HEADER HYDROLASE 14-OCT-12 3VZJ
TITLE CRYSTAL STRUCTURE OF THE BACILLUS CIRCULANS ENDO-BETA-(1,4)-XYLANASE
TITLE 2 (BCX) E172H MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: 562
KEYWDS XYLANASE, GH-11 GLYCOSIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.LUDWICZEK,I.D'ANGELO,G.N.YALLOWAY,M.OKON,J.E.NIELSEN,
AUTHOR 2 N.C.STRYNADKA,S.G.WITHERS,L.P.MCINTOSH
REVDAT 3 08-NOV-23 3VZJ 1 REMARK SEQADV
REVDAT 2 31-JUL-13 3VZJ 1 JRNL
REVDAT 1 08-MAY-13 3VZJ 0
JRNL AUTH M.L.LUDWICZEK,I.D'ANGELO,G.N.YALLOWAY,J.A.BROCKERMAN,M.OKON,
JRNL AUTH 2 J.E.NIELSEN,N.C.STRYNADKA,S.G.WITHERS,L.P.MCINTOSH
JRNL TITL STRATEGIES FOR MODULATING THE PH-DEPENDENT ACTIVITY OF A
JRNL TITL 2 FAMILY 11 GLYCOSIDE HYDROLASE
JRNL REF BIOCHEMISTRY V. 52 3138 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23578322
JRNL DOI 10.1021/BI400034M
REMARK 2
REMARK 2 RESOLUTION. 2.41 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) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 64.4
REMARK 3 NUMBER OF REFLECTIONS : 16311
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.343
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 832
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 38.1722 - 4.3709 0.61 2474 141 0.1682 0.2605
REMARK 3 2 4.3709 - 3.4700 0.64 2560 139 0.1960 0.3103
REMARK 3 3 3.4700 - 3.0316 0.66 2649 140 0.2369 0.3838
REMARK 3 4 3.0316 - 2.7545 0.68 2694 145 0.3012 0.3653
REMARK 3 5 2.7545 - 2.5571 0.68 2735 148 0.3329 0.4784
REMARK 3 6 2.5571 - 2.4064 0.60 2367 119 0.3353 0.4124
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 : 0.37
REMARK 3 B_SOL : 67.95
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.590
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18060
REMARK 3 B22 (A**2) : -0.76100
REMARK 3 B33 (A**2) : 1.94160
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01080
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 6000
REMARK 3 ANGLE : 1.237 8232
REMARK 3 CHIRALITY : 0.085 836
REMARK 3 PLANARITY : 0.006 1048
REMARK 3 DIHEDRAL : 20.684 1900
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 3VZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000095696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541
REMARK 200 MONOCHROMATOR : SI(111)
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31471
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 38.167
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 39.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-20% (NH4)2SO4, 40MM TRIS-HCL, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.36850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 90 C - N - CA ANGL. DEV. = 9.1 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 ASN A 32 41.15 71.20
REMARK 500 ASN A 54 88.52 -154.60
REMARK 500 ASN A 61 71.95 -112.82
REMARK 500 TRP A 85 168.85 174.77
REMARK 500 PRO A 90 152.41 -48.57
REMARK 500 THR A 97 -161.31 -129.19
REMARK 500 VAL A 98 121.67 173.48
REMARK 500 ASP A 101 30.49 72.96
REMARK 500 ASN A 114 76.86 66.85
REMARK 500 ALA A 115 149.28 -177.53
REMARK 500 PRO A 116 171.08 -53.98
REMARK 500 ASP A 121 -170.21 49.24
REMARK 500 ALA A 165 -161.38 -107.48
REMARK 500 GLN A 175 60.40 35.06
REMARK 500 ASP B 4 -2.27 -141.03
REMARK 500 ASN B 32 86.20 44.36
REMARK 500 TYR B 53 -167.92 -112.21
REMARK 500 ASN B 54 105.34 -166.35
REMARK 500 SER B 74 76.04 43.79
REMARK 500 ASN B 114 77.31 47.89
REMARK 500 ASP B 119 -17.90 -40.32
REMARK 500 ASP B 121 -141.11 37.24
REMARK 500 ALA B 165 -155.07 -98.85
REMARK 500 TRP C 6 105.36 -166.98
REMARK 500 ASN C 32 65.89 27.17
REMARK 500 THR C 33 -158.97 -87.82
REMARK 500 TRP C 58 77.73 -114.32
REMARK 500 TRP C 85 159.49 178.98
REMARK 500 LYS C 95 -7.07 -144.09
REMARK 500 ASN C 114 17.34 56.81
REMARK 500 ASP C 121 -136.44 57.91
REMARK 500 LYS C 154 -29.35 -36.11
REMARK 500 ALA C 165 -154.45 -69.43
REMARK 500 GLN C 167 116.39 -170.08
REMARK 500 ASN D 8 88.88 -153.53
REMARK 500 TYR D 53 -168.72 -167.83
REMARK 500 ASN D 54 115.10 -167.96
REMARK 500 ASN D 61 69.94 -104.09
REMARK 500 SER D 74 76.64 58.46
REMARK 500 ASN D 114 42.20 25.81
REMARK 500 ASP D 119 21.53 -56.36
REMARK 500 ASP D 121 -146.99 51.62
