HEADER HYDROLASE 08-JAN-10 3LB9
TITLE CRYSTAL STRUCTURE OF THE B. CIRCULANS CPA123 CIRCULAR PERMUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 65-182 AND 2-63;
COMPND 5 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;
SOURCE 3 ORGANISM_TAXID: 1397;
SOURCE 4 GENE: XLNA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21( DE3)
KEYWDS PERMUTATION, BCX, GLYCOSIDASE, XYLAN DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.D'ANGELO,S.REITINGER,M.LUDWICZEK,N.STRYNADKA,S.G.WITHERS,
AUTHOR 2 L.P.MCINTOSH
REVDAT 5 06-SEP-23 3LB9 1 REMARK
REVDAT 4 13-JUN-18 3LB9 1 KEYWDS SEQADV
REVDAT 3 26-JUL-17 3LB9 1 SOURCE REMARK
REVDAT 2 28-APR-10 3LB9 1 JRNL
REVDAT 1 23-MAR-10 3LB9 0
JRNL AUTH S.REITINGER,Y.YU,J.WICKI,M.LUDWICZEK,I.D'ANGELO,S.BATURIN,
JRNL AUTH 2 M.OKON,N.C.STRYNADKA,S.LUTZ,S.G.WITHERS,L.P.MCINTOSH
JRNL TITL CIRCULAR PERMUTATION OF BACILLUS CIRCULANS XYLANASE: A
JRNL TITL 2 KINETIC AND STRUCTURAL STUDY.
JRNL REF BIOCHEMISTRY V. 49 2464 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20163191
JRNL DOI 10.1021/BI100036F
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.490
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 9443
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 473
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.8767 - 4.3171 1.00 3011 159 0.1693 0.1993
REMARK 3 2 4.3171 - 3.4324 1.00 2980 157 0.1790 0.2885
REMARK 3 3 3.4324 - 3.0002 1.00 2979 157 0.2347 0.3326
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 2.52
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.680
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 4409
REMARK 3 ANGLE : 0.688 6050
REMARK 3 CHIRALITY : 0.049 616
REMARK 3 PLANARITY : 0.006 767
REMARK 3 DIHEDRAL : 17.601 1390
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LB9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057064.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.514
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : OSMICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10649
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : 0.14800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
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) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1147.
REMARK 200 R MERGE FOR SHELL (I) : 0.41200
REMARK 200 R SYM FOR SHELL (I) : 0.41200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1HV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-20 % (NH4)2SO4 40 MM TRIS-HCL, PH
REMARK 280 8, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.48500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 57.48500
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -25.89942
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 59.64999
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 PRO B 181 C - N - CD ANGL. DEV. = -28.6 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 ALA A 44 -150.83 -89.14
REMARK 500 GLN A 46 111.43 -161.55
REMARK 500 ASN A 97 48.06 36.10
REMARK 500 ALA A 120 88.64 -68.47
REMARK 500 ASN A 126 73.66 -114.54
REMARK 500 ASN A 179 33.42 106.08
REMARK 500 PRO A 181 -111.42 -86.27
REMARK 500 GLN B 46 113.76 -161.48
REMARK 500 SER B 55 -169.78 -165.96
REMARK 500 ALA B 66 -108.68 -147.09
REMARK 500 SER B 67 108.13 -172.88
REMARK 500 ASN B 97 48.65 38.05
REMARK 500 ASN B 126 65.17 -109.31
REMARK 500 SER B 182 -68.07 175.39
