HEADER HYDROLASE 26-APR-02 1LL6
TITLE STRUCTURE OF THE D169N MUTANT OF C. IMMITIS CHITINASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 36-427;
COMPND 5 EC: 3.2.1.14;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COCCIDIOIDES IMMITIS;
SOURCE 3 ORGANISM_TAXID: 5501;
SOURCE 4 GENE: CTS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3
KEYWDS BETA-ALPHA BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BORTONE,A.F.MONZINGO,S.ERNST,J.D.ROBERTUS
REVDAT 4 16-AUG-23 1LL6 1 REMARK
REVDAT 3 27-OCT-21 1LL6 1 SEQADV
REVDAT 2 24-FEB-09 1LL6 1 VERSN
REVDAT 1 18-DEC-02 1LL6 0
JRNL AUTH K.BORTONE,A.F.MONZINGO,S.ERNST,J.D.ROBERTUS
JRNL TITL THE STRUCTURE OF AN ALLOSAMIDIN COMPLEX WITH THE
JRNL TITL 2 COCCIDIOIDES IMMITIS CHITINASE DEFINES A ROLE FOR A SECOND
JRNL TITL 3 ACID RESIDUE IN SUBSTRATE-ASSISTED MECHANISM
JRNL REF J.MOL.BIOL. V. 320 293 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12079386
JRNL DOI 10.1016/S0022-2836(02)00444-8
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16310
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) : 0.182
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 826
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12332
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.978
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000016047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-00
REMARK 200 TEMPERATURE (KELVIN) : 123
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : DOUBLE FOCUSSING MIRRORS (NI &
REMARK 200 PT) + NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34083
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 94.0
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.22100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ID 1LL4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, SODIUM HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 HIS A 54 NE2 HIS A 54 CD2 -0.073
REMARK 500 HIS A 92 NE2 HIS A 92 CD2 -0.072
REMARK 500 HIS A 200 NE2 HIS A 200 CD2 -0.075
REMARK 500 HIS A 251 NE2 HIS A 251 CD2 -0.078
REMARK 500 HIS B 54 NE2 HIS B 54 CD2 -0.073
REMARK 500 HIS B 92 NE2 HIS B 92 CD2 -0.079
REMARK 500 HIS B 200 NE2 HIS B 200 CD2 -0.082
REMARK 500 HIS B 251 NE2 HIS B 251 CD2 -0.073
REMARK 500 HIS C 66 NE2 HIS C 66 CD2 -0.078
REMARK 500 HIS C 200 NE2 HIS C 200 CD2 -0.068
REMARK 500 HIS C 251 NE2 HIS C 251 CD2 -0.077
REMARK 500 HIS D 54 NE2 HIS D 54 CD2 -0.071
REMARK 500 HIS D 66 NE2 HIS D 66 CD2 -0.074
REMARK 500 HIS D 92 NE2 HIS D 92 CD2 -0.070
REMARK 500 HIS D 200 NE2 HIS D 200 CD2 -0.069
REMARK 500 HIS D 251 NE2 HIS D 251 CD2 -0.085
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 TRP A 47 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP A 47 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 86 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 86 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 98 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 98 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 VAL A 105 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 TRP A 131 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 131 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP A 170 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 GLU A 171 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 TYR A 172 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 219 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TRP A 234 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 234 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP A 245 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP A 245 CB - CG - CD1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TRP A 245 CE2 - CD2 - CG ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP A 245 CG - CD2 - CE3 ANGL. DEV. = 5.9 DEGREES
REMARK 500 MET A 252 CG - SD - CE ANGL. DEV. = -11.7 DEGREES
REMARK 500 TRP A 315 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP A 315 CE2 - CD2 - CG ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP A 320 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP A 320 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 377 CD1 - CG - CD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TRP A 377 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 377 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 378 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP A 378 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 407 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 407 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP B 47 CD1 - CG - CD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 TRP B 47 CE2 - CD2 - CG ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG B 75 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 TRP B 86 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP B 86 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP B 98 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 98 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 131 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP B 131 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG B 147 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TRP B 170 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP B 170 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 170 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 GLU B 171 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG B 190 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 190 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 134 ANGLE DEVIATIONS.
