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HEADER HYDROLASE 05-MAR-04 1UZA
TITLE CRYSTALLOGRAPHIC STRUCTURE OF A FERULOYL ESTERASE FROM
TITLE 2 ASPERGILLUS NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 SYNONYM: FERULIC ACID ESTERASE A, FAE-III,
COMPND 4 CINNAMOYL ESTERASE;
COMPND 5 CHAIN: A, B;
COMPND 6 EC: 3.1.1.73;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: N-ACETYLGLUCOSAMINE AT ASN 79
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER
KEYWDS HYDROLASE, SERINE ESTERASE, XYLAN DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.MCAULEY,A.SVENDSEN,S.A.PATKAR,K.S.WILSON
REVDAT 1 19-OCT-04 1UZA 0
JRNL AUTH K.E.MCAULEY,A.SVENDSEN,S.A.PATKAR,K.S.WILSON
JRNL TITL STRUCTURE OF A FERULOYL ESTERASE FROM ASPERGILLUS
JRNL TITL 2 NIGER
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 878 2004
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.536
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 64009
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 + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.1562
REMARK 3 FREE R VALUE : 0.1876
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.11
REMARK 3 FREE R VALUE TEST SET COUNT : 3252
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.5392
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4388
REMARK 3 BIN R VALUE (WORKING SET) : 0.168
REMARK 3 BIN FREE R VALUE SET COUNT : 223
REMARK 3 BIN FREE R VALUE : 0.231
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 398
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.530
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.131
REMARK 3 B22 (A**2) : 0.988
REMARK 3 B33 (A**2) : -1.128
REMARK 3 B12 (A**2) : 0.122
REMARK 3 B13 (A**2) : 0.318
REMARK 3 B23 (A**2) : 0.137
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.314
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4175 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3462 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 5711 ; 1.766 ; 1.925
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8100 ; 0.965 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 516 ; 6.035 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;38.612 ;25.640
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 621 ;12.886 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;11.628 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 633 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4749 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 816 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 923 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3527 ; 0.202 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED (A): 2186 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2221 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 301 ; 0.144 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 29 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 84 ; 0.198 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 28 ; 0.194 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3235 ; 1.388 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4174 ; 1.732 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1872 ; 2.915 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1537 ; 3.829 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 28 4
REMARK 3 1 B 1 B 28 4
REMARK 3 2 A 35 A 56 4
REMARK 3 2 B 35 B 56 4
REMARK 3 3 A 60 A 116 4
REMARK 3 3 B 60 B 116 4
REMARK 3 4 A 127 A 222 4
REMARK 3 4 B 127 B 222 4
REMARK 3 5 A 224 A 227 4
REMARK 3 5 B 224 B 227 4
REMARK 3 6 A 233 A 256 4
REMARK 3 6 B 233 B 256 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3169 ; 0.32 ; 0.50
REMARK 3 MEDIUM THERMAL 1 B (A**2): 3169 ; 0.92 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS :1.200
REMARK 3 ION PROBE RADIUS : 0.800
REMARK 3 SHRINKAGE RADIUS : 0.800
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 1UZA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 11-MAR-2004.
REMARK 100 THE EBI ID CODE IS EBI-20007.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH2
REMARK 200 BEAMLINE : ID14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64076
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 25.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 2.1
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.8
REMARK 200 R MERGE FOR SHELL (I) : 0.17
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.50
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 4TGL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULPHATE, 0.1M
REMARK 280 NA ACETATE PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 2 .. 260 A 2 .. 260 0.390
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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
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 BIOMOLECULE: 2
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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN DEGRADATION OF PLANT CELL WALLS. HYDROLYZES
REMARK 400 THE FERULOYL-ARABINOSE ESTER BOND IN ARABINOXYLANS, AND THE
REMARK 400 FERULOYL-GALACTOSE ESTER BOND IN PECTIN. BINDS TO CELLULOSE.
REMARK 400 FERULOYL-POLYSACCHARIDE + H(2)O = FERULATE + POLYSACCHARIDE.
