
REMARK 900 CHITINASE B FROM SERRATIA MARCESCENS WILDTYPE IN COMPLEX WITH
REMARK 900 INHIBITOR ALLOSAMIDIN
REMARK 900 RELATED ID: 1CTN RELATED DB: PDB
REMARK 900 CHITINASE A (E.C.3.2.1.14) (PH 5.5, 4 DEGREES C) SERRATIA
REMARK 900 MARCESCENS RECOMBINANT FORM EXPRESSED IN ESCHERICHIA COLI
DBREF 1E6Z A 2 499 UNP Q54276 Q54276_SERMA 2 499
DBREF 1E6Z B 2 499 UNP Q54276 Q54276_SERMA 2 499
SEQRES 1 A 498 SER THR ARG LYS ALA VAL ILE GLY TYR TYR PHE ILE PRO
SEQRES 2 A 498 THR ASN GLN ILE ASN ASN TYR THR GLU THR ASP THR SER
SEQRES 3 A 498 VAL VAL PRO PHE PRO VAL SER ASN ILE THR PRO ALA LYS
SEQRES 4 A 498 ALA LYS GLN LEU THR HIS ILE ASN PHE SER PHE LEU ASP
SEQRES 5 A 498 ILE ASN SER ASN LEU GLU CYS ALA TRP ASP PRO ALA THR
SEQRES 6 A 498 ASN ASP ALA LYS ALA ARG ASP VAL VAL ASN ARG LEU THR
SEQRES 7 A 498 ALA LEU LYS ALA HIS ASN PRO SER LEU ARG ILE MET PHE
SEQRES 8 A 498 SER ILE GLY GLY TRP TYR TYR SER ASN ASP LEU GLY VAL
SEQRES 9 A 498 SER HIS ALA ASN TYR VAL ASN ALA VAL LYS THR PRO ALA
SEQRES 10 A 498 SER ARG ALA LYS PHE ALA GLN SER CYS VAL ARG ILE MET
SEQRES 11 A 498 LYS ASP TYR GLY PHE ASP GLY VAL ASP ILE ASP TRP GLU
SEQRES 12 A 498 TYR PRO GLN ALA ALA GLU VAL ASP GLY PHE ILE ALA ALA
SEQRES 13 A 498 LEU GLN GLU ILE ARG THR LEU LEU ASN GLN GLN THR ILE
SEQRES 14 A 498 THR ASP GLY ARG GLN ALA LEU PRO TYR GLN LEU THR ILE
SEQRES 15 A 498 ALA GLY ALA GLY GLY ALA PHE PHE LEU SER ARG TYR TYR
SEQRES 16 A 498 SER LYS LEU ALA GLN ILE VAL ALA PRO LEU ASP TYR ILE
SEQRES 17 A 498 ASN LEU MET THR TYR ASP LEU ALA GLY PRO TRP GLU LYS
SEQRES 18 A 498 VAL THR ASN HIS GLN ALA ALA LEU PHE GLY ASP ALA ALA
SEQRES 19 A 498 GLY PRO THR PHE TYR ASN ALA LEU ARG GLU ALA ASN LEU
SEQRES 20 A 498 GLY TRP SER TRP GLU GLU LEU THR ARG ALA PHE PRO SER
SEQRES 21 A 498 PRO PHE SER LEU THR VAL ASP ALA ALA VAL GLN GLN HIS
SEQRES 22 A 498 LEU MET MET GLU GLY VAL PRO SER ALA LYS ILE VAL MET
SEQRES 23 A 498 GLY VAL PRO PHE TYR GLY ARG ALA PHE LYS GLY VAL SER
SEQRES 24 A 498 GLY GLY ASN GLY GLY GLN TYR SER SER HIS SER THR PRO
SEQRES 25 A 498 GLY GLU ASP PRO TYR PRO SER THR ASP TYR TRP LEU VAL
SEQRES 26 A 498 GLY CYS GLU GLU CYS VAL ARG ASP LYS ASP PRO ARG ILE
SEQRES 27 A 498 ALA SER TYR ARG GLN LEU GLU GLN MET LEU GLN GLY ASN
SEQRES 28 A 498 TYR GLY TYR GLN ARG LEU TRP ASN ASP LYS THR LYS THR
SEQRES 29 A 498 PRO TYR LEU TYR HIS ALA GLN ASN GLY LEU PHE VAL THR
SEQRES 30 A 498 TYR ASP ASP ALA GLU SER PHE LYS TYR LYS ALA LYS TYR
SEQRES 31 A 498 ILE LYS GLN GLN GLN LEU GLY GLY VAL MET PHE TRP HIS
SEQRES 32 A 498 LEU GLY GLN ASP ASN ARG ASN GLY ASP LEU LEU ALA ALA
