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HEADER LYASE 11-APR-02 1GXS
TITLE CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM SORGHUM
TITLE 2 BICOLOR IN COMPLEX WITH INHIBITOR BENZOIC ACID: A NOVEL
TITLE 3 CYANOGENIC ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 3 SYNONYM: HNL;
COMPND 4 CHAIN: A, C;
COMPND 5 EC: 4.1.2.11;
COMPND 6 OTHER_DETAILS: ISOENZYME II;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 9 SYNONYM: HNL;
COMPND 10 CHAIN: B, D;
COMPND 11 EC: 4.1.2.11;
COMPND 12 OTHER_DETAILS: ISOENZYME II
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SORGHUM BICOLOR;
SOURCE 3 ORGANISM_COMMON: SORGHUM;
SOURCE 4 TISSUE: PRIMARY LEAVES OF SEEDLINGS;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SORGHUM BICOLOR;
SOURCE 7 ORGANISM_COMMON: SORGHUM;
SOURCE 8 TISSUE: PRIMARY LEAVES OF SEEDLINGS
KEYWDS HYDROXYNITRILE LYASE, INHIBITOR COMPLEX, CYANOGENESIS
KEYWDS 2 MECHANISM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LAUBLE,B.MIEHLICH,S.FOERSTER,H.WAJANT,F.EFFENBERGER
REVDAT 1 01-OCT-02 1GXS 0
JRNL AUTH H.LAUBLE,B.MIEHLICH,S.FOERSTER,H.WAJANT,
JRNL AUTH 2 F.EFFENBERGER
JRNL TITL CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM
JRNL TITL 2 SORGHUM BICOLOR IN COMPLEX WITH THE INHIBITOR
JRNL TITL 3 BENZOIC ACID: A NOVEL CYANOGENIC ENZYME
JRNL REF BIOCHEMISTRY V. 41 12043 2002
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.3 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.2
REMARK 3 NUMBER OF REFLECTIONS : 50480
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) : 0.165
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.1
REMARK 3 FREE R VALUE TEST SET COUNT : 5122
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.5
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5693
REMARK 3 BIN R VALUE (WORKING SET) : 0.216
REMARK 3 BIN FREE R VALUE : 0.264
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.3
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 655
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6748
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 3.1
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.1
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.21
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) : 2.61 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.91 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.42 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.32 ; 2.50
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : PARAM19XHOH.PRO
REMARK 3 PARAMETER FILE 2 : PARBEZ.PRO
REMARK 3 PARAMETER FILE 3 : PARDKA.PRO
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPBEZ.PRO
REMARK 3 TOPOLOGY FILE 3 : TOPDKA.PRO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ASYMMETRIC UNIT CONTAINS 2
REMARK 3 ALPHA/BETA-DIMERS
REMARK 4
REMARK 4 1GXS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 12-APR-2002.
