HEADER CARBOHYDRATE BINDING MODULE 27-JAN-02 1GUI
TITLE CBM4 STRUCTURE AND FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMINARINASE 16A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 488-642;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 8 OTHER_DETAILS: CARBOHYDRATE BINDING MODULE OF LAMINARINASE 16A FROM
SOURCE 9 THERMOTOGA MARITIMA
KEYWDS CARBOHYDRATE BINDING MODULE, CBM, GLUCAN, CELLULOSE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NURIZZO,V.NOTENBOOM,G.J.DAVIES
REVDAT 5 13-DEC-23 1GUI 1 HETSYN
REVDAT 4 29-JUL-20 1GUI 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 1GUI 1 VERSN
REVDAT 2 24-FEB-09 1GUI 1 VERSN
REVDAT 1 26-SEP-02 1GUI 0
JRNL AUTH A.B.BORASTON,D.NURIZZO,V.NOTENBOOM,V.DUCROS,D.R.ROSE,
JRNL AUTH 2 D.G.KILBURN,G.J.DAVIES
JRNL TITL DIFFERENTIAL OLIGOSACCHARIDE RECOGNITION BY
JRNL TITL 2 EVOLUTIONARILY-RELATED BETA-1,4 AND BETA-1,3 GLUCAN-BINDING
JRNL TITL 3 MODULES
JRNL REF J.MOL.BIOL. V. 319 1143 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12079353
JRNL DOI 10.1016/S0022-2836(02)00374-1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.07
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23897
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1688
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1252
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.62000
REMARK 3 B22 (A**2) : -2.62000
REMARK 3 B33 (A**2) : 3.93000
REMARK 3 B12 (A**2) : -1.31000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.039
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1387 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1129 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1895 ; 1.593 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2624 ; 1.420 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 154 ; 6.833 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;32.865 ;25.070
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 178 ;11.387 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;12.944 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 214 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1483 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 279 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 204 ; 0.347 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1146 ; 0.256 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 615 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 66 ; 0.179 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.220 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 1 ; 0.228 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 17 ; 0.416 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.154 ; 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): 772 ; 0.717 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1260 ; 1.240 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 615 ; 2.160 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 635 ; 3.326 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 43.1520 13.4200 3.2350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.0868
REMARK 3 T33: 0.0095 T12: 0.0203
REMARK 3 T13: -0.0277 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.6626 L22: 4.4568
REMARK 3 L33: 1.5668 L12: 0.4451
REMARK 3 L13: -0.1022 L23: -0.2185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: 0.0852 S13: 0.0618
REMARK 3 S21: -0.2704 S22: 0.0111 S23: 0.2769
REMARK 3 S31: -0.0453 S32: -0.1173 S33: 0.0125
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1GUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1290009328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
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) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25221
