HEADER HYDROLASE 12-JUL-04 1W32
TITLE THE 3-DIMENSIONAL STRUCTURE OF A THERMOSTABLE MUTANT OF A XYLANASE
TITLE 2 (XYN10A) FROM CELLVIBRIO JAPONICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE A PRECURSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 265-611;
COMPND 5 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A, XYLA;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CELLVIBRIO JAPONICUS;
SOURCE 3 ORGANISM_TAXID: 155077;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: GM83 DE3;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-16B;
SOURCE 8 OTHER_DETAILS: ORGANISM FORMERLY KNOWN AS PSEUDOMONAS FLUORESCENS
KEYWDS XYLANASE, MUTANT, CALCIUM ION, THERMOSTABLE, GLYCOSYLE HYDROLASE,
KEYWDS 2 FAMILY 10, ERROR PRONE PCR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ANDREWS,E.J.TAYLOR,G.N.PELL,F.VINCENT,V.M.A.DUCROS,G.J.DAVIES,
AUTHOR 2 J.H.LAKEY,H.J.GILBERT
REVDAT 5 13-DEC-23 1W32 1 LINK
REVDAT 4 24-FEB-09 1W32 1 VERSN
REVDAT 3 22-DEC-04 1W32 1 JRNL
REVDAT 2 08-OCT-04 1W32 1 SSBOND
REVDAT 1 30-SEP-04 1W32 0
JRNL AUTH S.ANDREWS,E.J.TAYLOR,G.N.PELL,F.VINCENT,V.M.A.DUCROS,
JRNL AUTH 2 G.J.DAVIES,J.H.LAKEY,H.J.GILBERT
JRNL TITL THE USE OF FORCED PROTEIN EVOLUTION TO INVESTIGATE AND
JRNL TITL 2 IMPROVE STABILITY OF FAMILY 10 XYLANASES: THE PRODUCTION OF
JRNL TITL 3 CA2+-INDEPENDENT STABLE XYLANASES
JRNL REF J.BIOL.CHEM. V. 279 54369 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15452124
JRNL DOI 10.1074/JBC.M409044200
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 202740
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) : 0.122
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.144
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10712
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 743
REMARK 3 BIN FREE R VALUE : 0.2070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5406
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 1028
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.12000
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): 0.037
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.035
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.970
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7354 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6187 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10096 ; 1.406 ; 1.916
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14442 ; 0.763 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 970 ; 6.464 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 400 ;32.831 ;24.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1091 ;12.076 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;19.474 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1032 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8892 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1607 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1429 ; 0.248 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5839 ; 0.231 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3168 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3356 ; 0.094 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 756 ; 0.254 ; 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): 24 ; 0.164 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 60 ; 0.297 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 93 ; 0.264 ; 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): 4690 ; 1.070 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7422 ; 1.467 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3052 ; 2.120 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2673 ; 2.841 ; 4.500
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 1W32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1290020431.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
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 : 213551
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.550
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.52
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.420
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 1CLX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 75.13650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.67150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.67150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.70475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.67150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.67150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.56825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.67150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.67150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 112.70475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.67150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.67150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.56825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.13650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC
REMARK 400 LINKAGES IN XYLANS.