REMARK 100 THE EBI ID CODE IS EBI-9691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5.4
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 : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100992
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.3
REMARK 200 RESOLUTION RANGE LOW (A) : 17
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.0
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.7
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 3SC2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NA-CITRATE PH 5.4 USING
REMARK 280 1.6 M AMMONIUM SULFATE
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 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 75.35000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.35000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.85000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC
REMARK 300
REMARK 300 THE BIOLOGICALLY ACTIVE SUBUNIT IS A HETEROTETRAMER FORMED
REMARK 300 BY TWO AB-HETERODIMERS
REMARK 300
REMARK 300 THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 APPEARS
REMARK 300 TO BE A CASE OF STRONG CRYSTAL PACKING WITH
REMARK 300 THE MEAN DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS 5506.4 ANGSTROM**2
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, B, C, 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 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 GLN A 1
REMARK 465 LEU A 2
REMARK 465 GLN A 3
REMARK 465 GLN C 1
REMARK 465 LEU C 2
REMARK 465 GLN C 3
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 U
REMARK 525 B V
REMARK 525 C W
REMARK 525 D X
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES FOR DIMER AB
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES FOR DIMER CD
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ1
REMARK 800 SITE_DESCRIPTION: BEZ BINDING SITE FOR DIMER AB
REMARK 800
REMARK 800 SITE_IDENTIFIER: DK1
REMARK 800 SITE_DESCRIPTION: DKA BINDING SITE FOR DIMER AB
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ2
REMARK 800 SITE_DESCRIPTION: BEZ BINDING SITE FOR DIMER CD
REMARK 800
REMARK 800 SITE_IDENTIFIER: DK2
REMARK 800 SITE_DESCRIPTION: DKA BINDING SITE FOR DIMER CD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 VARIANTS LISTED IN SEQADV RECORDS WERE SUPPLIED BY THE
REMARK 999 AUTHORS OF THE PDB ENTRY, AND WERE NOT OBTAINED FROM THE
REMARK 999 SWISS-PROT ENTRY
DBREF 1GXS A 1 270 SWS Q8W4X3 Q8W4X3 56 325
DBREF 1GXS B 283 440 SWS Q8W4X3 Q8W4X3 338 495
DBREF 1GXS C 1 270 SWS Q8W4X3 Q8W4X3 56 325
DBREF 1GXS D 283 440 SWS Q8W4X3 Q8W4X3 338 495
