HEADER CELL ADHESION 31-JAN-08 2VN6
TITLE THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL
TITLE 2 BINDING MODE FOR ITS COHESIN PARTNER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCAFFOLDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 277-427;
COMPND 5 SYNONYM: COHESIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ENDOGLUCANASE A;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 410-473;
COMPND 11 SYNONYM: DOCKERIN, ENDO-1,4-BETA-GLUCANASE A, EGCCA,
COMPND 12 CELLULASE A;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM CELLULOLYTICUM;
SOURCE 3 ORGANISM_TAXID: 1521;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PET22B;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: CLOSTRIDIUM CELLULOLYTICUM;
SOURCE 9 ORGANISM_TAXID: 1521;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET22B
KEYWDS CELL ADHESION, CARBOHYDRATE METABOLISM, POLYSACCHARIDE
KEYWDS 2 DEGRADATION, HYDROLASE, GLYCOSIDASE, CELLULOSE DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.PINHEIRO,J.A.M.PRATES,M.R.PROCTOR,H.J.GILBERT,
AUTHOR 2 G.J.DAVIES,V.A.MONEY,C.MARTINEZ-FLEITES,E.A.BAYER,
AUTHOR 3 C.M.G.A.FONTES,H.P.FIEROBE
REVDAT 3 24-FEB-09 2VN6 1 VERSN
REVDAT 2 01-JUL-08 2VN6 1 JRNL
REVDAT 1 13-MAY-08 2VN6 0
JRNL AUTH B.A.PINHEIRO,M.R.PROCTOR,C.MARTINEZ-FLEITES,
JRNL AUTH 2 J.A.M.PRATES,V.A.MONEY,G.J.DAVIES,E.A.BAYER,
JRNL AUTH 3 C.M.G.A.FONTES,H.P.FIEROBE,H.J.GILBERT
JRNL TITL THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A
JRNL TITL 2 DUAL BINDING MODE FOR ITS COHESIN PARTNER.
JRNL REF J.BIOL.CHEM. V. 283 18422 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18445585
JRNL DOI 10.1074/JBC.M801533200
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0062
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 37165
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2321
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 329
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.693
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1640 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2233 ; 1.274 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 8.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 59 ;32.343 ;26.780
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 278 ; 9.677 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 275 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1195 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1074 ; 0.737 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1743 ; 1.206 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 566 ; 1.877 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 486 ; 2.795 ; 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 : 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 : 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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-08.
REMARK 100 THE PDBE ID CODE IS EBI-34936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39149
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.49
REMARK 200 RESOLUTION RANGE LOW (A) : 39.19
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.30
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 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 19.64550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.36250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.23800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.36250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.64550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.23800
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.6 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ALA 424 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LEU 425 TO THR
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 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 ILE A 93 -39.94 70.98
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 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 B1066 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 42 OD1
REMARK 620 2 ASP B 38 OD1 80.8
REMARK 620 3 ASN B 40 OD1 79.3 80.3
REMARK 620 4 GLU B 44 O 83.9 81.7 157.0
REMARK 620 5 ASP B 49 OD1 159.0 96.9 79.8 116.6
REMARK 620 6 ASP B 49 OD2 142.9 128.1 123.5 79.1 52.5
REMARK 620 7 HOH B2069 O 76.9 154.1 82.7 108.7 99.1 77.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1067 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 13 O
REMARK 620 2 ASP B 7 OD1 78.6
REMARK 620 3 ASP B 18 OD1 120.4 93.0
