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HEADER HYDROLASE 25-NOV-13 3WMT
TITLE CRYSTAL STRUCTURE OF FERULOYL ESTERASE B FROM ASPERGILLUS ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE FERULOYL ESTERASE B-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERULIC ACID ESTERASE B-1, FAEB-1;
COMPND 5 EC: 3.1.1.73;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_COMMON: YELLOW KOJI MOLD;
SOURCE 4 ORGANISM_TAXID: 510516;
SOURCE 5 STRAIN: RIB 40;
SOURCE 6 GENE: AO090001000066, AOFAEB, FAEB-1;
SOURCE 7 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS ALPHA/BETA-HYDROLASE FOLD, HYDROLASE, GLYCOSYLATION, EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SUZUKI,T.ISHIDA,K.IGARASHI,T.KOSEKI,S.FUSHINOBU
REVDAT 1 06-AUG-14 3WMT 0
JRNL AUTH K.SUZUKI,A.HORI,K.KAWAMOTO,R.R.THANGUDU,T.ISHIDA,K.IGARASHI,
JRNL AUTH 2 M.SAMEJIMA,T.WAKAGI,T.KOSEKI,S.FUSHINOBU
JRNL TITL CRYSTAL STRUCTURE OF A FERULOYL ESTERASE BELONGING TO THE
JRNL TITL 2 TANNASE FAMILY: A DISULFIDE BOND NEAR A CATALYTIC TRIAD
JRNL REF PROTEINS 2014
JRNL REFN ESSN 1097-0134
JRNL DOI 10.1002/PROT.24649
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.KOSEKI,A.HORI,S.SEKI,T.MURAYAMA,Y.SHIONO
REMARK 1 TITL CHARACTERIZATION OF TWO DISTINCT FERULOYL ESTERASES, AOFAEB
REMARK 1 TITL 2 AND AOFAEC, FROM ASPERGILLUS ORYZAE.
REMARK 1 REF APPL.MICROBIOL.BIOTECHNOL. V. 83 689 2009
REMARK 1 REFN ISSN 0175-7598
REMARK 1 PMID 19242690
REMARK 1 DOI 10.1007/S00253-009-1913-Z
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 147572
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) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7815
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.1530
REMARK 3 BIN FREE R VALUE SET COUNT : 556
REMARK 3 BIN FREE R VALUE : 0.1910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7688
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 1087
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8025 ; 0.026 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7087 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10938 ; 2.339 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16233 ; 1.044 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 997 ; 6.732 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;32.844 ;24.560
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1140 ;11.998 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1170 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9373 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1967 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3WMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB096532.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL
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 : 155503
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 FOR THE DATA SET : 46.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22900
REMARK 200 FOR SHELL : 7.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 43.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 1000, 0.1M TRIS-HCL (PH 7.0),
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 -X+1/2,Y+1/2,-Z
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 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 46.97700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.46850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.97700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.46850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B1093 LIES ON A SPECIAL POSITION.
