HEADER HYDROLASE 20-AUG-10 3AMG
TITLE CRYSTAL STRUCTURES OF THERMOTOGA MARITIMA CEL5A IN COMPLEX WITH
TITLE 2 CELLOBIOSE SUBSTRATE, MUTANT FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.1.4;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: MSB8;
SOURCE 5 GENE: TM_1751;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32 XA/LIC
KEYWDS GLYCOSYL HYDROLASE FAMILY 5, CELLULASE, BIOFUEL, HYPERTHERMOSTABLE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.H.WU,C.H.HUANG,T.P.KO,H.L.LAI,Y.MA,Y.S.CHENG,J.R.LIU,R.T.GUO
REVDAT 4 13-MAR-24 3AMG 1 HETSYN
REVDAT 3 29-JUL-20 3AMG 1 COMPND REMARK SEQADV HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 05-JUN-13 3AMG 1 JRNL SITE
REVDAT 1 17-AUG-11 3AMG 0
JRNL AUTH T.H.WU,C.H.HUANG,T.P.KO,H.L.LAI,Y.MA,C.C.CHEN,Y.S.CHENG,
JRNL AUTH 2 J.R.LIU,R.T.GUO
JRNL TITL DIVERSE SUBSTRATE RECOGNITION MECHANISM REVEALED BY
JRNL TITL 2 THERMOTOGA MARITIMA CEL5A STRUCTURES IN COMPLEX WITH
JRNL TITL 3 CELLOTETRAOSE, CELLOBIOSE AND MANNOTRIOSE
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1814 1832 2011
JRNL REFN ISSN 0006-3002
JRNL PMID 21839861
JRNL DOI 10.1016/J.BBAPAP.2011.07.020
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.21
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 20271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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 : 5038
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.74100
REMARK 3 B22 (A**2) : 0.54800
REMARK 3 B33 (A**2) : 10.19300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 13.67700
REMARK 3 B23 (A**2) : 0.00000
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 1.533 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.598 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.957 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.055 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 57.87
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CBI_DUNDEE.PAR
REMARK 3 PARAMETER FILE 4 : GLC_DUNDEE.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AMG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000029430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21337
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.387
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 36.67800
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
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, 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 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 MET A 1
REMARK 465 GLY A 313
REMARK 465 ASP A 314
REMARK 465 SER A 315
REMARK 465 ILE A 316
REMARK 465 GLU A 317
REMARK 465 MET B 1
REMARK 465 TRP B 217
REMARK 465 LEU B 218
REMARK 465 GLY B 219
REMARK 465 ARG B 220