SEQRES 33 A 498 LEU ASP ARG TYR PHE ASN ALA ALA ASP TYR ASP ASP SER
SEQRES 34 A 498 GLN LEU ASP MET GLY THR GLY LEU ARG TYR THR GLY VAL
SEQRES 35 A 498 GLY PRO GLY ASN LEU PRO ILE MET THR ALA PRO ALA TYR
SEQRES 36 A 498 VAL PRO GLY THR THR TYR ALA GLN GLY ALA LEU VAL SER
SEQRES 37 A 498 TYR GLN GLY TYR VAL TRP GLN THR LYS TRP GLY TYR ILE
SEQRES 38 A 498 THR SER ALA PRO GLY SER ASP SER ALA TRP LEU LYS VAL
SEQRES 39 A 498 GLY ARG VAL ALA
SEQRES 1 B 498 SER THR ARG LYS ALA VAL ILE GLY TYR TYR PHE ILE PRO
SEQRES 2 B 498 THR ASN GLN ILE ASN ASN TYR THR GLU THR ASP THR SER
SEQRES 3 B 498 VAL VAL PRO PHE PRO VAL SER ASN ILE THR PRO ALA LYS
SEQRES 4 B 498 ALA LYS GLN LEU THR HIS ILE ASN PHE SER PHE LEU ASP
SEQRES 5 B 498 ILE ASN SER ASN LEU GLU CYS ALA TRP ASP PRO ALA THR
SEQRES 6 B 498 ASN ASP ALA LYS ALA ARG ASP VAL VAL ASN ARG LEU THR
SEQRES 7 B 498 ALA LEU LYS ALA HIS ASN PRO SER LEU ARG ILE MET PHE
SEQRES 8 B 498 SER ILE GLY GLY TRP TYR TYR SER ASN ASP LEU GLY VAL
SEQRES 9 B 498 SER HIS ALA ASN TYR VAL ASN ALA VAL LYS THR PRO ALA
SEQRES 10 B 498 SER ARG ALA LYS PHE ALA GLN SER CYS VAL ARG ILE MET
SEQRES 11 B 498 LYS ASP TYR GLY PHE ASP GLY VAL ASP ILE ASP TRP GLU
SEQRES 12 B 498 TYR PRO GLN ALA ALA GLU VAL ASP GLY PHE ILE ALA ALA
SEQRES 13 B 498 LEU GLN GLU ILE ARG THR LEU LEU ASN GLN GLN THR ILE
SEQRES 14 B 498 THR ASP GLY ARG GLN ALA LEU PRO TYR GLN LEU THR ILE
SEQRES 15 B 498 ALA GLY ALA GLY GLY ALA PHE PHE LEU SER ARG TYR TYR
SEQRES 16 B 498 SER LYS LEU ALA GLN ILE VAL ALA PRO LEU ASP TYR ILE
SEQRES 17 B 498 ASN LEU MET THR TYR ASP LEU ALA GLY PRO TRP GLU LYS
SEQRES 18 B 498 VAL THR ASN HIS GLN ALA ALA LEU PHE GLY ASP ALA ALA
SEQRES 19 B 498 GLY PRO THR PHE TYR ASN ALA LEU ARG GLU ALA ASN LEU
SEQRES 20 B 498 GLY TRP SER TRP GLU GLU LEU THR ARG ALA PHE PRO SER
SEQRES 21 B 498 PRO PHE SER LEU THR VAL ASP ALA ALA VAL GLN GLN HIS
SEQRES 22 B 498 LEU MET MET GLU GLY VAL PRO SER ALA LYS ILE VAL MET
SEQRES 23 B 498 GLY VAL PRO PHE TYR GLY ARG ALA PHE LYS GLY VAL SER
SEQRES 24 B 498 GLY GLY ASN GLY GLY GLN TYR SER SER HIS SER THR PRO
SEQRES 25 B 498 GLY GLU ASP PRO TYR PRO SER THR ASP TYR TRP LEU VAL
SEQRES 26 B 498 GLY CYS GLU GLU CYS VAL ARG ASP LYS ASP PRO ARG ILE
SEQRES 27 B 498 ALA SER TYR ARG GLN LEU GLU GLN MET LEU GLN GLY ASN
SEQRES 28 B 498 TYR GLY TYR GLN ARG LEU TRP ASN ASP LYS THR LYS THR
SEQRES 29 B 498 PRO TYR LEU TYR HIS ALA GLN ASN GLY LEU PHE VAL THR
SEQRES 30 B 498 TYR ASP ASP ALA GLU SER PHE LYS TYR LYS ALA LYS TYR
SEQRES 31 B 498 ILE LYS GLN GLN GLN LEU GLY GLY VAL MET PHE TRP HIS
SEQRES 32 B 498 LEU GLY GLN ASP ASN ARG ASN GLY ASP LEU LEU ALA ALA