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 19
REMARK 465 ALA A 20
REMARK 465 ILE A 21
REMARK 465 ASP A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 SER A 25
REMARK 465 SER A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 GLY A 29
REMARK 465 SER A 30
REMARK 465 ASP A 31
REMARK 465 HIS A 32
REMARK 465 HIS A 33
REMARK 465 GLY A 34
REMARK 465 SER A 35
REMARK 465 GLU A 80
REMARK 465 ASP A 81
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 ILE B 21
REMARK 465 ASP B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 SER B 25
REMARK 465 SER B 26
REMARK 465 SER B 27
REMARK 465 ASN B 28
REMARK 465 GLY B 29
REMARK 465 SER B 30
REMARK 465 ASP B 31
REMARK 465 HIS B 32
REMARK 465 HIS B 33
REMARK 465 GLY B 34
REMARK 465 SER B 35
REMARK 465 ILE B 75
REMARK 465 CYS B 76
REMARK 465 GLY B 77
REMARK 465 GLY B 78
REMARK 465 ASP B 79
REMARK 465 GLU B 80
REMARK 465 ASP B 81
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 210 CG TRP A 210 CD1 0.153
REMARK 500 GLU A 423 CD GLU A 423 OE2 -0.108
REMARK 500 GLU A 493 CG GLU A 493 CD -0.094
REMARK 500 ARG A 522 CD ARG A 522 NE -0.118
REMARK 500 GLU A 534 CD GLU A 534 OE2 -0.108
REMARK 500 GLU A 538 CD GLU A 538 OE1 0.071
REMARK 500 GLU B 165 CD GLU B 165 OE2 0.069
REMARK 500 SER B 237 CB SER B 237 OG 0.092
REMARK 500 GLU B 423 CD GLU B 423 OE2 -0.108
REMARK 500 GLU B 442 CD GLU B 442 OE2 0.098
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ASP A 133 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 133 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 207 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TRP A 210 CG - CD1 - NE1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 PHE A 230 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 248 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 248 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 275 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LYS A 315 CD - CE - NZ ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU A 332 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 LEU A 332 CB - CG - CD2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 335 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 388 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 448 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 498 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 513 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 513 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 522 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 522 NE - CZ - NH2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG A 524 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLU B 107 OE1 - CD - OE2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 117 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 133 