REMARK 500 THR D 123 -169.55 -161.63
REMARK 500 LYS D 154 -37.03 -37.83
REMARK 500 ALA D 165 -153.35 -97.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HV1 RELATED DB: PDB
REMARK 900 DISSECTING ELECTROSTATIC INTERACTIONS AND THE PH-DEPENDENT ACTIVITY
REMARK 900 OF A FAMILY 11 GLYCOSIDASE
REMARK 900 RELATED ID: 3VZK RELATED DB: PDB
REMARK 900 RELATED ID: 3VZL RELATED DB: PDB
REMARK 900 RELATED ID: 3VZM RELATED DB: PDB
REMARK 900 RELATED ID: 3VZN RELATED DB: PDB
REMARK 900 RELATED ID: 3VZO RELATED DB: PDB
DBREF 3VZJ A 1 185 UNP P09850 XYNA_BACCI 29 213
DBREF 3VZJ B 1 185 UNP P09850 XYNA_BACCI 29 213
DBREF 3VZJ C 1 185 UNP P09850 XYNA_BACCI 29 213
DBREF 3VZJ D 1 185 UNP P09850 XYNA_BACCI 29 213
SEQADV 3VZJ HIS A 172 UNP P09850 GLU 200 ENGINEERED MUTATION
SEQADV 3VZJ HIS B 172 UNP P09850 GLU 200 ENGINEERED MUTATION
SEQADV 3VZJ HIS C 172 UNP P09850 GLU 200 ENGINEERED MUTATION
SEQADV 3VZJ HIS D 172 UNP P09850 GLU 200 ENGINEERED MUTATION
SEQRES 1 A 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 A 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 A 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 A 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 A 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 A 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 A 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 A 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 A 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 A 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 A 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 A 185 ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 A 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 A 185 ALA THR HIS GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 A 185 THR VAL TRP
SEQRES 1 B 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 B 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 B 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 B 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 B 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 B 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 B 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 B 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 B 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 B 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 B 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 B 185 ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 B 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 B 185 ALA THR HIS GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 B 185 THR VAL TRP
SEQRES 1 C 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 C 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 C 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 C 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 C 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 C 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 C 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 C 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 C 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 C 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 C 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 C 185 ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 C 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 C 185 ALA THR HIS GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 C 185 THR VAL TRP
SEQRES 1 D 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 D 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 D 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 D 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 D 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 D 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 D 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 D 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 D 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 D 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 D 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 D 185 ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 D 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 D 185 ALA THR HIS GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 D 185 THR VAL TRP