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 ALA A 1
REMARK 465 ALA B 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 261 CA C O CB CG1 CG2
REMARK 470 VAL B 261 CA C O CB CG1 CG2
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 Z
REMARK 525 B Y
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1USW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FERULIC ACID ESTERASE
REMARK 900 FROM ASPERGILLUS NIGER
REMARK 900 RELATED ID: 1UWC RELATED DB: PDB
REMARK 900 FERULOYL ESTERASE FROM ASPERGILLUS NIGER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICT DESCRIBED IN THE SEQADV RECORDS BELOW
REMARK 999 HAVE BEEN DESCRIBED IN UNIPROT ENTRY O42807 BY
REMARK 999 JUGE ET AL 2001. PUBMED ID: 12702357
DBREF 1UZA A 1 261 UNP O42807 FAEA_ASPNG 22 281
DBREF 1UZA B 1 261 UNP O42807 FAEA_ASPNG 22 281
SEQADV 1UZA GLU A 203 UNP O42807 ASP 224 CONFLICT SEE REMARK 999
SEQADV 1UZA GLN A 204 UNP O42807 GLU 225 CONFLICT SEE REMARK 999
SEQADV 1UZA GLU B 203 UNP O42807 ASP 224 CONFLICT SEE REMARK 999
SEQADV 1UZA GLN B 204 UNP O42807 GLU 225 CONFLICT SEE REMARK 999
SEQRES 1 A 261 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 A 261 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 A 261 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 A 261 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 A 261 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 A 261 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 A 261 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 A 261 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 A 261 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 A 261 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 A 261 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 A 261 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 A 261 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 A 261 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 A 261 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 A 261 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 A 261 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 A 261 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 A 261 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 A 261 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
SEQRES 21 A 261 VAL
SEQRES 1 B 261 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 B 261 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 B 261 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 B 261 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 B 261 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 B 261 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 B 261 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 B 261 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 B 261 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 B 261 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 B 261 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 B 261 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 B 261 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 B 261 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 B 261 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 B 261 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 B 261 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 B 261 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 B 261 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 B 261 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
SEQRES 21 B 261 VAL
HET NAG A1261 14
HET NAG B1261 14
HET SO4 A1262 5
HET SO4 B1262 5