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 GLU B 165 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU B 175 CB - CG - CD2 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG B 207 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU B 257 OE1 - CD - OE2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP B 272 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 275 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TYR B 325 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TYR B 325 OH - CZ - CE2 ANGL. DEV. = -16.9 DEGREES
REMARK 500 ARG B 335 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 GLU B 442 OE1 - CD - OE2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG B 448 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 498 CB - CG - OD1 ANGL. DEV. = -14.4 DEGREES
REMARK 500 ASP B 498 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 PHE B 499 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 LYS B 504 CD - CE - NZ ANGL. DEV. = -15.7 DEGREES
REMARK 500 TYR B 512 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 513 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 513 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 522 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
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 99 -176.96 -170.07
REMARK 500 LYS A 101 24.06 -146.99
REMARK 500 TYR A 172 -33.96 -163.78
REMARK 500 ASN A 195 -83.24 -108.85
REMARK 500 SER A 203 -123.83 73.73
REMARK 500 ALA A 227 65.48 29.66
REMARK 500 ALA A 229 33.26 -82.07
REMARK 500 TYR A 348 -32.48 -132.23
REMARK 500 ASP A 388 69.60 31.02
REMARK 500 PHE A 446 -14.88 -142.67
REMARK 500 ALA A 456 -158.73 -85.31
REMARK 500 ALA A 461 -128.88 -115.29
REMARK 500 ALA A 475 38.15 -148.21
REMARK 500 TYR B 172 -37.59 -166.52
REMARK 500 ASN B 195 -79.26 -101.32
REMARK 500 SER B 203 -123.39 75.21
REMARK 500 ALA B 227 62.85 32.45
REMARK 500 ALA B 229 32.70 -79.40
REMARK 500 TYR B 348 -30.77 -131.30
REMARK 500 ASP B 388 71.75 23.25
REMARK 500 PHE B 446 -18.28 -143.76
REMARK 500 ALA B 456 -159.26 -88.59
REMARK 500 ALA B 461 -126.70 -108.51
REMARK 500 ALA B 475 35.97 -149.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN A 437 0.07 SIDE CHAIN
REMARK 500 GLU A 538 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 606 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 281 O
REMARK 620 2 ALA A 277 O 152.1
REMARK 620 3 ASP A 279 OD1 88.3 79.1
REMARK 620 4 ASP A 272 OD1 77.3 75.2 73.0
REMARK 620 5 HOH A 705 O 83.9 114.4 70.7 139.3
REMARK 620 6 ASP A 272 O 94.1 82.4 143.8 72.4 145.5
REMARK 620 7 ASP A 275 OD2 78.4 126.2 141.0 136.8 71.5 74.3
REMARK 620 8 ASP A 275 OD1 129.2 77.3 126.9 141.6 77.1 77.8 50.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 281 O
REMARK 620 2 ALA B 277 O 152.5
REMARK 620 3 ASP B 279 OD1 87.2 79.3
