HEADER HYDROLASE 16-MAR-09 2WCS
TITLE CRYSTAL STRUCTURE OF DEBRANCHING ENZYME FROM NOSTOC PUNCTIFORME (NPDE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA AMYLASE, CATALYTIC REGION;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NOSTOC PUNCTIFORME DEBRANCHING ENZYME;
COMPND 5 EC: 3.2.1.54;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC PUNCTIFORME;
SOURCE 3 ORGANISM_TAXID: 272131;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MALTOOLIGOSACCHARIDES, HYDROLASE, GLYCOSIDASE, CYANOBACTERIA
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.DUMBREPATIL,J.H.CHOI,S.H.NAM,K.H.PARK,E.J.WOO
REVDAT 3 13-DEC-23 2WCS 1 REMARK
REVDAT 2 22-JUN-11 2WCS 1 KEYWDS JRNL REMARK FORMUL
REVDAT 1 29-SEP-09 2WCS 0
JRNL AUTH A.B.DUMBREPATIL,J.H.CHOI,J.T.PARK,M.J.KIM,T.J.KIM,E.J.WOO,
JRNL AUTH 2 K.H.PARK
JRNL TITL STRUCTURAL FEATURES OF THE NOSTOC PUNCTIFORME DEBRANCHING
JRNL TITL 2 ENZYME REVEAL THE BASIS OF ITS MECHANISM AND SUBSTRATE
JRNL TITL 3 SPECIFICITY.
JRNL REF PROTEINS V. 78 348 2010
JRNL REFN ISSN 0887-3585
JRNL PMID 19768689
JRNL DOI 10.1002/PROT.22548
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 16274
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 SET) : 0.224
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 785
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2333
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 90
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 86.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.02000
REMARK 3 B22 (A**2) : 12.02000
REMARK 3 B33 (A**2) : -24.04000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 47.20
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2WCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1290039063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.80
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 23.90
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.200
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: PDB ENTRY 2WC7
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V)POLYETHYLENE GYLCOL, 200MM
REMARK 280 TRIC-CL (PH8.5),100MM MGCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 85.68067
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 171.36133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 128.52100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 214.20167
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 42.84033
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 85.68067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 171.36133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 214.20167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 128.52100
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 42.84033
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: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.8 KCAL/MOL
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 BIOMT1 2 0.500000 -0.866025 0.000000 46.86550
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 81.17343
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -42.84033
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 ASP A 488
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 1 CG SD CE
REMARK 470 LEU A 376 N CA C CB CG CD1 CD2
REMARK 470 GLY A 487 CA C O
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 GLU A 154 O ASN A 168 2.18