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 TYR A 50 -107.45 -91.68
REMARK 500 ASP A 84 78.86 -153.31
REMARK 500 TRP A 86 -70.60 -59.33
REMARK 500 ASP A 99 -100.98 -72.43
REMARK 500 GLU A 100 129.15 65.32
REMARK 500 TYR A 106 -143.64 -129.46
REMARK 500 ASN A 136 65.42 -103.67
REMARK 500 PHE A 137 -56.53 -121.19
REMARK 500 PRO A 173 84.93 -54.63
REMARK 500 GLU A 174 7.45 -61.01
REMARK 500 ALA A 238 64.40 -100.75
REMARK 500 SER A 253 42.55 -152.67
REMARK 500 SER A 268 144.22 -170.68
REMARK 500 TRP A 315 -38.79 -139.89
REMARK 500 ALA A 339 82.17 45.40
REMARK 500 SER A 380 -19.33 -44.58
REMARK 500 THR A 385 -165.96 -105.38
REMARK 500 MET A 425 78.97 48.22
REMARK 500 PRO A 426 -173.94 -69.07
REMARK 500 TYR B 50 -109.11 -91.26
REMARK 500 ASP B 84 78.52 -151.43
REMARK 500 TRP B 86 -71.08 -58.88
REMARK 500 ASP B 99 -100.76 -74.34
REMARK 500 GLU B 100 128.80 64.53
REMARK 500 TYR B 106 -142.60 -128.79
REMARK 500 ASN B 136 65.37 -104.74
REMARK 500 PHE B 137 -54.43 -120.03
REMARK 500 PRO B 173 85.59 -55.59
REMARK 500 GLU B 174 6.60 -61.44
REMARK 500 SER B 253 43.51 -151.47
REMARK 500 TRP B 315 -37.96 -138.70
REMARK 500 ALA B 339 81.53 46.70
REMARK 500 THR B 385 -166.62 -104.79
REMARK 500 MET B 425 77.29 46.75
REMARK 500 PRO B 426 -173.55 -68.61
REMARK 500 TYR C 50 -109.41 -91.09
REMARK 500 ASP C 84 79.17 -153.41
REMARK 500 ASP C 99 -100.75 -71.73
REMARK 500 GLU C 100 128.47 64.89
REMARK 500 TYR C 106 -142.18 -129.07
REMARK 500 ASN C 136 64.47 -104.65
REMARK 500 PRO C 173 85.31 -56.04
REMARK 500 GLU C 174 6.42 -60.93
REMARK 500 SER C 253 44.78 -153.04
REMARK 500 TRP C 315 -38.06 -138.68
REMARK 500 ALA C 339 81.42 46.46
REMARK 500 SER C 380 -19.88 -43.55
REMARK 500 THR C 385 -167.70 -106.70
REMARK 500 MET C 425 78.80 47.33
REMARK 500 TYR D 50 -107.20 -91.23
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 TYR D 350 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D2K RELATED DB: PDB
REMARK 900 C. IMMITIS CHITINASE 1 AT 2.2 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1LL4 RELATED DB: PDB
REMARK 900 STRUCTURE OF C. IMMITIS CHITINASE 1 COMPLEXED WITH ALLOSAMIDIN
REMARK 900 RELATED ID: 1LL7 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE E171Q MUTANT OF C. IMMITIS CHITINASE 1
DBREF 1LL6 A 36 427 UNP P54196 CHI1_COCIM 36 427
DBREF 1LL6 B 36 427 UNP P54196 CHI1_COCIM 36 427
DBREF 1LL6 C 36 427 UNP P54196 CHI1_COCIM 36 427
DBREF 1LL6 D 36 427 UNP P54196 CHI1_COCIM 36 427
SEQADV 1LL6 ASN A 169 UNP P54196 ASP 169 ENGINEERED MUTATION
SEQADV 1LL6 ASN B 169 UNP P54196 ASP 169 ENGINEERED MUTATION