REMARK 620 4 ASP B 272 OD1 77.2 75.8 72.3
REMARK 620 5 ASP B 275 OD2 78.3 126.4 141.1 136.6
REMARK 620 6 ASP B 272 O 93.6 83.4 143.1 72.0 74.4
REMARK 620 7 HOH B 710 O 84.8 112.5 70.5 139.2 72.3 146.3
REMARK 620 8 ASP B 275 OD1 129.2 77.1 128.2 141.4 51.0 78.1 77.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 601 BOUND
REMARK 800 TO ASN A 49
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 602 BOUND
REMARK 800 TO ASN A 95
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 603 BOUND
REMARK 800 TO ASN A 234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 604 BOUND
REMARK 800 TO ASN A 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 605 BOUND
REMARK 800 TO ASN A 367
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 601 BOUND
REMARK 800 TO ASN B 95
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 602 BOUND
REMARK 800 TO ASN B 234
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 603 BOUND
REMARK 800 TO ASN B 298
DBREF 3WMT A 19 540 UNP Q2UP89 FAEB1_ASPOR 19 540
DBREF 3WMT B 19 540 UNP Q2UP89 FAEB1_ASPOR 19 540
SEQRES 1 A 522 ALA ALA ILE ASP SER THR SER SER SER ASN GLY SER ASP
SEQRES 2 A 522 HIS HIS GLY SER SER PHE GLN ALA GLU CYS GLU SER PHE
SEQRES 3 A 522 LYS ALA LYS ILE ASN VAL THR ASN ALA ASN VAL HIS SER
SEQRES 4 A 522 VAL THR TYR VAL PRO ALA GLY VAL ASN ILE SER MET ALA
SEQRES 5 A 522 ASP ASN PRO SER ILE CYS GLY GLY ASP GLU ASP PRO ILE
SEQRES 6 A 522 THR SER THR PHE ALA PHE CYS ARG ILE ALA LEU ASN VAL
SEQRES 7 A 522 THR THR SER SER LYS SER GLN ILE PHE MET GLU ALA TRP
SEQRES 8 A 522 LEU PRO SER ASN TYR SER GLY ARG PHE LEU SER THR GLY
SEQRES 9 A 522 ASN GLY GLY LEU GLY GLY CYS VAL LYS TYR ASP ASP MET
SEQRES 10 A 522 ALA TYR ALA ALA GLY TYR GLY PHE ALA THR VAL GLY THR
SEQRES 11 A 522 ASN ASN GLY HIS PHE GLY ASN ASN GLY VAL SER PHE TYR
SEQRES 12 A 522 GLN ASN THR GLU VAL VAL GLU ASP PHE ALA TYR ARG ALA
SEQRES 13 A 522 LEU HIS THR GLY VAL VAL VAL GLY LYS GLU LEU THR LYS
SEQRES 14 A 522 ASN PHE TYR PRO GLN GLY TYR ASN LYS SER TYR TYR LEU
SEQRES 15 A 522 GLY CYS SER THR GLY GLY ARG GLN GLY TRP LYS SER VAL
SEQRES 16 A 522 GLN THR PHE PRO ASP ASP PHE ASP GLY VAL VAL ALA GLY
SEQRES 17 A 522 ALA PRO ALA PHE ASN PHE ILE ASN LEU THR SER TRP GLY
SEQRES 18 A 522 ALA ARG PHE LEU THR LEU THR GLY ASP SER SER ALA GLU
SEQRES 19 A 522 THR PHE VAL THR GLU THR GLN TRP THR ALA VAL HIS ASN
SEQRES 20 A 522 GLU ILE ILE ARG GLN CYS ASP SER LEU ASP GLY ALA LYS
SEQRES 21 A 522 ASP GLY ILE ILE GLU ASP PRO ASP LEU CYS GLN PRO ILE
SEQRES 22 A 522 ILE GLU ALA LEU LEU CYS ASN ALA THR GLN SER SER THR
SEQRES 23 A 522 SER GLY THR CYS LEU THR GLY ALA GLN VAL LYS THR VAL
SEQRES 24 A 522 ASN GLY VAL PHE SER ALA THR TYR GLY LEU ASN GLY SER
SEQRES 25 A 522 PHE LEU TYR PRO ARG MET GLN PRO GLY SER GLU LEU ALA
SEQRES 26 A 522 ALA TYR SER SER TYR TYR SER GLY THR PRO PHE ALA TYR