REMARK 500 LYS C 14 118.62 -34.57
REMARK 500 ALA C 44 -157.66 -95.85
REMARK 500 SER C 55 -166.57 -129.91
REMARK 500 SER C 56 118.49 -176.15
REMARK 500 TRP C 64 -130.18 -159.30
REMARK 500 ALA C 66 -74.34 123.93
REMARK 500 ASN C 73 89.60 -151.92
REMARK 500 TYR C 178 178.77 86.66
REMARK 500 ASN C 179 -155.75 -121.11
REMARK 500 ALA C 180 -153.89 -131.33
REMARK 500 PRO C 181 -96.59 -120.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HV1 RELATED DB: PDB
DBREF 3LB9 A 66 183 UNP P09850 XYNA_BACCI 29 146
DBREF 3LB9 A 3 64 UNP P09850 XYNA_BACCI 152 213
DBREF 3LB9 B 66 183 UNP P09850 XYNA_BACCI 29 146
DBREF 3LB9 B 3 64 UNP P09850 XYNA_BACCI 152 213
DBREF 3LB9 C 66 183 UNP P09850 XYNA_BACCI 29 146
DBREF 3LB9 C 3 64 UNP P09850 XYNA_BACCI 152 213
SEQADV 3LB9 ALA A 2 UNP P09850 EXPRESSION TAG
SEQADV 3LB9 GLY A 65 UNP P09850 LINKER
SEQADV 3LB9 ALA B 2 UNP P09850 EXPRESSION TAG
SEQADV 3LB9 GLY B 65 UNP P09850 LINKER
SEQADV 3LB9 ALA C 2 UNP P09850 EXPRESSION TAG
SEQADV 3LB9 GLY C 65 UNP P09850 LINKER
SEQRES 1 A 182 ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS
SEQRES 2 A 182 ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN
SEQRES 3 A 182 HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY
SEQRES 4 A 182 SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR
SEQRES 5 A 182 GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA
SEQRES 6 A 182 SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY
SEQRES 7 A 182 ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER
SEQRES 8 A 182 VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS
SEQRES 9 A 182 GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR
SEQRES 10 A 182 ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU
SEQRES 11 A 182 THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR
SEQRES 12 A 182 TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY
SEQRES 13 A 182 THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR
SEQRES 14 A 182 ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE
SEQRES 1 B 182 ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS
SEQRES 2 B 182 ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN
SEQRES 3 B 182 HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY
SEQRES 4 B 182 SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR
SEQRES 5 B 182 GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA
SEQRES 6 B 182 SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY
SEQRES 7 B 182 ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER
SEQRES 8 B 182 VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS
SEQRES 9 B 182 GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR
SEQRES 10 B 182 ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU
SEQRES 11 B 182 THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR
SEQRES 12 B 182 TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY
SEQRES 13 B 182 THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR
SEQRES 14 B 182 ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE
SEQRES 1 C 182 ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS
SEQRES 2 C 182 ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN
SEQRES 3 C 182 HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY
SEQRES 4 C 182 SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR
SEQRES 5 C 182 GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA
SEQRES 6 C 182 SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY
SEQRES 7 C 182 ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER
SEQRES 8 C 182 VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS
SEQRES 9 C 182 GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR
SEQRES 10 C 182 ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU
SEQRES 11 C 182 THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR
SEQRES 12 C 182 TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY
SEQRES 13 C 182 THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR
SEQRES 14 C 182 ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE
FORMUL 4 HOH *40(H2 O)
HELIX 1 1 PHE A 25 SER A 34 1 10
HELIX 2 2 PHE B 25 SER B 34 1 10
HELIX 3 3 PHE C 25 SER C 34 1 10
SHEET 1 A 5 TYR A 70 THR A 75 0
SHEET 2 A 5 PHE A 101 TRP A 107 -1 O GLY A 104 N GLN A 72
SHEET 3 A 5 ASN A 42 THR A 62 -1 N THR A 50 O VAL A 103
SHEET 4 A 5 ASN A 90 SER A 96 -1 O TRP A 95 N GLY A 57
SHEET 5 A 5 ILE A 80 ASN A 85 -1 N ILE A 80 O SER A 96
SHEET 1 B 8 TYR A 70 THR A 75 0
SHEET 2 B 8 PHE A 101 TRP A 107 -1 O GLY A 104 N GLN A 72
SHEET 3 B 8 ASN A 42 THR A 62 -1 N THR A 50 O VAL A 103
SHEET 4 B 8 VAL A 122 ARG A 138 -1 O TYR A 134 N VAL A 47
SHEET 5 B 8 ILE A 142 TRP A 150 -1 O SER A 149 N LEU A 131
SHEET 6 B 8 THR A 3 ARG A 11 1 N SER A 9 O VAL A 147
SHEET 7 B 8 GLY A 168 TYR A 178 -1 O THR A 175 N GLN A 6
SHEET 8 B 8 THR A 158 SER A 165 -1 N GLY A 161 O ILE A 172
SHEET 1 C 2 ASN A 20 THR A 24 0
SHEET 2 C 2 THR A 115 ASN A 119 -1 O TYR A 118 N ALA A 21
SHEET 1 D 5 ASN B 20 THR B 24 0
SHEET 2 D 5 THR B 115 ARG B 138 -1 O ILE B 116 N ILE B 23
SHEET 3 D 5 ASN B 42 TRP B 64 -1 N SER B 56 O ASN B 126
SHEET 4 D 5 ASN B 90 SER B 96 -1 O VAL B 93 N SER B 59
SHEET 5 D 5 ILE B 80 ASN B 85 -1 N VAL B 84 O SER B 92
SHEET 1 E 8 TYR B 70 THR B 75 0
SHEET 2 E 8 ASN B 100 TRP B 107 -1 O GLY B 104 N GLN B 72
SHEET 3 E 8 ASN B 42 TRP B 64 -1 N THR B 50 O VAL B 103
SHEET 4 E 8 THR B 115 ARG B 138 -1 O ASN B 126 N SER B 56
SHEET 5 E 8 ILE B 142 SER B 149 -1 O ILE B 142 N THR B 137
SHEET 6 E 8 PHE B 4 ARG B 11 1 N THR B 5 O GLU B 143
SHEET 7 E 8 GLY B 168 ARG B 177 -1 O ARG B 177 N PHE B 4
SHEET 8 E 8 THR B 158 SER B 165 -1 N GLY B 161 O ILE B 172
SHEET 1 F 8 TYR C 70 THR C 75 0
SHEET 2 F 8 ASN C 100 TRP C 107 -1 O GLY C 104 N GLN C 72
SHEET 3 F 8 ASN C 42 TYR C 53 -1 N THR C 50 O VAL C 103
SHEET 4 F 8 GLY C 129 ARG C 138 -1 O TYR C 134 N VAL C 47
SHEET 5 F 8 ILE C 142 TRP C 150 -1 O SER C 149 N LEU C 131
SHEET 6 F 8 PHE C 4 ARG C 11 1 N ARG C 11 O VAL C 147
SHEET 7 F 8 GLY C 168 ARG C 177 -1 O TYR C 173 N TRP C 8
SHEET 8 F 8 THR C 158 SER C 165 -1 N GLY C 161 O ILE C 172
SHEET 1 G 5 ASN C 20 THR C 24 0
SHEET 2 G 5 THR C 115 ASN C 126 -1 O TYR C 118 N ALA C 21
SHEET 3 G 5 SER C 56 VAL C 63 -1 N SER C 56 O ASN C 126
SHEET 4 G 5 ASN C 90 SER C 96 -1 O TYR C 91 N VAL C 61
SHEET 5 G 5 ILE C 80 VAL C 81 -1 N ILE C 80 O SER C 96
CISPEP 1 SER A 139 PRO A 140 0 -2.77
CISPEP 2 SER B 139 PRO B 140 0 -1.53
CISPEP 3 PRO B 181 SER B 182 0 -11.39
CISPEP 4 SER C 139 PRO C 140 0 -2.20
CISPEP 5 ALA C 180 PRO C 181 0 -0.11
CRYST1 69.810 114.970 65.030 90.00 113.47 90.00 C 1 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014325 0.000000 0.006220 0.00000
SCALE2 0.000000 0.008698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016764 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