SEQADV 1LL6 ASN C 169 UNP P54196 ASP 169 ENGINEERED MUTATION
SEQADV 1LL6 ASN D 169 UNP P54196 ASP 169 ENGINEERED MUTATION
SEQRES 1 A 392 GLY GLY PHE ARG SER VAL VAL TYR PHE VAL ASN TRP ALA
SEQRES 2 A 392 ILE TYR GLY ARG GLY HIS ASN PRO GLN ASP LEU LYS ALA
SEQRES 3 A 392 ASP GLN PHE THR HIS ILE LEU TYR ALA PHE ALA ASN ILE
SEQRES 4 A 392 ARG PRO SER GLY GLU VAL TYR LEU SER ASP THR TRP ALA
SEQRES 5 A 392 ASP THR ASP LYS HIS TYR PRO GLY ASP LYS TRP ASP GLU
SEQRES 6 A 392 PRO GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN MET TYR
SEQRES 7 A 392 LEU LEU LYS LYS ASN ASN ARG ASN LEU LYS THR LEU LEU
SEQRES 8 A 392 SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE LYS THR
SEQRES 9 A 392 PRO ALA SER THR GLU GLU GLY ARG LYS LYS PHE ALA ASP
SEQRES 10 A 392 THR SER LEU LYS LEU MET LYS ASP LEU GLY PHE ASP GLY
SEQRES 11 A 392 ILE ASP ILE ASN TRP GLU TYR PRO GLU ASP GLU LYS GLN
SEQRES 12 A 392 ALA ASN ASP PHE VAL LEU LEU LEU LYS ALA CYS ARG GLU
SEQRES 13 A 392 ALA LEU ASP ALA TYR SER ALA LYS HIS PRO ASN GLY LYS
SEQRES 14 A 392 LYS PHE LEU LEU THR ILE ALA SER PRO ALA GLY PRO GLN
SEQRES 15 A 392 ASN TYR ASN LYS LEU LYS LEU ALA GLU MET ASP LYS TYR
SEQRES 16 A 392 LEU ASP PHE TRP ASN LEU MET ALA TYR ASP PHE SER GLY
SEQRES 17 A 392 SER TRP ASP LYS VAL SER GLY HIS MET SER ASN VAL PHE
SEQRES 18 A 392 PRO SER THR THR LYS PRO GLU SER THR PRO PHE SER SER
SEQRES 19 A 392 ASP LYS ALA VAL LYS ASP TYR ILE LYS ALA GLY VAL PRO
SEQRES 20 A 392 ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR GLY ARG
SEQRES 21 A 392 ALA PHE ALA SER THR ASP GLY ILE GLY THR SER PHE ASN
SEQRES 22 A 392 GLY VAL GLY GLY GLY SER TRP GLU ASN GLY VAL TRP ASP
SEQRES 23 A 392 TYR LYS ASP MET PRO GLN GLN GLY ALA GLN VAL THR GLU
SEQRES 24 A 392 LEU GLU ASP ILE ALA ALA SER TYR SER TYR ASP LYS ASN
SEQRES 25 A 392 LYS ARG TYR LEU ILE SER TYR ASP THR VAL LYS ILE ALA
SEQRES 26 A 392 GLY LYS LYS ALA GLU TYR ILE THR LYS ASN GLY MET GLY
SEQRES 27 A 392 GLY GLY MET TRP TRP GLU SER SER SER ASP LYS THR GLY
SEQRES 28 A 392 ASN GLU SER LEU VAL GLY THR VAL VAL ASN GLY LEU GLY
SEQRES 29 A 392 GLY THR GLY LYS LEU GLU GLN ARG GLU ASN GLU LEU SER
SEQRES 30 A 392 TYR PRO GLU SER VAL TYR ASP ASN LEU LYS ASN GLY MET
SEQRES 31 A 392 PRO SER
SEQRES 1 B 392 GLY GLY PHE ARG SER VAL VAL TYR PHE VAL ASN TRP ALA
SEQRES 2 B 392 ILE TYR GLY ARG GLY HIS ASN PRO GLN ASP LEU LYS ALA
SEQRES 3 B 392 ASP GLN PHE THR HIS ILE LEU TYR ALA PHE ALA ASN ILE
SEQRES 4 B 392 ARG PRO SER GLY GLU VAL TYR LEU SER ASP THR TRP ALA
SEQRES 5 B 392 ASP THR ASP LYS HIS TYR PRO GLY ASP LYS TRP ASP GLU