SEQRES 27 A 522 ALA GLU ASP TRP TYR ARG TYR VAL VAL PHE ASN ASN THR
SEQRES 28 A 522 ASN TRP ASP VAL ALA THR TRP THR VAL GLN ASP ALA ALA
SEQRES 29 A 522 ILE ALA ASN ALA GLN ASP PRO TYR GLN ILE SER THR TRP
SEQRES 30 A 522 ASN GLY ASP LEU SER PRO PHE GLN LYS LYS GLY GLY LYS
SEQRES 31 A 522 VAL LEU HIS TYR HIS GLY MET GLU ASP ALA ILE ILE SER
SEQRES 32 A 522 SER GLU SER SER LYS VAL TYR TYR LYS HIS VAL ALA ASP
SEQRES 33 A 522 THR MET ASN LEU SER PRO SER GLU LEU ASP SER PHE TYR
SEQRES 34 A 522 ARG PHE PHE PRO ILE SER GLY MET ALA HIS CYS ALA ASN
SEQRES 35 A 522 ALA ASP GLY PRO SER ALA ILE GLY GLN GLY THR GLY THR
SEQRES 36 A 522 PHE ALA GLY ASN ASN PRO GLN ASP ASN VAL LEU LEU ALA
SEQRES 37 A 522 MET VAL GLN TRP VAL GLU GLU GLY VAL ALA PRO ASP PHE
SEQRES 38 A 522 VAL ARG GLY ALA LYS LEU ASN GLY SER THR VAL GLU TYR
SEQRES 39 A 522 ARG ARG LYS HIS CYS LYS TYR PRO LYS ARG ASN ARG TYR
SEQRES 40 A 522 VAL GLY PRO GLY SER TYR THR ASP GLU ASN ALA TRP GLU
SEQRES 41 A 522 CYS VAL
SEQRES 1 B 522 ALA ALA ILE ASP SER THR SER SER SER ASN GLY SER ASP
SEQRES 2 B 522 HIS HIS GLY SER SER PHE GLN ALA GLU CYS GLU SER PHE
SEQRES 3 B 522 LYS ALA LYS ILE ASN VAL THR ASN ALA ASN VAL HIS SER
SEQRES 4 B 522 VAL THR TYR VAL PRO ALA GLY VAL ASN ILE SER MET ALA
SEQRES 5 B 522 ASP ASN PRO SER ILE CYS GLY GLY ASP GLU ASP PRO ILE
SEQRES 6 B 522 THR SER THR PHE ALA PHE CYS ARG ILE ALA LEU ASN VAL
SEQRES 7 B 522 THR THR SER SER LYS SER GLN ILE PHE MET GLU ALA TRP
SEQRES 8 B 522 LEU PRO SER ASN TYR SER GLY ARG PHE LEU SER THR GLY
SEQRES 9 B 522 ASN GLY GLY LEU GLY GLY CYS VAL LYS TYR ASP ASP MET
SEQRES 10 B 522 ALA TYR ALA ALA GLY TYR GLY PHE ALA THR VAL GLY THR
SEQRES 11 B 522 ASN ASN GLY HIS PHE GLY ASN ASN GLY VAL SER PHE TYR
SEQRES 12 B 522 GLN ASN THR GLU VAL VAL GLU ASP PHE ALA TYR ARG ALA
SEQRES 13 B 522 LEU HIS THR GLY VAL VAL VAL GLY LYS GLU LEU THR LYS
SEQRES 14 B 522 ASN PHE TYR PRO GLN GLY TYR ASN LYS SER TYR TYR LEU
SEQRES 15 B 522 GLY CYS SER THR GLY GLY ARG GLN GLY TRP LYS SER VAL
SEQRES 16 B 522 GLN THR PHE PRO ASP ASP PHE ASP GLY VAL VAL ALA GLY
SEQRES 17 B 522 ALA PRO ALA PHE ASN PHE ILE ASN LEU THR SER TRP GLY
SEQRES 18 B 522 ALA ARG PHE LEU THR LEU THR GLY ASP SER SER ALA GLU
SEQRES 19 B 522 THR PHE VAL THR GLU THR GLN TRP THR ALA VAL HIS ASN
SEQRES 20 B 522 GLU ILE ILE ARG GLN CYS ASP SER LEU ASP GLY ALA LYS
SEQRES 21 B 522 ASP GLY ILE ILE GLU ASP PRO ASP LEU CYS GLN PRO ILE
SEQRES 22 B 522 ILE GLU ALA LEU LEU CYS ASN ALA THR GLN SER SER THR
SEQRES 23 B 522 SER GLY THR CYS LEU THR GLY ALA GLN VAL LYS THR VAL
SEQRES 24 B 522 ASN GLY VAL PHE SER ALA THR TYR GLY LEU ASN GLY SER
SEQRES 25 B 522 PHE LEU TYR PRO ARG MET GLN PRO GLY SER GLU LEU ALA
SEQRES 26 B 522 ALA TYR SER SER TYR TYR SER GLY THR PRO PHE ALA TYR
SEQRES 27 B 522 ALA GLU ASP TRP TYR ARG TYR VAL VAL PHE ASN ASN THR
