HEADER HYDROLASE 26-MAY-99 1QPK
TITLE MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
TITLE 2 MALTOTETRAOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (MALTOTETRAOSE-FORMING AMYLASE);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI;
SOURCE 3 ORGANISM_TAXID: 316;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PUC18
KEYWDS BETA-ALPHA-BARRELS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA
REVDAT 5 03-NOV-21 1QPK 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 1QPK 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 FORMUL LINK SITE ATOM
REVDAT 3 04-OCT-17 1QPK 1 REMARK
REVDAT 2 24-FEB-09 1QPK 1 VERSN
REVDAT 1 17-NOV-99 1QPK 0
JRNL AUTH K.HASEGAWA,M.KUBOTA,Y.MATSUURA
JRNL TITL ROLES OF CATALYTIC RESIDUES IN ALPHA-AMYLASES AS EVIDENCED
JRNL TITL 2 BY THE STRUCTURES OF THE PRODUCT-COMPLEXED MUTANTS OF A
JRNL TITL 3 MALTOTETRAOSE-FORMING AMYLASE.
JRNL REF PROTEIN ENG. V. 12 819 1999
JRNL REFN ISSN 0269-2139
JRNL PMID 10556241
JRNL DOI 10.1093/PROTEIN/12.10.819
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA
REMARK 1 TITL CRYSTAL STRUCTURES OF A MUTANT MALTOTETRAOSE-FORMING
REMARK 1 TITL 2 EXO-AMYLASE COCRYSTALLIZED WITH MALTOPENTAOSE
REMARK 1 REF J.MOL.BIOL. V. 271 619 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1997.1222
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.MORISHITA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA
REMARK 1 TITL CRYSTAL STRUCTURE OF A MALTOTETRAOSE-FORMING EXO-AMYLASE
REMARK 1 TITL 2 FROM PSEUDOMONAS STUTZERI
REMARK 1 REF J.MOL.BIOL. V. 267 661 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1996.0887
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.034 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000009117.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-HCL, PH 7.5
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.60500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.36000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.36000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.60500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.75000
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: MONOMERIC
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 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 OD2 ASP A 334 OD1 ASP A 338 1.93
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 ASP A 82 CA ASP A 82 CB 0.153
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 11 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 16 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 82 CB - CA - C ANGL. DEV. = -14.6 DEGREES
REMARK 500 ASP A 82 CA - CB - CG ANGL. DEV. = -17.3 DEGREES
REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 82 CB - CG - OD2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 TYR A 122 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 CYS A 140 CA - CB - SG ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 152 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 212 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TYR A 227 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 279 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 279 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ASP A 343 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 346 CD - NE - CZ ANGL. DEV. = 56.3 DEGREES
REMARK 500 ARG A 346 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 353 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 358 NH1 - CZ - NH2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 358 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 360 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 417 NE - CZ - NH1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 417 NE - CZ - NH2 ANGL. DEV. = -6.3 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 HIS A 13 70.37 36.63
