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HEADER HYDROLASE 06-JUL-06 2HL6
TITLE STRUCTURE OF HOMOLOGOUSLY EXPRESSED FERRULATE ESTERASE OF
TITLE 2 ASPERGILLUS NIGER IN COMPLEX WITH CAPS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERULIC ACID ESTERASE A, FAE-III, CINNAMOYL
COMPND 5 ESTERASE, FERRULATE ESTERASE A;
COMPND 6 EC: 3.1.1.73;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_COMMON: FUNGI;
SOURCE 4 GENE: FAEA;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FUNGI;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAN52.3
KEYWDS ESTERASE, A/B HYDROLASE FOLD, GLYCOSYLATED, CAPS
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PARSIEGLA,I.HERPOEL-GIMBERT,J.DUBOTS
REVDAT 1 31-OCT-06 2HL6 0
JRNL AUTH I.BENOIT,M.ASTHER,G.SULZENBACHER,E.RECORD,
JRNL AUTH 2 L.MARMUSE,G.PARSIEGLA,I.HERPOEL-GIMBERT,M.ASTHER,
JRNL AUTH 3 C.BIGNON
JRNL TITL RESPECTIVE IMPORTANCE OF PROTEIN FOLDING AND
JRNL TITL 2 GLYCOSYLATION IN THE THERMAL STABILITY OF
JRNL TITL 3 RECOMBINANT FERULOYL ESTERASE A
JRNL REF FEBS LETT. V. 580 5815 2006
JRNL REFN ASTM FEBLAL NE ISSN 0014-5793
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 81358
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4079
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5264
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4856
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -0.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.433
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4345 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2739 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5947 ; 1.427 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6692 ; 0.934 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.070 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;36.393 ;25.610
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 616 ;11.601 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ; 9.659 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 669 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4850 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 830 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 937 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3022 ; 0.198 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2242 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2077 ; 0.091 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 450 ; 0.138 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.076 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.266 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.151 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3366 ; 1.092 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1068 ; 0.223 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4241 ; 1.316 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2010 ; 2.364 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1696 ; 3.425 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 260
REMARK 3 RESIDUE RANGE : B 1 B 260
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7851 8.9399 33.8177
REMARK 3 T TENSOR
REMARK 3 T11: -0.0162 T22: -0.0109
REMARK 3 T33: -0.0027 T12: -0.0013
REMARK 3 T13: 0.0057 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0692 L22: 0.0691
REMARK 3 L33: 0.2855 L12: -0.0006
REMARK 3 L13: 0.0714 L23: 0.0848
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.0096 S13: -0.0042
REMARK 3 S21: -0.0030 S22: 0.0037 S23: -0.0085
REMARK 3 S31: -0.0036 S32: 0.0381 S33: -0.0134
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2HL6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 10.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : SYNCHROTRON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81359
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 39.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 48.1
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 46.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.34700
REMARK 200 R SYM FOR SHELL (I) : 0.34700
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3TGL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.05M AMMONIUMSULFATE, 0.09M CAPS,
REMARK 280 10% ETHYLENEGLYCOL , PH 10.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
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 72.76000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.76000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 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 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, X
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, Y
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 O42807(UNP) SHOWS THE CONFLICTS(DE -> EQ)
REMARK 999 REF 2[NUCLEOTIDE SEQUENCE. JUGE N. ET AL.]
REMARK 999 "HIGH-LEVEL PRODUCTION OF RECOMBINANT
REMARK 999 ASPERGILLUS NIGER CINNAMOYL ESTERASE (FAEA)
REMARK 999 IN THE METHYLOTROPHIC YEAST PICHIA PASTORIS"
REMARK 999 THE DEPOSITORS SAY THE SEQUENCE INCERTAINITY
REMARK 999 HAS BEEN VERIFIED BY SEQUENCING THE GENE AND
REMARK 999 INSPECTION OF THE DENSITY.
DBREF 2HL6 A 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 2HL6 B 1 260 UNP O42807 FAEA_ASPNG 22 281
SEQADV 2HL6 GLU A 203 UNP O42807 ASP 224 SEE REMARK 999
SEQADV 2HL6 GLN A 204 UNP O42807 GLU 225 SEE REMARK 999
SEQADV 2HL6 GLU B 203 UNP O42807 ASP 224 SEE REMARK 999
SEQADV 2HL6 GLN B 204 UNP O42807 GLU 225 SEE REMARK 999
