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HEADER HYDROLASE 25-NOV-99 1QOZ
TITLE CATALYTIC CORE DOMAIN OF ACETYL XYLAN ESTERASE FROM
TITLE 2 TRICHODERMA REESEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: AXE;
COMPND 6 EC: 3.1.1.72
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHODERMA REESEI;
SOURCE 3 STRAIN: RUTC-30
KEYWDS HYDROLASE, ESTERASE, XYLAN DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.HAKULINEN,J.ROUVINEN
REVDAT 2 20-MAR-01 1QOZ 1 JRNL REMARK
REVDAT 1 24-NOV-00 1QOZ 0
JRNL AUTH N.HAKULINEN,M.TENKANEN,J.ROUVINEN
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE CATALYTIC CORE
JRNL TITL 2 OF ACETYLXYLAN ESTERASE FROM TRICHODERMA REESEI:
JRNL TITL 3 INSIGHTS INTO THE DEACETYLATION MECHANISM
JRNL REF J.STRUCT.BIOL. V. 132 180 2000
JRNL REFN ASTM JSBIEM US ISSN 1047-8477
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.HAKULINEN,M.TENKANEN,J.ROUVINEN
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 STUDIES OF THE CATALYTIC CORE OF ACETYLXYLAN
REMARK 1 TITL 3 ESTERASE FROM TRICHODERMA REESEI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 54 430 1998
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.9 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 25039
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) : 0.186
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2552
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.5
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1353
REMARK 3 BIN R VALUE (WORKING SET) : 0.279
REMARK 3 BIN FREE R VALUE : 0.320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 131
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 : 2922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 425
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.12
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.197
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.65
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.055
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QOZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 25-NOV-1999.
REMARK 100 THE EBI ID CODE IS EBI-4424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-1998
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NONE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU 200HB
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27058
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 99.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87
REMARK 200 DATA REDUNDANCY : 2.07
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.057
REMARK 200 FOR THE DATA SET : 14.9
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.9
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 46.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.247
REMARK 200 FOR SHELL : 2.38
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1BS9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M POTASSIUM/SODIUM TARTRATE,
REMARK 280 0.1 M TES, 9 MM TRITON-X, PH 8.2
