HEADER HYDROLASE 11-MAY-04 1WD4
TITLE CRYSTAL STRUCTURE OF ARABINOFURANOSIDASE COMPLEXED WITH ARABINOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-L-ARABINOFURANOSIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ARABINOFURANOSIDASE;
COMPND 5 EC: 3.2.1.55;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS KAWACHII;
SOURCE 3 ORGANISM_TAXID: 40384;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPICZAC
KEYWDS BETA-SANDWICH, BETA-TREFOIL, COMPLEX WITH ARABINOSE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MIYANAGA,T.KOSEKI,H.MATSUZAWA,T.WAKAGI,H.SHOUN,S.FUSHINOBU
REVDAT 5 29-JUL-20 1WD4 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 13-JUL-11 1WD4 1 VERSN
REVDAT 3 24-FEB-09 1WD4 1 VERSN
REVDAT 2 24-JAN-06 1WD4 1 JRNL
REVDAT 1 14-SEP-04 1WD4 0
JRNL AUTH A.MIYANAGA,T.KOSEKI,H.MATSUZAWA,T.WAKAGI,H.SHOUN,S.FUSHINOBU
JRNL TITL CRYSTAL STRUCTURE OF A FAMILY 54 ALPHA-L-ARABINOFURANOSIDASE
JRNL TITL 2 REVEALS A NOVEL CARBOHYDRATE-BINDING MODULE THAT CAN BIND
JRNL TITL 3 ARABINOSE
JRNL REF J.BIOL.CHEM. V. 279 44907 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15292273
JRNL DOI 10.1074/JBC.M405390200
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1877203.610
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 31098
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) : 0.188
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1575
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4758
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 251
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3579
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.90000
REMARK 3 B22 (A**2) : 18.51000
REMARK 3 B33 (A**2) : -10.61000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.13
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.730
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.610 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.460 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.110 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 54.31
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NAG2.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NAG2.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35261
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
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 (%) : 88.3
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) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
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: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, PH 5.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 19.73050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.06750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.06750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.73050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O4 NAG B 1 O5 NAG B 2 2.09
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 SER A 36 135.86 -174.15
REMARK 500 THR A 84 -168.43 -161.34
REMARK 500 GLU A 196 89.41 -167.39
REMARK 500 TRP A 206 -100.44 -119.49
REMARK 500 GLU A 221 129.67 81.93