SEQADV 1GXS LEU A 11 SWS Q8W4X3 PRO 66 VARIANT
SEQADV 1GXS ALA A 79 SWS Q8W4X3 PRO 134 VARIANT
SEQADV 1GXS GLY A 112 SWS Q8W4X3 VAL 167 VARIANT
SEQADV 1GXS SER A 203 SWS Q8W4X3 LEU 258 VARIANT
SEQADV 1GXS LEU C 11 SWS Q8W4X3 PRO 66 VARIANT
SEQADV 1GXS ALA C 79 SWS Q8W4X3 PRO 134 VARIANT
SEQADV 1GXS GLY C 112 SWS Q8W4X3 VAL 167 VARIANT
SEQADV 1GXS SER C 203 SWS Q8W4X3 LEU 258 VARIANT
SEQADV 1GXS THR B 408 SWS Q8W4X3 SER 463 VARIANT
SEQADV 1GXS VAL B 409 SWS Q8W4X3 PRO 464 VARIANT
SEQADV 1GXS ARG B 410 SWS Q8W4X3 SER 465 VARIANT
SEQADV 1GXS THR D 408 SWS Q8W4X3 SER 463 VARIANT
SEQADV 1GXS VAL D 409 SWS Q8W4X3 PRO 464 VARIANT
SEQADV 1GXS ARG D 410 SWS Q8W4X3 SER 465 VARIANT
SEQRES 1 A 270 GLN LEU GLN GLN GLN GLU ASP ASP ARG ILE LEU GLY LEU
SEQRES 2 A 270 PRO GLY GLN PRO ASN GLY VAL ALA PHE GLY MET TYR GLY
SEQRES 3 A 270 GLY TYR VAL THR ILE ASP ASP ASN ASN GLY ARG ALA LEU
SEQRES 4 A 270 TYR TYR TRP PHE GLN GLU ALA ASP THR ALA ASP PRO ALA
SEQRES 5 A 270 ALA ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY
SEQRES 6 A 270 CYS SER SER ILE GLY LEU GLY ALA MET GLN GLU LEU GLY
SEQRES 7 A 270 ALA PHE ARG VAL HIS THR ASN GLY GLU SER LEU LEU LEU
SEQRES 8 A 270 ASN GLU TYR ALA TRP ASN LYS ALA ALA ASN ILE LEU PHE
SEQRES 9 A 270 ALA GLU SER PRO ALA GLY VAL GLY PHE SER TYR SER ASN
SEQRES 10 A 270 THR SER SER ASP LEU SER MET GLY ASP ASP LYS MET ALA
SEQRES 11 A 270 GLN ASP THR TYR THR PHE LEU VAL LYS TRP PHE GLU ARG
SEQRES 12 A 270 PHE PRO HIS TYR ASN TYR ARG GLU PHE TYR ILE ALA GLY
SEQRES 13 A 270 GLU SER GLY HIS PHE ILE PRO GLN LEU SER GLN VAL VAL
SEQRES 14 A 270 TYR ARG ASN ARG ASN ASN SER PRO PHE ILE ASN PHE GLN
SEQRES 15 A 270 GLY LEU LEU VAL SER SER GLY LEU THR ASN ASP HIS GLU
SEQRES 16 A 270 ASP MET ILE GLY MET PHE GLU SER TRP TRP HIS HIS GLY
SEQRES 17 A 270 LEU ILE SER ASP GLU THR ARG ASP SER GLY LEU LYS VAL
SEQRES 18 A 270 CYS PRO GLY THR SER PHE MET HIS PRO THR PRO GLU CYS
SEQRES 19 A 270 THR GLU VAL TRP ASN LYS ALA LEU ALA GLU GLN GLY ASN
SEQRES 20 A 270 ILE ASN PRO TYR THR ILE TYR THR PRO THR CYS ASP ARG
SEQRES 21 A 270 GLU PRO SER PRO TYR GLN ARG ARG PHE TRP
SEQRES 1 B 158 LEU PRO PRO TYR ASP PRO CYS ALA VAL PHE ASN SER ILE
SEQRES 2 B 158 ASN TYR LEU ASN LEU PRO GLU VAL GLN THR ALA LEU HIS
SEQRES 3 B 158 ALA ASN VAL SER GLY ILE VAL GLU TYR PRO TRP THR VAL
SEQRES 4 B 158 CYS SER ASN THR ILE PHE ASP GLN TRP GLY GLN ALA ALA
SEQRES 5 B 158 ASP ASP LEU LEU PRO VAL TYR ARG GLU LEU ILE GLN ALA
SEQRES 6 B 158 GLY LEU ARG VAL TRP VAL TYR SER GLY ASP THR ASP SER
SEQRES 7 B 158 VAL VAL PRO VAL SER SER THR ARG ARG SER LEU ALA ALA