SEQRES 33 B 498 LEU ASP ARG TYR PHE ASN ALA ALA ASP TYR ASP ASP SER
SEQRES 34 B 498 GLN LEU ASP MET GLY THR GLY LEU ARG TYR THR GLY VAL
SEQRES 35 B 498 GLY PRO GLY ASN LEU PRO ILE MET THR ALA PRO ALA TYR
SEQRES 36 B 498 VAL PRO GLY THR THR TYR ALA GLN GLY ALA LEU VAL SER
SEQRES 37 B 498 TYR GLN GLY TYR VAL TRP GLN THR LYS TRP GLY TYR ILE
SEQRES 38 B 498 THR SER ALA PRO GLY SER ASP SER ALA TRP LEU LYS VAL
SEQRES 39 B 498 GLY ARG VAL ALA
HET NAG C 1 15
HET NAG C 2 14
HET SO4 A 501 5
HET NGO A 502 14
HET SO4 B 501 5
HET SO4 B 502 5
HET SO4 B 503 5
HET NGO B 504 14
HET NAG B 505 15
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM NGO 2-METHYL-4,5-DIHYDRO-(1,2-DIDEOXY-ALPHA-D-
HETNAM 2 NGO GLUCOPYRANOSO)[2,1-D]-1,3-OXAZOLE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN NGO N-ACETYLGLUCOSAMINE-OXAZOLINIUM ION INTERMEDIATE
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 5 NGO 2(C8 H14 N O5 1+)
FORMUL 11 HOH *933(H2 O)
HELIX 1 AA1 PRO A 14 ASN A 19 1 6
HELIX 2 AA2 PRO A 32 ILE A 36 5 5
HELIX 3 AA3 THR A 37 LEU A 44 1 8
HELIX 4 AA4 ASN A 67 LEU A 81 1 15
HELIX 5 AA5 LYS A 82 ASN A 85 5 4
HELIX 6 AA6 GLY A 96 ASN A 101 1 6
HELIX 7 AA7 SER A 106 VAL A 114 1 9
HELIX 8 AA8 THR A 116 GLY A 135 1 20
HELIX 9 AA9 GLU A 150 ASP A 172 1 23
HELIX 10 AB1 GLY A 188 SER A 193 1 6
HELIX 11 AB2 ARG A 194 SER A 197 5 4
HELIX 12 AB3 LYS A 198 ALA A 204 1 7
HELIX 13 AB4 ASN A 241 ALA A 246 5 6
HELIX 14 AB5 SER A 251 PHE A 259 1 9
HELIX 15 AB6 THR A 266 MET A 276 1 11
HELIX 16 AB7 PRO A 281 ALA A 283 5 3
HELIX 17 AB8 CYS A 328 LYS A 335 1 8
HELIX 18 AB9 TYR A 342 GLY A 351 1 10
HELIX 19 AC1 ASP A 381 GLN A 395 1 15
HELIX 20 AC2 HIS A 404 ASP A 408 5 5
HELIX 21 AC3 GLY A 412 ALA A 424 1 13
HELIX 22 AC4 PRO B 14 ASN B 20 1 7
HELIX 23 AC5 PRO B 32 ILE B 36 5 5
HELIX 24 AC6 THR B 37 LEU B 44 1 8
HELIX 25 AC7 ASN B 67 ALA B 80 1 14
HELIX 26 AC8 LEU B 81 ASN B 85 5 5
HELIX 27 AC9 GLY B 96 ASN B 101 1 6
HELIX 28 AD1 SER B 106 VAL B 114 1 9
HELIX 29 AD2 THR B 116 GLY B 135 1 20
HELIX 30 AD3 GLN B 147 ALA B 149 5 3
HELIX 31 AD4 GLU B 150 GLY B 173 1 24
HELIX 32 AD5 GLY B 188 SER B 193 1 6
HELIX 33 AD6 ARG B 194 SER B 197 5 4
HELIX 34 AD7 LYS B 198 ALA B 204 1 7
HELIX 35 AD8 ASN B 241 ALA B 246 5 6
HELIX 36 AD9 SER B 251 PHE B 259 1 9
HELIX 37 AE1 THR B 266 MET B 277 1 12
HELIX 38 AE2 PRO B 281 ALA B 283 5 3
HELIX 39 AE3 CYS B 328 ASP B 334 1 7
HELIX 40 AE4 TYR B 342 GLN B 350 1 9
HELIX 41 AE5 ASP B 381 GLN B 395 1 15
HELIX 42 AE6 HIS B 404 ASP B 408 5 5
HELIX 43 AE7 GLY B 412 ALA B 424 1 13
SHEET 1 AA110 CYS A 60 ALA A 61 0
SHEET 2 AA110 HIS A 46 ILE A 54 -1 N ASP A 53 O ALA A 61