REMARK 500 ASN A 223 134.07 171.88
REMARK 500 ALA A 252 102.70 -58.90
REMARK 500 SER A 343 175.23 65.49
REMARK 500 TYR A 359 15.57 -141.92
REMARK 500 ALA A 365 -157.39 -140.12
REMARK 500 ASP A 368 -135.29 62.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WD3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH NAG AT 1.75 A
DBREF 1WD4 A 19 499 GB 21280333 BAB96816 19 499
SEQADV 1WD4 MET A 18 GB 21280333 INITIATING METHIONINE
SEQRES 1 A 482 MET GLY PRO CYS ASP ILE TYR GLU ALA GLY ASP THR PRO
SEQRES 2 A 482 CYS VAL ALA ALA HIS SER THR THR ARG ALA LEU TYR SER
SEQRES 3 A 482 SER PHE SER GLY ALA LEU TYR GLN LEU GLN ARG GLY SER
SEQRES 4 A 482 ASP ASP THR THR THR THR ILE SER PRO LEU THR ALA GLY
SEQRES 5 A 482 GLY ILE ALA ASP ALA SER ALA GLN ASP THR PHE CYS ALA
SEQRES 6 A 482 ASN THR THR CYS LEU ILE THR ILE ILE TYR ASP GLN SER
SEQRES 7 A 482 GLY ASN GLY ASN HIS LEU THR GLN ALA PRO PRO GLY GLY
SEQRES 8 A 482 PHE ASP GLY PRO ASP THR ASP GLY TYR ASP ASN LEU ALA
SEQRES 9 A 482 SER ALA ILE GLY ALA PRO VAL THR LEU ASN GLY GLN LYS
SEQRES 10 A 482 ALA TYR GLY VAL PHE MET SER PRO GLY THR GLY TYR ARG
SEQRES 11 A 482 ASN ASN GLU ALA THR GLY THR ALA THR GLY ASP GLU ALA
SEQRES 12 A 482 GLU GLY MET TYR ALA VAL LEU ASP GLY THR HIS TYR ASN
SEQRES 13 A 482 ASP ALA CYS CYS PHE ASP TYR GLY ASN ALA GLU THR SER
SEQRES 14 A 482 SER THR ASP THR GLY ALA GLY HIS MET GLU ALA ILE TYR
SEQRES 15 A 482 LEU GLY ASN SER THR THR TRP GLY TYR GLY ALA GLY ASP
SEQRES 16 A 482 GLY PRO TRP ILE MET VAL ASP MET GLU ASN ASN LEU PHE
SEQRES 17 A 482 SER GLY ALA ASP GLU GLY TYR ASN SER GLY ASP PRO SER
SEQRES 18 A 482 ILE SER TYR ARG PHE VAL THR ALA ALA VAL LYS GLY GLY
SEQRES 19 A 482 ALA ASP LYS TRP ALA ILE ARG GLY ALA ASN ALA ALA SER
SEQRES 20 A 482 GLY SER LEU SER THR TYR TYR SER GLY ALA ARG PRO ASP
SEQRES 21 A 482 TYR SER GLY TYR ASN PRO MET SER LYS GLU GLY ALA ILE
SEQRES 22 A 482 ILE LEU GLY ILE GLY GLY ASP ASN SER ASN GLY ALA GLN
SEQRES 23 A 482 GLY THR PHE TYR GLU GLY VAL MET THR SER GLY TYR PRO
SEQRES 24 A 482 SER ASP ASP THR GLU ASN SER VAL GLN GLU ASN ILE VAL
SEQRES 25 A 482 ALA ALA LYS TYR VAL VAL GLY SER LEU VAL SER GLY PRO
SEQRES 26 A 482 SER PHE THR SER GLY GLU VAL VAL SER LEU ARG VAL THR
SEQRES 27 A 482 THR PRO GLY TYR THR THR ARG TYR ILE ALA HIS THR ASP
SEQRES 28 A 482 THR THR VAL ASN THR GLN VAL VAL ASP ASP ASP SER SER
SEQRES 29 A 482 THR THR LEU LYS GLU GLU ALA SER TRP THR VAL VAL THR
SEQRES 30 A 482 GLY LEU ALA ASN SER GLN CYS PHE SER PHE GLU SER VAL
SEQRES 31 A 482 ASP THR PRO GLY SER TYR ILE ARG HIS TYR ASN PHE GLU
SEQRES 32 A 482 LEU LEU LEU ASN ALA ASN ASP GLY THR LYS GLN PHE HIS
SEQRES 33 A 482 GLU ASP ALA THR PHE CYS PRO GLN ALA ALA LEU ASN GLY
SEQRES 34 A 482 GLU GLY THR SER LEU ARG SER TRP SER TYR PRO THR ARG
SEQRES 35 A 482 TYR PHE ARG HIS TYR GLU ASN VAL LEU TYR ALA ALA SER
SEQRES 36 A 482 ASN GLY GLY VAL GLN THR PHE ASP SER LYS THR SER PHE
SEQRES 37 A 482 ASN ASN ASP VAL SER PHE GLU ILE GLU THR ALA PHE ALA
SEQRES 38 A 482 SER
MODRES 1WD4 ASN A 202 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET AHR A 601 10
HET AHR A 602 10