REMARK 620 4 ASP B 18 OD2 78.5 117.0 53.2
REMARK 620 5 ASN B 9 OD1 155.9 84.5 77.2 124.9
REMARK 620 6 ASP B 11 OD1 81.1 86.8 158.1 144.3 80.9
REMARK 620 7 HOH B2030 O 105.9 164.6 97.0 78.4 86.4 79.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1066
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1067
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G1K RELATED DB: PDB
REMARK 900 COHESIN MODULE FROM THE CELLULOSOME OF
REMARK 900 CLOSTRIDIUMCELLULOLYTICUM
REMARK 900 RELATED ID: 1EDG RELATED DB: PDB
REMARK 900 SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE
REMARK 900 CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT
REMARK 900 15 DEGREE C
REMARK 900 RELATED ID: 1G43 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A FAMILY IIIA CBD
REMARK 900 FROM CLOSTRIDIUMCELLULOLYTICUM
REMARK 900 RELATED ID: 1EHX RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN
REMARK 900 MODULE OF THECELLULOSOMAL SCAFFOLDIN PROTEIN
REMARK 900 CIPC OF CLOSTRIDUMCELLULOLYTICUM
REMARK 900 RELATED ID: 2VN5 RELATED DB: PDB
REMARK 900 THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS
REMARK 900 A DUAL BINDING MODE FOR ITS COHESIN
REMARK 900 PARTNER
DBREF 2VN6 A 2 152 UNP Q45996 Q45996_CLOCE 277 427
DBREF 2VN6 B 2 65 UNP P17901 GUNA_CLOCE 410 473
SEQADV 2VN6 SER B 16 UNP P17901 ALA 424 ENGINEERED MUTATION
SEQADV 2VN6 THR B 17 UNP P17901 LEU 425 ENGINEERED MUTATION
SEQADV 2VN6 GLU B 65 UNP P17901 PRO 473 CONFLICT
SEQRES 1 A 151 THR VAL LEU PRO LYS ASP ILE PRO GLY ASP SER LEU LYS
SEQRES 2 A 151 VAL THR VAL GLY THR ALA ASN GLY LYS PRO GLY ASP THR
SEQRES 3 A 151 VAL THR VAL PRO VAL THR PHE ALA ASP VAL ALA LYS MET
SEQRES 4 A 151 LYS ASN VAL GLY THR CYS ASN PHE TYR LEU GLY TYR ASP
SEQRES 5 A 151 ALA SER LEU LEU GLU VAL VAL SER VAL ASP ALA GLY PRO
SEQRES 6 A 151 ILE VAL LYS ASN ALA ALA VAL ASN PHE SER SER SER ALA
SEQRES 7 A 151 SER ASN GLY THR ILE SER PHE LEU PHE LEU ASP ASN THR
SEQRES 8 A 151 ILE THR ASP GLU LEU ILE THR ALA ASP GLY VAL PHE ALA
SEQRES 9 A 151 ASN ILE LYS PHE LYS LEU LYS SER VAL THR ALA LYS THR
SEQRES 10 A 151 THR THR PRO VAL THR PHE LYS ASP GLY GLY ALA PHE GLY
SEQRES 11 A 151 ASP GLY THR MET SER LYS ILE ALA SER VAL THR LYS THR
SEQRES 12 A 151 ASN GLY SER VAL THR ILE ASP PRO
SEQRES 1 B 64 VAL ILE VAL TYR GLY ASP TYR ASN ASN ASP GLY ASN VAL
SEQRES 2 B 64 ASP SER THR ASP PHE ALA GLY LEU LYS LYS TYR ILE MET
SEQRES 3 B 64 ALA ALA ASP HIS ALA TYR VAL LYS ASN LEU ASP VAL ASN
SEQRES 4 B 64 LEU ASP ASN GLU VAL ASN ALA PHE ASP LEU ALA ILE LEU
SEQRES 5 B 64 LYS LYS TYR LEU LEU GLY MET VAL SER LYS LEU GLU
HET CA B1066 1
HET CA B1067 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 HOH *329(H2 O1)
HELIX 1 1 LEU A 4 ILE A 8 5 5
HELIX 2 2 ASN A 70 ASN A 74 1 5
HELIX 3 3 ASP B 15 ALA B 28 1 14
HELIX 4 4 VAL B 34 ASP B 38 5 5
HELIX 5 5 ASN B 46 LEU B 58 1 13
SHEET 1 AA 5 LEU A 57 ALA A 64 0
SHEET 2 AA 5 GLY A 102 LEU A 111 -1 O ASN A 106 N ASP A 63
SHEET 3 AA 5 THR A 27 ALA A 35 -1 O VAL A 28 N PHE A 109
SHEET 4 AA 5 LEU A 13 VAL A 17 -1 O LYS A 14 N ALA A 35
SHEET 5 AA 5 VAL A 141 THR A 144 1 O THR A 142 N VAL A 15
SHEET 1 AB 6 THR A 19 GLY A 22 0
SHEET 2 AB 6 GLY A 146 ILE A 150 1 O SER A 147 N ALA A 20
SHEET 3 AB 6 THR A 118 GLY A 131 -1 O THR A 118 N ILE A 150
SHEET 4 AB 6 THR A 45 GLY A 51 -1 O THR A 45 N GLY A 131
SHEET 5 AB 6 THR A 83 LEU A 89 -1 O ILE A 84 N LEU A 50
SHEET 6 AB 6 PHE A 75 SER A 80 -1 O SER A 76 N LEU A 87
LINK CA CA B1066 OD1 ASP B 42 1555 1555 2.40
LINK CA CA B1066 OD1 ASP B 38 1555 1555 2.38
LINK CA CA B1066 OD1 ASN B 40 1555 1555 2.36
LINK CA CA B1066 O GLU B 44 1555 1555 2.36
LINK CA CA B1066 OD1 ASP B 49 1555 1555 2.50
LINK CA CA B1066 OD2 ASP B 49 1555 1555 2.46
LINK CA CA B1066 O HOH B2069 1555 1555 2.44
LINK CA CA B1067 OD1 ASP B 7 1555 1555 2.41
LINK CA CA B1067 OD1 ASP B 18 1555 1555 2.46
LINK CA CA B1067 OD2 ASP B 18 1555 1555 2.43
LINK CA CA B1067 OD1 ASN B 9 1555 1555 2.34
LINK CA CA B1067 OD1 ASP B 11 1555 1555 2.41
LINK CA CA B1067 O HOH B2030 1555 1555 2.39
LINK CA CA B1067 O ASN B 13 1555 1555 2.38
SITE 1 AC1 6 ASP B 38 ASN B 40 ASP B 42 GLU B 44
SITE 2 AC1 6 ASP B 49 HOH B2069
SITE 1 AC2 6 ASP B 7 ASN B 9 ASP B 11 ASN B 13
SITE 2 AC2 6 ASP B 18 HOH B2030
CRYST1 39.291 60.476 100.725 90.00 90.00 90.00 P 21 21 21 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 0.025451 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016535 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009928 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