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 LYS A 26 -81.37 -104.35
REMARK 500 LYS A 30 67.93 -69.43
REMARK 500 LYS A 51 -68.26 -107.03
REMARK 500 THR A 76 -169.11 -72.07
REMARK 500 ASN A 84 43.92 37.05
REMARK 500 HIS A 85 31.54 -150.64
REMARK 500 ARG A 86 -19.06 -43.90
REMARK 500 SER A 128 -125.37 -124.87
REMARK 500 ASN A 149 35.81 -84.71
REMARK 500 ASN A 162 -86.78 -48.00
REMARK 500 ASN A 168 46.85 -83.68
REMARK 500 TRP A 172 117.96 -39.00
REMARK 500 LEU A 178 67.49 -112.76
REMARK 500 ASN A 182 77.82 -103.53
REMARK 500 ASN A 185 109.55 -52.20
REMARK 500 PHE A 220 -76.26 -51.33
REMARK 500 GLN A 253 -97.13 -126.37
REMARK 500 ASN A 259 83.19 -68.48
REMARK 500 GLN A 281 -1.01 69.48
REMARK 500 SER A 282 32.16 -93.60
REMARK 500 GLN A 286 77.45 -114.58
REMARK 500 PRO A 287 32.08 -81.30
REMARK 500 GLN A 305 54.55 -108.34
REMARK 500 LEU A 362 131.94 -37.18
REMARK 500 ASP A 367 -168.36 -118.67
REMARK 500 ALA A 378 77.50 -109.99
REMARK 500 ASN A 379 20.48 84.53
REMARK 500 ALA A 411 79.49 -167.06
REMARK 500 THR A 449 -161.79 -129.38
REMARK 500 TYR A 456 147.89 178.33
REMARK 500 THR A 458 79.62 37.64
REMARK 500 GLU A 460 -168.25 -120.90
REMARK 500 ALA A 461 76.99 45.41
REMARK 500 ASN A 464 -141.51 -105.36
REMARK 500 THR A 486 -58.96 71.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 166 ALA A 167 135.68
REMARK 500 VAL A 280 GLN A 281 45.58
REMARK 500 SER A 282 ARG A 283 145.79
REMARK 500 ILE A 366 ASP A 367 147.44
REMARK 500 ASP A 367 PRO A 368 -51.92
REMARK 500 ASP A 369 SER A 370 147.31
REMARK 500 ARG A 371 ARG A 372 106.52
REMARK 500 PHE A 374 PRO A 375 -117.34
REMARK 500 GLU A 377 ALA A 378 -138.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WC7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NOSTOC PUNCTIFORME DEBRANCHING ENZYME(NPDE)
REMARK 900 (ACARBOSE SOAKED)
REMARK 900 RELATED ID: 2WKG RELATED DB: PDB
REMARK 900 NOSTOC PUNCTIFORME DEBRANCHING ENZYME (NPDE) (NATIVE FORM)
DBREF 2WCS A 1 488 UNP B2IUW9 B2IUW9_NOSP7 1 488
SEQRES 1 A 488 MET GLN ILE GLN THR PRO ASP TRP VAL LYS HIS ALA VAL
SEQRES 2 A 488 PHE TYR GLN ILE PHE PRO ASP ARG PHE ALA ARG SER LYS
SEQRES 3 A 488 GLN PRO ARG LYS ARG LEU LEU GLN GLU ALA ARG TRP GLU
SEQRES 4 A 488 ASP TRP ASP SER MET PRO THR LEU GLN GLY TYR LYS GLY
SEQRES 5 A 488 GLY ASP LEU TRP GLY ILE MET GLU ASP LEU ASP TYR ILE
SEQRES 6 A 488 GLN ASN LEU GLY ILE ASN ALA ILE TYR PHE THR PRO ILE
SEQRES 7 A 488 PHE GLN SER ALA SER ASN HIS ARG TYR HIS THR HIS ASP
SEQRES 8 A 488 TYR TYR GLN VAL ASP PRO MET LEU GLY GLY ASN GLU ALA
SEQRES 9 A 488 PHE LYS GLU LEU LEU ASP ALA ALA HIS GLN ARG ASN ILE
SEQRES 10 A 488 LYS VAL VAL LEU ASP GLY VAL PHE ASN HIS SER SER ARG
SEQRES 11 A 488 GLY PHE PHE PHE PHE HIS ASP VAL LEU GLU ASN GLY PRO
SEQRES 12 A 488 HIS SER PRO TRP VAL ASN TRP PHE LYS ILE GLU GLY TRP
SEQRES 13 A 488 PRO LEU SER PRO TYR ASN GLY GLU PHE PRO ALA ASN TYR
SEQRES 14 A 488 VAL GLY TRP ALA GLY ASN ARG ALA LEU PRO GLU PHE ASN
SEQRES 15 A 488 HIS ASP ASN PRO GLU VAL ARG GLU TYR ILE MET GLU ILE
SEQRES 16 A 488 ALA GLU TYR TRP LEU LYS PHE GLY ILE ASP GLY TRP ARG
SEQRES 17 A 488 LEU ASP VAL PRO PHE GLU ILE LYS THR PRO GLY PHE TRP
SEQRES 18 A 488 GLN GLU PHE ARG ASP ARG THR LYS ALA ILE ASN PRO GLU
SEQRES 19 A 488 ALA TYR ILE VAL GLY GLU VAL TRP GLY ASP SER ARG GLN
SEQRES 20 A 488 TRP LEU ASP GLY THR GLN PHE ASP GLY VAL MET ASN TYR
SEQRES 21 A 488 LEU PHE ALA GLY PRO THR ILE ALA PHE ALA ALA GLY ASP