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 SO4 2(O4 S1 2-)
FORMUL 4 NAG 2(C8 H15 N1 O6)
FORMUL 5 HOH *398(H2 O1)
HELIX 1 1 SER A 7 ALA A 24 1 18
HELIX 2 2 TYR A 25 ASP A 27 5 3
HELIX 3 3 SER A 70 THR A 78 1 9
HELIX 4 4 GLY A 98 TYR A 122 1 25
HELIX 5 5 SER A 133 ALA A 148 1 16
HELIX 6 6 ASN A 165 PHE A 176 1 12
HELIX 7 7 GLY A 195 LEU A 199 5 5
HELIX 8 8 PRO A 201 GLY A 205 5 5
HELIX 9 9 SER A 220 GLN A 222 5 3
HELIX 10 10 GLN A 233 GLN A 238 1 6
HELIX 11 11 ASN A 244 THR A 248 1 5
HELIX 12 12 SER B 7 ALA B 24 1 18
HELIX 13 13 TYR B 25 ASP B 27 5 3
HELIX 14 14 SER B 70 THR B 78 1 9
HELIX 15 15 GLY B 98 TYR B 122 1 25
HELIX 16 16 SER B 133 ALA B 148 1 16
HELIX 17 17 ASN B 165 PHE B 176 1 12
HELIX 18 18 ILE B 196 LEU B 199 5 4
HELIX 19 19 PRO B 201 GLY B 205 5 5
HELIX 20 20 GLN B 233 GLY B 239 5 7
HELIX 21 21 ASN B 244 THR B 248 1 5
SHEET 1 AA 9 THR A 3 GLN A 4 0
SHEET 2 AA 9 THR A 224 CYS A 227 -1 O VAL A 226 N THR A 3
SHEET 3 AA 9 VAL A 211 SER A 215 -1 O GLU A 212 N CYS A 227
SHEET 4 AA 9 TYR A 186 HIS A 191 1 O TYR A 186 N VAL A 211
SHEET 5 AA 9 VAL A 153 PHE A 158 1 O LEU A 155 N PHE A 187
SHEET 6 AA 9 ALA A 126 HIS A 132 1 O LEU A 127 N ARG A 154
SHEET 7 AA 9 GLU A 60 PHE A 65 1 O ILE A 61 N THR A 128
SHEET 8 AA 9 ILE A 48 ASP A 55 -1 O TRP A 51 N VAL A 64
SHEET 9 AA 9 ILE A 35 ASN A 43 -1 O ILE A 36 N ARG A 54
SHEET 1 AB 2 LEU A 82 PRO A 84 0
SHEET 2 AB 2 GLU A 95 HIS A 97 -1 O VAL A 96 N THR A 83
SHEET 1 AC 2 THR A 249 TYR A 250 0
SHEET 2 AC 2 MET A 253 THR A 254 -1 O MET A 253 N TYR A 250
SHEET 1 BA 9 THR B 3 GLN B 4 0
SHEET 2 BA 9 THR B 224 CYS B 227 -1 O VAL B 226 N THR B 3
SHEET 3 BA 9 VAL B 211 SER B 215 -1 O GLU B 212 N CYS B 227
SHEET 4 BA 9 TYR B 186 HIS B 191 1 O TYR B 186 N VAL B 211
SHEET 5 BA 9 VAL B 153 PHE B 158 1 O LEU B 155 N PHE B 187
SHEET 6 BA 9 ALA B 126 HIS B 132 1 O LEU B 127 N ARG B 154
SHEET 7 BA 9 GLU B 60 PHE B 65 1 O ILE B 61 N THR B 128
SHEET 8 BA 9 ILE B 48 ASP B 55 -1 O TRP B 51 N VAL B 64
SHEET 9 BA 9 ILE B 35 ASN B 43 -1 O ILE B 36 N ARG B 54
SHEET 1 BB 2 LEU B 82 PRO B 84 0
SHEET 2 BB 2 GLU B 95 HIS B 97 -1 O VAL B 96 N THR B 83
SHEET 1 BC 2 THR B 249 TYR B 250 0
SHEET 2 BC 2 MET B 253 THR B 254 -1 O MET B 253 N TYR B 250
SSBOND 1 CYS A 29 CYS A 258 1555 1555
SSBOND 2 CYS A 91 CYS A 94 1555 1555
SSBOND 3 CYS A 227 CYS A 234 1555 1555
SSBOND 4 CYS B 29 CYS B 258 1555 1555
SSBOND 5 CYS B 91 CYS B 94 1555 1555
SSBOND 6 CYS B 227 CYS B 234 1555 1555
LINK ND2 ASN A 79 C1 NAG A1261 1555 1555
LINK ND2 ASN B 79 C1 NAG B1261 1555 1555
CISPEP 1 LEU A 199 PRO A 200 0 -11.74
CISPEP 2 ASP A 217 PRO A 218 0 -8.84
CISPEP 3 LEU B 199 PRO B 200 0 -9.69
CISPEP 4 ASP B 217 PRO B 218 0 -4.26
SITE 1 AC1 12 ASN A 79 THR A 83 GLY A 98 ILE A 102
SITE 2 AC1 12 ASN B 43 ILE B 105 SER B 106 GLN B 108
SITE 3 AC1 12 ASP B 109 GLN B 110 HOH Z 91 HOH Z 212
SITE 1 AC2 13 ASN A 43 ILE A 105 SER A 106 GLN A 108
SITE 2 AC2 13 ASP A 109 GLN A 110 ASN B 79 THR B 83
SITE 3 AC2 13 GLY B 98 TYR B 101 ILE B 102 HOH Y 65
SITE 4 AC2 13 HOH Y 181
SITE 1 AC3 9 ARG A 162 ALA A 207 HIS A 208 HOH Z 171
SITE 2 AC3 9 HOH Z 173 HOH Z 213 HOH Z 214 HOH Z 215
SITE 3 AC3 9 HOH Z 216
SITE 1 AC4 4 SER B 70 ASP B 71 LYS B 116 HOH Y 182
CRYST1 38.298 39.681 77.071 75.24 78.82 71.30 P 1 2
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 0.026111 -0.008839 -0.003401 0.00000
SCALE2 0.000000 0.026606 -0.005639 0.00000
SCALE3 0.000000 0.000000 0.013520 0.00000
MTRIX1 1 0.375560 0.901630 0.214530 20.76293 1
MTRIX2 1 0.900910 -0.409480 0.143820 15.65211 1
MTRIX3 1 0.217520 0.139260 -0.966070 37.79221 1
TER 2016 VAL A 261
TER 4041 VAL B 261
MASTER 298 0 4 21 26 0 11 9 4475 2 52 42
END |