SHEET 3 AA110 ARG A 89 GLY A 95 1 O SER A 93 N PHE A 49
SHEET 4 AA110 GLY A 138 ASP A 142 1 O ASP A 142 N ILE A 94
SHEET 5 AA110 GLN A 180 ALA A 186 1 O THR A 182 N ILE A 141
SHEET 6 AA110 TYR A 208 MET A 212 1 O MET A 212 N GLY A 185
SHEET 7 AA110 ILE A 285 PRO A 290 1 O VAL A 286 N LEU A 211
SHEET 8 AA110 GLY A 399 TRP A 403 1 O GLY A 399 N MET A 287
SHEET 9 AA110 ALA A 6 PHE A 12 1 N ALA A 6 O VAL A 400
SHEET 10 AA110 HIS A 46 ILE A 54 1 O HIS A 46 N GLY A 9
SHEET 1 AA2 5 ILE A 339 SER A 341 0
SHEET 2 AA2 5 TYR A 292 LYS A 297 -1 N GLY A 293 O ALA A 340
SHEET 3 AA2 5 LEU A 375 THR A 378 -1 O PHE A 376 N PHE A 296
SHEET 4 AA2 5 THR A 365 HIS A 370 -1 N HIS A 370 O LEU A 375
SHEET 5 AA2 5 TYR A 355 ASN A 360 -1 N LEU A 358 O TYR A 367
SHEET 1 AA3 3 LEU A 467 TYR A 470 0
SHEET 2 AA3 3 TYR A 473 THR A 477 -1 O TYR A 473 N TYR A 470
SHEET 3 AA3 3 TRP A 492 ARG A 497 -1 O LEU A 493 N GLN A 476
SHEET 1 AA410 CYS B 60 ALA B 61 0
SHEET 2 AA410 HIS B 46 ILE B 54 -1 N ASP B 53 O ALA B 61
SHEET 3 AA410 ARG B 89 GLY B 95 1 O SER B 93 N LEU B 52
SHEET 4 AA410 GLY B 138 ASP B 142 1 O ASP B 142 N ILE B 94
SHEET 5 AA410 GLN B 180 ALA B 186 1 O GLN B 180 N VAL B 139
SHEET 6 AA410 TYR B 208 MET B 212 1 O MET B 212 N GLY B 185
SHEET 7 AA410 ILE B 285 PRO B 290 1 O VAL B 286 N ILE B 209
SHEET 8 AA410 GLY B 399 TRP B 403 1 O MET B 401 N MET B 287
SHEET 9 AA410 ALA B 6 PHE B 12 1 N ALA B 6 O VAL B 400
SHEET 10 AA410 HIS B 46 ILE B 54 1 O HIS B 46 N GLY B 9
SHEET 1 AA5 5 ILE B 339 SER B 341 0
SHEET 2 AA5 5 TYR B 292 LYS B 297 -1 N GLY B 293 O ALA B 340
SHEET 3 AA5 5 LEU B 375 THR B 378 -1 O PHE B 376 N PHE B 296
SHEET 4 AA5 5 THR B 365 HIS B 370 -1 N HIS B 370 O LEU B 375
SHEET 5 AA5 5 TYR B 355 ASN B 360 -1 N LEU B 358 O TYR B 367
SHEET 1 AA6 3 LEU B 467 TYR B 470 0
SHEET 2 AA6 3 TYR B 473 THR B 477 -1 O TRP B 475 N VAL B 468
SHEET 3 AA6 3 TRP B 492 ARG B 497 -1 O LEU B 493 N GLN B 476
SSBOND 1 CYS A 328 CYS A 331 1555 1555 2.03
SSBOND 2 CYS B 328 CYS B 331 1555 1555 2.03
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
CISPEP 1 SER A 50 PHE A 51 0 -3.22
CISPEP 2 GLU A 144 TYR A 145 0 2.60
CISPEP 3 SER A 261 PRO A 262 0 -0.29
CISPEP 4 ASP A 316 PRO A 317 0 -1.73
CISPEP 5 TRP A 403 HIS A 404 0 -8.19
CISPEP 6 SER B 50 PHE B 51 0 1.80
CISPEP 7 GLU B 144 TYR B 145 0 -0.06
CISPEP 8 SER B 261 PRO B 262 0 -0.39
CISPEP 9 ASP B 316 PRO B 317 0 0.47
CISPEP 10 TRP B 403 HIS B 404 0 -8.30
CRYST1 55.801 103.811 186.359 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005366 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
(ATOM LINES ARE NOT SHOWN.)
END