SEQRES 8 B 158 LEU GLU LEU PRO VAL LYS THR SER TRP TYR PRO TRP TYR
SEQRES 9 B 158 MET ALA PRO THR GLU ARG GLU VAL GLY GLY TRP SER VAL
SEQRES 10 B 158 GLN TYR GLU GLY LEU THR TYR VAL THR VAL ARG GLY ALA
SEQRES 11 B 158 GLY HIS LEU VAL PRO VAL HIS ARG PRO ALA GLN ALA PHE
SEQRES 12 B 158 LEU LEU PHE LYS GLN PHE LEU LYS GLY GLU PRO MET PRO
SEQRES 13 B 158 ALA GLU
SEQRES 1 C 270 GLN LEU GLN GLN GLN GLU ASP ASP ARG ILE LEU GLY LEU
SEQRES 2 C 270 PRO GLY GLN PRO ASN GLY VAL ALA PHE GLY MET TYR GLY
SEQRES 3 C 270 GLY TYR VAL THR ILE ASP ASP ASN ASN GLY ARG ALA LEU
SEQRES 4 C 270 TYR TYR TRP PHE GLN GLU ALA ASP THR ALA ASP PRO ALA
SEQRES 5 C 270 ALA ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY
SEQRES 6 C 270 CYS SER SER ILE GLY LEU GLY ALA MET GLN GLU LEU GLY
SEQRES 7 C 270 ALA PHE ARG VAL HIS THR ASN GLY GLU SER LEU LEU LEU
SEQRES 8 C 270 ASN GLU TYR ALA TRP ASN LYS ALA ALA ASN ILE LEU PHE
SEQRES 9 C 270 ALA GLU SER PRO ALA GLY VAL GLY PHE SER TYR SER ASN
SEQRES 10 C 270 THR SER SER ASP LEU SER MET GLY ASP ASP LYS MET ALA
SEQRES 11 C 270 GLN ASP THR TYR THR PHE LEU VAL LYS TRP PHE GLU ARG
SEQRES 12 C 270 PHE PRO HIS TYR ASN TYR ARG GLU PHE TYR ILE ALA GLY
SEQRES 13 C 270 GLU SER GLY HIS PHE ILE PRO GLN LEU SER GLN VAL VAL
SEQRES 14 C 270 TYR ARG ASN ARG ASN ASN SER PRO PHE ILE ASN PHE GLN
SEQRES 15 C 270 GLY LEU LEU VAL SER SER GLY LEU THR ASN ASP HIS GLU
SEQRES 16 C 270 ASP MET ILE GLY MET PHE GLU SER TRP TRP HIS HIS GLY
SEQRES 17 C 270 LEU ILE SER ASP GLU THR ARG ASP SER GLY LEU LYS VAL
SEQRES 18 C 270 CYS PRO GLY THR SER PHE MET HIS PRO THR PRO GLU CYS
SEQRES 19 C 270 THR GLU VAL TRP ASN LYS ALA LEU ALA GLU GLN GLY ASN
SEQRES 20 C 270 ILE ASN PRO TYR THR ILE TYR THR PRO THR CYS ASP ARG
SEQRES 21 C 270 GLU PRO SER PRO TYR GLN ARG ARG PHE TRP
SEQRES 1 D 158 LEU PRO PRO TYR ASP PRO CYS ALA VAL PHE ASN SER ILE
SEQRES 2 D 158 ASN TYR LEU ASN LEU PRO GLU VAL GLN THR ALA LEU HIS
SEQRES 3 D 158 ALA ASN VAL SER GLY ILE VAL GLU TYR PRO TRP THR VAL
SEQRES 4 D 158 CYS SER ASN THR ILE PHE ASP GLN TRP GLY GLN ALA ALA
SEQRES 5 D 158 ASP ASP LEU LEU PRO VAL TYR ARG GLU LEU ILE GLN ALA
SEQRES 6 D 158 GLY LEU ARG VAL TRP VAL TYR SER GLY ASP THR ASP SER
SEQRES 7 D 158 VAL VAL PRO VAL SER SER THR ARG ARG SER LEU ALA ALA
SEQRES 8 D 158 LEU GLU LEU PRO VAL LYS THR SER TRP TYR PRO TRP TYR
SEQRES 9 D 158 MET ALA PRO THR GLU ARG GLU VAL GLY GLY TRP SER VAL
SEQRES 10 D 158 GLN TYR GLU GLY LEU THR TYR VAL THR VAL ARG GLY ALA
SEQRES 11 D 158 GLY HIS LEU VAL PRO VAL HIS ARG PRO ALA GLN ALA PHE