REMARK 400 ENGINEERED MUTATION: ASN 526 ASP IN CHAINS A, B
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 MET A 0
REMARK 465 ARG A 347
REMARK 465 MET B 0
REMARK 465 ARG B 347
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER B 55 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N ASP A 137 O HOH A 2250 1.29
REMARK 500 O HOH A 2114 O HOH A 2316 1.39
REMARK 500 OD1 ASN B 319 O HOH B 2477 1.48
REMARK 500 O HOH A 2106 O HOH A 2284 1.56
REMARK 500 OD1 ASN A 319 O HOH A 2482 1.58
REMARK 500 O HOH B 2113 O HOH B 2305 1.59
REMARK 500 O HOH A 2406 O HOH A 2431 1.60
REMARK 500 O HOH A 2106 O HOH A 2283 1.67
REMARK 500 OE2 GLU A 185 O HOH A 2310 1.67
REMARK 500 C PRO A 136 O HOH A 2250 1.81
REMARK 500 O ALA B 70 O HOH B 2139 1.83
REMARK 500 O ASP A 135 O HOH A 2250 1.90
REMARK 500 OD1 ASP A 135 O HOH A 2250 1.92
REMARK 500 N VAL A 271 O HOH A 2427 1.99
REMARK 500 O HOH B 2241 O HOH B 2329 1.99
REMARK 500 N GLY A 138 O HOH A 2250 2.04
REMARK 500 OE1 GLN A 318 O HOH A 2477 2.06
REMARK 500 C ASP A 135 O HOH A 2250 2.10
REMARK 500 O HOH B 2401 O HOH B 2425 2.11
REMARK 500 O HOH A 2401 O HOH A 2403 2.11
REMARK 500 O HOH A 2129 O HOH A 2334 2.14
REMARK 500 OG1 THR A 25 O HOH A 2045 2.14
REMARK 500 O HOH A 2212 O HOH A 2213 2.15
REMARK 500 NH2 ARG B 64 O HOH B 2132 2.15
REMARK 500 O HOH A 2466 O HOH A 2472 2.16
REMARK 500 O HOH A 2134 O HOH A 2338 2.16
REMARK 500 O HOH A 2184 O HOH A 2191 2.18
REMARK 500 OD1 ASP A 219 O HOH A 2349 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2184 O HOH B 2388 5545 1.88
REMARK 500 O HOH A 2409 O HOH B 2031 5545 1.89
REMARK 500 CG2 THR B 25 O HOH B 2133 7556 2.04
REMARK 500 O HOH B 2308 O HOH B 2486 3554 2.14
REMARK 500 O HOH B 2132 O HOH B 2132 7556 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 SER A 86 C TYR A 87 N -0.439
REMARK 500 SER B 26 C SER B 27 N 0.216
REMARK 500 SER B 26 C SER B 27 N 0.265
REMARK 500 SER B 55 CB SER B 55 OG 0.248
REMARK 500 SER B 55 CB SER B 55 OG -0.370
REMARK 500 SER B 86 C TYR B 87 N -0.446
REMARK 500 ALA B 105 C ARG B 106 N -0.141
REMARK 500 SER B 272 C CYS B 273 N 0.158
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 SER A 86 O - C - N ANGL. DEV. = -9.8 DEGREES
REMARK 500 SER B 26 CA - C - N ANGL. DEV. = -30.3 DEGREES
REMARK 500 SER B 26 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 SER B 27 C - N - CA ANGL. DEV. = -30.5 DEGREES
REMARK 500 SER B 27 CA - C - N ANGL. DEV. = -15.9 DEGREES
REMARK 500 ALA B 105 O - C - N ANGL. DEV. = 11.2 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 ALA A 16 33.49 -155.26
REMARK 500 ASN A 44 -38.15 -135.26
REMARK 500 ASN A 44 -27.15 -141.14