REMARK 465 LYS B 221
REMARK 465 TRP B 222
REMARK 465 GLY B 223
REMARK 465 SER B 224
REMARK 465 PRO B 225
REMARK 465 ASP B 226
REMARK 465 ASP B 227
REMARK 465 GLN B 228
REMARK 465 LYS B 229
REMARK 465 HIS B 230
REMARK 465 LEU B 231
REMARK 465 ILE B 232
REMARK 465 GLU B 233
REMARK 465 GLU B 234
REMARK 465 PHE B 235
REMARK 465 ASN B 236
REMARK 465 GLY B 313
REMARK 465 ASP B 314
REMARK 465 SER B 315
REMARK 465 ILE B 316
REMARK 465 GLU B 317
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 21 -98.68 -126.20
REMARK 500 ARG A 86 16.76 -66.47
REMARK 500 TYR A 97 71.03 -100.04
REMARK 500 ASP A 103 61.49 -153.05
REMARK 500 GLU A 127 9.58 -68.60
REMARK 500 ILE A 133 -71.80 -39.58
REMARK 500 ALA A 136 68.11 31.15
REMARK 500 LYS A 181 1.42 -63.74
REMARK 500 ASN A 190 55.30 -143.43
REMARK 500 ASN A 199 -63.25 -1.89
REMARK 500 PRO A 200 56.75 -69.95
REMARK 500 PRO A 225 -87.98 -61.11
REMARK 500 PHE A 254 132.45 -172.09
REMARK 500 GLU A 287 129.94 42.38
REMARK 500 SER A 290 -153.40 -70.99
REMARK 500 THR A 297 -76.52 -37.95
REMARK 500 ARG A 299 4.02 158.10
REMARK 500 LYS A 300 79.33 24.23
REMARK 500 LYS A 304 -38.06 -26.49
REMARK 500 ALA B 21 -104.60 -122.61
REMARK 500 ARG B 55 76.23 -101.57
REMARK 500 TYR B 66 42.05 75.43
REMARK 500 TYR B 125 160.84 -47.21
REMARK 500 ALA B 136 68.46 17.10
REMARK 500 HIS B 138 -178.75 -172.04
REMARK 500 LEU B 141 68.31 -105.10
REMARK 500 TRP B 173 32.65 70.69
REMARK 500 SER B 177 2.44 -64.93
REMARK 500 ALA B 178 24.14 -143.56
REMARK 500 LYS B 186 -10.88 -49.85
REMARK 500 LYS B 246 72.14 40.75
REMARK 500 GLU B 287 129.10 65.02
REMARK 500 CYS B 289 42.72 -141.96
REMARK 500 SER B 290 -129.97 -143.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE METABOLISM
REMARK 630 MOLECULE NAME: BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 BGC A 400
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AMC RELATED DB: PDB
REMARK 900 RELATED ID: 3AMD RELATED DB: PDB
REMARK 900 RELATED ID: 3AOF RELATED DB: PDB
REMARK 900 RELATED ID: 3AZR RELATED DB: PDB
REMARK 900 RELATED ID: 3AZS RELATED DB: PDB
REMARK 900 RELATED ID: 3AZT RELATED DB: PDB
DBREF 3AMG A 1 317 UNP Q9X273 Q9X273_THEMA 1 317
DBREF 3AMG B 1 317 UNP Q9X273 Q9X273_THEMA 1 317
SEQADV 3AMG ALA A 136 UNP Q9X273 GLU 136 ENGINEERED MUTATION
SEQADV 3AMG ALA B 136 UNP Q9X273 GLU 136 ENGINEERED MUTATION
SEQRES 1 A 317 MET GLY VAL ASP PRO PHE GLU ARG ASN LYS ILE LEU GLY
SEQRES 2 A 317 ARG GLY ILE ASN ILE GLY ASN ALA LEU GLU ALA PRO ASN
SEQRES 3 A 317 GLU GLY ASP TRP GLY VAL VAL ILE LYS ASP GLU PHE PHE
SEQRES 4 A 317 ASP ILE ILE LYS GLU ALA GLY PHE SER HIS VAL ARG ILE
SEQRES 5 A 317 PRO ILE ARG TRP SER THR HIS ALA TYR ALA PHE PRO PRO
SEQRES 6 A 317 TYR LYS ILE MET ASP ARG PHE PHE LYS ARG VAL ASP GLU