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 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 1 .. 206 B 1 .. 206 0.095
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK:
REMARK 295 TRANSFORMATION RELATES MOLECULE A TO MOLECULE B
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 BIOLOGICAL UNIT: MONOMER
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
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 SER B 207
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 168 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLY A 189 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ALA B 154 N - CA - C ANGL. DEV. = 7.2 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER A 90 59.35 -113.30
REMARK 500 SER B 90 60.45 -114.18
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 525
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CATALYTIC TRIAD (CHAIN A)
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CATALYTIC TRIAD (CHAIN B)
REMARK 800
DBREF 1QOZ A 1 207 SWS Q99034 Q99034 32 238
DBREF 1QOZ B 1 207 SWS Q99034 Q99034 32 238
SEQADV 1QOZ PCA A 1 GLN 1 MODIFICATION
SEQADV 1QOZ PCA B 1 GLN 1 MODIFICATION
SEQRES 1 A 207 PCA CYS PRO ALA ILE HIS VAL PHE GLY ALA ARG GLU THR
SEQRES 2 A 207 THR VAL SER GLN GLY TYR GLY SER SER ALA THR VAL VAL
SEQRES 3 A 207 ASN LEU VAL ILE GLN ALA HIS PRO GLY THR THR SER GLU
SEQRES 4 A 207 ALA ILE VAL TYR PRO ALA CYS GLY GLY GLN ALA SER CYS
SEQRES 5 A 207 GLY GLY ILE SER TYR ALA ASN SER VAL VAL ASN GLY THR
SEQRES 6 A 207 ASN ALA ALA ALA ALA ALA ILE ASN ASN PHE HIS ASN SER
SEQRES 7 A 207 CYS PRO ASP THR GLN LEU VAL LEU VAL GLY TYR SER GLN
SEQRES 8 A 207 GLY ALA GLN ILE PHE ASP ASN ALA LEU CYS GLY GLY GLY
SEQRES 9 A 207 ASP PRO GLY GLU GLY ILE THR ASN THR ALA VAL PRO LEU
SEQRES 10 A 207 THR ALA GLY ALA VAL SER ALA VAL LYS ALA ALA ILE PHE
SEQRES 11 A 207 MET GLY ASP PRO ARG ASN ILE HIS GLY LEU PRO TYR ASN
SEQRES 12 A 207 VAL GLY THR CYS THR THR GLN GLY PHE ASP ALA ARG PRO
SEQRES 13 A 207 ALA GLY PHE VAL CYS PRO SER ALA SER LYS ILE LYS SER
SEQRES 14 A 207 TYR CYS ASP ALA ALA ASP PRO TYR CYS CYS THR GLY ASN
SEQRES 15 A 207 ASP PRO ASN VAL HIS GLN GLY TYR GLY GLN GLU TYR GLY
SEQRES 16 A 207 GLN GLN ALA LEU ALA PHE ILE ASN SER GLN LEU SER
SEQRES 1 B 207 PCA CYS PRO ALA ILE HIS VAL PHE GLY ALA ARG GLU THR
SEQRES 2 B 207 THR VAL SER GLN GLY TYR GLY SER SER ALA THR VAL VAL
SEQRES 3 B 207 ASN LEU VAL ILE GLN ALA HIS PRO GLY THR THR SER GLU
SEQRES 4 B 207 ALA ILE VAL TYR PRO ALA CYS GLY GLY GLN ALA SER CYS
SEQRES 5 B 207 GLY GLY ILE SER TYR ALA ASN SER VAL VAL ASN GLY THR
SEQRES 6 B 207 ASN ALA ALA ALA ALA ALA ILE ASN ASN PHE HIS ASN SER
SEQRES 7 B 207 CYS PRO ASP THR GLN LEU VAL LEU VAL GLY TYR SER GLN
SEQRES 8 B 207 GLY ALA GLN ILE PHE ASP ASN ALA LEU CYS GLY GLY GLY
SEQRES 9 B 207 ASP PRO GLY GLU GLY ILE THR ASN THR ALA VAL PRO LEU
SEQRES 10 B 207 THR ALA GLY ALA VAL SER ALA VAL LYS ALA ALA ILE PHE
SEQRES 11 B 207 MET GLY ASP PRO ARG ASN ILE HIS GLY LEU PRO TYR ASN