REMARK 500 ASN A 33 17.86 51.54
REMARK 500 ASN A 148 -169.83 -129.43
REMARK 500 ASP A 151 108.95 -168.97
REMARK 500 ILE A 157 -111.95 57.39
REMARK 500 ALA A 211 63.26 -168.67
REMARK 500 LYS A 222 113.76 -161.47
REMARK 500 GLN A 301 119.32 -38.86
REMARK 500 TRP A 308 64.36 -159.12
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 452 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 1 OD2
REMARK 620 2 GLN A 2 O 75.9
REMARK 620 3 HIS A 13 O 160.2 84.4
REMARK 620 4 HIS A 13 ND1 95.9 87.1 80.5
REMARK 620 5 ASP A 16 OD2 99.6 89.2 82.3 162.7
REMARK 620 6 GLU A 17 OE1 98.6 164.5 99.8 79.0 106.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 451 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 116 OD1
REMARK 620 2 ASP A 151 OD1 164.5
REMARK 620 3 ASP A 151 OD2 139.3 49.0
REMARK 620 4 ASP A 154 O 103.5 82.8 104.3
REMARK 620 5 ASP A 162 OD1 85.4 81.1 126.5 84.1
REMARK 620 6 GLY A 197 O 78.4 116.4 74.1 86.9 159.1
REMARK 620 7 HOH A 553 O 75.4 97.1 78.9 175.4 91.4 97.2
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QI3 RELATED DB: PDB
REMARK 900 MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
REMARK 900 MALTOTETRAOSE
REMARK 900 RELATED ID: 1QI4 RELATED DB: PDB
REMARK 900 MUTANT (E219G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
REMARK 900 MALTOTETRAOSE
REMARK 900 RELATED ID: 1QI5 RELATED DB: PDB
REMARK 900 MUTANT (D294N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
REMARK 900 MALTOTETRAOSE
REMARK 900 RELATED ID: 2AMG RELATED DB: PDB
REMARK 900 MALTOTETRAOSE-FORMING EXO-AMYLASE
REMARK 900 RELATED ID: 1JDA RELATED DB: PDB
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE
REMARK 900 RELATED ID: 1JDC RELATED DB: PDB
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
REMARK 900 MALTOTETRAOSE (CRYSTAL TYPE 1)
REMARK 900 RELATED ID: 1JDD RELATED DB: PDB
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH
REMARK 900 MALTOTETRAOSE (CRYSTAL TYPE 2)
DBREF 1QPK A 1 418 UNP P13507 AMT4_PSEST 22 439
SEQADV 1QPK GLY A 193 UNP P13507 ASP 214 ENGINEERED MUTATION
SEQRES 1 A 418 ASP GLN ALA GLY LYS SER PRO ASN ALA VAL ARG TYR HIS
SEQRES 2 A 418 GLY GLY ASP GLU ILE ILE LEU GLN GLY PHE HIS TRP ASN
SEQRES 3 A 418 VAL VAL ARG GLU ALA PRO ASN ASP TRP TYR ASN ILE LEU
SEQRES 4 A 418 ARG GLN GLN ALA ALA THR ILE ALA ALA ASP GLY PHE SER
SEQRES 5 A 418 ALA ILE TRP MET PRO VAL PRO TRP ARG ASP PHE SER SER
SEQRES 6 A 418 TRP SER ASP GLY SER LYS SER GLY GLY GLY GLU GLY TYR
SEQRES 7 A 418 PHE TRP HIS ASP PHE ASN LYS ASN GLY ARG TYR GLY SER
SEQRES 8 A 418 ASP ALA GLN LEU ARG GLN ALA ALA SER ALA LEU GLY GLY
SEQRES 9 A 418 ALA GLY VAL LYS VAL LEU TYR ASP VAL VAL PRO ASN HIS
SEQRES 10 A 418 MET ASN ARG GLY TYR PRO ASP LYS GLU ILE ASN LEU PRO
SEQRES 11 A 418 ALA GLY GLN GLY PHE TRP ARG ASN ASP CYS ALA ASP PRO
SEQRES 12 A 418 GLY ASN TYR PRO ASN ASP CYS ASP ASP GLY ASP ARG PHE
SEQRES 13 A 418 ILE GLY GLY ASP ALA ASP LEU ASN THR GLY HIS PRO GLN
SEQRES 14 A 418 VAL TYR GLY MET PHE ARG ASP GLU PHE THR ASN LEU ARG
SEQRES 15 A 418 SER GLN TYR GLY ALA GLY GLY PHE ARG PHE GLY PHE VAL
SEQRES 16 A 418 ARG GLY TYR ALA PRO GLU ARG VAL ASN SER TRP MET THR
SEQRES 17 A 418 ASP SER ALA ASP ASN SER PHE CYS VAL GLY GLU LEU TRP
SEQRES 18 A 418 LYS GLY PRO SER GLU TYR PRO ASN TRP ASP TRP ARG ASN
SEQRES 19 A 418 THR ALA SER TRP GLN GLN ILE ILE LYS ASP TRP SER ASP
SEQRES 20 A 418 ARG ALA LYS CYS PRO VAL PHE ASP PHE ALA LEU LYS GLU
SEQRES 21 A 418 ARG MET GLN ASN GLY SER ILE ALA ASP TRP LYS HIS GLY