SEQRES 6 B 392 PRO GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN MET TYR
SEQRES 7 B 392 LEU LEU LYS LYS ASN ASN ARG ASN LEU LYS THR LEU LEU
SEQRES 8 B 392 SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE LYS THR
SEQRES 9 B 392 PRO ALA SER THR GLU GLU GLY ARG LYS LYS PHE ALA ASP
SEQRES 10 B 392 THR SER LEU LYS LEU MET LYS ASP LEU GLY PHE ASP GLY
SEQRES 11 B 392 ILE ASP ILE ASN TRP GLU TYR PRO GLU ASP GLU LYS GLN
SEQRES 12 B 392 ALA ASN ASP PHE VAL LEU LEU LEU LYS ALA CYS ARG GLU
SEQRES 13 B 392 ALA LEU ASP ALA TYR SER ALA LYS HIS PRO ASN GLY LYS
SEQRES 14 B 392 LYS PHE LEU LEU THR ILE ALA SER PRO ALA GLY PRO GLN
SEQRES 15 B 392 ASN TYR ASN LYS LEU LYS LEU ALA GLU MET ASP LYS TYR
SEQRES 16 B 392 LEU ASP PHE TRP ASN LEU MET ALA TYR ASP PHE SER GLY
SEQRES 17 B 392 SER TRP ASP LYS VAL SER GLY HIS MET SER ASN VAL PHE
SEQRES 18 B 392 PRO SER THR THR LYS PRO GLU SER THR PRO PHE SER SER
SEQRES 19 B 392 ASP LYS ALA VAL LYS ASP TYR ILE LYS ALA GLY VAL PRO
SEQRES 20 B 392 ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR GLY ARG
SEQRES 21 B 392 ALA PHE ALA SER THR ASP GLY ILE GLY THR SER PHE ASN
SEQRES 22 B 392 GLY VAL GLY GLY GLY SER TRP GLU ASN GLY VAL TRP ASP
SEQRES 23 B 392 TYR LYS ASP MET PRO GLN GLN GLY ALA GLN VAL THR GLU
SEQRES 24 B 392 LEU GLU ASP ILE ALA ALA SER TYR SER TYR ASP LYS ASN
SEQRES 25 B 392 LYS ARG TYR LEU ILE SER TYR ASP THR VAL LYS ILE ALA
SEQRES 26 B 392 GLY LYS LYS ALA GLU TYR ILE THR LYS ASN GLY MET GLY
SEQRES 27 B 392 GLY GLY MET TRP TRP GLU SER SER SER ASP LYS THR GLY
SEQRES 28 B 392 ASN GLU SER LEU VAL GLY THR VAL VAL ASN GLY LEU GLY
SEQRES 29 B 392 GLY THR GLY LYS LEU GLU GLN ARG GLU ASN GLU LEU SER
SEQRES 30 B 392 TYR PRO GLU SER VAL TYR ASP ASN LEU LYS ASN GLY MET
SEQRES 31 B 392 PRO SER
SEQRES 1 C 392 GLY GLY PHE ARG SER VAL VAL TYR PHE VAL ASN TRP ALA
SEQRES 2 C 392 ILE TYR GLY ARG GLY HIS ASN PRO GLN ASP LEU LYS ALA
SEQRES 3 C 392 ASP GLN PHE THR HIS ILE LEU TYR ALA PHE ALA ASN ILE
SEQRES 4 C 392 ARG PRO SER GLY GLU VAL TYR LEU SER ASP THR TRP ALA
SEQRES 5 C 392 ASP THR ASP LYS HIS TYR PRO GLY ASP LYS TRP ASP GLU
SEQRES 6 C 392 PRO GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN MET TYR
SEQRES 7 C 392 LEU LEU LYS LYS ASN ASN ARG ASN LEU LYS THR LEU LEU
SEQRES 8 C 392 SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE LYS THR
SEQRES 9 C 392 PRO ALA SER THR GLU GLU GLY ARG LYS LYS PHE ALA ASP
SEQRES 10 C 392 THR SER LEU LYS LEU MET LYS ASP LEU GLY PHE ASP GLY
SEQRES 11 C 392 ILE ASP ILE ASN TRP GLU TYR PRO GLU ASP GLU LYS GLN
SEQRES 12 C 392 ALA ASN ASP PHE VAL LEU LEU LEU LYS ALA CYS ARG GLU