SEQRES 28 B 522 ASN TRP ASP VAL ALA THR TRP THR VAL GLN ASP ALA ALA
SEQRES 29 B 522 ILE ALA ASN ALA GLN ASP PRO TYR GLN ILE SER THR TRP
SEQRES 30 B 522 ASN GLY ASP LEU SER PRO PHE GLN LYS LYS GLY GLY LYS
SEQRES 31 B 522 VAL LEU HIS TYR HIS GLY MET GLU ASP ALA ILE ILE SER
SEQRES 32 B 522 SER GLU SER SER LYS VAL TYR TYR LYS HIS VAL ALA ASP
SEQRES 33 B 522 THR MET ASN LEU SER PRO SER GLU LEU ASP SER PHE TYR
SEQRES 34 B 522 ARG PHE PHE PRO ILE SER GLY MET ALA HIS CYS ALA ASN
SEQRES 35 B 522 ALA ASP GLY PRO SER ALA ILE GLY GLN GLY THR GLY THR
SEQRES 36 B 522 PHE ALA GLY ASN ASN PRO GLN ASP ASN VAL LEU LEU ALA
SEQRES 37 B 522 MET VAL GLN TRP VAL GLU GLU GLY VAL ALA PRO ASP PHE
SEQRES 38 B 522 VAL ARG GLY ALA LYS LEU ASN GLY SER THR VAL GLU TYR
SEQRES 39 B 522 ARG ARG LYS HIS CYS LYS TYR PRO LYS ARG ASN ARG TYR
SEQRES 40 B 522 VAL GLY PRO GLY SER TYR THR ASP GLU ASN ALA TRP GLU
SEQRES 41 B 522 CYS VAL
MODRES 3WMT ASN A 298 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN A 95 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN B 298 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN A 49 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN B 95 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN A 367 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN B 234 ASN GLYCOSYLATION SITE
MODRES 3WMT ASN A 234 ASN GLYCOSYLATION SITE
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET CA A 606 1
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET CA B 604 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CA CALCIUM ION
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 8 CA 2(CA 2+)
FORMUL 13 HOH *1087(H2 O)
HELIX 1 1 SER A 36 LYS A 45 1 10
HELIX 2 2 ALA A 46 ILE A 48 5 3
HELIX 3 3 PRO A 73 GLY A 77 5 5
HELIX 4 4 LYS A 131 GLY A 140 1 10
HELIX 5 5 GLY A 157 TYR A 161 5 5
HELIX 6 6 ASN A 163 TYR A 172 1 10
HELIX 7 7 TYR A 172 TYR A 190 1 19
HELIX 8 8 SER A 203 PHE A 216 1 14
HELIX 9 9 ASN A 231 GLY A 247 1 17
HELIX 10 10 THR A 256 ASP A 272 1 17
HELIX 11 11 SER A 273 GLY A 276 5 4
HELIX 12 12 ASP A 284 CYS A 288 5 5
HELIX 13 13 ILE A 291 LEU A 296 5 6
HELIX 14 14 SER A 302 GLY A 306 5 5
HELIX 15 15 THR A 310 PHE A 321 1 12
HELIX 16 16 LEU A 327 GLY A 329 5 3
HELIX 17 17 SER A 340 TYR A 348 1 9
HELIX 18 18 PHE A 354 VAL A 364 1 11
HELIX 19 19 ASP A 372 TRP A 376 5 5
HELIX 20 20 THR A 377 ASP A 388 1 12
HELIX 21 21 PRO A 389 ILE A 392 5 4
HELIX 22 22 LEU A 399 LYS A 405 1 7
HELIX 23 23 SER A 421 ASN A 437 1 17
HELIX 24 24 SER A 439 ASP A 444 1 6
HELIX 25 25 GLY A 470 PHE A 474 5 5
HELIX 26 26 ASN A 478 ASP A 481 5 4
HELIX 27 27 ASN A 482 GLY A 494 1 13
HELIX 28 28 ASP A 533 ASN A 535 5 3
HELIX 29 29 PHE B 37 SER B 43 1 7
HELIX 30 30 PHE B 44 LYS B 47 5 4
HELIX 31 31 LYS B 131 GLY B 140 1 10
HELIX 32 32 GLY B 157 TYR B 161 5 5
HELIX 33 33 ASN B 163 TYR B 172 1 10