SEQRES 22 A 488 ARG VAL VAL LEU GLU GLN VAL GLN SER ARG ASP TYR GLN
SEQRES 23 A 488 PRO TYR PRO PRO LEU PHE ALA ALA GLU TYR ALA THR LYS
SEQRES 24 A 488 ILE GLN GLU VAL LEU GLN LEU TYR PRO TRP GLU ILE GLN
SEQRES 25 A 488 LEU THR GLN LEU ASN LEU LEU ALA SER HIS ASP THR ALA
SEQRES 26 A 488 ARG LEU MET THR ILE ALA GLY GLY ASP ILE ALA SER VAL
SEQRES 27 A 488 GLU LEU SER THR LEU LEU LEU LEU THR PHE PRO GLY ALA
SEQRES 28 A 488 PRO SER ILE TYR TYR GLY ASP GLU VAL GLY LEU PRO GLY
SEQRES 29 A 488 GLY ILE ASP PRO ASP SER ARG ARG GLY PHE PRO LEU GLU
SEQRES 30 A 488 ALA ASN TRP ASN GLN GLU ILE PHE ASN THR HIS ARG GLN
SEQRES 31 A 488 LEU ILE THR ILE ARG GLN THR TYR PRO ALA LEU ARG THR
SEQRES 32 A 488 GLY ASP TYR GLN VAL LEU TYR ALA GLN GLY GLN LEU TYR
SEQRES 33 A 488 LEU PHE ALA ARG THR LEU GLY THR GLU GLU LEU ILE ILE
SEQRES 34 A 488 ALA ILE ASN ALA GLY THR SER SER ALA THR ALA ASN VAL
SEQRES 35 A 488 ASP VAL ALA SER LEU HIS THR GLN PRO ASN LYS LEU LEU
SEQRES 36 A 488 TYR GLY THR ALA GLU ALA GLU TRP ASN GLY GLU GLU GLY
SEQRES 37 A 488 THR GLN GLN LEU SER LEU THR LEU PRO ALA ARG SER GLY
SEQRES 38 A 488 CYS ILE LEU GLY THR GLY ASP
FORMUL 2 HOH *46(H2 O)
HELIX 1 1 TRP A 8 ALA A 12 5 5
HELIX 2 2 PHE A 18 PHE A 22 5 5
HELIX 3 3 ASP A 40 SER A 43 5 4
HELIX 4 4 MET A 44 GLY A 49 1 6
HELIX 5 5 ASP A 54 ASP A 61 1 8
HELIX 6 6 ASP A 61 GLY A 69 1 9
HELIX 7 7 PRO A 97 LEU A 99 5 3
HELIX 8 8 GLY A 100 ARG A 115 1 16
HELIX 9 9 PHE A 132 GLY A 142 1 11
HELIX 10 10 PRO A 143 SER A 145 5 3
HELIX 11 11 TRP A 147 TRP A 150 5 4
HELIX 12 12 TRP A 172 ASN A 175 5 4
HELIX 13 13 ASN A 185 GLY A 203 1 19
HELIX 14 14 GLY A 219 ASN A 232 1 14
HELIX 15 15 SER A 245 LEU A 249 5 5
HELIX 16 16 ASN A 259 ALA A 271 1 13
HELIX 17 17 GLY A 272 VAL A 275 5 4
HELIX 18 18 PHE A 292 GLN A 305 1 14
HELIX 19 19 PRO A 308 LEU A 313 1 6
HELIX 20 20 ARG A 326 ALA A 331 1 6
HELIX 21 21 ASP A 334 LEU A 346 1 13
HELIX 22 22 GLY A 357 GLY A 361 5 5
HELIX 23 23 ASN A 381 TYR A 398 1 18
HELIX 24 24 PRO A 399 GLY A 404 1 6
SHEET 1 AA 8 GLY A 256 VAL A 257 0
SHEET 2 AA 8 TYR A 236 GLU A 240 1 N GLY A 239 O GLY A 256
SHEET 3 AA 8 GLY A 206 ASP A 210 1 O TRP A 207 N VAL A 238
SHEET 4 AA 8 LYS A 118 GLY A 123 1 O LEU A 121 N ARG A 208
SHEET 5 AA 8 ALA A 72 PHE A 75 1 O ILE A 73 N VAL A 120
SHEET 6 AA 8 PHE A 14 ILE A 17 1 O TYR A 15 N TYR A 74
SHEET 7 AA 8 ALA A 351 TYR A 355 1 O PRO A 352 N PHE A 14
SHEET 8 AA 8 LEU A 316 ASN A 317 1 O ASN A 317 N SER A 353
SHEET 1 AB 2 PHE A 79 SER A 81 0
SHEET 2 AB 2 THR A 89 VAL A 95 -1 N HIS A 90 O GLN A 80
SHEET 1 AC 5 ASP A 405 GLN A 412 0
SHEET 2 AC 5 LEU A 415 LEU A 422 -1 O LEU A 415 N GLN A 412
SHEET 3 AC 5 GLU A 425 ASN A 432 -1 O GLU A 425 N LEU A 422
SHEET 4 AC 5 SER A 480 GLY A 485 -1 O SER A 480 N ASN A 432
SHEET 5 AC 5 LYS A 453 TYR A 456 -1 O LYS A 453 N GLY A 485
SHEET 1 AD 3 ALA A 438 VAL A 442 0
SHEET 2 AD 3 LEU A 472 LEU A 476 -1 O LEU A 472 N VAL A 442
SHEET 3 AD 3 GLU A 460 TRP A 463 -1 O GLU A 460 N THR A 475
CISPEP 1 TRP A 156 PRO A 157 0 -0.01
CISPEP 2 TYR A 288 PRO A 289 0 -0.12
CISPEP 3 ALA A 378 ASN A 379 0 -8.15
CRYST1 93.731 93.731 257.042 90.00 90.00 120.00 P 61 2 2 12
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 0.010669 0.006160 0.000000 0.00000
SCALE2 0.000000 0.012319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003890 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