SEQRES 22 A 418 LEU ASN GLY ASN PRO ASP PRO ARG TRP ARG GLU VAL ALA
SEQRES 23 A 418 VAL THR PHE VAL ASP ASN HIS ASP THR GLY TYR SER PRO
SEQRES 24 A 418 GLY GLN ASN GLY GLY GLN HIS HIS TRP ALA LEU GLN ASP
SEQRES 25 A 418 GLY LEU ILE ARG GLN ALA TYR ALA TYR ILE LEU THR SER
SEQRES 26 A 418 PRO GLY THR PRO VAL VAL TYR TRP ASP HIS MET TYR ASP
SEQRES 27 A 418 TRP GLY TYR GLY ASP PHE ILE ARG GLN LEU ILE GLN VAL
SEQRES 28 A 418 ARG ARG ALA ALA GLY VAL ARG ALA ASP SER ALA ILE SER
SEQRES 29 A 418 PHE HIS SER GLY TYR SER GLY LEU VAL ALA THR VAL SER
SEQRES 30 A 418 GLY SER GLN GLN THR LEU VAL VAL ALA LEU ASN SER ASP
SEQRES 31 A 418 LEU GLY ASN PRO GLY GLN VAL ALA SER GLY SER PHE SER
SEQRES 32 A 418 GLU ALA VAL ASN ALA SER ASN GLY GLN VAL ARG VAL TRP
SEQRES 33 A 418 ARG SER
HET GLC B 1 12
HET GLC B 2 11
HET GLC B 3 11
HET GLC B 4 11
HET CA A 451 1
HET CA A 452 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 GLC 4(C6 H12 O6)
FORMUL 3 CA 2(CA 2+)
FORMUL 5 HOH *173(H2 O)
HELIX 1 1 TYR A 12 ASP A 16 5 5
HELIX 2 2 ASN A 26 ALA A 31 1 6
HELIX 3 3 ASP A 34 GLY A 50 1 17
HELIX 4 4 SER A 91 ALA A 105 1 15
HELIX 5 5 ARG A 137 CYS A 140 5 4
HELIX 6 6 HIS A 167 TYR A 185 1 19
HELIX 7 7 PHE A 194 TYR A 198 5 5
HELIX 8 8 ALA A 199 ALA A 211 1 13
HELIX 9 9 GLY A 223 TYR A 227 5 5
HELIX 10 10 ASP A 231 ALA A 236 5 6
HELIX 11 11 SER A 237 LYS A 250 1 14
HELIX 12 12 ASP A 255 GLY A 265 1 11
HELIX 13 13 SER A 266 GLY A 273 5 8
HELIX 14 14 GLY A 273 ASN A 277 5 5
HELIX 15 15 ASP A 279 GLU A 284 1 6
HELIX 16 16 GLY A 300 GLY A 304 5 5
HELIX 17 17 GLN A 311 GLY A 313 5 3
HELIX 18 18 LEU A 314 SER A 325 1 12
HELIX 19 19 TRP A 333 ASP A 338 1 6
HELIX 20 20 TYR A 341 GLY A 356 1 16
HELIX 21 21 ASN A 393 VAL A 397 5 5
HELIX 22 22 SER A 409 GLY A 411 5 3
SHEET 1 A 9 ILE A 19 GLN A 21 0
SHEET 2 A 9 ALA A 53 MET A 56 1 O ALA A 53 N LEU A 20
SHEET 3 A 9 ILE A 19 GLN A 21 1 O LEU A 20 N TRP A 55
SHEET 4 A 9 THR A 328 TYR A 332 1 O PRO A 329 N ILE A 19
SHEET 5 A 9 ALA A 286 THR A 288 1 O ALA A 286 N THR A 328
SHEET 6 A 9 VAL A 253 PHE A 254 1 O VAL A 253 N VAL A 287
SHEET 7 A 9 PHE A 215 GLY A 218 1 O GLY A 218 N PHE A 254
SHEET 8 A 9 ALA A 187 PHE A 192 1 O GLY A 188 N PHE A 215
SHEET 9 A 9 LYS A 108 VAL A 113 1 O VAL A 109 N GLY A 188
SHEET 1 B 2 TRP A 66 ASP A 68 0
SHEET 2 B 2 LYS A 71 GLY A 73 -1 O LYS A 71 N ASP A 68
SHEET 1 C 5 ALA A 362 HIS A 366 0
SHEET 2 C 5 LEU A 372 SER A 377 -1 O VAL A 373 N HIS A 366
SHEET 3 C 5 THR A 382 LEU A 387 -1 N LEU A 383 O VAL A 376
SHEET 4 C 5 VAL A 413 ARG A 417 -1 O ARG A 414 N ALA A 386
SHEET 5 C 5 SER A 403 ALA A 408 -1 N SER A 403 O ARG A 417
SSBOND 1 CYS A 140 CYS A 150 1555 1555 2.01
SSBOND 2 CYS A 216 CYS A 251 1555 1555 2.03
LINK O4 GLC B 1 C1 GLC B 2 1555 1555 1.38
LINK O4 GLC B 2 C1 GLC B 3 1555 1555 1.42
LINK O4 GLC B 3 C1 GLC B 4 1555 1555 1.42
LINK OD2 ASP A 1 CA CA A 452 1555 1555 1.99
LINK O GLN A 2 CA CA A 452 1555 1555 2.31
LINK O HIS A 13 CA CA A 452 1555 1555 2.19
LINK ND1 HIS A 13 CA CA A 452 1555 1555 2.45
LINK OD2 ASP A 16 CA CA A 452 1555 1555 2.27
LINK OE1 GLU A 17 CA CA A 452 1555 1555 2.20
LINK OD1 ASN A 116 CA CA A 451 1555 1555 2.47
LINK OD1 ASP A 151 CA CA A 451 1555 1555 2.51
LINK OD2 ASP A 151 CA CA A 451 1555 1555 2.70
LINK O ASP A 154 CA CA A 451 1555 1555 2.35
LINK OD1 ASP A 162 CA CA A 451 1555 1555 2.57
LINK O GLY A 197 CA CA A 451 1555 1555 2.39
LINK CA CA A 451 O HOH A 553 1555 1555 2.45
CRYST1 63.210 167.500 46.720 90.00 90.00 90.00 P 21 21 21 4
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 0.015820 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005970 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