SEQRES 7 A 317 VAL ILE ASN GLY ALA LEU LYS ARG GLY LEU ALA VAL VAL
SEQRES 8 A 317 ILE ASN ILE HIS HIS TYR GLU GLU LEU MET ASN ASP PRO
SEQRES 9 A 317 GLU GLU HIS LYS GLU ARG PHE LEU ALA LEU TRP LYS GLN
SEQRES 10 A 317 ILE ALA ASP ARG TYR LYS ASP TYR PRO GLU THR LEU PHE
SEQRES 11 A 317 PHE GLU ILE LEU ASN ALA PRO HIS GLY ASN LEU THR PRO
SEQRES 12 A 317 GLU LYS TRP ASN GLU LEU LEU GLU GLU ALA LEU LYS VAL
SEQRES 13 A 317 ILE ARG SER ILE ASP LYS LYS HIS THR ILE ILE ILE GLY
SEQRES 14 A 317 THR ALA GLU TRP GLY GLY ILE SER ALA LEU GLU LYS LEU
SEQRES 15 A 317 SER VAL PRO LYS TRP GLU LYS ASN SER ILE VAL THR ILE
SEQRES 16 A 317 HIS TYR TYR ASN PRO PHE GLU PHE THR HIS GLN GLY ALA
SEQRES 17 A 317 GLU TRP VAL GLU GLY SER GLU LYS TRP LEU GLY ARG LYS
SEQRES 18 A 317 TRP GLY SER PRO ASP ASP GLN LYS HIS LEU ILE GLU GLU
SEQRES 19 A 317 PHE ASN PHE ILE GLU GLU TRP SER LYS LYS ASN LYS ARG
SEQRES 20 A 317 PRO ILE TYR ILE GLY GLU PHE GLY ALA TYR ARG LYS ALA
SEQRES 21 A 317 ASP LEU GLU SER ARG ILE LYS TRP THR SER PHE VAL VAL
SEQRES 22 A 317 ARG GLU MET GLU LYS ARG ARG TRP SER TRP ALA TYR TRP
SEQRES 23 A 317 GLU PHE CYS SER GLY PHE GLY VAL TYR ASP THR LEU ARG
SEQRES 24 A 317 LYS THR TRP ASN LYS ASP LEU LEU GLU ALA LEU ILE GLY
SEQRES 25 A 317 GLY ASP SER ILE GLU
SEQRES 1 B 317 MET GLY VAL ASP PRO PHE GLU ARG ASN LYS ILE LEU GLY
SEQRES 2 B 317 ARG GLY ILE ASN ILE GLY ASN ALA LEU GLU ALA PRO ASN
SEQRES 3 B 317 GLU GLY ASP TRP GLY VAL VAL ILE LYS ASP GLU PHE PHE
SEQRES 4 B 317 ASP ILE ILE LYS GLU ALA GLY PHE SER HIS VAL ARG ILE
SEQRES 5 B 317 PRO ILE ARG TRP SER THR HIS ALA TYR ALA PHE PRO PRO
SEQRES 6 B 317 TYR LYS ILE MET ASP ARG PHE PHE LYS ARG VAL ASP GLU
SEQRES 7 B 317 VAL ILE ASN GLY ALA LEU LYS ARG GLY LEU ALA VAL VAL
SEQRES 8 B 317 ILE ASN ILE HIS HIS TYR GLU GLU LEU MET ASN ASP PRO
SEQRES 9 B 317 GLU GLU HIS LYS GLU ARG PHE LEU ALA LEU TRP LYS GLN
SEQRES 10 B 317 ILE ALA ASP ARG TYR LYS ASP TYR PRO GLU THR LEU PHE
SEQRES 11 B 317 PHE GLU ILE LEU ASN ALA PRO HIS GLY ASN LEU THR PRO
SEQRES 12 B 317 GLU LYS TRP ASN GLU LEU LEU GLU GLU ALA LEU LYS VAL
SEQRES 13 B 317 ILE ARG SER ILE ASP LYS LYS HIS THR ILE ILE ILE GLY
SEQRES 14 B 317 THR ALA GLU TRP GLY GLY ILE SER ALA LEU GLU LYS LEU
SEQRES 15 B 317 SER VAL PRO LYS TRP GLU LYS ASN SER ILE VAL THR ILE
SEQRES 16 B 317 HIS TYR TYR ASN PRO PHE GLU PHE THR HIS GLN GLY ALA
SEQRES 17 B 317 GLU TRP VAL GLU GLY SER GLU LYS TRP LEU GLY ARG LYS
SEQRES 18 B 317 TRP GLY SER PRO ASP ASP GLN LYS HIS LEU ILE GLU GLU
SEQRES 19 B 317 PHE ASN PHE ILE GLU GLU TRP SER LYS LYS ASN LYS ARG
SEQRES 20 B 317 PRO ILE TYR ILE GLY GLU PHE GLY ALA TYR ARG LYS ALA
SEQRES 21 B 317 ASP LEU GLU SER ARG ILE LYS TRP THR SER PHE VAL VAL
SEQRES 22 B 317 ARG GLU MET GLU LYS ARG ARG TRP SER TRP ALA TYR TRP