SEQRES 12 B 207 VAL GLY THR CYS THR THR GLN GLY PHE ASP ALA ARG PRO
SEQRES 13 B 207 ALA GLY PHE VAL CYS PRO SER ALA SER LYS ILE LYS SER
SEQRES 14 B 207 TYR CYS ASP ALA ALA ASP PRO TYR CYS CYS THR GLY ASN
SEQRES 15 B 207 ASP PRO ASN VAL HIS GLN GLY TYR GLY GLN GLU TYR GLY
SEQRES 16 B 207 GLN GLN ALA LEU ALA PHE ILE ASN SER GLN LEU SER
MODRES 1QOZ PCA A 1 GLN PYROGLUTAMIC ACID
MODRES 1QOZ PCA B 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET PCA B 1 8
HET NAG A 926 14
HET NAG B 927 14
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN PCA PYRROLIDONE CARBOXYLIC ACID
HETSYN PCA PCA
FORMUL 3 PCA 2(C5 H7 N1 O3)
FORMUL 4 NAG 2(C8 H15 N1 O6)
FORMUL 5 HOH *425(H2 O1)
HELIX 1 1 GLY A 20 SER A 22 5 3
HELIX 2 2 ALA A 23 ALA A 32 1 11
HELIX 3 3 ALA A 50 CYS A 52 5 3
HELIX 4 4 TYR A 57 SER A 78 1 22
HELIX 5 5 GLN A 91 CYS A 101 1 11
HELIX 6 6 PRO A 106 GLU A 108 5 3
HELIX 7 7 ALA A 119 ALA A 124 1 6
HELIX 8 8 ALA A 164 LYS A 166 5 3
HELIX 9 9 PRO A 184 GLN A 188 1 5
HELIX 10 10 TYR A 190 GLN A 205 1 16
HELIX 11 11 GLY B 20 SER B 22 5 3
HELIX 12 12 ALA B 23 ALA B 32 1 11
HELIX 13 13 ALA B 50 CYS B 52 5 3
HELIX 14 14 TYR B 57 SER B 78 1 22
HELIX 15 15 GLN B 91 CYS B 101 1 11
HELIX 16 16 PRO B 106 GLU B 108 5 3
HELIX 17 17 ALA B 119 ALA B 124 1 6
HELIX 18 18 ALA B 164 LYS B 166 5 3
HELIX 19 19 PRO B 184 GLN B 188 1 5
HELIX 20 20 TYR B 190 GLN B 205 1 16
SHEET 1 A 5 THR A 36 ALA A 40 0
SHEET 2 A 5 ILE A 5 ALA A 10 1 N ILE A 5 O THR A 37
SHEET 3 A 5 GLN A 83 TYR A 89 1 N GLN A 83 O HIS A 6
SHEET 4 A 5 VAL A 125 MET A 131 1 N LYS A 126 O LEU A 84
SHEET 5 A 5 ILE A 167 TYR A 170 1 N LYS A 168 O ALA A 128
SHEET 6 A 5 ASN A 143 VAL A 144 1
SHEET 1 B 5 THR B 36 ALA B 40 0
SHEET 2 B 5 ILE B 5 ALA B 10 1 N ILE B 5 O THR B 37
SHEET 3 B 5 GLN B 83 TYR B 89 1 N GLN B 83 O HIS B 6
SHEET 4 B 5 VAL B 125 MET B 131 1 N LYS B 126 O LEU B 84
SHEET 5 B 5 ILE B 167 TYR B 170 1 N LYS B 168 O ALA B 128
SHEET 6 A 5 ASN B 143 VAL B 144 1
SSBOND 1 CYS A 2 CYS A 79 1555 1555
SSBOND 2 CYS A 46 CYS A 52 1555 1555
SSBOND 3 CYS A 101 CYS A 161 1555 1555
SSBOND 4 CYS A 147 CYS A 179 1555 1555
SSBOND 5 CYS A 171 CYS A 178 1555 1555
SSBOND 6 CYS B 2 CYS B 79 1555 1555
SSBOND 7 CYS B 46 CYS B 52 1555 1555
SSBOND 8 CYS B 101 CYS B 161 1555 1555
SSBOND 9 CYS B 147 CYS B 179 1555 1555
SSBOND 10 CYS B 171 CYS B 178 1555 1555
LINK C PCA A 1 N CYS A 2 1555 1555
LINK ND2 ASN A 63 C1 NAG A 926 1555 1555
LINK C PCA B 1 N CYS B 2 1555 1555
LINK ND2 ASN B 63 C1 NAG B 927 1555 1555
SITE 1 AS1 3 SER A 90 ASP A 175 HIS A 187
SITE 1 AS2 3 SER B 90 ASP B 175 HIS B 187
CRYST1 50.300 61.000 40.000 107.70 113.50 98.80 P 1 2
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 0.019881 0.003078 0.010799 0.00000
SCALE2 0.000000 0.016589 0.007300 0.00000
SCALE3 0.000000 0.000000 0.029784 0.00000
MTRIX1 1 -0.684600 0.291100 -0.668200 22.27210 1
MTRIX2 1 0.293800 -0.728800 -0.618500 27.38550 1
MTRIX3 1 -0.667000 -0.619800 0.413400 -1.28620 1
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