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BEAST
REMARK 200 STARTING MODEL: PDB ENTRY 1GU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE 100MM SODIUM
REMARK 280 ACETATE PH4.6, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.09067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.54533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 16.54533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.09067
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 CARBOHYDRATE BINDING MODULE FAMILY 4
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 O3 BGC B 1 O5 BGC B 2 2.06
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 ASN A 20 57.92 -143.57
REMARK 500 GLU A 141 -47.93 76.45
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 200 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 8 O
REMARK 620 2 GLY A 47 O 80.8
REMARK 620 3 ASP A 150 OD1 88.1 79.6
REMARK 620 4 ASP A 150 OD2 129.8 75.5 44.6
REMARK 620 5 HOH A2004 O 87.3 108.7 169.7 142.2
REMARK 620 6 HOH A2096 O 163.0 86.9 101.3 56.9 85.5
REMARK 620 7 HOH A2099 O 98.1 167.3 87.7 96.0 83.9 96.4
REMARK 620 N 1 2 3 4 5 6
DBREF 1GUI A 3 157 UNP Q9WXN1 Q9WXN1 488 642
SEQRES 1 A 155 SER ILE ASN ASN GLY THR PHE ASP GLU PRO ILE VAL ASN
SEQRES 2 A 155 ASP GLN ALA ASN ASN PRO ASP GLU TRP PHE ILE TRP GLN
SEQRES 3 A 155 ALA GLY ASP TYR GLY ILE SER GLY ALA ARG VAL SER ASP
SEQRES 4 A 155 TYR GLY VAL ARG ASP GLY TYR ALA TYR ILE THR ILE ALA
SEQRES 5 A 155 ASP PRO GLY THR ASP THR TRP HIS ILE GLN PHE ASN GLN
SEQRES 6 A 155 TRP ILE GLY LEU TYR ARG GLY LYS THR TYR THR ILE SER
SEQRES 7 A 155 PHE LYS ALA LYS ALA ASP THR PRO ARG PRO ILE ASN VAL
SEQRES 8 A 155 LYS ILE LEU GLN ASN HIS ASP PRO TRP THR ASN TYR PHE
SEQRES 9 A 155 ALA GLN THR VAL ASN LEU THR ALA ASP TRP GLN THR PHE
SEQRES 10 A 155 THR PHE THR TYR THR HIS PRO ASP ASP ALA ASP GLU VAL
SEQRES 11 A 155 VAL GLN ILE SER PHE GLU LEU GLY GLU GLY THR ALA THR
SEQRES 12 A 155 THR ILE TYR PHE ASP ASP VAL THR VAL SER PRO GLN
HET BGC B 1 12
HET BGC B 2 11
HET BGC B 3 11
HET BGC B 4 11
HET BGC B 5 11
HET BGC B 6 11
HET CA A 200 1
HET GOL A 300 6
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 BGC 6(C6 H12 O6)
FORMUL 3 CA CA 2+
FORMUL 4 GOL 5(C3 H8 O3)
FORMUL 9 HOH *111(H2 O)
HELIX 1 1 GLY A 30 GLY A 33 5 4
HELIX 2 2 ASP A 59 TRP A 61 5 3
SHEET 1 AA 5 PHE A 25 GLN A 28 0
SHEET 2 AA 5 ILE A 63 GLY A 70 -1 O GLN A 64 N TRP A 27
SHEET 3 AA 5 VAL A 132 GLU A 138 -1 O VAL A 133 N ILE A 69
SHEET 4 AA 5 ARG A 89 LEU A 96 -1 O ASN A 92 N GLU A 138
SHEET 5 AA 5 ASN A 104 LEU A 112 -1 N TYR A 105 O ILE A 95
SHEET 1 AB 5 ARG A 38 ARG A 45 0
SHEET 2 AB 5 TYR A 48 ASP A 55 -1 O TYR A 48 N ARG A 45
SHEET 3 AB 5 THR A 146 PRO A 156 -1 O ILE A 147 N ILE A 51
SHEET 4 AB 5 THR A 76 ALA A 85 -1 O THR A 78 N SER A 155
SHEET 5 AB 5 GLN A 117 THR A 124 -1 O GLN A 117 N ALA A 83
LINK O3 BGC B 1 C1 BGC B 2 1555 1555 1.54
LINK O3 BGC B 2 C1 BGC B 3 1555 1555 1.46
LINK O3 BGC B 3 C1 BGC B 4 1555 1555 1.64
LINK O3 BGC B 4 C1 BGC B 5 1555 1555 1.70
LINK O3 BGC B 5 C1 BGC B 6 1555 1555 1.71
LINK O THR A 8 CA CA A 200 1555 1555 2.27
LINK O GLY A 47 CA CA A 200 1555 1555 2.21
LINK OD1 ASP A 150 CA CA A 200 1555 1555 2.40
LINK OD2 ASP A 150 CA CA A 200 1555 1555 3.02
LINK CA CA A 200 O HOH A2004 1555 1555 2.30
LINK CA CA A 200 O HOH A2096 1555 1555 2.33
LINK CA CA A 200 O HOH A2099 1555 1555 1.97
CISPEP 1 ASP A 100 PRO A 101 0 11.02
CRYST1 105.117 105.117 49.636 90.00 90.00 120.00 P 32 2 1 6
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 0.009513 0.005492 0.000000 0.00000
SCALE2 0.000000 0.010985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020147 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