SEQRES 13 C 392 ALA LEU ASP ALA TYR SER ALA LYS HIS PRO ASN GLY LYS
SEQRES 14 C 392 LYS PHE LEU LEU THR ILE ALA SER PRO ALA GLY PRO GLN
SEQRES 15 C 392 ASN TYR ASN LYS LEU LYS LEU ALA GLU MET ASP LYS TYR
SEQRES 16 C 392 LEU ASP PHE TRP ASN LEU MET ALA TYR ASP PHE SER GLY
SEQRES 17 C 392 SER TRP ASP LYS VAL SER GLY HIS MET SER ASN VAL PHE
SEQRES 18 C 392 PRO SER THR THR LYS PRO GLU SER THR PRO PHE SER SER
SEQRES 19 C 392 ASP LYS ALA VAL LYS ASP TYR ILE LYS ALA GLY VAL PRO
SEQRES 20 C 392 ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR GLY ARG
SEQRES 21 C 392 ALA PHE ALA SER THR ASP GLY ILE GLY THR SER PHE ASN
SEQRES 22 C 392 GLY VAL GLY GLY GLY SER TRP GLU ASN GLY VAL TRP ASP
SEQRES 23 C 392 TYR LYS ASP MET PRO GLN GLN GLY ALA GLN VAL THR GLU
SEQRES 24 C 392 LEU GLU ASP ILE ALA ALA SER TYR SER TYR ASP LYS ASN
SEQRES 25 C 392 LYS ARG TYR LEU ILE SER TYR ASP THR VAL LYS ILE ALA
SEQRES 26 C 392 GLY LYS LYS ALA GLU TYR ILE THR LYS ASN GLY MET GLY
SEQRES 27 C 392 GLY GLY MET TRP TRP GLU SER SER SER ASP LYS THR GLY
SEQRES 28 C 392 ASN GLU SER LEU VAL GLY THR VAL VAL ASN GLY LEU GLY
SEQRES 29 C 392 GLY THR GLY LYS LEU GLU GLN ARG GLU ASN GLU LEU SER
SEQRES 30 C 392 TYR PRO GLU SER VAL TYR ASP ASN LEU LYS ASN GLY MET
SEQRES 31 C 392 PRO SER
SEQRES 1 D 392 GLY GLY PHE ARG SER VAL VAL TYR PHE VAL ASN TRP ALA
SEQRES 2 D 392 ILE TYR GLY ARG GLY HIS ASN PRO GLN ASP LEU LYS ALA
SEQRES 3 D 392 ASP GLN PHE THR HIS ILE LEU TYR ALA PHE ALA ASN ILE
SEQRES 4 D 392 ARG PRO SER GLY GLU VAL TYR LEU SER ASP THR TRP ALA
SEQRES 5 D 392 ASP THR ASP LYS HIS TYR PRO GLY ASP LYS TRP ASP GLU
SEQRES 6 D 392 PRO GLY ASN ASN VAL TYR GLY CYS ILE LYS GLN MET TYR
SEQRES 7 D 392 LEU LEU LYS LYS ASN ASN ARG ASN LEU LYS THR LEU LEU
SEQRES 8 D 392 SER ILE GLY GLY TRP THR TYR SER PRO ASN PHE LYS THR
SEQRES 9 D 392 PRO ALA SER THR GLU GLU GLY ARG LYS LYS PHE ALA ASP
SEQRES 10 D 392 THR SER LEU LYS LEU MET LYS ASP LEU GLY PHE ASP GLY
SEQRES 11 D 392 ILE ASP ILE ASN TRP GLU TYR PRO GLU ASP GLU LYS GLN
SEQRES 12 D 392 ALA ASN ASP PHE VAL LEU LEU LEU LYS ALA CYS ARG GLU
SEQRES 13 D 392 ALA LEU ASP ALA TYR SER ALA LYS HIS PRO ASN GLY LYS
SEQRES 14 D 392 LYS PHE LEU LEU THR ILE ALA SER PRO ALA GLY PRO GLN
SEQRES 15 D 392 ASN TYR ASN LYS LEU LYS LEU ALA GLU MET ASP LYS TYR
SEQRES 16 D 392 LEU ASP PHE TRP ASN LEU MET ALA TYR ASP PHE SER GLY
SEQRES 17 D 392 SER TRP ASP LYS VAL SER GLY HIS MET SER ASN VAL PHE
SEQRES 18 D 392 PRO SER THR THR LYS PRO GLU SER THR PRO PHE SER SER
SEQRES 19 D 392 ASP LYS ALA VAL LYS ASP TYR ILE LYS ALA GLY VAL PRO
SEQRES 20 D 392 ALA ASN LYS ILE VAL LEU GLY MET PRO LEU TYR GLY ARG