REMARK 500 ASP A 134 80.03 -158.18
REMARK 500 GLU A 246 41.42 -145.19
REMARK 500 ALA B 16 18.86 -158.19
REMARK 500 ALA B 16 39.86 -144.93
REMARK 500 ASN B 44 -33.61 -136.42
REMARK 500 ASN B 44 -34.15 -134.59
REMARK 500 ASP B 134 45.92 -143.60
REMARK 500 ASN B 186 32.03 70.50
REMARK 500 GLU B 246 42.42 -145.53
REMARK 500 VAL B 271 -51.96 -127.25
REMARK 500 VAL B 271 -50.06 -127.25
REMARK 500 ASN B 328 -167.91 -100.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 86 10.84
REMARK 500 SER B 26 26.80
REMARK 500 SER B 27 -19.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2052 DISTANCE = 5.93 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 2269
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 A1347 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 253 O
REMARK 620 2 ASP A 256 OD1 83.5
REMARK 620 3 ASP A 256 OD2 77.5 52.3
REMARK 620 4 ASN A 258 O 136.9 109.7 79.5
REMARK 620 5 ASN A 261 OD1 151.3 83.6 113.6 71.8
REMARK 620 6 ASN A 262 ND2 94.0 149.0 156.9 93.2 84.1
REMARK 620 7 HOH A2385 O 76.6 83.2 130.3 143.8 76.5 66.4
REMARK 620 8 HOH A2405 O 71.1 129.6 79.6 69.2 135.4 77.4 128.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1347 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 253 O
REMARK 620 2 ASP A 256 OD1 80.1
REMARK 620 3 ASP A 256 OD2 82.7 51.5
REMARK 620 4 ASN A 258 O 138.1 75.7 106.9
REMARK 620 5 ASN A 261 OD1 153.5 111.0 86.0 68.3
REMARK 620 6 ASN A 262 ND2 98.1 159.5 149.0 93.2 79.7
REMARK 620 7 HOH A2385 O 80.7 118.5 68.5 141.1 72.8 80.9
REMARK 620 8 HOH A2405 O 69.9 73.5 122.0 70.6 135.6 86.5 146.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1347 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 253 O
REMARK 620 2 ASP B 256 OD2 81.9
REMARK 620 3 ASP B 256 OD1 78.4 51.1
REMARK 620 4 ASN B 258 O 138.9 108.0 78.1
REMARK 620 5 ASN B 261 OD1 152.0 83.2 109.7 68.6
REMARK 620 6 ASN B 262 OD1 96.0 150.7 157.2 92.9 85.6
REMARK 620 7 HOH B2381 O 67.5 121.5 74.0 73.8 140.1 83.5
REMARK 620 8 HOH B2389 O 74.8 127.0 77.6 67.5 132.6 79.6 7.8
REMARK 620 9 HOH B2398 O 79.2 78.1 126.6 141.5 74.7 72.7 136.5 139.4
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 700
REMARK 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA"
REMARK 700 AND "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-
REMARK 700 STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN
REMARK 700 WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1349
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1349
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1354
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CLX RELATED DB: PDB
REMARK 900 CATALYTIC CORE OF XYLANASE A