HELIX 34 34 TYR B 172 TYR B 190 1 19
HELIX 35 35 SER B 203 PHE B 216 1 14
HELIX 36 36 ASN B 231 GLY B 247 1 17
HELIX 37 37 THR B 256 ASP B 272 1 17
HELIX 38 38 SER B 273 GLY B 276 5 4
HELIX 39 39 ASP B 284 CYS B 288 5 5
HELIX 40 40 ILE B 291 LEU B 296 5 6
HELIX 41 41 SER B 302 GLY B 306 5 5
HELIX 42 42 THR B 310 PHE B 321 1 12
HELIX 43 43 LEU B 327 GLY B 329 5 3
HELIX 44 44 SER B 340 TYR B 348 1 9
HELIX 45 45 PHE B 354 VAL B 364 1 11
HELIX 46 46 ASP B 372 TRP B 376 5 5
HELIX 47 47 THR B 377 ASP B 388 1 12
HELIX 48 48 PRO B 389 ILE B 392 5 4
HELIX 49 49 LEU B 399 LYS B 405 1 7
HELIX 50 50 SER B 422 ASN B 437 1 16
HELIX 51 51 SER B 439 ASP B 444 1 6
HELIX 52 52 GLY B 470 PHE B 474 5 5
HELIX 53 53 ASN B 478 ASP B 481 5 4
HELIX 54 54 ASN B 482 GLY B 494 1 13
HELIX 55 55 ASP B 533 ASN B 535 5 3
SHEET 1 A 9 ALA A 53 VAL A 61 0
SHEET 2 A 9 PHE A 89 SER A 99 -1 O ARG A 91 N THR A 59
SHEET 3 A 9 SER A 102 PRO A 111 -1 O LEU A 110 N CYS A 90
SHEET 4 A 9 ALA A 144 THR A 148 -1 O THR A 145 N TRP A 109
SHEET 5 A 9 PHE A 118 SER A 120 1 N LEU A 119 O ALA A 144
SHEET 6 A 9 SER A 197 CYS A 202 1 O TYR A 198 N PHE A 118
SHEET 7 A 9 GLY A 222 GLY A 226 1 O VAL A 224 N TYR A 199
SHEET 8 A 9 LYS A 408 GLY A 414 1 O LEU A 410 N VAL A 223
SHEET 9 A 9 TYR A 447 ILE A 452 1 O ARG A 448 N HIS A 411
SHEET 1 B 2 THR A 324 TYR A 325 0
SHEET 2 B 2 PHE A 331 TYR A 333 -1 O TYR A 333 N THR A 324
SHEET 1 C 2 PHE A 499 ASN A 506 0
SHEET 2 C 2 THR A 509 CYS A 517 -1 O THR A 509 N ASN A 506
SHEET 1 D 2 ARG A 522 TYR A 525 0
SHEET 2 D 2 TRP A 537 VAL A 540 -1 O GLU A 538 N ARG A 524
SHEET 1 E 9 ALA B 53 VAL B 61 0
SHEET 2 E 9 PHE B 89 SER B 99 -1 O PHE B 89 N VAL B 61
SHEET 3 E 9 SER B 102 PRO B 111 -1 O LEU B 110 N CYS B 90
SHEET 4 E 9 ALA B 144 THR B 148 -1 O THR B 145 N TRP B 109
SHEET 5 E 9 PHE B 118 SER B 120 1 N LEU B 119 O ALA B 144
SHEET 6 E 9 SER B 197 CYS B 202 1 O TYR B 198 N PHE B 118
SHEET 7 E 9 GLY B 222 GLY B 226 1 O GLY B 226 N GLY B 201
SHEET 8 E 9 LYS B 408 GLY B 414 1 O LEU B 410 N VAL B 223
SHEET 9 E 9 TYR B 447 ILE B 452 1 O ILE B 452 N HIS B 413
SHEET 1 F 2 THR B 324 TYR B 325 0
SHEET 2 F 2 PHE B 331 TYR B 333 -1 O TYR B 333 N THR B 324
SHEET 1 G 2 PHE B 499 ASN B 506 0
SHEET 2 G 2 THR B 509 CYS B 517 -1 O THR B 509 N ASN B 506
SHEET 1 H 2 ASN B 523 TYR B 525 0
SHEET 2 H 2 TRP B 537 CYS B 539 -1 O GLU B 538 N ARG B 524
SSBOND 1 CYS A 41 CYS A 90 1555 1555 2.08
SSBOND 2 CYS A 76 CYS A 129 1555 1555 2.04
SSBOND 3 CYS A 202 CYS A 458 1555 1555 2.04
SSBOND 4 CYS A 271 CYS A 288 1555 1555 2.03
SSBOND 5 CYS A 297 CYS A 308 1555 1555 2.02
SSBOND 6 CYS A 517 CYS A 539 1555 1555 2.04
SSBOND 7 CYS B 41 CYS B 90 1555 1555 2.07
SSBOND 8 CYS B 202 CYS B 458 1555 1555 2.06
SSBOND 9 CYS B 271 CYS B 288 1555 1555 2.06
SSBOND 10 CYS B 297 CYS B 308 1555 1555 2.02
SSBOND 11 CYS B 517 CYS B 539 1555 1555 2.02