SEQRES 12 D 158 LEU LEU PHE LYS GLN PHE LEU LYS GLY GLU PRO MET PRO
SEQRES 13 D 158 ALA GLU
MODRES 1GXS ASN A 117 ASN GLYCOSYLATION SITE
MODRES 1GXS ASN B 310 ASN GLYCOSYLATION SITE
MODRES 1GXS ASN C 117 ASN GLYCOSYLATION SITE
MODRES 1GXS ASN D 310 ASN GLYCOSYLATION SITE
HET BEZ A 601 9
HET DKA A 701 12
HET NAG A1117 14
HET NAG A1118 14
HET FUC A1119 10
HET NAG B1310 14
HET BEZ C 602 9
HET DKA C 702 12
HET NAG C1117 14
HET NAG C1118 14
HET FUC C1119 10
HET NAG D1310 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
HETNAM FUC FUCOSE
HETNAM BEZ BENZOIC ACID
HETNAM DKA DECANOIC ACID
FORMUL 5 NAG 6(C8 H15 N1 O6)
FORMUL 6 FUC 2(C6 H12 O5)
FORMUL 7 BEZ 2(C7 H6 O2)
FORMUL 8 DKA 2(C10 H20 O2)
FORMUL 9 HOH *331(H2 O1)
HELIX 1 1 GLN A 4 ARG A 9 1 6
HELIX 2 2 ASP A 50 ALA A 54 5 5
HELIX 3 3 SER A 68 GLY A 78 5 11
HELIX 4 4 ALA A 95 ALA A 99 5 5
HELIX 5 5 THR A 118 SER A 123 5 6
HELIX 6 6 GLY A 125 PHE A 144 1 20
HELIX 7 7 PRO A 145 ASN A 148 5 4
HELIX 8 8 HIS A 160 ASN A 172 1 13
HELIX 9 9 ASN A 192 HIS A 207 1 16
HELIX 10 10 SER A 211 CYS A 222 1 12
HELIX 11 11 THR A 231 GLN A 245 1 15
HELIX 12 12 ALA B 290 ASN B 299 1 10
HELIX 13 13 LEU B 300 HIS B 308 1 9
HELIX 14 14 ASN B 310 ILE B 314 5 5
HELIX 15 15 SER B 323 GLN B 329 1 7
HELIX 16 16 LEU B 337 ALA B 347 1 11
HELIX 17 17 PRO B 363 ALA B 373 1 11
HELIX 18 18 LEU B 415 ARG B 420 1 6
HELIX 19 19 ARG B 420 GLY B 434 1 15
HELIX 20 20 GLN C 4 ASP C 8 5 5
HELIX 21 21 ASP C 50 ALA C 54 5 5
HELIX 22 22 SER C 68 LEU C 77 3 10
HELIX 23 23 ALA C 95 ALA C 99 5 5
HELIX 24 24 THR C 118 SER C 123 5 6
HELIX 25 25 GLY C 125 PHE C 144 1 20
HELIX 26 26 PRO C 145 ASN C 148 5 4
HELIX 27 27 HIS C 160 ASN C 172 1 13
HELIX 28 28 ASN C 192 HIS C 207 1 16
HELIX 29 29 SER C 211 CYS C 222 1 12
HELIX 30 30 THR C 231 GLN C 245 1 15
HELIX 31 31 ALA D 290 ASN D 299 1 10
HELIX 32 32 LEU D 300 HIS D 308 1 9
HELIX 33 33 ASN D 310 ILE D 314 5 5
HELIX 34 34 SER D 323 GLN D 329 1 7
HELIX 35 35 LEU D 337 ALA D 347 1 11
HELIX 36 36 PRO D 363 ALA D 373 1 11
HELIX 37 37 LEU D 415 ARG D 420 1 6
HELIX 38 38 ARG D 420 GLY D 434 1 15
SHEET 1 AA 3 MET A 24 ASP A 32 0
SHEET 2 AA 3 ARG A 37 GLN A 44 -1 O ARG A 37 N ILE A 31
SHEET 3 AA 3 TYR A 115 SER A 116 -1 O TYR A 115 N ALA A 38
SHEET 1 AB10 MET A 24 ASP A 32 0
SHEET 2 AB10 ARG A 37 GLN A 44 -1 O ARG A 37 N ILE A 31
SHEET 3 AB10 ASN A 101 ALA A 105 -1 O ILE A 102 N GLN A 44
SHEET 4 AB10 LEU A 56 ASN A 61 1 O VAL A 57 N LEU A 103
SHEET 5 AB10 GLU A 151 GLU A 157 1 O GLU A 151 N LEU A 56
SHEET 6 AB10 ASN A 180 SER A 187 1 O ASN A 180 N PHE A 152