REMARK 900 RELATED ID: 1E5N RELATED DB: PDB
REMARK 900 E246C MUTANT OF P FLUORESCENS SUBSP. CELLULOSA XYLANASE A IN
REMARK 900 COMPLEX WITH XYLOPENTAOSE
REMARK 900 RELATED ID: 1E8R RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE X CBD
REMARK 900 RELATED ID: 1QLD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE X CBM
REMARK 900 RELATED ID: 1W2P RELATED DB: PDB
REMARK 900 THE 3-DIMENSIONAL STRUCTURE OF A XYLANASE ( XYN10A) FROM CELLVIBRIO
REMARK 900 JAPONICUS
REMARK 900 RELATED ID: 1W2V RELATED DB: PDB
REMARK 900 THE 3-DIMENSIONAL STRUCTURE OF A THERMOSTABLE MUTANT OF A XYLANASE
REMARK 900 (XYN10A) FROM CELLVIBRIO JAPONICUS
REMARK 900 RELATED ID: 1W3H RELATED DB: PDB
REMARK 900 THE 3-DIMENSIONAL STRUCTURE OF A THERMOSTABLE MUTANT OF A XYLANASE
REMARK 900 (XYN10A) FROM CELLVIBRIO JAPONICUS
REMARK 900 RELATED ID: 1XYS RELATED DB: PDB
REMARK 900 CATALYTIC CORE OF XYLANASE A E246C MUTANT
DBREF 1W32 A 0 0 PDB 1W32 1W32 0 0
DBREF 1W32 A 1 347 UNP P14768 XYNA_PSEFL 265 611
DBREF 1W32 B 0 0 PDB 1W32 1W32 0 0
DBREF 1W32 B 1 347 UNP P14768 XYNA_PSEFL 265 611
SEQADV 1W32 ASN A 262 UNP P14768 ASP 526 ENGINEERED MUTATION
SEQADV 1W32 ASN B 262 UNP P14768 ASP 526 ENGINEERED MUTATION
SEQRES 1 A 348 MET GLY LEU ALA SER LEU ALA ASP PHE PRO ILE GLY VAL
SEQRES 2 A 348 ALA VAL ALA ALA SER GLY GLY ASN ALA ASP ILE PHE THR
SEQRES 3 A 348 SER SER ALA ARG GLN ASN ILE VAL ARG ALA GLU PHE ASN
SEQRES 4 A 348 GLN ILE THR ALA GLU ASN ILE MET LYS MET SER TYR MET
SEQRES 5 A 348 TYR SER GLY SER ASN PHE SER PHE THR ASN SER ASP ARG
SEQRES 6 A 348 LEU VAL SER TRP ALA ALA GLN ASN GLY GLN THR VAL HIS
SEQRES 7 A 348 GLY HIS ALA LEU VAL TRP HIS PRO SER TYR GLN LEU PRO
SEQRES 8 A 348 ASN TRP ALA SER ASP SER ASN ALA ASN PHE ARG GLN ASP
SEQRES 9 A 348 PHE ALA ARG HIS ILE ASP THR VAL ALA ALA HIS PHE ALA
SEQRES 10 A 348 GLY GLN VAL LYS SER TRP ASP VAL VAL ASN GLU ALA LEU
SEQRES 11 A 348 PHE ASP SER ALA ASP ASP PRO ASP GLY ARG GLY SER ALA
SEQRES 12 A 348 ASN GLY TYR ARG GLN SER VAL PHE TYR ARG GLN PHE GLY
SEQRES 13 A 348 GLY PRO GLU TYR ILE ASP GLU ALA PHE ARG ARG ALA ARG
SEQRES 14 A 348 ALA ALA ASP PRO THR ALA GLU LEU TYR TYR ASN ASP PHE
SEQRES 15 A 348 ASN THR GLU GLU ASN GLY ALA LYS THR THR ALA LEU VAL
SEQRES 16 A 348 ASN LEU VAL GLN ARG LEU LEU ASN ASN GLY VAL PRO ILE
SEQRES 17 A 348 ASP GLY VAL GLY PHE GLN MET HIS VAL MET ASN ASP TYR
SEQRES 18 A 348 PRO SER ILE ALA ASN ILE ARG GLN ALA MET GLN LYS ILE
SEQRES 19 A 348 VAL ALA LEU SER PRO THR LEU LYS ILE LYS ILE THR GLU
SEQRES 20 A 348 LEU ASP VAL ARG LEU ASN ASN PRO TYR ASP GLY ASN SER
SEQRES 21 A 348 SER ASN ASN TYR THR ASN ARG ASN ASP CYS ALA VAL SER