SEQRES 1 A 260 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 A 260 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 A 260 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 A 260 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 A 260 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 A 260 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 A 260 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 A 260 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 A 260 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 A 260 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 A 260 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 A 260 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 A 260 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 A 260 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 A 260 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 A 260 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 A 260 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 A 260 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 A 260 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 A 260 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
SEQRES 1 B 260 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 B 260 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 B 260 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 B 260 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 B 260 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 B 260 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 B 260 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 B 260 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 B 260 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 B 260 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 B 260 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 B 260 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 B 260 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 B 260 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 B 260 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 B 260 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 B 260 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 B 260 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 B 260 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 B 260 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
MODRES 2HL6 ASN A 79 ASN GLYCOSYLATION SITE
MODRES 2HL6 ASN B 79 ASN GLYCOSYLATION SITE
HET NAG X 300 14
HET NAG X 301 14
HET MAN X 302 11
HET MAN X 303 11
HET MAN X 304 11
HET NAG Y 310 14
HET NAG Y 311 14
HET MAN Y 312 11
HET SO4 270 5
HET SO4 271 5
HET SO4 272 5
HET SO4 273 5
HET EDO 290 4
HET EDO 291 4
HET EDO 292 4
HET EDO 293 4
HET EDO 294 4
HET EDO 295 4
HET EDO 296 4
HET EDO 297 4
HET CXS 280 14
HET CXS 281 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
HETSYN NAG NAG
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 4(C8 H15 N1 O6)
FORMUL 3 MAN 4(C6 H12 O6)
FORMUL 5 SO4 4(O4 S1 2-)
FORMUL 9 EDO 8(C2 H6 O2)
FORMUL 17 CXS 2(C9 H19 N1 O3 S1)
FORMUL 19 HOH *617(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 GLN A 166 PHE A 176 1 11
HELIX 7 7 GLY A 195 LEU A 199 5 5
HELIX 8 8 PRO A 201 GLN A 204 5 4
HELIX 9 9 GLN A 233 GLN A 238 5 6
HELIX 10 10 ASN A 244 THR A 248 1 5
HELIX 11 11 SER B 7 ALA B 24 1 18
HELIX 12 12 TYR B 25 ASP B 27 5 3
HELIX 13 13 SER B 70 THR B 78 1 9
HELIX 14 14 GLY B 98 TYR B 122 1 25
HELIX 15 15 SER B 133 ALA B 148 1 16
HELIX 16 16 ASN B 165 PHE B 176 1 12
HELIX 17 17 GLY B 195 LEU B 199 5 5
HELIX 18 18 PRO B 201 GLY B 205 5 5
HELIX 19 19 SER B 220 GLN B 222 5 3
HELIX 20 20 GLN B 233 GLN B 238 1 6
HELIX 21 21 ASN B 244 THR B 248 1 5
SHEET 1 A 9 SER A 2 GLN A 4 0
SHEET 2 A 9 THR A 224 CYS A 227 -1 O VAL A 226 N THR A 3
SHEET 3 A 9 VAL A 211 SER A 215 -1 N GLU A 212 O CYS A 227
SHEET 4 A 9 TYR A 186 HIS A 191 1 N ARG A 188 O VAL A 211
SHEET 5 A 9 VAL A 153 PHE A 158 1 N LEU A 155 O PHE A 187
SHEET 6 A 9 ALA A 126 HIS A 132 1 N LEU A 127 O ARG A 154
SHEET 7 A 9 GLU A 60 PHE A 65 1 N ILE A 61 O ALA A 126
SHEET 8 A 9 ILE A 48 ASP A 55 -1 N ASP A 55 O GLU A 60
SHEET 9 A 9 ILE A 35 ASN A 43 -1 N ILE A 36 O ARG A 54
SHEET 1 B 2 LEU A 82 PRO A 84 0
SHEET 2 B 2 GLU A 95 HIS A 97 -1 O VAL A 96 N THR A 83
SHEET 1 C 2 GLY A 164 ASN A 165 0
SHEET 2 C 2 TYR A 206 ALA A 207 -1 O ALA A 207 N GLY A 164
SHEET 1 D 2 THR A 249 TYR A 250 0
SHEET 2 D 2 MET A 253 THR A 254 -1 O MET A 253 N TYR A 250
SHEET 1 E 9 SER B 2 GLN B 4 0
SHEET 2 E 9 THR B 224 CYS B 227 -1 O VAL B 226 N THR B 3
SHEET 3 E 9 VAL B 211 SER B 215 -1 N GLU B 212 O CYS B 227
SHEET 4 E 9 TYR B 186 HIS B 191 1 N THR B 190 O SER B 215
SHEET 5 E 9 VAL B 153 PHE B 158 1 N LEU B 155 O PHE B 187
SHEET 6 E 9 ALA B 126 HIS B 132 1 N VAL B 129 O TYR B 156
SHEET 7 E 9 GLU B 60 PHE B 65 1 N ILE B 61 O ALA B 126
SHEET 8 E 9 ILE B 48 ASP B 55 -1 N TRP B 51 O VAL B 64
SHEET 9 E 9 ILE B 35 ASN B 43 -1 N ILE B 36 O ARG B 54
SHEET 1 F 2 LEU B 82 PRO B 84 0
SHEET 2 F 2 GLU B 95 HIS B 97 -1 O VAL B 96 N THR B 83
SHEET 1 G 2 THR B 249 TYR B 250 0
SHEET 2 G 2 MET B 253 THR B 254 -1 O MET B 253 N TYR B 250
SSBOND 1 CYS A 29 CYS A 258
SSBOND 2 CYS A 91 CYS A 94
SSBOND 3 CYS A 227 CYS A 234
SSBOND 4 CYS B 29 CYS B 258
SSBOND 5 CYS B 91 CYS B 94
SSBOND 6 CYS B 227 CYS B 234
LINK ND2 ASN A 79 C1 NAG X 300
LINK ND2 ASN B 79 C1 NAG Y 310
LINK O4 NAG X 300 C1 NAG X 301
LINK O4 NAG X 301 C1 MAN X 302
LINK O3 MAN X 302 C1 MAN X 303
LINK O2 MAN X 303 C1 MAN X 304
LINK O4 NAG Y 310 C1 NAG Y 311
LINK O4 NAG Y 311 C1 MAN Y 312
CISPEP 1 LEU A 199 PRO A 200 0 -14.06
CISPEP 2 ASP A 217 PRO A 218 0 -6.34
CISPEP 3 LEU B 199 PRO B 200 0 -12.13
CISPEP 4 ASP B 217 PRO B 218 0 -3.05
CRYST1 145.520 51.700 99.588 90.00 127.98 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 0.006872 0.000000 0.005365 0.00000
SCALE2 0.000000 0.019342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012739 0.00000
TER 2011 TRP A 260
TER 4061 TRP B 260
MASTER 259 0 22 21 28 0 0 6 4856 2 194 40
END |