SEQRES 21 D 392 ALA PHE ALA SER THR ASP GLY ILE GLY THR SER PHE ASN
SEQRES 22 D 392 GLY VAL GLY GLY GLY SER TRP GLU ASN GLY VAL TRP ASP
SEQRES 23 D 392 TYR LYS ASP MET PRO GLN GLN GLY ALA GLN VAL THR GLU
SEQRES 24 D 392 LEU GLU ASP ILE ALA ALA SER TYR SER TYR ASP LYS ASN
SEQRES 25 D 392 LYS ARG TYR LEU ILE SER TYR ASP THR VAL LYS ILE ALA
SEQRES 26 D 392 GLY LYS LYS ALA GLU TYR ILE THR LYS ASN GLY MET GLY
SEQRES 27 D 392 GLY GLY MET TRP TRP GLU SER SER SER ASP LYS THR GLY
SEQRES 28 D 392 ASN GLU SER LEU VAL GLY THR VAL VAL ASN GLY LEU GLY
SEQRES 29 D 392 GLY THR GLY LYS LEU GLU GLN ARG GLU ASN GLU LEU SER
SEQRES 30 D 392 TYR PRO GLU SER VAL TYR ASP ASN LEU LYS ASN GLY MET
SEQRES 31 D 392 PRO SER
FORMUL 5 HOH *43(H2 O)
HELIX 1 1 TRP A 47 TYR A 50 5 4
HELIX 2 2 ASN A 55 LEU A 59 5 5
HELIX 3 3 LYS A 60 PHE A 64 5 5
HELIX 4 4 ASP A 84 ASP A 90 1 7
HELIX 5 5 TYR A 106 ASN A 119 1 14
HELIX 6 6 TYR A 133 ASN A 136 5 4
HELIX 7 7 PHE A 137 THR A 143 1 7
HELIX 8 8 THR A 143 GLY A 162 1 20
HELIX 9 9 ASP A 175 LYS A 199 1 25
HELIX 10 10 GLY A 215 ASN A 220 1 6
HELIX 11 11 LYS A 223 LYS A 229 1 7
HELIX 12 12 LYS A 261 THR A 265 5 5
HELIX 13 13 SER A 268 GLY A 280 1 13
HELIX 14 14 PRO A 282 ASN A 284 5 3
HELIX 15 15 LYS A 323 MET A 325 5 3
HELIX 16 16 THR A 356 ASN A 370 1 15
HELIX 17 17 THR A 385 GLU A 388 5 4
HELIX 18 18 SER A 389 LEU A 398 1 10
HELIX 19 19 GLY A 400 LEU A 404 5 5
HELIX 20 20 TYR A 418 ASN A 423 1 6
HELIX 21 21 TRP B 47 TYR B 50 5 4
HELIX 22 22 ASN B 55 LEU B 59 5 5
HELIX 23 23 LYS B 60 PHE B 64 5 5
HELIX 24 24 ASP B 84 ASP B 90 1 7
HELIX 25 25 TYR B 106 ASN B 119 1 14
HELIX 26 26 TYR B 133 ASN B 136 5 4
HELIX 27 27 PHE B 137 THR B 143 1 7
HELIX 28 28 THR B 143 GLY B 162 1 20
HELIX 29 29 ASP B 175 LYS B 199 1 25
HELIX 30 30 GLY B 215 ASN B 220 1 6
HELIX 31 31 LYS B 223 LYS B 229 1 7
HELIX 32 32 LYS B 261 THR B 265 5 5
HELIX 33 33 SER B 268 GLY B 280 1 13
HELIX 34 34 PRO B 282 ASN B 284 5 3
HELIX 35 35 LYS B 323 MET B 325 5 3
HELIX 36 36 THR B 356 ASN B 370 1 15
HELIX 37 37 THR B 385 GLU B 388 5 4
HELIX 38 38 SER B 389 LEU B 398 1 10
HELIX 39 39 GLY B 400 LEU B 404 5 5
HELIX 40 40 TYR B 418 ASN B 423 1 6
HELIX 41 41 TRP C 47 TYR C 50 5 4
HELIX 42 42 ASN C 55 LEU C 59 5 5
HELIX 43 43 LYS C 60 PHE C 64 5 5
HELIX 44 44 ASP C 84 ASP C 90 1 7
HELIX 45 45 TYR C 106 ASN C 119 1 14
HELIX 46 46 TYR C 133 ASN C 136 5 4
HELIX 47 47 PHE C 137 THR C 143 1 7
HELIX 48 48 THR C 143 GLY C 162 1 20
HELIX 49 49 ASP C 175 LYS C 199 1 25
HELIX 50 50 GLY C 215 ASN C 220 1 6
HELIX 51 51 LYS C 223 LYS C 229 1 7