SEQRES 22 A 348 CYS ALA GLY LEU ASP ARG GLN LYS ALA ARG TYR LYS GLU
SEQRES 23 A 348 ILE VAL GLN ALA TYR LEU GLU VAL VAL PRO PRO GLY ARG
SEQRES 24 A 348 ARG GLY GLY ILE THR VAL TRP GLY ILE ALA ASP PRO ASP
SEQRES 25 A 348 SER TRP LEU TYR THR HIS GLN ASN LEU PRO ASP TRP PRO
SEQRES 26 A 348 LEU LEU PHE ASN ASP ASN LEU GLN PRO LYS PRO ALA TYR
SEQRES 27 A 348 GLN GLY VAL VAL GLU ALA LEU SER GLY ARG
SEQRES 1 B 348 MET GLY LEU ALA SER LEU ALA ASP PHE PRO ILE GLY VAL
SEQRES 2 B 348 ALA VAL ALA ALA SER GLY GLY ASN ALA ASP ILE PHE THR
SEQRES 3 B 348 SER SER ALA ARG GLN ASN ILE VAL ARG ALA GLU PHE ASN
SEQRES 4 B 348 GLN ILE THR ALA GLU ASN ILE MET LYS MET SER TYR MET
SEQRES 5 B 348 TYR SER GLY SER ASN PHE SER PHE THR ASN SER ASP ARG
SEQRES 6 B 348 LEU VAL SER TRP ALA ALA GLN ASN GLY GLN THR VAL HIS
SEQRES 7 B 348 GLY HIS ALA LEU VAL TRP HIS PRO SER TYR GLN LEU PRO
SEQRES 8 B 348 ASN TRP ALA SER ASP SER ASN ALA ASN PHE ARG GLN ASP
SEQRES 9 B 348 PHE ALA ARG HIS ILE ASP THR VAL ALA ALA HIS PHE ALA
SEQRES 10 B 348 GLY GLN VAL LYS SER TRP ASP VAL VAL ASN GLU ALA LEU
SEQRES 11 B 348 PHE ASP SER ALA ASP ASP PRO ASP GLY ARG GLY SER ALA
SEQRES 12 B 348 ASN GLY TYR ARG GLN SER VAL PHE TYR ARG GLN PHE GLY
SEQRES 13 B 348 GLY PRO GLU TYR ILE ASP GLU ALA PHE ARG ARG ALA ARG
SEQRES 14 B 348 ALA ALA ASP PRO THR ALA GLU LEU TYR TYR ASN ASP PHE
SEQRES 15 B 348 ASN THR GLU GLU ASN GLY ALA LYS THR THR ALA LEU VAL
SEQRES 16 B 348 ASN LEU VAL GLN ARG LEU LEU ASN ASN GLY VAL PRO ILE
SEQRES 17 B 348 ASP GLY VAL GLY PHE GLN MET HIS VAL MET ASN ASP TYR
SEQRES 18 B 348 PRO SER ILE ALA ASN ILE ARG GLN ALA MET GLN LYS ILE
SEQRES 19 B 348 VAL ALA LEU SER PRO THR LEU LYS ILE LYS ILE THR GLU
SEQRES 20 B 348 LEU ASP VAL ARG LEU ASN ASN PRO TYR ASP GLY ASN SER
SEQRES 21 B 348 SER ASN ASN TYR THR ASN ARG ASN ASP CYS ALA VAL SER
SEQRES 22 B 348 CYS ALA GLY LEU ASP ARG GLN LYS ALA ARG TYR LYS GLU
SEQRES 23 B 348 ILE VAL GLN ALA TYR LEU GLU VAL VAL PRO PRO GLY ARG
SEQRES 24 B 348 ARG GLY GLY ILE THR VAL TRP GLY ILE ALA ASP PRO ASP
SEQRES 25 B 348 SER TRP LEU TYR THR HIS GLN ASN LEU PRO ASP TRP PRO
SEQRES 26 B 348 LEU LEU PHE ASN ASP ASN LEU GLN PRO LYS PRO ALA TYR
SEQRES 27 B 348 GLN GLY VAL VAL GLU ALA LEU SER GLY ARG
HET CA A1347 2
HET EDO A1348 4
HET EDO A1349 4
HET CA B1347 1
HET EDO B1348 4
HET EDO B1349 4
HET EDO B1350 4
HET EDO B1351 4
HET EDO B1352 4
HET EDO B1353 4
HET EDO B1354 4
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 EDO 9(C2 H6 O2)
FORMUL 14 HOH *1028(H2 O)
HELIX 1 1 GLY A 1 ALA A 6 5 6
HELIX 2 2 SER A 26 PHE A 37 1 12
HELIX 3 3 LYS A 47 TYR A 50 5 4
HELIX 4 4 PHE A 59 ASN A 72 1 14
HELIX 5 5 PRO A 85 LEU A 89 5 5