SEQRES 23 B 317 GLU PHE CYS SER GLY PHE GLY VAL TYR ASP THR LEU ARG
SEQRES 24 B 317 LYS THR TRP ASN LYS ASP LEU LEU GLU ALA LEU ILE GLY
SEQRES 25 B 317 GLY ASP SER ILE GLU
HET BGC C 1 12
HET BGC C 2 11
HET BGC A 400 12
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 3 BGC 3(C6 H12 O6)
FORMUL 5 HOH *123(H2 O)
HELIX 1 1 ASP A 4 GLY A 13 1 10
HELIX 2 2 GLU A 37 ALA A 45 1 9
HELIX 3 3 ARG A 55 HIS A 59 5 5
HELIX 4 4 MET A 69 ARG A 86 1 18
HELIX 5 5 TYR A 97 ASP A 103 1 7
HELIX 6 6 ASP A 103 LYS A 123 1 21
HELIX 7 7 THR A 142 ASP A 161 1 20
HELIX 8 8 PRO A 200 HIS A 205 1 6
HELIX 9 9 GLY A 213 LEU A 218 5 6
HELIX 10 10 SER A 224 LYS A 244 1 21
HELIX 11 11 ASP A 261 ARG A 279 1 19
HELIX 12 12 ASN A 303 ILE A 311 1 9
HELIX 13 13 ASP B 4 GLY B 13 1 10
HELIX 14 14 ASP B 36 GLU B 44 1 9
HELIX 15 15 ARG B 55 ALA B 60 5 6
HELIX 16 16 MET B 69 ARG B 86 1 18
HELIX 17 17 TYR B 97 ASP B 103 1 7
HELIX 18 18 ASP B 103 LYS B 123 1 21
HELIX 19 19 THR B 142 ASP B 161 1 20
HELIX 20 20 PRO B 200 HIS B 205 1 6
HELIX 21 21 ILE B 238 LYS B 243 1 6
HELIX 22 22 ASP B 261 ARG B 279 1 19
HELIX 23 23 ASN B 303 ILE B 311 1 9
SHEET 1 A 9 ARG A 14 ASN A 17 0
SHEET 2 A 9 HIS A 49 ILE A 52 1 O ARG A 51 N ILE A 16
SHEET 3 A 9 ALA A 89 ILE A 94 1 O VAL A 91 N ILE A 52
SHEET 4 A 9 LEU A 129 LEU A 134 1 O PHE A 130 N VAL A 90
SHEET 5 A 9 ILE A 166 ILE A 168 1 O ILE A 167 N PHE A 131
SHEET 6 A 9 SER A 191 HIS A 196 1 O ILE A 192 N ILE A 168
SHEET 7 A 9 ILE A 249 GLU A 253 1 O TYR A 250 N ILE A 195
SHEET 8 A 9 SER A 282 TYR A 285 1 O SER A 282 N ILE A 251
SHEET 9 A 9 ARG A 14 ASN A 17 1 N GLY A 15 O TRP A 283
SHEET 1 B 2 TYR A 295 ASP A 296 0
SHEET 2 B 2 THR A 301 TRP A 302 -1 O THR A 301 N ASP A 296
SHEET 1 C 9 ARG B 14 ASN B 17 0
SHEET 2 C 9 HIS B 49 ILE B 52 1 O HIS B 49 N ILE B 16
SHEET 3 C 9 ALA B 89 ASN B 93 1 O ALA B 89 N VAL B 50
SHEET 4 C 9 LEU B 129 GLU B 132 1 O GLU B 132 N ILE B 92
SHEET 5 C 9 ILE B 166 ILE B 168 1 O ILE B 167 N PHE B 131
SHEET 6 C 9 SER B 191 HIS B 196 1 O THR B 194 N ILE B 168
SHEET 7 C 9 ILE B 249 GLU B 253 1 O TYR B 250 N ILE B 195
SHEET 8 C 9 SER B 282 TYR B 285 1 O SER B 282 N ILE B 249
SHEET 9 C 9 ARG B 14 ASN B 17 1 N ASN B 17 O TYR B 285
SHEET 1 D 2 TYR B 295 ASP B 296 0
SHEET 2 D 2 THR B 301 TRP B 302 -1 O THR B 301 N ASP B 296
LINK O4 BGC C 1 C1 BGC C 2 1555 1555 1.44
CISPEP 1 PRO A 64 PRO A 65 0 0.14
CISPEP 2 PRO B 64 PRO B 65 0 0.04
CISPEP 3 ASN B 199 PRO B 200 0 -0.22
CRYST1 60.979 73.356 62.192 90.00 97.57 90.00 P 1 21 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 0.016399 0.000000 0.002179 0.00000
SCALE2 0.000000 0.013632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016221 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