HELIX 52 52 LYS C 261 THR C 265 5 5
HELIX 53 53 SER C 268 GLY C 280 1 13
HELIX 54 54 PRO C 282 ASN C 284 5 3
HELIX 55 55 LYS C 323 MET C 325 5 3
HELIX 56 56 THR C 356 ASN C 370 1 15
HELIX 57 57 THR C 385 GLU C 388 5 4
HELIX 58 58 SER C 389 LEU C 398 1 10
HELIX 59 59 GLY C 400 LEU C 404 5 5
HELIX 60 60 TYR C 418 ASN C 423 1 6
HELIX 61 61 TRP D 47 TYR D 50 5 4
HELIX 62 62 ASN D 55 LEU D 59 5 5
HELIX 63 63 LYS D 60 PHE D 64 5 5
HELIX 64 64 ASP D 84 ASP D 90 1 7
HELIX 65 65 TYR D 106 ASN D 119 1 14
HELIX 66 66 TYR D 133 ASN D 136 5 4
HELIX 67 67 PHE D 137 THR D 143 1 7
HELIX 68 68 THR D 143 GLY D 162 1 20
HELIX 69 69 ASP D 175 LYS D 199 1 25
HELIX 70 70 GLY D 215 ASN D 220 1 6
HELIX 71 71 LYS D 223 LYS D 229 1 7
HELIX 72 72 LYS D 261 THR D 265 5 5
HELIX 73 73 SER D 268 GLY D 280 1 13
HELIX 74 74 PRO D 282 ASN D 284 5 3
HELIX 75 75 LYS D 323 MET D 325 5 3
HELIX 76 76 THR D 356 ASN D 370 1 15
HELIX 77 77 THR D 385 GLU D 388 5 4
HELIX 78 78 SER D 389 LEU D 398 1 10
HELIX 79 79 GLY D 400 LEU D 404 5 5
HELIX 80 80 TYR D 418 ASN D 423 1 6
SHEET 1 A10 VAL A 80 TYR A 81 0
SHEET 2 A10 HIS A 66 ILE A 74 -1 O ASN A 73 N TYR A 81
SHEET 3 A10 ARG A 39 VAL A 45 1 O SER A 40 N HIS A 66
SHEET 4 A10 GLY A 374 TRP A 378 1 O GLY A 375 N VAL A 41
SHEET 5 A10 ILE A 286 PRO A 291 1 O ILE A 286 N GLY A 374
SHEET 6 A10 PHE A 233 MET A 237 1 O TRP A 234 N VAL A 287
SHEET 7 A10 LEU A 207 PRO A 213 1 O LEU A 208 N PHE A 233
SHEET 8 A10 GLY A 165 ASN A 169 1 O ILE A 166 N THR A 209
SHEET 9 A10 LYS A 123 GLY A 129 1 O THR A 124 N GLY A 165
SHEET 10 A10 HIS A 66 ILE A 74 1 N ILE A 67 O LYS A 123
SHEET 1 B 5 GLN A 331 GLU A 334 0
SHEET 2 B 5 SER A 341 ASP A 345 -1 O TYR A 342 N THR A 333
SHEET 3 B 5 TYR A 350 SER A 353 -1 O TYR A 350 N ASP A 345
SHEET 4 B 5 TYR A 293 ALA A 298 -1 O ARG A 295 N SER A 353
SHEET 5 B 5 VAL A 319 ASP A 321 -1 O TRP A 320 N GLY A 294
SHEET 1 C10 VAL B 80 TYR B 81 0
SHEET 2 C10 HIS B 66 ILE B 74 -1 O ASN B 73 N TYR B 81
SHEET 3 C10 ARG B 39 VAL B 45 1 O SER B 40 N HIS B 66
SHEET 4 C10 GLY B 374 TRP B 378 1 O GLY B 375 N VAL B 41
SHEET 5 C10 ILE B 286 PRO B 291 1 O ILE B 286 N GLY B 374
SHEET 6 C10 PHE B 233 MET B 237 1 O TRP B 234 N VAL B 287
SHEET 7 C10 LEU B 207 PRO B 213 1 O LEU B 208 N PHE B 233
SHEET 8 C10 GLY B 165 ASN B 169 1 N ILE B 166 O LEU B 207
SHEET 9 C10 LYS B 123 GLY B 129 1 O THR B 124 N GLY B 165
SHEET 10 C10 HIS B 66 ILE B 74 1 N ILE B 67 O LYS B 123
SHEET 1 D 5 GLN B 331 LEU B 335 0
SHEET 2 D 5 ALA B 340 ASP B 345 -1 O ALA B 340 N LEU B 335
SHEET 3 D 5 TYR B 350 SER B 353 -1 O TYR B 350 N ASP B 345