HELIX 6 6 ASN A 99 PHE A 115 1 17
HELIX 7 7 ASP A 131 ASP A 135 5 5
HELIX 8 8 SER A 148 GLY A 155 1 8
HELIX 9 9 PRO A 157 ASP A 171 1 15
HELIX 10 10 GLY A 187 ASN A 203 1 17
HELIX 11 11 SER A 222 ALA A 235 1 14
HELIX 12 12 ASN A 265 ALA A 270 5 6
HELIX 13 13 CYS A 273 VAL A 294 1 22
HELIX 14 14 ASP A 309 SER A 312 5 4
HELIX 15 15 LYS A 334 GLY A 346 1 13
HELIX 16 16 GLY B 1 ALA B 6 5 6
HELIX 17 17 SER B 26 PHE B 37 1 12
HELIX 18 18 LYS B 47 TYR B 50 5 4
HELIX 19 19 PHE B 59 ASN B 72 1 14
HELIX 20 20 PRO B 85 LEU B 89 5 5
HELIX 21 21 ASN B 99 PHE B 115 1 17
HELIX 22 22 SER B 148 GLY B 155 1 8
HELIX 23 23 PRO B 157 ASP B 171 1 15
HELIX 24 24 GLY B 187 ASN B 203 1 17
HELIX 25 25 SER B 222 ALA B 235 1 14
HELIX 26 26 CYS B 273 VAL B 294 1 22
HELIX 27 27 ASP B 309 SER B 312 5 4
HELIX 28 28 LYS B 334 GLY B 346 1 13
SHEET 1 AA11 ILE A 10 VAL A 14 0
SHEET 2 AA11 ARG A 299 VAL A 304 1 O ILE A 302 N GLY A 11
SHEET 3 AA11 LYS A 241 ARG A 250 1 O ILE A 242 N GLY A 300
SHEET 4 AA11 GLY A 209 PHE A 212 1 O VAL A 210 N LYS A 243
SHEET 5 AA11 GLU A 175 ASP A 180 1 O TYR A 178 N GLY A 211
SHEET 6 AA11 SER A 121 ASN A 126 1 O TRP A 122 N TYR A 177
SHEET 7 AA11 THR A 75 VAL A 82 1 O GLY A 78 N ASP A 123
SHEET 8 AA11 GLN A 39 ALA A 42 1 O ILE A 40 N HIS A 77
SHEET 9 AA11 ILE A 10 VAL A 14 1 O VAL A 12 N THR A 41
SHEET 10 AA11 ARG A 299 VAL A 304 1 O ILE A 302 N GLY A 11
SHEET 11 AA11 ILE A 10 VAL A 14 1 O GLY A 11 N VAL A 304
SHEET 1 AB 2 TYR A 52 SER A 53 0
SHEET 2 AB 2 ASN A 56 PHE A 57 -1 O ASN A 56 N SER A 53
SHEET 1 AC 2 SER A 141 ALA A 142 0
SHEET 2 AC 2 TYR A 145 ARG A 146 -1 O TYR A 145 N ALA A 142
SHEET 1 AD 2 THR A 316 HIS A 317 0
SHEET 2 AD 2 LEU A 320 PRO A 321 -1 O LEU A 320 N HIS A 317
SHEET 1 BA10 ILE B 10 VAL B 14 0
SHEET 2 BA10 ARG B 299 VAL B 304 1 O ILE B 302 N GLY B 11
SHEET 3 BA10 LYS B 241 ARG B 250 1 O ILE B 242 N GLY B 300
SHEET 4 BA10 GLY B 209 PHE B 212 1 O VAL B 210 N LYS B 243
SHEET 5 BA10 GLU B 175 ASP B 180 1 O TYR B 178 N GLY B 211
SHEET 6 BA10 SER B 121 ASN B 126 1 O TRP B 122 N TYR B 177
SHEET 7 BA10 THR B 75 VAL B 82 1 O VAL B 76 N SER B 121
SHEET 8 BA10 GLN B 39 ALA B 42 1 O ILE B 40 N HIS B 77
SHEET 9 BA10 ILE B 10 VAL B 14 1 O VAL B 12 N THR B 41
SHEET 10 BA10 ILE B 10 VAL B 14 0
SHEET 1 BB 2 TYR B 52 SER B 53 0
SHEET 2 BB 2 ASN B 56 PHE B 57 -1 O ASN B 56 N SER B 53
SHEET 1 BC 2 SER B 141 ALA B 142 0
SHEET 2 BC 2 TYR B 145 ARG B 146 -1 O TYR B 145 N ALA B 142
SHEET 1 BD 2 THR B 316 HIS B 317 0
SHEET 2 BD 2 LEU B 320 PRO B 321 -1 O LEU B 320 N HIS B 317
SSBOND 1 CYS A 269 CYS A 273 1555 1555 2.13
SSBOND 2 CYS B 269 CYS B 273 1555 1555 2.96
LINK O AASN A 253 CA A CA A1347 1555 1555 2.41