HET AHR A 603 10
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM AHR ALPHA-L-ARABINOFURANOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 AHR 3(C5 H10 O5)
FORMUL 6 HOH *230(H2 O)
HELIX 1 1 GLY A 19 GLY A 27 1 9
HELIX 2 2 ASP A 73 CYS A 81 1 9
HELIX 3 3 ASP A 113 TYR A 117 5 5
HELIX 4 4 SER A 317 LYS A 332 1 16
HELIX 5 5 SER A 381 ALA A 388 1 8
HELIX 6 6 THR A 429 ALA A 436 1 8
HELIX 7 7 GLN A 477 SER A 481 5 5
HELIX 8 8 SER A 484 VAL A 489 1 6
SHEET 1 A 6 CYS A 31 SER A 36 0
SHEET 2 A 6 GLY A 304 THR A 312 -1 O GLY A 309 N HIS A 35
SHEET 3 A 6 GLU A 161 LEU A 167 -1 N GLY A 162 O THR A 312
SHEET 4 A 6 VAL A 244 GLY A 251 -1 O ALA A 246 N ALA A 165
SHEET 5 A 6 LYS A 254 ASN A 261 -1 O LYS A 254 N GLY A 251
SHEET 6 A 6 SER A 264 GLY A 273 -1 O TYR A 270 N ILE A 257
SHEET 1 B 5 CYS A 31 SER A 36 0
SHEET 2 B 5 GLY A 304 THR A 312 -1 O GLY A 309 N HIS A 35
SHEET 3 B 5 GLN A 133 MET A 140 -1 N VAL A 138 O PHE A 306
SHEET 4 B 5 ALA A 126 LEU A 130 -1 N VAL A 128 O ALA A 135
SHEET 5 B 5 TYR A 333 VAL A 335 -1 O VAL A 334 N THR A 129
SHEET 1 C 4 THR A 60 ILE A 63 0
SHEET 2 C 4 TYR A 50 ARG A 54 -1 N LEU A 52 O THR A 61
SHEET 3 C 4 CYS A 86 ILE A 91 -1 O ILE A 90 N GLN A 51
SHEET 4 C 4 ALA A 121 SER A 122 -1 O ALA A 121 N ILE A 88
SHEET 1 D10 THR A 60 ILE A 63 0
SHEET 2 D10 TYR A 50 ARG A 54 -1 N LEU A 52 O THR A 61
SHEET 3 D10 CYS A 86 ILE A 91 -1 O ILE A 90 N GLN A 51
SHEET 4 D10 LEU A 101 GLN A 103 -1 O LEU A 101 N ILE A 91
SHEET 5 D10 TYR A 146 ASN A 148 -1 O ARG A 147 N THR A 102
SHEET 6 D10 ALA A 289 LEU A 292 -1 O ILE A 290 N ASN A 148
SHEET 7 D10 ASP A 179 ALA A 183 -1 N ALA A 183 O ALA A 289
SHEET 8 D10 GLU A 196 GLY A 201 -1 O ILE A 198 N TYR A 180
SHEET 9 D10 TRP A 215 ASP A 219 -1 O ASP A 219 N ALA A 197
SHEET 10 D10 LEU A 224 PHE A 225 -1 O PHE A 225 N VAL A 218
SHEET 1 E 4 PHE A 402 SER A 406 0
SHEET 2 E 4 TRP A 390 THR A 394 -1 N THR A 391 O GLU A 405
SHEET 3 E 4 VAL A 349 VAL A 354 -1 N VAL A 350 O TRP A 390
SHEET 4 E 4 PHE A 491 THR A 495 -1 O GLU A 494 N SER A 351
SHEET 1 F 2 ARG A 362 THR A 367 0
SHEET 2 F 2 THR A 370 VAL A 375 -1 O ASN A 372 N ALA A 365
SHEET 1 G 2 SER A 412 TYR A 417 0
SHEET 2 G 2 GLU A 420 ALA A 425 -1 O LEU A 422 N ARG A 415
SHEET 1 H 2 PHE A 438 ALA A 442 0
SHEET 2 H 2 THR A 449 SER A 453 -1 O ARG A 452 N CYS A 439
SHEET 1 I 2 TYR A 460 TYR A 464 0
SHEET 2 I 2 VAL A 467 ALA A 471 -1 O VAL A 467 N TYR A 464
SSBOND 1 CYS A 21 CYS A 31 1555 1555 2.04
SSBOND 2 CYS A 81 CYS A 86 1555 1555 2.03
SSBOND 3 CYS A 176 CYS A 177 1555 1555 2.03
SSBOND 4 CYS A 401 CYS A 439 1555 1555 2.04
LINK ND2 ASN A 202 C1 NAG B 1 1555 1555 1.36
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.47
CISPEP 1 CYS A 176 CYS A 177 0 -1.12
CISPEP 2 GLY A 213 PRO A 214 0 0.40
CISPEP 3 ASN A 282 PRO A 283 0 -0.16
CRYST1 39.461 98.620 144.135 90.00 90.00 90.00 P 21 21 21 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 0.025341 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010140 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006938 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