SHEET 4 D 5 TYR B 293 ALA B 298 -1 O ARG B 295 N SER B 353
SHEET 5 D 5 VAL B 319 ASP B 321 -1 O TRP B 320 N GLY B 294
SHEET 1 E10 VAL C 80 TYR C 81 0
SHEET 2 E10 HIS C 66 ILE C 74 -1 O ASN C 73 N TYR C 81
SHEET 3 E10 ARG C 39 VAL C 45 1 O SER C 40 N HIS C 66
SHEET 4 E10 GLY C 374 TRP C 378 1 O GLY C 375 N VAL C 41
SHEET 5 E10 ILE C 286 PRO C 291 1 O ILE C 286 N GLY C 374
SHEET 6 E10 PHE C 233 MET C 237 1 O TRP C 234 N VAL C 287
SHEET 7 E10 LEU C 207 PRO C 213 1 O LEU C 208 N PHE C 233
SHEET 8 E10 GLY C 165 ASN C 169 1 O ILE C 166 N THR C 209
SHEET 9 E10 LYS C 123 GLY C 129 1 O THR C 124 N GLY C 165
SHEET 10 E10 HIS C 66 ILE C 74 1 O ILE C 67 N LEU C 125
SHEET 1 F 5 GLN C 331 LEU C 335 0
SHEET 2 F 5 ALA C 340 ASP C 345 -1 O ALA C 340 N LEU C 335
SHEET 3 F 5 TYR C 350 SER C 353 -1 O TYR C 350 N ASP C 345
SHEET 4 F 5 TYR C 293 ALA C 298 -1 O ARG C 295 N SER C 353
SHEET 5 F 5 VAL C 319 ASP C 321 -1 O TRP C 320 N GLY C 294
SHEET 1 G10 VAL D 80 TYR D 81 0
SHEET 2 G10 HIS D 66 ILE D 74 -1 O ASN D 73 N TYR D 81
SHEET 3 G10 ARG D 39 VAL D 45 1 O SER D 40 N HIS D 66
SHEET 4 G10 GLY D 374 TRP D 378 1 O GLY D 375 N VAL D 41
SHEET 5 G10 ILE D 286 PRO D 291 1 O ILE D 286 N GLY D 374
SHEET 6 G10 PHE D 233 MET D 237 1 O TRP D 234 N VAL D 287
SHEET 7 G10 LEU D 207 PRO D 213 1 O LEU D 208 N PHE D 233
SHEET 8 G10 GLY D 165 ASN D 169 1 N ILE D 166 O LEU D 207
SHEET 9 G10 LYS D 123 GLY D 129 1 O THR D 124 N GLY D 165
SHEET 10 G10 HIS D 66 ILE D 74 1 N ILE D 67 O LYS D 123
SHEET 1 H 5 GLN D 331 LEU D 335 0
SHEET 2 H 5 ALA D 340 ASP D 345 -1 O ALA D 340 N LEU D 335
SHEET 3 H 5 TYR D 350 SER D 353 -1 O TYR D 350 N ASP D 345
SHEET 4 H 5 TYR D 293 ALA D 298 -1 O ARG D 295 N SER D 353
SHEET 5 H 5 VAL D 319 ASP D 321 -1 O TRP D 320 N GLY D 294
CISPEP 1 ALA A 70 PHE A 71 0 0.26
CISPEP 2 GLU A 171 TYR A 172 0 -0.24
CISPEP 3 MET A 325 PRO A 326 0 -6.53
CISPEP 4 TRP A 378 GLU A 379 0 0.46
CISPEP 5 ALA B 70 PHE B 71 0 -0.39
CISPEP 6 GLU B 171 TYR B 172 0 0.37
CISPEP 7 MET B 325 PRO B 326 0 -6.98
CISPEP 8 TRP B 378 GLU B 379 0 0.73
CISPEP 9 ALA C 70 PHE C 71 0 0.43
CISPEP 10 GLU C 171 TYR C 172 0 -0.10
CISPEP 11 MET C 325 PRO C 326 0 -8.37
CISPEP 12 TRP C 378 GLU C 379 0 -0.21
CISPEP 13 ALA D 70 PHE D 71 0 0.28
CISPEP 14 GLU D 171 TYR D 172 0 0.10
CISPEP 15 MET D 325 PRO D 326 0 -8.33
CISPEP 16 TRP D 378 GLU D 379 0 -0.73
CRYST1 60.890 78.180 88.430 80.51 82.13 66.99 P 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 0.016423 -0.006975 -0.001429 0.00000
SCALE2 0.000000 0.013897 -0.001710 0.00000
SCALE3 0.000000 0.000000 0.011502 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