SHEET 7 AB10 ARG B 350 GLY B 356 1 O ARG B 350 N LEU A 184
SHEET 8 AB10 LEU B 404 VAL B 409 1 O THR B 405 N VAL B 353
SHEET 9 AB10 VAL B 394 TYR B 401 -1 O TRP B 397 N THR B 408
SHEET 10 AB10 VAL B 378 TYR B 386 -1 N LYS B 379 O GLN B 400
SHEET 1 AC 2 PHE A 80 VAL A 82 0
SHEET 2 AC 2 LEU A 89 LEU A 91 -1 O LEU A 90 N ARG A 81
SHEET 1 CA 3 MET C 24 ASP C 32 0
SHEET 2 CA 3 ARG C 37 GLN C 44 -1 O ARG C 37 N ILE C 31
SHEET 3 CA 3 TYR C 115 SER C 116 -1 O TYR C 115 N ALA C 38
SHEET 1 CB10 MET C 24 ASP C 32 0
SHEET 2 CB10 ARG C 37 GLN C 44 -1 O ARG C 37 N ILE C 31
SHEET 3 CB10 ASN C 101 ALA C 105 -1 O ILE C 102 N GLN C 44
SHEET 4 CB10 LEU C 56 LEU C 60 1 O VAL C 57 N LEU C 103
SHEET 5 CB10 GLU C 151 GLY C 156 1 O GLU C 151 N LEU C 56
SHEET 6 CB10 ASN C 180 SER C 187 1 O ASN C 180 N PHE C 152
SHEET 7 CB10 ARG D 350 GLY D 356 1 O ARG D 350 N LEU C 184
SHEET 8 CB10 THR D 405 VAL D 409 1 O THR D 405 N VAL D 353
SHEET 9 CB10 GLY D 396 TYR D 401 -1 O TRP D 397 N THR D 408
SHEET 10 CB10 VAL D 378 TRP D 385 -1 N LYS D 379 O GLN D 400
SHEET 1 CC 2 PHE C 80 VAL C 82 0
SHEET 2 CC 2 LEU C 89 LEU C 91 -1 O LEU C 90 N ARG C 81
SSBOND 1 CYS A 66 CYS B 322 1555 1555
SSBOND 2 CYS A 222 CYS A 234 1555 1555
SSBOND 3 CYS A 258 CYS B 289 1555 1555
SSBOND 4 CYS C 66 CYS D 322 1555 1555
SSBOND 5 CYS C 222 CYS C 234 1555 1555
SSBOND 6 CYS C 258 CYS D 289 1555 1555
LINK ND2 ASN A 117 C1 NAG A1117 1555 1555
LINK O3 NAG A1117 C1 FUC A1119 1555 1555
LINK O4 NAG A1117 C1 NAG A1118 1555 1555
LINK ND2 ASN B 310 C1 NAG B1310 1555 1555
LINK ND2 ASN C 117 C1 NAG C1117 1555 1555
LINK O4 NAG C1117 C1 NAG C1118 1555 1555
LINK O3 NAG C1117 C1 FUC C1119 1555 1555
LINK ND2 ASN D 310 C1 NAG D1310 1555 1555
CISPEP 1 GLY A 63 PRO A 64 0 -16.06
CISPEP 2 SER A 107 PRO A 108 0 -1.81
CISPEP 3 GLY C 63 PRO C 64 0 -6.70
CISPEP 4 SER C 107 PRO C 108 0 1.71
SITE 1 CA1 2 SER A 158 TRP A 270
SITE 1 CA2 2 SER C 158 TRP C 270
SITE 1 BZ1 8 GLY A 62 GLY A 63 PRO A 64 ASP A 126
SITE 2 BZ1 8 SER A 158 HIS A 160 PHE A 161 HOH U 40
SITE 1 DK1 8 ASN A 61 GLY A 62 GLU A 157 ASN A 249
SITE 2 DK1 8 TYR A 251 TRP A 270 HIS B 414 LEU B 415
SITE 1 BZ2 8 GLY C 62 GLY C 63 PRO C 64 ASP C 126
SITE 2 BZ2 8 SER C 158 HIS C 160 PHE C 161 HOH W 47
SITE 1 DK2 8 ASN C 61 GLY C 62 GLU C 157 ASN C 249
SITE 2 DK2 8 TYR C 251 TRP C 270 HIS D 414 LEU D 415
CRYST1 150.700 103.700 90.600 90.00 101.30 90.00 C 1 2 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 0.006636 0.000000 0.001326 0.00000
SCALE2 0.000000 0.009643 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011256 0.00000
END |