LINK O BASN A 253 CA B CA A1347 1555 1555 2.69
LINK OD1AASP A 256 CA A CA A1347 1555 1555 2.56
LINK OD2AASP A 256 CA A CA A1347 1555 1555 2.38
LINK OD1BASP A 256 CA B CA A1347 1555 1555 2.48
LINK OD2BASP A 256 CA B CA A1347 1555 1555 2.55
LINK O AASN A 258 CA A CA A1347 1555 1555 2.38
LINK O BASN A 258 CA B CA A1347 1555 1555 2.44
LINK OD1AASN A 261 CA A CA A1347 1555 1555 2.37
LINK OD1BASN A 261 CA B CA A1347 1555 1555 2.45
LINK ND2AASN A 262 CA A CA A1347 1555 1555 2.41
LINK ND2BASN A 262 CA B CA A1347 1555 1555 2.40
LINK CA A CA A1347 O HOH A2385 1555 1555 2.68
LINK CA B CA A1347 O HOH A2385 1555 1555 2.35
LINK CA A CA A1347 O HOH A2405 1555 1555 2.54
LINK CA B CA A1347 O HOH A2405 1555 1555 2.58
LINK O ASN B 253 CA CA B1347 1555 1555 2.48
LINK OD2 ASP B 256 CA CA B1347 1555 1555 2.60
LINK OD1 ASP B 256 CA CA B1347 1555 1555 2.45
LINK O ASN B 258 CA CA B1347 1555 1555 2.41
LINK OD1 ASN B 261 CA CA B1347 1555 1555 2.40
LINK OD1 ASN B 262 CA CA B1347 1555 1555 2.37
LINK CA CA B1347 O HOH B2381 1555 1555 2.66
LINK CA CA B1347 O HOH B2389 1555 1555 2.48
LINK CA CA B1347 O HOH B2398 1555 1555 2.51
CISPEP 1 HIS A 79 ALA A 80 0 10.62
CISPEP 2 TYR A 220 PRO A 221 0 -5.08
CISPEP 3 HIS B 79 ALA B 80 0 6.45
CISPEP 4 HIS B 79 ALA B 80 0 6.37
CISPEP 5 TYR B 220 PRO B 221 0 -4.44
SITE 1 AC1 7 ASN A 253 ASP A 256 ASN A 258 ASN A 261
SITE 2 AC1 7 ASN A 262 HOH A2385 HOH A2405
SITE 1 AC2 8 ASN B 253 ASP B 256 ASN B 258 ASN B 261
SITE 2 AC2 8 ASN B 262 HOH B2381 HOH B2389 HOH B2398
SITE 1 AC3 7 SER A 86 ASP A 137 ARG A 139 ARG A 152
SITE 2 AC3 7 HOH A2170 HOH A2508 HOH A2509
SITE 1 AC4 1 ARG A 299
SITE 1 AC5 5 PHE B 130 ASP B 131 SER B 132 ALA B 188
SITE 2 AC5 5 HOH B2508
SITE 1 AC6 8 ASP B 137 ARG B 139 ARG B 146 GLN B 147
SITE 2 AC6 8 HOH B2252 HOH B2509 HOH B2510 HOH B2511
SITE 1 AC7 6 ALA B 270 VAL B 271 LEU B 276 ASN B 328
SITE 2 AC7 6 HOH B2417 HOH B2512
SITE 1 AC8 4 ARG B 168 HOH B2514 HOH B2515 HOH B2516
SITE 1 AC9 8 THR B 25 SER B 26 SER B 27 ALA B 28
SITE 2 AC9 8 ARG B 29 HOH B2045 HOH B2140 HOH B2517
SITE 1 BC1 5 GLY B 1 SER B 4 TYR B 337 HOH B2495
SITE 2 BC1 5 HOH B2518
SITE 1 BC2 7 TYR A 52 GLY A 54 PRO A 90 ASN A 91
SITE 2 BC2 7 TRP A 92 HOH B2391 HOH B2519
CRYST1 95.343 95.343 150.273 90.00 90.00 90.00 P 43 21 2 16
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 0.010488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010488 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006655 0.00000
MTRIX1 1 0.997000 -0.056000 0.050000 7.74292 1
MTRIX2 1 0.060000 0.183000 -0.981000 68.86922 1
MTRIX3 1 0.045000 0.982000 0.186000 -30.29871 1
(ATOM LINES ARE NOT SHOWN.)
END