LINK ND2 ASN A 298 C1 NAG A 604 1555 1555 1.39
LINK ND2 ASN A 95 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN B 298 C1 NAG B 603 1555 1555 1.47
LINK ND2 ASN A 49 C1 NAG A 601 1555 1555 1.48
LINK ND2 ASN B 95 C1 NAG B 601 1555 1555 1.48
LINK ND2 ASN A 367 C1 NAG A 605 1555 1555 1.49
LINK ND2 ASN B 234 C1 NAG B 602 1555 1555 1.50
LINK ND2 ASN A 234 C1 NAG A 603 1555 1555 1.53
LINK O ILE A 281 CA CA A 606 1555 1555 2.29
LINK O ILE B 281 CA CA B 604 1555 1555 2.33
LINK O ALA A 277 CA CA A 606 1555 1555 2.37
LINK O ALA B 277 CA CA B 604 1555 1555 2.38
LINK OD1 ASP B 279 CA CA B 604 1555 1555 2.43
LINK OD1 ASP B 272 CA CA B 604 1555 1555 2.45
LINK OD1 ASP A 279 CA CA A 606 1555 1555 2.45
LINK OD1 ASP A 272 CA CA A 606 1555 1555 2.45
LINK OD2 ASP B 275 CA CA B 604 1555 1555 2.45
LINK O ASP B 272 CA CA B 604 1555 1555 2.46
LINK CA CA A 606 O HOH A 705 1555 1555 2.46
LINK CA CA B 604 O HOH B 710 1555 1555 2.47
LINK O ASP A 272 CA CA A 606 1555 1555 2.48
LINK OD2 ASP A 275 CA CA A 606 1555 1555 2.49
LINK OD1 ASP B 275 CA CA B 604 1555 1555 2.58
LINK OD1 ASP A 275 CA CA A 606 1555 1555 2.59
CISPEP 1 GLY A 127 GLY A 128 0 -10.68
CISPEP 2 TYR A 519 PRO A 520 0 11.95
CISPEP 3 GLY A 527 PRO A 528 0 -1.29
CISPEP 4 GLY B 127 GLY B 128 0 -7.30
CISPEP 5 TYR B 519 PRO B 520 0 7.25
CISPEP 6 GLY B 527 PRO B 528 0 3.83
SITE 1 AC1 6 ASP A 272 ASP A 275 ALA A 277 ASP A 279
SITE 2 AC1 6 ILE A 281 HOH A 705
SITE 1 AC2 6 ASP B 272 ASP B 275 ALA B 277 ASP B 279
SITE 2 AC2 6 ILE B 281 HOH B 710
SITE 1 AC3 12 ASN A 49 HOH A 766 HOH A 900 HOH A1006
SITE 2 AC3 12 HOH A1102 HOH A1120 LYS B 408 GLY B 494
SITE 3 AC3 12 PRO B 528 GLY B 529 HOH B 828 HOH B1005
SITE 1 AC4 8 HIS A 56 ASN A 95 GLN A 103 PHE A 105
SITE 2 AC4 8 ASN A 149 GLY A 151 HIS A 152 HOH A 963
SITE 1 AC5 9 ASN A 231 ASN A 234 PHE A 331 LEU A 332
SITE 2 AC5 9 ALA A 382 ASN A 385 TRP A 395 HOH A1226
SITE 3 AC5 9 HOH A1255
SITE 1 AC6 9 LEU A 296 ASN A 298 GLN A 301 HOH A 968
SITE 2 AC6 9 HOH A1008 HOH A1040 HOH A1062 HOH A1139
SITE 3 AC6 9 SER B 441
SITE 1 AC7 10 GLN A 162 ASN A 367 SER A 441 ASP A 444
SITE 2 AC7 10 ASP A 498 LYS A 518 HOH A 827 HOH A 977
SITE 3 AC7 10 HOH A1014 HOH A1109
SITE 1 AC8 8 HIS B 56 ASN B 95 GLN B 103 PHE B 105
SITE 2 AC8 8 ASN B 149 GLY B 151 HIS B 152 PHE B 153
SITE 1 AC9 9 ASN B 231 ASN B 234 PHE B 331 LEU B 332
SITE 2 AC9 9 ASN B 385 TRP B 395 HOH B 756 HOH B1006
SITE 3 AC9 9 HOH B1182
SITE 1 BC1 11 GLN A 162 SER A 441 HOH A 977 LEU B 296
SITE 2 BC1 11 ASN B 298 GLN B 301 HOH B 740 HOH B 967
SITE 3 BC1 11 HOH B 978 HOH B 993 HOH B1032
CRYST1 93.954 142.937 73.810 90.00 90.00 90.00 P 21 21 2 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 0.010644 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013548 0.00000
TER 3860 VAL A 540
TER 7690 VAL B 540
MASTER 533 0 10 55 30 0 26 6 8889 2 162 82
END |