HET SO4 A 201 5
HET SO4 D 201 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *74(H2 O)
HELIX 1 1 PHE A 146 SER A 155 1 10
HELIX 2 2 PHE B 146 HIS B 156 1 11
HELIX 3 3 PHE C 146 HIS C 156 1 11
HELIX 4 4 PHE D 146 LYS D 154 1 9
HELIX 5 5 SER D 155 GLY D 157 5 3
SHEET 1 A 8 TYR A 5 THR A 10 0
SHEET 2 A 8 ASN A 35 TRP A 42 -1 O GLY A 41 N TYR A 5
SHEET 3 A 8 ASN A 163 TYR A 174 -1 O THR A 171 N VAL A 38
SHEET 4 A 8 GLY A 64 ARG A 73 -1 N TYR A 69 O VAL A 168
SHEET 5 A 8 ILE A 77 TRP A 85 -1 O ASP A 83 N LEU A 66
SHEET 6 A 8 THR A 126 ARG A 132 1 O SER A 130 N VAL A 82
SHEET 7 A 8 GLY A 103 THR A 111 -1 N ASP A 106 O VAL A 131
SHEET 8 A 8 THR A 93 SER A 100 -1 N GLY A 96 O ILE A 107
SHEET 1 B 4 ILE A 15 ASN A 20 0
SHEET 2 B 4 ASN A 25 SER A 31 -1 O SER A 27 N VAL A 19
SHEET 3 B 4 SER A 177 TRP A 185 -1 O GLY A 178 N TRP A 30
SHEET 4 B 4 VAL A 57 ASN A 61 -1 N ALA A 59 O SER A 179
SHEET 1 C 5 ILE A 15 ASN A 20 0
SHEET 2 C 5 ASN A 25 SER A 31 -1 O SER A 27 N VAL A 19
SHEET 3 C 5 SER A 177 TRP A 185 -1 O GLY A 178 N TRP A 30
SHEET 4 C 5 THR A 50 TYR A 53 -1 N ASN A 52 O TRP A 185
SHEET 5 C 5 ALA A 142 THR A 145 -1 O ALA A 142 N TYR A 53
SHEET 1 D 8 TYR B 5 THR B 10 0
SHEET 2 D 8 PHE B 36 TRP B 42 -1 O GLY B 39 N GLN B 7
SHEET 3 D 8 ASN B 163 THR B 171 -1 O MET B 169 N LYS B 40
SHEET 4 D 8 TYR B 65 ARG B 73 -1 N TYR B 69 O VAL B 168
SHEET 5 D 8 ILE B 77 TRP B 85 -1 O ILE B 77 N THR B 72
SHEET 6 D 8 GLY B 120 ARG B 132 1 O SER B 130 N VAL B 82
SHEET 7 D 8 GLY B 103 SER B 117 -1 N ASP B 106 O VAL B 131
SHEET 8 D 8 THR B 93 SER B 100 -1 N VAL B 98 O TYR B 105
SHEET 1 E 4 ILE B 15 ASN B 20 0
SHEET 2 E 4 ASN B 25 SER B 31 -1 O ASN B 29 N ASN B 17
SHEET 3 E 4 SER B 177 TRP B 185 -1 O GLY B 178 N TRP B 30
SHEET 4 E 4 VAL B 57 ASN B 61 -1 N ALA B 59 O SER B 179
SHEET 1 F 5 ILE B 15 ASN B 20 0
SHEET 2 F 5 ASN B 25 SER B 31 -1 O ASN B 29 N ASN B 17
SHEET 3 F 5 SER B 177 TRP B 185 -1 O GLY B 178 N TRP B 30
SHEET 4 F 5 THR B 50 ASN B 54 -1 N ASN B 52 O TRP B 185
SHEET 5 F 5 ASN B 141 THR B 145 -1 O ILE B 144 N ILE B 51
SHEET 1 G 8 TYR C 5 THR C 10 0
SHEET 2 G 8 ASN C 35 TRP C 42 -1 O VAL C 37 N TRP C 9
SHEET 3 G 8 ASN C 163 TYR C 174 -1 O MET C 169 N LYS C 40
SHEET 4 G 8 GLY C 64 ARG C 73 -1 N ARG C 73 O ASN C 163
SHEET 5 G 8 ILE C 77 TRP C 85 -1 O ASP C 83 N LEU C 66
SHEET 6 G 8 PHE C 125 ARG C 132 1 O TYR C 128 N TYR C 80
SHEET 7 G 8 GLY C 103 ARG C 112 -1 N TYR C 108 O TRP C 129
SHEET 8 G 8 THR C 93 SER C 100 -1 N LYS C 95 O ILE C 107
SHEET 1 H 5 ILE C 15 ASN C 20 0
SHEET 2 H 5 ASN C 25 SER C 31 -1 O SER C 27 N VAL C 19
SHEET 3 H 5 SER C 177 TRP C 185 -1 O SER C 180 N VAL C 28
SHEET 4 H 5 THR C 50 ASN C 61 -1 N ALA C 59 O SER C 179
SHEET 5 H 5 ALA C 142 THR C 145 -1 O ALA C 142 N TYR C 53
SHEET 1 I 8 TYR D 5 THR D 10 0
SHEET 2 I 8 ASN D 35 TRP D 42 -1 O GLY D 39 N GLN D 7
SHEET 3 I 8 ASN D 163 TYR D 174 -1 O MET D 169 N LYS D 40
SHEET 4 I 8 GLY D 64 ARG D 73 -1 N ARG D 73 O ASN D 163
SHEET 5 I 8 ILE D 77 TRP D 85 -1 O TYR D 79 N GLY D 70
SHEET 6 I 8 GLY D 120 ARG D 132 1 O TYR D 128 N GLU D 78
SHEET 7 I 8 GLY D 103 SER D 117 -1 N ALA D 115 O THR D 123
SHEET 8 I 8 THR D 93 SER D 100 -1 N LYS D 95 O ILE D 107
SHEET 1 J 5 ILE D 15 ASN D 20 0
SHEET 2 J 5 ASN D 25 SER D 31 -1 O SER D 27 N VAL D 19
SHEET 3 J 5 SER D 177 THR D 183 -1 O VAL D 182 N TYR D 26
SHEET 4 J 5 THR D 50 ASN D 61 -1 N GLY D 56 O ASN D 181
SHEET 5 J 5 ASN D 141 THR D 145 -1 O ALA D 142 N TYR D 53
CISPEP 1 SER A 74 PRO A 75 0 0.73
CISPEP 2 SER B 74 PRO B 75 0 -2.49
CISPEP 3 HIS B 172 GLY B 173 0 -6.96
CISPEP 4 SER C 74 PRO C 75 0 0.24
CISPEP 5 SER D 74 PRO D 75 0 -1.62
SITE 1 AC1 2 LYS A 135 SER D 22
SITE 1 AC2 3 ARG D 132 LYS D 135 PRO D 137
CRYST1 52.174 86.737 73.090 90.00 89.89 90.00 P 1 21 1 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 0.019167 0.000000 -0.000037 0.00000
SCALE2 0.000000 0.011529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013682 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
